data_2PHL
# 
_entry.id   2PHL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2PHL         
WWPDB D_1000178469 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2PHL 
_pdbx_database_status.recvd_initial_deposition_date   1994-07-07 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    ? 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Lawrence, M.C.' 1 
'Izard, T.'      2 
'Beuchat, M.'    3 
'Blagrove, R.J.' 4 
'Colman, P.M.'   5 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 
;Structure of phaseolin at 2.2 A resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins.
;
J.Mol.Biol. 238 748 776 1994 JMOBAK UK 0022-2836 0070 ? 8182747 10.1006/jmbi.1994.1333 
1       'The Three-Dimensional Structure of the Seed Storage Protein Phaseolin at 3 Angstroms Resolution' 'Embo J.'   9   9   ?   
1990 EMJODG UK 0261-4189 0897 ? ?       ?                      
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Lawrence, M.C.'    1  
primary 'Izard, T.'         2  
primary 'Beuchat, M.'       3  
primary 'Blagrove, R.J.'    4  
primary 'Colman, P.M.'      5  
1       'Lawrence, M.C.'    6  
1       'Suzuki, E.'        7  
1       'Varghese, J.N.'    8  
1       'Davis, P.C.'       9  
1       'Van Donkelaar, A.' 10 
1       'Tulloch, P.A.'     11 
1       'Colman, P.M.'      12 
# 
_cell.entry_id           2PHL 
_cell.length_a           89.810 
_cell.length_b           114.080 
_cell.length_c           137.080 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         2PHL 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man PHASEOLIN              45043.035 3  ? ? ? ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   3  ? ? ? ? 
3 non-polymer syn 'PHOSPHATE ION'        94.971    3  ? ? ? ? 
4 water       nat water                  18.015    70 ? ? ? ? 
# 
_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       
;TSLREEEESQDNPFYFNSDNSWNTLFKNQYGHIRVLQRFDQQSKRLQNLEDYRLVEFRSKPETLLLPQQADAELLLVVRS
GSAILVLVKPDDRREYFFLTSDNPIFSDHQKIPAGTIFYLVNPDPKEDLRIIQLAMPVNNPQIHEFFLSSTEAQQSYLQE
FSKHILEASFNSKFEEINRVLFEEEGQQEGVIVNIDSEQIKELSKHAKSSSRKSLSKQDNTIGNEFGNLTERTDNSLNVL
ISSIEMEEGALFVPHYYSKAIVILVVNEGEAHVELVGPKGNKETLEYESYRAELSKDDVFVIPAAYPVAIKATSNVNFTG
FGINANNNNRNLLAGKTDNVISSIGRALDGKDVLGLTFSGSGDEVMKLINKQSGSYFVDAHHHQQEQQKGRKGAFVY
;
_entity_poly.pdbx_seq_one_letter_code_can   
;TSLREEEESQDNPFYFNSDNSWNTLFKNQYGHIRVLQRFDQQSKRLQNLEDYRLVEFRSKPETLLLPQQADAELLLVVRS
GSAILVLVKPDDRREYFFLTSDNPIFSDHQKIPAGTIFYLVNPDPKEDLRIIQLAMPVNNPQIHEFFLSSTEAQQSYLQE
FSKHILEASFNSKFEEINRVLFEEEGQQEGVIVNIDSEQIKELSKHAKSSSRKSLSKQDNTIGNEFGNLTERTDNSLNVL
ISSIEMEEGALFVPHYYSKAIVILVVNEGEAHVELVGPKGNKETLEYESYRAELSKDDVFVIPAAYPVAIKATSNVNFTG
FGINANNNNRNLLAGKTDNVISSIGRALDGKDVLGLTFSGSGDEVMKLINKQSGSYFVDAHHHQQEQQKGRKGAFVY
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   THR n 
1 2   SER n 
1 3   LEU n 
1 4   ARG n 
1 5   GLU n 
1 6   GLU n 
1 7   GLU n 
1 8   GLU n 
1 9   SER n 
1 10  GLN n 
1 11  ASP n 
1 12  ASN n 
1 13  PRO n 
1 14  PHE n 
1 15  TYR n 
1 16  PHE n 
1 17  ASN n 
1 18  SER n 
1 19  ASP n 
1 20  ASN n 
1 21  SER n 
1 22  TRP n 
1 23  ASN n 
1 24  THR n 
1 25  LEU n 
1 26  PHE n 
1 27  LYS n 
1 28  ASN n 
1 29  GLN n 
1 30  TYR n 
1 31  GLY n 
1 32  HIS n 
1 33  ILE n 
1 34  ARG n 
1 35  VAL n 
1 36  LEU n 
1 37  GLN n 
1 38  ARG n 
1 39  PHE n 
1 40  ASP n 
1 41  GLN n 
1 42  GLN n 
1 43  SER n 
1 44  LYS n 
1 45  ARG n 
1 46  LEU n 
1 47  GLN n 
1 48  ASN n 
1 49  LEU n 
1 50  GLU n 
1 51  ASP n 
1 52  TYR n 
1 53  ARG n 
1 54  LEU n 
1 55  VAL n 
1 56  GLU n 
1 57  PHE n 
1 58  ARG n 
1 59  SER n 
1 60  LYS n 
1 61  PRO n 
1 62  GLU n 
1 63  THR n 
1 64  LEU n 
1 65  LEU n 
1 66  LEU n 
1 67  PRO n 
1 68  GLN n 
1 69  GLN n 
1 70  ALA n 
1 71  ASP n 
1 72  ALA n 
1 73  GLU n 
1 74  LEU n 
1 75  LEU n 
1 76  LEU n 
1 77  VAL n 
1 78  VAL n 
1 79  ARG n 
1 80  SER n 
1 81  GLY n 
1 82  SER n 
1 83  ALA n 
1 84  ILE n 
1 85  LEU n 
1 86  VAL n 
1 87  LEU n 
1 88  VAL n 
1 89  LYS n 
1 90  PRO n 
1 91  ASP n 
1 92  ASP n 
1 93  ARG n 
1 94  ARG n 
1 95  GLU n 
1 96  TYR n 
1 97  PHE n 
1 98  PHE n 
1 99  LEU n 
1 100 THR n 
1 101 SER n 
1 102 ASP n 
1 103 ASN n 
1 104 PRO n 
1 105 ILE n 
1 106 PHE n 
1 107 SER n 
1 108 ASP n 
1 109 HIS n 
1 110 GLN n 
1 111 LYS n 
1 112 ILE n 
1 113 PRO n 
1 114 ALA n 
1 115 GLY n 
1 116 THR n 
1 117 ILE n 
1 118 PHE n 
1 119 TYR n 
1 120 LEU n 
1 121 VAL n 
1 122 ASN n 
1 123 PRO n 
1 124 ASP n 
1 125 PRO n 
1 126 LYS n 
1 127 GLU n 
1 128 ASP n 
1 129 LEU n 
1 130 ARG n 
1 131 ILE n 
1 132 ILE n 
1 133 GLN n 
1 134 LEU n 
1 135 ALA n 
1 136 MET n 
1 137 PRO n 
1 138 VAL n 
1 139 ASN n 
1 140 ASN n 
1 141 PRO n 
1 142 GLN n 
1 143 ILE n 
1 144 HIS n 
1 145 GLU n 
1 146 PHE n 
1 147 PHE n 
1 148 LEU n 
1 149 SER n 
1 150 SER n 
1 151 THR n 
1 152 GLU n 
1 153 ALA n 
1 154 GLN n 
1 155 GLN n 
1 156 SER n 
1 157 TYR n 
1 158 LEU n 
1 159 GLN n 
1 160 GLU n 
1 161 PHE n 
1 162 SER n 
1 163 LYS n 
1 164 HIS n 
1 165 ILE n 
1 166 LEU n 
1 167 GLU n 
1 168 ALA n 
1 169 SER n 
1 170 PHE n 
1 171 ASN n 
1 172 SER n 
1 173 LYS n 
1 174 PHE n 
1 175 GLU n 
1 176 GLU n 
1 177 ILE n 
1 178 ASN n 
1 179 ARG n 
1 180 VAL n 
1 181 LEU n 
1 182 PHE n 
1 183 GLU n 
1 184 GLU n 
1 185 GLU n 
1 186 GLY n 
1 187 GLN n 
1 188 GLN n 
1 189 GLU n 
1 190 GLY n 
1 191 VAL n 
1 192 ILE n 
1 193 VAL n 
1 194 ASN n 
1 195 ILE n 
1 196 ASP n 
1 197 SER n 
1 198 GLU n 
1 199 GLN n 
1 200 ILE n 
1 201 LYS n 
1 202 GLU n 
1 203 LEU n 
1 204 SER n 
1 205 LYS n 
1 206 HIS n 
1 207 ALA n 
1 208 LYS n 
1 209 SER n 
1 210 SER n 
1 211 SER n 
1 212 ARG n 
1 213 LYS n 
1 214 SER n 
1 215 LEU n 
1 216 SER n 
1 217 LYS n 
1 218 GLN n 
1 219 ASP n 
1 220 ASN n 
1 221 THR n 
1 222 ILE n 
1 223 GLY n 
1 224 ASN n 
1 225 GLU n 
1 226 PHE n 
1 227 GLY n 
1 228 ASN n 
1 229 LEU n 
1 230 THR n 
1 231 GLU n 
1 232 ARG n 
1 233 THR n 
1 234 ASP n 
1 235 ASN n 
1 236 SER n 
1 237 LEU n 
1 238 ASN n 
1 239 VAL n 
1 240 LEU n 
1 241 ILE n 
1 242 SER n 
1 243 SER n 
1 244 ILE n 
1 245 GLU n 
1 246 MET n 
1 247 GLU n 
1 248 GLU n 
1 249 GLY n 
1 250 ALA n 
1 251 LEU n 
1 252 PHE n 
1 253 VAL n 
1 254 PRO n 
1 255 HIS n 
1 256 TYR n 
1 257 TYR n 
1 258 SER n 
1 259 LYS n 
1 260 ALA n 
1 261 ILE n 
1 262 VAL n 
1 263 ILE n 
1 264 LEU n 
1 265 VAL n 
1 266 VAL n 
1 267 ASN n 
1 268 GLU n 
1 269 GLY n 
1 270 GLU n 
1 271 ALA n 
1 272 HIS n 
1 273 VAL n 
1 274 GLU n 
1 275 LEU n 
1 276 VAL n 
1 277 GLY n 
1 278 PRO n 
1 279 LYS n 
1 280 GLY n 
1 281 ASN n 
1 282 LYS n 
1 283 GLU n 
1 284 THR n 
1 285 LEU n 
1 286 GLU n 
1 287 TYR n 
1 288 GLU n 
1 289 SER n 
1 290 TYR n 
1 291 ARG n 
1 292 ALA n 
1 293 GLU n 
1 294 LEU n 
1 295 SER n 
1 296 LYS n 
1 297 ASP n 
1 298 ASP n 
1 299 VAL n 
1 300 PHE n 
1 301 VAL n 
1 302 ILE n 
1 303 PRO n 
1 304 ALA n 
1 305 ALA n 
1 306 TYR n 
1 307 PRO n 
1 308 VAL n 
1 309 ALA n 
1 310 ILE n 
1 311 LYS n 
1 312 ALA n 
1 313 THR n 
1 314 SER n 
1 315 ASN n 
1 316 VAL n 
1 317 ASN n 
1 318 PHE n 
1 319 THR n 
1 320 GLY n 
1 321 PHE n 
1 322 GLY n 
1 323 ILE n 
1 324 ASN n 
1 325 ALA n 
1 326 ASN n 
1 327 ASN n 
1 328 ASN n 
1 329 ASN n 
1 330 ARG n 
1 331 ASN n 
1 332 LEU n 
1 333 LEU n 
1 334 ALA n 
1 335 GLY n 
1 336 LYS n 
1 337 THR n 
1 338 ASP n 
1 339 ASN n 
1 340 VAL n 
1 341 ILE n 
1 342 SER n 
1 343 SER n 
1 344 ILE n 
1 345 GLY n 
1 346 ARG n 
1 347 ALA n 
1 348 LEU n 
1 349 ASP n 
1 350 GLY n 
1 351 LYS n 
1 352 ASP n 
1 353 VAL n 
1 354 LEU n 
1 355 GLY n 
1 356 LEU n 
1 357 THR n 
1 358 PHE n 
1 359 SER n 
1 360 GLY n 
1 361 SER n 
1 362 GLY n 
1 363 ASP n 
1 364 GLU n 
1 365 VAL n 
1 366 MET n 
1 367 LYS n 
1 368 LEU n 
1 369 ILE n 
1 370 ASN n 
1 371 LYS n 
1 372 GLN n 
1 373 SER n 
1 374 GLY n 
1 375 SER n 
1 376 TYR n 
1 377 PHE n 
1 378 VAL n 
1 379 ASP n 
1 380 ALA n 
1 381 HIS n 
1 382 HIS n 
1 383 HIS n 
1 384 GLN n 
1 385 GLN n 
1 386 GLU n 
1 387 GLN n 
1 388 GLN n 
1 389 LYS n 
1 390 GLY n 
1 391 ARG n 
1 392 LYS n 
1 393 GLY n 
1 394 ALA n 
1 395 PHE n 
1 396 VAL n 
1 397 TYR 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     Phaseolus 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Phaseolus vulgaris' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     3885 
_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      ? 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     ? 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PHSB_PHAVU 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P02853 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;MMRARVPLLLLGILFLASLSASFATSLREEEESQDNPFYFNSDNSWNTLFKNQYGHIRVLQRFDQQSKRLQNLEDYRLVE
FRSKPETLLLPQQADAELLLVVRSGSAILVLVKPDDRREYFFLTSDNPIFSDHQKIPAGTIFYLVNPDPKEDLRIIQLAM
PVNNPQIHEFFLSSTEAQQSYLQEFSKHILEASFNSKFEEINRVLFEEEGQQEGVIVNIDSEQIKELSKHAKSSSRKSLS
KQDNTIGNEFGNLTERTDNSLNVLISSIEMEEGALFVPHYYSKAIVILVVNEGEAHVELVGPKGNKETLEYESYRAELSK
DDVFVIPAAYPVAIKATSNVNFTGFGINANNNNRNLLAGKTDNVISSIGRALDGKDVLGLTFSGSGDEVMKLINKQSGSY
FVDAHHHQQEQQKGRKGAFVY
;
_struct_ref.pdbx_db_isoform            ? 
# 
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 2PHL A 1 ? 397 ? P02853 25 ? 421 ? 1 397 
2 1 2PHL B 1 ? 397 ? P02853 25 ? 421 ? 1 397 
3 1 2PHL C 1 ? 397 ? P02853 25 ? 421 ? 1 397 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE               ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE             ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'        ? 'C4 H7 N O4'     133.103 
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 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE          ? 'C9 H11 N O2'    165.189 
PO4 non-polymer         . 'PHOSPHATE ION'        ? 'O4 P -3'        94.971  
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 
# 
_exptl.entry_id          2PHL 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.60 
_exptl_crystal.density_percent_sol   52.65 
_exptl_crystal.description           ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           ? 
_diffrn.ambient_temp_details   ? 
# 
_refine.entry_id                                 2PHL 
_refine.ls_number_reflns_obs                     35333 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             6.0 
_refine.ls_d_res_high                            2.20 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          0.1780000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1780000 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8619 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         57 
_refine_hist.number_atoms_solvent             70 
_refine_hist.number_atoms_total               8746 
_refine_hist.d_res_high                       2.20 
_refine_hist.d_res_low                        6.0 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
x_bond_d                0.011 ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_na             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_prot           ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d               ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_na            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_prot          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg             1.80  ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             ?     ? ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            ?     ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct.entry_id                  2PHL 
_struct.title                     
;THE STRUCTURE OF PHASEOLIN AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR A COMMON VICILIN(SLASH)LEGUMIN STRUCTURE AND THE GENETIC ENGINEERING OF SEED STORAGE PROTEINS
;
_struct.pdbx_descriptor           PHASEOLIN 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2PHL 
_struct_keywords.pdbx_keywords   'PLANT SEED STORAGE PROTEIN(VICILIN)' 
_struct_keywords.text            'PLANT SEED STORAGE PROTEIN(VICILIN)' 
# 
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 2 ? 
G N N 3 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
# 
_struct_biol.id   1 
# 
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  N1A SER A 156 ? PHE A 161 ? SER A 156 PHE A 161 5 ? 6  
HELX_P HELX_P2  N2A SER A 162 ? ASN A 171 ? SER A 162 ASN A 171 1 ? 10 
HELX_P HELX_P3  N3A LYS A 173 ? PHE A 182 ? LYS A 173 PHE A 182 1 ? 10 
HELX_P HELX_P4  N4A ILE A 200 ? SER A 209 ? ILE A 200 SER A 209 1 ? 10 
HELX_P HELX_P5  C1A VAL A 340 ? ARG A 346 ? VAL A 340 ARG A 346 1 ? 7  
HELX_P HELX_P6  C2A ASP A 349 ? PHE A 358 ? ASP A 349 PHE A 358 1 ? 10 
HELX_P HELX_P7  C3A SER A 361 ? ASN A 370 ? SER A 361 ASN A 370 1 ? 10 
HELX_P HELX_P8  N1B SER B 156 ? PHE B 161 ? SER B 156 PHE B 161 5 ? 6  
HELX_P HELX_P9  N2B SER B 162 ? ASN B 171 ? SER B 162 ASN B 171 1 ? 10 
HELX_P HELX_P10 N3B LYS B 173 ? PHE B 182 ? LYS B 173 PHE B 182 1 ? 10 
HELX_P HELX_P11 N4B ILE B 200 ? SER B 209 ? ILE B 200 SER B 209 1 ? 10 
HELX_P HELX_P12 C1B VAL B 340 ? ARG B 346 ? VAL B 340 ARG B 346 1 ? 7  
HELX_P HELX_P13 C2B ASP B 349 ? PHE B 358 ? ASP B 349 PHE B 358 1 ? 10 
HELX_P HELX_P14 C3B SER B 361 ? ASN B 370 ? SER B 361 ASN B 370 1 ? 10 
HELX_P HELX_P15 N1C SER C 156 ? PHE C 161 ? SER C 156 PHE C 161 5 ? 6  
HELX_P HELX_P16 N2C SER C 162 ? ASN C 171 ? SER C 162 ASN C 171 1 ? 10 
HELX_P HELX_P17 N3C LYS C 173 ? PHE C 182 ? LYS C 173 PHE C 182 1 ? 10 
HELX_P HELX_P18 N4C ILE C 200 ? SER C 209 ? ILE C 200 SER C 209 1 ? 10 
HELX_P HELX_P19 C1C VAL C 340 ? ARG C 346 ? VAL C 340 ARG C 346 1 ? 7  
HELX_P HELX_P20 C2C ASP C 349 ? PHE C 358 ? ASP C 349 PHE C 358 1 ? 10 
HELX_P HELX_P21 C3C SER C 361 ? ASN C 370 ? SER C 361 ASN C 370 1 ? 10 
# 
_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 
covale1 covale ? ? A ASN 228 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 228 A NAG 900 1_555 ? ? ? ? ? ? ? 1.451 ? 
covale2 covale ? ? B ASN 228 ND2 ? ? ? 1_555 F NAG . C1 ? ? B ASN 228 B NAG 901 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale3 covale ? ? C ASN 228 ND2 ? ? ? 1_555 H NAG . C1 ? ? C ASN 228 C NAG 902 1_555 ? ? ? ? ? ? ? 1.411 ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
N1A ? 6 ? 
2AA ? 5 ? 
2BA ? 5 ? 
C1A ? 7 ? 
CAA ? 5 ? 
CBA ? 5 ? 
N1B ? 6 ? 
2AB ? 5 ? 
2BB ? 5 ? 
C1B ? 7 ? 
CAB ? 5 ? 
CBB ? 5 ? 
N1C ? 6 ? 
2AC ? 5 ? 
2BC ? 5 ? 
C1C ? 7 ? 
CAC ? 5 ? 
CBC ? 5 ? 
# 
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 
N1A 1 2 ? anti-parallel 
N1A 2 3 ? anti-parallel 
N1A 3 4 ? anti-parallel 
N1A 4 5 ? anti-parallel 
N1A 5 6 ? anti-parallel 
2AA 1 2 ? anti-parallel 
2AA 2 3 ? anti-parallel 
2AA 3 4 ? anti-parallel 
2AA 4 5 ? anti-parallel 
2BA 1 2 ? anti-parallel 
2BA 2 3 ? anti-parallel 
2BA 3 4 ? anti-parallel 
2BA 4 5 ? anti-parallel 
C1A 1 2 ? anti-parallel 
C1A 2 3 ? anti-parallel 
C1A 3 4 ? anti-parallel 
C1A 4 5 ? anti-parallel 
C1A 5 6 ? anti-parallel 
C1A 6 7 ? anti-parallel 
CAA 1 2 ? anti-parallel 
CAA 2 3 ? anti-parallel 
CAA 3 4 ? anti-parallel 
CAA 4 5 ? anti-parallel 
CBA 1 2 ? anti-parallel 
CBA 2 3 ? anti-parallel 
CBA 3 4 ? anti-parallel 
CBA 4 5 ? anti-parallel 
N1B 1 2 ? anti-parallel 
N1B 2 3 ? anti-parallel 
N1B 3 4 ? anti-parallel 
N1B 4 5 ? anti-parallel 
N1B 5 6 ? anti-parallel 
2AB 1 2 ? anti-parallel 
2AB 2 3 ? anti-parallel 
2AB 3 4 ? anti-parallel 
2AB 4 5 ? anti-parallel 
2BB 1 2 ? anti-parallel 
2BB 2 3 ? anti-parallel 
2BB 3 4 ? anti-parallel 
2BB 4 5 ? anti-parallel 
C1B 1 2 ? anti-parallel 
C1B 2 3 ? anti-parallel 
C1B 3 4 ? anti-parallel 
C1B 4 5 ? anti-parallel 
C1B 5 6 ? anti-parallel 
C1B 6 7 ? anti-parallel 
CAB 1 2 ? anti-parallel 
CAB 2 3 ? anti-parallel 
CAB 3 4 ? anti-parallel 
CAB 4 5 ? anti-parallel 
CBB 1 2 ? anti-parallel 
CBB 2 3 ? anti-parallel 
CBB 3 4 ? anti-parallel 
CBB 4 5 ? anti-parallel 
N1C 1 2 ? anti-parallel 
N1C 2 3 ? anti-parallel 
N1C 3 4 ? anti-parallel 
N1C 4 5 ? anti-parallel 
N1C 5 6 ? anti-parallel 
2AC 1 2 ? anti-parallel 
2AC 2 3 ? anti-parallel 
2AC 3 4 ? anti-parallel 
2AC 4 5 ? anti-parallel 
2BC 1 2 ? anti-parallel 
2BC 2 3 ? anti-parallel 
2BC 3 4 ? anti-parallel 
2BC 4 5 ? anti-parallel 
C1C 1 2 ? anti-parallel 
C1C 2 3 ? anti-parallel 
C1C 3 4 ? anti-parallel 
C1C 4 5 ? anti-parallel 
C1C 5 6 ? anti-parallel 
C1C 6 7 ? anti-parallel 
CAC 1 2 ? anti-parallel 
CAC 2 3 ? anti-parallel 
CAC 3 4 ? anti-parallel 
CAC 4 5 ? anti-parallel 
CBC 1 2 ? anti-parallel 
CBC 2 3 ? anti-parallel 
CBC 3 4 ? anti-parallel 
CBC 4 5 ? 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 
N1A 1 SER A 21  ? ASN A 28  ? SER A 21  ASN A 28  
N1A 2 TYR A 30  ? GLN A 37  ? TYR A 30  GLN A 37  
N1A 3 ARG A 53  ? LYS A 60  ? ARG A 53  LYS A 60  
N1A 4 LEU A 129 ? MET A 136 ? LEU A 129 MET A 136 
N1A 5 GLU A 73  ? SER A 80  ? GLU A 73  SER A 80  
N1A 6 ASP A 108 ? ILE A 112 ? ASP A 108 ILE A 112 
2AA 1 HIS A 144 ? LEU A 148 ? HIS A 144 LEU A 148 
2AA 2 GLU A 62  ? ASP A 71  ? GLU A 62  ASP A 71  
2AA 3 ILE A 117 ? ASN A 122 ? ILE A 117 ASN A 122 
2AA 4 GLY A 81  ? LYS A 89  ? GLY A 81  LYS A 89  
2AA 5 ARG A 93  ? SER A 101 ? ARG A 93  SER A 101 
2BA 1 VAL A 191 ? ILE A 195 ? VAL A 191 ILE A 195 
2BA 2 GLU A 62  ? ASP A 71  ? GLU A 62  ASP A 71  
2BA 3 ILE A 117 ? ASN A 122 ? ILE A 117 ASN A 122 
2BA 4 GLY A 81  ? LYS A 89  ? GLY A 81  LYS A 89  
2BA 5 ARG A 93  ? SER A 101 ? ARG A 93  SER A 101 
C1A 1 ASN A 220 ? ASN A 224 ? ASN A 220 ASN A 224 
C1A 2 PHE A 226 ? ASP A 234 ? PHE A 226 ASP A 234 
C1A 3 ASN A 238 ? GLU A 247 ? ASN A 238 GLU A 247 
C1A 4 VAL A 316 ? ASN A 324 ? VAL A 316 ASN A 324 
C1A 5 ILE A 261 ? GLU A 268 ? ILE A 261 GLU A 268 
C1A 6 ASP A 298 ? ILE A 302 ? ASP A 298 ILE A 302 
C1A 7 PHE A 14  ? PHE A 16  ? PHE A 14  PHE A 16  
CAA 1 ASN A 329 ? LEU A 333 ? ASN A 329 LEU A 333 
CAA 2 GLY A 249 ? SER A 258 ? GLY A 249 SER A 258 
CAA 3 PRO A 307 ? ALA A 312 ? PRO A 307 ALA A 312 
CAA 4 HIS A 272 ? GLY A 277 ? HIS A 272 GLY A 277 
CAA 5 GLU A 288 ? ALA A 292 ? GLU A 288 ALA A 292 
CBA 1 TYR A 376 ? ALA A 380 ? TYR A 376 ALA A 380 
CBA 2 GLY A 249 ? SER A 258 ? GLY A 249 SER A 258 
CBA 3 PRO A 307 ? ALA A 312 ? PRO A 307 ALA A 312 
CBA 4 HIS A 272 ? GLY A 277 ? HIS A 272 GLY A 277 
CBA 5 GLU A 288 ? ALA A 292 ? GLU A 288 ALA A 292 
N1B 1 SER B 21  ? ASN B 28  ? SER B 21  ASN B 28  
N1B 2 TYR B 30  ? GLN B 37  ? TYR B 30  GLN B 37  
N1B 3 ARG B 53  ? LYS B 60  ? ARG B 53  LYS B 60  
N1B 4 LEU B 129 ? MET B 136 ? LEU B 129 MET B 136 
N1B 5 GLU B 73  ? SER B 80  ? GLU B 73  SER B 80  
N1B 6 ASP B 108 ? ILE B 112 ? ASP B 108 ILE B 112 
2AB 1 HIS B 144 ? LEU B 148 ? HIS B 144 LEU B 148 
2AB 2 GLU B 62  ? ASP B 71  ? GLU B 62  ASP B 71  
2AB 3 ILE B 117 ? ASN B 122 ? ILE B 117 ASN B 122 
2AB 4 GLY B 81  ? LYS B 89  ? GLY B 81  LYS B 89  
2AB 5 ARG B 93  ? SER B 101 ? ARG B 93  SER B 101 
2BB 1 VAL B 191 ? ILE B 195 ? VAL B 191 ILE B 195 
2BB 2 GLU B 62  ? ASP B 71  ? GLU B 62  ASP B 71  
2BB 3 ILE B 117 ? ASN B 122 ? ILE B 117 ASN B 122 
2BB 4 GLY B 81  ? LYS B 89  ? GLY B 81  LYS B 89  
2BB 5 ARG B 93  ? SER B 101 ? ARG B 93  SER B 101 
C1B 1 ASN B 220 ? ASN B 224 ? ASN B 220 ASN B 224 
C1B 2 PHE B 226 ? ASP B 234 ? PHE B 226 ASP B 234 
C1B 3 ASN B 238 ? GLU B 247 ? ASN B 238 GLU B 247 
C1B 4 VAL B 316 ? ASN B 324 ? VAL B 316 ASN B 324 
C1B 5 ILE B 261 ? GLU B 268 ? ILE B 261 GLU B 268 
C1B 6 ASP B 298 ? ILE B 302 ? ASP B 298 ILE B 302 
C1B 7 PHE B 14  ? PHE B 16  ? PHE B 14  PHE B 16  
CAB 1 ASN B 329 ? LEU B 333 ? ASN B 329 LEU B 333 
CAB 2 GLY B 249 ? SER B 258 ? GLY B 249 SER B 258 
CAB 3 PRO B 307 ? ALA B 312 ? PRO B 307 ALA B 312 
CAB 4 HIS B 272 ? GLY B 277 ? HIS B 272 GLY B 277 
CAB 5 GLU B 288 ? ALA B 292 ? GLU B 288 ALA B 292 
CBB 1 TYR B 376 ? ALA B 380 ? TYR B 376 ALA B 380 
CBB 2 GLY B 249 ? SER B 258 ? GLY B 249 SER B 258 
CBB 3 PRO B 307 ? ALA B 312 ? PRO B 307 ALA B 312 
CBB 4 HIS B 272 ? GLY B 277 ? HIS B 272 GLY B 277 
CBB 5 GLU B 288 ? ALA B 292 ? GLU B 288 ALA B 292 
N1C 1 SER C 21  ? ASN C 28  ? SER C 21  ASN C 28  
N1C 2 TYR C 30  ? GLN C 37  ? TYR C 30  GLN C 37  
N1C 3 ARG C 53  ? LYS C 60  ? ARG C 53  LYS C 60  
N1C 4 LEU C 129 ? MET C 136 ? LEU C 129 MET C 136 
N1C 5 GLU C 73  ? SER C 80  ? GLU C 73  SER C 80  
N1C 6 ASP C 108 ? ILE C 112 ? ASP C 108 ILE C 112 
2AC 1 HIS C 144 ? LEU C 148 ? HIS C 144 LEU C 148 
2AC 2 GLU C 62  ? ASP C 71  ? GLU C 62  ASP C 71  
2AC 3 ILE C 117 ? ASN C 122 ? ILE C 117 ASN C 122 
2AC 4 GLY C 81  ? LYS C 89  ? GLY C 81  LYS C 89  
2AC 5 ARG C 93  ? SER C 101 ? ARG C 93  SER C 101 
2BC 1 VAL C 191 ? ILE C 195 ? VAL C 191 ILE C 195 
2BC 2 GLU C 62  ? ASP C 71  ? GLU C 62  ASP C 71  
2BC 3 ILE C 117 ? ASN C 122 ? ILE C 117 ASN C 122 
2BC 4 GLY C 81  ? LYS C 89  ? GLY C 81  LYS C 89  
2BC 5 ARG C 93  ? SER C 101 ? ARG C 93  SER C 101 
C1C 1 ASN C 220 ? ASN C 224 ? ASN C 220 ASN C 224 
C1C 2 PHE C 226 ? ASP C 234 ? PHE C 226 ASP C 234 
C1C 3 ASN C 238 ? GLU C 247 ? ASN C 238 GLU C 247 
C1C 4 VAL C 316 ? ASN C 324 ? VAL C 316 ASN C 324 
C1C 5 ILE C 261 ? GLU C 268 ? ILE C 261 GLU C 268 
C1C 6 ASP C 298 ? ILE C 302 ? ASP C 298 ILE C 302 
C1C 7 PHE C 14  ? PHE C 16  ? PHE C 14  PHE C 16  
CAC 1 ASN C 329 ? LEU C 333 ? ASN C 329 LEU C 333 
CAC 2 GLY C 249 ? SER C 258 ? GLY C 249 SER C 258 
CAC 3 PRO C 307 ? ALA C 312 ? PRO C 307 ALA C 312 
CAC 4 HIS C 272 ? GLY C 277 ? HIS C 272 GLY C 277 
CAC 5 GLU C 288 ? ALA C 292 ? GLU C 288 ALA C 292 
CBC 1 TYR C 376 ? ALA C 380 ? TYR C 376 ALA C 380 
CBC 2 GLY C 249 ? SER C 258 ? GLY C 249 SER C 258 
CBC 3 PRO C 307 ? ALA C 312 ? PRO C 307 ALA C 312 
CBC 4 HIS C 272 ? GLY C 277 ? HIS C 272 GLY C 277 
CBC 5 GLU C 288 ? ALA C 292 ? GLU C 288 ALA C 292 
# 
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 
N1A 1 2 O PHE A 26  ? O PHE A 26  N ILE A 33  ? N ILE A 33  
N1A 2 3 O HIS A 32  ? O HIS A 32  N ARG A 58  ? N ARG A 58  
N1A 3 4 O PHE A 57  ? O PHE A 57  N ILE A 131 ? N ILE A 131 
N1A 4 5 O ILE A 132 ? O ILE A 132 N VAL A 77  ? N VAL A 77  
N1A 5 6 O LEU A 76  ? O LEU A 76  N GLN A 110 ? N GLN A 110 
2AA 1 2 O PHE A 146 ? O PHE A 146 N GLN A 69  ? N GLN A 69  
2AA 2 3 N GLN A 68  ? N GLN A 68  O PHE A 118 ? O PHE A 118 
2AA 3 4 N TYR A 119 ? N TYR A 119 O VAL A 86  ? O VAL A 86  
2AA 4 5 N LEU A 85  ? N LEU A 85  O PHE A 97  ? O PHE A 97  
2BA 1 2 O VAL A 193 ? O VAL A 193 N LEU A 64  ? N LEU A 64  
2BA 2 3 N GLN A 68  ? N GLN A 68  O PHE A 118 ? O PHE A 118 
2BA 3 4 N TYR A 119 ? N TYR A 119 O VAL A 86  ? O VAL A 86  
2BA 4 5 N LEU A 85  ? N LEU A 85  O PHE A 97  ? O PHE A 97  
C1A 1 2 O ASN A 224 ? O ASN A 224 N GLY A 227 ? N GLY A 227 
C1A 2 3 O ASN A 228 ? O ASN A 228 N GLU A 245 ? N GLU A 245 
C1A 3 4 O ILE A 244 ? O ILE A 244 N PHE A 318 ? N PHE A 318 
C1A 4 5 O THR A 319 ? O THR A 319 N VAL A 265 ? N VAL A 265 
C1A 5 6 O LEU A 264 ? O LEU A 264 N PHE A 300 ? N PHE A 300 
C1A 6 7 O VAL A 299 ? O VAL A 299 N PHE A 16  ? N PHE A 16  
CAA 1 2 O ASN A 331 ? O ASN A 331 N TYR A 256 ? N TYR A 256 
CAA 2 3 O HIS A 255 ? O HIS A 255 N VAL A 308 ? N VAL A 308 
CAA 3 4 O ALA A 309 ? O ALA A 309 N GLU A 274 ? N GLU A 274 
CAA 4 5 O VAL A 273 ? O VAL A 273 N ALA A 292 ? N ALA A 292 
CBA 1 2 O VAL A 378 ? O VAL A 378 N LEU A 251 ? N LEU A 251 
CBA 2 3 O HIS A 255 ? O HIS A 255 N VAL A 308 ? N VAL A 308 
CBA 3 4 O ALA A 309 ? O ALA A 309 N GLU A 274 ? N GLU A 274 
CBA 4 5 O VAL A 273 ? O VAL A 273 N ALA A 292 ? N ALA A 292 
N1B 1 2 O PHE B 26  ? O PHE B 26  N ILE B 33  ? N ILE B 33  
N1B 2 3 O HIS B 32  ? O HIS B 32  N ARG B 58  ? N ARG B 58  
N1B 3 4 O PHE B 57  ? O PHE B 57  N ILE B 131 ? N ILE B 131 
N1B 4 5 O ILE B 132 ? O ILE B 132 N VAL B 77  ? N VAL B 77  
N1B 5 6 O LEU B 76  ? O LEU B 76  N GLN B 110 ? N GLN B 110 
2AB 1 2 O PHE B 146 ? O PHE B 146 N GLN B 69  ? N GLN B 69  
2AB 2 3 N GLN B 68  ? N GLN B 68  O PHE B 118 ? O PHE B 118 
2AB 3 4 N TYR B 119 ? N TYR B 119 O VAL B 86  ? O VAL B 86  
2AB 4 5 N LEU B 85  ? N LEU B 85  O PHE B 97  ? O PHE B 97  
2BB 1 2 O VAL B 193 ? O VAL B 193 N LEU B 64  ? N LEU B 64  
2BB 2 3 N GLN B 68  ? N GLN B 68  O PHE B 118 ? O PHE B 118 
2BB 3 4 N TYR B 119 ? N TYR B 119 O VAL B 86  ? O VAL B 86  
2BB 4 5 N LEU B 85  ? N LEU B 85  O PHE B 97  ? O PHE B 97  
C1B 1 2 O ASN B 224 ? O ASN B 224 N GLY B 227 ? N GLY B 227 
C1B 2 3 O ASN B 228 ? O ASN B 228 N GLU B 245 ? N GLU B 245 
C1B 3 4 O ILE B 244 ? O ILE B 244 N PHE B 318 ? N PHE B 318 
C1B 4 5 O THR B 319 ? O THR B 319 N VAL B 265 ? N VAL B 265 
C1B 5 6 O LEU B 264 ? O LEU B 264 N PHE B 300 ? N PHE B 300 
C1B 6 7 O VAL B 299 ? O VAL B 299 N PHE B 16  ? N PHE B 16  
CAB 1 2 O ASN B 331 ? O ASN B 331 N TYR B 256 ? N TYR B 256 
CAB 2 3 O HIS B 255 ? O HIS B 255 N VAL B 308 ? N VAL B 308 
CAB 3 4 O ALA B 309 ? O ALA B 309 N GLU B 274 ? N GLU B 274 
CAB 4 5 O VAL B 273 ? O VAL B 273 N ALA B 292 ? N ALA B 292 
CBB 1 2 O VAL B 378 ? O VAL B 378 N LEU B 251 ? N LEU B 251 
CBB 2 3 O HIS B 255 ? O HIS B 255 N VAL B 308 ? N VAL B 308 
CBB 3 4 O ALA B 309 ? O ALA B 309 N GLU B 274 ? N GLU B 274 
CBB 4 5 O VAL B 273 ? O VAL B 273 N ALA B 292 ? N ALA B 292 
N1C 1 2 O PHE C 26  ? O PHE C 26  N ILE C 33  ? N ILE C 33  
N1C 2 3 O HIS C 32  ? O HIS C 32  N ARG C 58  ? N ARG C 58  
N1C 3 4 O PHE C 57  ? O PHE C 57  N ILE C 131 ? N ILE C 131 
N1C 4 5 O ILE C 132 ? O ILE C 132 N VAL C 77  ? N VAL C 77  
N1C 5 6 O LEU C 76  ? O LEU C 76  N GLN C 110 ? N GLN C 110 
2AC 1 2 O PHE C 146 ? O PHE C 146 N GLN C 69  ? N GLN C 69  
2AC 2 3 N GLN C 68  ? N GLN C 68  O PHE C 118 ? O PHE C 118 
2AC 3 4 N TYR C 119 ? N TYR C 119 O VAL C 86  ? O VAL C 86  
2AC 4 5 N LEU C 85  ? N LEU C 85  O PHE C 97  ? O PHE C 97  
2BC 1 2 O VAL C 193 ? O VAL C 193 N LEU C 64  ? N LEU C 64  
2BC 2 3 N GLN C 68  ? N GLN C 68  O PHE C 118 ? O PHE C 118 
2BC 3 4 N TYR C 119 ? N TYR C 119 O VAL C 86  ? O VAL C 86  
2BC 4 5 N LEU C 85  ? N LEU C 85  O PHE C 97  ? O PHE C 97  
C1C 1 2 O ASN C 224 ? O ASN C 224 N GLY C 227 ? N GLY C 227 
C1C 2 3 O ASN C 228 ? O ASN C 228 N GLU C 245 ? N GLU C 245 
C1C 3 4 O ILE C 244 ? O ILE C 244 N PHE C 318 ? N PHE C 318 
C1C 4 5 O THR C 319 ? O THR C 319 N VAL C 265 ? N VAL C 265 
C1C 5 6 O LEU C 264 ? O LEU C 264 N PHE C 300 ? N PHE C 300 
C1C 6 7 O VAL C 299 ? O VAL C 299 N PHE C 16  ? N PHE C 16  
CAC 1 2 O ASN C 331 ? O ASN C 331 N TYR C 256 ? N TYR C 256 
CAC 2 3 O HIS C 255 ? O HIS C 255 N VAL C 308 ? N VAL C 308 
CAC 3 4 O ALA C 309 ? O ALA C 309 N GLU C 274 ? N GLU C 274 
CAC 4 5 O VAL C 273 ? O VAL C 273 N ALA C 292 ? N ALA C 292 
CBC 1 2 O VAL C 378 ? O VAL C 378 N LEU C 251 ? N LEU C 251 
CBC 2 3 O HIS C 255 ? O HIS C 255 N VAL C 308 ? N VAL C 308 
CBC 3 4 O ALA C 309 ? O ALA C 309 N GLU C 274 ? N GLU C 274 
CBC 4 5 O VAL C 273 ? O VAL C 273 N ALA C 292 ? N ALA C 292 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE NAG A 900' 
AC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE NAG B 901' 
AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NAG C 902' 
AC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE PO4 A 950' 
AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE PO4 B 951' 
AC6 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE PO4 C 952' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 7 ASN A 224 ? ASN A 224 . ? 1_555 ? 
2  AC1 7 GLU A 225 ? GLU A 225 . ? 1_555 ? 
3  AC1 7 PHE A 226 ? PHE A 226 . ? 1_555 ? 
4  AC1 7 GLY A 227 ? GLY A 227 . ? 1_555 ? 
5  AC1 7 ASN A 228 ? ASN A 228 . ? 1_555 ? 
6  AC1 7 GLU A 245 ? GLU A 245 . ? 1_555 ? 
7  AC1 7 GLU A 247 ? GLU A 247 . ? 1_555 ? 
8  AC2 3 ASN B 224 ? ASN B 224 . ? 1_555 ? 
9  AC2 3 GLU B 225 ? GLU B 225 . ? 1_555 ? 
10 AC2 3 ASN B 228 ? ASN B 228 . ? 1_555 ? 
11 AC3 5 ASN C 224 ? ASN C 224 . ? 1_555 ? 
12 AC3 5 GLU C 225 ? GLU C 225 . ? 1_555 ? 
13 AC3 5 PHE C 226 ? PHE C 226 . ? 1_555 ? 
14 AC3 5 ASN C 228 ? ASN C 228 . ? 1_555 ? 
15 AC3 5 GLU C 247 ? GLU C 247 . ? 1_555 ? 
16 AC4 7 HIS A 32  ? HIS A 32  . ? 1_555 ? 
17 AC4 7 ARG A 34  ? ARG A 34  . ? 1_555 ? 
18 AC4 7 GLU A 56  ? GLU A 56  . ? 1_555 ? 
19 AC4 7 ARG A 58  ? ARG A 58  . ? 1_555 ? 
20 AC4 7 ARG A 130 ? ARG A 130 . ? 1_555 ? 
21 AC4 7 LYS A 296 ? LYS A 296 . ? 1_555 ? 
22 AC4 7 ASP A 297 ? ASP A 297 . ? 1_555 ? 
23 AC5 6 HIS B 32  ? HIS B 32  . ? 1_555 ? 
24 AC5 6 GLU B 56  ? GLU B 56  . ? 1_555 ? 
25 AC5 6 ARG B 58  ? ARG B 58  . ? 1_555 ? 
26 AC5 6 ARG B 130 ? ARG B 130 . ? 1_555 ? 
27 AC5 6 LYS B 296 ? LYS B 296 . ? 1_555 ? 
28 AC5 6 ASP B 297 ? ASP B 297 . ? 1_555 ? 
29 AC6 8 HIS C 32  ? HIS C 32  . ? 1_555 ? 
30 AC6 8 ARG C 34  ? ARG C 34  . ? 1_555 ? 
31 AC6 8 GLU C 56  ? GLU C 56  . ? 1_555 ? 
32 AC6 8 ARG C 58  ? ARG C 58  . ? 1_555 ? 
33 AC6 8 ARG C 79  ? ARG C 79  . ? 1_555 ? 
34 AC6 8 ARG C 130 ? ARG C 130 . ? 1_555 ? 
35 AC6 8 LYS C 296 ? LYS C 296 . ? 1_555 ? 
36 AC6 8 ASP C 297 ? ASP C 297 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2PHL 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    2PHL 
_atom_sites.fract_transf_matrix[1][1]   0.011135 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.008766 
_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]   0.007295 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
P 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASP A 1 11  ? 33.237 25.134  87.202  1.00 60.05 ? 11  ASP A N   1 
ATOM   2    C CA  . ASP A 1 11  ? 32.421 25.065  85.994  1.00 58.83 ? 11  ASP A CA  1 
ATOM   3    C C   . ASP A 1 11  ? 32.335 23.641  85.450  1.00 52.41 ? 11  ASP A C   1 
ATOM   4    O O   . ASP A 1 11  ? 33.217 22.815  85.679  1.00 53.24 ? 11  ASP A O   1 
ATOM   5    C CB  . ASP A 1 11  ? 32.962 26.008  84.901  1.00 66.20 ? 11  ASP A CB  1 
ATOM   6    C CG  . ASP A 1 11  ? 32.425 27.440  85.026  1.00 71.49 ? 11  ASP A CG  1 
ATOM   7    O OD1 . ASP A 1 11  ? 31.263 27.693  84.618  1.00 71.32 ? 11  ASP A OD1 1 
ATOM   8    O OD2 . ASP A 1 11  ? 33.183 28.315  85.510  1.00 74.90 ? 11  ASP A OD2 1 
ATOM   9    N N   . ASN A 1 12  ? 31.274 23.389  84.693  1.00 43.60 ? 12  ASN A N   1 
ATOM   10   C CA  . ASN A 1 12  ? 31.025 22.091  84.105  1.00 32.90 ? 12  ASN A CA  1 
ATOM   11   C C   . ASN A 1 12  ? 31.437 22.230  82.654  1.00 29.28 ? 12  ASN A C   1 
ATOM   12   O O   . ASN A 1 12  ? 30.899 23.068  81.941  1.00 31.38 ? 12  ASN A O   1 
ATOM   13   C CB  . ASN A 1 12  ? 29.527 21.790  84.202  1.00 30.87 ? 12  ASN A CB  1 
ATOM   14   C CG  . ASN A 1 12  ? 29.193 20.354  83.878  1.00 31.72 ? 12  ASN A CG  1 
ATOM   15   O OD1 . ASN A 1 12  ? 29.916 19.688  83.126  1.00 34.26 ? 12  ASN A OD1 1 
ATOM   16   N ND2 . ASN A 1 12  ? 28.090 19.860  84.441  1.00 27.52 ? 12  ASN A ND2 1 
ATOM   17   N N   . PRO A 1 13  ? 32.453 21.475  82.218  1.00 28.57 ? 13  PRO A N   1 
ATOM   18   C CA  . PRO A 1 13  ? 32.904 21.565  80.816  1.00 28.16 ? 13  PRO A CA  1 
ATOM   19   C C   . PRO A 1 13  ? 32.004 20.871  79.793  1.00 25.51 ? 13  PRO A C   1 
ATOM   20   O O   . PRO A 1 13  ? 32.122 21.128  78.594  1.00 30.16 ? 13  PRO A O   1 
ATOM   21   C CB  . PRO A 1 13  ? 34.298 20.941  80.856  1.00 31.40 ? 13  PRO A CB  1 
ATOM   22   C CG  . PRO A 1 13  ? 34.237 20.008  82.035  1.00 25.68 ? 13  PRO A CG  1 
ATOM   23   C CD  . PRO A 1 13  ? 33.414 20.725  83.052  1.00 26.19 ? 13  PRO A CD  1 
ATOM   24   N N   . PHE A 1 14  ? 31.068 20.065  80.297  1.00 20.82 ? 14  PHE A N   1 
ATOM   25   C CA  . PHE A 1 14  ? 30.119 19.288  79.514  1.00 17.15 ? 14  PHE A CA  1 
ATOM   26   C C   . PHE A 1 14  ? 28.789 19.952  79.275  1.00 16.96 ? 14  PHE A C   1 
ATOM   27   O O   . PHE A 1 14  ? 27.939 19.378  78.622  1.00 21.61 ? 14  PHE A O   1 
ATOM   28   C CB  . PHE A 1 14  ? 29.858 17.958  80.212  1.00 12.49 ? 14  PHE A CB  1 
ATOM   29   C CG  . PHE A 1 14  ? 31.111 17.244  80.629  1.00 19.04 ? 14  PHE A CG  1 
ATOM   30   C CD1 . PHE A 1 14  ? 31.932 16.631  79.678  1.00 17.57 ? 14  PHE A CD1 1 
ATOM   31   C CD2 . PHE A 1 14  ? 31.524 17.260  81.965  1.00 12.29 ? 14  PHE A CD2 1 
ATOM   32   C CE1 . PHE A 1 14  ? 33.154 16.056  80.054  1.00 21.42 ? 14  PHE A CE1 1 
ATOM   33   C CE2 . PHE A 1 14  ? 32.730 16.694  82.344  1.00 12.54 ? 14  PHE A CE2 1 
ATOM   34   C CZ  . PHE A 1 14  ? 33.556 16.091  81.400  1.00 19.16 ? 14  PHE A CZ  1 
ATOM   35   N N   . TYR A 1 15  ? 28.605 21.159  79.791  1.00 21.50 ? 15  TYR A N   1 
ATOM   36   C CA  . TYR A 1 15  ? 27.345 21.887  79.654  1.00 21.05 ? 15  TYR A CA  1 
ATOM   37   C C   . TYR A 1 15  ? 27.449 23.065  78.681  1.00 22.37 ? 15  TYR A C   1 
ATOM   38   O O   . TYR A 1 15  ? 28.384 23.872  78.770  1.00 26.76 ? 15  TYR A O   1 
ATOM   39   C CB  . TYR A 1 15  ? 26.899 22.378  81.037  1.00 18.35 ? 15  TYR A CB  1 
ATOM   40   C CG  . TYR A 1 15  ? 25.573 23.089  81.046  1.00 17.31 ? 15  TYR A CG  1 
ATOM   41   C CD1 . TYR A 1 15  ? 24.398 22.417  80.733  1.00 17.20 ? 15  TYR A CD1 1 
ATOM   42   C CD2 . TYR A 1 15  ? 25.498 24.450  81.329  1.00 16.08 ? 15  TYR A CD2 1 
ATOM   43   C CE1 . TYR A 1 15  ? 23.191 23.079  80.696  1.00 13.02 ? 15  TYR A CE1 1 
ATOM   44   C CE2 . TYR A 1 15  ? 24.290 25.128  81.293  1.00 12.48 ? 15  TYR A CE2 1 
ATOM   45   C CZ  . TYR A 1 15  ? 23.148 24.440  80.978  1.00 18.47 ? 15  TYR A CZ  1 
ATOM   46   O OH  . TYR A 1 15  ? 21.959 25.122  80.937  1.00 26.00 ? 15  TYR A OH  1 
ATOM   47   N N   . PHE A 1 16  ? 26.501 23.144  77.751  1.00 22.41 ? 16  PHE A N   1 
ATOM   48   C CA  . PHE A 1 16  ? 26.456 24.213  76.752  1.00 23.79 ? 16  PHE A CA  1 
ATOM   49   C C   . PHE A 1 16  ? 25.135 24.990  76.885  1.00 26.13 ? 16  PHE A C   1 
ATOM   50   O O   . PHE A 1 16  ? 24.087 24.569  76.377  1.00 22.82 ? 16  PHE A O   1 
ATOM   51   C CB  . PHE A 1 16  ? 26.623 23.628  75.338  1.00 25.06 ? 16  PHE A CB  1 
ATOM   52   C CG  . PHE A 1 16  ? 28.004 23.100  75.062  1.00 27.35 ? 16  PHE A CG  1 
ATOM   53   C CD1 . PHE A 1 16  ? 28.458 21.923  75.681  1.00 20.37 ? 16  PHE A CD1 1 
ATOM   54   C CD2 . PHE A 1 16  ? 28.890 23.827  74.263  1.00 21.63 ? 16  PHE A CD2 1 
ATOM   55   C CE1 . PHE A 1 16  ? 29.775 21.493  75.513  1.00 21.69 ? 16  PHE A CE1 1 
ATOM   56   C CE2 . PHE A 1 16  ? 30.215 23.400  74.090  1.00 19.50 ? 16  PHE A CE2 1 
ATOM   57   C CZ  . PHE A 1 16  ? 30.657 22.237  74.715  1.00 23.27 ? 16  PHE A CZ  1 
ATOM   58   N N   . ASN A 1 17  ? 25.187 26.088  77.641  1.00 28.55 ? 17  ASN A N   1 
ATOM   59   C CA  . ASN A 1 17  ? 24.029 26.950  77.909  1.00 27.53 ? 17  ASN A CA  1 
ATOM   60   C C   . ASN A 1 17  ? 23.566 27.706  76.665  1.00 29.59 ? 17  ASN A C   1 
ATOM   61   O O   . ASN A 1 17  ? 24.241 28.627  76.196  1.00 31.75 ? 17  ASN A O   1 
ATOM   62   C CB  . ASN A 1 17  ? 24.393 27.927  79.031  1.00 27.30 ? 17  ASN A CB  1 
ATOM   63   C CG  . ASN A 1 17  ? 23.404 29.048  79.184  1.00 26.92 ? 17  ASN A CG  1 
ATOM   64   O OD1 . ASN A 1 17  ? 23.793 30.205  79.288  1.00 31.17 ? 17  ASN A OD1 1 
ATOM   65   N ND2 . ASN A 1 17  ? 22.124 28.722  79.209  1.00 29.42 ? 17  ASN A ND2 1 
ATOM   66   N N   . SER A 1 18  ? 22.401 27.332  76.150  1.00 28.52 ? 18  SER A N   1 
ATOM   67   C CA  . SER A 1 18  ? 21.850 27.945  74.950  1.00 30.16 ? 18  SER A CA  1 
ATOM   68   C C   . SER A 1 18  ? 22.002 29.450  74.910  1.00 29.27 ? 18  SER A C   1 
ATOM   69   O O   . SER A 1 18  ? 22.427 30.002  73.906  1.00 33.99 ? 18  SER A O   1 
ATOM   70   C CB  . SER A 1 18  ? 20.381 27.571  74.794  1.00 30.37 ? 18  SER A CB  1 
ATOM   71   O OG  . SER A 1 18  ? 19.626 28.053  75.891  1.00 40.79 ? 18  SER A OG  1 
ATOM   72   N N   . ASP A 1 19  ? 21.710 30.102  76.026  1.00 34.27 ? 19  ASP A N   1 
ATOM   73   C CA  . ASP A 1 19  ? 21.801 31.560  76.131  1.00 37.56 ? 19  ASP A CA  1 
ATOM   74   C C   . ASP A 1 19  ? 23.146 32.109  75.663  1.00 37.58 ? 19  ASP A C   1 
ATOM   75   O O   . ASP A 1 19  ? 23.270 33.302  75.383  1.00 37.74 ? 19  ASP A O   1 
ATOM   76   C CB  . ASP A 1 19  ? 21.519 32.020  77.567  1.00 43.82 ? 19  ASP A CB  1 
ATOM   77   C CG  . ASP A 1 19  ? 20.088 31.756  78.007  1.00 48.43 ? 19  ASP A CG  1 
ATOM   78   O OD1 . ASP A 1 19  ? 19.191 31.643  77.142  1.00 55.08 ? 19  ASP A OD1 1 
ATOM   79   O OD2 . ASP A 1 19  ? 19.859 31.682  79.232  1.00 57.72 ? 19  ASP A OD2 1 
ATOM   80   N N   . ASN A 1 20  ? 24.170 31.267  75.642  1.00 35.69 ? 20  ASN A N   1 
ATOM   81   C CA  . ASN A 1 20  ? 25.453 31.734  75.164  1.00 39.74 ? 20  ASN A CA  1 
ATOM   82   C C   . ASN A 1 20  ? 26.357 30.689  74.480  1.00 39.45 ? 20  ASN A C   1 
ATOM   83   O O   . ASN A 1 20  ? 27.583 30.808  74.502  1.00 41.17 ? 20  ASN A O   1 
ATOM   84   C CB  . ASN A 1 20  ? 26.185 32.536  76.250  1.00 44.77 ? 20  ASN A CB  1 
ATOM   85   C CG  . ASN A 1 20  ? 26.759 31.673  77.349  1.00 50.77 ? 20  ASN A CG  1 
ATOM   86   O OD1 . ASN A 1 20  ? 27.913 31.845  77.738  1.00 52.45 ? 20  ASN A OD1 1 
ATOM   87   N ND2 . ASN A 1 20  ? 25.955 30.769  77.884  1.00 56.72 ? 20  ASN A ND2 1 
ATOM   88   N N   . SER A 1 21  ? 25.750 29.718  73.794  1.00 36.78 ? 21  SER A N   1 
ATOM   89   C CA  . SER A 1 21  ? 26.524 28.693  73.091  1.00 35.04 ? 21  SER A CA  1 
ATOM   90   C C   . SER A 1 21  ? 26.264 28.565  71.587  1.00 34.88 ? 21  SER A C   1 
ATOM   91   O O   . SER A 1 21  ? 27.098 27.992  70.874  1.00 34.62 ? 21  SER A O   1 
ATOM   92   C CB  . SER A 1 21  ? 26.372 27.332  73.767  1.00 35.46 ? 21  SER A CB  1 
ATOM   93   O OG  . SER A 1 21  ? 27.114 27.283  74.976  1.00 41.33 ? 21  SER A OG  1 
ATOM   94   N N   . TRP A 1 22  ? 25.108 29.048  71.123  1.00 27.63 ? 22  TRP A N   1 
ATOM   95   C CA  . TRP A 1 22  ? 24.742 29.020  69.701  1.00 28.18 ? 22  TRP A CA  1 
ATOM   96   C C   . TRP A 1 22  ? 25.014 30.386  69.050  1.00 28.20 ? 22  TRP A C   1 
ATOM   97   O O   . TRP A 1 22  ? 25.040 31.411  69.732  1.00 32.90 ? 22  TRP A O   1 
ATOM   98   C CB  . TRP A 1 22  ? 23.242 28.758  69.534  1.00 25.56 ? 22  TRP A CB  1 
ATOM   99   C CG  . TRP A 1 22  ? 22.777 27.461  70.023  1.00 28.86 ? 22  TRP A CG  1 
ATOM   100  C CD1 . TRP A 1 22  ? 22.345 27.165  71.283  1.00 25.59 ? 22  TRP A CD1 1 
ATOM   101  C CD2 . TRP A 1 22  ? 22.652 26.254  69.256  1.00 32.85 ? 22  TRP A CD2 1 
ATOM   102  N NE1 . TRP A 1 22  ? 21.955 25.846  71.352  1.00 31.14 ? 22  TRP A NE1 1 
ATOM   103  C CE2 . TRP A 1 22  ? 22.138 25.262  70.121  1.00 34.91 ? 22  TRP A CE2 1 
ATOM   104  C CE3 . TRP A 1 22  ? 22.940 25.910  67.930  1.00 29.86 ? 22  TRP A CE3 1 
ATOM   105  C CZ2 . TRP A 1 22  ? 21.895 23.947  69.696  1.00 32.28 ? 22  TRP A CZ2 1 
ATOM   106  C CZ3 . TRP A 1 22  ? 22.701 24.609  67.515  1.00 31.01 ? 22  TRP A CZ3 1 
ATOM   107  C CH2 . TRP A 1 22  ? 22.187 23.642  68.395  1.00 29.63 ? 22  TRP A CH2 1 
ATOM   108  N N   . ASN A 1 23  ? 25.166 30.415  67.734  1.00 25.06 ? 23  ASN A N   1 
ATOM   109  C CA  . ASN A 1 23  ? 25.363 31.678  67.040  1.00 26.59 ? 23  ASN A CA  1 
ATOM   110  C C   . ASN A 1 23  ? 24.471 31.681  65.812  1.00 21.97 ? 23  ASN A C   1 
ATOM   111  O O   . ASN A 1 23  ? 24.383 30.670  65.140  1.00 22.08 ? 23  ASN A O   1 
ATOM   112  C CB  . ASN A 1 23  ? 26.827 31.872  66.659  1.00 36.00 ? 23  ASN A CB  1 
ATOM   113  C CG  . ASN A 1 23  ? 27.424 33.126  67.293  1.00 49.96 ? 23  ASN A CG  1 
ATOM   114  O OD1 . ASN A 1 23  ? 26.896 34.231  67.125  1.00 59.96 ? 23  ASN A OD1 1 
ATOM   115  N ND2 . ASN A 1 23  ? 28.510 32.959  68.047  1.00 52.93 ? 23  ASN A ND2 1 
ATOM   116  N N   . THR A 1 24  ? 23.785 32.789  65.541  1.00 20.13 ? 24  THR A N   1 
ATOM   117  C CA  . THR A 1 24  ? 22.873 32.896  64.398  1.00 25.01 ? 24  THR A CA  1 
ATOM   118  C C   . THR A 1 24  ? 23.573 33.062  63.057  1.00 22.86 ? 24  THR A C   1 
ATOM   119  O O   . THR A 1 24  ? 24.377 33.952  62.901  1.00 26.98 ? 24  THR A O   1 
ATOM   120  C CB  . THR A 1 24  ? 21.920 34.109  64.543  1.00 26.02 ? 24  THR A CB  1 
ATOM   121  O OG1 . THR A 1 24  ? 21.254 34.036  65.799  1.00 39.78 ? 24  THR A OG1 1 
ATOM   122  C CG2 . THR A 1 24  ? 20.857 34.107  63.451  1.00 31.90 ? 24  THR A CG2 1 
ATOM   123  N N   . LEU A 1 25  ? 23.297 32.189  62.107  1.00 21.08 ? 25  LEU A N   1 
ATOM   124  C CA  . LEU A 1 25  ? 23.880 32.313  60.772  1.00 22.06 ? 25  LEU A CA  1 
ATOM   125  C C   . LEU A 1 25  ? 22.987 33.304  60.012  1.00 22.33 ? 25  LEU A C   1 
ATOM   126  O O   . LEU A 1 25  ? 23.452 34.324  59.472  1.00 24.71 ? 25  LEU A O   1 
ATOM   127  C CB  . LEU A 1 25  ? 23.841 30.962  60.044  1.00 22.62 ? 25  LEU A CB  1 
ATOM   128  C CG  . LEU A 1 25  ? 25.126 30.392  59.457  1.00 29.41 ? 25  LEU A CG  1 
ATOM   129  C CD1 . LEU A 1 25  ? 25.699 31.309  58.402  1.00 33.46 ? 25  LEU A CD1 1 
ATOM   130  C CD2 . LEU A 1 25  ? 26.126 30.234  60.562  1.00 35.18 ? 25  LEU A CD2 1 
ATOM   131  N N   . PHE A 1 26  ? 21.689 33.008  60.039  1.00 20.27 ? 26  PHE A N   1 
ATOM   132  C CA  . PHE A 1 26  ? 20.671 33.778  59.358  1.00 20.13 ? 26  PHE A CA  1 
ATOM   133  C C   . PHE A 1 26  ? 19.374 33.736  60.157  1.00 22.56 ? 26  PHE A C   1 
ATOM   134  O O   . PHE A 1 26  ? 19.053 32.735  60.812  1.00 24.68 ? 26  PHE A O   1 
ATOM   135  C CB  . PHE A 1 26  ? 20.413 33.176  57.955  1.00 15.54 ? 26  PHE A CB  1 
ATOM   136  C CG  . PHE A 1 26  ? 19.262 33.827  57.221  1.00 17.68 ? 26  PHE A CG  1 
ATOM   137  C CD1 . PHE A 1 26  ? 19.459 34.999  56.485  1.00 21.51 ? 26  PHE A CD1 1 
ATOM   138  C CD2 . PHE A 1 26  ? 17.965 33.339  57.359  1.00 22.71 ? 26  PHE A CD2 1 
ATOM   139  C CE1 . PHE A 1 26  ? 18.386 35.684  55.913  1.00 14.99 ? 26  PHE A CE1 1 
ATOM   140  C CE2 . PHE A 1 26  ? 16.880 34.013  56.792  1.00 22.35 ? 26  PHE A CE2 1 
ATOM   141  C CZ  . PHE A 1 26  ? 17.093 35.192  56.070  1.00 23.87 ? 26  PHE A CZ  1 
ATOM   142  N N   . LYS A 1 27  ? 18.612 34.818  60.096  1.00 24.96 ? 27  LYS A N   1 
ATOM   143  C CA  . LYS A 1 27  ? 17.327 34.861  60.786  1.00 29.26 ? 27  LYS A CA  1 
ATOM   144  C C   . LYS A 1 27  ? 16.424 35.921  60.184  1.00 26.95 ? 27  LYS A C   1 
ATOM   145  O O   . LYS A 1 27  ? 16.856 37.030  59.880  1.00 30.63 ? 27  LYS A O   1 
ATOM   146  C CB  . LYS A 1 27  ? 17.504 35.122  62.293  1.00 30.88 ? 27  LYS A CB  1 
ATOM   147  C CG  . LYS A 1 27  ? 17.600 36.589  62.702  1.00 35.77 ? 27  LYS A CG  1 
ATOM   148  C CD  . LYS A 1 27  ? 17.476 36.706  64.189  1.00 41.76 ? 27  LYS A CD  1 
ATOM   149  C CE  . LYS A 1 27  ? 16.214 35.982  64.665  1.00 48.66 ? 27  LYS A CE  1 
ATOM   150  N NZ  . LYS A 1 27  ? 16.115 35.915  66.165  1.00 60.69 ? 27  LYS A NZ  1 
ATOM   151  N N   . ASN A 1 28  ? 15.181 35.571  59.947  1.00 23.20 ? 28  ASN A N   1 
ATOM   152  C CA  . ASN A 1 28  ? 14.278 36.556  59.413  1.00 27.72 ? 28  ASN A CA  1 
ATOM   153  C C   . ASN A 1 28  ? 12.885 36.194  59.877  1.00 30.06 ? 28  ASN A C   1 
ATOM   154  O O   . ASN A 1 28  ? 12.686 35.143  60.489  1.00 32.63 ? 28  ASN A O   1 
ATOM   155  C CB  . ASN A 1 28  ? 14.427 36.732  57.874  1.00 27.13 ? 28  ASN A CB  1 
ATOM   156  C CG  . ASN A 1 28  ? 13.661 35.700  57.041  1.00 29.18 ? 28  ASN A CG  1 
ATOM   157  O OD1 . ASN A 1 28  ? 13.094 34.743  57.557  1.00 26.98 ? 28  ASN A OD1 1 
ATOM   158  N ND2 . ASN A 1 28  ? 13.643 35.916  55.725  1.00 19.32 ? 28  ASN A ND2 1 
ATOM   159  N N   . GLN A 1 29  ? 11.949 37.108  59.682  1.00 27.69 ? 29  GLN A N   1 
ATOM   160  C CA  . GLN A 1 29  ? 10.568 36.903  60.078  1.00 26.88 ? 29  GLN A CA  1 
ATOM   161  C C   . GLN A 1 29  ? 9.944  35.525  59.759  1.00 25.81 ? 29  GLN A C   1 
ATOM   162  O O   . GLN A 1 29  ? 8.841  35.237  60.214  1.00 29.67 ? 29  GLN A O   1 
ATOM   163  C CB  . GLN A 1 29  ? 9.721  38.034  59.497  1.00 26.78 ? 29  GLN A CB  1 
ATOM   164  C CG  . GLN A 1 29  ? 10.185 38.529  58.128  1.00 26.48 ? 29  GLN A CG  1 
ATOM   165  C CD  . GLN A 1 29  ? 9.016  38.847  57.248  1.00 32.15 ? 29  GLN A CD  1 
ATOM   166  O OE1 . GLN A 1 29  ? 7.890  38.543  57.590  1.00 36.72 ? 29  GLN A OE1 1 
ATOM   167  N NE2 . GLN A 1 29  ? 9.271  39.450  56.098  1.00 45.40 ? 29  GLN A NE2 1 
ATOM   168  N N   . TYR A 1 30  ? 10.644 34.675  59.007  1.00 22.53 ? 30  TYR A N   1 
ATOM   169  C CA  . TYR A 1 30  ? 10.126 33.357  58.668  1.00 20.50 ? 30  TYR A CA  1 
ATOM   170  C C   . TYR A 1 30  ? 10.898 32.208  59.279  1.00 21.19 ? 30  TYR A C   1 
ATOM   171  O O   . TYR A 1 30  ? 10.407 31.089  59.280  1.00 27.79 ? 30  TYR A O   1 
ATOM   172  C CB  . TYR A 1 30  ? 10.076 33.160  57.156  1.00 19.10 ? 30  TYR A CB  1 
ATOM   173  C CG  . TYR A 1 30  ? 9.101  34.070  56.456  1.00 23.39 ? 30  TYR A CG  1 
ATOM   174  C CD1 . TYR A 1 30  ? 7.726  33.856  56.552  1.00 23.43 ? 30  TYR A CD1 1 
ATOM   175  C CD2 . TYR A 1 30  ? 9.550  35.167  55.715  1.00 18.70 ? 30  TYR A CD2 1 
ATOM   176  C CE1 . TYR A 1 30  ? 6.831  34.706  55.939  1.00 23.43 ? 30  TYR A CE1 1 
ATOM   177  C CE2 . TYR A 1 30  ? 8.662  36.022  55.102  1.00 21.20 ? 30  TYR A CE2 1 
ATOM   178  C CZ  . TYR A 1 30  ? 7.308  35.793  55.217  1.00 23.97 ? 30  TYR A CZ  1 
ATOM   179  O OH  . TYR A 1 30  ? 6.429  36.670  54.629  1.00 29.70 ? 30  TYR A OH  1 
ATOM   180  N N   . GLY A 1 31  ? 12.115 32.457  59.749  1.00 22.83 ? 31  GLY A N   1 
ATOM   181  C CA  . GLY A 1 31  ? 12.895 31.395  60.354  1.00 19.33 ? 31  GLY A CA  1 
ATOM   182  C C   . GLY A 1 31  ? 14.295 31.800  60.791  1.00 21.09 ? 31  GLY A C   1 
ATOM   183  O O   . GLY A 1 31  ? 14.635 33.008  60.803  1.00 18.20 ? 31  GLY A O   1 
ATOM   184  N N   . HIS A 1 32  ? 15.092 30.796  61.182  1.00 14.05 ? 32  HIS A N   1 
ATOM   185  C CA  . HIS A 1 32  ? 16.472 31.007  61.619  1.00 16.91 ? 32  HIS A CA  1 
ATOM   186  C C   . HIS A 1 32  ? 17.343 29.754  61.545  1.00 18.43 ? 32  HIS A C   1 
ATOM   187  O O   . HIS A 1 32  ? 16.843 28.622  61.536  1.00 20.18 ? 32  HIS A O   1 
ATOM   188  C CB  . HIS A 1 32  ? 16.532 31.563  63.056  1.00 23.80 ? 32  HIS A CB  1 
ATOM   189  C CG  . HIS A 1 32  ? 16.063 30.603  64.109  1.00 22.53 ? 32  HIS A CG  1 
ATOM   190  N ND1 . HIS A 1 32  ? 14.793 30.644  64.638  1.00 23.87 ? 32  HIS A ND1 1 
ATOM   191  C CD2 . HIS A 1 32  ? 16.716 29.622  64.780  1.00 28.09 ? 32  HIS A CD2 1 
ATOM   192  C CE1 . HIS A 1 32  ? 14.684 29.742  65.596  1.00 27.08 ? 32  HIS A CE1 1 
ATOM   193  N NE2 . HIS A 1 32  ? 15.838 29.110  65.703  1.00 20.51 ? 32  HIS A NE2 1 
ATOM   194  N N   . ILE A 1 33  ? 18.652 29.989  61.531  1.00 21.46 ? 33  ILE A N   1 
ATOM   195  C CA  . ILE A 1 33  ? 19.682 28.955  61.480  1.00 24.34 ? 33  ILE A CA  1 
ATOM   196  C C   . ILE A 1 33  ? 20.785 29.457  62.420  1.00 28.64 ? 33  ILE A C   1 
ATOM   197  O O   . ILE A 1 33  ? 21.226 30.603  62.291  1.00 34.70 ? 33  ILE A O   1 
ATOM   198  C CB  . ILE A 1 33  ? 20.346 28.848  60.066  1.00 24.39 ? 33  ILE A CB  1 
ATOM   199  C CG1 . ILE A 1 33  ? 19.308 28.533  58.984  1.00 23.55 ? 33  ILE A CG1 1 
ATOM   200  C CG2 . ILE A 1 33  ? 21.497 27.826  60.093  1.00 18.52 ? 33  ILE A CG2 1 
ATOM   201  C CD1 . ILE A 1 33  ? 19.817 28.726  57.570  1.00 21.34 ? 33  ILE A CD1 1 
ATOM   202  N N   . ARG A 1 34  ? 21.187 28.642  63.386  1.00 25.31 ? 34  ARG A N   1 
ATOM   203  C CA  . ARG A 1 34  ? 22.257 29.014  64.291  1.00 23.49 ? 34  ARG A CA  1 
ATOM   204  C C   . ARG A 1 34  ? 23.173 27.800  64.281  1.00 23.96 ? 34  ARG A C   1 
ATOM   205  O O   . ARG A 1 34  ? 22.710 26.691  64.014  1.00 24.14 ? 34  ARG A O   1 
ATOM   206  C CB  . ARG A 1 34  ? 21.763 29.168  65.743  1.00 27.92 ? 34  ARG A CB  1 
ATOM   207  C CG  . ARG A 1 34  ? 20.463 29.895  66.001  1.00 32.01 ? 34  ARG A CG  1 
ATOM   208  C CD  . ARG A 1 34  ? 20.197 29.888  67.513  1.00 46.66 ? 34  ARG A CD  1 
ATOM   209  N NE  . ARG A 1 34  ? 18.771 29.835  67.860  1.00 59.76 ? 34  ARG A NE  1 
ATOM   210  C CZ  . ARG A 1 34  ? 18.254 29.139  68.880  1.00 63.12 ? 34  ARG A CZ  1 
ATOM   211  N NH1 . ARG A 1 34  ? 19.020 28.390  69.667  1.00 61.46 ? 34  ARG A NH1 1 
ATOM   212  N NH2 . ARG A 1 34  ? 16.947 29.169  69.099  1.00 66.75 ? 34  ARG A NH2 1 
ATOM   213  N N   . VAL A 1 35  ? 24.456 27.993  64.583  1.00 22.04 ? 35  VAL A N   1 
ATOM   214  C CA  . VAL A 1 35  ? 25.395 26.866  64.679  1.00 23.50 ? 35  VAL A CA  1 
ATOM   215  C C   . VAL A 1 35  ? 25.979 26.815  66.098  1.00 22.33 ? 35  VAL A C   1 
ATOM   216  O O   . VAL A 1 35  ? 26.284 27.859  66.692  1.00 19.38 ? 35  VAL A O   1 
ATOM   217  C CB  . VAL A 1 35  ? 26.573 26.970  63.694  1.00 22.77 ? 35  VAL A CB  1 
ATOM   218  C CG1 . VAL A 1 35  ? 27.465 25.742  63.836  1.00 25.38 ? 35  VAL A CG1 1 
ATOM   219  C CG2 . VAL A 1 35  ? 26.050 27.067  62.256  1.00 27.78 ? 35  VAL A CG2 1 
ATOM   220  N N   . LEU A 1 36  ? 26.115 25.610  66.644  1.00 18.30 ? 36  LEU A N   1 
ATOM   221  C CA  . LEU A 1 36  ? 26.683 25.460  67.972  1.00 13.79 ? 36  LEU A CA  1 
ATOM   222  C C   . LEU A 1 36  ? 28.196 25.689  67.898  1.00 14.17 ? 36  LEU A C   1 
ATOM   223  O O   . LEU A 1 36  ? 28.843 25.333  66.915  1.00 13.25 ? 36  LEU A O   1 
ATOM   224  C CB  . LEU A 1 36  ? 26.387 24.057  68.537  1.00 20.52 ? 36  LEU A CB  1 
ATOM   225  C CG  . LEU A 1 36  ? 27.010 23.719  69.920  1.00 19.36 ? 36  LEU A CG  1 
ATOM   226  C CD1 . LEU A 1 36  ? 26.438 24.631  71.002  1.00 18.85 ? 36  LEU A CD1 1 
ATOM   227  C CD2 . LEU A 1 36  ? 26.754 22.292  70.300  1.00 18.95 ? 36  LEU A CD2 1 
ATOM   228  N N   . GLN A 1 37  ? 28.757 26.293  68.929  1.00 12.93 ? 37  GLN A N   1 
ATOM   229  C CA  . GLN A 1 37  ? 30.196 26.539  68.990  1.00 16.26 ? 37  GLN A CA  1 
ATOM   230  C C   . GLN A 1 37  ? 30.960 25.219  68.995  1.00 15.71 ? 37  GLN A C   1 
ATOM   231  O O   . GLN A 1 37  ? 30.364 24.165  69.201  1.00 20.75 ? 37  GLN A O   1 
ATOM   232  C CB  . GLN A 1 37  ? 30.537 27.302  70.274  1.00 24.86 ? 37  GLN A CB  1 
ATOM   233  C CG  . GLN A 1 37  ? 30.186 26.543  71.541  1.00 36.09 ? 37  GLN A CG  1 
ATOM   234  C CD  . GLN A 1 37  ? 30.779 27.181  72.786  1.00 43.57 ? 37  GLN A CD  1 
ATOM   235  O OE1 . GLN A 1 37  ? 31.437 26.512  73.587  1.00 48.34 ? 37  GLN A OE1 1 
ATOM   236  N NE2 . GLN A 1 37  ? 30.551 28.481  72.954  1.00 43.51 ? 37  GLN A NE2 1 
ATOM   237  N N   . ARG A 1 38  ? 32.278 25.285  68.819  1.00 12.04 ? 38  ARG A N   1 
ATOM   238  C CA  . ARG A 1 38  ? 33.121 24.098  68.809  1.00 20.17 ? 38  ARG A CA  1 
ATOM   239  C C   . ARG A 1 38  ? 33.281 23.460  70.180  1.00 26.05 ? 38  ARG A C   1 
ATOM   240  O O   . ARG A 1 38  ? 33.589 24.125  71.162  1.00 31.86 ? 38  ARG A O   1 
ATOM   241  C CB  . ARG A 1 38  ? 34.501 24.418  68.233  1.00 20.26 ? 38  ARG A CB  1 
ATOM   242  C CG  . ARG A 1 38  ? 34.478 24.624  66.725  1.00 27.45 ? 38  ARG A CG  1 
ATOM   243  C CD  . ARG A 1 38  ? 35.814 25.093  66.194  1.00 30.14 ? 38  ARG A CD  1 
ATOM   244  N NE  . ARG A 1 38  ? 36.848 24.099  66.445  1.00 39.68 ? 38  ARG A NE  1 
ATOM   245  C CZ  . ARG A 1 38  ? 38.049 24.120  65.879  1.00 40.07 ? 38  ARG A CZ  1 
ATOM   246  N NH1 . ARG A 1 38  ? 38.361 25.094  65.030  1.00 40.50 ? 38  ARG A NH1 1 
ATOM   247  N NH2 . ARG A 1 38  ? 38.913 23.142  66.121  1.00 37.75 ? 38  ARG A NH2 1 
ATOM   248  N N   . PHE A 1 39  ? 33.159 22.147  70.221  1.00 29.68 ? 39  PHE A N   1 
ATOM   249  C CA  . PHE A 1 39  ? 33.287 21.425  71.465  1.00 28.56 ? 39  PHE A CA  1 
ATOM   250  C C   . PHE A 1 39  ? 34.695 21.511  72.077  1.00 31.91 ? 39  PHE A C   1 
ATOM   251  O O   . PHE A 1 39  ? 34.856 21.807  73.270  1.00 34.73 ? 39  PHE A O   1 
ATOM   252  C CB  . PHE A 1 39  ? 32.906 19.977  71.214  1.00 32.95 ? 39  PHE A CB  1 
ATOM   253  C CG  . PHE A 1 39  ? 31.542 19.812  70.609  1.00 32.53 ? 39  PHE A CG  1 
ATOM   254  C CD1 . PHE A 1 39  ? 30.403 20.021  71.371  1.00 24.24 ? 39  PHE A CD1 1 
ATOM   255  C CD2 . PHE A 1 39  ? 31.396 19.414  69.280  1.00 34.91 ? 39  PHE A CD2 1 
ATOM   256  C CE1 . PHE A 1 39  ? 29.140 19.830  70.824  1.00 27.72 ? 39  PHE A CE1 1 
ATOM   257  C CE2 . PHE A 1 39  ? 30.132 19.224  68.726  1.00 30.58 ? 39  PHE A CE2 1 
ATOM   258  C CZ  . PHE A 1 39  ? 29.003 19.429  69.499  1.00 26.91 ? 39  PHE A CZ  1 
ATOM   259  N N   . ASP A 1 40  ? 35.711 21.259  71.257  1.00 32.92 ? 40  ASP A N   1 
ATOM   260  C CA  . ASP A 1 40  ? 37.105 21.275  71.701  1.00 29.74 ? 40  ASP A CA  1 
ATOM   261  C C   . ASP A 1 40  ? 37.568 22.654  72.156  1.00 33.76 ? 40  ASP A C   1 
ATOM   262  O O   . ASP A 1 40  ? 38.606 22.781  72.814  1.00 36.00 ? 40  ASP A O   1 
ATOM   263  C CB  . ASP A 1 40  ? 38.032 20.739  70.598  1.00 29.06 ? 40  ASP A CB  1 
ATOM   264  C CG  . ASP A 1 40  ? 38.064 21.630  69.363  1.00 16.13 ? 40  ASP A CG  1 
ATOM   265  O OD1 . ASP A 1 40  ? 36.994 21.910  68.813  1.00 25.04 ? 40  ASP A OD1 1 
ATOM   266  O OD2 . ASP A 1 40  ? 39.157 22.050  68.933  1.00 22.22 ? 40  ASP A OD2 1 
ATOM   267  N N   . GLN A 1 41  ? 36.819 23.689  71.790  1.00 31.17 ? 41  GLN A N   1 
ATOM   268  C CA  . GLN A 1 41  ? 37.186 25.029  72.199  1.00 30.76 ? 41  GLN A CA  1 
ATOM   269  C C   . GLN A 1 41  ? 36.689 25.323  73.594  1.00 32.58 ? 41  GLN A C   1 
ATOM   270  O O   . GLN A 1 41  ? 37.352 26.012  74.363  1.00 29.36 ? 41  GLN A O   1 
ATOM   271  C CB  . GLN A 1 41  ? 36.680 26.051  71.217  1.00 34.17 ? 41  GLN A CB  1 
ATOM   272  C CG  . GLN A 1 41  ? 37.809 26.588  70.393  1.00 50.32 ? 41  GLN A CG  1 
ATOM   273  C CD  . GLN A 1 41  ? 37.392 26.853  68.975  1.00 62.26 ? 41  GLN A CD  1 
ATOM   274  O OE1 . GLN A 1 41  ? 38.043 26.394  68.037  1.00 66.70 ? 41  GLN A OE1 1 
ATOM   275  N NE2 . GLN A 1 41  ? 36.273 27.568  68.803  1.00 66.43 ? 41  GLN A NE2 1 
ATOM   276  N N   . GLN A 1 42  ? 35.509 24.817  73.928  1.00 35.06 ? 42  GLN A N   1 
ATOM   277  C CA  . GLN A 1 42  ? 35.007 25.016  75.269  1.00 32.73 ? 42  GLN A CA  1 
ATOM   278  C C   . GLN A 1 42  ? 36.028 24.350  76.181  1.00 32.37 ? 42  GLN A C   1 
ATOM   279  O O   . GLN A 1 42  ? 36.392 24.907  77.222  1.00 40.01 ? 42  GLN A O   1 
ATOM   280  C CB  . GLN A 1 42  ? 33.634 24.368  75.457  1.00 31.04 ? 42  GLN A CB  1 
ATOM   281  C CG  . GLN A 1 42  ? 33.240 24.208  76.929  1.00 35.54 ? 42  GLN A CG  1 
ATOM   282  C CD  . GLN A 1 42  ? 31.804 24.588  77.203  1.00 39.03 ? 42  GLN A CD  1 
ATOM   283  O OE1 . GLN A 1 42  ? 31.326 25.629  76.753  1.00 43.35 ? 42  GLN A OE1 1 
ATOM   284  N NE2 . GLN A 1 42  ? 31.102 23.741  77.932  1.00 41.06 ? 42  GLN A NE2 1 
ATOM   285  N N   . SER A 1 43  ? 36.535 23.188  75.775  1.00 29.82 ? 43  SER A N   1 
ATOM   286  C CA  . SER A 1 43  ? 37.502 22.479  76.600  1.00 31.39 ? 43  SER A CA  1 
ATOM   287  C C   . SER A 1 43  ? 38.220 21.334  75.900  1.00 32.64 ? 43  SER A C   1 
ATOM   288  O O   . SER A 1 43  ? 37.616 20.557  75.158  1.00 36.47 ? 43  SER A O   1 
ATOM   289  C CB  . SER A 1 43  ? 36.820 21.997  77.912  1.00 34.28 ? 43  SER A CB  1 
ATOM   290  O OG  . SER A 1 43  ? 36.878 20.592  78.144  1.00 26.04 ? 43  SER A OG  1 
ATOM   291  N N   . LYS A 1 44  ? 39.510 21.215  76.188  1.00 31.98 ? 44  LYS A N   1 
ATOM   292  C CA  . LYS A 1 44  ? 40.332 20.166  75.621  1.00 33.33 ? 44  LYS A CA  1 
ATOM   293  C C   . LYS A 1 44  ? 39.845 18.773  75.982  1.00 32.68 ? 44  LYS A C   1 
ATOM   294  O O   . LYS A 1 44  ? 40.176 17.828  75.296  1.00 33.25 ? 44  LYS A O   1 
ATOM   295  C CB  . LYS A 1 44  ? 41.778 20.319  76.070  1.00 35.84 ? 44  LYS A CB  1 
ATOM   296  C CG  . LYS A 1 44  ? 42.508 21.484  75.433  1.00 47.04 ? 44  LYS A CG  1 
ATOM   297  C CD  . LYS A 1 44  ? 43.746 21.864  76.239  1.00 57.66 ? 44  LYS A CD  1 
ATOM   298  C CE  . LYS A 1 44  ? 43.380 22.731  77.451  1.00 65.29 ? 44  LYS A CE  1 
ATOM   299  N NZ  . LYS A 1 44  ? 42.337 22.141  78.360  1.00 67.85 ? 44  LYS A NZ  1 
ATOM   300  N N   . ARG A 1 45  ? 39.095 18.622  77.072  1.00 35.17 ? 45  ARG A N   1 
ATOM   301  C CA  . ARG A 1 45  ? 38.596 17.294  77.448  1.00 35.75 ? 45  ARG A CA  1 
ATOM   302  C C   . ARG A 1 45  ? 37.764 16.769  76.293  1.00 36.96 ? 45  ARG A C   1 
ATOM   303  O O   . ARG A 1 45  ? 37.732 15.563  76.032  1.00 38.82 ? 45  ARG A O   1 
ATOM   304  C CB  . ARG A 1 45  ? 37.645 17.347  78.638  1.00 36.13 ? 45  ARG A CB  1 
ATOM   305  C CG  . ARG A 1 45  ? 38.156 17.884  79.918  1.00 33.72 ? 45  ARG A CG  1 
ATOM   306  C CD  . ARG A 1 45  ? 37.179 17.438  80.984  1.00 33.62 ? 45  ARG A CD  1 
ATOM   307  N NE  . ARG A 1 45  ? 37.380 18.128  82.243  1.00 36.14 ? 45  ARG A NE  1 
ATOM   308  C CZ  . ARG A 1 45  ? 37.398 17.536  83.430  1.00 37.53 ? 45  ARG A CZ  1 
ATOM   309  N NH1 . ARG A 1 45  ? 37.243 16.218  83.542  1.00 36.99 ? 45  ARG A NH1 1 
ATOM   310  N NH2 . ARG A 1 45  ? 37.581 18.275  84.513  1.00 40.39 ? 45  ARG A NH2 1 
ATOM   311  N N   . LEU A 1 46  ? 37.070 17.704  75.644  1.00 35.06 ? 46  LEU A N   1 
ATOM   312  C CA  . LEU A 1 46  ? 36.168 17.449  74.525  1.00 33.13 ? 46  LEU A CA  1 
ATOM   313  C C   . LEU A 1 46  ? 36.880 17.410  73.171  1.00 34.28 ? 46  LEU A C   1 
ATOM   314  O O   . LEU A 1 46  ? 36.272 17.715  72.139  1.00 33.15 ? 46  LEU A O   1 
ATOM   315  C CB  . LEU A 1 46  ? 35.089 18.548  74.504  1.00 29.49 ? 46  LEU A CB  1 
ATOM   316  C CG  . LEU A 1 46  ? 33.812 18.447  75.351  1.00 26.86 ? 46  LEU A CG  1 
ATOM   317  C CD1 . LEU A 1 46  ? 34.081 17.950  76.750  1.00 23.36 ? 46  LEU A CD1 1 
ATOM   318  C CD2 . LEU A 1 46  ? 33.136 19.789  75.391  1.00 23.44 ? 46  LEU A CD2 1 
ATOM   319  N N   . GLN A 1 47  ? 38.138 16.984  73.160  1.00 36.26 ? 47  GLN A N   1 
ATOM   320  C CA  . GLN A 1 47  ? 38.912 16.957  71.915  1.00 38.72 ? 47  GLN A CA  1 
ATOM   321  C C   . GLN A 1 47  ? 38.503 15.954  70.848  1.00 37.58 ? 47  GLN A C   1 
ATOM   322  O O   . GLN A 1 47  ? 38.681 16.219  69.663  1.00 40.09 ? 47  GLN A O   1 
ATOM   323  C CB  . GLN A 1 47  ? 40.405 16.788  72.181  1.00 44.55 ? 47  GLN A CB  1 
ATOM   324  C CG  . GLN A 1 47  ? 40.814 15.384  72.554  1.00 49.92 ? 47  GLN A CG  1 
ATOM   325  C CD  . GLN A 1 47  ? 42.279 15.169  72.310  1.00 53.91 ? 47  GLN A CD  1 
ATOM   326  O OE1 . GLN A 1 47  ? 43.115 15.588  73.110  1.00 55.59 ? 47  GLN A OE1 1 
ATOM   327  N NE2 . GLN A 1 47  ? 42.609 14.524  71.194  1.00 54.35 ? 47  GLN A NE2 1 
ATOM   328  N N   . ASN A 1 48  ? 37.989 14.797  71.235  1.00 30.29 ? 48  ASN A N   1 
ATOM   329  C CA  . ASN A 1 48  ? 37.596 13.837  70.224  1.00 24.95 ? 48  ASN A CA  1 
ATOM   330  C C   . ASN A 1 48  ? 36.279 14.178  69.555  1.00 25.85 ? 48  ASN A C   1 
ATOM   331  O O   . ASN A 1 48  ? 35.664 13.323  68.933  1.00 30.31 ? 48  ASN A O   1 
ATOM   332  C CB  . ASN A 1 48  ? 37.574 12.434  70.798  1.00 19.50 ? 48  ASN A CB  1 
ATOM   333  C CG  . ASN A 1 48  ? 38.954 11.878  70.951  1.00 26.83 ? 48  ASN A CG  1 
ATOM   334  O OD1 . ASN A 1 48  ? 39.922 12.458  70.452  1.00 32.74 ? 48  ASN A OD1 1 
ATOM   335  N ND2 . ASN A 1 48  ? 39.072 10.763  71.646  1.00 29.14 ? 48  ASN A ND2 1 
ATOM   336  N N   . LEU A 1 49  ? 35.826 15.417  69.733  1.00 23.28 ? 49  LEU A N   1 
ATOM   337  C CA  . LEU A 1 49  ? 34.601 15.907  69.124  1.00 21.08 ? 49  LEU A CA  1 
ATOM   338  C C   . LEU A 1 49  ? 34.953 17.077  68.203  1.00 20.07 ? 49  LEU A C   1 
ATOM   339  O O   . LEU A 1 49  ? 34.075 17.651  67.587  1.00 13.30 ? 49  LEU A O   1 
ATOM   340  C CB  . LEU A 1 49  ? 33.578 16.381  70.178  1.00 18.84 ? 49  LEU A CB  1 
ATOM   341  C CG  . LEU A 1 49  ? 32.812 15.278  70.922  1.00 24.88 ? 49  LEU A CG  1 
ATOM   342  C CD1 . LEU A 1 49  ? 31.772 15.875  71.802  1.00 14.58 ? 49  LEU A CD1 1 
ATOM   343  C CD2 . LEU A 1 49  ? 32.182 14.279  69.934  1.00 22.22 ? 49  LEU A CD2 1 
ATOM   344  N N   . GLU A 1 50  ? 36.239 17.379  68.062  1.00 17.58 ? 50  GLU A N   1 
ATOM   345  C CA  . GLU A 1 50  ? 36.658 18.505  67.240  1.00 27.41 ? 50  GLU A CA  1 
ATOM   346  C C   . GLU A 1 50  ? 36.069 18.461  65.826  1.00 29.72 ? 50  GLU A C   1 
ATOM   347  O O   . GLU A 1 50  ? 35.854 19.504  65.196  1.00 30.75 ? 50  GLU A O   1 
ATOM   348  C CB  . GLU A 1 50  ? 38.186 18.573  67.143  1.00 31.54 ? 50  GLU A CB  1 
ATOM   349  C CG  . GLU A 1 50  ? 38.682 19.777  66.312  1.00 44.92 ? 50  GLU A CG  1 
ATOM   350  C CD  . GLU A 1 50  ? 40.168 19.739  65.987  1.00 49.86 ? 50  GLU A CD  1 
ATOM   351  O OE1 . GLU A 1 50  ? 40.779 18.654  66.137  1.00 52.14 ? 50  GLU A OE1 1 
ATOM   352  O OE2 . GLU A 1 50  ? 40.710 20.794  65.561  1.00 48.67 ? 50  GLU A OE2 1 
ATOM   353  N N   . ASP A 1 51  ? 35.734 17.261  65.370  1.00 26.46 ? 51  ASP A N   1 
ATOM   354  C CA  . ASP A 1 51  ? 35.226 17.086  64.031  1.00 26.34 ? 51  ASP A CA  1 
ATOM   355  C C   . ASP A 1 51  ? 33.734 17.134  63.841  1.00 24.34 ? 51  ASP A C   1 
ATOM   356  O O   . ASP A 1 51  ? 33.273 16.934  62.730  1.00 24.27 ? 51  ASP A O   1 
ATOM   357  C CB  . ASP A 1 51  ? 35.756 15.778  63.462  1.00 36.95 ? 51  ASP A CB  1 
ATOM   358  C CG  . ASP A 1 51  ? 37.267 15.766  63.331  1.00 43.99 ? 51  ASP A CG  1 
ATOM   359  O OD1 . ASP A 1 51  ? 37.844 16.828  62.986  1.00 49.82 ? 51  ASP A OD1 1 
ATOM   360  O OD2 . ASP A 1 51  ? 37.869 14.686  63.552  1.00 49.57 ? 51  ASP A OD2 1 
ATOM   361  N N   . TYR A 1 52  ? 32.964 17.340  64.897  1.00 17.64 ? 52  TYR A N   1 
ATOM   362  C CA  . TYR A 1 52  ? 31.511 17.392  64.734  1.00 15.07 ? 52  TYR A CA  1 
ATOM   363  C C   . TYR A 1 52  ? 30.916 18.720  65.102  1.00 12.98 ? 52  TYR A C   1 
ATOM   364  O O   . TYR A 1 52  ? 31.483 19.448  65.902  1.00 21.67 ? 52  TYR A O   1 
ATOM   365  C CB  . TYR A 1 52  ? 30.835 16.306  65.546  1.00 14.48 ? 52  TYR A CB  1 
ATOM   366  C CG  . TYR A 1 52  ? 31.313 14.943  65.185  1.00 20.15 ? 52  TYR A CG  1 
ATOM   367  C CD1 . TYR A 1 52  ? 32.494 14.448  65.728  1.00 20.42 ? 52  TYR A CD1 1 
ATOM   368  C CD2 . TYR A 1 52  ? 30.579 14.131  64.321  1.00 20.58 ? 52  TYR A CD2 1 
ATOM   369  C CE1 . TYR A 1 52  ? 32.940 13.178  65.431  1.00 16.76 ? 52  TYR A CE1 1 
ATOM   370  C CE2 . TYR A 1 52  ? 31.016 12.854  64.011  1.00 23.89 ? 52  TYR A CE2 1 
ATOM   371  C CZ  . TYR A 1 52  ? 32.200 12.384  64.573  1.00 26.24 ? 52  TYR A CZ  1 
ATOM   372  O OH  . TYR A 1 52  ? 32.645 11.111  64.295  1.00 33.78 ? 52  TYR A OH  1 
ATOM   373  N N   . ARG A 1 53  ? 29.743 19.004  64.574  1.00 12.31 ? 53  ARG A N   1 
ATOM   374  C CA  . ARG A 1 53  ? 29.091 20.264  64.874  1.00 18.63 ? 53  ARG A CA  1 
ATOM   375  C C   . ARG A 1 53  ? 27.589 20.039  64.920  1.00 19.82 ? 53  ARG A C   1 
ATOM   376  O O   . ARG A 1 53  ? 27.101 18.999  64.453  1.00 24.15 ? 53  ARG A O   1 
ATOM   377  C CB  . ARG A 1 53  ? 29.414 21.332  63.815  1.00 14.65 ? 53  ARG A CB  1 
ATOM   378  C CG  . ARG A 1 53  ? 30.906 21.702  63.675  1.00 14.79 ? 53  ARG A CG  1 
ATOM   379  C CD  . ARG A 1 53  ? 31.558 22.267  64.949  1.00 14.78 ? 53  ARG A CD  1 
ATOM   380  N NE  . ARG A 1 53  ? 30.960 23.536  65.325  1.00 26.37 ? 53  ARG A NE  1 
ATOM   381  C CZ  . ARG A 1 53  ? 31.239 24.689  64.726  1.00 25.93 ? 53  ARG A CZ  1 
ATOM   382  N NH1 . ARG A 1 53  ? 32.177 24.735  63.771  1.00 24.91 ? 53  ARG A NH1 1 
ATOM   383  N NH2 . ARG A 1 53  ? 30.638 25.801  65.152  1.00 24.04 ? 53  ARG A NH2 1 
ATOM   384  N N   . LEU A 1 54  ? 26.872 21.009  65.482  1.00 19.24 ? 54  LEU A N   1 
ATOM   385  C CA  . LEU A 1 54  ? 25.422 20.968  65.595  1.00 17.59 ? 54  LEU A CA  1 
ATOM   386  C C   . LEU A 1 54  ? 24.820 22.206  64.933  1.00 21.07 ? 54  LEU A C   1 
ATOM   387  O O   . LEU A 1 54  ? 25.193 23.334  65.267  1.00 15.08 ? 54  LEU A O   1 
ATOM   388  C CB  . LEU A 1 54  ? 24.999 20.945  67.071  1.00 18.70 ? 54  LEU A CB  1 
ATOM   389  C CG  . LEU A 1 54  ? 24.451 19.668  67.690  1.00 15.88 ? 54  LEU A CG  1 
ATOM   390  C CD1 . LEU A 1 54  ? 25.466 18.579  67.613  1.00 13.14 ? 54  LEU A CD1 1 
ATOM   391  C CD2 . LEU A 1 54  ? 24.030 19.946  69.106  1.00 15.61 ? 54  LEU A CD2 1 
ATOM   392  N N   . VAL A 1 55  ? 23.896 21.976  63.998  1.00 18.41 ? 55  VAL A N   1 
ATOM   393  C CA  . VAL A 1 55  ? 23.185 23.040  63.309  1.00 16.75 ? 55  VAL A CA  1 
ATOM   394  C C   . VAL A 1 55  ? 21.700 22.925  63.702  1.00 21.49 ? 55  VAL A C   1 
ATOM   395  O O   . VAL A 1 55  ? 21.144 21.812  63.814  1.00 17.61 ? 55  VAL A O   1 
ATOM   396  C CB  . VAL A 1 55  ? 23.362 22.938  61.779  1.00 19.82 ? 55  VAL A CB  1 
ATOM   397  C CG1 . VAL A 1 55  ? 22.430 23.889  61.075  1.00 17.63 ? 55  VAL A CG1 1 
ATOM   398  C CG2 . VAL A 1 55  ? 24.811 23.234  61.411  1.00 11.49 ? 55  VAL A CG2 1 
ATOM   399  N N   . GLU A 1 56  ? 21.074 24.081  63.908  1.00 21.29 ? 56  GLU A N   1 
ATOM   400  C CA  . GLU A 1 56  ? 19.684 24.161  64.342  1.00 23.97 ? 56  GLU A CA  1 
ATOM   401  C C   . GLU A 1 56  ? 18.926 25.137  63.427  1.00 21.84 ? 56  GLU A C   1 
ATOM   402  O O   . GLU A 1 56  ? 19.412 26.217  63.099  1.00 20.00 ? 56  GLU A O   1 
ATOM   403  C CB  . GLU A 1 56  ? 19.689 24.602  65.816  1.00 26.05 ? 56  GLU A CB  1 
ATOM   404  C CG  . GLU A 1 56  ? 18.370 24.713  66.496  1.00 23.02 ? 56  GLU A CG  1 
ATOM   405  C CD  . GLU A 1 56  ? 17.920 26.133  66.575  1.00 29.63 ? 56  GLU A CD  1 
ATOM   406  O OE1 . GLU A 1 56  ? 18.751 26.990  66.931  1.00 31.19 ? 56  GLU A OE1 1 
ATOM   407  O OE2 . GLU A 1 56  ? 16.748 26.390  66.262  1.00 26.88 ? 56  GLU A OE2 1 
ATOM   408  N N   . PHE A 1 57  ? 17.719 24.762  63.030  1.00 22.38 ? 57  PHE A N   1 
ATOM   409  C CA  . PHE A 1 57  ? 16.955 25.572  62.101  1.00 18.27 ? 57  PHE A CA  1 
ATOM   410  C C   . PHE A 1 57  ? 15.485 25.470  62.432  1.00 22.98 ? 57  PHE A C   1 
ATOM   411  O O   . PHE A 1 57  ? 15.006 24.365  62.707  1.00 26.69 ? 57  PHE A O   1 
ATOM   412  C CB  . PHE A 1 57  ? 17.221 25.034  60.674  1.00 18.50 ? 57  PHE A CB  1 
ATOM   413  C CG  . PHE A 1 57  ? 16.160 25.381  59.664  1.00 13.32 ? 57  PHE A CG  1 
ATOM   414  C CD1 . PHE A 1 57  ? 15.045 24.576  59.515  1.00 14.64 ? 57  PHE A CD1 1 
ATOM   415  C CD2 . PHE A 1 57  ? 16.268 26.529  58.899  1.00 14.77 ? 57  PHE A CD2 1 
ATOM   416  C CE1 . PHE A 1 57  ? 14.051 24.912  58.633  1.00 15.34 ? 57  PHE A CE1 1 
ATOM   417  C CE2 . PHE A 1 57  ? 15.275 26.876  58.006  1.00 11.03 ? 57  PHE A CE2 1 
ATOM   418  C CZ  . PHE A 1 57  ? 14.162 26.071  57.872  1.00 14.77 ? 57  PHE A CZ  1 
ATOM   419  N N   . ARG A 1 58  ? 14.776 26.608  62.407  1.00 23.04 ? 58  ARG A N   1 
ATOM   420  C CA  . ARG A 1 58  ? 13.333 26.643  62.669  1.00 20.30 ? 58  ARG A CA  1 
ATOM   421  C C   . ARG A 1 58  ? 12.642 27.480  61.609  1.00 23.42 ? 58  ARG A C   1 
ATOM   422  O O   . ARG A 1 58  ? 13.096 28.591  61.317  1.00 27.71 ? 58  ARG A O   1 
ATOM   423  C CB  . ARG A 1 58  ? 13.007 27.226  64.032  1.00 18.56 ? 58  ARG A CB  1 
ATOM   424  C CG  . ARG A 1 58  ? 11.533 27.145  64.295  1.00 14.19 ? 58  ARG A CG  1 
ATOM   425  C CD  . ARG A 1 58  ? 11.096 28.254  65.178  1.00 28.99 ? 58  ARG A CD  1 
ATOM   426  N NE  . ARG A 1 58  ? 10.890 27.805  66.546  1.00 36.28 ? 58  ARG A NE  1 
ATOM   427  C CZ  . ARG A 1 58  ? 9.753  27.282  66.992  1.00 39.74 ? 58  ARG A CZ  1 
ATOM   428  N NH1 . ARG A 1 58  ? 8.712  27.124  66.177  1.00 30.64 ? 58  ARG A NH1 1 
ATOM   429  N NH2 . ARG A 1 58  ? 9.638  26.976  68.276  1.00 40.70 ? 58  ARG A NH2 1 
ATOM   430  N N   . SER A 1 59  ? 11.498 26.992  61.120  1.00 24.78 ? 59  SER A N   1 
ATOM   431  C CA  . SER A 1 59  ? 10.728 27.648  60.058  1.00 23.30 ? 59  SER A CA  1 
ATOM   432  C C   . SER A 1 59  ? 9.223  27.847  60.375  1.00 23.83 ? 59  SER A C   1 
ATOM   433  O O   . SER A 1 59  ? 8.633  27.059  61.110  1.00 21.47 ? 59  SER A O   1 
ATOM   434  C CB  . SER A 1 59  ? 10.858 26.806  58.799  1.00 15.78 ? 59  SER A CB  1 
ATOM   435  O OG  . SER A 1 59  ? 10.579 27.583  57.671  1.00 30.95 ? 59  SER A OG  1 
ATOM   436  N N   . LYS A 1 60  ? 8.614  28.901  59.827  1.00 23.64 ? 60  LYS A N   1 
ATOM   437  C CA  . LYS A 1 60  ? 7.177  29.196  60.033  1.00 24.43 ? 60  LYS A CA  1 
ATOM   438  C C   . LYS A 1 60  ? 6.407  28.371  59.025  1.00 23.91 ? 60  LYS A C   1 
ATOM   439  O O   . LYS A 1 60  ? 7.003  27.866  58.071  1.00 29.28 ? 60  LYS A O   1 
ATOM   440  C CB  . LYS A 1 60  ? 6.895  30.667  59.752  1.00 23.79 ? 60  LYS A CB  1 
ATOM   441  C CG  . LYS A 1 60  ? 6.414  31.456  60.927  1.00 35.63 ? 60  LYS A CG  1 
ATOM   442  C CD  . LYS A 1 60  ? 7.523  31.697  61.930  1.00 44.18 ? 60  LYS A CD  1 
ATOM   443  C CE  . LYS A 1 60  ? 6.956  32.307  63.180  1.00 52.16 ? 60  LYS A CE  1 
ATOM   444  N NZ  . LYS A 1 60  ? 5.923  31.384  63.747  1.00 60.57 ? 60  LYS A NZ  1 
ATOM   445  N N   . PRO A 1 61  ? 5.083  28.222  59.192  1.00 23.68 ? 61  PRO A N   1 
ATOM   446  C CA  . PRO A 1 61  ? 4.419  27.405  58.165  1.00 21.18 ? 61  PRO A CA  1 
ATOM   447  C C   . PRO A 1 61  ? 4.447  27.946  56.727  1.00 20.54 ? 61  PRO A C   1 
ATOM   448  O O   . PRO A 1 61  ? 4.569  29.164  56.489  1.00 17.63 ? 61  PRO A O   1 
ATOM   449  C CB  . PRO A 1 61  ? 2.992  27.211  58.709  1.00 14.87 ? 61  PRO A CB  1 
ATOM   450  C CG  . PRO A 1 61  ? 2.856  28.196  59.791  1.00 17.32 ? 61  PRO A CG  1 
ATOM   451  C CD  . PRO A 1 61  ? 4.232  28.338  60.384  1.00 24.16 ? 61  PRO A CD  1 
ATOM   452  N N   . GLU A 1 62  ? 4.452  27.005  55.787  1.00 20.87 ? 62  GLU A N   1 
ATOM   453  C CA  . GLU A 1 62  ? 4.467  27.292  54.361  1.00 22.82 ? 62  GLU A CA  1 
ATOM   454  C C   . GLU A 1 62  ? 5.627  28.185  53.898  1.00 24.35 ? 62  GLU A C   1 
ATOM   455  O O   . GLU A 1 62  ? 5.446  29.284  53.354  1.00 24.33 ? 62  GLU A O   1 
ATOM   456  C CB  . GLU A 1 62  ? 3.105  27.831  53.946  1.00 24.27 ? 62  GLU A CB  1 
ATOM   457  C CG  . GLU A 1 62  ? 1.965  26.920  54.397  1.00 28.89 ? 62  GLU A CG  1 
ATOM   458  C CD  . GLU A 1 62  ? 0.631  27.240  53.722  1.00 34.58 ? 62  GLU A CD  1 
ATOM   459  O OE1 . GLU A 1 62  ? 0.376  28.431  53.411  1.00 33.41 ? 62  GLU A OE1 1 
ATOM   460  O OE2 . GLU A 1 62  ? -0.161 26.289  53.504  1.00 37.56 ? 62  GLU A OE2 1 
ATOM   461  N N   . THR A 1 63  ? 6.833  27.668  54.094  1.00 25.59 ? 63  THR A N   1 
ATOM   462  C CA  . THR A 1 63  ? 8.050  28.358  53.731  1.00 20.86 ? 63  THR A CA  1 
ATOM   463  C C   . THR A 1 63  ? 8.960  27.395  52.982  1.00 20.31 ? 63  THR A C   1 
ATOM   464  O O   . THR A 1 63  ? 8.676  26.194  52.895  1.00 19.29 ? 63  THR A O   1 
ATOM   465  C CB  . THR A 1 63  ? 8.800  28.867  54.985  1.00 24.42 ? 63  THR A CB  1 
ATOM   466  O OG1 . THR A 1 63  ? 8.709  27.879  56.014  1.00 26.77 ? 63  THR A OG1 1 
ATOM   467  C CG2 . THR A 1 63  ? 8.210  30.183  55.497  1.00 22.18 ? 63  THR A CG2 1 
ATOM   468  N N   . LEU A 1 64  ? 10.027 27.960  52.417  1.00 22.58 ? 64  LEU A N   1 
ATOM   469  C CA  . LEU A 1 64  ? 11.056 27.248  51.670  1.00 19.29 ? 64  LEU A CA  1 
ATOM   470  C C   . LEU A 1 64  ? 12.413 27.863  52.033  1.00 18.88 ? 64  LEU A C   1 
ATOM   471  O O   . LEU A 1 64  ? 12.529 29.087  52.219  1.00 14.66 ? 64  LEU A O   1 
ATOM   472  C CB  . LEU A 1 64  ? 10.807 27.414  50.162  1.00 20.03 ? 64  LEU A CB  1 
ATOM   473  C CG  . LEU A 1 64  ? 11.953 27.154  49.163  1.00 20.93 ? 64  LEU A CG  1 
ATOM   474  C CD1 . LEU A 1 64  ? 12.061 25.685  48.769  1.00 18.04 ? 64  LEU A CD1 1 
ATOM   475  C CD2 . LEU A 1 64  ? 11.719 27.989  47.916  1.00 27.61 ? 64  LEU A CD2 1 
ATOM   476  N N   . LEU A 1 65  ? 13.418 27.005  52.189  1.00 20.43 ? 65  LEU A N   1 
ATOM   477  C CA  . LEU A 1 65  ? 14.799 27.416  52.473  1.00 17.83 ? 65  LEU A CA  1 
ATOM   478  C C   . LEU A 1 65  ? 15.434 27.311  51.077  1.00 23.20 ? 65  LEU A C   1 
ATOM   479  O O   . LEU A 1 65  ? 15.420 26.223  50.484  1.00 23.39 ? 65  LEU A O   1 
ATOM   480  C CB  . LEU A 1 65  ? 15.435 26.376  53.383  1.00 18.59 ? 65  LEU A CB  1 
ATOM   481  C CG  . LEU A 1 65  ? 16.491 26.758  54.407  1.00 16.31 ? 65  LEU A CG  1 
ATOM   482  C CD1 . LEU A 1 65  ? 17.512 25.653  54.504  1.00 13.85 ? 65  LEU A CD1 1 
ATOM   483  C CD2 . LEU A 1 65  ? 17.135 28.068  54.062  1.00 19.30 ? 65  LEU A CD2 1 
ATOM   484  N N   . LEU A 1 66  ? 15.941 28.419  50.530  1.00 22.49 ? 66  LEU A N   1 
ATOM   485  C CA  . LEU A 1 66  ? 16.510 28.424  49.176  1.00 18.53 ? 66  LEU A CA  1 
ATOM   486  C C   . LEU A 1 66  ? 17.669 27.465  49.018  1.00 19.22 ? 66  LEU A C   1 
ATOM   487  O O   . LEU A 1 66  ? 18.363 27.191  49.983  1.00 20.67 ? 66  LEU A O   1 
ATOM   488  C CB  . LEU A 1 66  ? 16.876 29.848  48.741  1.00 19.93 ? 66  LEU A CB  1 
ATOM   489  C CG  . LEU A 1 66  ? 15.670 30.808  48.760  1.00 21.61 ? 66  LEU A CG  1 
ATOM   490  C CD1 . LEU A 1 66  ? 16.135 32.251  48.598  1.00 22.99 ? 66  LEU A CD1 1 
ATOM   491  C CD2 . LEU A 1 66  ? 14.609 30.445  47.713  1.00 15.03 ? 66  LEU A CD2 1 
ATOM   492  N N   . PRO A 1 67  ? 17.925 26.975  47.783  1.00 17.04 ? 67  PRO A N   1 
ATOM   493  C CA  . PRO A 1 67  ? 18.998 26.024  47.487  1.00 11.13 ? 67  PRO A CA  1 
ATOM   494  C C   . PRO A 1 67  ? 20.415 26.382  47.886  1.00 10.44 ? 67  PRO A C   1 
ATOM   495  O O   . PRO A 1 67  ? 20.888 27.506  47.685  1.00 13.90 ? 67  PRO A O   1 
ATOM   496  C CB  . PRO A 1 67  ? 18.866 25.816  45.985  1.00 11.18 ? 67  PRO A CB  1 
ATOM   497  C CG  . PRO A 1 67  ? 17.405 26.021  45.757  1.00 12.83 ? 67  PRO A CG  1 
ATOM   498  C CD  . PRO A 1 67  ? 17.179 27.276  46.545  1.00 16.78 ? 67  PRO A CD  1 
ATOM   499  N N   . GLN A 1 68  ? 21.121 25.392  48.409  1.00 7.80  ? 68  GLN A N   1 
ATOM   500  C CA  . GLN A 1 68  ? 22.489 25.602  48.846  1.00 5.27  ? 68  GLN A CA  1 
ATOM   501  C C   . GLN A 1 68  ? 23.156 24.264  48.833  1.00 9.53  ? 68  GLN A C   1 
ATOM   502  O O   . GLN A 1 68  ? 22.486 23.251  48.686  1.00 12.63 ? 68  GLN A O   1 
ATOM   503  C CB  . GLN A 1 68  ? 22.466 26.075  50.310  1.00 11.15 ? 68  GLN A CB  1 
ATOM   504  C CG  . GLN A 1 68  ? 21.655 25.134  51.230  1.00 16.61 ? 68  GLN A CG  1 
ATOM   505  C CD  . GLN A 1 68  ? 22.182 25.014  52.656  1.00 23.15 ? 68  GLN A CD  1 
ATOM   506  O OE1 . GLN A 1 68  ? 21.467 24.563  53.532  1.00 30.44 ? 68  GLN A OE1 1 
ATOM   507  N NE2 . GLN A 1 68  ? 23.432 25.397  52.889  1.00 25.89 ? 68  GLN A NE2 1 
ATOM   508  N N   . GLN A 1 69  ? 24.472 24.262  49.012  1.00 12.96 ? 69  GLN A N   1 
ATOM   509  C CA  . GLN A 1 69  ? 25.237 23.031  49.161  1.00 18.57 ? 69  GLN A CA  1 
ATOM   510  C C   . GLN A 1 69  ? 26.254 23.386  50.284  1.00 20.48 ? 69  GLN A C   1 
ATOM   511  O O   . GLN A 1 69  ? 26.625 24.561  50.442  1.00 22.12 ? 69  GLN A O   1 
ATOM   512  C CB  . GLN A 1 69  ? 25.893 22.589  47.835  1.00 19.30 ? 69  GLN A CB  1 
ATOM   513  C CG  . GLN A 1 69  ? 27.354 22.939  47.621  1.00 19.63 ? 69  GLN A CG  1 
ATOM   514  C CD  . GLN A 1 69  ? 27.548 24.241  46.867  1.00 23.35 ? 69  GLN A CD  1 
ATOM   515  O OE1 . GLN A 1 69  ? 28.650 24.794  46.839  1.00 27.10 ? 69  GLN A OE1 1 
ATOM   516  N NE2 . GLN A 1 69  ? 26.486 24.723  46.221  1.00 14.30 ? 69  GLN A NE2 1 
ATOM   517  N N   . ALA A 1 70  ? 26.593 22.441  51.153  1.00 18.23 ? 70  ALA A N   1 
ATOM   518  C CA  . ALA A 1 70  ? 27.553 22.734  52.235  1.00 19.05 ? 70  ALA A CA  1 
ATOM   519  C C   . ALA A 1 70  ? 28.716 21.743  52.193  1.00 16.91 ? 70  ALA A C   1 
ATOM   520  O O   . ALA A 1 70  ? 28.567 20.658  51.629  1.00 20.70 ? 70  ALA A O   1 
ATOM   521  C CB  . ALA A 1 70  ? 26.859 22.677  53.581  1.00 17.43 ? 70  ALA A CB  1 
ATOM   522  N N   . ASP A 1 71  ? 29.868 22.109  52.752  1.00 13.58 ? 71  ASP A N   1 
ATOM   523  C CA  . ASP A 1 71  ? 31.039 21.228  52.754  1.00 14.42 ? 71  ASP A CA  1 
ATOM   524  C C   . ASP A 1 71  ? 31.045 20.249  53.945  1.00 20.17 ? 71  ASP A C   1 
ATOM   525  O O   . ASP A 1 71  ? 32.101 20.022  54.567  1.00 20.28 ? 71  ASP A O   1 
ATOM   526  C CB  . ASP A 1 71  ? 32.335 22.060  52.735  1.00 13.06 ? 71  ASP A CB  1 
ATOM   527  C CG  . ASP A 1 71  ? 32.526 22.902  53.997  1.00 13.97 ? 71  ASP A CG  1 
ATOM   528  O OD1 . ASP A 1 71  ? 31.605 22.961  54.829  1.00 14.99 ? 71  ASP A OD1 1 
ATOM   529  O OD2 . ASP A 1 71  ? 33.617 23.486  54.173  1.00 20.41 ? 71  ASP A OD2 1 
ATOM   530  N N   . ALA A 1 72  ? 29.889 19.656  54.257  1.00 18.81 ? 72  ALA A N   1 
ATOM   531  C CA  . ALA A 1 72  ? 29.808 18.748  55.400  1.00 19.22 ? 72  ALA A CA  1 
ATOM   532  C C   . ALA A 1 72  ? 28.743 17.669  55.268  1.00 20.87 ? 72  ALA A C   1 
ATOM   533  O O   . ALA A 1 72  ? 27.753 17.849  54.554  1.00 25.42 ? 72  ALA A O   1 
ATOM   534  C CB  . ALA A 1 72  ? 29.562 19.550  56.661  1.00 13.44 ? 72  ALA A CB  1 
ATOM   535  N N   . GLU A 1 73  ? 28.986 16.507  55.865  1.00 18.65 ? 73  GLU A N   1 
ATOM   536  C CA  . GLU A 1 73  ? 27.974 15.443  55.845  1.00 18.58 ? 73  GLU A CA  1 
ATOM   537  C C   . GLU A 1 73  ? 26.926 15.908  56.848  1.00 20.55 ? 73  GLU A C   1 
ATOM   538  O O   . GLU A 1 73  ? 27.272 16.372  57.946  1.00 24.96 ? 73  GLU A O   1 
ATOM   539  C CB  . GLU A 1 73  ? 28.549 14.119  56.370  1.00 20.82 ? 73  GLU A CB  1 
ATOM   540  C CG  . GLU A 1 73  ? 29.443 13.364  55.436  1.00 29.20 ? 73  GLU A CG  1 
ATOM   541  C CD  . GLU A 1 73  ? 28.657 12.657  54.350  1.00 42.01 ? 73  GLU A CD  1 
ATOM   542  O OE1 . GLU A 1 73  ? 27.637 11.994  54.691  1.00 43.87 ? 73  GLU A OE1 1 
ATOM   543  O OE2 . GLU A 1 73  ? 29.062 12.770  53.161  1.00 42.04 ? 73  GLU A OE2 1 
ATOM   544  N N   . LEU A 1 74  ? 25.661 15.788  56.497  1.00 18.45 ? 74  LEU A N   1 
ATOM   545  C CA  . LEU A 1 74  ? 24.609 16.177  57.418  1.00 18.34 ? 74  LEU A CA  1 
ATOM   546  C C   . LEU A 1 74  ? 23.743 14.991  57.797  1.00 18.08 ? 74  LEU A C   1 
ATOM   547  O O   . LEU A 1 74  ? 23.522 14.091  56.998  1.00 23.95 ? 74  LEU A O   1 
ATOM   548  C CB  . LEU A 1 74  ? 23.690 17.235  56.779  1.00 17.58 ? 74  LEU A CB  1 
ATOM   549  C CG  . LEU A 1 74  ? 23.922 18.745  56.927  1.00 14.01 ? 74  LEU A CG  1 
ATOM   550  C CD1 . LEU A 1 74  ? 25.376 19.029  57.143  1.00 5.19  ? 74  LEU A CD1 1 
ATOM   551  C CD2 . LEU A 1 74  ? 23.392 19.480  55.667  1.00 17.42 ? 74  LEU A CD2 1 
ATOM   552  N N   . LEU A 1 75  ? 23.297 14.971  59.041  1.00 19.06 ? 75  LEU A N   1 
ATOM   553  C CA  . LEU A 1 75  ? 22.365 13.966  59.506  1.00 18.55 ? 75  LEU A CA  1 
ATOM   554  C C   . LEU A 1 75  ? 21.268 14.887  60.055  1.00 20.29 ? 75  LEU A C   1 
ATOM   555  O O   . LEU A 1 75  ? 21.458 15.545  61.088  1.00 21.03 ? 75  LEU A O   1 
ATOM   556  C CB  . LEU A 1 75  ? 22.970 13.096  60.596  1.00 18.85 ? 75  LEU A CB  1 
ATOM   557  C CG  . LEU A 1 75  ? 21.938 12.081  61.088  1.00 23.56 ? 75  LEU A CG  1 
ATOM   558  C CD1 . LEU A 1 75  ? 21.612 11.117  59.965  1.00 11.49 ? 75  LEU A CD1 1 
ATOM   559  C CD2 . LEU A 1 75  ? 22.433 11.357  62.341  1.00 21.75 ? 75  LEU A CD2 1 
ATOM   560  N N   . LEU A 1 76  ? 20.177 15.006  59.292  1.00 20.69 ? 76  LEU A N   1 
ATOM   561  C CA  . LEU A 1 76  ? 19.039 15.875  59.588  1.00 23.35 ? 76  LEU A CA  1 
ATOM   562  C C   . LEU A 1 76  ? 17.940 15.183  60.406  1.00 27.96 ? 76  LEU A C   1 
ATOM   563  O O   . LEU A 1 76  ? 17.540 14.046  60.116  1.00 27.05 ? 76  LEU A O   1 
ATOM   564  C CB  . LEU A 1 76  ? 18.496 16.411  58.257  1.00 22.48 ? 76  LEU A CB  1 
ATOM   565  C CG  . LEU A 1 76  ? 17.528 17.584  58.138  1.00 25.16 ? 76  LEU A CG  1 
ATOM   566  C CD1 . LEU A 1 76  ? 17.827 18.321  56.859  1.00 21.45 ? 76  LEU A CD1 1 
ATOM   567  C CD2 . LEU A 1 76  ? 16.080 17.133  58.162  1.00 21.98 ? 76  LEU A CD2 1 
ATOM   568  N N   . VAL A 1 77  ? 17.458 15.867  61.441  1.00 29.23 ? 77  VAL A N   1 
ATOM   569  C CA  . VAL A 1 77  ? 16.434 15.302  62.311  1.00 26.19 ? 77  VAL A CA  1 
ATOM   570  C C   . VAL A 1 77  ? 15.252 16.237  62.643  1.00 26.43 ? 77  VAL A C   1 
ATOM   571  O O   . VAL A 1 77  ? 15.443 17.292  63.249  1.00 29.74 ? 77  VAL A O   1 
ATOM   572  C CB  . VAL A 1 77  ? 17.063 14.846  63.634  1.00 23.34 ? 77  VAL A CB  1 
ATOM   573  C CG1 . VAL A 1 77  ? 16.054 14.067  64.453  1.00 20.46 ? 77  VAL A CG1 1 
ATOM   574  C CG2 . VAL A 1 77  ? 18.295 14.023  63.365  1.00 25.96 ? 77  VAL A CG2 1 
ATOM   575  N N   . VAL A 1 78  ? 14.036 15.829  62.269  1.00 22.30 ? 78  VAL A N   1 
ATOM   576  C CA  . VAL A 1 78  ? 12.841 16.601  62.560  1.00 20.10 ? 78  VAL A CA  1 
ATOM   577  C C   . VAL A 1 78  ? 12.513 16.397  64.053  1.00 22.12 ? 78  VAL A C   1 
ATOM   578  O O   . VAL A 1 78  ? 12.159 15.302  64.476  1.00 19.99 ? 78  VAL A O   1 
ATOM   579  C CB  . VAL A 1 78  ? 11.635 16.191  61.647  1.00 16.44 ? 78  VAL A CB  1 
ATOM   580  C CG1 . VAL A 1 78  ? 10.380 16.981  61.990  1.00 4.94  ? 78  VAL A CG1 1 
ATOM   581  C CG2 . VAL A 1 78  ? 11.971 16.465  60.199  1.00 15.77 ? 78  VAL A CG2 1 
ATOM   582  N N   . ARG A 1 79  ? 12.702 17.449  64.846  1.00 21.76 ? 79  ARG A N   1 
ATOM   583  C CA  . ARG A 1 79  ? 12.427 17.390  66.272  1.00 20.57 ? 79  ARG A CA  1 
ATOM   584  C C   . ARG A 1 79  ? 10.995 17.868  66.551  1.00 26.20 ? 79  ARG A C   1 
ATOM   585  O O   . ARG A 1 79  ? 10.477 17.679  67.645  1.00 27.81 ? 79  ARG A O   1 
ATOM   586  C CB  . ARG A 1 79  ? 13.466 18.215  67.048  1.00 20.25 ? 79  ARG A CB  1 
ATOM   587  C CG  . ARG A 1 79  ? 13.389 19.715  66.828  1.00 23.66 ? 79  ARG A CG  1 
ATOM   588  C CD  . ARG A 1 79  ? 14.690 20.464  67.108  1.00 20.56 ? 79  ARG A CD  1 
ATOM   589  N NE  . ARG A 1 79  ? 15.088 20.449  68.511  1.00 25.93 ? 79  ARG A NE  1 
ATOM   590  C CZ  . ARG A 1 79  ? 15.726 21.440  69.139  1.00 27.69 ? 79  ARG A CZ  1 
ATOM   591  N NH1 . ARG A 1 79  ? 16.033 22.562  68.510  1.00 27.92 ? 79  ARG A NH1 1 
ATOM   592  N NH2 . ARG A 1 79  ? 16.052 21.312  70.422  1.00 31.99 ? 79  ARG A NH2 1 
ATOM   593  N N   . SER A 1 80  ? 10.369 18.508  65.566  1.00 27.70 ? 80  SER A N   1 
ATOM   594  C CA  . SER A 1 80  ? 8.987  18.992  65.672  1.00 27.80 ? 80  SER A CA  1 
ATOM   595  C C   . SER A 1 80  ? 8.541  19.348  64.263  1.00 27.14 ? 80  SER A C   1 
ATOM   596  O O   . SER A 1 80  ? 9.315  19.927  63.495  1.00 30.76 ? 80  SER A O   1 
ATOM   597  C CB  . SER A 1 80  ? 8.865  20.263  66.536  1.00 33.73 ? 80  SER A CB  1 
ATOM   598  O OG  . SER A 1 80  ? 9.421  20.123  67.835  1.00 41.99 ? 80  SER A OG  1 
ATOM   599  N N   . GLY A 1 81  ? 7.306  18.993  63.925  1.00 23.13 ? 81  GLY A N   1 
ATOM   600  C CA  . GLY A 1 81  ? 6.773  19.304  62.617  1.00 22.20 ? 81  GLY A CA  1 
ATOM   601  C C   . GLY A 1 81  ? 6.991  18.279  61.514  1.00 20.39 ? 81  GLY A C   1 
ATOM   602  O O   . GLY A 1 81  ? 7.208  17.087  61.753  1.00 19.88 ? 81  GLY A O   1 
ATOM   603  N N   . SER A 1 82  ? 6.897  18.767  60.285  1.00 22.09 ? 82  SER A N   1 
ATOM   604  C CA  . SER A 1 82  ? 7.047  17.963  59.086  1.00 19.88 ? 82  SER A CA  1 
ATOM   605  C C   . SER A 1 82  ? 7.867  18.757  58.089  1.00 19.98 ? 82  SER A C   1 
ATOM   606  O O   . SER A 1 82  ? 7.844  19.988  58.093  1.00 20.41 ? 82  SER A O   1 
ATOM   607  C CB  . SER A 1 82  ? 5.678  17.701  58.478  1.00 18.48 ? 82  SER A CB  1 
ATOM   608  O OG  . SER A 1 82  ? 4.754  17.345  59.484  1.00 21.43 ? 82  SER A OG  1 
ATOM   609  N N   . ALA A 1 83  ? 8.521  18.063  57.174  1.00 21.44 ? 83  ALA A N   1 
ATOM   610  C CA  . ALA A 1 83  ? 9.326  18.743  56.175  1.00 23.10 ? 83  ALA A CA  1 
ATOM   611  C C   . ALA A 1 83  ? 9.356  17.953  54.887  1.00 24.08 ? 83  ALA A C   1 
ATOM   612  O O   . ALA A 1 83  ? 9.130  16.742  54.886  1.00 21.09 ? 83  ALA A O   1 
ATOM   613  C CB  . ALA A 1 83  ? 10.744 18.927  56.690  1.00 21.88 ? 83  ALA A CB  1 
ATOM   614  N N   . ILE A 1 84  ? 9.557  18.659  53.781  1.00 27.92 ? 84  ILE A N   1 
ATOM   615  C CA  . ILE A 1 84  ? 9.706  18.015  52.467  1.00 26.39 ? 84  ILE A CA  1 
ATOM   616  C C   . ILE A 1 84  ? 11.138 18.384  52.103  1.00 23.38 ? 84  ILE A C   1 
ATOM   617  O O   . ILE A 1 84  ? 11.471 19.572  52.015  1.00 21.91 ? 84  ILE A O   1 
ATOM   618  C CB  . ILE A 1 84  ? 8.762  18.564  51.383  1.00 22.96 ? 84  ILE A CB  1 
ATOM   619  C CG1 . ILE A 1 84  ? 7.294  18.306  51.761  1.00 26.76 ? 84  ILE A CG1 1 
ATOM   620  C CG2 . ILE A 1 84  ? 9.079  17.889  50.054  1.00 18.94 ? 84  ILE A CG2 1 
ATOM   621  C CD1 . ILE A 1 84  ? 6.290  19.204  51.013  1.00 24.11 ? 84  ILE A CD1 1 
ATOM   622  N N   . LEU A 1 85  ? 11.986 17.363  52.021  1.00 19.82 ? 85  LEU A N   1 
ATOM   623  C CA  . LEU A 1 85  ? 13.402 17.510  51.698  1.00 20.58 ? 85  LEU A CA  1 
ATOM   624  C C   . LEU A 1 85  ? 13.658 16.991  50.296  1.00 15.14 ? 85  LEU A C   1 
ATOM   625  O O   . LEU A 1 85  ? 13.206 15.910  49.948  1.00 21.17 ? 85  LEU A O   1 
ATOM   626  C CB  . LEU A 1 85  ? 14.239 16.696  52.696  1.00 20.80 ? 85  LEU A CB  1 
ATOM   627  C CG  . LEU A 1 85  ? 15.720 16.436  52.410  1.00 23.94 ? 85  LEU A CG  1 
ATOM   628  C CD1 . LEU A 1 85  ? 16.538 17.736  52.518  1.00 22.71 ? 85  LEU A CD1 1 
ATOM   629  C CD2 . LEU A 1 85  ? 16.231 15.390  53.383  1.00 22.43 ? 85  LEU A CD2 1 
ATOM   630  N N   . VAL A 1 86  ? 14.388 17.741  49.486  1.00 18.98 ? 86  VAL A N   1 
ATOM   631  C CA  . VAL A 1 86  ? 14.660 17.276  48.138  1.00 14.60 ? 86  VAL A CA  1 
ATOM   632  C C   . VAL A 1 86  ? 16.120 17.453  47.792  1.00 14.67 ? 86  VAL A C   1 
ATOM   633  O O   . VAL A 1 86  ? 16.718 18.492  48.126  1.00 11.12 ? 86  VAL A O   1 
ATOM   634  C CB  . VAL A 1 86  ? 13.675 17.892  47.092  1.00 21.50 ? 86  VAL A CB  1 
ATOM   635  C CG1 . VAL A 1 86  ? 13.265 19.276  47.490  1.00 25.68 ? 86  VAL A CG1 1 
ATOM   636  C CG2 . VAL A 1 86  ? 14.273 17.890  45.694  1.00 19.83 ? 86  VAL A CG2 1 
ATOM   637  N N   . LEU A 1 87  ? 16.721 16.363  47.294  1.00 9.96  ? 87  LEU A N   1 
ATOM   638  C CA  . LEU A 1 87  ? 18.123 16.339  46.881  1.00 6.66  ? 87  LEU A CA  1 
ATOM   639  C C   . LEU A 1 87  ? 18.195 16.458  45.341  1.00 14.43 ? 87  LEU A C   1 
ATOM   640  O O   . LEU A 1 87  ? 17.493 15.727  44.641  1.00 12.24 ? 87  LEU A O   1 
ATOM   641  C CB  . LEU A 1 87  ? 18.771 15.030  47.296  1.00 2.32  ? 87  LEU A CB  1 
ATOM   642  C CG  . LEU A 1 87  ? 19.331 14.929  48.724  1.00 17.95 ? 87  LEU A CG  1 
ATOM   643  C CD1 . LEU A 1 87  ? 18.540 15.785  49.733  1.00 7.12  ? 87  LEU A CD1 1 
ATOM   644  C CD2 . LEU A 1 87  ? 19.354 13.466  49.136  1.00 17.45 ? 87  LEU A CD2 1 
ATOM   645  N N   . VAL A 1 88  ? 19.057 17.359  44.847  1.00 18.61 ? 88  VAL A N   1 
ATOM   646  C CA  . VAL A 1 88  ? 19.259 17.637  43.411  1.00 17.44 ? 88  VAL A CA  1 
ATOM   647  C C   . VAL A 1 88  ? 20.648 17.203  42.946  1.00 19.85 ? 88  VAL A C   1 
ATOM   648  O O   . VAL A 1 88  ? 21.642 17.856  43.252  1.00 17.45 ? 88  VAL A O   1 
ATOM   649  C CB  . VAL A 1 88  ? 19.114 19.158  43.084  1.00 11.56 ? 88  VAL A CB  1 
ATOM   650  C CG1 . VAL A 1 88  ? 19.268 19.374  41.581  1.00 16.76 ? 88  VAL A CG1 1 
ATOM   651  C CG2 . VAL A 1 88  ? 17.776 19.679  43.554  1.00 7.74  ? 88  VAL A CG2 1 
ATOM   652  N N   . LYS A 1 89  ? 20.710 16.066  42.258  1.00 23.63 ? 89  LYS A N   1 
ATOM   653  C CA  . LYS A 1 89  ? 21.972 15.534  41.737  1.00 29.22 ? 89  LYS A CA  1 
ATOM   654  C C   . LYS A 1 89  ? 22.164 16.132  40.332  1.00 29.27 ? 89  LYS A C   1 
ATOM   655  O O   . LYS A 1 89  ? 21.176 16.414  39.647  1.00 27.37 ? 89  LYS A O   1 
ATOM   656  C CB  . LYS A 1 89  ? 21.941 13.998  41.738  1.00 33.62 ? 89  LYS A CB  1 
ATOM   657  C CG  . LYS A 1 89  ? 22.063 13.384  43.150  1.00 37.28 ? 89  LYS A CG  1 
ATOM   658  C CD  . LYS A 1 89  ? 21.414 12.010  43.200  1.00 44.51 ? 89  LYS A CD  1 
ATOM   659  C CE  . LYS A 1 89  ? 21.879 11.185  44.391  1.00 50.74 ? 89  LYS A CE  1 
ATOM   660  N NZ  . LYS A 1 89  ? 21.518 11.762  45.724  1.00 55.98 ? 89  LYS A NZ  1 
ATOM   661  N N   . PRO A 1 90  ? 23.432 16.309  39.885  1.00 27.81 ? 90  PRO A N   1 
ATOM   662  C CA  . PRO A 1 90  ? 23.822 16.886  38.598  1.00 27.35 ? 90  PRO A CA  1 
ATOM   663  C C   . PRO A 1 90  ? 23.366 16.216  37.319  1.00 27.30 ? 90  PRO A C   1 
ATOM   664  O O   . PRO A 1 90  ? 23.048 16.908  36.355  1.00 32.86 ? 90  PRO A O   1 
ATOM   665  C CB  . PRO A 1 90  ? 25.336 16.965  38.712  1.00 27.12 ? 90  PRO A CB  1 
ATOM   666  C CG  . PRO A 1 90  ? 25.648 15.750  39.432  1.00 31.42 ? 90  PRO A CG  1 
ATOM   667  C CD  . PRO A 1 90  ? 24.616 15.746  40.550  1.00 29.70 ? 90  PRO A CD  1 
ATOM   668  N N   . ASP A 1 91  ? 23.294 14.895  37.282  1.00 28.04 ? 91  ASP A N   1 
ATOM   669  C CA  . ASP A 1 91  ? 22.843 14.244  36.054  1.00 27.43 ? 91  ASP A CA  1 
ATOM   670  C C   . ASP A 1 91  ? 21.331 14.056  35.999  1.00 27.75 ? 91  ASP A C   1 
ATOM   671  O O   . ASP A 1 91  ? 20.833 12.938  35.911  1.00 28.02 ? 91  ASP A O   1 
ATOM   672  C CB  . ASP A 1 91  ? 23.578 12.930  35.812  1.00 27.67 ? 91  ASP A CB  1 
ATOM   673  C CG  . ASP A 1 91  ? 23.677 12.082  37.062  1.00 31.96 ? 91  ASP A CG  1 
ATOM   674  O OD1 . ASP A 1 91  ? 22.892 12.309  38.022  1.00 26.37 ? 91  ASP A OD1 1 
ATOM   675  O OD2 . ASP A 1 91  ? 24.565 11.197  37.080  1.00 35.57 ? 91  ASP A OD2 1 
ATOM   676  N N   . ASP A 1 92  ? 20.618 15.170  36.122  1.00 26.67 ? 92  ASP A N   1 
ATOM   677  C CA  . ASP A 1 92  ? 19.163 15.202  36.045  1.00 28.45 ? 92  ASP A CA  1 
ATOM   678  C C   . ASP A 1 92  ? 18.450 14.248  36.991  1.00 28.71 ? 92  ASP A C   1 
ATOM   679  O O   . ASP A 1 92  ? 17.583 13.477  36.579  1.00 27.86 ? 92  ASP A O   1 
ATOM   680  C CB  . ASP A 1 92  ? 18.724 14.948  34.594  1.00 34.97 ? 92  ASP A CB  1 
ATOM   681  C CG  . ASP A 1 92  ? 17.352 15.505  34.289  1.00 37.75 ? 92  ASP A CG  1 
ATOM   682  O OD1 . ASP A 1 92  ? 17.222 16.742  34.242  1.00 38.78 ? 92  ASP A OD1 1 
ATOM   683  O OD2 . ASP A 1 92  ? 16.405 14.712  34.083  1.00 47.70 ? 92  ASP A OD2 1 
ATOM   684  N N   . ARG A 1 93  ? 18.798 14.313  38.269  1.00 32.30 ? 93  ARG A N   1 
ATOM   685  C CA  . ARG A 1 93  ? 18.148 13.468  39.261  1.00 32.24 ? 93  ARG A CA  1 
ATOM   686  C C   . ARG A 1 93  ? 17.861 14.203  40.571  1.00 34.38 ? 93  ARG A C   1 
ATOM   687  O O   . ARG A 1 93  ? 18.633 15.073  40.977  1.00 34.21 ? 93  ARG A O   1 
ATOM   688  C CB  . ARG A 1 93  ? 18.985 12.223  39.545  1.00 30.43 ? 93  ARG A CB  1 
ATOM   689  C CG  . ARG A 1 93  ? 18.859 11.150  38.499  1.00 29.91 ? 93  ARG A CG  1 
ATOM   690  C CD  . ARG A 1 93  ? 19.658 9.931   38.884  1.00 39.30 ? 93  ARG A CD  1 
ATOM   691  N NE  . ARG A 1 93  ? 21.088 10.219  39.000  1.00 44.98 ? 93  ARG A NE  1 
ATOM   692  C CZ  . ARG A 1 93  ? 21.822 9.949   40.076  1.00 46.00 ? 93  ARG A CZ  1 
ATOM   693  N NH1 . ARG A 1 93  ? 21.266 9.392   41.145  1.00 49.16 ? 93  ARG A NH1 1 
ATOM   694  N NH2 . ARG A 1 93  ? 23.124 10.205  40.075  1.00 53.62 ? 93  ARG A NH2 1 
ATOM   695  N N   . ARG A 1 94  ? 16.720 13.876  41.188  1.00 33.81 ? 94  ARG A N   1 
ATOM   696  C CA  . ARG A 1 94  ? 16.308 14.434  42.481  1.00 29.70 ? 94  ARG A CA  1 
ATOM   697  C C   . ARG A 1 94  ? 15.790 13.303  43.359  1.00 30.61 ? 94  ARG A C   1 
ATOM   698  O O   . ARG A 1 94  ? 15.339 12.270  42.844  1.00 27.67 ? 94  ARG A O   1 
ATOM   699  C CB  . ARG A 1 94  ? 15.187 15.473  42.362  1.00 23.97 ? 94  ARG A CB  1 
ATOM   700  C CG  . ARG A 1 94  ? 15.509 16.655  41.540  1.00 18.90 ? 94  ARG A CG  1 
ATOM   701  C CD  . ARG A 1 94  ? 14.805 16.468  40.249  1.00 11.64 ? 94  ARG A CD  1 
ATOM   702  N NE  . ARG A 1 94  ? 15.665 16.851  39.156  1.00 25.49 ? 94  ARG A NE  1 
ATOM   703  C CZ  . ARG A 1 94  ? 15.471 16.495  37.898  1.00 21.29 ? 94  ARG A CZ  1 
ATOM   704  N NH1 . ARG A 1 94  ? 14.471 15.692  37.575  1.00 9.92  ? 94  ARG A NH1 1 
ATOM   705  N NH2 . ARG A 1 94  ? 16.319 16.910  36.982  1.00 20.28 ? 94  ARG A NH2 1 
ATOM   706  N N   . GLU A 1 95  ? 15.822 13.529  44.673  1.00 26.52 ? 95  GLU A N   1 
ATOM   707  C CA  . GLU A 1 95  ? 15.356 12.562  45.662  1.00 25.63 ? 95  GLU A CA  1 
ATOM   708  C C   . GLU A 1 95  ? 14.411 13.330  46.560  1.00 21.83 ? 95  GLU A C   1 
ATOM   709  O O   . GLU A 1 95  ? 14.798 14.367  47.092  1.00 17.81 ? 95  GLU A O   1 
ATOM   710  C CB  . GLU A 1 95  ? 16.540 12.018  46.465  1.00 31.80 ? 95  GLU A CB  1 
ATOM   711  C CG  . GLU A 1 95  ? 16.928 10.581  46.125  1.00 40.49 ? 95  GLU A CG  1 
ATOM   712  C CD  . GLU A 1 95  ? 18.434 10.355  46.134  1.00 47.98 ? 95  GLU A CD  1 
ATOM   713  O OE1 . GLU A 1 95  ? 19.045 10.388  47.225  1.00 51.84 ? 95  GLU A OE1 1 
ATOM   714  O OE2 . GLU A 1 95  ? 19.010 10.141  45.039  1.00 54.01 ? 95  GLU A OE2 1 
ATOM   715  N N   . TYR A 1 96  ? 13.169 12.854  46.668  1.00 21.83 ? 96  TYR A N   1 
ATOM   716  C CA  . TYR A 1 96  ? 12.125 13.504  47.477  1.00 21.73 ? 96  TYR A CA  1 
ATOM   717  C C   . TYR A 1 96  ? 11.866 12.768  48.774  1.00 20.92 ? 96  TYR A C   1 
ATOM   718  O O   . TYR A 1 96  ? 11.626 11.571  48.752  1.00 21.10 ? 96  TYR A O   1 
ATOM   719  C CB  . TYR A 1 96  ? 10.798 13.583  46.698  1.00 22.23 ? 96  TYR A CB  1 
ATOM   720  C CG  . TYR A 1 96  ? 10.896 14.301  45.371  1.00 23.88 ? 96  TYR A CG  1 
ATOM   721  C CD1 . TYR A 1 96  ? 11.405 13.649  44.257  1.00 20.82 ? 96  TYR A CD1 1 
ATOM   722  C CD2 . TYR A 1 96  ? 10.540 15.646  45.249  1.00 20.60 ? 96  TYR A CD2 1 
ATOM   723  C CE1 . TYR A 1 96  ? 11.569 14.302  43.067  1.00 24.28 ? 96  TYR A CE1 1 
ATOM   724  C CE2 . TYR A 1 96  ? 10.699 16.311  44.055  1.00 24.58 ? 96  TYR A CE2 1 
ATOM   725  C CZ  . TYR A 1 96  ? 11.219 15.629  42.960  1.00 24.48 ? 96  TYR A CZ  1 
ATOM   726  O OH  . TYR A 1 96  ? 11.389 16.250  41.742  1.00 22.67 ? 96  TYR A OH  1 
ATOM   727  N N   . PHE A 1 97  ? 11.875 13.482  49.894  1.00 22.17 ? 97  PHE A N   1 
ATOM   728  C CA  . PHE A 1 97  ? 11.632 12.866  51.207  1.00 23.47 ? 97  PHE A CA  1 
ATOM   729  C C   . PHE A 1 97  ? 10.645 13.695  51.996  1.00 24.95 ? 97  PHE A C   1 
ATOM   730  O O   . PHE A 1 97  ? 10.760 14.934  52.058  1.00 24.61 ? 97  PHE A O   1 
ATOM   731  C CB  . PHE A 1 97  ? 12.893 12.801  52.087  1.00 12.68 ? 97  PHE A CB  1 
ATOM   732  C CG  . PHE A 1 97  ? 14.078 12.196  51.429  1.00 19.11 ? 97  PHE A CG  1 
ATOM   733  C CD1 . PHE A 1 97  ? 14.260 10.826  51.419  1.00 16.41 ? 97  PHE A CD1 1 
ATOM   734  C CD2 . PHE A 1 97  ? 15.040 13.003  50.833  1.00 22.05 ? 97  PHE A CD2 1 
ATOM   735  C CE1 . PHE A 1 97  ? 15.378 10.271  50.825  1.00 15.02 ? 97  PHE A CE1 1 
ATOM   736  C CE2 . PHE A 1 97  ? 16.166 12.450  50.235  1.00 19.22 ? 97  PHE A CE2 1 
ATOM   737  C CZ  . PHE A 1 97  ? 16.330 11.083  50.232  1.00 22.51 ? 97  PHE A CZ  1 
ATOM   738  N N   . PHE A 1 98  ? 9.703  12.998  52.629  1.00 26.71 ? 98  PHE A N   1 
ATOM   739  C CA  . PHE A 1 98  ? 8.713  13.622  53.497  1.00 28.56 ? 98  PHE A CA  1 
ATOM   740  C C   . PHE A 1 98  ? 9.077  13.130  54.914  1.00 29.31 ? 98  PHE A C   1 
ATOM   741  O O   . PHE A 1 98  ? 9.130  11.921  55.180  1.00 28.95 ? 98  PHE A O   1 
ATOM   742  C CB  . PHE A 1 98  ? 7.297  13.189  53.109  1.00 30.11 ? 98  PHE A CB  1 
ATOM   743  C CG  . PHE A 1 98  ? 6.208  13.962  53.808  1.00 25.89 ? 98  PHE A CG  1 
ATOM   744  C CD1 . PHE A 1 98  ? 5.727  13.553  55.050  1.00 32.80 ? 98  PHE A CD1 1 
ATOM   745  C CD2 . PHE A 1 98  ? 5.663  15.094  53.219  1.00 30.65 ? 98  PHE A CD2 1 
ATOM   746  C CE1 . PHE A 1 98  ? 4.725  14.255  55.697  1.00 31.83 ? 98  PHE A CE1 1 
ATOM   747  C CE2 . PHE A 1 98  ? 4.651  15.814  53.856  1.00 36.39 ? 98  PHE A CE2 1 
ATOM   748  C CZ  . PHE A 1 98  ? 4.179  15.391  55.103  1.00 32.23 ? 98  PHE A CZ  1 
ATOM   749  N N   . LEU A 1 99  ? 9.399  14.067  55.796  1.00 28.24 ? 99  LEU A N   1 
ATOM   750  C CA  . LEU A 1 99  ? 9.781  13.735  57.156  1.00 28.19 ? 99  LEU A CA  1 
ATOM   751  C C   . LEU A 1 99  ? 8.818  14.371  58.163  1.00 29.63 ? 99  LEU A C   1 
ATOM   752  O O   . LEU A 1 99  ? 8.343  15.491  57.945  1.00 25.37 ? 99  LEU A O   1 
ATOM   753  C CB  . LEU A 1 99  ? 11.215 14.214  57.437  1.00 28.97 ? 99  LEU A CB  1 
ATOM   754  C CG  . LEU A 1 99  ? 12.443 13.539  56.797  1.00 28.39 ? 99  LEU A CG  1 
ATOM   755  C CD1 . LEU A 1 99  ? 12.156 12.081  56.621  1.00 27.55 ? 99  LEU A CD1 1 
ATOM   756  C CD2 . LEU A 1 99  ? 12.828 14.151  55.464  1.00 31.38 ? 99  LEU A CD2 1 
ATOM   757  N N   . THR A 1 100 ? 8.508  13.628  59.230  1.00 29.45 ? 100 THR A N   1 
ATOM   758  C CA  . THR A 1 100 ? 7.621  14.065  60.318  1.00 35.10 ? 100 THR A CA  1 
ATOM   759  C C   . THR A 1 100 ? 8.181  13.548  61.645  1.00 38.23 ? 100 THR A C   1 
ATOM   760  O O   . THR A 1 100 ? 8.992  12.628  61.666  1.00 37.26 ? 100 THR A O   1 
ATOM   761  C CB  . THR A 1 100 ? 6.140  13.554  60.166  1.00 35.83 ? 100 THR A CB  1 
ATOM   762  O OG1 . THR A 1 100 ? 6.108  12.234  59.598  1.00 40.32 ? 100 THR A OG1 1 
ATOM   763  C CG2 . THR A 1 100 ? 5.329  14.479  59.297  1.00 38.68 ? 100 THR A CG2 1 
ATOM   764  N N   . SER A 1 101 ? 7.768  14.154  62.749  1.00 43.40 ? 101 SER A N   1 
ATOM   765  C CA  . SER A 1 101 ? 8.241  13.726  64.045  1.00 49.28 ? 101 SER A CA  1 
ATOM   766  C C   . SER A 1 101 ? 7.460  12.574  64.674  1.00 57.91 ? 101 SER A C   1 
ATOM   767  O O   . SER A 1 101 ? 8.069  11.659  65.225  1.00 59.84 ? 101 SER A O   1 
ATOM   768  C CB  . SER A 1 101 ? 8.260  14.906  65.013  1.00 45.22 ? 101 SER A CB  1 
ATOM   769  O OG  . SER A 1 101 ? 6.950  15.373  65.281  1.00 48.71 ? 101 SER A OG  1 
ATOM   770  N N   . ASP A 1 102 ? 6.128  12.582  64.545  1.00 68.77 ? 102 ASP A N   1 
ATOM   771  C CA  . ASP A 1 102 ? 5.296  11.550  65.197  1.00 79.13 ? 102 ASP A CA  1 
ATOM   772  C C   . ASP A 1 102 ? 4.585  10.390  64.475  1.00 82.10 ? 102 ASP A C   1 
ATOM   773  O O   . ASP A 1 102 ? 4.503  9.290   65.044  1.00 82.92 ? 102 ASP A O   1 
ATOM   774  C CB  . ASP A 1 102 ? 4.295  12.217  66.162  1.00 82.36 ? 102 ASP A CB  1 
ATOM   775  C CG  . ASP A 1 102 ? 4.646  11.990  67.643  1.00 83.57 ? 102 ASP A CG  1 
ATOM   776  O OD1 . ASP A 1 102 ? 5.717  11.408  67.948  1.00 84.01 ? 102 ASP A OD1 1 
ATOM   777  O OD2 . ASP A 1 102 ? 3.838  12.403  68.508  1.00 85.01 ? 102 ASP A OD2 1 
ATOM   778  N N   . ASN A 1 103 ? 4.008  10.615  63.297  1.00 84.46 ? 103 ASN A N   1 
ATOM   779  C CA  . ASN A 1 103 ? 3.308  9.513   62.615  1.00 84.41 ? 103 ASN A CA  1 
ATOM   780  C C   . ASN A 1 103 ? 4.266  8.418   62.130  1.00 82.48 ? 103 ASN A C   1 
ATOM   781  O O   . ASN A 1 103 ? 5.275  8.694   61.487  1.00 85.71 ? 103 ASN A O   1 
ATOM   782  C CB  . ASN A 1 103 ? 2.335  10.035  61.521  1.00 84.78 ? 103 ASN A CB  1 
ATOM   783  C CG  . ASN A 1 103 ? 2.855  9.876   60.081  1.00 83.45 ? 103 ASN A CG  1 
ATOM   784  O OD1 . ASN A 1 103 ? 4.047  9.957   59.804  1.00 85.02 ? 103 ASN A OD1 1 
ATOM   785  N ND2 . ASN A 1 103 ? 1.927  9.696   59.153  1.00 80.51 ? 103 ASN A ND2 1 
ATOM   786  N N   . PRO A 1 104 ? 4.001  7.165   62.521  1.00 79.46 ? 104 PRO A N   1 
ATOM   787  C CA  . PRO A 1 104 ? 4.808  5.993   62.162  1.00 76.79 ? 104 PRO A CA  1 
ATOM   788  C C   . PRO A 1 104 ? 4.789  5.621   60.684  1.00 72.85 ? 104 PRO A C   1 
ATOM   789  O O   . PRO A 1 104 ? 5.202  4.525   60.318  1.00 73.88 ? 104 PRO A O   1 
ATOM   790  C CB  . PRO A 1 104 ? 4.174  4.879   63.000  1.00 79.46 ? 104 PRO A CB  1 
ATOM   791  C CG  . PRO A 1 104 ? 3.644  5.607   64.184  1.00 82.01 ? 104 PRO A CG  1 
ATOM   792  C CD  . PRO A 1 104 ? 3.005  6.808   63.539  1.00 81.73 ? 104 PRO A CD  1 
ATOM   793  N N   . ILE A 1 105 ? 4.317  6.520   59.832  1.00 67.11 ? 105 ILE A N   1 
ATOM   794  C CA  . ILE A 1 105 ? 4.253  6.212   58.414  1.00 62.59 ? 105 ILE A CA  1 
ATOM   795  C C   . ILE A 1 105 ? 5.488  6.702   57.663  1.00 59.16 ? 105 ILE A C   1 
ATOM   796  O O   . ILE A 1 105 ? 5.858  6.129   56.641  1.00 57.30 ? 105 ILE A O   1 
ATOM   797  C CB  . ILE A 1 105 ? 3.005  6.828   57.763  1.00 64.10 ? 105 ILE A CB  1 
ATOM   798  C CG1 . ILE A 1 105 ? 1.827  6.811   58.740  1.00 62.09 ? 105 ILE A CG1 1 
ATOM   799  C CG2 . ILE A 1 105 ? 2.667  6.079   56.482  1.00 65.22 ? 105 ILE A CG2 1 
ATOM   800  C CD1 . ILE A 1 105 ? 1.553  5.469   59.360  1.00 67.47 ? 105 ILE A CD1 1 
ATOM   801  N N   . PHE A 1 106 ? 6.108  7.770   58.161  1.00 53.61 ? 106 PHE A N   1 
ATOM   802  C CA  . PHE A 1 106 ? 7.291  8.347   57.528  1.00 46.07 ? 106 PHE A CA  1 
ATOM   803  C C   . PHE A 1 106 ? 8.432  8.419   58.524  1.00 44.84 ? 106 PHE A C   1 
ATOM   804  O O   . PHE A 1 106 ? 8.206  8.381   59.741  1.00 46.20 ? 106 PHE A O   1 
ATOM   805  C CB  . PHE A 1 106 ? 6.994  9.772   57.051  1.00 42.04 ? 106 PHE A CB  1 
ATOM   806  C CG  . PHE A 1 106 ? 5.707  9.904   56.317  1.00 36.19 ? 106 PHE A CG  1 
ATOM   807  C CD1 . PHE A 1 106 ? 5.557  9.374   55.052  1.00 31.18 ? 106 PHE A CD1 1 
ATOM   808  C CD2 . PHE A 1 106 ? 4.630  10.525  56.904  1.00 38.26 ? 106 PHE A CD2 1 
ATOM   809  C CE1 . PHE A 1 106 ? 4.353  9.456   54.381  1.00 30.01 ? 106 PHE A CE1 1 
ATOM   810  C CE2 . PHE A 1 106 ? 3.420  10.612  56.236  1.00 38.01 ? 106 PHE A CE2 1 
ATOM   811  C CZ  . PHE A 1 106 ? 3.286  10.073  54.971  1.00 32.32 ? 106 PHE A CZ  1 
ATOM   812  N N   . SER A 1 107 ? 9.656  8.559   58.015  1.00 38.32 ? 107 SER A N   1 
ATOM   813  C CA  . SER A 1 107 ? 10.807 8.672   58.894  1.00 29.98 ? 107 SER A CA  1 
ATOM   814  C C   . SER A 1 107 ? 10.941 10.092  59.451  1.00 27.75 ? 107 SER A C   1 
ATOM   815  O O   . SER A 1 107 ? 10.370 11.045  58.924  1.00 27.58 ? 107 SER A O   1 
ATOM   816  C CB  . SER A 1 107 ? 12.079 8.287   58.163  1.00 27.52 ? 107 SER A CB  1 
ATOM   817  O OG  . SER A 1 107 ? 13.207 8.485   58.996  1.00 31.35 ? 107 SER A OG  1 
ATOM   818  N N   . ASP A 1 108 ? 11.737 10.219  60.504  1.00 27.08 ? 108 ASP A N   1 
ATOM   819  C CA  . ASP A 1 108 ? 11.982 11.495  61.159  1.00 19.40 ? 108 ASP A CA  1 
ATOM   820  C C   . ASP A 1 108 ? 13.404 11.996  60.932  1.00 18.05 ? 108 ASP A C   1 
ATOM   821  O O   . ASP A 1 108 ? 13.810 12.964  61.543  1.00 21.17 ? 108 ASP A O   1 
ATOM   822  C CB  . ASP A 1 108 ? 11.703 11.375  62.661  1.00 17.82 ? 108 ASP A CB  1 
ATOM   823  C CG  . ASP A 1 108 ? 12.815 10.666  63.430  1.00 22.37 ? 108 ASP A CG  1 
ATOM   824  O OD1 . ASP A 1 108 ? 13.350 9.632   62.974  1.00 23.32 ? 108 ASP A OD1 1 
ATOM   825  O OD2 . ASP A 1 108 ? 13.132 11.142  64.537  1.00 28.52 ? 108 ASP A OD2 1 
ATOM   826  N N   . HIS A 1 109 ? 14.185 11.319  60.101  1.00 17.19 ? 109 HIS A N   1 
ATOM   827  C CA  . HIS A 1 109 ? 15.537 11.776  59.846  1.00 19.07 ? 109 HIS A CA  1 
ATOM   828  C C   . HIS A 1 109 ? 16.042 11.366  58.476  1.00 24.07 ? 109 HIS A C   1 
ATOM   829  O O   . HIS A 1 109 ? 15.478 10.448  57.856  1.00 22.75 ? 109 HIS A O   1 
ATOM   830  C CB  . HIS A 1 109 ? 16.473 11.254  60.903  1.00 22.72 ? 109 HIS A CB  1 
ATOM   831  C CG  . HIS A 1 109 ? 16.425 9.776   61.059  1.00 29.33 ? 109 HIS A CG  1 
ATOM   832  N ND1 . HIS A 1 109 ? 16.841 8.911   60.075  1.00 36.24 ? 109 HIS A ND1 1 
ATOM   833  C CD2 . HIS A 1 109 ? 15.992 9.003   62.083  1.00 36.29 ? 109 HIS A CD2 1 
ATOM   834  C CE1 . HIS A 1 109 ? 16.669 7.667   60.481  1.00 41.09 ? 109 HIS A CE1 1 
ATOM   835  N NE2 . HIS A 1 109 ? 16.153 7.697   61.699  1.00 41.91 ? 109 HIS A NE2 1 
ATOM   836  N N   . GLN A 1 110 ? 17.144 12.003  58.045  1.00 27.34 ? 110 GLN A N   1 
ATOM   837  C CA  . GLN A 1 110 ? 17.759 11.757  56.735  1.00 24.11 ? 110 GLN A CA  1 
ATOM   838  C C   . GLN A 1 110 ? 19.199 12.295  56.575  1.00 24.13 ? 110 GLN A C   1 
ATOM   839  O O   . GLN A 1 110 ? 19.482 13.465  56.815  1.00 28.27 ? 110 GLN A O   1 
ATOM   840  C CB  . GLN A 1 110 ? 16.867 12.356  55.649  1.00 25.36 ? 110 GLN A CB  1 
ATOM   841  C CG  . GLN A 1 110 ? 17.248 11.976  54.234  1.00 34.00 ? 110 GLN A CG  1 
ATOM   842  C CD  . GLN A 1 110 ? 17.301 10.471  54.051  1.00 38.29 ? 110 GLN A CD  1 
ATOM   843  O OE1 . GLN A 1 110 ? 18.308 9.936   53.601  1.00 38.67 ? 110 GLN A OE1 1 
ATOM   844  N NE2 . GLN A 1 110 ? 16.236 9.777   54.446  1.00 37.60 ? 110 GLN A NE2 1 
ATOM   845  N N   . LYS A 1 111 ? 20.105 11.415  56.177  1.00 19.65 ? 111 LYS A N   1 
ATOM   846  C CA  . LYS A 1 111 ? 21.499 11.751  55.944  1.00 17.93 ? 111 LYS A CA  1 
ATOM   847  C C   . LYS A 1 111 ? 21.594 12.509  54.587  1.00 22.81 ? 111 LYS A C   1 
ATOM   848  O O   . LYS A 1 111 ? 20.857 12.220  53.642  1.00 22.52 ? 111 LYS A O   1 
ATOM   849  C CB  . LYS A 1 111 ? 22.277 10.436  55.898  1.00 18.51 ? 111 LYS A CB  1 
ATOM   850  C CG  . LYS A 1 111 ? 23.735 10.504  55.427  1.00 28.91 ? 111 LYS A CG  1 
ATOM   851  C CD  . LYS A 1 111 ? 24.234 9.090   55.107  1.00 37.13 ? 111 LYS A CD  1 
ATOM   852  C CE  . LYS A 1 111 ? 23.993 8.154   56.302  1.00 47.96 ? 111 LYS A CE  1 
ATOM   853  N NZ  . LYS A 1 111 ? 24.001 6.686   55.997  1.00 52.27 ? 111 LYS A NZ  1 
ATOM   854  N N   . ILE A 1 112 ? 22.456 13.510  54.503  1.00 21.95 ? 112 ILE A N   1 
ATOM   855  C CA  . ILE A 1 112 ? 22.618 14.268  53.274  1.00 18.51 ? 112 ILE A CA  1 
ATOM   856  C C   . ILE A 1 112 ? 24.125 14.254  53.000  1.00 22.22 ? 112 ILE A C   1 
ATOM   857  O O   . ILE A 1 112 ? 24.916 14.817  53.765  1.00 21.86 ? 112 ILE A O   1 
ATOM   858  C CB  . ILE A 1 112 ? 22.109 15.725  53.440  1.00 20.19 ? 112 ILE A CB  1 
ATOM   859  C CG1 . ILE A 1 112 ? 20.689 15.743  54.007  1.00 9.49  ? 112 ILE A CG1 1 
ATOM   860  C CG2 . ILE A 1 112 ? 22.092 16.459  52.095  1.00 19.89 ? 112 ILE A CG2 1 
ATOM   861  C CD1 . ILE A 1 112 ? 20.164 17.166  54.204  1.00 4.33  ? 112 ILE A CD1 1 
ATOM   862  N N   . PRO A 1 113 ? 24.550 13.602  51.903  1.00 18.99 ? 113 PRO A N   1 
ATOM   863  C CA  . PRO A 1 113 ? 25.967 13.515  51.547  1.00 11.79 ? 113 PRO A CA  1 
ATOM   864  C C   . PRO A 1 113 ? 26.581 14.900  51.383  1.00 16.67 ? 113 PRO A C   1 
ATOM   865  O O   . PRO A 1 113 ? 25.896 15.814  50.958  1.00 23.39 ? 113 PRO A O   1 
ATOM   866  C CB  . PRO A 1 113 ? 25.928 12.767  50.225  1.00 15.69 ? 113 PRO A CB  1 
ATOM   867  C CG  . PRO A 1 113 ? 24.640 12.012  50.276  1.00 11.98 ? 113 PRO A CG  1 
ATOM   868  C CD  . PRO A 1 113 ? 23.708 12.988  50.861  1.00 14.06 ? 113 PRO A CD  1 
ATOM   869  N N   . ALA A 1 114 ? 27.869 15.051  51.690  1.00 18.05 ? 114 ALA A N   1 
ATOM   870  C CA  . ALA A 1 114 ? 28.564 16.348  51.573  1.00 18.49 ? 114 ALA A CA  1 
ATOM   871  C C   . ALA A 1 114 ? 28.439 16.919  50.189  1.00 17.10 ? 114 ALA A C   1 
ATOM   872  O O   . ALA A 1 114 ? 28.359 16.166  49.223  1.00 21.06 ? 114 ALA A O   1 
ATOM   873  C CB  . ALA A 1 114 ? 30.051 16.191  51.893  1.00 9.63  ? 114 ALA A CB  1 
ATOM   874  N N   . GLY A 1 115 ? 28.428 18.242  50.099  1.00 16.31 ? 115 GLY A N   1 
ATOM   875  C CA  . GLY A 1 115 ? 28.366 18.917  48.805  1.00 16.67 ? 115 GLY A CA  1 
ATOM   876  C C   . GLY A 1 115 ? 27.207 18.709  47.846  1.00 18.36 ? 115 GLY A C   1 
ATOM   877  O O   . GLY A 1 115 ? 27.318 19.093  46.673  1.00 21.47 ? 115 GLY A O   1 
ATOM   878  N N   . THR A 1 116 ? 26.081 18.196  48.347  1.00 21.39 ? 116 THR A N   1 
ATOM   879  C CA  . THR A 1 116 ? 24.856 17.933  47.557  1.00 20.74 ? 116 THR A CA  1 
ATOM   880  C C   . THR A 1 116 ? 23.865 19.103  47.614  1.00 21.82 ? 116 THR A C   1 
ATOM   881  O O   . THR A 1 116 ? 23.546 19.568  48.722  1.00 18.00 ? 116 THR A O   1 
ATOM   882  C CB  . THR A 1 116 ? 24.101 16.691  48.114  1.00 15.42 ? 116 THR A CB  1 
ATOM   883  O OG1 . THR A 1 116 ? 24.939 15.532  48.017  1.00 22.67 ? 116 THR A OG1 1 
ATOM   884  C CG2 . THR A 1 116 ? 22.783 16.452  47.375  1.00 5.58  ? 116 THR A CG2 1 
ATOM   885  N N   . ILE A 1 117 ? 23.346 19.544  46.455  1.00 13.21 ? 117 ILE A N   1 
ATOM   886  C CA  . ILE A 1 117 ? 22.381 20.650  46.449  1.00 17.13 ? 117 ILE A CA  1 
ATOM   887  C C   . ILE A 1 117 ? 21.063 20.160  47.022  1.00 17.19 ? 117 ILE A C   1 
ATOM   888  O O   . ILE A 1 117 ? 20.595 19.091  46.653  1.00 19.50 ? 117 ILE A O   1 
ATOM   889  C CB  . ILE A 1 117 ? 22.147 21.261  45.016  1.00 15.34 ? 117 ILE A CB  1 
ATOM   890  C CG1 . ILE A 1 117 ? 23.335 22.139  44.610  1.00 19.32 ? 117 ILE A CG1 1 
ATOM   891  C CG2 . ILE A 1 117 ? 20.860 22.103  44.967  1.00 3.70  ? 117 ILE A CG2 1 
ATOM   892  C CD1 . ILE A 1 117 ? 23.391 23.492  45.279  1.00 13.95 ? 117 ILE A CD1 1 
ATOM   893  N N   . PHE A 1 118 ? 20.511 20.906  47.981  1.00 22.12 ? 118 PHE A N   1 
ATOM   894  C CA  . PHE A 1 118 ? 19.235 20.543  48.612  1.00 19.88 ? 118 PHE A CA  1 
ATOM   895  C C   . PHE A 1 118 ? 18.397 21.753  49.039  1.00 16.75 ? 118 PHE A C   1 
ATOM   896  O O   . PHE A 1 118 ? 18.934 22.832  49.274  1.00 19.19 ? 118 PHE A O   1 
ATOM   897  C CB  . PHE A 1 118 ? 19.456 19.586  49.816  1.00 22.05 ? 118 PHE A CB  1 
ATOM   898  C CG  . PHE A 1 118 ? 20.023 20.249  51.060  1.00 13.18 ? 118 PHE A CG  1 
ATOM   899  C CD1 . PHE A 1 118 ? 21.407 20.429  51.214  1.00 8.69  ? 118 PHE A CD1 1 
ATOM   900  C CD2 . PHE A 1 118 ? 19.176 20.676  52.084  1.00 19.74 ? 118 PHE A CD2 1 
ATOM   901  C CE1 . PHE A 1 118 ? 21.935 21.025  52.373  1.00 14.93 ? 118 PHE A CE1 1 
ATOM   902  C CE2 . PHE A 1 118 ? 19.687 21.272  53.255  1.00 16.03 ? 118 PHE A CE2 1 
ATOM   903  C CZ  . PHE A 1 118 ? 21.076 21.447  53.396  1.00 12.36 ? 118 PHE A CZ  1 
ATOM   904  N N   . TYR A 1 119 ? 17.076 21.594  49.011  1.00 16.52 ? 119 TYR A N   1 
ATOM   905  C CA  . TYR A 1 119 ? 16.170 22.637  49.446  1.00 17.14 ? 119 TYR A CA  1 
ATOM   906  C C   . TYR A 1 119 ? 15.108 22.032  50.376  1.00 18.06 ? 119 TYR A C   1 
ATOM   907  O O   . TYR A 1 119 ? 14.906 20.818  50.383  1.00 21.46 ? 119 TYR A O   1 
ATOM   908  C CB  . TYR A 1 119 ? 15.635 23.524  48.306  1.00 15.21 ? 119 TYR A CB  1 
ATOM   909  C CG  . TYR A 1 119 ? 14.832 22.892  47.204  1.00 14.30 ? 119 TYR A CG  1 
ATOM   910  C CD1 . TYR A 1 119 ? 13.461 22.765  47.321  1.00 17.68 ? 119 TYR A CD1 1 
ATOM   911  C CD2 . TYR A 1 119 ? 15.434 22.470  46.010  1.00 24.56 ? 119 TYR A CD2 1 
ATOM   912  C CE1 . TYR A 1 119 ? 12.694 22.236  46.287  1.00 21.78 ? 119 TYR A CE1 1 
ATOM   913  C CE2 . TYR A 1 119 ? 14.665 21.930  44.949  1.00 14.46 ? 119 TYR A CE2 1 
ATOM   914  C CZ  . TYR A 1 119 ? 13.294 21.815  45.109  1.00 20.13 ? 119 TYR A CZ  1 
ATOM   915  O OH  . TYR A 1 119 ? 12.502 21.208  44.155  1.00 24.64 ? 119 TYR A OH  1 
ATOM   916  N N   . LEU A 1 120 ? 14.516 22.865  51.223  1.00 17.60 ? 120 LEU A N   1 
ATOM   917  C CA  . LEU A 1 120 ? 13.594 22.403  52.257  1.00 18.71 ? 120 LEU A CA  1 
ATOM   918  C C   . LEU A 1 120 ? 12.294 23.174  52.329  1.00 18.38 ? 120 LEU A C   1 
ATOM   919  O O   . LEU A 1 120 ? 12.286 24.410  52.217  1.00 15.53 ? 120 LEU A O   1 
ATOM   920  C CB  . LEU A 1 120 ? 14.303 22.560  53.599  1.00 16.50 ? 120 LEU A CB  1 
ATOM   921  C CG  . LEU A 1 120 ? 13.977 21.788  54.853  1.00 19.98 ? 120 LEU A CG  1 
ATOM   922  C CD1 . LEU A 1 120 ? 14.484 20.365  54.772  1.00 19.20 ? 120 LEU A CD1 1 
ATOM   923  C CD2 . LEU A 1 120 ? 14.679 22.504  55.960  1.00 19.23 ? 120 LEU A CD2 1 
ATOM   924  N N   . VAL A 1 121 ? 11.222 22.442  52.619  1.00 13.81 ? 121 VAL A N   1 
ATOM   925  C CA  . VAL A 1 121 ? 9.888  23.008  52.729  1.00 15.18 ? 121 VAL A CA  1 
ATOM   926  C C   . VAL A 1 121 ? 9.111  22.551  53.998  1.00 14.75 ? 121 VAL A C   1 
ATOM   927  O O   . VAL A 1 121 ? 9.173  21.393  54.382  1.00 12.25 ? 121 VAL A O   1 
ATOM   928  C CB  . VAL A 1 121 ? 9.033  22.577  51.485  1.00 15.67 ? 121 VAL A CB  1 
ATOM   929  C CG1 . VAL A 1 121 ? 7.595  23.116  51.576  1.00 15.28 ? 121 VAL A CG1 1 
ATOM   930  C CG2 . VAL A 1 121 ? 9.695  22.995  50.194  1.00 11.86 ? 121 VAL A CG2 1 
ATOM   931  N N   . ASN A 1 122 ? 8.398  23.477  54.637  1.00 18.08 ? 122 ASN A N   1 
ATOM   932  C CA  . ASN A 1 122 ? 7.505  23.162  55.762  1.00 21.57 ? 122 ASN A CA  1 
ATOM   933  C C   . ASN A 1 122 ? 6.133  23.328  55.098  1.00 18.54 ? 122 ASN A C   1 
ATOM   934  O O   . ASN A 1 122 ? 5.623  24.443  55.003  1.00 18.63 ? 122 ASN A O   1 
ATOM   935  C CB  . ASN A 1 122 ? 7.634  24.180  56.896  1.00 20.60 ? 122 ASN A CB  1 
ATOM   936  C CG  . ASN A 1 122 ? 6.467  24.112  57.892  1.00 22.35 ? 122 ASN A CG  1 
ATOM   937  O OD1 . ASN A 1 122 ? 6.174  25.084  58.571  1.00 25.52 ? 122 ASN A OD1 1 
ATOM   938  N ND2 . ASN A 1 122 ? 5.841  22.955  58.012  1.00 26.89 ? 122 ASN A ND2 1 
ATOM   939  N N   . PRO A 1 123 ? 5.522  22.222  54.626  1.00 22.04 ? 123 PRO A N   1 
ATOM   940  C CA  . PRO A 1 123 ? 4.215  22.269  53.956  1.00 24.70 ? 123 PRO A CA  1 
ATOM   941  C C   . PRO A 1 123 ? 2.992  22.458  54.829  1.00 31.17 ? 123 PRO A C   1 
ATOM   942  O O   . PRO A 1 123 ? 1.889  22.634  54.316  1.00 38.33 ? 123 PRO A O   1 
ATOM   943  C CB  . PRO A 1 123 ? 4.161  20.926  53.242  1.00 19.90 ? 123 PRO A CB  1 
ATOM   944  C CG  . PRO A 1 123 ? 4.827  20.040  54.202  1.00 16.21 ? 123 PRO A CG  1 
ATOM   945  C CD  . PRO A 1 123 ? 6.036  20.837  54.634  1.00 18.76 ? 123 PRO A CD  1 
ATOM   946  N N   . ASP A 1 124 ? 3.180  22.384  56.142  1.00 36.63 ? 124 ASP A N   1 
ATOM   947  C CA  . ASP A 1 124 ? 2.089  22.534  57.101  1.00 34.95 ? 124 ASP A CA  1 
ATOM   948  C C   . ASP A 1 124 ? 1.537  23.967  57.104  1.00 36.88 ? 124 ASP A C   1 
ATOM   949  O O   . ASP A 1 124 ? 2.286  24.945  57.005  1.00 37.69 ? 124 ASP A O   1 
ATOM   950  C CB  . ASP A 1 124 ? 2.590  22.148  58.486  1.00 37.00 ? 124 ASP A CB  1 
ATOM   951  C CG  . ASP A 1 124 ? 1.498  21.607  59.365  1.00 39.69 ? 124 ASP A CG  1 
ATOM   952  O OD1 . ASP A 1 124 ? 0.701  22.422  59.883  1.00 43.27 ? 124 ASP A OD1 1 
ATOM   953  O OD2 . ASP A 1 124 ? 1.448  20.369  59.545  1.00 41.58 ? 124 ASP A OD2 1 
ATOM   954  N N   . PRO A 1 125 ? 0.211  24.110  57.226  1.00 37.10 ? 125 PRO A N   1 
ATOM   955  C CA  . PRO A 1 125 ? -0.409 25.431  57.234  1.00 36.31 ? 125 PRO A CA  1 
ATOM   956  C C   . PRO A 1 125 ? -0.559 26.053  58.627  1.00 38.83 ? 125 PRO A C   1 
ATOM   957  O O   . PRO A 1 125 ? -0.979 27.206  58.754  1.00 41.44 ? 125 PRO A O   1 
ATOM   958  C CB  . PRO A 1 125 ? -1.750 25.145  56.600  1.00 35.16 ? 125 PRO A CB  1 
ATOM   959  C CG  . PRO A 1 125 ? -2.107 23.851  57.244  1.00 38.19 ? 125 PRO A CG  1 
ATOM   960  C CD  . PRO A 1 125 ? -0.817 23.059  57.142  1.00 39.13 ? 125 PRO A CD  1 
ATOM   961  N N   . LYS A 1 126 ? -0.184 25.316  59.667  1.00 39.70 ? 126 LYS A N   1 
ATOM   962  C CA  . LYS A 1 126 ? -0.308 25.838  61.021  1.00 40.02 ? 126 LYS A CA  1 
ATOM   963  C C   . LYS A 1 126 ? 0.913  25.653  61.920  1.00 40.91 ? 126 LYS A C   1 
ATOM   964  O O   . LYS A 1 126 ? 1.218  26.520  62.741  1.00 40.41 ? 126 LYS A O   1 
ATOM   965  C CB  . LYS A 1 126 ? -1.546 25.241  61.678  1.00 45.08 ? 126 LYS A CB  1 
ATOM   966  C CG  . LYS A 1 126 ? -2.834 25.692  61.013  1.00 56.42 ? 126 LYS A CG  1 
ATOM   967  C CD  . LYS A 1 126 ? -4.040 24.863  61.428  1.00 65.33 ? 126 LYS A CD  1 
ATOM   968  C CE  . LYS A 1 126 ? -4.017 23.462  60.824  1.00 70.15 ? 126 LYS A CE  1 
ATOM   969  N NZ  . LYS A 1 126 ? -5.306 22.748  61.074  1.00 73.30 ? 126 LYS A NZ  1 
ATOM   970  N N   . GLU A 1 127 ? 1.656  24.572  61.702  1.00 40.45 ? 127 GLU A N   1 
ATOM   971  C CA  . GLU A 1 127 ? 2.832  24.233  62.517  1.00 40.36 ? 127 GLU A CA  1 
ATOM   972  C C   . GLU A 1 127 ? 4.204  24.741  62.067  1.00 35.92 ? 127 GLU A C   1 
ATOM   973  O O   . GLU A 1 127 ? 4.489  24.800  60.875  1.00 37.81 ? 127 GLU A O   1 
ATOM   974  C CB  . GLU A 1 127 ? 2.913  22.714  62.640  1.00 45.00 ? 127 GLU A CB  1 
ATOM   975  C CG  . GLU A 1 127 ? 1.672  22.074  63.223  1.00 52.18 ? 127 GLU A CG  1 
ATOM   976  C CD  . GLU A 1 127 ? 1.816  21.788  64.694  1.00 57.08 ? 127 GLU A CD  1 
ATOM   977  O OE1 . GLU A 1 127 ? 2.130  22.726  65.460  1.00 58.23 ? 127 GLU A OE1 1 
ATOM   978  O OE2 . GLU A 1 127 ? 1.630  20.614  65.077  1.00 63.22 ? 127 GLU A OE2 1 
ATOM   979  N N   . ASP A 1 128 ? 5.064  25.060  63.031  1.00 32.71 ? 128 ASP A N   1 
ATOM   980  C CA  . ASP A 1 128 ? 6.429  25.498  62.728  1.00 33.07 ? 128 ASP A CA  1 
ATOM   981  C C   . ASP A 1 128 ? 7.309  24.255  62.538  1.00 32.24 ? 128 ASP A C   1 
ATOM   982  O O   . ASP A 1 128 ? 6.943  23.157  62.963  1.00 35.07 ? 128 ASP A O   1 
ATOM   983  C CB  . ASP A 1 128 ? 7.006  26.365  63.857  1.00 33.79 ? 128 ASP A CB  1 
ATOM   984  C CG  . ASP A 1 128 ? 6.585  27.838  63.762  1.00 36.43 ? 128 ASP A CG  1 
ATOM   985  O OD1 . ASP A 1 128 ? 5.450  28.127  63.316  1.00 39.31 ? 128 ASP A OD1 1 
ATOM   986  O OD2 . ASP A 1 128 ? 7.400  28.712  64.146  1.00 33.63 ? 128 ASP A OD2 1 
ATOM   987  N N   . LEU A 1 129 ? 8.465  24.428  61.908  1.00 25.80 ? 129 LEU A N   1 
ATOM   988  C CA  . LEU A 1 129 ? 9.373  23.329  61.656  1.00 20.22 ? 129 LEU A CA  1 
ATOM   989  C C   . LEU A 1 129 ? 10.561 23.492  62.564  1.00 23.91 ? 129 LEU A C   1 
ATOM   990  O O   . LEU A 1 129 ? 11.204 24.548  62.544  1.00 27.83 ? 129 LEU A O   1 
ATOM   991  C CB  . LEU A 1 129 ? 9.892  23.397  60.219  1.00 17.90 ? 129 LEU A CB  1 
ATOM   992  C CG  . LEU A 1 129 ? 10.081 22.110  59.426  1.00 17.52 ? 129 LEU A CG  1 
ATOM   993  C CD1 . LEU A 1 129 ? 11.027 22.338  58.268  1.00 13.92 ? 129 LEU A CD1 1 
ATOM   994  C CD2 . LEU A 1 129 ? 10.588 21.012  60.317  1.00 19.16 ? 129 LEU A CD2 1 
ATOM   995  N N   . ARG A 1 130 ? 10.874 22.462  63.342  1.00 19.50 ? 130 ARG A N   1 
ATOM   996  C CA  . ARG A 1 130 ? 12.043 22.519  64.210  1.00 23.29 ? 130 ARG A CA  1 
ATOM   997  C C   . ARG A 1 130 ? 12.913 21.357  63.797  1.00 23.63 ? 130 ARG A C   1 
ATOM   998  O O   . ARG A 1 130 ? 12.444 20.207  63.785  1.00 24.14 ? 130 ARG A O   1 
ATOM   999  C CB  . ARG A 1 130 ? 11.669 22.417  65.696  1.00 20.76 ? 130 ARG A CB  1 
ATOM   1000 C CG  . ARG A 1 130 ? 10.814 23.573  66.210  1.00 22.30 ? 130 ARG A CG  1 
ATOM   1001 C CD  . ARG A 1 130 ? 10.446 23.395  67.671  1.00 21.67 ? 130 ARG A CD  1 
ATOM   1002 N NE  . ARG A 1 130 ? 11.590 23.640  68.544  1.00 28.13 ? 130 ARG A NE  1 
ATOM   1003 C CZ  . ARG A 1 130 ? 11.825 22.990  69.684  1.00 29.98 ? 130 ARG A CZ  1 
ATOM   1004 N NH1 . ARG A 1 130 ? 10.998 22.028  70.083  1.00 28.46 ? 130 ARG A NH1 1 
ATOM   1005 N NH2 . ARG A 1 130 ? 12.903 23.289  70.411  1.00 27.88 ? 130 ARG A NH2 1 
ATOM   1006 N N   . ILE A 1 131 ? 14.166 21.671  63.450  1.00 23.32 ? 131 ILE A N   1 
ATOM   1007 C CA  . ILE A 1 131 ? 15.166 20.697  63.003  1.00 19.96 ? 131 ILE A CA  1 
ATOM   1008 C C   . ILE A 1 131 ? 16.492 20.782  63.755  1.00 17.75 ? 131 ILE A C   1 
ATOM   1009 O O   . ILE A 1 131 ? 17.033 21.859  63.996  1.00 21.15 ? 131 ILE A O   1 
ATOM   1010 C CB  . ILE A 1 131 ? 15.483 20.877  61.495  1.00 19.33 ? 131 ILE A CB  1 
ATOM   1011 C CG1 . ILE A 1 131 ? 14.414 20.232  60.637  1.00 17.26 ? 131 ILE A CG1 1 
ATOM   1012 C CG2 . ILE A 1 131 ? 16.838 20.305  61.155  1.00 18.67 ? 131 ILE A CG2 1 
ATOM   1013 C CD1 . ILE A 1 131 ? 14.455 20.718  59.215  1.00 20.94 ? 131 ILE A CD1 1 
ATOM   1014 N N   . ILE A 1 132 ? 17.062 19.622  64.031  1.00 18.52 ? 132 ILE A N   1 
ATOM   1015 C CA  . ILE A 1 132 ? 18.336 19.536  64.718  1.00 21.09 ? 132 ILE A CA  1 
ATOM   1016 C C   . ILE A 1 132 ? 19.199 18.608  63.820  1.00 20.59 ? 132 ILE A C   1 
ATOM   1017 O O   . ILE A 1 132 ? 18.679 17.632  63.259  1.00 17.62 ? 132 ILE A O   1 
ATOM   1018 C CB  . ILE A 1 132 ? 18.124 18.969  66.164  1.00 23.27 ? 132 ILE A CB  1 
ATOM   1019 C CG1 . ILE A 1 132 ? 19.400 19.064  67.006  1.00 23.21 ? 132 ILE A CG1 1 
ATOM   1020 C CG2 . ILE A 1 132 ? 17.593 17.538  66.107  1.00 27.60 ? 132 ILE A CG2 1 
ATOM   1021 C CD1 . ILE A 1 132 ? 19.842 20.483  67.336  1.00 19.92 ? 132 ILE A CD1 1 
ATOM   1022 N N   . GLN A 1 133 ? 20.476 18.949  63.608  1.00 18.69 ? 133 GLN A N   1 
ATOM   1023 C CA  . GLN A 1 133 ? 21.314 18.112  62.768  1.00 24.13 ? 133 GLN A CA  1 
ATOM   1024 C C   . GLN A 1 133 ? 22.769 18.053  63.131  1.00 22.45 ? 133 GLN A C   1 
ATOM   1025 O O   . GLN A 1 133 ? 23.363 19.079  63.495  1.00 22.25 ? 133 GLN A O   1 
ATOM   1026 C CB  . GLN A 1 133 ? 21.188 18.518  61.300  1.00 26.85 ? 133 GLN A CB  1 
ATOM   1027 C CG  . GLN A 1 133 ? 21.749 19.860  60.958  1.00 30.03 ? 133 GLN A CG  1 
ATOM   1028 C CD  . GLN A 1 133 ? 21.302 20.322  59.592  1.00 41.35 ? 133 GLN A CD  1 
ATOM   1029 O OE1 . GLN A 1 133 ? 21.121 21.518  59.357  1.00 48.54 ? 133 GLN A OE1 1 
ATOM   1030 N NE2 . GLN A 1 133 ? 21.095 19.376  58.681  1.00 43.24 ? 133 GLN A NE2 1 
ATOM   1031 N N   . LEU A 1 134 ? 23.329 16.843  62.999  1.00 19.71 ? 134 LEU A N   1 
ATOM   1032 C CA  . LEU A 1 134 ? 24.747 16.573  63.266  1.00 17.94 ? 134 LEU A CA  1 
ATOM   1033 C C   . LEU A 1 134 ? 25.518 16.798  61.956  1.00 18.84 ? 134 LEU A C   1 
ATOM   1034 O O   . LEU A 1 134 ? 25.127 16.270  60.913  1.00 18.07 ? 134 LEU A O   1 
ATOM   1035 C CB  . LEU A 1 134 ? 24.947 15.129  63.735  1.00 12.39 ? 134 LEU A CB  1 
ATOM   1036 C CG  . LEU A 1 134 ? 26.347 14.844  64.285  1.00 13.42 ? 134 LEU A CG  1 
ATOM   1037 C CD1 . LEU A 1 134 ? 26.603 15.687  65.521  1.00 11.86 ? 134 LEU A CD1 1 
ATOM   1038 C CD2 . LEU A 1 134 ? 26.513 13.359  64.579  1.00 12.85 ? 134 LEU A CD2 1 
ATOM   1039 N N   . ALA A 1 135 ? 26.628 17.531  62.029  1.00 17.19 ? 135 ALA A N   1 
ATOM   1040 C CA  . ALA A 1 135 ? 27.420 17.859  60.860  1.00 15.84 ? 135 ALA A CA  1 
ATOM   1041 C C   . ALA A 1 135 ? 28.837 17.366  60.982  1.00 19.57 ? 135 ALA A C   1 
ATOM   1042 O O   . ALA A 1 135 ? 29.398 17.394  62.063  1.00 22.75 ? 135 ALA A O   1 
ATOM   1043 C CB  . ALA A 1 135 ? 27.429 19.348  60.689  1.00 17.37 ? 135 ALA A CB  1 
ATOM   1044 N N   . MET A 1 136 ? 29.423 16.924  59.877  1.00 21.03 ? 136 MET A N   1 
ATOM   1045 C CA  . MET A 1 136 ? 30.822 16.472  59.873  1.00 24.44 ? 136 MET A CA  1 
ATOM   1046 C C   . MET A 1 136 ? 31.530 17.199  58.715  1.00 24.59 ? 136 MET A C   1 
ATOM   1047 O O   . MET A 1 136 ? 31.470 16.735  57.566  1.00 27.01 ? 136 MET A O   1 
ATOM   1048 C CB  . MET A 1 136 ? 30.917 14.952  59.666  1.00 27.83 ? 136 MET A CB  1 
ATOM   1049 C CG  . MET A 1 136 ? 30.365 14.111  60.798  1.00 28.16 ? 136 MET A CG  1 
ATOM   1050 S SD  . MET A 1 136 ? 28.577 14.027  60.833  1.00 46.53 ? 136 MET A SD  1 
ATOM   1051 C CE  . MET A 1 136 ? 28.247 12.441  59.882  1.00 24.10 ? 136 MET A CE  1 
ATOM   1052 N N   . PRO A 1 137 ? 32.124 18.391  58.983  1.00 22.82 ? 137 PRO A N   1 
ATOM   1053 C CA  . PRO A 1 137 ? 32.804 19.147  57.923  1.00 18.62 ? 137 PRO A CA  1 
ATOM   1054 C C   . PRO A 1 137 ? 33.992 18.454  57.288  1.00 21.21 ? 137 PRO A C   1 
ATOM   1055 O O   . PRO A 1 137 ? 34.785 17.789  57.965  1.00 26.54 ? 137 PRO A O   1 
ATOM   1056 C CB  . PRO A 1 137 ? 33.144 20.485  58.592  1.00 19.07 ? 137 PRO A CB  1 
ATOM   1057 C CG  . PRO A 1 137 ? 33.118 20.159  60.103  1.00 18.40 ? 137 PRO A CG  1 
ATOM   1058 C CD  . PRO A 1 137 ? 31.990 19.201  60.214  1.00 15.56 ? 137 PRO A CD  1 
ATOM   1059 N N   . VAL A 1 138 ? 34.104 18.602  55.972  1.00 16.87 ? 138 VAL A N   1 
ATOM   1060 C CA  . VAL A 1 138 ? 35.156 17.944  55.241  1.00 8.92  ? 138 VAL A CA  1 
ATOM   1061 C C   . VAL A 1 138 ? 36.490 18.627  55.231  1.00 7.60  ? 138 VAL A C   1 
ATOM   1062 O O   . VAL A 1 138 ? 37.500 17.957  55.301  1.00 5.76  ? 138 VAL A O   1 
ATOM   1063 C CB  . VAL A 1 138 ? 34.729 17.697  53.768  1.00 17.53 ? 138 VAL A CB  1 
ATOM   1064 C CG1 . VAL A 1 138 ? 35.843 17.020  52.980  1.00 14.09 ? 138 VAL A CG1 1 
ATOM   1065 C CG2 . VAL A 1 138 ? 33.486 16.870  53.722  1.00 14.29 ? 138 VAL A CG2 1 
ATOM   1066 N N   . ASN A 1 139 ? 36.507 19.956  55.156  1.00 8.47  ? 139 ASN A N   1 
ATOM   1067 C CA  . ASN A 1 139 ? 37.756 20.705  55.037  1.00 10.65 ? 139 ASN A CA  1 
ATOM   1068 C C   . ASN A 1 139 ? 38.596 21.080  56.274  1.00 12.77 ? 139 ASN A C   1 
ATOM   1069 O O   . ASN A 1 139 ? 39.845 21.120  56.223  1.00 9.39  ? 139 ASN A O   1 
ATOM   1070 C CB  . ASN A 1 139 ? 37.487 21.953  54.193  1.00 5.55  ? 139 ASN A CB  1 
ATOM   1071 C CG  . ASN A 1 139 ? 37.036 21.606  52.764  1.00 7.26  ? 139 ASN A CG  1 
ATOM   1072 O OD1 . ASN A 1 139 ? 37.787 21.029  51.965  1.00 8.63  ? 139 ASN A OD1 1 
ATOM   1073 N ND2 . ASN A 1 139 ? 35.811 21.953  52.446  1.00 2.00  ? 139 ASN A ND2 1 
ATOM   1074 N N   . ASN A 1 140 ? 37.911 21.427  57.353  1.00 18.01 ? 140 ASN A N   1 
ATOM   1075 C CA  . ASN A 1 140 ? 38.549 21.848  58.606  1.00 17.10 ? 140 ASN A CA  1 
ATOM   1076 C C   . ASN A 1 140 ? 37.380 21.947  59.578  1.00 19.23 ? 140 ASN A C   1 
ATOM   1077 O O   . ASN A 1 140 ? 36.273 21.561  59.208  1.00 16.50 ? 140 ASN A O   1 
ATOM   1078 C CB  . ASN A 1 140 ? 39.316 23.184  58.438  1.00 16.86 ? 140 ASN A CB  1 
ATOM   1079 C CG  . ASN A 1 140 ? 38.466 24.298  57.822  1.00 20.72 ? 140 ASN A CG  1 
ATOM   1080 O OD1 . ASN A 1 140 ? 37.309 24.528  58.202  1.00 19.36 ? 140 ASN A OD1 1 
ATOM   1081 N ND2 . ASN A 1 140 ? 39.040 24.988  56.848  1.00 27.28 ? 140 ASN A ND2 1 
ATOM   1082 N N   . PRO A 1 141 ? 37.595 22.425  60.828  1.00 21.18 ? 141 PRO A N   1 
ATOM   1083 C CA  . PRO A 1 141 ? 36.485 22.518  61.791  1.00 18.56 ? 141 PRO A CA  1 
ATOM   1084 C C   . PRO A 1 141 ? 35.254 23.360  61.514  1.00 19.96 ? 141 PRO A C   1 
ATOM   1085 O O   . PRO A 1 141 ? 34.236 23.158  62.159  1.00 26.97 ? 141 PRO A O   1 
ATOM   1086 C CB  . PRO A 1 141 ? 37.178 22.960  63.074  1.00 17.21 ? 141 PRO A CB  1 
ATOM   1087 C CG  . PRO A 1 141 ? 38.544 22.348  62.949  1.00 17.22 ? 141 PRO A CG  1 
ATOM   1088 C CD  . PRO A 1 141 ? 38.882 22.676  61.508  1.00 16.75 ? 141 PRO A CD  1 
ATOM   1089 N N   . GLN A 1 142 ? 35.374 24.340  60.644  1.00 23.14 ? 142 GLN A N   1 
ATOM   1090 C CA  . GLN A 1 142 ? 34.257 25.212  60.291  1.00 26.40 ? 142 GLN A CA  1 
ATOM   1091 C C   . GLN A 1 142 ? 33.269 24.525  59.350  1.00 27.72 ? 142 GLN A C   1 
ATOM   1092 O O   . GLN A 1 142 ? 33.604 23.569  58.656  1.00 30.00 ? 142 GLN A O   1 
ATOM   1093 C CB  . GLN A 1 142 ? 34.788 26.473  59.585  1.00 26.19 ? 142 GLN A CB  1 
ATOM   1094 C CG  . GLN A 1 142 ? 35.209 27.553  60.521  1.00 33.29 ? 142 GLN A CG  1 
ATOM   1095 C CD  . GLN A 1 142 ? 35.942 27.008  61.703  1.00 34.65 ? 142 GLN A CD  1 
ATOM   1096 O OE1 . GLN A 1 142 ? 37.032 26.453  61.565  1.00 40.77 ? 142 GLN A OE1 1 
ATOM   1097 N NE2 . GLN A 1 142 ? 35.331 27.105  62.887  1.00 38.25 ? 142 GLN A NE2 1 
ATOM   1098 N N   . ILE A 1 143 ? 32.026 24.979  59.363  1.00 28.28 ? 143 ILE A N   1 
ATOM   1099 C CA  . ILE A 1 143 ? 31.027 24.430  58.452  1.00 31.10 ? 143 ILE A CA  1 
ATOM   1100 C C   . ILE A 1 143 ? 30.675 25.576  57.523  1.00 29.66 ? 143 ILE A C   1 
ATOM   1101 O O   . ILE A 1 143 ? 30.353 26.670  57.971  1.00 34.95 ? 143 ILE A O   1 
ATOM   1102 C CB  . ILE A 1 143 ? 29.768 23.838  59.148  1.00 31.84 ? 143 ILE A CB  1 
ATOM   1103 C CG1 . ILE A 1 143 ? 28.525 24.166  58.325  1.00 35.20 ? 143 ILE A CG1 1 
ATOM   1104 C CG2 . ILE A 1 143 ? 29.663 24.277  60.613  1.00 35.57 ? 143 ILE A CG2 1 
ATOM   1105 C CD1 . ILE A 1 143 ? 27.658 22.977  58.070  1.00 41.21 ? 143 ILE A CD1 1 
ATOM   1106 N N   . HIS A 1 144 ? 30.749 25.307  56.224  1.00 29.49 ? 144 HIS A N   1 
ATOM   1107 C CA  . HIS A 1 144 ? 30.496 26.310  55.205  1.00 21.32 ? 144 HIS A CA  1 
ATOM   1108 C C   . HIS A 1 144 ? 29.257 26.020  54.364  1.00 20.15 ? 144 HIS A C   1 
ATOM   1109 O O   . HIS A 1 144 ? 29.132 24.926  53.796  1.00 18.26 ? 144 HIS A O   1 
ATOM   1110 C CB  . HIS A 1 144 ? 31.736 26.438  54.318  1.00 22.93 ? 144 HIS A CB  1 
ATOM   1111 C CG  . HIS A 1 144 ? 32.980 26.821  55.061  1.00 18.67 ? 144 HIS A CG  1 
ATOM   1112 N ND1 . HIS A 1 144 ? 33.987 25.926  55.359  1.00 19.81 ? 144 HIS A ND1 1 
ATOM   1113 C CD2 . HIS A 1 144 ? 33.345 27.991  55.644  1.00 9.47  ? 144 HIS A CD2 1 
ATOM   1114 C CE1 . HIS A 1 144 ? 34.907 26.521  56.093  1.00 16.24 ? 144 HIS A CE1 1 
ATOM   1115 N NE2 . HIS A 1 144 ? 34.540 27.774  56.280  1.00 13.06 ? 144 HIS A NE2 1 
ATOM   1116 N N   . GLU A 1 145 ? 28.323 26.980  54.317  1.00 23.00 ? 145 GLU A N   1 
ATOM   1117 C CA  . GLU A 1 145 ? 27.101 26.857  53.514  1.00 21.50 ? 145 GLU A CA  1 
ATOM   1118 C C   . GLU A 1 145 ? 27.165 27.763  52.297  1.00 19.40 ? 145 GLU A C   1 
ATOM   1119 O O   . GLU A 1 145 ? 27.291 28.984  52.424  1.00 18.48 ? 145 GLU A O   1 
ATOM   1120 C CB  . GLU A 1 145 ? 25.874 27.284  54.292  1.00 25.21 ? 145 GLU A CB  1 
ATOM   1121 C CG  . GLU A 1 145 ? 25.590 26.486  55.508  1.00 41.72 ? 145 GLU A CG  1 
ATOM   1122 C CD  . GLU A 1 145 ? 24.325 26.949  56.169  1.00 48.76 ? 145 GLU A CD  1 
ATOM   1123 O OE1 . GLU A 1 145 ? 23.300 27.079  55.453  1.00 51.85 ? 145 GLU A OE1 1 
ATOM   1124 O OE2 . GLU A 1 145 ? 24.364 27.194  57.397  1.00 54.20 ? 145 GLU A OE2 1 
ATOM   1125 N N   . PHE A 1 146 ? 27.066 27.175  51.118  1.00 17.57 ? 146 PHE A N   1 
ATOM   1126 C CA  . PHE A 1 146 ? 27.074 27.962  49.908  1.00 12.27 ? 146 PHE A CA  1 
ATOM   1127 C C   . PHE A 1 146 ? 25.661 28.104  49.363  1.00 13.55 ? 146 PHE A C   1 
ATOM   1128 O O   . PHE A 1 146 ? 25.049 27.112  48.990  1.00 13.71 ? 146 PHE A O   1 
ATOM   1129 C CB  . PHE A 1 146 ? 27.977 27.306  48.907  1.00 11.61 ? 146 PHE A CB  1 
ATOM   1130 C CG  . PHE A 1 146 ? 29.422 27.486  49.209  1.00 14.60 ? 146 PHE A CG  1 
ATOM   1131 C CD1 . PHE A 1 146 ? 30.099 26.575  50.019  1.00 18.79 ? 146 PHE A CD1 1 
ATOM   1132 C CD2 . PHE A 1 146 ? 30.132 28.561  48.656  1.00 16.97 ? 146 PHE A CD2 1 
ATOM   1133 C CE1 . PHE A 1 146 ? 31.481 26.730  50.275  1.00 19.19 ? 146 PHE A CE1 1 
ATOM   1134 C CE2 . PHE A 1 146 ? 31.512 28.725  48.904  1.00 14.99 ? 146 PHE A CE2 1 
ATOM   1135 C CZ  . PHE A 1 146 ? 32.182 27.808  49.712  1.00 19.29 ? 146 PHE A CZ  1 
ATOM   1136 N N   . PHE A 1 147 ? 25.128 29.327  49.383  1.00 12.75 ? 147 PHE A N   1 
ATOM   1137 C CA  . PHE A 1 147 ? 23.783 29.611  48.890  1.00 18.19 ? 147 PHE A CA  1 
ATOM   1138 C C   . PHE A 1 147 ? 23.836 30.028  47.454  1.00 20.41 ? 147 PHE A C   1 
ATOM   1139 O O   . PHE A 1 147 ? 24.661 30.853  47.073  1.00 24.84 ? 147 PHE A O   1 
ATOM   1140 C CB  . PHE A 1 147 ? 23.098 30.711  49.700  1.00 15.77 ? 147 PHE A CB  1 
ATOM   1141 C CG  . PHE A 1 147 ? 22.458 30.217  50.957  1.00 12.34 ? 147 PHE A CG  1 
ATOM   1142 C CD1 . PHE A 1 147 ? 21.173 29.716  50.931  1.00 14.12 ? 147 PHE A CD1 1 
ATOM   1143 C CD2 . PHE A 1 147 ? 23.173 30.164  52.140  1.00 17.67 ? 147 PHE A CD2 1 
ATOM   1144 C CE1 . PHE A 1 147 ? 20.610 29.164  52.052  1.00 16.18 ? 147 PHE A CE1 1 
ATOM   1145 C CE2 . PHE A 1 147 ? 22.614 29.609  53.277  1.00 17.02 ? 147 PHE A CE2 1 
ATOM   1146 C CZ  . PHE A 1 147 ? 21.332 29.106  53.233  1.00 18.16 ? 147 PHE A CZ  1 
ATOM   1147 N N   . LEU A 1 148 ? 22.952 29.442  46.658  1.00 25.35 ? 148 LEU A N   1 
ATOM   1148 C CA  . LEU A 1 148 ? 22.883 29.720  45.239  1.00 21.83 ? 148 LEU A CA  1 
ATOM   1149 C C   . LEU A 1 148 ? 22.138 31.019  45.013  1.00 23.45 ? 148 LEU A C   1 
ATOM   1150 O O   . LEU A 1 148 ? 22.451 31.766  44.081  1.00 20.71 ? 148 LEU A O   1 
ATOM   1151 C CB  . LEU A 1 148 ? 22.140 28.592  44.529  1.00 25.06 ? 148 LEU A CB  1 
ATOM   1152 C CG  . LEU A 1 148 ? 22.792 28.008  43.261  1.00 30.55 ? 148 LEU A CG  1 
ATOM   1153 C CD1 . LEU A 1 148 ? 21.808 27.128  42.535  1.00 30.27 ? 148 LEU A CD1 1 
ATOM   1154 C CD2 . LEU A 1 148 ? 23.280 29.100  42.339  1.00 25.80 ? 148 LEU A CD2 1 
ATOM   1155 N N   . SER A 1 149 ? 21.187 31.294  45.908  1.00 23.52 ? 149 SER A N   1 
ATOM   1156 C CA  . SER A 1 149 ? 20.325 32.472  45.839  1.00 22.18 ? 149 SER A CA  1 
ATOM   1157 C C   . SER A 1 149 ? 20.971 33.846  45.880  1.00 23.49 ? 149 SER A C   1 
ATOM   1158 O O   . SER A 1 149 ? 22.082 34.031  46.384  1.00 18.50 ? 149 SER A O   1 
ATOM   1159 C CB  . SER A 1 149 ? 19.225 32.397  46.915  1.00 22.28 ? 149 SER A CB  1 
ATOM   1160 O OG  . SER A 1 149 ? 19.765 32.249  48.230  1.00 21.37 ? 149 SER A OG  1 
ATOM   1161 N N   . SER A 1 150 ? 20.232 34.800  45.325  1.00 23.90 ? 150 SER A N   1 
ATOM   1162 C CA  . SER A 1 150 ? 20.612 36.204  45.279  1.00 25.06 ? 150 SER A CA  1 
ATOM   1163 C C   . SER A 1 150 ? 19.420 36.864  45.966  1.00 26.72 ? 150 SER A C   1 
ATOM   1164 O O   . SER A 1 150 ? 18.300 36.801  45.448  1.00 29.07 ? 150 SER A O   1 
ATOM   1165 C CB  . SER A 1 150 ? 20.704 36.688  43.823  1.00 22.98 ? 150 SER A CB  1 
ATOM   1166 O OG  . SER A 1 150 ? 21.789 37.590  43.665  1.00 21.86 ? 150 SER A OG  1 
ATOM   1167 N N   . THR A 1 151 ? 19.629 37.414  47.159  1.00 24.00 ? 151 THR A N   1 
ATOM   1168 C CA  . THR A 1 151 ? 18.543 38.045  47.909  1.00 23.06 ? 151 THR A CA  1 
ATOM   1169 C C   . THR A 1 151 ? 19.098 39.289  48.540  1.00 25.96 ? 151 THR A C   1 
ATOM   1170 O O   . THR A 1 151 ? 20.321 39.474  48.568  1.00 31.28 ? 151 THR A O   1 
ATOM   1171 C CB  . THR A 1 151 ? 18.084 37.164  49.055  1.00 18.65 ? 151 THR A CB  1 
ATOM   1172 O OG1 . THR A 1 151 ? 19.174 36.974  49.980  1.00 20.26 ? 151 THR A OG1 1 
ATOM   1173 C CG2 . THR A 1 151 ? 17.616 35.831  48.533  1.00 23.27 ? 151 THR A CG2 1 
ATOM   1174 N N   . GLU A 1 152 ? 18.230 40.102  49.133  1.00 25.32 ? 152 GLU A N   1 
ATOM   1175 C CA  . GLU A 1 152 ? 18.706 41.327  49.771  1.00 26.73 ? 152 GLU A CA  1 
ATOM   1176 C C   . GLU A 1 152 ? 19.677 41.029  50.890  1.00 22.14 ? 152 GLU A C   1 
ATOM   1177 O O   . GLU A 1 152 ? 20.509 41.858  51.182  1.00 23.75 ? 152 GLU A O   1 
ATOM   1178 C CB  . GLU A 1 152 ? 17.556 42.177  50.302  1.00 32.45 ? 152 GLU A CB  1 
ATOM   1179 C CG  . GLU A 1 152 ? 16.462 42.391  49.276  1.00 48.89 ? 152 GLU A CG  1 
ATOM   1180 C CD  . GLU A 1 152 ? 15.557 43.561  49.591  1.00 55.78 ? 152 GLU A CD  1 
ATOM   1181 O OE1 . GLU A 1 152 ? 15.344 43.860  50.785  1.00 59.04 ? 152 GLU A OE1 1 
ATOM   1182 O OE2 . GLU A 1 152 ? 15.060 44.186  48.624  1.00 65.91 ? 152 GLU A OE2 1 
ATOM   1183 N N   . ALA A 1 153 ? 19.604 39.836  51.475  1.00 18.13 ? 153 ALA A N   1 
ATOM   1184 C CA  . ALA A 1 153 ? 20.497 39.490  52.562  1.00 20.40 ? 153 ALA A CA  1 
ATOM   1185 C C   . ALA A 1 153 ? 21.799 38.847  52.136  1.00 24.02 ? 153 ALA A C   1 
ATOM   1186 O O   . ALA A 1 153 ? 22.713 38.721  52.944  1.00 25.71 ? 153 ALA A O   1 
ATOM   1187 C CB  . ALA A 1 153 ? 19.795 38.616  53.556  1.00 23.85 ? 153 ALA A CB  1 
ATOM   1188 N N   . GLN A 1 154 ? 21.899 38.402  50.891  1.00 25.44 ? 154 GLN A N   1 
ATOM   1189 C CA  . GLN A 1 154 ? 23.143 37.777  50.440  1.00 26.92 ? 154 GLN A CA  1 
ATOM   1190 C C   . GLN A 1 154 ? 23.266 37.657  48.915  1.00 29.37 ? 154 GLN A C   1 
ATOM   1191 O O   . GLN A 1 154 ? 22.256 37.560  48.212  1.00 26.82 ? 154 GLN A O   1 
ATOM   1192 C CB  . GLN A 1 154 ? 23.362 36.402  51.130  1.00 21.47 ? 154 GLN A CB  1 
ATOM   1193 C CG  . GLN A 1 154 ? 22.172 35.407  51.122  1.00 18.43 ? 154 GLN A CG  1 
ATOM   1194 C CD  . GLN A 1 154 ? 21.863 34.823  49.733  1.00 27.82 ? 154 GLN A CD  1 
ATOM   1195 O OE1 . GLN A 1 154 ? 20.703 34.761  49.329  1.00 30.79 ? 154 GLN A OE1 1 
ATOM   1196 N NE2 . GLN A 1 154 ? 22.899 34.392  49.005  1.00 23.51 ? 154 GLN A NE2 1 
ATOM   1197 N N   . GLN A 1 155 ? 24.508 37.719  48.427  1.00 30.70 ? 155 GLN A N   1 
ATOM   1198 C CA  . GLN A 1 155 ? 24.825 37.588  47.005  1.00 29.22 ? 155 GLN A CA  1 
ATOM   1199 C C   . GLN A 1 155 ? 25.040 36.121  46.769  1.00 25.86 ? 155 GLN A C   1 
ATOM   1200 O O   . GLN A 1 155 ? 25.312 35.374  47.706  1.00 27.77 ? 155 GLN A O   1 
ATOM   1201 C CB  . GLN A 1 155 ? 26.108 38.340  46.636  1.00 30.37 ? 155 GLN A CB  1 
ATOM   1202 C CG  . GLN A 1 155 ? 25.999 39.851  46.768  1.00 44.36 ? 155 GLN A CG  1 
ATOM   1203 C CD  . GLN A 1 155 ? 27.007 40.621  45.917  1.00 53.34 ? 155 GLN A CD  1 
ATOM   1204 O OE1 . GLN A 1 155 ? 26.730 41.742  45.475  1.00 57.11 ? 155 GLN A OE1 1 
ATOM   1205 N NE2 . GLN A 1 155 ? 28.178 40.032  45.687  1.00 57.81 ? 155 GLN A NE2 1 
ATOM   1206 N N   . SER A 1 156 ? 24.843 35.713  45.528  1.00 28.38 ? 156 SER A N   1 
ATOM   1207 C CA  . SER A 1 156 ? 25.006 34.334  45.089  1.00 27.11 ? 156 SER A CA  1 
ATOM   1208 C C   . SER A 1 156 ? 26.496 34.075  44.836  1.00 29.05 ? 156 SER A C   1 
ATOM   1209 O O   . SER A 1 156 ? 27.205 34.965  44.345  1.00 27.99 ? 156 SER A O   1 
ATOM   1210 C CB  . SER A 1 156 ? 24.207 34.152  43.795  1.00 27.54 ? 156 SER A CB  1 
ATOM   1211 O OG  . SER A 1 156 ? 24.614 33.005  43.078  1.00 24.86 ? 156 SER A OG  1 
ATOM   1212 N N   . TYR A 1 157 ? 26.992 32.876  45.144  1.00 27.38 ? 157 TYR A N   1 
ATOM   1213 C CA  . TYR A 1 157 ? 28.408 32.624  44.888  1.00 22.78 ? 157 TYR A CA  1 
ATOM   1214 C C   . TYR A 1 157 ? 28.864 32.858  43.434  1.00 19.92 ? 157 TYR A C   1 
ATOM   1215 O O   . TYR A 1 157 ? 30.023 33.190  43.187  1.00 16.68 ? 157 TYR A O   1 
ATOM   1216 C CB  . TYR A 1 157 ? 28.891 31.266  45.458  1.00 24.04 ? 157 TYR A CB  1 
ATOM   1217 C CG  . TYR A 1 157 ? 28.175 29.994  45.056  1.00 23.61 ? 157 TYR A CG  1 
ATOM   1218 C CD1 . TYR A 1 157 ? 28.414 29.381  43.822  1.00 20.74 ? 157 TYR A CD1 1 
ATOM   1219 C CD2 . TYR A 1 157 ? 27.326 29.359  45.945  1.00 17.35 ? 157 TYR A CD2 1 
ATOM   1220 C CE1 . TYR A 1 157 ? 27.822 28.157  43.496  1.00 22.88 ? 157 TYR A CE1 1 
ATOM   1221 C CE2 . TYR A 1 157 ? 26.728 28.136  45.633  1.00 23.23 ? 157 TYR A CE2 1 
ATOM   1222 C CZ  . TYR A 1 157 ? 26.977 27.541  44.409  1.00 25.26 ? 157 TYR A CZ  1 
ATOM   1223 O OH  . TYR A 1 157 ? 26.365 26.340  44.109  1.00 21.47 ? 157 TYR A OH  1 
ATOM   1224 N N   . LEU A 1 158 ? 27.931 32.749  42.493  1.00 21.09 ? 158 LEU A N   1 
ATOM   1225 C CA  . LEU A 1 158 ? 28.204 32.969  41.060  1.00 19.62 ? 158 LEU A CA  1 
ATOM   1226 C C   . LEU A 1 158 ? 28.691 34.391  40.840  1.00 15.18 ? 158 LEU A C   1 
ATOM   1227 O O   . LEU A 1 158 ? 29.495 34.636  39.942  1.00 24.16 ? 158 LEU A O   1 
ATOM   1228 C CB  . LEU A 1 158 ? 26.935 32.755  40.237  1.00 11.13 ? 158 LEU A CB  1 
ATOM   1229 C CG  . LEU A 1 158 ? 26.350 31.338  40.155  1.00 21.05 ? 158 LEU A CG  1 
ATOM   1230 C CD1 . LEU A 1 158 ? 24.866 31.388  39.784  1.00 20.18 ? 158 LEU A CD1 1 
ATOM   1231 C CD2 . LEU A 1 158 ? 27.125 30.509  39.132  1.00 15.62 ? 158 LEU A CD2 1 
ATOM   1232 N N   . GLN A 1 159 ? 28.221 35.315  41.684  1.00 17.11 ? 159 GLN A N   1 
ATOM   1233 C CA  . GLN A 1 159 ? 28.587 36.739  41.617  1.00 14.99 ? 159 GLN A CA  1 
ATOM   1234 C C   . GLN A 1 159 ? 30.020 37.028  42.086  1.00 22.99 ? 159 GLN A C   1 
ATOM   1235 O O   . GLN A 1 159 ? 30.428 38.186  42.206  1.00 26.27 ? 159 GLN A O   1 
ATOM   1236 C CB  . GLN A 1 159 ? 27.657 37.586  42.473  1.00 14.93 ? 159 GLN A CB  1 
ATOM   1237 C CG  . GLN A 1 159 ? 26.179 37.434  42.224  1.00 19.33 ? 159 GLN A CG  1 
ATOM   1238 C CD  . GLN A 1 159 ? 25.361 38.363  43.127  1.00 20.63 ? 159 GLN A CD  1 
ATOM   1239 O OE1 . GLN A 1 159 ? 24.476 37.926  43.874  1.00 17.87 ? 159 GLN A OE1 1 
ATOM   1240 N NE2 . GLN A 1 159 ? 25.669 39.650  43.067  1.00 18.24 ? 159 GLN A NE2 1 
ATOM   1241 N N   . GLU A 1 160 ? 30.743 36.001  42.489  1.00 23.41 ? 160 GLU A N   1 
ATOM   1242 C CA  . GLU A 1 160 ? 32.102 36.224  42.925  1.00 25.55 ? 160 GLU A CA  1 
ATOM   1243 C C   . GLU A 1 160 ? 33.044 35.899  41.778  1.00 26.93 ? 160 GLU A C   1 
ATOM   1244 O O   . GLU A 1 160 ? 34.270 35.954  41.928  1.00 30.09 ? 160 GLU A O   1 
ATOM   1245 C CB  . GLU A 1 160 ? 32.404 35.366  44.144  1.00 30.31 ? 160 GLU A CB  1 
ATOM   1246 C CG  . GLU A 1 160 ? 31.510 35.689  45.333  1.00 37.16 ? 160 GLU A CG  1 
ATOM   1247 C CD  . GLU A 1 160 ? 31.680 37.116  45.835  1.00 41.03 ? 160 GLU A CD  1 
ATOM   1248 O OE1 . GLU A 1 160 ? 32.777 37.695  45.646  1.00 45.09 ? 160 GLU A OE1 1 
ATOM   1249 O OE2 . GLU A 1 160 ? 30.719 37.652  46.432  1.00 40.07 ? 160 GLU A OE2 1 
ATOM   1250 N N   . PHE A 1 161 ? 32.467 35.540  40.634  1.00 23.22 ? 161 PHE A N   1 
ATOM   1251 C CA  . PHE A 1 161 ? 33.270 35.211  39.472  1.00 25.38 ? 161 PHE A CA  1 
ATOM   1252 C C   . PHE A 1 161 ? 33.378 36.461  38.605  1.00 26.17 ? 161 PHE A C   1 
ATOM   1253 O O   . PHE A 1 161 ? 32.483 37.308  38.629  1.00 24.65 ? 161 PHE A O   1 
ATOM   1254 C CB  . PHE A 1 161 ? 32.659 34.028  38.713  1.00 21.02 ? 161 PHE A CB  1 
ATOM   1255 C CG  . PHE A 1 161 ? 32.894 32.679  39.372  1.00 15.92 ? 161 PHE A CG  1 
ATOM   1256 C CD1 . PHE A 1 161 ? 34.154 32.101  39.369  1.00 12.27 ? 161 PHE A CD1 1 
ATOM   1257 C CD2 . PHE A 1 161 ? 31.842 31.975  39.952  1.00 15.75 ? 161 PHE A CD2 1 
ATOM   1258 C CE1 . PHE A 1 161 ? 34.372 30.847  39.919  1.00 13.45 ? 161 PHE A CE1 1 
ATOM   1259 C CE2 . PHE A 1 161 ? 32.048 30.713  40.506  1.00 16.54 ? 161 PHE A CE2 1 
ATOM   1260 C CZ  . PHE A 1 161 ? 33.323 30.152  40.484  1.00 14.63 ? 161 PHE A CZ  1 
ATOM   1261 N N   . SER A 1 162 ? 34.490 36.595  37.879  1.00 27.81 ? 162 SER A N   1 
ATOM   1262 C CA  . SER A 1 162 ? 34.717 37.761  37.016  1.00 29.09 ? 162 SER A CA  1 
ATOM   1263 C C   . SER A 1 162 ? 33.761 37.837  35.823  1.00 27.14 ? 162 SER A C   1 
ATOM   1264 O O   . SER A 1 162 ? 33.322 36.822  35.307  1.00 24.11 ? 162 SER A O   1 
ATOM   1265 C CB  . SER A 1 162 ? 36.171 37.813  36.537  1.00 28.46 ? 162 SER A CB  1 
ATOM   1266 O OG  . SER A 1 162 ? 36.479 36.714  35.696  1.00 31.71 ? 162 SER A OG  1 
ATOM   1267 N N   . LYS A 1 163 ? 33.487 39.059  35.378  1.00 29.11 ? 163 LYS A N   1 
ATOM   1268 C CA  . LYS A 1 163 ? 32.581 39.343  34.264  1.00 27.85 ? 163 LYS A CA  1 
ATOM   1269 C C   . LYS A 1 163 ? 32.836 38.487  33.045  1.00 26.35 ? 163 LYS A C   1 
ATOM   1270 O O   . LYS A 1 163 ? 31.893 37.939  32.477  1.00 27.20 ? 163 LYS A O   1 
ATOM   1271 C CB  . LYS A 1 163 ? 32.695 40.820  33.877  1.00 34.99 ? 163 LYS A CB  1 
ATOM   1272 C CG  . LYS A 1 163 ? 31.869 41.247  32.667  1.00 49.86 ? 163 LYS A CG  1 
ATOM   1273 C CD  . LYS A 1 163 ? 32.235 42.667  32.213  1.00 51.90 ? 163 LYS A CD  1 
ATOM   1274 C CE  . LYS A 1 163 ? 32.758 42.671  30.781  1.00 56.39 ? 163 LYS A CE  1 
ATOM   1275 N NZ  . LYS A 1 163 ? 33.954 41.791  30.574  1.00 57.85 ? 163 LYS A NZ  1 
ATOM   1276 N N   . HIS A 1 164 ? 34.098 38.391  32.629  1.00 21.01 ? 164 HIS A N   1 
ATOM   1277 C CA  . HIS A 1 164 ? 34.445 37.594  31.463  1.00 25.92 ? 164 HIS A CA  1 
ATOM   1278 C C   . HIS A 1 164 ? 34.268 36.088  31.680  1.00 26.13 ? 164 HIS A C   1 
ATOM   1279 O O   . HIS A 1 164 ? 33.969 35.366  30.715  1.00 27.35 ? 164 HIS A O   1 
ATOM   1280 C CB  . HIS A 1 164 ? 35.867 37.906  30.995  1.00 35.86 ? 164 HIS A CB  1 
ATOM   1281 C CG  . HIS A 1 164 ? 36.368 36.999  29.906  1.00 48.00 ? 164 HIS A CG  1 
ATOM   1282 N ND1 . HIS A 1 164 ? 37.639 36.457  29.914  1.00 50.95 ? 164 HIS A ND1 1 
ATOM   1283 C CD2 . HIS A 1 164 ? 35.769 36.531  28.784  1.00 51.83 ? 164 HIS A CD2 1 
ATOM   1284 C CE1 . HIS A 1 164 ? 37.802 35.695  28.848  1.00 48.78 ? 164 HIS A CE1 1 
ATOM   1285 N NE2 . HIS A 1 164 ? 36.682 35.722  28.147  1.00 55.87 ? 164 HIS A NE2 1 
ATOM   1286 N N   . ILE A 1 165 ? 34.474 35.603  32.911  1.00 25.22 ? 165 ILE A N   1 
ATOM   1287 C CA  . ILE A 1 165 ? 34.308 34.168  33.201  1.00 24.30 ? 165 ILE A CA  1 
ATOM   1288 C C   . ILE A 1 165 ? 32.829 33.827  33.045  1.00 26.19 ? 165 ILE A C   1 
ATOM   1289 O O   . ILE A 1 165 ? 32.471 32.815  32.428  1.00 26.41 ? 165 ILE A O   1 
ATOM   1290 C CB  . ILE A 1 165 ? 34.840 33.771  34.632  1.00 26.57 ? 165 ILE A CB  1 
ATOM   1291 C CG1 . ILE A 1 165 ? 36.299 33.321  34.558  1.00 27.49 ? 165 ILE A CG1 1 
ATOM   1292 C CG2 . ILE A 1 165 ? 34.062 32.589  35.236  1.00 26.54 ? 165 ILE A CG2 1 
ATOM   1293 C CD1 . ILE A 1 165 ? 37.229 34.356  34.052  1.00 34.54 ? 165 ILE A CD1 1 
ATOM   1294 N N   . LEU A 1 166 ? 31.988 34.746  33.525  1.00 26.68 ? 166 LEU A N   1 
ATOM   1295 C CA  . LEU A 1 166 ? 30.526 34.632  33.488  1.00 24.66 ? 166 LEU A CA  1 
ATOM   1296 C C   . LEU A 1 166 ? 29.966 34.714  32.064  1.00 25.16 ? 166 LEU A C   1 
ATOM   1297 O O   . LEU A 1 166 ? 29.190 33.850  31.656  1.00 30.47 ? 166 LEU A O   1 
ATOM   1298 C CB  . LEU A 1 166 ? 29.911 35.727  34.378  1.00 23.14 ? 166 LEU A CB  1 
ATOM   1299 C CG  . LEU A 1 166 ? 29.206 35.367  35.703  1.00 26.43 ? 166 LEU A CG  1 
ATOM   1300 C CD1 . LEU A 1 166 ? 29.676 34.052  36.319  1.00 18.46 ? 166 LEU A CD1 1 
ATOM   1301 C CD2 . LEU A 1 166 ? 29.387 36.498  36.677  1.00 20.00 ? 166 LEU A CD2 1 
ATOM   1302 N N   . GLU A 1 167 ? 30.367 35.736  31.303  1.00 24.64 ? 167 GLU A N   1 
ATOM   1303 C CA  . GLU A 1 167 ? 29.895 35.895  29.926  1.00 22.77 ? 167 GLU A CA  1 
ATOM   1304 C C   . GLU A 1 167 ? 30.259 34.646  29.128  1.00 25.47 ? 167 GLU A C   1 
ATOM   1305 O O   . GLU A 1 167 ? 29.405 34.063  28.460  1.00 26.65 ? 167 GLU A O   1 
ATOM   1306 C CB  . GLU A 1 167 ? 30.483 37.151  29.286  1.00 16.71 ? 167 GLU A CB  1 
ATOM   1307 C CG  . GLU A 1 167 ? 29.849 38.458  29.796  1.00 26.36 ? 167 GLU A CG  1 
ATOM   1308 C CD  . GLU A 1 167 ? 30.441 39.747  29.190  1.00 33.75 ? 167 GLU A CD  1 
ATOM   1309 O OE1 . GLU A 1 167 ? 31.605 39.741  28.729  1.00 39.82 ? 167 GLU A OE1 1 
ATOM   1310 O OE2 . GLU A 1 167 ? 29.752 40.791  29.201  1.00 33.29 ? 167 GLU A OE2 1 
ATOM   1311 N N   . ALA A 1 168 ? 31.500 34.187  29.286  1.00 24.58 ? 168 ALA A N   1 
ATOM   1312 C CA  . ALA A 1 168 ? 31.995 32.992  28.612  1.00 21.97 ? 168 ALA A CA  1 
ATOM   1313 C C   . ALA A 1 168 ? 31.237 31.708  29.011  1.00 22.09 ? 168 ALA A C   1 
ATOM   1314 O O   . ALA A 1 168 ? 30.808 30.907  28.169  1.00 14.97 ? 168 ALA A O   1 
ATOM   1315 C CB  . ALA A 1 168 ? 33.468 32.836  28.898  1.00 22.56 ? 168 ALA A CB  1 
ATOM   1316 N N   . SER A 1 169 ? 31.093 31.500  30.308  1.00 20.11 ? 169 SER A N   1 
ATOM   1317 C CA  . SER A 1 169 ? 30.393 30.334  30.784  1.00 19.25 ? 169 SER A CA  1 
ATOM   1318 C C   . SER A 1 169 ? 28.970 30.239  30.227  1.00 22.65 ? 169 SER A C   1 
ATOM   1319 O O   . SER A 1 169 ? 28.574 29.193  29.686  1.00 16.59 ? 169 SER A O   1 
ATOM   1320 C CB  . SER A 1 169 ? 30.340 30.367  32.300  1.00 17.64 ? 169 SER A CB  1 
ATOM   1321 O OG  . SER A 1 169 ? 31.646 30.438  32.810  1.00 17.64 ? 169 SER A OG  1 
ATOM   1322 N N   . PHE A 1 170 ? 28.197 31.315  30.378  1.00 21.91 ? 170 PHE A N   1 
ATOM   1323 C CA  . PHE A 1 170 ? 26.805 31.299  29.925  1.00 23.20 ? 170 PHE A CA  1 
ATOM   1324 C C   . PHE A 1 170 ? 26.589 31.628  28.451  1.00 23.66 ? 170 PHE A C   1 
ATOM   1325 O O   . PHE A 1 170 ? 25.567 31.260  27.880  1.00 26.57 ? 170 PHE A O   1 
ATOM   1326 C CB  . PHE A 1 170 ? 25.949 32.219  30.802  1.00 19.33 ? 170 PHE A CB  1 
ATOM   1327 C CG  . PHE A 1 170 ? 25.892 31.786  32.234  1.00 26.03 ? 170 PHE A CG  1 
ATOM   1328 C CD1 . PHE A 1 170 ? 25.380 30.540  32.577  1.00 25.58 ? 170 PHE A CD1 1 
ATOM   1329 C CD2 . PHE A 1 170 ? 26.415 32.590  33.238  1.00 27.21 ? 170 PHE A CD2 1 
ATOM   1330 C CE1 . PHE A 1 170 ? 25.399 30.097  33.912  1.00 23.96 ? 170 PHE A CE1 1 
ATOM   1331 C CE2 . PHE A 1 170 ? 26.439 32.151  34.578  1.00 25.00 ? 170 PHE A CE2 1 
ATOM   1332 C CZ  . PHE A 1 170 ? 25.931 30.902  34.902  1.00 23.51 ? 170 PHE A CZ  1 
ATOM   1333 N N   . ASN A 1 171 ? 27.575 32.265  27.827  1.00 21.83 ? 171 ASN A N   1 
ATOM   1334 C CA  . ASN A 1 171 ? 27.455 32.672  26.429  1.00 23.78 ? 171 ASN A CA  1 
ATOM   1335 C C   . ASN A 1 171 ? 26.358 33.765  26.326  1.00 24.76 ? 171 ASN A C   1 
ATOM   1336 O O   . ASN A 1 171 ? 25.354 33.607  25.629  1.00 24.56 ? 171 ASN A O   1 
ATOM   1337 C CB  . ASN A 1 171 ? 27.122 31.447  25.572  1.00 20.51 ? 171 ASN A CB  1 
ATOM   1338 C CG  . ASN A 1 171 ? 27.153 31.747  24.097  1.00 20.81 ? 171 ASN A CG  1 
ATOM   1339 O OD1 . ASN A 1 171 ? 28.044 32.435  23.617  1.00 33.30 ? 171 ASN A OD1 1 
ATOM   1340 N ND2 . ASN A 1 171 ? 26.183 31.235  23.369  1.00 25.99 ? 171 ASN A ND2 1 
ATOM   1341 N N   . SER A 1 172 ? 26.529 34.841  27.100  1.00 29.24 ? 172 SER A N   1 
ATOM   1342 C CA  . SER A 1 172 ? 25.585 35.970  27.153  1.00 29.22 ? 172 SER A CA  1 
ATOM   1343 C C   . SER A 1 172 ? 26.306 37.186  27.703  1.00 31.64 ? 172 SER A C   1 
ATOM   1344 O O   . SER A 1 172 ? 27.219 37.051  28.519  1.00 38.65 ? 172 SER A O   1 
ATOM   1345 C CB  . SER A 1 172 ? 24.411 35.678  28.089  1.00 24.64 ? 172 SER A CB  1 
ATOM   1346 O OG  . SER A 1 172 ? 23.629 34.604  27.615  1.00 28.26 ? 172 SER A OG  1 
ATOM   1347 N N   . LYS A 1 173 ? 25.898 38.377  27.276  1.00 30.46 ? 173 LYS A N   1 
ATOM   1348 C CA  . LYS A 1 173 ? 26.548 39.593  27.754  1.00 29.24 ? 173 LYS A CA  1 
ATOM   1349 C C   . LYS A 1 173 ? 26.274 39.760  29.245  1.00 26.46 ? 173 LYS A C   1 
ATOM   1350 O O   . LYS A 1 173 ? 25.205 39.394  29.741  1.00 26.28 ? 173 LYS A O   1 
ATOM   1351 C CB  . LYS A 1 173 ? 26.108 40.821  26.942  1.00 31.02 ? 173 LYS A CB  1 
ATOM   1352 C CG  . LYS A 1 173 ? 26.559 40.804  25.482  1.00 25.62 ? 173 LYS A CG  1 
ATOM   1353 C CD  . LYS A 1 173 ? 27.986 40.275  25.343  1.00 22.83 ? 173 LYS A CD  1 
ATOM   1354 C CE  . LYS A 1 173 ? 28.709 40.801  24.093  1.00 33.49 ? 173 LYS A CE  1 
ATOM   1355 N NZ  . LYS A 1 173 ? 28.004 40.534  22.799  1.00 34.21 ? 173 LYS A NZ  1 
ATOM   1356 N N   . PHE A 1 174 ? 27.204 40.368  29.949  1.00 22.08 ? 174 PHE A N   1 
ATOM   1357 C CA  . PHE A 1 174 ? 27.034 40.494  31.369  1.00 27.49 ? 174 PHE A CA  1 
ATOM   1358 C C   . PHE A 1 174 ? 25.726 41.142  31.737  1.00 27.96 ? 174 PHE A C   1 
ATOM   1359 O O   . PHE A 1 174 ? 25.150 40.784  32.748  1.00 35.85 ? 174 PHE A O   1 
ATOM   1360 C CB  . PHE A 1 174 ? 28.257 41.158  32.026  1.00 36.43 ? 174 PHE A CB  1 
ATOM   1361 C CG  . PHE A 1 174 ? 28.092 42.618  32.335  1.00 43.83 ? 174 PHE A CG  1 
ATOM   1362 C CD1 . PHE A 1 174 ? 27.477 43.031  33.517  1.00 46.76 ? 174 PHE A CD1 1 
ATOM   1363 C CD2 . PHE A 1 174 ? 28.568 43.583  31.457  1.00 45.23 ? 174 PHE A CD2 1 
ATOM   1364 C CE1 . PHE A 1 174 ? 27.334 44.383  33.816  1.00 47.35 ? 174 PHE A CE1 1 
ATOM   1365 C CE2 . PHE A 1 174 ? 28.431 44.943  31.749  1.00 46.78 ? 174 PHE A CE2 1 
ATOM   1366 C CZ  . PHE A 1 174 ? 27.810 45.340  32.932  1.00 46.88 ? 174 PHE A CZ  1 
ATOM   1367 N N   . GLU A 1 175 ? 25.207 42.025  30.889  1.00 27.00 ? 175 GLU A N   1 
ATOM   1368 C CA  . GLU A 1 175 ? 23.934 42.694  31.180  1.00 27.34 ? 175 GLU A CA  1 
ATOM   1369 C C   . GLU A 1 175 ? 22.715 41.761  31.168  1.00 26.46 ? 175 GLU A C   1 
ATOM   1370 O O   . GLU A 1 175 ? 21.834 41.905  32.001  1.00 26.97 ? 175 GLU A O   1 
ATOM   1371 C CB  . GLU A 1 175 ? 23.701 43.899  30.265  1.00 30.54 ? 175 GLU A CB  1 
ATOM   1372 C CG  . GLU A 1 175 ? 24.722 45.035  30.433  1.00 28.75 ? 175 GLU A CG  1 
ATOM   1373 C CD  . GLU A 1 175 ? 25.616 45.220  29.206  1.00 26.33 ? 175 GLU A CD  1 
ATOM   1374 O OE1 . GLU A 1 175 ? 25.855 44.224  28.465  1.00 17.02 ? 175 GLU A OE1 1 
ATOM   1375 O OE2 . GLU A 1 175 ? 26.092 46.361  28.993  1.00 22.32 ? 175 GLU A OE2 1 
ATOM   1376 N N   . GLU A 1 176 ? 22.669 40.792  30.258  1.00 29.44 ? 176 GLU A N   1 
ATOM   1377 C CA  . GLU A 1 176 ? 21.548 39.850  30.231  1.00 30.55 ? 176 GLU A CA  1 
ATOM   1378 C C   . GLU A 1 176 ? 21.607 39.107  31.557  1.00 28.76 ? 176 GLU A C   1 
ATOM   1379 O O   . GLU A 1 176 ? 20.634 39.053  32.307  1.00 25.96 ? 176 GLU A O   1 
ATOM   1380 C CB  . GLU A 1 176 ? 21.698 38.782  29.130  1.00 38.10 ? 176 GLU A CB  1 
ATOM   1381 C CG  . GLU A 1 176 ? 22.060 39.248  27.706  1.00 56.13 ? 176 GLU A CG  1 
ATOM   1382 C CD  . GLU A 1 176 ? 22.282 38.060  26.736  1.00 61.79 ? 176 GLU A CD  1 
ATOM   1383 O OE1 . GLU A 1 176 ? 21.560 37.051  26.882  1.00 66.54 ? 176 GLU A OE1 1 
ATOM   1384 O OE2 . GLU A 1 176 ? 23.165 38.128  25.840  1.00 53.87 ? 176 GLU A OE2 1 
ATOM   1385 N N   . ILE A 1 177 ? 22.783 38.557  31.839  1.00 27.47 ? 177 ILE A N   1 
ATOM   1386 C CA  . ILE A 1 177 ? 23.007 37.775  33.051  1.00 28.18 ? 177 ILE A CA  1 
ATOM   1387 C C   . ILE A 1 177 ? 22.611 38.520  34.316  1.00 24.91 ? 177 ILE A C   1 
ATOM   1388 O O   . ILE A 1 177 ? 21.947 37.969  35.175  1.00 26.02 ? 177 ILE A O   1 
ATOM   1389 C CB  . ILE A 1 177 ? 24.470 37.270  33.167  1.00 27.13 ? 177 ILE A CB  1 
ATOM   1390 C CG1 . ILE A 1 177 ? 24.871 36.500  31.900  1.00 23.26 ? 177 ILE A CG1 1 
ATOM   1391 C CG2 . ILE A 1 177 ? 24.603 36.340  34.369  1.00 25.14 ? 177 ILE A CG2 1 
ATOM   1392 C CD1 . ILE A 1 177 ? 26.303 36.046  31.899  1.00 18.88 ? 177 ILE A CD1 1 
ATOM   1393 N N   . ASN A 1 178 ? 22.966 39.786  34.400  1.00 24.03 ? 178 ASN A N   1 
ATOM   1394 C CA  . ASN A 1 178 ? 22.623 40.570  35.570  1.00 26.69 ? 178 ASN A CA  1 
ATOM   1395 C C   . ASN A 1 178 ? 21.105 40.681  35.742  1.00 25.21 ? 178 ASN A C   1 
ATOM   1396 O O   . ASN A 1 178 ? 20.575 40.517  36.827  1.00 30.73 ? 178 ASN A O   1 
ATOM   1397 C CB  . ASN A 1 178 ? 23.234 41.963  35.459  1.00 22.32 ? 178 ASN A CB  1 
ATOM   1398 C CG  . ASN A 1 178 ? 23.020 42.774  36.697  1.00 26.01 ? 178 ASN A CG  1 
ATOM   1399 O OD1 . ASN A 1 178 ? 23.719 42.601  37.687  1.00 33.86 ? 178 ASN A OD1 1 
ATOM   1400 N ND2 . ASN A 1 178 ? 22.028 43.641  36.671  1.00 29.05 ? 178 ASN A ND2 1 
ATOM   1401 N N   . ARG A 1 179 ? 20.417 40.910  34.642  1.00 21.72 ? 179 ARG A N   1 
ATOM   1402 C CA  . ARG A 1 179 ? 18.976 41.083  34.588  1.00 18.44 ? 179 ARG A CA  1 
ATOM   1403 C C   . ARG A 1 179 ? 18.242 39.804  34.953  1.00 18.98 ? 179 ARG A C   1 
ATOM   1404 O O   . ARG A 1 179 ? 17.185 39.830  35.542  1.00 25.34 ? 179 ARG A O   1 
ATOM   1405 C CB  . ARG A 1 179 ? 18.652 41.445  33.141  1.00 23.30 ? 179 ARG A CB  1 
ATOM   1406 C CG  . ARG A 1 179 ? 17.476 42.330  32.855  1.00 27.26 ? 179 ARG A CG  1 
ATOM   1407 C CD  . ARG A 1 179 ? 17.737 43.084  31.534  1.00 31.50 ? 179 ARG A CD  1 
ATOM   1408 N NE  . ARG A 1 179 ? 18.124 42.197  30.428  1.00 46.75 ? 179 ARG A NE  1 
ATOM   1409 C CZ  . ARG A 1 179 ? 18.937 42.540  29.419  1.00 52.82 ? 179 ARG A CZ  1 
ATOM   1410 N NH1 . ARG A 1 179 ? 19.469 43.762  29.352  1.00 49.30 ? 179 ARG A NH1 1 
ATOM   1411 N NH2 . ARG A 1 179 ? 19.240 41.646  28.478  1.00 52.56 ? 179 ARG A NH2 1 
ATOM   1412 N N   . VAL A 1 180 ? 18.787 38.668  34.575  1.00 22.10 ? 180 VAL A N   1 
ATOM   1413 C CA  . VAL A 1 180 ? 18.113 37.411  34.842  1.00 22.41 ? 180 VAL A CA  1 
ATOM   1414 C C   . VAL A 1 180 ? 18.445 36.802  36.199  1.00 24.15 ? 180 VAL A C   1 
ATOM   1415 O O   . VAL A 1 180 ? 17.555 36.305  36.889  1.00 27.99 ? 180 VAL A O   1 
ATOM   1416 C CB  . VAL A 1 180 ? 18.432 36.399  33.729  1.00 20.02 ? 180 VAL A CB  1 
ATOM   1417 C CG1 . VAL A 1 180 ? 17.691 35.100  33.939  1.00 21.24 ? 180 VAL A CG1 1 
ATOM   1418 C CG2 . VAL A 1 180 ? 18.074 36.983  32.389  1.00 16.95 ? 180 VAL A CG2 1 
ATOM   1419 N N   . LEU A 1 181 ? 19.716 36.852  36.590  1.00 21.86 ? 181 LEU A N   1 
ATOM   1420 C CA  . LEU A 1 181 ? 20.157 36.255  37.849  1.00 22.65 ? 181 LEU A CA  1 
ATOM   1421 C C   . LEU A 1 181 ? 20.357 37.151  39.069  1.00 22.16 ? 181 LEU A C   1 
ATOM   1422 O O   . LEU A 1 181 ? 19.928 36.810  40.175  1.00 25.40 ? 181 LEU A O   1 
ATOM   1423 C CB  . LEU A 1 181 ? 21.445 35.453  37.598  1.00 23.71 ? 181 LEU A CB  1 
ATOM   1424 C CG  . LEU A 1 181 ? 21.448 34.019  37.010  1.00 20.62 ? 181 LEU A CG  1 
ATOM   1425 C CD1 . LEU A 1 181 ? 20.396 33.792  35.998  1.00 19.16 ? 181 LEU A CD1 1 
ATOM   1426 C CD2 . LEU A 1 181 ? 22.786 33.722  36.429  1.00 17.69 ? 181 LEU A CD2 1 
ATOM   1427 N N   . PHE A 1 182 ? 20.909 38.337  38.851  1.00 24.73 ? 182 PHE A N   1 
ATOM   1428 C CA  . PHE A 1 182 ? 21.261 39.234  39.945  1.00 24.24 ? 182 PHE A CA  1 
ATOM   1429 C C   . PHE A 1 182 ? 20.557 40.560  40.204  1.00 26.72 ? 182 PHE A C   1 
ATOM   1430 O O   . PHE A 1 182 ? 20.658 41.098  41.297  1.00 25.12 ? 182 PHE A O   1 
ATOM   1431 C CB  . PHE A 1 182 ? 22.745 39.519  39.840  1.00 19.68 ? 182 PHE A CB  1 
ATOM   1432 C CG  . PHE A 1 182 ? 23.573 38.304  39.620  1.00 17.49 ? 182 PHE A CG  1 
ATOM   1433 C CD1 . PHE A 1 182 ? 23.257 37.106  40.246  1.00 23.14 ? 182 PHE A CD1 1 
ATOM   1434 C CD2 . PHE A 1 182 ? 24.689 38.358  38.812  1.00 16.77 ? 182 PHE A CD2 1 
ATOM   1435 C CE1 . PHE A 1 182 ? 24.046 35.994  40.068  1.00 18.07 ? 182 PHE A CE1 1 
ATOM   1436 C CE2 . PHE A 1 182 ? 25.478 37.249  38.636  1.00 16.49 ? 182 PHE A CE2 1 
ATOM   1437 C CZ  . PHE A 1 182 ? 25.160 36.068  39.261  1.00 10.40 ? 182 PHE A CZ  1 
ATOM   1438 N N   . GLU A 1 183 ? 19.878 41.098  39.207  1.00 29.84 ? 183 GLU A N   1 
ATOM   1439 C CA  . GLU A 1 183 ? 19.196 42.391  39.321  1.00 36.24 ? 183 GLU A CA  1 
ATOM   1440 C C   . GLU A 1 183 ? 18.527 42.601  40.684  1.00 36.88 ? 183 GLU A C   1 
ATOM   1441 O O   . GLU A 1 183 ? 17.720 41.784  41.130  1.00 35.29 ? 183 GLU A O   1 
ATOM   1442 C CB  . GLU A 1 183 ? 18.182 42.513  38.190  1.00 39.46 ? 183 GLU A CB  1 
ATOM   1443 C CG  . GLU A 1 183 ? 17.542 43.844  38.013  1.00 43.84 ? 183 GLU A CG  1 
ATOM   1444 C CD  . GLU A 1 183 ? 16.263 43.708  37.227  1.00 50.45 ? 183 GLU A CD  1 
ATOM   1445 O OE1 . GLU A 1 183 ? 16.341 43.401  36.019  1.00 51.23 ? 183 GLU A OE1 1 
ATOM   1446 O OE2 . GLU A 1 183 ? 15.173 43.866  37.820  1.00 55.74 ? 183 GLU A OE2 1 
ATOM   1447 N N   . GLU A 1 184 ? 18.905 43.693  41.344  1.00 40.56 ? 184 GLU A N   1 
ATOM   1448 C CA  . GLU A 1 184 ? 18.391 44.054  42.669  1.00 44.58 ? 184 GLU A CA  1 
ATOM   1449 C C   . GLU A 1 184 ? 16.877 43.980  42.734  1.00 47.60 ? 184 GLU A C   1 
ATOM   1450 O O   . GLU A 1 184 ? 16.309 43.343  43.623  1.00 52.08 ? 184 GLU A O   1 
ATOM   1451 C CB  . GLU A 1 184 ? 18.851 45.465  43.042  1.00 45.08 ? 184 GLU A CB  1 
ATOM   1452 C CG  . GLU A 1 184 ? 19.681 45.528  44.310  1.00 46.50 ? 184 GLU A CG  1 
ATOM   1453 C CD  . GLU A 1 184 ? 20.880 46.462  44.199  1.00 51.53 ? 184 GLU A CD  1 
ATOM   1454 O OE1 . GLU A 1 184 ? 20.708 47.641  43.827  1.00 62.11 ? 184 GLU A OE1 1 
ATOM   1455 O OE2 . GLU A 1 184 ? 22.004 46.019  44.495  1.00 47.58 ? 184 GLU A OE2 1 
ATOM   1456 N N   . GLU A 1 185 ? 16.231 44.648  41.786  1.00 49.29 ? 185 GLU A N   1 
ATOM   1457 C CA  . GLU A 1 185 ? 14.778 44.679  41.697  1.00 48.18 ? 185 GLU A CA  1 
ATOM   1458 C C   . GLU A 1 185 ? 14.208 43.305  41.339  1.00 46.87 ? 185 GLU A C   1 
ATOM   1459 O O   . GLU A 1 185 ? 14.098 42.956  40.162  1.00 46.75 ? 185 GLU A O   1 
ATOM   1460 C CB  . GLU A 1 185 ? 14.358 45.715  40.648  1.00 51.50 ? 185 GLU A CB  1 
ATOM   1461 C CG  . GLU A 1 185 ? 12.868 45.795  40.393  1.00 57.08 ? 185 GLU A CG  1 
ATOM   1462 C CD  . GLU A 1 185 ? 12.495 47.007  39.580  1.00 60.29 ? 185 GLU A CD  1 
ATOM   1463 O OE1 . GLU A 1 185 ? 12.329 48.087  40.186  1.00 64.79 ? 185 GLU A OE1 1 
ATOM   1464 O OE2 . GLU A 1 185 ? 12.376 46.884  38.342  1.00 63.61 ? 185 GLU A OE2 1 
ATOM   1465 N N   . GLY A 1 186 ? 13.861 42.524  42.352  1.00 41.73 ? 186 GLY A N   1 
ATOM   1466 C CA  . GLY A 1 186 ? 13.297 41.219  42.084  1.00 41.77 ? 186 GLY A CA  1 
ATOM   1467 C C   . GLY A 1 186 ? 13.804 40.169  43.035  1.00 39.36 ? 186 GLY A C   1 
ATOM   1468 O O   . GLY A 1 186 ? 13.222 39.089  43.181  1.00 41.38 ? 186 GLY A O   1 
ATOM   1469 N N   . GLN A 1 187 ? 14.918 40.469  43.677  1.00 40.31 ? 187 GLN A N   1 
ATOM   1470 C CA  . GLN A 1 187 ? 15.492 39.521  44.617  1.00 37.62 ? 187 GLN A CA  1 
ATOM   1471 C C   . GLN A 1 187 ? 14.622 39.433  45.870  1.00 31.53 ? 187 GLN A C   1 
ATOM   1472 O O   . GLN A 1 187 ? 13.994 40.409  46.280  1.00 30.30 ? 187 GLN A O   1 
ATOM   1473 C CB  . GLN A 1 187 ? 16.943 39.908  44.955  1.00 36.07 ? 187 GLN A CB  1 
ATOM   1474 C CG  . GLN A 1 187 ? 17.121 41.265  45.635  1.00 35.35 ? 187 GLN A CG  1 
ATOM   1475 C CD  . GLN A 1 187 ? 18.547 41.781  45.526  1.00 33.67 ? 187 GLN A CD  1 
ATOM   1476 O OE1 . GLN A 1 187 ? 19.316 41.344  44.670  1.00 33.58 ? 187 GLN A OE1 1 
ATOM   1477 N NE2 . GLN A 1 187 ? 18.905 42.711  46.392  1.00 31.41 ? 187 GLN A NE2 1 
ATOM   1478 N N   . GLN A 1 188 ? 14.493 38.229  46.403  1.00 27.57 ? 188 GLN A N   1 
ATOM   1479 C CA  . GLN A 1 188 ? 13.724 38.032  47.618  1.00 23.85 ? 188 GLN A CA  1 
ATOM   1480 C C   . GLN A 1 188 ? 14.514 38.726  48.743  1.00 25.17 ? 188 GLN A C   1 
ATOM   1481 O O   . GLN A 1 188 ? 15.667 39.132  48.552  1.00 25.58 ? 188 GLN A O   1 
ATOM   1482 C CB  . GLN A 1 188 ? 13.571 36.534  47.888  1.00 20.08 ? 188 GLN A CB  1 
ATOM   1483 C CG  . GLN A 1 188 ? 12.893 35.764  46.761  1.00 20.73 ? 188 GLN A CG  1 
ATOM   1484 C CD  . GLN A 1 188 ? 11.419 36.122  46.608  1.00 29.11 ? 188 GLN A CD  1 
ATOM   1485 O OE1 . GLN A 1 188 ? 10.635 35.968  47.538  1.00 34.50 ? 188 GLN A OE1 1 
ATOM   1486 N NE2 . GLN A 1 188 ? 11.041 36.612  45.438  1.00 31.13 ? 188 GLN A NE2 1 
ATOM   1487 N N   . GLU A 1 189 ? 13.914 38.857  49.917  1.00 27.81 ? 189 GLU A N   1 
ATOM   1488 C CA  . GLU A 1 189 ? 14.596 39.514  51.026  1.00 28.72 ? 189 GLU A CA  1 
ATOM   1489 C C   . GLU A 1 189 ? 15.678 38.637  51.682  1.00 28.70 ? 189 GLU A C   1 
ATOM   1490 O O   . GLU A 1 189 ? 16.752 39.129  52.034  1.00 28.45 ? 189 GLU A O   1 
ATOM   1491 C CB  . GLU A 1 189 ? 13.573 39.977  52.056  1.00 34.69 ? 189 GLU A CB  1 
ATOM   1492 C CG  . GLU A 1 189 ? 12.466 40.834  51.464  1.00 49.75 ? 189 GLU A CG  1 
ATOM   1493 C CD  . GLU A 1 189 ? 11.483 41.339  52.514  1.00 63.31 ? 189 GLU A CD  1 
ATOM   1494 O OE1 . GLU A 1 189 ? 10.866 40.509  53.222  1.00 70.92 ? 189 GLU A OE1 1 
ATOM   1495 O OE2 . GLU A 1 189 ? 11.323 42.575  52.635  1.00 70.42 ? 189 GLU A OE2 1 
ATOM   1496 N N   . GLY A 1 190 ? 15.435 37.328  51.769  1.00 27.43 ? 190 GLY A N   1 
ATOM   1497 C CA  . GLY A 1 190 ? 16.412 36.443  52.388  1.00 23.35 ? 190 GLY A CA  1 
ATOM   1498 C C   . GLY A 1 190 ? 16.250 35.005  51.959  1.00 17.58 ? 190 GLY A C   1 
ATOM   1499 O O   . GLY A 1 190 ? 15.416 34.709  51.113  1.00 25.79 ? 190 GLY A O   1 
ATOM   1500 N N   . VAL A 1 191 ? 17.019 34.118  52.582  1.00 16.96 ? 191 VAL A N   1 
ATOM   1501 C CA  . VAL A 1 191 ? 17.015 32.693  52.266  1.00 13.62 ? 191 VAL A CA  1 
ATOM   1502 C C   . VAL A 1 191 ? 15.827 31.860  52.730  1.00 15.09 ? 191 VAL A C   1 
ATOM   1503 O O   . VAL A 1 191 ? 15.694 30.699  52.321  1.00 16.51 ? 191 VAL A O   1 
ATOM   1504 C CB  . VAL A 1 191 ? 18.330 32.022  52.683  1.00 10.80 ? 191 VAL A CB  1 
ATOM   1505 C CG1 . VAL A 1 191 ? 19.504 32.742  52.060  1.00 13.43 ? 191 VAL A CG1 1 
ATOM   1506 C CG2 . VAL A 1 191 ? 18.484 32.015  54.172  1.00 14.70 ? 191 VAL A CG2 1 
ATOM   1507 N N   . ILE A 1 192 ? 14.990 32.397  53.613  1.00 16.14 ? 192 ILE A N   1 
ATOM   1508 C CA  . ILE A 1 192 ? 13.791 31.663  54.035  1.00 16.96 ? 192 ILE A CA  1 
ATOM   1509 C C   . ILE A 1 192 ? 12.705 32.407  53.280  1.00 19.78 ? 192 ILE A C   1 
ATOM   1510 O O   . ILE A 1 192 ? 12.649 33.643  53.345  1.00 22.17 ? 192 ILE A O   1 
ATOM   1511 C CB  . ILE A 1 192 ? 13.482 31.758  55.533  1.00 18.27 ? 192 ILE A CB  1 
ATOM   1512 C CG1 . ILE A 1 192 ? 14.707 31.404  56.391  1.00 20.27 ? 192 ILE A CG1 1 
ATOM   1513 C CG2 . ILE A 1 192 ? 12.306 30.842  55.845  1.00 22.44 ? 192 ILE A CG2 1 
ATOM   1514 C CD1 . ILE A 1 192 ? 14.799 29.966  56.825  1.00 19.96 ? 192 ILE A CD1 1 
ATOM   1515 N N   . VAL A 1 193 ? 11.842 31.682  52.570  1.00 18.43 ? 193 VAL A N   1 
ATOM   1516 C CA  . VAL A 1 193 ? 10.814 32.330  51.750  1.00 18.08 ? 193 VAL A CA  1 
ATOM   1517 C C   . VAL A 1 193 ? 9.391  31.839  52.007  1.00 18.98 ? 193 VAL A C   1 
ATOM   1518 O O   . VAL A 1 193 ? 9.160  30.658  52.241  1.00 20.93 ? 193 VAL A O   1 
ATOM   1519 C CB  . VAL A 1 193 ? 11.172 32.147  50.218  1.00 16.49 ? 193 VAL A CB  1 
ATOM   1520 C CG1 . VAL A 1 193 ? 10.070 32.646  49.339  1.00 15.28 ? 193 VAL A CG1 1 
ATOM   1521 C CG2 . VAL A 1 193 ? 12.449 32.888  49.875  1.00 15.00 ? 193 VAL A CG2 1 
ATOM   1522 N N   . ASN A 1 194 ? 8.435  32.755  51.954  1.00 23.47 ? 194 ASN A N   1 
ATOM   1523 C CA  . ASN A 1 194 ? 7.025  32.423  52.139  1.00 26.99 ? 194 ASN A CA  1 
ATOM   1524 C C   . ASN A 1 194 ? 6.475  31.928  50.796  1.00 33.05 ? 194 ASN A C   1 
ATOM   1525 O O   . ASN A 1 194 ? 6.512  32.668  49.797  1.00 34.39 ? 194 ASN A O   1 
ATOM   1526 C CB  . ASN A 1 194 ? 6.265  33.695  52.541  1.00 31.38 ? 194 ASN A CB  1 
ATOM   1527 C CG  . ASN A 1 194 ? 4.782  33.452  52.884  1.00 41.97 ? 194 ASN A CG  1 
ATOM   1528 O OD1 . ASN A 1 194 ? 4.154  34.302  53.528  1.00 51.24 ? 194 ASN A OD1 1 
ATOM   1529 N ND2 . ASN A 1 194 ? 4.220  32.320  52.465  1.00 43.34 ? 194 ASN A ND2 1 
ATOM   1530 N N   . ILE A 1 195 ? 6.002  30.681  50.749  1.00 35.37 ? 195 ILE A N   1 
ATOM   1531 C CA  . ILE A 1 195 ? 5.410  30.160  49.513  1.00 33.44 ? 195 ILE A CA  1 
ATOM   1532 C C   . ILE A 1 195 ? 3.910  29.860  49.681  1.00 41.25 ? 195 ILE A C   1 
ATOM   1533 O O   . ILE A 1 195 ? 3.395  29.739  50.803  1.00 40.34 ? 195 ILE A O   1 
ATOM   1534 C CB  . ILE A 1 195 ? 6.156  28.947  48.930  1.00 23.72 ? 195 ILE A CB  1 
ATOM   1535 C CG1 . ILE A 1 195 ? 5.953  27.711  49.793  1.00 23.23 ? 195 ILE A CG1 1 
ATOM   1536 C CG2 . ILE A 1 195 ? 7.610  29.257  48.782  1.00 21.32 ? 195 ILE A CG2 1 
ATOM   1537 C CD1 . ILE A 1 195 ? 6.643  26.491  49.205  1.00 20.62 ? 195 ILE A CD1 1 
ATOM   1538 N N   . ASP A 1 196 ? 3.211  29.773  48.553  1.00 48.30 ? 196 ASP A N   1 
ATOM   1539 C CA  . ASP A 1 196 ? 1.769  29.555  48.530  1.00 51.50 ? 196 ASP A CA  1 
ATOM   1540 C C   . ASP A 1 196 ? 1.308  28.104  48.568  1.00 48.61 ? 196 ASP A C   1 
ATOM   1541 O O   . ASP A 1 196 ? 1.783  27.258  47.825  1.00 46.50 ? 196 ASP A O   1 
ATOM   1542 C CB  . ASP A 1 196 ? 1.157  30.284  47.321  1.00 59.83 ? 196 ASP A CB  1 
ATOM   1543 C CG  . ASP A 1 196 ? -0.364 30.176  47.273  1.00 71.96 ? 196 ASP A CG  1 
ATOM   1544 O OD1 . ASP A 1 196 ? -1.035 30.587  48.247  1.00 76.32 ? 196 ASP A OD1 1 
ATOM   1545 O OD2 . ASP A 1 196 ? -0.894 29.681  46.253  1.00 79.47 ? 196 ASP A OD2 1 
ATOM   1546 N N   . SER A 1 197 ? 0.319  27.871  49.415  1.00 50.04 ? 197 SER A N   1 
ATOM   1547 C CA  . SER A 1 197 ? -0.306 26.574  49.631  1.00 55.22 ? 197 SER A CA  1 
ATOM   1548 C C   . SER A 1 197 ? -0.526 25.730  48.384  1.00 56.31 ? 197 SER A C   1 
ATOM   1549 O O   . SER A 1 197 ? -0.272 24.524  48.387  1.00 54.57 ? 197 SER A O   1 
ATOM   1550 C CB  . SER A 1 197 ? -1.647 26.793  50.333  1.00 57.80 ? 197 SER A CB  1 
ATOM   1551 O OG  . SER A 1 197 ? -2.293 27.955  49.828  1.00 62.30 ? 197 SER A OG  1 
ATOM   1552 N N   . GLU A 1 198 ? -1.024 26.362  47.331  1.00 59.42 ? 198 GLU A N   1 
ATOM   1553 C CA  . GLU A 1 198 ? -1.284 25.668  46.079  1.00 64.00 ? 198 GLU A CA  1 
ATOM   1554 C C   . GLU A 1 198 ? -0.009 25.074  45.461  1.00 63.23 ? 198 GLU A C   1 
ATOM   1555 O O   . GLU A 1 198 ? -0.064 24.004  44.863  1.00 64.38 ? 198 GLU A O   1 
ATOM   1556 C CB  . GLU A 1 198 ? -2.022 26.597  45.100  1.00 71.84 ? 198 GLU A CB  1 
ATOM   1557 C CG  . GLU A 1 198 ? -2.242 26.040  43.683  1.00 84.79 ? 198 GLU A CG  1 
ATOM   1558 C CD  . GLU A 1 198 ? -2.975 24.699  43.651  1.00 90.94 ? 198 GLU A CD  1 
ATOM   1559 O OE1 . GLU A 1 198 ? -3.968 24.535  44.395  1.00 95.50 ? 198 GLU A OE1 1 
ATOM   1560 O OE2 . GLU A 1 198 ? -2.556 23.811  42.870  1.00 92.43 ? 198 GLU A OE2 1 
ATOM   1561 N N   . GLN A 1 199 ? 1.136  25.734  45.630  1.00 62.38 ? 199 GLN A N   1 
ATOM   1562 C CA  . GLN A 1 199 ? 2.387  25.210  45.086  1.00 64.01 ? 199 GLN A CA  1 
ATOM   1563 C C   . GLN A 1 199 ? 2.759  23.849  45.725  1.00 64.47 ? 199 GLN A C   1 
ATOM   1564 O O   . GLN A 1 199 ? 2.981  22.857  45.024  1.00 65.95 ? 199 GLN A O   1 
ATOM   1565 C CB  . GLN A 1 199 ? 3.546  26.213  45.283  1.00 65.81 ? 199 GLN A CB  1 
ATOM   1566 C CG  . GLN A 1 199 ? 4.877  25.765  44.613  1.00 73.07 ? 199 GLN A CG  1 
ATOM   1567 C CD  . GLN A 1 199 ? 6.168  26.306  45.276  1.00 75.79 ? 199 GLN A CD  1 
ATOM   1568 O OE1 . GLN A 1 199 ? 6.276  27.494  45.582  1.00 78.55 ? 199 GLN A OE1 1 
ATOM   1569 N NE2 . GLN A 1 199 ? 7.159  25.426  45.460  1.00 71.01 ? 199 GLN A NE2 1 
ATOM   1570 N N   . ILE A 1 200 ? 2.767  23.791  47.054  1.00 63.69 ? 200 ILE A N   1 
ATOM   1571 C CA  . ILE A 1 200 ? 3.150  22.579  47.789  1.00 62.98 ? 200 ILE A CA  1 
ATOM   1572 C C   . ILE A 1 200 ? 2.183  21.406  47.777  1.00 62.80 ? 200 ILE A C   1 
ATOM   1573 O O   . ILE A 1 200 ? 2.453  20.377  48.406  1.00 60.65 ? 200 ILE A O   1 
ATOM   1574 C CB  . ILE A 1 200 ? 3.460  22.906  49.251  1.00 62.61 ? 200 ILE A CB  1 
ATOM   1575 C CG1 . ILE A 1 200 ? 2.221  23.494  49.929  1.00 63.86 ? 200 ILE A CG1 1 
ATOM   1576 C CG2 . ILE A 1 200 ? 4.637  23.849  49.319  1.00 63.95 ? 200 ILE A CG2 1 
ATOM   1577 C CD1 . ILE A 1 200 ? 2.496  24.209  51.235  1.00 66.49 ? 200 ILE A CD1 1 
ATOM   1578 N N   . LYS A 1 201 ? 1.077  21.551  47.055  1.00 63.27 ? 201 LYS A N   1 
ATOM   1579 C CA  . LYS A 1 201 ? 0.057  20.511  46.964  1.00 62.55 ? 201 LYS A CA  1 
ATOM   1580 C C   . LYS A 1 201 ? 0.567  19.245  46.269  1.00 59.80 ? 201 LYS A C   1 
ATOM   1581 O O   . LYS A 1 201 ? 0.557  18.158  46.858  1.00 55.31 ? 201 LYS A O   1 
ATOM   1582 C CB  . LYS A 1 201 ? -1.174 21.055  46.233  1.00 67.89 ? 201 LYS A CB  1 
ATOM   1583 C CG  . LYS A 1 201 ? -2.486 20.360  46.592  1.00 75.46 ? 201 LYS A CG  1 
ATOM   1584 C CD  . LYS A 1 201 ? -3.667 21.001  45.873  1.00 79.84 ? 201 LYS A CD  1 
ATOM   1585 C CE  . LYS A 1 201 ? -3.539 20.850  44.363  1.00 82.82 ? 201 LYS A CE  1 
ATOM   1586 N NZ  . LYS A 1 201 ? -4.607 21.592  43.641  1.00 86.57 ? 201 LYS A NZ  1 
ATOM   1587 N N   . GLU A 1 202 ? 1.021  19.391  45.027  1.00 57.62 ? 202 GLU A N   1 
ATOM   1588 C CA  . GLU A 1 202 ? 1.536  18.257  44.265  1.00 59.46 ? 202 GLU A CA  1 
ATOM   1589 C C   . GLU A 1 202 ? 2.900  17.734  44.755  1.00 55.96 ? 202 GLU A C   1 
ATOM   1590 O O   . GLU A 1 202 ? 3.251  16.571  44.508  1.00 54.13 ? 202 GLU A O   1 
ATOM   1591 C CB  . GLU A 1 202 ? 1.569  18.575  42.764  1.00 68.47 ? 202 GLU A CB  1 
ATOM   1592 C CG  . GLU A 1 202 ? 2.316  19.855  42.385  1.00 80.50 ? 202 GLU A CG  1 
ATOM   1593 C CD  . GLU A 1 202 ? 2.478  20.020  40.872  1.00 86.99 ? 202 GLU A CD  1 
ATOM   1594 O OE1 . GLU A 1 202 ? 1.526  19.696  40.121  1.00 90.94 ? 202 GLU A OE1 1 
ATOM   1595 O OE2 . GLU A 1 202 ? 3.562  20.474  40.434  1.00 89.87 ? 202 GLU A OE2 1 
ATOM   1596 N N   . LEU A 1 203 ? 3.673  18.592  45.423  1.00 49.21 ? 203 LEU A N   1 
ATOM   1597 C CA  . LEU A 1 203 ? 4.961  18.184  45.973  1.00 40.85 ? 203 LEU A CA  1 
ATOM   1598 C C   . LEU A 1 203 ? 4.690  17.181  47.093  1.00 39.60 ? 203 LEU A C   1 
ATOM   1599 O O   . LEU A 1 203 ? 5.358  16.160  47.175  1.00 38.40 ? 203 LEU A O   1 
ATOM   1600 C CB  . LEU A 1 203 ? 5.731  19.377  46.546  1.00 33.81 ? 203 LEU A CB  1 
ATOM   1601 C CG  . LEU A 1 203 ? 7.155  19.663  46.042  1.00 26.79 ? 203 LEU A CG  1 
ATOM   1602 C CD1 . LEU A 1 203 ? 7.894  20.578  47.008  1.00 13.10 ? 203 LEU A CD1 1 
ATOM   1603 C CD2 . LEU A 1 203 ? 7.923  18.392  45.884  1.00 23.23 ? 203 LEU A CD2 1 
ATOM   1604 N N   . SER A 1 204 ? 3.719  17.469  47.959  1.00 40.94 ? 204 SER A N   1 
ATOM   1605 C CA  . SER A 1 204 ? 3.384  16.544  49.054  1.00 40.44 ? 204 SER A CA  1 
ATOM   1606 C C   . SER A 1 204 ? 3.094  15.145  48.546  1.00 38.62 ? 204 SER A C   1 
ATOM   1607 O O   . SER A 1 204 ? 3.683  14.189  49.040  1.00 35.26 ? 204 SER A O   1 
ATOM   1608 C CB  . SER A 1 204 ? 2.180  17.020  49.868  1.00 41.53 ? 204 SER A CB  1 
ATOM   1609 O OG  . SER A 1 204 ? 2.536  18.103  50.691  1.00 44.56 ? 204 SER A OG  1 
ATOM   1610 N N   . LYS A 1 205 ? 2.194  15.029  47.565  1.00 34.87 ? 205 LYS A N   1 
ATOM   1611 C CA  . LYS A 1 205 ? 1.841  13.730  47.002  1.00 34.09 ? 205 LYS A CA  1 
ATOM   1612 C C   . LYS A 1 205 ? 3.068  12.995  46.524  1.00 33.96 ? 205 LYS A C   1 
ATOM   1613 O O   . LYS A 1 205 ? 3.376  11.918  47.018  1.00 39.03 ? 205 LYS A O   1 
ATOM   1614 C CB  . LYS A 1 205 ? 0.844  13.874  45.853  1.00 41.75 ? 205 LYS A CB  1 
ATOM   1615 C CG  . LYS A 1 205 ? -0.588 14.115  46.325  1.00 50.96 ? 205 LYS A CG  1 
ATOM   1616 C CD  . LYS A 1 205 ? -1.603 13.849  45.223  1.00 56.27 ? 205 LYS A CD  1 
ATOM   1617 C CE  . LYS A 1 205 ? -2.987 13.575  45.807  1.00 56.93 ? 205 LYS A CE  1 
ATOM   1618 N NZ  . LYS A 1 205 ? -3.043 12.306  46.601  1.00 54.88 ? 205 LYS A NZ  1 
ATOM   1619 N N   . HIS A 1 206 ? 3.779  13.590  45.574  1.00 33.24 ? 206 HIS A N   1 
ATOM   1620 C CA  . HIS A 1 206 ? 4.997  13.015  45.025  1.00 30.89 ? 206 HIS A CA  1 
ATOM   1621 C C   . HIS A 1 206 ? 5.956  12.621  46.151  1.00 31.01 ? 206 HIS A C   1 
ATOM   1622 O O   . HIS A 1 206 ? 6.409  11.480  46.216  1.00 33.10 ? 206 HIS A O   1 
ATOM   1623 C CB  . HIS A 1 206 ? 5.650  14.049  44.116  1.00 39.65 ? 206 HIS A CB  1 
ATOM   1624 C CG  . HIS A 1 206 ? 6.778  13.515  43.286  1.00 49.10 ? 206 HIS A CG  1 
ATOM   1625 N ND1 . HIS A 1 206 ? 7.290  12.247  43.438  1.00 54.31 ? 206 HIS A ND1 1 
ATOM   1626 C CD2 . HIS A 1 206 ? 7.495  14.098  42.296  1.00 50.36 ? 206 HIS A CD2 1 
ATOM   1627 C CE1 . HIS A 1 206 ? 8.280  12.068  42.577  1.00 55.47 ? 206 HIS A CE1 1 
ATOM   1628 N NE2 . HIS A 1 206 ? 8.422  13.175  41.875  1.00 54.80 ? 206 HIS A NE2 1 
ATOM   1629 N N   . ALA A 1 207 ? 6.256  13.560  47.039  1.00 31.26 ? 207 ALA A N   1 
ATOM   1630 C CA  . ALA A 1 207 ? 7.157  13.307  48.159  1.00 31.84 ? 207 ALA A CA  1 
ATOM   1631 C C   . ALA A 1 207 ? 6.683  12.146  49.017  1.00 36.50 ? 207 ALA A C   1 
ATOM   1632 O O   . ALA A 1 207 ? 7.446  11.210  49.237  1.00 38.66 ? 207 ALA A O   1 
ATOM   1633 C CB  . ALA A 1 207 ? 7.308  14.544  49.010  1.00 27.65 ? 207 ALA A CB  1 
ATOM   1634 N N   . LYS A 1 208 ? 5.427  12.191  49.475  1.00 38.98 ? 208 LYS A N   1 
ATOM   1635 C CA  . LYS A 1 208 ? 4.856  11.136  50.330  1.00 41.29 ? 208 LYS A CA  1 
ATOM   1636 C C   . LYS A 1 208 ? 4.823  9.760   49.714  1.00 43.37 ? 208 LYS A C   1 
ATOM   1637 O O   . LYS A 1 208 ? 4.639  8.791   50.430  1.00 49.60 ? 208 LYS A O   1 
ATOM   1638 C CB  . LYS A 1 208 ? 3.440  11.460  50.780  1.00 37.78 ? 208 LYS A CB  1 
ATOM   1639 C CG  . LYS A 1 208 ? 3.349  12.628  51.689  1.00 38.03 ? 208 LYS A CG  1 
ATOM   1640 C CD  . LYS A 1 208 ? 1.918  12.928  52.000  1.00 36.82 ? 208 LYS A CD  1 
ATOM   1641 C CE  . LYS A 1 208 ? 1.798  14.296  52.622  1.00 38.19 ? 208 LYS A CE  1 
ATOM   1642 N NZ  . LYS A 1 208 ? 0.420  14.488  53.115  1.00 41.12 ? 208 LYS A NZ  1 
ATOM   1643 N N   . SER A 1 209 ? 4.922  9.669   48.395  1.00 45.63 ? 209 SER A N   1 
ATOM   1644 C CA  . SER A 1 209 ? 4.925  8.369   47.737  1.00 48.54 ? 209 SER A CA  1 
ATOM   1645 C C   . SER A 1 209 ? 6.354  7.831   47.571  1.00 48.39 ? 209 SER A C   1 
ATOM   1646 O O   . SER A 1 209 ? 6.567  6.717   47.097  1.00 48.86 ? 209 SER A O   1 
ATOM   1647 C CB  . SER A 1 209 ? 4.179  8.462   46.410  1.00 47.63 ? 209 SER A CB  1 
ATOM   1648 O OG  . SER A 1 209 ? 2.822  8.793   46.678  1.00 52.13 ? 209 SER A OG  1 
ATOM   1649 N N   . SER A 1 210 ? 7.320  8.649   47.975  1.00 47.80 ? 210 SER A N   1 
ATOM   1650 C CA  . SER A 1 210 ? 8.735  8.309   47.946  1.00 45.80 ? 210 SER A CA  1 
ATOM   1651 C C   . SER A 1 210 ? 9.094  8.423   49.428  1.00 47.21 ? 210 SER A C   1 
ATOM   1652 O O   . SER A 1 210 ? 9.083  7.432   50.145  1.00 49.69 ? 210 SER A O   1 
ATOM   1653 C CB  . SER A 1 210 ? 9.501  9.338   47.123  1.00 44.53 ? 210 SER A CB  1 
ATOM   1654 O OG  . SER A 1 210 ? 8.688  9.876   46.090  1.00 42.44 ? 210 SER A OG  1 
ATOM   1655 N N   . ASN A 1 220 ? 13.739 0.412   68.084  1.00 64.08 ? 220 ASN A N   1 
ATOM   1656 C CA  . ASN A 1 220 ? 13.026 -0.146  69.236  1.00 62.93 ? 220 ASN A CA  1 
ATOM   1657 C C   . ASN A 1 220 ? 12.858 0.800   70.431  1.00 55.91 ? 220 ASN A C   1 
ATOM   1658 O O   . ASN A 1 220 ? 13.789 1.496   70.845  1.00 55.29 ? 220 ASN A O   1 
ATOM   1659 C CB  . ASN A 1 220 ? 13.682 -1.457  69.703  1.00 72.63 ? 220 ASN A CB  1 
ATOM   1660 C CG  . ASN A 1 220 ? 12.794 -2.687  69.452  1.00 81.39 ? 220 ASN A CG  1 
ATOM   1661 O OD1 . ASN A 1 220 ? 11.905 -2.673  68.583  1.00 85.09 ? 220 ASN A OD1 1 
ATOM   1662 N ND2 . ASN A 1 220 ? 13.035 -3.758  70.213  1.00 82.94 ? 220 ASN A ND2 1 
ATOM   1663 N N   . THR A 1 221 ? 11.652 0.804   70.977  1.00 49.68 ? 221 THR A N   1 
ATOM   1664 C CA  . THR A 1 221 ? 11.321 1.628   72.118  1.00 45.33 ? 221 THR A CA  1 
ATOM   1665 C C   . THR A 1 221 ? 11.381 0.828   73.425  1.00 46.41 ? 221 THR A C   1 
ATOM   1666 O O   . THR A 1 221 ? 11.057 -0.361  73.469  1.00 47.57 ? 221 THR A O   1 
ATOM   1667 C CB  . THR A 1 221 ? 9.895  2.219   71.966  1.00 42.83 ? 221 THR A CB  1 
ATOM   1668 O OG1 . THR A 1 221 ? 9.852  3.111   70.852  1.00 36.07 ? 221 THR A OG1 1 
ATOM   1669 C CG2 . THR A 1 221 ? 9.480  2.973   73.200  1.00 43.55 ? 221 THR A CG2 1 
ATOM   1670 N N   . ILE A 1 222 ? 11.832 1.493   74.476  1.00 45.73 ? 222 ILE A N   1 
ATOM   1671 C CA  . ILE A 1 222 ? 11.911 0.936   75.811  1.00 45.37 ? 222 ILE A CA  1 
ATOM   1672 C C   . ILE A 1 222 ? 11.273 2.061   76.619  1.00 47.04 ? 222 ILE A C   1 
ATOM   1673 O O   . ILE A 1 222 ? 11.499 3.238   76.340  1.00 46.81 ? 222 ILE A O   1 
ATOM   1674 C CB  . ILE A 1 222 ? 13.375 0.770   76.287  1.00 48.07 ? 222 ILE A CB  1 
ATOM   1675 C CG1 . ILE A 1 222 ? 14.151 -0.139  75.340  1.00 50.23 ? 222 ILE A CG1 1 
ATOM   1676 C CG2 . ILE A 1 222 ? 13.415 0.189   77.684  1.00 48.58 ? 222 ILE A CG2 1 
ATOM   1677 C CD1 . ILE A 1 222 ? 15.591 -0.373  75.762  1.00 55.40 ? 222 ILE A CD1 1 
ATOM   1678 N N   . GLY A 1 223 ? 10.447 1.717   77.591  1.00 46.84 ? 223 GLY A N   1 
ATOM   1679 C CA  . GLY A 1 223 ? 9.819  2.748   78.386  1.00 46.31 ? 223 GLY A CA  1 
ATOM   1680 C C   . GLY A 1 223 ? 8.618  2.232   79.140  1.00 44.05 ? 223 GLY A C   1 
ATOM   1681 O O   . GLY A 1 223 ? 8.394  1.027   79.224  1.00 47.73 ? 223 GLY A O   1 
ATOM   1682 N N   . ASN A 1 224 ? 7.828  3.149   79.673  1.00 39.47 ? 224 ASN A N   1 
ATOM   1683 C CA  . ASN A 1 224 ? 6.658  2.792   80.449  1.00 34.55 ? 224 ASN A CA  1 
ATOM   1684 C C   . ASN A 1 224 ? 5.884  4.074   80.743  1.00 36.64 ? 224 ASN A C   1 
ATOM   1685 O O   . ASN A 1 224 ? 6.027  5.064   80.025  1.00 35.90 ? 224 ASN A O   1 
ATOM   1686 C CB  . ASN A 1 224 ? 7.094  2.082   81.740  1.00 28.14 ? 224 ASN A CB  1 
ATOM   1687 C CG  . ASN A 1 224 ? 8.201  2.822   82.475  1.00 21.57 ? 224 ASN A CG  1 
ATOM   1688 O OD1 . ASN A 1 224 ? 8.074  4.001   82.800  1.00 25.84 ? 224 ASN A OD1 1 
ATOM   1689 N ND2 . ASN A 1 224 ? 9.284  2.131   82.744  1.00 27.10 ? 224 ASN A ND2 1 
ATOM   1690 N N   . GLU A 1 225 ? 5.110  4.096   81.818  1.00 35.98 ? 225 GLU A N   1 
ATOM   1691 C CA  . GLU A 1 225 ? 4.345  5.288   82.114  1.00 38.72 ? 225 GLU A CA  1 
ATOM   1692 C C   . GLU A 1 225 ? 5.201  6.488   82.485  1.00 38.17 ? 225 GLU A C   1 
ATOM   1693 O O   . GLU A 1 225 ? 4.755  7.622   82.376  1.00 44.04 ? 225 GLU A O   1 
ATOM   1694 C CB  . GLU A 1 225 ? 3.302  5.020   83.209  1.00 45.95 ? 225 GLU A CB  1 
ATOM   1695 C CG  . GLU A 1 225 ? 3.857  4.619   84.586  1.00 53.27 ? 225 GLU A CG  1 
ATOM   1696 C CD  . GLU A 1 225 ? 4.058  3.111   84.767  1.00 58.51 ? 225 GLU A CD  1 
ATOM   1697 O OE1 . GLU A 1 225 ? 3.814  2.328   83.818  1.00 62.67 ? 225 GLU A OE1 1 
ATOM   1698 O OE2 . GLU A 1 225 ? 4.455  2.704   85.879  1.00 61.86 ? 225 GLU A OE2 1 
ATOM   1699 N N   . PHE A 1 226 ? 6.439  6.256   82.882  1.00 35.69 ? 226 PHE A N   1 
ATOM   1700 C CA  . PHE A 1 226 ? 7.294  7.358   83.294  1.00 34.16 ? 226 PHE A CA  1 
ATOM   1701 C C   . PHE A 1 226 ? 8.182  7.980   82.201  1.00 35.01 ? 226 PHE A C   1 
ATOM   1702 O O   . PHE A 1 226 ? 8.703  9.097   82.357  1.00 34.81 ? 226 PHE A O   1 
ATOM   1703 C CB  . PHE A 1 226 ? 8.119  6.914   84.503  1.00 32.59 ? 226 PHE A CB  1 
ATOM   1704 C CG  . PHE A 1 226 ? 7.279  6.484   85.672  1.00 35.22 ? 226 PHE A CG  1 
ATOM   1705 C CD1 . PHE A 1 226 ? 6.586  7.424   86.432  1.00 35.54 ? 226 PHE A CD1 1 
ATOM   1706 C CD2 . PHE A 1 226 ? 7.129  5.138   85.983  1.00 36.28 ? 226 PHE A CD2 1 
ATOM   1707 C CE1 . PHE A 1 226 ? 5.757  7.027   87.473  1.00 34.45 ? 226 PHE A CE1 1 
ATOM   1708 C CE2 . PHE A 1 226 ? 6.295  4.734   87.034  1.00 32.99 ? 226 PHE A CE2 1 
ATOM   1709 C CZ  . PHE A 1 226 ? 5.611  5.677   87.773  1.00 32.46 ? 226 PHE A CZ  1 
ATOM   1710 N N   . GLY A 1 227 ? 8.356  7.265   81.096  1.00 31.33 ? 227 GLY A N   1 
ATOM   1711 C CA  . GLY A 1 227 ? 9.183  7.782   80.030  1.00 28.89 ? 227 GLY A CA  1 
ATOM   1712 C C   . GLY A 1 227 ? 9.475  6.732   78.994  1.00 28.79 ? 227 GLY A C   1 
ATOM   1713 O O   . GLY A 1 227 ? 9.379  5.535   79.260  1.00 29.67 ? 227 GLY A O   1 
ATOM   1714 N N   . ASN A 1 228 ? 9.840  7.181   77.807  1.00 34.44 ? 228 ASN A N   1 
ATOM   1715 C CA  . ASN A 1 228 ? 10.145 6.270   76.725  1.00 35.66 ? 228 ASN A CA  1 
ATOM   1716 C C   . ASN A 1 228 ? 11.437 6.662   75.997  1.00 35.36 ? 228 ASN A C   1 
ATOM   1717 O O   . ASN A 1 228 ? 11.837 7.836   75.993  1.00 34.24 ? 228 ASN A O   1 
ATOM   1718 C CB  . ASN A 1 228 ? 8.936  6.156   75.790  1.00 36.86 ? 228 ASN A CB  1 
ATOM   1719 C CG  . ASN A 1 228 ? 7.943  5.091   76.256  1.00 42.86 ? 228 ASN A CG  1 
ATOM   1720 O OD1 . ASN A 1 228 ? 8.278  3.907   76.282  1.00 40.66 ? 228 ASN A OD1 1 
ATOM   1721 N ND2 . ASN A 1 228 ? 6.750  5.487   76.687  1.00 47.32 ? 228 ASN A ND2 1 
ATOM   1722 N N   . LEU A 1 229 ? 12.119 5.648   75.467  1.00 33.63 ? 229 LEU A N   1 
ATOM   1723 C CA  . LEU A 1 229 ? 13.379 5.798   74.746  1.00 32.06 ? 229 LEU A CA  1 
ATOM   1724 C C   . LEU A 1 229 ? 13.307 5.063   73.402  1.00 32.72 ? 229 LEU A C   1 
ATOM   1725 O O   . LEU A 1 229 ? 12.975 3.879   73.340  1.00 28.27 ? 229 LEU A O   1 
ATOM   1726 C CB  . LEU A 1 229 ? 14.539 5.235   75.587  1.00 30.28 ? 229 LEU A CB  1 
ATOM   1727 C CG  . LEU A 1 229 ? 16.009 5.330   75.133  1.00 26.13 ? 229 LEU A CG  1 
ATOM   1728 C CD1 . LEU A 1 229 ? 16.438 6.724   74.789  1.00 24.26 ? 229 LEU A CD1 1 
ATOM   1729 C CD2 . LEU A 1 229 ? 16.834 4.925   76.289  1.00 31.05 ? 229 LEU A CD2 1 
ATOM   1730 N N   . THR A 1 230 ? 13.638 5.776   72.333  1.00 36.62 ? 230 THR A N   1 
ATOM   1731 C CA  . THR A 1 230 ? 13.628 5.220   70.992  1.00 35.46 ? 230 THR A CA  1 
ATOM   1732 C C   . THR A 1 230 ? 14.985 5.498   70.363  1.00 37.54 ? 230 THR A C   1 
ATOM   1733 O O   . THR A 1 230 ? 15.351 6.665   70.179  1.00 39.59 ? 230 THR A O   1 
ATOM   1734 C CB  . THR A 1 230 ? 12.528 5.874   70.188  1.00 37.95 ? 230 THR A CB  1 
ATOM   1735 O OG1 . THR A 1 230 ? 11.297 5.731   70.910  1.00 44.37 ? 230 THR A OG1 1 
ATOM   1736 C CG2 . THR A 1 230 ? 12.398 5.230   68.815  1.00 36.60 ? 230 THR A CG2 1 
ATOM   1737 N N   . GLU A 1 231 ? 15.720 4.432   70.032  1.00 38.25 ? 231 GLU A N   1 
ATOM   1738 C CA  . GLU A 1 231 ? 17.066 4.540   69.449  1.00 39.41 ? 231 GLU A CA  1 
ATOM   1739 C C   . GLU A 1 231 ? 17.219 3.928   68.047  1.00 38.54 ? 231 GLU A C   1 
ATOM   1740 O O   . GLU A 1 231 ? 16.648 2.880   67.763  1.00 37.03 ? 231 GLU A O   1 
ATOM   1741 C CB  . GLU A 1 231 ? 18.071 3.881   70.394  1.00 37.69 ? 231 GLU A CB  1 
ATOM   1742 C CG  . GLU A 1 231 ? 19.212 4.766   70.840  1.00 35.43 ? 231 GLU A CG  1 
ATOM   1743 C CD  . GLU A 1 231 ? 19.774 4.335   72.193  1.00 40.02 ? 231 GLU A CD  1 
ATOM   1744 O OE1 . GLU A 1 231 ? 19.897 3.108   72.415  1.00 36.75 ? 231 GLU A OE1 1 
ATOM   1745 O OE2 . GLU A 1 231 ? 20.084 5.218   73.034  1.00 32.74 ? 231 GLU A OE2 1 
ATOM   1746 N N   . ARG A 1 232 ? 18.004 4.580   67.190  1.00 40.89 ? 232 ARG A N   1 
ATOM   1747 C CA  . ARG A 1 232 ? 18.255 4.120   65.819  1.00 43.80 ? 232 ARG A CA  1 
ATOM   1748 C C   . ARG A 1 232 ? 19.738 4.256   65.531  1.00 43.71 ? 232 ARG A C   1 
ATOM   1749 O O   . ARG A 1 232 ? 20.295 5.322   65.765  1.00 45.51 ? 232 ARG A O   1 
ATOM   1750 C CB  . ARG A 1 232 ? 17.519 4.992   64.795  1.00 47.59 ? 232 ARG A CB  1 
ATOM   1751 C CG  . ARG A 1 232 ? 16.000 4.859   64.751  1.00 59.21 ? 232 ARG A CG  1 
ATOM   1752 C CD  . ARG A 1 232 ? 15.311 5.599   65.892  1.00 67.00 ? 232 ARG A CD  1 
ATOM   1753 N NE  . ARG A 1 232 ? 14.851 6.938   65.531  1.00 68.33 ? 232 ARG A NE  1 
ATOM   1754 C CZ  . ARG A 1 232 ? 14.727 7.935   66.402  1.00 68.98 ? 232 ARG A CZ  1 
ATOM   1755 N NH1 . ARG A 1 232 ? 15.040 7.755   67.680  1.00 68.81 ? 232 ARG A NH1 1 
ATOM   1756 N NH2 . ARG A 1 232 ? 14.228 9.097   66.010  1.00 69.60 ? 232 ARG A NH2 1 
ATOM   1757 N N   . THR A 1 233 ? 20.369 3.211   64.996  1.00 44.05 ? 233 THR A N   1 
ATOM   1758 C CA  . THR A 1 233 ? 21.801 3.261   64.668  1.00 45.18 ? 233 THR A CA  1 
ATOM   1759 C C   . THR A 1 233 ? 22.064 3.221   63.158  1.00 47.91 ? 233 THR A C   1 
ATOM   1760 O O   . THR A 1 233 ? 21.605 2.309   62.475  1.00 45.80 ? 233 THR A O   1 
ATOM   1761 C CB  . THR A 1 233 ? 22.579 2.082   65.291  1.00 43.57 ? 233 THR A CB  1 
ATOM   1762 O OG1 . THR A 1 233 ? 22.322 2.010   66.699  1.00 44.60 ? 233 THR A OG1 1 
ATOM   1763 C CG2 . THR A 1 233 ? 24.074 2.265   65.072  1.00 42.42 ? 233 THR A CG2 1 
ATOM   1764 N N   . ASP A 1 234 ? 22.788 4.213   62.641  1.00 49.46 ? 234 ASP A N   1 
ATOM   1765 C CA  . ASP A 1 234 ? 23.135 4.254   61.221  1.00 49.22 ? 234 ASP A CA  1 
ATOM   1766 C C   . ASP A 1 234 ? 24.494 3.601   61.086  1.00 50.61 ? 234 ASP A C   1 
ATOM   1767 O O   . ASP A 1 234 ? 25.523 4.269   61.218  1.00 50.14 ? 234 ASP A O   1 
ATOM   1768 C CB  . ASP A 1 234 ? 23.222 5.690   60.702  1.00 51.89 ? 234 ASP A CB  1 
ATOM   1769 C CG  . ASP A 1 234 ? 23.530 5.759   59.200  1.00 51.81 ? 234 ASP A CG  1 
ATOM   1770 O OD1 . ASP A 1 234 ? 24.615 5.327   58.764  1.00 41.90 ? 234 ASP A OD1 1 
ATOM   1771 O OD2 . ASP A 1 234 ? 22.679 6.265   58.447  1.00 55.37 ? 234 ASP A OD2 1 
ATOM   1772 N N   . ASN A 1 235 ? 24.469 2.299   60.820  1.00 53.24 ? 235 ASN A N   1 
ATOM   1773 C CA  . ASN A 1 235 ? 25.643 1.426   60.645  1.00 54.00 ? 235 ASN A CA  1 
ATOM   1774 C C   . ASN A 1 235 ? 26.836 1.981   59.839  1.00 50.76 ? 235 ASN A C   1 
ATOM   1775 O O   . ASN A 1 235 ? 27.994 1.853   60.249  1.00 47.11 ? 235 ASN A O   1 
ATOM   1776 C CB  . ASN A 1 235 ? 25.165 0.114   60.012  1.00 61.40 ? 235 ASN A CB  1 
ATOM   1777 C CG  . ASN A 1 235 ? 24.124 0.345   58.901  1.00 68.22 ? 235 ASN A CG  1 
ATOM   1778 O OD1 . ASN A 1 235 ? 22.945 0.566   59.185  1.00 70.33 ? 235 ASN A OD1 1 
ATOM   1779 N ND2 . ASN A 1 235 ? 24.567 0.331   57.640  1.00 69.69 ? 235 ASN A ND2 1 
ATOM   1780 N N   . SER A 1 236 ? 26.551 2.548   58.671  1.00 49.66 ? 236 SER A N   1 
ATOM   1781 C CA  . SER A 1 236 ? 27.581 3.114   57.814  1.00 47.88 ? 236 SER A CA  1 
ATOM   1782 C C   . SER A 1 236 ? 28.188 4.378   58.413  1.00 44.79 ? 236 SER A C   1 
ATOM   1783 O O   . SER A 1 236 ? 29.383 4.619   58.265  1.00 44.94 ? 236 SER A O   1 
ATOM   1784 C CB  . SER A 1 236 ? 27.005 3.408   56.428  1.00 52.90 ? 236 SER A CB  1 
ATOM   1785 O OG  . SER A 1 236 ? 25.757 4.074   56.523  1.00 58.87 ? 236 SER A OG  1 
ATOM   1786 N N   . LEU A 1 237 ? 27.355 5.205   59.045  1.00 42.70 ? 237 LEU A N   1 
ATOM   1787 C CA  . LEU A 1 237 ? 27.832 6.432   59.690  1.00 39.04 ? 237 LEU A CA  1 
ATOM   1788 C C   . LEU A 1 237 ? 28.402 6.111   61.077  1.00 34.76 ? 237 LEU A C   1 
ATOM   1789 O O   . LEU A 1 237 ? 29.190 6.891   61.616  1.00 30.65 ? 237 LEU A O   1 
ATOM   1790 C CB  . LEU A 1 237 ? 26.719 7.466   59.848  1.00 42.52 ? 237 LEU A CB  1 
ATOM   1791 C CG  . LEU A 1 237 ? 26.579 8.626   58.862  1.00 47.54 ? 237 LEU A CG  1 
ATOM   1792 C CD1 . LEU A 1 237 ? 26.011 9.820   59.637  1.00 45.41 ? 237 LEU A CD1 1 
ATOM   1793 C CD2 . LEU A 1 237 ? 27.919 9.002   58.227  1.00 47.28 ? 237 LEU A CD2 1 
ATOM   1794 N N   . ASN A 1 238 ? 27.981 4.981   61.654  1.00 30.04 ? 238 ASN A N   1 
ATOM   1795 C CA  . ASN A 1 238 ? 28.461 4.549   62.974  1.00 26.70 ? 238 ASN A CA  1 
ATOM   1796 C C   . ASN A 1 238 ? 28.060 5.613   63.993  1.00 23.20 ? 238 ASN A C   1 
ATOM   1797 O O   . ASN A 1 238 ? 28.857 6.041   64.837  1.00 26.47 ? 238 ASN A O   1 
ATOM   1798 C CB  . ASN A 1 238 ? 29.980 4.374   62.905  1.00 25.11 ? 238 ASN A CB  1 
ATOM   1799 C CG  . ASN A 1 238 ? 30.563 3.801   64.156  1.00 29.49 ? 238 ASN A CG  1 
ATOM   1800 O OD1 . ASN A 1 238 ? 29.859 3.248   64.986  1.00 34.97 ? 238 ASN A OD1 1 
ATOM   1801 N ND2 . ASN A 1 238 ? 31.868 3.934   64.309  1.00 32.73 ? 238 ASN A ND2 1 
ATOM   1802 N N   . VAL A 1 239 ? 26.804 6.038   63.888  1.00 20.17 ? 239 VAL A N   1 
ATOM   1803 C CA  . VAL A 1 239 ? 26.217 7.079   64.736  1.00 20.60 ? 239 VAL A CA  1 
ATOM   1804 C C   . VAL A 1 239 ? 24.769 6.700   65.092  1.00 20.87 ? 239 VAL A C   1 
ATOM   1805 O O   . VAL A 1 239 ? 24.057 6.123   64.271  1.00 26.02 ? 239 VAL A O   1 
ATOM   1806 C CB  . VAL A 1 239 ? 26.278 8.460   63.990  1.00 15.45 ? 239 VAL A CB  1 
ATOM   1807 C CG1 . VAL A 1 239 ? 25.291 9.448   64.555  1.00 18.05 ? 239 VAL A CG1 1 
ATOM   1808 C CG2 . VAL A 1 239 ? 27.687 9.032   64.067  1.00 12.01 ? 239 VAL A CG2 1 
ATOM   1809 N N   . LEU A 1 240 ? 24.317 6.995   66.301  1.00 20.00 ? 240 LEU A N   1 
ATOM   1810 C CA  . LEU A 1 240 ? 22.949 6.637   66.632  1.00 19.86 ? 240 LEU A CA  1 
ATOM   1811 C C   . LEU A 1 240 ? 22.091 7.813   67.091  1.00 20.30 ? 240 LEU A C   1 
ATOM   1812 O O   . LEU A 1 240 ? 22.621 8.784   67.622  1.00 26.66 ? 240 LEU A O   1 
ATOM   1813 C CB  . LEU A 1 240 ? 22.948 5.496   67.642  1.00 22.93 ? 240 LEU A CB  1 
ATOM   1814 C CG  . LEU A 1 240 ? 22.594 5.641   69.120  1.00 27.40 ? 240 LEU A CG  1 
ATOM   1815 C CD1 . LEU A 1 240 ? 22.655 4.249   69.725  1.00 30.34 ? 240 LEU A CD1 1 
ATOM   1816 C CD2 . LEU A 1 240 ? 23.547 6.567   69.844  1.00 29.79 ? 240 LEU A CD2 1 
ATOM   1817 N N   . ILE A 1 241 ? 20.788 7.757   66.810  1.00 20.05 ? 241 ILE A N   1 
ATOM   1818 C CA  . ILE A 1 241 ? 19.845 8.800   67.205  1.00 25.09 ? 241 ILE A CA  1 
ATOM   1819 C C   . ILE A 1 241 ? 18.888 8.244   68.256  1.00 26.69 ? 241 ILE A C   1 
ATOM   1820 O O   . ILE A 1 241 ? 18.367 7.140   68.110  1.00 25.28 ? 241 ILE A O   1 
ATOM   1821 C CB  . ILE A 1 241 ? 19.002 9.391   66.011  1.00 32.21 ? 241 ILE A CB  1 
ATOM   1822 C CG1 . ILE A 1 241 ? 18.924 8.430   64.810  1.00 30.67 ? 241 ILE A CG1 1 
ATOM   1823 C CG2 . ILE A 1 241 ? 19.548 10.736  65.595  1.00 34.59 ? 241 ILE A CG2 1 
ATOM   1824 C CD1 . ILE A 1 241 ? 20.176 8.387   63.966  1.00 35.88 ? 241 ILE A CD1 1 
ATOM   1825 N N   . SER A 1 242 ? 18.672 9.026   69.309  1.00 27.23 ? 242 SER A N   1 
ATOM   1826 C CA  . SER A 1 242 ? 17.806 8.664   70.427  1.00 24.22 ? 242 SER A CA  1 
ATOM   1827 C C   . SER A 1 242 ? 16.759 9.730   70.636  1.00 23.16 ? 242 SER A C   1 
ATOM   1828 O O   . SER A 1 242 ? 17.086 10.919  70.661  1.00 26.28 ? 242 SER A O   1 
ATOM   1829 C CB  . SER A 1 242 ? 18.618 8.627   71.726  1.00 23.07 ? 242 SER A CB  1 
ATOM   1830 O OG  . SER A 1 242 ? 19.753 7.782   71.635  1.00 40.23 ? 242 SER A OG  1 
ATOM   1831 N N   . SER A 1 243 ? 15.514 9.323   70.813  1.00 22.13 ? 243 SER A N   1 
ATOM   1832 C CA  . SER A 1 243 ? 14.452 10.270  71.101  1.00 24.98 ? 243 SER A CA  1 
ATOM   1833 C C   . SER A 1 243 ? 14.031 9.929   72.534  1.00 25.01 ? 243 SER A C   1 
ATOM   1834 O O   . SER A 1 243 ? 13.888 8.754   72.868  1.00 24.82 ? 243 SER A O   1 
ATOM   1835 C CB  . SER A 1 243 ? 13.326 10.114  70.092  1.00 31.36 ? 243 SER A CB  1 
ATOM   1836 O OG  . SER A 1 243 ? 13.835 10.316  68.770  1.00 40.52 ? 243 SER A OG  1 
ATOM   1837 N N   . ILE A 1 244 ? 13.955 10.933  73.402  1.00 25.19 ? 244 ILE A N   1 
ATOM   1838 C CA  . ILE A 1 244 ? 13.621 10.698  74.811  1.00 28.49 ? 244 ILE A CA  1 
ATOM   1839 C C   . ILE A 1 244 ? 12.528 11.605  75.358  1.00 30.67 ? 244 ILE A C   1 
ATOM   1840 O O   . ILE A 1 244 ? 12.620 12.833  75.299  1.00 26.26 ? 244 ILE A O   1 
ATOM   1841 C CB  . ILE A 1 244 ? 14.854 10.907  75.739  1.00 33.60 ? 244 ILE A CB  1 
ATOM   1842 C CG1 . ILE A 1 244 ? 16.099 10.232  75.166  1.00 40.95 ? 244 ILE A CG1 1 
ATOM   1843 C CG2 . ILE A 1 244 ? 14.592 10.341  77.116  1.00 29.74 ? 244 ILE A CG2 1 
ATOM   1844 C CD1 . ILE A 1 244 ? 17.366 10.525  75.969  1.00 45.70 ? 244 ILE A CD1 1 
ATOM   1845 N N   . GLU A 1 245 ? 11.494 10.984  75.907  1.00 35.06 ? 245 GLU A N   1 
ATOM   1846 C CA  . GLU A 1 245 ? 10.394 11.710  76.514  1.00 34.22 ? 245 GLU A CA  1 
ATOM   1847 C C   . GLU A 1 245 ? 10.169 11.089  77.897  1.00 36.13 ? 245 GLU A C   1 
ATOM   1848 O O   . GLU A 1 245 ? 10.164 9.861   78.055  1.00 36.86 ? 245 GLU A O   1 
ATOM   1849 C CB  . GLU A 1 245 ? 9.132  11.650  75.647  1.00 32.89 ? 245 GLU A CB  1 
ATOM   1850 C CG  . GLU A 1 245 ? 8.777  10.276  75.113  1.00 40.11 ? 245 GLU A CG  1 
ATOM   1851 C CD  . GLU A 1 245 ? 7.369  10.229  74.537  1.00 44.45 ? 245 GLU A CD  1 
ATOM   1852 O OE1 . GLU A 1 245 ? 6.982  11.188  73.844  1.00 51.52 ? 245 GLU A OE1 1 
ATOM   1853 O OE2 . GLU A 1 245 ? 6.640  9.243   74.784  1.00 44.48 ? 245 GLU A OE2 1 
ATOM   1854 N N   . MET A 1 246 ? 10.096 11.947  78.905  1.00 33.07 ? 246 MET A N   1 
ATOM   1855 C CA  . MET A 1 246 ? 9.892  11.523  80.280  1.00 30.55 ? 246 MET A CA  1 
ATOM   1856 C C   . MET A 1 246 ? 8.828  12.441  80.860  1.00 30.84 ? 246 MET A C   1 
ATOM   1857 O O   . MET A 1 246 ? 8.850  13.655  80.596  1.00 35.85 ? 246 MET A O   1 
ATOM   1858 C CB  . MET A 1 246 ? 11.191 11.719  81.060  1.00 31.00 ? 246 MET A CB  1 
ATOM   1859 C CG  . MET A 1 246 ? 12.355 10.908  80.587  1.00 24.96 ? 246 MET A CG  1 
ATOM   1860 S SD  . MET A 1 246 ? 13.857 11.551  81.303  1.00 35.05 ? 246 MET A SD  1 
ATOM   1861 C CE  . MET A 1 246 ? 13.499 11.423  83.120  1.00 24.09 ? 246 MET A CE  1 
ATOM   1862 N N   . GLU A 1 247 ? 7.875  11.892  81.609  1.00 27.66 ? 247 GLU A N   1 
ATOM   1863 C CA  . GLU A 1 247 ? 6.851  12.749  82.192  1.00 27.23 ? 247 GLU A CA  1 
ATOM   1864 C C   . GLU A 1 247 ? 7.484  13.472  83.371  1.00 22.83 ? 247 GLU A C   1 
ATOM   1865 O O   . GLU A 1 247 ? 8.578  13.133  83.795  1.00 24.03 ? 247 GLU A O   1 
ATOM   1866 C CB  . GLU A 1 247 ? 5.620  11.949  82.628  1.00 31.78 ? 247 GLU A CB  1 
ATOM   1867 C CG  . GLU A 1 247 ? 5.805  11.165  83.908  1.00 52.02 ? 247 GLU A CG  1 
ATOM   1868 C CD  . GLU A 1 247 ? 4.536  11.090  84.757  1.00 64.06 ? 247 GLU A CD  1 
ATOM   1869 O OE1 . GLU A 1 247 ? 3.425  10.982  84.185  1.00 69.09 ? 247 GLU A OE1 1 
ATOM   1870 O OE2 . GLU A 1 247 ? 4.654  11.141  86.003  1.00 68.12 ? 247 GLU A OE2 1 
ATOM   1871 N N   . GLU A 1 248 ? 6.830  14.491  83.889  1.00 23.28 ? 248 GLU A N   1 
ATOM   1872 C CA  . GLU A 1 248 ? 7.399  15.212  85.023  1.00 27.42 ? 248 GLU A CA  1 
ATOM   1873 C C   . GLU A 1 248 ? 7.643  14.357  86.286  1.00 26.64 ? 248 GLU A C   1 
ATOM   1874 O O   . GLU A 1 248 ? 6.777  13.584  86.716  1.00 23.78 ? 248 GLU A O   1 
ATOM   1875 C CB  . GLU A 1 248 ? 6.517  16.401  85.369  1.00 27.24 ? 248 GLU A CB  1 
ATOM   1876 C CG  . GLU A 1 248 ? 6.953  17.123  86.610  1.00 28.37 ? 248 GLU A CG  1 
ATOM   1877 C CD  . GLU A 1 248 ? 6.105  18.341  86.902  1.00 39.22 ? 248 GLU A CD  1 
ATOM   1878 O OE1 . GLU A 1 248 ? 5.466  18.892  85.969  1.00 38.01 ? 248 GLU A OE1 1 
ATOM   1879 O OE2 . GLU A 1 248 ? 6.092  18.752  88.081  1.00 48.39 ? 248 GLU A OE2 1 
ATOM   1880 N N   . GLY A 1 249 ? 8.827  14.515  86.874  1.00 30.60 ? 249 GLY A N   1 
ATOM   1881 C CA  . GLY A 1 249 ? 9.187  13.782  88.082  1.00 33.88 ? 249 GLY A CA  1 
ATOM   1882 C C   . GLY A 1 249 ? 9.823  12.416  87.855  1.00 35.41 ? 249 GLY A C   1 
ATOM   1883 O O   . GLY A 1 249 ? 10.194 11.728  88.815  1.00 32.05 ? 249 GLY A O   1 
ATOM   1884 N N   . ALA A 1 250 ? 9.891  12.002  86.591  1.00 33.38 ? 250 ALA A N   1 
ATOM   1885 C CA  . ALA A 1 250 ? 10.471 10.722  86.209  1.00 30.66 ? 250 ALA A CA  1 
ATOM   1886 C C   . ALA A 1 250 ? 11.986 10.788  86.322  1.00 32.56 ? 250 ALA A C   1 
ATOM   1887 O O   . ALA A 1 250 ? 12.585 11.863  86.161  1.00 28.82 ? 250 ALA A O   1 
ATOM   1888 C CB  . ALA A 1 250 ? 10.080 10.373  84.770  1.00 30.75 ? 250 ALA A CB  1 
ATOM   1889 N N   . LEU A 1 251 ? 12.596 9.627   86.583  1.00 34.65 ? 251 LEU A N   1 
ATOM   1890 C CA  . LEU A 1 251 ? 14.044 9.499   86.711  1.00 27.87 ? 251 LEU A CA  1 
ATOM   1891 C C   . LEU A 1 251 ? 14.554 8.416   85.788  1.00 26.98 ? 251 LEU A C   1 
ATOM   1892 O O   . LEU A 1 251 ? 13.951 7.346   85.684  1.00 23.76 ? 251 LEU A O   1 
ATOM   1893 C CB  . LEU A 1 251 ? 14.436 9.129   88.141  1.00 25.91 ? 251 LEU A CB  1 
ATOM   1894 C CG  . LEU A 1 251 ? 15.918 8.835   88.427  1.00 29.55 ? 251 LEU A CG  1 
ATOM   1895 C CD1 . LEU A 1 251 ? 16.681 10.132  88.606  1.00 30.83 ? 251 LEU A CD1 1 
ATOM   1896 C CD2 . LEU A 1 251 ? 16.058 7.987   89.687  1.00 30.52 ? 251 LEU A CD2 1 
ATOM   1897 N N   . PHE A 1 252 ? 15.644 8.724   85.092  1.00 27.56 ? 252 PHE A N   1 
ATOM   1898 C CA  . PHE A 1 252 ? 16.311 7.781   84.208  1.00 28.52 ? 252 PHE A CA  1 
ATOM   1899 C C   . PHE A 1 252 ? 17.493 7.403   85.097  1.00 32.01 ? 252 PHE A C   1 
ATOM   1900 O O   . PHE A 1 252 ? 18.481 8.145   85.210  1.00 32.50 ? 252 PHE A O   1 
ATOM   1901 C CB  . PHE A 1 252 ? 16.767 8.467   82.911  1.00 30.67 ? 252 PHE A CB  1 
ATOM   1902 C CG  . PHE A 1 252 ? 17.285 7.512   81.844  1.00 31.55 ? 252 PHE A CG  1 
ATOM   1903 C CD1 . PHE A 1 252 ? 17.514 6.158   82.130  1.00 24.62 ? 252 PHE A CD1 1 
ATOM   1904 C CD2 . PHE A 1 252 ? 17.580 7.985   80.561  1.00 29.66 ? 252 PHE A CD2 1 
ATOM   1905 C CE1 . PHE A 1 252 ? 18.033 5.290   81.162  1.00 27.49 ? 252 PHE A CE1 1 
ATOM   1906 C CE2 . PHE A 1 252 ? 18.100 7.121   79.581  1.00 32.19 ? 252 PHE A CE2 1 
ATOM   1907 C CZ  . PHE A 1 252 ? 18.328 5.769   79.883  1.00 26.78 ? 252 PHE A CZ  1 
ATOM   1908 N N   . VAL A 1 253 ? 17.322 6.286   85.801  1.00 33.84 ? 253 VAL A N   1 
ATOM   1909 C CA  . VAL A 1 253 ? 18.300 5.779   86.758  1.00 29.12 ? 253 VAL A CA  1 
ATOM   1910 C C   . VAL A 1 253 ? 19.748 5.716   86.258  1.00 27.02 ? 253 VAL A C   1 
ATOM   1911 O O   . VAL A 1 253 ? 20.002 5.778   85.044  1.00 27.40 ? 253 VAL A O   1 
ATOM   1912 C CB  . VAL A 1 253 ? 17.839 4.396   87.372  1.00 29.13 ? 253 VAL A CB  1 
ATOM   1913 C CG1 . VAL A 1 253 ? 16.436 4.518   87.949  1.00 26.35 ? 253 VAL A CG1 1 
ATOM   1914 C CG2 . VAL A 1 253 ? 17.899 3.266   86.358  1.00 24.06 ? 253 VAL A CG2 1 
ATOM   1915 N N   . PRO A 1 254 ? 20.718 5.701   87.198  1.00 23.26 ? 254 PRO A N   1 
ATOM   1916 C CA  . PRO A 1 254 ? 22.151 5.639   86.891  1.00 21.52 ? 254 PRO A CA  1 
ATOM   1917 C C   . PRO A 1 254 ? 22.488 4.585   85.829  1.00 21.11 ? 254 PRO A C   1 
ATOM   1918 O O   . PRO A 1 254 ? 22.167 3.412   85.981  1.00 21.56 ? 254 PRO A O   1 
ATOM   1919 C CB  . PRO A 1 254 ? 22.757 5.304   88.254  1.00 19.95 ? 254 PRO A CB  1 
ATOM   1920 C CG  . PRO A 1 254 ? 21.895 6.128   89.184  1.00 10.76 ? 254 PRO A CG  1 
ATOM   1921 C CD  . PRO A 1 254 ? 20.508 5.845   88.659  1.00 19.77 ? 254 PRO A CD  1 
ATOM   1922 N N   . HIS A 1 255 ? 23.130 5.017   84.748  1.00 24.68 ? 255 HIS A N   1 
ATOM   1923 C CA  . HIS A 1 255 ? 23.506 4.118   83.659  1.00 20.23 ? 255 HIS A CA  1 
ATOM   1924 C C   . HIS A 1 255 ? 24.739 4.659   82.937  1.00 23.56 ? 255 HIS A C   1 
ATOM   1925 O O   . HIS A 1 255 ? 25.269 5.710   83.305  1.00 23.39 ? 255 HIS A O   1 
ATOM   1926 C CB  . HIS A 1 255 ? 22.346 4.008   82.663  1.00 21.85 ? 255 HIS A CB  1 
ATOM   1927 C CG  . HIS A 1 255 ? 21.982 5.308   81.998  1.00 20.27 ? 255 HIS A CG  1 
ATOM   1928 N ND1 . HIS A 1 255 ? 21.340 6.331   82.659  1.00 26.46 ? 255 HIS A ND1 1 
ATOM   1929 C CD2 . HIS A 1 255 ? 22.164 5.740   80.730  1.00 21.38 ? 255 HIS A CD2 1 
ATOM   1930 C CE1 . HIS A 1 255 ? 21.140 7.336   81.829  1.00 24.99 ? 255 HIS A CE1 1 
ATOM   1931 N NE2 . HIS A 1 255 ? 21.630 7.005   80.649  1.00 22.56 ? 255 HIS A NE2 1 
ATOM   1932 N N   . TYR A 1 256 ? 25.222 3.924   81.943  1.00 22.15 ? 256 TYR A N   1 
ATOM   1933 C CA  . TYR A 1 256 ? 26.357 4.371   81.126  1.00 21.64 ? 256 TYR A CA  1 
ATOM   1934 C C   . TYR A 1 256 ? 26.320 3.584   79.825  1.00 20.74 ? 256 TYR A C   1 
ATOM   1935 O O   . TYR A 1 256 ? 25.550 2.627   79.707  1.00 16.25 ? 256 TYR A O   1 
ATOM   1936 C CB  . TYR A 1 256 ? 27.717 4.241   81.849  1.00 20.95 ? 256 TYR A CB  1 
ATOM   1937 C CG  . TYR A 1 256 ? 28.363 2.858   81.884  1.00 21.57 ? 256 TYR A CG  1 
ATOM   1938 C CD1 . TYR A 1 256 ? 28.984 2.314   80.750  1.00 22.90 ? 256 TYR A CD1 1 
ATOM   1939 C CD2 . TYR A 1 256 ? 28.368 2.110   83.049  1.00 17.73 ? 256 TYR A CD2 1 
ATOM   1940 C CE1 . TYR A 1 256 ? 29.588 1.060   80.790  1.00 17.83 ? 256 TYR A CE1 1 
ATOM   1941 C CE2 . TYR A 1 256 ? 28.958 0.867   83.095  1.00 20.22 ? 256 TYR A CE2 1 
ATOM   1942 C CZ  . TYR A 1 256 ? 29.566 0.343   81.970  1.00 18.94 ? 256 TYR A CZ  1 
ATOM   1943 O OH  . TYR A 1 256 ? 30.137 -0.913  82.049  1.00 21.18 ? 256 TYR A OH  1 
ATOM   1944 N N   . TYR A 1 257 ? 27.050 4.067   78.823  1.00 25.88 ? 257 TYR A N   1 
ATOM   1945 C CA  . TYR A 1 257 ? 27.125 3.432   77.499  1.00 22.75 ? 257 TYR A CA  1 
ATOM   1946 C C   . TYR A 1 257 ? 28.579 3.049   77.307  1.00 21.36 ? 257 TYR A C   1 
ATOM   1947 O O   . TYR A 1 257 ? 29.465 3.897   77.389  1.00 20.60 ? 257 TYR A O   1 
ATOM   1948 C CB  . TYR A 1 257 ? 26.708 4.413   76.396  1.00 25.76 ? 257 TYR A CB  1 
ATOM   1949 C CG  . TYR A 1 257 ? 25.216 4.575   76.183  1.00 28.85 ? 257 TYR A CG  1 
ATOM   1950 C CD1 . TYR A 1 257 ? 24.305 4.368   77.221  1.00 30.23 ? 257 TYR A CD1 1 
ATOM   1951 C CD2 . TYR A 1 257 ? 24.718 4.978   74.947  1.00 31.07 ? 257 TYR A CD2 1 
ATOM   1952 C CE1 . TYR A 1 257 ? 22.943 4.566   77.037  1.00 30.40 ? 257 TYR A CE1 1 
ATOM   1953 C CE2 . TYR A 1 257 ? 23.351 5.176   74.750  1.00 30.22 ? 257 TYR A CE2 1 
ATOM   1954 C CZ  . TYR A 1 257 ? 22.469 4.967   75.799  1.00 29.74 ? 257 TYR A CZ  1 
ATOM   1955 O OH  . TYR A 1 257 ? 21.112 5.143   75.606  1.00 28.02 ? 257 TYR A OH  1 
ATOM   1956 N N   . SER A 1 258 ? 28.819 1.777   77.041  1.00 17.38 ? 258 SER A N   1 
ATOM   1957 C CA  . SER A 1 258 ? 30.153 1.259   76.886  1.00 15.27 ? 258 SER A CA  1 
ATOM   1958 C C   . SER A 1 258 ? 31.142 2.006   76.029  1.00 20.62 ? 258 SER A C   1 
ATOM   1959 O O   . SER A 1 258 ? 32.314 2.141   76.434  1.00 22.89 ? 258 SER A O   1 
ATOM   1960 C CB  . SER A 1 258 ? 30.075 -0.159  76.376  1.00 17.01 ? 258 SER A CB  1 
ATOM   1961 O OG  . SER A 1 258 ? 29.471 -0.210  75.095  1.00 26.53 ? 258 SER A OG  1 
ATOM   1962 N N   . LYS A 1 259 ? 30.703 2.430   74.831  1.00 23.25 ? 259 LYS A N   1 
ATOM   1963 C CA  . LYS A 1 259 ? 31.580 3.128   73.861  1.00 22.41 ? 259 LYS A CA  1 
ATOM   1964 C C   . LYS A 1 259 ? 31.115 4.390   73.132  1.00 20.23 ? 259 LYS A C   1 
ATOM   1965 O O   . LYS A 1 259 ? 31.947 5.149   72.661  1.00 17.97 ? 259 LYS A O   1 
ATOM   1966 C CB  . LYS A 1 259 ? 32.108 2.156   72.789  1.00 25.48 ? 259 LYS A CB  1 
ATOM   1967 C CG  . LYS A 1 259 ? 31.315 0.863   72.590  1.00 30.63 ? 259 LYS A CG  1 
ATOM   1968 C CD  . LYS A 1 259 ? 31.224 0.528   71.140  1.00 35.48 ? 259 LYS A CD  1 
ATOM   1969 C CE  . LYS A 1 259 ? 32.580 0.658   70.473  1.00 45.65 ? 259 LYS A CE  1 
ATOM   1970 N NZ  . LYS A 1 259 ? 32.504 0.652   68.980  1.00 45.51 ? 259 LYS A NZ  1 
ATOM   1971 N N   . ALA A 1 260 ? 29.814 4.594   73.000  1.00 23.23 ? 260 ALA A N   1 
ATOM   1972 C CA  . ALA A 1 260 ? 29.264 5.768   72.309  1.00 21.99 ? 260 ALA A CA  1 
ATOM   1973 C C   . ALA A 1 260 ? 29.392 7.038   73.144  1.00 24.75 ? 260 ALA A C   1 
ATOM   1974 O O   . ALA A 1 260 ? 29.037 7.012   74.325  1.00 28.35 ? 260 ALA A O   1 
ATOM   1975 C CB  . ALA A 1 260 ? 27.776 5.517   72.001  1.00 18.61 ? 260 ALA A CB  1 
ATOM   1976 N N   . ILE A 1 261 ? 29.933 8.128   72.587  1.00 22.57 ? 261 ILE A N   1 
ATOM   1977 C CA  . ILE A 1 261 ? 29.998 9.383   73.358  1.00 21.98 ? 261 ILE A CA  1 
ATOM   1978 C C   . ILE A 1 261 ? 28.694 10.085  72.991  1.00 22.90 ? 261 ILE A C   1 
ATOM   1979 O O   . ILE A 1 261 ? 28.355 10.183  71.816  1.00 29.63 ? 261 ILE A O   1 
ATOM   1980 C CB  . ILE A 1 261 ? 31.301 10.222  73.116  1.00 21.96 ? 261 ILE A CB  1 
ATOM   1981 C CG1 . ILE A 1 261 ? 31.001 11.574  72.501  1.00 27.37 ? 261 ILE A CG1 1 
ATOM   1982 C CG2 . ILE A 1 261 ? 32.358 9.434   72.391  1.00 16.71 ? 261 ILE A CG2 1 
ATOM   1983 C CD1 . ILE A 1 261 ? 30.767 12.623  73.530  1.00 26.36 ? 261 ILE A CD1 1 
ATOM   1984 N N   . VAL A 1 262 ? 27.913 10.488  73.985  1.00 18.92 ? 262 VAL A N   1 
ATOM   1985 C CA  . VAL A 1 262 ? 26.591 11.053  73.713  1.00 18.42 ? 262 VAL A CA  1 
ATOM   1986 C C   . VAL A 1 262 ? 26.368 12.562  73.801  1.00 20.34 ? 262 VAL A C   1 
ATOM   1987 O O   . VAL A 1 262 ? 26.787 13.194  74.754  1.00 21.56 ? 262 VAL A O   1 
ATOM   1988 C CB  . VAL A 1 262 ? 25.527 10.342  74.593  1.00 13.25 ? 262 VAL A CB  1 
ATOM   1989 C CG1 . VAL A 1 262 ? 24.158 11.008  74.439  1.00 19.96 ? 262 VAL A CG1 1 
ATOM   1990 C CG2 . VAL A 1 262 ? 25.414 8.877   74.209  1.00 10.34 ? 262 VAL A CG2 1 
ATOM   1991 N N   . ILE A 1 263 ? 25.676 13.119  72.808  1.00 20.53 ? 263 ILE A N   1 
ATOM   1992 C CA  . ILE A 1 263 ? 25.351 14.549  72.772  1.00 20.87 ? 263 ILE A CA  1 
ATOM   1993 C C   . ILE A 1 263 ? 23.837 14.745  72.946  1.00 24.31 ? 263 ILE A C   1 
ATOM   1994 O O   . ILE A 1 263 ? 23.063 14.425  72.039  1.00 24.57 ? 263 ILE A O   1 
ATOM   1995 C CB  . ILE A 1 263 ? 25.737 15.208  71.432  1.00 12.90 ? 263 ILE A CB  1 
ATOM   1996 C CG1 . ILE A 1 263 ? 27.147 14.807  71.012  1.00 16.32 ? 263 ILE A CG1 1 
ATOM   1997 C CG2 . ILE A 1 263 ? 25.731 16.718  71.585  1.00 9.88  ? 263 ILE A CG2 1 
ATOM   1998 C CD1 . ILE A 1 263 ? 27.514 15.272  69.570  1.00 12.65 ? 263 ILE A CD1 1 
ATOM   1999 N N   . LEU A 1 264 ? 23.425 15.258  74.107  1.00 26.10 ? 264 LEU A N   1 
ATOM   2000 C CA  . LEU A 1 264 ? 22.008 15.513  74.403  1.00 28.39 ? 264 LEU A CA  1 
ATOM   2001 C C   . LEU A 1 264 ? 21.578 16.941  74.085  1.00 23.55 ? 264 LEU A C   1 
ATOM   2002 O O   . LEU A 1 264 ? 22.305 17.893  74.333  1.00 22.74 ? 264 LEU A O   1 
ATOM   2003 C CB  . LEU A 1 264 ? 21.695 15.249  75.876  1.00 35.35 ? 264 LEU A CB  1 
ATOM   2004 C CG  . LEU A 1 264 ? 21.003 13.966  76.333  1.00 40.63 ? 264 LEU A CG  1 
ATOM   2005 C CD1 . LEU A 1 264 ? 20.340 14.288  77.671  1.00 42.38 ? 264 LEU A CD1 1 
ATOM   2006 C CD2 . LEU A 1 264 ? 19.940 13.496  75.335  1.00 39.49 ? 264 LEU A CD2 1 
ATOM   2007 N N   . VAL A 1 265 ? 20.353 17.078  73.607  1.00 24.68 ? 265 VAL A N   1 
ATOM   2008 C CA  . VAL A 1 265 ? 19.790 18.373  73.250  1.00 23.79 ? 265 VAL A CA  1 
ATOM   2009 C C   . VAL A 1 265 ? 18.367 18.393  73.832  1.00 26.19 ? 265 VAL A C   1 
ATOM   2010 O O   . VAL A 1 265 ? 17.610 17.414  73.688  1.00 26.00 ? 265 VAL A O   1 
ATOM   2011 C CB  . VAL A 1 265 ? 19.745 18.534  71.669  1.00 19.65 ? 265 VAL A CB  1 
ATOM   2012 C CG1 . VAL A 1 265 ? 19.241 19.910  71.248  1.00 21.12 ? 265 VAL A CG1 1 
ATOM   2013 C CG2 . VAL A 1 265 ? 21.102 18.313  71.095  1.00 14.71 ? 265 VAL A CG2 1 
ATOM   2014 N N   . VAL A 1 266 ? 18.027 19.459  74.554  1.00 26.30 ? 266 VAL A N   1 
ATOM   2015 C CA  . VAL A 1 266 ? 16.675 19.577  75.112  1.00 24.63 ? 266 VAL A CA  1 
ATOM   2016 C C   . VAL A 1 266 ? 15.799 20.222  74.022  1.00 25.62 ? 266 VAL A C   1 
ATOM   2017 O O   . VAL A 1 266 ? 16.125 21.309  73.526  1.00 26.40 ? 266 VAL A O   1 
ATOM   2018 C CB  . VAL A 1 266 ? 16.620 20.489  76.400  1.00 25.59 ? 266 VAL A CB  1 
ATOM   2019 C CG1 . VAL A 1 266 ? 15.287 20.303  77.118  1.00 16.21 ? 266 VAL A CG1 1 
ATOM   2020 C CG2 . VAL A 1 266 ? 17.793 20.212  77.355  1.00 20.31 ? 266 VAL A CG2 1 
ATOM   2021 N N   . ASN A 1 267 ? 14.721 19.548  73.624  1.00 23.76 ? 267 ASN A N   1 
ATOM   2022 C CA  . ASN A 1 267 ? 13.808 20.083  72.611  1.00 24.14 ? 267 ASN A CA  1 
ATOM   2023 C C   . ASN A 1 267 ? 12.803 21.024  73.249  1.00 30.88 ? 267 ASN A C   1 
ATOM   2024 O O   . ASN A 1 267 ? 12.471 22.077  72.703  1.00 29.03 ? 267 ASN A O   1 
ATOM   2025 C CB  . ASN A 1 267 ? 13.037 18.960  71.910  1.00 18.66 ? 267 ASN A CB  1 
ATOM   2026 C CG  . ASN A 1 267 ? 13.936 18.039  71.126  1.00 11.12 ? 267 ASN A CG  1 
ATOM   2027 O OD1 . ASN A 1 267 ? 15.093 18.354  70.872  1.00 18.47 ? 267 ASN A OD1 1 
ATOM   2028 N ND2 . ASN A 1 267 ? 13.432 16.865  70.792  1.00 19.23 ? 267 ASN A ND2 1 
ATOM   2029 N N   . GLU A 1 268 ? 12.333 20.626  74.428  1.00 37.80 ? 268 GLU A N   1 
ATOM   2030 C CA  . GLU A 1 268 ? 11.335 21.370  75.186  1.00 37.11 ? 268 GLU A CA  1 
ATOM   2031 C C   . GLU A 1 268 ? 11.353 20.800  76.611  1.00 33.47 ? 268 GLU A C   1 
ATOM   2032 O O   . GLU A 1 268 ? 11.645 19.610  76.793  1.00 29.78 ? 268 GLU A O   1 
ATOM   2033 C CB  . GLU A 1 268 ? 9.962  21.137  74.536  1.00 44.95 ? 268 GLU A CB  1 
ATOM   2034 C CG  . GLU A 1 268 ? 8.913  22.192  74.826  1.00 62.63 ? 268 GLU A CG  1 
ATOM   2035 C CD  . GLU A 1 268 ? 9.221  23.523  74.160  1.00 73.39 ? 268 GLU A CD  1 
ATOM   2036 O OE1 . GLU A 1 268 ? 9.940  24.341  74.782  1.00 79.09 ? 268 GLU A OE1 1 
ATOM   2037 O OE2 . GLU A 1 268 ? 8.740  23.750  73.020  1.00 79.45 ? 268 GLU A OE2 1 
ATOM   2038 N N   . GLY A 1 269 ? 11.092 21.642  77.613  1.00 30.17 ? 269 GLY A N   1 
ATOM   2039 C CA  . GLY A 1 269 ? 11.072 21.162  78.985  1.00 28.94 ? 269 GLY A CA  1 
ATOM   2040 C C   . GLY A 1 269 ? 12.295 21.523  79.816  1.00 37.34 ? 269 GLY A C   1 
ATOM   2041 O O   . GLY A 1 269 ? 13.136 22.352  79.397  1.00 39.74 ? 269 GLY A O   1 
ATOM   2042 N N   . GLU A 1 270 ? 12.387 20.913  81.004  1.00 36.97 ? 270 GLU A N   1 
ATOM   2043 C CA  . GLU A 1 270 ? 13.491 21.134  81.951  1.00 36.89 ? 270 GLU A CA  1 
ATOM   2044 C C   . GLU A 1 270 ? 13.944 19.824  82.617  1.00 34.90 ? 270 GLU A C   1 
ATOM   2045 O O   . GLU A 1 270 ? 13.116 18.959  82.940  1.00 33.55 ? 270 GLU A O   1 
ATOM   2046 C CB  . GLU A 1 270 ? 13.051 22.102  83.059  1.00 37.93 ? 270 GLU A CB  1 
ATOM   2047 C CG  . GLU A 1 270 ? 12.563 23.442  82.569  1.00 49.64 ? 270 GLU A CG  1 
ATOM   2048 C CD  . GLU A 1 270 ? 12.358 24.445  83.685  1.00 59.96 ? 270 GLU A CD  1 
ATOM   2049 O OE1 . GLU A 1 270 ? 11.975 24.038  84.808  1.00 66.98 ? 270 GLU A OE1 1 
ATOM   2050 O OE2 . GLU A 1 270 ? 12.579 25.651  83.434  1.00 64.56 ? 270 GLU A OE2 1 
ATOM   2051 N N   . ALA A 1 271 ? 15.238 19.717  82.911  1.00 32.79 ? 271 ALA A N   1 
ATOM   2052 C CA  . ALA A 1 271 ? 15.773 18.517  83.550  1.00 29.30 ? 271 ALA A CA  1 
ATOM   2053 C C   . ALA A 1 271 ? 17.012 18.781  84.394  1.00 26.02 ? 271 ALA A C   1 
ATOM   2054 O O   . ALA A 1 271 ? 17.716 19.770  84.206  1.00 25.33 ? 271 ALA A O   1 
ATOM   2055 C CB  . ALA A 1 271 ? 16.068 17.422  82.489  1.00 29.39 ? 271 ALA A CB  1 
ATOM   2056 N N   . HIS A 1 272 ? 17.235 17.900  85.359  1.00 25.80 ? 272 HIS A N   1 
ATOM   2057 C CA  . HIS A 1 272 ? 18.377 17.952  86.260  1.00 27.12 ? 272 HIS A CA  1 
ATOM   2058 C C   . HIS A 1 272 ? 19.261 16.727  85.975  1.00 27.70 ? 272 HIS A C   1 
ATOM   2059 O O   . HIS A 1 272 ? 18.812 15.580  86.077  1.00 31.91 ? 272 HIS A O   1 
ATOM   2060 C CB  . HIS A 1 272 ? 17.902 17.919  87.719  1.00 21.35 ? 272 HIS A CB  1 
ATOM   2061 C CG  . HIS A 1 272 ? 18.967 17.507  88.680  1.00 21.06 ? 272 HIS A CG  1 
ATOM   2062 N ND1 . HIS A 1 272 ? 19.869 18.398  89.226  1.00 22.71 ? 272 HIS A ND1 1 
ATOM   2063 C CD2 . HIS A 1 272 ? 19.347 16.275  89.113  1.00 18.33 ? 272 HIS A CD2 1 
ATOM   2064 C CE1 . HIS A 1 272 ? 20.765 17.740  89.941  1.00 18.85 ? 272 HIS A CE1 1 
ATOM   2065 N NE2 . HIS A 1 272 ? 20.466 16.452  89.886  1.00 17.46 ? 272 HIS A NE2 1 
ATOM   2066 N N   . VAL A 1 273 ? 20.541 16.960  85.747  1.00 29.05 ? 273 VAL A N   1 
ATOM   2067 C CA  . VAL A 1 273 ? 21.451 15.871  85.425  1.00 27.97 ? 273 VAL A CA  1 
ATOM   2068 C C   . VAL A 1 273 ? 22.699 15.775  86.323  1.00 26.64 ? 273 VAL A C   1 
ATOM   2069 O O   . VAL A 1 273 ? 23.129 16.762  86.943  1.00 25.60 ? 273 VAL A O   1 
ATOM   2070 C CB  . VAL A 1 273 ? 21.862 15.980  83.906  1.00 29.83 ? 273 VAL A CB  1 
ATOM   2071 C CG1 . VAL A 1 273 ? 22.323 17.389  83.588  1.00 30.50 ? 273 VAL A CG1 1 
ATOM   2072 C CG2 . VAL A 1 273 ? 22.966 14.994  83.555  1.00 35.94 ? 273 VAL A CG2 1 
ATOM   2073 N N   . GLU A 1 274 ? 23.198 14.557  86.491  1.00 22.10 ? 274 GLU A N   1 
ATOM   2074 C CA  . GLU A 1 274 ? 24.416 14.349  87.261  1.00 25.99 ? 274 GLU A CA  1 
ATOM   2075 C C   . GLU A 1 274 ? 25.277 13.356  86.470  1.00 26.05 ? 274 GLU A C   1 
ATOM   2076 O O   . GLU A 1 274 ? 24.801 12.279  86.081  1.00 29.81 ? 274 GLU A O   1 
ATOM   2077 C CB  . GLU A 1 274 ? 24.130 13.799  88.668  1.00 23.09 ? 274 GLU A CB  1 
ATOM   2078 C CG  . GLU A 1 274 ? 22.719 13.994  89.172  1.00 24.45 ? 274 GLU A CG  1 
ATOM   2079 C CD  . GLU A 1 274 ? 22.637 13.939  90.683  1.00 30.09 ? 274 GLU A CD  1 
ATOM   2080 O OE1 . GLU A 1 274 ? 22.995 12.905  91.287  1.00 32.38 ? 274 GLU A OE1 1 
ATOM   2081 O OE2 . GLU A 1 274 ? 22.257 14.960  91.273  1.00 24.27 ? 274 GLU A OE2 1 
ATOM   2082 N N   . LEU A 1 275 ? 26.515 13.742  86.182  1.00 23.04 ? 275 LEU A N   1 
ATOM   2083 C CA  . LEU A 1 275 ? 27.440 12.890  85.439  1.00 23.54 ? 275 LEU A CA  1 
ATOM   2084 C C   . LEU A 1 275 ? 28.630 12.715  86.348  1.00 22.23 ? 275 LEU A C   1 
ATOM   2085 O O   . LEU A 1 275 ? 29.046 13.678  87.004  1.00 22.37 ? 275 LEU A O   1 
ATOM   2086 C CB  . LEU A 1 275 ? 27.902 13.575  84.130  1.00 23.43 ? 275 LEU A CB  1 
ATOM   2087 C CG  . LEU A 1 275 ? 29.138 12.997  83.410  1.00 22.80 ? 275 LEU A CG  1 
ATOM   2088 C CD1 . LEU A 1 275 ? 28.766 11.729  82.654  1.00 25.24 ? 275 LEU A CD1 1 
ATOM   2089 C CD2 . LEU A 1 275 ? 29.717 13.993  82.433  1.00 20.31 ? 275 LEU A CD2 1 
ATOM   2090 N N   . VAL A 1 276 ? 29.178 11.501  86.391  1.00 24.68 ? 276 VAL A N   1 
ATOM   2091 C CA  . VAL A 1 276 ? 30.338 11.219  87.233  1.00 26.38 ? 276 VAL A CA  1 
ATOM   2092 C C   . VAL A 1 276 ? 31.523 10.967  86.340  1.00 27.20 ? 276 VAL A C   1 
ATOM   2093 O O   . VAL A 1 276 ? 31.400 10.305  85.312  1.00 30.98 ? 276 VAL A O   1 
ATOM   2094 C CB  . VAL A 1 276 ? 30.155 9.982   88.150  1.00 22.82 ? 276 VAL A CB  1 
ATOM   2095 C CG1 . VAL A 1 276 ? 31.279 9.925   89.124  1.00 17.57 ? 276 VAL A CG1 1 
ATOM   2096 C CG2 . VAL A 1 276 ? 28.850 10.061  88.903  1.00 21.32 ? 276 VAL A CG2 1 
ATOM   2097 N N   . GLY A 1 277 ? 32.667 11.513  86.720  1.00 30.67 ? 277 GLY A N   1 
ATOM   2098 C CA  . GLY A 1 277 ? 33.862 11.324  85.928  1.00 33.71 ? 277 GLY A CA  1 
ATOM   2099 C C   . GLY A 1 277 ? 35.063 11.669  86.767  1.00 36.71 ? 277 GLY A C   1 
ATOM   2100 O O   . GLY A 1 277 ? 34.923 11.879  87.976  1.00 36.68 ? 277 GLY A O   1 
ATOM   2101 N N   . PRO A 1 278 ? 36.257 11.746  86.155  1.00 40.66 ? 278 PRO A N   1 
ATOM   2102 C CA  . PRO A 1 278 ? 37.535 12.068  86.800  1.00 42.24 ? 278 PRO A CA  1 
ATOM   2103 C C   . PRO A 1 278 ? 37.593 13.486  87.384  1.00 42.90 ? 278 PRO A C   1 
ATOM   2104 O O   . PRO A 1 278 ? 37.201 14.468  86.727  1.00 42.72 ? 278 PRO A O   1 
ATOM   2105 C CB  . PRO A 1 278 ? 38.535 11.890  85.660  1.00 41.58 ? 278 PRO A CB  1 
ATOM   2106 C CG  . PRO A 1 278 ? 37.732 12.309  84.467  1.00 42.70 ? 278 PRO A CG  1 
ATOM   2107 C CD  . PRO A 1 278 ? 36.441 11.582  84.704  1.00 40.99 ? 278 PRO A CD  1 
ATOM   2108 N N   . LYS A 1 279 ? 38.047 13.572  88.634  1.00 42.15 ? 279 LYS A N   1 
ATOM   2109 C CA  . LYS A 1 279 ? 38.166 14.843  89.323  1.00 42.47 ? 279 LYS A CA  1 
ATOM   2110 C C   . LYS A 1 279 ? 39.304 15.634  88.692  1.00 43.27 ? 279 LYS A C   1 
ATOM   2111 O O   . LYS A 1 279 ? 40.469 15.426  89.018  1.00 45.33 ? 279 LYS A O   1 
ATOM   2112 C CB  . LYS A 1 279 ? 38.431 14.607  90.817  1.00 46.14 ? 279 LYS A CB  1 
ATOM   2113 C CG  . LYS A 1 279 ? 38.968 15.830  91.576  1.00 49.31 ? 279 LYS A CG  1 
ATOM   2114 C CD  . LYS A 1 279 ? 39.385 15.496  93.007  1.00 50.87 ? 279 LYS A CD  1 
ATOM   2115 C CE  . LYS A 1 279 ? 38.246 15.702  93.997  1.00 54.00 ? 279 LYS A CE  1 
ATOM   2116 N NZ  . LYS A 1 279 ? 37.077 14.805  93.781  1.00 53.58 ? 279 LYS A NZ  1 
ATOM   2117 N N   . GLY A 1 280 ? 38.969 16.509  87.754  1.00 45.20 ? 280 GLY A N   1 
ATOM   2118 C CA  . GLY A 1 280 ? 39.984 17.321  87.101  1.00 44.84 ? 280 GLY A CA  1 
ATOM   2119 C C   . GLY A 1 280 ? 40.726 16.595  85.994  1.00 47.27 ? 280 GLY A C   1 
ATOM   2120 O O   . GLY A 1 280 ? 40.213 15.651  85.388  1.00 49.96 ? 280 GLY A O   1 
ATOM   2121 N N   . GLU A 1 283 ? 44.204 11.775  85.720  1.00 29.66 ? 283 GLU A N   1 
ATOM   2122 C CA  . GLU A 1 283 ? 44.445 10.334  85.790  1.00 31.28 ? 283 GLU A CA  1 
ATOM   2123 C C   . GLU A 1 283 ? 44.661 9.800   87.223  1.00 30.73 ? 283 GLU A C   1 
ATOM   2124 O O   . GLU A 1 283 ? 45.799 9.735   87.712  1.00 28.73 ? 283 GLU A O   1 
ATOM   2125 C CB  . GLU A 1 283 ? 45.622 9.966   84.879  1.00 30.23 ? 283 GLU A CB  1 
ATOM   2126 C CG  . GLU A 1 283 ? 45.191 9.558   83.462  1.00 29.86 ? 283 GLU A CG  1 
ATOM   2127 C CD  . GLU A 1 283 ? 46.348 9.398   82.507  1.00 25.88 ? 283 GLU A CD  1 
ATOM   2128 O OE1 . GLU A 1 283 ? 47.507 9.303   82.953  1.00 30.76 ? 283 GLU A OE1 1 
ATOM   2129 O OE2 . GLU A 1 283 ? 46.095 9.372   81.291  1.00 30.18 ? 283 GLU A OE2 1 
ATOM   2130 N N   . THR A 1 284 ? 43.563 9.397   87.867  1.00 28.10 ? 284 THR A N   1 
ATOM   2131 C CA  . THR A 1 284 ? 43.568 8.891   89.244  1.00 34.45 ? 284 THR A CA  1 
ATOM   2132 C C   . THR A 1 284 ? 42.298 8.066   89.519  1.00 35.88 ? 284 THR A C   1 
ATOM   2133 O O   . THR A 1 284 ? 41.607 7.661   88.585  1.00 40.45 ? 284 THR A O   1 
ATOM   2134 C CB  . THR A 1 284 ? 43.628 10.059  90.296  1.00 34.02 ? 284 THR A CB  1 
ATOM   2135 O OG1 . THR A 1 284 ? 42.646 11.071  89.998  1.00 28.56 ? 284 THR A OG1 1 
ATOM   2136 C CG2 . THR A 1 284 ? 45.030 10.668  90.366  1.00 39.58 ? 284 THR A CG2 1 
ATOM   2137 N N   . LEU A 1 285 ? 41.993 7.820   90.793  1.00 32.17 ? 285 LEU A N   1 
ATOM   2138 C CA  . LEU A 1 285 ? 40.802 7.065   91.145  1.00 32.80 ? 285 LEU A CA  1 
ATOM   2139 C C   . LEU A 1 285 ? 39.736 7.970   91.780  1.00 34.17 ? 285 LEU A C   1 
ATOM   2140 O O   . LEU A 1 285 ? 38.641 7.512   92.098  1.00 37.27 ? 285 LEU A O   1 
ATOM   2141 C CB  . LEU A 1 285 ? 41.158 5.898   92.076  1.00 33.38 ? 285 LEU A CB  1 
ATOM   2142 C CG  . LEU A 1 285 ? 42.285 4.938   91.663  1.00 34.74 ? 285 LEU A CG  1 
ATOM   2143 C CD1 . LEU A 1 285 ? 42.458 3.820   92.690  1.00 31.52 ? 285 LEU A CD1 1 
ATOM   2144 C CD2 . LEU A 1 285 ? 42.007 4.345   90.305  1.00 37.03 ? 285 LEU A CD2 1 
ATOM   2145 N N   . GLU A 1 286 ? 40.056 9.253   91.947  1.00 37.67 ? 286 GLU A N   1 
ATOM   2146 C CA  . GLU A 1 286 ? 39.135 10.239  92.533  1.00 40.32 ? 286 GLU A CA  1 
ATOM   2147 C C   . GLU A 1 286 ? 38.081 10.722  91.540  1.00 39.57 ? 286 GLU A C   1 
ATOM   2148 O O   . GLU A 1 286 ? 38.422 11.193  90.456  1.00 40.01 ? 286 GLU A O   1 
ATOM   2149 C CB  . GLU A 1 286 ? 39.907 11.467  93.025  1.00 45.18 ? 286 GLU A CB  1 
ATOM   2150 C CG  . GLU A 1 286 ? 40.500 11.355  94.419  1.00 58.51 ? 286 GLU A CG  1 
ATOM   2151 C CD  . GLU A 1 286 ? 40.455 12.688  95.169  1.00 67.16 ? 286 GLU A CD  1 
ATOM   2152 O OE1 . GLU A 1 286 ? 39.386 13.019  95.740  1.00 68.40 ? 286 GLU A OE1 1 
ATOM   2153 O OE2 . GLU A 1 286 ? 41.479 13.410  95.176  1.00 72.40 ? 286 GLU A OE2 1 
ATOM   2154 N N   . TYR A 1 287 ? 36.809 10.671  91.928  1.00 40.98 ? 287 TYR A N   1 
ATOM   2155 C CA  . TYR A 1 287 ? 35.730 11.119  91.036  1.00 37.66 ? 287 TYR A CA  1 
ATOM   2156 C C   . TYR A 1 287 ? 35.257 12.515  91.382  1.00 36.65 ? 287 TYR A C   1 
ATOM   2157 O O   . TYR A 1 287 ? 35.818 13.166  92.261  1.00 33.01 ? 287 TYR A O   1 
ATOM   2158 C CB  . TYR A 1 287 ? 34.560 10.121  91.016  1.00 32.43 ? 287 TYR A CB  1 
ATOM   2159 C CG  . TYR A 1 287 ? 35.015 8.754   90.597  1.00 34.19 ? 287 TYR A CG  1 
ATOM   2160 C CD1 . TYR A 1 287 ? 35.963 8.616   89.596  1.00 34.29 ? 287 TYR A CD1 1 
ATOM   2161 C CD2 . TYR A 1 287 ? 34.625 7.618   91.289  1.00 35.16 ? 287 TYR A CD2 1 
ATOM   2162 C CE1 . TYR A 1 287 ? 36.539 7.401   89.304  1.00 40.52 ? 287 TYR A CE1 1 
ATOM   2163 C CE2 . TYR A 1 287 ? 35.194 6.380   90.997  1.00 44.41 ? 287 TYR A CE2 1 
ATOM   2164 C CZ  . TYR A 1 287 ? 36.168 6.280   90.004  1.00 41.93 ? 287 TYR A CZ  1 
ATOM   2165 O OH  . TYR A 1 287 ? 36.849 5.091   89.756  1.00 42.33 ? 287 TYR A OH  1 
ATOM   2166 N N   . GLU A 1 288 ? 34.250 12.974  90.654  1.00 36.43 ? 288 GLU A N   1 
ATOM   2167 C CA  . GLU A 1 288 ? 33.686 14.297  90.832  1.00 40.10 ? 288 GLU A CA  1 
ATOM   2168 C C   . GLU A 1 288 ? 32.299 14.196  90.241  1.00 40.58 ? 288 GLU A C   1 
ATOM   2169 O O   . GLU A 1 288 ? 32.077 13.378  89.342  1.00 43.65 ? 288 GLU A O   1 
ATOM   2170 C CB  . GLU A 1 288 ? 34.485 15.301  89.998  1.00 44.38 ? 288 GLU A CB  1 
ATOM   2171 C CG  . GLU A 1 288 ? 34.292 16.752  90.361  1.00 55.06 ? 288 GLU A CG  1 
ATOM   2172 C CD  . GLU A 1 288 ? 35.195 17.172  91.504  1.00 64.70 ? 288 GLU A CD  1 
ATOM   2173 O OE1 . GLU A 1 288 ? 34.786 17.043  92.685  1.00 69.25 ? 288 GLU A OE1 1 
ATOM   2174 O OE2 . GLU A 1 288 ? 36.330 17.616  91.215  1.00 70.91 ? 288 GLU A OE2 1 
ATOM   2175 N N   . SER A 1 289 ? 31.366 14.995  90.749  1.00 40.45 ? 289 SER A N   1 
ATOM   2176 C CA  . SER A 1 289 ? 30.001 15.008  90.230  1.00 37.35 ? 289 SER A CA  1 
ATOM   2177 C C   . SER A 1 289 ? 29.842 16.271  89.396  1.00 35.53 ? 289 SER A C   1 
ATOM   2178 O O   . SER A 1 289 ? 30.267 17.343  89.820  1.00 37.03 ? 289 SER A O   1 
ATOM   2179 C CB  . SER A 1 289 ? 28.991 15.023  91.372  1.00 38.04 ? 289 SER A CB  1 
ATOM   2180 O OG  . SER A 1 289 ? 27.656 14.909  90.896  1.00 38.08 ? 289 SER A OG  1 
ATOM   2181 N N   . TYR A 1 290 ? 29.314 16.124  88.184  1.00 32.50 ? 290 TYR A N   1 
ATOM   2182 C CA  . TYR A 1 290 ? 29.087 17.249  87.283  1.00 27.83 ? 290 TYR A CA  1 
ATOM   2183 C C   . TYR A 1 290 ? 27.583 17.336  87.118  1.00 30.06 ? 290 TYR A C   1 
ATOM   2184 O O   . TYR A 1 290 ? 26.999 16.602  86.326  1.00 32.90 ? 290 TYR A O   1 
ATOM   2185 C CB  . TYR A 1 290 ? 29.749 16.998  85.923  1.00 21.82 ? 290 TYR A CB  1 
ATOM   2186 C CG  . TYR A 1 290 ? 31.258 17.016  85.964  1.00 18.78 ? 290 TYR A CG  1 
ATOM   2187 C CD1 . TYR A 1 290 ? 31.963 18.226  85.900  1.00 13.61 ? 290 TYR A CD1 1 
ATOM   2188 C CD2 . TYR A 1 290 ? 31.982 15.835  86.091  1.00 9.63  ? 290 TYR A CD2 1 
ATOM   2189 C CE1 . TYR A 1 290 ? 33.351 18.258  85.966  1.00 13.29 ? 290 TYR A CE1 1 
ATOM   2190 C CE2 . TYR A 1 290 ? 33.385 15.851  86.153  1.00 14.87 ? 290 TYR A CE2 1 
ATOM   2191 C CZ  . TYR A 1 290 ? 34.062 17.067  86.097  1.00 16.17 ? 290 TYR A CZ  1 
ATOM   2192 O OH  . TYR A 1 290 ? 35.442 17.097  86.228  1.00 21.11 ? 290 TYR A OH  1 
ATOM   2193 N N   . ARG A 1 291 ? 26.939 18.174  87.913  1.00 29.07 ? 291 ARG A N   1 
ATOM   2194 C CA  . ARG A 1 291 ? 25.490 18.280  87.832  1.00 31.88 ? 291 ARG A CA  1 
ATOM   2195 C C   . ARG A 1 291 ? 25.126 19.500  86.987  1.00 29.77 ? 291 ARG A C   1 
ATOM   2196 O O   . ARG A 1 291 ? 26.003 20.304  86.664  1.00 31.58 ? 291 ARG A O   1 
ATOM   2197 C CB  . ARG A 1 291 ? 24.879 18.386  89.236  1.00 37.72 ? 291 ARG A CB  1 
ATOM   2198 C CG  . ARG A 1 291 ? 25.488 17.477  90.323  1.00 47.28 ? 291 ARG A CG  1 
ATOM   2199 C CD  . ARG A 1 291 ? 24.674 17.606  91.634  1.00 54.80 ? 291 ARG A CD  1 
ATOM   2200 N NE  . ARG A 1 291 ? 25.206 16.878  92.794  1.00 59.07 ? 291 ARG A NE  1 
ATOM   2201 C CZ  . ARG A 1 291 ? 25.343 15.555  92.885  1.00 59.75 ? 291 ARG A CZ  1 
ATOM   2202 N NH1 . ARG A 1 291 ? 25.058 14.765  91.859  1.00 60.39 ? 291 ARG A NH1 1 
ATOM   2203 N NH2 . ARG A 1 291 ? 25.822 15.020  93.997  1.00 57.85 ? 291 ARG A NH2 1 
ATOM   2204 N N   . ALA A 1 292 ? 23.857 19.623  86.597  1.00 24.52 ? 292 ALA A N   1 
ATOM   2205 C CA  . ALA A 1 292 ? 23.426 20.757  85.789  1.00 23.61 ? 292 ALA A CA  1 
ATOM   2206 C C   . ALA A 1 292 ? 21.922 20.812  85.652  1.00 24.85 ? 292 ALA A C   1 
ATOM   2207 O O   . ALA A 1 292 ? 21.262 19.776  85.692  1.00 25.19 ? 292 ALA A O   1 
ATOM   2208 C CB  . ALA A 1 292 ? 24.055 20.685  84.428  1.00 25.46 ? 292 ALA A CB  1 
ATOM   2209 N N   . GLU A 1 293 ? 21.379 22.029  85.567  1.00 26.23 ? 293 GLU A N   1 
ATOM   2210 C CA  . GLU A 1 293 ? 19.942 22.231  85.399  1.00 27.53 ? 293 GLU A CA  1 
ATOM   2211 C C   . GLU A 1 293 ? 19.677 22.609  83.931  1.00 33.75 ? 293 GLU A C   1 
ATOM   2212 O O   . GLU A 1 293 ? 19.959 23.738  83.507  1.00 35.89 ? 293 GLU A O   1 
ATOM   2213 C CB  . GLU A 1 293 ? 19.430 23.314  86.347  1.00 28.97 ? 293 GLU A CB  1 
ATOM   2214 C CG  . GLU A 1 293 ? 19.771 23.071  87.836  1.00 30.42 ? 293 GLU A CG  1 
ATOM   2215 C CD  . GLU A 1 293 ? 19.613 21.607  88.310  1.00 31.48 ? 293 GLU A CD  1 
ATOM   2216 O OE1 . GLU A 1 293 ? 18.528 21.004  88.124  1.00 21.24 ? 293 GLU A OE1 1 
ATOM   2217 O OE2 . GLU A 1 293 ? 20.585 21.074  88.898  1.00 32.73 ? 293 GLU A OE2 1 
ATOM   2218 N N   . LEU A 1 294 ? 19.161 21.644  83.165  1.00 27.68 ? 294 LEU A N   1 
ATOM   2219 C CA  . LEU A 1 294 ? 18.895 21.796  81.744  1.00 24.99 ? 294 LEU A CA  1 
ATOM   2220 C C   . LEU A 1 294 ? 17.549 22.370  81.339  1.00 25.75 ? 294 LEU A C   1 
ATOM   2221 O O   . LEU A 1 294 ? 16.534 22.114  81.972  1.00 27.98 ? 294 LEU A O   1 
ATOM   2222 C CB  . LEU A 1 294 ? 19.056 20.436  81.064  1.00 29.44 ? 294 LEU A CB  1 
ATOM   2223 C CG  . LEU A 1 294 ? 20.403 19.879  80.582  1.00 27.46 ? 294 LEU A CG  1 
ATOM   2224 C CD1 . LEU A 1 294 ? 21.487 19.968  81.615  1.00 25.77 ? 294 LEU A CD1 1 
ATOM   2225 C CD2 . LEU A 1 294 ? 20.172 18.437  80.176  1.00 28.13 ? 294 LEU A CD2 1 
ATOM   2226 N N   . SER A 1 295 ? 17.540 23.058  80.203  1.00 24.42 ? 295 SER A N   1 
ATOM   2227 C CA  . SER A 1 295 ? 16.325 23.646  79.633  1.00 25.46 ? 295 SER A CA  1 
ATOM   2228 C C   . SER A 1 295 ? 16.454 23.648  78.084  1.00 24.36 ? 295 SER A C   1 
ATOM   2229 O O   . SER A 1 295 ? 17.486 23.241  77.540  1.00 22.22 ? 295 SER A O   1 
ATOM   2230 C CB  . SER A 1 295 ? 16.087 25.059  80.182  1.00 25.12 ? 295 SER A CB  1 
ATOM   2231 O OG  . SER A 1 295 ? 17.097 25.975  79.779  1.00 33.73 ? 295 SER A OG  1 
ATOM   2232 N N   . LYS A 1 296 ? 15.423 24.101  77.384  1.00 21.46 ? 296 LYS A N   1 
ATOM   2233 C CA  . LYS A 1 296 ? 15.432 24.110  75.913  1.00 25.80 ? 296 LYS A CA  1 
ATOM   2234 C C   . LYS A 1 296 ? 16.723 24.596  75.222  1.00 22.35 ? 296 LYS A C   1 
ATOM   2235 O O   . LYS A 1 296 ? 17.304 25.622  75.593  1.00 25.47 ? 296 LYS A O   1 
ATOM   2236 C CB  . LYS A 1 296 ? 14.225 24.893  75.385  1.00 22.91 ? 296 LYS A CB  1 
ATOM   2237 C CG  . LYS A 1 296 ? 14.078 24.902  73.875  1.00 27.75 ? 296 LYS A CG  1 
ATOM   2238 C CD  . LYS A 1 296 ? 13.621 26.278  73.412  1.00 29.71 ? 296 LYS A CD  1 
ATOM   2239 C CE  . LYS A 1 296 ? 12.149 26.326  73.137  1.00 30.83 ? 296 LYS A CE  1 
ATOM   2240 N NZ  . LYS A 1 296 ? 11.869 26.082  71.686  1.00 37.20 ? 296 LYS A NZ  1 
ATOM   2241 N N   . ASP A 1 297 ? 17.116 23.855  74.186  1.00 21.69 ? 297 ASP A N   1 
ATOM   2242 C CA  . ASP A 1 297 ? 18.298 24.111  73.381  1.00 16.94 ? 297 ASP A CA  1 
ATOM   2243 C C   . ASP A 1 297 ? 19.627 23.998  74.082  1.00 21.94 ? 297 ASP A C   1 
ATOM   2244 O O   . ASP A 1 297 ? 20.670 24.241  73.468  1.00 22.53 ? 297 ASP A O   1 
ATOM   2245 C CB  . ASP A 1 297 ? 18.201 25.444  72.651  1.00 21.96 ? 297 ASP A CB  1 
ATOM   2246 C CG  . ASP A 1 297 ? 17.208 25.411  71.503  1.00 26.82 ? 297 ASP A CG  1 
ATOM   2247 O OD1 . ASP A 1 297 ? 16.965 24.324  70.944  1.00 31.62 ? 297 ASP A OD1 1 
ATOM   2248 O OD2 . ASP A 1 297 ? 16.663 26.478  71.154  1.00 32.68 ? 297 ASP A OD2 1 
ATOM   2249 N N   . ASP A 1 298 ? 19.616 23.643  75.368  1.00 22.42 ? 298 ASP A N   1 
ATOM   2250 C CA  . ASP A 1 298 ? 20.872 23.460  76.103  1.00 18.37 ? 298 ASP A CA  1 
ATOM   2251 C C   . ASP A 1 298 ? 21.429 22.161  75.564  1.00 16.17 ? 298 ASP A C   1 
ATOM   2252 O O   . ASP A 1 298 ? 20.649 21.282  75.173  1.00 18.20 ? 298 ASP A O   1 
ATOM   2253 C CB  . ASP A 1 298 ? 20.610 23.306  77.610  1.00 19.98 ? 298 ASP A CB  1 
ATOM   2254 C CG  . ASP A 1 298 ? 20.403 24.633  78.323  1.00 20.56 ? 298 ASP A CG  1 
ATOM   2255 O OD1 . ASP A 1 298 ? 20.682 25.674  77.727  1.00 18.83 ? 298 ASP A OD1 1 
ATOM   2256 O OD2 . ASP A 1 298 ? 19.985 24.649  79.501  1.00 28.55 ? 298 ASP A OD2 1 
ATOM   2257 N N   . VAL A 1 299 ? 22.751 22.038  75.519  1.00 15.65 ? 299 VAL A N   1 
ATOM   2258 C CA  . VAL A 1 299 ? 23.409 20.819  75.041  1.00 17.07 ? 299 VAL A CA  1 
ATOM   2259 C C   . VAL A 1 299 ? 24.257 20.290  76.184  1.00 25.03 ? 299 VAL A C   1 
ATOM   2260 O O   . VAL A 1 299 ? 24.767 21.083  76.995  1.00 26.04 ? 299 VAL A O   1 
ATOM   2261 C CB  . VAL A 1 299 ? 24.318 21.094  73.819  1.00 19.73 ? 299 VAL A CB  1 
ATOM   2262 C CG1 . VAL A 1 299 ? 25.176 19.873  73.505  1.00 20.89 ? 299 VAL A CG1 1 
ATOM   2263 C CG2 . VAL A 1 299 ? 23.473 21.463  72.609  1.00 7.92  ? 299 VAL A CG2 1 
ATOM   2264 N N   . PHE A 1 300 ? 24.369 18.959  76.270  1.00 28.27 ? 300 PHE A N   1 
ATOM   2265 C CA  . PHE A 1 300 ? 25.148 18.272  77.317  1.00 28.09 ? 300 PHE A CA  1 
ATOM   2266 C C   . PHE A 1 300 ? 25.842 17.032  76.738  1.00 28.39 ? 300 PHE A C   1 
ATOM   2267 O O   . PHE A 1 300 ? 25.198 16.177  76.132  1.00 28.10 ? 300 PHE A O   1 
ATOM   2268 C CB  . PHE A 1 300 ? 24.244 17.845  78.490  1.00 29.15 ? 300 PHE A CB  1 
ATOM   2269 C CG  . PHE A 1 300 ? 24.999 17.541  79.763  1.00 22.74 ? 300 PHE A CG  1 
ATOM   2270 C CD1 . PHE A 1 300 ? 25.542 18.571  80.529  1.00 28.77 ? 300 PHE A CD1 1 
ATOM   2271 C CD2 . PHE A 1 300 ? 25.185 16.239  80.185  1.00 18.88 ? 300 PHE A CD2 1 
ATOM   2272 C CE1 . PHE A 1 300 ? 26.267 18.304  81.698  1.00 27.60 ? 300 PHE A CE1 1 
ATOM   2273 C CE2 . PHE A 1 300 ? 25.910 15.961  81.355  1.00 24.81 ? 300 PHE A CE2 1 
ATOM   2274 C CZ  . PHE A 1 300 ? 26.452 16.998  82.109  1.00 24.02 ? 300 PHE A CZ  1 
ATOM   2275 N N   . VAL A 1 301 ? 27.149 16.946  76.964  1.00 25.39 ? 301 VAL A N   1 
ATOM   2276 C CA  . VAL A 1 301 ? 27.993 15.859  76.494  1.00 23.29 ? 301 VAL A CA  1 
ATOM   2277 C C   . VAL A 1 301 ? 28.191 14.776  77.548  1.00 25.00 ? 301 VAL A C   1 
ATOM   2278 O O   . VAL A 1 301 ? 28.735 15.021  78.616  1.00 26.33 ? 301 VAL A O   1 
ATOM   2279 C CB  . VAL A 1 301 ? 29.383 16.394  76.107  1.00 20.74 ? 301 VAL A CB  1 
ATOM   2280 C CG1 . VAL A 1 301 ? 30.278 15.273  75.632  1.00 17.17 ? 301 VAL A CG1 1 
ATOM   2281 C CG2 . VAL A 1 301 ? 29.248 17.451  75.034  1.00 27.05 ? 301 VAL A CG2 1 
ATOM   2282 N N   . ILE A 1 302 ? 27.798 13.561  77.213  1.00 23.70 ? 302 ILE A N   1 
ATOM   2283 C CA  . ILE A 1 302 ? 27.955 12.428  78.102  1.00 20.63 ? 302 ILE A CA  1 
ATOM   2284 C C   . ILE A 1 302 ? 29.073 11.569  77.501  1.00 21.03 ? 302 ILE A C   1 
ATOM   2285 O O   . ILE A 1 302 ? 28.900 10.932  76.464  1.00 17.28 ? 302 ILE A O   1 
ATOM   2286 C CB  . ILE A 1 302 ? 26.616 11.635  78.208  1.00 22.74 ? 302 ILE A CB  1 
ATOM   2287 C CG1 . ILE A 1 302 ? 25.480 12.605  78.566  1.00 14.26 ? 302 ILE A CG1 1 
ATOM   2288 C CG2 . ILE A 1 302 ? 26.733 10.500  79.247  1.00 15.69 ? 302 ILE A CG2 1 
ATOM   2289 C CD1 . ILE A 1 302 ? 24.077 12.127  78.179  1.00 4.35  ? 302 ILE A CD1 1 
ATOM   2290 N N   . PRO A 1 303 ? 30.277 11.652  78.074  1.00 21.52 ? 303 PRO A N   1 
ATOM   2291 C CA  . PRO A 1 303 ? 31.441 10.888  77.609  1.00 22.57 ? 303 PRO A CA  1 
ATOM   2292 C C   . PRO A 1 303 ? 31.219 9.369   77.750  1.00 25.07 ? 303 PRO A C   1 
ATOM   2293 O O   . PRO A 1 303 ? 30.545 8.915   78.685  1.00 25.94 ? 303 PRO A O   1 
ATOM   2294 C CB  . PRO A 1 303 ? 32.546 11.379  78.545  1.00 22.74 ? 303 PRO A CB  1 
ATOM   2295 C CG  . PRO A 1 303 ? 32.117 12.795  78.869  1.00 17.78 ? 303 PRO A CG  1 
ATOM   2296 C CD  . PRO A 1 303 ? 30.660 12.595  79.138  1.00 18.06 ? 303 PRO A CD  1 
ATOM   2297 N N   . ALA A 1 304 ? 31.812 8.583   76.856  1.00 21.50 ? 304 ALA A N   1 
ATOM   2298 C CA  . ALA A 1 304 ? 31.656 7.128   76.900  1.00 18.00 ? 304 ALA A CA  1 
ATOM   2299 C C   . ALA A 1 304 ? 32.203 6.532   78.190  1.00 12.51 ? 304 ALA A C   1 
ATOM   2300 O O   . ALA A 1 304 ? 33.352 6.785   78.550  1.00 9.86  ? 304 ALA A O   1 
ATOM   2301 C CB  . ALA A 1 304 ? 32.347 6.499   75.729  1.00 11.85 ? 304 ALA A CB  1 
ATOM   2302 N N   . ALA A 1 305 ? 31.377 5.718   78.851  1.00 19.94 ? 305 ALA A N   1 
ATOM   2303 C CA  . ALA A 1 305 ? 31.703 5.010   80.112  1.00 19.56 ? 305 ALA A CA  1 
ATOM   2304 C C   . ALA A 1 305 ? 31.511 5.802   81.402  1.00 21.63 ? 305 ALA A C   1 
ATOM   2305 O O   . ALA A 1 305 ? 31.714 5.282   82.496  1.00 23.82 ? 305 ALA A O   1 
ATOM   2306 C CB  . ALA A 1 305 ? 33.115 4.406   80.067  1.00 20.02 ? 305 ALA A CB  1 
ATOM   2307 N N   . TYR A 1 306 ? 31.110 7.055   81.275  1.00 22.93 ? 306 TYR A N   1 
ATOM   2308 C CA  . TYR A 1 306 ? 30.879 7.894   82.433  1.00 19.89 ? 306 TYR A CA  1 
ATOM   2309 C C   . TYR A 1 306 ? 29.437 7.697   82.903  1.00 20.92 ? 306 TYR A C   1 
ATOM   2310 O O   . TYR A 1 306 ? 28.498 7.754   82.106  1.00 21.47 ? 306 TYR A O   1 
ATOM   2311 C CB  . TYR A 1 306 ? 31.116 9.376   82.081  1.00 16.59 ? 306 TYR A CB  1 
ATOM   2312 C CG  . TYR A 1 306 ? 32.557 9.792   81.840  1.00 16.51 ? 306 TYR A CG  1 
ATOM   2313 C CD1 . TYR A 1 306 ? 33.507 8.900   81.333  1.00 17.65 ? 306 TYR A CD1 1 
ATOM   2314 C CD2 . TYR A 1 306 ? 32.961 11.093  82.095  1.00 15.84 ? 306 TYR A CD2 1 
ATOM   2315 C CE1 . TYR A 1 306 ? 34.825 9.301   81.093  1.00 16.28 ? 306 TYR A CE1 1 
ATOM   2316 C CE2 . TYR A 1 306 ? 34.287 11.505  81.858  1.00 12.14 ? 306 TYR A CE2 1 
ATOM   2317 C CZ  . TYR A 1 306 ? 35.201 10.614  81.360  1.00 15.27 ? 306 TYR A CZ  1 
ATOM   2318 O OH  . TYR A 1 306 ? 36.491 11.041  81.125  1.00 18.07 ? 306 TYR A OH  1 
ATOM   2319 N N   . PRO A 1 307 ? 29.246 7.367   84.187  1.00 18.87 ? 307 PRO A N   1 
ATOM   2320 C CA  . PRO A 1 307 ? 27.907 7.162   84.754  1.00 16.29 ? 307 PRO A CA  1 
ATOM   2321 C C   . PRO A 1 307 ? 27.077 8.467   84.749  1.00 17.09 ? 307 PRO A C   1 
ATOM   2322 O O   . PRO A 1 307 ? 27.581 9.552   85.061  1.00 14.45 ? 307 PRO A O   1 
ATOM   2323 C CB  . PRO A 1 307 ? 28.217 6.668   86.169  1.00 9.77  ? 307 PRO A CB  1 
ATOM   2324 C CG  . PRO A 1 307 ? 29.466 5.929   85.982  1.00 15.12 ? 307 PRO A CG  1 
ATOM   2325 C CD  . PRO A 1 307 ? 30.276 6.822   85.080  1.00 14.78 ? 307 PRO A CD  1 
ATOM   2326 N N   . VAL A 1 308 ? 25.785 8.343   84.480  1.00 16.14 ? 308 VAL A N   1 
ATOM   2327 C CA  . VAL A 1 308 ? 24.929 9.505   84.396  1.00 18.57 ? 308 VAL A CA  1 
ATOM   2328 C C   . VAL A 1 308 ? 23.482 9.161   84.796  1.00 18.05 ? 308 VAL A C   1 
ATOM   2329 O O   . VAL A 1 308 ? 23.024 8.015   84.630  1.00 18.19 ? 308 VAL A O   1 
ATOM   2330 C CB  . VAL A 1 308 ? 24.996 10.059  82.940  1.00 17.37 ? 308 VAL A CB  1 
ATOM   2331 C CG1 . VAL A 1 308 ? 24.442 9.020   81.965  1.00 9.30  ? 308 VAL A CG1 1 
ATOM   2332 C CG2 . VAL A 1 308 ? 24.287 11.422  82.809  1.00 11.85 ? 308 VAL A CG2 1 
ATOM   2333 N N   . ALA A 1 309 ? 22.779 10.153  85.341  1.00 18.95 ? 309 ALA A N   1 
ATOM   2334 C CA  . ALA A 1 309 ? 21.394 10.006  85.783  1.00 15.46 ? 309 ALA A CA  1 
ATOM   2335 C C   . ALA A 1 309 ? 20.626 11.259  85.391  1.00 15.25 ? 309 ALA A C   1 
ATOM   2336 O O   . ALA A 1 309 ? 21.134 12.359  85.566  1.00 21.03 ? 309 ALA A O   1 
ATOM   2337 C CB  . ALA A 1 309 ? 21.364 9.824   87.293  1.00 23.02 ? 309 ALA A CB  1 
ATOM   2338 N N   . ILE A 1 310 ? 19.381 11.107  84.954  1.00 13.32 ? 310 ILE A N   1 
ATOM   2339 C CA  . ILE A 1 310 ? 18.569 12.253  84.522  1.00 20.78 ? 310 ILE A CA  1 
ATOM   2340 C C   . ILE A 1 310 ? 17.234 12.320  85.266  1.00 25.95 ? 310 ILE A C   1 
ATOM   2341 O O   . ILE A 1 310 ? 16.430 11.379  85.222  1.00 28.74 ? 310 ILE A O   1 
ATOM   2342 C CB  . ILE A 1 310 ? 18.259 12.155  82.991  1.00 27.17 ? 310 ILE A CB  1 
ATOM   2343 C CG1 . ILE A 1 310 ? 19.559 12.043  82.192  1.00 26.49 ? 310 ILE A CG1 1 
ATOM   2344 C CG2 . ILE A 1 310 ? 17.424 13.341  82.514  1.00 27.32 ? 310 ILE A CG2 1 
ATOM   2345 C CD1 . ILE A 1 310 ? 19.369 11.360  80.854  1.00 33.89 ? 310 ILE A CD1 1 
ATOM   2346 N N   . LYS A 1 311 ? 16.962 13.456  85.890  1.00 27.00 ? 311 LYS A N   1 
ATOM   2347 C CA  . LYS A 1 311 ? 15.727 13.624  86.625  1.00 26.09 ? 311 LYS A CA  1 
ATOM   2348 C C   . LYS A 1 311 ? 14.915 14.696  85.925  1.00 28.03 ? 311 LYS A C   1 
ATOM   2349 O O   . LYS A 1 311 ? 15.379 15.822  85.739  1.00 27.32 ? 311 LYS A O   1 
ATOM   2350 C CB  . LYS A 1 311 ? 16.051 14.038  88.057  1.00 31.31 ? 311 LYS A CB  1 
ATOM   2351 C CG  . LYS A 1 311 ? 14.964 13.747  89.084  1.00 39.95 ? 311 LYS A CG  1 
ATOM   2352 C CD  . LYS A 1 311 ? 13.844 14.742  89.041  1.00 48.20 ? 311 LYS A CD  1 
ATOM   2353 C CE  . LYS A 1 311 ? 12.916 14.542  90.214  1.00 54.47 ? 311 LYS A CE  1 
ATOM   2354 N NZ  . LYS A 1 311 ? 11.879 15.611  90.232  1.00 64.32 ? 311 LYS A NZ  1 
ATOM   2355 N N   . ALA A 1 312 ? 13.687 14.367  85.566  1.00 27.11 ? 312 ALA A N   1 
ATOM   2356 C CA  . ALA A 1 312 ? 12.846 15.313  84.867  1.00 27.61 ? 312 ALA A CA  1 
ATOM   2357 C C   . ALA A 1 312 ? 12.161 16.333  85.770  1.00 29.73 ? 312 ALA A C   1 
ATOM   2358 O O   . ALA A 1 312 ? 11.334 15.983  86.610  1.00 34.49 ? 312 ALA A O   1 
ATOM   2359 C CB  . ALA A 1 312 ? 11.820 14.565  84.025  1.00 27.91 ? 312 ALA A CB  1 
ATOM   2360 N N   . THR A 1 313 ? 12.527 17.597  85.606  1.00 30.14 ? 313 THR A N   1 
ATOM   2361 C CA  . THR A 1 313 ? 11.922 18.679  86.371  1.00 29.88 ? 313 THR A CA  1 
ATOM   2362 C C   . THR A 1 313 ? 10.498 19.007  85.864  1.00 33.21 ? 313 THR A C   1 
ATOM   2363 O O   . THR A 1 313 ? 9.644  19.478  86.621  1.00 34.99 ? 313 THR A O   1 
ATOM   2364 C CB  . THR A 1 313 ? 12.835 19.894  86.342  1.00 31.09 ? 313 THR A CB  1 
ATOM   2365 O OG1 . THR A 1 313 ? 13.813 19.744  87.374  1.00 34.56 ? 313 THR A OG1 1 
ATOM   2366 C CG2 . THR A 1 313 ? 12.069 21.197  86.523  1.00 32.90 ? 313 THR A CG2 1 
ATOM   2367 N N   . SER A 1 314 ? 10.240 18.784  84.583  1.00 31.18 ? 314 SER A N   1 
ATOM   2368 C CA  . SER A 1 314 ? 8.911  19.013  84.043  1.00 31.78 ? 314 SER A CA  1 
ATOM   2369 C C   . SER A 1 314 ? 8.771  17.971  82.951  1.00 32.59 ? 314 SER A C   1 
ATOM   2370 O O   . SER A 1 314 ? 9.582  17.045  82.881  1.00 32.22 ? 314 SER A O   1 
ATOM   2371 C CB  . SER A 1 314 ? 8.791  20.430  83.477  1.00 33.15 ? 314 SER A CB  1 
ATOM   2372 O OG  . SER A 1 314 ? 9.492  20.582  82.253  1.00 38.57 ? 314 SER A OG  1 
ATOM   2373 N N   . ASN A 1 315 ? 7.721  18.058  82.144  1.00 32.12 ? 315 ASN A N   1 
ATOM   2374 C CA  . ASN A 1 315 ? 7.588  17.116  81.043  1.00 33.30 ? 315 ASN A CA  1 
ATOM   2375 C C   . ASN A 1 315 ? 8.669  17.588  80.071  1.00 35.76 ? 315 ASN A C   1 
ATOM   2376 O O   . ASN A 1 315 ? 8.760  18.796  79.760  1.00 35.48 ? 315 ASN A O   1 
ATOM   2377 C CB  . ASN A 1 315 ? 6.194  17.192  80.448  1.00 32.45 ? 315 ASN A CB  1 
ATOM   2378 C CG  . ASN A 1 315 ? 5.128  16.912  81.479  1.00 34.83 ? 315 ASN A CG  1 
ATOM   2379 O OD1 . ASN A 1 315 ? 5.022  15.799  81.990  1.00 33.94 ? 315 ASN A OD1 1 
ATOM   2380 N ND2 . ASN A 1 315 ? 4.364  17.934  81.830  1.00 34.26 ? 315 ASN A ND2 1 
ATOM   2381 N N   . VAL A 1 316 ? 9.525  16.661  79.646  1.00 34.94 ? 316 VAL A N   1 
ATOM   2382 C CA  . VAL A 1 316 ? 10.654 17.014  78.795  1.00 31.29 ? 316 VAL A CA  1 
ATOM   2383 C C   . VAL A 1 316 ? 10.931 16.018  77.669  1.00 31.28 ? 316 VAL A C   1 
ATOM   2384 O O   . VAL A 1 316 ? 10.698 14.815  77.809  1.00 27.43 ? 316 VAL A O   1 
ATOM   2385 C CB  . VAL A 1 316 ? 11.909 17.195  79.685  1.00 27.28 ? 316 VAL A CB  1 
ATOM   2386 C CG1 . VAL A 1 316 ? 12.252 15.886  80.368  1.00 20.34 ? 316 VAL A CG1 1 
ATOM   2387 C CG2 . VAL A 1 316 ? 13.065 17.759  78.901  1.00 26.13 ? 316 VAL A CG2 1 
ATOM   2388 N N   . ASN A 1 317 ? 11.395 16.553  76.541  1.00 34.02 ? 317 ASN A N   1 
ATOM   2389 C CA  . ASN A 1 317 ? 11.702 15.762  75.357  1.00 33.49 ? 317 ASN A CA  1 
ATOM   2390 C C   . ASN A 1 317 ? 13.114 16.101  74.870  1.00 30.88 ? 317 ASN A C   1 
ATOM   2391 O O   . ASN A 1 317 ? 13.466 17.282  74.735  1.00 27.79 ? 317 ASN A O   1 
ATOM   2392 C CB  . ASN A 1 317 ? 10.671 16.039  74.265  1.00 41.16 ? 317 ASN A CB  1 
ATOM   2393 C CG  . ASN A 1 317 ? 10.929 15.229  73.003  1.00 59.69 ? 317 ASN A CG  1 
ATOM   2394 O OD1 . ASN A 1 317 ? 11.260 15.782  71.947  1.00 65.04 ? 317 ASN A OD1 1 
ATOM   2395 N ND2 . ASN A 1 317 ? 10.788 13.910  73.107  1.00 66.52 ? 317 ASN A ND2 1 
ATOM   2396 N N   . PHE A 1 318 ? 13.931 15.070  74.660  1.00 28.62 ? 318 PHE A N   1 
ATOM   2397 C CA  . PHE A 1 318 ? 15.309 15.243  74.217  1.00 26.70 ? 318 PHE A CA  1 
ATOM   2398 C C   . PHE A 1 318 ? 15.533 14.577  72.879  1.00 28.36 ? 318 PHE A C   1 
ATOM   2399 O O   . PHE A 1 318 ? 14.805 13.669  72.495  1.00 31.47 ? 318 PHE A O   1 
ATOM   2400 C CB  . PHE A 1 318 ? 16.292 14.520  75.139  1.00 25.94 ? 318 PHE A CB  1 
ATOM   2401 C CG  . PHE A 1 318 ? 16.184 14.858  76.584  1.00 26.37 ? 318 PHE A CG  1 
ATOM   2402 C CD1 . PHE A 1 318 ? 15.252 14.209  77.395  1.00 30.78 ? 318 PHE A CD1 1 
ATOM   2403 C CD2 . PHE A 1 318 ? 17.106 15.718  77.171  1.00 25.86 ? 318 PHE A CD2 1 
ATOM   2404 C CE1 . PHE A 1 318 ? 15.243 14.403  78.772  1.00 27.09 ? 318 PHE A CE1 1 
ATOM   2405 C CE2 . PHE A 1 318 ? 17.106 15.920  78.549  1.00 29.55 ? 318 PHE A CE2 1 
ATOM   2406 C CZ  . PHE A 1 318 ? 16.174 15.259  79.349  1.00 27.32 ? 318 PHE A CZ  1 
ATOM   2407 N N   . THR A 1 319 ? 16.642 14.949  72.254  1.00 31.13 ? 319 THR A N   1 
ATOM   2408 C CA  . THR A 1 319 ? 17.100 14.366  71.006  1.00 26.39 ? 319 THR A CA  1 
ATOM   2409 C C   . THR A 1 319 ? 18.581 14.114  71.264  1.00 25.06 ? 319 THR A C   1 
ATOM   2410 O O   . THR A 1 319 ? 19.282 15.006  71.749  1.00 18.55 ? 319 THR A O   1 
ATOM   2411 C CB  . THR A 1 319 ? 17.005 15.327  69.831  1.00 31.20 ? 319 THR A CB  1 
ATOM   2412 O OG1 . THR A 1 319 ? 15.635 15.694  69.613  1.00 38.02 ? 319 THR A OG1 1 
ATOM   2413 C CG2 . THR A 1 319 ? 17.585 14.666  68.574  1.00 26.06 ? 319 THR A CG2 1 
ATOM   2414 N N   . GLY A 1 320 ? 19.058 12.918  70.936  1.00 25.32 ? 320 GLY A N   1 
ATOM   2415 C CA  . GLY A 1 320 ? 20.451 12.604  71.176  1.00 23.41 ? 320 GLY A CA  1 
ATOM   2416 C C   . GLY A 1 320 ? 21.194 12.069  69.978  1.00 24.32 ? 320 GLY A C   1 
ATOM   2417 O O   . GLY A 1 320 ? 20.604 11.474  69.072  1.00 24.05 ? 320 GLY A O   1 
ATOM   2418 N N   . PHE A 1 321 ? 22.492 12.342  69.944  1.00 23.66 ? 321 PHE A N   1 
ATOM   2419 C CA  . PHE A 1 321 ? 23.342 11.853  68.869  1.00 23.65 ? 321 PHE A CA  1 
ATOM   2420 C C   . PHE A 1 321 ? 24.463 11.107  69.553  1.00 20.28 ? 321 PHE A C   1 
ATOM   2421 O O   . PHE A 1 321 ? 25.180 11.701  70.356  1.00 20.49 ? 321 PHE A O   1 
ATOM   2422 C CB  . PHE A 1 321 ? 23.951 13.010  68.067  1.00 22.37 ? 321 PHE A CB  1 
ATOM   2423 C CG  . PHE A 1 321 ? 22.976 13.731  67.180  1.00 17.46 ? 321 PHE A CG  1 
ATOM   2424 C CD1 . PHE A 1 321 ? 22.490 13.125  66.018  1.00 18.80 ? 321 PHE A CD1 1 
ATOM   2425 C CD2 . PHE A 1 321 ? 22.560 15.027  67.497  1.00 16.15 ? 321 PHE A CD2 1 
ATOM   2426 C CE1 . PHE A 1 321 ? 21.590 13.808  65.163  1.00 25.02 ? 321 PHE A CE1 1 
ATOM   2427 C CE2 . PHE A 1 321 ? 21.661 15.729  66.662  1.00 24.81 ? 321 PHE A CE2 1 
ATOM   2428 C CZ  . PHE A 1 321 ? 21.171 15.125  65.489  1.00 22.65 ? 321 PHE A CZ  1 
ATOM   2429 N N   . GLY A 1 322 ? 24.567 9.802   69.320  1.00 18.94 ? 322 GLY A N   1 
ATOM   2430 C CA  . GLY A 1 322 ? 25.653 9.051   69.925  1.00 18.56 ? 322 GLY A CA  1 
ATOM   2431 C C   . GLY A 1 322 ? 26.685 8.752   68.855  1.00 19.82 ? 322 GLY A C   1 
ATOM   2432 O O   . GLY A 1 322 ? 26.332 8.156   67.838  1.00 27.07 ? 322 GLY A O   1 
ATOM   2433 N N   . ILE A 1 323 ? 27.934 9.179   69.032  1.00 18.97 ? 323 ILE A N   1 
ATOM   2434 C CA  . ILE A 1 323 ? 28.955 8.891   68.024  1.00 22.14 ? 323 ILE A CA  1 
ATOM   2435 C C   . ILE A 1 323 ? 29.937 7.766   68.440  1.00 24.66 ? 323 ILE A C   1 
ATOM   2436 O O   . ILE A 1 323 ? 30.261 7.629   69.623  1.00 25.76 ? 323 ILE A O   1 
ATOM   2437 C CB  . ILE A 1 323 ? 29.690 10.185  67.527  1.00 16.83 ? 323 ILE A CB  1 
ATOM   2438 C CG1 . ILE A 1 323 ? 30.746 10.647  68.491  1.00 14.65 ? 323 ILE A CG1 1 
ATOM   2439 C CG2 . ILE A 1 323 ? 28.721 11.296  67.290  1.00 15.02 ? 323 ILE A CG2 1 
ATOM   2440 C CD1 . ILE A 1 323 ? 32.116 10.506  67.900  1.00 5.98  ? 323 ILE A CD1 1 
ATOM   2441 N N   . ASN A 1 324 ? 30.379 6.958   67.469  1.00 23.57 ? 324 ASN A N   1 
ATOM   2442 C CA  . ASN A 1 324 ? 31.277 5.821   67.716  1.00 21.81 ? 324 ASN A CA  1 
ATOM   2443 C C   . ASN A 1 324 ? 30.351 4.877   68.436  1.00 24.29 ? 324 ASN A C   1 
ATOM   2444 O O   . ASN A 1 324 ? 30.539 4.543   69.599  1.00 29.09 ? 324 ASN A O   1 
ATOM   2445 C CB  . ASN A 1 324 ? 32.465 6.248   68.587  1.00 25.74 ? 324 ASN A CB  1 
ATOM   2446 C CG  . ASN A 1 324 ? 33.268 5.080   69.109  1.00 31.65 ? 324 ASN A CG  1 
ATOM   2447 O OD1 . ASN A 1 324 ? 33.729 4.236   68.351  1.00 38.06 ? 324 ASN A OD1 1 
ATOM   2448 N ND2 . ASN A 1 324 ? 33.450 5.032   70.413  1.00 32.73 ? 324 ASN A ND2 1 
ATOM   2449 N N   . ALA A 1 325 ? 29.301 4.501   67.724  1.00 26.23 ? 325 ALA A N   1 
ATOM   2450 C CA  . ALA A 1 325 ? 28.239 3.666   68.259  1.00 29.26 ? 325 ALA A CA  1 
ATOM   2451 C C   . ALA A 1 325 ? 28.183 2.167   67.925  1.00 32.98 ? 325 ALA A C   1 
ATOM   2452 O O   . ALA A 1 325 ? 27.587 1.399   68.678  1.00 34.14 ? 325 ALA A O   1 
ATOM   2453 C CB  . ALA A 1 325 ? 26.903 4.306   67.896  1.00 25.74 ? 325 ALA A CB  1 
ATOM   2454 N N   . ASN A 1 326 ? 28.755 1.742   66.804  1.00 32.35 ? 326 ASN A N   1 
ATOM   2455 C CA  . ASN A 1 326 ? 28.665 0.338   66.420  1.00 33.75 ? 326 ASN A CA  1 
ATOM   2456 C C   . ASN A 1 326 ? 29.154 -0.540  67.553  1.00 31.41 ? 326 ASN A C   1 
ATOM   2457 O O   . ASN A 1 326 ? 30.256 -0.367  68.032  1.00 31.40 ? 326 ASN A O   1 
ATOM   2458 C CB  . ASN A 1 326 ? 29.433 0.056   65.112  1.00 41.72 ? 326 ASN A CB  1 
ATOM   2459 C CG  . ASN A 1 326 ? 28.846 0.817   63.882  1.00 51.81 ? 326 ASN A CG  1 
ATOM   2460 O OD1 . ASN A 1 326 ? 27.645 1.122   63.808  1.00 57.00 ? 326 ASN A OD1 1 
ATOM   2461 N ND2 . ASN A 1 326 ? 29.709 1.122   62.920  1.00 51.78 ? 326 ASN A ND2 1 
ATOM   2462 N N   . ASN A 1 327 ? 28.268 -1.394  68.051  1.00 30.98 ? 327 ASN A N   1 
ATOM   2463 C CA  . ASN A 1 327 ? 28.546 -2.335  69.147  1.00 31.93 ? 327 ASN A CA  1 
ATOM   2464 C C   . ASN A 1 327 ? 28.497 -1.785  70.587  1.00 30.02 ? 327 ASN A C   1 
ATOM   2465 O O   . ASN A 1 327 ? 28.869 -2.465  71.524  1.00 33.58 ? 327 ASN A O   1 
ATOM   2466 C CB  . ASN A 1 327 ? 29.848 -3.112  68.906  1.00 35.56 ? 327 ASN A CB  1 
ATOM   2467 C CG  . ASN A 1 327 ? 29.809 -3.973  67.631  1.00 38.48 ? 327 ASN A CG  1 
ATOM   2468 O OD1 . ASN A 1 327 ? 28.740 -4.274  67.095  1.00 33.85 ? 327 ASN A OD1 1 
ATOM   2469 N ND2 . ASN A 1 327 ? 30.992 -4.377  67.150  1.00 38.30 ? 327 ASN A ND2 1 
ATOM   2470 N N   . ASN A 1 328 ? 27.984 -0.575  70.759  1.00 29.77 ? 328 ASN A N   1 
ATOM   2471 C CA  . ASN A 1 328 ? 27.830 0.054   72.070  1.00 25.41 ? 328 ASN A CA  1 
ATOM   2472 C C   . ASN A 1 328 ? 26.804 -0.709  72.904  1.00 25.87 ? 328 ASN A C   1 
ATOM   2473 O O   . ASN A 1 328 ? 25.829 -1.239  72.369  1.00 23.82 ? 328 ASN A O   1 
ATOM   2474 C CB  . ASN A 1 328 ? 27.362 1.507   71.881  1.00 25.86 ? 328 ASN A CB  1 
ATOM   2475 C CG  . ASN A 1 328 ? 26.954 2.188   73.179  1.00 16.11 ? 328 ASN A CG  1 
ATOM   2476 O OD1 . ASN A 1 328 ? 27.754 2.857   73.815  1.00 28.14 ? 328 ASN A OD1 1 
ATOM   2477 N ND2 . ASN A 1 328 ? 25.688 2.088   73.526  1.00 19.45 ? 328 ASN A ND2 1 
ATOM   2478 N N   . ASN A 1 329 ? 27.017 -0.727  74.217  1.00 25.45 ? 329 ASN A N   1 
ATOM   2479 C CA  . ASN A 1 329 ? 26.131 -1.396  75.172  1.00 25.17 ? 329 ASN A CA  1 
ATOM   2480 C C   . ASN A 1 329 ? 25.598 -0.427  76.207  1.00 24.59 ? 329 ASN A C   1 
ATOM   2481 O O   . ASN A 1 329 ? 26.263 0.526   76.610  1.00 26.36 ? 329 ASN A O   1 
ATOM   2482 C CB  . ASN A 1 329 ? 26.853 -2.504  75.915  1.00 30.44 ? 329 ASN A CB  1 
ATOM   2483 C CG  . ASN A 1 329 ? 27.013 -3.755  75.092  1.00 36.13 ? 329 ASN A CG  1 
ATOM   2484 O OD1 . ASN A 1 329 ? 27.855 -4.589  75.404  1.00 46.79 ? 329 ASN A OD1 1 
ATOM   2485 N ND2 . ASN A 1 329 ? 26.201 -3.912  74.053  1.00 39.34 ? 329 ASN A ND2 1 
ATOM   2486 N N   . ARG A 1 330 ? 24.406 -0.721  76.680  1.00 22.32 ? 330 ARG A N   1 
ATOM   2487 C CA  . ARG A 1 330 ? 23.750 0.110   77.660  1.00 24.21 ? 330 ARG A CA  1 
ATOM   2488 C C   . ARG A 1 330 ? 23.840 -0.546  79.031  1.00 22.97 ? 330 ARG A C   1 
ATOM   2489 O O   . ARG A 1 330 ? 23.131 -1.519  79.310  1.00 19.35 ? 330 ARG A O   1 
ATOM   2490 C CB  . ARG A 1 330 ? 22.292 0.254   77.271  1.00 23.01 ? 330 ARG A CB  1 
ATOM   2491 C CG  . ARG A 1 330 ? 21.858 1.659   77.159  1.00 26.70 ? 330 ARG A CG  1 
ATOM   2492 C CD  . ARG A 1 330 ? 21.312 1.885   75.813  1.00 27.52 ? 330 ARG A CD  1 
ATOM   2493 N NE  . ARG A 1 330 ? 19.959 2.378   75.919  1.00 29.35 ? 330 ARG A NE  1 
ATOM   2494 C CZ  . ARG A 1 330 ? 18.907 1.712   75.482  1.00 35.76 ? 330 ARG A CZ  1 
ATOM   2495 N NH1 . ARG A 1 330 ? 19.074 0.520   74.904  1.00 38.96 ? 330 ARG A NH1 1 
ATOM   2496 N NH2 . ARG A 1 330 ? 17.694 2.234   75.646  1.00 32.72 ? 330 ARG A NH2 1 
ATOM   2497 N N   . ASN A 1 331 ? 24.720 -0.038  79.879  1.00 21.84 ? 331 ASN A N   1 
ATOM   2498 C CA  . ASN A 1 331 ? 24.858 -0.622  81.205  1.00 25.01 ? 331 ASN A CA  1 
ATOM   2499 C C   . ASN A 1 331 ? 24.054 0.130   82.243  1.00 27.88 ? 331 ASN A C   1 
ATOM   2500 O O   . ASN A 1 331 ? 24.223 1.345   82.423  1.00 28.77 ? 331 ASN A O   1 
ATOM   2501 C CB  . ASN A 1 331 ? 26.319 -0.687  81.619  1.00 23.25 ? 331 ASN A CB  1 
ATOM   2502 C CG  . ASN A 1 331 ? 27.076 -1.772  80.891  1.00 27.98 ? 331 ASN A CG  1 
ATOM   2503 O OD1 . ASN A 1 331 ? 27.371 -1.666  79.694  1.00 27.53 ? 331 ASN A OD1 1 
ATOM   2504 N ND2 . ASN A 1 331 ? 27.399 -2.830  81.608  1.00 31.54 ? 331 ASN A ND2 1 
ATOM   2505 N N   . LEU A 1 332 ? 23.104 -0.568  82.858  1.00 27.12 ? 332 LEU A N   1 
ATOM   2506 C CA  . LEU A 1 332 ? 22.303 0.046   83.902  1.00 25.05 ? 332 LEU A CA  1 
ATOM   2507 C C   . LEU A 1 332 ? 22.763 -0.443  85.278  1.00 25.07 ? 332 LEU A C   1 
ATOM   2508 O O   . LEU A 1 332 ? 23.208 -1.587  85.440  1.00 18.27 ? 332 LEU A O   1 
ATOM   2509 C CB  . LEU A 1 332 ? 20.808 -0.197  83.700  1.00 22.79 ? 332 LEU A CB  1 
ATOM   2510 C CG  . LEU A 1 332 ? 20.113 0.916   82.928  1.00 23.96 ? 332 LEU A CG  1 
ATOM   2511 C CD1 . LEU A 1 332 ? 20.129 0.567   81.462  1.00 17.30 ? 332 LEU A CD1 1 
ATOM   2512 C CD2 . LEU A 1 332 ? 18.702 1.075   83.415  1.00 18.66 ? 332 LEU A CD2 1 
ATOM   2513 N N   . LEU A 1 333 ? 22.629 0.443   86.261  1.00 25.73 ? 333 LEU A N   1 
ATOM   2514 C CA  . LEU A 1 333 ? 23.047 0.178   87.631  1.00 22.16 ? 333 LEU A CA  1 
ATOM   2515 C C   . LEU A 1 333 ? 21.883 0.029   88.636  1.00 24.76 ? 333 LEU A C   1 
ATOM   2516 O O   . LEU A 1 333 ? 22.103 -0.137  89.849  1.00 23.12 ? 333 LEU A O   1 
ATOM   2517 C CB  . LEU A 1 333 ? 24.038 1.280   88.028  1.00 18.05 ? 333 LEU A CB  1 
ATOM   2518 C CG  . LEU A 1 333 ? 25.173 1.425   86.992  1.00 18.06 ? 333 LEU A CG  1 
ATOM   2519 C CD1 . LEU A 1 333 ? 25.852 2.769   87.059  1.00 16.98 ? 333 LEU A CD1 1 
ATOM   2520 C CD2 . LEU A 1 333 ? 26.166 0.302   87.129  1.00 6.57  ? 333 LEU A CD2 1 
ATOM   2521 N N   . ALA A 1 334 ? 20.651 0.035   88.127  1.00 23.48 ? 334 ALA A N   1 
ATOM   2522 C CA  . ALA A 1 334 ? 19.458 -0.107  88.961  1.00 26.31 ? 334 ALA A CA  1 
ATOM   2523 C C   . ALA A 1 334 ? 18.278 -0.614  88.135  1.00 29.46 ? 334 ALA A C   1 
ATOM   2524 O O   . ALA A 1 334 ? 18.206 -0.354  86.925  1.00 33.88 ? 334 ALA A O   1 
ATOM   2525 C CB  . ALA A 1 334 ? 19.102 1.224   89.621  1.00 20.26 ? 334 ALA A CB  1 
ATOM   2526 N N   . GLY A 1 335 ? 17.381 -1.368  88.774  1.00 33.18 ? 335 GLY A N   1 
ATOM   2527 C CA  . GLY A 1 335 ? 16.201 -1.887  88.087  1.00 35.52 ? 335 GLY A CA  1 
ATOM   2528 C C   . GLY A 1 335 ? 16.289 -3.291  87.507  1.00 37.51 ? 335 GLY A C   1 
ATOM   2529 O O   . GLY A 1 335 ? 17.336 -3.939  87.600  1.00 40.80 ? 335 GLY A O   1 
ATOM   2530 N N   . LYS A 1 336 ? 15.208 -3.730  86.855  1.00 38.29 ? 336 LYS A N   1 
ATOM   2531 C CA  . LYS A 1 336 ? 15.110 -5.066  86.269  1.00 38.42 ? 336 LYS A CA  1 
ATOM   2532 C C   . LYS A 1 336 ? 15.740 -5.330  84.905  1.00 37.97 ? 336 LYS A C   1 
ATOM   2533 O O   . LYS A 1 336 ? 16.125 -6.464  84.634  1.00 39.63 ? 336 LYS A O   1 
ATOM   2534 C CB  . LYS A 1 336 ? 13.657 -5.524  86.229  1.00 45.37 ? 336 LYS A CB  1 
ATOM   2535 C CG  . LYS A 1 336 ? 13.047 -5.722  87.593  1.00 60.87 ? 336 LYS A CG  1 
ATOM   2536 C CD  . LYS A 1 336 ? 13.818 -6.761  88.420  1.00 67.16 ? 336 LYS A CD  1 
ATOM   2537 C CE  . LYS A 1 336 ? 13.405 -6.714  89.893  1.00 70.17 ? 336 LYS A CE  1 
ATOM   2538 N NZ  . LYS A 1 336 ? 14.142 -7.701  90.727  1.00 71.13 ? 336 LYS A NZ  1 
ATOM   2539 N N   . THR A 1 337 ? 15.797 -4.343  84.015  1.00 34.78 ? 337 THR A N   1 
ATOM   2540 C CA  . THR A 1 337 ? 16.403 -4.603  82.712  1.00 31.30 ? 337 THR A CA  1 
ATOM   2541 C C   . THR A 1 337 ? 17.785 -3.970  82.532  1.00 31.74 ? 337 THR A C   1 
ATOM   2542 O O   . THR A 1 337 ? 18.029 -2.835  82.974  1.00 26.28 ? 337 THR A O   1 
ATOM   2543 C CB  . THR A 1 337 ? 15.492 -4.195  81.558  1.00 25.49 ? 337 THR A CB  1 
ATOM   2544 O OG1 . THR A 1 337 ? 14.231 -4.851  81.688  1.00 25.45 ? 337 THR A OG1 1 
ATOM   2545 C CG2 . THR A 1 337 ? 16.094 -4.609  80.257  1.00 29.42 ? 337 THR A CG2 1 
ATOM   2546 N N   . ASP A 1 338 ? 18.689 -4.747  81.924  1.00 29.67 ? 338 ASP A N   1 
ATOM   2547 C CA  . ASP A 1 338 ? 20.061 -4.328  81.645  1.00 28.15 ? 338 ASP A CA  1 
ATOM   2548 C C   . ASP A 1 338 ? 20.872 -3.859  82.855  1.00 29.33 ? 338 ASP A C   1 
ATOM   2549 O O   . ASP A 1 338 ? 21.664 -2.919  82.745  1.00 31.31 ? 338 ASP A O   1 
ATOM   2550 C CB  . ASP A 1 338 ? 20.086 -3.255  80.546  1.00 24.24 ? 338 ASP A CB  1 
ATOM   2551 C CG  . ASP A 1 338 ? 19.684 -3.803  79.196  1.00 23.02 ? 338 ASP A CG  1 
ATOM   2552 O OD1 . ASP A 1 338 ? 20.212 -4.856  78.815  1.00 28.62 ? 338 ASP A OD1 1 
ATOM   2553 O OD2 . ASP A 1 338 ? 18.836 -3.198  78.512  1.00 26.52 ? 338 ASP A OD2 1 
ATOM   2554 N N   . ASN A 1 339 ? 20.704 -4.527  83.997  1.00 28.43 ? 339 ASN A N   1 
ATOM   2555 C CA  . ASN A 1 339 ? 21.453 -4.172  85.208  1.00 24.76 ? 339 ASN A CA  1 
ATOM   2556 C C   . ASN A 1 339 ? 22.766 -4.978  85.280  1.00 25.86 ? 339 ASN A C   1 
ATOM   2557 O O   . ASN A 1 339 ? 22.747 -6.222  85.408  1.00 23.48 ? 339 ASN A O   1 
ATOM   2558 C CB  . ASN A 1 339 ? 20.594 -4.429  86.447  1.00 26.99 ? 339 ASN A CB  1 
ATOM   2559 C CG  . ASN A 1 339 ? 21.269 -3.982  87.748  1.00 23.65 ? 339 ASN A CG  1 
ATOM   2560 O OD1 . ASN A 1 339 ? 22.503 -3.931  87.846  1.00 17.28 ? 339 ASN A OD1 1 
ATOM   2561 N ND2 . ASN A 1 339 ? 20.458 -3.684  88.755  1.00 21.23 ? 339 ASN A ND2 1 
ATOM   2562 N N   . VAL A 1 340 ? 23.902 -4.281  85.205  1.00 24.44 ? 340 VAL A N   1 
ATOM   2563 C CA  . VAL A 1 340 ? 25.200 -4.962  85.250  1.00 25.79 ? 340 VAL A CA  1 
ATOM   2564 C C   . VAL A 1 340 ? 25.389 -5.658  86.574  1.00 29.53 ? 340 VAL A C   1 
ATOM   2565 O O   . VAL A 1 340 ? 25.825 -6.813  86.617  1.00 32.32 ? 340 VAL A O   1 
ATOM   2566 C CB  . VAL A 1 340 ? 26.441 -4.033  85.150  1.00 24.20 ? 340 VAL A CB  1 
ATOM   2567 C CG1 . VAL A 1 340 ? 27.394 -4.561  84.082  1.00 23.35 ? 340 VAL A CG1 1 
ATOM   2568 C CG2 . VAL A 1 340 ? 26.072 -2.585  84.973  1.00 25.89 ? 340 VAL A CG2 1 
ATOM   2569 N N   . ILE A 1 341 ? 25.106 -4.923  87.647  1.00 27.99 ? 341 ILE A N   1 
ATOM   2570 C CA  . ILE A 1 341 ? 25.263 -5.415  89.012  1.00 26.85 ? 341 ILE A CA  1 
ATOM   2571 C C   . ILE A 1 341 ? 24.593 -6.780  89.244  1.00 25.42 ? 341 ILE A C   1 
ATOM   2572 O O   . ILE A 1 341 ? 25.204 -7.671  89.820  1.00 28.19 ? 341 ILE A O   1 
ATOM   2573 C CB  . ILE A 1 341 ? 24.784 -4.355  90.017  1.00 25.33 ? 341 ILE A CB  1 
ATOM   2574 C CG1 . ILE A 1 341 ? 25.463 -3.013  89.705  1.00 28.26 ? 341 ILE A CG1 1 
ATOM   2575 C CG2 . ILE A 1 341 ? 25.129 -4.772  91.456  1.00 34.67 ? 341 ILE A CG2 1 
ATOM   2576 C CD1 . ILE A 1 341 ? 25.054 -1.870  90.641  1.00 19.18 ? 341 ILE A CD1 1 
ATOM   2577 N N   . SER A 1 342 ? 23.369 -6.968  88.760  1.00 24.40 ? 342 SER A N   1 
ATOM   2578 C CA  . SER A 1 342 ? 22.707 -8.257  88.915  1.00 24.53 ? 342 SER A CA  1 
ATOM   2579 C C   . SER A 1 342 ? 23.451 -9.329  88.118  1.00 28.28 ? 342 SER A C   1 
ATOM   2580 O O   . SER A 1 342 ? 23.521 -10.488 88.526  1.00 29.02 ? 342 SER A O   1 
ATOM   2581 C CB  . SER A 1 342 ? 21.263 -8.175  88.427  1.00 27.65 ? 342 SER A CB  1 
ATOM   2582 O OG  . SER A 1 342 ? 20.570 -7.131  89.088  1.00 35.24 ? 342 SER A OG  1 
ATOM   2583 N N   . SER A 1 343 ? 24.007 -8.937  86.973  1.00 29.35 ? 343 SER A N   1 
ATOM   2584 C CA  . SER A 1 343 ? 24.745 -9.865  86.140  1.00 24.74 ? 343 SER A CA  1 
ATOM   2585 C C   . SER A 1 343 ? 26.034 -10.329 86.825  1.00 23.25 ? 343 SER A C   1 
ATOM   2586 O O   . SER A 1 343 ? 26.421 -11.493 86.687  1.00 25.42 ? 343 SER A O   1 
ATOM   2587 C CB  . SER A 1 343 ? 25.028 -9.238  84.781  1.00 25.30 ? 343 SER A CB  1 
ATOM   2588 O OG  . SER A 1 343 ? 25.462 -10.215 83.850  1.00 30.11 ? 343 SER A OG  1 
ATOM   2589 N N   . ILE A 1 344 ? 26.709 -9.444  87.558  1.00 22.97 ? 344 ILE A N   1 
ATOM   2590 C CA  . ILE A 1 344 ? 27.924 -9.855  88.281  1.00 24.33 ? 344 ILE A CA  1 
ATOM   2591 C C   . ILE A 1 344 ? 27.512 -10.929 89.312  1.00 29.33 ? 344 ILE A C   1 
ATOM   2592 O O   . ILE A 1 344 ? 28.258 -11.860 89.595  1.00 29.98 ? 344 ILE A O   1 
ATOM   2593 C CB  . ILE A 1 344 ? 28.571 -8.707  89.087  1.00 19.06 ? 344 ILE A CB  1 
ATOM   2594 C CG1 . ILE A 1 344 ? 28.940 -7.541  88.192  1.00 16.38 ? 344 ILE A CG1 1 
ATOM   2595 C CG2 . ILE A 1 344 ? 29.835 -9.192  89.773  1.00 18.85 ? 344 ILE A CG2 1 
ATOM   2596 C CD1 . ILE A 1 344 ? 29.607 -6.420  88.955  1.00 13.58 ? 344 ILE A CD1 1 
ATOM   2597 N N   . GLY A 1 345 ? 26.320 -10.778 89.878  1.00 30.78 ? 345 GLY A N   1 
ATOM   2598 C CA  . GLY A 1 345 ? 25.848 -11.731 90.854  1.00 32.36 ? 345 GLY A CA  1 
ATOM   2599 C C   . GLY A 1 345 ? 25.585 -13.101 90.266  1.00 32.92 ? 345 GLY A C   1 
ATOM   2600 O O   . GLY A 1 345 ? 25.777 -14.114 90.939  1.00 37.87 ? 345 GLY A O   1 
ATOM   2601 N N   . ARG A 1 346 ? 25.164 -13.149 89.010  1.00 30.22 ? 346 ARG A N   1 
ATOM   2602 C CA  . ARG A 1 346 ? 24.869 -14.428 88.382  1.00 27.26 ? 346 ARG A CA  1 
ATOM   2603 C C   . ARG A 1 346 ? 26.068 -15.134 87.787  1.00 24.49 ? 346 ARG A C   1 
ATOM   2604 O O   . ARG A 1 346 ? 25.932 -16.174 87.166  1.00 23.92 ? 346 ARG A O   1 
ATOM   2605 C CB  . ARG A 1 346 ? 23.742 -14.276 87.366  1.00 23.86 ? 346 ARG A CB  1 
ATOM   2606 C CG  . ARG A 1 346 ? 22.488 -13.772 88.017  1.00 26.87 ? 346 ARG A CG  1 
ATOM   2607 C CD  . ARG A 1 346 ? 21.256 -14.315 87.358  1.00 45.00 ? 346 ARG A CD  1 
ATOM   2608 N NE  . ARG A 1 346 ? 20.716 -13.364 86.399  1.00 61.13 ? 346 ARG A NE  1 
ATOM   2609 C CZ  . ARG A 1 346 ? 20.242 -12.166 86.727  1.00 67.71 ? 346 ARG A CZ  1 
ATOM   2610 N NH1 . ARG A 1 346 ? 20.235 -11.772 87.996  1.00 70.89 ? 346 ARG A NH1 1 
ATOM   2611 N NH2 . ARG A 1 346 ? 19.791 -11.353 85.780  1.00 70.93 ? 346 ARG A NH2 1 
ATOM   2612 N N   . ALA A 1 347 ? 27.243 -14.548 87.955  1.00 27.77 ? 347 ALA A N   1 
ATOM   2613 C CA  . ALA A 1 347 ? 28.455 -15.155 87.450  1.00 31.32 ? 347 ALA A CA  1 
ATOM   2614 C C   . ALA A 1 347 ? 28.747 -16.349 88.379  1.00 36.55 ? 347 ALA A C   1 
ATOM   2615 O O   . ALA A 1 347 ? 28.044 -16.540 89.381  1.00 33.26 ? 347 ALA A O   1 
ATOM   2616 C CB  . ALA A 1 347 ? 29.586 -14.149 87.475  1.00 24.97 ? 347 ALA A CB  1 
ATOM   2617 N N   . LEU A 1 348 ? 29.795 -17.119 88.068  1.00 39.78 ? 348 LEU A N   1 
ATOM   2618 C CA  . LEU A 1 348 ? 30.169 -18.294 88.847  1.00 39.65 ? 348 LEU A CA  1 
ATOM   2619 C C   . LEU A 1 348 ? 30.177 -18.072 90.334  1.00 44.68 ? 348 LEU A C   1 
ATOM   2620 O O   . LEU A 1 348 ? 29.462 -18.745 91.076  1.00 55.28 ? 348 LEU A O   1 
ATOM   2621 C CB  . LEU A 1 348 ? 31.515 -18.830 88.420  1.00 37.59 ? 348 LEU A CB  1 
ATOM   2622 C CG  . LEU A 1 348 ? 31.375 -20.181 87.732  1.00 44.39 ? 348 LEU A CG  1 
ATOM   2623 C CD1 . LEU A 1 348 ? 32.691 -20.533 87.081  1.00 53.02 ? 348 LEU A CD1 1 
ATOM   2624 C CD2 . LEU A 1 348 ? 30.953 -21.256 88.728  1.00 45.29 ? 348 LEU A CD2 1 
ATOM   2625 N N   . ASP A 1 349 ? 31.018 -17.174 90.797  1.00 44.37 ? 349 ASP A N   1 
ATOM   2626 C CA  . ASP A 1 349 ? 31.043 -16.905 92.218  1.00 43.46 ? 349 ASP A CA  1 
ATOM   2627 C C   . ASP A 1 349 ? 30.619 -15.458 92.322  1.00 41.61 ? 349 ASP A C   1 
ATOM   2628 O O   . ASP A 1 349 ? 31.234 -14.666 93.039  1.00 42.81 ? 349 ASP A O   1 
ATOM   2629 C CB  . ASP A 1 349 ? 32.450 -17.117 92.758  1.00 55.26 ? 349 ASP A CB  1 
ATOM   2630 C CG  . ASP A 1 349 ? 33.017 -18.470 92.371  1.00 64.47 ? 349 ASP A CG  1 
ATOM   2631 O OD1 . ASP A 1 349 ? 32.801 -19.449 93.121  1.00 72.18 ? 349 ASP A OD1 1 
ATOM   2632 O OD2 . ASP A 1 349 ? 33.667 -18.561 91.305  1.00 70.49 ? 349 ASP A OD2 1 
ATOM   2633 N N   . GLY A 1 350 ? 29.571 -15.121 91.574  1.00 36.29 ? 350 GLY A N   1 
ATOM   2634 C CA  . GLY A 1 350 ? 29.061 -13.768 91.562  1.00 35.42 ? 350 GLY A CA  1 
ATOM   2635 C C   . GLY A 1 350 ? 28.889 -13.202 92.953  1.00 36.63 ? 350 GLY A C   1 
ATOM   2636 O O   . GLY A 1 350 ? 29.417 -12.135 93.271  1.00 36.18 ? 350 GLY A O   1 
ATOM   2637 N N   . LYS A 1 351 ? 28.178 -13.938 93.796  1.00 36.06 ? 351 LYS A N   1 
ATOM   2638 C CA  . LYS A 1 351 ? 27.945 -13.516 95.167  1.00 37.11 ? 351 LYS A CA  1 
ATOM   2639 C C   . LYS A 1 351 ? 29.236 -13.224 95.938  1.00 35.43 ? 351 LYS A C   1 
ATOM   2640 O O   . LYS A 1 351 ? 29.306 -12.226 96.638  1.00 40.50 ? 351 LYS A O   1 
ATOM   2641 C CB  . LYS A 1 351 ? 27.092 -14.547 95.909  1.00 41.47 ? 351 LYS A CB  1 
ATOM   2642 C CG  . LYS A 1 351 ? 25.706 -14.783 95.302  1.00 43.14 ? 351 LYS A CG  1 
ATOM   2643 C CD  . LYS A 1 351 ? 24.788 -15.488 96.308  1.00 50.91 ? 351 LYS A CD  1 
ATOM   2644 C CE  . LYS A 1 351 ? 23.426 -15.844 95.710  1.00 52.49 ? 351 LYS A CE  1 
ATOM   2645 N NZ  . LYS A 1 351 ? 22.505 -16.440 96.735  1.00 54.66 ? 351 LYS A NZ  1 
ATOM   2646 N N   . ASP A 1 352 ? 30.265 -14.056 95.781  1.00 35.47 ? 352 ASP A N   1 
ATOM   2647 C CA  . ASP A 1 352 ? 31.540 -13.833 96.478  1.00 33.73 ? 352 ASP A CA  1 
ATOM   2648 C C   . ASP A 1 352 ? 32.201 -12.546 95.962  1.00 31.09 ? 352 ASP A C   1 
ATOM   2649 O O   . ASP A 1 352 ? 32.775 -11.781 96.729  1.00 30.42 ? 352 ASP A O   1 
ATOM   2650 C CB  . ASP A 1 352 ? 32.518 -15.009 96.279  1.00 36.88 ? 352 ASP A CB  1 
ATOM   2651 C CG  . ASP A 1 352 ? 31.962 -16.353 96.752  1.00 43.18 ? 352 ASP A CG  1 
ATOM   2652 O OD1 . ASP A 1 352 ? 30.753 -16.624 96.580  1.00 52.40 ? 352 ASP A OD1 1 
ATOM   2653 O OD2 . ASP A 1 352 ? 32.751 -17.170 97.265  1.00 41.42 ? 352 ASP A OD2 1 
ATOM   2654 N N   . VAL A 1 353 ? 32.173 -12.341 94.647  1.00 28.43 ? 353 VAL A N   1 
ATOM   2655 C CA  . VAL A 1 353 ? 32.756 -11.141 94.057  1.00 22.18 ? 353 VAL A CA  1 
ATOM   2656 C C   . VAL A 1 353 ? 32.008 -9.930  94.611  1.00 20.24 ? 353 VAL A C   1 
ATOM   2657 O O   . VAL A 1 353 ? 32.618 -9.049  95.204  1.00 23.00 ? 353 VAL A O   1 
ATOM   2658 C CB  . VAL A 1 353 ? 32.685 -11.173 92.487  1.00 20.80 ? 353 VAL A CB  1 
ATOM   2659 C CG1 . VAL A 1 353 ? 33.043 -9.808  91.867  1.00 9.78  ? 353 VAL A CG1 1 
ATOM   2660 C CG2 . VAL A 1 353 ? 33.645 -12.206 91.969  1.00 21.43 ? 353 VAL A CG2 1 
ATOM   2661 N N   . LEU A 1 354 ? 30.682 -9.931  94.480  1.00 20.81 ? 354 LEU A N   1 
ATOM   2662 C CA  . LEU A 1 354 ? 29.858 -8.829  94.964  1.00 21.93 ? 354 LEU A CA  1 
ATOM   2663 C C   . LEU A 1 354 ? 30.099 -8.664  96.454  1.00 25.76 ? 354 LEU A C   1 
ATOM   2664 O O   . LEU A 1 354 ? 30.116 -7.552  96.978  1.00 28.90 ? 354 LEU A O   1 
ATOM   2665 C CB  . LEU A 1 354 ? 28.372 -9.086  94.673  1.00 19.81 ? 354 LEU A CB  1 
ATOM   2666 C CG  . LEU A 1 354 ? 27.837 -8.786  93.263  1.00 22.08 ? 354 LEU A CG  1 
ATOM   2667 C CD1 . LEU A 1 354 ? 26.420 -9.336  93.085  1.00 18.27 ? 354 LEU A CD1 1 
ATOM   2668 C CD2 . LEU A 1 354 ? 27.859 -7.293  93.026  1.00 18.83 ? 354 LEU A CD2 1 
ATOM   2669 N N   . GLY A 1 355 ? 30.380 -9.779  97.111  1.00 29.62 ? 355 GLY A N   1 
ATOM   2670 C CA  . GLY A 1 355 ? 30.651 -9.749  98.531  1.00 31.54 ? 355 GLY A CA  1 
ATOM   2671 C C   . GLY A 1 355 ? 31.874 -8.906  98.839  1.00 32.86 ? 355 GLY A C   1 
ATOM   2672 O O   . GLY A 1 355 ? 31.877 -8.114  99.794  1.00 36.47 ? 355 GLY A O   1 
ATOM   2673 N N   . LEU A 1 356 ? 32.913 -9.066  98.024  1.00 29.24 ? 356 LEU A N   1 
ATOM   2674 C CA  . LEU A 1 356 ? 34.152 -8.325  98.215  1.00 28.89 ? 356 LEU A CA  1 
ATOM   2675 C C   . LEU A 1 356 ? 34.123 -6.929  97.612  1.00 30.15 ? 356 LEU A C   1 
ATOM   2676 O O   . LEU A 1 356 ? 34.976 -6.083  97.932  1.00 25.78 ? 356 LEU A O   1 
ATOM   2677 C CB  . LEU A 1 356 ? 35.327 -9.116  97.655  1.00 27.78 ? 356 LEU A CB  1 
ATOM   2678 C CG  . LEU A 1 356 ? 35.650 -10.447 98.340  1.00 30.93 ? 356 LEU A CG  1 
ATOM   2679 C CD1 . LEU A 1 356 ? 36.501 -11.326 97.413  1.00 37.64 ? 356 LEU A CD1 1 
ATOM   2680 C CD2 . LEU A 1 356 ? 36.373 -10.189 99.653  1.00 37.03 ? 356 LEU A CD2 1 
ATOM   2681 N N   . THR A 1 357 ? 33.120 -6.684  96.771  1.00 31.95 ? 357 THR A N   1 
ATOM   2682 C CA  . THR A 1 357 ? 32.975 -5.401  96.099  1.00 32.10 ? 357 THR A CA  1 
ATOM   2683 C C   . THR A 1 357 ? 32.311 -4.344  96.964  1.00 31.88 ? 357 THR A C   1 
ATOM   2684 O O   . THR A 1 357 ? 32.632 -3.151  96.851  1.00 29.66 ? 357 THR A O   1 
ATOM   2685 C CB  . THR A 1 357 ? 32.182 -5.563  94.794  1.00 31.57 ? 357 THR A CB  1 
ATOM   2686 O OG1 . THR A 1 357 ? 32.795 -6.583  94.010  1.00 34.37 ? 357 THR A OG1 1 
ATOM   2687 C CG2 . THR A 1 357 ? 32.191 -4.275  93.987  1.00 33.37 ? 357 THR A CG2 1 
ATOM   2688 N N   . PHE A 1 358 ? 31.364 -4.785  97.793  1.00 31.55 ? 358 PHE A N   1 
ATOM   2689 C CA  . PHE A 1 358 ? 30.614 -3.896  98.680  1.00 31.35 ? 358 PHE A CA  1 
ATOM   2690 C C   . PHE A 1 358 ? 30.753 -4.316  100.138 1.00 34.24 ? 358 PHE A C   1 
ATOM   2691 O O   . PHE A 1 358 ? 31.336 -5.368  100.433 1.00 40.52 ? 358 PHE A O   1 
ATOM   2692 C CB  . PHE A 1 358 ? 29.137 -3.873  98.278  1.00 22.81 ? 358 PHE A CB  1 
ATOM   2693 C CG  . PHE A 1 358 ? 28.899 -3.289  96.925  1.00 18.67 ? 358 PHE A CG  1 
ATOM   2694 C CD1 . PHE A 1 358 ? 29.117 -1.920  96.693  1.00 21.69 ? 358 PHE A CD1 1 
ATOM   2695 C CD2 . PHE A 1 358 ? 28.530 -4.101  95.861  1.00 14.47 ? 358 PHE A CD2 1 
ATOM   2696 C CE1 . PHE A 1 358 ? 28.977 -1.370  95.415  1.00 9.71  ? 358 PHE A CE1 1 
ATOM   2697 C CE2 . PHE A 1 358 ? 28.389 -3.563  94.579  1.00 12.57 ? 358 PHE A CE2 1 
ATOM   2698 C CZ  . PHE A 1 358 ? 28.616 -2.191  94.361  1.00 7.95  ? 358 PHE A CZ  1 
ATOM   2699 N N   . SER A 1 359 ? 30.273 -3.469  101.047 1.00 35.69 ? 359 SER A N   1 
ATOM   2700 C CA  . SER A 1 359 ? 30.333 -3.767  102.479 1.00 30.29 ? 359 SER A CA  1 
ATOM   2701 C C   . SER A 1 359 ? 29.502 -5.001  102.775 1.00 31.09 ? 359 SER A C   1 
ATOM   2702 O O   . SER A 1 359 ? 30.003 -5.970  103.338 1.00 34.96 ? 359 SER A O   1 
ATOM   2703 C CB  . SER A 1 359 ? 29.814 -2.590  103.296 1.00 28.98 ? 359 SER A CB  1 
ATOM   2704 O OG  . SER A 1 359 ? 30.652 -1.463  103.134 1.00 28.85 ? 359 SER A OG  1 
ATOM   2705 N N   . GLY A 1 360 ? 28.250 -4.984  102.335 1.00 29.04 ? 360 GLY A N   1 
ATOM   2706 C CA  . GLY A 1 360 ? 27.371 -6.110  102.569 1.00 31.63 ? 360 GLY A CA  1 
ATOM   2707 C C   . GLY A 1 360 ? 27.821 -7.437  101.982 1.00 33.71 ? 360 GLY A C   1 
ATOM   2708 O O   . GLY A 1 360 ? 28.811 -7.527  101.261 1.00 40.09 ? 360 GLY A O   1 
ATOM   2709 N N   . SER A 1 361 ? 27.099 -8.491  102.326 1.00 30.74 ? 361 SER A N   1 
ATOM   2710 C CA  . SER A 1 361 ? 27.412 -9.811  101.817 1.00 31.48 ? 361 SER A CA  1 
ATOM   2711 C C   . SER A 1 361 ? 26.785 -9.863  100.425 1.00 33.36 ? 361 SER A C   1 
ATOM   2712 O O   . SER A 1 361 ? 25.978 -8.991  100.077 1.00 35.22 ? 361 SER A O   1 
ATOM   2713 C CB  . SER A 1 361 ? 26.794 -10.883 102.732 1.00 23.13 ? 361 SER A CB  1 
ATOM   2714 O OG  . SER A 1 361 ? 25.378 -10.796 102.750 1.00 19.66 ? 361 SER A OG  1 
ATOM   2715 N N   . GLY A 1 362 ? 27.121 -10.890 99.647  1.00 34.69 ? 362 GLY A N   1 
ATOM   2716 C CA  . GLY A 1 362 ? 26.559 -11.028 98.308  1.00 31.66 ? 362 GLY A CA  1 
ATOM   2717 C C   . GLY A 1 362 ? 25.054 -11.264 98.288  1.00 30.00 ? 362 GLY A C   1 
ATOM   2718 O O   . GLY A 1 362 ? 24.382 -10.816 97.371  1.00 30.74 ? 362 GLY A O   1 
ATOM   2719 N N   . ASP A 1 363 ? 24.552 -11.996 99.284  1.00 30.11 ? 363 ASP A N   1 
ATOM   2720 C CA  . ASP A 1 363 ? 23.130 -12.314 99.455  1.00 31.17 ? 363 ASP A CA  1 
ATOM   2721 C C   . ASP A 1 363 ? 22.399 -10.998 99.714  1.00 30.18 ? 363 ASP A C   1 
ATOM   2722 O O   . ASP A 1 363 ? 21.307 -10.779 99.199  1.00 30.52 ? 363 ASP A O   1 
ATOM   2723 C CB  . ASP A 1 363 ? 22.942 -13.219 100.704 1.00 39.39 ? 363 ASP A CB  1 
ATOM   2724 C CG  . ASP A 1 363 ? 22.254 -14.574 100.403 1.00 41.18 ? 363 ASP A CG  1 
ATOM   2725 O OD1 . ASP A 1 363 ? 22.918 -15.432 99.774  1.00 46.84 ? 363 ASP A OD1 1 
ATOM   2726 O OD2 . ASP A 1 363 ? 21.092 -14.815 100.855 1.00 35.48 ? 363 ASP A OD2 1 
ATOM   2727 N N   . GLU A 1 364 ? 22.995 -10.158 100.565 1.00 32.45 ? 364 GLU A N   1 
ATOM   2728 C CA  . GLU A 1 364 ? 22.443 -8.858  100.944 1.00 30.90 ? 364 GLU A CA  1 
ATOM   2729 C C   . GLU A 1 364 ? 22.360 -7.871  99.774  1.00 33.53 ? 364 GLU A C   1 
ATOM   2730 O O   . GLU A 1 364 ? 21.296 -7.317  99.495  1.00 35.11 ? 364 GLU A O   1 
ATOM   2731 C CB  . GLU A 1 364 ? 23.265 -8.221  102.084 1.00 36.55 ? 364 GLU A CB  1 
ATOM   2732 C CG  . GLU A 1 364 ? 22.917 -8.672  103.521 1.00 36.00 ? 364 GLU A CG  1 
ATOM   2733 C CD  . GLU A 1 364 ? 23.803 -8.016  104.596 1.00 40.44 ? 364 GLU A CD  1 
ATOM   2734 O OE1 . GLU A 1 364 ? 25.037 -8.062  104.479 1.00 44.16 ? 364 GLU A OE1 1 
ATOM   2735 O OE2 . GLU A 1 364 ? 23.276 -7.460  105.583 1.00 46.68 ? 364 GLU A OE2 1 
ATOM   2736 N N   . VAL A 1 365 ? 23.466 -7.644  99.073  1.00 33.85 ? 365 VAL A N   1 
ATOM   2737 C CA  . VAL A 1 365 ? 23.427 -6.685  97.971  1.00 33.94 ? 365 VAL A CA  1 
ATOM   2738 C C   . VAL A 1 365 ? 22.550 -7.194  96.821  1.00 31.12 ? 365 VAL A C   1 
ATOM   2739 O O   . VAL A 1 365 ? 21.908 -6.412  96.121  1.00 28.00 ? 365 VAL A O   1 
ATOM   2740 C CB  . VAL A 1 365 ? 24.858 -6.235  97.504  1.00 35.38 ? 365 VAL A CB  1 
ATOM   2741 C CG1 . VAL A 1 365 ? 25.879 -6.411  98.633  1.00 28.09 ? 365 VAL A CG1 1 
ATOM   2742 C CG2 . VAL A 1 365 ? 25.279 -6.935  96.244  1.00 30.89 ? 365 VAL A CG2 1 
ATOM   2743 N N   . MET A 1 366 ? 22.466 -8.512  96.698  1.00 29.13 ? 366 MET A N   1 
ATOM   2744 C CA  . MET A 1 366 ? 21.649 -9.170  95.682  1.00 31.49 ? 366 MET A CA  1 
ATOM   2745 C C   . MET A 1 366 ? 20.164 -8.917  95.987  1.00 30.96 ? 366 MET A C   1 
ATOM   2746 O O   . MET A 1 366 ? 19.373 -8.621  95.094  1.00 34.25 ? 366 MET A O   1 
ATOM   2747 C CB  . MET A 1 366 ? 21.952 -10.672 95.700  1.00 35.75 ? 366 MET A CB  1 
ATOM   2748 C CG  . MET A 1 366 ? 21.793 -11.399 94.375  1.00 41.26 ? 366 MET A CG  1 
ATOM   2749 S SD  . MET A 1 366 ? 22.738 -10.640 93.064  1.00 39.66 ? 366 MET A SD  1 
ATOM   2750 C CE  . MET A 1 366 ? 21.581 -10.742 91.714  1.00 41.54 ? 366 MET A CE  1 
ATOM   2751 N N   . LYS A 1 367 ? 19.795 -9.044  97.255  1.00 29.17 ? 367 LYS A N   1 
ATOM   2752 C CA  . LYS A 1 367 ? 18.435 -8.804  97.701  1.00 23.90 ? 367 LYS A CA  1 
ATOM   2753 C C   . LYS A 1 367 ? 18.115 -7.315  97.571  1.00 27.15 ? 367 LYS A C   1 
ATOM   2754 O O   . LYS A 1 367 ? 16.962 -6.942  97.321  1.00 27.59 ? 367 LYS A O   1 
ATOM   2755 C CB  . LYS A 1 367 ? 18.274 -9.204  99.170  1.00 23.00 ? 367 LYS A CB  1 
ATOM   2756 C CG  . LYS A 1 367 ? 18.206 -10.687 99.448  1.00 24.43 ? 367 LYS A CG  1 
ATOM   2757 C CD  . LYS A 1 367 ? 17.276 -10.957 100.636 1.00 30.02 ? 367 LYS A CD  1 
ATOM   2758 C CE  . LYS A 1 367 ? 18.009 -10.982 101.980 1.00 29.41 ? 367 LYS A CE  1 
ATOM   2759 N NZ  . LYS A 1 367 ? 18.385 -12.374 102.330 1.00 21.90 ? 367 LYS A NZ  1 
ATOM   2760 N N   . LEU A 1 368 ? 19.118 -6.464  97.797  1.00 26.97 ? 368 LEU A N   1 
ATOM   2761 C CA  . LEU A 1 368 ? 18.933 -5.014  97.692  1.00 30.09 ? 368 LEU A CA  1 
ATOM   2762 C C   . LEU A 1 368 ? 18.537 -4.678  96.261  1.00 34.03 ? 368 LEU A C   1 
ATOM   2763 O O   . LEU A 1 368 ? 17.443 -4.178  95.999  1.00 35.47 ? 368 LEU A O   1 
ATOM   2764 C CB  . LEU A 1 368 ? 20.217 -4.253  98.043  1.00 27.44 ? 368 LEU A CB  1 
ATOM   2765 C CG  . LEU A 1 368 ? 20.085 -2.730  97.846  1.00 31.01 ? 368 LEU A CG  1 
ATOM   2766 C CD1 . LEU A 1 368 ? 19.022 -2.212  98.804  1.00 35.79 ? 368 LEU A CD1 1 
ATOM   2767 C CD2 . LEU A 1 368 ? 21.404 -1.972  98.053  1.00 24.75 ? 368 LEU A CD2 1 
ATOM   2768 N N   . ILE A 1 369 ? 19.401 -5.061  95.333  1.00 35.87 ? 369 ILE A N   1 
ATOM   2769 C CA  . ILE A 1 369 ? 19.180 -4.818  93.917  1.00 36.62 ? 369 ILE A CA  1 
ATOM   2770 C C   . ILE A 1 369 ? 17.782 -5.234  93.470  1.00 36.09 ? 369 ILE A C   1 
ATOM   2771 O O   . ILE A 1 369 ? 17.257 -4.692  92.507  1.00 41.33 ? 369 ILE A O   1 
ATOM   2772 C CB  . ILE A 1 369 ? 20.296 -5.519  93.058  1.00 37.67 ? 369 ILE A CB  1 
ATOM   2773 C CG1 . ILE A 1 369 ? 21.653 -4.809  93.248  1.00 33.27 ? 369 ILE A CG1 1 
ATOM   2774 C CG2 . ILE A 1 369 ? 19.932 -5.550  91.592  1.00 45.88 ? 369 ILE A CG2 1 
ATOM   2775 C CD1 . ILE A 1 369 ? 21.631 -3.281  93.048  1.00 23.76 ? 369 ILE A CD1 1 
ATOM   2776 N N   . ASN A 1 370 ? 17.135 -6.116  94.222  1.00 35.12 ? 370 ASN A N   1 
ATOM   2777 C CA  . ASN A 1 370 ? 15.801 -6.583  93.846  1.00 38.30 ? 370 ASN A CA  1 
ATOM   2778 C C   . ASN A 1 370 ? 14.567 -5.796  94.271  1.00 33.51 ? 370 ASN A C   1 
ATOM   2779 O O   . ASN A 1 370 ? 13.462 -6.132  93.848  1.00 33.64 ? 370 ASN A O   1 
ATOM   2780 C CB  . ASN A 1 370 ? 15.605 -8.038  94.274  1.00 48.22 ? 370 ASN A CB  1 
ATOM   2781 C CG  . ASN A 1 370 ? 16.260 -9.010  93.336  1.00 55.86 ? 370 ASN A CG  1 
ATOM   2782 O OD1 . ASN A 1 370 ? 15.801 -9.195  92.213  1.00 67.09 ? 370 ASN A OD1 1 
ATOM   2783 N ND2 . ASN A 1 370 ? 17.340 -9.644  93.783  1.00 60.32 ? 370 ASN A ND2 1 
ATOM   2784 N N   . LYS A 1 371 ? 14.730 -4.754  95.076  1.00 33.36 ? 371 LYS A N   1 
ATOM   2785 C CA  . LYS A 1 371 ? 13.572 -3.990  95.556  1.00 31.88 ? 371 LYS A CA  1 
ATOM   2786 C C   . LYS A 1 371 ? 12.867 -3.143  94.504  1.00 32.47 ? 371 LYS A C   1 
ATOM   2787 O O   . LYS A 1 371 ? 11.693 -2.822  94.643  1.00 32.26 ? 371 LYS A O   1 
ATOM   2788 C CB  . LYS A 1 371 ? 13.949 -3.063  96.721  1.00 34.24 ? 371 LYS A CB  1 
ATOM   2789 C CG  . LYS A 1 371 ? 14.375 -3.703  98.034  1.00 33.63 ? 371 LYS A CG  1 
ATOM   2790 C CD  . LYS A 1 371 ? 14.242 -2.635  99.135  1.00 46.58 ? 371 LYS A CD  1 
ATOM   2791 C CE  . LYS A 1 371 ? 14.677 -3.099  100.535 1.00 55.66 ? 371 LYS A CE  1 
ATOM   2792 N NZ  . LYS A 1 371 ? 16.165 -3.137  100.732 1.00 58.82 ? 371 LYS A NZ  1 
ATOM   2793 N N   . GLN A 1 372 ? 13.617 -2.706  93.502  1.00 34.13 ? 372 GLN A N   1 
ATOM   2794 C CA  . GLN A 1 372 ? 13.100 -1.855  92.433  1.00 30.40 ? 372 GLN A CA  1 
ATOM   2795 C C   . GLN A 1 372 ? 12.549 -2.692  91.284  1.00 28.28 ? 372 GLN A C   1 
ATOM   2796 O O   . GLN A 1 372 ? 13.298 -3.313  90.536  1.00 25.23 ? 372 GLN A O   1 
ATOM   2797 C CB  . GLN A 1 372 ? 14.231 -0.926  91.933  1.00 33.22 ? 372 GLN A CB  1 
ATOM   2798 C CG  . GLN A 1 372 ? 13.892 -0.048  90.735  1.00 23.84 ? 372 GLN A CG  1 
ATOM   2799 C CD  . GLN A 1 372 ? 12.778 0.888   91.057  1.00 23.59 ? 372 GLN A CD  1 
ATOM   2800 O OE1 . GLN A 1 372 ? 11.620 0.582   90.822  1.00 28.05 ? 372 GLN A OE1 1 
ATOM   2801 N NE2 . GLN A 1 372 ? 13.104 2.013   91.644  1.00 22.72 ? 372 GLN A NE2 1 
ATOM   2802 N N   . SER A 1 373 ? 11.236 -2.696  91.140  1.00 26.83 ? 373 SER A N   1 
ATOM   2803 C CA  . SER A 1 373 ? 10.619 -3.470  90.074  1.00 31.37 ? 373 SER A CA  1 
ATOM   2804 C C   . SER A 1 373 ? 10.732 -2.792  88.714  1.00 31.51 ? 373 SER A C   1 
ATOM   2805 O O   . SER A 1 373 ? 10.582 -3.445  87.678  1.00 32.45 ? 373 SER A O   1 
ATOM   2806 C CB  . SER A 1 373 ? 9.143  -3.761  90.402  1.00 34.51 ? 373 SER A CB  1 
ATOM   2807 O OG  . SER A 1 373 ? 8.520  -2.695  91.113  1.00 40.07 ? 373 SER A OG  1 
ATOM   2808 N N   . GLY A 1 374 ? 11.010 -1.491  88.728  1.00 32.43 ? 374 GLY A N   1 
ATOM   2809 C CA  . GLY A 1 374 ? 11.103 -0.726  87.497  1.00 33.57 ? 374 GLY A CA  1 
ATOM   2810 C C   . GLY A 1 374 ? 12.298 -1.036  86.625  1.00 35.11 ? 374 GLY A C   1 
ATOM   2811 O O   . GLY A 1 374 ? 13.239 -1.707  87.059  1.00 35.80 ? 374 GLY A O   1 
ATOM   2812 N N   . SER A 1 375 ? 12.246 -0.536  85.389  1.00 35.02 ? 375 SER A N   1 
ATOM   2813 C CA  . SER A 1 375 ? 13.310 -0.700  84.397  1.00 32.54 ? 375 SER A CA  1 
ATOM   2814 C C   . SER A 1 375 ? 13.536 0.618   83.659  1.00 30.99 ? 375 SER A C   1 
ATOM   2815 O O   . SER A 1 375 ? 12.583 1.200   83.118  1.00 28.43 ? 375 SER A O   1 
ATOM   2816 C CB  . SER A 1 375 ? 12.939 -1.792  83.396  1.00 33.69 ? 375 SER A CB  1 
ATOM   2817 O OG  . SER A 1 375 ? 12.955 -3.068  84.009  1.00 34.31 ? 375 SER A OG  1 
ATOM   2818 N N   . TYR A 1 376 ? 14.783 1.096   83.665  1.00 27.99 ? 376 TYR A N   1 
ATOM   2819 C CA  . TYR A 1 376 ? 15.152 2.346   82.999  1.00 24.93 ? 376 TYR A CA  1 
ATOM   2820 C C   . TYR A 1 376 ? 14.585 3.629   83.614  1.00 25.40 ? 376 TYR A C   1 
ATOM   2821 O O   . TYR A 1 376 ? 15.339 4.451   84.125  1.00 24.64 ? 376 TYR A O   1 
ATOM   2822 C CB  . TYR A 1 376 ? 14.757 2.290   81.517  1.00 31.61 ? 376 TYR A CB  1 
ATOM   2823 C CG  . TYR A 1 376 ? 15.723 1.533   80.639  1.00 31.39 ? 376 TYR A CG  1 
ATOM   2824 C CD1 . TYR A 1 376 ? 15.954 0.168   80.826  1.00 27.50 ? 376 TYR A CD1 1 
ATOM   2825 C CD2 . TYR A 1 376 ? 16.443 2.201   79.635  1.00 28.49 ? 376 TYR A CD2 1 
ATOM   2826 C CE1 . TYR A 1 376 ? 16.888 -0.505  80.032  1.00 27.70 ? 376 TYR A CE1 1 
ATOM   2827 C CE2 . TYR A 1 376 ? 17.370 1.545   78.855  1.00 18.69 ? 376 TYR A CE2 1 
ATOM   2828 C CZ  . TYR A 1 376 ? 17.594 0.203   79.061  1.00 22.66 ? 376 TYR A CZ  1 
ATOM   2829 O OH  . TYR A 1 376 ? 18.591 -0.396  78.363  1.00 25.80 ? 376 TYR A OH  1 
ATOM   2830 N N   . PHE A 1 377 ? 13.273 3.830   83.487  1.00 24.76 ? 377 PHE A N   1 
ATOM   2831 C CA  . PHE A 1 377 ? 12.607 5.025   84.004  1.00 27.03 ? 377 PHE A CA  1 
ATOM   2832 C C   . PHE A 1 377 ? 11.873 4.682   85.282  1.00 33.11 ? 377 PHE A C   1 
ATOM   2833 O O   . PHE A 1 377 ? 11.158 3.673   85.371  1.00 38.49 ? 377 PHE A O   1 
ATOM   2834 C CB  . PHE A 1 377 ? 11.679 5.624   82.950  1.00 20.96 ? 377 PHE A CB  1 
ATOM   2835 C CG  . PHE A 1 377 ? 12.384 5.934   81.641  1.00 18.56 ? 377 PHE A CG  1 
ATOM   2836 C CD1 . PHE A 1 377 ? 13.170 7.070   81.514  1.00 15.66 ? 377 PHE A CD1 1 
ATOM   2837 C CD2 . PHE A 1 377 ? 12.338 5.040   80.589  1.00 23.03 ? 377 PHE A CD2 1 
ATOM   2838 C CE1 . PHE A 1 377 ? 13.906 7.314   80.376  1.00 23.84 ? 377 PHE A CE1 1 
ATOM   2839 C CE2 . PHE A 1 377 ? 13.071 5.267   79.437  1.00 27.37 ? 377 PHE A CE2 1 
ATOM   2840 C CZ  . PHE A 1 377 ? 13.862 6.410   79.330  1.00 27.63 ? 377 PHE A CZ  1 
ATOM   2841 N N   . VAL A 1 378 ? 12.005 5.563   86.258  1.00 36.99 ? 378 VAL A N   1 
ATOM   2842 C CA  . VAL A 1 378 ? 11.441 5.334   87.576  1.00 37.05 ? 378 VAL A CA  1 
ATOM   2843 C C   . VAL A 1 378 ? 10.695 6.557   88.149  1.00 40.45 ? 378 VAL A C   1 
ATOM   2844 O O   . VAL A 1 378 ? 10.869 7.687   87.674  1.00 43.64 ? 378 VAL A O   1 
ATOM   2845 C CB  . VAL A 1 378 ? 12.620 4.886   88.473  1.00 33.20 ? 378 VAL A CB  1 
ATOM   2846 C CG1 . VAL A 1 378 ? 12.892 5.859   89.618  1.00 22.57 ? 378 VAL A CG1 1 
ATOM   2847 C CG2 . VAL A 1 378 ? 12.437 3.454   88.887  1.00 35.56 ? 378 VAL A CG2 1 
ATOM   2848 N N   . ASP A 1 379 ? 9.829  6.335   89.130  1.00 39.24 ? 379 ASP A N   1 
ATOM   2849 C CA  . ASP A 1 379 ? 9.104  7.442   89.726  1.00 42.78 ? 379 ASP A CA  1 
ATOM   2850 C C   . ASP A 1 379 ? 10.063 8.035   90.723  1.00 45.08 ? 379 ASP A C   1 
ATOM   2851 O O   . ASP A 1 379 ? 10.687 7.298   91.466  1.00 48.61 ? 379 ASP A O   1 
ATOM   2852 C CB  . ASP A 1 379 ? 7.860  6.927   90.457  1.00 47.17 ? 379 ASP A CB  1 
ATOM   2853 C CG  . ASP A 1 379 ? 6.978  8.050   91.042  1.00 50.46 ? 379 ASP A CG  1 
ATOM   2854 O OD1 . ASP A 1 379 ? 7.492  9.007   91.658  1.00 49.97 ? 379 ASP A OD1 1 
ATOM   2855 O OD2 . ASP A 1 379 ? 5.740  7.943   90.931  1.00 51.98 ? 379 ASP A OD2 1 
ATOM   2856 N N   . ALA A 1 380 ? 10.237 9.351   90.679  1.00 51.16 ? 380 ALA A N   1 
ATOM   2857 C CA  . ALA A 1 380 ? 11.095 10.074  91.622  1.00 56.45 ? 380 ALA A CA  1 
ATOM   2858 C C   . ALA A 1 380 ? 10.506 11.464  91.746  1.00 61.90 ? 380 ALA A C   1 
ATOM   2859 O O   . ALA A 1 380 ? 11.225 12.458  91.665  1.00 61.62 ? 380 ALA A O   1 
ATOM   2860 C CB  . ALA A 1 380 ? 12.511 10.166  91.104  1.00 57.23 ? 380 ALA A CB  1 
ATOM   2861 N N   . HIS A 1 381 ? 9.181  11.512  91.908  1.00 68.58 ? 381 HIS A N   1 
ATOM   2862 C CA  . HIS A 1 381 ? 8.420  12.762  92.020  1.00 73.39 ? 381 HIS A CA  1 
ATOM   2863 C C   . HIS A 1 381 ? 8.701  13.488  93.332  1.00 74.16 ? 381 HIS A C   1 
ATOM   2864 O O   . HIS A 1 381 ? 8.404  14.673  93.467  1.00 76.13 ? 381 HIS A O   1 
ATOM   2865 C CB  . HIS A 1 381 ? 6.910  12.493  91.894  1.00 75.46 ? 381 HIS A CB  1 
ATOM   2866 C CG  . HIS A 1 381 ? 6.479  12.011  90.538  1.00 82.34 ? 381 HIS A CG  1 
ATOM   2867 N ND1 . HIS A 1 381 ? 7.212  11.115  89.785  1.00 83.16 ? 381 HIS A ND1 1 
ATOM   2868 C CD2 . HIS A 1 381 ? 5.372  12.291  89.806  1.00 84.71 ? 381 HIS A CD2 1 
ATOM   2869 C CE1 . HIS A 1 381 ? 6.577  10.863  88.652  1.00 82.42 ? 381 HIS A CE1 1 
ATOM   2870 N NE2 . HIS A 1 381 ? 5.459  11.566  88.641  1.00 84.55 ? 381 HIS A NE2 1 
ATOM   2871 N N   . ASP B 1 11  ? 69.567 13.840  74.654  1.00 65.05 ? 11  ASP B N   1 
ATOM   2872 C CA  . ASP B 1 11  ? 68.181 13.389  74.678  1.00 63.87 ? 11  ASP B CA  1 
ATOM   2873 C C   . ASP B 1 11  ? 67.869 12.429  73.526  1.00 58.05 ? 11  ASP B C   1 
ATOM   2874 O O   . ASP B 1 11  ? 67.895 12.815  72.345  1.00 57.94 ? 11  ASP B O   1 
ATOM   2875 C CB  . ASP B 1 11  ? 67.222 14.588  74.610  1.00 72.46 ? 11  ASP B CB  1 
ATOM   2876 C CG  . ASP B 1 11  ? 65.747 14.174  74.689  1.00 78.77 ? 11  ASP B CG  1 
ATOM   2877 O OD1 . ASP B 1 11  ? 65.123 13.920  73.629  1.00 79.69 ? 11  ASP B OD1 1 
ATOM   2878 O OD2 . ASP B 1 11  ? 65.211 14.118  75.821  1.00 83.80 ? 11  ASP B OD2 1 
ATOM   2879 N N   . ASN B 1 12  ? 67.625 11.171  73.883  1.00 47.35 ? 12  ASN B N   1 
ATOM   2880 C CA  . ASN B 1 12  ? 67.258 10.147  72.916  1.00 38.26 ? 12  ASN B CA  1 
ATOM   2881 C C   . ASN B 1 12  ? 65.763 10.148  73.092  1.00 32.40 ? 12  ASN B C   1 
ATOM   2882 O O   . ASN B 1 12  ? 65.249 9.634   74.077  1.00 37.39 ? 12  ASN B O   1 
ATOM   2883 C CB  . ASN B 1 12  ? 67.826 8.787   73.313  1.00 35.06 ? 12  ASN B CB  1 
ATOM   2884 C CG  . ASN B 1 12  ? 67.330 7.674   72.424  1.00 30.66 ? 12  ASN B CG  1 
ATOM   2885 O OD1 . ASN B 1 12  ? 66.258 7.780   71.825  1.00 31.32 ? 12  ASN B OD1 1 
ATOM   2886 N ND2 . ASN B 1 12  ? 68.103 6.600   72.326  1.00 29.47 ? 12  ASN B ND2 1 
ATOM   2887 N N   . PRO B 1 13  ? 65.045 10.776  72.174  1.00 24.59 ? 13  PRO B N   1 
ATOM   2888 C CA  . PRO B 1 13  ? 63.589 10.834  72.283  1.00 23.40 ? 13  PRO B CA  1 
ATOM   2889 C C   . PRO B 1 13  ? 62.772 9.547   72.134  1.00 23.76 ? 13  PRO B C   1 
ATOM   2890 O O   . PRO B 1 13  ? 61.555 9.569   72.331  1.00 28.68 ? 13  PRO B O   1 
ATOM   2891 C CB  . PRO B 1 13  ? 63.216 11.900  71.259  1.00 24.51 ? 13  PRO B CB  1 
ATOM   2892 C CG  . PRO B 1 13  ? 64.323 11.818  70.225  1.00 20.35 ? 13  PRO B CG  1 
ATOM   2893 C CD  . PRO B 1 13  ? 65.553 11.574  71.046  1.00 21.82 ? 13  PRO B CD  1 
ATOM   2894 N N   . PHE B 1 14  ? 63.427 8.420   71.865  1.00 23.25 ? 14  PHE B N   1 
ATOM   2895 C CA  . PHE B 1 14  ? 62.715 7.151   71.691  1.00 21.12 ? 14  PHE B CA  1 
ATOM   2896 C C   . PHE B 1 14  ? 62.883 6.211   72.878  1.00 23.55 ? 14  PHE B C   1 
ATOM   2897 O O   . PHE B 1 14  ? 62.256 5.150   72.939  1.00 26.40 ? 14  PHE B O   1 
ATOM   2898 C CB  . PHE B 1 14  ? 63.179 6.438   70.416  1.00 17.79 ? 14  PHE B CB  1 
ATOM   2899 C CG  . PHE B 1 14  ? 63.215 7.320   69.197  1.00 15.75 ? 14  PHE B CG  1 
ATOM   2900 C CD1 . PHE B 1 14  ? 62.053 7.688   68.549  1.00 18.04 ? 14  PHE B CD1 1 
ATOM   2901 C CD2 . PHE B 1 14  ? 64.426 7.826   68.729  1.00 20.13 ? 14  PHE B CD2 1 
ATOM   2902 C CE1 . PHE B 1 14  ? 62.102 8.558   67.456  1.00 12.67 ? 14  PHE B CE1 1 
ATOM   2903 C CE2 . PHE B 1 14  ? 64.481 8.686   67.649  1.00 6.47  ? 14  PHE B CE2 1 
ATOM   2904 C CZ  . PHE B 1 14  ? 63.318 9.053   67.016  1.00 12.66 ? 14  PHE B CZ  1 
ATOM   2905 N N   . TYR B 1 15  ? 63.737 6.591   73.820  1.00 27.27 ? 15  TYR B N   1 
ATOM   2906 C CA  . TYR B 1 15  ? 63.987 5.771   74.997  1.00 23.49 ? 15  TYR B CA  1 
ATOM   2907 C C   . TYR B 1 15  ? 63.247 6.342   76.195  1.00 25.90 ? 15  TYR B C   1 
ATOM   2908 O O   . TYR B 1 15  ? 63.379 7.527   76.513  1.00 25.41 ? 15  TYR B O   1 
ATOM   2909 C CB  . TYR B 1 15  ? 65.489 5.713   75.279  1.00 24.24 ? 15  TYR B CB  1 
ATOM   2910 C CG  . TYR B 1 15  ? 65.837 5.121   76.633  1.00 24.79 ? 15  TYR B CG  1 
ATOM   2911 C CD1 . TYR B 1 15  ? 65.445 3.827   76.976  1.00 24.94 ? 15  TYR B CD1 1 
ATOM   2912 C CD2 . TYR B 1 15  ? 66.500 5.888   77.593  1.00 26.90 ? 15  TYR B CD2 1 
ATOM   2913 C CE1 . TYR B 1 15  ? 65.695 3.311   78.250  1.00 34.18 ? 15  TYR B CE1 1 
ATOM   2914 C CE2 . TYR B 1 15  ? 66.751 5.388   78.868  1.00 32.08 ? 15  TYR B CE2 1 
ATOM   2915 C CZ  . TYR B 1 15  ? 66.346 4.106   79.189  1.00 35.29 ? 15  TYR B CZ  1 
ATOM   2916 O OH  . TYR B 1 15  ? 66.578 3.648   80.459  1.00 43.57 ? 15  TYR B OH  1 
ATOM   2917 N N   . PHE B 1 16  ? 62.453 5.495   76.841  1.00 28.32 ? 16  PHE B N   1 
ATOM   2918 C CA  . PHE B 1 16  ? 61.681 5.869   78.023  1.00 25.61 ? 16  PHE B CA  1 
ATOM   2919 C C   . PHE B 1 16  ? 62.214 5.130   79.261  1.00 28.48 ? 16  PHE B C   1 
ATOM   2920 O O   . PHE B 1 16  ? 61.898 3.950   79.469  1.00 26.45 ? 16  PHE B O   1 
ATOM   2921 C CB  . PHE B 1 16  ? 60.204 5.516   77.818  1.00 24.22 ? 16  PHE B CB  1 
ATOM   2922 C CG  . PHE B 1 16  ? 59.467 6.478   76.941  1.00 27.06 ? 16  PHE B CG  1 
ATOM   2923 C CD1 . PHE B 1 16  ? 59.575 6.403   75.552  1.00 27.21 ? 16  PHE B CD1 1 
ATOM   2924 C CD2 . PHE B 1 16  ? 58.663 7.468   77.500  1.00 27.09 ? 16  PHE B CD2 1 
ATOM   2925 C CE1 . PHE B 1 16  ? 58.896 7.300   74.733  1.00 23.00 ? 16  PHE B CE1 1 
ATOM   2926 C CE2 . PHE B 1 16  ? 57.977 8.371   76.696  1.00 25.73 ? 16  PHE B CE2 1 
ATOM   2927 C CZ  . PHE B 1 16  ? 58.095 8.288   75.305  1.00 24.30 ? 16  PHE B CZ  1 
ATOM   2928 N N   . ASN B 1 17  ? 63.042 5.800   80.064  1.00 30.85 ? 17  ASN B N   1 
ATOM   2929 C CA  . ASN B 1 17  ? 63.584 5.172   81.276  1.00 34.88 ? 17  ASN B CA  1 
ATOM   2930 C C   . ASN B 1 17  ? 62.471 4.845   82.280  1.00 34.60 ? 17  ASN B C   1 
ATOM   2931 O O   . ASN B 1 17  ? 61.561 5.646   82.499  1.00 34.21 ? 17  ASN B O   1 
ATOM   2932 C CB  . ASN B 1 17  ? 64.615 6.072   81.945  1.00 37.81 ? 17  ASN B CB  1 
ATOM   2933 C CG  . ASN B 1 17  ? 65.128 5.490   83.244  1.00 43.04 ? 17  ASN B CG  1 
ATOM   2934 O OD1 . ASN B 1 17  ? 65.315 4.278   83.364  1.00 47.97 ? 17  ASN B OD1 1 
ATOM   2935 N ND2 . ASN B 1 17  ? 65.313 6.338   84.242  1.00 43.86 ? 17  ASN B ND2 1 
ATOM   2936 N N   . SER B 1 18  ? 62.555 3.684   82.913  1.00 36.14 ? 18  SER B N   1 
ATOM   2937 C CA  . SER B 1 18  ? 61.544 3.264   83.886  1.00 40.35 ? 18  SER B CA  1 
ATOM   2938 C C   . SER B 1 18  ? 61.502 4.193   85.101  1.00 40.53 ? 18  SER B C   1 
ATOM   2939 O O   . SER B 1 18  ? 60.441 4.422   85.670  1.00 43.03 ? 18  SER B O   1 
ATOM   2940 C CB  . SER B 1 18  ? 61.834 1.843   84.366  1.00 41.67 ? 18  SER B CB  1 
ATOM   2941 O OG  . SER B 1 18  ? 62.289 1.042   83.294  1.00 57.64 ? 18  SER B OG  1 
ATOM   2942 N N   . ASP B 1 19  ? 62.648 4.759   85.470  1.00 40.97 ? 19  ASP B N   1 
ATOM   2943 C CA  . ASP B 1 19  ? 62.721 5.640   86.621  1.00 41.40 ? 19  ASP B CA  1 
ATOM   2944 C C   . ASP B 1 19  ? 61.987 6.952   86.448  1.00 40.22 ? 19  ASP B C   1 
ATOM   2945 O O   . ASP B 1 19  ? 62.047 7.798   87.317  1.00 43.61 ? 19  ASP B O   1 
ATOM   2946 C CB  . ASP B 1 19  ? 64.175 5.906   87.004  1.00 49.08 ? 19  ASP B CB  1 
ATOM   2947 C CG  . ASP B 1 19  ? 64.838 4.697   87.662  1.00 59.05 ? 19  ASP B CG  1 
ATOM   2948 O OD1 . ASP B 1 19  ? 64.551 4.426   88.851  1.00 63.84 ? 19  ASP B OD1 1 
ATOM   2949 O OD2 . ASP B 1 19  ? 65.655 4.018   86.998  1.00 60.32 ? 19  ASP B OD2 1 
ATOM   2950 N N   . ASN B 1 20  ? 61.279 7.125   85.341  1.00 42.75 ? 20  ASN B N   1 
ATOM   2951 C CA  . ASN B 1 20  ? 60.551 8.366   85.113  1.00 45.92 ? 20  ASN B CA  1 
ATOM   2952 C C   . ASN B 1 20  ? 59.228 8.153   84.415  1.00 45.97 ? 20  ASN B C   1 
ATOM   2953 O O   . ASN B 1 20  ? 58.209 8.738   84.787  1.00 52.21 ? 20  ASN B O   1 
ATOM   2954 C CB  . ASN B 1 20  ? 61.332 9.307   84.200  1.00 50.51 ? 20  ASN B CB  1 
ATOM   2955 C CG  . ASN B 1 20  ? 62.763 9.431   84.582  1.00 56.08 ? 20  ASN B CG  1 
ATOM   2956 O OD1 . ASN B 1 20  ? 63.593 8.632   84.151  1.00 61.71 ? 20  ASN B OD1 1 
ATOM   2957 N ND2 . ASN B 1 20  ? 63.081 10.442  85.387  1.00 61.86 ? 20  ASN B ND2 1 
ATOM   2958 N N   . SER B 1 21  ? 59.266 7.344   83.367  1.00 39.45 ? 21  SER B N   1 
ATOM   2959 C CA  . SER B 1 21  ? 58.113 7.107   82.530  1.00 34.11 ? 21  SER B CA  1 
ATOM   2960 C C   . SER B 1 21  ? 56.805 6.500   83.038  1.00 33.91 ? 21  SER B C   1 
ATOM   2961 O O   . SER B 1 21  ? 55.748 6.826   82.512  1.00 36.83 ? 21  SER B O   1 
ATOM   2962 C CB  . SER B 1 21  ? 58.606 6.416   81.283  1.00 32.17 ? 21  SER B CB  1 
ATOM   2963 O OG  . SER B 1 21  ? 59.652 7.198   80.720  1.00 33.20 ? 21  SER B OG  1 
ATOM   2964 N N   . TRP B 1 22  ? 56.852 5.645   84.049  1.00 34.55 ? 22  TRP B N   1 
ATOM   2965 C CA  . TRP B 1 22  ? 55.635 5.025   84.571  1.00 32.22 ? 22  TRP B CA  1 
ATOM   2966 C C   . TRP B 1 22  ? 55.031 5.841   85.717  1.00 36.15 ? 22  TRP B C   1 
ATOM   2967 O O   . TRP B 1 22  ? 55.748 6.491   86.459  1.00 39.67 ? 22  TRP B O   1 
ATOM   2968 C CB  . TRP B 1 22  ? 55.942 3.608   85.054  1.00 25.16 ? 22  TRP B CB  1 
ATOM   2969 C CG  . TRP B 1 22  ? 56.404 2.678   83.981  1.00 23.75 ? 22  TRP B CG  1 
ATOM   2970 C CD1 . TRP B 1 22  ? 57.692 2.399   83.637  1.00 23.25 ? 22  TRP B CD1 1 
ATOM   2971 C CD2 . TRP B 1 22  ? 55.579 1.877   83.133  1.00 23.31 ? 22  TRP B CD2 1 
ATOM   2972 N NE1 . TRP B 1 22  ? 57.721 1.468   82.627  1.00 28.72 ? 22  TRP B NE1 1 
ATOM   2973 C CE2 . TRP B 1 22  ? 56.434 1.135   82.301  1.00 26.85 ? 22  TRP B CE2 1 
ATOM   2974 C CE3 . TRP B 1 22  ? 54.198 1.712   83.004  1.00 24.53 ? 22  TRP B CE3 1 
ATOM   2975 C CZ2 . TRP B 1 22  ? 55.949 0.240   81.353  1.00 22.62 ? 22  TRP B CZ2 1 
ATOM   2976 C CZ3 . TRP B 1 22  ? 53.720 0.828   82.069  1.00 21.54 ? 22  TRP B CZ3 1 
ATOM   2977 C CH2 . TRP B 1 22  ? 54.593 0.102   81.253  1.00 22.86 ? 22  TRP B CH2 1 
ATOM   2978 N N   . ASN B 1 23  ? 53.717 5.779   85.877  1.00 38.01 ? 23  ASN B N   1 
ATOM   2979 C CA  . ASN B 1 23  ? 53.040 6.519   86.927  1.00 37.66 ? 23  ASN B CA  1 
ATOM   2980 C C   . ASN B 1 23  ? 52.219 5.566   87.744  1.00 39.67 ? 23  ASN B C   1 
ATOM   2981 O O   . ASN B 1 23  ? 51.381 4.856   87.213  1.00 40.27 ? 23  ASN B O   1 
ATOM   2982 C CB  . ASN B 1 23  ? 52.123 7.580   86.337  1.00 47.61 ? 23  ASN B CB  1 
ATOM   2983 C CG  . ASN B 1 23  ? 52.875 8.816   85.898  1.00 58.18 ? 23  ASN B CG  1 
ATOM   2984 O OD1 . ASN B 1 23  ? 53.275 8.945   84.737  1.00 66.50 ? 23  ASN B OD1 1 
ATOM   2985 N ND2 . ASN B 1 23  ? 53.048 9.753   86.824  1.00 64.75 ? 23  ASN B ND2 1 
ATOM   2986 N N   . THR B 1 24  ? 52.445 5.564   89.049  1.00 40.70 ? 24  THR B N   1 
ATOM   2987 C CA  . THR B 1 24  ? 51.735 4.671   89.935  1.00 39.45 ? 24  THR B CA  1 
ATOM   2988 C C   . THR B 1 24  ? 50.299 5.106   90.001  1.00 38.39 ? 24  THR B C   1 
ATOM   2989 O O   . THR B 1 24  ? 50.023 6.285   90.183  1.00 41.17 ? 24  THR B O   1 
ATOM   2990 C CB  . THR B 1 24  ? 52.298 4.742   91.362  1.00 44.20 ? 24  THR B CB  1 
ATOM   2991 O OG1 . THR B 1 24  ? 53.705 5.026   91.310  1.00 52.14 ? 24  THR B OG1 1 
ATOM   2992 C CG2 . THR B 1 24  ? 52.068 3.418   92.095  1.00 41.64 ? 24  THR B CG2 1 
ATOM   2993 N N   . LEU B 1 25  ? 49.392 4.159   89.815  1.00 34.58 ? 25  LEU B N   1 
ATOM   2994 C CA  . LEU B 1 25  ? 47.968 4.429   89.895  1.00 32.37 ? 25  LEU B CA  1 
ATOM   2995 C C   . LEU B 1 25  ? 47.493 3.765   91.198  1.00 33.03 ? 25  LEU B C   1 
ATOM   2996 O O   . LEU B 1 25  ? 46.752 4.346   91.978  1.00 33.20 ? 25  LEU B O   1 
ATOM   2997 C CB  . LEU B 1 25  ? 47.248 3.853   88.671  1.00 32.74 ? 25  LEU B CB  1 
ATOM   2998 C CG  . LEU B 1 25  ? 45.787 4.255   88.490  1.00 33.64 ? 25  LEU B CG  1 
ATOM   2999 C CD1 . LEU B 1 25  ? 45.684 5.760   88.260  1.00 36.22 ? 25  LEU B CD1 1 
ATOM   3000 C CD2 . LEU B 1 25  ? 45.179 3.497   87.336  1.00 34.60 ? 25  LEU B CD2 1 
ATOM   3001 N N   . PHE B 1 26  ? 47.950 2.546   91.441  1.00 32.49 ? 26  PHE B N   1 
ATOM   3002 C CA  . PHE B 1 26  ? 47.586 1.842   92.652  1.00 32.68 ? 26  PHE B CA  1 
ATOM   3003 C C   . PHE B 1 26  ? 48.704 0.916   93.079  1.00 33.85 ? 26  PHE B C   1 
ATOM   3004 O O   . PHE B 1 26  ? 49.492 0.462   92.243  1.00 33.70 ? 26  PHE B O   1 
ATOM   3005 C CB  . PHE B 1 26  ? 46.296 1.046   92.489  1.00 31.97 ? 26  PHE B CB  1 
ATOM   3006 C CG  . PHE B 1 26  ? 45.872 0.335   93.751  1.00 31.30 ? 26  PHE B CG  1 
ATOM   3007 C CD1 . PHE B 1 26  ? 45.207 1.036   94.769  1.00 26.13 ? 26  PHE B CD1 1 
ATOM   3008 C CD2 . PHE B 1 26  ? 46.181 -1.016  93.943  1.00 24.60 ? 26  PHE B CD2 1 
ATOM   3009 C CE1 . PHE B 1 26  ? 44.859 0.411   95.955  1.00 22.04 ? 26  PHE B CE1 1 
ATOM   3010 C CE2 . PHE B 1 26  ? 45.841 -1.647  95.123  1.00 29.57 ? 26  PHE B CE2 1 
ATOM   3011 C CZ  . PHE B 1 26  ? 45.172 -0.925  96.143  1.00 25.54 ? 26  PHE B CZ  1 
ATOM   3012 N N   . LYS B 1 27  ? 48.754 0.634   94.381  1.00 33.21 ? 27  LYS B N   1 
ATOM   3013 C CA  . LYS B 1 27  ? 49.783 -0.223  94.955  1.00 33.69 ? 27  LYS B CA  1 
ATOM   3014 C C   . LYS B 1 27  ? 49.429 -0.549  96.403  1.00 34.14 ? 27  LYS B C   1 
ATOM   3015 O O   . LYS B 1 27  ? 48.891 0.294   97.126  1.00 37.58 ? 27  LYS B O   1 
ATOM   3016 C CB  . LYS B 1 27  ? 51.110 0.532   94.942  1.00 34.96 ? 27  LYS B CB  1 
ATOM   3017 C CG  . LYS B 1 27  ? 52.335 -0.308  95.155  1.00 37.43 ? 27  LYS B CG  1 
ATOM   3018 C CD  . LYS B 1 27  ? 53.503 0.598   95.404  1.00 40.27 ? 27  LYS B CD  1 
ATOM   3019 C CE  . LYS B 1 27  ? 54.792 -0.162  95.321  1.00 48.33 ? 27  LYS B CE  1 
ATOM   3020 N NZ  . LYS B 1 27  ? 55.921 0.701   95.770  1.00 55.83 ? 27  LYS B NZ  1 
ATOM   3021 N N   . ASN B 1 28  ? 49.693 -1.779  96.814  1.00 30.47 ? 28  ASN B N   1 
ATOM   3022 C CA  . ASN B 1 28  ? 49.450 -2.208  98.188  1.00 31.61 ? 28  ASN B CA  1 
ATOM   3023 C C   . ASN B 1 28  ? 50.266 -3.464  98.350  1.00 32.84 ? 28  ASN B C   1 
ATOM   3024 O O   . ASN B 1 28  ? 51.005 -3.826  97.444  1.00 37.66 ? 28  ASN B O   1 
ATOM   3025 C CB  . ASN B 1 28  ? 47.957 -2.434  98.495  1.00 32.12 ? 28  ASN B CB  1 
ATOM   3026 C CG  . ASN B 1 28  ? 47.350 -3.614  97.750  1.00 34.68 ? 28  ASN B CG  1 
ATOM   3027 O OD1 . ASN B 1 28  ? 48.043 -4.517  97.298  1.00 35.66 ? 28  ASN B OD1 1 
ATOM   3028 N ND2 . ASN B 1 28  ? 46.029 -3.624  97.661  1.00 33.89 ? 28  ASN B ND2 1 
ATOM   3029 N N   . GLN B 1 29  ? 50.173 -4.128  99.488  1.00 36.12 ? 29  GLN B N   1 
ATOM   3030 C CA  . GLN B 1 29  ? 50.967 -5.335  99.682  1.00 39.09 ? 29  GLN B CA  1 
ATOM   3031 C C   . GLN B 1 29  ? 50.756 -6.440  98.642  1.00 37.60 ? 29  GLN B C   1 
ATOM   3032 O O   . GLN B 1 29  ? 51.658 -7.248  98.414  1.00 37.26 ? 29  GLN B O   1 
ATOM   3033 C CB  . GLN B 1 29  ? 50.779 -5.902  101.095 1.00 50.72 ? 29  GLN B CB  1 
ATOM   3034 C CG  . GLN B 1 29  ? 49.357 -5.858  101.649 1.00 66.14 ? 29  GLN B CG  1 
ATOM   3035 C CD  . GLN B 1 29  ? 49.019 -4.506  102.267 1.00 77.38 ? 29  GLN B CD  1 
ATOM   3036 O OE1 . GLN B 1 29  ? 48.498 -3.610  101.592 1.00 79.49 ? 29  GLN B OE1 1 
ATOM   3037 N NE2 . GLN B 1 29  ? 49.329 -4.349  103.554 1.00 82.30 ? 29  GLN B NE2 1 
ATOM   3038 N N   . TYR B 1 30  ? 49.585 -6.452  98.003  1.00 34.67 ? 30  TYR B N   1 
ATOM   3039 C CA  . TYR B 1 30  ? 49.222 -7.471  97.015  1.00 32.95 ? 30  TYR B CA  1 
ATOM   3040 C C   . TYR B 1 30  ? 49.499 -7.231  95.532  1.00 33.77 ? 30  TYR B C   1 
ATOM   3041 O O   . TYR B 1 30  ? 49.327 -8.151  94.727  1.00 34.45 ? 30  TYR B O   1 
ATOM   3042 C CB  . TYR B 1 30  ? 47.758 -7.819  97.170  1.00 34.11 ? 30  TYR B CB  1 
ATOM   3043 C CG  . TYR B 1 30  ? 47.464 -8.433  98.491  1.00 38.92 ? 30  TYR B CG  1 
ATOM   3044 C CD1 . TYR B 1 30  ? 47.893 -9.718  98.778  1.00 44.82 ? 30  TYR B CD1 1 
ATOM   3045 C CD2 . TYR B 1 30  ? 46.770 -7.735  99.462  1.00 42.15 ? 30  TYR B CD2 1 
ATOM   3046 C CE1 . TYR B 1 30  ? 47.641 -10.303 99.999  1.00 50.42 ? 30  TYR B CE1 1 
ATOM   3047 C CE2 . TYR B 1 30  ? 46.509 -8.310  100.699 1.00 52.05 ? 30  TYR B CE2 1 
ATOM   3048 C CZ  . TYR B 1 30  ? 46.947 -9.597  100.957 1.00 53.21 ? 30  TYR B CZ  1 
ATOM   3049 O OH  . TYR B 1 30  ? 46.681 -10.199 102.161 1.00 65.59 ? 30  TYR B OH  1 
ATOM   3050 N N   . GLY B 1 31  ? 49.874 -6.007  95.166  1.00 30.86 ? 31  GLY B N   1 
ATOM   3051 C CA  . GLY B 1 31  ? 50.162 -5.703  93.784  1.00 25.31 ? 31  GLY B CA  1 
ATOM   3052 C C   . GLY B 1 31  ? 50.155 -4.222  93.481  1.00 27.08 ? 31  GLY B C   1 
ATOM   3053 O O   . GLY B 1 31  ? 49.993 -3.390  94.384  1.00 26.64 ? 31  GLY B O   1 
ATOM   3054 N N   . HIS B 1 32  ? 50.274 -3.892  92.196  1.00 27.78 ? 32  HIS B N   1 
ATOM   3055 C CA  . HIS B 1 32  ? 50.303 -2.500  91.746  1.00 28.04 ? 32  HIS B CA  1 
ATOM   3056 C C   . HIS B 1 32  ? 49.850 -2.319  90.299  1.00 28.16 ? 32  HIS B C   1 
ATOM   3057 O O   . HIS B 1 32  ? 49.911 -3.269  89.505  1.00 26.29 ? 32  HIS B O   1 
ATOM   3058 C CB  . HIS B 1 32  ? 51.726 -1.935  91.895  1.00 27.53 ? 32  HIS B CB  1 
ATOM   3059 C CG  . HIS B 1 32  ? 52.749 -2.594  91.016  1.00 28.74 ? 32  HIS B CG  1 
ATOM   3060 N ND1 . HIS B 1 32  ? 52.643 -2.627  89.638  1.00 31.47 ? 32  HIS B ND1 1 
ATOM   3061 C CD2 . HIS B 1 32  ? 53.913 -3.221  91.314  1.00 23.98 ? 32  HIS B CD2 1 
ATOM   3062 C CE1 . HIS B 1 32  ? 53.698 -3.244  89.130  1.00 32.47 ? 32  HIS B CE1 1 
ATOM   3063 N NE2 . HIS B 1 32  ? 54.482 -3.611  90.126  1.00 31.10 ? 32  HIS B NE2 1 
ATOM   3064 N N   . ILE B 1 33  ? 49.476 -1.077  89.959  1.00 32.04 ? 33  ILE B N   1 
ATOM   3065 C CA  . ILE B 1 33  ? 49.047 -0.656  88.605  1.00 28.38 ? 33  ILE B CA  1 
ATOM   3066 C C   . ILE B 1 33  ? 49.736 0.679   88.270  1.00 30.20 ? 33  ILE B C   1 
ATOM   3067 O O   . ILE B 1 33  ? 49.640 1.642   89.046  1.00 28.89 ? 33  ILE B O   1 
ATOM   3068 C CB  . ILE B 1 33  ? 47.536 -0.364  88.515  1.00 25.47 ? 33  ILE B CB  1 
ATOM   3069 C CG1 . ILE B 1 33  ? 46.704 -1.529  89.069  1.00 19.64 ? 33  ILE B CG1 1 
ATOM   3070 C CG2 . ILE B 1 33  ? 47.178 -0.040  87.065  1.00 28.17 ? 33  ILE B CG2 1 
ATOM   3071 C CD1 . ILE B 1 33  ? 45.191 -1.248  89.125  1.00 16.77 ? 33  ILE B CD1 1 
ATOM   3072 N N   . ARG B 1 34  ? 50.392 0.748   87.115  1.00 28.21 ? 34  ARG B N   1 
ATOM   3073 C CA  . ARG B 1 34  ? 51.098 1.957   86.669  1.00 28.36 ? 34  ARG B CA  1 
ATOM   3074 C C   . ARG B 1 34  ? 50.753 2.195   85.191  1.00 29.68 ? 34  ARG B C   1 
ATOM   3075 O O   . ARG B 1 34  ? 50.527 1.239   84.447  1.00 28.14 ? 34  ARG B O   1 
ATOM   3076 C CB  . ARG B 1 34  ? 52.633 1.775   86.752  1.00 29.48 ? 34  ARG B CB  1 
ATOM   3077 C CG  . ARG B 1 34  ? 53.230 1.418   88.095  1.00 30.58 ? 34  ARG B CG  1 
ATOM   3078 C CD  . ARG B 1 34  ? 54.228 0.293   87.934  1.00 34.74 ? 34  ARG B CD  1 
ATOM   3079 N NE  . ARG B 1 34  ? 55.640 0.684   87.961  1.00 47.37 ? 34  ARG B NE  1 
ATOM   3080 C CZ  . ARG B 1 34  ? 56.540 0.347   87.024  1.00 52.90 ? 34  ARG B CZ  1 
ATOM   3081 N NH1 . ARG B 1 34  ? 56.169 -0.372  85.964  1.00 48.46 ? 34  ARG B NH1 1 
ATOM   3082 N NH2 . ARG B 1 34  ? 57.834 0.667   87.176  1.00 49.22 ? 34  ARG B NH2 1 
ATOM   3083 N N   . VAL B 1 35  ? 50.762 3.454   84.759  1.00 28.78 ? 35  VAL B N   1 
ATOM   3084 C CA  . VAL B 1 35  ? 50.479 3.804   83.360  1.00 29.78 ? 35  VAL B CA  1 
ATOM   3085 C C   . VAL B 1 35  ? 51.714 4.523   82.800  1.00 28.45 ? 35  VAL B C   1 
ATOM   3086 O O   . VAL B 1 35  ? 52.417 5.208   83.539  1.00 30.54 ? 35  VAL B O   1 
ATOM   3087 C CB  . VAL B 1 35  ? 49.231 4.748   83.246  1.00 26.38 ? 35  VAL B CB  1 
ATOM   3088 C CG1 . VAL B 1 35  ? 49.001 5.159   81.835  1.00 34.75 ? 35  VAL B CG1 1 
ATOM   3089 C CG2 . VAL B 1 35  ? 48.004 4.040   83.712  1.00 32.69 ? 35  VAL B CG2 1 
ATOM   3090 N N   . LEU B 1 36  ? 52.043 4.301   81.534  1.00 29.09 ? 36  LEU B N   1 
ATOM   3091 C CA  . LEU B 1 36  ? 53.182 4.998   80.957  1.00 26.76 ? 36  LEU B CA  1 
ATOM   3092 C C   . LEU B 1 36  ? 52.693 6.373   80.485  1.00 23.59 ? 36  LEU B C   1 
ATOM   3093 O O   . LEU B 1 36  ? 51.518 6.560   80.172  1.00 19.50 ? 36  LEU B O   1 
ATOM   3094 C CB  . LEU B 1 36  ? 53.802 4.181   79.815  1.00 31.48 ? 36  LEU B CB  1 
ATOM   3095 C CG  . LEU B 1 36  ? 54.893 4.763   78.890  1.00 36.01 ? 36  LEU B CG  1 
ATOM   3096 C CD1 . LEU B 1 36  ? 56.053 5.253   79.668  1.00 36.81 ? 36  LEU B CD1 1 
ATOM   3097 C CD2 . LEU B 1 36  ? 55.358 3.750   77.849  1.00 36.07 ? 36  LEU B CD2 1 
ATOM   3098 N N   . GLN B 1 37  ? 53.577 7.356   80.547  1.00 25.32 ? 37  GLN B N   1 
ATOM   3099 C CA  . GLN B 1 37  ? 53.272 8.716   80.132  1.00 24.41 ? 37  GLN B CA  1 
ATOM   3100 C C   . GLN B 1 37  ? 53.055 8.869   78.617  1.00 25.63 ? 37  GLN B C   1 
ATOM   3101 O O   . GLN B 1 37  ? 53.690 8.175   77.817  1.00 24.64 ? 37  GLN B O   1 
ATOM   3102 C CB  . GLN B 1 37  ? 54.423 9.619   80.538  1.00 23.37 ? 37  GLN B CB  1 
ATOM   3103 C CG  . GLN B 1 37  ? 55.740 9.213   79.925  1.00 26.07 ? 37  GLN B CG  1 
ATOM   3104 C CD  . GLN B 1 37  ? 56.743 10.329  79.959  1.00 32.59 ? 37  GLN B CD  1 
ATOM   3105 O OE1 . GLN B 1 37  ? 57.019 10.968  78.943  1.00 36.78 ? 37  GLN B OE1 1 
ATOM   3106 N NE2 . GLN B 1 37  ? 57.280 10.599  81.140  1.00 43.16 ? 37  GLN B NE2 1 
ATOM   3107 N N   . ARG B 1 38  ? 52.202 9.826   78.242  1.00 26.74 ? 38  ARG B N   1 
ATOM   3108 C CA  . ARG B 1 38  ? 51.904 10.142  76.841  1.00 20.41 ? 38  ARG B CA  1 
ATOM   3109 C C   . ARG B 1 38  ? 53.197 10.188  76.048  1.00 21.30 ? 38  ARG B C   1 
ATOM   3110 O O   . ARG B 1 38  ? 54.170 10.813  76.456  1.00 23.57 ? 38  ARG B O   1 
ATOM   3111 C CB  . ARG B 1 38  ? 51.243 11.519  76.710  1.00 12.81 ? 38  ARG B CB  1 
ATOM   3112 C CG  . ARG B 1 38  ? 50.002 11.708  77.546  1.00 20.54 ? 38  ARG B CG  1 
ATOM   3113 C CD  . ARG B 1 38  ? 48.805 11.990  76.695  1.00 16.72 ? 38  ARG B CD  1 
ATOM   3114 N NE  . ARG B 1 38  ? 48.442 13.399  76.648  1.00 22.22 ? 38  ARG B NE  1 
ATOM   3115 C CZ  . ARG B 1 38  ? 48.428 14.127  75.540  1.00 30.04 ? 38  ARG B CZ  1 
ATOM   3116 N NH1 . ARG B 1 38  ? 48.831 13.623  74.388  1.00 36.10 ? 38  ARG B NH1 1 
ATOM   3117 N NH2 . ARG B 1 38  ? 48.070 15.391  75.591  1.00 40.87 ? 38  ARG B NH2 1 
ATOM   3118 N N   . PHE B 1 39  ? 53.175 9.563   74.882  1.00 25.84 ? 39  PHE B N   1 
ATOM   3119 C CA  . PHE B 1 39  ? 54.332 9.516   74.004  1.00 23.81 ? 39  PHE B CA  1 
ATOM   3120 C C   . PHE B 1 39  ? 54.609 10.873  73.403  1.00 23.47 ? 39  PHE B C   1 
ATOM   3121 O O   . PHE B 1 39  ? 55.733 11.363  73.454  1.00 22.36 ? 39  PHE B O   1 
ATOM   3122 C CB  . PHE B 1 39  ? 54.089 8.526   72.864  1.00 21.94 ? 39  PHE B CB  1 
ATOM   3123 C CG  . PHE B 1 39  ? 53.970 7.105   73.307  1.00 14.13 ? 39  PHE B CG  1 
ATOM   3124 C CD1 . PHE B 1 39  ? 55.097 6.334   73.485  1.00 14.36 ? 39  PHE B CD1 1 
ATOM   3125 C CD2 . PHE B 1 39  ? 52.728 6.530   73.492  1.00 16.73 ? 39  PHE B CD2 1 
ATOM   3126 C CE1 . PHE B 1 39  ? 54.994 5.002   73.836  1.00 20.01 ? 39  PHE B CE1 1 
ATOM   3127 C CE2 . PHE B 1 39  ? 52.605 5.197   73.844  1.00 14.15 ? 39  PHE B CE2 1 
ATOM   3128 C CZ  . PHE B 1 39  ? 53.736 4.432   74.016  1.00 18.99 ? 39  PHE B CZ  1 
ATOM   3129 N N   . ASP B 1 40  ? 53.574 11.472  72.830  1.00 26.75 ? 40  ASP B N   1 
ATOM   3130 C CA  . ASP B 1 40  ? 53.697 12.766  72.166  1.00 31.76 ? 40  ASP B CA  1 
ATOM   3131 C C   . ASP B 1 40  ? 54.116 13.906  73.089  1.00 33.68 ? 40  ASP B C   1 
ATOM   3132 O O   . ASP B 1 40  ? 54.527 14.984  72.634  1.00 35.84 ? 40  ASP B O   1 
ATOM   3133 C CB  . ASP B 1 40  ? 52.396 13.116  71.442  1.00 28.53 ? 40  ASP B CB  1 
ATOM   3134 C CG  . ASP B 1 40  ? 51.222 13.222  72.379  1.00 34.17 ? 40  ASP B CG  1 
ATOM   3135 O OD1 . ASP B 1 40  ? 51.149 12.424  73.338  1.00 27.47 ? 40  ASP B OD1 1 
ATOM   3136 O OD2 . ASP B 1 40  ? 50.377 14.120  72.166  1.00 41.33 ? 40  ASP B OD2 1 
ATOM   3137 N N   . GLN B 1 41  ? 54.030 13.675  74.389  1.00 35.42 ? 41  GLN B N   1 
ATOM   3138 C CA  . GLN B 1 41  ? 54.404 14.722  75.310  1.00 37.90 ? 41  GLN B CA  1 
ATOM   3139 C C   . GLN B 1 41  ? 55.900 14.729  75.453  1.00 38.81 ? 41  GLN B C   1 
ATOM   3140 O O   . GLN B 1 41  ? 56.492 15.786  75.675  1.00 40.60 ? 41  GLN B O   1 
ATOM   3141 C CB  . GLN B 1 41  ? 53.688 14.574  76.646  1.00 42.49 ? 41  GLN B CB  1 
ATOM   3142 C CG  . GLN B 1 41  ? 52.899 15.840  77.030  1.00 49.17 ? 41  GLN B CG  1 
ATOM   3143 C CD  . GLN B 1 41  ? 51.725 16.179  76.091  1.00 52.29 ? 41  GLN B CD  1 
ATOM   3144 O OE1 . GLN B 1 41  ? 50.579 16.250  76.531  1.00 52.99 ? 41  GLN B OE1 1 
ATOM   3145 N NE2 . GLN B 1 41  ? 52.018 16.442  74.815  1.00 50.45 ? 41  GLN B NE2 1 
ATOM   3146 N N   . GLN B 1 42  ? 56.500 13.550  75.277  1.00 39.27 ? 42  GLN B N   1 
ATOM   3147 C CA  . GLN B 1 42  ? 57.953 13.371  75.326  1.00 36.02 ? 42  GLN B CA  1 
ATOM   3148 C C   . GLN B 1 42  ? 58.573 13.996  74.075  1.00 32.44 ? 42  GLN B C   1 
ATOM   3149 O O   . GLN B 1 42  ? 59.603 14.652  74.134  1.00 32.70 ? 42  GLN B O   1 
ATOM   3150 C CB  . GLN B 1 42  ? 58.307 11.875  75.375  1.00 36.92 ? 42  GLN B CB  1 
ATOM   3151 C CG  . GLN B 1 42  ? 59.750 11.539  74.944  1.00 42.34 ? 42  GLN B CG  1 
ATOM   3152 C CD  . GLN B 1 42  ? 60.476 10.607  75.913  1.00 44.13 ? 42  GLN B CD  1 
ATOM   3153 O OE1 . GLN B 1 42  ? 60.369 10.752  77.129  1.00 49.21 ? 42  GLN B OE1 1 
ATOM   3154 N NE2 . GLN B 1 42  ? 61.224 9.654   75.374  1.00 42.55 ? 42  GLN B NE2 1 
ATOM   3155 N N   . SER B 1 43  ? 57.903 13.839  72.949  1.00 33.52 ? 43  SER B N   1 
ATOM   3156 C CA  . SER B 1 43  ? 58.422 14.358  71.708  1.00 33.97 ? 43  SER B CA  1 
ATOM   3157 C C   . SER B 1 43  ? 57.311 14.442  70.704  1.00 34.07 ? 43  SER B C   1 
ATOM   3158 O O   . SER B 1 43  ? 56.469 13.548  70.630  1.00 35.36 ? 43  SER B O   1 
ATOM   3159 C CB  . SER B 1 43  ? 59.485 13.402  71.172  1.00 31.95 ? 43  SER B CB  1 
ATOM   3160 O OG  . SER B 1 43  ? 60.076 13.916  69.995  1.00 37.38 ? 43  SER B OG  1 
ATOM   3161 N N   . LYS B 1 44  ? 57.351 15.492  69.890  1.00 35.50 ? 44  LYS B N   1 
ATOM   3162 C CA  . LYS B 1 44  ? 56.355 15.701  68.836  1.00 35.42 ? 44  LYS B CA  1 
ATOM   3163 C C   . LYS B 1 44  ? 56.655 14.789  67.631  1.00 29.93 ? 44  LYS B C   1 
ATOM   3164 O O   . LYS B 1 44  ? 55.823 14.617  66.751  1.00 31.17 ? 44  LYS B O   1 
ATOM   3165 C CB  . LYS B 1 44  ? 56.306 17.189  68.445  1.00 36.09 ? 44  LYS B CB  1 
ATOM   3166 C CG  . LYS B 1 44  ? 54.907 17.817  68.535  1.00 41.84 ? 44  LYS B CG  1 
ATOM   3167 C CD  . LYS B 1 44  ? 54.028 17.069  69.540  1.00 50.60 ? 44  LYS B CD  1 
ATOM   3168 C CE  . LYS B 1 44  ? 52.542 17.181  69.189  1.00 56.20 ? 44  LYS B CE  1 
ATOM   3169 N NZ  . LYS B 1 44  ? 51.709 16.120  69.837  1.00 55.74 ? 44  LYS B NZ  1 
ATOM   3170 N N   . ARG B 1 45  ? 57.831 14.161  67.658  1.00 31.31 ? 45  ARG B N   1 
ATOM   3171 C CA  . ARG B 1 45  ? 58.293 13.230  66.629  1.00 29.30 ? 45  ARG B CA  1 
ATOM   3172 C C   . ARG B 1 45  ? 57.546 11.921  66.792  1.00 29.66 ? 45  ARG B C   1 
ATOM   3173 O O   . ARG B 1 45  ? 57.625 11.023  65.946  1.00 31.46 ? 45  ARG B O   1 
ATOM   3174 C CB  . ARG B 1 45  ? 59.768 12.926  66.825  1.00 25.63 ? 45  ARG B CB  1 
ATOM   3175 C CG  . ARG B 1 45  ? 60.670 14.107  66.705  1.00 32.91 ? 45  ARG B CG  1 
ATOM   3176 C CD  . ARG B 1 45  ? 62.042 13.738  67.220  1.00 39.21 ? 45  ARG B CD  1 
ATOM   3177 N NE  . ARG B 1 45  ? 62.804 12.988  66.242  1.00 39.58 ? 45  ARG B NE  1 
ATOM   3178 C CZ  . ARG B 1 45  ? 64.092 13.192  66.008  1.00 42.32 ? 45  ARG B CZ  1 
ATOM   3179 N NH1 . ARG B 1 45  ? 64.752 14.110  66.704  1.00 43.10 ? 45  ARG B NH1 1 
ATOM   3180 N NH2 . ARG B 1 45  ? 64.692 12.560  65.004  1.00 42.36 ? 45  ARG B NH2 1 
ATOM   3181 N N   . LEU B 1 46  ? 56.895 11.786  67.936  1.00 30.43 ? 46  LEU B N   1 
ATOM   3182 C CA  . LEU B 1 46  ? 56.120 10.604  68.260  1.00 30.60 ? 46  LEU B CA  1 
ATOM   3183 C C   . LEU B 1 46  ? 54.646 10.991  68.296  1.00 32.32 ? 46  LEU B C   1 
ATOM   3184 O O   . LEU B 1 46  ? 53.883 10.436  69.097  1.00 36.07 ? 46  LEU B O   1 
ATOM   3185 C CB  . LEU B 1 46  ? 56.545 10.083  69.639  1.00 30.47 ? 46  LEU B CB  1 
ATOM   3186 C CG  . LEU B 1 46  ? 57.537 8.924   69.808  1.00 25.38 ? 46  LEU B CG  1 
ATOM   3187 C CD1 . LEU B 1 46  ? 58.429 8.765   68.603  1.00 17.46 ? 46  LEU B CD1 1 
ATOM   3188 C CD2 . LEU B 1 46  ? 58.346 9.167   71.058  1.00 12.51 ? 46  LEU B CD2 1 
ATOM   3189 N N   . GLN B 1 47  ? 54.230 11.935  67.449  1.00 30.88 ? 47  GLN B N   1 
ATOM   3190 C CA  . GLN B 1 47  ? 52.834 12.334  67.487  1.00 32.49 ? 47  GLN B CA  1 
ATOM   3191 C C   . GLN B 1 47  ? 51.874 11.329  66.938  1.00 31.80 ? 47  GLN B C   1 
ATOM   3192 O O   . GLN B 1 47  ? 50.719 11.321  67.337  1.00 34.12 ? 47  GLN B O   1 
ATOM   3193 C CB  . GLN B 1 47  ? 52.559 13.740  66.950  1.00 32.15 ? 47  GLN B CB  1 
ATOM   3194 C CG  . GLN B 1 47  ? 52.810 14.006  65.501  1.00 38.32 ? 47  GLN B CG  1 
ATOM   3195 C CD  . GLN B 1 47  ? 52.627 15.489  65.175  1.00 46.73 ? 47  GLN B CD  1 
ATOM   3196 O OE1 . GLN B 1 47  ? 52.433 15.867  64.023  1.00 51.57 ? 47  GLN B OE1 1 
ATOM   3197 N NE2 . GLN B 1 47  ? 52.699 16.334  66.196  1.00 50.40 ? 47  GLN B NE2 1 
ATOM   3198 N N   . ASN B 1 48  ? 52.341 10.404  66.118  1.00 32.47 ? 48  ASN B N   1 
ATOM   3199 C CA  . ASN B 1 48  ? 51.403 9.416   65.636  1.00 34.27 ? 48  ASN B CA  1 
ATOM   3200 C C   . ASN B 1 48  ? 51.115 8.328   66.673  1.00 37.85 ? 48  ASN B C   1 
ATOM   3201 O O   . ASN B 1 48  ? 50.359 7.393   66.406  1.00 43.81 ? 48  ASN B O   1 
ATOM   3202 C CB  . ASN B 1 48  ? 51.806 8.864   64.276  1.00 33.37 ? 48  ASN B CB  1 
ATOM   3203 C CG  . ASN B 1 48  ? 51.438 9.821   63.137  1.00 39.38 ? 48  ASN B CG  1 
ATOM   3204 O OD1 . ASN B 1 48  ? 51.165 11.002  63.367  1.00 37.56 ? 48  ASN B OD1 1 
ATOM   3205 N ND2 . ASN B 1 48  ? 51.429 9.317   61.908  1.00 34.44 ? 48  ASN B ND2 1 
ATOM   3206 N N   . LEU B 1 49  ? 51.667 8.491   67.881  1.00 36.24 ? 49  LEU B N   1 
ATOM   3207 C CA  . LEU B 1 49  ? 51.440 7.556   68.991  1.00 31.88 ? 49  LEU B CA  1 
ATOM   3208 C C   . LEU B 1 49  ? 50.625 8.205   70.110  1.00 32.12 ? 49  LEU B C   1 
ATOM   3209 O O   . LEU B 1 49  ? 50.473 7.617   71.187  1.00 31.43 ? 49  LEU B O   1 
ATOM   3210 C CB  . LEU B 1 49  ? 52.765 7.029   69.571  1.00 26.58 ? 49  LEU B CB  1 
ATOM   3211 C CG  . LEU B 1 49  ? 53.431 5.867   68.828  1.00 23.45 ? 49  LEU B CG  1 
ATOM   3212 C CD1 . LEU B 1 49  ? 54.774 5.562   69.445  1.00 8.70  ? 49  LEU B CD1 1 
ATOM   3213 C CD2 . LEU B 1 49  ? 52.538 4.631   68.839  1.00 20.83 ? 49  LEU B CD2 1 
ATOM   3214 N N   . GLU B 1 50  ? 50.086 9.397   69.835  1.00 31.94 ? 50  GLU B N   1 
ATOM   3215 C CA  . GLU B 1 50  ? 49.269 10.177  70.781  1.00 31.78 ? 50  GLU B CA  1 
ATOM   3216 C C   . GLU B 1 50  ? 48.095 9.420   71.391  1.00 30.82 ? 50  GLU B C   1 
ATOM   3217 O O   . GLU B 1 50  ? 47.788 9.570   72.580  1.00 26.47 ? 50  GLU B O   1 
ATOM   3218 C CB  . GLU B 1 50  ? 48.698 11.401  70.077  1.00 31.75 ? 50  GLU B CB  1 
ATOM   3219 C CG  . GLU B 1 50  ? 47.708 12.177  70.933  1.00 42.55 ? 50  GLU B CG  1 
ATOM   3220 C CD  . GLU B 1 50  ? 47.116 13.379  70.223  1.00 49.71 ? 50  GLU B CD  1 
ATOM   3221 O OE1 . GLU B 1 50  ? 47.147 13.391  68.961  1.00 52.37 ? 50  GLU B OE1 1 
ATOM   3222 O OE2 . GLU B 1 50  ? 46.622 14.302  70.932  1.00 43.51 ? 50  GLU B OE2 1 
ATOM   3223 N N   . ASP B 1 51  ? 47.404 8.685   70.521  1.00 32.47 ? 51  ASP B N   1 
ATOM   3224 C CA  . ASP B 1 51  ? 46.233 7.881   70.849  1.00 32.65 ? 51  ASP B CA  1 
ATOM   3225 C C   . ASP B 1 51  ? 46.491 6.524   71.514  1.00 28.77 ? 51  ASP B C   1 
ATOM   3226 O O   . ASP B 1 51  ? 45.564 5.729   71.645  1.00 24.16 ? 51  ASP B O   1 
ATOM   3227 C CB  . ASP B 1 51  ? 45.423 7.623   69.573  1.00 45.35 ? 51  ASP B CB  1 
ATOM   3228 C CG  . ASP B 1 51  ? 44.757 8.880   69.023  1.00 59.55 ? 51  ASP B CG  1 
ATOM   3229 O OD1 . ASP B 1 51  ? 44.607 9.881   69.777  1.00 63.97 ? 51  ASP B OD1 1 
ATOM   3230 O OD2 . ASP B 1 51  ? 44.362 8.847   67.827  1.00 67.06 ? 51  ASP B OD2 1 
ATOM   3231 N N   . TYR B 1 52  ? 47.739 6.217   71.852  1.00 22.75 ? 52  TYR B N   1 
ATOM   3232 C CA  . TYR B 1 52  ? 48.036 4.956   72.495  1.00 19.72 ? 52  TYR B CA  1 
ATOM   3233 C C   . TYR B 1 52  ? 48.718 5.109   73.835  1.00 21.87 ? 52  TYR B C   1 
ATOM   3234 O O   . TYR B 1 52  ? 49.607 5.946   73.990  1.00 24.48 ? 52  TYR B O   1 
ATOM   3235 C CB  . TYR B 1 52  ? 48.915 4.146   71.598  1.00 19.37 ? 52  TYR B CB  1 
ATOM   3236 C CG  . TYR B 1 52  ? 48.184 3.709   70.392  1.00 20.33 ? 52  TYR B CG  1 
ATOM   3237 C CD1 . TYR B 1 52  ? 47.434 2.545   70.421  1.00 22.18 ? 52  TYR B CD1 1 
ATOM   3238 C CD2 . TYR B 1 52  ? 48.244 4.448   69.202  1.00 18.55 ? 52  TYR B CD2 1 
ATOM   3239 C CE1 . TYR B 1 52  ? 46.758 2.111   69.302  1.00 22.05 ? 52  TYR B CE1 1 
ATOM   3240 C CE2 . TYR B 1 52  ? 47.565 4.017   68.079  1.00 19.57 ? 52  TYR B CE2 1 
ATOM   3241 C CZ  . TYR B 1 52  ? 46.823 2.838   68.145  1.00 19.52 ? 52  TYR B CZ  1 
ATOM   3242 O OH  . TYR B 1 52  ? 46.146 2.360   67.047  1.00 36.21 ? 52  TYR B OH  1 
ATOM   3243 N N   . ARG B 1 53  ? 48.327 4.282   74.796  1.00 24.27 ? 53  ARG B N   1 
ATOM   3244 C CA  . ARG B 1 53  ? 48.926 4.327   76.127  1.00 23.75 ? 53  ARG B CA  1 
ATOM   3245 C C   . ARG B 1 53  ? 49.243 2.939   76.658  1.00 24.09 ? 53  ARG B C   1 
ATOM   3246 O O   . ARG B 1 53  ? 48.662 1.965   76.195  1.00 27.40 ? 53  ARG B O   1 
ATOM   3247 C CB  . ARG B 1 53  ? 48.030 5.114   77.081  1.00 23.65 ? 53  ARG B CB  1 
ATOM   3248 C CG  . ARG B 1 53  ? 48.276 6.630   76.958  1.00 28.76 ? 53  ARG B CG  1 
ATOM   3249 C CD  . ARG B 1 53  ? 47.250 7.396   77.727  1.00 34.19 ? 53  ARG B CD  1 
ATOM   3250 N NE  . ARG B 1 53  ? 47.798 8.507   78.503  1.00 30.52 ? 53  ARG B NE  1 
ATOM   3251 C CZ  . ARG B 1 53  ? 48.670 8.381   79.497  1.00 29.15 ? 53  ARG B CZ  1 
ATOM   3252 N NH1 . ARG B 1 53  ? 49.134 7.198   79.844  1.00 26.31 ? 53  ARG B NH1 1 
ATOM   3253 N NH2 . ARG B 1 53  ? 49.021 9.445   80.204  1.00 38.25 ? 53  ARG B NH2 1 
ATOM   3254 N N   . LEU B 1 54  ? 50.225 2.836   77.548  1.00 19.39 ? 54  LEU B N   1 
ATOM   3255 C CA  . LEU B 1 54  ? 50.582 1.547   78.117  1.00 22.08 ? 54  LEU B CA  1 
ATOM   3256 C C   . LEU B 1 54  ? 50.232 1.423   79.599  1.00 21.99 ? 54  LEU B C   1 
ATOM   3257 O O   . LEU B 1 54  ? 50.433 2.355   80.372  1.00 21.57 ? 54  LEU B O   1 
ATOM   3258 C CB  . LEU B 1 54  ? 52.073 1.275   77.940  1.00 25.16 ? 54  LEU B CB  1 
ATOM   3259 C CG  . LEU B 1 54  ? 52.602 0.719   76.621  1.00 20.17 ? 54  LEU B CG  1 
ATOM   3260 C CD1 . LEU B 1 54  ? 54.079 0.416   76.760  1.00 8.40  ? 54  LEU B CD1 1 
ATOM   3261 C CD2 . LEU B 1 54  ? 51.844 -0.544  76.283  1.00 23.33 ? 54  LEU B CD2 1 
ATOM   3262 N N   . VAL B 1 55  ? 49.707 0.263   79.985  1.00 26.88 ? 55  VAL B N   1 
ATOM   3263 C CA  . VAL B 1 55  ? 49.340 -0.016  81.378  1.00 28.15 ? 55  VAL B CA  1 
ATOM   3264 C C   . VAL B 1 55  ? 49.943 -1.357  81.801  1.00 29.01 ? 55  VAL B C   1 
ATOM   3265 O O   . VAL B 1 55  ? 49.862 -2.360  81.081  1.00 30.51 ? 55  VAL B O   1 
ATOM   3266 C CB  . VAL B 1 55  ? 47.804 -0.031  81.596  1.00 27.52 ? 55  VAL B CB  1 
ATOM   3267 C CG1 . VAL B 1 55  ? 47.479 -0.257  83.061  1.00 27.22 ? 55  VAL B CG1 1 
ATOM   3268 C CG2 . VAL B 1 55  ? 47.202 1.285   81.150  1.00 31.09 ? 55  VAL B CG2 1 
ATOM   3269 N N   . GLU B 1 56  ? 50.573 -1.349  82.966  1.00 27.62 ? 56  GLU B N   1 
ATOM   3270 C CA  . GLU B 1 56  ? 51.248 -2.516  83.517  1.00 26.40 ? 56  GLU B CA  1 
ATOM   3271 C C   . GLU B 1 56  ? 50.596 -2.900  84.868  1.00 29.38 ? 56  GLU B C   1 
ATOM   3272 O O   . GLU B 1 56  ? 50.162 -2.028  85.637  1.00 28.79 ? 56  GLU B O   1 
ATOM   3273 C CB  . GLU B 1 56  ? 52.736 -2.168  83.625  1.00 24.07 ? 56  GLU B CB  1 
ATOM   3274 C CG  . GLU B 1 56  ? 53.577 -3.151  84.336  1.00 31.48 ? 56  GLU B CG  1 
ATOM   3275 C CD  . GLU B 1 56  ? 53.894 -2.707  85.736  1.00 28.31 ? 56  GLU B CD  1 
ATOM   3276 O OE1 . GLU B 1 56  ? 53.104 -1.959  86.329  1.00 34.52 ? 56  GLU B OE1 1 
ATOM   3277 O OE2 . GLU B 1 56  ? 54.940 -3.113  86.255  1.00 31.03 ? 56  GLU B OE2 1 
ATOM   3278 N N   . PHE B 1 57  ? 50.515 -4.197  85.147  1.00 24.74 ? 57  PHE B N   1 
ATOM   3279 C CA  . PHE B 1 57  ? 49.856 -4.686  86.350  1.00 24.24 ? 57  PHE B CA  1 
ATOM   3280 C C   . PHE B 1 57  ? 50.612 -5.846  86.941  1.00 27.39 ? 57  PHE B C   1 
ATOM   3281 O O   . PHE B 1 57  ? 51.079 -6.722  86.200  1.00 30.98 ? 57  PHE B O   1 
ATOM   3282 C CB  . PHE B 1 57  ? 48.447 -5.162  85.980  1.00 21.02 ? 57  PHE B CB  1 
ATOM   3283 C CG  . PHE B 1 57  ? 47.768 -5.976  87.046  1.00 21.84 ? 57  PHE B CG  1 
ATOM   3284 C CD1 . PHE B 1 57  ? 47.234 -5.367  88.173  1.00 22.80 ? 57  PHE B CD1 1 
ATOM   3285 C CD2 . PHE B 1 57  ? 47.655 -7.349  86.918  1.00 23.91 ? 57  PHE B CD2 1 
ATOM   3286 C CE1 . PHE B 1 57  ? 46.604 -6.102  89.150  1.00 19.84 ? 57  PHE B CE1 1 
ATOM   3287 C CE2 . PHE B 1 57  ? 47.021 -8.100  87.893  1.00 26.54 ? 57  PHE B CE2 1 
ATOM   3288 C CZ  . PHE B 1 57  ? 46.494 -7.472  89.014  1.00 25.13 ? 57  PHE B CZ  1 
ATOM   3289 N N   . ARG B 1 58  ? 50.671 -5.894  88.273  1.00 29.21 ? 58  ARG B N   1 
ATOM   3290 C CA  . ARG B 1 58  ? 51.367 -6.973  88.963  1.00 27.45 ? 58  ARG B CA  1 
ATOM   3291 C C   . ARG B 1 58  ? 50.669 -7.364  90.239  1.00 27.79 ? 58  ARG B C   1 
ATOM   3292 O O   . ARG B 1 58  ? 50.242 -6.496  90.986  1.00 26.35 ? 58  ARG B O   1 
ATOM   3293 C CB  . ARG B 1 58  ? 52.799 -6.574  89.305  1.00 26.72 ? 58  ARG B CB  1 
ATOM   3294 C CG  . ARG B 1 58  ? 53.582 -7.756  89.820  1.00 34.74 ? 58  ARG B CG  1 
ATOM   3295 C CD  . ARG B 1 58  ? 55.036 -7.457  90.102  1.00 41.24 ? 58  ARG B CD  1 
ATOM   3296 N NE  . ARG B 1 58  ? 55.708 -8.702  90.452  1.00 46.47 ? 58  ARG B NE  1 
ATOM   3297 C CZ  . ARG B 1 58  ? 56.896 -9.072  89.995  1.00 47.77 ? 58  ARG B CZ  1 
ATOM   3298 N NH1 . ARG B 1 58  ? 57.585 -8.268  89.194  1.00 49.58 ? 58  ARG B NH1 1 
ATOM   3299 N NH2 . ARG B 1 58  ? 57.403 -10.241 90.362  1.00 45.19 ? 58  ARG B NH2 1 
ATOM   3300 N N   . SER B 1 59  ? 50.554 -8.662  90.493  1.00 28.71 ? 59  SER B N   1 
ATOM   3301 C CA  . SER B 1 59  ? 49.924 -9.125  91.728  1.00 34.01 ? 59  SER B CA  1 
ATOM   3302 C C   . SER B 1 59  ? 50.504 -10.427 92.306  1.00 34.30 ? 59  SER B C   1 
ATOM   3303 O O   . SER B 1 59  ? 51.035 -11.282 91.587  1.00 37.83 ? 59  SER B O   1 
ATOM   3304 C CB  . SER B 1 59  ? 48.402 -9.218  91.573  1.00 30.43 ? 59  SER B CB  1 
ATOM   3305 O OG  . SER B 1 59  ? 48.041 -10.187 90.609  1.00 44.83 ? 59  SER B OG  1 
ATOM   3306 N N   . LYS B 1 60  ? 50.423 -10.553 93.623  1.00 33.71 ? 60  LYS B N   1 
ATOM   3307 C CA  . LYS B 1 60  ? 50.927 -11.724 94.318  1.00 33.49 ? 60  LYS B CA  1 
ATOM   3308 C C   . LYS B 1 60  ? 49.938 -12.862 94.060  1.00 34.09 ? 60  LYS B C   1 
ATOM   3309 O O   . LYS B 1 60  ? 48.849 -12.644 93.536  1.00 32.86 ? 60  LYS B O   1 
ATOM   3310 C CB  . LYS B 1 60  ? 50.996 -11.425 95.814  1.00 36.75 ? 60  LYS B CB  1 
ATOM   3311 C CG  . LYS B 1 60  ? 51.500 -10.036 96.156  1.00 41.51 ? 60  LYS B CG  1 
ATOM   3312 C CD  . LYS B 1 60  ? 52.929 -10.026 96.703  1.00 47.89 ? 60  LYS B CD  1 
ATOM   3313 C CE  . LYS B 1 60  ? 53.982 -10.459 95.684  1.00 49.55 ? 60  LYS B CE  1 
ATOM   3314 N NZ  . LYS B 1 60  ? 54.193 -11.936 95.662  1.00 52.15 ? 60  LYS B NZ  1 
ATOM   3315 N N   . PRO B 1 61  ? 50.314 -14.100 94.427  1.00 29.57 ? 61  PRO B N   1 
ATOM   3316 C CA  . PRO B 1 61  ? 49.459 -15.268 94.233  1.00 29.06 ? 61  PRO B CA  1 
ATOM   3317 C C   . PRO B 1 61  ? 48.119 -15.206 94.964  1.00 30.29 ? 61  PRO B C   1 
ATOM   3318 O O   . PRO B 1 61  ? 48.002 -14.600 96.047  1.00 32.03 ? 61  PRO B O   1 
ATOM   3319 C CB  . PRO B 1 61  ? 50.323 -16.408 94.741  1.00 27.67 ? 61  PRO B CB  1 
ATOM   3320 C CG  . PRO B 1 61  ? 51.705 -15.938 94.406  1.00 28.24 ? 61  PRO B CG  1 
ATOM   3321 C CD  . PRO B 1 61  ? 51.663 -14.511 94.851  1.00 28.31 ? 61  PRO B CD  1 
ATOM   3322 N N   . GLU B 1 62  ? 47.121 -15.840 94.358  1.00 31.00 ? 62  GLU B N   1 
ATOM   3323 C CA  . GLU B 1 62  ? 45.764 -15.908 94.870  1.00 35.02 ? 62  GLU B CA  1 
ATOM   3324 C C   . GLU B 1 62  ? 45.205 -14.539 95.294  1.00 38.84 ? 62  GLU B C   1 
ATOM   3325 O O   . GLU B 1 62  ? 45.068 -14.217 96.485  1.00 40.62 ? 62  GLU B O   1 
ATOM   3326 C CB  . GLU B 1 62  ? 45.673 -16.932 95.999  1.00 37.51 ? 62  GLU B CB  1 
ATOM   3327 C CG  . GLU B 1 62  ? 46.210 -18.317 95.646  1.00 39.94 ? 62  GLU B CG  1 
ATOM   3328 C CD  . GLU B 1 62  ? 46.077 -19.325 96.783  1.00 41.19 ? 62  GLU B CD  1 
ATOM   3329 O OE1 . GLU B 1 62  ? 46.316 -18.949 97.957  1.00 36.16 ? 62  GLU B OE1 1 
ATOM   3330 O OE2 . GLU B 1 62  ? 45.725 -20.495 96.493  1.00 39.62 ? 62  GLU B OE2 1 
ATOM   3331 N N   . THR B 1 63  ? 44.881 -13.726 94.294  1.00 42.66 ? 63  THR B N   1 
ATOM   3332 C CA  . THR B 1 63  ? 44.334 -12.386 94.494  1.00 41.05 ? 63  THR B CA  1 
ATOM   3333 C C   . THR B 1 63  ? 43.281 -12.089 93.443  1.00 40.76 ? 63  THR B C   1 
ATOM   3334 O O   . THR B 1 63  ? 43.223 -12.739 92.394  1.00 38.80 ? 63  THR B O   1 
ATOM   3335 C CB  . THR B 1 63  ? 45.413 -11.299 94.340  1.00 40.01 ? 63  THR B CB  1 
ATOM   3336 O OG1 . THR B 1 63  ? 46.272 -11.650 93.247  1.00 34.23 ? 63  THR B OG1 1 
ATOM   3337 C CG2 . THR B 1 63  ? 46.193 -11.115 95.631  1.00 33.77 ? 63  THR B CG2 1 
ATOM   3338 N N   . LEU B 1 64  ? 42.476 -11.071 93.709  1.00 41.28 ? 64  LEU B N   1 
ATOM   3339 C CA  . LEU B 1 64  ? 41.428 -10.660 92.794  1.00 37.34 ? 64  LEU B CA  1 
ATOM   3340 C C   . LEU B 1 64  ? 41.395 -9.148  92.636  1.00 34.74 ? 64  LEU B C   1 
ATOM   3341 O O   . LEU B 1 64  ? 41.502 -8.413  93.632  1.00 30.41 ? 64  LEU B O   1 
ATOM   3342 C CB  . LEU B 1 64  ? 40.076 -11.165 93.301  1.00 36.32 ? 64  LEU B CB  1 
ATOM   3343 C CG  . LEU B 1 64  ? 38.810 -10.502 92.748  1.00 42.56 ? 64  LEU B CG  1 
ATOM   3344 C CD1 . LEU B 1 64  ? 37.854 -11.538 92.206  1.00 45.87 ? 64  LEU B CD1 1 
ATOM   3345 C CD2 . LEU B 1 64  ? 38.138 -9.669  93.828  1.00 44.49 ? 64  LEU B CD2 1 
ATOM   3346 N N   . LEU B 1 65  ? 41.337 -8.688  91.387  1.00 28.81 ? 65  LEU B N   1 
ATOM   3347 C CA  . LEU B 1 65  ? 41.215 -7.268  91.094  1.00 27.98 ? 65  LEU B CA  1 
ATOM   3348 C C   . LEU B 1 65  ? 39.703 -7.086  90.978  1.00 27.94 ? 65  LEU B C   1 
ATOM   3349 O O   . LEU B 1 65  ? 39.049 -7.764  90.168  1.00 26.93 ? 65  LEU B O   1 
ATOM   3350 C CB  . LEU B 1 65  ? 41.829 -6.922  89.747  1.00 22.64 ? 65  LEU B CB  1 
ATOM   3351 C CG  . LEU B 1 65  ? 42.610 -5.634  89.458  1.00 22.07 ? 65  LEU B CG  1 
ATOM   3352 C CD1 . LEU B 1 65  ? 42.402 -5.272  87.975  1.00 23.28 ? 65  LEU B CD1 1 
ATOM   3353 C CD2 . LEU B 1 65  ? 42.258 -4.475  90.323  1.00 20.47 ? 65  LEU B CD2 1 
ATOM   3354 N N   . LEU B 1 66  ? 39.155 -6.220  91.825  1.00 27.90 ? 66  LEU B N   1 
ATOM   3355 C CA  . LEU B 1 66  ? 37.727 -5.920  91.858  1.00 28.14 ? 66  LEU B CA  1 
ATOM   3356 C C   . LEU B 1 66  ? 37.150 -5.265  90.561  1.00 29.79 ? 66  LEU B C   1 
ATOM   3357 O O   . LEU B 1 66  ? 37.868 -4.601  89.802  1.00 26.84 ? 66  LEU B O   1 
ATOM   3358 C CB  . LEU B 1 66  ? 37.447 -5.042  93.083  1.00 29.38 ? 66  LEU B CB  1 
ATOM   3359 C CG  . LEU B 1 66  ? 37.722 -5.734  94.416  1.00 28.49 ? 66  LEU B CG  1 
ATOM   3360 C CD1 . LEU B 1 66  ? 37.782 -4.721  95.516  1.00 21.30 ? 66  LEU B CD1 1 
ATOM   3361 C CD2 . LEU B 1 66  ? 36.649 -6.759  94.685  1.00 31.41 ? 66  LEU B CD2 1 
ATOM   3362 N N   . PRO B 1 67  ? 35.833 -5.450  90.308  1.00 29.12 ? 67  PRO B N   1 
ATOM   3363 C CA  . PRO B 1 67  ? 35.100 -4.931  89.159  1.00 26.86 ? 67  PRO B CA  1 
ATOM   3364 C C   . PRO B 1 67  ? 35.347 -3.475  88.831  1.00 28.47 ? 67  PRO B C   1 
ATOM   3365 O O   . PRO B 1 67  ? 35.296 -2.597  89.713  1.00 25.78 ? 67  PRO B O   1 
ATOM   3366 C CB  . PRO B 1 67  ? 33.648 -5.144  89.574  1.00 25.73 ? 67  PRO B CB  1 
ATOM   3367 C CG  . PRO B 1 67  ? 33.707 -6.423  90.236  1.00 27.50 ? 67  PRO B CG  1 
ATOM   3368 C CD  . PRO B 1 67  ? 34.915 -6.241  91.148  1.00 31.84 ? 67  PRO B CD  1 
ATOM   3369 N N   . GLN B 1 68  ? 35.527 -3.232  87.531  1.00 26.47 ? 68  GLN B N   1 
ATOM   3370 C CA  . GLN B 1 68  ? 35.745 -1.896  86.979  1.00 28.05 ? 68  GLN B CA  1 
ATOM   3371 C C   . GLN B 1 68  ? 35.422 -1.930  85.489  1.00 23.44 ? 68  GLN B C   1 
ATOM   3372 O O   . GLN B 1 68  ? 35.208 -2.999  84.925  1.00 26.94 ? 68  GLN B O   1 
ATOM   3373 C CB  . GLN B 1 68  ? 37.215 -1.498  87.102  1.00 26.22 ? 68  GLN B CB  1 
ATOM   3374 C CG  . GLN B 1 68  ? 38.081 -2.163  86.036  1.00 26.13 ? 68  GLN B CG  1 
ATOM   3375 C CD  . GLN B 1 68  ? 39.490 -1.680  86.063  1.00 23.75 ? 68  GLN B CD  1 
ATOM   3376 O OE1 . GLN B 1 68  ? 39.752 -0.494  85.867  1.00 31.82 ? 68  GLN B OE1 1 
ATOM   3377 N NE2 . GLN B 1 68  ? 40.417 -2.586  86.307  1.00 25.26 ? 68  GLN B NE2 1 
ATOM   3378 N N   . GLN B 1 69  ? 35.448 -0.750  84.876  1.00 24.51 ? 69  GLN B N   1 
ATOM   3379 C CA  . GLN B 1 69  ? 35.271 -0.531  83.431  1.00 25.72 ? 69  GLN B CA  1 
ATOM   3380 C C   . GLN B 1 69  ? 36.090 0.731   83.098  1.00 27.08 ? 69  GLN B C   1 
ATOM   3381 O O   . GLN B 1 69  ? 36.106 1.693   83.869  1.00 29.34 ? 69  GLN B O   1 
ATOM   3382 C CB  . GLN B 1 69  ? 33.791 -0.375  83.024  1.00 23.19 ? 69  GLN B CB  1 
ATOM   3383 C CG  . GLN B 1 69  ? 32.845 0.275   84.069  1.00 31.18 ? 69  GLN B CG  1 
ATOM   3384 C CD  . GLN B 1 69  ? 32.578 1.740   83.796  1.00 29.59 ? 69  GLN B CD  1 
ATOM   3385 O OE1 . GLN B 1 69  ? 33.047 2.283   82.801  1.00 43.47 ? 69  GLN B OE1 1 
ATOM   3386 N NE2 . GLN B 1 69  ? 31.805 2.381   84.658  1.00 24.83 ? 69  GLN B NE2 1 
ATOM   3387 N N   . ALA B 1 70  ? 36.870 0.692   82.029  1.00 25.08 ? 70  ALA B N   1 
ATOM   3388 C CA  . ALA B 1 70  ? 37.672 1.859   81.647  1.00 19.87 ? 70  ALA B CA  1 
ATOM   3389 C C   . ALA B 1 70  ? 37.142 2.404   80.327  1.00 18.96 ? 70  ALA B C   1 
ATOM   3390 O O   . ALA B 1 70  ? 36.423 1.717   79.616  1.00 19.57 ? 70  ALA B O   1 
ATOM   3391 C CB  . ALA B 1 70  ? 39.134 1.485   81.506  1.00 16.83 ? 70  ALA B CB  1 
ATOM   3392 N N   . ASP B 1 71  ? 37.479 3.637   79.996  1.00 15.07 ? 71  ASP B N   1 
ATOM   3393 C CA  . ASP B 1 71  ? 37.004 4.208   78.751  1.00 20.54 ? 71  ASP B CA  1 
ATOM   3394 C C   . ASP B 1 71  ? 38.025 4.021   77.621  1.00 20.62 ? 71  ASP B C   1 
ATOM   3395 O O   . ASP B 1 71  ? 38.276 4.940   76.851  1.00 22.45 ? 71  ASP B O   1 
ATOM   3396 C CB  . ASP B 1 71  ? 36.686 5.692   78.960  1.00 22.40 ? 71  ASP B CB  1 
ATOM   3397 C CG  . ASP B 1 71  ? 37.912 6.510   79.311  1.00 19.25 ? 71  ASP B CG  1 
ATOM   3398 O OD1 . ASP B 1 71  ? 38.910 5.927   79.789  1.00 25.61 ? 71  ASP B OD1 1 
ATOM   3399 O OD2 . ASP B 1 71  ? 37.880 7.737   79.107  1.00 23.43 ? 71  ASP B OD2 1 
ATOM   3400 N N   . ALA B 1 72  ? 38.602 2.832   77.521  1.00 19.48 ? 72  ALA B N   1 
ATOM   3401 C CA  . ALA B 1 72  ? 39.592 2.539   76.495  1.00 21.33 ? 72  ALA B CA  1 
ATOM   3402 C C   . ALA B 1 72  ? 39.499 1.094   76.048  1.00 22.26 ? 72  ALA B C   1 
ATOM   3403 O O   . ALA B 1 72  ? 38.995 0.246   76.770  1.00 24.64 ? 72  ALA B O   1 
ATOM   3404 C CB  . ALA B 1 72  ? 40.982 2.799   77.021  1.00 13.42 ? 72  ALA B CB  1 
ATOM   3405 N N   . GLU B 1 73  ? 39.976 0.824   74.844  1.00 24.48 ? 73  GLU B N   1 
ATOM   3406 C CA  . GLU B 1 73  ? 39.995 -0.524  74.315  1.00 27.10 ? 73  GLU B CA  1 
ATOM   3407 C C   . GLU B 1 73  ? 41.308 -1.111  74.859  1.00 26.23 ? 73  GLU B C   1 
ATOM   3408 O O   . GLU B 1 73  ? 42.356 -0.479  74.729  1.00 28.65 ? 73  GLU B O   1 
ATOM   3409 C CB  . GLU B 1 73  ? 40.043 -0.452  72.790  1.00 33.37 ? 73  GLU B CB  1 
ATOM   3410 C CG  . GLU B 1 73  ? 39.694 -1.754  72.078  1.00 46.55 ? 73  GLU B CG  1 
ATOM   3411 C CD  . GLU B 1 73  ? 38.194 -1.926  71.806  1.00 52.89 ? 73  GLU B CD  1 
ATOM   3412 O OE1 . GLU B 1 73  ? 37.350 -1.310  72.503  1.00 52.56 ? 73  GLU B OE1 1 
ATOM   3413 O OE2 . GLU B 1 73  ? 37.863 -2.691  70.874  1.00 56.96 ? 73  GLU B OE2 1 
ATOM   3414 N N   . LEU B 1 74  ? 41.265 -2.278  75.492  1.00 20.35 ? 74  LEU B N   1 
ATOM   3415 C CA  . LEU B 1 74  ? 42.480 -2.878  76.045  1.00 20.92 ? 74  LEU B CA  1 
ATOM   3416 C C   . LEU B 1 74  ? 42.828 -4.165  75.357  1.00 19.03 ? 74  LEU B C   1 
ATOM   3417 O O   . LEU B 1 74  ? 41.965 -4.992  75.098  1.00 23.00 ? 74  LEU B O   1 
ATOM   3418 C CB  . LEU B 1 74  ? 42.321 -3.278  77.522  1.00 23.26 ? 74  LEU B CB  1 
ATOM   3419 C CG  . LEU B 1 74  ? 41.989 -2.361  78.692  1.00 24.30 ? 74  LEU B CG  1 
ATOM   3420 C CD1 . LEU B 1 74  ? 42.669 -1.027  78.492  1.00 29.37 ? 74  LEU B CD1 1 
ATOM   3421 C CD2 . LEU B 1 74  ? 40.485 -2.209  78.806  1.00 36.35 ? 74  LEU B CD2 1 
ATOM   3422 N N   . LEU B 1 75  ? 44.118 -4.377  75.182  1.00 21.07 ? 75  LEU B N   1 
ATOM   3423 C CA  . LEU B 1 75  ? 44.638 -5.595  74.602  1.00 21.46 ? 75  LEU B CA  1 
ATOM   3424 C C   . LEU B 1 75  ? 45.542 -6.085  75.728  1.00 22.56 ? 75  LEU B C   1 
ATOM   3425 O O   . LEU B 1 75  ? 46.668 -5.614  75.884  1.00 21.76 ? 75  LEU B O   1 
ATOM   3426 C CB  . LEU B 1 75  ? 45.445 -5.293  73.339  1.00 24.66 ? 75  LEU B CB  1 
ATOM   3427 C CG  . LEU B 1 75  ? 46.347 -6.420  72.821  1.00 27.71 ? 75  LEU B CG  1 
ATOM   3428 C CD1 . LEU B 1 75  ? 45.585 -7.743  72.743  1.00 25.16 ? 75  LEU B CD1 1 
ATOM   3429 C CD2 . LEU B 1 75  ? 46.903 -6.013  71.470  1.00 29.04 ? 75  LEU B CD2 1 
ATOM   3430 N N   . LEU B 1 76  ? 45.016 -6.998  76.535  1.00 23.28 ? 76  LEU B N   1 
ATOM   3431 C CA  . LEU B 1 76  ? 45.734 -7.540  77.674  1.00 25.84 ? 76  LEU B CA  1 
ATOM   3432 C C   . LEU B 1 76  ? 46.688 -8.689  77.363  1.00 25.98 ? 76  LEU B C   1 
ATOM   3433 O O   . LEU B 1 76  ? 46.261 -9.718  76.842  1.00 30.94 ? 76  LEU B O   1 
ATOM   3434 C CB  . LEU B 1 76  ? 44.705 -7.967  78.724  1.00 26.85 ? 76  LEU B CB  1 
ATOM   3435 C CG  . LEU B 1 76  ? 45.098 -8.567  80.067  1.00 29.45 ? 76  LEU B CG  1 
ATOM   3436 C CD1 . LEU B 1 76  ? 43.949 -8.363  81.050  1.00 29.54 ? 76  LEU B CD1 1 
ATOM   3437 C CD2 . LEU B 1 76  ? 45.420 -10.049 79.908  1.00 33.43 ? 76  LEU B CD2 1 
ATOM   3438 N N   . VAL B 1 77  ? 47.970 -8.520  77.690  1.00 24.83 ? 77  VAL B N   1 
ATOM   3439 C CA  . VAL B 1 77  ? 48.964 -9.580  77.491  1.00 22.46 ? 77  VAL B CA  1 
ATOM   3440 C C   . VAL B 1 77  ? 49.532 -10.066 78.837  1.00 27.78 ? 77  VAL B C   1 
ATOM   3441 O O   . VAL B 1 77  ? 49.851 -9.257  79.712  1.00 28.88 ? 77  VAL B O   1 
ATOM   3442 C CB  . VAL B 1 77  ? 50.152 -9.126  76.621  1.00 20.89 ? 77  VAL B CB  1 
ATOM   3443 C CG1 . VAL B 1 77  ? 51.179 -10.250 76.526  1.00 19.88 ? 77  VAL B CG1 1 
ATOM   3444 C CG2 . VAL B 1 77  ? 49.682 -8.746  75.200  1.00 24.21 ? 77  VAL B CG2 1 
ATOM   3445 N N   . VAL B 1 78  ? 49.624 -11.381 79.024  1.00 29.14 ? 78  VAL B N   1 
ATOM   3446 C CA  . VAL B 1 78  ? 50.191 -11.925 80.260  1.00 34.92 ? 78  VAL B CA  1 
ATOM   3447 C C   . VAL B 1 78  ? 51.657 -12.259 79.951  1.00 36.59 ? 78  VAL B C   1 
ATOM   3448 O O   . VAL B 1 78  ? 51.943 -13.121 79.104  1.00 39.54 ? 78  VAL B O   1 
ATOM   3449 C CB  . VAL B 1 78  ? 49.413 -13.183 80.771  1.00 37.37 ? 78  VAL B CB  1 
ATOM   3450 C CG1 . VAL B 1 78  ? 50.149 -13.848 81.934  1.00 38.67 ? 78  VAL B CG1 1 
ATOM   3451 C CG2 . VAL B 1 78  ? 48.018 -12.775 81.238  1.00 34.51 ? 78  VAL B CG2 1 
ATOM   3452 N N   . ARG B 1 79  ? 52.570 -11.503 80.567  1.00 31.85 ? 79  ARG B N   1 
ATOM   3453 C CA  . ARG B 1 79  ? 54.002 -11.683 80.363  1.00 27.46 ? 79  ARG B CA  1 
ATOM   3454 C C   . ARG B 1 79  ? 54.642 -12.590 81.429  1.00 29.46 ? 79  ARG B C   1 
ATOM   3455 O O   . ARG B 1 79  ? 55.854 -12.727 81.488  1.00 34.32 ? 79  ARG B O   1 
ATOM   3456 C CB  . ARG B 1 79  ? 54.704 -10.316 80.273  1.00 19.22 ? 79  ARG B CB  1 
ATOM   3457 C CG  . ARG B 1 79  ? 54.904 -9.617  81.591  1.00 18.57 ? 79  ARG B CG  1 
ATOM   3458 C CD  . ARG B 1 79  ? 54.696 -8.133  81.468  1.00 13.91 ? 79  ARG B CD  1 
ATOM   3459 N NE  . ARG B 1 79  ? 55.944 -7.372  81.403  1.00 24.11 ? 79  ARG B NE  1 
ATOM   3460 C CZ  . ARG B 1 79  ? 56.209 -6.253  82.095  1.00 26.15 ? 79  ARG B CZ  1 
ATOM   3461 N NH1 . ARG B 1 79  ? 55.329 -5.747  82.962  1.00 24.20 ? 79  ARG B NH1 1 
ATOM   3462 N NH2 . ARG B 1 79  ? 57.380 -5.645  81.942  1.00 28.96 ? 79  ARG B NH2 1 
ATOM   3463 N N   . SER B 1 80  ? 53.823 -13.212 82.266  1.00 32.42 ? 80  SER B N   1 
ATOM   3464 C CA  . SER B 1 80  ? 54.306 -14.127 83.298  1.00 34.02 ? 80  SER B CA  1 
ATOM   3465 C C   . SER B 1 80  ? 53.180 -14.584 84.183  1.00 32.70 ? 80  SER B C   1 
ATOM   3466 O O   . SER B 1 80  ? 52.428 -13.763 84.711  1.00 30.97 ? 80  SER B O   1 
ATOM   3467 C CB  . SER B 1 80  ? 55.376 -13.495 84.187  1.00 42.61 ? 80  SER B CB  1 
ATOM   3468 O OG  . SER B 1 80  ? 55.815 -14.430 85.168  1.00 48.93 ? 80  SER B OG  1 
ATOM   3469 N N   . GLY B 1 81  ? 53.082 -15.899 84.342  1.00 32.14 ? 81  GLY B N   1 
ATOM   3470 C CA  . GLY B 1 81  ? 52.063 -16.488 85.192  1.00 33.10 ? 81  GLY B CA  1 
ATOM   3471 C C   . GLY B 1 81  ? 50.808 -16.923 84.476  1.00 33.77 ? 81  GLY B C   1 
ATOM   3472 O O   . GLY B 1 81  ? 50.848 -17.204 83.271  1.00 34.14 ? 81  GLY B O   1 
ATOM   3473 N N   . SER B 1 82  ? 49.716 -17.018 85.240  1.00 31.87 ? 82  SER B N   1 
ATOM   3474 C CA  . SER B 1 82  ? 48.400 -17.403 84.737  1.00 30.93 ? 82  SER B CA  1 
ATOM   3475 C C   . SER B 1 82  ? 47.357 -16.411 85.208  1.00 30.42 ? 82  SER B C   1 
ATOM   3476 O O   . SER B 1 82  ? 47.603 -15.644 86.132  1.00 34.34 ? 82  SER B O   1 
ATOM   3477 C CB  . SER B 1 82  ? 48.026 -18.782 85.244  1.00 31.01 ? 82  SER B CB  1 
ATOM   3478 O OG  . SER B 1 82  ? 48.898 -19.743 84.693  1.00 35.94 ? 82  SER B OG  1 
ATOM   3479 N N   . ALA B 1 83  ? 46.172 -16.448 84.621  1.00 31.23 ? 83  ALA B N   1 
ATOM   3480 C CA  . ALA B 1 83  ? 45.138 -15.510 85.032  1.00 31.25 ? 83  ALA B CA  1 
ATOM   3481 C C   . ALA B 1 83  ? 43.748 -15.931 84.617  1.00 31.26 ? 83  ALA B C   1 
ATOM   3482 O O   . ALA B 1 83  ? 43.571 -16.599 83.592  1.00 32.23 ? 83  ALA B O   1 
ATOM   3483 C CB  . ALA B 1 83  ? 45.432 -14.116 84.475  1.00 24.34 ? 83  ALA B CB  1 
ATOM   3484 N N   . ILE B 1 84  ? 42.770 -15.613 85.464  1.00 30.66 ? 84  ILE B N   1 
ATOM   3485 C CA  . ILE B 1 84  ? 41.381 -15.893 85.128  1.00 30.08 ? 84  ILE B CA  1 
ATOM   3486 C C   . ILE B 1 84  ? 40.692 -14.561 84.890  1.00 27.21 ? 84  ILE B C   1 
ATOM   3487 O O   . ILE B 1 84  ? 40.672 -13.694 85.757  1.00 24.28 ? 84  ILE B O   1 
ATOM   3488 C CB  . ILE B 1 84  ? 40.626 -16.679 86.195  1.00 26.66 ? 84  ILE B CB  1 
ATOM   3489 C CG1 . ILE B 1 84  ? 41.214 -18.090 86.325  1.00 29.77 ? 84  ILE B CG1 1 
ATOM   3490 C CG2 . ILE B 1 84  ? 39.173 -16.804 85.778  1.00 18.89 ? 84  ILE B CG2 1 
ATOM   3491 C CD1 . ILE B 1 84  ? 40.747 -18.825 87.571  1.00 29.62 ? 84  ILE B CD1 1 
ATOM   3492 N N   . LEU B 1 85  ? 40.209 -14.388 83.667  1.00 30.39 ? 85  LEU B N   1 
ATOM   3493 C CA  . LEU B 1 85  ? 39.528 -13.175 83.263  1.00 30.14 ? 85  LEU B CA  1 
ATOM   3494 C C   . LEU B 1 85  ? 38.046 -13.427 82.982  1.00 30.58 ? 85  LEU B C   1 
ATOM   3495 O O   . LEU B 1 85  ? 37.690 -14.354 82.240  1.00 30.88 ? 85  LEU B O   1 
ATOM   3496 C CB  . LEU B 1 85  ? 40.195 -12.621 81.998  1.00 31.06 ? 85  LEU B CB  1 
ATOM   3497 C CG  . LEU B 1 85  ? 39.627 -11.372 81.325  1.00 24.63 ? 85  LEU B CG  1 
ATOM   3498 C CD1 . LEU B 1 85  ? 39.919 -10.115 82.129  1.00 27.28 ? 85  LEU B CD1 1 
ATOM   3499 C CD2 . LEU B 1 85  ? 40.235 -11.259 79.943  1.00 32.38 ? 85  LEU B CD2 1 
ATOM   3500 N N   . VAL B 1 86  ? 37.185 -12.658 83.636  1.00 27.25 ? 86  VAL B N   1 
ATOM   3501 C CA  . VAL B 1 86  ? 35.763 -12.773 83.378  1.00 28.38 ? 86  VAL B CA  1 
ATOM   3502 C C   . VAL B 1 86  ? 35.195 -11.390 83.033  1.00 30.52 ? 86  VAL B C   1 
ATOM   3503 O O   . VAL B 1 86  ? 35.392 -10.413 83.768  1.00 25.00 ? 86  VAL B O   1 
ATOM   3504 C CB  . VAL B 1 86  ? 34.936 -13.529 84.501  1.00 29.34 ? 86  VAL B CB  1 
ATOM   3505 C CG1 . VAL B 1 86  ? 35.790 -13.859 85.728  1.00 20.31 ? 86  VAL B CG1 1 
ATOM   3506 C CG2 . VAL B 1 86  ? 33.661 -12.775 84.852  1.00 24.27 ? 86  VAL B CG2 1 
ATOM   3507 N N   . LEU B 1 87  ? 34.640 -11.309 81.820  1.00 28.13 ? 87  LEU B N   1 
ATOM   3508 C CA  . LEU B 1 87  ? 34.036 -10.113 81.292  1.00 20.03 ? 87  LEU B CA  1 
ATOM   3509 C C   . LEU B 1 87  ? 32.540 -10.289 81.516  1.00 20.88 ? 87  LEU B C   1 
ATOM   3510 O O   . LEU B 1 87  ? 32.005 -11.386 81.297  1.00 18.92 ? 87  LEU B O   1 
ATOM   3511 C CB  . LEU B 1 87  ? 34.370 -9.990  79.805  1.00 24.73 ? 87  LEU B CB  1 
ATOM   3512 C CG  . LEU B 1 87  ? 35.647 -9.252  79.340  1.00 27.90 ? 87  LEU B CG  1 
ATOM   3513 C CD1 . LEU B 1 87  ? 36.890 -9.582  80.125  1.00 26.52 ? 87  LEU B CD1 1 
ATOM   3514 C CD2 . LEU B 1 87  ? 35.898 -9.572  77.900  1.00 30.80 ? 87  LEU B CD2 1 
ATOM   3515 N N   . VAL B 1 88  ? 31.894 -9.238  82.035  1.00 22.83 ? 88  VAL B N   1 
ATOM   3516 C CA  . VAL B 1 88  ? 30.454 -9.230  82.336  1.00 24.65 ? 88  VAL B CA  1 
ATOM   3517 C C   . VAL B 1 88  ? 29.619 -8.319  81.413  1.00 28.06 ? 88  VAL B C   1 
ATOM   3518 O O   . VAL B 1 88  ? 29.901 -7.126  81.261  1.00 28.05 ? 88  VAL B O   1 
ATOM   3519 C CB  . VAL B 1 88  ? 30.196 -8.822  83.792  1.00 21.52 ? 88  VAL B CB  1 
ATOM   3520 C CG1 . VAL B 1 88  ? 28.710 -8.850  84.081  1.00 22.52 ? 88  VAL B CG1 1 
ATOM   3521 C CG2 . VAL B 1 88  ? 30.963 -9.745  84.741  1.00 17.53 ? 88  VAL B CG2 1 
ATOM   3522 N N   . LYS B 1 89  ? 28.553 -8.882  80.858  1.00 28.95 ? 89  LYS B N   1 
ATOM   3523 C CA  . LYS B 1 89  ? 27.679 -8.182  79.939  1.00 32.13 ? 89  LYS B CA  1 
ATOM   3524 C C   . LYS B 1 89  ? 26.391 -7.784  80.645  1.00 34.25 ? 89  LYS B C   1 
ATOM   3525 O O   . LYS B 1 89  ? 25.778 -8.625  81.310  1.00 37.57 ? 89  LYS B O   1 
ATOM   3526 C CB  . LYS B 1 89  ? 27.387 -9.090  78.751  1.00 35.77 ? 89  LYS B CB  1 
ATOM   3527 C CG  . LYS B 1 89  ? 28.636 -9.513  77.986  1.00 42.46 ? 89  LYS B CG  1 
ATOM   3528 C CD  . LYS B 1 89  ? 29.386 -8.299  77.441  1.00 51.57 ? 89  LYS B CD  1 
ATOM   3529 C CE  . LYS B 1 89  ? 30.519 -8.710  76.511  1.00 56.45 ? 89  LYS B CE  1 
ATOM   3530 N NZ  . LYS B 1 89  ? 31.233 -7.551  75.895  1.00 55.61 ? 89  LYS B NZ  1 
ATOM   3531 N N   . PRO B 1 90  ? 25.888 -6.548  80.387  1.00 32.66 ? 90  PRO B N   1 
ATOM   3532 C CA  . PRO B 1 90  ? 24.671 -5.986  80.984  1.00 30.15 ? 90  PRO B CA  1 
ATOM   3533 C C   . PRO B 1 90  ? 23.406 -6.779  80.745  1.00 32.39 ? 90  PRO B C   1 
ATOM   3534 O O   . PRO B 1 90  ? 22.417 -6.582  81.439  1.00 34.36 ? 90  PRO B O   1 
ATOM   3535 C CB  . PRO B 1 90  ? 24.590 -4.601  80.351  1.00 25.25 ? 90  PRO B CB  1 
ATOM   3536 C CG  . PRO B 1 90  ? 25.073 -4.857  79.020  1.00 24.37 ? 90  PRO B CG  1 
ATOM   3537 C CD  . PRO B 1 90  ? 26.310 -5.699  79.260  1.00 29.05 ? 90  PRO B CD  1 
ATOM   3538 N N   . ASP B 1 91  ? 23.437 -7.688  79.782  1.00 34.84 ? 91  ASP B N   1 
ATOM   3539 C CA  . ASP B 1 91  ? 22.265 -8.484  79.496  1.00 36.37 ? 91  ASP B CA  1 
ATOM   3540 C C   . ASP B 1 91  ? 22.410 -9.911  79.984  1.00 38.53 ? 91  ASP B C   1 
ATOM   3541 O O   . ASP B 1 91  ? 22.196 -10.856 79.240  1.00 40.05 ? 91  ASP B O   1 
ATOM   3542 C CB  . ASP B 1 91  ? 21.938 -8.444  78.009  1.00 42.97 ? 91  ASP B CB  1 
ATOM   3543 C CG  . ASP B 1 91  ? 23.069 -8.962  77.145  1.00 51.07 ? 91  ASP B CG  1 
ATOM   3544 O OD1 . ASP B 1 91  ? 24.248 -8.885  77.568  1.00 52.93 ? 91  ASP B OD1 1 
ATOM   3545 O OD2 . ASP B 1 91  ? 22.770 -9.454  76.034  1.00 58.80 ? 91  ASP B OD2 1 
ATOM   3546 N N   . ASP B 1 92  ? 22.855 -10.059 81.220  1.00 41.51 ? 92  ASP B N   1 
ATOM   3547 C CA  . ASP B 1 92  ? 22.974 -11.371 81.838  1.00 45.02 ? 92  ASP B CA  1 
ATOM   3548 C C   . ASP B 1 92  ? 23.749 -12.421 81.043  1.00 47.40 ? 92  ASP B C   1 
ATOM   3549 O O   . ASP B 1 92  ? 23.244 -13.524 80.810  1.00 47.99 ? 92  ASP B O   1 
ATOM   3550 C CB  . ASP B 1 92  ? 21.565 -11.903 82.164  1.00 46.69 ? 92  ASP B CB  1 
ATOM   3551 C CG  . ASP B 1 92  ? 21.568 -12.998 83.217  1.00 46.99 ? 92  ASP B CG  1 
ATOM   3552 O OD1 . ASP B 1 92  ? 22.419 -12.953 84.135  1.00 47.27 ? 92  ASP B OD1 1 
ATOM   3553 O OD2 . ASP B 1 92  ? 20.693 -13.886 83.143  1.00 45.06 ? 92  ASP B OD2 1 
ATOM   3554 N N   . ARG B 1 93  ? 24.958 -12.074 80.609  1.00 47.38 ? 93  ARG B N   1 
ATOM   3555 C CA  . ARG B 1 93  ? 25.818 -13.017 79.891  1.00 48.28 ? 93  ARG B CA  1 
ATOM   3556 C C   . ARG B 1 93  ? 27.182 -12.766 80.499  1.00 44.63 ? 93  ARG B C   1 
ATOM   3557 O O   . ARG B 1 93  ? 27.463 -11.638 80.917  1.00 45.55 ? 93  ARG B O   1 
ATOM   3558 C CB  . ARG B 1 93  ? 25.882 -12.737 78.379  1.00 53.69 ? 93  ARG B CB  1 
ATOM   3559 C CG  . ARG B 1 93  ? 25.569 -13.945 77.459  1.00 61.49 ? 93  ARG B CG  1 
ATOM   3560 C CD  . ARG B 1 93  ? 26.315 -15.262 77.794  1.00 64.83 ? 93  ARG B CD  1 
ATOM   3561 N NE  . ARG B 1 93  ? 27.738 -15.333 77.396  1.00 61.26 ? 93  ARG B NE  1 
ATOM   3562 C CZ  . ARG B 1 93  ? 28.192 -15.460 76.116  1.00 60.07 ? 93  ARG B CZ  1 
ATOM   3563 N NH1 . ARG B 1 93  ? 27.313 -15.516 75.030  1.00 57.72 ? 93  ARG B NH1 1 
ATOM   3564 N NH2 . ARG B 1 93  ? 29.543 -15.558 75.914  1.00 58.94 ? 93  ARG B NH2 1 
ATOM   3565 N N   . ARG B 1 94  ? 28.014 -13.805 80.530  1.00 36.57 ? 94  ARG B N   1 
ATOM   3566 C CA  . ARG B 1 94  ? 29.352 -13.736 81.088  1.00 34.43 ? 94  ARG B CA  1 
ATOM   3567 C C   . ARG B 1 94  ? 30.292 -14.465 80.140  1.00 37.54 ? 94  ARG B C   1 
ATOM   3568 O O   . ARG B 1 94  ? 29.854 -15.337 79.377  1.00 42.90 ? 94  ARG B O   1 
ATOM   3569 C CB  . ARG B 1 94  ? 29.402 -14.424 82.464  1.00 34.27 ? 94  ARG B CB  1 
ATOM   3570 C CG  . ARG B 1 94  ? 29.496 -13.496 83.697  1.00 29.87 ? 94  ARG B CG  1 
ATOM   3571 C CD  . ARG B 1 94  ? 28.131 -13.173 84.319  1.00 23.70 ? 94  ARG B CD  1 
ATOM   3572 N NE  . ARG B 1 94  ? 27.240 -14.321 84.234  1.00 25.14 ? 94  ARG B NE  1 
ATOM   3573 C CZ  . ARG B 1 94  ? 25.917 -14.243 84.213  1.00 27.11 ? 94  ARG B CZ  1 
ATOM   3574 N NH1 . ARG B 1 94  ? 25.321 -13.064 84.312  1.00 35.03 ? 94  ARG B NH1 1 
ATOM   3575 N NH2 . ARG B 1 94  ? 25.196 -15.312 83.933  1.00 26.20 ? 94  ARG B NH2 1 
ATOM   3576 N N   . GLU B 1 95  ? 31.580 -14.113 80.211  1.00 39.19 ? 95  GLU B N   1 
ATOM   3577 C CA  . GLU B 1 95  ? 32.633 -14.705 79.379  1.00 37.07 ? 95  GLU B CA  1 
ATOM   3578 C C   . GLU B 1 95  ? 33.871 -14.934 80.234  1.00 34.45 ? 95  GLU B C   1 
ATOM   3579 O O   . GLU B 1 95  ? 34.322 -14.018 80.921  1.00 34.74 ? 95  GLU B O   1 
ATOM   3580 C CB  . GLU B 1 95  ? 32.969 -13.782 78.203  1.00 40.09 ? 95  GLU B CB  1 
ATOM   3581 C CG  . GLU B 1 95  ? 32.080 -13.995 76.995  1.00 48.86 ? 95  GLU B CG  1 
ATOM   3582 C CD  . GLU B 1 95  ? 31.774 -12.700 76.245  1.00 56.02 ? 95  GLU B CD  1 
ATOM   3583 O OE1 . GLU B 1 95  ? 30.755 -12.038 76.576  1.00 57.15 ? 95  GLU B OE1 1 
ATOM   3584 O OE2 . GLU B 1 95  ? 32.543 -12.361 75.316  1.00 56.16 ? 95  GLU B OE2 1 
ATOM   3585 N N   . TYR B 1 96  ? 34.420 -16.150 80.181  1.00 31.78 ? 96  TYR B N   1 
ATOM   3586 C CA  . TYR B 1 96  ? 35.594 -16.512 80.985  1.00 28.83 ? 96  TYR B CA  1 
ATOM   3587 C C   . TYR B 1 96  ? 36.766 -16.841 80.088  1.00 30.58 ? 96  TYR B C   1 
ATOM   3588 O O   . TYR B 1 96  ? 36.591 -17.333 78.974  1.00 36.54 ? 96  TYR B O   1 
ATOM   3589 C CB  . TYR B 1 96  ? 35.305 -17.752 81.864  1.00 26.68 ? 96  TYR B CB  1 
ATOM   3590 C CG  . TYR B 1 96  ? 34.055 -17.667 82.731  1.00 21.57 ? 96  TYR B CG  1 
ATOM   3591 C CD1 . TYR B 1 96  ? 32.798 -18.014 82.220  1.00 13.86 ? 96  TYR B CD1 1 
ATOM   3592 C CD2 . TYR B 1 96  ? 34.121 -17.168 84.035  1.00 17.86 ? 96  TYR B CD2 1 
ATOM   3593 C CE1 . TYR B 1 96  ? 31.648 -17.849 82.978  1.00 21.12 ? 96  TYR B CE1 1 
ATOM   3594 C CE2 . TYR B 1 96  ? 32.976 -17.003 84.804  1.00 15.61 ? 96  TYR B CE2 1 
ATOM   3595 C CZ  . TYR B 1 96  ? 31.747 -17.336 84.272  1.00 17.26 ? 96  TYR B CZ  1 
ATOM   3596 O OH  . TYR B 1 96  ? 30.603 -17.111 85.005  1.00 18.57 ? 96  TYR B OH  1 
ATOM   3597 N N   . PHE B 1 97  ? 37.966 -16.553 80.556  1.00 28.83 ? 97  PHE B N   1 
ATOM   3598 C CA  . PHE B 1 97  ? 39.137 -16.885 79.779  1.00 23.98 ? 97  PHE B CA  1 
ATOM   3599 C C   . PHE B 1 97  ? 40.251 -17.186 80.762  1.00 26.34 ? 97  PHE B C   1 
ATOM   3600 O O   . PHE B 1 97  ? 40.437 -16.443 81.741  1.00 29.51 ? 97  PHE B O   1 
ATOM   3601 C CB  . PHE B 1 97  ? 39.614 -15.709 78.928  1.00 25.79 ? 97  PHE B CB  1 
ATOM   3602 C CG  . PHE B 1 97  ? 38.540 -14.977 78.194  1.00 24.93 ? 97  PHE B CG  1 
ATOM   3603 C CD1 . PHE B 1 97  ? 37.927 -13.866 78.769  1.00 24.38 ? 97  PHE B CD1 1 
ATOM   3604 C CD2 . PHE B 1 97  ? 38.223 -15.318 76.885  1.00 22.21 ? 97  PHE B CD2 1 
ATOM   3605 C CE1 . PHE B 1 97  ? 37.028 -13.103 78.059  1.00 29.59 ? 97  PHE B CE1 1 
ATOM   3606 C CE2 . PHE B 1 97  ? 37.322 -14.560 76.158  1.00 25.81 ? 97  PHE B CE2 1 
ATOM   3607 C CZ  . PHE B 1 97  ? 36.721 -13.448 76.740  1.00 31.54 ? 97  PHE B CZ  1 
ATOM   3608 N N   . PHE B 1 98  ? 40.987 -18.263 80.498  1.00 23.54 ? 98  PHE B N   1 
ATOM   3609 C CA  . PHE B 1 98  ? 42.137 -18.658 81.297  1.00 25.37 ? 98  PHE B CA  1 
ATOM   3610 C C   . PHE B 1 98  ? 43.413 -18.305 80.548  1.00 31.85 ? 98  PHE B C   1 
ATOM   3611 O O   . PHE B 1 98  ? 43.746 -18.959 79.554  1.00 33.22 ? 98  PHE B O   1 
ATOM   3612 C CB  . PHE B 1 98  ? 42.151 -20.148 81.535  1.00 22.58 ? 98  PHE B CB  1 
ATOM   3613 C CG  . PHE B 1 98  ? 43.223 -20.559 82.460  1.00 30.39 ? 98  PHE B CG  1 
ATOM   3614 C CD1 . PHE B 1 98  ? 44.513 -20.764 81.994  1.00 26.40 ? 98  PHE B CD1 1 
ATOM   3615 C CD2 . PHE B 1 98  ? 42.973 -20.643 83.829  1.00 34.14 ? 98  PHE B CD2 1 
ATOM   3616 C CE1 . PHE B 1 98  ? 45.538 -21.039 82.866  1.00 30.07 ? 98  PHE B CE1 1 
ATOM   3617 C CE2 . PHE B 1 98  ? 43.997 -20.919 84.719  1.00 34.48 ? 98  PHE B CE2 1 
ATOM   3618 C CZ  . PHE B 1 98  ? 45.288 -21.117 84.236  1.00 35.86 ? 98  PHE B CZ  1 
ATOM   3619 N N   . LEU B 1 99  ? 44.138 -17.293 81.009  1.00 36.04 ? 99  LEU B N   1 
ATOM   3620 C CA  . LEU B 1 99  ? 45.368 -16.896 80.325  1.00 40.62 ? 99  LEU B CA  1 
ATOM   3621 C C   . LEU B 1 99  ? 46.663 -17.363 81.036  1.00 44.73 ? 99  LEU B C   1 
ATOM   3622 O O   . LEU B 1 99  ? 46.768 -17.286 82.266  1.00 47.13 ? 99  LEU B O   1 
ATOM   3623 C CB  . LEU B 1 99  ? 45.389 -15.362 80.117  1.00 39.08 ? 99  LEU B CB  1 
ATOM   3624 C CG  . LEU B 1 99  ? 44.425 -14.617 79.174  1.00 35.26 ? 99  LEU B CG  1 
ATOM   3625 C CD1 . LEU B 1 99  ? 43.862 -15.543 78.107  1.00 33.20 ? 99  LEU B CD1 1 
ATOM   3626 C CD2 . LEU B 1 99  ? 43.316 -13.959 79.932  1.00 28.40 ? 99  LEU B CD2 1 
ATOM   3627 N N   . THR B 1 100 ? 47.631 -17.859 80.261  1.00 46.36 ? 100 THR B N   1 
ATOM   3628 C CA  . THR B 1 100 ? 48.932 -18.328 80.773  1.00 46.09 ? 100 THR B CA  1 
ATOM   3629 C C   . THR B 1 100 ? 49.981 -17.912 79.752  1.00 50.77 ? 100 THR B C   1 
ATOM   3630 O O   . THR B 1 100 ? 49.829 -18.196 78.553  1.00 49.19 ? 100 THR B O   1 
ATOM   3631 C CB  . THR B 1 100 ? 49.040 -19.870 80.854  1.00 41.18 ? 100 THR B CB  1 
ATOM   3632 O OG1 . THR B 1 100 ? 47.961 -20.410 81.611  1.00 45.59 ? 100 THR B OG1 1 
ATOM   3633 C CG2 . THR B 1 100 ? 50.313 -20.249 81.537  1.00 38.93 ? 100 THR B CG2 1 
ATOM   3634 N N   . SER B 1 101 ? 51.085 -17.347 80.234  1.00 54.23 ? 101 SER B N   1 
ATOM   3635 C CA  . SER B 1 101 ? 52.160 -16.881 79.356  1.00 61.09 ? 101 SER B CA  1 
ATOM   3636 C C   . SER B 1 101 ? 52.864 -17.931 78.473  1.00 68.17 ? 101 SER B C   1 
ATOM   3637 O O   . SER B 1 101 ? 53.243 -17.632 77.328  1.00 69.26 ? 101 SER B O   1 
ATOM   3638 C CB  . SER B 1 101 ? 53.220 -16.129 80.162  1.00 54.20 ? 101 SER B CB  1 
ATOM   3639 O OG  . SER B 1 101 ? 54.139 -17.027 80.754  1.00 54.89 ? 101 SER B OG  1 
ATOM   3640 N N   . ASP B 1 102 ? 53.069 -19.141 78.993  1.00 74.80 ? 102 ASP B N   1 
ATOM   3641 C CA  . ASP B 1 102 ? 53.783 -20.142 78.204  1.00 80.44 ? 102 ASP B CA  1 
ATOM   3642 C C   . ASP B 1 102 ? 53.060 -21.360 77.634  1.00 83.42 ? 102 ASP B C   1 
ATOM   3643 O O   . ASP B 1 102 ? 52.963 -21.487 76.410  1.00 86.06 ? 102 ASP B O   1 
ATOM   3644 C CB  . ASP B 1 102 ? 55.057 -20.590 78.923  1.00 80.61 ? 102 ASP B CB  1 
ATOM   3645 C CG  . ASP B 1 102 ? 56.190 -20.891 77.955  1.00 79.62 ? 102 ASP B CG  1 
ATOM   3646 O OD1 . ASP B 1 102 ? 55.919 -21.208 76.774  1.00 80.11 ? 102 ASP B OD1 1 
ATOM   3647 O OD2 . ASP B 1 102 ? 57.360 -20.792 78.374  1.00 81.81 ? 102 ASP B OD2 1 
ATOM   3648 N N   . ASN B 1 103 ? 52.635 -22.289 78.494  1.00 84.97 ? 103 ASN B N   1 
ATOM   3649 C CA  . ASN B 1 103 ? 51.960 -23.507 78.023  1.00 85.59 ? 103 ASN B CA  1 
ATOM   3650 C C   . ASN B 1 103 ? 51.017 -23.324 76.827  1.00 82.39 ? 103 ASN B C   1 
ATOM   3651 O O   . ASN B 1 103 ? 49.940 -22.735 76.945  1.00 83.71 ? 103 ASN B O   1 
ATOM   3652 C CB  . ASN B 1 103 ? 51.268 -24.273 79.164  1.00 89.87 ? 103 ASN B CB  1 
ATOM   3653 C CG  . ASN B 1 103 ? 50.672 -23.363 80.213  1.00 94.88 ? 103 ASN B CG  1 
ATOM   3654 O OD1 . ASN B 1 103 ? 51.355 -22.976 81.161  1.00 97.33 ? 103 ASN B OD1 1 
ATOM   3655 N ND2 . ASN B 1 103 ? 49.396 -23.026 80.062  1.00 97.20 ? 103 ASN B ND2 1 
ATOM   3656 N N   . PRO B 1 104 ? 51.393 -23.909 75.676  1.00 78.05 ? 104 PRO B N   1 
ATOM   3657 C CA  . PRO B 1 104 ? 50.737 -23.920 74.366  1.00 74.25 ? 104 PRO B CA  1 
ATOM   3658 C C   . PRO B 1 104 ? 49.300 -24.435 74.301  1.00 71.50 ? 104 PRO B C   1 
ATOM   3659 O O   . PRO B 1 104 ? 48.774 -24.679 73.216  1.00 70.60 ? 104 PRO B O   1 
ATOM   3660 C CB  . PRO B 1 104 ? 51.668 -24.804 73.543  1.00 76.45 ? 104 PRO B CB  1 
ATOM   3661 C CG  . PRO B 1 104 ? 52.189 -25.769 74.561  1.00 76.41 ? 104 PRO B CG  1 
ATOM   3662 C CD  . PRO B 1 104 ? 52.552 -24.821 75.660  1.00 77.63 ? 104 PRO B CD  1 
ATOM   3663 N N   . ILE B 1 105 ? 48.670 -24.633 75.447  1.00 68.02 ? 105 ILE B N   1 
ATOM   3664 C CA  . ILE B 1 105 ? 47.301 -25.104 75.450  1.00 62.56 ? 105 ILE B CA  1 
ATOM   3665 C C   . ILE B 1 105 ? 46.364 -23.910 75.616  1.00 60.06 ? 105 ILE B C   1 
ATOM   3666 O O   . ILE B 1 105 ? 45.261 -23.910 75.079  1.00 60.22 ? 105 ILE B O   1 
ATOM   3667 C CB  . ILE B 1 105 ? 47.063 -26.145 76.567  1.00 64.22 ? 105 ILE B CB  1 
ATOM   3668 C CG1 . ILE B 1 105 ? 45.665 -26.744 76.441  1.00 65.20 ? 105 ILE B CG1 1 
ATOM   3669 C CG2 . ILE B 1 105 ? 47.270 -25.528 77.941  1.00 65.52 ? 105 ILE B CG2 1 
ATOM   3670 C CD1 . ILE B 1 105 ? 45.470 -27.543 75.170  1.00 67.45 ? 105 ILE B CD1 1 
ATOM   3671 N N   . PHE B 1 106 ? 46.836 -22.869 76.304  1.00 55.23 ? 106 PHE B N   1 
ATOM   3672 C CA  . PHE B 1 106 ? 46.037 -21.671 76.558  1.00 51.27 ? 106 PHE B CA  1 
ATOM   3673 C C   . PHE B 1 106 ? 46.675 -20.457 75.906  1.00 46.20 ? 106 PHE B C   1 
ATOM   3674 O O   . PHE B 1 106 ? 47.864 -20.488 75.594  1.00 49.18 ? 106 PHE B O   1 
ATOM   3675 C CB  . PHE B 1 106 ? 45.922 -21.436 78.069  1.00 54.21 ? 106 PHE B CB  1 
ATOM   3676 C CG  . PHE B 1 106 ? 45.343 -22.609 78.829  1.00 62.01 ? 106 PHE B CG  1 
ATOM   3677 C CD1 . PHE B 1 106 ? 44.248 -23.314 78.331  1.00 62.78 ? 106 PHE B CD1 1 
ATOM   3678 C CD2 . PHE B 1 106 ? 45.897 -23.014 80.040  1.00 66.44 ? 106 PHE B CD2 1 
ATOM   3679 C CE1 . PHE B 1 106 ? 43.713 -24.406 79.021  1.00 63.12 ? 106 PHE B CE1 1 
ATOM   3680 C CE2 . PHE B 1 106 ? 45.367 -24.104 80.739  1.00 68.31 ? 106 PHE B CE2 1 
ATOM   3681 C CZ  . PHE B 1 106 ? 44.271 -24.800 80.223  1.00 65.56 ? 106 PHE B CZ  1 
ATOM   3682 N N   . SER B 1 107 ? 45.898 -19.394 75.702  1.00 40.16 ? 107 SER B N   1 
ATOM   3683 C CA  . SER B 1 107 ? 46.430 -18.171 75.098  1.00 34.29 ? 107 SER B CA  1 
ATOM   3684 C C   . SER B 1 107 ? 47.032 -17.233 76.141  1.00 29.58 ? 107 SER B C   1 
ATOM   3685 O O   . SER B 1 107 ? 46.805 -17.391 77.330  1.00 28.59 ? 107 SER B O   1 
ATOM   3686 C CB  . SER B 1 107 ? 45.350 -17.422 74.314  1.00 35.23 ? 107 SER B CB  1 
ATOM   3687 O OG  . SER B 1 107 ? 45.873 -16.233 73.722  1.00 35.53 ? 107 SER B OG  1 
ATOM   3688 N N   . ASP B 1 108 ? 47.729 -16.207 75.674  1.00 28.52 ? 108 ASP B N   1 
ATOM   3689 C CA  . ASP B 1 108 ? 48.368 -15.236 76.554  1.00 27.38 ? 108 ASP B CA  1 
ATOM   3690 C C   . ASP B 1 108 ? 47.941 -13.787 76.291  1.00 27.03 ? 108 ASP B C   1 
ATOM   3691 O O   . ASP B 1 108 ? 48.689 -12.872 76.591  1.00 29.05 ? 108 ASP B O   1 
ATOM   3692 C CB  . ASP B 1 108 ? 49.875 -15.335 76.408  1.00 29.88 ? 108 ASP B CB  1 
ATOM   3693 C CG  . ASP B 1 108 ? 50.345 -14.906 75.049  1.00 30.08 ? 108 ASP B CG  1 
ATOM   3694 O OD1 . ASP B 1 108 ? 49.647 -15.184 74.050  1.00 36.74 ? 108 ASP B OD1 1 
ATOM   3695 O OD2 . ASP B 1 108 ? 51.414 -14.277 74.980  1.00 39.73 ? 108 ASP B OD2 1 
ATOM   3696 N N   . HIS B 1 109 ? 46.803 -13.591 75.630  1.00 25.81 ? 109 HIS B N   1 
ATOM   3697 C CA  . HIS B 1 109 ? 46.256 -12.256 75.366  1.00 25.65 ? 109 HIS B CA  1 
ATOM   3698 C C   . HIS B 1 109 ? 44.755 -12.308 75.087  1.00 20.94 ? 109 HIS B C   1 
ATOM   3699 O O   . HIS B 1 109 ? 44.221 -13.337 74.684  1.00 16.41 ? 109 HIS B O   1 
ATOM   3700 C CB  . HIS B 1 109 ? 46.975 -11.552 74.224  1.00 29.23 ? 109 HIS B CB  1 
ATOM   3701 C CG  . HIS B 1 109 ? 46.973 -12.321 72.944  1.00 40.12 ? 109 HIS B CG  1 
ATOM   3702 N ND1 . HIS B 1 109 ? 47.870 -13.336 72.688  1.00 46.94 ? 109 HIS B ND1 1 
ATOM   3703 C CD2 . HIS B 1 109 ? 46.240 -12.174 71.817  1.00 40.29 ? 109 HIS B CD2 1 
ATOM   3704 C CE1 . HIS B 1 109 ? 47.702 -13.777 71.455  1.00 44.65 ? 109 HIS B CE1 1 
ATOM   3705 N NE2 . HIS B 1 109 ? 46.718 -13.086 70.904  1.00 50.67 ? 109 HIS B NE2 1 
ATOM   3706 N N   . GLN B 1 110 ? 44.072 -11.206 75.343  1.00 19.99 ? 110 GLN B N   1 
ATOM   3707 C CA  . GLN B 1 110 ? 42.647 -11.140 75.124  1.00 19.59 ? 110 GLN B CA  1 
ATOM   3708 C C   . GLN B 1 110 ? 42.273 -9.690  75.028  1.00 24.47 ? 110 GLN B C   1 
ATOM   3709 O O   . GLN B 1 110 ? 42.740 -8.881  75.826  1.00 29.02 ? 110 GLN B O   1 
ATOM   3710 C CB  . GLN B 1 110 ? 41.899 -11.775 76.295  1.00 27.07 ? 110 GLN B CB  1 
ATOM   3711 C CG  . GLN B 1 110 ? 40.365 -11.653 76.233  1.00 28.11 ? 110 GLN B CG  1 
ATOM   3712 C CD  . GLN B 1 110 ? 39.766 -12.279 74.974  1.00 28.80 ? 110 GLN B CD  1 
ATOM   3713 O OE1 . GLN B 1 110 ? 38.754 -11.810 74.465  1.00 33.54 ? 110 GLN B OE1 1 
ATOM   3714 N NE2 . GLN B 1 110 ? 40.381 -13.352 74.480  1.00 36.83 ? 110 GLN B NE2 1 
ATOM   3715 N N   . LYS B 1 111 ? 41.466 -9.348  74.030  1.00 27.99 ? 111 LYS B N   1 
ATOM   3716 C CA  . LYS B 1 111 ? 41.023 -7.970  73.865  1.00 28.17 ? 111 LYS B CA  1 
ATOM   3717 C C   . LYS B 1 111 ? 39.800 -7.752  74.726  1.00 24.50 ? 111 LYS B C   1 
ATOM   3718 O O   . LYS B 1 111 ? 38.983 -8.651  74.883  1.00 22.71 ? 111 LYS B O   1 
ATOM   3719 C CB  . LYS B 1 111 ? 40.655 -7.671  72.415  1.00 33.11 ? 111 LYS B CB  1 
ATOM   3720 C CG  . LYS B 1 111 ? 40.466 -6.190  72.135  1.00 35.63 ? 111 LYS B CG  1 
ATOM   3721 C CD  . LYS B 1 111 ? 39.793 -5.970  70.805  1.00 44.12 ? 111 LYS B CD  1 
ATOM   3722 C CE  . LYS B 1 111 ? 38.349 -6.424  70.835  1.00 46.85 ? 111 LYS B CE  1 
ATOM   3723 N NZ  . LYS B 1 111 ? 37.571 -5.530  71.719  1.00 53.34 ? 111 LYS B NZ  1 
ATOM   3724 N N   . ILE B 1 112 ? 39.672 -6.545  75.261  1.00 19.71 ? 112 ILE B N   1 
ATOM   3725 C CA  . ILE B 1 112 ? 38.544 -6.196  76.088  1.00 17.64 ? 112 ILE B CA  1 
ATOM   3726 C C   . ILE B 1 112 ? 37.970 -4.922  75.524  1.00 15.35 ? 112 ILE B C   1 
ATOM   3727 O O   . ILE B 1 112 ? 38.660 -3.927  75.455  1.00 17.89 ? 112 ILE B O   1 
ATOM   3728 C CB  . ILE B 1 112 ? 38.968 -5.953  77.558  1.00 19.72 ? 112 ILE B CB  1 
ATOM   3729 C CG1 . ILE B 1 112 ? 39.562 -7.231  78.172  1.00 14.46 ? 112 ILE B CG1 1 
ATOM   3730 C CG2 . ILE B 1 112 ? 37.766 -5.518  78.371  1.00 26.88 ? 112 ILE B CG2 1 
ATOM   3731 C CD1 . ILE B 1 112 ? 40.176 -7.006  79.505  1.00 9.39  ? 112 ILE B CD1 1 
ATOM   3732 N N   . PRO B 1 113 ? 36.698 -4.939  75.099  1.00 14.49 ? 113 PRO B N   1 
ATOM   3733 C CA  . PRO B 1 113 ? 36.010 -3.785  74.533  1.00 14.28 ? 113 PRO B CA  1 
ATOM   3734 C C   . PRO B 1 113 ? 35.844 -2.655  75.549  1.00 20.73 ? 113 PRO B C   1 
ATOM   3735 O O   . PRO B 1 113 ? 35.634 -2.900  76.735  1.00 26.65 ? 113 PRO B O   1 
ATOM   3736 C CB  . PRO B 1 113 ? 34.648 -4.369  74.170  1.00 12.75 ? 113 PRO B CB  1 
ATOM   3737 C CG  . PRO B 1 113 ? 34.938 -5.803  73.938  1.00 13.67 ? 113 PRO B CG  1 
ATOM   3738 C CD  . PRO B 1 113 ? 35.800 -6.101  75.104  1.00 15.67 ? 113 PRO B CD  1 
ATOM   3739 N N   . ALA B 1 114 ? 35.903 -1.419  75.065  1.00 22.32 ? 114 ALA B N   1 
ATOM   3740 C CA  . ALA B 1 114 ? 35.747 -0.230  75.884  1.00 19.14 ? 114 ALA B CA  1 
ATOM   3741 C C   . ALA B 1 114 ? 34.492 -0.289  76.770  1.00 25.88 ? 114 ALA B C   1 
ATOM   3742 O O   . ALA B 1 114 ? 33.418 -0.727  76.329  1.00 26.43 ? 114 ALA B O   1 
ATOM   3743 C CB  . ALA B 1 114 ? 35.676 0.994   74.985  1.00 20.76 ? 114 ALA B CB  1 
ATOM   3744 N N   . GLY B 1 115 ? 34.649 0.140   78.025  1.00 25.47 ? 115 GLY B N   1 
ATOM   3745 C CA  . GLY B 1 115 ? 33.553 0.161   78.976  1.00 19.96 ? 115 GLY B CA  1 
ATOM   3746 C C   . GLY B 1 115 ? 32.903 -1.166  79.324  1.00 20.61 ? 115 GLY B C   1 
ATOM   3747 O O   . GLY B 1 115 ? 31.720 -1.195  79.682  1.00 20.76 ? 115 GLY B O   1 
ATOM   3748 N N   . THR B 1 116 ? 33.650 -2.263  79.222  1.00 17.67 ? 116 THR B N   1 
ATOM   3749 C CA  . THR B 1 116 ? 33.113 -3.578  79.560  1.00 16.68 ? 116 THR B CA  1 
ATOM   3750 C C   . THR B 1 116 ? 33.604 -3.918  80.968  1.00 21.43 ? 116 THR B C   1 
ATOM   3751 O O   . THR B 1 116 ? 34.816 -3.919  81.219  1.00 24.27 ? 116 THR B O   1 
ATOM   3752 C CB  . THR B 1 116 ? 33.632 -4.642  78.597  1.00 8.24  ? 116 THR B CB  1 
ATOM   3753 O OG1 . THR B 1 116 ? 33.391 -4.198  77.262  1.00 25.46 ? 116 THR B OG1 1 
ATOM   3754 C CG2 . THR B 1 116 ? 32.937 -5.987  78.825  1.00 2.00  ? 116 THR B CG2 1 
ATOM   3755 N N   . ILE B 1 117 ? 32.680 -4.184  81.887  1.00 22.74 ? 117 ILE B N   1 
ATOM   3756 C CA  . ILE B 1 117 ? 33.063 -4.511  83.261  1.00 24.56 ? 117 ILE B CA  1 
ATOM   3757 C C   . ILE B 1 117 ? 33.822 -5.832  83.277  1.00 25.43 ? 117 ILE B C   1 
ATOM   3758 O O   . ILE B 1 117 ? 33.417 -6.788  82.609  1.00 28.88 ? 117 ILE B O   1 
ATOM   3759 C CB  . ILE B 1 117 ? 31.815 -4.528  84.215  1.00 25.69 ? 117 ILE B CB  1 
ATOM   3760 C CG1 . ILE B 1 117 ? 31.426 -3.086  84.552  1.00 28.07 ? 117 ILE B CG1 1 
ATOM   3761 C CG2 . ILE B 1 117 ? 32.105 -5.279  85.504  1.00 24.06 ? 117 ILE B CG2 1 
ATOM   3762 C CD1 . ILE B 1 117 ? 30.170 -2.951  85.326  1.00 33.79 ? 117 ILE B CD1 1 
ATOM   3763 N N   . PHE B 1 118 ? 34.969 -5.855  83.949  1.00 22.33 ? 118 PHE B N   1 
ATOM   3764 C CA  . PHE B 1 118 ? 35.763 -7.073  84.034  1.00 25.12 ? 118 PHE B CA  1 
ATOM   3765 C C   . PHE B 1 118 ? 36.510 -7.148  85.360  1.00 27.36 ? 118 PHE B C   1 
ATOM   3766 O O   . PHE B 1 118 ? 36.729 -6.124  86.015  1.00 29.10 ? 118 PHE B O   1 
ATOM   3767 C CB  . PHE B 1 118 ? 36.781 -7.132  82.894  1.00 18.50 ? 118 PHE B CB  1 
ATOM   3768 C CG  . PHE B 1 118 ? 37.828 -6.042  82.959  1.00 24.65 ? 118 PHE B CG  1 
ATOM   3769 C CD1 . PHE B 1 118 ? 37.500 -4.715  82.651  1.00 28.06 ? 118 PHE B CD1 1 
ATOM   3770 C CD2 . PHE B 1 118 ? 39.144 -6.336  83.318  1.00 18.64 ? 118 PHE B CD2 1 
ATOM   3771 C CE1 . PHE B 1 118 ? 38.469 -3.697  82.697  1.00 20.69 ? 118 PHE B CE1 1 
ATOM   3772 C CE2 . PHE B 1 118 ? 40.123 -5.325  83.367  1.00 14.14 ? 118 PHE B CE2 1 
ATOM   3773 C CZ  . PHE B 1 118 ? 39.785 -4.010  83.057  1.00 17.22 ? 118 PHE B CZ  1 
ATOM   3774 N N   . TYR B 1 119 ? 36.860 -8.370  85.765  1.00 26.71 ? 119 TYR B N   1 
ATOM   3775 C CA  . TYR B 1 119 ? 37.641 -8.601  86.974  1.00 26.07 ? 119 TYR B CA  1 
ATOM   3776 C C   . TYR B 1 119 ? 38.696 -9.668  86.674  1.00 25.16 ? 119 TYR B C   1 
ATOM   3777 O O   . TYR B 1 119 ? 38.513 -10.500 85.791  1.00 26.43 ? 119 TYR B O   1 
ATOM   3778 C CB  . TYR B 1 119 ? 36.772 -8.902  88.202  1.00 21.57 ? 119 TYR B CB  1 
ATOM   3779 C CG  . TYR B 1 119 ? 35.775 -10.036 88.092  1.00 21.33 ? 119 TYR B CG  1 
ATOM   3780 C CD1 . TYR B 1 119 ? 34.476 -9.812  87.628  1.00 18.82 ? 119 TYR B CD1 1 
ATOM   3781 C CD2 . TYR B 1 119 ? 36.092 -11.307 88.556  1.00 16.58 ? 119 TYR B CD2 1 
ATOM   3782 C CE1 . TYR B 1 119 ? 33.511 -10.817 87.643  1.00 18.22 ? 119 TYR B CE1 1 
ATOM   3783 C CE2 . TYR B 1 119 ? 35.139 -12.321 88.572  1.00 22.38 ? 119 TYR B CE2 1 
ATOM   3784 C CZ  . TYR B 1 119 ? 33.853 -12.073 88.122  1.00 22.15 ? 119 TYR B CZ  1 
ATOM   3785 O OH  . TYR B 1 119 ? 32.915 -13.078 88.190  1.00 21.55 ? 119 TYR B OH  1 
ATOM   3786 N N   . LEU B 1 120 ? 39.804 -9.618  87.400  1.00 31.54 ? 120 LEU B N   1 
ATOM   3787 C CA  . LEU B 1 120 ? 40.949 -10.507 87.191  1.00 32.45 ? 120 LEU B CA  1 
ATOM   3788 C C   . LEU B 1 120 ? 41.319 -11.289 88.461  1.00 35.35 ? 120 LEU B C   1 
ATOM   3789 O O   . LEU B 1 120 ? 41.226 -10.775 89.587  1.00 35.73 ? 120 LEU B O   1 
ATOM   3790 C CB  . LEU B 1 120 ? 42.131 -9.619  86.799  1.00 33.61 ? 120 LEU B CB  1 
ATOM   3791 C CG  . LEU B 1 120 ? 43.073 -9.764  85.622  1.00 29.91 ? 120 LEU B CG  1 
ATOM   3792 C CD1 . LEU B 1 120 ? 42.356 -10.050 84.336  1.00 30.60 ? 120 LEU B CD1 1 
ATOM   3793 C CD2 . LEU B 1 120 ? 43.805 -8.451  85.520  1.00 34.51 ? 120 LEU B CD2 1 
ATOM   3794 N N   . VAL B 1 121 ? 41.777 -12.518 88.261  1.00 36.82 ? 121 VAL B N   1 
ATOM   3795 C CA  . VAL B 1 121 ? 42.173 -13.407 89.347  1.00 35.03 ? 121 VAL B CA  1 
ATOM   3796 C C   . VAL B 1 121 ? 43.555 -13.995 89.010  1.00 35.16 ? 121 VAL B C   1 
ATOM   3797 O O   . VAL B 1 121 ? 43.841 -14.307 87.844  1.00 31.36 ? 121 VAL B O   1 
ATOM   3798 C CB  . VAL B 1 121 ? 41.173 -14.633 89.480  1.00 36.45 ? 121 VAL B CB  1 
ATOM   3799 C CG1 . VAL B 1 121 ? 41.676 -15.622 90.536  1.00 32.32 ? 121 VAL B CG1 1 
ATOM   3800 C CG2 . VAL B 1 121 ? 39.727 -14.178 89.801  1.00 29.52 ? 121 VAL B CG2 1 
ATOM   3801 N N   . ASN B 1 122 ? 44.422 -14.085 90.016  1.00 33.74 ? 122 ASN B N   1 
ATOM   3802 C CA  . ASN B 1 122 ? 45.739 -14.717 89.876  1.00 33.80 ? 122 ASN B CA  1 
ATOM   3803 C C   . ASN B 1 122 ? 45.526 -16.040 90.632  1.00 37.46 ? 122 ASN B C   1 
ATOM   3804 O O   . ASN B 1 122 ? 45.531 -16.068 91.863  1.00 36.36 ? 122 ASN B O   1 
ATOM   3805 C CB  . ASN B 1 122 ? 46.820 -13.891 90.556  1.00 29.92 ? 122 ASN B CB  1 
ATOM   3806 C CG  . ASN B 1 122 ? 48.153 -14.595 90.593  1.00 33.53 ? 122 ASN B CG  1 
ATOM   3807 O OD1 . ASN B 1 122 ? 48.283 -15.715 90.111  1.00 38.87 ? 122 ASN B OD1 1 
ATOM   3808 N ND2 . ASN B 1 122 ? 49.157 -13.946 91.170  1.00 33.86 ? 122 ASN B ND2 1 
ATOM   3809 N N   . PRO B 1 123 ? 45.276 -17.144 89.901  1.00 40.60 ? 123 PRO B N   1 
ATOM   3810 C CA  . PRO B 1 123 ? 45.037 -18.466 90.489  1.00 42.10 ? 123 PRO B CA  1 
ATOM   3811 C C   . PRO B 1 123 ? 46.212 -19.207 91.142  1.00 44.70 ? 123 PRO B C   1 
ATOM   3812 O O   . PRO B 1 123 ? 46.017 -19.936 92.115  1.00 49.60 ? 123 PRO B O   1 
ATOM   3813 C CB  . PRO B 1 123 ? 44.478 -19.247 89.306  1.00 40.43 ? 123 PRO B CB  1 
ATOM   3814 C CG  . PRO B 1 123 ? 45.297 -18.742 88.189  1.00 36.91 ? 123 PRO B CG  1 
ATOM   3815 C CD  . PRO B 1 123 ? 45.284 -17.237 88.427  1.00 39.25 ? 123 PRO B CD  1 
ATOM   3816 N N   . ASP B 1 124 ? 47.423 -19.019 90.632  1.00 45.32 ? 124 ASP B N   1 
ATOM   3817 C CA  . ASP B 1 124 ? 48.584 -19.724 91.175  1.00 47.06 ? 124 ASP B CA  1 
ATOM   3818 C C   . ASP B 1 124 ? 48.914 -19.431 92.642  1.00 48.14 ? 124 ASP B C   1 
ATOM   3819 O O   . ASP B 1 124 ? 48.716 -18.314 93.130  1.00 45.67 ? 124 ASP B O   1 
ATOM   3820 C CB  . ASP B 1 124 ? 49.821 -19.464 90.316  1.00 51.05 ? 124 ASP B CB  1 
ATOM   3821 C CG  . ASP B 1 124 ? 50.696 -20.691 90.184  1.00 49.90 ? 124 ASP B CG  1 
ATOM   3822 O OD1 . ASP B 1 124 ? 50.269 -21.630 89.485  1.00 54.65 ? 124 ASP B OD1 1 
ATOM   3823 O OD2 . ASP B 1 124 ? 51.782 -20.733 90.795  1.00 44.89 ? 124 ASP B OD2 1 
ATOM   3824 N N   . PRO B 1 125 ? 49.446 -20.443 93.359  1.00 49.25 ? 125 PRO B N   1 
ATOM   3825 C CA  . PRO B 1 125 ? 49.800 -20.274 94.766  1.00 46.94 ? 125 PRO B CA  1 
ATOM   3826 C C   . PRO B 1 125 ? 51.247 -19.837 94.913  1.00 45.99 ? 125 PRO B C   1 
ATOM   3827 O O   . PRO B 1 125 ? 51.652 -19.421 95.993  1.00 44.75 ? 125 PRO B O   1 
ATOM   3828 C CB  . PRO B 1 125 ? 49.614 -21.685 95.345  1.00 47.67 ? 125 PRO B CB  1 
ATOM   3829 C CG  . PRO B 1 125 ? 49.113 -22.559 94.174  1.00 45.06 ? 125 PRO B CG  1 
ATOM   3830 C CD  . PRO B 1 125 ? 49.610 -21.854 92.966  1.00 48.35 ? 125 PRO B CD  1 
ATOM   3831 N N   . LYS B 1 126 ? 52.023 -19.945 93.833  1.00 44.61 ? 126 LYS B N   1 
ATOM   3832 C CA  . LYS B 1 126 ? 53.442 -19.581 93.879  1.00 48.61 ? 126 LYS B CA  1 
ATOM   3833 C C   . LYS B 1 126 ? 53.824 -18.380 93.020  1.00 47.22 ? 126 LYS B C   1 
ATOM   3834 O O   . LYS B 1 126 ? 54.443 -17.434 93.504  1.00 45.74 ? 126 LYS B O   1 
ATOM   3835 C CB  . LYS B 1 126 ? 54.329 -20.769 93.461  1.00 51.35 ? 126 LYS B CB  1 
ATOM   3836 C CG  . LYS B 1 126 ? 54.065 -22.083 94.194  1.00 53.69 ? 126 LYS B CG  1 
ATOM   3837 C CD  . LYS B 1 126 ? 55.369 -22.823 94.564  1.00 58.43 ? 126 LYS B CD  1 
ATOM   3838 C CE  . LYS B 1 126 ? 56.255 -23.179 93.359  1.00 60.23 ? 126 LYS B CE  1 
ATOM   3839 N NZ  . LYS B 1 126 ? 57.534 -23.863 93.772  1.00 55.36 ? 126 LYS B NZ  1 
ATOM   3840 N N   . GLU B 1 127 ? 53.496 -18.470 91.733  1.00 49.85 ? 127 GLU B N   1 
ATOM   3841 C CA  . GLU B 1 127 ? 53.799 -17.452 90.735  1.00 51.34 ? 127 GLU B CA  1 
ATOM   3842 C C   . GLU B 1 127 ? 52.977 -16.180 90.803  1.00 49.96 ? 127 GLU B C   1 
ATOM   3843 O O   . GLU B 1 127 ? 51.803 -16.207 91.181  1.00 49.76 ? 127 GLU B O   1 
ATOM   3844 C CB  . GLU B 1 127 ? 53.649 -18.048 89.331  1.00 59.45 ? 127 GLU B CB  1 
ATOM   3845 C CG  . GLU B 1 127 ? 54.959 -18.447 88.646  1.00 72.34 ? 127 GLU B CG  1 
ATOM   3846 C CD  . GLU B 1 127 ? 55.637 -17.295 87.888  1.00 80.38 ? 127 GLU B CD  1 
ATOM   3847 O OE1 . GLU B 1 127 ? 55.974 -16.254 88.516  1.00 82.59 ? 127 GLU B OE1 1 
ATOM   3848 O OE2 . GLU B 1 127 ? 55.845 -17.449 86.657  1.00 80.83 ? 127 GLU B OE2 1 
ATOM   3849 N N   . ASP B 1 128 ? 53.612 -15.074 90.409  1.00 50.47 ? 128 ASP B N   1 
ATOM   3850 C CA  . ASP B 1 128 ? 52.977 -13.753 90.349  1.00 49.00 ? 128 ASP B CA  1 
ATOM   3851 C C   . ASP B 1 128 ? 52.414 -13.552 88.935  1.00 48.97 ? 128 ASP B C   1 
ATOM   3852 O O   . ASP B 1 128 ? 52.932 -14.117 87.959  1.00 47.17 ? 128 ASP B O   1 
ATOM   3853 C CB  . ASP B 1 128 ? 53.987 -12.627 90.629  1.00 45.76 ? 128 ASP B CB  1 
ATOM   3854 C CG  . ASP B 1 128 ? 54.196 -12.366 92.113  1.00 46.96 ? 128 ASP B CG  1 
ATOM   3855 O OD1 . ASP B 1 128 ? 53.731 -13.175 92.947  1.00 49.86 ? 128 ASP B OD1 1 
ATOM   3856 O OD2 . ASP B 1 128 ? 54.837 -11.338 92.444  1.00 41.97 ? 128 ASP B OD2 1 
ATOM   3857 N N   . LEU B 1 129 ? 51.355 -12.749 88.841  1.00 47.91 ? 129 LEU B N   1 
ATOM   3858 C CA  . LEU B 1 129 ? 50.721 -12.440 87.565  1.00 39.44 ? 129 LEU B CA  1 
ATOM   3859 C C   . LEU B 1 129 ? 51.358 -11.150 87.097  1.00 37.77 ? 129 LEU B C   1 
ATOM   3860 O O   . LEU B 1 129 ? 51.269 -10.130 87.784  1.00 35.88 ? 129 LEU B O   1 
ATOM   3861 C CB  . LEU B 1 129 ? 49.225 -12.188 87.746  1.00 33.12 ? 129 LEU B CB  1 
ATOM   3862 C CG  . LEU B 1 129 ? 48.277 -12.576 86.612  1.00 29.99 ? 129 LEU B CG  1 
ATOM   3863 C CD1 . LEU B 1 129 ? 47.040 -11.724 86.737  1.00 32.95 ? 129 LEU B CD1 1 
ATOM   3864 C CD2 . LEU B 1 129 ? 48.897 -12.409 85.234  1.00 31.17 ? 129 LEU B CD2 1 
ATOM   3865 N N   . ARG B 1 130 ? 52.034 -11.205 85.956  1.00 35.90 ? 130 ARG B N   1 
ATOM   3866 C CA  . ARG B 1 130 ? 52.654 -10.017 85.392  1.00 34.07 ? 130 ARG B CA  1 
ATOM   3867 C C   . ARG B 1 130 ? 52.012 -9.701  84.036  1.00 34.37 ? 130 ARG B C   1 
ATOM   3868 O O   . ARG B 1 130 ? 52.125 -10.467 83.075  1.00 28.16 ? 130 ARG B O   1 
ATOM   3869 C CB  . ARG B 1 130 ? 54.172 -10.183 85.339  1.00 32.81 ? 130 ARG B CB  1 
ATOM   3870 C CG  . ARG B 1 130 ? 54.827 -9.495  86.525  1.00 30.68 ? 130 ARG B CG  1 
ATOM   3871 C CD  . ARG B 1 130 ? 56.257 -9.843  86.704  1.00 20.05 ? 130 ARG B CD  1 
ATOM   3872 N NE  . ARG B 1 130 ? 56.999 -9.965  85.452  1.00 29.67 ? 130 ARG B NE  1 
ATOM   3873 C CZ  . ARG B 1 130 ? 57.737 -9.005  84.904  1.00 30.72 ? 130 ARG B CZ  1 
ATOM   3874 N NH1 . ARG B 1 130 ? 57.821 -7.809  85.471  1.00 35.50 ? 130 ARG B NH1 1 
ATOM   3875 N NH2 . ARG B 1 130 ? 58.535 -9.291  83.886  1.00 37.44 ? 130 ARG B NH2 1 
ATOM   3876 N N   . ILE B 1 131 ? 51.285 -8.586  84.002  1.00 34.36 ? 131 ILE B N   1 
ATOM   3877 C CA  . ILE B 1 131 ? 50.542 -8.151  82.820  1.00 33.84 ? 131 ILE B CA  1 
ATOM   3878 C C   . ILE B 1 131 ? 50.996 -6.797  82.243  1.00 35.92 ? 131 ILE B C   1 
ATOM   3879 O O   . ILE B 1 131 ? 51.385 -5.870  82.976  1.00 37.80 ? 131 ILE B O   1 
ATOM   3880 C CB  . ILE B 1 131 ? 49.002 -8.109  83.138  1.00 28.95 ? 131 ILE B CB  1 
ATOM   3881 C CG1 . ILE B 1 131 ? 48.439 -9.514  83.179  1.00 28.68 ? 131 ILE B CG1 1 
ATOM   3882 C CG2 . ILE B 1 131 ? 48.228 -7.317  82.121  1.00 26.87 ? 131 ILE B CG2 1 
ATOM   3883 C CD1 . ILE B 1 131 ? 46.993 -9.543  83.573  1.00 31.32 ? 131 ILE B CD1 1 
ATOM   3884 N N   . ILE B 1 132 ? 50.922 -6.705  80.917  1.00 32.65 ? 132 ILE B N   1 
ATOM   3885 C CA  . ILE B 1 132 ? 51.272 -5.509  80.170  1.00 27.93 ? 132 ILE B CA  1 
ATOM   3886 C C   . ILE B 1 132 ? 50.123 -5.358  79.161  1.00 25.12 ? 132 ILE B C   1 
ATOM   3887 O O   . ILE B 1 132 ? 49.635 -6.356  78.629  1.00 22.47 ? 132 ILE B O   1 
ATOM   3888 C CB  . ILE B 1 132 ? 52.636 -5.709  79.465  1.00 27.60 ? 132 ILE B CB  1 
ATOM   3889 C CG1 . ILE B 1 132 ? 53.143 -4.392  78.858  1.00 30.08 ? 132 ILE B CG1 1 
ATOM   3890 C CG2 . ILE B 1 132 ? 52.548 -6.838  78.456  1.00 28.30 ? 132 ILE B CG2 1 
ATOM   3891 C CD1 . ILE B 1 132 ? 53.747 -3.412  79.885  1.00 29.16 ? 132 ILE B CD1 1 
ATOM   3892 N N   . GLN B 1 133 ? 49.602 -4.148  78.981  1.00 23.95 ? 133 GLN B N   1 
ATOM   3893 C CA  . GLN B 1 133 ? 48.509 -3.985  78.040  1.00 22.59 ? 133 GLN B CA  1 
ATOM   3894 C C   . GLN B 1 133 ? 48.507 -2.708  77.225  1.00 22.45 ? 133 GLN B C   1 
ATOM   3895 O O   . GLN B 1 133 ? 48.978 -1.674  77.698  1.00 18.24 ? 133 GLN B O   1 
ATOM   3896 C CB  . GLN B 1 133 ? 47.168 -4.151  78.738  1.00 22.35 ? 133 GLN B CB  1 
ATOM   3897 C CG  . GLN B 1 133 ? 46.745 -2.977  79.572  1.00 34.70 ? 133 GLN B CG  1 
ATOM   3898 C CD  . GLN B 1 133 ? 45.737 -3.381  80.618  1.00 37.08 ? 133 GLN B CD  1 
ATOM   3899 O OE1 . GLN B 1 133 ? 44.700 -3.951  80.300  1.00 40.51 ? 133 GLN B OE1 1 
ATOM   3900 N NE2 . GLN B 1 133 ? 46.061 -3.135  81.877  1.00 39.37 ? 133 GLN B NE2 1 
ATOM   3901 N N   . LEU B 1 134 ? 48.047 -2.835  75.969  1.00 20.20 ? 134 LEU B N   1 
ATOM   3902 C CA  . LEU B 1 134 ? 47.928 -1.724  75.040  1.00 17.25 ? 134 LEU B CA  1 
ATOM   3903 C C   . LEU B 1 134 ? 46.503 -1.203  75.217  1.00 18.88 ? 134 LEU B C   1 
ATOM   3904 O O   . LEU B 1 134 ? 45.544 -1.972  75.197  1.00 24.94 ? 134 LEU B O   1 
ATOM   3905 C CB  . LEU B 1 134 ? 48.137 -2.188  73.595  1.00 11.96 ? 134 LEU B CB  1 
ATOM   3906 C CG  . LEU B 1 134 ? 48.093 -1.141  72.469  1.00 17.76 ? 134 LEU B CG  1 
ATOM   3907 C CD1 . LEU B 1 134 ? 49.211 -0.138  72.592  1.00 12.61 ? 134 LEU B CD1 1 
ATOM   3908 C CD2 . LEU B 1 134 ? 48.207 -1.835  71.121  1.00 17.43 ? 134 LEU B CD2 1 
ATOM   3909 N N   . ALA B 1 135 ? 46.374 0.086   75.492  1.00 18.64 ? 135 ALA B N   1 
ATOM   3910 C CA  . ALA B 1 135 ? 45.081 0.688   75.678  1.00 14.40 ? 135 ALA B CA  1 
ATOM   3911 C C   . ALA B 1 135 ? 44.892 1.795   74.640  1.00 15.72 ? 135 ALA B C   1 
ATOM   3912 O O   . ALA B 1 135 ? 45.854 2.429   74.177  1.00 14.04 ? 135 ALA B O   1 
ATOM   3913 C CB  . ALA B 1 135 ? 44.973 1.226   77.080  1.00 20.16 ? 135 ALA B CB  1 
ATOM   3914 N N   . MET B 1 136 ? 43.651 1.983   74.219  1.00 19.09 ? 136 MET B N   1 
ATOM   3915 C CA  . MET B 1 136 ? 43.336 2.992   73.224  1.00 21.71 ? 136 MET B CA  1 
ATOM   3916 C C   . MET B 1 136 ? 42.102 3.749   73.686  1.00 18.75 ? 136 MET B C   1 
ATOM   3917 O O   . MET B 1 136 ? 40.961 3.300   73.489  1.00 7.33  ? 136 MET B O   1 
ATOM   3918 C CB  . MET B 1 136 ? 43.141 2.303   71.867  1.00 31.52 ? 136 MET B CB  1 
ATOM   3919 C CG  . MET B 1 136 ? 44.281 1.297   71.572  1.00 39.80 ? 136 MET B CG  1 
ATOM   3920 S SD  . MET B 1 136 ? 43.840 -0.205  70.666  1.00 54.21 ? 136 MET B SD  1 
ATOM   3921 C CE  . MET B 1 136 ? 43.464 -1.375  71.932  1.00 38.28 ? 136 MET B CE  1 
ATOM   3922 N N   . PRO B 1 137 ? 42.319 4.867   74.409  1.00 21.62 ? 137 PRO B N   1 
ATOM   3923 C CA  . PRO B 1 137 ? 41.228 5.703   74.935  1.00 18.69 ? 137 PRO B CA  1 
ATOM   3924 C C   . PRO B 1 137 ? 40.239 6.218   73.878  1.00 18.33 ? 137 PRO B C   1 
ATOM   3925 O O   . PRO B 1 137 ? 40.614 6.540   72.754  1.00 22.99 ? 137 PRO B O   1 
ATOM   3926 C CB  . PRO B 1 137 ? 41.969 6.841   75.651  1.00 15.62 ? 137 PRO B CB  1 
ATOM   3927 C CG  . PRO B 1 137 ? 43.282 6.223   76.053  1.00 18.62 ? 137 PRO B CG  1 
ATOM   3928 C CD  . PRO B 1 137 ? 43.640 5.377   74.844  1.00 17.22 ? 137 PRO B CD  1 
ATOM   3929 N N   . VAL B 1 138 ? 38.975 6.284   74.275  1.00 16.05 ? 138 VAL B N   1 
ATOM   3930 C CA  . VAL B 1 138 ? 37.856 6.726   73.454  1.00 11.94 ? 138 VAL B CA  1 
ATOM   3931 C C   . VAL B 1 138 ? 37.535 8.232   73.533  1.00 15.73 ? 138 VAL B C   1 
ATOM   3932 O O   . VAL B 1 138 ? 37.337 8.889   72.490  1.00 8.54  ? 138 VAL B O   1 
ATOM   3933 C CB  . VAL B 1 138 ? 36.580 5.956   73.878  1.00 12.62 ? 138 VAL B CB  1 
ATOM   3934 C CG1 . VAL B 1 138 ? 35.382 6.430   73.133  1.00 17.13 ? 138 VAL B CG1 1 
ATOM   3935 C CG2 . VAL B 1 138 ? 36.754 4.469   73.658  1.00 10.56 ? 138 VAL B CG2 1 
ATOM   3936 N N   . ASN B 1 139 ? 37.481 8.776   74.752  1.00 12.34 ? 139 ASN B N   1 
ATOM   3937 C CA  . ASN B 1 139 ? 37.092 10.188  74.963  1.00 18.39 ? 139 ASN B CA  1 
ATOM   3938 C C   . ASN B 1 139 ? 38.114 11.257  74.574  1.00 22.38 ? 139 ASN B C   1 
ATOM   3939 O O   . ASN B 1 139 ? 37.782 12.252  73.917  1.00 20.10 ? 139 ASN B O   1 
ATOM   3940 C CB  . ASN B 1 139 ? 36.639 10.423  76.419  1.00 19.22 ? 139 ASN B CB  1 
ATOM   3941 C CG  . ASN B 1 139 ? 35.423 9.596   76.800  1.00 24.44 ? 139 ASN B CG  1 
ATOM   3942 O OD1 . ASN B 1 139 ? 34.435 9.534   76.064  1.00 28.67 ? 139 ASN B OD1 1 
ATOM   3943 N ND2 . ASN B 1 139 ? 35.491 8.947   77.957  1.00 31.64 ? 139 ASN B ND2 1 
ATOM   3944 N N   . ASN B 1 140 ? 39.329 11.081  75.090  1.00 25.88 ? 140 ASN B N   1 
ATOM   3945 C CA  . ASN B 1 140 ? 40.487 11.949  74.855  1.00 24.02 ? 140 ASN B CA  1 
ATOM   3946 C C   . ASN B 1 140 ? 41.664 11.038  75.207  1.00 23.04 ? 140 ASN B C   1 
ATOM   3947 O O   . ASN B 1 140 ? 41.448 9.952   75.754  1.00 28.01 ? 140 ASN B O   1 
ATOM   3948 C CB  . ASN B 1 140 ? 40.433 13.250  75.681  1.00 27.74 ? 140 ASN B CB  1 
ATOM   3949 C CG  . ASN B 1 140 ? 40.194 13.008  77.155  1.00 25.26 ? 140 ASN B CG  1 
ATOM   3950 O OD1 . ASN B 1 140 ? 40.989 12.354  77.825  1.00 30.36 ? 140 ASN B OD1 1 
ATOM   3951 N ND2 . ASN B 1 140 ? 39.082 13.523  77.664  1.00 26.25 ? 140 ASN B ND2 1 
ATOM   3952 N N   . PRO B 1 141 ? 42.910 11.481  74.983  1.00 17.57 ? 141 PRO B N   1 
ATOM   3953 C CA  . PRO B 1 141 ? 44.087 10.650  75.263  1.00 18.58 ? 141 PRO B CA  1 
ATOM   3954 C C   . PRO B 1 141 ? 44.465 10.188  76.667  1.00 15.75 ? 141 PRO B C   1 
ATOM   3955 O O   . PRO B 1 141 ? 45.529 9.615   76.845  1.00 17.95 ? 141 PRO B O   1 
ATOM   3956 C CB  . PRO B 1 141 ? 45.212 11.425  74.574  1.00 18.04 ? 141 PRO B CB  1 
ATOM   3957 C CG  . PRO B 1 141 ? 44.799 12.835  74.776  1.00 15.24 ? 141 PRO B CG  1 
ATOM   3958 C CD  . PRO B 1 141 ? 43.313 12.824  74.526  1.00 17.34 ? 141 PRO B CD  1 
ATOM   3959 N N   . GLN B 1 142 ? 43.582 10.370  77.637  1.00 20.10 ? 142 GLN B N   1 
ATOM   3960 C CA  . GLN B 1 142 ? 43.856 9.976   79.023  1.00 20.61 ? 142 GLN B CA  1 
ATOM   3961 C C   . GLN B 1 142 ? 43.075 8.732   79.370  1.00 21.56 ? 142 GLN B C   1 
ATOM   3962 O O   . GLN B 1 142 ? 41.935 8.589   78.946  1.00 27.88 ? 142 GLN B O   1 
ATOM   3963 C CB  . GLN B 1 142 ? 43.451 11.098  79.941  1.00 22.16 ? 142 GLN B CB  1 
ATOM   3964 C CG  . GLN B 1 142 ? 44.280 12.315  79.727  1.00 43.43 ? 142 GLN B CG  1 
ATOM   3965 C CD  . GLN B 1 142 ? 44.815 12.805  81.024  1.00 59.44 ? 142 GLN B CD  1 
ATOM   3966 O OE1 . GLN B 1 142 ? 44.316 12.415  82.089  1.00 67.01 ? 142 GLN B OE1 1 
ATOM   3967 N NE2 . GLN B 1 142 ? 45.853 13.639  80.973  1.00 68.73 ? 142 GLN B NE2 1 
ATOM   3968 N N   . ILE B 1 143 ? 43.653 7.839   80.158  1.00 20.17 ? 143 ILE B N   1 
ATOM   3969 C CA  . ILE B 1 143 ? 42.954 6.606   80.471  1.00 23.71 ? 143 ILE B CA  1 
ATOM   3970 C C   . ILE B 1 143 ? 42.168 6.709   81.779  1.00 24.85 ? 143 ILE B C   1 
ATOM   3971 O O   . ILE B 1 143 ? 42.716 7.079   82.802  1.00 28.95 ? 143 ILE B O   1 
ATOM   3972 C CB  . ILE B 1 143 ? 43.941 5.395   80.400  1.00 22.29 ? 143 ILE B CB  1 
ATOM   3973 C CG1 . ILE B 1 143 ? 43.287 4.104   80.874  1.00 26.09 ? 143 ILE B CG1 1 
ATOM   3974 C CG2 . ILE B 1 143 ? 45.169 5.666   81.205  1.00 33.36 ? 143 ILE B CG2 1 
ATOM   3975 C CD1 . ILE B 1 143 ? 42.048 3.769   80.141  1.00 28.59 ? 143 ILE B CD1 1 
ATOM   3976 N N   . HIS B 1 144 ? 40.871 6.421   81.725  1.00 25.32 ? 144 HIS B N   1 
ATOM   3977 C CA  . HIS B 1 144 ? 40.006 6.510   82.902  1.00 25.98 ? 144 HIS B CA  1 
ATOM   3978 C C   . HIS B 1 144 ? 39.409 5.167   83.324  1.00 26.86 ? 144 HIS B C   1 
ATOM   3979 O O   . HIS B 1 144 ? 38.654 4.560   82.571  1.00 23.35 ? 144 HIS B O   1 
ATOM   3980 C CB  . HIS B 1 144 ? 38.848 7.502   82.671  1.00 26.11 ? 144 HIS B CB  1 
ATOM   3981 C CG  . HIS B 1 144 ? 39.275 8.837   82.122  1.00 30.15 ? 144 HIS B CG  1 
ATOM   3982 N ND1 . HIS B 1 144 ? 38.728 9.381   80.973  1.00 23.41 ? 144 HIS B ND1 1 
ATOM   3983 C CD2 . HIS B 1 144 ? 40.206 9.726   82.548  1.00 24.49 ? 144 HIS B CD2 1 
ATOM   3984 C CE1 . HIS B 1 144 ? 39.316 10.538  80.712  1.00 21.28 ? 144 HIS B CE1 1 
ATOM   3985 N NE2 . HIS B 1 144 ? 40.212 10.770  81.653  1.00 19.83 ? 144 HIS B NE2 1 
ATOM   3986 N N   . GLU B 1 145 ? 39.751 4.729   84.539  1.00 28.72 ? 145 GLU B N   1 
ATOM   3987 C CA  . GLU B 1 145 ? 39.243 3.483   85.133  1.00 29.80 ? 145 GLU B CA  1 
ATOM   3988 C C   . GLU B 1 145 ? 38.171 3.778   86.192  1.00 28.39 ? 145 GLU B C   1 
ATOM   3989 O O   . GLU B 1 145 ? 38.426 4.464   87.188  1.00 31.56 ? 145 GLU B O   1 
ATOM   3990 C CB  . GLU B 1 145 ? 40.372 2.675   85.769  1.00 29.34 ? 145 GLU B CB  1 
ATOM   3991 C CG  . GLU B 1 145 ? 41.223 1.947   84.761  1.00 43.96 ? 145 GLU B CG  1 
ATOM   3992 C CD  . GLU B 1 145 ? 42.515 1.410   85.351  1.00 52.28 ? 145 GLU B CD  1 
ATOM   3993 O OE1 . GLU B 1 145 ? 42.609 1.311   86.595  1.00 57.42 ? 145 GLU B OE1 1 
ATOM   3994 O OE2 . GLU B 1 145 ? 43.441 1.099   84.564  1.00 54.75 ? 145 GLU B OE2 1 
ATOM   3995 N N   . PHE B 1 146 ? 36.973 3.266   85.965  1.00 21.11 ? 146 PHE B N   1 
ATOM   3996 C CA  . PHE B 1 146 ? 35.879 3.463   86.873  1.00 20.45 ? 146 PHE B CA  1 
ATOM   3997 C C   . PHE B 1 146 ? 35.675 2.230   87.757  1.00 22.93 ? 146 PHE B C   1 
ATOM   3998 O O   . PHE B 1 146 ? 35.150 1.207   87.318  1.00 24.29 ? 146 PHE B O   1 
ATOM   3999 C CB  . PHE B 1 146 ? 34.611 3.770   86.072  1.00 27.07 ? 146 PHE B CB  1 
ATOM   4000 C CG  . PHE B 1 146 ? 34.621 5.116   85.399  1.00 26.63 ? 146 PHE B CG  1 
ATOM   4001 C CD1 . PHE B 1 146 ? 35.275 5.298   84.183  1.00 28.17 ? 146 PHE B CD1 1 
ATOM   4002 C CD2 . PHE B 1 146 ? 33.952 6.199   85.969  1.00 26.42 ? 146 PHE B CD2 1 
ATOM   4003 C CE1 . PHE B 1 146 ? 35.257 6.537   83.547  1.00 24.64 ? 146 PHE B CE1 1 
ATOM   4004 C CE2 . PHE B 1 146 ? 33.929 7.456   85.330  1.00 20.35 ? 146 PHE B CE2 1 
ATOM   4005 C CZ  . PHE B 1 146 ? 34.574 7.620   84.132  1.00 23.26 ? 146 PHE B CZ  1 
ATOM   4006 N N   . PHE B 1 147 ? 36.136 2.303   88.997  1.00 23.08 ? 147 PHE B N   1 
ATOM   4007 C CA  . PHE B 1 147 ? 35.962 1.168   89.900  1.00 21.36 ? 147 PHE B CA  1 
ATOM   4008 C C   . PHE B 1 147 ? 34.572 1.187   90.526  1.00 18.19 ? 147 PHE B C   1 
ATOM   4009 O O   . PHE B 1 147 ? 34.091 2.240   90.938  1.00 19.80 ? 147 PHE B O   1 
ATOM   4010 C CB  . PHE B 1 147 ? 37.058 1.152   90.960  1.00 16.60 ? 147 PHE B CB  1 
ATOM   4011 C CG  . PHE B 1 147 ? 38.335 0.506   90.495  1.00 14.66 ? 147 PHE B CG  1 
ATOM   4012 C CD1 . PHE B 1 147 ? 38.411 -0.881  90.332  1.00 13.53 ? 147 PHE B CD1 1 
ATOM   4013 C CD2 . PHE B 1 147 ? 39.469 1.270   90.259  1.00 7.50  ? 147 PHE B CD2 1 
ATOM   4014 C CE1 . PHE B 1 147 ? 39.599 -1.485  89.944  1.00 13.21 ? 147 PHE B CE1 1 
ATOM   4015 C CE2 . PHE B 1 147 ? 40.669 0.682   89.869  1.00 11.19 ? 147 PHE B CE2 1 
ATOM   4016 C CZ  . PHE B 1 147 ? 40.735 -0.705  89.717  1.00 15.16 ? 147 PHE B CZ  1 
ATOM   4017 N N   . LEU B 1 148 ? 33.912 0.033   90.535  1.00 16.90 ? 148 LEU B N   1 
ATOM   4018 C CA  . LEU B 1 148 ? 32.559 -0.083  91.091  1.00 18.48 ? 148 LEU B CA  1 
ATOM   4019 C C   . LEU B 1 148 ? 32.627 -0.282  92.611  1.00 21.85 ? 148 LEU B C   1 
ATOM   4020 O O   . LEU B 1 148 ? 31.682 0.019   93.323  1.00 30.81 ? 148 LEU B O   1 
ATOM   4021 C CB  . LEU B 1 148 ? 31.806 -1.252  90.421  1.00 12.35 ? 148 LEU B CB  1 
ATOM   4022 C CG  . LEU B 1 148 ? 30.313 -1.563  90.666  1.00 12.29 ? 148 LEU B CG  1 
ATOM   4023 C CD1 . LEU B 1 148 ? 29.431 -0.346  90.397  1.00 10.61 ? 148 LEU B CD1 1 
ATOM   4024 C CD2 . LEU B 1 148 ? 29.826 -2.768  89.846  1.00 8.56  ? 148 LEU B CD2 1 
ATOM   4025 N N   . SER B 1 149 ? 33.778 -0.703  93.112  1.00 24.09 ? 149 SER B N   1 
ATOM   4026 C CA  . SER B 1 149 ? 33.944 -0.962  94.538  1.00 23.16 ? 149 SER B CA  1 
ATOM   4027 C C   . SER B 1 149 ? 34.112 0.244   95.464  1.00 26.32 ? 149 SER B C   1 
ATOM   4028 O O   . SER B 1 149 ? 34.530 1.329   95.034  1.00 24.93 ? 149 SER B O   1 
ATOM   4029 C CB  . SER B 1 149 ? 35.130 -1.908  94.719  1.00 17.24 ? 149 SER B CB  1 
ATOM   4030 O OG  . SER B 1 149 ? 36.287 -1.438  94.039  1.00 11.63 ? 149 SER B OG  1 
ATOM   4031 N N   . SER B 1 150 ? 33.761 0.040   96.737  1.00 27.24 ? 150 SER B N   1 
ATOM   4032 C CA  . SER B 1 150 ? 33.934 1.045   97.786  1.00 27.36 ? 150 SER B CA  1 
ATOM   4033 C C   . SER B 1 150 ? 34.952 0.424   98.730  1.00 30.28 ? 150 SER B C   1 
ATOM   4034 O O   . SER B 1 150 ? 34.646 -0.556  99.414  1.00 33.02 ? 150 SER B O   1 
ATOM   4035 C CB  . SER B 1 150 ? 32.653 1.255   98.580  1.00 26.11 ? 150 SER B CB  1 
ATOM   4036 O OG  . SER B 1 150 ? 31.742 2.101   97.917  1.00 44.39 ? 150 SER B OG  1 
ATOM   4037 N N   . THR B 1 151 ? 36.174 0.931   98.741  1.00 31.88 ? 151 THR B N   1 
ATOM   4038 C CA  . THR B 1 151 ? 37.174 0.378   99.642  1.00 34.59 ? 151 THR B CA  1 
ATOM   4039 C C   . THR B 1 151 ? 37.788 1.511   100.442 1.00 39.08 ? 151 THR B C   1 
ATOM   4040 O O   . THR B 1 151 ? 37.312 2.652   100.368 1.00 41.87 ? 151 THR B O   1 
ATOM   4041 C CB  . THR B 1 151 ? 38.265 -0.348  98.875  1.00 31.56 ? 151 THR B CB  1 
ATOM   4042 O OG1 . THR B 1 151 ? 38.792 0.537   97.883  1.00 29.75 ? 151 THR B OG1 1 
ATOM   4043 C CG2 . THR B 1 151 ? 37.701 -1.602  98.214  1.00 24.57 ? 151 THR B CG2 1 
ATOM   4044 N N   . GLU B 1 152 ? 38.813 1.203   101.231 1.00 42.00 ? 152 GLU B N   1 
ATOM   4045 C CA  . GLU B 1 152 ? 39.478 2.236   102.020 1.00 48.83 ? 152 GLU B CA  1 
ATOM   4046 C C   . GLU B 1 152 ? 40.250 3.149   101.050 1.00 46.96 ? 152 GLU B C   1 
ATOM   4047 O O   . GLU B 1 152 ? 40.258 4.380   101.178 1.00 48.13 ? 152 GLU B O   1 
ATOM   4048 C CB  . GLU B 1 152 ? 40.423 1.603   103.049 1.00 54.96 ? 152 GLU B CB  1 
ATOM   4049 C CG  . GLU B 1 152 ? 41.086 2.612   103.992 1.00 69.03 ? 152 GLU B CG  1 
ATOM   4050 C CD  . GLU B 1 152 ? 42.100 1.979   104.946 1.00 77.72 ? 152 GLU B CD  1 
ATOM   4051 O OE1 . GLU B 1 152 ? 41.705 1.121   105.774 1.00 79.09 ? 152 GLU B OE1 1 
ATOM   4052 O OE2 . GLU B 1 152 ? 43.295 2.354   104.871 1.00 83.15 ? 152 GLU B OE2 1 
ATOM   4053 N N   . ALA B 1 153 ? 40.851 2.531   100.044 1.00 42.97 ? 153 ALA B N   1 
ATOM   4054 C CA  . ALA B 1 153 ? 41.606 3.262   99.041  1.00 39.31 ? 153 ALA B CA  1 
ATOM   4055 C C   . ALA B 1 153 ? 40.742 4.176   98.175  1.00 39.56 ? 153 ALA B C   1 
ATOM   4056 O O   . ALA B 1 153 ? 41.115 5.321   97.922  1.00 43.78 ? 153 ALA B O   1 
ATOM   4057 C CB  . ALA B 1 153 ? 42.353 2.290   98.152  1.00 25.05 ? 153 ALA B CB  1 
ATOM   4058 N N   . GLN B 1 154 ? 39.573 3.694   97.756  1.00 38.07 ? 154 GLN B N   1 
ATOM   4059 C CA  . GLN B 1 154 ? 38.734 4.469   96.856  1.00 33.24 ? 154 GLN B CA  1 
ATOM   4060 C C   . GLN B 1 154 ? 37.232 4.400   97.123  1.00 36.64 ? 154 GLN B C   1 
ATOM   4061 O O   . GLN B 1 154 ? 36.751 3.444   97.739  1.00 38.75 ? 154 GLN B O   1 
ATOM   4062 C CB  . GLN B 1 154 ? 39.050 4.032   95.409  1.00 31.47 ? 154 GLN B CB  1 
ATOM   4063 C CG  . GLN B 1 154 ? 39.016 2.513   95.161  1.00 21.49 ? 154 GLN B CG  1 
ATOM   4064 C CD  . GLN B 1 154 ? 37.601 1.980   94.988  1.00 29.36 ? 154 GLN B CD  1 
ATOM   4065 O OE1 . GLN B 1 154 ? 37.300 0.838   95.342  1.00 32.41 ? 154 GLN B OE1 1 
ATOM   4066 N NE2 . GLN B 1 154 ? 36.726 2.801   94.439  1.00 29.58 ? 154 GLN B NE2 1 
ATOM   4067 N N   . GLN B 1 155 ? 36.505 5.406   96.619  1.00 35.28 ? 155 GLN B N   1 
ATOM   4068 C CA  . GLN B 1 155 ? 35.043 5.521   96.748  1.00 34.68 ? 155 GLN B CA  1 
ATOM   4069 C C   . GLN B 1 155 ? 34.376 4.990   95.470  1.00 33.79 ? 155 GLN B C   1 
ATOM   4070 O O   . GLN B 1 155 ? 34.859 5.248   94.370  1.00 35.18 ? 155 GLN B O   1 
ATOM   4071 C CB  . GLN B 1 155 ? 34.654 6.998   96.918  1.00 34.29 ? 155 GLN B CB  1 
ATOM   4072 C CG  . GLN B 1 155 ? 34.108 7.406   98.285  1.00 47.52 ? 155 GLN B CG  1 
ATOM   4073 C CD  . GLN B 1 155 ? 33.845 8.912   98.392  1.00 54.68 ? 155 GLN B CD  1 
ATOM   4074 O OE1 . GLN B 1 155 ? 34.774 9.708   98.497  1.00 62.96 ? 155 GLN B OE1 1 
ATOM   4075 N NE2 . GLN B 1 155 ? 32.578 9.304   98.349  1.00 58.27 ? 155 GLN B NE2 1 
ATOM   4076 N N   . SER B 1 156 ? 33.286 4.243   95.605  1.00 30.79 ? 156 SER B N   1 
ATOM   4077 C CA  . SER B 1 156 ? 32.573 3.734   94.445  1.00 27.37 ? 156 SER B CA  1 
ATOM   4078 C C   . SER B 1 156 ? 31.880 4.897   93.764  1.00 31.34 ? 156 SER B C   1 
ATOM   4079 O O   . SER B 1 156 ? 31.371 5.793   94.449  1.00 34.50 ? 156 SER B O   1 
ATOM   4080 C CB  . SER B 1 156 ? 31.531 2.726   94.868  1.00 20.72 ? 156 SER B CB  1 
ATOM   4081 O OG  . SER B 1 156 ? 30.647 2.437   93.799  1.00 25.32 ? 156 SER B OG  1 
ATOM   4082 N N   . TYR B 1 157 ? 31.790 4.858   92.431  1.00 29.19 ? 157 TYR B N   1 
ATOM   4083 C CA  . TYR B 1 157 ? 31.156 5.946   91.686  1.00 26.53 ? 157 TYR B CA  1 
ATOM   4084 C C   . TYR B 1 157 ? 29.665 6.134   91.918  1.00 25.22 ? 157 TYR B C   1 
ATOM   4085 O O   . TYR B 1 157 ? 29.126 7.193   91.631  1.00 26.94 ? 157 TYR B O   1 
ATOM   4086 C CB  . TYR B 1 157 ? 31.498 5.913   90.183  1.00 25.83 ? 157 TYR B CB  1 
ATOM   4087 C CG  . TYR B 1 157 ? 31.163 4.642   89.452  1.00 21.60 ? 157 TYR B CG  1 
ATOM   4088 C CD1 . TYR B 1 157 ? 29.834 4.282   89.204  1.00 21.40 ? 157 TYR B CD1 1 
ATOM   4089 C CD2 . TYR B 1 157 ? 32.175 3.793   89.000  1.00 24.05 ? 157 TYR B CD2 1 
ATOM   4090 C CE1 . TYR B 1 157 ? 29.518 3.104   88.530  1.00 23.63 ? 157 TYR B CE1 1 
ATOM   4091 C CE2 . TYR B 1 157 ? 31.871 2.610   88.322  1.00 22.92 ? 157 TYR B CE2 1 
ATOM   4092 C CZ  . TYR B 1 157 ? 30.538 2.275   88.098  1.00 25.43 ? 157 TYR B CZ  1 
ATOM   4093 O OH  . TYR B 1 157 ? 30.227 1.087   87.478  1.00 31.68 ? 157 TYR B OH  1 
ATOM   4094 N N   . LEU B 1 158 ? 28.995 5.121   92.456  1.00 27.14 ? 158 LEU B N   1 
ATOM   4095 C CA  . LEU B 1 158 ? 27.566 5.243   92.749  1.00 21.29 ? 158 LEU B CA  1 
ATOM   4096 C C   . LEU B 1 158 ? 27.451 6.251   93.888  1.00 20.82 ? 158 LEU B C   1 
ATOM   4097 O O   . LEU B 1 158 ? 26.444 6.921   94.018  1.00 22.59 ? 158 LEU B O   1 
ATOM   4098 C CB  . LEU B 1 158 ? 26.981 3.901   93.187  1.00 23.14 ? 158 LEU B CB  1 
ATOM   4099 C CG  . LEU B 1 158 ? 27.003 2.712   92.214  1.00 27.05 ? 158 LEU B CG  1 
ATOM   4100 C CD1 . LEU B 1 158 ? 26.801 1.372   92.960  1.00 22.80 ? 158 LEU B CD1 1 
ATOM   4101 C CD2 . LEU B 1 158 ? 25.927 2.922   91.161  1.00 24.83 ? 158 LEU B CD2 1 
ATOM   4102 N N   . GLN B 1 159 ? 28.526 6.398   94.660  1.00 20.94 ? 159 GLN B N   1 
ATOM   4103 C CA  . GLN B 1 159 ? 28.585 7.319   95.799  1.00 25.08 ? 159 GLN B CA  1 
ATOM   4104 C C   . GLN B 1 159 ? 28.626 8.790   95.419  1.00 27.75 ? 159 GLN B C   1 
ATOM   4105 O O   . GLN B 1 159 ? 28.603 9.664   96.299  1.00 22.06 ? 159 GLN B O   1 
ATOM   4106 C CB  . GLN B 1 159 ? 29.807 7.010   96.654  1.00 25.82 ? 159 GLN B CB  1 
ATOM   4107 C CG  . GLN B 1 159 ? 29.689 5.701   97.403  1.00 27.68 ? 159 GLN B CG  1 
ATOM   4108 C CD  . GLN B 1 159 ? 30.919 5.374   98.219  1.00 28.41 ? 159 GLN B CD  1 
ATOM   4109 O OE1 . GLN B 1 159 ? 31.897 4.854   97.690  1.00 29.84 ? 159 GLN B OE1 1 
ATOM   4110 N NE2 . GLN B 1 159 ? 30.878 5.669   99.511  1.00 20.25 ? 159 GLN B NE2 1 
ATOM   4111 N N   . GLU B 1 160 ? 28.704 9.060   94.115  1.00 26.89 ? 160 GLU B N   1 
ATOM   4112 C CA  . GLU B 1 160 ? 28.765 10.426  93.620  1.00 24.78 ? 160 GLU B CA  1 
ATOM   4113 C C   . GLU B 1 160 ? 27.412 11.034  93.370  1.00 28.68 ? 160 GLU B C   1 
ATOM   4114 O O   . GLU B 1 160 ? 27.261 12.251  93.441  1.00 32.67 ? 160 GLU B O   1 
ATOM   4115 C CB  . GLU B 1 160 ? 29.594 10.489  92.359  1.00 26.42 ? 160 GLU B CB  1 
ATOM   4116 C CG  . GLU B 1 160 ? 31.032 10.139  92.606  1.00 32.82 ? 160 GLU B CG  1 
ATOM   4117 C CD  . GLU B 1 160 ? 31.661 11.035  93.655  1.00 36.11 ? 160 GLU B CD  1 
ATOM   4118 O OE1 . GLU B 1 160 ? 31.389 12.259  93.618  1.00 29.75 ? 160 GLU B OE1 1 
ATOM   4119 O OE2 . GLU B 1 160 ? 32.422 10.518  94.514  1.00 40.64 ? 160 GLU B OE2 1 
ATOM   4120 N N   . PHE B 1 161 ? 26.429 10.192  93.079  1.00 28.25 ? 161 PHE B N   1 
ATOM   4121 C CA  . PHE B 1 161 ? 25.079 10.661  92.817  1.00 28.67 ? 161 PHE B CA  1 
ATOM   4122 C C   . PHE B 1 161 ? 24.478 11.241  94.090  1.00 32.64 ? 161 PHE B C   1 
ATOM   4123 O O   . PHE B 1 161 ? 25.037 11.076  95.164  1.00 36.39 ? 161 PHE B O   1 
ATOM   4124 C CB  . PHE B 1 161 ? 24.234 9.519   92.268  1.00 23.02 ? 161 PHE B CB  1 
ATOM   4125 C CG  . PHE B 1 161 ? 24.781 8.938   91.004  1.00 22.28 ? 161 PHE B CG  1 
ATOM   4126 C CD1 . PHE B 1 161 ? 24.570 9.573   89.778  1.00 21.24 ? 161 PHE B CD1 1 
ATOM   4127 C CD2 . PHE B 1 161 ? 25.517 7.766   91.025  1.00 24.40 ? 161 PHE B CD2 1 
ATOM   4128 C CE1 . PHE B 1 161 ? 25.079 9.050   88.603  1.00 14.74 ? 161 PHE B CE1 1 
ATOM   4129 C CE2 . PHE B 1 161 ? 26.038 7.231   89.834  1.00 26.81 ? 161 PHE B CE2 1 
ATOM   4130 C CZ  . PHE B 1 161 ? 25.812 7.880   88.626  1.00 16.85 ? 161 PHE B CZ  1 
ATOM   4131 N N   . SER B 1 162 ? 23.359 11.946  93.970  1.00 34.67 ? 162 SER B N   1 
ATOM   4132 C CA  . SER B 1 162 ? 22.732 12.547  95.130  1.00 33.39 ? 162 SER B CA  1 
ATOM   4133 C C   . SER B 1 162 ? 21.826 11.550  95.835  1.00 32.61 ? 162 SER B C   1 
ATOM   4134 O O   . SER B 1 162 ? 21.224 10.685  95.188  1.00 30.91 ? 162 SER B O   1 
ATOM   4135 C CB  . SER B 1 162 ? 21.977 13.798  94.718  1.00 34.06 ? 162 SER B CB  1 
ATOM   4136 O OG  . SER B 1 162 ? 21.097 13.516  93.659  1.00 38.39 ? 162 SER B OG  1 
ATOM   4137 N N   . LYS B 1 163 ? 21.727 11.694  97.158  1.00 31.46 ? 163 LYS B N   1 
ATOM   4138 C CA  . LYS B 1 163 ? 20.941 10.808  98.017  1.00 35.63 ? 163 LYS B CA  1 
ATOM   4139 C C   . LYS B 1 163 ? 19.562 10.364  97.533  1.00 37.00 ? 163 LYS B C   1 
ATOM   4140 O O   . LYS B 1 163 ? 19.295 9.166   97.451  1.00 38.43 ? 163 LYS B O   1 
ATOM   4141 C CB  . LYS B 1 163 ? 20.811 11.397  99.427  1.00 43.24 ? 163 LYS B CB  1 
ATOM   4142 C CG  . LYS B 1 163 ? 22.129 11.810  100.076 1.00 54.67 ? 163 LYS B CG  1 
ATOM   4143 C CD  . LYS B 1 163 ? 21.919 12.259  101.529 1.00 59.05 ? 163 LYS B CD  1 
ATOM   4144 C CE  . LYS B 1 163 ? 23.060 13.165  102.028 1.00 64.15 ? 163 LYS B CE  1 
ATOM   4145 N NZ  . LYS B 1 163 ? 24.395 12.502  102.139 1.00 64.26 ? 163 LYS B NZ  1 
ATOM   4146 N N   . HIS B 1 164 ? 18.663 11.300  97.242  1.00 40.18 ? 164 HIS B N   1 
ATOM   4147 C CA  . HIS B 1 164 ? 17.349 10.874  96.794  1.00 44.23 ? 164 HIS B CA  1 
ATOM   4148 C C   . HIS B 1 164 ? 17.363 10.250  95.405  1.00 42.16 ? 164 HIS B C   1 
ATOM   4149 O O   . HIS B 1 164 ? 16.403 9.588   95.015  1.00 42.07 ? 164 HIS B O   1 
ATOM   4150 C CB  . HIS B 1 164 ? 16.280 11.967  96.909  1.00 53.04 ? 164 HIS B CB  1 
ATOM   4151 C CG  . HIS B 1 164 ? 14.918 11.422  97.235  1.00 65.75 ? 164 HIS B CG  1 
ATOM   4152 N ND1 . HIS B 1 164 ? 13.998 12.103  98.004  1.00 71.86 ? 164 HIS B ND1 1 
ATOM   4153 C CD2 . HIS B 1 164 ? 14.352 10.220  96.958  1.00 68.99 ? 164 HIS B CD2 1 
ATOM   4154 C CE1 . HIS B 1 164 ? 12.931 11.345  98.192  1.00 72.93 ? 164 HIS B CE1 1 
ATOM   4155 N NE2 . HIS B 1 164 ? 13.121 10.196  97.568  1.00 70.00 ? 164 HIS B NE2 1 
ATOM   4156 N N   . ILE B 1 165 ? 18.443 10.454  94.658  1.00 40.46 ? 165 ILE B N   1 
ATOM   4157 C CA  . ILE B 1 165 ? 18.546 9.843   93.348  1.00 36.38 ? 165 ILE B CA  1 
ATOM   4158 C C   . ILE B 1 165 ? 18.870 8.378   93.603  1.00 37.69 ? 165 ILE B C   1 
ATOM   4159 O O   . ILE B 1 165 ? 18.406 7.497   92.864  1.00 36.07 ? 165 ILE B O   1 
ATOM   4160 C CB  . ILE B 1 165 ? 19.619 10.516  92.468  1.00 38.33 ? 165 ILE B CB  1 
ATOM   4161 C CG1 . ILE B 1 165 ? 19.058 11.832  91.910  1.00 39.65 ? 165 ILE B CG1 1 
ATOM   4162 C CG2 . ILE B 1 165 ? 20.085 9.566   91.354  1.00 37.47 ? 165 ILE B CG2 1 
ATOM   4163 C CD1 . ILE B 1 165 ? 19.467 12.167  90.479  1.00 40.74 ? 165 ILE B CD1 1 
ATOM   4164 N N   . LEU B 1 166 ? 19.620 8.118   94.679  1.00 36.72 ? 166 LEU B N   1 
ATOM   4165 C CA  . LEU B 1 166 ? 19.976 6.747   95.060  1.00 34.81 ? 166 LEU B CA  1 
ATOM   4166 C C   . LEU B 1 166 ? 18.796 5.999   95.685  1.00 33.99 ? 166 LEU B C   1 
ATOM   4167 O O   . LEU B 1 166 ? 18.598 4.795   95.429  1.00 32.72 ? 166 LEU B O   1 
ATOM   4168 C CB  . LEU B 1 166 ? 21.169 6.724   96.013  1.00 34.30 ? 166 LEU B CB  1 
ATOM   4169 C CG  . LEU B 1 166 ? 22.581 6.673   95.420  1.00 33.83 ? 166 LEU B CG  1 
ATOM   4170 C CD1 . LEU B 1 166 ? 22.645 5.707   94.222  1.00 32.81 ? 166 LEU B CD1 1 
ATOM   4171 C CD2 . LEU B 1 166 ? 22.987 8.059   94.993  1.00 37.91 ? 166 LEU B CD2 1 
ATOM   4172 N N   . GLU B 1 167 ? 17.997 6.724   96.471  1.00 34.53 ? 167 GLU B N   1 
ATOM   4173 C CA  . GLU B 1 167 ? 16.815 6.160   97.130  1.00 33.67 ? 167 GLU B CA  1 
ATOM   4174 C C   . GLU B 1 167 ? 15.766 5.762   96.113  1.00 34.75 ? 167 GLU B C   1 
ATOM   4175 O O   . GLU B 1 167 ? 15.227 4.649   96.150  1.00 33.26 ? 167 GLU B O   1 
ATOM   4176 C CB  . GLU B 1 167 ? 16.165 7.190   98.036  1.00 33.69 ? 167 GLU B CB  1 
ATOM   4177 C CG  . GLU B 1 167 ? 17.083 7.875   98.987  1.00 39.73 ? 167 GLU B CG  1 
ATOM   4178 C CD  . GLU B 1 167 ? 16.327 8.494   100.139 1.00 42.44 ? 167 GLU B CD  1 
ATOM   4179 O OE1 . GLU B 1 167 ? 15.565 9.458   99.920  1.00 45.61 ? 167 GLU B OE1 1 
ATOM   4180 O OE2 . GLU B 1 167 ? 16.483 7.996   101.267 1.00 47.87 ? 167 GLU B OE2 1 
ATOM   4181 N N   . ALA B 1 168 ? 15.455 6.727   95.244  1.00 34.99 ? 168 ALA B N   1 
ATOM   4182 C CA  . ALA B 1 168 ? 14.454 6.608   94.183  1.00 32.92 ? 168 ALA B CA  1 
ATOM   4183 C C   . ALA B 1 168 ? 14.783 5.537   93.159  1.00 30.14 ? 168 ALA B C   1 
ATOM   4184 O O   . ALA B 1 168 ? 13.874 4.936   92.593  1.00 30.01 ? 168 ALA B O   1 
ATOM   4185 C CB  . ALA B 1 168 ? 14.261 7.956   93.494  1.00 32.35 ? 168 ALA B CB  1 
ATOM   4186 N N   . SER B 1 169 ? 16.077 5.329   92.921  1.00 30.04 ? 169 SER B N   1 
ATOM   4187 C CA  . SER B 1 169 ? 16.559 4.316   91.987  1.00 31.58 ? 169 SER B CA  1 
ATOM   4188 C C   . SER B 1 169 ? 16.439 2.934   92.606  1.00 30.65 ? 169 SER B C   1 
ATOM   4189 O O   . SER B 1 169 ? 15.709 2.085   92.103  1.00 29.11 ? 169 SER B O   1 
ATOM   4190 C CB  . SER B 1 169 ? 18.029 4.552   91.629  1.00 29.33 ? 169 SER B CB  1 
ATOM   4191 O OG  . SER B 1 169 ? 18.199 5.730   90.873  1.00 37.14 ? 169 SER B OG  1 
ATOM   4192 N N   . PHE B 1 170 ? 17.163 2.722   93.706  1.00 33.82 ? 170 PHE B N   1 
ATOM   4193 C CA  . PHE B 1 170 ? 17.177 1.430   94.395  1.00 34.00 ? 170 PHE B CA  1 
ATOM   4194 C C   . PHE B 1 170 ? 15.887 1.096   95.141  1.00 35.90 ? 170 PHE B C   1 
ATOM   4195 O O   . PHE B 1 170 ? 15.673 -0.050  95.555  1.00 35.89 ? 170 PHE B O   1 
ATOM   4196 C CB  . PHE B 1 170 ? 18.392 1.341   95.313  1.00 25.60 ? 170 PHE B CB  1 
ATOM   4197 C CG  . PHE B 1 170 ? 19.702 1.323   94.573  1.00 29.85 ? 170 PHE B CG  1 
ATOM   4198 C CD1 . PHE B 1 170 ? 19.993 0.300   93.665  1.00 30.02 ? 170 PHE B CD1 1 
ATOM   4199 C CD2 . PHE B 1 170 ? 20.649 2.323   94.777  1.00 33.94 ? 170 PHE B CD2 1 
ATOM   4200 C CE1 . PHE B 1 170 ? 21.210 0.269   92.969  1.00 28.92 ? 170 PHE B CE1 1 
ATOM   4201 C CE2 . PHE B 1 170 ? 21.873 2.311   94.088  1.00 32.98 ? 170 PHE B CE2 1 
ATOM   4202 C CZ  . PHE B 1 170 ? 22.151 1.277   93.181  1.00 34.62 ? 170 PHE B CZ  1 
ATOM   4203 N N   . ASN B 1 171 ? 15.035 2.106   95.317  1.00 37.62 ? 171 ASN B N   1 
ATOM   4204 C CA  . ASN B 1 171 ? 13.753 1.931   95.986  1.00 37.51 ? 171 ASN B CA  1 
ATOM   4205 C C   . ASN B 1 171 ? 13.908 1.621   97.483  1.00 39.99 ? 171 ASN B C   1 
ATOM   4206 O O   . ASN B 1 171 ? 13.134 0.846   98.045  1.00 38.30 ? 171 ASN B O   1 
ATOM   4207 C CB  . ASN B 1 171 ? 12.979 0.813   95.296  1.00 37.97 ? 171 ASN B CB  1 
ATOM   4208 C CG  . ASN B 1 171 ? 11.557 0.744   95.742  1.00 41.38 ? 171 ASN B CG  1 
ATOM   4209 O OD1 . ASN B 1 171 ? 10.959 1.767   96.070  1.00 43.83 ? 171 ASN B OD1 1 
ATOM   4210 N ND2 . ASN B 1 171 ? 10.991 -0.461  95.754  1.00 39.27 ? 171 ASN B ND2 1 
ATOM   4211 N N   . SER B 1 172 ? 14.916 2.227   98.114  1.00 42.37 ? 172 SER B N   1 
ATOM   4212 C CA  . SER B 1 172 ? 15.197 2.038   99.538  1.00 44.19 ? 172 SER B CA  1 
ATOM   4213 C C   . SER B 1 172 ? 15.584 3.376   100.155 1.00 44.31 ? 172 SER B C   1 
ATOM   4214 O O   . SER B 1 172 ? 15.740 4.374   99.442  1.00 43.08 ? 172 SER B O   1 
ATOM   4215 C CB  . SER B 1 172 ? 16.370 1.075   99.747  1.00 45.20 ? 172 SER B CB  1 
ATOM   4216 O OG  . SER B 1 172 ? 16.205 -0.132  99.034  1.00 53.39 ? 172 SER B OG  1 
ATOM   4217 N N   . LYS B 1 173 ? 15.718 3.380   101.484 1.00 44.07 ? 173 LYS B N   1 
ATOM   4218 C CA  . LYS B 1 173 ? 16.122 4.555   102.247 1.00 40.63 ? 173 LYS B CA  1 
ATOM   4219 C C   . LYS B 1 173 ? 17.637 4.562   102.273 1.00 38.58 ? 173 LYS B C   1 
ATOM   4220 O O   . LYS B 1 173 ? 18.266 3.523   102.498 1.00 34.87 ? 173 LYS B O   1 
ATOM   4221 C CB  . LYS B 1 173 ? 15.610 4.478   103.684 1.00 46.93 ? 173 LYS B CB  1 
ATOM   4222 C CG  . LYS B 1 173 ? 14.187 4.945   103.876 1.00 57.35 ? 173 LYS B CG  1 
ATOM   4223 C CD  . LYS B 1 173 ? 13.849 5.052   105.354 1.00 68.40 ? 173 LYS B CD  1 
ATOM   4224 C CE  . LYS B 1 173 ? 14.009 3.710   106.073 1.00 76.61 ? 173 LYS B CE  1 
ATOM   4225 N NZ  . LYS B 1 173 ? 13.503 3.753   107.487 1.00 80.84 ? 173 LYS B NZ  1 
ATOM   4226 N N   . PHE B 1 174 ? 18.222 5.739   102.118 1.00 36.21 ? 174 PHE B N   1 
ATOM   4227 C CA  . PHE B 1 174 ? 19.664 5.855   102.092 1.00 36.01 ? 174 PHE B CA  1 
ATOM   4228 C C   . PHE B 1 174 ? 20.404 5.030   103.124 1.00 33.94 ? 174 PHE B C   1 
ATOM   4229 O O   . PHE B 1 174 ? 21.405 4.414   102.807 1.00 34.66 ? 174 PHE B O   1 
ATOM   4230 C CB  . PHE B 1 174 ? 20.114 7.309   102.207 1.00 37.94 ? 174 PHE B CB  1 
ATOM   4231 C CG  . PHE B 1 174 ? 21.573 7.493   101.934 1.00 37.68 ? 174 PHE B CG  1 
ATOM   4232 C CD1 . PHE B 1 174 ? 22.032 7.605   100.633 1.00 41.46 ? 174 PHE B CD1 1 
ATOM   4233 C CD2 . PHE B 1 174 ? 22.493 7.448   102.958 1.00 39.51 ? 174 PHE B CD2 1 
ATOM   4234 C CE1 . PHE B 1 174 ? 23.383 7.662   100.355 1.00 41.84 ? 174 PHE B CE1 1 
ATOM   4235 C CE2 . PHE B 1 174 ? 23.843 7.503   102.691 1.00 44.40 ? 174 PHE B CE2 1 
ATOM   4236 C CZ  . PHE B 1 174 ? 24.290 7.608   101.381 1.00 44.84 ? 174 PHE B CZ  1 
ATOM   4237 N N   . GLU B 1 175 ? 19.935 5.031   104.362 1.00 38.80 ? 175 GLU B N   1 
ATOM   4238 C CA  . GLU B 1 175 ? 20.622 4.272   105.410 1.00 42.89 ? 175 GLU B CA  1 
ATOM   4239 C C   . GLU B 1 175 ? 20.718 2.783   105.058 1.00 43.56 ? 175 GLU B C   1 
ATOM   4240 O O   . GLU B 1 175 ? 21.766 2.161   105.248 1.00 46.51 ? 175 GLU B O   1 
ATOM   4241 C CB  . GLU B 1 175 ? 19.999 4.490   106.801 1.00 45.09 ? 175 GLU B CB  1 
ATOM   4242 C CG  . GLU B 1 175 ? 18.619 5.173   106.832 1.00 56.54 ? 175 GLU B CG  1 
ATOM   4243 C CD  . GLU B 1 175 ? 18.646 6.649   106.411 1.00 59.99 ? 175 GLU B CD  1 
ATOM   4244 O OE1 . GLU B 1 175 ? 19.510 7.415   106.909 1.00 60.15 ? 175 GLU B OE1 1 
ATOM   4245 O OE2 . GLU B 1 175 ? 17.790 7.035   105.581 1.00 61.29 ? 175 GLU B OE2 1 
ATOM   4246 N N   . GLU B 1 176 ? 19.654 2.238   104.477 1.00 40.64 ? 176 GLU B N   1 
ATOM   4247 C CA  . GLU B 1 176 ? 19.633 0.838   104.067 1.00 41.25 ? 176 GLU B CA  1 
ATOM   4248 C C   . GLU B 1 176 ? 20.660 0.601   102.956 1.00 39.23 ? 176 GLU B C   1 
ATOM   4249 O O   . GLU B 1 176 ? 21.511 -0.289  103.047 1.00 39.04 ? 176 GLU B O   1 
ATOM   4250 C CB  . GLU B 1 176 ? 18.231 0.479   103.568 1.00 44.82 ? 176 GLU B CB  1 
ATOM   4251 C CG  . GLU B 1 176 ? 18.124 -0.787  102.732 1.00 53.26 ? 176 GLU B CG  1 
ATOM   4252 C CD  . GLU B 1 176 ? 18.543 -2.046  103.470 1.00 61.48 ? 176 GLU B CD  1 
ATOM   4253 O OE1 . GLU B 1 176 ? 19.047 -1.962  104.621 1.00 64.30 ? 176 GLU B OE1 1 
ATOM   4254 O OE2 . GLU B 1 176 ? 18.366 -3.134  102.877 1.00 68.15 ? 176 GLU B OE2 1 
ATOM   4255 N N   . ILE B 1 177 ? 20.563 1.427   101.919 1.00 38.52 ? 177 ILE B N   1 
ATOM   4256 C CA  . ILE B 1 177 ? 21.429 1.393   100.741 1.00 33.90 ? 177 ILE B CA  1 
ATOM   4257 C C   . ILE B 1 177 ? 22.898 1.557   101.118 1.00 34.47 ? 177 ILE B C   1 
ATOM   4258 O O   . ILE B 1 177 ? 23.785 0.925   100.540 1.00 33.39 ? 177 ILE B O   1 
ATOM   4259 C CB  . ILE B 1 177 ? 21.051 2.559   99.786  1.00 35.56 ? 177 ILE B CB  1 
ATOM   4260 C CG1 . ILE B 1 177 ? 19.673 2.314   99.167  1.00 33.23 ? 177 ILE B CG1 1 
ATOM   4261 C CG2 . ILE B 1 177 ? 22.140 2.780   98.735  1.00 36.40 ? 177 ILE B CG2 1 
ATOM   4262 C CD1 . ILE B 1 177 ? 19.085 3.531   98.547  1.00 33.84 ? 177 ILE B CD1 1 
ATOM   4263 N N   . ASN B 1 178 ? 23.147 2.425   102.087 1.00 33.08 ? 178 ASN B N   1 
ATOM   4264 C CA  . ASN B 1 178 ? 24.495 2.696   102.517 1.00 32.90 ? 178 ASN B CA  1 
ATOM   4265 C C   . ASN B 1 178 ? 25.066 1.546   103.310 1.00 33.84 ? 178 ASN B C   1 
ATOM   4266 O O   . ASN B 1 178 ? 26.192 1.099   103.085 1.00 38.01 ? 178 ASN B O   1 
ATOM   4267 C CB  . ASN B 1 178 ? 24.532 3.957   103.357 1.00 33.37 ? 178 ASN B CB  1 
ATOM   4268 C CG  . ASN B 1 178 ? 25.935 4.382   103.664 1.00 37.85 ? 178 ASN B CG  1 
ATOM   4269 O OD1 . ASN B 1 178 ? 26.622 4.941   102.807 1.00 42.11 ? 178 ASN B OD1 1 
ATOM   4270 N ND2 . ASN B 1 178 ? 26.399 4.078   104.871 1.00 41.80 ? 178 ASN B ND2 1 
ATOM   4271 N N   . ARG B 1 179 ? 24.278 1.055   104.241 1.00 34.79 ? 179 ARG B N   1 
ATOM   4272 C CA  . ARG B 1 179 ? 24.722 -0.033  105.079 1.00 34.96 ? 179 ARG B CA  1 
ATOM   4273 C C   . ARG B 1 179 ? 25.131 -1.211  104.209 1.00 31.95 ? 179 ARG B C   1 
ATOM   4274 O O   . ARG B 1 179 ? 26.263 -1.675  104.282 1.00 31.58 ? 179 ARG B O   1 
ATOM   4275 C CB  . ARG B 1 179 ? 23.599 -0.414  106.035 1.00 35.95 ? 179 ARG B CB  1 
ATOM   4276 C CG  . ARG B 1 179 ? 24.044 -1.056  107.329 1.00 38.83 ? 179 ARG B CG  1 
ATOM   4277 C CD  . ARG B 1 179 ? 23.619 -2.497  107.364 1.00 32.73 ? 179 ARG B CD  1 
ATOM   4278 N NE  . ARG B 1 179 ? 22.248 -2.667  106.897 1.00 26.52 ? 179 ARG B NE  1 
ATOM   4279 C CZ  . ARG B 1 179 ? 21.745 -3.838  106.523 1.00 29.20 ? 179 ARG B CZ  1 
ATOM   4280 N NH1 . ARG B 1 179 ? 22.498 -4.936  106.575 1.00 28.36 ? 179 ARG B NH1 1 
ATOM   4281 N NH2 . ARG B 1 179 ? 20.506 -3.906  106.059 1.00 36.29 ? 179 ARG B NH2 1 
ATOM   4282 N N   . VAL B 1 180 ? 24.243 -1.627  103.319 1.00 32.62 ? 180 VAL B N   1 
ATOM   4283 C CA  . VAL B 1 180 ? 24.541 -2.768  102.449 1.00 34.50 ? 180 VAL B CA  1 
ATOM   4284 C C   . VAL B 1 180 ? 25.680 -2.540  101.440 1.00 36.53 ? 180 VAL B C   1 
ATOM   4285 O O   . VAL B 1 180 ? 26.403 -3.482  101.079 1.00 33.96 ? 180 VAL B O   1 
ATOM   4286 C CB  . VAL B 1 180 ? 23.316 -3.207  101.637 1.00 30.10 ? 180 VAL B CB  1 
ATOM   4287 C CG1 . VAL B 1 180 ? 23.544 -4.597  101.101 1.00 29.88 ? 180 VAL B CG1 1 
ATOM   4288 C CG2 . VAL B 1 180 ? 22.048 -3.124  102.468 1.00 32.21 ? 180 VAL B CG2 1 
ATOM   4289 N N   . LEU B 1 181 ? 25.846 -1.295  101.003 1.00 34.68 ? 181 LEU B N   1 
ATOM   4290 C CA  . LEU B 1 181 ? 26.853 -0.971  100.006 1.00 32.74 ? 181 LEU B CA  1 
ATOM   4291 C C   . LEU B 1 181 ? 28.119 -0.259  100.449 1.00 31.53 ? 181 LEU B C   1 
ATOM   4292 O O   . LEU B 1 181 ? 29.218 -0.734  100.193 1.00 29.96 ? 181 LEU B O   1 
ATOM   4293 C CB  . LEU B 1 181 ? 26.215 -0.109  98.908  1.00 32.55 ? 181 LEU B CB  1 
ATOM   4294 C CG  . LEU B 1 181 ? 25.562 -0.611  97.622  1.00 26.97 ? 181 LEU B CG  1 
ATOM   4295 C CD1 . LEU B 1 181 ? 25.238 -2.093  97.642  1.00 23.55 ? 181 LEU B CD1 1 
ATOM   4296 C CD2 . LEU B 1 181 ? 24.326 0.218   97.383  1.00 27.71 ? 181 LEU B CD2 1 
ATOM   4297 N N   . PHE B 1 182 ? 27.944 0.890   101.095 1.00 30.76 ? 182 PHE B N   1 
ATOM   4298 C CA  . PHE B 1 182 ? 29.039 1.772   101.479 1.00 30.72 ? 182 PHE B CA  1 
ATOM   4299 C C   . PHE B 1 182 ? 29.621 1.825   102.897 1.00 36.12 ? 182 PHE B C   1 
ATOM   4300 O O   . PHE B 1 182 ? 30.629 2.516   103.112 1.00 37.14 ? 182 PHE B O   1 
ATOM   4301 C CB  . PHE B 1 182 ? 28.625 3.188   101.096 1.00 26.19 ? 182 PHE B CB  1 
ATOM   4302 C CG  . PHE B 1 182 ? 28.027 3.301   99.716  1.00 26.77 ? 182 PHE B CG  1 
ATOM   4303 C CD1 . PHE B 1 182 ? 28.592 2.615   98.631  1.00 20.43 ? 182 PHE B CD1 1 
ATOM   4304 C CD2 . PHE B 1 182 ? 26.922 4.135   99.491  1.00 18.81 ? 182 PHE B CD2 1 
ATOM   4305 C CE1 . PHE B 1 182 ? 28.074 2.766   97.357  1.00 23.10 ? 182 PHE B CE1 1 
ATOM   4306 C CE2 . PHE B 1 182 ? 26.400 4.286   98.209  1.00 26.22 ? 182 PHE B CE2 1 
ATOM   4307 C CZ  . PHE B 1 182 ? 26.980 3.601   97.138  1.00 19.95 ? 182 PHE B CZ  1 
ATOM   4308 N N   . GLU B 1 183 ? 28.970 1.175   103.862 1.00 42.35 ? 183 GLU B N   1 
ATOM   4309 C CA  . GLU B 1 183 ? 29.415 1.179   105.272 1.00 45.77 ? 183 GLU B CA  1 
ATOM   4310 C C   . GLU B 1 183 ? 30.934 1.039   105.438 1.00 47.44 ? 183 GLU B C   1 
ATOM   4311 O O   . GLU B 1 183 ? 31.508 -0.010  105.145 1.00 45.03 ? 183 GLU B O   1 
ATOM   4312 C CB  . GLU B 1 183 ? 28.711 0.056   106.054 1.00 51.99 ? 183 GLU B CB  1 
ATOM   4313 C CG  . GLU B 1 183 ? 28.864 0.113   107.581 1.00 61.07 ? 183 GLU B CG  1 
ATOM   4314 C CD  . GLU B 1 183 ? 27.543 0.395   108.292 1.00 70.14 ? 183 GLU B CD  1 
ATOM   4315 O OE1 . GLU B 1 183 ? 26.940 1.463   108.049 1.00 75.84 ? 183 GLU B OE1 1 
ATOM   4316 O OE2 . GLU B 1 183 ? 27.095 -0.451  109.095 1.00 74.73 ? 183 GLU B OE2 1 
ATOM   4317 N N   . GLU B 1 184 ? 31.579 2.092   105.939 1.00 49.22 ? 184 GLU B N   1 
ATOM   4318 C CA  . GLU B 1 184 ? 33.025 2.067   106.151 1.00 51.13 ? 184 GLU B CA  1 
ATOM   4319 C C   . GLU B 1 184 ? 33.509 0.789   106.820 1.00 50.97 ? 184 GLU B C   1 
ATOM   4320 O O   . GLU B 1 184 ? 34.637 0.371   106.621 1.00 52.95 ? 184 GLU B O   1 
ATOM   4321 C CB  . GLU B 1 184 ? 33.492 3.300   106.923 1.00 52.11 ? 184 GLU B CB  1 
ATOM   4322 C CG  . GLU B 1 184 ? 33.583 4.535   106.066 1.00 60.55 ? 184 GLU B CG  1 
ATOM   4323 C CD  . GLU B 1 184 ? 34.461 4.313   104.832 1.00 71.75 ? 184 GLU B CD  1 
ATOM   4324 O OE1 . GLU B 1 184 ? 35.629 3.871   104.977 1.00 73.79 ? 184 GLU B OE1 1 
ATOM   4325 O OE2 . GLU B 1 184 ? 33.975 4.573   103.707 1.00 77.43 ? 184 GLU B OE2 1 
ATOM   4326 N N   . GLU B 1 185 ? 32.668 0.180   107.637 1.00 55.43 ? 185 GLU B N   1 
ATOM   4327 C CA  . GLU B 1 185 ? 33.038 -1.072  108.272 1.00 61.80 ? 185 GLU B CA  1 
ATOM   4328 C C   . GLU B 1 185 ? 32.763 -2.143  107.230 1.00 61.40 ? 185 GLU B C   1 
ATOM   4329 O O   . GLU B 1 185 ? 31.828 -2.017  106.444 1.00 64.36 ? 185 GLU B O   1 
ATOM   4330 C CB  . GLU B 1 185 ? 32.161 -1.347  109.500 1.00 68.27 ? 185 GLU B CB  1 
ATOM   4331 C CG  . GLU B 1 185 ? 32.428 -0.457  110.700 1.00 78.84 ? 185 GLU B CG  1 
ATOM   4332 C CD  . GLU B 1 185 ? 31.708 -0.939  111.948 1.00 85.89 ? 185 GLU B CD  1 
ATOM   4333 O OE1 . GLU B 1 185 ? 30.503 -1.268  111.853 1.00 90.78 ? 185 GLU B OE1 1 
ATOM   4334 O OE2 . GLU B 1 185 ? 32.349 -0.995  113.022 1.00 89.94 ? 185 GLU B OE2 1 
ATOM   4335 N N   . GLY B 1 186 ? 33.566 -3.197  107.209 1.00 60.26 ? 186 GLY B N   1 
ATOM   4336 C CA  . GLY B 1 186 ? 33.320 -4.257  106.243 1.00 59.62 ? 186 GLY B CA  1 
ATOM   4337 C C   . GLY B 1 186 ? 33.960 -4.039  104.883 1.00 57.42 ? 186 GLY B C   1 
ATOM   4338 O O   . GLY B 1 186 ? 34.066 -4.976  104.083 1.00 62.02 ? 186 GLY B O   1 
ATOM   4339 N N   . GLN B 1 187 ? 34.354 -2.807  104.591 1.00 49.97 ? 187 GLN B N   1 
ATOM   4340 C CA  . GLN B 1 187 ? 35.007 -2.528  103.324 1.00 46.70 ? 187 GLN B CA  1 
ATOM   4341 C C   . GLN B 1 187 ? 36.400 -3.178  103.260 1.00 46.84 ? 187 GLN B C   1 
ATOM   4342 O O   . GLN B 1 187 ? 37.116 -3.272  104.275 1.00 43.95 ? 187 GLN B O   1 
ATOM   4343 C CB  . GLN B 1 187 ? 35.245 -1.038  103.171 1.00 43.20 ? 187 GLN B CB  1 
ATOM   4344 C CG  . GLN B 1 187 ? 34.066 -0.159  103.057 1.00 36.89 ? 187 GLN B CG  1 
ATOM   4345 C CD  . GLN B 1 187 ? 34.517 1.275   102.893 1.00 38.35 ? 187 GLN B CD  1 
ATOM   4346 O OE1 . GLN B 1 187 ? 33.807 2.086   102.316 1.00 46.03 ? 187 GLN B OE1 1 
ATOM   4347 N NE2 . GLN B 1 187 ? 35.723 1.593   103.383 1.00 29.29 ? 187 GLN B NE2 1 
ATOM   4348 N N   . GLN B 1 188 ? 36.803 -3.573  102.056 1.00 42.78 ? 188 GLN B N   1 
ATOM   4349 C CA  . GLN B 1 188 ? 38.136 -4.117  101.861 1.00 40.45 ? 188 GLN B CA  1 
ATOM   4350 C C   . GLN B 1 188 ? 39.081 -2.905  101.853 1.00 41.78 ? 188 GLN B C   1 
ATOM   4351 O O   . GLN B 1 188 ? 38.640 -1.749  101.724 1.00 36.24 ? 188 GLN B O   1 
ATOM   4352 C CB  . GLN B 1 188 ? 38.231 -4.864  100.529 1.00 42.17 ? 188 GLN B CB  1 
ATOM   4353 C CG  . GLN B 1 188 ? 37.498 -6.179  100.507 1.00 40.73 ? 188 GLN B CG  1 
ATOM   4354 C CD  . GLN B 1 188 ? 37.869 -7.041  101.695 1.00 42.59 ? 188 GLN B CD  1 
ATOM   4355 O OE1 . GLN B 1 188 ? 39.040 -7.098  102.084 1.00 47.34 ? 188 GLN B OE1 1 
ATOM   4356 N NE2 . GLN B 1 188 ? 36.874 -7.692  102.300 1.00 36.33 ? 188 GLN B NE2 1 
ATOM   4357 N N   . GLU B 1 189 ? 40.376 -3.158  101.999 1.00 42.81 ? 189 GLU B N   1 
ATOM   4358 C CA  . GLU B 1 189 ? 41.345 -2.073  102.012 1.00 44.11 ? 189 GLU B CA  1 
ATOM   4359 C C   . GLU B 1 189 ? 41.483 -1.426  100.638 1.00 40.87 ? 189 GLU B C   1 
ATOM   4360 O O   . GLU B 1 189 ? 41.151 -0.255  100.462 1.00 40.06 ? 189 GLU B O   1 
ATOM   4361 C CB  . GLU B 1 189 ? 42.701 -2.580  102.509 1.00 53.29 ? 189 GLU B CB  1 
ATOM   4362 C CG  . GLU B 1 189 ? 43.858 -1.572  102.404 1.00 67.18 ? 189 GLU B CG  1 
ATOM   4363 C CD  . GLU B 1 189 ? 44.756 -1.824  101.193 1.00 74.33 ? 189 GLU B CD  1 
ATOM   4364 O OE1 . GLU B 1 189 ? 45.401 -2.905  101.151 1.00 77.14 ? 189 GLU B OE1 1 
ATOM   4365 O OE2 . GLU B 1 189 ? 44.818 -0.941  100.296 1.00 73.92 ? 189 GLU B OE2 1 
ATOM   4366 N N   . GLY B 1 190 ? 41.907 -2.216  99.658  1.00 38.87 ? 190 GLY B N   1 
ATOM   4367 C CA  . GLY B 1 190 ? 42.107 -1.693  98.323  1.00 31.56 ? 190 GLY B CA  1 
ATOM   4368 C C   . GLY B 1 190 ? 41.443 -2.503  97.246  1.00 25.67 ? 190 GLY B C   1 
ATOM   4369 O O   . GLY B 1 190 ? 40.636 -3.371  97.545  1.00 26.35 ? 190 GLY B O   1 
ATOM   4370 N N   . VAL B 1 191 ? 41.818 -2.222  95.999  1.00 25.44 ? 191 VAL B N   1 
ATOM   4371 C CA  . VAL B 1 191 ? 41.250 -2.877  94.824  1.00 22.33 ? 191 VAL B CA  1 
ATOM   4372 C C   . VAL B 1 191 ? 41.881 -4.213  94.462  1.00 22.54 ? 191 VAL B C   1 
ATOM   4373 O O   . VAL B 1 191 ? 41.346 -4.954  93.644  1.00 22.11 ? 191 VAL B O   1 
ATOM   4374 C CB  . VAL B 1 191 ? 41.208 -1.920  93.615  1.00 22.64 ? 191 VAL B CB  1 
ATOM   4375 C CG1 . VAL B 1 191 ? 40.380 -0.713  93.956  1.00 18.66 ? 191 VAL B CG1 1 
ATOM   4376 C CG2 . VAL B 1 191 ? 42.602 -1.483  93.212  1.00 25.24 ? 191 VAL B CG2 1 
ATOM   4377 N N   . ILE B 1 192 ? 43.052 -4.493  95.012  1.00 22.63 ? 192 ILE B N   1 
ATOM   4378 C CA  . ILE B 1 192 ? 43.678 -5.789  94.786  1.00 28.09 ? 192 ILE B CA  1 
ATOM   4379 C C   . ILE B 1 192 ? 43.474 -6.477  96.136  1.00 32.39 ? 192 ILE B C   1 
ATOM   4380 O O   . ILE B 1 192 ? 44.003 -6.058  97.170  1.00 35.54 ? 192 ILE B O   1 
ATOM   4381 C CB  . ILE B 1 192 ? 45.170 -5.693  94.407  1.00 30.03 ? 192 ILE B CB  1 
ATOM   4382 C CG1 . ILE B 1 192 ? 45.330 -4.855  93.135  1.00 37.19 ? 192 ILE B CG1 1 
ATOM   4383 C CG2 . ILE B 1 192 ? 45.710 -7.080  94.108  1.00 31.41 ? 192 ILE B CG2 1 
ATOM   4384 C CD1 . ILE B 1 192 ? 46.754 -4.610  92.704  1.00 37.79 ? 192 ILE B CD1 1 
ATOM   4385 N N   . VAL B 1 193 ? 42.605 -7.470  96.122  1.00 35.04 ? 193 VAL B N   1 
ATOM   4386 C CA  . VAL B 1 193 ? 42.226 -8.202  97.302  1.00 34.66 ? 193 VAL B CA  1 
ATOM   4387 C C   . VAL B 1 193 ? 42.762 -9.624  97.280  1.00 39.78 ? 193 VAL B C   1 
ATOM   4388 O O   . VAL B 1 193 ? 42.931 -10.239 96.235  1.00 38.96 ? 193 VAL B O   1 
ATOM   4389 C CB  . VAL B 1 193 ? 40.691 -8.182  97.421  1.00 32.57 ? 193 VAL B CB  1 
ATOM   4390 C CG1 . VAL B 1 193 ? 40.225 -8.948  98.617  1.00 38.18 ? 193 VAL B CG1 1 
ATOM   4391 C CG2 . VAL B 1 193 ? 40.221 -6.752  97.513  1.00 28.72 ? 193 VAL B CG2 1 
ATOM   4392 N N   . ASN B 1 194 ? 43.040 -10.128 98.468  1.00 44.77 ? 194 ASN B N   1 
ATOM   4393 C CA  . ASN B 1 194 ? 43.584 -11.457 98.681  1.00 48.54 ? 194 ASN B CA  1 
ATOM   4394 C C   . ASN B 1 194 ? 42.452 -12.485 98.715  1.00 48.35 ? 194 ASN B C   1 
ATOM   4395 O O   . ASN B 1 194 ? 41.703 -12.526 99.677  1.00 53.04 ? 194 ASN B O   1 
ATOM   4396 C CB  . ASN B 1 194 ? 44.334 -11.394 100.020 1.00 53.39 ? 194 ASN B CB  1 
ATOM   4397 C CG  . ASN B 1 194 ? 44.646 -12.745 100.603 1.00 61.48 ? 194 ASN B CG  1 
ATOM   4398 O OD1 . ASN B 1 194 ? 44.724 -12.879 101.822 1.00 67.95 ? 194 ASN B OD1 1 
ATOM   4399 N ND2 . ASN B 1 194 ? 44.873 -13.742 99.755  1.00 67.42 ? 194 ASN B ND2 1 
ATOM   4400 N N   . ILE B 1 195 ? 42.290 -13.304 97.681  1.00 47.97 ? 195 ILE B N   1 
ATOM   4401 C CA  . ILE B 1 195 ? 41.201 -14.277 97.741  1.00 47.87 ? 195 ILE B CA  1 
ATOM   4402 C C   . ILE B 1 195 ? 41.598 -15.664 98.247  1.00 52.23 ? 195 ILE B C   1 
ATOM   4403 O O   . ILE B 1 195 ? 42.781 -16.035 98.256  1.00 48.83 ? 195 ILE B O   1 
ATOM   4404 C CB  . ILE B 1 195 ? 40.342 -14.350 96.446  1.00 47.41 ? 195 ILE B CB  1 
ATOM   4405 C CG1 . ILE B 1 195 ? 41.208 -14.378 95.189  1.00 50.88 ? 195 ILE B CG1 1 
ATOM   4406 C CG2 . ILE B 1 195 ? 39.357 -13.206 96.414  1.00 45.53 ? 195 ILE B CG2 1 
ATOM   4407 C CD1 . ILE B 1 195 ? 41.782 -15.737 94.866  1.00 55.70 ? 195 ILE B CD1 1 
ATOM   4408 N N   . ASP B 1 196 ? 40.593 -16.427 98.670  1.00 56.13 ? 196 ASP B N   1 
ATOM   4409 C CA  . ASP B 1 196 ? 40.810 -17.749 99.244  1.00 58.76 ? 196 ASP B CA  1 
ATOM   4410 C C   . ASP B 1 196 ? 40.703 -18.969 98.333  1.00 58.44 ? 196 ASP B C   1 
ATOM   4411 O O   . ASP B 1 196 ? 39.685 -19.232 97.686  1.00 51.45 ? 196 ASP B O   1 
ATOM   4412 C CB  . ASP B 1 196 ? 39.947 -17.916 100.505 1.00 64.53 ? 196 ASP B CB  1 
ATOM   4413 C CG  . ASP B 1 196 ? 39.889 -19.348 100.993 1.00 67.75 ? 196 ASP B CG  1 
ATOM   4414 O OD1 . ASP B 1 196 ? 40.960 -19.938 101.269 1.00 67.19 ? 196 ASP B OD1 1 
ATOM   4415 O OD2 . ASP B 1 196 ? 38.761 -19.881 101.088 1.00 71.00 ? 196 ASP B OD2 1 
ATOM   4416 N N   . SER B 1 197 ? 41.759 -19.764 98.434  1.00 61.80 ? 197 SER B N   1 
ATOM   4417 C CA  . SER B 1 197 ? 41.988 -21.004 97.715  1.00 64.50 ? 197 SER B CA  1 
ATOM   4418 C C   . SER B 1 197 ? 40.775 -21.842 97.353  1.00 66.21 ? 197 SER B C   1 
ATOM   4419 O O   . SER B 1 197 ? 40.733 -22.445 96.281  1.00 67.66 ? 197 SER B O   1 
ATOM   4420 C CB  . SER B 1 197 ? 42.942 -21.849 98.553  1.00 66.90 ? 197 SER B CB  1 
ATOM   4421 O OG  . SER B 1 197 ? 42.534 -21.834 99.919  1.00 69.32 ? 197 SER B OG  1 
ATOM   4422 N N   . GLU B 1 198 ? 39.823 -21.930 98.271  1.00 68.04 ? 198 GLU B N   1 
ATOM   4423 C CA  . GLU B 1 198 ? 38.624 -22.721 98.044  1.00 71.47 ? 198 GLU B CA  1 
ATOM   4424 C C   . GLU B 1 198 ? 37.767 -22.190 96.903  1.00 72.35 ? 198 GLU B C   1 
ATOM   4425 O O   . GLU B 1 198 ? 37.546 -22.889 95.918  1.00 74.12 ? 198 GLU B O   1 
ATOM   4426 C CB  . GLU B 1 198 ? 37.797 -22.819 99.334  1.00 75.23 ? 198 GLU B CB  1 
ATOM   4427 C CG  . GLU B 1 198 ? 38.149 -24.001 100.246 1.00 78.32 ? 198 GLU B CG  1 
ATOM   4428 C CD  . GLU B 1 198 ? 39.644 -24.167 100.456 1.00 81.45 ? 198 GLU B CD  1 
ATOM   4429 O OE1 . GLU B 1 198 ? 40.217 -23.461 101.315 1.00 80.11 ? 198 GLU B OE1 1 
ATOM   4430 O OE2 . GLU B 1 198 ? 40.244 -25.008 99.751  1.00 83.90 ? 198 GLU B OE2 1 
ATOM   4431 N N   . GLN B 1 199 ? 37.366 -20.927 97.012  1.00 72.14 ? 199 GLN B N   1 
ATOM   4432 C CA  . GLN B 1 199 ? 36.504 -20.249 96.033  1.00 73.21 ? 199 GLN B CA  1 
ATOM   4433 C C   . GLN B 1 199 ? 36.894 -20.374 94.545  1.00 73.72 ? 199 GLN B C   1 
ATOM   4434 O O   . GLN B 1 199 ? 36.049 -20.653 93.679  1.00 71.61 ? 199 GLN B O   1 
ATOM   4435 C CB  . GLN B 1 199 ? 36.427 -18.757 96.385  1.00 73.50 ? 199 GLN B CB  1 
ATOM   4436 C CG  . GLN B 1 199 ? 36.274 -18.466 97.872  1.00 70.64 ? 199 GLN B CG  1 
ATOM   4437 C CD  . GLN B 1 199 ? 37.076 -17.254 98.329  1.00 67.37 ? 199 GLN B CD  1 
ATOM   4438 O OE1 . GLN B 1 199 ? 37.759 -16.610 97.542  1.00 63.08 ? 199 GLN B OE1 1 
ATOM   4439 N NE2 . GLN B 1 199 ? 37.006 -16.953 99.617  1.00 68.98 ? 199 GLN B NE2 1 
ATOM   4440 N N   . ILE B 1 200 ? 38.178 -20.190 94.259  1.00 73.33 ? 200 ILE B N   1 
ATOM   4441 C CA  . ILE B 1 200 ? 38.667 -20.213 92.887  1.00 72.72 ? 200 ILE B CA  1 
ATOM   4442 C C   . ILE B 1 200 ? 38.898 -21.540 92.168  1.00 73.42 ? 200 ILE B C   1 
ATOM   4443 O O   . ILE B 1 200 ? 39.184 -21.530 90.969  1.00 75.04 ? 200 ILE B O   1 
ATOM   4444 C CB  . ILE B 1 200 ? 39.912 -19.312 92.719  1.00 71.14 ? 200 ILE B CB  1 
ATOM   4445 C CG1 . ILE B 1 200 ? 41.174 -20.051 93.150  1.00 68.02 ? 200 ILE B CG1 1 
ATOM   4446 C CG2 . ILE B 1 200 ? 39.733 -18.021 93.524  1.00 69.60 ? 200 ILE B CG2 1 
ATOM   4447 C CD1 . ILE B 1 200 ? 42.415 -19.207 93.056  1.00 70.40 ? 200 ILE B CD1 1 
ATOM   4448 N N   . LYS B 1 201 ? 38.787 -22.672 92.854  1.00 72.51 ? 201 LYS B N   1 
ATOM   4449 C CA  . LYS B 1 201 ? 38.974 -23.950 92.161  1.00 72.28 ? 201 LYS B CA  1 
ATOM   4450 C C   . LYS B 1 201 ? 37.796 -24.156 91.217  1.00 70.95 ? 201 LYS B C   1 
ATOM   4451 O O   . LYS B 1 201 ? 37.935 -24.697 90.119  1.00 69.93 ? 201 LYS B O   1 
ATOM   4452 C CB  . LYS B 1 201 ? 39.018 -25.120 93.134  1.00 72.62 ? 201 LYS B CB  1 
ATOM   4453 C CG  . LYS B 1 201 ? 40.204 -25.141 94.065  1.00 76.19 ? 201 LYS B CG  1 
ATOM   4454 C CD  . LYS B 1 201 ? 40.151 -26.381 94.953  1.00 76.92 ? 201 LYS B CD  1 
ATOM   4455 C CE  . LYS B 1 201 ? 38.738 -26.626 95.505  1.00 79.04 ? 201 LYS B CE  1 
ATOM   4456 N NZ  . LYS B 1 201 ? 38.131 -25.445 96.195  1.00 75.43 ? 201 LYS B NZ  1 
ATOM   4457 N N   . GLU B 1 202 ? 36.643 -23.669 91.651  1.00 70.25 ? 202 GLU B N   1 
ATOM   4458 C CA  . GLU B 1 202 ? 35.401 -23.777 90.900  1.00 70.33 ? 202 GLU B CA  1 
ATOM   4459 C C   . GLU B 1 202 ? 35.489 -22.952 89.614  1.00 65.60 ? 202 GLU B C   1 
ATOM   4460 O O   . GLU B 1 202 ? 35.144 -23.429 88.527  1.00 65.28 ? 202 GLU B O   1 
ATOM   4461 C CB  . GLU B 1 202 ? 34.229 -23.292 91.774  1.00 75.70 ? 202 GLU B CB  1 
ATOM   4462 C CG  . GLU B 1 202 ? 33.935 -24.164 93.020  1.00 81.42 ? 202 GLU B CG  1 
ATOM   4463 C CD  . GLU B 1 202 ? 35.086 -24.211 94.027  1.00 82.77 ? 202 GLU B CD  1 
ATOM   4464 O OE1 . GLU B 1 202 ? 35.770 -23.181 94.181  1.00 82.03 ? 202 GLU B OE1 1 
ATOM   4465 O OE2 . GLU B 1 202 ? 35.309 -25.272 94.662  1.00 82.41 ? 202 GLU B OE2 1 
ATOM   4466 N N   . LEU B 1 203 ? 35.975 -21.722 89.761  1.00 60.32 ? 203 LEU B N   1 
ATOM   4467 C CA  . LEU B 1 203 ? 36.140 -20.784 88.658  1.00 54.13 ? 203 LEU B CA  1 
ATOM   4468 C C   . LEU B 1 203 ? 37.172 -21.283 87.631  1.00 55.67 ? 203 LEU B C   1 
ATOM   4469 O O   . LEU B 1 203 ? 36.875 -21.403 86.432  1.00 52.27 ? 203 LEU B O   1 
ATOM   4470 C CB  . LEU B 1 203 ? 36.585 -19.428 89.208  1.00 45.33 ? 203 LEU B CB  1 
ATOM   4471 C CG  . LEU B 1 203 ? 35.775 -18.200 88.807  1.00 41.87 ? 203 LEU B CG  1 
ATOM   4472 C CD1 . LEU B 1 203 ? 36.512 -16.958 89.247  1.00 40.37 ? 203 LEU B CD1 1 
ATOM   4473 C CD2 . LEU B 1 203 ? 35.560 -18.171 87.310  1.00 43.18 ? 203 LEU B CD2 1 
ATOM   4474 N N   . SER B 1 204 ? 38.381 -21.561 88.112  1.00 55.44 ? 204 SER B N   1 
ATOM   4475 C CA  . SER B 1 204 ? 39.477 -22.034 87.274  1.00 56.99 ? 204 SER B CA  1 
ATOM   4476 C C   . SER B 1 204 ? 39.037 -23.151 86.350  1.00 57.02 ? 204 SER B C   1 
ATOM   4477 O O   . SER B 1 204 ? 39.313 -23.123 85.156  1.00 56.61 ? 204 SER B O   1 
ATOM   4478 C CB  . SER B 1 204 ? 40.624 -22.524 88.152  1.00 60.55 ? 204 SER B CB  1 
ATOM   4479 O OG  . SER B 1 204 ? 41.096 -21.486 88.999  1.00 68.49 ? 204 SER B OG  1 
ATOM   4480 N N   . LYS B 1 205 ? 38.325 -24.116 86.922  1.00 58.03 ? 205 LYS B N   1 
ATOM   4481 C CA  . LYS B 1 205 ? 37.801 -25.278 86.212  1.00 55.96 ? 205 LYS B CA  1 
ATOM   4482 C C   . LYS B 1 205 ? 36.931 -24.881 85.016  1.00 52.93 ? 205 LYS B C   1 
ATOM   4483 O O   . LYS B 1 205 ? 37.225 -25.242 83.875  1.00 49.65 ? 205 LYS B O   1 
ATOM   4484 C CB  . LYS B 1 205 ? 36.994 -26.120 87.200  1.00 60.93 ? 205 LYS B CB  1 
ATOM   4485 C CG  . LYS B 1 205 ? 36.456 -27.437 86.688  1.00 66.85 ? 205 LYS B CG  1 
ATOM   4486 C CD  . LYS B 1 205 ? 35.649 -28.093 87.804  1.00 73.51 ? 205 LYS B CD  1 
ATOM   4487 C CE  . LYS B 1 205 ? 34.979 -29.381 87.354  1.00 79.99 ? 205 LYS B CE  1 
ATOM   4488 N NZ  . LYS B 1 205 ? 34.095 -29.952 88.418  1.00 82.92 ? 205 LYS B NZ  1 
ATOM   4489 N N   . HIS B 1 206 ? 35.879 -24.112 85.276  1.00 51.34 ? 206 HIS B N   1 
ATOM   4490 C CA  . HIS B 1 206 ? 34.979 -23.680 84.213  1.00 51.24 ? 206 HIS B CA  1 
ATOM   4491 C C   . HIS B 1 206 ? 35.695 -22.802 83.194  1.00 49.56 ? 206 HIS B C   1 
ATOM   4492 O O   . HIS B 1 206 ? 35.444 -22.899 81.990  1.00 44.03 ? 206 HIS B O   1 
ATOM   4493 C CB  . HIS B 1 206 ? 33.773 -22.930 84.794  1.00 54.55 ? 206 HIS B CB  1 
ATOM   4494 C CG  . HIS B 1 206 ? 32.788 -22.466 83.762  1.00 57.78 ? 206 HIS B CG  1 
ATOM   4495 N ND1 . HIS B 1 206 ? 32.776 -22.946 82.468  1.00 58.44 ? 206 HIS B ND1 1 
ATOM   4496 C CD2 . HIS B 1 206 ? 31.790 -21.552 83.830  1.00 60.19 ? 206 HIS B CD2 1 
ATOM   4497 C CE1 . HIS B 1 206 ? 31.816 -22.350 81.785  1.00 61.75 ? 206 HIS B CE1 1 
ATOM   4498 N NE2 . HIS B 1 206 ? 31.202 -21.499 82.588  1.00 61.03 ? 206 HIS B NE2 1 
ATOM   4499 N N   . ALA B 1 207 ? 36.558 -21.922 83.689  1.00 50.85 ? 207 ALA B N   1 
ATOM   4500 C CA  . ALA B 1 207 ? 37.304 -21.019 82.829  1.00 49.44 ? 207 ALA B CA  1 
ATOM   4501 C C   . ALA B 1 207 ? 38.187 -21.825 81.899  1.00 48.41 ? 207 ALA B C   1 
ATOM   4502 O O   . ALA B 1 207 ? 38.217 -21.556 80.704  1.00 50.27 ? 207 ALA B O   1 
ATOM   4503 C CB  . ALA B 1 207 ? 38.137 -20.055 83.665  1.00 49.89 ? 207 ALA B CB  1 
ATOM   4504 N N   . LYS B 1 208 ? 38.869 -22.835 82.441  1.00 49.49 ? 208 LYS B N   1 
ATOM   4505 C CA  . LYS B 1 208 ? 39.750 -23.699 81.654  1.00 47.97 ? 208 LYS B CA  1 
ATOM   4506 C C   . LYS B 1 208 ? 39.004 -24.488 80.590  1.00 45.52 ? 208 LYS B C   1 
ATOM   4507 O O   . LYS B 1 208 ? 39.539 -24.715 79.521  1.00 45.40 ? 208 LYS B O   1 
ATOM   4508 C CB  . LYS B 1 208 ? 40.566 -24.638 82.544  1.00 51.61 ? 208 LYS B CB  1 
ATOM   4509 C CG  . LYS B 1 208 ? 41.972 -24.115 82.880  1.00 57.71 ? 208 LYS B CG  1 
ATOM   4510 C CD  . LYS B 1 208 ? 42.210 -23.954 84.388  1.00 58.58 ? 208 LYS B CD  1 
ATOM   4511 C CE  . LYS B 1 208 ? 42.277 -25.289 85.125  1.00 58.96 ? 208 LYS B CE  1 
ATOM   4512 N NZ  . LYS B 1 208 ? 42.137 -25.115 86.606  1.00 58.07 ? 208 LYS B NZ  1 
ATOM   4513 N N   . SER B 1 209 ? 37.772 -24.896 80.851  1.00 45.06 ? 209 SER B N   1 
ATOM   4514 C CA  . SER B 1 209 ? 37.029 -25.611 79.827  1.00 50.46 ? 209 SER B CA  1 
ATOM   4515 C C   . SER B 1 209 ? 37.019 -24.727 78.589  1.00 53.99 ? 209 SER B C   1 
ATOM   4516 O O   . SER B 1 209 ? 37.104 -25.219 77.468  1.00 57.43 ? 209 SER B O   1 
ATOM   4517 C CB  . SER B 1 209 ? 35.595 -25.860 80.270  1.00 52.35 ? 209 SER B CB  1 
ATOM   4518 O OG  . SER B 1 209 ? 35.574 -26.306 81.610  1.00 64.61 ? 209 SER B OG  1 
ATOM   4519 N N   . SER B 1 210 ? 36.933 -23.416 78.805  1.00 56.79 ? 210 SER B N   1 
ATOM   4520 C CA  . SER B 1 210 ? 36.922 -22.443 77.717  1.00 58.00 ? 210 SER B CA  1 
ATOM   4521 C C   . SER B 1 210 ? 38.319 -21.938 77.345  1.00 57.38 ? 210 SER B C   1 
ATOM   4522 O O   . SER B 1 210 ? 38.503 -21.359 76.283  1.00 59.45 ? 210 SER B O   1 
ATOM   4523 C CB  . SER B 1 210 ? 35.997 -21.274 78.059  1.00 60.30 ? 210 SER B CB  1 
ATOM   4524 O OG  . SER B 1 210 ? 34.667 -21.729 78.276  1.00 64.46 ? 210 SER B OG  1 
ATOM   4525 N N   . ASN B 1 220 ? 54.007 -17.593 64.071  1.00 62.28 ? 220 ASN B N   1 
ATOM   4526 C CA  . ASN B 1 220 ? 54.869 -18.610 64.676  1.00 63.96 ? 220 ASN B CA  1 
ATOM   4527 C C   . ASN B 1 220 ? 56.254 -18.084 65.058  1.00 59.18 ? 220 ASN B C   1 
ATOM   4528 O O   . ASN B 1 220 ? 56.523 -16.883 64.968  1.00 58.49 ? 220 ASN B O   1 
ATOM   4529 C CB  . ASN B 1 220 ? 55.003 -19.845 63.762  1.00 73.71 ? 220 ASN B CB  1 
ATOM   4530 C CG  . ASN B 1 220 ? 54.017 -20.967 64.122  1.00 80.30 ? 220 ASN B CG  1 
ATOM   4531 O OD1 . ASN B 1 220 ? 53.854 -21.319 65.292  1.00 84.31 ? 220 ASN B OD1 1 
ATOM   4532 N ND2 . ASN B 1 220 ? 53.373 -21.542 63.108  1.00 82.22 ? 220 ASN B ND2 1 
ATOM   4533 N N   . THR B 1 221 ? 57.139 -19.003 65.431  1.00 54.42 ? 221 THR B N   1 
ATOM   4534 C CA  . THR B 1 221 ? 58.484 -18.666 65.877  1.00 51.23 ? 221 THR B CA  1 
ATOM   4535 C C   . THR B 1 221 ? 59.611 -18.763 64.845  1.00 50.01 ? 221 THR B C   1 
ATOM   4536 O O   . THR B 1 221 ? 59.587 -19.628 63.964  1.00 48.12 ? 221 THR B O   1 
ATOM   4537 C CB  . THR B 1 221 ? 58.862 -19.565 67.064  1.00 49.41 ? 221 THR B CB  1 
ATOM   4538 O OG1 . THR B 1 221 ? 57.728 -19.706 67.930  1.00 50.58 ? 221 THR B OG1 1 
ATOM   4539 C CG2 . THR B 1 221 ? 60.000 -18.965 67.850  1.00 50.86 ? 221 THR B CG2 1 
ATOM   4540 N N   . ILE B 1 222 ? 60.577 -17.846 64.959  1.00 48.11 ? 222 ILE B N   1 
ATOM   4541 C CA  . ILE B 1 222 ? 61.779 -17.803 64.119  1.00 45.11 ? 222 ILE B CA  1 
ATOM   4542 C C   . ILE B 1 222 ? 62.875 -17.546 65.139  1.00 43.54 ? 222 ILE B C   1 
ATOM   4543 O O   . ILE B 1 222 ? 62.892 -16.502 65.779  1.00 43.24 ? 222 ILE B O   1 
ATOM   4544 C CB  . ILE B 1 222 ? 61.818 -16.617 63.126  1.00 43.44 ? 222 ILE B CB  1 
ATOM   4545 C CG1 . ILE B 1 222 ? 60.492 -16.453 62.407  1.00 46.20 ? 222 ILE B CG1 1 
ATOM   4546 C CG2 . ILE B 1 222 ? 62.878 -16.863 62.065  1.00 42.97 ? 222 ILE B CG2 1 
ATOM   4547 C CD1 . ILE B 1 222 ? 60.498 -15.278 61.453  1.00 52.09 ? 222 ILE B CD1 1 
ATOM   4548 N N   . GLY B 1 223 ? 63.746 -18.526 65.336  1.00 48.26 ? 223 GLY B N   1 
ATOM   4549 C CA  . GLY B 1 223 ? 64.828 -18.392 66.300  1.00 47.24 ? 223 GLY B CA  1 
ATOM   4550 C C   . GLY B 1 223 ? 65.866 -19.486 66.144  1.00 44.84 ? 223 GLY B C   1 
ATOM   4551 O O   . GLY B 1 223 ? 65.721 -20.379 65.309  1.00 44.98 ? 223 GLY B O   1 
ATOM   4552 N N   . ASN B 1 224 ? 66.915 -19.426 66.949  1.00 41.69 ? 224 ASN B N   1 
ATOM   4553 C CA  . ASN B 1 224 ? 67.986 -20.408 66.878  1.00 40.58 ? 224 ASN B CA  1 
ATOM   4554 C C   . ASN B 1 224 ? 68.714 -20.483 68.216  1.00 40.36 ? 224 ASN B C   1 
ATOM   4555 O O   . ASN B 1 224 ? 68.182 -20.074 69.235  1.00 39.56 ? 224 ASN B O   1 
ATOM   4556 C CB  . ASN B 1 224 ? 68.960 -20.072 65.719  1.00 32.56 ? 224 ASN B CB  1 
ATOM   4557 C CG  . ASN B 1 224 ? 69.492 -18.644 65.779  1.00 34.36 ? 224 ASN B CG  1 
ATOM   4558 O OD1 . ASN B 1 224 ? 69.512 -18.017 66.841  1.00 39.26 ? 224 ASN B OD1 1 
ATOM   4559 N ND2 . ASN B 1 224 ? 69.927 -18.124 64.639  1.00 30.63 ? 224 ASN B ND2 1 
ATOM   4560 N N   . GLU B 1 225 ? 69.947 -20.974 68.193  1.00 42.99 ? 225 GLU B N   1 
ATOM   4561 C CA  . GLU B 1 225 ? 70.761 -21.119 69.395  1.00 44.62 ? 225 GLU B CA  1 
ATOM   4562 C C   . GLU B 1 225 ? 70.789 -19.851 70.244  1.00 41.11 ? 225 GLU B C   1 
ATOM   4563 O O   . GLU B 1 225 ? 70.748 -19.917 71.472  1.00 39.36 ? 225 GLU B O   1 
ATOM   4564 C CB  . GLU B 1 225 ? 72.215 -21.478 69.025  1.00 44.25 ? 225 GLU B CB  1 
ATOM   4565 C CG  . GLU B 1 225 ? 72.397 -22.623 68.015  1.00 56.77 ? 225 GLU B CG  1 
ATOM   4566 C CD  . GLU B 1 225 ? 72.272 -22.190 66.534  1.00 63.02 ? 225 GLU B CD  1 
ATOM   4567 O OE1 . GLU B 1 225 ? 72.947 -21.221 66.122  1.00 69.47 ? 225 GLU B OE1 1 
ATOM   4568 O OE2 . GLU B 1 225 ? 71.511 -22.830 65.771  1.00 61.35 ? 225 GLU B OE2 1 
ATOM   4569 N N   . PHE B 1 226 ? 70.779 -18.706 69.574  1.00 39.22 ? 226 PHE B N   1 
ATOM   4570 C CA  . PHE B 1 226 ? 70.911 -17.405 70.227  1.00 38.64 ? 226 PHE B CA  1 
ATOM   4571 C C   . PHE B 1 226 ? 69.690 -16.573 70.572  1.00 37.23 ? 226 PHE B C   1 
ATOM   4572 O O   . PHE B 1 226 ? 69.772 -15.708 71.448  1.00 35.07 ? 226 PHE B O   1 
ATOM   4573 C CB  . PHE B 1 226 ? 71.888 -16.559 69.414  1.00 36.18 ? 226 PHE B CB  1 
ATOM   4574 C CG  . PHE B 1 226 ? 73.103 -17.327 68.975  1.00 42.43 ? 226 PHE B CG  1 
ATOM   4575 C CD1 . PHE B 1 226 ? 73.085 -18.061 67.792  1.00 45.53 ? 226 PHE B CD1 1 
ATOM   4576 C CD2 . PHE B 1 226 ? 74.246 -17.361 69.761  1.00 44.76 ? 226 PHE B CD2 1 
ATOM   4577 C CE1 . PHE B 1 226 ? 74.183 -18.813 67.406  1.00 46.40 ? 226 PHE B CE1 1 
ATOM   4578 C CE2 . PHE B 1 226 ? 75.344 -18.109 69.383  1.00 43.97 ? 226 PHE B CE2 1 
ATOM   4579 C CZ  . PHE B 1 226 ? 75.314 -18.838 68.203  1.00 46.99 ? 226 PHE B CZ  1 
ATOM   4580 N N   . GLY B 1 227 ? 68.573 -16.813 69.892  1.00 36.35 ? 227 GLY B N   1 
ATOM   4581 C CA  . GLY B 1 227 ? 67.379 -16.035 70.153  1.00 34.17 ? 227 GLY B CA  1 
ATOM   4582 C C   . GLY B 1 227 ? 66.146 -16.642 69.532  1.00 33.74 ? 227 GLY B C   1 
ATOM   4583 O O   . GLY B 1 227 ? 66.236 -17.676 68.884  1.00 34.88 ? 227 GLY B O   1 
ATOM   4584 N N   . ASN B 1 228 ? 64.993 -16.020 69.766  1.00 37.63 ? 228 ASN B N   1 
ATOM   4585 C CA  . ASN B 1 228 ? 63.716 -16.480 69.222  1.00 38.14 ? 228 ASN B CA  1 
ATOM   4586 C C   . ASN B 1 228 ? 62.751 -15.330 69.104  1.00 35.82 ? 228 ASN B C   1 
ATOM   4587 O O   . ASN B 1 228 ? 62.759 -14.410 69.926  1.00 34.41 ? 228 ASN B O   1 
ATOM   4588 C CB  . ASN B 1 228 ? 63.109 -17.598 70.061  1.00 45.58 ? 228 ASN B CB  1 
ATOM   4589 C CG  . ASN B 1 228 ? 63.523 -18.957 69.573  1.00 53.86 ? 228 ASN B CG  1 
ATOM   4590 O OD1 . ASN B 1 228 ? 62.974 -19.462 68.595  1.00 55.02 ? 228 ASN B OD1 1 
ATOM   4591 N ND2 . ASN B 1 228 ? 64.545 -19.521 70.203  1.00 63.49 ? 228 ASN B ND2 1 
ATOM   4592 N N   . LEU B 1 229 ? 61.917 -15.391 68.076  1.00 33.43 ? 229 LEU B N   1 
ATOM   4593 C CA  . LEU B 1 229 ? 60.969 -14.337 67.811  1.00 33.67 ? 229 LEU B CA  1 
ATOM   4594 C C   . LEU B 1 229 ? 59.600 -14.892 67.432  1.00 35.04 ? 229 LEU B C   1 
ATOM   4595 O O   . LEU B 1 229 ? 59.476 -15.659 66.472  1.00 37.04 ? 229 LEU B O   1 
ATOM   4596 C CB  . LEU B 1 229 ? 61.541 -13.447 66.699  1.00 33.11 ? 229 LEU B CB  1 
ATOM   4597 C CG  . LEU B 1 229 ? 60.628 -12.462 65.965  1.00 36.41 ? 229 LEU B CG  1 
ATOM   4598 C CD1 . LEU B 1 229 ? 60.235 -11.347 66.911  1.00 33.97 ? 229 LEU B CD1 1 
ATOM   4599 C CD2 . LEU B 1 229 ? 61.315 -11.914 64.689  1.00 32.18 ? 229 LEU B CD2 1 
ATOM   4600 N N   . THR B 1 230 ? 58.582 -14.543 68.219  1.00 35.07 ? 230 THR B N   1 
ATOM   4601 C CA  . THR B 1 230 ? 57.213 -14.988 67.948  1.00 34.53 ? 230 THR B CA  1 
ATOM   4602 C C   . THR B 1 230 ? 56.272 -13.803 67.815  1.00 31.51 ? 230 THR B C   1 
ATOM   4603 O O   . THR B 1 230 ? 56.117 -13.008 68.744  1.00 31.05 ? 230 THR B O   1 
ATOM   4604 C CB  . THR B 1 230 ? 56.680 -15.967 69.021  1.00 36.49 ? 230 THR B CB  1 
ATOM   4605 O OG1 . THR B 1 230 ? 57.428 -17.193 68.967  1.00 35.34 ? 230 THR B OG1 1 
ATOM   4606 C CG2 . THR B 1 230 ? 55.197 -16.272 68.769  1.00 31.36 ? 230 THR B CG2 1 
ATOM   4607 N N   . GLU B 1 231 ? 55.604 -13.728 66.669  1.00 29.88 ? 231 GLU B N   1 
ATOM   4608 C CA  . GLU B 1 231 ? 54.700 -12.624 66.380  1.00 28.57 ? 231 GLU B CA  1 
ATOM   4609 C C   . GLU B 1 231 ? 53.334 -13.099 65.972  1.00 26.81 ? 231 GLU B C   1 
ATOM   4610 O O   . GLU B 1 231 ? 53.207 -14.113 65.323  1.00 30.75 ? 231 GLU B O   1 
ATOM   4611 C CB  . GLU B 1 231 ? 55.279 -11.746 65.263  1.00 23.59 ? 231 GLU B CB  1 
ATOM   4612 C CG  . GLU B 1 231 ? 56.267 -10.727 65.757  1.00 24.58 ? 231 GLU B CG  1 
ATOM   4613 C CD  . GLU B 1 231 ? 56.921 -9.968  64.642  1.00 27.29 ? 231 GLU B CD  1 
ATOM   4614 O OE1 . GLU B 1 231 ? 56.249 -9.663  63.654  1.00 33.61 ? 231 GLU B OE1 1 
ATOM   4615 O OE2 . GLU B 1 231 ? 58.118 -9.690  64.738  1.00 33.13 ? 231 GLU B OE2 1 
ATOM   4616 N N   . ARG B 1 232 ? 52.315 -12.341 66.332  1.00 32.94 ? 232 ARG B N   1 
ATOM   4617 C CA  . ARG B 1 232 ? 50.944 -12.681 65.994  1.00 40.72 ? 232 ARG B CA  1 
ATOM   4618 C C   . ARG B 1 232 ? 50.235 -11.375 65.668  1.00 41.81 ? 232 ARG B C   1 
ATOM   4619 O O   . ARG B 1 232 ? 50.460 -10.367 66.335  1.00 42.03 ? 232 ARG B O   1 
ATOM   4620 C CB  . ARG B 1 232 ? 50.277 -13.436 67.155  1.00 48.24 ? 232 ARG B CB  1 
ATOM   4621 C CG  . ARG B 1 232 ? 50.380 -12.741 68.513  1.00 60.75 ? 232 ARG B CG  1 
ATOM   4622 C CD  . ARG B 1 232 ? 50.706 -13.719 69.652  1.00 63.99 ? 232 ARG B CD  1 
ATOM   4623 N NE  . ARG B 1 232 ? 52.118 -13.680 70.047  1.00 65.33 ? 232 ARG B NE  1 
ATOM   4624 C CZ  . ARG B 1 232 ? 52.669 -14.522 70.917  1.00 64.95 ? 232 ARG B CZ  1 
ATOM   4625 N NH1 . ARG B 1 232 ? 51.937 -15.484 71.464  1.00 68.54 ? 232 ARG B NH1 1 
ATOM   4626 N NH2 . ARG B 1 232 ? 53.954 -14.420 71.227  1.00 61.23 ? 232 ARG B NH2 1 
ATOM   4627 N N   . THR B 1 233 ? 49.441 -11.379 64.600  1.00 44.41 ? 233 THR B N   1 
ATOM   4628 C CA  . THR B 1 233 ? 48.746 -10.181 64.157  1.00 48.57 ? 233 THR B CA  1 
ATOM   4629 C C   . THR B 1 233 ? 47.244 -10.293 64.281  1.00 51.71 ? 233 THR B C   1 
ATOM   4630 O O   . THR B 1 233 ? 46.644 -11.262 63.816  1.00 54.09 ? 233 THR B O   1 
ATOM   4631 C CB  . THR B 1 233 ? 49.095 -9.830  62.679  1.00 47.08 ? 233 THR B CB  1 
ATOM   4632 O OG1 . THR B 1 233 ? 50.479 -9.459  62.578  1.00 51.15 ? 233 THR B OG1 1 
ATOM   4633 C CG2 . THR B 1 233 ? 48.236 -8.678  62.170  1.00 48.47 ? 233 THR B CG2 1 
ATOM   4634 N N   . ASP B 1 234 ? 46.642 -9.285  64.905  1.00 55.88 ? 234 ASP B N   1 
ATOM   4635 C CA  . ASP B 1 234 ? 45.199 -9.224  65.073  1.00 58.92 ? 234 ASP B CA  1 
ATOM   4636 C C   . ASP B 1 234 ? 44.648 -8.300  63.996  1.00 58.79 ? 234 ASP B C   1 
ATOM   4637 O O   . ASP B 1 234 ? 44.668 -7.076  64.134  1.00 58.61 ? 234 ASP B O   1 
ATOM   4638 C CB  . ASP B 1 234 ? 44.837 -8.684  66.455  1.00 64.37 ? 234 ASP B CB  1 
ATOM   4639 C CG  . ASP B 1 234 ? 43.341 -8.551  66.652  1.00 65.92 ? 234 ASP B CG  1 
ATOM   4640 O OD1 . ASP B 1 234 ? 42.588 -9.390  66.110  1.00 64.33 ? 234 ASP B OD1 1 
ATOM   4641 O OD2 . ASP B 1 234 ? 42.927 -7.601  67.348  1.00 68.92 ? 234 ASP B OD2 1 
ATOM   4642 N N   . ASN B 1 235 ? 44.160 -8.910  62.923  1.00 59.69 ? 235 ASN B N   1 
ATOM   4643 C CA  . ASN B 1 235 ? 43.599 -8.192  61.788  1.00 58.31 ? 235 ASN B CA  1 
ATOM   4644 C C   . ASN B 1 235 ? 42.518 -7.189  62.187  1.00 60.07 ? 235 ASN B C   1 
ATOM   4645 O O   . ASN B 1 235 ? 42.358 -6.149  61.535  1.00 60.17 ? 235 ASN B O   1 
ATOM   4646 C CB  . ASN B 1 235 ? 43.034 -9.190  60.774  1.00 55.85 ? 235 ASN B CB  1 
ATOM   4647 C CG  . ASN B 1 235 ? 44.058 -9.616  59.741  1.00 54.78 ? 235 ASN B CG  1 
ATOM   4648 O OD1 . ASN B 1 235 ? 43.857 -9.414  58.542  1.00 58.19 ? 235 ASN B OD1 1 
ATOM   4649 N ND2 . ASN B 1 235 ? 45.155 -10.214 60.194  1.00 48.76 ? 235 ASN B ND2 1 
ATOM   4650 N N   . SER B 1 236 ? 41.786 -7.493  63.259  1.00 57.88 ? 236 SER B N   1 
ATOM   4651 C CA  . SER B 1 236 ? 40.729 -6.607  63.714  1.00 55.89 ? 236 SER B CA  1 
ATOM   4652 C C   . SER B 1 236 ? 41.337 -5.305  64.223  1.00 55.02 ? 236 SER B C   1 
ATOM   4653 O O   . SER B 1 236 ? 41.048 -4.231  63.683  1.00 55.43 ? 236 SER B O   1 
ATOM   4654 C CB  . SER B 1 236 ? 39.880 -7.279  64.801  1.00 58.89 ? 236 SER B CB  1 
ATOM   4655 O OG  . SER B 1 236 ? 40.604 -7.434  66.011  1.00 64.47 ? 236 SER B OG  1 
ATOM   4656 N N   . LEU B 1 237 ? 42.207 -5.400  65.231  1.00 50.09 ? 237 LEU B N   1 
ATOM   4657 C CA  . LEU B 1 237 ? 42.830 -4.209  65.782  1.00 46.06 ? 237 LEU B CA  1 
ATOM   4658 C C   . LEU B 1 237 ? 43.890 -3.585  64.896  1.00 44.37 ? 237 LEU B C   1 
ATOM   4659 O O   . LEU B 1 237 ? 44.202 -2.412  65.064  1.00 43.52 ? 237 LEU B O   1 
ATOM   4660 C CB  . LEU B 1 237 ? 43.405 -4.463  67.178  1.00 47.68 ? 237 LEU B CB  1 
ATOM   4661 C CG  . LEU B 1 237 ? 42.442 -4.375  68.376  1.00 50.48 ? 237 LEU B CG  1 
ATOM   4662 C CD1 . LEU B 1 237 ? 43.213 -4.485  69.687  1.00 49.03 ? 237 LEU B CD1 1 
ATOM   4663 C CD2 . LEU B 1 237 ? 41.661 -3.065  68.356  1.00 50.53 ? 237 LEU B CD2 1 
ATOM   4664 N N   . ASN B 1 238 ? 44.428 -4.350  63.946  1.00 44.83 ? 238 ASN B N   1 
ATOM   4665 C CA  . ASN B 1 238 ? 45.485 -3.859  63.040  1.00 42.30 ? 238 ASN B CA  1 
ATOM   4666 C C   . ASN B 1 238 ? 46.746 -3.699  63.900  1.00 39.19 ? 238 ASN B C   1 
ATOM   4667 O O   . ASN B 1 238 ? 47.591 -2.818  63.670  1.00 36.34 ? 238 ASN B O   1 
ATOM   4668 C CB  . ASN B 1 238 ? 45.056 -2.528  62.391  1.00 41.03 ? 238 ASN B CB  1 
ATOM   4669 C CG  . ASN B 1 238 ? 46.049 -2.004  61.375  1.00 40.70 ? 238 ASN B CG  1 
ATOM   4670 O OD1 . ASN B 1 238 ? 46.116 -2.482  60.249  1.00 42.63 ? 238 ASN B OD1 1 
ATOM   4671 N ND2 . ASN B 1 238 ? 46.795 -0.986  61.756  1.00 43.81 ? 238 ASN B ND2 1 
ATOM   4672 N N   . VAL B 1 239 ? 46.841 -4.574  64.905  1.00 37.14 ? 239 VAL B N   1 
ATOM   4673 C CA  . VAL B 1 239 ? 47.954 -4.604  65.854  1.00 34.42 ? 239 VAL B CA  1 
ATOM   4674 C C   . VAL B 1 239 ? 48.695 -5.946  65.764  1.00 34.53 ? 239 VAL B C   1 
ATOM   4675 O O   . VAL B 1 239 ? 48.135 -6.939  65.311  1.00 31.31 ? 239 VAL B O   1 
ATOM   4676 C CB  . VAL B 1 239 ? 47.452 -4.346  67.295  1.00 31.34 ? 239 VAL B CB  1 
ATOM   4677 C CG1 . VAL B 1 239 ? 48.481 -4.786  68.316  1.00 27.04 ? 239 VAL B CG1 1 
ATOM   4678 C CG2 . VAL B 1 239 ? 47.164 -2.849  67.487  1.00 26.63 ? 239 VAL B CG2 1 
ATOM   4679 N N   . LEU B 1 240 ? 49.967 -5.944  66.152  1.00 34.11 ? 240 LEU B N   1 
ATOM   4680 C CA  . LEU B 1 240 ? 50.822 -7.130  66.124  1.00 35.24 ? 240 LEU B CA  1 
ATOM   4681 C C   . LEU B 1 240 ? 51.435 -7.330  67.522  1.00 34.53 ? 240 LEU B C   1 
ATOM   4682 O O   . LEU B 1 240 ? 51.735 -6.348  68.203  1.00 35.86 ? 240 LEU B O   1 
ATOM   4683 C CB  . LEU B 1 240 ? 51.898 -6.865  65.086  1.00 36.15 ? 240 LEU B CB  1 
ATOM   4684 C CG  . LEU B 1 240 ? 53.079 -7.737  64.719  1.00 39.24 ? 240 LEU B CG  1 
ATOM   4685 C CD1 . LEU B 1 240 ? 53.593 -7.276  63.366  1.00 37.53 ? 240 LEU B CD1 1 
ATOM   4686 C CD2 . LEU B 1 240 ? 54.164 -7.571  65.750  1.00 45.00 ? 240 LEU B CD2 1 
ATOM   4687 N N   . ILE B 1 241 ? 51.602 -8.576  67.961  1.00 29.65 ? 241 ILE B N   1 
ATOM   4688 C CA  . ILE B 1 241 ? 52.179 -8.858  69.286  1.00 30.90 ? 241 ILE B CA  1 
ATOM   4689 C C   . ILE B 1 241 ? 53.398 -9.792  69.148  1.00 30.51 ? 241 ILE B C   1 
ATOM   4690 O O   . ILE B 1 241 ? 53.285 -10.909 68.639  1.00 32.87 ? 241 ILE B O   1 
ATOM   4691 C CB  . ILE B 1 241 ? 51.132 -9.509  70.225  1.00 29.21 ? 241 ILE B CB  1 
ATOM   4692 C CG1 . ILE B 1 241 ? 49.901 -8.619  70.343  1.00 29.50 ? 241 ILE B CG1 1 
ATOM   4693 C CG2 . ILE B 1 241 ? 51.712 -9.749  71.600  1.00 29.91 ? 241 ILE B CG2 1 
ATOM   4694 C CD1 . ILE B 1 241 ? 48.691 -9.354  70.855  1.00 33.69 ? 241 ILE B CD1 1 
ATOM   4695 N N   . SER B 1 242 ? 54.553 -9.338  69.621  1.00 29.77 ? 242 SER B N   1 
ATOM   4696 C CA  . SER B 1 242 ? 55.784 -10.111 69.528  1.00 28.95 ? 242 SER B CA  1 
ATOM   4697 C C   . SER B 1 242 ? 56.208 -10.658 70.875  1.00 32.64 ? 242 SER B C   1 
ATOM   4698 O O   . SER B 1 242 ? 55.708 -10.235 71.912  1.00 36.72 ? 242 SER B O   1 
ATOM   4699 C CB  . SER B 1 242 ? 56.930 -9.220  69.041  1.00 30.84 ? 242 SER B CB  1 
ATOM   4700 O OG  . SER B 1 242 ? 56.613 -8.457  67.883  1.00 41.35 ? 242 SER B OG  1 
ATOM   4701 N N   . SER B 1 243 ? 57.185 -11.555 70.842  1.00 35.77 ? 243 SER B N   1 
ATOM   4702 C CA  . SER B 1 243 ? 57.792 -12.145 72.031  1.00 38.73 ? 243 SER B CA  1 
ATOM   4703 C C   . SER B 1 243 ? 59.218 -12.372 71.583  1.00 37.86 ? 243 SER B C   1 
ATOM   4704 O O   . SER B 1 243 ? 59.450 -13.109 70.628  1.00 41.01 ? 243 SER B O   1 
ATOM   4705 C CB  . SER B 1 243 ? 57.166 -13.496 72.384  1.00 43.38 ? 243 SER B CB  1 
ATOM   4706 O OG  . SER B 1 243 ? 55.782 -13.381 72.673  1.00 54.93 ? 243 SER B OG  1 
ATOM   4707 N N   . ILE B 1 244 ? 60.169 -11.695 72.208  1.00 37.65 ? 244 ILE B N   1 
ATOM   4708 C CA  . ILE B 1 244 ? 61.560 -11.864 71.820  1.00 38.81 ? 244 ILE B CA  1 
ATOM   4709 C C   . ILE B 1 244 ? 62.427 -12.351 73.000  1.00 41.25 ? 244 ILE B C   1 
ATOM   4710 O O   . ILE B 1 244 ? 62.491 -11.704 74.060  1.00 38.44 ? 244 ILE B O   1 
ATOM   4711 C CB  . ILE B 1 244 ? 62.131 -10.542 71.221  1.00 39.81 ? 244 ILE B CB  1 
ATOM   4712 C CG1 . ILE B 1 244 ? 61.248 -10.064 70.057  1.00 36.97 ? 244 ILE B CG1 1 
ATOM   4713 C CG2 . ILE B 1 244 ? 63.584 -10.743 70.751  1.00 36.39 ? 244 ILE B CG2 1 
ATOM   4714 C CD1 . ILE B 1 244 ? 61.605 -8.676  69.528  1.00 33.28 ? 244 ILE B CD1 1 
ATOM   4715 N N   . GLU B 1 245 ? 63.063 -13.508 72.816  1.00 39.95 ? 245 GLU B N   1 
ATOM   4716 C CA  . GLU B 1 245 ? 63.935 -14.096 73.824  1.00 38.26 ? 245 GLU B CA  1 
ATOM   4717 C C   . GLU B 1 245 ? 65.350 -14.151 73.274  1.00 36.13 ? 245 GLU B C   1 
ATOM   4718 O O   . GLU B 1 245 ? 65.563 -14.716 72.214  1.00 38.89 ? 245 GLU B O   1 
ATOM   4719 C CB  . GLU B 1 245 ? 63.519 -15.528 74.121  1.00 42.60 ? 245 GLU B CB  1 
ATOM   4720 C CG  . GLU B 1 245 ? 62.206 -15.718 74.842  1.00 55.84 ? 245 GLU B CG  1 
ATOM   4721 C CD  . GLU B 1 245 ? 62.122 -17.106 75.493  1.00 66.61 ? 245 GLU B CD  1 
ATOM   4722 O OE1 . GLU B 1 245 ? 62.832 -18.033 75.026  1.00 69.54 ? 245 GLU B OE1 1 
ATOM   4723 O OE2 . GLU B 1 245 ? 61.363 -17.271 76.482  1.00 72.37 ? 245 GLU B OE2 1 
ATOM   4724 N N   . MET B 1 246 ? 66.325 -13.606 73.989  1.00 34.21 ? 246 MET B N   1 
ATOM   4725 C CA  . MET B 1 246 ? 67.704 -13.651 73.521  1.00 33.29 ? 246 MET B CA  1 
ATOM   4726 C C   . MET B 1 246 ? 68.606 -14.021 74.681  1.00 38.37 ? 246 MET B C   1 
ATOM   4727 O O   . MET B 1 246 ? 68.360 -13.586 75.804  1.00 43.79 ? 246 MET B O   1 
ATOM   4728 C CB  . MET B 1 246 ? 68.132 -12.296 72.968  1.00 32.59 ? 246 MET B CB  1 
ATOM   4729 C CG  . MET B 1 246 ? 67.467 -11.881 71.676  1.00 31.52 ? 246 MET B CG  1 
ATOM   4730 S SD  . MET B 1 246 ? 68.313 -10.456 70.986  1.00 39.73 ? 246 MET B SD  1 
ATOM   4731 C CE  . MET B 1 246 ? 67.476 -9.176  71.773  1.00 40.18 ? 246 MET B CE  1 
ATOM   4732 N N   . GLU B 1 247 ? 69.640 -14.826 74.431  1.00 42.33 ? 247 GLU B N   1 
ATOM   4733 C CA  . GLU B 1 247 ? 70.575 -15.226 75.493  1.00 42.57 ? 247 GLU B CA  1 
ATOM   4734 C C   . GLU B 1 247 ? 71.838 -14.373 75.421  1.00 42.27 ? 247 GLU B C   1 
ATOM   4735 O O   . GLU B 1 247 ? 72.219 -13.955 74.330  1.00 40.55 ? 247 GLU B O   1 
ATOM   4736 C CB  . GLU B 1 247 ? 70.923 -16.721 75.394  1.00 44.35 ? 247 GLU B CB  1 
ATOM   4737 C CG  . GLU B 1 247 ? 71.612 -17.153 74.096  1.00 47.98 ? 247 GLU B CG  1 
ATOM   4738 C CD  . GLU B 1 247 ? 72.116 -18.599 74.156  1.00 54.66 ? 247 GLU B CD  1 
ATOM   4739 O OE1 . GLU B 1 247 ? 71.304 -19.502 74.472  1.00 60.04 ? 247 GLU B OE1 1 
ATOM   4740 O OE2 . GLU B 1 247 ? 73.324 -18.838 73.894  1.00 54.35 ? 247 GLU B OE2 1 
ATOM   4741 N N   . GLU B 1 248 ? 72.483 -14.144 76.570  1.00 40.38 ? 248 GLU B N   1 
ATOM   4742 C CA  . GLU B 1 248 ? 73.704 -13.323 76.678  1.00 42.27 ? 248 GLU B CA  1 
ATOM   4743 C C   . GLU B 1 248 ? 74.674 -13.340 75.481  1.00 40.86 ? 248 GLU B C   1 
ATOM   4744 O O   . GLU B 1 248 ? 75.101 -14.400 75.003  1.00 42.14 ? 248 GLU B O   1 
ATOM   4745 C CB  . GLU B 1 248 ? 74.456 -13.660 77.981  1.00 46.15 ? 248 GLU B CB  1 
ATOM   4746 C CG  . GLU B 1 248 ? 75.842 -12.975 78.179  1.00 56.78 ? 248 GLU B CG  1 
ATOM   4747 C CD  . GLU B 1 248 ? 77.061 -13.804 77.669  1.00 64.71 ? 248 GLU B CD  1 
ATOM   4748 O OE1 . GLU B 1 248 ? 77.027 -15.061 77.709  1.00 64.35 ? 248 GLU B OE1 1 
ATOM   4749 O OE2 . GLU B 1 248 ? 78.072 -13.189 77.245  1.00 66.76 ? 248 GLU B OE2 1 
ATOM   4750 N N   . GLY B 1 249 ? 75.029 -12.152 75.005  1.00 37.87 ? 249 GLY B N   1 
ATOM   4751 C CA  . GLY B 1 249 ? 75.941 -12.055 73.883  1.00 39.36 ? 249 GLY B CA  1 
ATOM   4752 C C   . GLY B 1 249 ? 75.326 -12.201 72.497  1.00 38.77 ? 249 GLY B C   1 
ATOM   4753 O O   . GLY B 1 249 ? 76.042 -12.048 71.508  1.00 39.88 ? 249 GLY B O   1 
ATOM   4754 N N   . ALA B 1 250 ? 74.038 -12.545 72.420  1.00 38.98 ? 250 ALA B N   1 
ATOM   4755 C CA  . ALA B 1 250 ? 73.334 -12.697 71.144  1.00 38.24 ? 250 ALA B CA  1 
ATOM   4756 C C   . ALA B 1 250 ? 73.109 -11.333 70.511  1.00 39.36 ? 250 ALA B C   1 
ATOM   4757 O O   . ALA B 1 250 ? 73.143 -10.297 71.199  1.00 41.36 ? 250 ALA B O   1 
ATOM   4758 C CB  . ALA B 1 250 ? 72.005 -13.410 71.329  1.00 37.16 ? 250 ALA B CB  1 
ATOM   4759 N N   . LEU B 1 251 ? 72.868 -11.342 69.203  1.00 36.44 ? 251 LEU B N   1 
ATOM   4760 C CA  . LEU B 1 251 ? 72.674 -10.121 68.443  1.00 33.18 ? 251 LEU B CA  1 
ATOM   4761 C C   . LEU B 1 251 ? 71.588 -10.261 67.397  1.00 33.49 ? 251 LEU B C   1 
ATOM   4762 O O   . LEU B 1 251 ? 71.580 -11.209 66.620  1.00 30.11 ? 251 LEU B O   1 
ATOM   4763 C CB  . LEU B 1 251 ? 73.978 -9.715  67.750  1.00 30.86 ? 251 LEU B CB  1 
ATOM   4764 C CG  . LEU B 1 251 ? 73.904 -8.481  66.854  1.00 32.00 ? 251 LEU B CG  1 
ATOM   4765 C CD1 . LEU B 1 251 ? 73.657 -7.225  67.685  1.00 29.54 ? 251 LEU B CD1 1 
ATOM   4766 C CD2 . LEU B 1 251 ? 75.185 -8.353  66.071  1.00 32.18 ? 251 LEU B CD2 1 
ATOM   4767 N N   . PHE B 1 252 ? 70.667 -9.303  67.414  1.00 34.08 ? 252 PHE B N   1 
ATOM   4768 C CA  . PHE B 1 252 ? 69.564 -9.215  66.474  1.00 30.90 ? 252 PHE B CA  1 
ATOM   4769 C C   . PHE B 1 252 ? 70.132 -8.251  65.448  1.00 26.05 ? 252 PHE B C   1 
ATOM   4770 O O   . PHE B 1 252 ? 70.184 -7.038  65.674  1.00 25.76 ? 252 PHE B O   1 
ATOM   4771 C CB  . PHE B 1 252 ? 68.332 -8.598  67.146  1.00 31.88 ? 252 PHE B CB  1 
ATOM   4772 C CG  . PHE B 1 252 ? 67.031 -8.896  66.442  1.00 32.50 ? 252 PHE B CG  1 
ATOM   4773 C CD1 . PHE B 1 252 ? 67.011 -9.245  65.086  1.00 32.47 ? 252 PHE B CD1 1 
ATOM   4774 C CD2 . PHE B 1 252 ? 65.826 -8.834  67.140  1.00 29.43 ? 252 PHE B CD2 1 
ATOM   4775 C CE1 . PHE B 1 252 ? 65.813 -9.528  64.439  1.00 33.16 ? 252 PHE B CE1 1 
ATOM   4776 C CE2 . PHE B 1 252 ? 64.628 -9.112  66.509  1.00 35.78 ? 252 PHE B CE2 1 
ATOM   4777 C CZ  . PHE B 1 252 ? 64.624 -9.462  65.143  1.00 37.64 ? 252 PHE B CZ  1 
ATOM   4778 N N   . VAL B 1 253 ? 70.609 -8.819  64.350  1.00 26.74 ? 253 VAL B N   1 
ATOM   4779 C CA  . VAL B 1 253 ? 71.236 -8.068  63.267  1.00 24.97 ? 253 VAL B CA  1 
ATOM   4780 C C   . VAL B 1 253 ? 70.368 -6.917  62.778  1.00 20.96 ? 253 VAL B C   1 
ATOM   4781 O O   . VAL B 1 253 ? 69.134 -6.948  62.938  1.00 16.77 ? 253 VAL B O   1 
ATOM   4782 C CB  . VAL B 1 253 ? 71.557 -9.005  62.033  1.00 28.76 ? 253 VAL B CB  1 
ATOM   4783 C CG1 . VAL B 1 253 ? 72.442 -10.193 62.438  1.00 28.25 ? 253 VAL B CG1 1 
ATOM   4784 C CG2 . VAL B 1 253 ? 70.264 -9.482  61.357  1.00 30.13 ? 253 VAL B CG2 1 
ATOM   4785 N N   . PRO B 1 254 ? 71.002 -5.882  62.182  1.00 21.07 ? 254 PRO B N   1 
ATOM   4786 C CA  . PRO B 1 254 ? 70.294 -4.712  61.649  1.00 20.66 ? 254 PRO B CA  1 
ATOM   4787 C C   . PRO B 1 254 ? 69.122 -5.162  60.776  1.00 20.03 ? 254 PRO B C   1 
ATOM   4788 O O   . PRO B 1 254 ? 69.198 -6.177  60.063  1.00 25.20 ? 254 PRO B O   1 
ATOM   4789 C CB  . PRO B 1 254 ? 71.370 -4.021  60.820  1.00 19.84 ? 254 PRO B CB  1 
ATOM   4790 C CG  . PRO B 1 254 ? 72.582 -4.253  61.614  1.00 16.59 ? 254 PRO B CG  1 
ATOM   4791 C CD  . PRO B 1 254 ? 72.460 -5.714  62.026  1.00 19.67 ? 254 PRO B CD  1 
ATOM   4792 N N   . HIS B 1 255 ? 68.028 -4.420  60.869  1.00 17.92 ? 255 HIS B N   1 
ATOM   4793 C CA  . HIS B 1 255 ? 66.809 -4.716  60.143  1.00 15.93 ? 255 HIS B CA  1 
ATOM   4794 C C   . HIS B 1 255 ? 65.840 -3.565  60.361  1.00 13.88 ? 255 HIS B C   1 
ATOM   4795 O O   . HIS B 1 255 ? 66.158 -2.642  61.085  1.00 14.61 ? 255 HIS B O   1 
ATOM   4796 C CB  . HIS B 1 255 ? 66.197 -5.994  60.715  1.00 19.28 ? 255 HIS B CB  1 
ATOM   4797 C CG  . HIS B 1 255 ? 65.765 -5.873  62.148  1.00 24.02 ? 255 HIS B CG  1 
ATOM   4798 N ND1 . HIS B 1 255 ? 66.654 -5.936  63.199  1.00 18.91 ? 255 HIS B ND1 1 
ATOM   4799 C CD2 . HIS B 1 255 ? 64.543 -5.700  62.698  1.00 21.32 ? 255 HIS B CD2 1 
ATOM   4800 C CE1 . HIS B 1 255 ? 65.997 -5.808  64.336  1.00 24.24 ? 255 HIS B CE1 1 
ATOM   4801 N NE2 . HIS B 1 255 ? 64.711 -5.661  64.059  1.00 25.49 ? 255 HIS B NE2 1 
ATOM   4802 N N   . TYR B 1 256 ? 64.691 -3.596  59.691  1.00 20.66 ? 256 TYR B N   1 
ATOM   4803 C CA  . TYR B 1 256 ? 63.646 -2.584  59.870  1.00 18.73 ? 256 TYR B CA  1 
ATOM   4804 C C   . TYR B 1 256 ? 62.304 -3.208  59.489  1.00 21.46 ? 256 TYR B C   1 
ATOM   4805 O O   . TYR B 1 256 ? 62.253 -4.196  58.749  1.00 20.26 ? 256 TYR B O   1 
ATOM   4806 C CB  . TYR B 1 256 ? 63.905 -1.313  59.039  1.00 17.71 ? 256 TYR B CB  1 
ATOM   4807 C CG  . TYR B 1 256 ? 63.682 -1.441  57.536  1.00 18.00 ? 256 TYR B CG  1 
ATOM   4808 C CD1 . TYR B 1 256 ? 62.398 -1.434  56.988  1.00 19.81 ? 256 TYR B CD1 1 
ATOM   4809 C CD2 . TYR B 1 256 ? 64.762 -1.579  56.652  1.00 28.55 ? 256 TYR B CD2 1 
ATOM   4810 C CE1 . TYR B 1 256 ? 62.190 -1.565  55.598  1.00 15.70 ? 256 TYR B CE1 1 
ATOM   4811 C CE2 . TYR B 1 256 ? 64.559 -1.721  55.252  1.00 20.70 ? 256 TYR B CE2 1 
ATOM   4812 C CZ  . TYR B 1 256 ? 63.274 -1.715  54.741  1.00 22.02 ? 256 TYR B CZ  1 
ATOM   4813 O OH  . TYR B 1 256 ? 63.068 -1.902  53.381  1.00 17.10 ? 256 TYR B OH  1 
ATOM   4814 N N   . TYR B 1 257 ? 61.248 -2.713  60.123  1.00 22.78 ? 257 TYR B N   1 
ATOM   4815 C CA  . TYR B 1 257 ? 59.884 -3.133  59.862  1.00 20.70 ? 257 TYR B CA  1 
ATOM   4816 C C   . TYR B 1 257 ? 59.358 -2.027  58.981  1.00 20.62 ? 257 TYR B C   1 
ATOM   4817 O O   . TYR B 1 257 ? 59.393 -0.856  59.346  1.00 14.58 ? 257 TYR B O   1 
ATOM   4818 C CB  . TYR B 1 257 ? 59.080 -3.214  61.157  1.00 24.19 ? 257 TYR B CB  1 
ATOM   4819 C CG  . TYR B 1 257 ? 59.260 -4.528  61.876  1.00 26.58 ? 257 TYR B CG  1 
ATOM   4820 C CD1 . TYR B 1 257 ? 60.438 -5.260  61.736  1.00 27.75 ? 257 TYR B CD1 1 
ATOM   4821 C CD2 . TYR B 1 257 ? 58.259 -5.035  62.716  1.00 27.73 ? 257 TYR B CD2 1 
ATOM   4822 C CE1 . TYR B 1 257 ? 60.619 -6.460  62.418  1.00 31.81 ? 257 TYR B CE1 1 
ATOM   4823 C CE2 . TYR B 1 257 ? 58.429 -6.240  63.405  1.00 26.69 ? 257 TYR B CE2 1 
ATOM   4824 C CZ  . TYR B 1 257 ? 59.613 -6.939  63.247  1.00 31.01 ? 257 TYR B CZ  1 
ATOM   4825 O OH  . TYR B 1 257 ? 59.802 -8.115  63.913  1.00 33.52 ? 257 TYR B OH  1 
ATOM   4826 N N   . SER B 1 258 ? 58.890 -2.420  57.801  1.00 22.17 ? 258 SER B N   1 
ATOM   4827 C CA  . SER B 1 258 ? 58.362 -1.536  56.777  1.00 23.17 ? 258 SER B CA  1 
ATOM   4828 C C   . SER B 1 258 ? 57.193 -0.590  57.100  1.00 27.69 ? 258 SER B C   1 
ATOM   4829 O O   . SER B 1 258 ? 57.244 0.587   56.717  1.00 30.46 ? 258 SER B O   1 
ATOM   4830 C CB  . SER B 1 258 ? 57.993 -2.368  55.559  1.00 22.85 ? 258 SER B CB  1 
ATOM   4831 O OG  . SER B 1 258 ? 56.834 -3.160  55.799  1.00 27.45 ? 258 SER B OG  1 
ATOM   4832 N N   . LYS B 1 259 ? 56.106 -1.109  57.684  1.00 27.04 ? 259 LYS B N   1 
ATOM   4833 C CA  . LYS B 1 259 ? 54.949 -0.262  58.016  1.00 29.59 ? 259 LYS B CA  1 
ATOM   4834 C C   . LYS B 1 259 ? 54.631 -0.115  59.508  1.00 26.11 ? 259 LYS B C   1 
ATOM   4835 O O   . LYS B 1 259 ? 53.996 0.869   59.916  1.00 26.70 ? 259 LYS B O   1 
ATOM   4836 C CB  . LYS B 1 259 ? 53.645 -0.741  57.352  1.00 37.39 ? 259 LYS B CB  1 
ATOM   4837 C CG  . LYS B 1 259 ? 53.540 -0.548  55.884  1.00 53.20 ? 259 LYS B CG  1 
ATOM   4838 C CD  . LYS B 1 259 ? 53.804 -1.907  55.182  1.00 71.50 ? 259 LYS B CD  1 
ATOM   4839 C CE  . LYS B 1 259 ? 53.966 -1.820  53.610  1.00 76.66 ? 259 LYS B CE  1 
ATOM   4840 N NZ  . LYS B 1 259 ? 53.948 -3.175  52.882  1.00 75.90 ? 259 LYS B NZ  1 
ATOM   4841 N N   . ALA B 1 260 ? 55.021 -1.087  60.316  1.00 18.67 ? 260 ALA B N   1 
ATOM   4842 C CA  . ALA B 1 260 ? 54.684 -1.027  61.739  1.00 19.14 ? 260 ALA B CA  1 
ATOM   4843 C C   . ALA B 1 260 ? 55.514 -0.084  62.640  1.00 22.27 ? 260 ALA B C   1 
ATOM   4844 O O   . ALA B 1 260 ? 56.732 0.065   62.442  1.00 26.24 ? 260 ALA B O   1 
ATOM   4845 C CB  . ALA B 1 260 ? 54.699 -2.444  62.304  1.00 8.07  ? 260 ALA B CB  1 
ATOM   4846 N N   . ILE B 1 261 ? 54.847 0.619   63.567  1.00 23.44 ? 261 ILE B N   1 
ATOM   4847 C CA  . ILE B 1 261 ? 55.552 1.452   64.557  1.00 23.30 ? 261 ILE B CA  1 
ATOM   4848 C C   . ILE B 1 261 ? 55.695 0.444   65.721  1.00 22.58 ? 261 ILE B C   1 
ATOM   4849 O O   . ILE B 1 261 ? 54.693 -0.138  66.154  1.00 23.66 ? 261 ILE B O   1 
ATOM   4850 C CB  . ILE B 1 261 ? 54.707 2.634   65.063  1.00 20.96 ? 261 ILE B CB  1 
ATOM   4851 C CG1 . ILE B 1 261 ? 54.349 3.582   63.927  1.00 16.34 ? 261 ILE B CG1 1 
ATOM   4852 C CG2 . ILE B 1 261 ? 55.457 3.378   66.153  1.00 26.21 ? 261 ILE B CG2 1 
ATOM   4853 C CD1 . ILE B 1 261 ? 53.480 4.715   64.376  1.00 13.24 ? 261 ILE B CD1 1 
ATOM   4854 N N   . VAL B 1 262 ? 56.902 0.229   66.236  1.00 20.46 ? 262 VAL B N   1 
ATOM   4855 C CA  . VAL B 1 262 ? 57.068 -0.778  67.283  1.00 23.33 ? 262 VAL B CA  1 
ATOM   4856 C C   . VAL B 1 262 ? 57.413 -0.279  68.671  1.00 20.18 ? 262 VAL B C   1 
ATOM   4857 O O   . VAL B 1 262 ? 58.421 0.389   68.849  1.00 26.93 ? 262 VAL B O   1 
ATOM   4858 C CB  . VAL B 1 262 ? 58.110 -1.872  66.846  1.00 23.61 ? 262 VAL B CB  1 
ATOM   4859 C CG1 . VAL B 1 262 ? 58.392 -2.839  67.962  1.00 11.13 ? 262 VAL B CG1 1 
ATOM   4860 C CG2 . VAL B 1 262 ? 57.571 -2.674  65.665  1.00 27.11 ? 262 VAL B CG2 1 
ATOM   4861 N N   . ILE B 1 263 ? 56.577 -0.639  69.644  1.00 21.34 ? 263 ILE B N   1 
ATOM   4862 C CA  . ILE B 1 263 ? 56.767 -0.284  71.065  1.00 16.88 ? 263 ILE B CA  1 
ATOM   4863 C C   . ILE B 1 263 ? 57.394 -1.518  71.742  1.00 19.35 ? 263 ILE B C   1 
ATOM   4864 O O   . ILE B 1 263 ? 56.751 -2.576  71.793  1.00 20.34 ? 263 ILE B O   1 
ATOM   4865 C CB  . ILE B 1 263 ? 55.397 -0.076  71.806  1.00 16.66 ? 263 ILE B CB  1 
ATOM   4866 C CG1 . ILE B 1 263 ? 54.483 0.925   71.106  1.00 16.29 ? 263 ILE B CG1 1 
ATOM   4867 C CG2 . ILE B 1 263 ? 55.635 0.350   73.232  1.00 21.53 ? 263 ILE B CG2 1 
ATOM   4868 C CD1 . ILE B 1 263 ? 55.020 2.299   71.094  1.00 28.58 ? 263 ILE B CD1 1 
ATOM   4869 N N   . LEU B 1 264 ? 58.631 -1.412  72.227  1.00 26.55 ? 264 LEU B N   1 
ATOM   4870 C CA  . LEU B 1 264 ? 59.307 -2.528  72.920  1.00 27.15 ? 264 LEU B CA  1 
ATOM   4871 C C   . LEU B 1 264 ? 59.364 -2.327  74.452  1.00 29.81 ? 264 LEU B C   1 
ATOM   4872 O O   . LEU B 1 264 ? 59.519 -1.204  74.929  1.00 28.74 ? 264 LEU B O   1 
ATOM   4873 C CB  . LEU B 1 264 ? 60.749 -2.657  72.436  1.00 26.74 ? 264 LEU B CB  1 
ATOM   4874 C CG  . LEU B 1 264 ? 61.249 -3.769  71.519  1.00 31.24 ? 264 LEU B CG  1 
ATOM   4875 C CD1 . LEU B 1 264 ? 62.777 -3.770  71.563  1.00 30.20 ? 264 LEU B CD1 1 
ATOM   4876 C CD2 . LEU B 1 264 ? 60.716 -5.116  71.926  1.00 25.99 ? 264 LEU B CD2 1 
ATOM   4877 N N   . VAL B 1 265 ? 59.303 -3.423  75.207  1.00 34.08 ? 265 VAL B N   1 
ATOM   4878 C CA  . VAL B 1 265 ? 59.366 -3.376  76.680  1.00 35.45 ? 265 VAL B CA  1 
ATOM   4879 C C   . VAL B 1 265 ? 60.203 -4.540  77.233  1.00 33.50 ? 265 VAL B C   1 
ATOM   4880 O O   . VAL B 1 265 ? 59.978 -5.716  76.904  1.00 33.15 ? 265 VAL B O   1 
ATOM   4881 C CB  . VAL B 1 265 ? 57.943 -3.442  77.359  1.00 35.89 ? 265 VAL B CB  1 
ATOM   4882 C CG1 . VAL B 1 265 ? 58.062 -3.215  78.861  1.00 33.35 ? 265 VAL B CG1 1 
ATOM   4883 C CG2 . VAL B 1 265 ? 56.995 -2.408  76.764  1.00 38.12 ? 265 VAL B CG2 1 
ATOM   4884 N N   . VAL B 1 266 ? 61.186 -4.203  78.051  1.00 31.96 ? 266 VAL B N   1 
ATOM   4885 C CA  . VAL B 1 266 ? 62.045 -5.208  78.643  1.00 34.68 ? 266 VAL B CA  1 
ATOM   4886 C C   . VAL B 1 266 ? 61.308 -5.912  79.780  1.00 37.11 ? 266 VAL B C   1 
ATOM   4887 O O   . VAL B 1 266 ? 60.856 -5.250  80.717  1.00 37.26 ? 266 VAL B O   1 
ATOM   4888 C CB  . VAL B 1 266 ? 63.296 -4.559  79.229  1.00 35.06 ? 266 VAL B CB  1 
ATOM   4889 C CG1 . VAL B 1 266 ? 64.217 -5.627  79.797  1.00 33.58 ? 266 VAL B CG1 1 
ATOM   4890 C CG2 . VAL B 1 266 ? 64.000 -3.711  78.189  1.00 29.65 ? 266 VAL B CG2 1 
ATOM   4891 N N   . ASN B 1 267 ? 61.129 -7.228  79.672  1.00 37.63 ? 267 ASN B N   1 
ATOM   4892 C CA  . ASN B 1 267 ? 60.461 -7.988  80.735  1.00 38.51 ? 267 ASN B CA  1 
ATOM   4893 C C   . ASN B 1 267 ? 61.461 -8.398  81.807  1.00 37.71 ? 267 ASN B C   1 
ATOM   4894 O O   . ASN B 1 267 ? 61.160 -8.359  82.998  1.00 37.24 ? 267 ASN B O   1 
ATOM   4895 C CB  . ASN B 1 267 ? 59.800 -9.258  80.209  1.00 36.75 ? 267 ASN B CB  1 
ATOM   4896 C CG  . ASN B 1 267 ? 58.577 -8.983  79.397  1.00 35.19 ? 267 ASN B CG  1 
ATOM   4897 O OD1 . ASN B 1 267 ? 58.042 -7.878  79.406  1.00 29.62 ? 267 ASN B OD1 1 
ATOM   4898 N ND2 . ASN B 1 267 ? 58.130 -9.990  78.659  1.00 37.65 ? 267 ASN B ND2 1 
ATOM   4899 N N   . GLU B 1 268 ? 62.636 -8.827  81.363  1.00 37.03 ? 268 GLU B N   1 
ATOM   4900 C CA  . GLU B 1 268 ? 63.714 -9.266  82.233  1.00 37.79 ? 268 GLU B CA  1 
ATOM   4901 C C   . GLU B 1 268 ? 64.991 -9.190  81.408  1.00 37.72 ? 268 GLU B C   1 
ATOM   4902 O O   . GLU B 1 268 ? 64.967 -9.426  80.206  1.00 37.87 ? 268 GLU B O   1 
ATOM   4903 C CB  . GLU B 1 268 ? 63.479 -10.717 82.665  1.00 40.33 ? 268 GLU B CB  1 
ATOM   4904 C CG  . GLU B 1 268 ? 62.690 -10.901 83.957  1.00 50.93 ? 268 GLU B CG  1 
ATOM   4905 C CD  . GLU B 1 268 ? 63.505 -10.573 85.212  1.00 58.60 ? 268 GLU B CD  1 
ATOM   4906 O OE1 . GLU B 1 268 ? 64.310 -11.431 85.642  1.00 66.65 ? 268 GLU B OE1 1 
ATOM   4907 O OE2 . GLU B 1 268 ? 63.343 -9.466  85.773  1.00 59.05 ? 268 GLU B OE2 1 
ATOM   4908 N N   . GLY B 1 269 ? 66.110 -8.875  82.045  1.00 38.38 ? 269 GLY B N   1 
ATOM   4909 C CA  . GLY B 1 269 ? 67.361 -8.794  81.321  1.00 34.42 ? 269 GLY B CA  1 
ATOM   4910 C C   . GLY B 1 269 ? 67.687 -7.358  81.013  1.00 36.76 ? 269 GLY B C   1 
ATOM   4911 O O   . GLY B 1 269 ? 67.036 -6.431  81.532  1.00 35.39 ? 269 GLY B O   1 
ATOM   4912 N N   . GLU B 1 270 ? 68.734 -7.182  80.211  1.00 40.59 ? 270 GLU B N   1 
ATOM   4913 C CA  . GLU B 1 270 ? 69.211 -5.867  79.763  1.00 45.41 ? 270 GLU B CA  1 
ATOM   4914 C C   . GLU B 1 270 ? 69.849 -6.043  78.378  1.00 42.40 ? 270 GLU B C   1 
ATOM   4915 O O   . GLU B 1 270 ? 70.353 -7.130  78.072  1.00 40.79 ? 270 GLU B O   1 
ATOM   4916 C CB  . GLU B 1 270 ? 70.212 -5.288  80.767  1.00 49.30 ? 270 GLU B CB  1 
ATOM   4917 C CG  . GLU B 1 270 ? 71.358 -6.208  81.102  1.00 60.55 ? 270 GLU B CG  1 
ATOM   4918 C CD  . GLU B 1 270 ? 71.991 -5.868  82.433  1.00 67.24 ? 270 GLU B CD  1 
ATOM   4919 O OE1 . GLU B 1 270 ? 72.880 -4.986  82.459  1.00 68.98 ? 270 GLU B OE1 1 
ATOM   4920 O OE2 . GLU B 1 270 ? 71.590 -6.480  83.453  1.00 72.16 ? 270 GLU B OE2 1 
ATOM   4921 N N   . ALA B 1 271 ? 69.820 -4.998  77.545  1.00 41.57 ? 271 ALA B N   1 
ATOM   4922 C CA  . ALA B 1 271 ? 70.375 -5.083  76.178  1.00 40.56 ? 271 ALA B CA  1 
ATOM   4923 C C   . ALA B 1 271 ? 70.804 -3.751  75.543  1.00 37.12 ? 271 ALA B C   1 
ATOM   4924 O O   . ALA B 1 271 ? 70.316 -2.682  75.934  1.00 36.74 ? 271 ALA B O   1 
ATOM   4925 C CB  . ALA B 1 271 ? 69.371 -5.783  75.264  1.00 44.76 ? 271 ALA B CB  1 
ATOM   4926 N N   . HIS B 1 272 ? 71.734 -3.817  74.589  1.00 29.07 ? 272 HIS B N   1 
ATOM   4927 C CA  . HIS B 1 272 ? 72.192 -2.623  73.893  1.00 28.88 ? 272 HIS B CA  1 
ATOM   4928 C C   . HIS B 1 272 ? 71.361 -2.374  72.644  1.00 29.00 ? 272 HIS B C   1 
ATOM   4929 O O   . HIS B 1 272 ? 71.245 -3.241  71.761  1.00 23.25 ? 272 HIS B O   1 
ATOM   4930 C CB  . HIS B 1 272 ? 73.655 -2.765  73.498  1.00 29.50 ? 272 HIS B CB  1 
ATOM   4931 C CG  . HIS B 1 272 ? 74.198 -1.580  72.755  1.00 29.47 ? 272 HIS B CG  1 
ATOM   4932 N ND1 . HIS B 1 272 ? 74.167 -0.301  73.266  1.00 30.45 ? 272 HIS B ND1 1 
ATOM   4933 C CD2 . HIS B 1 272 ? 74.845 -1.490  71.565  1.00 27.01 ? 272 HIS B CD2 1 
ATOM   4934 C CE1 . HIS B 1 272 ? 74.782 0.523   72.438  1.00 33.01 ? 272 HIS B CE1 1 
ATOM   4935 N NE2 . HIS B 1 272 ? 75.205 -0.175  71.399  1.00 28.75 ? 272 HIS B NE2 1 
ATOM   4936 N N   . VAL B 1 273 ? 70.849 -1.154  72.524  1.00 31.56 ? 273 VAL B N   1 
ATOM   4937 C CA  . VAL B 1 273 ? 70.026 -0.816  71.372  1.00 28.00 ? 273 VAL B CA  1 
ATOM   4938 C C   . VAL B 1 273 ? 70.638 0.313   70.554  1.00 28.68 ? 273 VAL B C   1 
ATOM   4939 O O   . VAL B 1 273 ? 71.166 1.277   71.105  1.00 26.56 ? 273 VAL B O   1 
ATOM   4940 C CB  . VAL B 1 273 ? 68.575 -0.487  71.801  1.00 24.26 ? 273 VAL B CB  1 
ATOM   4941 C CG1 . VAL B 1 273 ? 68.432 0.946   72.222  1.00 26.85 ? 273 VAL B CG1 1 
ATOM   4942 C CG2 . VAL B 1 273 ? 67.609 -0.821  70.706  1.00 21.14 ? 273 VAL B CG2 1 
ATOM   4943 N N   . GLU B 1 274 ? 70.663 0.115   69.238  1.00 29.34 ? 274 GLU B N   1 
ATOM   4944 C CA  . GLU B 1 274 ? 71.188 1.099   68.292  1.00 28.53 ? 274 GLU B CA  1 
ATOM   4945 C C   . GLU B 1 274 ? 70.113 1.353   67.215  1.00 27.33 ? 274 GLU B C   1 
ATOM   4946 O O   . GLU B 1 274 ? 69.659 0.413   66.555  1.00 24.76 ? 274 GLU B O   1 
ATOM   4947 C CB  . GLU B 1 274 ? 72.467 0.574   67.626  1.00 28.98 ? 274 GLU B CB  1 
ATOM   4948 C CG  . GLU B 1 274 ? 73.502 0.062   68.600  1.00 23.77 ? 274 GLU B CG  1 
ATOM   4949 C CD  . GLU B 1 274 ? 74.930 0.129   68.061  1.00 31.45 ? 274 GLU B CD  1 
ATOM   4950 O OE1 . GLU B 1 274 ? 75.162 0.293   66.827  1.00 29.54 ? 274 GLU B OE1 1 
ATOM   4951 O OE2 . GLU B 1 274 ? 75.841 0.035   68.888  1.00 33.94 ? 274 GLU B OE2 1 
ATOM   4952 N N   . LEU B 1 275 ? 69.691 2.609   67.075  1.00 22.72 ? 275 LEU B N   1 
ATOM   4953 C CA  . LEU B 1 275 ? 68.674 2.996   66.108  1.00 22.99 ? 275 LEU B CA  1 
ATOM   4954 C C   . LEU B 1 275 ? 69.218 4.105   65.212  1.00 27.10 ? 275 LEU B C   1 
ATOM   4955 O O   . LEU B 1 275 ? 69.800 5.071   65.710  1.00 29.10 ? 275 LEU B O   1 
ATOM   4956 C CB  . LEU B 1 275 ? 67.420 3.523   66.821  1.00 22.33 ? 275 LEU B CB  1 
ATOM   4957 C CG  . LEU B 1 275 ? 66.237 4.007   65.957  1.00 19.58 ? 275 LEU B CG  1 
ATOM   4958 C CD1 . LEU B 1 275 ? 65.321 2.855   65.627  1.00 13.97 ? 275 LEU B CD1 1 
ATOM   4959 C CD2 . LEU B 1 275 ? 65.434 5.105   66.645  1.00 18.59 ? 275 LEU B CD2 1 
ATOM   4960 N N   . VAL B 1 276 ? 69.029 3.966   63.903  1.00 25.37 ? 276 VAL B N   1 
ATOM   4961 C CA  . VAL B 1 276 ? 69.472 4.966   62.946  1.00 24.16 ? 276 VAL B CA  1 
ATOM   4962 C C   . VAL B 1 276 ? 68.226 5.729   62.500  1.00 24.81 ? 276 VAL B C   1 
ATOM   4963 O O   . VAL B 1 276 ? 67.321 5.165   61.901  1.00 22.76 ? 276 VAL B O   1 
ATOM   4964 C CB  . VAL B 1 276 ? 70.171 4.312   61.716  1.00 24.01 ? 276 VAL B CB  1 
ATOM   4965 C CG1 . VAL B 1 276 ? 70.802 5.370   60.839  1.00 21.64 ? 276 VAL B CG1 1 
ATOM   4966 C CG2 . VAL B 1 276 ? 71.240 3.343   62.167  1.00 28.87 ? 276 VAL B CG2 1 
ATOM   4967 N N   . GLY B 1 277 ? 68.137 6.995   62.868  1.00 26.91 ? 277 GLY B N   1 
ATOM   4968 C CA  . GLY B 1 277 ? 66.986 7.774   62.464  1.00 33.33 ? 277 GLY B CA  1 
ATOM   4969 C C   . GLY B 1 277 ? 67.468 9.009   61.731  1.00 37.88 ? 277 GLY B C   1 
ATOM   4970 O O   . GLY B 1 277 ? 68.654 9.078   61.395  1.00 39.50 ? 277 GLY B O   1 
ATOM   4971 N N   . PRO B 1 278 ? 66.578 9.971   61.412  1.00 41.21 ? 278 PRO B N   1 
ATOM   4972 C CA  . PRO B 1 278 ? 66.984 11.197  60.714  1.00 41.08 ? 278 PRO B CA  1 
ATOM   4973 C C   . PRO B 1 278 ? 67.652 12.133  61.728  1.00 38.62 ? 278 PRO B C   1 
ATOM   4974 O O   . PRO B 1 278 ? 67.259 12.170  62.894  1.00 35.14 ? 278 PRO B O   1 
ATOM   4975 C CB  . PRO B 1 278 ? 65.652 11.754  60.223  1.00 44.13 ? 278 PRO B CB  1 
ATOM   4976 C CG  . PRO B 1 278 ? 64.707 11.363  61.329  1.00 46.17 ? 278 PRO B CG  1 
ATOM   4977 C CD  . PRO B 1 278 ? 65.114 9.934   61.602  1.00 43.25 ? 278 PRO B CD  1 
ATOM   4978 N N   . LYS B 1 279 ? 68.693 12.836  61.296  1.00 40.48 ? 279 LYS B N   1 
ATOM   4979 C CA  . LYS B 1 279 ? 69.420 13.750  62.159  1.00 42.96 ? 279 LYS B CA  1 
ATOM   4980 C C   . LYS B 1 279 ? 68.505 14.885  62.597  1.00 46.51 ? 279 LYS B C   1 
ATOM   4981 O O   . LYS B 1 279 ? 68.449 15.932  61.941  1.00 49.98 ? 279 LYS B O   1 
ATOM   4982 C CB  . LYS B 1 279 ? 70.624 14.307  61.413  1.00 43.70 ? 279 LYS B CB  1 
ATOM   4983 C CG  . LYS B 1 279 ? 71.456 15.256  62.226  1.00 51.38 ? 279 LYS B CG  1 
ATOM   4984 C CD  . LYS B 1 279 ? 72.558 15.856  61.383  1.00 60.29 ? 279 LYS B CD  1 
ATOM   4985 C CE  . LYS B 1 279 ? 72.959 17.232  61.900  1.00 65.88 ? 279 LYS B CE  1 
ATOM   4986 N NZ  . LYS B 1 279 ? 71.851 18.235  61.776  1.00 67.31 ? 279 LYS B NZ  1 
ATOM   4987 N N   . GLY B 1 280 ? 67.768 14.663  63.686  1.00 46.47 ? 280 GLY B N   1 
ATOM   4988 C CA  . GLY B 1 280 ? 66.846 15.667  64.196  1.00 45.26 ? 280 GLY B CA  1 
ATOM   4989 C C   . GLY B 1 280 ? 65.461 15.574  63.568  1.00 45.94 ? 280 GLY B C   1 
ATOM   4990 O O   . GLY B 1 280 ? 64.626 16.478  63.701  1.00 43.06 ? 280 GLY B O   1 
ATOM   4991 N N   . GLU B 1 283 ? 64.605 17.194  57.646  1.00 43.53 ? 283 GLU B N   1 
ATOM   4992 C CA  . GLU B 1 283 ? 64.357 16.726  56.283  1.00 45.88 ? 283 GLU B CA  1 
ATOM   4993 C C   . GLU B 1 283 ? 65.595 16.841  55.391  1.00 44.60 ? 283 GLU B C   1 
ATOM   4994 O O   . GLU B 1 283 ? 65.666 17.730  54.546  1.00 47.28 ? 283 GLU B O   1 
ATOM   4995 C CB  . GLU B 1 283 ? 63.202 17.512  55.670  1.00 47.24 ? 283 GLU B CB  1 
ATOM   4996 C CG  . GLU B 1 283 ? 62.209 16.650  54.918  1.00 44.88 ? 283 GLU B CG  1 
ATOM   4997 C CD  . GLU B 1 283 ? 60.822 17.257  54.910  1.00 43.77 ? 283 GLU B CD  1 
ATOM   4998 O OE1 . GLU B 1 283 ? 60.568 18.132  54.051  1.00 47.00 ? 283 GLU B OE1 1 
ATOM   4999 O OE2 . GLU B 1 283 ? 59.998 16.862  55.767  1.00 33.66 ? 283 GLU B OE2 1 
ATOM   5000 N N   . THR B 1 284 ? 66.554 15.932  55.597  1.00 44.83 ? 284 THR B N   1 
ATOM   5001 C CA  . THR B 1 284 ? 67.828 15.874  54.862  1.00 42.24 ? 284 THR B CA  1 
ATOM   5002 C C   . THR B 1 284 ? 68.244 14.414  54.697  1.00 38.88 ? 284 THR B C   1 
ATOM   5003 O O   . THR B 1 284 ? 67.512 13.503  55.073  1.00 39.75 ? 284 THR B O   1 
ATOM   5004 C CB  . THR B 1 284 ? 68.999 16.582  55.632  1.00 45.90 ? 284 THR B CB  1 
ATOM   5005 O OG1 . THR B 1 284 ? 69.165 15.986  56.932  1.00 43.15 ? 284 THR B OG1 1 
ATOM   5006 C CG2 . THR B 1 284 ? 68.766 18.090  55.764  1.00 46.89 ? 284 THR B CG2 1 
ATOM   5007 N N   . LEU B 1 285 ? 69.441 14.198  54.174  1.00 35.30 ? 285 LEU B N   1 
ATOM   5008 C CA  . LEU B 1 285 ? 69.956 12.845  53.981  1.00 31.28 ? 285 LEU B CA  1 
ATOM   5009 C C   . LEU B 1 285 ? 71.070 12.634  55.001  1.00 30.03 ? 285 LEU B C   1 
ATOM   5010 O O   . LEU B 1 285 ? 72.062 11.955  54.725  1.00 27.54 ? 285 LEU B O   1 
ATOM   5011 C CB  . LEU B 1 285 ? 70.532 12.688  52.566  1.00 27.71 ? 285 LEU B CB  1 
ATOM   5012 C CG  . LEU B 1 285 ? 69.739 13.240  51.390  1.00 23.80 ? 285 LEU B CG  1 
ATOM   5013 C CD1 . LEU B 1 285 ? 70.489 12.934  50.096  1.00 26.06 ? 285 LEU B CD1 1 
ATOM   5014 C CD2 . LEU B 1 285 ? 68.351 12.625  51.373  1.00 22.57 ? 285 LEU B CD2 1 
ATOM   5015 N N   . GLU B 1 286 ? 70.915 13.235  56.176  1.00 29.54 ? 286 GLU B N   1 
ATOM   5016 C CA  . GLU B 1 286 ? 71.935 13.118  57.215  1.00 32.27 ? 286 GLU B CA  1 
ATOM   5017 C C   . GLU B 1 286 ? 71.388 12.299  58.367  1.00 27.53 ? 286 GLU B C   1 
ATOM   5018 O O   . GLU B 1 286 ? 70.344 12.633  58.916  1.00 24.60 ? 286 GLU B O   1 
ATOM   5019 C CB  . GLU B 1 286 ? 72.354 14.512  57.687  1.00 37.86 ? 286 GLU B CB  1 
ATOM   5020 C CG  . GLU B 1 286 ? 73.803 14.617  58.154  1.00 40.70 ? 286 GLU B CG  1 
ATOM   5021 C CD  . GLU B 1 286 ? 74.316 16.047  58.160  1.00 45.98 ? 286 GLU B CD  1 
ATOM   5022 O OE1 . GLU B 1 286 ? 73.856 16.851  57.318  1.00 50.17 ? 286 GLU B OE1 1 
ATOM   5023 O OE2 . GLU B 1 286 ? 75.191 16.361  58.993  1.00 49.88 ? 286 GLU B OE2 1 
ATOM   5024 N N   . TYR B 1 287 ? 72.065 11.208  58.706  1.00 27.45 ? 287 TYR B N   1 
ATOM   5025 C CA  . TYR B 1 287 ? 71.584 10.358  59.778  1.00 31.54 ? 287 TYR B CA  1 
ATOM   5026 C C   . TYR B 1 287 ? 72.206 10.660  61.120  1.00 35.15 ? 287 TYR B C   1 
ATOM   5027 O O   . TYR B 1 287 ? 72.875 11.675  61.304  1.00 38.44 ? 287 TYR B O   1 
ATOM   5028 C CB  . TYR B 1 287 ? 71.730 8.881   59.419  1.00 33.61 ? 287 TYR B CB  1 
ATOM   5029 C CG  . TYR B 1 287 ? 71.049 8.557   58.120  1.00 35.65 ? 287 TYR B CG  1 
ATOM   5030 C CD1 . TYR B 1 287 ? 69.670 8.728   57.967  1.00 33.52 ? 287 TYR B CD1 1 
ATOM   5031 C CD2 . TYR B 1 287 ? 71.801 8.215   56.996  1.00 40.10 ? 287 TYR B CD2 1 
ATOM   5032 C CE1 . TYR B 1 287 ? 69.068 8.590   56.723  1.00 34.55 ? 287 TYR B CE1 1 
ATOM   5033 C CE2 . TYR B 1 287 ? 71.210 8.069   55.743  1.00 38.34 ? 287 TYR B CE2 1 
ATOM   5034 C CZ  . TYR B 1 287 ? 69.852 8.267   55.612  1.00 39.34 ? 287 TYR B CZ  1 
ATOM   5035 O OH  . TYR B 1 287 ? 69.312 8.208   54.349  1.00 42.21 ? 287 TYR B OH  1 
ATOM   5036 N N   . GLU B 1 288 ? 71.933 9.791   62.078  1.00 37.96 ? 288 GLU B N   1 
ATOM   5037 C CA  . GLU B 1 288 ? 72.434 9.957   63.419  1.00 35.54 ? 288 GLU B CA  1 
ATOM   5038 C C   . GLU B 1 288 ? 72.014 8.690   64.136  1.00 31.10 ? 288 GLU B C   1 
ATOM   5039 O O   . GLU B 1 288 ? 71.008 8.073   63.763  1.00 29.30 ? 288 GLU B O   1 
ATOM   5040 C CB  . GLU B 1 288 ? 71.757 11.173  64.025  1.00 39.54 ? 288 GLU B CB  1 
ATOM   5041 C CG  . GLU B 1 288 ? 72.307 11.598  65.352  1.00 59.26 ? 288 GLU B CG  1 
ATOM   5042 C CD  . GLU B 1 288 ? 71.614 12.836  65.883  1.00 68.46 ? 288 GLU B CD  1 
ATOM   5043 O OE1 . GLU B 1 288 ? 70.480 13.136  65.432  1.00 74.75 ? 288 GLU B OE1 1 
ATOM   5044 O OE2 . GLU B 1 288 ? 72.210 13.510  66.751  1.00 74.91 ? 288 GLU B OE2 1 
ATOM   5045 N N   . SER B 1 289 ? 72.787 8.276   65.133  1.00 28.74 ? 289 SER B N   1 
ATOM   5046 C CA  . SER B 1 289 ? 72.457 7.063   65.864  1.00 31.28 ? 289 SER B CA  1 
ATOM   5047 C C   . SER B 1 289 ? 71.871 7.392   67.245  1.00 32.84 ? 289 SER B C   1 
ATOM   5048 O O   . SER B 1 289 ? 72.298 8.348   67.894  1.00 34.68 ? 289 SER B O   1 
ATOM   5049 C CB  . SER B 1 289 ? 73.698 6.182   65.989  1.00 32.33 ? 289 SER B CB  1 
ATOM   5050 O OG  . SER B 1 289 ? 73.335 4.837   66.252  1.00 42.98 ? 289 SER B OG  1 
ATOM   5051 N N   . TYR B 1 290 ? 70.874 6.616   67.665  1.00 32.60 ? 290 TYR B N   1 
ATOM   5052 C CA  . TYR B 1 290 ? 70.201 6.795   68.952  1.00 31.40 ? 290 TYR B CA  1 
ATOM   5053 C C   . TYR B 1 290 ? 70.444 5.547   69.786  1.00 30.79 ? 290 TYR B C   1 
ATOM   5054 O O   . TYR B 1 290 ? 69.582 4.683   69.911  1.00 33.40 ? 290 TYR B O   1 
ATOM   5055 C CB  . TYR B 1 290 ? 68.694 7.018   68.744  1.00 30.59 ? 290 TYR B CB  1 
ATOM   5056 C CG  . TYR B 1 290 ? 68.395 8.293   67.992  1.00 35.93 ? 290 TYR B CG  1 
ATOM   5057 C CD1 . TYR B 1 290 ? 68.417 9.514   68.648  1.00 35.86 ? 290 TYR B CD1 1 
ATOM   5058 C CD2 . TYR B 1 290 ? 68.189 8.296   66.602  1.00 36.35 ? 290 TYR B CD2 1 
ATOM   5059 C CE1 . TYR B 1 290 ? 68.254 10.706  67.953  1.00 33.86 ? 290 TYR B CE1 1 
ATOM   5060 C CE2 . TYR B 1 290 ? 68.026 9.500   65.895  1.00 29.70 ? 290 TYR B CE2 1 
ATOM   5061 C CZ  . TYR B 1 290 ? 68.067 10.695  66.588  1.00 26.44 ? 290 TYR B CZ  1 
ATOM   5062 O OH  . TYR B 1 290 ? 67.959 11.902  65.957  1.00 30.03 ? 290 TYR B OH  1 
ATOM   5063 N N   . ARG B 1 291 ? 71.651 5.433   70.311  1.00 30.07 ? 291 ARG B N   1 
ATOM   5064 C CA  . ARG B 1 291 ? 72.026 4.283   71.116  1.00 31.44 ? 291 ARG B CA  1 
ATOM   5065 C C   . ARG B 1 291 ? 71.442 4.399   72.526  1.00 29.41 ? 291 ARG B C   1 
ATOM   5066 O O   . ARG B 1 291 ? 71.223 5.492   73.040  1.00 30.85 ? 291 ARG B O   1 
ATOM   5067 C CB  . ARG B 1 291 ? 73.553 4.154   71.184  1.00 33.54 ? 291 ARG B CB  1 
ATOM   5068 C CG  . ARG B 1 291 ? 74.312 4.388   69.861  1.00 36.78 ? 291 ARG B CG  1 
ATOM   5069 C CD  . ARG B 1 291 ? 75.642 3.626   69.870  1.00 44.41 ? 291 ARG B CD  1 
ATOM   5070 N NE  . ARG B 1 291 ? 76.605 4.034   68.843  1.00 51.20 ? 291 ARG B NE  1 
ATOM   5071 C CZ  . ARG B 1 291 ? 76.580 3.651   67.568  1.00 52.25 ? 291 ARG B CZ  1 
ATOM   5072 N NH1 . ARG B 1 291 ? 75.608 2.876   67.114  1.00 53.57 ? 291 ARG B NH1 1 
ATOM   5073 N NH2 . ARG B 1 291 ? 77.515 4.079   66.729  1.00 54.94 ? 291 ARG B NH2 1 
ATOM   5074 N N   . ALA B 1 292 ? 71.126 3.266   73.127  1.00 30.38 ? 292 ALA B N   1 
ATOM   5075 C CA  . ALA B 1 292 ? 70.580 3.260   74.477  1.00 29.76 ? 292 ALA B CA  1 
ATOM   5076 C C   . ALA B 1 292 ? 70.830 1.918   75.186  1.00 31.01 ? 292 ALA B C   1 
ATOM   5077 O O   . ALA B 1 292 ? 71.140 0.898   74.554  1.00 31.93 ? 292 ALA B O   1 
ATOM   5078 C CB  . ALA B 1 292 ? 69.107 3.597   74.444  1.00 28.08 ? 292 ALA B CB  1 
ATOM   5079 N N   . GLU B 1 293 ? 70.792 1.937   76.507  1.00 31.51 ? 293 GLU B N   1 
ATOM   5080 C CA  . GLU B 1 293 ? 71.018 0.719   77.253  1.00 30.84 ? 293 GLU B CA  1 
ATOM   5081 C C   . GLU B 1 293 ? 69.744 0.411   78.019  1.00 32.21 ? 293 GLU B C   1 
ATOM   5082 O O   . GLU B 1 293 ? 69.364 1.126   78.953  1.00 34.37 ? 293 GLU B O   1 
ATOM   5083 C CB  . GLU B 1 293 ? 72.232 0.870   78.163  1.00 34.80 ? 293 GLU B CB  1 
ATOM   5084 C CG  . GLU B 1 293 ? 73.348 -0.154  77.887  1.00 41.67 ? 293 GLU B CG  1 
ATOM   5085 C CD  . GLU B 1 293 ? 74.014 0.004   76.519  1.00 44.07 ? 293 GLU B CD  1 
ATOM   5086 O OE1 . GLU B 1 293 ? 74.227 1.149   76.054  1.00 48.43 ? 293 GLU B OE1 1 
ATOM   5087 O OE2 . GLU B 1 293 ? 74.343 -1.034  75.912  1.00 41.26 ? 293 GLU B OE2 1 
ATOM   5088 N N   . LEU B 1 294 ? 69.060 -0.629  77.552  1.00 30.52 ? 294 LEU B N   1 
ATOM   5089 C CA  . LEU B 1 294 ? 67.793 -1.077  78.088  1.00 27.59 ? 294 LEU B CA  1 
ATOM   5090 C C   . LEU B 1 294 ? 67.907 -2.029  79.265  1.00 29.07 ? 294 LEU B C   1 
ATOM   5091 O O   . LEU B 1 294 ? 68.787 -2.893  79.297  1.00 26.60 ? 294 LEU B O   1 
ATOM   5092 C CB  . LEU B 1 294 ? 67.002 -1.752  76.973  1.00 24.16 ? 294 LEU B CB  1 
ATOM   5093 C CG  . LEU B 1 294 ? 66.269 -0.896  75.945  1.00 24.50 ? 294 LEU B CG  1 
ATOM   5094 C CD1 . LEU B 1 294 ? 66.785 0.529   75.908  1.00 21.25 ? 294 LEU B CD1 1 
ATOM   5095 C CD2 . LEU B 1 294 ? 66.388 -1.568  74.577  1.00 30.20 ? 294 LEU B CD2 1 
ATOM   5096 N N   . SER B 1 295 ? 66.955 -1.898  80.185  1.00 31.26 ? 295 SER B N   1 
ATOM   5097 C CA  . SER B 1 295 ? 66.863 -2.722  81.388  1.00 32.22 ? 295 SER B CA  1 
ATOM   5098 C C   . SER B 1 295 ? 65.379 -2.889  81.733  1.00 32.02 ? 295 SER B C   1 
ATOM   5099 O O   . SER B 1 295 ? 64.523 -2.236  81.122  1.00 32.46 ? 295 SER B O   1 
ATOM   5100 C CB  . SER B 1 295 ? 67.601 -2.053  82.554  1.00 38.52 ? 295 SER B CB  1 
ATOM   5101 O OG  . SER B 1 295 ? 66.985 -0.837  82.947  1.00 45.12 ? 295 SER B OG  1 
ATOM   5102 N N   . LYS B 1 296 ? 65.085 -3.757  82.698  1.00 29.25 ? 296 LYS B N   1 
ATOM   5103 C CA  . LYS B 1 296 ? 63.709 -4.045  83.122  1.00 27.41 ? 296 LYS B CA  1 
ATOM   5104 C C   . LYS B 1 296 ? 62.745 -2.865  83.108  1.00 26.86 ? 296 LYS B C   1 
ATOM   5105 O O   . LYS B 1 296 ? 63.078 -1.779  83.564  1.00 30.20 ? 296 LYS B O   1 
ATOM   5106 C CB  . LYS B 1 296 ? 63.722 -4.687  84.511  1.00 27.01 ? 296 LYS B CB  1 
ATOM   5107 C CG  . LYS B 1 296 ? 62.377 -5.022  85.075  1.00 24.83 ? 296 LYS B CG  1 
ATOM   5108 C CD  . LYS B 1 296 ? 62.260 -6.518  85.266  1.00 33.53 ? 296 LYS B CD  1 
ATOM   5109 C CE  . LYS B 1 296 ? 60.910 -6.912  85.865  1.00 34.46 ? 296 LYS B CE  1 
ATOM   5110 N NZ  . LYS B 1 296 ? 60.748 -6.343  87.232  1.00 41.53 ? 296 LYS B NZ  1 
ATOM   5111 N N   . ASP B 1 297 ? 61.549 -3.098  82.574  1.00 29.08 ? 297 ASP B N   1 
ATOM   5112 C CA  . ASP B 1 297 ? 60.483 -2.098  82.482  1.00 28.59 ? 297 ASP B CA  1 
ATOM   5113 C C   . ASP B 1 297 ? 60.720 -0.867  81.606  1.00 26.78 ? 297 ASP B C   1 
ATOM   5114 O O   . ASP B 1 297 ? 59.891 0.060   81.581  1.00 24.81 ? 297 ASP B O   1 
ATOM   5115 C CB  . ASP B 1 297 ? 59.977 -1.695  83.867  1.00 30.61 ? 297 ASP B CB  1 
ATOM   5116 C CG  . ASP B 1 297 ? 59.027 -2.717  84.452  1.00 35.15 ? 297 ASP B CG  1 
ATOM   5117 O OD1 . ASP B 1 297 ? 58.401 -3.468  83.667  1.00 38.58 ? 297 ASP B OD1 1 
ATOM   5118 O OD2 . ASP B 1 297 ? 58.899 -2.765  85.698  1.00 37.84 ? 297 ASP B OD2 1 
ATOM   5119 N N   . ASP B 1 298 ? 61.861 -0.835  80.927  1.00 23.06 ? 298 ASP B N   1 
ATOM   5120 C CA  . ASP B 1 298 ? 62.155 0.254   80.011  1.00 22.37 ? 298 ASP B CA  1 
ATOM   5121 C C   . ASP B 1 298 ? 61.328 0.018   78.727  1.00 21.72 ? 298 ASP B C   1 
ATOM   5122 O O   . ASP B 1 298 ? 61.017 -1.125  78.375  1.00 16.35 ? 298 ASP B O   1 
ATOM   5123 C CB  . ASP B 1 298 ? 63.652 0.270   79.661  1.00 22.59 ? 298 ASP B CB  1 
ATOM   5124 C CG  . ASP B 1 298 ? 64.486 1.107   80.625  1.00 16.65 ? 298 ASP B CG  1 
ATOM   5125 O OD1 . ASP B 1 298 ? 63.914 1.915   81.375  1.00 23.21 ? 298 ASP B OD1 1 
ATOM   5126 O OD2 . ASP B 1 298 ? 65.733 0.982   80.608  1.00 17.79 ? 298 ASP B OD2 1 
ATOM   5127 N N   . VAL B 1 299 ? 60.945 1.107   78.066  1.00 24.23 ? 299 VAL B N   1 
ATOM   5128 C CA  . VAL B 1 299 ? 60.170 1.059   76.824  1.00 22.99 ? 299 VAL B CA  1 
ATOM   5129 C C   . VAL B 1 299 ? 60.961 1.809   75.748  1.00 23.23 ? 299 VAL B C   1 
ATOM   5130 O O   . VAL B 1 299 ? 61.408 2.939   75.981  1.00 21.89 ? 299 VAL B O   1 
ATOM   5131 C CB  . VAL B 1 299 ? 58.794 1.774   76.975  1.00 20.08 ? 299 VAL B CB  1 
ATOM   5132 C CG1 . VAL B 1 299 ? 58.038 1.772   75.670  1.00 20.02 ? 299 VAL B CG1 1 
ATOM   5133 C CG2 . VAL B 1 299 ? 57.963 1.110   78.038  1.00 12.28 ? 299 VAL B CG2 1 
ATOM   5134 N N   . PHE B 1 300 ? 61.152 1.176   74.591  1.00 23.38 ? 300 PHE B N   1 
ATOM   5135 C CA  . PHE B 1 300 ? 61.869 1.794   73.478  1.00 17.99 ? 300 PHE B CA  1 
ATOM   5136 C C   . PHE B 1 300 ? 60.980 1.797   72.226  1.00 20.11 ? 300 PHE B C   1 
ATOM   5137 O O   . PHE B 1 300 ? 60.430 0.763   71.837  1.00 17.98 ? 300 PHE B O   1 
ATOM   5138 C CB  . PHE B 1 300 ? 63.173 1.045   73.206  1.00 20.26 ? 300 PHE B CB  1 
ATOM   5139 C CG  . PHE B 1 300 ? 64.163 1.815   72.365  1.00 22.54 ? 300 PHE B CG  1 
ATOM   5140 C CD1 . PHE B 1 300 ? 65.046 2.720   72.958  1.00 17.37 ? 300 PHE B CD1 1 
ATOM   5141 C CD2 . PHE B 1 300 ? 64.223 1.621   70.983  1.00 21.50 ? 300 PHE B CD2 1 
ATOM   5142 C CE1 . PHE B 1 300 ? 65.980 3.421   72.190  1.00 25.83 ? 300 PHE B CE1 1 
ATOM   5143 C CE2 . PHE B 1 300 ? 65.140 2.308   70.204  1.00 22.79 ? 300 PHE B CE2 1 
ATOM   5144 C CZ  . PHE B 1 300 ? 66.027 3.216   70.803  1.00 27.86 ? 300 PHE B CZ  1 
ATOM   5145 N N   . VAL B 1 301 ? 60.815 2.972   71.628  1.00 18.06 ? 301 VAL B N   1 
ATOM   5146 C CA  . VAL B 1 301 ? 60.012 3.151   70.426  1.00 18.33 ? 301 VAL B CA  1 
ATOM   5147 C C   . VAL B 1 301 ? 60.812 3.049   69.104  1.00 16.96 ? 301 VAL B C   1 
ATOM   5148 O O   . VAL B 1 301 ? 61.854 3.685   68.932  1.00 16.32 ? 301 VAL B O   1 
ATOM   5149 C CB  . VAL B 1 301 ? 59.280 4.521   70.491  1.00 21.67 ? 301 VAL B CB  1 
ATOM   5150 C CG1 . VAL B 1 301 ? 58.620 4.862   69.150  1.00 9.01  ? 301 VAL B CG1 1 
ATOM   5151 C CG2 . VAL B 1 301 ? 58.252 4.504   71.628  1.00 14.99 ? 301 VAL B CG2 1 
ATOM   5152 N N   . ILE B 1 302 ? 60.326 2.248   68.164  1.00 14.95 ? 302 ILE B N   1 
ATOM   5153 C CA  . ILE B 1 302 ? 61.006 2.136   66.883  1.00 16.93 ? 302 ILE B CA  1 
ATOM   5154 C C   . ILE B 1 302 ? 60.044 2.523   65.739  1.00 18.34 ? 302 ILE B C   1 
ATOM   5155 O O   . ILE B 1 302 ? 59.037 1.856   65.508  1.00 25.30 ? 302 ILE B O   1 
ATOM   5156 C CB  . ILE B 1 302 ? 61.537 0.734   66.658  1.00 18.54 ? 302 ILE B CB  1 
ATOM   5157 C CG1 . ILE B 1 302 ? 62.317 0.261   67.871  1.00 11.94 ? 302 ILE B CG1 1 
ATOM   5158 C CG2 . ILE B 1 302 ? 62.478 0.734   65.455  1.00 20.58 ? 302 ILE B CG2 1 
ATOM   5159 C CD1 . ILE B 1 302 ? 62.721 -1.186  67.794  1.00 10.32 ? 302 ILE B CD1 1 
ATOM   5160 N N   . PRO B 1 303 ? 60.278 3.673   65.096  1.00 20.07 ? 303 PRO B N   1 
ATOM   5161 C CA  . PRO B 1 303 ? 59.452 4.174   63.996  1.00 19.56 ? 303 PRO B CA  1 
ATOM   5162 C C   . PRO B 1 303 ? 59.444 3.274   62.761  1.00 20.72 ? 303 PRO B C   1 
ATOM   5163 O O   . PRO B 1 303 ? 60.431 2.596   62.488  1.00 21.69 ? 303 PRO B O   1 
ATOM   5164 C CB  . PRO B 1 303 ? 60.117 5.506   63.672  1.00 20.53 ? 303 PRO B CB  1 
ATOM   5165 C CG  . PRO B 1 303 ? 60.640 5.962   64.988  1.00 19.13 ? 303 PRO B CG  1 
ATOM   5166 C CD  . PRO B 1 303 ? 61.258 4.692   65.514  1.00 19.65 ? 303 PRO B CD  1 
ATOM   5167 N N   . ALA B 1 304 ? 58.353 3.315   61.991  1.00 17.65 ? 304 ALA B N   1 
ATOM   5168 C CA  . ALA B 1 304 ? 58.227 2.524   60.768  1.00 16.51 ? 304 ALA B CA  1 
ATOM   5169 C C   . ALA B 1 304 ? 59.388 2.870   59.830  1.00 18.72 ? 304 ALA B C   1 
ATOM   5170 O O   . ALA B 1 304 ? 59.704 4.047   59.651  1.00 20.42 ? 304 ALA B O   1 
ATOM   5171 C CB  . ALA B 1 304 ? 56.888 2.804   60.082  1.00 8.96  ? 304 ALA B CB  1 
ATOM   5172 N N   . ALA B 1 305 ? 60.033 1.829   59.288  1.00 20.04 ? 305 ALA B N   1 
ATOM   5173 C CA  . ALA B 1 305 ? 61.193 1.898   58.371  1.00 16.53 ? 305 ALA B CA  1 
ATOM   5174 C C   . ALA B 1 305 ? 62.558 2.368   58.923  1.00 15.05 ? 305 ALA B C   1 
ATOM   5175 O O   . ALA B 1 305 ? 63.472 2.584   58.148  1.00 19.57 ? 305 ALA B O   1 
ATOM   5176 C CB  . ALA B 1 305 ? 60.840 2.660   57.073  1.00 9.88  ? 305 ALA B CB  1 
ATOM   5177 N N   . TYR B 1 306 ? 62.715 2.535   60.237  1.00 19.69 ? 306 TYR B N   1 
ATOM   5178 C CA  . TYR B 1 306 ? 64.021 2.955   60.806  1.00 18.76 ? 306 TYR B CA  1 
ATOM   5179 C C   . TYR B 1 306 ? 64.795 1.702   61.166  1.00 16.17 ? 306 TYR B C   1 
ATOM   5180 O O   . TYR B 1 306 ? 64.271 0.844   61.851  1.00 17.49 ? 306 TYR B O   1 
ATOM   5181 C CB  . TYR B 1 306 ? 63.837 3.770   62.089  1.00 19.39 ? 306 TYR B CB  1 
ATOM   5182 C CG  . TYR B 1 306 ? 63.300 5.157   61.886  1.00 18.82 ? 306 TYR B CG  1 
ATOM   5183 C CD1 . TYR B 1 306 ? 62.384 5.442   60.872  1.00 19.30 ? 306 TYR B CD1 1 
ATOM   5184 C CD2 . TYR B 1 306 ? 63.695 6.193   62.718  1.00 20.99 ? 306 TYR B CD2 1 
ATOM   5185 C CE1 . TYR B 1 306 ? 61.882 6.737   60.698  1.00 14.74 ? 306 TYR B CE1 1 
ATOM   5186 C CE2 . TYR B 1 306 ? 63.195 7.483   62.557  1.00 22.05 ? 306 TYR B CE2 1 
ATOM   5187 C CZ  . TYR B 1 306 ? 62.291 7.748   61.547  1.00 17.79 ? 306 TYR B CZ  1 
ATOM   5188 O OH  . TYR B 1 306 ? 61.801 9.029   61.407  1.00 22.15 ? 306 TYR B OH  1 
ATOM   5189 N N   . PRO B 1 307 ? 66.060 1.598   60.750  1.00 18.87 ? 307 PRO B N   1 
ATOM   5190 C CA  . PRO B 1 307 ? 66.901 0.421   61.039  1.00 19.66 ? 307 PRO B CA  1 
ATOM   5191 C C   . PRO B 1 307 ? 67.316 0.308   62.507  1.00 20.35 ? 307 PRO B C   1 
ATOM   5192 O O   . PRO B 1 307 ? 67.703 1.284   63.145  1.00 22.56 ? 307 PRO B O   1 
ATOM   5193 C CB  . PRO B 1 307 ? 68.124 0.639   60.130  1.00 17.95 ? 307 PRO B CB  1 
ATOM   5194 C CG  . PRO B 1 307 ? 67.602 1.563   59.036  1.00 22.93 ? 307 PRO B CG  1 
ATOM   5195 C CD  . PRO B 1 307 ? 66.758 2.527   59.852  1.00 20.18 ? 307 PRO B CD  1 
ATOM   5196 N N   . VAL B 1 308 ? 67.334 -0.906  63.018  1.00 21.74 ? 308 VAL B N   1 
ATOM   5197 C CA  . VAL B 1 308 ? 67.680 -1.106  64.405  1.00 24.23 ? 308 VAL B CA  1 
ATOM   5198 C C   . VAL B 1 308 ? 68.472 -2.396  64.584  1.00 24.85 ? 308 VAL B C   1 
ATOM   5199 O O   . VAL B 1 308 ? 68.397 -3.299  63.755  1.00 28.87 ? 308 VAL B O   1 
ATOM   5200 C CB  . VAL B 1 308 ? 66.376 -1.121  65.279  1.00 22.20 ? 308 VAL B CB  1 
ATOM   5201 C CG1 . VAL B 1 308 ? 65.480 -2.322  64.904  1.00 19.29 ? 308 VAL B CG1 1 
ATOM   5202 C CG2 . VAL B 1 308 ? 66.716 -1.120  66.781  1.00 26.42 ? 308 VAL B CG2 1 
ATOM   5203 N N   . ALA B 1 309 ? 69.294 -2.440  65.620  1.00 24.52 ? 309 ALA B N   1 
ATOM   5204 C CA  . ALA B 1 309 ? 70.061 -3.631  65.948  1.00 25.60 ? 309 ALA B CA  1 
ATOM   5205 C C   . ALA B 1 309 ? 69.972 -3.675  67.469  1.00 27.17 ? 309 ALA B C   1 
ATOM   5206 O O   . ALA B 1 309 ? 69.967 -2.607  68.106  1.00 25.62 ? 309 ALA B O   1 
ATOM   5207 C CB  . ALA B 1 309 ? 71.508 -3.491  65.500  1.00 28.45 ? 309 ALA B CB  1 
ATOM   5208 N N   . ILE B 1 310 ? 69.835 -4.883  68.029  1.00 25.92 ? 310 ILE B N   1 
ATOM   5209 C CA  . ILE B 1 310 ? 69.722 -5.086  69.477  1.00 22.03 ? 310 ILE B CA  1 
ATOM   5210 C C   . ILE B 1 310 ? 70.622 -6.231  69.892  1.00 28.65 ? 310 ILE B C   1 
ATOM   5211 O O   . ILE B 1 310 ? 70.536 -7.311  69.312  1.00 28.31 ? 310 ILE B O   1 
ATOM   5212 C CB  . ILE B 1 310 ? 68.278 -5.477  69.901  1.00 19.65 ? 310 ILE B CB  1 
ATOM   5213 C CG1 . ILE B 1 310 ? 67.264 -4.584  69.206  1.00 14.47 ? 310 ILE B CG1 1 
ATOM   5214 C CG2 . ILE B 1 310 ? 68.090 -5.299  71.417  1.00 17.94 ? 310 ILE B CG2 1 
ATOM   5215 C CD1 . ILE B 1 310 ? 65.822 -4.855  69.548  1.00 6.64  ? 310 ILE B CD1 1 
ATOM   5216 N N   . LYS B 1 311 ? 71.502 -5.995  70.870  1.00 33.82 ? 311 LYS B N   1 
ATOM   5217 C CA  . LYS B 1 311 ? 72.400 -7.038  71.385  1.00 32.87 ? 311 LYS B CA  1 
ATOM   5218 C C   . LYS B 1 311 ? 72.151 -7.317  72.877  1.00 33.16 ? 311 LYS B C   1 
ATOM   5219 O O   . LYS B 1 311 ? 72.093 -6.398  73.713  1.00 22.49 ? 311 LYS B O   1 
ATOM   5220 C CB  . LYS B 1 311 ? 73.868 -6.676  71.190  1.00 40.04 ? 311 LYS B CB  1 
ATOM   5221 C CG  . LYS B 1 311 ? 74.799 -7.752  71.726  1.00 49.17 ? 311 LYS B CG  1 
ATOM   5222 C CD  . LYS B 1 311 ? 76.213 -7.238  71.918  1.00 58.79 ? 311 LYS B CD  1 
ATOM   5223 C CE  . LYS B 1 311 ? 77.013 -8.165  72.837  1.00 66.52 ? 311 LYS B CE  1 
ATOM   5224 N NZ  . LYS B 1 311 ? 77.187 -9.532  72.260  1.00 71.37 ? 311 LYS B NZ  1 
ATOM   5225 N N   . ALA B 1 312 ? 72.044 -8.599  73.198  1.00 31.51 ? 312 ALA B N   1 
ATOM   5226 C CA  . ALA B 1 312 ? 71.790 -9.021  74.555  1.00 31.45 ? 312 ALA B CA  1 
ATOM   5227 C C   . ALA B 1 312 ? 73.027 -8.833  75.393  1.00 31.87 ? 312 ALA B C   1 
ATOM   5228 O O   . ALA B 1 312 ? 74.073 -9.395  75.085  1.00 33.14 ? 312 ALA B O   1 
ATOM   5229 C CB  . ALA B 1 312 ? 71.352 -10.485 74.591  1.00 30.80 ? 312 ALA B CB  1 
ATOM   5230 N N   . THR B 1 313 ? 72.895 -8.000  76.423  1.00 35.09 ? 313 THR B N   1 
ATOM   5231 C CA  . THR B 1 313 ? 73.949 -7.710  77.388  1.00 33.82 ? 313 THR B CA  1 
ATOM   5232 C C   . THR B 1 313 ? 73.823 -8.714  78.538  1.00 31.79 ? 313 THR B C   1 
ATOM   5233 O O   . THR B 1 313 ? 74.716 -8.879  79.355  1.00 35.73 ? 313 THR B O   1 
ATOM   5234 C CB  . THR B 1 313 ? 73.833 -6.257  77.880  1.00 36.56 ? 313 THR B CB  1 
ATOM   5235 O OG1 . THR B 1 313 ? 74.435 -5.391  76.909  1.00 37.13 ? 313 THR B OG1 1 
ATOM   5236 C CG2 . THR B 1 313 ? 74.510 -6.064  79.212  1.00 40.91 ? 313 THR B CG2 1 
ATOM   5237 N N   . SER B 1 314 ? 72.698 -9.397  78.576  1.00 32.18 ? 314 SER B N   1 
ATOM   5238 C CA  . SER B 1 314 ? 72.444 -10.427 79.557  1.00 34.79 ? 314 SER B CA  1 
ATOM   5239 C C   . SER B 1 314 ? 71.357 -11.237 78.863  1.00 38.43 ? 314 SER B C   1 
ATOM   5240 O O   . SER B 1 314 ? 71.047 -10.969 77.695  1.00 42.51 ? 314 SER B O   1 
ATOM   5241 C CB  . SER B 1 314 ? 71.925 -9.807  80.859  1.00 30.92 ? 314 SER B CB  1 
ATOM   5242 O OG  . SER B 1 314 ? 70.546 -9.487  80.788  1.00 34.09 ? 314 SER B OG  1 
ATOM   5243 N N   . ASN B 1 315 ? 70.829 -12.273 79.503  1.00 39.46 ? 315 ASN B N   1 
ATOM   5244 C CA  . ASN B 1 315 ? 69.738 -12.988 78.856  1.00 39.81 ? 315 ASN B CA  1 
ATOM   5245 C C   . ASN B 1 315 ? 68.588 -12.014 79.004  1.00 40.58 ? 315 ASN B C   1 
ATOM   5246 O O   . ASN B 1 315 ? 68.415 -11.400 80.074  1.00 39.73 ? 315 ASN B O   1 
ATOM   5247 C CB  . ASN B 1 315 ? 69.437 -14.299 79.543  1.00 45.88 ? 315 ASN B CB  1 
ATOM   5248 C CG  . ASN B 1 315 ? 70.486 -15.316 79.275  1.00 50.96 ? 315 ASN B CG  1 
ATOM   5249 O OD1 . ASN B 1 315 ? 71.583 -15.222 79.808  1.00 59.88 ? 315 ASN B OD1 1 
ATOM   5250 N ND2 . ASN B 1 315 ? 70.196 -16.256 78.389  1.00 55.10 ? 315 ASN B ND2 1 
ATOM   5251 N N   . VAL B 1 316 ? 67.817 -11.850 77.939  1.00 37.18 ? 316 VAL B N   1 
ATOM   5252 C CA  . VAL B 1 316 ? 66.741 -10.883 77.955  1.00 33.41 ? 316 VAL B CA  1 
ATOM   5253 C C   . VAL B 1 316 ? 65.508 -11.292 77.153  1.00 35.67 ? 316 VAL B C   1 
ATOM   5254 O O   . VAL B 1 316 ? 65.598 -12.057 76.180  1.00 38.30 ? 316 VAL B O   1 
ATOM   5255 C CB  . VAL B 1 316 ? 67.312 -9.499  77.452  1.00 31.19 ? 316 VAL B CB  1 
ATOM   5256 C CG1 . VAL B 1 316 ? 68.064 -9.676  76.139  1.00 27.13 ? 316 VAL B CG1 1 
ATOM   5257 C CG2 . VAL B 1 316 ? 66.218 -8.453  77.296  1.00 28.77 ? 316 VAL B CG2 1 
ATOM   5258 N N   . ASN B 1 317 ? 64.338 -10.888 77.635  1.00 33.44 ? 317 ASN B N   1 
ATOM   5259 C CA  . ASN B 1 317 ? 63.128 -11.133 76.882  1.00 35.36 ? 317 ASN B CA  1 
ATOM   5260 C C   . ASN B 1 317 ? 62.225 -9.908  76.903  1.00 30.56 ? 317 ASN B C   1 
ATOM   5261 O O   . ASN B 1 317 ? 62.206 -9.153  77.870  1.00 22.92 ? 317 ASN B O   1 
ATOM   5262 C CB  . ASN B 1 317 ? 62.432 -12.437 77.258  1.00 45.22 ? 317 ASN B CB  1 
ATOM   5263 C CG  . ASN B 1 317 ? 62.087 -12.521 78.702  1.00 53.87 ? 317 ASN B CG  1 
ATOM   5264 O OD1 . ASN B 1 317 ? 61.687 -11.532 79.322  1.00 63.80 ? 317 ASN B OD1 1 
ATOM   5265 N ND2 . ASN B 1 317 ? 62.215 -13.721 79.261  1.00 56.95 ? 317 ASN B ND2 1 
ATOM   5266 N N   . PHE B 1 318 ? 61.603 -9.642  75.758  1.00 31.78 ? 318 PHE B N   1 
ATOM   5267 C CA  . PHE B 1 318 ? 60.742 -8.479  75.579  1.00 31.74 ? 318 PHE B CA  1 
ATOM   5268 C C   . PHE B 1 318 ? 59.380 -8.893  75.080  1.00 32.30 ? 318 PHE B C   1 
ATOM   5269 O O   . PHE B 1 318 ? 59.180 -10.018 74.618  1.00 28.10 ? 318 PHE B O   1 
ATOM   5270 C CB  . PHE B 1 318 ? 61.269 -7.538  74.465  1.00 33.10 ? 318 PHE B CB  1 
ATOM   5271 C CG  . PHE B 1 318 ? 62.762 -7.297  74.466  1.00 32.46 ? 318 PHE B CG  1 
ATOM   5272 C CD1 . PHE B 1 318 ? 63.642 -8.257  73.961  1.00 30.06 ? 318 PHE B CD1 1 
ATOM   5273 C CD2 . PHE B 1 318 ? 63.277 -6.080  74.915  1.00 29.02 ? 318 PHE B CD2 1 
ATOM   5274 C CE1 . PHE B 1 318 ? 65.011 -8.010  73.901  1.00 26.17 ? 318 PHE B CE1 1 
ATOM   5275 C CE2 . PHE B 1 318 ? 64.643 -5.818  74.862  1.00 27.31 ? 318 PHE B CE2 1 
ATOM   5276 C CZ  . PHE B 1 318 ? 65.517 -6.789  74.351  1.00 30.27 ? 318 PHE B CZ  1 
ATOM   5277 N N   . THR B 1 319 ? 58.476 -7.922  75.106  1.00 32.85 ? 319 THR B N   1 
ATOM   5278 C CA  . THR B 1 319 ? 57.131 -8.053  74.571  1.00 32.81 ? 319 THR B CA  1 
ATOM   5279 C C   . THR B 1 319 ? 56.984 -6.754  73.803  1.00 34.40 ? 319 THR B C   1 
ATOM   5280 O O   . THR B 1 319 ? 57.427 -5.703  74.286  1.00 33.14 ? 319 THR B O   1 
ATOM   5281 C CB  . THR B 1 319 ? 56.067 -8.057  75.630  1.00 32.42 ? 319 THR B CB  1 
ATOM   5282 O OG1 . THR B 1 319 ? 56.193 -9.247  76.421  1.00 37.26 ? 319 THR B OG1 1 
ATOM   5283 C CG2 . THR B 1 319 ? 54.687 -7.985  74.966  1.00 29.54 ? 319 THR B CG2 1 
ATOM   5284 N N   . GLY B 1 320 ? 56.416 -6.825  72.601  1.00 33.70 ? 320 GLY B N   1 
ATOM   5285 C CA  . GLY B 1 320 ? 56.245 -5.629  71.802  1.00 23.24 ? 320 GLY B CA  1 
ATOM   5286 C C   . GLY B 1 320 ? 54.892 -5.587  71.131  1.00 21.53 ? 320 GLY B C   1 
ATOM   5287 O O   . GLY B 1 320 ? 54.243 -6.616  70.922  1.00 14.06 ? 320 GLY B O   1 
ATOM   5288 N N   . PHE B 1 321 ? 54.412 -4.376  70.895  1.00 17.51 ? 321 PHE B N   1 
ATOM   5289 C CA  . PHE B 1 321 ? 53.153 -4.181  70.200  1.00 15.94 ? 321 PHE B CA  1 
ATOM   5290 C C   . PHE B 1 321 ? 53.545 -3.401  68.944  1.00 17.09 ? 321 PHE B C   1 
ATOM   5291 O O   . PHE B 1 321 ? 54.334 -2.448  69.004  1.00 18.84 ? 321 PHE B O   1 
ATOM   5292 C CB  . PHE B 1 321 ? 52.170 -3.360  71.024  1.00 4.87  ? 321 PHE B CB  1 
ATOM   5293 C CG  . PHE B 1 321 ? 51.835 -3.959  72.349  1.00 10.93 ? 321 PHE B CG  1 
ATOM   5294 C CD1 . PHE B 1 321 ? 52.609 -3.657  73.469  1.00 14.42 ? 321 PHE B CD1 1 
ATOM   5295 C CD2 . PHE B 1 321 ? 50.751 -4.830  72.478  1.00 8.53  ? 321 PHE B CD2 1 
ATOM   5296 C CE1 . PHE B 1 321 ? 52.310 -4.218  74.707  1.00 18.71 ? 321 PHE B CE1 1 
ATOM   5297 C CE2 . PHE B 1 321 ? 50.436 -5.398  73.697  1.00 15.60 ? 321 PHE B CE2 1 
ATOM   5298 C CZ  . PHE B 1 321 ? 51.225 -5.090  74.827  1.00 14.52 ? 321 PHE B CZ  1 
ATOM   5299 N N   . GLY B 1 322 ? 53.055 -3.841  67.802  1.00 19.46 ? 322 GLY B N   1 
ATOM   5300 C CA  . GLY B 1 322 ? 53.382 -3.148  66.573  1.00 16.90 ? 322 GLY B CA  1 
ATOM   5301 C C   . GLY B 1 322 ? 52.080 -2.586  66.077  1.00 20.32 ? 322 GLY B C   1 
ATOM   5302 O O   . GLY B 1 322 ? 51.096 -3.344  65.993  1.00 17.99 ? 322 GLY B O   1 
ATOM   5303 N N   . ILE B 1 323 ? 52.012 -1.269  65.871  1.00 14.26 ? 323 ILE B N   1 
ATOM   5304 C CA  . ILE B 1 323 ? 50.789 -0.701  65.359  1.00 18.94 ? 323 ILE B CA  1 
ATOM   5305 C C   . ILE B 1 323 ? 51.026 -0.462  63.852  1.00 23.33 ? 323 ILE B C   1 
ATOM   5306 O O   . ILE B 1 323 ? 52.163 -0.183  63.442  1.00 25.98 ? 323 ILE B O   1 
ATOM   5307 C CB  . ILE B 1 323 ? 50.327 0.565   66.161  1.00 23.07 ? 323 ILE B CB  1 
ATOM   5308 C CG1 . ILE B 1 323 ? 50.779 1.849   65.489  1.00 28.08 ? 323 ILE B CG1 1 
ATOM   5309 C CG2 . ILE B 1 323 ? 50.883 0.547   67.585  1.00 19.35 ? 323 ILE B CG2 1 
ATOM   5310 C CD1 . ILE B 1 323 ? 50.239 3.083   66.167  1.00 34.53 ? 323 ILE B CD1 1 
ATOM   5311 N N   . ASN B 1 324 ? 49.982 -0.680  63.039  1.00 24.91 ? 324 ASN B N   1 
ATOM   5312 C CA  . ASN B 1 324 ? 50.022 -0.537  61.560  1.00 25.55 ? 324 ASN B CA  1 
ATOM   5313 C C   . ASN B 1 324 ? 50.554 -1.850  61.021  1.00 23.78 ? 324 ASN B C   1 
ATOM   5314 O O   . ASN B 1 324 ? 51.173 -1.907  59.965  1.00 26.37 ? 324 ASN B O   1 
ATOM   5315 C CB  . ASN B 1 324 ? 50.966 0.597   61.138  1.00 26.81 ? 324 ASN B CB  1 
ATOM   5316 C CG  . ASN B 1 324 ? 50.464 1.375   59.945  1.00 30.70 ? 324 ASN B CG  1 
ATOM   5317 O OD1 . ASN B 1 324 ? 49.253 1.481   59.713  1.00 29.87 ? 324 ASN B OD1 1 
ATOM   5318 N ND2 . ASN B 1 324 ? 51.391 1.961   59.196  1.00 30.22 ? 324 ASN B ND2 1 
ATOM   5319 N N   . ALA B 1 325 ? 50.222 -2.913  61.734  1.00 21.66 ? 325 ALA B N   1 
ATOM   5320 C CA  . ALA B 1 325 ? 50.704 -4.247  61.443  1.00 27.15 ? 325 ALA B CA  1 
ATOM   5321 C C   . ALA B 1 325 ? 50.226 -4.984  60.213  1.00 32.93 ? 325 ALA B C   1 
ATOM   5322 O O   . ALA B 1 325 ? 50.874 -5.945  59.795  1.00 35.67 ? 325 ALA B O   1 
ATOM   5323 C CB  . ALA B 1 325 ? 50.487 -5.122  62.657  1.00 33.21 ? 325 ALA B CB  1 
ATOM   5324 N N   . ASN B 1 326 ? 49.102 -4.569  59.639  1.00 39.11 ? 326 ASN B N   1 
ATOM   5325 C CA  . ASN B 1 326 ? 48.551 -5.273  58.487  1.00 42.55 ? 326 ASN B CA  1 
ATOM   5326 C C   . ASN B 1 326 ? 49.394 -5.064  57.215  1.00 44.43 ? 326 ASN B C   1 
ATOM   5327 O O   . ASN B 1 326 ? 49.516 -3.949  56.721  1.00 44.31 ? 326 ASN B O   1 
ATOM   5328 C CB  . ASN B 1 326 ? 47.064 -4.902  58.313  1.00 46.01 ? 326 ASN B CB  1 
ATOM   5329 C CG  . ASN B 1 326 ? 46.185 -5.295  59.552  1.00 51.09 ? 326 ASN B CG  1 
ATOM   5330 O OD1 . ASN B 1 326 ? 46.568 -6.134  60.380  1.00 50.38 ? 326 ASN B OD1 1 
ATOM   5331 N ND2 . ASN B 1 326 ? 45.007 -4.680  59.663  1.00 52.64 ? 326 ASN B ND2 1 
ATOM   5332 N N   . ASN B 1 327 ? 50.041 -6.135  56.743  1.00 43.70 ? 327 ASN B N   1 
ATOM   5333 C CA  . ASN B 1 327 ? 50.908 -6.097  55.546  1.00 42.70 ? 327 ASN B CA  1 
ATOM   5334 C C   . ASN B 1 327 ? 52.299 -5.499  55.790  1.00 38.68 ? 327 ASN B C   1 
ATOM   5335 O O   . ASN B 1 327 ? 52.812 -4.748  54.965  1.00 37.45 ? 327 ASN B O   1 
ATOM   5336 C CB  . ASN B 1 327 ? 50.244 -5.333  54.401  1.00 50.39 ? 327 ASN B CB  1 
ATOM   5337 C CG  . ASN B 1 327 ? 49.063 -6.058  53.836  1.00 61.04 ? 327 ASN B CG  1 
ATOM   5338 O OD1 . ASN B 1 327 ? 48.994 -7.289  53.891  1.00 69.28 ? 327 ASN B OD1 1 
ATOM   5339 N ND2 . ASN B 1 327 ? 48.108 -5.307  53.303  1.00 64.35 ? 327 ASN B ND2 1 
ATOM   5340 N N   . ASN B 1 328 ? 52.902 -5.848  56.918  1.00 33.47 ? 328 ASN B N   1 
ATOM   5341 C CA  . ASN B 1 328 ? 54.220 -5.356  57.297  1.00 30.72 ? 328 ASN B CA  1 
ATOM   5342 C C   . ASN B 1 328 ? 55.199 -6.409  56.851  1.00 31.14 ? 328 ASN B C   1 
ATOM   5343 O O   . ASN B 1 328 ? 54.840 -7.590  56.809  1.00 31.34 ? 328 ASN B O   1 
ATOM   5344 C CB  . ASN B 1 328 ? 54.283 -5.202  58.819  1.00 28.29 ? 328 ASN B CB  1 
ATOM   5345 C CG  . ASN B 1 328 ? 55.665 -4.891  59.321  1.00 27.42 ? 328 ASN B CG  1 
ATOM   5346 O OD1 . ASN B 1 328 ? 56.187 -3.799  59.099  1.00 29.96 ? 328 ASN B OD1 1 
ATOM   5347 N ND2 . ASN B 1 328 ? 56.261 -5.843  60.035  1.00 23.71 ? 328 ASN B ND2 1 
ATOM   5348 N N   . ASN B 1 329 ? 56.422 -5.985  56.520  1.00 31.88 ? 329 ASN B N   1 
ATOM   5349 C CA  . ASN B 1 329 ? 57.487 -6.892  56.065  1.00 29.86 ? 329 ASN B CA  1 
ATOM   5350 C C   . ASN B 1 329 ? 58.692 -6.672  56.924  1.00 27.27 ? 329 ASN B C   1 
ATOM   5351 O O   . ASN B 1 329 ? 59.047 -5.532  57.210  1.00 30.04 ? 329 ASN B O   1 
ATOM   5352 C CB  . ASN B 1 329 ? 57.934 -6.590  54.637  1.00 32.92 ? 329 ASN B CB  1 
ATOM   5353 C CG  . ASN B 1 329 ? 56.919 -6.965  53.623  1.00 38.60 ? 329 ASN B CG  1 
ATOM   5354 O OD1 . ASN B 1 329 ? 56.148 -7.908  53.811  1.00 42.65 ? 329 ASN B OD1 1 
ATOM   5355 N ND2 . ASN B 1 329 ? 56.891 -6.219  52.526  1.00 42.26 ? 329 ASN B ND2 1 
ATOM   5356 N N   . ARG B 1 330 ? 59.363 -7.755  57.269  1.00 23.57 ? 330 ARG B N   1 
ATOM   5357 C CA  . ARG B 1 330 ? 60.544 -7.682  58.085  1.00 26.76 ? 330 ARG B CA  1 
ATOM   5358 C C   . ARG B 1 330 ? 61.711 -7.722  57.093  1.00 27.70 ? 330 ARG B C   1 
ATOM   5359 O O   . ARG B 1 330 ? 61.854 -8.686  56.336  1.00 30.51 ? 330 ARG B O   1 
ATOM   5360 C CB  . ARG B 1 330 ? 60.542 -8.876  59.023  1.00 30.10 ? 330 ARG B CB  1 
ATOM   5361 C CG  . ARG B 1 330 ? 61.358 -8.701  60.270  1.00 48.03 ? 330 ARG B CG  1 
ATOM   5362 C CD  . ARG B 1 330 ? 61.120 -9.853  61.244  1.00 55.26 ? 330 ARG B CD  1 
ATOM   5363 N NE  . ARG B 1 330 ? 59.710 -10.027 61.604  1.00 55.12 ? 330 ARG B NE  1 
ATOM   5364 C CZ  . ARG B 1 330 ? 58.995 -11.111 61.317  1.00 58.17 ? 330 ARG B CZ  1 
ATOM   5365 N NH1 . ARG B 1 330 ? 59.539 -12.123 60.657  1.00 60.36 ? 330 ARG B NH1 1 
ATOM   5366 N NH2 . ARG B 1 330 ? 57.740 -11.205 61.722  1.00 58.55 ? 330 ARG B NH2 1 
ATOM   5367 N N   . ASN B 1 331 ? 62.485 -6.636  57.032  1.00 26.75 ? 331 ASN B N   1 
ATOM   5368 C CA  . ASN B 1 331 ? 63.620 -6.537  56.106  1.00 25.63 ? 331 ASN B CA  1 
ATOM   5369 C C   . ASN B 1 331 ? 64.934 -6.589  56.854  1.00 28.47 ? 331 ASN B C   1 
ATOM   5370 O O   . ASN B 1 331 ? 65.264 -5.651  57.589  1.00 27.67 ? 331 ASN B O   1 
ATOM   5371 C CB  . ASN B 1 331 ? 63.579 -5.235  55.296  1.00 23.53 ? 331 ASN B CB  1 
ATOM   5372 C CG  . ASN B 1 331 ? 62.413 -5.182  54.331  1.00 23.19 ? 331 ASN B CG  1 
ATOM   5373 O OD1 . ASN B 1 331 ? 62.501 -5.665  53.204  1.00 27.60 ? 331 ASN B OD1 1 
ATOM   5374 N ND2 . ASN B 1 331 ? 61.308 -4.595  54.768  1.00 26.40 ? 331 ASN B ND2 1 
ATOM   5375 N N   . LEU B 1 332 ? 65.691 -7.671  56.635  1.00 28.45 ? 332 LEU B N   1 
ATOM   5376 C CA  . LEU B 1 332 ? 66.988 -7.889  57.270  1.00 23.18 ? 332 LEU B CA  1 
ATOM   5377 C C   . LEU B 1 332 ? 68.180 -7.447  56.429  1.00 22.94 ? 332 LEU B C   1 
ATOM   5378 O O   . LEU B 1 332 ? 68.191 -7.596  55.200  1.00 24.11 ? 332 LEU B O   1 
ATOM   5379 C CB  . LEU B 1 332 ? 67.128 -9.346  57.676  1.00 21.77 ? 332 LEU B CB  1 
ATOM   5380 C CG  . LEU B 1 332 ? 66.369 -9.697  58.962  1.00 23.83 ? 332 LEU B CG  1 
ATOM   5381 C CD1 . LEU B 1 332 ? 64.846 -9.582  58.818  1.00 21.69 ? 332 LEU B CD1 1 
ATOM   5382 C CD2 . LEU B 1 332 ? 66.770 -11.072 59.399  1.00 28.73 ? 332 LEU B CD2 1 
ATOM   5383 N N   . LEU B 1 333 ? 69.204 -6.941  57.108  1.00 20.11 ? 333 LEU B N   1 
ATOM   5384 C CA  . LEU B 1 333 ? 70.382 -6.433  56.437  1.00 18.84 ? 333 LEU B CA  1 
ATOM   5385 C C   . LEU B 1 333 ? 71.656 -7.248  56.623  1.00 21.10 ? 333 LEU B C   1 
ATOM   5386 O O   . LEU B 1 333 ? 72.764 -6.746  56.403  1.00 21.15 ? 333 LEU B O   1 
ATOM   5387 C CB  . LEU B 1 333 ? 70.606 -4.981  56.858  1.00 20.42 ? 333 LEU B CB  1 
ATOM   5388 C CG  . LEU B 1 333 ? 69.492 -3.998  56.476  1.00 22.02 ? 333 LEU B CG  1 
ATOM   5389 C CD1 . LEU B 1 333 ? 69.405 -2.869  57.501  1.00 22.98 ? 333 LEU B CD1 1 
ATOM   5390 C CD2 . LEU B 1 333 ? 69.724 -3.454  55.056  1.00 23.52 ? 333 LEU B CD2 1 
ATOM   5391 N N   . ALA B 1 334 ? 71.493 -8.504  57.025  1.00 20.06 ? 334 ALA B N   1 
ATOM   5392 C CA  . ALA B 1 334 ? 72.611 -9.421  57.228  1.00 18.59 ? 334 ALA B CA  1 
ATOM   5393 C C   . ALA B 1 334 ? 71.972 -10.784 57.400  1.00 19.72 ? 334 ALA B C   1 
ATOM   5394 O O   . ALA B 1 334 ? 70.771 -10.860 57.652  1.00 22.48 ? 334 ALA B O   1 
ATOM   5395 C CB  . ALA B 1 334 ? 73.405 -9.038  58.476  1.00 21.91 ? 334 ALA B CB  1 
ATOM   5396 N N   . GLY B 1 335 ? 72.748 -11.855 57.243  1.00 25.16 ? 335 GLY B N   1 
ATOM   5397 C CA  . GLY B 1 335 ? 72.187 -13.193 57.393  1.00 26.11 ? 335 GLY B CA  1 
ATOM   5398 C C   . GLY B 1 335 ? 71.640 -13.806 56.106  1.00 32.68 ? 335 GLY B C   1 
ATOM   5399 O O   . GLY B 1 335 ? 71.516 -13.125 55.059  1.00 32.96 ? 335 GLY B O   1 
ATOM   5400 N N   . LYS B 1 336 ? 71.267 -15.085 56.195  1.00 32.31 ? 336 LYS B N   1 
ATOM   5401 C CA  . LYS B 1 336 ? 70.760 -15.844 55.053  1.00 29.90 ? 336 LYS B CA  1 
ATOM   5402 C C   . LYS B 1 336 ? 69.267 -15.713 54.814  1.00 28.45 ? 336 LYS B C   1 
ATOM   5403 O O   . LYS B 1 336 ? 68.790 -15.895 53.683  1.00 27.30 ? 336 LYS B O   1 
ATOM   5404 C CB  . LYS B 1 336 ? 71.172 -17.315 55.196  1.00 32.60 ? 336 LYS B CB  1 
ATOM   5405 C CG  . LYS B 1 336 ? 70.209 -18.336 54.575  1.00 45.93 ? 336 LYS B CG  1 
ATOM   5406 C CD  . LYS B 1 336 ? 69.870 -19.467 55.580  1.00 53.46 ? 336 LYS B CD  1 
ATOM   5407 C CE  . LYS B 1 336 ? 68.827 -20.462 55.039  1.00 52.26 ? 336 LYS B CE  1 
ATOM   5408 N NZ  . LYS B 1 336 ? 67.473 -19.863 54.826  1.00 50.59 ? 336 LYS B NZ  1 
ATOM   5409 N N   . THR B 1 337 ? 68.524 -15.387 55.863  1.00 27.90 ? 337 THR B N   1 
ATOM   5410 C CA  . THR B 1 337 ? 67.077 -15.258 55.732  1.00 29.36 ? 337 THR B CA  1 
ATOM   5411 C C   . THR B 1 337 ? 66.539 -13.833 55.787  1.00 28.39 ? 337 THR B C   1 
ATOM   5412 O O   . THR B 1 337 ? 66.872 -13.066 56.696  1.00 30.69 ? 337 THR B O   1 
ATOM   5413 C CB  . THR B 1 337 ? 66.362 -16.113 56.771  1.00 29.78 ? 337 THR B CB  1 
ATOM   5414 O OG1 . THR B 1 337 ? 66.770 -17.481 56.628  1.00 38.01 ? 337 THR B OG1 1 
ATOM   5415 C CG2 . THR B 1 337 ? 64.865 -16.028 56.595  1.00 33.15 ? 337 THR B CG2 1 
ATOM   5416 N N   . ASP B 1 338 ? 65.719 -13.501 54.782  1.00 27.85 ? 338 ASP B N   1 
ATOM   5417 C CA  . ASP B 1 338 ? 65.058 -12.199 54.627  1.00 22.73 ? 338 ASP B CA  1 
ATOM   5418 C C   . ASP B 1 338 ? 65.974 -11.019 54.417  1.00 21.96 ? 338 ASP B C   1 
ATOM   5419 O O   . ASP B 1 338 ? 65.654 -9.912  54.837  1.00 21.65 ? 338 ASP B O   1 
ATOM   5420 C CB  . ASP B 1 338 ? 64.139 -11.925 55.812  1.00 26.53 ? 338 ASP B CB  1 
ATOM   5421 C CG  . ASP B 1 338 ? 62.934 -12.823 55.814  1.00 26.58 ? 338 ASP B CG  1 
ATOM   5422 O OD1 . ASP B 1 338 ? 62.529 -13.215 54.713  1.00 27.48 ? 338 ASP B OD1 1 
ATOM   5423 O OD2 . ASP B 1 338 ? 62.401 -13.142 56.897  1.00 31.91 ? 338 ASP B OD2 1 
ATOM   5424 N N   . ASN B 1 339 ? 67.094 -11.263 53.736  1.00 25.57 ? 339 ASN B N   1 
ATOM   5425 C CA  . ASN B 1 339 ? 68.100 -10.247 53.448  1.00 24.32 ? 339 ASN B CA  1 
ATOM   5426 C C   . ASN B 1 339 ? 67.794 -9.495  52.152  1.00 22.11 ? 339 ASN B C   1 
ATOM   5427 O O   . ASN B 1 339 ? 67.946 -10.031 51.058  1.00 17.14 ? 339 ASN B O   1 
ATOM   5428 C CB  . ASN B 1 339 ? 69.497 -10.888 53.392  1.00 24.81 ? 339 ASN B CB  1 
ATOM   5429 C CG  . ASN B 1 339 ? 70.607 -9.867  53.223  1.00 19.67 ? 339 ASN B CG  1 
ATOM   5430 O OD1 . ASN B 1 339 ? 70.461 -8.902  52.472  1.00 31.88 ? 339 ASN B OD1 1 
ATOM   5431 N ND2 . ASN B 1 339 ? 71.735 -10.088 53.895  1.00 15.00 ? 339 ASN B ND2 1 
ATOM   5432 N N   . VAL B 1 340 ? 67.402 -8.232  52.291  1.00 21.10 ? 340 VAL B N   1 
ATOM   5433 C CA  . VAL B 1 340 ? 67.072 -7.397  51.140  1.00 19.32 ? 340 VAL B CA  1 
ATOM   5434 C C   . VAL B 1 340 ? 68.223 -7.045  50.227  1.00 19.77 ? 340 VAL B C   1 
ATOM   5435 O O   . VAL B 1 340 ? 67.997 -6.795  49.053  1.00 21.48 ? 340 VAL B O   1 
ATOM   5436 C CB  . VAL B 1 340 ? 66.415 -6.069  51.533  1.00 18.36 ? 340 VAL B CB  1 
ATOM   5437 C CG1 . VAL B 1 340 ? 64.944 -6.251  51.642  1.00 16.70 ? 340 VAL B CG1 1 
ATOM   5438 C CG2 . VAL B 1 340 ? 67.023 -5.530  52.822  1.00 15.85 ? 340 VAL B CG2 1 
ATOM   5439 N N   . ILE B 1 341 ? 69.437 -6.959  50.768  1.00 21.72 ? 341 ILE B N   1 
ATOM   5440 C CA  . ILE B 1 341 ? 70.609 -6.621  49.964  1.00 23.10 ? 341 ILE B CA  1 
ATOM   5441 C C   . ILE B 1 341 ? 70.926 -7.744  48.989  1.00 21.22 ? 341 ILE B C   1 
ATOM   5442 O O   . ILE B 1 341 ? 71.307 -7.480  47.849  1.00 20.27 ? 341 ILE B O   1 
ATOM   5443 C CB  . ILE B 1 341 ? 71.828 -6.298  50.823  1.00 24.62 ? 341 ILE B CB  1 
ATOM   5444 C CG1 . ILE B 1 341 ? 71.494 -5.164  51.793  1.00 24.96 ? 341 ILE B CG1 1 
ATOM   5445 C CG2 . ILE B 1 341 ? 72.956 -5.830  49.942  1.00 31.41 ? 341 ILE B CG2 1 
ATOM   5446 C CD1 . ILE B 1 341 ? 72.677 -4.667  52.576  1.00 27.29 ? 341 ILE B CD1 1 
ATOM   5447 N N   . SER B 1 342 ? 70.770 -8.990  49.437  1.00 21.74 ? 342 SER B N   1 
ATOM   5448 C CA  . SER B 1 342 ? 70.973 -10.152 48.564  1.00 25.20 ? 342 SER B CA  1 
ATOM   5449 C C   . SER B 1 342 ? 69.880 -10.079 47.509  1.00 26.51 ? 342 SER B C   1 
ATOM   5450 O O   . SER B 1 342 ? 70.134 -10.256 46.309  1.00 25.56 ? 342 SER B O   1 
ATOM   5451 C CB  . SER B 1 342 ? 70.812 -11.463 49.323  1.00 21.74 ? 342 SER B CB  1 
ATOM   5452 O OG  . SER B 1 342 ? 71.855 -11.638 50.263  1.00 31.87 ? 342 SER B OG  1 
ATOM   5453 N N   . SER B 1 343 ? 68.666 -9.771  47.975  1.00 28.19 ? 343 SER B N   1 
ATOM   5454 C CA  . SER B 1 343 ? 67.518 -9.651  47.095  1.00 21.27 ? 343 SER B CA  1 
ATOM   5455 C C   . SER B 1 343 ? 67.782 -8.639  45.995  1.00 23.69 ? 343 SER B C   1 
ATOM   5456 O O   . SER B 1 343 ? 67.471 -8.916  44.842  1.00 21.31 ? 343 SER B O   1 
ATOM   5457 C CB  . SER B 1 343 ? 66.266 -9.289  47.866  1.00 17.73 ? 343 SER B CB  1 
ATOM   5458 O OG  . SER B 1 343 ? 65.135 -9.505  47.046  1.00 23.24 ? 343 SER B OG  1 
ATOM   5459 N N   . ILE B 1 344 ? 68.366 -7.483  46.335  1.00 23.95 ? 344 ILE B N   1 
ATOM   5460 C CA  . ILE B 1 344 ? 68.688 -6.480  45.311  1.00 23.29 ? 344 ILE B CA  1 
ATOM   5461 C C   . ILE B 1 344 ? 69.664 -7.147  44.340  1.00 22.33 ? 344 ILE B C   1 
ATOM   5462 O O   . ILE B 1 344 ? 69.444 -7.142  43.128  1.00 25.45 ? 344 ILE B O   1 
ATOM   5463 C CB  . ILE B 1 344 ? 69.382 -5.172  45.867  1.00 20.37 ? 344 ILE B CB  1 
ATOM   5464 C CG1 . ILE B 1 344 ? 68.424 -4.349  46.724  1.00 11.43 ? 344 ILE B CG1 1 
ATOM   5465 C CG2 . ILE B 1 344 ? 69.856 -4.271  44.684  1.00 8.52  ? 344 ILE B CG2 1 
ATOM   5466 C CD1 . ILE B 1 344 ? 69.118 -3.263  47.517  1.00 17.90 ? 344 ILE B CD1 1 
ATOM   5467 N N   . GLY B 1 345 ? 70.717 -7.744  44.889  1.00 21.23 ? 345 GLY B N   1 
ATOM   5468 C CA  . GLY B 1 345 ? 71.708 -8.413  44.073  1.00 20.27 ? 345 GLY B CA  1 
ATOM   5469 C C   . GLY B 1 345 ? 71.119 -9.460  43.142  1.00 23.73 ? 345 GLY B C   1 
ATOM   5470 O O   . GLY B 1 345 ? 71.711 -9.764  42.115  1.00 25.69 ? 345 GLY B O   1 
ATOM   5471 N N   . ARG B 1 346 ? 69.947 -9.996  43.470  1.00 26.39 ? 346 ARG B N   1 
ATOM   5472 C CA  . ARG B 1 346 ? 69.326 -11.021 42.631  1.00 23.34 ? 346 ARG B CA  1 
ATOM   5473 C C   . ARG B 1 346 ? 68.332 -10.542 41.561  1.00 24.31 ? 346 ARG B C   1 
ATOM   5474 O O   . ARG B 1 346 ? 67.834 -11.342 40.751  1.00 25.59 ? 346 ARG B O   1 
ATOM   5475 C CB  . ARG B 1 346 ? 68.751 -12.141 43.508  1.00 23.64 ? 346 ARG B CB  1 
ATOM   5476 C CG  . ARG B 1 346 ? 69.848 -13.060 44.088  1.00 16.32 ? 346 ARG B CG  1 
ATOM   5477 C CD  . ARG B 1 346 ? 69.332 -13.931 45.209  1.00 27.52 ? 346 ARG B CD  1 
ATOM   5478 N NE  . ARG B 1 346 ? 68.247 -14.819 44.790  1.00 40.48 ? 346 ARG B NE  1 
ATOM   5479 C CZ  . ARG B 1 346 ? 68.407 -16.091 44.409  1.00 43.67 ? 346 ARG B CZ  1 
ATOM   5480 N NH1 . ARG B 1 346 ? 69.616 -16.643 44.382  1.00 45.26 ? 346 ARG B NH1 1 
ATOM   5481 N NH2 . ARG B 1 346 ? 67.354 -16.821 44.058  1.00 37.30 ? 346 ARG B NH2 1 
ATOM   5482 N N   . ALA B 1 347 ? 68.105 -9.230  41.506  1.00 23.94 ? 347 ALA B N   1 
ATOM   5483 C CA  . ALA B 1 347 ? 67.195 -8.619  40.522  1.00 18.19 ? 347 ALA B CA  1 
ATOM   5484 C C   . ALA B 1 347 ? 67.756 -8.851  39.114  1.00 19.64 ? 347 ALA B C   1 
ATOM   5485 O O   . ALA B 1 347 ? 68.893 -9.300  38.982  1.00 16.09 ? 347 ALA B O   1 
ATOM   5486 C CB  . ALA B 1 347 ? 67.068 -7.113  40.810  1.00 20.34 ? 347 ALA B CB  1 
ATOM   5487 N N   . LEU B 1 348 ? 67.026 -8.463  38.067  1.00 25.06 ? 348 LEU B N   1 
ATOM   5488 C CA  . LEU B 1 348 ? 67.519 -8.672  36.690  1.00 27.96 ? 348 LEU B CA  1 
ATOM   5489 C C   . LEU B 1 348 ? 68.920 -8.146  36.396  1.00 33.03 ? 348 LEU B C   1 
ATOM   5490 O O   . LEU B 1 348 ? 69.829 -8.943  36.099  1.00 41.28 ? 348 LEU B O   1 
ATOM   5491 C CB  . LEU B 1 348 ? 66.507 -8.250  35.609  1.00 22.14 ? 348 LEU B CB  1 
ATOM   5492 C CG  . LEU B 1 348 ? 65.434 -9.343  35.397  1.00 27.22 ? 348 LEU B CG  1 
ATOM   5493 C CD1 . LEU B 1 348 ? 64.271 -8.834  34.612  1.00 25.33 ? 348 LEU B CD1 1 
ATOM   5494 C CD2 . LEU B 1 348 ? 66.023 -10.606 34.755  1.00 18.75 ? 348 LEU B CD2 1 
ATOM   5495 N N   . ASP B 1 349 ? 69.151 -6.844  36.450  1.00 33.54 ? 349 ASP B N   1 
ATOM   5496 C CA  . ASP B 1 349 ? 70.539 -6.413  36.206  1.00 36.94 ? 349 ASP B CA  1 
ATOM   5497 C C   . ASP B 1 349 ? 71.183 -5.986  37.558  1.00 35.06 ? 349 ASP B C   1 
ATOM   5498 O O   . ASP B 1 349 ? 72.145 -5.224  37.613  1.00 33.02 ? 349 ASP B O   1 
ATOM   5499 C CB  . ASP B 1 349 ? 70.605 -5.336  35.085  1.00 39.44 ? 349 ASP B CB  1 
ATOM   5500 C CG  . ASP B 1 349 ? 70.544 -5.952  33.633  1.00 47.83 ? 349 ASP B CG  1 
ATOM   5501 O OD1 . ASP B 1 349 ? 71.584 -6.452  33.153  1.00 50.50 ? 349 ASP B OD1 1 
ATOM   5502 O OD2 . ASP B 1 349 ? 69.487 -5.925  32.951  1.00 39.26 ? 349 ASP B OD2 1 
ATOM   5503 N N   . GLY B 1 350 ? 70.719 -6.644  38.622  1.00 36.67 ? 350 GLY B N   1 
ATOM   5504 C CA  . GLY B 1 350 ? 71.120 -6.383  40.003  1.00 36.45 ? 350 GLY B CA  1 
ATOM   5505 C C   . GLY B 1 350 ? 72.536 -6.147  40.505  1.00 36.45 ? 350 GLY B C   1 
ATOM   5506 O O   . GLY B 1 350 ? 72.774 -5.230  41.301  1.00 30.85 ? 350 GLY B O   1 
ATOM   5507 N N   . LYS B 1 351 ? 73.475 -6.994  40.111  1.00 40.61 ? 351 LYS B N   1 
ATOM   5508 C CA  . LYS B 1 351 ? 74.856 -6.836  40.570  1.00 44.31 ? 351 LYS B CA  1 
ATOM   5509 C C   . LYS B 1 351 ? 75.404 -5.467  40.161  1.00 43.07 ? 351 LYS B C   1 
ATOM   5510 O O   . LYS B 1 351 ? 76.191 -4.864  40.899  1.00 44.32 ? 351 LYS B O   1 
ATOM   5511 C CB  . LYS B 1 351 ? 75.748 -7.971  40.041  1.00 50.83 ? 351 LYS B CB  1 
ATOM   5512 C CG  . LYS B 1 351 ? 75.267 -9.367  40.432  1.00 55.97 ? 351 LYS B CG  1 
ATOM   5513 C CD  . LYS B 1 351 ? 75.015 -10.263 39.194  1.00 66.87 ? 351 LYS B CD  1 
ATOM   5514 C CE  . LYS B 1 351 ? 73.965 -9.704  38.188  1.00 64.69 ? 351 LYS B CE  1 
ATOM   5515 N NZ  . LYS B 1 351 ? 72.565 -9.675  38.707  1.00 64.09 ? 351 LYS B NZ  1 
ATOM   5516 N N   . ASP B 1 352 ? 74.975 -4.965  39.003  1.00 38.32 ? 352 ASP B N   1 
ATOM   5517 C CA  . ASP B 1 352 ? 75.417 -3.653  38.561  1.00 33.97 ? 352 ASP B CA  1 
ATOM   5518 C C   . ASP B 1 352 ? 74.881 -2.565  39.513  1.00 30.93 ? 352 ASP B C   1 
ATOM   5519 O O   . ASP B 1 352 ? 75.547 -1.551  39.753  1.00 30.87 ? 352 ASP B O   1 
ATOM   5520 C CB  . ASP B 1 352 ? 74.956 -3.381  37.132  1.00 37.90 ? 352 ASP B CB  1 
ATOM   5521 C CG  . ASP B 1 352 ? 75.698 -4.219  36.104  1.00 41.42 ? 352 ASP B CG  1 
ATOM   5522 O OD1 . ASP B 1 352 ? 76.955 -4.207  36.098  1.00 40.59 ? 352 ASP B OD1 1 
ATOM   5523 O OD2 . ASP B 1 352 ? 75.014 -4.877  35.290  1.00 43.84 ? 352 ASP B OD2 1 
ATOM   5524 N N   . VAL B 1 353 ? 73.684 -2.773  40.053  1.00 25.99 ? 353 VAL B N   1 
ATOM   5525 C CA  . VAL B 1 353 ? 73.095 -1.817  40.979  1.00 26.44 ? 353 VAL B CA  1 
ATOM   5526 C C   . VAL B 1 353 ? 73.906 -1.813  42.277  1.00 26.99 ? 353 VAL B C   1 
ATOM   5527 O O   . VAL B 1 353 ? 74.258 -0.748  42.799  1.00 26.75 ? 353 VAL B O   1 
ATOM   5528 C CB  . VAL B 1 353 ? 71.617 -2.161  41.254  1.00 26.32 ? 353 VAL B CB  1 
ATOM   5529 C CG1 . VAL B 1 353 ? 71.056 -1.320  42.383  1.00 27.57 ? 353 VAL B CG1 1 
ATOM   5530 C CG2 . VAL B 1 353 ? 70.812 -1.927  40.011  1.00 21.73 ? 353 VAL B CG2 1 
ATOM   5531 N N   . LEU B 1 354 ? 74.244 -3.002  42.777  1.00 27.40 ? 354 LEU B N   1 
ATOM   5532 C CA  . LEU B 1 354 ? 75.041 -3.118  44.012  1.00 24.76 ? 354 LEU B CA  1 
ATOM   5533 C C   . LEU B 1 354 ? 76.437 -2.523  43.862  1.00 24.97 ? 354 LEU B C   1 
ATOM   5534 O O   . LEU B 1 354 ? 76.964 -1.922  44.794  1.00 27.76 ? 354 LEU B O   1 
ATOM   5535 C CB  . LEU B 1 354 ? 75.182 -4.578  44.448  1.00 19.47 ? 354 LEU B CB  1 
ATOM   5536 C CG  . LEU B 1 354 ? 73.968 -5.247  45.104  1.00 22.65 ? 354 LEU B CG  1 
ATOM   5537 C CD1 . LEU B 1 354 ? 74.358 -6.656  45.439  1.00 15.76 ? 354 LEU B CD1 1 
ATOM   5538 C CD2 . LEU B 1 354 ? 73.482 -4.502  46.372  1.00 8.53  ? 354 LEU B CD2 1 
ATOM   5539 N N   . GLY B 1 355 ? 77.028 -2.676  42.684  1.00 20.63 ? 355 GLY B N   1 
ATOM   5540 C CA  . GLY B 1 355 ? 78.351 -2.150  42.468  1.00 22.86 ? 355 GLY B CA  1 
ATOM   5541 C C   . GLY B 1 355 ? 78.378 -0.638  42.436  1.00 24.93 ? 355 GLY B C   1 
ATOM   5542 O O   . GLY B 1 355 ? 79.429 -0.038  42.667  1.00 28.55 ? 355 GLY B O   1 
ATOM   5543 N N   . LEU B 1 356 ? 77.236 -0.031  42.112  1.00 23.63 ? 356 LEU B N   1 
ATOM   5544 C CA  . LEU B 1 356 ? 77.106 1.426   42.042  1.00 23.48 ? 356 LEU B CA  1 
ATOM   5545 C C   . LEU B 1 356 ? 76.641 1.973   43.392  1.00 23.47 ? 356 LEU B C   1 
ATOM   5546 O O   . LEU B 1 356 ? 76.862 3.141   43.708  1.00 23.13 ? 356 LEU B O   1 
ATOM   5547 C CB  . LEU B 1 356 ? 76.109 1.826   40.944  1.00 22.15 ? 356 LEU B CB  1 
ATOM   5548 C CG  . LEU B 1 356 ? 76.573 1.810   39.479  1.00 24.35 ? 356 LEU B CG  1 
ATOM   5549 C CD1 . LEU B 1 356 ? 75.407 1.693   38.543  1.00 19.89 ? 356 LEU B CD1 1 
ATOM   5550 C CD2 . LEU B 1 356 ? 77.349 3.051   39.168  1.00 26.20 ? 356 LEU B CD2 1 
ATOM   5551 N N   . THR B 1 357 ? 76.031 1.111   44.200  1.00 24.64 ? 357 THR B N   1 
ATOM   5552 C CA  . THR B 1 357 ? 75.526 1.487   45.520  1.00 22.44 ? 357 THR B CA  1 
ATOM   5553 C C   . THR B 1 357 ? 76.641 1.561   46.564  1.00 26.50 ? 357 THR B C   1 
ATOM   5554 O O   . THR B 1 357 ? 76.654 2.436   47.421  1.00 30.81 ? 357 THR B O   1 
ATOM   5555 C CB  . THR B 1 357 ? 74.502 0.439   45.992  1.00 20.62 ? 357 THR B CB  1 
ATOM   5556 O OG1 . THR B 1 357 ? 73.396 0.411   45.089  1.00 17.07 ? 357 THR B OG1 1 
ATOM   5557 C CG2 . THR B 1 357 ? 74.019 0.734   47.393  1.00 17.01 ? 357 THR B CG2 1 
ATOM   5558 N N   . PHE B 1 358 ? 77.536 0.586   46.517  1.00 31.73 ? 358 PHE B N   1 
ATOM   5559 C CA  . PHE B 1 358 ? 78.646 0.473   47.450  1.00 29.61 ? 358 PHE B CA  1 
ATOM   5560 C C   . PHE B 1 358 ? 79.978 0.637   46.717  1.00 32.95 ? 358 PHE B C   1 
ATOM   5561 O O   . PHE B 1 358 ? 80.010 0.672   45.477  1.00 35.85 ? 358 PHE B O   1 
ATOM   5562 C CB  . PHE B 1 358 ? 78.542 -0.886  48.128  1.00 29.22 ? 358 PHE B CB  1 
ATOM   5563 C CG  . PHE B 1 358 ? 77.267 -1.060  48.930  1.00 27.45 ? 358 PHE B CG  1 
ATOM   5564 C CD1 . PHE B 1 358 ? 77.083 -0.364  50.141  1.00 22.57 ? 358 PHE B CD1 1 
ATOM   5565 C CD2 . PHE B 1 358 ? 76.257 -1.902  48.485  1.00 23.30 ? 358 PHE B CD2 1 
ATOM   5566 C CE1 . PHE B 1 358 ? 75.932 -0.498  50.890  1.00 9.79  ? 358 PHE B CE1 1 
ATOM   5567 C CE2 . PHE B 1 358 ? 75.084 -2.052  49.229  1.00 24.10 ? 358 PHE B CE2 1 
ATOM   5568 C CZ  . PHE B 1 358 ? 74.923 -1.346  50.439  1.00 19.73 ? 358 PHE B CZ  1 
ATOM   5569 N N   . SER B 1 359 ? 81.079 0.783   47.439  1.00 29.64 ? 359 SER B N   1 
ATOM   5570 C CA  . SER B 1 359 ? 82.338 0.939   46.722  1.00 35.75 ? 359 SER B CA  1 
ATOM   5571 C C   . SER B 1 359 ? 82.874 -0.294  45.992  1.00 35.46 ? 359 SER B C   1 
ATOM   5572 O O   . SER B 1 359 ? 83.425 -0.175  44.906  1.00 38.49 ? 359 SER B O   1 
ATOM   5573 C CB  . SER B 1 359 ? 83.408 1.561   47.597  1.00 34.75 ? 359 SER B CB  1 
ATOM   5574 O OG  . SER B 1 359 ? 83.291 2.972   47.530  1.00 47.13 ? 359 SER B OG  1 
ATOM   5575 N N   . GLY B 1 360 ? 82.695 -1.476  46.569  1.00 36.54 ? 360 GLY B N   1 
ATOM   5576 C CA  . GLY B 1 360 ? 83.173 -2.682  45.923  1.00 35.38 ? 360 GLY B CA  1 
ATOM   5577 C C   . GLY B 1 360 ? 82.480 -2.940  44.595  1.00 37.35 ? 360 GLY B C   1 
ATOM   5578 O O   . GLY B 1 360 ? 81.908 -2.033  43.968  1.00 35.16 ? 360 GLY B O   1 
ATOM   5579 N N   . SER B 1 361 ? 82.573 -4.185  44.147  1.00 36.58 ? 361 SER B N   1 
ATOM   5580 C CA  . SER B 1 361 ? 81.946 -4.602  42.906  1.00 36.50 ? 361 SER B CA  1 
ATOM   5581 C C   . SER B 1 361 ? 80.731 -5.418  43.322  1.00 34.60 ? 361 SER B C   1 
ATOM   5582 O O   . SER B 1 361 ? 80.634 -5.809  44.487  1.00 35.16 ? 361 SER B O   1 
ATOM   5583 C CB  . SER B 1 361 ? 82.920 -5.453  42.084  1.00 40.77 ? 361 SER B CB  1 
ATOM   5584 O OG  . SER B 1 361 ? 83.557 -6.442  42.877  1.00 43.23 ? 361 SER B OG  1 
ATOM   5585 N N   . GLY B 1 362 ? 79.796 -5.646  42.400  1.00 31.11 ? 362 GLY B N   1 
ATOM   5586 C CA  . GLY B 1 362 ? 78.618 -6.431  42.733  1.00 30.10 ? 362 GLY B CA  1 
ATOM   5587 C C   . GLY B 1 362 ? 79.019 -7.801  43.252  1.00 32.58 ? 362 GLY B C   1 
ATOM   5588 O O   . GLY B 1 362 ? 78.398 -8.347  44.163  1.00 36.25 ? 362 GLY B O   1 
ATOM   5589 N N   . ASP B 1 363 ? 80.098 -8.329  42.685  1.00 32.75 ? 363 ASP B N   1 
ATOM   5590 C CA  . ASP B 1 363 ? 80.637 -9.627  43.045  1.00 34.72 ? 363 ASP B CA  1 
ATOM   5591 C C   . ASP B 1 363 ? 81.225 -9.550  44.444  1.00 31.47 ? 363 ASP B C   1 
ATOM   5592 O O   . ASP B 1 363 ? 80.950 -10.405 45.275  1.00 30.81 ? 363 ASP B O   1 
ATOM   5593 C CB  . ASP B 1 363 ? 81.707 -10.044 42.034  1.00 43.14 ? 363 ASP B CB  1 
ATOM   5594 C CG  . ASP B 1 363 ? 81.165 -10.127 40.596  1.00 57.50 ? 363 ASP B CG  1 
ATOM   5595 O OD1 . ASP B 1 363 ? 80.417 -11.088 40.302  1.00 61.10 ? 363 ASP B OD1 1 
ATOM   5596 O OD2 . ASP B 1 363 ? 81.490 -9.241  39.758  1.00 62.61 ? 363 ASP B OD2 1 
ATOM   5597 N N   . GLU B 1 364 ? 82.034 -8.529  44.705  1.00 31.91 ? 364 GLU B N   1 
ATOM   5598 C CA  . GLU B 1 364 ? 82.627 -8.359  46.029  1.00 34.74 ? 364 GLU B CA  1 
ATOM   5599 C C   . GLU B 1 364 ? 81.560 -8.234  47.100  1.00 34.41 ? 364 GLU B C   1 
ATOM   5600 O O   . GLU B 1 364 ? 81.637 -8.900  48.124  1.00 36.06 ? 364 GLU B O   1 
ATOM   5601 C CB  . GLU B 1 364 ? 83.513 -7.111  46.093  1.00 39.87 ? 364 GLU B CB  1 
ATOM   5602 C CG  . GLU B 1 364 ? 84.870 -7.257  45.439  1.00 51.12 ? 364 GLU B CG  1 
ATOM   5603 C CD  . GLU B 1 364 ? 85.696 -5.982  45.514  1.00 54.84 ? 364 GLU B CD  1 
ATOM   5604 O OE1 . GLU B 1 364 ? 85.982 -5.520  46.637  1.00 58.51 ? 364 GLU B OE1 1 
ATOM   5605 O OE2 . GLU B 1 364 ? 86.055 -5.439  44.447  1.00 59.44 ? 364 GLU B OE2 1 
ATOM   5606 N N   . VAL B 1 365 ? 80.549 -7.397  46.874  1.00 36.81 ? 365 VAL B N   1 
ATOM   5607 C CA  . VAL B 1 365 ? 79.522 -7.234  47.900  1.00 37.40 ? 365 VAL B CA  1 
ATOM   5608 C C   . VAL B 1 365 ? 78.758 -8.530  48.174  1.00 36.20 ? 365 VAL B C   1 
ATOM   5609 O O   . VAL B 1 365 ? 78.545 -8.883  49.332  1.00 33.21 ? 365 VAL B O   1 
ATOM   5610 C CB  . VAL B 1 365 ? 78.565 -5.983  47.676  1.00 39.21 ? 365 VAL B CB  1 
ATOM   5611 C CG1 . VAL B 1 365 ? 79.199 -4.942  46.739  1.00 38.00 ? 365 VAL B CG1 1 
ATOM   5612 C CG2 . VAL B 1 365 ? 77.185 -6.394  47.247  1.00 32.68 ? 365 VAL B CG2 1 
ATOM   5613 N N   . MET B 1 366 ? 78.431 -9.281  47.126  1.00 33.60 ? 366 MET B N   1 
ATOM   5614 C CA  . MET B 1 366 ? 77.712 -10.534 47.309  1.00 34.56 ? 366 MET B CA  1 
ATOM   5615 C C   . MET B 1 366 ? 78.552 -11.487 48.141  1.00 36.69 ? 366 MET B C   1 
ATOM   5616 O O   . MET B 1 366 ? 78.048 -12.142 49.052  1.00 35.29 ? 366 MET B O   1 
ATOM   5617 C CB  . MET B 1 366 ? 77.356 -11.146 45.959  1.00 37.18 ? 366 MET B CB  1 
ATOM   5618 C CG  . MET B 1 366 ? 76.332 -10.328 45.146  1.00 40.64 ? 366 MET B CG  1 
ATOM   5619 S SD  . MET B 1 366 ? 74.598 -10.533 45.685  1.00 50.38 ? 366 MET B SD  1 
ATOM   5620 C CE  . MET B 1 366 ? 74.488 -9.432  47.091  1.00 40.94 ? 366 MET B CE  1 
ATOM   5621 N N   . LYS B 1 367 ? 79.853 -11.495 47.862  1.00 39.36 ? 367 LYS B N   1 
ATOM   5622 C CA  . LYS B 1 367 ? 80.820 -12.330 48.570  1.00 40.95 ? 367 LYS B CA  1 
ATOM   5623 C C   . LYS B 1 367 ? 80.786 -12.051 50.074  1.00 37.61 ? 367 LYS B C   1 
ATOM   5624 O O   . LYS B 1 367 ? 80.817 -12.959 50.904  1.00 37.67 ? 367 LYS B O   1 
ATOM   5625 C CB  . LYS B 1 367 ? 82.228 -12.073 47.996  1.00 47.30 ? 367 LYS B CB  1 
ATOM   5626 C CG  . LYS B 1 367 ? 83.386 -11.868 49.030  1.00 57.52 ? 367 LYS B CG  1 
ATOM   5627 C CD  . LYS B 1 367 ? 83.696 -10.382 49.314  1.00 57.13 ? 367 LYS B CD  1 
ATOM   5628 C CE  . LYS B 1 367 ? 84.876 -10.188 50.255  1.00 59.11 ? 367 LYS B CE  1 
ATOM   5629 N NZ  . LYS B 1 367 ? 86.184 -10.532 49.622  1.00 65.43 ? 367 LYS B NZ  1 
ATOM   5630 N N   . LEU B 1 368 ? 80.748 -10.774 50.413  1.00 38.63 ? 368 LEU B N   1 
ATOM   5631 C CA  . LEU B 1 368 ? 80.707 -10.354 51.801  1.00 39.11 ? 368 LEU B CA  1 
ATOM   5632 C C   . LEU B 1 368 ? 79.363 -10.735 52.389  1.00 38.27 ? 368 LEU B C   1 
ATOM   5633 O O   . LEU B 1 368 ? 79.286 -11.368 53.443  1.00 43.18 ? 368 LEU B O   1 
ATOM   5634 C CB  . LEU B 1 368 ? 80.883 -8.836  51.881  1.00 38.01 ? 368 LEU B CB  1 
ATOM   5635 C CG  . LEU B 1 368 ? 80.842 -8.228  53.276  1.00 39.67 ? 368 LEU B CG  1 
ATOM   5636 C CD1 . LEU B 1 368 ? 82.043 -8.729  54.063  1.00 38.26 ? 368 LEU B CD1 1 
ATOM   5637 C CD2 . LEU B 1 368 ? 80.839 -6.703  53.178  1.00 41.99 ? 368 LEU B CD2 1 
ATOM   5638 N N   . ILE B 1 369 ? 78.306 -10.423 51.647  1.00 38.13 ? 369 ILE B N   1 
ATOM   5639 C CA  . ILE B 1 369 ? 76.940 -10.673 52.087  1.00 37.98 ? 369 ILE B CA  1 
ATOM   5640 C C   . ILE B 1 369 ? 76.674 -12.149 52.367  1.00 38.10 ? 369 ILE B C   1 
ATOM   5641 O O   . ILE B 1 369 ? 75.780 -12.487 53.136  1.00 38.84 ? 369 ILE B O   1 
ATOM   5642 C CB  . ILE B 1 369 ? 75.911 -10.046 51.094  1.00 30.92 ? 369 ILE B CB  1 
ATOM   5643 C CG1 . ILE B 1 369 ? 74.759 -9.430  51.858  1.00 26.40 ? 369 ILE B CG1 1 
ATOM   5644 C CG2 . ILE B 1 369 ? 75.380 -11.069 50.115  1.00 39.81 ? 369 ILE B CG2 1 
ATOM   5645 C CD1 . ILE B 1 369 ? 75.169 -8.283  52.727  1.00 17.83 ? 369 ILE B CD1 1 
ATOM   5646 N N   . ASN B 1 370 ? 77.506 -13.020 51.806  1.00 41.10 ? 370 ASN B N   1 
ATOM   5647 C CA  . ASN B 1 370 ? 77.337 -14.444 52.022  1.00 40.19 ? 370 ASN B CA  1 
ATOM   5648 C C   . ASN B 1 370 ? 78.234 -15.049 53.079  1.00 34.85 ? 370 ASN B C   1 
ATOM   5649 O O   . ASN B 1 370 ? 78.011 -16.184 53.462  1.00 37.53 ? 370 ASN B O   1 
ATOM   5650 C CB  . ASN B 1 370 ? 77.433 -15.223 50.711  1.00 45.65 ? 370 ASN B CB  1 
ATOM   5651 C CG  . ASN B 1 370 ? 76.218 -15.000 49.807  1.00 56.50 ? 370 ASN B CG  1 
ATOM   5652 O OD1 . ASN B 1 370 ? 76.045 -13.924 49.224  1.00 59.78 ? 370 ASN B OD1 1 
ATOM   5653 N ND2 . ASN B 1 370 ? 75.373 -16.021 49.685  1.00 60.69 ? 370 ASN B ND2 1 
ATOM   5654 N N   . LYS B 1 371 ? 79.244 -14.323 53.560  1.00 33.97 ? 371 LYS B N   1 
ATOM   5655 C CA  . LYS B 1 371 ? 80.110 -14.880 54.624  1.00 39.26 ? 371 LYS B CA  1 
ATOM   5656 C C   . LYS B 1 371 ? 79.303 -15.403 55.840  1.00 37.55 ? 371 LYS B C   1 
ATOM   5657 O O   . LYS B 1 371 ? 79.467 -16.547 56.265  1.00 34.74 ? 371 LYS B O   1 
ATOM   5658 C CB  . LYS B 1 371 ? 81.164 -13.863 55.077  1.00 36.92 ? 371 LYS B CB  1 
ATOM   5659 C CG  . LYS B 1 371 ? 82.190 -13.556 54.003  1.00 44.70 ? 371 LYS B CG  1 
ATOM   5660 C CD  . LYS B 1 371 ? 83.294 -12.644 54.507  1.00 47.58 ? 371 LYS B CD  1 
ATOM   5661 C CE  . LYS B 1 371 ? 84.301 -12.346 53.396  1.00 54.48 ? 371 LYS B CE  1 
ATOM   5662 N NZ  . LYS B 1 371 ? 85.474 -11.524 53.844  1.00 57.47 ? 371 LYS B NZ  1 
ATOM   5663 N N   . GLN B 1 372 ? 78.389 -14.564 56.337  1.00 42.85 ? 372 GLN B N   1 
ATOM   5664 C CA  . GLN B 1 372 ? 77.488 -14.871 57.460  1.00 37.98 ? 372 GLN B CA  1 
ATOM   5665 C C   . GLN B 1 372 ? 76.567 -16.056 57.127  1.00 35.07 ? 372 GLN B C   1 
ATOM   5666 O O   . GLN B 1 372 ? 75.783 -16.004 56.186  1.00 28.35 ? 372 GLN B O   1 
ATOM   5667 C CB  . GLN B 1 372 ? 76.640 -13.630 57.784  1.00 35.58 ? 372 GLN B CB  1 
ATOM   5668 C CG  . GLN B 1 372 ? 75.611 -13.829 58.884  1.00 32.93 ? 372 GLN B CG  1 
ATOM   5669 C CD  . GLN B 1 372 ? 76.224 -14.312 60.186  1.00 35.69 ? 372 GLN B CD  1 
ATOM   5670 O OE1 . GLN B 1 372 ? 76.014 -15.450 60.592  1.00 37.12 ? 372 GLN B OE1 1 
ATOM   5671 N NE2 . GLN B 1 372 ? 76.978 -13.449 60.848  1.00 36.41 ? 372 GLN B NE2 1 
ATOM   5672 N N   . SER B 1 373 ? 76.633 -17.102 57.940  1.00 36.23 ? 373 SER B N   1 
ATOM   5673 C CA  . SER B 1 373 ? 75.817 -18.296 57.722  1.00 38.56 ? 373 SER B CA  1 
ATOM   5674 C C   . SER B 1 373 ? 74.515 -18.345 58.518  1.00 36.44 ? 373 SER B C   1 
ATOM   5675 O O   . SER B 1 373 ? 73.635 -19.161 58.225  1.00 37.13 ? 373 SER B O   1 
ATOM   5676 C CB  . SER B 1 373 ? 76.651 -19.535 58.026  1.00 44.26 ? 373 SER B CB  1 
ATOM   5677 O OG  . SER B 1 373 ? 77.880 -19.154 58.638  1.00 54.51 ? 373 SER B OG  1 
ATOM   5678 N N   . GLY B 1 374 ? 74.405 -17.496 59.538  1.00 34.70 ? 374 GLY B N   1 
ATOM   5679 C CA  . GLY B 1 374 ? 73.207 -17.464 60.357  1.00 30.70 ? 374 GLY B CA  1 
ATOM   5680 C C   . GLY B 1 374 ? 72.070 -16.596 59.831  1.00 28.69 ? 374 GLY B C   1 
ATOM   5681 O O   . GLY B 1 374 ? 72.196 -15.887 58.830  1.00 21.64 ? 374 GLY B O   1 
ATOM   5682 N N   . SER B 1 375 ? 70.958 -16.624 60.555  1.00 32.36 ? 375 SER B N   1 
ATOM   5683 C CA  . SER B 1 375 ? 69.773 -15.859 60.201  1.00 34.36 ? 375 SER B CA  1 
ATOM   5684 C C   . SER B 1 375 ? 69.172 -15.245 61.466  1.00 34.76 ? 375 SER B C   1 
ATOM   5685 O O   . SER B 1 375 ? 69.093 -15.906 62.509  1.00 33.93 ? 375 SER B O   1 
ATOM   5686 C CB  . SER B 1 375 ? 68.740 -16.779 59.534  1.00 38.59 ? 375 SER B CB  1 
ATOM   5687 O OG  . SER B 1 375 ? 69.310 -17.577 58.494  1.00 44.62 ? 375 SER B OG  1 
ATOM   5688 N N   . TYR B 1 376 ? 68.781 -13.973 61.364  1.00 36.69 ? 376 TYR B N   1 
ATOM   5689 C CA  . TYR B 1 376 ? 68.157 -13.210 62.454  1.00 35.43 ? 376 TYR B CA  1 
ATOM   5690 C C   . TYR B 1 376 ? 68.999 -12.954 63.707  1.00 32.41 ? 376 TYR B C   1 
ATOM   5691 O O   . TYR B 1 376 ? 69.460 -11.841 63.937  1.00 26.17 ? 376 TYR B O   1 
ATOM   5692 C CB  . TYR B 1 376 ? 66.812 -13.848 62.861  1.00 34.67 ? 376 TYR B CB  1 
ATOM   5693 C CG  . TYR B 1 376 ? 65.637 -13.459 61.999  1.00 31.60 ? 376 TYR B CG  1 
ATOM   5694 C CD1 . TYR B 1 376 ? 65.461 -13.999 60.718  1.00 34.60 ? 376 TYR B CD1 1 
ATOM   5695 C CD2 . TYR B 1 376 ? 64.724 -12.504 62.444  1.00 37.94 ? 376 TYR B CD2 1 
ATOM   5696 C CE1 . TYR B 1 376 ? 64.398 -13.579 59.894  1.00 38.02 ? 376 TYR B CE1 1 
ATOM   5697 C CE2 . TYR B 1 376 ? 63.670 -12.078 61.645  1.00 37.91 ? 376 TYR B CE2 1 
ATOM   5698 C CZ  . TYR B 1 376 ? 63.514 -12.607 60.373  1.00 39.73 ? 376 TYR B CZ  1 
ATOM   5699 O OH  . TYR B 1 376 ? 62.506 -12.102 59.586  1.00 37.00 ? 376 TYR B OH  1 
ATOM   5700 N N   . PHE B 1 377 ? 69.151 -13.986 64.528  1.00 34.72 ? 377 PHE B N   1 
ATOM   5701 C CA  . PHE B 1 377 ? 69.895 -13.901 65.786  1.00 34.29 ? 377 PHE B CA  1 
ATOM   5702 C C   . PHE B 1 377 ? 71.291 -14.506 65.668  1.00 35.09 ? 377 PHE B C   1 
ATOM   5703 O O   . PHE B 1 377 ? 71.455 -15.723 65.521  1.00 39.62 ? 377 PHE B O   1 
ATOM   5704 C CB  . PHE B 1 377 ? 69.100 -14.596 66.882  1.00 29.19 ? 377 PHE B CB  1 
ATOM   5705 C CG  . PHE B 1 377 ? 67.683 -14.122 66.977  1.00 25.91 ? 377 PHE B CG  1 
ATOM   5706 C CD1 . PHE B 1 377 ? 67.397 -12.860 67.475  1.00 19.75 ? 377 PHE B CD1 1 
ATOM   5707 C CD2 . PHE B 1 377 ? 66.632 -14.947 66.587  1.00 22.80 ? 377 PHE B CD2 1 
ATOM   5708 C CE1 . PHE B 1 377 ? 66.073 -12.429 67.592  1.00 19.34 ? 377 PHE B CE1 1 
ATOM   5709 C CE2 . PHE B 1 377 ? 65.314 -14.523 66.702  1.00 24.21 ? 377 PHE B CE2 1 
ATOM   5710 C CZ  . PHE B 1 377 ? 65.031 -13.260 67.209  1.00 20.68 ? 377 PHE B CZ  1 
ATOM   5711 N N   . VAL B 1 378 ? 72.283 -13.626 65.724  1.00 35.07 ? 378 VAL B N   1 
ATOM   5712 C CA  . VAL B 1 378 ? 73.702 -13.950 65.597  1.00 33.89 ? 378 VAL B CA  1 
ATOM   5713 C C   . VAL B 1 378 ? 74.427 -13.924 66.955  1.00 35.32 ? 378 VAL B C   1 
ATOM   5714 O O   . VAL B 1 378 ? 73.835 -13.614 67.981  1.00 37.10 ? 378 VAL B O   1 
ATOM   5715 C CB  . VAL B 1 378 ? 74.312 -12.939 64.566  1.00 31.85 ? 378 VAL B CB  1 
ATOM   5716 C CG1 . VAL B 1 378 ? 75.750 -12.570 64.862  1.00 30.69 ? 378 VAL B CG1 1 
ATOM   5717 C CG2 . VAL B 1 378 ? 74.151 -13.486 63.164  1.00 26.04 ? 378 VAL B CG2 1 
ATOM   5718 N N   . ASP B 1 379 ? 75.661 -14.389 66.979  1.00 37.46 ? 379 ASP B N   1 
ATOM   5719 C CA  . ASP B 1 379 ? 76.446 -14.364 68.194  1.00 44.93 ? 379 ASP B CA  1 
ATOM   5720 C C   . ASP B 1 379 ? 77.366 -13.158 68.054  1.00 46.25 ? 379 ASP B C   1 
ATOM   5721 O O   . ASP B 1 379 ? 78.061 -13.032 67.051  1.00 49.22 ? 379 ASP B O   1 
ATOM   5722 C CB  . ASP B 1 379 ? 77.280 -15.633 68.287  1.00 53.29 ? 379 ASP B CB  1 
ATOM   5723 C CG  . ASP B 1 379 ? 78.195 -15.633 69.487  1.00 60.47 ? 379 ASP B CG  1 
ATOM   5724 O OD1 . ASP B 1 379 ? 77.731 -16.018 70.586  1.00 63.52 ? 379 ASP B OD1 1 
ATOM   5725 O OD2 . ASP B 1 379 ? 79.372 -15.238 69.330  1.00 63.68 ? 379 ASP B OD2 1 
ATOM   5726 N N   . ALA B 1 380 ? 77.420 -12.286 69.050  1.00 47.29 ? 380 ALA B N   1 
ATOM   5727 C CA  . ALA B 1 380 ? 78.278 -11.122 68.909  1.00 49.01 ? 380 ALA B CA  1 
ATOM   5728 C C   . ALA B 1 380 ? 79.351 -10.942 69.967  1.00 53.57 ? 380 ALA B C   1 
ATOM   5729 O O   . ALA B 1 380 ? 79.419 -9.896  70.602  1.00 56.32 ? 380 ALA B O   1 
ATOM   5730 C CB  . ALA B 1 380 ? 77.442 -9.865  68.786  1.00 48.78 ? 380 ALA B CB  1 
ATOM   5731 N N   . HIS B 1 381 ? 80.191 -11.957 70.162  1.00 58.30 ? 381 HIS B N   1 
ATOM   5732 C CA  . HIS B 1 381 ? 81.294 -11.861 71.126  1.00 62.31 ? 381 HIS B CA  1 
ATOM   5733 C C   . HIS B 1 381 ? 82.406 -12.880 70.909  1.00 64.86 ? 381 HIS B C   1 
ATOM   5734 O O   . HIS B 1 381 ? 82.409 -13.954 71.511  1.00 71.07 ? 381 HIS B O   1 
ATOM   5735 C CB  . HIS B 1 381 ? 80.809 -11.863 72.598  1.00 65.42 ? 381 HIS B CB  1 
ATOM   5736 C CG  . HIS B 1 381 ? 79.949 -13.034 72.983  1.00 68.36 ? 381 HIS B CG  1 
ATOM   5737 N ND1 . HIS B 1 381 ? 79.625 -13.316 74.295  1.00 68.90 ? 381 HIS B ND1 1 
ATOM   5738 C CD2 . HIS B 1 381 ? 79.317 -13.971 72.235  1.00 68.67 ? 381 HIS B CD2 1 
ATOM   5739 C CE1 . HIS B 1 381 ? 78.831 -14.370 74.339  1.00 68.83 ? 381 HIS B CE1 1 
ATOM   5740 N NE2 . HIS B 1 381 ? 78.628 -14.786 73.102  1.00 70.81 ? 381 HIS B NE2 1 
ATOM   5741 N N   . GLN C 1 10  ? 49.894 34.226  52.894  1.00 56.06 ? 10  GLN C N   1 
ATOM   5742 C CA  . GLN C 1 10  ? 48.939 35.039  53.657  1.00 57.72 ? 10  GLN C CA  1 
ATOM   5743 C C   . GLN C 1 10  ? 47.742 35.450  52.794  1.00 53.73 ? 10  GLN C C   1 
ATOM   5744 O O   . GLN C 1 10  ? 46.684 34.850  52.882  1.00 56.34 ? 10  GLN C O   1 
ATOM   5745 C CB  . GLN C 1 10  ? 49.606 36.311  54.230  1.00 60.66 ? 10  GLN C CB  1 
ATOM   5746 C CG  . GLN C 1 10  ? 50.764 36.107  55.218  1.00 59.28 ? 10  GLN C CG  1 
ATOM   5747 C CD  . GLN C 1 10  ? 50.379 35.336  56.477  1.00 61.64 ? 10  GLN C CD  1 
ATOM   5748 O OE1 . GLN C 1 10  ? 51.071 34.391  56.858  1.00 61.46 ? 10  GLN C OE1 1 
ATOM   5749 N NE2 . GLN C 1 10  ? 49.288 35.744  57.133  1.00 56.26 ? 10  GLN C NE2 1 
ATOM   5750 N N   . ASP C 1 11  ? 47.939 36.477  51.970  1.00 51.29 ? 11  ASP C N   1 
ATOM   5751 C CA  . ASP C 1 11  ? 46.928 37.022  51.065  1.00 49.55 ? 11  ASP C CA  1 
ATOM   5752 C C   . ASP C 1 11  ? 45.901 36.001  50.545  1.00 42.12 ? 11  ASP C C   1 
ATOM   5753 O O   . ASP C 1 11  ? 44.699 36.130  50.773  1.00 40.19 ? 11  ASP C O   1 
ATOM   5754 C CB  . ASP C 1 11  ? 47.642 37.683  49.877  1.00 63.46 ? 11  ASP C CB  1 
ATOM   5755 C CG  . ASP C 1 11  ? 48.520 36.686  49.064  1.00 75.05 ? 11  ASP C CG  1 
ATOM   5756 O OD1 . ASP C 1 11  ? 49.135 35.763  49.661  1.00 77.71 ? 11  ASP C OD1 1 
ATOM   5757 O OD2 . ASP C 1 11  ? 48.594 36.828  47.817  1.00 81.54 ? 11  ASP C OD2 1 
ATOM   5758 N N   . ASN C 1 12  ? 46.394 35.023  49.796  1.00 35.17 ? 12  ASN C N   1 
ATOM   5759 C CA  . ASN C 1 12  ? 45.582 33.970  49.231  1.00 30.45 ? 12  ASN C CA  1 
ATOM   5760 C C   . ASN C 1 12  ? 46.269 32.774  49.830  1.00 27.15 ? 12  ASN C C   1 
ATOM   5761 O O   . ASN C 1 12  ? 47.450 32.541  49.570  1.00 30.08 ? 12  ASN C O   1 
ATOM   5762 C CB  . ASN C 1 12  ? 45.696 33.933  47.695  1.00 26.16 ? 12  ASN C CB  1 
ATOM   5763 C CG  . ASN C 1 12  ? 44.931 32.758  47.065  1.00 28.53 ? 12  ASN C CG  1 
ATOM   5764 O OD1 . ASN C 1 12  ? 44.420 31.873  47.765  1.00 27.34 ? 12  ASN C OD1 1 
ATOM   5765 N ND2 . ASN C 1 12  ? 44.856 32.749  45.738  1.00 20.05 ? 12  ASN C ND2 1 
ATOM   5766 N N   . PRO C 1 13  ? 45.591 32.099  50.763  1.00 26.95 ? 13  PRO C N   1 
ATOM   5767 C CA  . PRO C 1 13  ? 46.104 30.912  51.451  1.00 25.86 ? 13  PRO C CA  1 
ATOM   5768 C C   . PRO C 1 13  ? 46.135 29.614  50.633  1.00 26.85 ? 13  PRO C C   1 
ATOM   5769 O O   . PRO C 1 13  ? 46.787 28.648  51.043  1.00 28.31 ? 13  PRO C O   1 
ATOM   5770 C CB  . PRO C 1 13  ? 45.152 30.788  52.637  1.00 24.15 ? 13  PRO C CB  1 
ATOM   5771 C CG  . PRO C 1 13  ? 43.862 31.361  52.079  1.00 22.79 ? 13  PRO C CG  1 
ATOM   5772 C CD  . PRO C 1 13  ? 44.358 32.591  51.408  1.00 20.10 ? 13  PRO C CD  1 
ATOM   5773 N N   . PHE C 1 14  ? 45.451 29.590  49.488  1.00 27.12 ? 14  PHE C N   1 
ATOM   5774 C CA  . PHE C 1 14  ? 45.379 28.381  48.659  1.00 24.78 ? 14  PHE C CA  1 
ATOM   5775 C C   . PHE C 1 14  ? 46.403 28.264  47.554  1.00 22.34 ? 14  PHE C C   1 
ATOM   5776 O O   . PHE C 1 14  ? 46.489 27.217  46.904  1.00 25.08 ? 14  PHE C O   1 
ATOM   5777 C CB  . PHE C 1 14  ? 43.986 28.233  48.037  1.00 21.58 ? 14  PHE C CB  1 
ATOM   5778 C CG  . PHE C 1 14  ? 42.867 28.397  49.021  1.00 22.99 ? 14  PHE C CG  1 
ATOM   5779 C CD1 . PHE C 1 14  ? 42.575 27.393  49.938  1.00 18.97 ? 14  PHE C CD1 1 
ATOM   5780 C CD2 . PHE C 1 14  ? 42.150 29.588  49.085  1.00 20.12 ? 14  PHE C CD2 1 
ATOM   5781 C CE1 . PHE C 1 14  ? 41.591 27.584  50.909  1.00 14.63 ? 14  PHE C CE1 1 
ATOM   5782 C CE2 . PHE C 1 14  ? 41.167 29.772  50.052  1.00 21.06 ? 14  PHE C CE2 1 
ATOM   5783 C CZ  . PHE C 1 14  ? 40.893 28.772  50.963  1.00 10.86 ? 14  PHE C CZ  1 
ATOM   5784 N N   . TYR C 1 15  ? 47.218 29.297  47.381  1.00 22.77 ? 15  TYR C N   1 
ATOM   5785 C CA  . TYR C 1 15  ? 48.204 29.315  46.311  1.00 19.54 ? 15  TYR C CA  1 
ATOM   5786 C C   . TYR C 1 15  ? 49.575 29.059  46.846  1.00 21.91 ? 15  TYR C C   1 
ATOM   5787 O O   . TYR C 1 15  ? 49.921 29.582  47.883  1.00 25.02 ? 15  TYR C O   1 
ATOM   5788 C CB  . TYR C 1 15  ? 48.161 30.679  45.625  1.00 20.64 ? 15  TYR C CB  1 
ATOM   5789 C CG  . TYR C 1 15  ? 49.199 30.954  44.557  1.00 19.97 ? 15  TYR C CG  1 
ATOM   5790 C CD1 . TYR C 1 15  ? 49.414 30.062  43.511  1.00 25.36 ? 15  TYR C CD1 1 
ATOM   5791 C CD2 . TYR C 1 15  ? 49.961 32.118  44.592  1.00 16.08 ? 15  TYR C CD2 1 
ATOM   5792 C CE1 . TYR C 1 15  ? 50.366 30.318  42.539  1.00 18.10 ? 15  TYR C CE1 1 
ATOM   5793 C CE2 . TYR C 1 15  ? 50.906 32.379  43.624  1.00 20.25 ? 15  TYR C CE2 1 
ATOM   5794 C CZ  . TYR C 1 15  ? 51.109 31.473  42.609  1.00 17.00 ? 15  TYR C CZ  1 
ATOM   5795 O OH  . TYR C 1 15  ? 52.122 31.683  41.717  1.00 25.32 ? 15  TYR C OH  1 
ATOM   5796 N N   . PHE C 1 16  ? 50.335 28.215  46.149  1.00 23.09 ? 16  PHE C N   1 
ATOM   5797 C CA  . PHE C 1 16  ? 51.707 27.901  46.528  1.00 22.31 ? 16  PHE C CA  1 
ATOM   5798 C C   . PHE C 1 16  ? 52.651 28.199  45.362  1.00 21.46 ? 16  PHE C C   1 
ATOM   5799 O O   . PHE C 1 16  ? 52.698 27.457  44.385  1.00 17.20 ? 16  PHE C O   1 
ATOM   5800 C CB  . PHE C 1 16  ? 51.839 26.434  46.963  1.00 21.26 ? 16  PHE C CB  1 
ATOM   5801 C CG  . PHE C 1 16  ? 51.072 26.097  48.216  1.00 18.49 ? 16  PHE C CG  1 
ATOM   5802 C CD1 . PHE C 1 16  ? 49.697 25.899  48.179  1.00 19.27 ? 16  PHE C CD1 1 
ATOM   5803 C CD2 . PHE C 1 16  ? 51.732 25.946  49.423  1.00 18.09 ? 16  PHE C CD2 1 
ATOM   5804 C CE1 . PHE C 1 16  ? 49.001 25.551  49.319  1.00 12.03 ? 16  PHE C CE1 1 
ATOM   5805 C CE2 . PHE C 1 16  ? 51.042 25.598  50.574  1.00 12.80 ? 16  PHE C CE2 1 
ATOM   5806 C CZ  . PHE C 1 16  ? 49.675 25.401  50.514  1.00 14.02 ? 16  PHE C CZ  1 
ATOM   5807 N N   . ASN C 1 17  ? 53.366 29.317  45.473  1.00 23.54 ? 17  ASN C N   1 
ATOM   5808 C CA  . ASN C 1 17  ? 54.313 29.777  44.473  1.00 25.65 ? 17  ASN C CA  1 
ATOM   5809 C C   . ASN C 1 17  ? 55.507 28.857  44.513  1.00 27.50 ? 17  ASN C C   1 
ATOM   5810 O O   . ASN C 1 17  ? 56.135 28.715  45.550  1.00 26.33 ? 17  ASN C O   1 
ATOM   5811 C CB  . ASN C 1 17  ? 54.777 31.209  44.792  1.00 32.94 ? 17  ASN C CB  1 
ATOM   5812 C CG  . ASN C 1 17  ? 55.642 31.815  43.679  1.00 37.59 ? 17  ASN C CG  1 
ATOM   5813 O OD1 . ASN C 1 17  ? 56.680 31.266  43.309  1.00 38.01 ? 17  ASN C OD1 1 
ATOM   5814 N ND2 . ASN C 1 17  ? 55.191 32.932  43.119  1.00 42.76 ? 17  ASN C ND2 1 
ATOM   5815 N N   . SER C 1 18  ? 55.878 28.321  43.359  1.00 27.74 ? 18  SER C N   1 
ATOM   5816 C CA  . SER C 1 18  ? 56.991 27.397  43.252  1.00 31.28 ? 18  SER C CA  1 
ATOM   5817 C C   . SER C 1 18  ? 58.276 27.970  43.794  1.00 33.88 ? 18  SER C C   1 
ATOM   5818 O O   . SER C 1 18  ? 59.044 27.260  44.445  1.00 36.18 ? 18  SER C O   1 
ATOM   5819 C CB  . SER C 1 18  ? 57.181 26.956  41.796  1.00 33.83 ? 18  SER C CB  1 
ATOM   5820 O OG  . SER C 1 18  ? 57.080 28.059  40.896  1.00 40.78 ? 18  SER C OG  1 
ATOM   5821 N N   . ASP C 1 19  ? 58.496 29.261  43.551  1.00 37.76 ? 19  ASP C N   1 
ATOM   5822 C CA  . ASP C 1 19  ? 59.711 29.943  44.004  1.00 39.95 ? 19  ASP C CA  1 
ATOM   5823 C C   . ASP C 1 19  ? 59.974 29.711  45.482  1.00 38.58 ? 19  ASP C C   1 
ATOM   5824 O O   . ASP C 1 19  ? 61.042 29.244  45.877  1.00 39.17 ? 19  ASP C O   1 
ATOM   5825 C CB  . ASP C 1 19  ? 59.627 31.459  43.761  1.00 41.30 ? 19  ASP C CB  1 
ATOM   5826 C CG  . ASP C 1 19  ? 59.708 31.835  42.291  1.00 44.77 ? 19  ASP C CG  1 
ATOM   5827 O OD1 . ASP C 1 19  ? 60.107 30.979  41.463  1.00 46.79 ? 19  ASP C OD1 1 
ATOM   5828 O OD2 . ASP C 1 19  ? 59.379 33.007  41.977  1.00 45.35 ? 19  ASP C OD2 1 
ATOM   5829 N N   . ASN C 1 20  ? 58.980 30.001  46.301  1.00 36.08 ? 20  ASN C N   1 
ATOM   5830 C CA  . ASN C 1 20  ? 59.169 29.844  47.723  1.00 39.14 ? 20  ASN C CA  1 
ATOM   5831 C C   . ASN C 1 20  ? 58.374 28.726  48.388  1.00 34.56 ? 20  ASN C C   1 
ATOM   5832 O O   . ASN C 1 20  ? 58.008 28.849  49.551  1.00 40.87 ? 20  ASN C O   1 
ATOM   5833 C CB  . ASN C 1 20  ? 58.921 31.190  48.417  1.00 42.54 ? 20  ASN C CB  1 
ATOM   5834 C CG  . ASN C 1 20  ? 57.541 31.733  48.153  1.00 44.43 ? 20  ASN C CG  1 
ATOM   5835 O OD1 . ASN C 1 20  ? 57.238 32.147  47.039  1.00 50.64 ? 20  ASN C OD1 1 
ATOM   5836 N ND2 . ASN C 1 20  ? 56.694 31.742  49.178  1.00 46.84 ? 20  ASN C ND2 1 
ATOM   5837 N N   . SER C 1 21  ? 58.171 27.611  47.698  1.00 29.46 ? 21  SER C N   1 
ATOM   5838 C CA  . SER C 1 21  ? 57.402 26.518  48.274  1.00 24.93 ? 21  SER C CA  1 
ATOM   5839 C C   . SER C 1 21  ? 58.034 25.138  48.276  1.00 29.51 ? 21  SER C C   1 
ATOM   5840 O O   . SER C 1 21  ? 57.608 24.271  49.057  1.00 29.13 ? 21  SER C O   1 
ATOM   5841 C CB  . SER C 1 21  ? 56.048 26.443  47.612  1.00 18.18 ? 21  SER C CB  1 
ATOM   5842 O OG  . SER C 1 21  ? 55.341 27.656  47.807  1.00 26.85 ? 21  SER C OG  1 
ATOM   5843 N N   . TRP C 1 22  ? 59.027 24.931  47.406  1.00 28.83 ? 22  TRP C N   1 
ATOM   5844 C CA  . TRP C 1 22  ? 59.740 23.652  47.285  1.00 29.44 ? 22  TRP C CA  1 
ATOM   5845 C C   . TRP C 1 22  ? 61.115 23.739  47.947  1.00 29.96 ? 22  TRP C C   1 
ATOM   5846 O O   . TRP C 1 22  ? 61.777 24.760  47.822  1.00 39.12 ? 22  TRP C O   1 
ATOM   5847 C CB  . TRP C 1 22  ? 59.959 23.317  45.804  1.00 25.82 ? 22  TRP C CB  1 
ATOM   5848 C CG  . TRP C 1 22  ? 58.709 23.089  45.034  1.00 22.17 ? 22  TRP C CG  1 
ATOM   5849 C CD1 . TRP C 1 22  ? 58.010 24.009  44.317  1.00 17.96 ? 22  TRP C CD1 1 
ATOM   5850 C CD2 . TRP C 1 22  ? 57.984 21.851  44.931  1.00 18.91 ? 22  TRP C CD2 1 
ATOM   5851 N NE1 . TRP C 1 22  ? 56.884 23.426  43.783  1.00 25.79 ? 22  TRP C NE1 1 
ATOM   5852 C CE2 . TRP C 1 22  ? 56.842 22.103  44.150  1.00 17.64 ? 22  TRP C CE2 1 
ATOM   5853 C CE3 . TRP C 1 22  ? 58.192 20.555  45.437  1.00 16.43 ? 22  TRP C CE3 1 
ATOM   5854 C CZ2 . TRP C 1 22  ? 55.897 21.104  43.850  1.00 17.77 ? 22  TRP C CZ2 1 
ATOM   5855 C CZ3 . TRP C 1 22  ? 57.247 19.557  45.140  1.00 15.96 ? 22  TRP C CZ3 1 
ATOM   5856 C CH2 . TRP C 1 22  ? 56.113 19.844  44.357  1.00 11.15 ? 22  TRP C CH2 1 
ATOM   5857 N N   . ASN C 1 23  ? 61.555 22.698  48.646  1.00 25.88 ? 23  ASN C N   1 
ATOM   5858 C CA  . ASN C 1 23  ? 62.882 22.733  49.252  1.00 24.56 ? 23  ASN C CA  1 
ATOM   5859 C C   . ASN C 1 23  ? 63.667 21.598  48.629  1.00 25.04 ? 23  ASN C C   1 
ATOM   5860 O O   . ASN C 1 23  ? 63.156 20.493  48.546  1.00 28.26 ? 23  ASN C O   1 
ATOM   5861 C CB  . ASN C 1 23  ? 62.795 22.547  50.765  1.00 29.81 ? 23  ASN C CB  1 
ATOM   5862 C CG  . ASN C 1 23  ? 62.095 23.716  51.474  1.00 38.45 ? 23  ASN C CG  1 
ATOM   5863 O OD1 . ASN C 1 23  ? 62.743 24.676  51.903  1.00 42.26 ? 23  ASN C OD1 1 
ATOM   5864 N ND2 . ASN C 1 23  ? 60.778 23.618  51.635  1.00 40.81 ? 23  ASN C ND2 1 
ATOM   5865 N N   . THR C 1 24  ? 64.875 21.862  48.139  1.00 26.71 ? 24  THR C N   1 
ATOM   5866 C CA  . THR C 1 24  ? 65.700 20.808  47.514  1.00 26.48 ? 24  THR C CA  1 
ATOM   5867 C C   . THR C 1 24  ? 66.351 19.798  48.457  1.00 28.17 ? 24  THR C C   1 
ATOM   5868 O O   . THR C 1 24  ? 67.142 20.155  49.332  1.00 28.78 ? 24  THR C O   1 
ATOM   5869 C CB  . THR C 1 24  ? 66.845 21.376  46.660  1.00 28.73 ? 24  THR C CB  1 
ATOM   5870 O OG1 . THR C 1 24  ? 66.328 22.344  45.739  1.00 32.81 ? 24  THR C OG1 1 
ATOM   5871 C CG2 . THR C 1 24  ? 67.539 20.230  45.864  1.00 27.90 ? 24  THR C CG2 1 
ATOM   5872 N N   . LEU C 1 25  ? 66.082 18.525  48.206  1.00 27.70 ? 25  LEU C N   1 
ATOM   5873 C CA  . LEU C 1 25  ? 66.637 17.450  49.005  1.00 27.74 ? 25  LEU C CA  1 
ATOM   5874 C C   . LEU C 1 25  ? 67.996 17.026  48.453  1.00 27.89 ? 25  LEU C C   1 
ATOM   5875 O O   . LEU C 1 25  ? 68.933 16.777  49.202  1.00 30.55 ? 25  LEU C O   1 
ATOM   5876 C CB  . LEU C 1 25  ? 65.684 16.267  48.981  1.00 28.97 ? 25  LEU C CB  1 
ATOM   5877 C CG  . LEU C 1 25  ? 65.400 15.531  50.283  1.00 29.14 ? 25  LEU C CG  1 
ATOM   5878 C CD1 . LEU C 1 25  ? 65.489 14.061  49.993  1.00 26.51 ? 25  LEU C CD1 1 
ATOM   5879 C CD2 . LEU C 1 25  ? 66.379 15.895  51.369  1.00 31.43 ? 25  LEU C CD2 1 
ATOM   5880 N N   . PHE C 1 26  ? 68.078 16.925  47.131  1.00 29.72 ? 26  PHE C N   1 
ATOM   5881 C CA  . PHE C 1 26  ? 69.292 16.539  46.423  1.00 25.20 ? 26  PHE C CA  1 
ATOM   5882 C C   . PHE C 1 26  ? 69.216 17.152  45.030  1.00 27.72 ? 26  PHE C C   1 
ATOM   5883 O O   . PHE C 1 26  ? 68.129 17.361  44.477  1.00 28.89 ? 26  PHE C O   1 
ATOM   5884 C CB  . PHE C 1 26  ? 69.397 15.010  46.305  1.00 24.22 ? 26  PHE C CB  1 
ATOM   5885 C CG  . PHE C 1 26  ? 70.651 14.526  45.579  1.00 26.40 ? 26  PHE C CG  1 
ATOM   5886 C CD1 . PHE C 1 26  ? 71.898 14.540  46.214  1.00 22.76 ? 26  PHE C CD1 1 
ATOM   5887 C CD2 . PHE C 1 26  ? 70.579 14.039  44.273  1.00 25.83 ? 26  PHE C CD2 1 
ATOM   5888 C CE1 . PHE C 1 26  ? 73.039 14.077  45.564  1.00 17.22 ? 26  PHE C CE1 1 
ATOM   5889 C CE2 . PHE C 1 26  ? 71.723 13.574  43.616  1.00 21.22 ? 26  PHE C CE2 1 
ATOM   5890 C CZ  . PHE C 1 26  ? 72.948 13.592  44.261  1.00 19.70 ? 26  PHE C CZ  1 
ATOM   5891 N N   . LYS C 1 27  ? 70.377 17.425  44.459  1.00 29.63 ? 27  LYS C N   1 
ATOM   5892 C CA  . LYS C 1 27  ? 70.455 18.016  43.138  1.00 31.76 ? 27  LYS C CA  1 
ATOM   5893 C C   . LYS C 1 27  ? 71.878 17.858  42.649  1.00 30.38 ? 27  LYS C C   1 
ATOM   5894 O O   . LYS C 1 27  ? 72.820 17.878  43.437  1.00 25.84 ? 27  LYS C O   1 
ATOM   5895 C CB  . LYS C 1 27  ? 70.098 19.506  43.205  1.00 38.62 ? 27  LYS C CB  1 
ATOM   5896 C CG  . LYS C 1 27  ? 70.276 20.238  41.907  1.00 44.51 ? 27  LYS C CG  1 
ATOM   5897 C CD  . LYS C 1 27  ? 70.124 21.733  42.087  1.00 56.41 ? 27  LYS C CD  1 
ATOM   5898 C CE  . LYS C 1 27  ? 70.282 22.427  40.733  1.00 69.15 ? 27  LYS C CE  1 
ATOM   5899 N NZ  . LYS C 1 27  ? 70.164 23.916  40.786  1.00 74.87 ? 27  LYS C NZ  1 
ATOM   5900 N N   . ASN C 1 28  ? 72.022 17.594  41.361  1.00 27.36 ? 28  ASN C N   1 
ATOM   5901 C CA  . ASN C 1 28  ? 73.328 17.455  40.765  1.00 25.89 ? 28  ASN C CA  1 
ATOM   5902 C C   . ASN C 1 28  ? 73.148 17.488  39.262  1.00 26.73 ? 28  ASN C C   1 
ATOM   5903 O O   . ASN C 1 28  ? 72.040 17.720  38.762  1.00 25.41 ? 28  ASN C O   1 
ATOM   5904 C CB  . ASN C 1 28  ? 74.116 16.209  41.284  1.00 25.00 ? 28  ASN C CB  1 
ATOM   5905 C CG  . ASN C 1 28  ? 73.670 14.870  40.673  1.00 26.77 ? 28  ASN C CG  1 
ATOM   5906 O OD1 . ASN C 1 28  ? 72.881 14.803  39.739  1.00 27.65 ? 28  ASN C OD1 1 
ATOM   5907 N ND2 . ASN C 1 28  ? 74.225 13.793  41.200  1.00 32.53 ? 28  ASN C ND2 1 
ATOM   5908 N N   . GLN C 1 29  ? 74.256 17.335  38.556  1.00 27.13 ? 29  GLN C N   1 
ATOM   5909 C CA  . GLN C 1 29  ? 74.270 17.363  37.107  1.00 31.58 ? 29  GLN C CA  1 
ATOM   5910 C C   . GLN C 1 29  ? 73.229 16.438  36.486  1.00 31.15 ? 29  GLN C C   1 
ATOM   5911 O O   . GLN C 1 29  ? 72.627 16.776  35.471  1.00 33.81 ? 29  GLN C O   1 
ATOM   5912 C CB  . GLN C 1 29  ? 75.675 17.018  36.597  1.00 32.21 ? 29  GLN C CB  1 
ATOM   5913 C CG  . GLN C 1 29  ? 76.598 16.407  37.667  1.00 39.99 ? 29  GLN C CG  1 
ATOM   5914 C CD  . GLN C 1 29  ? 77.613 15.441  37.097  1.00 46.81 ? 29  GLN C CD  1 
ATOM   5915 O OE1 . GLN C 1 29  ? 77.561 15.090  35.914  1.00 54.59 ? 29  GLN C OE1 1 
ATOM   5916 N NE2 . GLN C 1 29  ? 78.549 15.007  37.930  1.00 45.12 ? 29  GLN C NE2 1 
ATOM   5917 N N   . TYR C 1 30  ? 72.958 15.317  37.144  1.00 29.52 ? 30  TYR C N   1 
ATOM   5918 C CA  . TYR C 1 30  ? 72.012 14.340  36.625  1.00 28.80 ? 30  TYR C CA  1 
ATOM   5919 C C   . TYR C 1 30  ? 70.516 14.492  36.910  1.00 31.72 ? 30  TYR C C   1 
ATOM   5920 O O   . TYR C 1 30  ? 69.696 13.970  36.151  1.00 34.22 ? 30  TYR C O   1 
ATOM   5921 C CB  . TYR C 1 30  ? 72.493 12.950  36.995  1.00 27.73 ? 30  TYR C CB  1 
ATOM   5922 C CG  . TYR C 1 30  ? 73.843 12.662  36.398  1.00 34.22 ? 30  TYR C CG  1 
ATOM   5923 C CD1 . TYR C 1 30  ? 73.962 12.346  35.057  1.00 38.88 ? 30  TYR C CD1 1 
ATOM   5924 C CD2 . TYR C 1 30  ? 75.001 12.726  37.162  1.00 31.23 ? 30  TYR C CD2 1 
ATOM   5925 C CE1 . TYR C 1 30  ? 75.188 12.096  34.483  1.00 39.10 ? 30  TYR C CE1 1 
ATOM   5926 C CE2 . TYR C 1 30  ? 76.239 12.475  36.598  1.00 35.08 ? 30  TYR C CE2 1 
ATOM   5927 C CZ  . TYR C 1 30  ? 76.322 12.155  35.248  1.00 39.31 ? 30  TYR C CZ  1 
ATOM   5928 O OH  . TYR C 1 30  ? 77.528 11.853  34.652  1.00 41.53 ? 30  TYR C OH  1 
ATOM   5929 N N   . GLY C 1 31  ? 70.148 15.180  37.989  1.00 32.35 ? 31  GLY C N   1 
ATOM   5930 C CA  . GLY C 1 31  ? 68.739 15.362  38.301  1.00 31.72 ? 31  GLY C CA  1 
ATOM   5931 C C   . GLY C 1 31  ? 68.555 16.018  39.652  1.00 34.89 ? 31  GLY C C   1 
ATOM   5932 O O   . GLY C 1 31  ? 69.504 16.606  40.186  1.00 36.99 ? 31  GLY C O   1 
ATOM   5933 N N   . HIS C 1 32  ? 67.347 15.938  40.210  1.00 33.40 ? 32  HIS C N   1 
ATOM   5934 C CA  . HIS C 1 32  ? 67.070 16.524  41.526  1.00 31.32 ? 32  HIS C CA  1 
ATOM   5935 C C   . HIS C 1 32  ? 65.776 16.000  42.127  1.00 31.83 ? 32  HIS C C   1 
ATOM   5936 O O   . HIS C 1 32  ? 64.876 15.558  41.391  1.00 23.60 ? 32  HIS C O   1 
ATOM   5937 C CB  . HIS C 1 32  ? 66.988 18.051  41.449  1.00 30.94 ? 32  HIS C CB  1 
ATOM   5938 C CG  . HIS C 1 32  ? 65.832 18.551  40.642  1.00 31.99 ? 32  HIS C CG  1 
ATOM   5939 N ND1 . HIS C 1 32  ? 65.904 18.726  39.277  1.00 30.58 ? 32  HIS C ND1 1 
ATOM   5940 C CD2 . HIS C 1 32  ? 64.570 18.884  40.999  1.00 32.27 ? 32  HIS C CD2 1 
ATOM   5941 C CE1 . HIS C 1 32  ? 64.734 19.142  38.828  1.00 32.52 ? 32  HIS C CE1 1 
ATOM   5942 N NE2 . HIS C 1 32  ? 63.907 19.246  39.851  1.00 33.46 ? 32  HIS C NE2 1 
ATOM   5943 N N   . ILE C 1 33  ? 65.681 16.134  43.457  1.00 33.56 ? 33  ILE C N   1 
ATOM   5944 C CA  . ILE C 1 33  ? 64.518 15.720  44.260  1.00 29.83 ? 33  ILE C CA  1 
ATOM   5945 C C   . ILE C 1 33  ? 64.115 16.915  45.140  1.00 26.67 ? 33  ILE C C   1 
ATOM   5946 O O   . ILE C 1 33  ? 64.948 17.462  45.844  1.00 23.55 ? 33  ILE C O   1 
ATOM   5947 C CB  . ILE C 1 33  ? 64.871 14.543  45.225  1.00 31.10 ? 33  ILE C CB  1 
ATOM   5948 C CG1 . ILE C 1 33  ? 65.700 13.467  44.515  1.00 31.60 ? 33  ILE C CG1 1 
ATOM   5949 C CG2 . ILE C 1 33  ? 63.614 13.903  45.754  1.00 26.24 ? 33  ILE C CG2 1 
ATOM   5950 C CD1 . ILE C 1 33  ? 66.360 12.477  45.480  1.00 25.89 ? 33  ILE C CD1 1 
ATOM   5951 N N   . ARG C 1 34  ? 62.865 17.344  45.047  1.00 27.45 ? 34  ARG C N   1 
ATOM   5952 C CA  . ARG C 1 34  ? 62.336 18.446  45.852  1.00 29.39 ? 34  ARG C CA  1 
ATOM   5953 C C   . ARG C 1 34  ? 61.122 17.957  46.650  1.00 29.14 ? 34  ARG C C   1 
ATOM   5954 O O   . ARG C 1 34  ? 60.409 17.039  46.230  1.00 30.92 ? 34  ARG C O   1 
ATOM   5955 C CB  . ARG C 1 34  ? 61.929 19.650  44.978  1.00 28.31 ? 34  ARG C CB  1 
ATOM   5956 C CG  . ARG C 1 34  ? 63.040 20.654  44.772  1.00 42.45 ? 34  ARG C CG  1 
ATOM   5957 C CD  . ARG C 1 34  ? 63.177 21.092  43.325  1.00 49.13 ? 34  ARG C CD  1 
ATOM   5958 N NE  . ARG C 1 34  ? 62.197 22.102  42.957  1.00 62.50 ? 34  ARG C NE  1 
ATOM   5959 C CZ  . ARG C 1 34  ? 61.876 22.410  41.704  1.00 69.98 ? 34  ARG C CZ  1 
ATOM   5960 N NH1 . ARG C 1 34  ? 62.461 21.774  40.691  1.00 72.03 ? 34  ARG C NH1 1 
ATOM   5961 N NH2 . ARG C 1 34  ? 60.952 23.336  41.462  1.00 71.97 ? 34  ARG C NH2 1 
ATOM   5962 N N   . VAL C 1 35  ? 60.897 18.582  47.797  1.00 28.10 ? 35  VAL C N   1 
ATOM   5963 C CA  . VAL C 1 35  ? 59.791 18.253  48.679  1.00 24.88 ? 35  VAL C CA  1 
ATOM   5964 C C   . VAL C 1 35  ? 58.996 19.554  48.906  1.00 25.06 ? 35  VAL C C   1 
ATOM   5965 O O   . VAL C 1 35  ? 59.609 20.601  49.129  1.00 25.58 ? 35  VAL C O   1 
ATOM   5966 C CB  . VAL C 1 35  ? 60.366 17.716  50.016  1.00 23.45 ? 35  VAL C CB  1 
ATOM   5967 C CG1 . VAL C 1 35  ? 59.257 17.237  50.957  1.00 19.65 ? 35  VAL C CG1 1 
ATOM   5968 C CG2 . VAL C 1 35  ? 61.325 16.580  49.723  1.00 24.40 ? 35  VAL C CG2 1 
ATOM   5969 N N   . LEU C 1 36  ? 57.664 19.517  48.760  1.00 23.99 ? 36  LEU C N   1 
ATOM   5970 C CA  . LEU C 1 36  ? 56.837 20.721  48.980  1.00 25.60 ? 36  LEU C CA  1 
ATOM   5971 C C   . LEU C 1 36  ? 56.667 21.029  50.493  1.00 27.56 ? 36  LEU C C   1 
ATOM   5972 O O   . LEU C 1 36  ? 56.720 20.130  51.347  1.00 26.79 ? 36  LEU C O   1 
ATOM   5973 C CB  . LEU C 1 36  ? 55.441 20.602  48.308  1.00 19.51 ? 36  LEU C CB  1 
ATOM   5974 C CG  . LEU C 1 36  ? 54.567 21.888  48.229  1.00 21.76 ? 36  LEU C CG  1 
ATOM   5975 C CD1 . LEU C 1 36  ? 55.055 22.827  47.146  1.00 17.54 ? 36  LEU C CD1 1 
ATOM   5976 C CD2 . LEU C 1 36  ? 53.081 21.586  48.014  1.00 11.67 ? 36  LEU C CD2 1 
ATOM   5977 N N   . GLN C 1 37  ? 56.530 22.310  50.825  1.00 26.22 ? 37  GLN C N   1 
ATOM   5978 C CA  . GLN C 1 37  ? 56.354 22.697  52.210  1.00 19.40 ? 37  GLN C CA  1 
ATOM   5979 C C   . GLN C 1 37  ? 55.028 22.108  52.717  1.00 21.85 ? 37  GLN C C   1 
ATOM   5980 O O   . GLN C 1 37  ? 54.134 21.832  51.916  1.00 16.49 ? 37  GLN C O   1 
ATOM   5981 C CB  . GLN C 1 37  ? 56.368 24.226  52.351  1.00 21.71 ? 37  GLN C CB  1 
ATOM   5982 C CG  . GLN C 1 37  ? 55.170 24.945  51.767  1.00 28.35 ? 37  GLN C CG  1 
ATOM   5983 C CD  . GLN C 1 37  ? 54.887 26.275  52.465  1.00 35.51 ? 37  GLN C CD  1 
ATOM   5984 O OE1 . GLN C 1 37  ? 54.370 26.290  53.584  1.00 42.77 ? 37  GLN C OE1 1 
ATOM   5985 N NE2 . GLN C 1 37  ? 55.236 27.393  51.819  1.00 34.86 ? 37  GLN C NE2 1 
ATOM   5986 N N   . ARG C 1 38  ? 54.902 21.928  54.039  1.00 19.71 ? 38  ARG C N   1 
ATOM   5987 C CA  . ARG C 1 38  ? 53.690 21.379  54.651  1.00 19.82 ? 38  ARG C CA  1 
ATOM   5988 C C   . ARG C 1 38  ? 52.467 22.199  54.319  1.00 24.84 ? 38  ARG C C   1 
ATOM   5989 O O   . ARG C 1 38  ? 52.519 23.432  54.339  1.00 23.24 ? 38  ARG C O   1 
ATOM   5990 C CB  . ARG C 1 38  ? 53.801 21.358  56.170  1.00 29.36 ? 38  ARG C CB  1 
ATOM   5991 C CG  . ARG C 1 38  ? 54.455 20.134  56.770  1.00 32.79 ? 38  ARG C CG  1 
ATOM   5992 C CD  . ARG C 1 38  ? 53.638 19.706  57.972  1.00 39.53 ? 38  ARG C CD  1 
ATOM   5993 N NE  . ARG C 1 38  ? 54.363 19.857  59.222  1.00 39.43 ? 38  ARG C NE  1 
ATOM   5994 C CZ  . ARG C 1 38  ? 53.807 19.775  60.425  1.00 39.63 ? 38  ARG C CZ  1 
ATOM   5995 N NH1 . ARG C 1 38  ? 52.500 19.579  60.563  1.00 38.15 ? 38  ARG C NH1 1 
ATOM   5996 N NH2 . ARG C 1 38  ? 54.562 19.918  61.496  1.00 43.89 ? 38  ARG C NH2 1 
ATOM   5997 N N   . PHE C 1 39  ? 51.349 21.518  54.079  1.00 25.19 ? 39  PHE C N   1 
ATOM   5998 C CA  . PHE C 1 39  ? 50.111 22.216  53.759  1.00 26.47 ? 39  PHE C CA  1 
ATOM   5999 C C   . PHE C 1 39  ? 49.633 23.050  54.933  1.00 26.74 ? 39  PHE C C   1 
ATOM   6000 O O   . PHE C 1 39  ? 49.364 24.246  54.775  1.00 27.92 ? 39  PHE C O   1 
ATOM   6001 C CB  . PHE C 1 39  ? 49.016 21.243  53.279  1.00 23.11 ? 39  PHE C CB  1 
ATOM   6002 C CG  . PHE C 1 39  ? 49.271 20.698  51.891  1.00 30.15 ? 39  PHE C CG  1 
ATOM   6003 C CD1 . PHE C 1 39  ? 49.102 21.509  50.769  1.00 29.45 ? 39  PHE C CD1 1 
ATOM   6004 C CD2 . PHE C 1 39  ? 49.722 19.390  51.709  1.00 27.79 ? 39  PHE C CD2 1 
ATOM   6005 C CE1 . PHE C 1 39  ? 49.382 21.027  49.488  1.00 28.34 ? 39  PHE C CE1 1 
ATOM   6006 C CE2 . PHE C 1 39  ? 50.002 18.898  50.439  1.00 25.52 ? 39  PHE C CE2 1 
ATOM   6007 C CZ  . PHE C 1 39  ? 49.832 19.723  49.322  1.00 26.10 ? 39  PHE C CZ  1 
ATOM   6008 N N   . ASP C 1 40  ? 49.573 22.436  56.111  1.00 24.87 ? 40  ASP C N   1 
ATOM   6009 C CA  . ASP C 1 40  ? 49.131 23.138  57.305  1.00 28.87 ? 40  ASP C CA  1 
ATOM   6010 C C   . ASP C 1 40  ? 50.079 24.258  57.752  1.00 29.95 ? 40  ASP C C   1 
ATOM   6011 O O   . ASP C 1 40  ? 49.635 25.265  58.297  1.00 33.89 ? 40  ASP C O   1 
ATOM   6012 C CB  . ASP C 1 40  ? 48.821 22.152  58.454  1.00 28.88 ? 40  ASP C CB  1 
ATOM   6013 C CG  . ASP C 1 40  ? 50.006 21.256  58.820  1.00 33.12 ? 40  ASP C CG  1 
ATOM   6014 O OD1 . ASP C 1 40  ? 50.582 20.608  57.923  1.00 38.61 ? 40  ASP C OD1 1 
ATOM   6015 O OD2 . ASP C 1 40  ? 50.353 21.181  60.021  1.00 40.52 ? 40  ASP C OD2 1 
ATOM   6016 N N   . GLN C 1 41  ? 51.372 24.126  57.480  1.00 30.32 ? 41  GLN C N   1 
ATOM   6017 C CA  . GLN C 1 41  ? 52.291 25.175  57.888  1.00 35.14 ? 41  GLN C CA  1 
ATOM   6018 C C   . GLN C 1 41  ? 52.035 26.469  57.132  1.00 32.32 ? 41  GLN C C   1 
ATOM   6019 O O   . GLN C 1 41  ? 52.419 27.532  57.577  1.00 37.66 ? 41  GLN C O   1 
ATOM   6020 C CB  . GLN C 1 41  ? 53.752 24.746  57.753  1.00 37.44 ? 41  GLN C CB  1 
ATOM   6021 C CG  . GLN C 1 41  ? 54.171 23.573  58.667  1.00 49.48 ? 41  GLN C CG  1 
ATOM   6022 C CD  . GLN C 1 41  ? 53.414 23.496  59.998  1.00 55.86 ? 41  GLN C CD  1 
ATOM   6023 O OE1 . GLN C 1 41  ? 52.644 22.561  60.230  1.00 60.84 ? 41  GLN C OE1 1 
ATOM   6024 N NE2 . GLN C 1 41  ? 53.647 24.461  60.877  1.00 59.94 ? 41  GLN C NE2 1 
ATOM   6025 N N   . GLN C 1 42  ? 51.397 26.384  55.982  1.00 29.06 ? 42  GLN C N   1 
ATOM   6026 C CA  . GLN C 1 42  ? 51.090 27.583  55.234  1.00 31.86 ? 42  GLN C CA  1 
ATOM   6027 C C   . GLN C 1 42  ? 49.852 28.238  55.844  1.00 33.05 ? 42  GLN C C   1 
ATOM   6028 O O   . GLN C 1 42  ? 49.891 29.413  56.215  1.00 37.11 ? 42  GLN C O   1 
ATOM   6029 C CB  . GLN C 1 42  ? 50.838 27.267  53.757  1.00 30.91 ? 42  GLN C CB  1 
ATOM   6030 C CG  . GLN C 1 42  ? 50.107 28.381  53.031  1.00 34.30 ? 42  GLN C CG  1 
ATOM   6031 C CD  . GLN C 1 42  ? 50.506 28.497  51.583  1.00 41.51 ? 42  GLN C CD  1 
ATOM   6032 O OE1 . GLN C 1 42  ? 51.662 28.783  51.266  1.00 41.52 ? 42  GLN C OE1 1 
ATOM   6033 N NE2 . GLN C 1 42  ? 49.555 28.269  50.688  1.00 41.83 ? 42  GLN C NE2 1 
ATOM   6034 N N   . SER C 1 43  ? 48.759 27.478  55.937  1.00 32.89 ? 43  SER C N   1 
ATOM   6035 C CA  . SER C 1 43  ? 47.501 27.986  56.481  1.00 30.79 ? 43  SER C CA  1 
ATOM   6036 C C   . SER C 1 43  ? 46.764 26.997  57.352  1.00 32.12 ? 43  SER C C   1 
ATOM   6037 O O   . SER C 1 43  ? 46.628 25.829  57.018  1.00 33.16 ? 43  SER C O   1 
ATOM   6038 C CB  . SER C 1 43  ? 46.565 28.461  55.367  1.00 32.80 ? 43  SER C CB  1 
ATOM   6039 O OG  . SER C 1 43  ? 45.317 28.892  55.891  1.00 24.24 ? 43  SER C OG  1 
ATOM   6040 N N   . LYS C 1 44  ? 46.212 27.514  58.440  1.00 33.35 ? 44  LYS C N   1 
ATOM   6041 C CA  . LYS C 1 44  ? 45.468 26.713  59.387  1.00 34.31 ? 44  LYS C CA  1 
ATOM   6042 C C   . LYS C 1 44  ? 44.187 26.249  58.699  1.00 33.54 ? 44  LYS C C   1 
ATOM   6043 O O   . LYS C 1 44  ? 43.567 25.272  59.122  1.00 38.56 ? 44  LYS C O   1 
ATOM   6044 C CB  . LYS C 1 44  ? 45.137 27.552  60.620  1.00 31.70 ? 44  LYS C CB  1 
ATOM   6045 C CG  . LYS C 1 44  ? 45.162 26.801  61.931  1.00 39.00 ? 44  LYS C CG  1 
ATOM   6046 C CD  . LYS C 1 44  ? 46.592 26.562  62.432  1.00 47.54 ? 44  LYS C CD  1 
ATOM   6047 C CE  . LYS C 1 44  ? 46.696 26.709  63.974  1.00 52.55 ? 44  LYS C CE  1 
ATOM   6048 N NZ  . LYS C 1 44  ? 46.498 28.111  64.530  1.00 48.33 ? 44  LYS C NZ  1 
ATOM   6049 N N   . ARG C 1 45  ? 43.780 26.954  57.647  1.00 30.75 ? 45  ARG C N   1 
ATOM   6050 C CA  . ARG C 1 45  ? 42.579 26.573  56.923  1.00 28.15 ? 45  ARG C CA  1 
ATOM   6051 C C   . ARG C 1 45  ? 42.824 25.195  56.321  1.00 31.02 ? 45  ARG C C   1 
ATOM   6052 O O   . ARG C 1 45  ? 41.897 24.397  56.221  1.00 35.43 ? 45  ARG C O   1 
ATOM   6053 C CB  . ARG C 1 45  ? 42.277 27.541  55.779  1.00 27.18 ? 45  ARG C CB  1 
ATOM   6054 C CG  . ARG C 1 45  ? 42.029 28.992  56.148  1.00 32.97 ? 45  ARG C CG  1 
ATOM   6055 C CD  . ARG C 1 45  ? 41.714 29.794  54.890  1.00 33.92 ? 45  ARG C CD  1 
ATOM   6056 N NE  . ARG C 1 45  ? 41.378 31.199  55.121  1.00 31.53 ? 45  ARG C NE  1 
ATOM   6057 C CZ  . ARG C 1 45  ? 40.278 31.797  54.650  1.00 40.97 ? 45  ARG C CZ  1 
ATOM   6058 N NH1 . ARG C 1 45  ? 39.364 31.110  53.965  1.00 39.77 ? 45  ARG C NH1 1 
ATOM   6059 N NH2 . ARG C 1 45  ? 40.065 33.086  54.897  1.00 43.28 ? 45  ARG C NH2 1 
ATOM   6060 N N   . LEU C 1 46  ? 44.070 24.926  55.917  1.00 32.38 ? 46  LEU C N   1 
ATOM   6061 C CA  . LEU C 1 46  ? 44.460 23.641  55.294  1.00 30.90 ? 46  LEU C CA  1 
ATOM   6062 C C   . LEU C 1 46  ? 44.798 22.560  56.312  1.00 28.56 ? 46  LEU C C   1 
ATOM   6063 O O   . LEU C 1 46  ? 45.734 21.781  56.130  1.00 26.69 ? 46  LEU C O   1 
ATOM   6064 C CB  . LEU C 1 46  ? 45.659 23.841  54.352  1.00 29.83 ? 46  LEU C CB  1 
ATOM   6065 C CG  . LEU C 1 46  ? 45.443 24.590  53.031  1.00 34.72 ? 46  LEU C CG  1 
ATOM   6066 C CD1 . LEU C 1 46  ? 45.292 26.073  53.259  1.00 34.69 ? 46  LEU C CD1 1 
ATOM   6067 C CD2 . LEU C 1 46  ? 46.651 24.359  52.174  1.00 38.30 ? 46  LEU C CD2 1 
ATOM   6068 N N   . GLN C 1 47  ? 43.996 22.486  57.362  1.00 32.52 ? 47  GLN C N   1 
ATOM   6069 C CA  . GLN C 1 47  ? 44.220 21.538  58.437  1.00 30.07 ? 47  GLN C CA  1 
ATOM   6070 C C   . GLN C 1 47  ? 44.149 20.080  58.030  1.00 27.92 ? 47  GLN C C   1 
ATOM   6071 O O   . GLN C 1 47  ? 45.043 19.320  58.373  1.00 32.28 ? 47  GLN C O   1 
ATOM   6072 C CB  . GLN C 1 47  ? 43.245 21.809  59.583  1.00 34.89 ? 47  GLN C CB  1 
ATOM   6073 C CG  . GLN C 1 47  ? 43.653 21.184  60.910  1.00 43.85 ? 47  GLN C CG  1 
ATOM   6074 C CD  . GLN C 1 47  ? 42.578 21.318  61.989  1.00 51.66 ? 47  GLN C CD  1 
ATOM   6075 O OE1 . GLN C 1 47  ? 42.334 22.415  62.522  1.00 54.12 ? 47  GLN C OE1 1 
ATOM   6076 N NE2 . GLN C 1 47  ? 41.929 20.197  62.317  1.00 51.17 ? 47  GLN C NE2 1 
ATOM   6077 N N   . ASN C 1 48  ? 43.137 19.695  57.254  1.00 29.00 ? 48  ASN C N   1 
ATOM   6078 C CA  . ASN C 1 48  ? 42.970 18.291  56.868  1.00 28.95 ? 48  ASN C CA  1 
ATOM   6079 C C   . ASN C 1 48  ? 43.928 17.672  55.867  1.00 31.87 ? 48  ASN C C   1 
ATOM   6080 O O   . ASN C 1 48  ? 43.691 16.565  55.365  1.00 36.12 ? 48  ASN C O   1 
ATOM   6081 C CB  . ASN C 1 48  ? 41.527 17.991  56.493  1.00 27.41 ? 48  ASN C CB  1 
ATOM   6082 C CG  . ASN C 1 48  ? 40.602 18.063  57.696  1.00 30.48 ? 48  ASN C CG  1 
ATOM   6083 O OD1 . ASN C 1 48  ? 41.025 18.429  58.797  1.00 28.68 ? 48  ASN C OD1 1 
ATOM   6084 N ND2 . ASN C 1 48  ? 39.335 17.746  57.492  1.00 34.71 ? 48  ASN C ND2 1 
ATOM   6085 N N   . LEU C 1 49  ? 45.029 18.372  55.607  1.00 28.15 ? 49  LEU C N   1 
ATOM   6086 C CA  . LEU C 1 49  ? 46.059 17.888  54.706  1.00 20.80 ? 49  LEU C CA  1 
ATOM   6087 C C   . LEU C 1 49  ? 47.317 17.785  55.522  1.00 18.42 ? 49  LEU C C   1 
ATOM   6088 O O   . LEU C 1 49  ? 48.404 17.687  54.965  1.00 15.98 ? 49  LEU C O   1 
ATOM   6089 C CB  . LEU C 1 49  ? 46.294 18.870  53.543  1.00 15.73 ? 49  LEU C CB  1 
ATOM   6090 C CG  . LEU C 1 49  ? 45.155 19.042  52.532  1.00 13.85 ? 49  LEU C CG  1 
ATOM   6091 C CD1 . LEU C 1 49  ? 45.524 20.104  51.589  1.00 10.17 ? 49  LEU C CD1 1 
ATOM   6092 C CD2 . LEU C 1 49  ? 44.839 17.771  51.783  1.00 15.96 ? 49  LEU C CD2 1 
ATOM   6093 N N   . GLU C 1 50  ? 47.189 17.795  56.850  1.00 19.14 ? 50  GLU C N   1 
ATOM   6094 C CA  . GLU C 1 50  ? 48.382 17.720  57.675  1.00 18.82 ? 50  GLU C CA  1 
ATOM   6095 C C   . GLU C 1 50  ? 49.225 16.507  57.300  1.00 18.51 ? 50  GLU C C   1 
ATOM   6096 O O   . GLU C 1 50  ? 50.449 16.594  57.182  1.00 12.23 ? 50  GLU C O   1 
ATOM   6097 C CB  . GLU C 1 50  ? 48.043 17.686  59.175  1.00 27.02 ? 50  GLU C CB  1 
ATOM   6098 C CG  . GLU C 1 50  ? 49.301 17.503  60.051  1.00 35.84 ? 50  GLU C CG  1 
ATOM   6099 C CD  . GLU C 1 50  ? 49.036 17.595  61.552  1.00 41.35 ? 50  GLU C CD  1 
ATOM   6100 O OE1 . GLU C 1 50  ? 47.885 17.307  61.976  1.00 46.03 ? 50  GLU C OE1 1 
ATOM   6101 O OE2 . GLU C 1 50  ? 49.986 17.951  62.300  1.00 38.58 ? 50  GLU C OE2 1 
ATOM   6102 N N   . ASP C 1 51  ? 48.551 15.397  57.030  1.00 26.16 ? 51  ASP C N   1 
ATOM   6103 C CA  . ASP C 1 51  ? 49.239 14.153  56.697  1.00 29.76 ? 51  ASP C CA  1 
ATOM   6104 C C   . ASP C 1 51  ? 49.496 13.800  55.232  1.00 27.66 ? 51  ASP C C   1 
ATOM   6105 O O   . ASP C 1 51  ? 49.681 12.634  54.919  1.00 28.32 ? 51  ASP C O   1 
ATOM   6106 C CB  . ASP C 1 51  ? 48.561 12.983  57.407  1.00 42.71 ? 51  ASP C CB  1 
ATOM   6107 C CG  . ASP C 1 51  ? 47.039 13.079  57.394  1.00 54.06 ? 51  ASP C CG  1 
ATOM   6108 O OD1 . ASP C 1 51  ? 46.455 13.532  56.375  1.00 57.70 ? 51  ASP C OD1 1 
ATOM   6109 O OD2 . ASP C 1 51  ? 46.433 12.699  58.425  1.00 58.53 ? 51  ASP C OD2 1 
ATOM   6110 N N   . TYR C 1 52  ? 49.531 14.797  54.352  1.00 26.55 ? 52  TYR C N   1 
ATOM   6111 C CA  . TYR C 1 52  ? 49.800 14.579  52.920  1.00 25.08 ? 52  TYR C CA  1 
ATOM   6112 C C   . TYR C 1 52  ? 50.936 15.479  52.385  1.00 26.20 ? 52  TYR C C   1 
ATOM   6113 O O   . TYR C 1 52  ? 51.062 16.640  52.774  1.00 28.71 ? 52  TYR C O   1 
ATOM   6114 C CB  . TYR C 1 52  ? 48.532 14.797  52.104  1.00 20.63 ? 52  TYR C CB  1 
ATOM   6115 C CG  . TYR C 1 52  ? 47.515 13.704  52.294  1.00 22.39 ? 52  TYR C CG  1 
ATOM   6116 C CD1 . TYR C 1 52  ? 47.653 12.497  51.636  1.00 20.34 ? 52  TYR C CD1 1 
ATOM   6117 C CD2 . TYR C 1 52  ? 46.392 13.894  53.106  1.00 25.24 ? 52  TYR C CD2 1 
ATOM   6118 C CE1 . TYR C 1 52  ? 46.709 11.514  51.756  1.00 20.77 ? 52  TYR C CE1 1 
ATOM   6119 C CE2 . TYR C 1 52  ? 45.432 12.905  53.240  1.00 22.47 ? 52  TYR C CE2 1 
ATOM   6120 C CZ  . TYR C 1 52  ? 45.594 11.714  52.547  1.00 25.32 ? 52  TYR C CZ  1 
ATOM   6121 O OH  . TYR C 1 52  ? 44.604 10.739  52.567  1.00 39.66 ? 52  TYR C OH  1 
ATOM   6122 N N   . ARG C 1 53  ? 51.741 14.954  51.468  1.00 27.01 ? 53  ARG C N   1 
ATOM   6123 C CA  . ARG C 1 53  ? 52.863 15.712  50.925  1.00 24.59 ? 53  ARG C CA  1 
ATOM   6124 C C   . ARG C 1 53  ? 53.082 15.480  49.444  1.00 23.93 ? 53  ARG C C   1 
ATOM   6125 O O   . ARG C 1 53  ? 52.551 14.528  48.880  1.00 26.45 ? 53  ARG C O   1 
ATOM   6126 C CB  . ARG C 1 53  ? 54.136 15.300  51.660  1.00 28.73 ? 53  ARG C CB  1 
ATOM   6127 C CG  . ARG C 1 53  ? 54.269 15.803  53.090  1.00 25.32 ? 53  ARG C CG  1 
ATOM   6128 C CD  . ARG C 1 53  ? 54.647 17.287  53.142  1.00 24.88 ? 53  ARG C CD  1 
ATOM   6129 N NE  . ARG C 1 53  ? 55.597 17.507  54.211  1.00 19.00 ? 53  ARG C NE  1 
ATOM   6130 C CZ  . ARG C 1 53  ? 56.813 17.983  54.029  1.00 24.81 ? 53  ARG C CZ  1 
ATOM   6131 N NH1 . ARG C 1 53  ? 57.208 18.318  52.813  1.00 35.21 ? 53  ARG C NH1 1 
ATOM   6132 N NH2 . ARG C 1 53  ? 57.673 18.010  55.038  1.00 27.79 ? 53  ARG C NH2 1 
ATOM   6133 N N   . LEU C 1 54  ? 53.856 16.358  48.814  1.00 24.66 ? 54  LEU C N   1 
ATOM   6134 C CA  . LEU C 1 54  ? 54.181 16.205  47.397  1.00 25.81 ? 54  LEU C CA  1 
ATOM   6135 C C   . LEU C 1 54  ? 55.689 16.164  47.216  1.00 24.80 ? 54  LEU C C   1 
ATOM   6136 O O   . LEU C 1 54  ? 56.421 16.925  47.843  1.00 31.49 ? 54  LEU C O   1 
ATOM   6137 C CB  . LEU C 1 54  ? 53.633 17.361  46.538  1.00 16.86 ? 54  LEU C CB  1 
ATOM   6138 C CG  . LEU C 1 54  ? 52.133 17.664  46.370  1.00 25.34 ? 54  LEU C CG  1 
ATOM   6139 C CD1 . LEU C 1 54  ? 52.016 18.837  45.409  1.00 26.62 ? 54  LEU C CD1 1 
ATOM   6140 C CD2 . LEU C 1 54  ? 51.296 16.475  45.865  1.00 22.71 ? 54  LEU C CD2 1 
ATOM   6141 N N   . VAL C 1 55  ? 56.154 15.252  46.378  1.00 28.35 ? 55  VAL C N   1 
ATOM   6142 C CA  . VAL C 1 55  ? 57.574 15.152  46.071  1.00 26.44 ? 55  VAL C CA  1 
ATOM   6143 C C   . VAL C 1 55  ? 57.689 15.243  44.550  1.00 25.94 ? 55  VAL C C   1 
ATOM   6144 O O   . VAL C 1 55  ? 56.868 14.692  43.822  1.00 23.72 ? 55  VAL C O   1 
ATOM   6145 C CB  . VAL C 1 55  ? 58.219 13.841  46.567  1.00 25.74 ? 55  VAL C CB  1 
ATOM   6146 C CG1 . VAL C 1 55  ? 59.696 13.837  46.189  1.00 26.22 ? 55  VAL C CG1 1 
ATOM   6147 C CG2 . VAL C 1 55  ? 58.059 13.692  48.082  1.00 24.89 ? 55  VAL C CG2 1 
ATOM   6148 N N   . GLU C 1 56  ? 58.714 15.935  44.083  1.00 26.42 ? 56  GLU C N   1 
ATOM   6149 C CA  . GLU C 1 56  ? 58.928 16.143  42.667  1.00 26.66 ? 56  GLU C CA  1 
ATOM   6150 C C   . GLU C 1 56  ? 60.337 15.655  42.366  1.00 29.06 ? 56  GLU C C   1 
ATOM   6151 O O   . GLU C 1 56  ? 61.276 15.928  43.120  1.00 30.18 ? 56  GLU C O   1 
ATOM   6152 C CB  . GLU C 1 56  ? 58.754 17.642  42.376  1.00 29.33 ? 56  GLU C CB  1 
ATOM   6153 C CG  . GLU C 1 56  ? 59.170 18.125  40.994  1.00 30.97 ? 56  GLU C CG  1 
ATOM   6154 C CD  . GLU C 1 56  ? 60.508 18.817  41.020  1.00 28.74 ? 56  GLU C CD  1 
ATOM   6155 O OE1 . GLU C 1 56  ? 60.598 19.915  41.588  1.00 33.29 ? 56  GLU C OE1 1 
ATOM   6156 O OE2 . GLU C 1 56  ? 61.483 18.248  40.499  1.00 40.66 ? 56  GLU C OE2 1 
ATOM   6157 N N   . PHE C 1 57  ? 60.490 14.936  41.263  1.00 28.21 ? 57  PHE C N   1 
ATOM   6158 C CA  . PHE C 1 57  ? 61.782 14.384  40.895  1.00 26.97 ? 57  PHE C CA  1 
ATOM   6159 C C   . PHE C 1 57  ? 62.044 14.521  39.406  1.00 31.05 ? 57  PHE C C   1 
ATOM   6160 O O   . PHE C 1 57  ? 61.102 14.502  38.604  1.00 32.47 ? 57  PHE C O   1 
ATOM   6161 C CB  . PHE C 1 57  ? 61.809 12.919  41.313  1.00 28.72 ? 57  PHE C CB  1 
ATOM   6162 C CG  . PHE C 1 57  ? 62.834 12.096  40.613  1.00 25.11 ? 57  PHE C CG  1 
ATOM   6163 C CD1 . PHE C 1 57  ? 64.132 12.024  41.096  1.00 23.78 ? 57  PHE C CD1 1 
ATOM   6164 C CD2 . PHE C 1 57  ? 62.491 11.352  39.497  1.00 23.64 ? 57  PHE C CD2 1 
ATOM   6165 C CE1 . PHE C 1 57  ? 65.078 11.212  40.478  1.00 28.00 ? 57  PHE C CE1 1 
ATOM   6166 C CE2 . PHE C 1 57  ? 63.426 10.543  38.878  1.00 24.18 ? 57  PHE C CE2 1 
ATOM   6167 C CZ  . PHE C 1 57  ? 64.722 10.472  39.370  1.00 26.92 ? 57  PHE C CZ  1 
ATOM   6168 N N   . ARG C 1 58  ? 63.319 14.669  39.044  1.00 32.74 ? 58  ARG C N   1 
ATOM   6169 C CA  . ARG C 1 58  ? 63.709 14.791  37.635  1.00 34.87 ? 58  ARG C CA  1 
ATOM   6170 C C   . ARG C 1 58  ? 65.007 14.030  37.360  1.00 35.88 ? 58  ARG C C   1 
ATOM   6171 O O   . ARG C 1 58  ? 65.864 13.921  38.250  1.00 37.40 ? 58  ARG C O   1 
ATOM   6172 C CB  . ARG C 1 58  ? 63.824 16.261  37.200  1.00 30.51 ? 58  ARG C CB  1 
ATOM   6173 C CG  . ARG C 1 58  ? 63.871 16.432  35.686  1.00 24.72 ? 58  ARG C CG  1 
ATOM   6174 C CD  . ARG C 1 58  ? 63.613 17.847  35.248  1.00 26.63 ? 58  ARG C CD  1 
ATOM   6175 N NE  . ARG C 1 58  ? 63.650 17.941  33.790  1.00 37.56 ? 58  ARG C NE  1 
ATOM   6176 C CZ  . ARG C 1 58  ? 63.045 18.878  33.060  1.00 41.90 ? 58  ARG C CZ  1 
ATOM   6177 N NH1 . ARG C 1 58  ? 62.354 19.860  33.627  1.00 41.47 ? 58  ARG C NH1 1 
ATOM   6178 N NH2 . ARG C 1 58  ? 63.156 18.843  31.740  1.00 45.44 ? 58  ARG C NH2 1 
ATOM   6179 N N   . SER C 1 59  ? 65.123 13.490  36.139  1.00 36.15 ? 59  SER C N   1 
ATOM   6180 C CA  . SER C 1 59  ? 66.285 12.703  35.699  1.00 31.02 ? 59  SER C CA  1 
ATOM   6181 C C   . SER C 1 59  ? 66.686 13.002  34.263  1.00 29.18 ? 59  SER C C   1 
ATOM   6182 O O   . SER C 1 59  ? 65.819 13.295  33.437  1.00 28.72 ? 59  SER C O   1 
ATOM   6183 C CB  . SER C 1 59  ? 65.932 11.220  35.759  1.00 23.46 ? 59  SER C CB  1 
ATOM   6184 O OG  . SER C 1 59  ? 66.925 10.510  36.440  1.00 24.57 ? 59  SER C OG  1 
ATOM   6185 N N   . LYS C 1 60  ? 67.995 12.970  33.991  1.00 28.13 ? 60  LYS C N   1 
ATOM   6186 C CA  . LYS C 1 60  ? 68.538 13.157  32.640  1.00 30.91 ? 60  LYS C CA  1 
ATOM   6187 C C   . LYS C 1 60  ? 68.437 11.790  31.927  1.00 31.04 ? 60  LYS C C   1 
ATOM   6188 O O   . LYS C 1 60  ? 68.289 10.751  32.583  1.00 31.12 ? 60  LYS C O   1 
ATOM   6189 C CB  . LYS C 1 60  ? 70.016 13.561  32.691  1.00 36.01 ? 60  LYS C CB  1 
ATOM   6190 C CG  . LYS C 1 60  ? 70.331 15.012  33.043  1.00 40.89 ? 60  LYS C CG  1 
ATOM   6191 C CD  . LYS C 1 60  ? 70.095 15.947  31.878  1.00 44.87 ? 60  LYS C CD  1 
ATOM   6192 C CE  . LYS C 1 60  ? 68.690 16.518  31.925  1.00 52.51 ? 60  LYS C CE  1 
ATOM   6193 N NZ  . LYS C 1 60  ? 68.372 17.328  30.716  1.00 57.74 ? 60  LYS C NZ  1 
ATOM   6194 N N   . PRO C 1 61  ? 68.491 11.769  30.580  1.00 31.51 ? 61  PRO C N   1 
ATOM   6195 C CA  . PRO C 1 61  ? 68.394 10.454  29.926  1.00 30.26 ? 61  PRO C CA  1 
ATOM   6196 C C   . PRO C 1 61  ? 69.450 9.465   30.429  1.00 28.43 ? 61  PRO C C   1 
ATOM   6197 O O   . PRO C 1 61  ? 70.539 9.860   30.809  1.00 33.54 ? 61  PRO C O   1 
ATOM   6198 C CB  . PRO C 1 61  ? 68.534 10.785  28.431  1.00 27.95 ? 61  PRO C CB  1 
ATOM   6199 C CG  . PRO C 1 61  ? 69.086 12.202  28.405  1.00 32.08 ? 61  PRO C CG  1 
ATOM   6200 C CD  . PRO C 1 61  ? 68.479 12.863  29.591  1.00 28.24 ? 61  PRO C CD  1 
ATOM   6201 N N   . GLU C 1 62  ? 69.089 8.192   30.514  1.00 30.35 ? 62  GLU C N   1 
ATOM   6202 C CA  . GLU C 1 62  ? 69.988 7.134   30.986  1.00 30.26 ? 62  GLU C CA  1 
ATOM   6203 C C   . GLU C 1 62  ? 70.663 7.325   32.349  1.00 31.30 ? 62  GLU C C   1 
ATOM   6204 O O   . GLU C 1 62  ? 71.884 7.256   32.467  1.00 32.12 ? 62  GLU C O   1 
ATOM   6205 C CB  . GLU C 1 62  ? 71.024 6.798   29.925  1.00 28.20 ? 62  GLU C CB  1 
ATOM   6206 C CG  . GLU C 1 62  ? 70.401 6.096   28.740  1.00 37.10 ? 62  GLU C CG  1 
ATOM   6207 C CD  . GLU C 1 62  ? 71.403 5.659   27.694  1.00 39.99 ? 62  GLU C CD  1 
ATOM   6208 O OE1 . GLU C 1 62  ? 72.605 5.974   27.840  1.00 41.08 ? 62  GLU C OE1 1 
ATOM   6209 O OE2 . GLU C 1 62  ? 70.970 4.997   26.719  1.00 42.03 ? 62  GLU C OE2 1 
ATOM   6210 N N   . THR C 1 63  ? 69.862 7.504   33.390  1.00 30.43 ? 63  THR C N   1 
ATOM   6211 C CA  . THR C 1 63  ? 70.390 7.668   34.739  1.00 30.08 ? 63  THR C CA  1 
ATOM   6212 C C   . THR C 1 63  ? 69.704 6.676   35.701  1.00 31.27 ? 63  THR C C   1 
ATOM   6213 O O   . THR C 1 63  ? 68.669 6.084   35.364  1.00 32.37 ? 63  THR C O   1 
ATOM   6214 C CB  . THR C 1 63  ? 70.228 9.128   35.224  1.00 27.25 ? 63  THR C CB  1 
ATOM   6215 O OG1 . THR C 1 63  ? 68.902 9.590   34.936  1.00 28.18 ? 63  THR C OG1 1 
ATOM   6216 C CG2 . THR C 1 63  ? 71.219 10.028  34.528  1.00 24.99 ? 63  THR C CG2 1 
ATOM   6217 N N   . LEU C 1 64  ? 70.334 6.442   36.853  1.00 30.02 ? 64  LEU C N   1 
ATOM   6218 C CA  . LEU C 1 64  ? 69.824 5.525   37.871  1.00 28.97 ? 64  LEU C CA  1 
ATOM   6219 C C   . LEU C 1 64  ? 69.754 6.264   39.197  1.00 31.00 ? 64  LEU C C   1 
ATOM   6220 O O   . LEU C 1 64  ? 70.642 7.071   39.486  1.00 30.67 ? 64  LEU C O   1 
ATOM   6221 C CB  . LEU C 1 64  ? 70.783 4.336   38.062  1.00 19.82 ? 64  LEU C CB  1 
ATOM   6222 C CG  . LEU C 1 64  ? 70.426 3.337   39.176  1.00 15.48 ? 64  LEU C CG  1 
ATOM   6223 C CD1 . LEU C 1 64  ? 69.461 2.293   38.701  1.00 18.60 ? 64  LEU C CD1 1 
ATOM   6224 C CD2 . LEU C 1 64  ? 71.638 2.649   39.680  1.00 23.26 ? 64  LEU C CD2 1 
ATOM   6225 N N   . LEU C 1 65  ? 68.712 5.969   39.986  1.00 31.32 ? 65  LEU C N   1 
ATOM   6226 C CA  . LEU C 1 65  ? 68.519 6.511   41.330  1.00 26.48 ? 65  LEU C CA  1 
ATOM   6227 C C   . LEU C 1 65  ? 68.739 5.308   42.257  1.00 24.57 ? 65  LEU C C   1 
ATOM   6228 O O   . LEU C 1 65  ? 68.004 4.330   42.191  1.00 24.86 ? 65  LEU C O   1 
ATOM   6229 C CB  . LEU C 1 65  ? 67.090 6.993   41.497  1.00 26.92 ? 65  LEU C CB  1 
ATOM   6230 C CG  . LEU C 1 65  ? 66.753 8.231   42.333  1.00 17.68 ? 65  LEU C CG  1 
ATOM   6231 C CD1 . LEU C 1 65  ? 65.323 8.142   42.754  1.00 12.15 ? 65  LEU C CD1 1 
ATOM   6232 C CD2 . LEU C 1 65  ? 67.626 8.419   43.511  1.00 19.69 ? 65  LEU C CD2 1 
ATOM   6233 N N   . LEU C 1 66  ? 69.774 5.372   43.084  1.00 29.22 ? 66  LEU C N   1 
ATOM   6234 C CA  . LEU C 1 66  ? 70.141 4.292   44.010  1.00 29.98 ? 66  LEU C CA  1 
ATOM   6235 C C   . LEU C 1 66  ? 69.039 3.856   44.995  1.00 28.38 ? 66  LEU C C   1 
ATOM   6236 O O   . LEU C 1 66  ? 68.193 4.665   45.393  1.00 31.10 ? 66  LEU C O   1 
ATOM   6237 C CB  . LEU C 1 66  ? 71.431 4.678   44.760  1.00 28.48 ? 66  LEU C CB  1 
ATOM   6238 C CG  . LEU C 1 66  ? 72.551 5.133   43.808  1.00 26.33 ? 66  LEU C CG  1 
ATOM   6239 C CD1 . LEU C 1 66  ? 73.744 5.657   44.575  1.00 19.58 ? 66  LEU C CD1 1 
ATOM   6240 C CD2 . LEU C 1 66  ? 72.949 4.014   42.854  1.00 15.48 ? 66  LEU C CD2 1 
ATOM   6241 N N   . PRO C 1 67  ? 69.062 2.571   45.429  1.00 26.76 ? 67  PRO C N   1 
ATOM   6242 C CA  . PRO C 1 67  ? 68.078 1.998   46.361  1.00 23.69 ? 67  PRO C CA  1 
ATOM   6243 C C   . PRO C 1 67  ? 67.823 2.763   47.625  1.00 18.82 ? 67  PRO C C   1 
ATOM   6244 O O   . PRO C 1 67  ? 68.738 3.271   48.259  1.00 15.74 ? 67  PRO C O   1 
ATOM   6245 C CB  . PRO C 1 67  ? 68.645 0.613   46.675  1.00 18.87 ? 67  PRO C CB  1 
ATOM   6246 C CG  . PRO C 1 67  ? 70.087 0.759   46.427  1.00 27.17 ? 67  PRO C CG  1 
ATOM   6247 C CD  . PRO C 1 67  ? 70.121 1.585   45.162  1.00 28.54 ? 67  PRO C CD  1 
ATOM   6248 N N   . GLN C 1 68  ? 66.567 2.740   48.033  1.00 19.71 ? 68  GLN C N   1 
ATOM   6249 C CA  . GLN C 1 68  ? 66.146 3.440   49.226  1.00 23.66 ? 68  GLN C CA  1 
ATOM   6250 C C   . GLN C 1 68  ? 64.746 2.989   49.638  1.00 23.62 ? 68  GLN C C   1 
ATOM   6251 O O   . GLN C 1 68  ? 63.950 2.517   48.815  1.00 26.95 ? 68  GLN C O   1 
ATOM   6252 C CB  . GLN C 1 68  ? 66.085 4.954   48.950  1.00 19.53 ? 68  GLN C CB  1 
ATOM   6253 C CG  . GLN C 1 68  ? 64.864 5.335   48.102  1.00 27.02 ? 68  GLN C CG  1 
ATOM   6254 C CD  . GLN C 1 68  ? 64.600 6.812   48.024  1.00 27.68 ? 68  GLN C CD  1 
ATOM   6255 O OE1 . GLN C 1 68  ? 64.317 7.329   46.951  1.00 27.82 ? 68  GLN C OE1 1 
ATOM   6256 N NE2 . GLN C 1 68  ? 64.642 7.498   49.168  1.00 27.34 ? 68  GLN C NE2 1 
ATOM   6257 N N   . GLN C 1 69  ? 64.457 3.150   50.922  1.00 25.35 ? 69  GLN C N   1 
ATOM   6258 C CA  . GLN C 1 69  ? 63.148 2.851   51.453  1.00 25.42 ? 69  GLN C CA  1 
ATOM   6259 C C   . GLN C 1 69  ? 62.740 4.162   52.152  1.00 26.41 ? 69  GLN C C   1 
ATOM   6260 O O   . GLN C 1 69  ? 63.605 4.915   52.621  1.00 27.02 ? 69  GLN C O   1 
ATOM   6261 C CB  . GLN C 1 69  ? 63.208 1.665   52.423  1.00 18.59 ? 69  GLN C CB  1 
ATOM   6262 C CG  . GLN C 1 69  ? 63.450 2.023   53.865  1.00 14.52 ? 69  GLN C CG  1 
ATOM   6263 C CD  . GLN C 1 69  ? 64.875 1.851   54.296  1.00 17.05 ? 69  GLN C CD  1 
ATOM   6264 O OE1 . GLN C 1 69  ? 65.219 2.155   55.430  1.00 19.49 ? 69  GLN C OE1 1 
ATOM   6265 N NE2 . GLN C 1 69  ? 65.711 1.345   53.412  1.00 22.09 ? 69  GLN C NE2 1 
ATOM   6266 N N   . ALA C 1 70  ? 61.454 4.499   52.101  1.00 27.68 ? 70  ALA C N   1 
ATOM   6267 C CA  . ALA C 1 70  ? 60.950 5.721   52.738  1.00 26.40 ? 70  ALA C CA  1 
ATOM   6268 C C   . ALA C 1 70  ? 59.822 5.335   53.690  1.00 25.51 ? 70  ALA C C   1 
ATOM   6269 O O   . ALA C 1 70  ? 59.200 4.286   53.527  1.00 20.45 ? 70  ALA C O   1 
ATOM   6270 C CB  . ALA C 1 70  ? 60.450 6.723   51.687  1.00 20.73 ? 70  ALA C CB  1 
ATOM   6271 N N   . ASP C 1 71  ? 59.567 6.179   54.684  1.00 26.40 ? 71  ASP C N   1 
ATOM   6272 C CA  . ASP C 1 71  ? 58.516 5.896   55.664  1.00 27.94 ? 71  ASP C CA  1 
ATOM   6273 C C   . ASP C 1 71  ? 57.169 6.521   55.291  1.00 27.95 ? 71  ASP C C   1 
ATOM   6274 O O   . ASP C 1 71  ? 56.424 6.965   56.160  1.00 35.64 ? 71  ASP C O   1 
ATOM   6275 C CB  . ASP C 1 71  ? 58.953 6.347   57.071  1.00 23.60 ? 71  ASP C CB  1 
ATOM   6276 C CG  . ASP C 1 71  ? 59.182 7.851   57.180  1.00 25.47 ? 71  ASP C CG  1 
ATOM   6277 O OD1 . ASP C 1 71  ? 59.372 8.520   56.136  1.00 17.66 ? 71  ASP C OD1 1 
ATOM   6278 O OD2 . ASP C 1 71  ? 59.176 8.364   58.320  1.00 19.57 ? 71  ASP C OD2 1 
ATOM   6279 N N   . ALA C 1 72  ? 56.841 6.502   54.007  1.00 24.20 ? 72  ALA C N   1 
ATOM   6280 C CA  . ALA C 1 72  ? 55.611 7.071   53.513  1.00 24.76 ? 72  ALA C CA  1 
ATOM   6281 C C   . ALA C 1 72  ? 55.067 6.171   52.415  1.00 26.86 ? 72  ALA C C   1 
ATOM   6282 O O   . ALA C 1 72  ? 55.842 5.536   51.709  1.00 27.35 ? 72  ALA C O   1 
ATOM   6283 C CB  . ALA C 1 72  ? 55.887 8.432   52.945  1.00 24.28 ? 72  ALA C CB  1 
ATOM   6284 N N   . GLU C 1 73  ? 53.745 6.078   52.291  1.00 25.18 ? 73  GLU C N   1 
ATOM   6285 C CA  . GLU C 1 73  ? 53.153 5.272   51.230  1.00 25.29 ? 73  GLU C CA  1 
ATOM   6286 C C   . GLU C 1 73  ? 53.135 6.236   50.059  1.00 25.49 ? 73  GLU C C   1 
ATOM   6287 O O   . GLU C 1 73  ? 52.615 7.346   50.178  1.00 23.68 ? 73  GLU C O   1 
ATOM   6288 C CB  . GLU C 1 73  ? 51.733 4.842   51.590  1.00 28.85 ? 73  GLU C CB  1 
ATOM   6289 C CG  . GLU C 1 73  ? 51.431 3.370   51.349  1.00 33.73 ? 73  GLU C CG  1 
ATOM   6290 C CD  . GLU C 1 73  ? 50.191 3.166   50.482  1.00 42.97 ? 73  GLU C CD  1 
ATOM   6291 O OE1 . GLU C 1 73  ? 49.086 3.560   50.931  1.00 41.96 ? 73  GLU C OE1 1 
ATOM   6292 O OE2 . GLU C 1 73  ? 50.317 2.614   49.354  1.00 44.52 ? 73  GLU C OE2 1 
ATOM   6293 N N   . LEU C 1 74  ? 53.745 5.831   48.952  1.00 24.27 ? 74  LEU C N   1 
ATOM   6294 C CA  . LEU C 1 74  ? 53.842 6.679   47.769  1.00 26.90 ? 74  LEU C CA  1 
ATOM   6295 C C   . LEU C 1 74  ? 52.962 6.343   46.572  1.00 29.23 ? 74  LEU C C   1 
ATOM   6296 O O   . LEU C 1 74  ? 52.776 5.169   46.229  1.00 29.02 ? 74  LEU C O   1 
ATOM   6297 C CB  . LEU C 1 74  ? 55.272 6.652   47.255  1.00 23.26 ? 74  LEU C CB  1 
ATOM   6298 C CG  . LEU C 1 74  ? 56.316 7.641   47.710  1.00 19.05 ? 74  LEU C CG  1 
ATOM   6299 C CD1 . LEU C 1 74  ? 55.778 8.481   48.806  1.00 19.91 ? 74  LEU C CD1 1 
ATOM   6300 C CD2 . LEU C 1 74  ? 57.567 6.870   48.128  1.00 20.92 ? 74  LEU C CD2 1 
ATOM   6301 N N   . LEU C 1 75  ? 52.459 7.390   45.919  1.00 30.11 ? 75  LEU C N   1 
ATOM   6302 C CA  . LEU C 1 75  ? 51.687 7.236   44.698  1.00 28.27 ? 75  LEU C CA  1 
ATOM   6303 C C   . LEU C 1 75  ? 52.441 8.055   43.674  1.00 25.50 ? 75  LEU C C   1 
ATOM   6304 O O   . LEU C 1 75  ? 52.367 9.294   43.654  1.00 23.87 ? 75  LEU C O   1 
ATOM   6305 C CB  . LEU C 1 75  ? 50.240 7.712   44.827  1.00 30.98 ? 75  LEU C CB  1 
ATOM   6306 C CG  . LEU C 1 75  ? 49.502 7.548   43.492  1.00 25.98 ? 75  LEU C CG  1 
ATOM   6307 C CD1 . LEU C 1 75  ? 49.598 6.127   42.974  1.00 27.20 ? 75  LEU C CD1 1 
ATOM   6308 C CD2 . LEU C 1 75  ? 48.078 7.993   43.613  1.00 28.57 ? 75  LEU C CD2 1 
ATOM   6309 N N   . LEU C 1 76  ? 53.218 7.320   42.882  1.00 27.31 ? 76  LEU C N   1 
ATOM   6310 C CA  . LEU C 1 76  ? 54.075 7.840   41.829  1.00 28.61 ? 76  LEU C CA  1 
ATOM   6311 C C   . LEU C 1 76  ? 53.325 8.050   40.501  1.00 28.55 ? 76  LEU C C   1 
ATOM   6312 O O   . LEU C 1 76  ? 52.596 7.166   40.022  1.00 27.21 ? 76  LEU C O   1 
ATOM   6313 C CB  . LEU C 1 76  ? 55.251 6.868   41.657  1.00 29.01 ? 76  LEU C CB  1 
ATOM   6314 C CG  . LEU C 1 76  ? 56.502 7.240   40.856  1.00 31.92 ? 76  LEU C CG  1 
ATOM   6315 C CD1 . LEU C 1 76  ? 57.656 6.350   41.299  1.00 24.18 ? 76  LEU C CD1 1 
ATOM   6316 C CD2 . LEU C 1 76  ? 56.251 7.118   39.348  1.00 28.80 ? 76  LEU C CD2 1 
ATOM   6317 N N   . VAL C 1 77  ? 53.513 9.231   39.915  1.00 29.44 ? 77  VAL C N   1 
ATOM   6318 C CA  . VAL C 1 77  ? 52.883 9.599   38.647  1.00 27.34 ? 77  VAL C CA  1 
ATOM   6319 C C   . VAL C 1 77  ? 53.901 10.235  37.698  1.00 29.54 ? 77  VAL C C   1 
ATOM   6320 O O   . VAL C 1 77  ? 54.565 11.211  38.052  1.00 33.38 ? 77  VAL C O   1 
ATOM   6321 C CB  . VAL C 1 77  ? 51.717 10.598  38.875  1.00 24.89 ? 77  VAL C CB  1 
ATOM   6322 C CG1 . VAL C 1 77  ? 51.241 11.185  37.568  1.00 21.92 ? 77  VAL C CG1 1 
ATOM   6323 C CG2 . VAL C 1 77  ? 50.575 9.901   39.564  1.00 27.00 ? 77  VAL C CG2 1 
ATOM   6324 N N   . VAL C 1 78  ? 54.024 9.668   36.502  1.00 27.05 ? 78  VAL C N   1 
ATOM   6325 C CA  . VAL C 1 78  ? 54.932 10.175  35.486  1.00 26.83 ? 78  VAL C CA  1 
ATOM   6326 C C   . VAL C 1 78  ? 54.261 11.316  34.694  1.00 29.73 ? 78  VAL C C   1 
ATOM   6327 O O   . VAL C 1 78  ? 53.225 11.110  34.023  1.00 27.42 ? 78  VAL C O   1 
ATOM   6328 C CB  . VAL C 1 78  ? 55.345 9.053   34.501  1.00 29.15 ? 78  VAL C CB  1 
ATOM   6329 C CG1 . VAL C 1 78  ? 56.338 9.593   33.447  1.00 24.90 ? 78  VAL C CG1 1 
ATOM   6330 C CG2 . VAL C 1 78  ? 55.929 7.866   35.265  1.00 18.11 ? 78  VAL C CG2 1 
ATOM   6331 N N   . ARG C 1 79  ? 54.847 12.511  34.793  1.00 27.28 ? 79  ARG C N   1 
ATOM   6332 C CA  . ARG C 1 79  ? 54.345 13.692  34.097  1.00 28.64 ? 79  ARG C CA  1 
ATOM   6333 C C   . ARG C 1 79  ? 55.005 13.928  32.727  1.00 32.22 ? 79  ARG C C   1 
ATOM   6334 O O   . ARG C 1 79  ? 54.735 14.947  32.078  1.00 36.51 ? 79  ARG C O   1 
ATOM   6335 C CB  . ARG C 1 79  ? 54.477 14.945  34.960  1.00 22.32 ? 79  ARG C CB  1 
ATOM   6336 C CG  . ARG C 1 79  ? 55.411 14.802  36.109  1.00 29.28 ? 79  ARG C CG  1 
ATOM   6337 C CD  . ARG C 1 79  ? 56.120 16.099  36.414  1.00 28.35 ? 79  ARG C CD  1 
ATOM   6338 N NE  . ARG C 1 79  ? 55.204 17.147  36.833  1.00 26.09 ? 79  ARG C NE  1 
ATOM   6339 C CZ  . ARG C 1 79  ? 55.542 18.180  37.600  1.00 18.94 ? 79  ARG C CZ  1 
ATOM   6340 N NH1 . ARG C 1 79  ? 56.787 18.319  38.087  1.00 2.00  ? 79  ARG C NH1 1 
ATOM   6341 N NH2 . ARG C 1 79  ? 54.601 19.058  37.906  1.00 15.20 ? 79  ARG C NH2 1 
ATOM   6342 N N   . SER C 1 80  ? 55.921 13.031  32.341  1.00 34.50 ? 80  SER C N   1 
ATOM   6343 C CA  . SER C 1 80  ? 56.631 13.048  31.045  1.00 29.74 ? 80  SER C CA  1 
ATOM   6344 C C   . SER C 1 80  ? 57.824 12.108  31.063  1.00 24.73 ? 80  SER C C   1 
ATOM   6345 O O   . SER C 1 80  ? 58.552 12.015  32.057  1.00 21.94 ? 80  SER C O   1 
ATOM   6346 C CB  . SER C 1 80  ? 57.085 14.451  30.609  1.00 31.66 ? 80  SER C CB  1 
ATOM   6347 O OG  . SER C 1 80  ? 58.360 14.783  31.126  1.00 44.57 ? 80  SER C OG  1 
ATOM   6348 N N   . GLY C 1 81  ? 58.005 11.403  29.954  1.00 21.33 ? 81  GLY C N   1 
ATOM   6349 C CA  . GLY C 1 81  ? 59.099 10.464  29.823  1.00 16.06 ? 81  GLY C CA  1 
ATOM   6350 C C   . GLY C 1 81  ? 58.713 9.035   30.149  1.00 16.57 ? 81  GLY C C   1 
ATOM   6351 O O   . GLY C 1 81  ? 57.523 8.678   30.223  1.00 13.50 ? 81  GLY C O   1 
ATOM   6352 N N   . SER C 1 82  ? 59.729 8.215   30.375  1.00 16.77 ? 82  SER C N   1 
ATOM   6353 C CA  . SER C 1 82  ? 59.503 6.810   30.679  1.00 21.41 ? 82  SER C CA  1 
ATOM   6354 C C   . SER C 1 82  ? 60.342 6.414   31.873  1.00 18.33 ? 82  SER C C   1 
ATOM   6355 O O   . SER C 1 82  ? 61.358 7.028   32.144  1.00 22.10 ? 82  SER C O   1 
ATOM   6356 C CB  . SER C 1 82  ? 59.917 5.953   29.482  1.00 22.48 ? 82  SER C CB  1 
ATOM   6357 O OG  . SER C 1 82  ? 59.666 6.644   28.271  1.00 36.30 ? 82  SER C OG  1 
ATOM   6358 N N   . ALA C 1 83  ? 59.971 5.347   32.550  1.00 19.01 ? 83  ALA C N   1 
ATOM   6359 C CA  . ALA C 1 83  ? 60.768 4.934   33.678  1.00 16.50 ? 83  ALA C CA  1 
ATOM   6360 C C   . ALA C 1 83  ? 60.576 3.471   33.915  1.00 13.60 ? 83  ALA C C   1 
ATOM   6361 O O   . ALA C 1 83  ? 59.583 2.911   33.503  1.00 13.21 ? 83  ALA C O   1 
ATOM   6362 C CB  . ALA C 1 83  ? 60.364 5.720   34.899  1.00 21.16 ? 83  ALA C CB  1 
ATOM   6363 N N   . ILE C 1 84  ? 61.583 2.837   34.494  1.00 19.06 ? 84  ILE C N   1 
ATOM   6364 C CA  . ILE C 1 84  ? 61.503 1.423   34.855  1.00 21.39 ? 84  ILE C CA  1 
ATOM   6365 C C   . ILE C 1 84  ? 61.599 1.492   36.365  1.00 22.35 ? 84  ILE C C   1 
ATOM   6366 O O   . ILE C 1 84  ? 62.555 2.052   36.913  1.00 20.12 ? 84  ILE C O   1 
ATOM   6367 C CB  . ILE C 1 84  ? 62.712 0.565   34.353  1.00 23.53 ? 84  ILE C CB  1 
ATOM   6368 C CG1 . ILE C 1 84  ? 62.807 0.575   32.811  1.00 24.11 ? 84  ILE C CG1 1 
ATOM   6369 C CG2 . ILE C 1 84  ? 62.570 -0.883  34.859  1.00 20.78 ? 84  ILE C CG2 1 
ATOM   6370 C CD1 . ILE C 1 84  ? 64.083 -0.071  32.278  1.00 21.19 ? 84  ILE C CD1 1 
ATOM   6371 N N   . LEU C 1 85  ? 60.601 0.943   37.033  1.00 23.54 ? 85  LEU C N   1 
ATOM   6372 C CA  . LEU C 1 85  ? 60.578 0.942   38.477  1.00 23.40 ? 85  LEU C CA  1 
ATOM   6373 C C   . LEU C 1 85  ? 60.693 -0.483  39.015  1.00 22.65 ? 85  LEU C C   1 
ATOM   6374 O O   . LEU C 1 85  ? 60.000 -1.394  38.538  1.00 20.82 ? 85  LEU C O   1 
ATOM   6375 C CB  . LEU C 1 85  ? 59.267 1.578   38.958  1.00 28.01 ? 85  LEU C CB  1 
ATOM   6376 C CG  . LEU C 1 85  ? 58.958 1.604   40.461  1.00 24.95 ? 85  LEU C CG  1 
ATOM   6377 C CD1 . LEU C 1 85  ? 59.972 2.486   41.242  1.00 18.13 ? 85  LEU C CD1 1 
ATOM   6378 C CD2 . LEU C 1 85  ? 57.529 2.090   40.645  1.00 24.80 ? 85  LEU C CD2 1 
ATOM   6379 N N   . VAL C 1 86  ? 61.603 -0.690  39.966  1.00 21.56 ? 86  VAL C N   1 
ATOM   6380 C CA  . VAL C 1 86  ? 61.728 -2.000  40.569  1.00 18.34 ? 86  VAL C CA  1 
ATOM   6381 C C   . VAL C 1 86  ? 61.627 -1.935  42.078  1.00 21.62 ? 86  VAL C C   1 
ATOM   6382 O O   . VAL C 1 86  ? 62.222 -1.067  42.713  1.00 20.02 ? 86  VAL C O   1 
ATOM   6383 C CB  . VAL C 1 86  ? 62.954 -2.827  40.049  1.00 20.69 ? 86  VAL C CB  1 
ATOM   6384 C CG1 . VAL C 1 86  ? 63.845 -1.995  39.132  1.00 15.10 ? 86  VAL C CG1 1 
ATOM   6385 C CG2 . VAL C 1 86  ? 63.716 -3.487  41.191  1.00 11.48 ? 86  VAL C CG2 1 
ATOM   6386 N N   . LEU C 1 87  ? 60.713 -2.761  42.593  1.00 22.59 ? 87  LEU C N   1 
ATOM   6387 C CA  . LEU C 1 87  ? 60.403 -2.927  44.019  1.00 20.35 ? 87  LEU C CA  1 
ATOM   6388 C C   . LEU C 1 87  ? 61.069 -4.209  44.505  1.00 21.34 ? 87  LEU C C   1 
ATOM   6389 O O   . LEU C 1 87  ? 60.857 -5.287  43.921  1.00 19.64 ? 87  LEU C O   1 
ATOM   6390 C CB  . LEU C 1 87  ? 58.880 -3.040  44.223  1.00 14.40 ? 87  LEU C CB  1 
ATOM   6391 C CG  . LEU C 1 87  ? 58.093 -1.746  44.405  1.00 15.89 ? 87  LEU C CG  1 
ATOM   6392 C CD1 . LEU C 1 87  ? 58.526 -0.665  43.418  1.00 16.02 ? 87  LEU C CD1 1 
ATOM   6393 C CD2 . LEU C 1 87  ? 56.625 -2.052  44.230  1.00 13.74 ? 87  LEU C CD2 1 
ATOM   6394 N N   . VAL C 1 88  ? 61.855 -4.102  45.576  1.00 22.91 ? 88  VAL C N   1 
ATOM   6395 C CA  . VAL C 1 88  ? 62.582 -5.252  46.120  1.00 16.00 ? 88  VAL C CA  1 
ATOM   6396 C C   . VAL C 1 88  ? 62.013 -5.730  47.447  1.00 18.83 ? 88  VAL C C   1 
ATOM   6397 O O   . VAL C 1 88  ? 61.890 -4.968  48.402  1.00 9.73  ? 88  VAL C O   1 
ATOM   6398 C CB  . VAL C 1 88  ? 64.096 -4.967  46.259  1.00 13.00 ? 88  VAL C CB  1 
ATOM   6399 C CG1 . VAL C 1 88  ? 64.816 -6.254  46.550  1.00 10.31 ? 88  VAL C CG1 1 
ATOM   6400 C CG2 . VAL C 1 88  ? 64.668 -4.339  44.964  1.00 12.16 ? 88  VAL C CG2 1 
ATOM   6401 N N   . LYS C 1 89  ? 61.689 -7.011  47.491  1.00 19.70 ? 89  LYS C N   1 
ATOM   6402 C CA  . LYS C 1 89  ? 61.092 -7.618  48.664  1.00 27.93 ? 89  LYS C CA  1 
ATOM   6403 C C   . LYS C 1 89  ? 62.115 -8.473  49.392  1.00 29.70 ? 89  LYS C C   1 
ATOM   6404 O O   . LYS C 1 89  ? 62.940 -9.117  48.749  1.00 31.52 ? 89  LYS C O   1 
ATOM   6405 C CB  . LYS C 1 89  ? 59.915 -8.499  48.240  1.00 32.94 ? 89  LYS C CB  1 
ATOM   6406 C CG  . LYS C 1 89  ? 58.840 -7.798  47.415  1.00 33.89 ? 89  LYS C CG  1 
ATOM   6407 C CD  . LYS C 1 89  ? 58.081 -6.765  48.229  1.00 39.81 ? 89  LYS C CD  1 
ATOM   6408 C CE  . LYS C 1 89  ? 56.856 -6.284  47.481  1.00 40.64 ? 89  LYS C CE  1 
ATOM   6409 N NZ  . LYS C 1 89  ? 56.115 -5.232  48.237  1.00 48.83 ? 89  LYS C NZ  1 
ATOM   6410 N N   . PRO C 1 90  ? 62.017 -8.560  50.734  1.00 28.97 ? 90  PRO C N   1 
ATOM   6411 C CA  . PRO C 1 90  ? 62.925 -9.338  51.593  1.00 27.67 ? 90  PRO C CA  1 
ATOM   6412 C C   . PRO C 1 90  ? 62.918 -10.858 51.370  1.00 26.01 ? 90  PRO C C   1 
ATOM   6413 O O   . PRO C 1 90  ? 63.919 -11.533 51.608  1.00 24.28 ? 90  PRO C O   1 
ATOM   6414 C CB  . PRO C 1 90  ? 62.450 -8.972  53.000  1.00 30.28 ? 90  PRO C CB  1 
ATOM   6415 C CG  . PRO C 1 90  ? 60.977 -8.719  52.803  1.00 29.54 ? 90  PRO C CG  1 
ATOM   6416 C CD  . PRO C 1 90  ? 60.968 -7.907  51.542  1.00 26.37 ? 90  PRO C CD  1 
ATOM   6417 N N   . ASP C 1 91  ? 61.790 -11.389 50.920  1.00 25.13 ? 91  ASP C N   1 
ATOM   6418 C CA  . ASP C 1 91  ? 61.664 -12.817 50.658  1.00 27.59 ? 91  ASP C CA  1 
ATOM   6419 C C   . ASP C 1 91  ? 62.114 -13.241 49.248  1.00 30.67 ? 91  ASP C C   1 
ATOM   6420 O O   . ASP C 1 91  ? 61.486 -14.093 48.631  1.00 30.68 ? 91  ASP C O   1 
ATOM   6421 C CB  . ASP C 1 91  ? 60.222 -13.256 50.893  1.00 28.10 ? 91  ASP C CB  1 
ATOM   6422 C CG  . ASP C 1 91  ? 59.222 -12.332 50.242  1.00 34.96 ? 91  ASP C CG  1 
ATOM   6423 O OD1 . ASP C 1 91  ? 59.551 -11.688 49.227  1.00 44.92 ? 91  ASP C OD1 1 
ATOM   6424 O OD2 . ASP C 1 91  ? 58.093 -12.231 50.746  1.00 45.35 ? 91  ASP C OD2 1 
ATOM   6425 N N   . ASP C 1 92  ? 63.178 -12.625 48.737  1.00 31.17 ? 92  ASP C N   1 
ATOM   6426 C CA  . ASP C 1 92  ? 63.727 -12.956 47.424  1.00 27.56 ? 92  ASP C CA  1 
ATOM   6427 C C   . ASP C 1 92  ? 62.674 -12.867 46.341  1.00 27.29 ? 92  ASP C C   1 
ATOM   6428 O O   . ASP C 1 92  ? 62.447 -13.822 45.603  1.00 27.32 ? 92  ASP C O   1 
ATOM   6429 C CB  . ASP C 1 92  ? 64.319 -14.365 47.447  1.00 28.28 ? 92  ASP C CB  1 
ATOM   6430 C CG  . ASP C 1 92  ? 65.257 -14.631 46.281  1.00 28.09 ? 92  ASP C CG  1 
ATOM   6431 O OD1 . ASP C 1 92  ? 65.804 -13.673 45.711  1.00 35.96 ? 92  ASP C OD1 1 
ATOM   6432 O OD2 . ASP C 1 92  ? 65.470 -15.804 45.945  1.00 24.45 ? 92  ASP C OD2 1 
ATOM   6433 N N   . ARG C 1 93  ? 62.019 -11.719 46.256  1.00 28.91 ? 93  ARG C N   1 
ATOM   6434 C CA  . ARG C 1 93  ? 60.979 -11.510 45.256  1.00 30.86 ? 93  ARG C CA  1 
ATOM   6435 C C   . ARG C 1 93  ? 61.100 -10.080 44.745  1.00 25.99 ? 93  ARG C C   1 
ATOM   6436 O O   . ARG C 1 93  ? 61.477 -9.193  45.490  1.00 30.05 ? 93  ARG C O   1 
ATOM   6437 C CB  . ARG C 1 93  ? 59.596 -11.744 45.872  1.00 34.16 ? 93  ARG C CB  1 
ATOM   6438 C CG  . ARG C 1 93  ? 58.549 -12.188 44.868  1.00 46.47 ? 93  ARG C CG  1 
ATOM   6439 C CD  . ARG C 1 93  ? 58.910 -13.556 44.293  1.00 56.57 ? 93  ARG C CD  1 
ATOM   6440 N NE  . ARG C 1 93  ? 58.386 -13.760 42.944  1.00 62.06 ? 93  ARG C NE  1 
ATOM   6441 C CZ  . ARG C 1 93  ? 59.123 -14.154 41.908  1.00 66.16 ? 93  ARG C CZ  1 
ATOM   6442 N NH1 . ARG C 1 93  ? 60.422 -14.388 42.052  1.00 66.68 ? 93  ARG C NH1 1 
ATOM   6443 N NH2 . ARG C 1 93  ? 58.561 -14.309 40.720  1.00 69.28 ? 93  ARG C NH2 1 
ATOM   6444 N N   . ARG C 1 94  ? 60.822 -9.860  43.474  1.00 22.81 ? 94  ARG C N   1 
ATOM   6445 C CA  . ARG C 1 94  ? 60.921 -8.521  42.925  1.00 21.96 ? 94  ARG C CA  1 
ATOM   6446 C C   . ARG C 1 94  ? 59.723 -8.151  42.061  1.00 22.90 ? 94  ARG C C   1 
ATOM   6447 O O   . ARG C 1 94  ? 58.984 -9.027  41.636  1.00 25.64 ? 94  ARG C O   1 
ATOM   6448 C CB  . ARG C 1 94  ? 62.218 -8.403  42.145  1.00 22.05 ? 94  ARG C CB  1 
ATOM   6449 C CG  . ARG C 1 94  ? 63.409 -8.326  43.063  1.00 30.61 ? 94  ARG C CG  1 
ATOM   6450 C CD  . ARG C 1 94  ? 64.619 -9.002  42.519  1.00 27.97 ? 94  ARG C CD  1 
ATOM   6451 N NE  . ARG C 1 94  ? 64.455 -10.447 42.432  1.00 31.50 ? 94  ARG C NE  1 
ATOM   6452 C CZ  . ARG C 1 94  ? 64.823 -11.314 43.372  1.00 34.39 ? 94  ARG C CZ  1 
ATOM   6453 N NH1 . ARG C 1 94  ? 65.364 -10.889 44.507  1.00 37.42 ? 94  ARG C NH1 1 
ATOM   6454 N NH2 . ARG C 1 94  ? 64.741 -12.620 43.135  1.00 37.23 ? 94  ARG C NH2 1 
ATOM   6455 N N   . GLU C 1 95  ? 59.505 -6.861  41.839  1.00 19.18 ? 95  GLU C N   1 
ATOM   6456 C CA  . GLU C 1 95  ? 58.400 -6.405  41.023  1.00 18.99 ? 95  GLU C CA  1 
ATOM   6457 C C   . GLU C 1 95  ? 58.909 -5.337  40.079  1.00 20.03 ? 95  GLU C C   1 
ATOM   6458 O O   . GLU C 1 95  ? 59.498 -4.360  40.507  1.00 19.34 ? 95  GLU C O   1 
ATOM   6459 C CB  . GLU C 1 95  ? 57.261 -5.892  41.895  1.00 28.36 ? 95  GLU C CB  1 
ATOM   6460 C CG  . GLU C 1 95  ? 56.353 -7.010  42.367  1.00 42.26 ? 95  GLU C CG  1 
ATOM   6461 C CD  . GLU C 1 95  ? 55.702 -6.750  43.719  1.00 51.64 ? 95  GLU C CD  1 
ATOM   6462 O OE1 . GLU C 1 95  ? 54.792 -5.891  43.797  1.00 56.59 ? 95  GLU C OE1 1 
ATOM   6463 O OE2 . GLU C 1 95  ? 56.085 -7.434  44.698  1.00 56.64 ? 95  GLU C OE2 1 
ATOM   6464 N N   . TYR C 1 96  ? 58.671 -5.548  38.788  1.00 23.54 ? 96  TYR C N   1 
ATOM   6465 C CA  . TYR C 1 96  ? 59.129 -4.663  37.715  1.00 22.42 ? 96  TYR C CA  1 
ATOM   6466 C C   . TYR C 1 96  ? 57.998 -3.920  37.072  1.00 19.09 ? 96  TYR C C   1 
ATOM   6467 O O   . TYR C 1 96  ? 56.966 -4.513  36.810  1.00 26.50 ? 96  TYR C O   1 
ATOM   6468 C CB  . TYR C 1 96  ? 59.797 -5.512  36.659  1.00 16.97 ? 96  TYR C CB  1 
ATOM   6469 C CG  . TYR C 1 96  ? 60.968 -6.258  37.191  1.00 16.62 ? 96  TYR C CG  1 
ATOM   6470 C CD1 . TYR C 1 96  ? 62.221 -5.667  37.224  1.00 19.34 ? 96  TYR C CD1 1 
ATOM   6471 C CD2 . TYR C 1 96  ? 60.836 -7.566  37.632  1.00 15.53 ? 96  TYR C CD2 1 
ATOM   6472 C CE1 . TYR C 1 96  ? 63.312 -6.360  37.674  1.00 22.02 ? 96  TYR C CE1 1 
ATOM   6473 C CE2 . TYR C 1 96  ? 61.926 -8.278  38.090  1.00 13.07 ? 96  TYR C CE2 1 
ATOM   6474 C CZ  . TYR C 1 96  ? 63.162 -7.674  38.102  1.00 17.00 ? 96  TYR C CZ  1 
ATOM   6475 O OH  . TYR C 1 96  ? 64.276 -8.391  38.469  1.00 22.90 ? 96  TYR C OH  1 
ATOM   6476 N N   . PHE C 1 97  ? 58.209 -2.646  36.758  1.00 22.87 ? 97  PHE C N   1 
ATOM   6477 C CA  . PHE C 1 97  ? 57.161 -1.823  36.148  1.00 24.30 ? 97  PHE C CA  1 
ATOM   6478 C C   . PHE C 1 97  ? 57.681 -0.856  35.090  1.00 25.41 ? 97  PHE C C   1 
ATOM   6479 O O   . PHE C 1 97  ? 58.652 -0.144  35.331  1.00 24.69 ? 97  PHE C O   1 
ATOM   6480 C CB  . PHE C 1 97  ? 56.456 -0.952  37.206  1.00 21.37 ? 97  PHE C CB  1 
ATOM   6481 C CG  . PHE C 1 97  ? 55.721 -1.724  38.269  1.00 24.76 ? 97  PHE C CG  1 
ATOM   6482 C CD1 . PHE C 1 97  ? 54.447 -2.214  38.040  1.00 26.36 ? 97  PHE C CD1 1 
ATOM   6483 C CD2 . PHE C 1 97  ? 56.300 -1.942  39.516  1.00 24.77 ? 97  PHE C CD2 1 
ATOM   6484 C CE1 . PHE C 1 97  ? 53.769 -2.908  39.036  1.00 23.67 ? 97  PHE C CE1 1 
ATOM   6485 C CE2 . PHE C 1 97  ? 55.626 -2.636  40.514  1.00 20.38 ? 97  PHE C CE2 1 
ATOM   6486 C CZ  . PHE C 1 97  ? 54.362 -3.117  40.274  1.00 19.09 ? 97  PHE C CZ  1 
ATOM   6487 N N   . PHE C 1 98  ? 57.057 -0.835  33.916  1.00 22.13 ? 98  PHE C N   1 
ATOM   6488 C CA  . PHE C 1 98  ? 57.450 0.161   32.938  1.00 27.31 ? 98  PHE C CA  1 
ATOM   6489 C C   . PHE C 1 98  ? 56.315 1.202   32.921  1.00 26.48 ? 98  PHE C C   1 
ATOM   6490 O O   . PHE C 1 98  ? 55.131 0.859   32.765  1.00 24.73 ? 98  PHE C O   1 
ATOM   6491 C CB  . PHE C 1 98  ? 57.711 -0.404  31.543  1.00 32.58 ? 98  PHE C CB  1 
ATOM   6492 C CG  . PHE C 1 98  ? 58.307 0.614   30.614  1.00 36.84 ? 98  PHE C CG  1 
ATOM   6493 C CD1 . PHE C 1 98  ? 57.486 1.488   29.900  1.00 41.48 ? 98  PHE C CD1 1 
ATOM   6494 C CD2 . PHE C 1 98  ? 59.682 0.773   30.534  1.00 34.20 ? 98  PHE C CD2 1 
ATOM   6495 C CE1 . PHE C 1 98  ? 58.021 2.508   29.131  1.00 40.57 ? 98  PHE C CE1 1 
ATOM   6496 C CE2 . PHE C 1 98  ? 60.233 1.786   29.769  1.00 37.84 ? 98  PHE C CE2 1 
ATOM   6497 C CZ  . PHE C 1 98  ? 59.401 2.660   29.064  1.00 41.68 ? 98  PHE C CZ  1 
ATOM   6498 N N   . LEU C 1 99  ? 56.678 2.465   33.122  1.00 29.00 ? 99  LEU C N   1 
ATOM   6499 C CA  . LEU C 1 99  ? 55.702 3.549   33.194  1.00 33.09 ? 99  LEU C CA  1 
ATOM   6500 C C   . LEU C 1 99  ? 55.985 4.597   32.143  1.00 37.92 ? 99  LEU C C   1 
ATOM   6501 O O   . LEU C 1 99  ? 57.150 4.925   31.898  1.00 36.27 ? 99  LEU C O   1 
ATOM   6502 C CB  . LEU C 1 99  ? 55.749 4.209   34.583  1.00 35.42 ? 99  LEU C CB  1 
ATOM   6503 C CG  . LEU C 1 99  ? 54.998 3.677   35.818  1.00 31.50 ? 99  LEU C CG  1 
ATOM   6504 C CD1 . LEU C 1 99  ? 55.124 2.187   35.957  1.00 26.87 ? 99  LEU C CD1 1 
ATOM   6505 C CD2 . LEU C 1 99  ? 55.541 4.356   37.061  1.00 33.06 ? 99  LEU C CD2 1 
ATOM   6506 N N   . THR C 1 100 ? 54.922 5.123   31.536  1.00 40.09 ? 100 THR C N   1 
ATOM   6507 C CA  . THR C 1 100 ? 55.050 6.151   30.508  1.00 45.40 ? 100 THR C CA  1 
ATOM   6508 C C   . THR C 1 100 ? 53.902 7.122   30.675  1.00 47.68 ? 100 THR C C   1 
ATOM   6509 O O   . THR C 1 100 ? 52.865 6.758   31.208  1.00 47.61 ? 100 THR C O   1 
ATOM   6510 C CB  . THR C 1 100 ? 54.980 5.578   29.078  1.00 41.16 ? 100 THR C CB  1 
ATOM   6511 O OG1 . THR C 1 100 ? 55.325 4.190   29.082  1.00 42.52 ? 100 THR C OG1 1 
ATOM   6512 C CG2 . THR C 1 100 ? 55.969 6.312   28.198  1.00 44.65 ? 100 THR C CG2 1 
ATOM   6513 N N   . SER C 1 101 ? 54.076 8.340   30.181  1.00 51.87 ? 101 SER C N   1 
ATOM   6514 C CA  . SER C 1 101 ? 53.058 9.368   30.305  1.00 57.49 ? 101 SER C CA  1 
ATOM   6515 C C   . SER C 1 101 ? 51.918 9.346   29.291  1.00 64.55 ? 101 SER C C   1 
ATOM   6516 O O   . SER C 1 101 ? 50.750 9.477   29.674  1.00 64.86 ? 101 SER C O   1 
ATOM   6517 C CB  . SER C 1 101 ? 53.720 10.742  30.258  1.00 58.27 ? 101 SER C CB  1 
ATOM   6518 O OG  . SER C 1 101 ? 54.295 10.991  28.975  1.00 61.37 ? 101 SER C OG  1 
ATOM   6519 N N   . ASP C 1 102 ? 52.254 9.213   28.001  1.00 72.12 ? 102 ASP C N   1 
ATOM   6520 C CA  . ASP C 1 102 ? 51.242 9.268   26.936  1.00 75.01 ? 102 ASP C CA  1 
ATOM   6521 C C   . ASP C 1 102 ? 50.781 8.066   26.119  1.00 76.15 ? 102 ASP C C   1 
ATOM   6522 O O   . ASP C 1 102 ? 49.615 8.033   25.724  1.00 77.20 ? 102 ASP C O   1 
ATOM   6523 C CB  . ASP C 1 102 ? 51.545 10.422  25.975  1.00 76.90 ? 102 ASP C CB  1 
ATOM   6524 C CG  . ASP C 1 102 ? 50.403 11.437  25.900  1.00 81.26 ? 102 ASP C CG  1 
ATOM   6525 O OD1 . ASP C 1 102 ? 49.254 11.086  26.254  1.00 82.12 ? 102 ASP C OD1 1 
ATOM   6526 O OD2 . ASP C 1 102 ? 50.653 12.594  25.493  1.00 84.23 ? 102 ASP C OD2 1 
ATOM   6527 N N   . ASN C 1 103 ? 51.655 7.114   25.800  1.00 76.91 ? 103 ASN C N   1 
ATOM   6528 C CA  . ASN C 1 103 ? 51.193 5.966   25.007  1.00 76.82 ? 103 ASN C CA  1 
ATOM   6529 C C   . ASN C 1 103 ? 50.295 5.016   25.811  1.00 73.39 ? 103 ASN C C   1 
ATOM   6530 O O   . ASN C 1 103 ? 50.767 4.274   26.670  1.00 72.93 ? 103 ASN C O   1 
ATOM   6531 C CB  . ASN C 1 103 ? 52.357 5.222   24.330  1.00 80.68 ? 103 ASN C CB  1 
ATOM   6532 C CG  . ASN C 1 103 ? 53.180 4.404   25.292  1.00 82.93 ? 103 ASN C CG  1 
ATOM   6533 O OD1 . ASN C 1 103 ? 53.219 4.676   26.487  1.00 90.13 ? 103 ASN C OD1 1 
ATOM   6534 N ND2 . ASN C 1 103 ? 53.863 3.404   24.768  1.00 83.57 ? 103 ASN C ND2 1 
ATOM   6535 N N   . PRO C 1 104 ? 48.991 4.981   25.479  1.00 71.53 ? 104 PRO C N   1 
ATOM   6536 C CA  . PRO C 1 104 ? 47.914 4.178   26.080  1.00 68.31 ? 104 PRO C CA  1 
ATOM   6537 C C   . PRO C 1 104 ? 48.189 2.703   26.395  1.00 65.09 ? 104 PRO C C   1 
ATOM   6538 O O   . PRO C 1 104 ? 47.303 2.010   26.898  1.00 62.07 ? 104 PRO C O   1 
ATOM   6539 C CB  . PRO C 1 104 ? 46.792 4.299   25.046  1.00 70.84 ? 104 PRO C CB  1 
ATOM   6540 C CG  . PRO C 1 104 ? 46.991 5.671   24.500  1.00 72.07 ? 104 PRO C CG  1 
ATOM   6541 C CD  . PRO C 1 104 ? 48.486 5.697   24.289  1.00 72.36 ? 104 PRO C CD  1 
ATOM   6542 N N   . ILE C 1 105 ? 49.398 2.228   26.100  1.00 62.19 ? 105 ILE C N   1 
ATOM   6543 C CA  . ILE C 1 105 ? 49.765 0.835   26.328  1.00 58.80 ? 105 ILE C CA  1 
ATOM   6544 C C   . ILE C 1 105 ? 50.370 0.487   27.680  1.00 53.75 ? 105 ILE C C   1 
ATOM   6545 O O   . ILE C 1 105 ? 50.245 -0.649  28.123  1.00 54.25 ? 105 ILE C O   1 
ATOM   6546 C CB  . ILE C 1 105 ? 50.694 0.316   25.214  1.00 60.20 ? 105 ILE C CB  1 
ATOM   6547 C CG1 . ILE C 1 105 ? 51.814 1.324   24.944  1.00 59.91 ? 105 ILE C CG1 1 
ATOM   6548 C CG2 . ILE C 1 105 ? 49.884 0.044   23.952  1.00 63.77 ? 105 ILE C CG2 1 
ATOM   6549 C CD1 . ILE C 1 105 ? 52.740 0.926   23.820  1.00 61.85 ? 105 ILE C CD1 1 
ATOM   6550 N N   . PHE C 1 106 ? 51.052 1.439   28.312  1.00 48.59 ? 106 PHE C N   1 
ATOM   6551 C CA  . PHE C 1 106 ? 51.672 1.212   29.622  1.00 40.99 ? 106 PHE C CA  1 
ATOM   6552 C C   . PHE C 1 106 ? 51.036 2.187   30.598  1.00 37.08 ? 106 PHE C C   1 
ATOM   6553 O O   . PHE C 1 106 ? 50.468 3.188   30.175  1.00 38.27 ? 106 PHE C O   1 
ATOM   6554 C CB  . PHE C 1 106 ? 53.180 1.494   29.577  1.00 41.13 ? 106 PHE C CB  1 
ATOM   6555 C CG  . PHE C 1 106 ? 53.961 0.604   28.639  1.00 39.97 ? 106 PHE C CG  1 
ATOM   6556 C CD1 . PHE C 1 106 ? 54.150 0.966   27.311  1.00 35.68 ? 106 PHE C CD1 1 
ATOM   6557 C CD2 . PHE C 1 106 ? 54.557 -0.566  29.099  1.00 38.38 ? 106 PHE C CD2 1 
ATOM   6558 C CE1 . PHE C 1 106 ? 54.919 0.183   26.459  1.00 36.51 ? 106 PHE C CE1 1 
ATOM   6559 C CE2 . PHE C 1 106 ? 55.330 -1.359  28.250  1.00 39.41 ? 106 PHE C CE2 1 
ATOM   6560 C CZ  . PHE C 1 106 ? 55.511 -0.981  26.928  1.00 35.57 ? 106 PHE C CZ  1 
ATOM   6561 N N   . SER C 1 107 ? 51.169 1.930   31.895  1.00 33.51 ? 107 SER C N   1 
ATOM   6562 C CA  . SER C 1 107 ? 50.596 2.819   32.910  1.00 26.87 ? 107 SER C CA  1 
ATOM   6563 C C   . SER C 1 107 ? 51.481 4.043   33.222  1.00 26.82 ? 107 SER C C   1 
ATOM   6564 O O   . SER C 1 107 ? 52.707 4.034   33.000  1.00 26.56 ? 107 SER C O   1 
ATOM   6565 C CB  . SER C 1 107 ? 50.308 2.028   34.192  1.00 27.05 ? 107 SER C CB  1 
ATOM   6566 O OG  . SER C 1 107 ? 49.688 2.826   35.202  1.00 34.88 ? 107 SER C OG  1 
ATOM   6567 N N   . ASP C 1 108 ? 50.855 5.121   33.688  1.00 23.24 ? 108 ASP C N   1 
ATOM   6568 C CA  . ASP C 1 108 ? 51.618 6.306   34.042  1.00 23.15 ? 108 ASP C CA  1 
ATOM   6569 C C   . ASP C 1 108 ? 51.797 6.456   35.546  1.00 25.51 ? 108 ASP C C   1 
ATOM   6570 O O   . ASP C 1 108 ? 52.336 7.461   36.009  1.00 24.47 ? 108 ASP C O   1 
ATOM   6571 C CB  . ASP C 1 108 ? 50.979 7.581   33.477  1.00 24.86 ? 108 ASP C CB  1 
ATOM   6572 C CG  . ASP C 1 108 ? 49.623 7.916   34.093  1.00 26.52 ? 108 ASP C CG  1 
ATOM   6573 O OD1 . ASP C 1 108 ? 49.131 7.200   34.982  1.00 32.90 ? 108 ASP C OD1 1 
ATOM   6574 O OD2 . ASP C 1 108 ? 49.046 8.944   33.685  1.00 28.93 ? 108 ASP C OD2 1 
ATOM   6575 N N   . HIS C 1 109 ? 51.339 5.480   36.319  1.00 26.64 ? 109 HIS C N   1 
ATOM   6576 C CA  . HIS C 1 109 ? 51.444 5.600   37.774  1.00 25.55 ? 109 HIS C CA  1 
ATOM   6577 C C   . HIS C 1 109 ? 51.495 4.261   38.468  1.00 24.18 ? 109 HIS C C   1 
ATOM   6578 O O   . HIS C 1 109 ? 50.952 3.272   37.955  1.00 23.48 ? 109 HIS C O   1 
ATOM   6579 C CB  . HIS C 1 109 ? 50.245 6.378   38.316  1.00 28.08 ? 109 HIS C CB  1 
ATOM   6580 C CG  . HIS C 1 109 ? 48.941 5.655   38.162  1.00 27.96 ? 109 HIS C CG  1 
ATOM   6581 N ND1 . HIS C 1 109 ? 48.287 5.543   36.955  1.00 30.88 ? 109 HIS C ND1 1 
ATOM   6582 C CD2 . HIS C 1 109 ? 48.187 4.979   39.058  1.00 31.46 ? 109 HIS C CD2 1 
ATOM   6583 C CE1 . HIS C 1 109 ? 47.190 4.829   37.113  1.00 36.44 ? 109 HIS C CE1 1 
ATOM   6584 N NE2 . HIS C 1 109 ? 47.104 4.474   38.380  1.00 37.76 ? 109 HIS C NE2 1 
ATOM   6585 N N   . GLN C 1 110 ? 52.046 4.271   39.682  1.00 22.26 ? 110 GLN C N   1 
ATOM   6586 C CA  . GLN C 1 110 ? 52.175 3.073   40.506  1.00 23.23 ? 110 GLN C CA  1 
ATOM   6587 C C   . GLN C 1 110 ? 52.264 3.486   41.976  1.00 27.25 ? 110 GLN C C   1 
ATOM   6588 O O   . GLN C 1 110 ? 52.752 4.583   42.285  1.00 27.08 ? 110 GLN C O   1 
ATOM   6589 C CB  . GLN C 1 110 ? 53.442 2.300   40.104  1.00 20.50 ? 110 GLN C CB  1 
ATOM   6590 C CG  . GLN C 1 110 ? 53.668 1.007   40.862  1.00 22.01 ? 110 GLN C CG  1 
ATOM   6591 C CD  . GLN C 1 110 ? 52.510 0.048   40.715  1.00 29.39 ? 110 GLN C CD  1 
ATOM   6592 O OE1 . GLN C 1 110 ? 51.990 -0.456  41.703  1.00 18.53 ? 110 GLN C OE1 1 
ATOM   6593 N NE2 . GLN C 1 110 ? 52.075 -0.187  39.476  1.00 27.19 ? 110 GLN C NE2 1 
ATOM   6594 N N   . LYS C 1 111 ? 51.742 2.647   42.868  1.00 26.36 ? 111 LYS C N   1 
ATOM   6595 C CA  . LYS C 1 111 ? 51.813 2.939   44.298  1.00 30.06 ? 111 LYS C CA  1 
ATOM   6596 C C   . LYS C 1 111 ? 52.956 2.106   44.898  1.00 29.74 ? 111 LYS C C   1 
ATOM   6597 O O   . LYS C 1 111 ? 53.143 0.922   44.563  1.00 25.38 ? 111 LYS C O   1 
ATOM   6598 C CB  . LYS C 1 111 ? 50.506 2.616   45.038  1.00 29.18 ? 111 LYS C CB  1 
ATOM   6599 C CG  . LYS C 1 111 ? 50.242 1.127   45.173  1.00 46.18 ? 111 LYS C CG  1 
ATOM   6600 C CD  . LYS C 1 111 ? 49.313 0.774   46.332  1.00 54.81 ? 111 LYS C CD  1 
ATOM   6601 C CE  . LYS C 1 111 ? 47.851 0.996   45.970  1.00 60.64 ? 111 LYS C CE  1 
ATOM   6602 N NZ  . LYS C 1 111 ? 47.409 0.292   44.730  1.00 61.10 ? 111 LYS C NZ  1 
ATOM   6603 N N   . ILE C 1 112 ? 53.755 2.752   45.741  1.00 25.74 ? 112 ILE C N   1 
ATOM   6604 C CA  . ILE C 1 112 ? 54.859 2.085   46.390  1.00 24.21 ? 112 ILE C CA  1 
ATOM   6605 C C   . ILE C 1 112 ? 54.540 2.080   47.870  1.00 19.73 ? 112 ILE C C   1 
ATOM   6606 O O   . ILE C 1 112 ? 54.371 3.125   48.473  1.00 27.38 ? 112 ILE C O   1 
ATOM   6607 C CB  . ILE C 1 112 ? 56.187 2.829   46.146  1.00 20.90 ? 112 ILE C CB  1 
ATOM   6608 C CG1 . ILE C 1 112 ? 56.365 3.084   44.644  1.00 18.58 ? 112 ILE C CG1 1 
ATOM   6609 C CG2 . ILE C 1 112 ? 57.348 1.999   46.716  1.00 17.66 ? 112 ILE C CG2 1 
ATOM   6610 C CD1 . ILE C 1 112 ? 57.483 4.013   44.285  1.00 19.76 ? 112 ILE C CD1 1 
ATOM   6611 N N   . PRO C 1 113 ? 54.396 0.899   48.460  1.00 19.06 ? 113 PRO C N   1 
ATOM   6612 C CA  . PRO C 1 113 ? 54.090 0.831   49.891  1.00 15.57 ? 113 PRO C CA  1 
ATOM   6613 C C   . PRO C 1 113 ? 55.207 1.357   50.785  1.00 19.01 ? 113 PRO C C   1 
ATOM   6614 O O   . PRO C 1 113 ? 56.366 1.438   50.387  1.00 25.79 ? 113 PRO C O   1 
ATOM   6615 C CB  . PRO C 1 113 ? 53.849 -0.655  50.110  1.00 18.07 ? 113 PRO C CB  1 
ATOM   6616 C CG  . PRO C 1 113 ? 53.358 -1.131  48.747  1.00 21.98 ? 113 PRO C CG  1 
ATOM   6617 C CD  . PRO C 1 113 ? 54.303 -0.426  47.825  1.00 16.08 ? 113 PRO C CD  1 
ATOM   6618 N N   . ALA C 1 114 ? 54.856 1.694   52.019  1.00 21.15 ? 114 ALA C N   1 
ATOM   6619 C CA  . ALA C 1 114 ? 55.819 2.218   52.973  1.00 21.91 ? 114 ALA C CA  1 
ATOM   6620 C C   . ALA C 1 114 ? 56.903 1.202   53.265  1.00 21.97 ? 114 ALA C C   1 
ATOM   6621 O O   . ALA C 1 114 ? 56.663 -0.005  53.233  1.00 21.14 ? 114 ALA C O   1 
ATOM   6622 C CB  . ALA C 1 114 ? 55.118 2.629   54.258  1.00 18.02 ? 114 ALA C CB  1 
ATOM   6623 N N   . GLY C 1 115 ? 58.113 1.695   53.496  1.00 21.14 ? 115 GLY C N   1 
ATOM   6624 C CA  . GLY C 1 115 ? 59.225 0.812   53.797  1.00 24.51 ? 115 GLY C CA  1 
ATOM   6625 C C   . GLY C 1 115 ? 59.678 -0.194  52.753  1.00 21.06 ? 115 GLY C C   1 
ATOM   6626 O O   . GLY C 1 115 ? 60.418 -1.121  53.096  1.00 20.55 ? 115 GLY C O   1 
ATOM   6627 N N   . THR C 1 116 ? 59.264 -0.022  51.494  1.00 20.38 ? 116 THR C N   1 
ATOM   6628 C CA  . THR C 1 116 ? 59.678 -0.926  50.427  1.00 18.93 ? 116 THR C CA  1 
ATOM   6629 C C   . THR C 1 116 ? 60.917 -0.337  49.737  1.00 20.85 ? 116 THR C C   1 
ATOM   6630 O O   . THR C 1 116 ? 60.967 0.868   49.459  1.00 19.88 ? 116 THR C O   1 
ATOM   6631 C CB  . THR C 1 116 ? 58.537 -1.169  49.397  1.00 23.50 ? 116 THR C CB  1 
ATOM   6632 O OG1 . THR C 1 116 ? 57.385 -1.697  50.081  1.00 20.49 ? 116 THR C OG1 1 
ATOM   6633 C CG2 . THR C 1 116 ? 58.981 -2.176  48.293  1.00 17.02 ? 116 THR C CG2 1 
ATOM   6634 N N   . ILE C 1 117 ? 61.950 -1.161  49.569  1.00 17.15 ? 117 ILE C N   1 
ATOM   6635 C CA  . ILE C 1 117 ? 63.198 -0.741  48.917  1.00 17.64 ? 117 ILE C CA  1 
ATOM   6636 C C   . ILE C 1 117 ? 62.887 -0.602  47.453  1.00 15.82 ? 117 ILE C C   1 
ATOM   6637 O O   . ILE C 1 117 ? 62.233 -1.472  46.900  1.00 18.27 ? 117 ILE C O   1 
ATOM   6638 C CB  . ILE C 1 117 ? 64.314 -1.824  49.031  1.00 15.73 ? 117 ILE C CB  1 
ATOM   6639 C CG1 . ILE C 1 117 ? 64.935 -1.838  50.437  1.00 17.07 ? 117 ILE C CG1 1 
ATOM   6640 C CG2 . ILE C 1 117 ? 65.400 -1.574  47.951  1.00 14.51 ? 117 ILE C CG2 1 
ATOM   6641 C CD1 . ILE C 1 117 ? 65.962 -0.697  50.675  1.00 14.06 ? 117 ILE C CD1 1 
ATOM   6642 N N   . PHE C 1 118 ? 63.337 0.466   46.815  1.00 17.99 ? 118 PHE C N   1 
ATOM   6643 C CA  . PHE C 1 118 ? 63.066 0.599   45.377  1.00 21.18 ? 118 PHE C CA  1 
ATOM   6644 C C   . PHE C 1 118 ? 64.114 1.412   44.628  1.00 23.36 ? 118 PHE C C   1 
ATOM   6645 O O   . PHE C 1 118 ? 64.892 2.139   45.237  1.00 28.17 ? 118 PHE C O   1 
ATOM   6646 C CB  . PHE C 1 118 ? 61.686 1.226   45.159  1.00 20.74 ? 118 PHE C CB  1 
ATOM   6647 C CG  . PHE C 1 118 ? 61.584 2.656   45.624  1.00 23.85 ? 118 PHE C CG  1 
ATOM   6648 C CD1 . PHE C 1 118 ? 61.355 2.949   46.974  1.00 28.75 ? 118 PHE C CD1 1 
ATOM   6649 C CD2 . PHE C 1 118 ? 61.714 3.711   44.717  1.00 23.29 ? 118 PHE C CD2 1 
ATOM   6650 C CE1 . PHE C 1 118 ? 61.252 4.268   47.416  1.00 26.85 ? 118 PHE C CE1 1 
ATOM   6651 C CE2 . PHE C 1 118 ? 61.613 5.039   45.146  1.00 26.62 ? 118 PHE C CE2 1 
ATOM   6652 C CZ  . PHE C 1 118 ? 61.379 5.315   46.504  1.00 26.27 ? 118 PHE C CZ  1 
ATOM   6653 N N   . TYR C 1 119 ? 64.184 1.249   43.315  1.00 22.63 ? 119 TYR C N   1 
ATOM   6654 C CA  . TYR C 1 119 ? 65.108 2.037   42.521  1.00 22.01 ? 119 TYR C CA  1 
ATOM   6655 C C   . TYR C 1 119 ? 64.483 2.281   41.151  1.00 23.71 ? 119 TYR C C   1 
ATOM   6656 O O   . TYR C 1 119 ? 63.723 1.464   40.639  1.00 24.73 ? 119 TYR C O   1 
ATOM   6657 C CB  . TYR C 1 119 ? 66.535 1.457   42.479  1.00 25.93 ? 119 TYR C CB  1 
ATOM   6658 C CG  . TYR C 1 119 ? 66.699 0.088   41.861  1.00 28.40 ? 119 TYR C CG  1 
ATOM   6659 C CD1 . TYR C 1 119 ? 66.869 -0.068  40.473  1.00 25.82 ? 119 TYR C CD1 1 
ATOM   6660 C CD2 . TYR C 1 119 ? 66.743 -1.048  42.668  1.00 29.37 ? 119 TYR C CD2 1 
ATOM   6661 C CE1 . TYR C 1 119 ? 67.091 -1.325  39.912  1.00 25.82 ? 119 TYR C CE1 1 
ATOM   6662 C CE2 . TYR C 1 119 ? 66.957 -2.309  42.126  1.00 30.83 ? 119 TYR C CE2 1 
ATOM   6663 C CZ  . TYR C 1 119 ? 67.140 -2.451  40.751  1.00 33.36 ? 119 TYR C CZ  1 
ATOM   6664 O OH  . TYR C 1 119 ? 67.436 -3.713  40.257  1.00 34.93 ? 119 TYR C OH  1 
ATOM   6665 N N   . LEU C 1 120 ? 64.806 3.429   40.578  1.00 22.73 ? 120 LEU C N   1 
ATOM   6666 C CA  . LEU C 1 120 ? 64.230 3.890   39.330  1.00 24.67 ? 120 LEU C CA  1 
ATOM   6667 C C   . LEU C 1 120 ? 65.281 4.151   38.237  1.00 23.94 ? 120 LEU C C   1 
ATOM   6668 O O   . LEU C 1 120 ? 66.371 4.661   38.533  1.00 26.89 ? 120 LEU C O   1 
ATOM   6669 C CB  . LEU C 1 120 ? 63.511 5.193   39.692  1.00 26.24 ? 120 LEU C CB  1 
ATOM   6670 C CG  . LEU C 1 120 ? 62.250 5.778   39.094  1.00 30.89 ? 120 LEU C CG  1 
ATOM   6671 C CD1 . LEU C 1 120 ? 61.141 4.735   38.931  1.00 30.28 ? 120 LEU C CD1 1 
ATOM   6672 C CD2 . LEU C 1 120 ? 61.841 6.880   40.056  1.00 30.39 ? 120 LEU C CD2 1 
ATOM   6673 N N   . VAL C 1 121 ? 64.968 3.792   36.991  1.00 21.63 ? 121 VAL C N   1 
ATOM   6674 C CA  . VAL C 1 121 ? 65.896 4.013   35.883  1.00 21.87 ? 121 VAL C CA  1 
ATOM   6675 C C   . VAL C 1 121 ? 65.238 4.828   34.782  1.00 21.66 ? 121 VAL C C   1 
ATOM   6676 O O   . VAL C 1 121 ? 64.022 4.736   34.561  1.00 19.86 ? 121 VAL C O   1 
ATOM   6677 C CB  . VAL C 1 121 ? 66.362 2.699   35.194  1.00 21.42 ? 121 VAL C CB  1 
ATOM   6678 C CG1 . VAL C 1 121 ? 67.519 2.996   34.303  1.00 29.37 ? 121 VAL C CG1 1 
ATOM   6679 C CG2 . VAL C 1 121 ? 66.759 1.644   36.176  1.00 23.60 ? 121 VAL C CG2 1 
ATOM   6680 N N   . ASN C 1 122 ? 66.034 5.656   34.111  1.00 23.68 ? 122 ASN C N   1 
ATOM   6681 C CA  . ASN C 1 122 ? 65.531 6.433   32.973  1.00 25.05 ? 122 ASN C CA  1 
ATOM   6682 C C   . ASN C 1 122 ? 66.132 5.739   31.738  1.00 23.99 ? 122 ASN C C   1 
ATOM   6683 O O   . ASN C 1 122 ? 67.291 5.951   31.365  1.00 24.11 ? 122 ASN C O   1 
ATOM   6684 C CB  . ASN C 1 122 ? 65.977 7.892   33.062  1.00 25.36 ? 122 ASN C CB  1 
ATOM   6685 C CG  . ASN C 1 122 ? 65.412 8.748   31.943  1.00 26.88 ? 122 ASN C CG  1 
ATOM   6686 O OD1 . ASN C 1 122 ? 65.688 9.942   31.886  1.00 30.45 ? 122 ASN C OD1 1 
ATOM   6687 N ND2 . ASN C 1 122 ? 64.598 8.156   31.066  1.00 16.14 ? 122 ASN C ND2 1 
ATOM   6688 N N   . PRO C 1 123 ? 65.350 4.861   31.107  1.00 24.66 ? 123 PRO C N   1 
ATOM   6689 C CA  . PRO C 1 123 ? 65.859 4.152   29.939  1.00 25.83 ? 123 PRO C CA  1 
ATOM   6690 C C   . PRO C 1 123 ? 66.123 5.011   28.699  1.00 31.71 ? 123 PRO C C   1 
ATOM   6691 O O   . PRO C 1 123 ? 67.070 4.758   27.943  1.00 33.95 ? 123 PRO C O   1 
ATOM   6692 C CB  . PRO C 1 123 ? 64.765 3.115   29.695  1.00 25.37 ? 123 PRO C CB  1 
ATOM   6693 C CG  . PRO C 1 123 ? 63.510 3.850   30.110  1.00 17.52 ? 123 PRO C CG  1 
ATOM   6694 C CD  . PRO C 1 123 ? 63.953 4.484   31.396  1.00 21.57 ? 123 PRO C CD  1 
ATOM   6695 N N   . ASP C 1 124 ? 65.309 6.043   28.507  1.00 34.85 ? 124 ASP C N   1 
ATOM   6696 C CA  . ASP C 1 124 ? 65.448 6.876   27.334  1.00 37.25 ? 124 ASP C CA  1 
ATOM   6697 C C   . ASP C 1 124 ? 66.808 7.548   27.133  1.00 38.80 ? 124 ASP C C   1 
ATOM   6698 O O   . ASP C 1 124 ? 67.398 8.090   28.075  1.00 36.66 ? 124 ASP C O   1 
ATOM   6699 C CB  . ASP C 1 124 ? 64.331 7.895   27.258  1.00 38.88 ? 124 ASP C CB  1 
ATOM   6700 C CG  . ASP C 1 124 ? 63.934 8.187   25.834  1.00 42.63 ? 124 ASP C CG  1 
ATOM   6701 O OD1 . ASP C 1 124 ? 64.544 9.092   25.226  1.00 48.08 ? 124 ASP C OD1 1 
ATOM   6702 O OD2 . ASP C 1 124 ? 63.039 7.484   25.307  1.00 46.43 ? 124 ASP C OD2 1 
ATOM   6703 N N   . PRO C 1 125 ? 67.333 7.481   25.887  1.00 38.01 ? 125 PRO C N   1 
ATOM   6704 C CA  . PRO C 1 125 ? 68.620 8.059   25.476  1.00 35.15 ? 125 PRO C CA  1 
ATOM   6705 C C   . PRO C 1 125 ? 68.583 9.564   25.168  1.00 32.58 ? 125 PRO C C   1 
ATOM   6706 O O   . PRO C 1 125 ? 69.620 10.195  25.037  1.00 31.83 ? 125 PRO C O   1 
ATOM   6707 C CB  . PRO C 1 125 ? 68.946 7.253   24.219  1.00 34.84 ? 125 PRO C CB  1 
ATOM   6708 C CG  . PRO C 1 125 ? 67.578 7.048   23.602  1.00 27.53 ? 125 PRO C CG  1 
ATOM   6709 C CD  . PRO C 1 125 ? 66.777 6.629   24.809  1.00 33.67 ? 125 PRO C CD  1 
ATOM   6710 N N   . LYS C 1 126 ? 67.394 10.138  25.069  1.00 31.24 ? 126 LYS C N   1 
ATOM   6711 C CA  . LYS C 1 126 ? 67.278 11.546  24.735  1.00 35.50 ? 126 LYS C CA  1 
ATOM   6712 C C   . LYS C 1 126 ? 66.365 12.381  25.627  1.00 37.22 ? 126 LYS C C   1 
ATOM   6713 O O   . LYS C 1 126 ? 66.623 13.571  25.807  1.00 39.10 ? 126 LYS C O   1 
ATOM   6714 C CB  . LYS C 1 126 ? 66.818 11.681  23.284  1.00 42.57 ? 126 LYS C CB  1 
ATOM   6715 C CG  . LYS C 1 126 ? 67.784 11.098  22.241  1.00 53.52 ? 126 LYS C CG  1 
ATOM   6716 C CD  . LYS C 1 126 ? 68.968 12.037  21.933  1.00 59.55 ? 126 LYS C CD  1 
ATOM   6717 C CE  . LYS C 1 126 ? 70.325 11.319  22.024  1.00 59.57 ? 126 LYS C CE  1 
ATOM   6718 N NZ  . LYS C 1 126 ? 70.366 10.024  21.272  1.00 58.61 ? 126 LYS C NZ  1 
ATOM   6719 N N   . GLU C 1 127 ? 65.315 11.762  26.175  1.00 37.16 ? 127 GLU C N   1 
ATOM   6720 C CA  . GLU C 1 127 ? 64.316 12.421  27.034  1.00 36.11 ? 127 GLU C CA  1 
ATOM   6721 C C   . GLU C 1 127 ? 64.626 12.428  28.529  1.00 36.34 ? 127 GLU C C   1 
ATOM   6722 O O   . GLU C 1 127 ? 65.281 11.521  29.036  1.00 40.40 ? 127 GLU C O   1 
ATOM   6723 C CB  . GLU C 1 127 ? 62.987 11.695  26.901  1.00 38.85 ? 127 GLU C CB  1 
ATOM   6724 C CG  . GLU C 1 127 ? 62.396 11.676  25.530  1.00 49.98 ? 127 GLU C CG  1 
ATOM   6725 C CD  . GLU C 1 127 ? 61.578 12.898  25.272  1.00 58.43 ? 127 GLU C CD  1 
ATOM   6726 O OE1 . GLU C 1 127 ? 60.363 12.856  25.576  1.00 62.91 ? 127 GLU C OE1 1 
ATOM   6727 O OE2 . GLU C 1 127 ? 62.151 13.899  24.783  1.00 62.40 ? 127 GLU C OE2 1 
ATOM   6728 N N   . ASP C 1 128 ? 64.112 13.428  29.237  1.00 35.07 ? 128 ASP C N   1 
ATOM   6729 C CA  . ASP C 1 128 ? 64.280 13.504  30.698  1.00 34.33 ? 128 ASP C CA  1 
ATOM   6730 C C   . ASP C 1 128 ? 63.110 12.711  31.289  1.00 33.72 ? 128 ASP C C   1 
ATOM   6731 O O   . ASP C 1 128 ? 62.200 12.311  30.558  1.00 35.56 ? 128 ASP C O   1 
ATOM   6732 C CB  . ASP C 1 128 ? 64.175 14.953  31.212  1.00 34.81 ? 128 ASP C CB  1 
ATOM   6733 C CG  . ASP C 1 128 ? 65.378 15.811  30.856  1.00 38.76 ? 128 ASP C CG  1 
ATOM   6734 O OD1 . ASP C 1 128 ? 66.316 15.329  30.174  1.00 42.14 ? 128 ASP C OD1 1 
ATOM   6735 O OD2 . ASP C 1 128 ? 65.390 16.987  31.275  1.00 37.02 ? 128 ASP C OD2 1 
ATOM   6736 N N   . LEU C 1 129 ? 63.114 12.522  32.605  1.00 29.11 ? 129 LEU C N   1 
ATOM   6737 C CA  . LEU C 1 129 ? 62.042 11.801  33.291  1.00 28.01 ? 129 LEU C CA  1 
ATOM   6738 C C   . LEU C 1 129 ? 61.486 12.739  34.347  1.00 29.69 ? 129 LEU C C   1 
ATOM   6739 O O   . LEU C 1 129 ? 62.225 13.134  35.252  1.00 34.00 ? 129 LEU C O   1 
ATOM   6740 C CB  . LEU C 1 129 ? 62.599 10.579  34.007  1.00 22.09 ? 129 LEU C CB  1 
ATOM   6741 C CG  . LEU C 1 129 ? 61.652 9.471   34.446  1.00 20.94 ? 129 LEU C CG  1 
ATOM   6742 C CD1 . LEU C 1 129 ? 62.114 9.073   35.807  1.00 24.89 ? 129 LEU C CD1 1 
ATOM   6743 C CD2 . LEU C 1 129 ? 60.196 9.860   34.470  1.00 16.36 ? 129 LEU C CD2 1 
ATOM   6744 N N   . ARG C 1 130 ? 60.212 13.111  34.229  1.00 26.44 ? 130 ARG C N   1 
ATOM   6745 C CA  . ARG C 1 130 ? 59.599 13.997  35.199  1.00 21.53 ? 130 ARG C CA  1 
ATOM   6746 C C   . ARG C 1 130 ? 58.507 13.245  35.960  1.00 25.72 ? 130 ARG C C   1 
ATOM   6747 O O   . ARG C 1 130 ? 57.562 12.716  35.355  1.00 19.74 ? 130 ARG C O   1 
ATOM   6748 C CB  . ARG C 1 130 ? 59.055 15.253  34.531  1.00 23.08 ? 130 ARG C CB  1 
ATOM   6749 C CG  . ARG C 1 130 ? 60.093 16.100  33.816  1.00 18.08 ? 130 ARG C CG  1 
ATOM   6750 C CD  . ARG C 1 130 ? 59.856 17.586  34.046  1.00 17.91 ? 130 ARG C CD  1 
ATOM   6751 N NE  . ARG C 1 130 ? 58.617 18.084  33.443  1.00 22.42 ? 130 ARG C NE  1 
ATOM   6752 C CZ  . ARG C 1 130 ? 57.799 18.977  34.006  1.00 26.72 ? 130 ARG C CZ  1 
ATOM   6753 N NH1 . ARG C 1 130 ? 58.046 19.483  35.211  1.00 31.97 ? 130 ARG C NH1 1 
ATOM   6754 N NH2 . ARG C 1 130 ? 56.750 19.422  33.333  1.00 29.06 ? 130 ARG C NH2 1 
ATOM   6755 N N   . ILE C 1 131 ? 58.662 13.199  37.286  1.00 25.65 ? 131 ILE C N   1 
ATOM   6756 C CA  . ILE C 1 131 ? 57.753 12.497  38.202  1.00 24.96 ? 131 ILE C CA  1 
ATOM   6757 C C   . ILE C 1 131 ? 57.162 13.446  39.255  1.00 23.91 ? 131 ILE C C   1 
ATOM   6758 O O   . ILE C 1 131 ? 57.848 14.333  39.766  1.00 26.96 ? 131 ILE C O   1 
ATOM   6759 C CB  . ILE C 1 131 ? 58.512 11.335  38.973  1.00 23.73 ? 131 ILE C CB  1 
ATOM   6760 C CG1 . ILE C 1 131 ? 58.780 10.145  38.055  1.00 27.62 ? 131 ILE C CG1 1 
ATOM   6761 C CG2 . ILE C 1 131 ? 57.729 10.862  40.208  1.00 27.01 ? 131 ILE C CG2 1 
ATOM   6762 C CD1 . ILE C 1 131 ? 59.463 8.974   38.751  1.00 23.39 ? 131 ILE C CD1 1 
ATOM   6763 N N   . ILE C 1 132 ? 55.876 13.283  39.539  1.00 23.21 ? 132 ILE C N   1 
ATOM   6764 C CA  . ILE C 1 132 ? 55.208 14.071  40.567  1.00 24.24 ? 132 ILE C CA  1 
ATOM   6765 C C   . ILE C 1 132 ? 54.603 12.960  41.442  1.00 24.67 ? 132 ILE C C   1 
ATOM   6766 O O   . ILE C 1 132 ? 54.123 11.945  40.910  1.00 21.88 ? 132 ILE C O   1 
ATOM   6767 C CB  . ILE C 1 132 ? 54.147 15.084  39.957  1.00 22.70 ? 132 ILE C CB  1 
ATOM   6768 C CG1 . ILE C 1 132 ? 53.445 15.892  41.066  1.00 22.07 ? 132 ILE C CG1 1 
ATOM   6769 C CG2 . ILE C 1 132 ? 53.128 14.361  39.083  1.00 17.33 ? 132 ILE C CG2 1 
ATOM   6770 C CD1 . ILE C 1 132 ? 54.390 16.618  42.041  1.00 10.30 ? 132 ILE C CD1 1 
ATOM   6771 N N   . GLN C 1 133 ? 54.730 13.076  42.764  1.00 19.69 ? 133 GLN C N   1 
ATOM   6772 C CA  . GLN C 1 133 ? 54.202 12.036  43.616  1.00 20.67 ? 133 GLN C CA  1 
ATOM   6773 C C   . GLN C 1 133 ? 53.535 12.451  44.934  1.00 24.34 ? 133 GLN C C   1 
ATOM   6774 O O   . GLN C 1 133 ? 53.991 13.372  45.623  1.00 25.50 ? 133 GLN C O   1 
ATOM   6775 C CB  . GLN C 1 133 ? 55.274 10.974  43.868  1.00 22.68 ? 133 GLN C CB  1 
ATOM   6776 C CG  . GLN C 1 133 ? 56.575 11.443  44.511  1.00 36.56 ? 133 GLN C CG  1 
ATOM   6777 C CD  . GLN C 1 133 ? 57.513 10.286  44.853  1.00 38.00 ? 133 GLN C CD  1 
ATOM   6778 O OE1 . GLN C 1 133 ? 57.195 9.127   44.621  1.00 46.18 ? 133 GLN C OE1 1 
ATOM   6779 N NE2 . GLN C 1 133 ? 58.661 10.600  45.427  1.00 40.68 ? 133 GLN C NE2 1 
ATOM   6780 N N   . LEU C 1 134 ? 52.420 11.791  45.253  1.00 22.11 ? 134 LEU C N   1 
ATOM   6781 C CA  . LEU C 1 134 ? 51.705 12.058  46.483  1.00 19.68 ? 134 LEU C CA  1 
ATOM   6782 C C   . LEU C 1 134 ? 52.300 11.123  47.547  1.00 23.76 ? 134 LEU C C   1 
ATOM   6783 O O   . LEU C 1 134 ? 52.500 9.932   47.292  1.00 21.34 ? 134 LEU C O   1 
ATOM   6784 C CB  . LEU C 1 134 ? 50.210 11.784  46.305  1.00 16.41 ? 134 LEU C CB  1 
ATOM   6785 C CG  . LEU C 1 134 ? 49.299 12.014  47.528  1.00 10.25 ? 134 LEU C CG  1 
ATOM   6786 C CD1 . LEU C 1 134 ? 49.326 13.497  47.965  1.00 9.49  ? 134 LEU C CD1 1 
ATOM   6787 C CD2 . LEU C 1 134 ? 47.886 11.553  47.218  1.00 5.14  ? 134 LEU C CD2 1 
ATOM   6788 N N   . ALA C 1 135 ? 52.521 11.653  48.747  1.00 24.46 ? 135 ALA C N   1 
ATOM   6789 C CA  . ALA C 1 135 ? 53.091 10.883  49.837  1.00 26.37 ? 135 ALA C CA  1 
ATOM   6790 C C   . ALA C 1 135 ? 52.247 10.942  51.104  1.00 25.07 ? 135 ALA C C   1 
ATOM   6791 O O   . ALA C 1 135 ? 51.774 12.002  51.478  1.00 28.01 ? 135 ALA C O   1 
ATOM   6792 C CB  . ALA C 1 135 ? 54.473 11.401  50.136  1.00 25.82 ? 135 ALA C CB  1 
ATOM   6793 N N   . MET C 1 136 ? 52.051 9.797   51.750  1.00 23.25 ? 136 MET C N   1 
ATOM   6794 C CA  . MET C 1 136 ? 51.308 9.721   52.996  1.00 25.56 ? 136 MET C CA  1 
ATOM   6795 C C   . MET C 1 136 ? 52.238 9.081   54.031  1.00 26.45 ? 136 MET C C   1 
ATOM   6796 O O   . MET C 1 136 ? 52.315 7.855   54.148  1.00 29.53 ? 136 MET C O   1 
ATOM   6797 C CB  . MET C 1 136 ? 49.983 8.953   52.829  1.00 34.36 ? 136 MET C CB  1 
ATOM   6798 C CG  . MET C 1 136 ? 49.956 7.840   51.767  1.00 47.41 ? 136 MET C CG  1 
ATOM   6799 S SD  . MET C 1 136 ? 49.005 8.189   50.211  1.00 53.56 ? 136 MET C SD  1 
ATOM   6800 C CE  . MET C 1 136 ? 47.356 8.263   50.851  1.00 42.07 ? 136 MET C CE  1 
ATOM   6801 N N   . PRO C 1 137 ? 52.980 9.920   54.787  1.00 24.78 ? 137 PRO C N   1 
ATOM   6802 C CA  . PRO C 1 137 ? 53.939 9.511   55.816  1.00 17.13 ? 137 PRO C CA  1 
ATOM   6803 C C   . PRO C 1 137 ? 53.306 8.744   56.969  1.00 16.01 ? 137 PRO C C   1 
ATOM   6804 O O   . PRO C 1 137 ? 52.196 9.047   57.402  1.00 18.46 ? 137 PRO C O   1 
ATOM   6805 C CB  . PRO C 1 137 ? 54.531 10.847  56.279  1.00 17.23 ? 137 PRO C CB  1 
ATOM   6806 C CG  . PRO C 1 137 ? 54.075 11.875  55.271  1.00 11.12 ? 137 PRO C CG  1 
ATOM   6807 C CD  . PRO C 1 137 ? 52.752 11.374  54.864  1.00 21.65 ? 137 PRO C CD  1 
ATOM   6808 N N   . VAL C 1 138 ? 54.056 7.790   57.499  1.00 16.46 ? 138 VAL C N   1 
ATOM   6809 C CA  . VAL C 1 138 ? 53.591 6.943   58.576  1.00 18.13 ? 138 VAL C CA  1 
ATOM   6810 C C   . VAL C 1 138 ? 53.877 7.437   59.995  1.00 21.01 ? 138 VAL C C   1 
ATOM   6811 O O   . VAL C 1 138 ? 53.044 7.343   60.893  1.00 20.37 ? 138 VAL C O   1 
ATOM   6812 C CB  . VAL C 1 138 ? 54.254 5.545   58.477  1.00 22.70 ? 138 VAL C CB  1 
ATOM   6813 C CG1 . VAL C 1 138 ? 53.564 4.527   59.398  1.00 22.73 ? 138 VAL C CG1 1 
ATOM   6814 C CG2 . VAL C 1 138 ? 54.228 5.049   57.066  1.00 30.83 ? 138 VAL C CG2 1 
ATOM   6815 N N   . ASN C 1 139 ? 55.090 7.914   60.198  1.00 23.95 ? 139 ASN C N   1 
ATOM   6816 C CA  . ASN C 1 139 ? 55.547 8.331   61.517  1.00 21.78 ? 139 ASN C CA  1 
ATOM   6817 C C   . ASN C 1 139 ? 55.063 9.663   62.108  1.00 24.12 ? 139 ASN C C   1 
ATOM   6818 O O   . ASN C 1 139 ? 54.668 9.732   63.282  1.00 23.12 ? 139 ASN C O   1 
ATOM   6819 C CB  . ASN C 1 139 ? 57.081 8.199   61.548  1.00 19.41 ? 139 ASN C CB  1 
ATOM   6820 C CG  . ASN C 1 139 ? 57.551 6.742   61.378  1.00 17.19 ? 139 ASN C CG  1 
ATOM   6821 O OD1 . ASN C 1 139 ? 57.128 5.865   62.107  1.00 12.06 ? 139 ASN C OD1 1 
ATOM   6822 N ND2 . ASN C 1 139 ? 58.437 6.497   60.425  1.00 15.95 ? 139 ASN C ND2 1 
ATOM   6823 N N   . ASN C 1 140 ? 55.136 10.715  61.304  1.00 24.41 ? 140 ASN C N   1 
ATOM   6824 C CA  . ASN C 1 140 ? 54.726 12.066  61.691  1.00 25.50 ? 140 ASN C CA  1 
ATOM   6825 C C   . ASN C 1 140 ? 54.670 12.829  60.367  1.00 26.05 ? 140 ASN C C   1 
ATOM   6826 O O   . ASN C 1 140 ? 54.856 12.197  59.320  1.00 26.72 ? 140 ASN C O   1 
ATOM   6827 C CB  . ASN C 1 140 ? 55.720 12.681  62.680  1.00 24.80 ? 140 ASN C CB  1 
ATOM   6828 C CG  . ASN C 1 140 ? 57.163 12.576  62.222  1.00 26.04 ? 140 ASN C CG  1 
ATOM   6829 O OD1 . ASN C 1 140 ? 57.543 13.105  61.172  1.00 31.75 ? 140 ASN C OD1 1 
ATOM   6830 N ND2 . ASN C 1 140 ? 57.979 11.900  63.013  1.00 18.86 ? 140 ASN C ND2 1 
ATOM   6831 N N   . PRO C 1 141 ? 54.422 14.165  60.372  1.00 23.10 ? 141 PRO C N   1 
ATOM   6832 C CA  . PRO C 1 141 ? 54.352 14.904  59.098  1.00 24.83 ? 141 PRO C CA  1 
ATOM   6833 C C   . PRO C 1 141 ? 55.563 14.982  58.152  1.00 26.31 ? 141 PRO C C   1 
ATOM   6834 O O   . PRO C 1 141 ? 55.402 15.313  56.961  1.00 23.11 ? 141 PRO C O   1 
ATOM   6835 C CB  . PRO C 1 141 ? 53.838 16.282  59.529  1.00 18.40 ? 141 PRO C CB  1 
ATOM   6836 C CG  . PRO C 1 141 ? 52.958 15.959  60.651  1.00 21.13 ? 141 PRO C CG  1 
ATOM   6837 C CD  . PRO C 1 141 ? 53.837 14.987  61.441  1.00 22.83 ? 141 PRO C CD  1 
ATOM   6838 N N   . GLN C 1 142 ? 56.753 14.664  58.658  1.00 25.00 ? 142 GLN C N   1 
ATOM   6839 C CA  . GLN C 1 142 ? 57.957 14.692  57.835  1.00 27.96 ? 142 GLN C CA  1 
ATOM   6840 C C   . GLN C 1 142 ? 58.071 13.406  57.050  1.00 28.66 ? 142 GLN C C   1 
ATOM   6841 O O   . GLN C 1 142 ? 57.716 12.342  57.554  1.00 30.31 ? 142 GLN C O   1 
ATOM   6842 C CB  . GLN C 1 142 ? 59.214 14.829  58.703  1.00 31.93 ? 142 GLN C CB  1 
ATOM   6843 C CG  . GLN C 1 142 ? 59.628 16.250  59.035  1.00 33.41 ? 142 GLN C CG  1 
ATOM   6844 C CD  . GLN C 1 142 ? 58.483 17.102  59.508  1.00 41.05 ? 142 GLN C CD  1 
ATOM   6845 O OE1 . GLN C 1 142 ? 57.805 16.779  60.487  1.00 47.51 ? 142 GLN C OE1 1 
ATOM   6846 N NE2 . GLN C 1 142 ? 58.245 18.200  58.805  1.00 45.15 ? 142 GLN C NE2 1 
ATOM   6847 N N   . ILE C 1 143 ? 58.616 13.510  55.840  1.00 28.14 ? 143 ILE C N   1 
ATOM   6848 C CA  . ILE C 1 143 ? 58.840 12.355  54.970  1.00 27.15 ? 143 ILE C CA  1 
ATOM   6849 C C   . ILE C 1 143 ? 60.355 12.072  55.037  1.00 26.67 ? 143 ILE C C   1 
ATOM   6850 O O   . ILE C 1 143 ? 61.157 12.984  54.863  1.00 27.98 ? 143 ILE C O   1 
ATOM   6851 C CB  . ILE C 1 143 ? 58.305 12.611  53.482  1.00 22.36 ? 143 ILE C CB  1 
ATOM   6852 C CG1 . ILE C 1 143 ? 58.977 11.694  52.461  1.00 24.17 ? 143 ILE C CG1 1 
ATOM   6853 C CG2 . ILE C 1 143 ? 58.559 14.016  53.042  1.00 21.99 ? 143 ILE C CG2 1 
ATOM   6854 C CD1 . ILE C 1 143 ? 58.623 10.228  52.570  1.00 28.54 ? 143 ILE C CD1 1 
ATOM   6855 N N   . HIS C 1 144 ? 60.734 10.851  55.423  1.00 25.16 ? 144 HIS C N   1 
ATOM   6856 C CA  . HIS C 1 144 ? 62.149 10.474  55.527  1.00 25.44 ? 144 HIS C CA  1 
ATOM   6857 C C   . HIS C 1 144 ? 62.492 9.450   54.447  1.00 29.45 ? 144 HIS C C   1 
ATOM   6858 O O   . HIS C 1 144 ? 61.651 8.609   54.117  1.00 29.34 ? 144 HIS C O   1 
ATOM   6859 C CB  . HIS C 1 144 ? 62.466 9.909   56.918  1.00 25.17 ? 144 HIS C CB  1 
ATOM   6860 C CG  . HIS C 1 144 ? 62.039 10.808  58.041  1.00 28.84 ? 144 HIS C CG  1 
ATOM   6861 N ND1 . HIS C 1 144 ? 60.963 10.521  58.854  1.00 29.62 ? 144 HIS C ND1 1 
ATOM   6862 C CD2 . HIS C 1 144 ? 62.485 12.025  58.431  1.00 32.39 ? 144 HIS C CD2 1 
ATOM   6863 C CE1 . HIS C 1 144 ? 60.756 11.527  59.686  1.00 28.47 ? 144 HIS C CE1 1 
ATOM   6864 N NE2 . HIS C 1 144 ? 61.666 12.453  59.451  1.00 31.69 ? 144 HIS C NE2 1 
ATOM   6865 N N   . GLU C 1 145 ? 63.694 9.560   53.868  1.00 31.04 ? 145 GLU C N   1 
ATOM   6866 C CA  . GLU C 1 145 ? 64.175 8.647   52.812  1.00 35.59 ? 145 GLU C CA  1 
ATOM   6867 C C   . GLU C 1 145 ? 65.508 8.049   53.224  1.00 29.88 ? 145 GLU C C   1 
ATOM   6868 O O   . GLU C 1 145 ? 66.487 8.766   53.311  1.00 36.25 ? 145 GLU C O   1 
ATOM   6869 C CB  . GLU C 1 145 ? 64.372 9.410   51.488  1.00 40.26 ? 145 GLU C CB  1 
ATOM   6870 C CG  . GLU C 1 145 ? 63.089 10.028  50.942  1.00 51.21 ? 145 GLU C CG  1 
ATOM   6871 C CD  . GLU C 1 145 ? 63.296 10.894  49.713  1.00 57.23 ? 145 GLU C CD  1 
ATOM   6872 O OE1 . GLU C 1 145 ? 63.944 10.430  48.749  1.00 59.18 ? 145 GLU C OE1 1 
ATOM   6873 O OE2 . GLU C 1 145 ? 62.783 12.037  49.705  1.00 60.37 ? 145 GLU C OE2 1 
ATOM   6874 N N   . PHE C 1 146 ? 65.559 6.756   53.506  1.00 24.47 ? 146 PHE C N   1 
ATOM   6875 C CA  . PHE C 1 146 ? 66.820 6.155   53.895  1.00 16.18 ? 146 PHE C CA  1 
ATOM   6876 C C   . PHE C 1 146 ? 67.540 5.588   52.685  1.00 21.47 ? 146 PHE C C   1 
ATOM   6877 O O   . PHE C 1 146 ? 67.051 4.661   52.057  1.00 18.87 ? 146 PHE C O   1 
ATOM   6878 C CB  . PHE C 1 146 ? 66.582 5.055   54.909  1.00 16.99 ? 146 PHE C CB  1 
ATOM   6879 C CG  . PHE C 1 146 ? 65.991 5.548   56.189  1.00 16.21 ? 146 PHE C CG  1 
ATOM   6880 C CD1 . PHE C 1 146 ? 64.646 5.900   56.255  1.00 16.59 ? 146 PHE C CD1 1 
ATOM   6881 C CD2 . PHE C 1 146 ? 66.788 5.705   57.327  1.00 17.97 ? 146 PHE C CD2 1 
ATOM   6882 C CE1 . PHE C 1 146 ? 64.093 6.406   57.427  1.00 18.43 ? 146 PHE C CE1 1 
ATOM   6883 C CE2 . PHE C 1 146 ? 66.246 6.210   58.507  1.00 9.04  ? 146 PHE C CE2 1 
ATOM   6884 C CZ  . PHE C 1 146 ? 64.889 6.561   58.550  1.00 2.00  ? 146 PHE C CZ  1 
ATOM   6885 N N   . PHE C 1 147 ? 68.686 6.168   52.343  1.00 24.17 ? 147 PHE C N   1 
ATOM   6886 C CA  . PHE C 1 147 ? 69.496 5.709   51.220  1.00 25.49 ? 147 PHE C CA  1 
ATOM   6887 C C   . PHE C 1 147 ? 70.531 4.654   51.641  1.00 25.36 ? 147 PHE C C   1 
ATOM   6888 O O   . PHE C 1 147 ? 71.260 4.824   52.630  1.00 28.91 ? 147 PHE C O   1 
ATOM   6889 C CB  . PHE C 1 147 ? 70.164 6.900   50.528  1.00 24.86 ? 147 PHE C CB  1 
ATOM   6890 C CG  . PHE C 1 147 ? 69.320 7.520   49.438  1.00 24.47 ? 147 PHE C CG  1 
ATOM   6891 C CD1 . PHE C 1 147 ? 69.300 6.970   48.160  1.00 22.80 ? 147 PHE C CD1 1 
ATOM   6892 C CD2 . PHE C 1 147 ? 68.547 8.652   49.687  1.00 25.69 ? 147 PHE C CD2 1 
ATOM   6893 C CE1 . PHE C 1 147 ? 68.519 7.539   47.136  1.00 24.19 ? 147 PHE C CE1 1 
ATOM   6894 C CE2 . PHE C 1 147 ? 67.769 9.228   48.673  1.00 25.10 ? 147 PHE C CE2 1 
ATOM   6895 C CZ  . PHE C 1 147 ? 67.757 8.666   47.392  1.00 25.33 ? 147 PHE C CZ  1 
ATOM   6896 N N   . LEU C 1 148 ? 70.536 3.534   50.922  1.00 29.56 ? 148 LEU C N   1 
ATOM   6897 C CA  . LEU C 1 148 ? 71.439 2.407   51.189  1.00 26.51 ? 148 LEU C CA  1 
ATOM   6898 C C   . LEU C 1 148 ? 72.850 2.683   50.721  1.00 25.39 ? 148 LEU C C   1 
ATOM   6899 O O   . LEU C 1 148 ? 73.800 2.064   51.184  1.00 24.39 ? 148 LEU C O   1 
ATOM   6900 C CB  . LEU C 1 148 ? 70.950 1.158   50.454  1.00 22.71 ? 148 LEU C CB  1 
ATOM   6901 C CG  . LEU C 1 148 ? 70.904 -0.185  51.184  1.00 20.94 ? 148 LEU C CG  1 
ATOM   6902 C CD1 . LEU C 1 148 ? 71.098 -1.280  50.182  1.00 18.64 ? 148 LEU C CD1 1 
ATOM   6903 C CD2 . LEU C 1 148 ? 71.950 -0.283  52.256  1.00 14.35 ? 148 LEU C CD2 1 
ATOM   6904 N N   . SER C 1 149 ? 72.964 3.583   49.756  1.00 30.79 ? 149 SER C N   1 
ATOM   6905 C CA  . SER C 1 149 ? 74.236 3.954   49.153  1.00 34.12 ? 149 SER C CA  1 
ATOM   6906 C C   . SER C 1 149 ? 75.257 4.733   50.000  1.00 36.92 ? 149 SER C C   1 
ATOM   6907 O O   . SER C 1 149 ? 74.923 5.380   51.009  1.00 37.16 ? 149 SER C O   1 
ATOM   6908 C CB  . SER C 1 149 ? 73.958 4.739   47.865  1.00 33.46 ? 149 SER C CB  1 
ATOM   6909 O OG  . SER C 1 149 ? 72.838 5.593   48.020  1.00 34.33 ? 149 SER C OG  1 
ATOM   6910 N N   . SER C 1 150 ? 76.509 4.643   49.555  1.00 35.36 ? 150 SER C N   1 
ATOM   6911 C CA  . SER C 1 150 ? 77.640 5.348   50.137  1.00 33.68 ? 150 SER C CA  1 
ATOM   6912 C C   . SER C 1 150 ? 78.136 6.212   48.971  1.00 34.30 ? 150 SER C C   1 
ATOM   6913 O O   . SER C 1 150 ? 78.589 5.673   47.950  1.00 34.99 ? 150 SER C O   1 
ATOM   6914 C CB  . SER C 1 150 ? 78.747 4.366   50.529  1.00 32.31 ? 150 SER C CB  1 
ATOM   6915 O OG  . SER C 1 150 ? 79.181 4.571   51.867  1.00 40.84 ? 150 SER C OG  1 
ATOM   6916 N N   . THR C 1 151 ? 77.934 7.522   49.051  1.00 30.18 ? 151 THR C N   1 
ATOM   6917 C CA  . THR C 1 151 ? 78.416 8.400   48.000  1.00 32.09 ? 151 THR C CA  1 
ATOM   6918 C C   . THR C 1 151 ? 79.028 9.651   48.632  1.00 34.18 ? 151 THR C C   1 
ATOM   6919 O O   . THR C 1 151 ? 78.915 9.854   49.843  1.00 36.62 ? 151 THR C O   1 
ATOM   6920 C CB  . THR C 1 151 ? 77.304 8.780   46.988  1.00 30.52 ? 151 THR C CB  1 
ATOM   6921 O OG1 . THR C 1 151 ? 76.319 9.609   47.620  1.00 36.09 ? 151 THR C OG1 1 
ATOM   6922 C CG2 . THR C 1 151 ? 76.639 7.525   46.443  1.00 25.66 ? 151 THR C CG2 1 
ATOM   6923 N N   . GLU C 1 152 ? 79.708 10.462  47.823  1.00 32.08 ? 152 GLU C N   1 
ATOM   6924 C CA  . GLU C 1 152 ? 80.319 11.685  48.303  1.00 29.29 ? 152 GLU C CA  1 
ATOM   6925 C C   . GLU C 1 152 ? 79.259 12.537  48.995  1.00 32.11 ? 152 GLU C C   1 
ATOM   6926 O O   . GLU C 1 152 ? 79.550 13.227  49.976  1.00 36.45 ? 152 GLU C O   1 
ATOM   6927 C CB  . GLU C 1 152 ? 80.889 12.452  47.122  1.00 35.16 ? 152 GLU C CB  1 
ATOM   6928 C CG  . GLU C 1 152 ? 82.360 12.836  47.253  1.00 47.84 ? 152 GLU C CG  1 
ATOM   6929 C CD  . GLU C 1 152 ? 83.249 12.162  46.208  1.00 53.91 ? 152 GLU C CD  1 
ATOM   6930 O OE1 . GLU C 1 152 ? 83.308 12.680  45.060  1.00 52.40 ? 152 GLU C OE1 1 
ATOM   6931 O OE2 . GLU C 1 152 ? 83.889 11.127  46.543  1.00 55.31 ? 152 GLU C OE2 1 
ATOM   6932 N N   . ALA C 1 153 ? 78.026 12.457  48.491  1.00 30.04 ? 153 ALA C N   1 
ATOM   6933 C CA  . ALA C 1 153 ? 76.880 13.216  49.008  1.00 27.50 ? 153 ALA C CA  1 
ATOM   6934 C C   . ALA C 1 153 ? 76.321 12.744  50.335  1.00 29.37 ? 153 ALA C C   1 
ATOM   6935 O O   . ALA C 1 153 ? 75.924 13.545  51.177  1.00 36.18 ? 153 ALA C O   1 
ATOM   6936 C CB  . ALA C 1 153 ? 75.757 13.215  47.990  1.00 22.84 ? 153 ALA C CB  1 
ATOM   6937 N N   . GLN C 1 154 ? 76.231 11.439  50.511  1.00 27.70 ? 154 GLN C N   1 
ATOM   6938 C CA  . GLN C 1 154 ? 75.660 10.931  51.729  1.00 24.08 ? 154 GLN C CA  1 
ATOM   6939 C C   . GLN C 1 154 ? 76.212 9.585   52.101  1.00 25.21 ? 154 GLN C C   1 
ATOM   6940 O O   . GLN C 1 154 ? 76.638 8.818   51.243  1.00 24.60 ? 154 GLN C O   1 
ATOM   6941 C CB  . GLN C 1 154 ? 74.133 10.844  51.573  1.00 25.47 ? 154 GLN C CB  1 
ATOM   6942 C CG  . GLN C 1 154 ? 73.649 10.209  50.273  1.00 20.63 ? 154 GLN C CG  1 
ATOM   6943 C CD  . GLN C 1 154 ? 73.875 8.700   50.198  1.00 33.00 ? 154 GLN C CD  1 
ATOM   6944 O OE1 . GLN C 1 154 ? 74.218 8.167   49.127  1.00 31.21 ? 154 GLN C OE1 1 
ATOM   6945 N NE2 . GLN C 1 154 ? 73.672 7.999   51.325  1.00 28.49 ? 154 GLN C NE2 1 
ATOM   6946 N N   . GLN C 1 155 ? 76.176 9.292   53.391  1.00 27.91 ? 155 GLN C N   1 
ATOM   6947 C CA  . GLN C 1 155 ? 76.645 8.010   53.864  1.00 33.17 ? 155 GLN C CA  1 
ATOM   6948 C C   . GLN C 1 155 ? 75.459 7.071   53.984  1.00 34.00 ? 155 GLN C C   1 
ATOM   6949 O O   . GLN C 1 155 ? 74.297 7.496   54.046  1.00 34.96 ? 155 GLN C O   1 
ATOM   6950 C CB  . GLN C 1 155 ? 77.388 8.140   55.197  1.00 35.41 ? 155 GLN C CB  1 
ATOM   6951 C CG  . GLN C 1 155 ? 78.695 8.933   55.075  1.00 47.58 ? 155 GLN C CG  1 
ATOM   6952 C CD  . GLN C 1 155 ? 79.470 9.040   56.377  1.00 52.31 ? 155 GLN C CD  1 
ATOM   6953 O OE1 . GLN C 1 155 ? 80.698 9.092   56.373  1.00 58.93 ? 155 GLN C OE1 1 
ATOM   6954 N NE2 . GLN C 1 155 ? 78.758 9.093   57.496  1.00 58.22 ? 155 GLN C NE2 1 
ATOM   6955 N N   . SER C 1 156 ? 75.758 5.786   53.932  1.00 31.92 ? 156 SER C N   1 
ATOM   6956 C CA  . SER C 1 156 ? 74.736 4.781   54.044  1.00 28.19 ? 156 SER C CA  1 
ATOM   6957 C C   . SER C 1 156 ? 74.344 4.645   55.524  1.00 32.04 ? 156 SER C C   1 
ATOM   6958 O O   . SER C 1 156 ? 75.195 4.844   56.409  1.00 33.73 ? 156 SER C O   1 
ATOM   6959 C CB  . SER C 1 156 ? 75.291 3.469   53.518  1.00 15.85 ? 156 SER C CB  1 
ATOM   6960 O OG  . SER C 1 156 ? 74.333 2.466   53.698  1.00 13.55 ? 156 SER C OG  1 
ATOM   6961 N N   . TYR C 1 157 ? 73.072 4.332   55.803  1.00 30.10 ? 157 TYR C N   1 
ATOM   6962 C CA  . TYR C 1 157 ? 72.640 4.148   57.191  1.00 25.62 ? 157 TYR C CA  1 
ATOM   6963 C C   . TYR C 1 157 ? 73.351 2.956   57.810  1.00 26.11 ? 157 TYR C C   1 
ATOM   6964 O O   . TYR C 1 157 ? 73.343 2.776   59.024  1.00 25.54 ? 157 TYR C O   1 
ATOM   6965 C CB  . TYR C 1 157 ? 71.111 4.034   57.334  1.00 24.18 ? 157 TYR C CB  1 
ATOM   6966 C CG  . TYR C 1 157 ? 70.416 3.043   56.434  1.00 20.55 ? 157 TYR C CG  1 
ATOM   6967 C CD1 . TYR C 1 157 ? 70.357 1.688   56.759  1.00 16.15 ? 157 TYR C CD1 1 
ATOM   6968 C CD2 . TYR C 1 157 ? 69.769 3.473   55.280  1.00 22.00 ? 157 TYR C CD2 1 
ATOM   6969 C CE1 . TYR C 1 157 ? 69.666 0.795   55.956  1.00 22.63 ? 157 TYR C CE1 1 
ATOM   6970 C CE2 . TYR C 1 157 ? 69.071 2.590   54.464  1.00 17.37 ? 157 TYR C CE2 1 
ATOM   6971 C CZ  . TYR C 1 157 ? 69.015 1.257   54.803  1.00 24.21 ? 157 TYR C CZ  1 
ATOM   6972 O OH  . TYR C 1 157 ? 68.249 0.408   54.029  1.00 22.17 ? 157 TYR C OH  1 
ATOM   6973 N N   . LEU C 1 158 ? 74.011 2.166   56.966  1.00 27.76 ? 158 LEU C N   1 
ATOM   6974 C CA  . LEU C 1 158 ? 74.777 1.030   57.445  1.00 29.18 ? 158 LEU C CA  1 
ATOM   6975 C C   . LEU C 1 158 ? 75.912 1.605   58.284  1.00 28.99 ? 158 LEU C C   1 
ATOM   6976 O O   . LEU C 1 158 ? 76.085 1.221   59.435  1.00 31.60 ? 158 LEU C O   1 
ATOM   6977 C CB  . LEU C 1 158 ? 75.306 0.208   56.267  1.00 27.31 ? 158 LEU C CB  1 
ATOM   6978 C CG  . LEU C 1 158 ? 74.226 -0.639  55.568  1.00 30.31 ? 158 LEU C CG  1 
ATOM   6979 C CD1 . LEU C 1 158 ? 74.772 -1.336  54.349  1.00 24.95 ? 158 LEU C CD1 1 
ATOM   6980 C CD2 . LEU C 1 158 ? 73.656 -1.659  56.549  1.00 24.21 ? 158 LEU C CD2 1 
ATOM   6981 N N   . GLN C 1 159 ? 76.574 2.632   57.742  1.00 30.97 ? 159 GLN C N   1 
ATOM   6982 C CA  . GLN C 1 159 ? 77.699 3.342   58.398  1.00 31.53 ? 159 GLN C CA  1 
ATOM   6983 C C   . GLN C 1 159 ? 77.385 3.935   59.795  1.00 30.98 ? 159 GLN C C   1 
ATOM   6984 O O   . GLN C 1 159 ? 78.272 4.425   60.484  1.00 25.48 ? 159 GLN C O   1 
ATOM   6985 C CB  . GLN C 1 159 ? 78.200 4.489   57.485  1.00 26.59 ? 159 GLN C CB  1 
ATOM   6986 C CG  . GLN C 1 159 ? 79.427 4.181   56.631  1.00 25.60 ? 159 GLN C CG  1 
ATOM   6987 C CD  . GLN C 1 159 ? 79.607 5.153   55.438  1.00 34.53 ? 159 GLN C CD  1 
ATOM   6988 O OE1 . GLN C 1 159 ? 80.469 6.038   55.460  1.00 36.45 ? 159 GLN C OE1 1 
ATOM   6989 N NE2 . GLN C 1 159 ? 78.801 4.970   54.391  1.00 17.41 ? 159 GLN C NE2 1 
ATOM   6990 N N   . GLU C 1 160 ? 76.130 3.886   60.207  1.00 30.74 ? 160 GLU C N   1 
ATOM   6991 C CA  . GLU C 1 160 ? 75.743 4.457   61.473  1.00 30.63 ? 160 GLU C CA  1 
ATOM   6992 C C   . GLU C 1 160 ? 75.726 3.519   62.676  1.00 31.12 ? 160 GLU C C   1 
ATOM   6993 O O   . GLU C 1 160 ? 75.472 3.965   63.801  1.00 30.98 ? 160 GLU C O   1 
ATOM   6994 C CB  . GLU C 1 160 ? 74.396 5.141   61.306  1.00 36.10 ? 160 GLU C CB  1 
ATOM   6995 C CG  . GLU C 1 160 ? 74.452 6.362   60.418  1.00 35.38 ? 160 GLU C CG  1 
ATOM   6996 C CD  . GLU C 1 160 ? 75.176 7.517   61.065  1.00 36.06 ? 160 GLU C CD  1 
ATOM   6997 O OE1 . GLU C 1 160 ? 75.406 7.486   62.297  1.00 31.78 ? 160 GLU C OE1 1 
ATOM   6998 O OE2 . GLU C 1 160 ? 75.517 8.465   60.328  1.00 47.47 ? 160 GLU C OE2 1 
ATOM   6999 N N   . PHE C 1 161 ? 75.926 2.222   62.440  1.00 28.95 ? 161 PHE C N   1 
ATOM   7000 C CA  . PHE C 1 161 ? 75.964 1.247   63.533  1.00 25.92 ? 161 PHE C CA  1 
ATOM   7001 C C   . PHE C 1 161 ? 77.405 1.118   63.975  1.00 27.58 ? 161 PHE C C   1 
ATOM   7002 O O   . PHE C 1 161 ? 78.320 1.562   63.286  1.00 22.25 ? 161 PHE C O   1 
ATOM   7003 C CB  . PHE C 1 161 ? 75.443 -0.119  63.100  1.00 20.61 ? 161 PHE C CB  1 
ATOM   7004 C CG  . PHE C 1 161 ? 73.956 -0.171  62.899  1.00 21.87 ? 161 PHE C CG  1 
ATOM   7005 C CD1 . PHE C 1 161 ? 73.082 0.073   63.961  1.00 16.53 ? 161 PHE C CD1 1 
ATOM   7006 C CD2 . PHE C 1 161 ? 73.422 -0.503  61.659  1.00 19.63 ? 161 PHE C CD2 1 
ATOM   7007 C CE1 . PHE C 1 161 ? 71.694 -0.016  63.795  1.00 20.72 ? 161 PHE C CE1 1 
ATOM   7008 C CE2 . PHE C 1 161 ? 72.033 -0.595  61.483  1.00 21.91 ? 161 PHE C CE2 1 
ATOM   7009 C CZ  . PHE C 1 161 ? 71.171 -0.351  62.557  1.00 23.39 ? 161 PHE C CZ  1 
ATOM   7010 N N   . SER C 1 162 ? 77.615 0.467   65.108  1.00 33.45 ? 162 SER C N   1 
ATOM   7011 C CA  . SER C 1 162 ? 78.966 0.314   65.639  1.00 35.10 ? 162 SER C CA  1 
ATOM   7012 C C   . SER C 1 162 ? 79.808 -0.728  64.912  1.00 33.33 ? 162 SER C C   1 
ATOM   7013 O O   . SER C 1 162 ? 79.298 -1.784  64.545  1.00 34.38 ? 162 SER C O   1 
ATOM   7014 C CB  . SER C 1 162 ? 78.899 -0.012  67.137  1.00 37.05 ? 162 SER C CB  1 
ATOM   7015 O OG  . SER C 1 162 ? 78.084 -1.150  67.376  1.00 41.34 ? 162 SER C OG  1 
ATOM   7016 N N   . LYS C 1 163 ? 81.097 -0.431  64.749  1.00 35.27 ? 163 LYS C N   1 
ATOM   7017 C CA  . LYS C 1 163 ? 82.063 -1.312  64.094  1.00 39.57 ? 163 LYS C CA  1 
ATOM   7018 C C   . LYS C 1 163 ? 81.937 -2.755  64.531  1.00 41.04 ? 163 LYS C C   1 
ATOM   7019 O O   . LYS C 1 163 ? 81.978 -3.666  63.700  1.00 44.70 ? 163 LYS C O   1 
ATOM   7020 C CB  . LYS C 1 163 ? 83.500 -0.864  64.379  1.00 44.21 ? 163 LYS C CB  1 
ATOM   7021 C CG  . LYS C 1 163 ? 84.544 -1.982  64.178  1.00 55.79 ? 163 LYS C CG  1 
ATOM   7022 C CD  . LYS C 1 163 ? 85.945 -1.595  64.640  1.00 64.91 ? 163 LYS C CD  1 
ATOM   7023 C CE  . LYS C 1 163 ? 86.479 -0.420  63.836  1.00 73.07 ? 163 LYS C CE  1 
ATOM   7024 N NZ  . LYS C 1 163 ? 87.854 -0.024  64.257  1.00 82.17 ? 163 LYS C NZ  1 
ATOM   7025 N N   . HIS C 1 164 ? 81.820 -2.964  65.837  1.00 38.52 ? 164 HIS C N   1 
ATOM   7026 C CA  . HIS C 1 164 ? 81.703 -4.303  66.369  1.00 40.67 ? 164 HIS C CA  1 
ATOM   7027 C C   . HIS C 1 164 ? 80.370 -4.967  66.058  1.00 39.57 ? 164 HIS C C   1 
ATOM   7028 O O   . HIS C 1 164 ? 80.313 -6.187  65.900  1.00 39.75 ? 164 HIS C O   1 
ATOM   7029 C CB  . HIS C 1 164 ? 82.029 -4.306  67.858  1.00 51.04 ? 164 HIS C CB  1 
ATOM   7030 C CG  . HIS C 1 164 ? 83.480 -4.038  68.150  1.00 59.10 ? 164 HIS C CG  1 
ATOM   7031 N ND1 . HIS C 1 164 ? 83.937 -3.644  69.390  1.00 61.23 ? 164 HIS C ND1 1 
ATOM   7032 C CD2 . HIS C 1 164 ? 84.578 -4.127  67.358  1.00 59.45 ? 164 HIS C CD2 1 
ATOM   7033 C CE1 . HIS C 1 164 ? 85.251 -3.506  69.353  1.00 61.69 ? 164 HIS C CE1 1 
ATOM   7034 N NE2 . HIS C 1 164 ? 85.665 -3.793  68.130  1.00 59.72 ? 164 HIS C NE2 1 
ATOM   7035 N N   . ILE C 1 165 ? 79.310 -4.171  65.914  1.00 39.67 ? 165 ILE C N   1 
ATOM   7036 C CA  . ILE C 1 165 ? 77.993 -4.712  65.566  1.00 35.52 ? 165 ILE C CA  1 
ATOM   7037 C C   . ILE C 1 165 ? 78.023 -5.099  64.082  1.00 36.81 ? 165 ILE C C   1 
ATOM   7038 O O   . ILE C 1 165 ? 77.558 -6.181  63.708  1.00 39.11 ? 165 ILE C O   1 
ATOM   7039 C CB  . ILE C 1 165 ? 76.836 -3.716  65.934  1.00 33.48 ? 165 ILE C CB  1 
ATOM   7040 C CG1 . ILE C 1 165 ? 76.108 -4.246  67.165  1.00 34.72 ? 165 ILE C CG1 1 
ATOM   7041 C CG2 . ILE C 1 165 ? 75.830 -3.525  64.806  1.00 24.86 ? 165 ILE C CG2 1 
ATOM   7042 C CD1 . ILE C 1 165 ? 75.045 -3.329  67.718  1.00 40.29 ? 165 ILE C CD1 1 
ATOM   7043 N N   . LEU C 1 166 ? 78.657 -4.262  63.262  1.00 34.24 ? 166 LEU C N   1 
ATOM   7044 C CA  . LEU C 1 166 ? 78.784 -4.532  61.833  1.00 37.16 ? 166 LEU C CA  1 
ATOM   7045 C C   . LEU C 1 166 ? 79.628 -5.786  61.637  1.00 37.12 ? 166 LEU C C   1 
ATOM   7046 O O   . LEU C 1 166 ? 79.318 -6.607  60.774  1.00 38.33 ? 166 LEU C O   1 
ATOM   7047 C CB  . LEU C 1 166 ? 79.421 -3.339  61.113  1.00 39.87 ? 166 LEU C CB  1 
ATOM   7048 C CG  . LEU C 1 166 ? 78.543 -2.449  60.213  1.00 44.95 ? 166 LEU C CG  1 
ATOM   7049 C CD1 . LEU C 1 166 ? 77.077 -2.488  60.614  1.00 41.93 ? 166 LEU C CD1 1 
ATOM   7050 C CD2 . LEU C 1 166 ? 79.079 -1.011  60.226  1.00 41.65 ? 166 LEU C CD2 1 
ATOM   7051 N N   . GLU C 1 167 ? 80.656 -5.956  62.471  1.00 36.80 ? 167 GLU C N   1 
ATOM   7052 C CA  . GLU C 1 167 ? 81.538 -7.125  62.398  1.00 33.59 ? 167 GLU C CA  1 
ATOM   7053 C C   . GLU C 1 167 ? 80.804 -8.424  62.710  1.00 34.57 ? 167 GLU C C   1 
ATOM   7054 O O   . GLU C 1 167 ? 80.912 -9.411  61.963  1.00 35.95 ? 167 GLU C O   1 
ATOM   7055 C CB  . GLU C 1 167 ? 82.727 -6.979  63.346  1.00 28.80 ? 167 GLU C CB  1 
ATOM   7056 C CG  . GLU C 1 167 ? 83.763 -5.943  62.922  1.00 26.10 ? 167 GLU C CG  1 
ATOM   7057 C CD  . GLU C 1 167 ? 85.072 -6.071  63.691  1.00 29.30 ? 167 GLU C CD  1 
ATOM   7058 O OE1 . GLU C 1 167 ? 85.053 -6.463  64.879  1.00 34.35 ? 167 GLU C OE1 1 
ATOM   7059 O OE2 . GLU C 1 167 ? 86.128 -5.787  63.105  1.00 25.41 ? 167 GLU C OE2 1 
ATOM   7060 N N   . ALA C 1 168 ? 80.064 -8.424  63.813  1.00 33.33 ? 168 ALA C N   1 
ATOM   7061 C CA  . ALA C 1 168 ? 79.295 -9.591  64.211  1.00 33.11 ? 168 ALA C CA  1 
ATOM   7062 C C   . ALA C 1 168 ? 78.231 -9.910  63.158  1.00 37.56 ? 168 ALA C C   1 
ATOM   7063 O O   . ALA C 1 168 ? 78.027 -11.082 62.808  1.00 40.13 ? 168 ALA C O   1 
ATOM   7064 C CB  . ALA C 1 168 ? 78.624 -9.345  65.546  1.00 24.72 ? 168 ALA C CB  1 
ATOM   7065 N N   . SER C 1 169 ? 77.562 -8.864  62.665  1.00 36.00 ? 169 SER C N   1 
ATOM   7066 C CA  . SER C 1 169 ? 76.510 -9.018  61.670  1.00 37.72 ? 169 SER C CA  1 
ATOM   7067 C C   . SER C 1 169 ? 76.993 -9.664  60.372  1.00 37.90 ? 169 SER C C   1 
ATOM   7068 O O   . SER C 1 169 ? 76.441 -10.674 59.941  1.00 38.62 ? 169 SER C O   1 
ATOM   7069 C CB  . SER C 1 169 ? 75.868 -7.666  61.354  1.00 38.22 ? 169 SER C CB  1 
ATOM   7070 O OG  . SER C 1 169 ? 75.287 -7.091  62.507  1.00 34.72 ? 169 SER C OG  1 
ATOM   7071 N N   . PHE C 1 170 ? 78.032 -9.091  59.772  1.00 38.44 ? 170 PHE C N   1 
ATOM   7072 C CA  . PHE C 1 170 ? 78.581 -9.589  58.515  1.00 37.32 ? 170 PHE C CA  1 
ATOM   7073 C C   . PHE C 1 170 ? 79.606 -10.716 58.640  1.00 41.24 ? 170 PHE C C   1 
ATOM   7074 O O   . PHE C 1 170 ? 80.010 -11.293 57.616  1.00 38.29 ? 170 PHE C O   1 
ATOM   7075 C CB  . PHE C 1 170 ? 79.173 -8.436  57.705  1.00 32.44 ? 170 PHE C CB  1 
ATOM   7076 C CG  . PHE C 1 170 ? 78.147 -7.491  57.177  1.00 35.83 ? 170 PHE C CG  1 
ATOM   7077 C CD1 . PHE C 1 170 ? 77.255 -7.895  56.192  1.00 36.66 ? 170 PHE C CD1 1 
ATOM   7078 C CD2 . PHE C 1 170 ? 78.043 -6.205  57.681  1.00 36.42 ? 170 PHE C CD2 1 
ATOM   7079 C CE1 . PHE C 1 170 ? 76.269 -7.031  55.720  1.00 38.24 ? 170 PHE C CE1 1 
ATOM   7080 C CE2 . PHE C 1 170 ? 77.061 -5.335  57.214  1.00 42.51 ? 170 PHE C CE2 1 
ATOM   7081 C CZ  . PHE C 1 170 ? 76.169 -5.752  56.229  1.00 39.05 ? 170 PHE C CZ  1 
ATOM   7082 N N   . ASN C 1 171 ? 80.024 -11.025 59.875  1.00 42.39 ? 171 ASN C N   1 
ATOM   7083 C CA  . ASN C 1 171 ? 80.997 -12.095 60.117  1.00 43.99 ? 171 ASN C CA  1 
ATOM   7084 C C   . ASN C 1 171 ? 82.191 -11.802 59.214  1.00 43.44 ? 171 ASN C C   1 
ATOM   7085 O O   . ASN C 1 171 ? 82.576 -12.588 58.344  1.00 39.77 ? 171 ASN C O   1 
ATOM   7086 C CB  . ASN C 1 171 ? 80.366 -13.456 59.786  1.00 50.52 ? 171 ASN C CB  1 
ATOM   7087 C CG  . ASN C 1 171 ? 81.299 -14.625 60.047  1.00 52.70 ? 171 ASN C CG  1 
ATOM   7088 O OD1 . ASN C 1 171 ? 81.515 -15.469 59.172  1.00 53.05 ? 171 ASN C OD1 1 
ATOM   7089 N ND2 . ASN C 1 171 ? 81.829 -14.703 61.261  1.00 51.10 ? 171 ASN C ND2 1 
ATOM   7090 N N   . SER C 1 172 ? 82.743 -10.618 59.425  1.00 45.67 ? 172 SER C N   1 
ATOM   7091 C CA  . SER C 1 172 ? 83.865 -10.128 58.657  1.00 46.13 ? 172 SER C CA  1 
ATOM   7092 C C   . SER C 1 172 ? 84.612 -9.118  59.515  1.00 48.15 ? 172 SER C C   1 
ATOM   7093 O O   . SER C 1 172 ? 84.059 -8.573  60.463  1.00 51.78 ? 172 SER C O   1 
ATOM   7094 C CB  . SER C 1 172 ? 83.337 -9.447  57.399  1.00 41.66 ? 172 SER C CB  1 
ATOM   7095 O OG  . SER C 1 172 ? 84.331 -8.640  56.797  1.00 51.29 ? 172 SER C OG  1 
ATOM   7096 N N   . LYS C 1 173 ? 85.884 -8.904  59.215  1.00 51.22 ? 173 LYS C N   1 
ATOM   7097 C CA  . LYS C 1 173 ? 86.662 -7.927  59.956  1.00 50.88 ? 173 LYS C CA  1 
ATOM   7098 C C   . LYS C 1 173 ? 86.292 -6.576  59.367  1.00 47.79 ? 173 LYS C C   1 
ATOM   7099 O O   . LYS C 1 173 ? 86.144 -6.427  58.151  1.00 46.51 ? 173 LYS C O   1 
ATOM   7100 C CB  . LYS C 1 173 ? 88.158 -8.201  59.787  1.00 59.54 ? 173 LYS C CB  1 
ATOM   7101 C CG  . LYS C 1 173 ? 88.605 -9.544  60.374  1.00 69.71 ? 173 LYS C CG  1 
ATOM   7102 C CD  . LYS C 1 173 ? 89.821 -10.124 59.632  1.00 77.71 ? 173 LYS C CD  1 
ATOM   7103 C CE  . LYS C 1 173 ? 89.601 -10.222 58.090  1.00 82.80 ? 173 LYS C CE  1 
ATOM   7104 N NZ  . LYS C 1 173 ? 88.381 -10.987 57.614  1.00 79.82 ? 173 LYS C NZ  1 
ATOM   7105 N N   . PHE C 1 174 ? 86.144 -5.584  60.226  1.00 46.07 ? 174 PHE C N   1 
ATOM   7106 C CA  . PHE C 1 174 ? 85.771 -4.257  59.774  1.00 46.28 ? 174 PHE C CA  1 
ATOM   7107 C C   . PHE C 1 174 ? 86.627 -3.640  58.668  1.00 44.74 ? 174 PHE C C   1 
ATOM   7108 O O   . PHE C 1 174 ? 86.200 -2.695  58.012  1.00 44.53 ? 174 PHE C O   1 
ATOM   7109 C CB  . PHE C 1 174 ? 85.687 -3.288  60.945  1.00 46.23 ? 174 PHE C CB  1 
ATOM   7110 C CG  . PHE C 1 174 ? 85.190 -1.943  60.547  1.00 49.81 ? 174 PHE C CG  1 
ATOM   7111 C CD1 . PHE C 1 174 ? 83.857 -1.763  60.213  1.00 49.21 ? 174 PHE C CD1 1 
ATOM   7112 C CD2 . PHE C 1 174 ? 86.063 -0.875  60.434  1.00 52.63 ? 174 PHE C CD2 1 
ATOM   7113 C CE1 . PHE C 1 174 ? 83.397 -0.549  59.770  1.00 51.77 ? 174 PHE C CE1 1 
ATOM   7114 C CE2 . PHE C 1 174 ? 85.615 0.350   59.990  1.00 56.07 ? 174 PHE C CE2 1 
ATOM   7115 C CZ  . PHE C 1 174 ? 84.273 0.515   59.655  1.00 55.85 ? 174 PHE C CZ  1 
ATOM   7116 N N   . GLU C 1 175 ? 87.836 -4.144  58.470  1.00 46.21 ? 175 GLU C N   1 
ATOM   7117 C CA  . GLU C 1 175 ? 88.699 -3.591  57.431  1.00 48.72 ? 175 GLU C CA  1 
ATOM   7118 C C   . GLU C 1 175 ? 88.201 -3.964  56.024  1.00 45.50 ? 175 GLU C C   1 
ATOM   7119 O O   . GLU C 1 175 ? 88.234 -3.147  55.101  1.00 39.86 ? 175 GLU C O   1 
ATOM   7120 C CB  . GLU C 1 175 ? 90.153 -4.031  57.657  1.00 57.51 ? 175 GLU C CB  1 
ATOM   7121 C CG  . GLU C 1 175 ? 91.081 -3.632  56.512  1.00 74.63 ? 175 GLU C CG  1 
ATOM   7122 C CD  . GLU C 1 175 ? 92.544 -3.530  56.921  1.00 81.23 ? 175 GLU C CD  1 
ATOM   7123 O OE1 . GLU C 1 175 ? 93.188 -4.606  57.083  1.00 85.84 ? 175 GLU C OE1 1 
ATOM   7124 O OE2 . GLU C 1 175 ? 93.040 -2.362  57.058  1.00 80.21 ? 175 GLU C OE2 1 
ATOM   7125 N N   . GLU C 1 176 ? 87.703 -5.196  55.902  1.00 47.57 ? 176 GLU C N   1 
ATOM   7126 C CA  . GLU C 1 176 ? 87.156 -5.760  54.663  1.00 44.91 ? 176 GLU C CA  1 
ATOM   7127 C C   . GLU C 1 176 ? 85.735 -5.207  54.443  1.00 40.73 ? 176 GLU C C   1 
ATOM   7128 O O   . GLU C 1 176 ? 85.318 -4.942  53.311  1.00 34.33 ? 176 GLU C O   1 
ATOM   7129 C CB  . GLU C 1 176 ? 87.135 -7.298  54.781  1.00 48.93 ? 176 GLU C CB  1 
ATOM   7130 C CG  . GLU C 1 176 ? 86.692 -8.050  53.538  1.00 59.59 ? 176 GLU C CG  1 
ATOM   7131 C CD  . GLU C 1 176 ? 87.570 -7.778  52.318  1.00 70.90 ? 176 GLU C CD  1 
ATOM   7132 O OE1 . GLU C 1 176 ? 88.719 -7.293  52.480  1.00 76.18 ? 176 GLU C OE1 1 
ATOM   7133 O OE2 . GLU C 1 176 ? 87.106 -8.062  51.188  1.00 71.64 ? 176 GLU C OE2 1 
ATOM   7134 N N   . ILE C 1 177 ? 85.005 -5.040  55.547  1.00 39.28 ? 177 ILE C N   1 
ATOM   7135 C CA  . ILE C 1 177 ? 83.656 -4.488  55.513  1.00 37.31 ? 177 ILE C CA  1 
ATOM   7136 C C   . ILE C 1 177 ? 83.793 -3.075  54.969  1.00 35.98 ? 177 ILE C C   1 
ATOM   7137 O O   . ILE C 1 177 ? 83.087 -2.698  54.051  1.00 41.19 ? 177 ILE C O   1 
ATOM   7138 C CB  . ILE C 1 177 ? 83.001 -4.453  56.928  1.00 34.99 ? 177 ILE C CB  1 
ATOM   7139 C CG1 . ILE C 1 177 ? 82.794 -5.878  57.456  1.00 31.93 ? 177 ILE C CG1 1 
ATOM   7140 C CG2 . ILE C 1 177 ? 81.667 -3.727  56.881  1.00 34.47 ? 177 ILE C CG2 1 
ATOM   7141 C CD1 . ILE C 1 177 ? 82.203 -5.956  58.861  1.00 25.04 ? 177 ILE C CD1 1 
ATOM   7142 N N   . ASN C 1 178 ? 84.732 -2.306  55.505  1.00 32.62 ? 178 ASN C N   1 
ATOM   7143 C CA  . ASN C 1 178 ? 84.961 -0.948  55.031  1.00 34.54 ? 178 ASN C CA  1 
ATOM   7144 C C   . ASN C 1 178 ? 85.486 -0.935  53.594  1.00 35.81 ? 178 ASN C C   1 
ATOM   7145 O O   . ASN C 1 178 ? 85.155 -0.049  52.810  1.00 33.83 ? 178 ASN C O   1 
ATOM   7146 C CB  . ASN C 1 178 ? 85.957 -0.228  55.928  1.00 34.44 ? 178 ASN C CB  1 
ATOM   7147 C CG  . ASN C 1 178 ? 86.242 1.179   55.455  1.00 37.98 ? 178 ASN C CG  1 
ATOM   7148 O OD1 . ASN C 1 178 ? 85.483 2.107   55.734  1.00 35.33 ? 178 ASN C OD1 1 
ATOM   7149 N ND2 . ASN C 1 178 ? 87.333 1.342   54.720  1.00 43.53 ? 178 ASN C ND2 1 
ATOM   7150 N N   . ARG C 1 179 ? 86.352 -1.891  53.273  1.00 38.07 ? 179 ARG C N   1 
ATOM   7151 C CA  . ARG C 1 179 ? 86.918 -2.003  51.934  1.00 37.72 ? 179 ARG C CA  1 
ATOM   7152 C C   . ARG C 1 179 ? 85.778 -2.136  50.936  1.00 37.35 ? 179 ARG C C   1 
ATOM   7153 O O   . ARG C 1 179 ? 85.351 -1.166  50.314  1.00 35.28 ? 179 ARG C O   1 
ATOM   7154 C CB  . ARG C 1 179 ? 87.813 -3.243  51.844  1.00 35.87 ? 179 ARG C CB  1 
ATOM   7155 C CG  . ARG C 1 179 ? 88.665 -3.302  50.581  1.00 42.00 ? 179 ARG C CG  1 
ATOM   7156 C CD  . ARG C 1 179 ? 89.604 -4.532  50.544  1.00 45.51 ? 179 ARG C CD  1 
ATOM   7157 N NE  . ARG C 1 179 ? 88.913 -5.754  50.133  1.00 49.81 ? 179 ARG C NE  1 
ATOM   7158 C CZ  . ARG C 1 179 ? 88.288 -5.914  48.967  1.00 48.17 ? 179 ARG C CZ  1 
ATOM   7159 N NH1 . ARG C 1 179 ? 88.269 -4.939  48.061  1.00 45.72 ? 179 ARG C NH1 1 
ATOM   7160 N NH2 . ARG C 1 179 ? 87.627 -7.034  48.730  1.00 48.92 ? 179 ARG C NH2 1 
ATOM   7161 N N   . VAL C 1 180 ? 85.198 -3.326  50.932  1.00 39.72 ? 180 VAL C N   1 
ATOM   7162 C CA  . VAL C 1 180 ? 84.106 -3.707  50.048  1.00 42.57 ? 180 VAL C CA  1 
ATOM   7163 C C   . VAL C 1 180 ? 82.872 -2.799  49.935  1.00 39.37 ? 180 VAL C C   1 
ATOM   7164 O O   . VAL C 1 180 ? 82.276 -2.707  48.871  1.00 40.85 ? 180 VAL C O   1 
ATOM   7165 C CB  . VAL C 1 180 ? 83.620 -5.122  50.437  1.00 44.51 ? 180 VAL C CB  1 
ATOM   7166 C CG1 . VAL C 1 180 ? 82.557 -5.612  49.467  1.00 49.62 ? 180 VAL C CG1 1 
ATOM   7167 C CG2 . VAL C 1 180 ? 84.796 -6.080  50.469  1.00 47.43 ? 180 VAL C CG2 1 
ATOM   7168 N N   . LEU C 1 181 ? 82.500 -2.127  51.017  1.00 37.58 ? 181 LEU C N   1 
ATOM   7169 C CA  . LEU C 1 181 ? 81.295 -1.304  51.054  1.00 33.66 ? 181 LEU C CA  1 
ATOM   7170 C C   . LEU C 1 181 ? 81.452 0.208   51.085  1.00 33.23 ? 181 LEU C C   1 
ATOM   7171 O O   . LEU C 1 181 ? 80.978 0.898   50.197  1.00 35.13 ? 181 LEU C O   1 
ATOM   7172 C CB  . LEU C 1 181 ? 80.466 -1.706  52.282  1.00 32.06 ? 181 LEU C CB  1 
ATOM   7173 C CG  . LEU C 1 181 ? 79.185 -2.549  52.304  1.00 35.19 ? 181 LEU C CG  1 
ATOM   7174 C CD1 . LEU C 1 181 ? 79.261 -3.844  51.526  1.00 29.20 ? 181 LEU C CD1 1 
ATOM   7175 C CD2 . LEU C 1 181 ? 78.878 -2.831  53.771  1.00 40.32 ? 181 LEU C CD2 1 
ATOM   7176 N N   . PHE C 1 182 ? 82.122 0.708   52.114  1.00 35.56 ? 182 PHE C N   1 
ATOM   7177 C CA  . PHE C 1 182 ? 82.271 2.141   52.341  1.00 37.78 ? 182 PHE C CA  1 
ATOM   7178 C C   . PHE C 1 182 ? 83.498 2.900   51.847  1.00 42.17 ? 182 PHE C C   1 
ATOM   7179 O O   . PHE C 1 182 ? 83.505 4.126   51.902  1.00 43.62 ? 182 PHE C O   1 
ATOM   7180 C CB  . PHE C 1 182 ? 82.151 2.422   53.845  1.00 39.17 ? 182 PHE C CB  1 
ATOM   7181 C CG  . PHE C 1 182 ? 81.135 1.553   54.571  1.00 42.44 ? 182 PHE C CG  1 
ATOM   7182 C CD1 . PHE C 1 182 ? 79.842 1.389   54.084  1.00 44.31 ? 182 PHE C CD1 1 
ATOM   7183 C CD2 . PHE C 1 182 ? 81.466 0.946   55.778  1.00 40.65 ? 182 PHE C CD2 1 
ATOM   7184 C CE1 . PHE C 1 182 ? 78.904 0.637   54.795  1.00 42.76 ? 182 PHE C CE1 1 
ATOM   7185 C CE2 . PHE C 1 182 ? 80.532 0.196   56.488  1.00 37.81 ? 182 PHE C CE2 1 
ATOM   7186 C CZ  . PHE C 1 182 ? 79.259 0.042   56.001  1.00 37.21 ? 182 PHE C CZ  1 
ATOM   7187 N N   . GLU C 1 183 ? 84.539 2.212   51.395  1.00 46.93 ? 183 GLU C N   1 
ATOM   7188 C CA  . GLU C 1 183 ? 85.764 2.894   50.966  1.00 46.51 ? 183 GLU C CA  1 
ATOM   7189 C C   . GLU C 1 183 ? 85.518 4.078   50.022  1.00 47.53 ? 183 GLU C C   1 
ATOM   7190 O O   . GLU C 1 183 ? 85.112 3.899   48.878  1.00 46.19 ? 183 GLU C O   1 
ATOM   7191 C CB  . GLU C 1 183 ? 86.724 1.880   50.337  1.00 50.50 ? 183 GLU C CB  1 
ATOM   7192 C CG  . GLU C 1 183 ? 88.210 2.189   50.515  1.00 59.08 ? 183 GLU C CG  1 
ATOM   7193 C CD  . GLU C 1 183 ? 88.661 2.104   51.973  1.00 68.33 ? 183 GLU C CD  1 
ATOM   7194 O OE1 . GLU C 1 183 ? 88.443 3.086   52.722  1.00 73.00 ? 183 GLU C OE1 1 
ATOM   7195 O OE2 . GLU C 1 183 ? 89.234 1.062   52.377  1.00 71.87 ? 183 GLU C OE2 1 
ATOM   7196 N N   . GLU C 1 184 ? 85.789 5.295   50.481  1.00 50.63 ? 184 GLU C N   1 
ATOM   7197 C CA  . GLU C 1 184 ? 85.570 6.459   49.623  1.00 53.57 ? 184 GLU C CA  1 
ATOM   7198 C C   . GLU C 1 184 ? 86.462 6.486   48.390  1.00 54.03 ? 184 GLU C C   1 
ATOM   7199 O O   . GLU C 1 184 ? 86.233 7.245   47.443  1.00 52.93 ? 184 GLU C O   1 
ATOM   7200 C CB  . GLU C 1 184 ? 85.664 7.767   50.403  1.00 57.64 ? 184 GLU C CB  1 
ATOM   7201 C CG  . GLU C 1 184 ? 86.958 8.035   51.109  1.00 65.48 ? 184 GLU C CG  1 
ATOM   7202 C CD  . GLU C 1 184 ? 86.959 9.416   51.738  1.00 71.64 ? 184 GLU C CD  1 
ATOM   7203 O OE1 . GLU C 1 184 ? 86.123 9.648   52.642  1.00 74.28 ? 184 GLU C OE1 1 
ATOM   7204 O OE2 . GLU C 1 184 ? 87.773 10.274  51.313  1.00 72.79 ? 184 GLU C OE2 1 
ATOM   7205 N N   . GLU C 1 185 ? 87.444 5.598   48.380  1.00 57.48 ? 185 GLU C N   1 
ATOM   7206 C CA  . GLU C 1 185 ? 88.367 5.467   47.259  1.00 58.64 ? 185 GLU C CA  1 
ATOM   7207 C C   . GLU C 1 185 ? 87.674 4.584   46.214  1.00 53.77 ? 185 GLU C C   1 
ATOM   7208 O O   . GLU C 1 185 ? 88.265 3.628   45.725  1.00 56.80 ? 185 GLU C O   1 
ATOM   7209 C CB  . GLU C 1 185 ? 89.668 4.801   47.750  1.00 61.96 ? 185 GLU C CB  1 
ATOM   7210 C CG  . GLU C 1 185 ? 90.965 5.437   47.253  1.00 70.84 ? 185 GLU C CG  1 
ATOM   7211 C CD  . GLU C 1 185 ? 91.236 5.186   45.772  1.00 75.88 ? 185 GLU C CD  1 
ATOM   7212 O OE1 . GLU C 1 185 ? 91.652 4.060   45.415  1.00 78.21 ? 185 GLU C OE1 1 
ATOM   7213 O OE2 . GLU C 1 185 ? 91.050 6.123   44.966  1.00 77.98 ? 185 GLU C OE2 1 
ATOM   7214 N N   . GLY C 1 186 ? 86.418 4.881   45.898  1.00 48.01 ? 186 GLY C N   1 
ATOM   7215 C CA  . GLY C 1 186 ? 85.705 4.071   44.928  1.00 43.69 ? 186 GLY C CA  1 
ATOM   7216 C C   . GLY C 1 186 ? 84.212 4.340   44.847  1.00 42.14 ? 186 GLY C C   1 
ATOM   7217 O O   . GLY C 1 186 ? 83.489 3.693   44.088  1.00 41.80 ? 186 GLY C O   1 
ATOM   7218 N N   . GLN C 1 187 ? 83.740 5.326   45.594  1.00 38.68 ? 187 GLN C N   1 
ATOM   7219 C CA  . GLN C 1 187 ? 82.316 5.637   45.587  1.00 36.68 ? 187 GLN C CA  1 
ATOM   7220 C C   . GLN C 1 187 ? 81.843 6.644   44.546  1.00 32.84 ? 187 GLN C C   1 
ATOM   7221 O O   . GLN C 1 187 ? 82.633 7.379   43.952  1.00 32.36 ? 187 GLN C O   1 
ATOM   7222 C CB  . GLN C 1 187 ? 81.891 6.108   46.963  1.00 33.09 ? 187 GLN C CB  1 
ATOM   7223 C CG  . GLN C 1 187 ? 82.526 7.386   47.370  1.00 30.23 ? 187 GLN C CG  1 
ATOM   7224 C CD  . GLN C 1 187 ? 82.408 7.573   48.841  1.00 34.30 ? 187 GLN C CD  1 
ATOM   7225 O OE1 . GLN C 1 187 ? 82.052 6.635   49.563  1.00 25.23 ? 187 GLN C OE1 1 
ATOM   7226 N NE2 . GLN C 1 187 ? 82.711 8.779   49.314  1.00 32.13 ? 187 GLN C NE2 1 
ATOM   7227 N N   . GLN C 1 188 ? 80.535 6.681   44.334  1.00 31.19 ? 188 GLN C N   1 
ATOM   7228 C CA  . GLN C 1 188 ? 79.980 7.616   43.373  1.00 30.75 ? 188 GLN C CA  1 
ATOM   7229 C C   . GLN C 1 188 ? 79.841 8.988   44.021  1.00 30.78 ? 188 GLN C C   1 
ATOM   7230 O O   . GLN C 1 188 ? 79.882 9.133   45.252  1.00 29.44 ? 188 GLN C O   1 
ATOM   7231 C CB  . GLN C 1 188 ? 78.617 7.141   42.856  1.00 31.91 ? 188 GLN C CB  1 
ATOM   7232 C CG  . GLN C 1 188 ? 78.595 5.735   42.260  1.00 33.38 ? 188 GLN C CG  1 
ATOM   7233 C CD  . GLN C 1 188 ? 79.500 5.586   41.065  1.00 31.84 ? 188 GLN C CD  1 
ATOM   7234 O OE1 . GLN C 1 188 ? 79.252 6.174   40.012  1.00 39.28 ? 188 GLN C OE1 1 
ATOM   7235 N NE2 . GLN C 1 188 ? 80.565 4.806   41.219  1.00 25.90 ? 188 GLN C NE2 1 
ATOM   7236 N N   . GLU C 1 189 ? 79.627 9.985   43.179  1.00 29.53 ? 189 GLU C N   1 
ATOM   7237 C CA  . GLU C 1 189 ? 79.487 11.361  43.609  1.00 35.37 ? 189 GLU C CA  1 
ATOM   7238 C C   . GLU C 1 189 ? 78.142 11.647  44.283  1.00 36.71 ? 189 GLU C C   1 
ATOM   7239 O O   . GLU C 1 189 ? 78.071 12.469  45.194  1.00 36.64 ? 189 GLU C O   1 
ATOM   7240 C CB  . GLU C 1 189 ? 79.711 12.254  42.391  1.00 40.68 ? 189 GLU C CB  1 
ATOM   7241 C CG  . GLU C 1 189 ? 79.160 13.668  42.446  1.00 53.98 ? 189 GLU C CG  1 
ATOM   7242 C CD  . GLU C 1 189 ? 79.140 14.319  41.054  1.00 61.43 ? 189 GLU C CD  1 
ATOM   7243 O OE1 . GLU C 1 189 ? 80.229 14.492  40.451  1.00 62.91 ? 189 GLU C OE1 1 
ATOM   7244 O OE2 . GLU C 1 189 ? 78.035 14.638  40.555  1.00 60.14 ? 189 GLU C OE2 1 
ATOM   7245 N N   . GLY C 1 190 ? 77.094 10.929  43.874  1.00 38.27 ? 190 GLY C N   1 
ATOM   7246 C CA  . GLY C 1 190 ? 75.765 11.140  44.438  1.00 31.68 ? 190 GLY C CA  1 
ATOM   7247 C C   . GLY C 1 190 ? 74.770 10.007  44.221  1.00 31.63 ? 190 GLY C C   1 
ATOM   7248 O O   . GLY C 1 190 ? 75.108 8.949   43.666  1.00 29.89 ? 190 GLY C O   1 
ATOM   7249 N N   . VAL C 1 191 ? 73.519 10.263  44.610  1.00 30.34 ? 191 VAL C N   1 
ATOM   7250 C CA  . VAL C 1 191 ? 72.442 9.277   44.533  1.00 22.19 ? 191 VAL C CA  1 
ATOM   7251 C C   . VAL C 1 191 ? 71.795 9.135   43.162  1.00 22.35 ? 191 VAL C C   1 
ATOM   7252 O O   . VAL C 1 191 ? 71.074 8.170   42.913  1.00 23.52 ? 191 VAL C O   1 
ATOM   7253 C CB  . VAL C 1 191 ? 71.373 9.523   45.641  1.00 17.16 ? 191 VAL C CB  1 
ATOM   7254 C CG1 . VAL C 1 191 ? 72.044 9.653   46.984  1.00 17.54 ? 191 VAL C CG1 1 
ATOM   7255 C CG2 . VAL C 1 191 ? 70.573 10.767  45.376  1.00 10.91 ? 191 VAL C CG2 1 
ATOM   7256 N N   . ILE C 1 192 ? 71.973 10.133  42.305  1.00 24.13 ? 192 ILE C N   1 
ATOM   7257 C CA  . ILE C 1 192 ? 71.447 10.065  40.943  1.00 19.42 ? 192 ILE C CA  1 
ATOM   7258 C C   . ILE C 1 192 ? 72.744 9.848   40.200  1.00 22.57 ? 192 ILE C C   1 
ATOM   7259 O O   . ILE C 1 192 ? 73.658 10.678  40.245  1.00 22.90 ? 192 ILE C O   1 
ATOM   7260 C CB  . ILE C 1 192 ? 70.746 11.363  40.478  1.00 17.66 ? 192 ILE C CB  1 
ATOM   7261 C CG1 . ILE C 1 192 ? 69.566 11.684  41.400  1.00 14.68 ? 192 ILE C CG1 1 
ATOM   7262 C CG2 . ILE C 1 192 ? 70.236 11.190  39.054  1.00 18.19 ? 192 ILE C CG2 1 
ATOM   7263 C CD1 . ILE C 1 192 ? 68.631 12.753  40.870  1.00 19.81 ? 192 ILE C CD1 1 
ATOM   7264 N N   . VAL C 1 193 ? 72.822 8.719   39.518  1.00 24.09 ? 193 VAL C N   1 
ATOM   7265 C CA  . VAL C 1 193 ? 74.045 8.317   38.841  1.00 27.29 ? 193 VAL C CA  1 
ATOM   7266 C C   . VAL C 1 193 ? 73.813 7.990   37.366  1.00 30.85 ? 193 VAL C C   1 
ATOM   7267 O O   . VAL C 1 193 ? 72.686 7.753   36.938  1.00 33.98 ? 193 VAL C O   1 
ATOM   7268 C CB  . VAL C 1 193 ? 74.601 7.143   39.646  1.00 23.07 ? 193 VAL C CB  1 
ATOM   7269 C CG1 . VAL C 1 193 ? 74.528 5.858   38.893  1.00 21.28 ? 193 VAL C CG1 1 
ATOM   7270 C CG2 . VAL C 1 193 ? 75.950 7.463   40.190  1.00 28.46 ? 193 VAL C CG2 1 
ATOM   7271 N N   . ASN C 1 194 ? 74.878 8.003   36.587  1.00 34.07 ? 194 ASN C N   1 
ATOM   7272 C CA  . ASN C 1 194 ? 74.777 7.738   35.156  1.00 38.20 ? 194 ASN C CA  1 
ATOM   7273 C C   . ASN C 1 194 ? 74.989 6.275   34.786  1.00 35.25 ? 194 ASN C C   1 
ATOM   7274 O O   . ASN C 1 194 ? 75.908 5.652   35.282  1.00 41.29 ? 194 ASN C O   1 
ATOM   7275 C CB  . ASN C 1 194 ? 75.813 8.581   34.437  1.00 43.72 ? 194 ASN C CB  1 
ATOM   7276 C CG  . ASN C 1 194 ? 75.936 8.220   32.994  1.00 55.52 ? 194 ASN C CG  1 
ATOM   7277 O OD1 . ASN C 1 194 ? 75.357 8.876   32.131  1.00 68.05 ? 194 ASN C OD1 1 
ATOM   7278 N ND2 . ASN C 1 194 ? 76.676 7.152   32.712  1.00 59.94 ? 194 ASN C ND2 1 
ATOM   7279 N N   . ILE C 1 195 ? 74.182 5.728   33.892  1.00 30.97 ? 195 ILE C N   1 
ATOM   7280 C CA  . ILE C 1 195 ? 74.380 4.331   33.502  1.00 34.12 ? 195 ILE C CA  1 
ATOM   7281 C C   . ILE C 1 195 ? 74.563 4.080   31.991  1.00 38.27 ? 195 ILE C C   1 
ATOM   7282 O O   . ILE C 1 195 ? 74.517 5.000   31.165  1.00 36.61 ? 195 ILE C O   1 
ATOM   7283 C CB  . ILE C 1 195 ? 73.291 3.375   34.080  1.00 29.12 ? 195 ILE C CB  1 
ATOM   7284 C CG1 . ILE C 1 195 ? 71.881 3.877   33.763  1.00 28.53 ? 195 ILE C CG1 1 
ATOM   7285 C CG2 . ILE C 1 195 ? 73.491 3.188   35.563  1.00 27.94 ? 195 ILE C CG2 1 
ATOM   7286 C CD1 . ILE C 1 195 ? 71.074 2.913   32.915  1.00 23.00 ? 195 ILE C CD1 1 
ATOM   7287 N N   . ASP C 1 196 ? 74.772 2.819   31.644  1.00 39.67 ? 196 ASP C N   1 
ATOM   7288 C CA  . ASP C 1 196 ? 74.991 2.423   30.272  1.00 41.97 ? 196 ASP C CA  1 
ATOM   7289 C C   . ASP C 1 196 ? 73.777 1.724   29.713  1.00 42.73 ? 196 ASP C C   1 
ATOM   7290 O O   . ASP C 1 196 ? 73.209 0.852   30.359  1.00 44.39 ? 196 ASP C O   1 
ATOM   7291 C CB  . ASP C 1 196 ? 76.147 1.444   30.229  1.00 46.85 ? 196 ASP C CB  1 
ATOM   7292 C CG  . ASP C 1 196 ? 76.896 1.483   28.932  1.00 51.64 ? 196 ASP C CG  1 
ATOM   7293 O OD1 . ASP C 1 196 ? 76.286 1.268   27.854  1.00 55.47 ? 196 ASP C OD1 1 
ATOM   7294 O OD2 . ASP C 1 196 ? 78.121 1.717   29.008  1.00 57.39 ? 196 ASP C OD2 1 
ATOM   7295 N N   . SER C 1 197 ? 73.440 2.055   28.473  1.00 45.19 ? 197 SER C N   1 
ATOM   7296 C CA  . SER C 1 197 ? 72.311 1.445   27.764  1.00 50.08 ? 197 SER C CA  1 
ATOM   7297 C C   . SER C 1 197 ? 72.453 -0.087  27.738  1.00 48.06 ? 197 SER C C   1 
ATOM   7298 O O   . SER C 1 197 ? 71.479 -0.827  27.841  1.00 48.03 ? 197 SER C O   1 
ATOM   7299 C CB  . SER C 1 197 ? 72.250 1.995   26.322  1.00 53.84 ? 197 SER C CB  1 
ATOM   7300 O OG  . SER C 1 197 ? 73.547 2.346   25.827  1.00 54.53 ? 197 SER C OG  1 
ATOM   7301 N N   . GLU C 1 198 ? 73.692 -0.538  27.605  1.00 49.67 ? 198 GLU C N   1 
ATOM   7302 C CA  . GLU C 1 198 ? 74.004 -1.948  27.556  1.00 47.39 ? 198 GLU C CA  1 
ATOM   7303 C C   . GLU C 1 198 ? 73.749 -2.624  28.886  1.00 43.56 ? 198 GLU C C   1 
ATOM   7304 O O   . GLU C 1 198 ? 73.228 -3.726  28.914  1.00 43.86 ? 198 GLU C O   1 
ATOM   7305 C CB  . GLU C 1 198 ? 75.453 -2.149  27.107  1.00 55.49 ? 198 GLU C CB  1 
ATOM   7306 C CG  . GLU C 1 198 ? 75.718 -1.687  25.668  1.00 63.43 ? 198 GLU C CG  1 
ATOM   7307 C CD  . GLU C 1 198 ? 77.029 -2.218  25.098  1.00 69.74 ? 198 GLU C CD  1 
ATOM   7308 O OE1 . GLU C 1 198 ? 77.178 -3.459  24.963  1.00 70.52 ? 198 GLU C OE1 1 
ATOM   7309 O OE2 . GLU C 1 198 ? 77.905 -1.387  24.771  1.00 70.07 ? 198 GLU C OE2 1 
ATOM   7310 N N   . GLN C 1 199 ? 74.097 -1.965  29.988  1.00 41.46 ? 199 GLN C N   1 
ATOM   7311 C CA  . GLN C 1 199 ? 73.873 -2.549  31.312  1.00 43.36 ? 199 GLN C CA  1 
ATOM   7312 C C   . GLN C 1 199 ? 72.406 -2.986  31.485  1.00 42.81 ? 199 GLN C C   1 
ATOM   7313 O O   . GLN C 1 199 ? 72.120 -4.156  31.724  1.00 43.04 ? 199 GLN C O   1 
ATOM   7314 C CB  . GLN C 1 199 ? 74.249 -1.555  32.432  1.00 49.58 ? 199 GLN C CB  1 
ATOM   7315 C CG  . GLN C 1 199 ? 75.749 -1.216  32.562  1.00 55.98 ? 199 GLN C CG  1 
ATOM   7316 C CD  . GLN C 1 199 ? 76.074 -0.241  33.712  1.00 55.43 ? 199 GLN C CD  1 
ATOM   7317 O OE1 . GLN C 1 199 ? 75.894 0.975   33.592  1.00 49.15 ? 199 GLN C OE1 1 
ATOM   7318 N NE2 . GLN C 1 199 ? 76.584 -0.778  34.814  1.00 56.60 ? 199 GLN C NE2 1 
ATOM   7319 N N   . ILE C 1 200 ? 71.473 -2.061  31.289  1.00 42.32 ? 200 ILE C N   1 
ATOM   7320 C CA  . ILE C 1 200 ? 70.061 -2.369  31.465  1.00 43.11 ? 200 ILE C CA  1 
ATOM   7321 C C   . ILE C 1 200 ? 69.374 -3.175  30.361  1.00 47.96 ? 200 ILE C C   1 
ATOM   7322 O O   . ILE C 1 200 ? 68.138 -3.186  30.284  1.00 52.34 ? 200 ILE C O   1 
ATOM   7323 C CB  . ILE C 1 200 ? 69.251 -1.100  31.732  1.00 38.79 ? 200 ILE C CB  1 
ATOM   7324 C CG1 . ILE C 1 200 ? 69.406 -0.115  30.585  1.00 38.36 ? 200 ILE C CG1 1 
ATOM   7325 C CG2 . ILE C 1 200 ? 69.721 -0.454  33.001  1.00 41.54 ? 200 ILE C CG2 1 
ATOM   7326 C CD1 . ILE C 1 200 ? 68.366 0.964   30.603  1.00 36.24 ? 200 ILE C CD1 1 
ATOM   7327 N N   . LYS C 1 201 ? 70.149 -3.922  29.579  1.00 49.35 ? 201 LYS C N   1 
ATOM   7328 C CA  . LYS C 1 201 ? 69.619 -4.723  28.465  1.00 50.40 ? 201 LYS C CA  1 
ATOM   7329 C C   . LYS C 1 201 ? 68.542 -5.761  28.854  1.00 47.82 ? 201 LYS C C   1 
ATOM   7330 O O   . LYS C 1 201 ? 67.460 -5.793  28.257  1.00 41.25 ? 201 LYS C O   1 
ATOM   7331 C CB  . LYS C 1 201 ? 70.781 -5.428  27.746  1.00 57.60 ? 201 LYS C CB  1 
ATOM   7332 C CG  . LYS C 1 201 ? 70.552 -5.744  26.269  1.00 64.27 ? 201 LYS C CG  1 
ATOM   7333 C CD  . LYS C 1 201 ? 70.676 -4.499  25.397  1.00 67.62 ? 201 LYS C CD  1 
ATOM   7334 C CE  . LYS C 1 201 ? 70.328 -4.808  23.948  1.00 73.01 ? 201 LYS C CE  1 
ATOM   7335 N NZ  . LYS C 1 201 ? 68.902 -5.231  23.774  1.00 75.67 ? 201 LYS C NZ  1 
ATOM   7336 N N   . GLU C 1 202 ? 68.845 -6.594  29.859  1.00 48.18 ? 202 GLU C N   1 
ATOM   7337 C CA  . GLU C 1 202 ? 67.923 -7.639  30.326  1.00 44.36 ? 202 GLU C CA  1 
ATOM   7338 C C   . GLU C 1 202 ? 66.668 -7.043  30.952  1.00 41.71 ? 202 GLU C C   1 
ATOM   7339 O O   . GLU C 1 202 ? 65.549 -7.391  30.580  1.00 37.57 ? 202 GLU C O   1 
ATOM   7340 C CB  . GLU C 1 202 ? 68.620 -8.556  31.346  1.00 46.19 ? 202 GLU C CB  1 
ATOM   7341 C CG  . GLU C 1 202 ? 69.643 -9.534  30.751  1.00 53.51 ? 202 GLU C CG  1 
ATOM   7342 C CD  . GLU C 1 202 ? 69.022 -10.571 29.802  1.00 58.11 ? 202 GLU C CD  1 
ATOM   7343 O OE1 . GLU C 1 202 ? 67.962 -11.131 30.142  1.00 62.82 ? 202 GLU C OE1 1 
ATOM   7344 O OE2 . GLU C 1 202 ? 69.589 -10.834 28.714  1.00 60.78 ? 202 GLU C OE2 1 
ATOM   7345 N N   . LEU C 1 203 ? 66.897 -6.120  31.883  1.00 39.40 ? 203 LEU C N   1 
ATOM   7346 C CA  . LEU C 1 203 ? 65.876 -5.404  32.647  1.00 39.13 ? 203 LEU C CA  1 
ATOM   7347 C C   . LEU C 1 203 ? 64.748 -4.816  31.780  1.00 40.90 ? 203 LEU C C   1 
ATOM   7348 O O   . LEU C 1 203 ? 63.593 -5.244  31.856  1.00 39.94 ? 203 LEU C O   1 
ATOM   7349 C CB  . LEU C 1 203 ? 66.565 -4.259  33.403  1.00 36.32 ? 203 LEU C CB  1 
ATOM   7350 C CG  . LEU C 1 203 ? 66.143 -3.691  34.762  1.00 31.87 ? 203 LEU C CG  1 
ATOM   7351 C CD1 . LEU C 1 203 ? 66.386 -2.185  34.731  1.00 26.98 ? 203 LEU C CD1 1 
ATOM   7352 C CD2 . LEU C 1 203 ? 64.698 -4.001  35.097  1.00 27.06 ? 203 LEU C CD2 1 
ATOM   7353 N N   . SER C 1 204 ? 65.088 -3.803  30.994  1.00 38.73 ? 204 SER C N   1 
ATOM   7354 C CA  . SER C 1 204 ? 64.138 -3.128  30.133  1.00 40.88 ? 204 SER C CA  1 
ATOM   7355 C C   . SER C 1 204 ? 63.202 -4.093  29.423  1.00 43.40 ? 204 SER C C   1 
ATOM   7356 O O   . SER C 1 204 ? 61.994 -3.861  29.355  1.00 48.13 ? 204 SER C O   1 
ATOM   7357 C CB  . SER C 1 204 ? 64.899 -2.338  29.097  1.00 39.50 ? 204 SER C CB  1 
ATOM   7358 O OG  . SER C 1 204 ? 65.837 -3.196  28.481  1.00 48.77 ? 204 SER C OG  1 
ATOM   7359 N N   . LYS C 1 205 ? 63.760 -5.172  28.893  1.00 41.75 ? 205 LYS C N   1 
ATOM   7360 C CA  . LYS C 1 205 ? 62.968 -6.158  28.183  1.00 41.32 ? 205 LYS C CA  1 
ATOM   7361 C C   . LYS C 1 205 ? 61.860 -6.706  29.051  1.00 39.89 ? 205 LYS C C   1 
ATOM   7362 O O   . LYS C 1 205 ? 60.692 -6.601  28.699  1.00 39.60 ? 205 LYS C O   1 
ATOM   7363 C CB  . LYS C 1 205 ? 63.850 -7.302  27.697  1.00 47.94 ? 205 LYS C CB  1 
ATOM   7364 C CG  . LYS C 1 205 ? 64.910 -6.891  26.696  1.00 57.37 ? 205 LYS C CG  1 
ATOM   7365 C CD  . LYS C 1 205 ? 65.867 -8.038  26.423  1.00 66.58 ? 205 LYS C CD  1 
ATOM   7366 C CE  . LYS C 1 205 ? 65.127 -9.287  25.972  1.00 64.79 ? 205 LYS C CE  1 
ATOM   7367 N NZ  . LYS C 1 205 ? 66.079 -10.416 25.906  1.00 69.69 ? 205 LYS C NZ  1 
ATOM   7368 N N   . HIS C 1 206 ? 62.217 -7.257  30.205  1.00 38.37 ? 206 HIS C N   1 
ATOM   7369 C CA  . HIS C 1 206 ? 61.217 -7.827  31.101  1.00 39.04 ? 206 HIS C CA  1 
ATOM   7370 C C   . HIS C 1 206 ? 60.257 -6.786  31.637  1.00 38.02 ? 206 HIS C C   1 
ATOM   7371 O O   . HIS C 1 206 ? 59.092 -7.085  31.931  1.00 36.37 ? 206 HIS C O   1 
ATOM   7372 C CB  . HIS C 1 206 ? 61.855 -8.547  32.272  1.00 39.60 ? 206 HIS C CB  1 
ATOM   7373 C CG  . HIS C 1 206 ? 60.851 -9.155  33.197  1.00 46.19 ? 206 HIS C CG  1 
ATOM   7374 N ND1 . HIS C 1 206 ? 60.515 -8.590  34.409  1.00 50.74 ? 206 HIS C ND1 1 
ATOM   7375 C CD2 . HIS C 1 206 ? 60.054 -10.242 33.053  1.00 44.63 ? 206 HIS C CD2 1 
ATOM   7376 C CE1 . HIS C 1 206 ? 59.552 -9.300  34.969  1.00 51.51 ? 206 HIS C CE1 1 
ATOM   7377 N NE2 . HIS C 1 206 ? 59.256 -10.307 34.166  1.00 50.89 ? 206 HIS C NE2 1 
ATOM   7378 N N   . ALA C 1 207 ? 60.774 -5.585  31.840  1.00 38.52 ? 207 ALA C N   1 
ATOM   7379 C CA  . ALA C 1 207 ? 59.958 -4.491  32.311  1.00 39.66 ? 207 ALA C CA  1 
ATOM   7380 C C   . ALA C 1 207 ? 58.838 -4.338  31.266  1.00 44.12 ? 207 ALA C C   1 
ATOM   7381 O O   . ALA C 1 207 ? 57.670 -4.624  31.548  1.00 47.33 ? 207 ALA C O   1 
ATOM   7382 C CB  . ALA C 1 207 ? 60.800 -3.220  32.422  1.00 30.57 ? 207 ALA C CB  1 
ATOM   7383 N N   . LYS C 1 208 ? 59.210 -4.019  30.032  1.00 46.39 ? 208 LYS C N   1 
ATOM   7384 C CA  . LYS C 1 208 ? 58.235 -3.858  28.966  1.00 47.81 ? 208 LYS C CA  1 
ATOM   7385 C C   . LYS C 1 208 ? 57.351 -5.075  28.702  1.00 49.62 ? 208 LYS C C   1 
ATOM   7386 O O   . LYS C 1 208 ? 56.319 -4.948  28.061  1.00 54.93 ? 208 LYS C O   1 
ATOM   7387 C CB  . LYS C 1 208 ? 58.908 -3.405  27.674  1.00 50.03 ? 208 LYS C CB  1 
ATOM   7388 C CG  . LYS C 1 208 ? 58.919 -1.887  27.489  1.00 54.64 ? 208 LYS C CG  1 
ATOM   7389 C CD  . LYS C 1 208 ? 60.261 -1.246  27.834  1.00 59.31 ? 208 LYS C CD  1 
ATOM   7390 C CE  . LYS C 1 208 ? 61.322 -1.525  26.767  1.00 60.57 ? 208 LYS C CE  1 
ATOM   7391 N NZ  . LYS C 1 208 ? 62.566 -0.734  27.001  1.00 62.27 ? 208 LYS C NZ  1 
ATOM   7392 N N   . SER C 1 209 ? 57.755 -6.254  29.160  1.00 51.27 ? 209 SER C N   1 
ATOM   7393 C CA  . SER C 1 209 ? 56.935 -7.449  28.965  1.00 50.38 ? 209 SER C CA  1 
ATOM   7394 C C   . SER C 1 209 ? 55.946 -7.634  30.097  1.00 54.48 ? 209 SER C C   1 
ATOM   7395 O O   . SER C 1 209 ? 55.064 -8.482  30.012  1.00 58.00 ? 209 SER C O   1 
ATOM   7396 C CB  . SER C 1 209 ? 57.782 -8.710  28.822  1.00 45.46 ? 209 SER C CB  1 
ATOM   7397 O OG  . SER C 1 209 ? 58.239 -8.831  27.497  1.00 39.61 ? 209 SER C OG  1 
ATOM   7398 N N   . SER C 1 210 ? 56.131 -6.892  31.182  1.00 57.02 ? 210 SER C N   1 
ATOM   7399 C CA  . SER C 1 210 ? 55.217 -6.976  32.310  1.00 60.72 ? 210 SER C CA  1 
ATOM   7400 C C   . SER C 1 210 ? 54.288 -5.770  32.279  1.00 63.65 ? 210 SER C C   1 
ATOM   7401 O O   . SER C 1 210 ? 53.076 -5.931  32.250  1.00 67.31 ? 210 SER C O   1 
ATOM   7402 C CB  . SER C 1 210 ? 55.985 -7.040  33.624  1.00 60.49 ? 210 SER C CB  1 
ATOM   7403 O OG  . SER C 1 210 ? 56.903 -8.119  33.596  1.00 61.74 ? 210 SER C OG  1 
ATOM   7404 N N   . ASN C 1 220 ? 37.531 6.874   30.709  1.00 71.86 ? 220 ASN C N   1 
ATOM   7405 C CA  . ASN C 1 220 ? 37.560 7.760   31.875  1.00 71.58 ? 220 ASN C CA  1 
ATOM   7406 C C   . ASN C 1 220 ? 37.696 9.220   31.437  1.00 67.46 ? 220 ASN C C   1 
ATOM   7407 O O   . ASN C 1 220 ? 37.617 10.137  32.270  1.00 65.36 ? 220 ASN C O   1 
ATOM   7408 C CB  . ASN C 1 220 ? 38.740 7.408   32.797  1.00 78.02 ? 220 ASN C CB  1 
ATOM   7409 C CG  . ASN C 1 220 ? 38.740 5.947   33.238  1.00 82.16 ? 220 ASN C CG  1 
ATOM   7410 O OD1 . ASN C 1 220 ? 39.722 5.229   33.041  1.00 85.94 ? 220 ASN C OD1 1 
ATOM   7411 N ND2 . ASN C 1 220 ? 37.648 5.507   33.846  1.00 83.83 ? 220 ASN C ND2 1 
ATOM   7412 N N   . THR C 1 221 ? 37.893 9.420   30.132  1.00 60.67 ? 221 THR C N   1 
ATOM   7413 C CA  . THR C 1 221 ? 38.070 10.750  29.555  1.00 56.50 ? 221 THR C CA  1 
ATOM   7414 C C   . THR C 1 221 ? 36.789 11.486  29.202  1.00 53.96 ? 221 THR C C   1 
ATOM   7415 O O   . THR C 1 221 ? 35.817 10.886  28.765  1.00 57.58 ? 221 THR C O   1 
ATOM   7416 C CB  . THR C 1 221 ? 38.981 10.691  28.311  1.00 53.47 ? 221 THR C CB  1 
ATOM   7417 O OG1 . THR C 1 221 ? 40.316 10.389  28.729  1.00 53.36 ? 221 THR C OG1 1 
ATOM   7418 C CG2 . THR C 1 221 ? 38.983 12.012  27.554  1.00 50.20 ? 221 THR C CG2 1 
ATOM   7419 N N   . ILE C 1 222 ? 36.789 12.789  29.433  1.00 48.46 ? 222 ILE C N   1 
ATOM   7420 C CA  . ILE C 1 222 ? 35.655 13.617  29.108  1.00 47.92 ? 222 ILE C CA  1 
ATOM   7421 C C   . ILE C 1 222 ? 36.309 14.891  28.641  1.00 48.87 ? 222 ILE C C   1 
ATOM   7422 O O   . ILE C 1 222 ? 37.115 15.489  29.356  1.00 46.18 ? 222 ILE C O   1 
ATOM   7423 C CB  . ILE C 1 222 ? 34.701 13.843  30.321  1.00 49.59 ? 222 ILE C CB  1 
ATOM   7424 C CG1 . ILE C 1 222 ? 33.394 14.464  29.843  1.00 56.85 ? 222 ILE C CG1 1 
ATOM   7425 C CG2 . ILE C 1 222 ? 35.295 14.769  31.346  1.00 51.17 ? 222 ILE C CG2 1 
ATOM   7426 C CD1 . ILE C 1 222 ? 32.275 14.414  30.874  1.00 62.77 ? 222 ILE C CD1 1 
ATOM   7427 N N   . GLY C 1 223 ? 36.079 15.216  27.375  1.00 51.34 ? 223 GLY C N   1 
ATOM   7428 C CA  . GLY C 1 223 ? 36.674 16.411  26.806  1.00 49.08 ? 223 GLY C CA  1 
ATOM   7429 C C   . GLY C 1 223 ? 36.221 16.716  25.395  1.00 44.87 ? 223 GLY C C   1 
ATOM   7430 O O   . GLY C 1 223 ? 35.475 15.957  24.779  1.00 47.50 ? 223 GLY C O   1 
ATOM   7431 N N   . ASN C 1 224 ? 36.736 17.806  24.857  1.00 40.30 ? 224 ASN C N   1 
ATOM   7432 C CA  . ASN C 1 224 ? 36.358 18.244  23.539  1.00 37.94 ? 224 ASN C CA  1 
ATOM   7433 C C   . ASN C 1 224 ? 37.554 18.921  22.887  1.00 40.76 ? 224 ASN C C   1 
ATOM   7434 O O   . ASN C 1 224 ? 38.701 18.611  23.217  1.00 43.20 ? 224 ASN C O   1 
ATOM   7435 C CB  . ASN C 1 224 ? 35.172 19.208  23.655  1.00 35.48 ? 224 ASN C CB  1 
ATOM   7436 C CG  . ASN C 1 224 ? 35.383 20.291  24.720  1.00 36.40 ? 224 ASN C CG  1 
ATOM   7437 O OD1 . ASN C 1 224 ? 36.499 20.777  24.924  1.00 39.93 ? 224 ASN C OD1 1 
ATOM   7438 N ND2 . ASN C 1 224 ? 34.306 20.682  25.383  1.00 35.07 ? 224 ASN C ND2 1 
ATOM   7439 N N   . GLU C 1 225 ? 37.291 19.828  21.948  1.00 40.54 ? 225 GLU C N   1 
ATOM   7440 C CA  . GLU C 1 225 ? 38.361 20.541  21.251  1.00 40.53 ? 225 GLU C CA  1 
ATOM   7441 C C   . GLU C 1 225 ? 39.112 21.541  22.145  1.00 37.46 ? 225 GLU C C   1 
ATOM   7442 O O   . GLU C 1 225 ? 40.233 21.945  21.830  1.00 37.72 ? 225 GLU C O   1 
ATOM   7443 C CB  . GLU C 1 225 ? 37.805 21.249  20.006  1.00 42.86 ? 225 GLU C CB  1 
ATOM   7444 C CG  . GLU C 1 225 ? 36.438 21.912  20.218  1.00 56.46 ? 225 GLU C CG  1 
ATOM   7445 C CD  . GLU C 1 225 ? 36.249 23.210  19.427  1.00 59.93 ? 225 GLU C CD  1 
ATOM   7446 O OE1 . GLU C 1 225 ? 37.247 23.777  18.917  1.00 61.64 ? 225 GLU C OE1 1 
ATOM   7447 O OE2 . GLU C 1 225 ? 35.089 23.678  19.345  1.00 63.22 ? 225 GLU C OE2 1 
ATOM   7448 N N   . PHE C 1 226 ? 38.509 21.916  23.271  1.00 34.34 ? 226 PHE C N   1 
ATOM   7449 C CA  . PHE C 1 226 ? 39.130 22.870  24.176  1.00 27.66 ? 226 PHE C CA  1 
ATOM   7450 C C   . PHE C 1 226 ? 39.926 22.273  25.301  1.00 23.87 ? 226 PHE C C   1 
ATOM   7451 O O   . PHE C 1 226 ? 40.872 22.883  25.786  1.00 24.48 ? 226 PHE C O   1 
ATOM   7452 C CB  . PHE C 1 226 ? 38.082 23.790  24.735  1.00 29.55 ? 226 PHE C CB  1 
ATOM   7453 C CG  . PHE C 1 226 ? 37.425 24.604  23.691  1.00 28.53 ? 226 PHE C CG  1 
ATOM   7454 C CD1 . PHE C 1 226 ? 38.128 25.598  23.042  1.00 25.64 ? 226 PHE C CD1 1 
ATOM   7455 C CD2 . PHE C 1 226 ? 36.121 24.349  23.318  1.00 26.41 ? 226 PHE C CD2 1 
ATOM   7456 C CE1 . PHE C 1 226 ? 37.541 26.318  22.039  1.00 28.40 ? 226 PHE C CE1 1 
ATOM   7457 C CE2 . PHE C 1 226 ? 35.531 25.065  22.316  1.00 29.62 ? 226 PHE C CE2 1 
ATOM   7458 C CZ  . PHE C 1 226 ? 36.239 26.054  21.671  1.00 29.54 ? 226 PHE C CZ  1 
ATOM   7459 N N   . GLY C 1 227 ? 39.540 21.085  25.728  1.00 21.89 ? 227 GLY C N   1 
ATOM   7460 C CA  . GLY C 1 227 ? 40.263 20.448  26.803  1.00 21.34 ? 227 GLY C CA  1 
ATOM   7461 C C   . GLY C 1 227 ? 39.842 19.019  27.018  1.00 20.51 ? 227 GLY C C   1 
ATOM   7462 O O   . GLY C 1 227 ? 38.787 18.586  26.555  1.00 19.63 ? 227 GLY C O   1 
ATOM   7463 N N   . ASN C 1 228 ? 40.666 18.292  27.753  1.00 23.52 ? 228 ASN C N   1 
ATOM   7464 C CA  . ASN C 1 228 ? 40.385 16.895  28.057  1.00 25.95 ? 228 ASN C CA  1 
ATOM   7465 C C   . ASN C 1 228 ? 40.658 16.567  29.521  1.00 21.45 ? 228 ASN C C   1 
ATOM   7466 O O   . ASN C 1 228 ? 41.719 16.889  30.032  1.00 16.64 ? 228 ASN C O   1 
ATOM   7467 C CB  . ASN C 1 228 ? 41.253 15.982  27.188  1.00 29.93 ? 228 ASN C CB  1 
ATOM   7468 C CG  . ASN C 1 228 ? 40.631 15.681  25.843  1.00 34.65 ? 228 ASN C CG  1 
ATOM   7469 O OD1 . ASN C 1 228 ? 39.455 15.361  25.737  1.00 38.48 ? 228 ASN C OD1 1 
ATOM   7470 N ND2 . ASN C 1 228 ? 41.462 15.714  24.817  1.00 46.78 ? 228 ASN C ND2 1 
ATOM   7471 N N   . LEU C 1 229 ? 39.710 15.914  30.180  1.00 22.67 ? 229 LEU C N   1 
ATOM   7472 C CA  . LEU C 1 229 ? 39.887 15.512  31.567  1.00 26.25 ? 229 LEU C CA  1 
ATOM   7473 C C   . LEU C 1 229 ? 39.979 13.988  31.585  1.00 27.69 ? 229 LEU C C   1 
ATOM   7474 O O   . LEU C 1 229 ? 39.273 13.316  30.827  1.00 24.88 ? 229 LEU C O   1 
ATOM   7475 C CB  . LEU C 1 229 ? 38.679 15.919  32.411  1.00 29.31 ? 229 LEU C CB  1 
ATOM   7476 C CG  . LEU C 1 229 ? 38.867 16.711  33.714  1.00 32.56 ? 229 LEU C CG  1 
ATOM   7477 C CD1 . LEU C 1 229 ? 37.556 16.782  34.464  1.00 30.36 ? 229 LEU C CD1 1 
ATOM   7478 C CD2 . LEU C 1 229 ? 39.942 16.129  34.587  1.00 27.12 ? 229 LEU C CD2 1 
ATOM   7479 N N   . THR C 1 230 ? 40.884 13.448  32.396  1.00 28.27 ? 230 THR C N   1 
ATOM   7480 C CA  . THR C 1 230 ? 41.027 12.003  32.534  1.00 29.99 ? 230 THR C CA  1 
ATOM   7481 C C   . THR C 1 230 ? 41.314 11.707  34.003  1.00 29.19 ? 230 THR C C   1 
ATOM   7482 O O   . THR C 1 230 ? 42.364 12.105  34.536  1.00 27.26 ? 230 THR C O   1 
ATOM   7483 C CB  . THR C 1 230 ? 42.168 11.437  31.672  1.00 32.97 ? 230 THR C CB  1 
ATOM   7484 O OG1 . THR C 1 230 ? 42.052 11.934  30.326  1.00 36.80 ? 230 THR C OG1 1 
ATOM   7485 C CG2 . THR C 1 230 ? 42.105 9.898   31.664  1.00 28.54 ? 230 THR C CG2 1 
ATOM   7486 N N   . GLU C 1 231 ? 40.352 11.058  34.656  1.00 27.14 ? 231 GLU C N   1 
ATOM   7487 C CA  . GLU C 1 231 ? 40.469 10.703  36.072  1.00 33.30 ? 231 GLU C CA  1 
ATOM   7488 C C   . GLU C 1 231 ? 40.423 9.197   36.321  1.00 33.75 ? 231 GLU C C   1 
ATOM   7489 O O   . GLU C 1 231 ? 39.896 8.427   35.518  1.00 34.28 ? 231 GLU C O   1 
ATOM   7490 C CB  . GLU C 1 231 ? 39.372 11.378  36.910  1.00 33.82 ? 231 GLU C CB  1 
ATOM   7491 C CG  . GLU C 1 231 ? 39.209 12.849  36.629  1.00 36.12 ? 231 GLU C CG  1 
ATOM   7492 C CD  . GLU C 1 231 ? 38.485 13.599  37.712  1.00 30.97 ? 231 GLU C CD  1 
ATOM   7493 O OE1 . GLU C 1 231 ? 37.549 13.059  38.320  1.00 34.76 ? 231 GLU C OE1 1 
ATOM   7494 O OE2 . GLU C 1 231 ? 38.859 14.754  37.943  1.00 34.01 ? 231 GLU C OE2 1 
ATOM   7495 N N   . ARG C 1 232 ? 40.967 8.792   37.458  1.00 34.49 ? 232 ARG C N   1 
ATOM   7496 C CA  . ARG C 1 232 ? 41.012 7.401   37.850  1.00 34.37 ? 232 ARG C CA  1 
ATOM   7497 C C   . ARG C 1 232 ? 40.944 7.436   39.369  1.00 37.53 ? 232 ARG C C   1 
ATOM   7498 O O   . ARG C 1 232 ? 41.355 8.423   39.989  1.00 35.77 ? 232 ARG C O   1 
ATOM   7499 C CB  . ARG C 1 232 ? 42.324 6.792   37.360  1.00 37.76 ? 232 ARG C CB  1 
ATOM   7500 C CG  . ARG C 1 232 ? 42.464 6.839   35.831  1.00 47.61 ? 232 ARG C CG  1 
ATOM   7501 C CD  . ARG C 1 232 ? 43.909 6.855   35.335  1.00 50.43 ? 232 ARG C CD  1 
ATOM   7502 N NE  . ARG C 1 232 ? 44.530 8.182   35.320  1.00 50.22 ? 232 ARG C NE  1 
ATOM   7503 C CZ  . ARG C 1 232 ? 45.714 8.429   34.756  1.00 52.53 ? 232 ARG C CZ  1 
ATOM   7504 N NH1 . ARG C 1 232 ? 46.377 7.441   34.174  1.00 53.20 ? 232 ARG C NH1 1 
ATOM   7505 N NH2 . ARG C 1 232 ? 46.247 9.647   34.773  1.00 48.48 ? 232 ARG C NH2 1 
ATOM   7506 N N   . THR C 1 233 ? 40.370 6.398   39.969  1.00 41.71 ? 233 THR C N   1 
ATOM   7507 C CA  . THR C 1 233 ? 40.245 6.329   41.425  1.00 45.42 ? 233 THR C CA  1 
ATOM   7508 C C   . THR C 1 233 ? 40.737 5.025   42.042  1.00 44.92 ? 233 THR C C   1 
ATOM   7509 O O   . THR C 1 233 ? 40.166 3.964   41.794  1.00 46.33 ? 233 THR C O   1 
ATOM   7510 C CB  . THR C 1 233 ? 38.786 6.513   41.864  1.00 47.40 ? 233 THR C CB  1 
ATOM   7511 O OG1 . THR C 1 233 ? 37.958 5.640   41.089  1.00 55.96 ? 233 THR C OG1 1 
ATOM   7512 C CG2 . THR C 1 233 ? 38.335 7.945   41.654  1.00 51.67 ? 233 THR C CG2 1 
ATOM   7513 N N   . ASP C 1 234 ? 41.794 5.112   42.846  1.00 47.46 ? 234 ASP C N   1 
ATOM   7514 C CA  . ASP C 1 234 ? 42.341 3.957   43.549  1.00 46.45 ? 234 ASP C CA  1 
ATOM   7515 C C   . ASP C 1 234 ? 41.427 3.734   44.756  1.00 46.79 ? 234 ASP C C   1 
ATOM   7516 O O   . ASP C 1 234 ? 41.643 4.319   45.825  1.00 43.19 ? 234 ASP C O   1 
ATOM   7517 C CB  . ASP C 1 234 ? 43.759 4.271   44.026  1.00 50.93 ? 234 ASP C CB  1 
ATOM   7518 C CG  . ASP C 1 234 ? 44.451 3.071   44.668  1.00 54.77 ? 234 ASP C CG  1 
ATOM   7519 O OD1 . ASP C 1 234 ? 43.765 2.180   45.221  1.00 53.17 ? 234 ASP C OD1 1 
ATOM   7520 O OD2 . ASP C 1 234 ? 45.702 3.030   44.621  1.00 58.17 ? 234 ASP C OD2 1 
ATOM   7521 N N   . ASN C 1 235 ? 40.425 2.877   44.585  1.00 48.91 ? 235 ASN C N   1 
ATOM   7522 C CA  . ASN C 1 235 ? 39.450 2.580   45.636  1.00 52.62 ? 235 ASN C CA  1 
ATOM   7523 C C   . ASN C 1 235 ? 40.028 2.110   46.979  1.00 53.66 ? 235 ASN C C   1 
ATOM   7524 O O   . ASN C 1 235 ? 39.434 2.354   48.040  1.00 53.80 ? 235 ASN C O   1 
ATOM   7525 C CB  . ASN C 1 235 ? 38.394 1.602   45.115  1.00 55.69 ? 235 ASN C CB  1 
ATOM   7526 C CG  . ASN C 1 235 ? 37.518 2.219   44.029  1.00 63.20 ? 235 ASN C CG  1 
ATOM   7527 O OD1 . ASN C 1 235 ? 37.524 1.767   42.879  1.00 67.11 ? 235 ASN C OD1 1 
ATOM   7528 N ND2 . ASN C 1 235 ? 36.781 3.273   44.383  1.00 63.03 ? 235 ASN C ND2 1 
ATOM   7529 N N   . SER C 1 236 ? 41.183 1.453   46.938  1.00 52.38 ? 236 SER C N   1 
ATOM   7530 C CA  . SER C 1 236 ? 41.828 1.000   48.154  1.00 53.05 ? 236 SER C CA  1 
ATOM   7531 C C   . SER C 1 236 ? 42.399 2.180   48.901  1.00 52.78 ? 236 SER C C   1 
ATOM   7532 O O   . SER C 1 236 ? 42.341 2.225   50.128  1.00 54.92 ? 236 SER C O   1 
ATOM   7533 C CB  . SER C 1 236 ? 42.944 0.009   47.851  1.00 55.52 ? 236 SER C CB  1 
ATOM   7534 O OG  . SER C 1 236 ? 42.410 -1.296  47.723  1.00 67.75 ? 236 SER C OG  1 
ATOM   7535 N N   . LEU C 1 237 ? 42.937 3.142   48.161  1.00 50.33 ? 237 LEU C N   1 
ATOM   7536 C CA  . LEU C 1 237 ? 43.517 4.322   48.778  1.00 50.21 ? 237 LEU C CA  1 
ATOM   7537 C C   . LEU C 1 237 ? 42.597 5.521   48.877  1.00 47.39 ? 237 LEU C C   1 
ATOM   7538 O O   . LEU C 1 237 ? 43.001 6.546   49.415  1.00 48.44 ? 237 LEU C O   1 
ATOM   7539 C CB  . LEU C 1 237 ? 44.809 4.722   48.076  1.00 55.78 ? 237 LEU C CB  1 
ATOM   7540 C CG  . LEU C 1 237 ? 46.027 4.143   48.779  1.00 62.26 ? 237 LEU C CG  1 
ATOM   7541 C CD1 . LEU C 1 237 ? 46.811 3.339   47.803  1.00 64.49 ? 237 LEU C CD1 1 
ATOM   7542 C CD2 . LEU C 1 237 ? 46.864 5.240   49.401  1.00 67.27 ? 237 LEU C CD2 1 
ATOM   7543 N N   . ASN C 1 238 ? 41.395 5.416   48.314  1.00 43.24 ? 238 ASN C N   1 
ATOM   7544 C CA  . ASN C 1 238 ? 40.409 6.494   48.361  1.00 38.39 ? 238 ASN C CA  1 
ATOM   7545 C C   . ASN C 1 238 ? 40.999 7.803   47.844  1.00 39.19 ? 238 ASN C C   1 
ATOM   7546 O O   . ASN C 1 238 ? 40.738 8.881   48.408  1.00 37.05 ? 238 ASN C O   1 
ATOM   7547 C CB  . ASN C 1 238 ? 39.928 6.677   49.796  1.00 35.08 ? 238 ASN C CB  1 
ATOM   7548 C CG  . ASN C 1 238 ? 38.529 7.196   49.882  1.00 30.58 ? 238 ASN C CG  1 
ATOM   7549 O OD1 . ASN C 1 238 ? 38.222 8.286   49.422  1.00 36.35 ? 238 ASN C OD1 1 
ATOM   7550 N ND2 . ASN C 1 238 ? 37.654 6.406   50.475  1.00 37.97 ? 238 ASN C ND2 1 
ATOM   7551 N N   . VAL C 1 239 ? 41.826 7.696   46.801  1.00 35.34 ? 239 VAL C N   1 
ATOM   7552 C CA  . VAL C 1 239 ? 42.464 8.853   46.174  1.00 33.76 ? 239 VAL C CA  1 
ATOM   7553 C C   . VAL C 1 239 ? 42.204 8.793   44.666  1.00 32.29 ? 239 VAL C C   1 
ATOM   7554 O O   . VAL C 1 239 ? 42.264 7.722   44.050  1.00 32.72 ? 239 VAL C O   1 
ATOM   7555 C CB  . VAL C 1 239 ? 44.020 8.920   46.444  1.00 32.55 ? 239 VAL C CB  1 
ATOM   7556 C CG1 . VAL C 1 239 ? 44.639 10.137  45.764  1.00 25.84 ? 239 VAL C CG1 1 
ATOM   7557 C CG2 . VAL C 1 239 ? 44.307 9.013   47.930  1.00 32.25 ? 239 VAL C CG2 1 
ATOM   7558 N N   . LEU C 1 240 ? 41.952 9.971   44.096  1.00 34.80 ? 240 LEU C N   1 
ATOM   7559 C CA  . LEU C 1 240 ? 41.663 10.197  42.685  1.00 30.59 ? 240 LEU C CA  1 
ATOM   7560 C C   . LEU C 1 240 ? 42.864 10.882  42.001  1.00 30.61 ? 240 LEU C C   1 
ATOM   7561 O O   . LEU C 1 240 ? 43.547 11.718  42.597  1.00 31.41 ? 240 LEU C O   1 
ATOM   7562 C CB  . LEU C 1 240 ? 40.396 11.054  42.619  1.00 30.26 ? 240 LEU C CB  1 
ATOM   7563 C CG  . LEU C 1 240 ? 39.885 11.887  41.451  1.00 35.62 ? 240 LEU C CG  1 
ATOM   7564 C CD1 . LEU C 1 240 ? 38.405 12.179  41.678  1.00 33.15 ? 240 LEU C CD1 1 
ATOM   7565 C CD2 . LEU C 1 240 ? 40.683 13.197  41.361  1.00 41.02 ? 240 LEU C CD2 1 
ATOM   7566 N N   . ILE C 1 241 ? 43.112 10.512  40.750  1.00 33.19 ? 241 ILE C N   1 
ATOM   7567 C CA  . ILE C 1 241 ? 44.221 11.040  39.951  1.00 34.78 ? 241 ILE C CA  1 
ATOM   7568 C C   . ILE C 1 241 ? 43.669 11.644  38.659  1.00 32.05 ? 241 ILE C C   1 
ATOM   7569 O O   . ILE C 1 241 ? 43.016 10.946  37.884  1.00 32.82 ? 241 ILE C O   1 
ATOM   7570 C CB  . ILE C 1 241 ? 45.205 9.891   39.578  1.00 41.24 ? 241 ILE C CB  1 
ATOM   7571 C CG1 . ILE C 1 241 ? 45.611 9.112   40.833  1.00 45.83 ? 241 ILE C CG1 1 
ATOM   7572 C CG2 . ILE C 1 241 ? 46.455 10.440  38.912  1.00 41.83 ? 241 ILE C CG2 1 
ATOM   7573 C CD1 . ILE C 1 241 ? 46.380 7.854   40.535  1.00 51.38 ? 241 ILE C CD1 1 
ATOM   7574 N N   . SER C 1 242 ? 43.910 12.933  38.439  1.00 30.81 ? 242 SER C N   1 
ATOM   7575 C CA  . SER C 1 242 ? 43.424 13.612  37.244  1.00 28.96 ? 242 SER C CA  1 
ATOM   7576 C C   . SER C 1 242 ? 44.552 14.122  36.364  1.00 34.39 ? 242 SER C C   1 
ATOM   7577 O O   . SER C 1 242 ? 45.685 14.316  36.830  1.00 36.15 ? 242 SER C O   1 
ATOM   7578 C CB  . SER C 1 242 ? 42.579 14.806  37.637  1.00 25.06 ? 242 SER C CB  1 
ATOM   7579 O OG  . SER C 1 242 ? 41.660 14.456  38.645  1.00 32.29 ? 242 SER C OG  1 
ATOM   7580 N N   . SER C 1 243 ? 44.230 14.342  35.092  1.00 34.50 ? 243 SER C N   1 
ATOM   7581 C CA  . SER C 1 243 ? 45.167 14.890  34.113  1.00 34.21 ? 243 SER C CA  1 
ATOM   7582 C C   . SER C 1 243 ? 44.334 15.843  33.292  1.00 33.03 ? 243 SER C C   1 
ATOM   7583 O O   . SER C 1 243 ? 43.253 15.474  32.846  1.00 35.02 ? 243 SER C O   1 
ATOM   7584 C CB  . SER C 1 243 ? 45.718 13.802  33.199  1.00 38.82 ? 243 SER C CB  1 
ATOM   7585 O OG  . SER C 1 243 ? 46.406 12.810  33.942  1.00 53.22 ? 243 SER C OG  1 
ATOM   7586 N N   . ILE C 1 244 ? 44.772 17.088  33.167  1.00 32.14 ? 244 ILE C N   1 
ATOM   7587 C CA  . ILE C 1 244 ? 44.019 18.067  32.388  1.00 35.07 ? 244 ILE C CA  1 
ATOM   7588 C C   . ILE C 1 244 ? 44.929 18.708  31.338  1.00 34.24 ? 244 ILE C C   1 
ATOM   7589 O O   . ILE C 1 244 ? 46.100 18.996  31.625  1.00 32.98 ? 244 ILE C O   1 
ATOM   7590 C CB  . ILE C 1 244 ? 43.438 19.220  33.283  1.00 36.07 ? 244 ILE C CB  1 
ATOM   7591 C CG1 . ILE C 1 244 ? 42.405 18.696  34.275  1.00 38.87 ? 244 ILE C CG1 1 
ATOM   7592 C CG2 . ILE C 1 244 ? 42.755 20.266  32.432  1.00 40.91 ? 244 ILE C CG2 1 
ATOM   7593 C CD1 . ILE C 1 244 ? 42.926 18.567  35.680  1.00 38.56 ? 244 ILE C CD1 1 
ATOM   7594 N N   . GLU C 1 245 ? 44.412 18.859  30.117  1.00 36.30 ? 245 GLU C N   1 
ATOM   7595 C CA  . GLU C 1 245 ? 45.130 19.529  29.025  1.00 32.18 ? 245 GLU C CA  1 
ATOM   7596 C C   . GLU C 1 245 ? 44.087 20.503  28.508  1.00 27.09 ? 245 GLU C C   1 
ATOM   7597 O O   . GLU C 1 245 ? 42.919 20.145  28.395  1.00 23.56 ? 245 GLU C O   1 
ATOM   7598 C CB  . GLU C 1 245 ? 45.489 18.588  27.883  1.00 36.95 ? 245 GLU C CB  1 
ATOM   7599 C CG  . GLU C 1 245 ? 45.932 17.216  28.269  1.00 54.42 ? 245 GLU C CG  1 
ATOM   7600 C CD  . GLU C 1 245 ? 45.437 16.181  27.265  1.00 68.25 ? 245 GLU C CD  1 
ATOM   7601 O OE1 . GLU C 1 245 ? 45.408 16.481  26.042  1.00 69.72 ? 245 GLU C OE1 1 
ATOM   7602 O OE2 . GLU C 1 245 ? 45.046 15.072  27.707  1.00 77.80 ? 245 GLU C OE2 1 
ATOM   7603 N N   . MET C 1 246 ? 44.494 21.739  28.259  1.00 26.91 ? 246 MET C N   1 
ATOM   7604 C CA  . MET C 1 246 ? 43.596 22.764  27.749  1.00 30.71 ? 246 MET C CA  1 
ATOM   7605 C C   . MET C 1 246 ? 44.280 23.614  26.659  1.00 33.84 ? 246 MET C C   1 
ATOM   7606 O O   . MET C 1 246 ? 45.505 23.864  26.696  1.00 32.94 ? 246 MET C O   1 
ATOM   7607 C CB  . MET C 1 246 ? 43.130 23.677  28.892  1.00 28.64 ? 246 MET C CB  1 
ATOM   7608 C CG  . MET C 1 246 ? 42.212 23.035  29.918  1.00 30.27 ? 246 MET C CG  1 
ATOM   7609 S SD  . MET C 1 246 ? 41.986 24.095  31.379  1.00 25.82 ? 246 MET C SD  1 
ATOM   7610 C CE  . MET C 1 246 ? 40.881 25.282  30.676  1.00 29.52 ? 246 MET C CE  1 
ATOM   7611 N N   . GLU C 1 247 ? 43.495 24.019  25.665  1.00 38.78 ? 247 GLU C N   1 
ATOM   7612 C CA  . GLU C 1 247 ? 44.014 24.858  24.588  1.00 47.01 ? 247 GLU C CA  1 
ATOM   7613 C C   . GLU C 1 247 ? 44.032 26.300  25.094  1.00 47.33 ? 247 GLU C C   1 
ATOM   7614 O O   . GLU C 1 247 ? 43.121 26.724  25.829  1.00 46.97 ? 247 GLU C O   1 
ATOM   7615 C CB  . GLU C 1 247 ? 43.146 24.727  23.342  1.00 49.53 ? 247 GLU C CB  1 
ATOM   7616 C CG  . GLU C 1 247 ? 43.226 23.358  22.697  1.00 63.21 ? 247 GLU C CG  1 
ATOM   7617 C CD  . GLU C 1 247 ? 44.610 23.056  22.145  1.00 74.19 ? 247 GLU C CD  1 
ATOM   7618 O OE1 . GLU C 1 247 ? 45.561 22.867  22.946  1.00 79.47 ? 247 GLU C OE1 1 
ATOM   7619 O OE2 . GLU C 1 247 ? 44.747 23.011  20.901  1.00 78.42 ? 247 GLU C OE2 1 
ATOM   7620 N N   . GLU C 1 248 ? 45.075 27.044  24.741  1.00 43.69 ? 248 GLU C N   1 
ATOM   7621 C CA  . GLU C 1 248 ? 45.184 28.411  25.210  1.00 37.16 ? 248 GLU C CA  1 
ATOM   7622 C C   . GLU C 1 248 ? 43.906 29.146  24.864  1.00 34.45 ? 248 GLU C C   1 
ATOM   7623 O O   . GLU C 1 248 ? 43.350 28.957  23.792  1.00 37.18 ? 248 GLU C O   1 
ATOM   7624 C CB  . GLU C 1 248 ? 46.425 29.075  24.627  1.00 37.35 ? 248 GLU C CB  1 
ATOM   7625 C CG  . GLU C 1 248 ? 46.192 30.032  23.500  1.00 43.43 ? 248 GLU C CG  1 
ATOM   7626 C CD  . GLU C 1 248 ? 46.113 31.443  23.987  1.00 53.10 ? 248 GLU C CD  1 
ATOM   7627 O OE1 . GLU C 1 248 ? 47.182 32.025  24.277  1.00 59.36 ? 248 GLU C OE1 1 
ATOM   7628 O OE2 . GLU C 1 248 ? 44.986 31.965  24.101  1.00 61.24 ? 248 GLU C OE2 1 
ATOM   7629 N N   . GLY C 1 249 ? 43.384 29.893  25.827  1.00 34.04 ? 249 GLY C N   1 
ATOM   7630 C CA  . GLY C 1 249 ? 42.157 30.638  25.628  1.00 31.02 ? 249 GLY C CA  1 
ATOM   7631 C C   . GLY C 1 249 ? 40.907 29.854  25.972  1.00 30.74 ? 249 GLY C C   1 
ATOM   7632 O O   . GLY C 1 249 ? 39.795 30.315  25.682  1.00 31.79 ? 249 GLY C O   1 
ATOM   7633 N N   . ALA C 1 250 ? 41.090 28.676  26.574  1.00 30.36 ? 250 ALA C N   1 
ATOM   7634 C CA  . ALA C 1 250 ? 39.984 27.798  26.972  1.00 30.24 ? 250 ALA C CA  1 
ATOM   7635 C C   . ALA C 1 250 ? 39.570 28.036  28.425  1.00 32.00 ? 250 ALA C C   1 
ATOM   7636 O O   . ALA C 1 250 ? 40.356 28.536  29.234  1.00 31.40 ? 250 ALA C O   1 
ATOM   7637 C CB  . ALA C 1 250 ? 40.367 26.316  26.774  1.00 23.15 ? 250 ALA C CB  1 
ATOM   7638 N N   . LEU C 1 251 ? 38.349 27.628  28.756  1.00 31.26 ? 251 LEU C N   1 
ATOM   7639 C CA  . LEU C 1 251 ? 37.827 27.788  30.097  1.00 30.66 ? 251 LEU C CA  1 
ATOM   7640 C C   . LEU C 1 251 ? 37.154 26.523  30.616  1.00 27.81 ? 251 LEU C C   1 
ATOM   7641 O O   . LEU C 1 251 ? 36.348 25.925  29.906  1.00 27.27 ? 251 LEU C O   1 
ATOM   7642 C CB  . LEU C 1 251 ? 36.806 28.945  30.124  1.00 33.14 ? 251 LEU C CB  1 
ATOM   7643 C CG  . LEU C 1 251 ? 36.072 29.256  31.447  1.00 32.84 ? 251 LEU C CG  1 
ATOM   7644 C CD1 . LEU C 1 251 ? 37.055 29.671  32.539  1.00 31.15 ? 251 LEU C CD1 1 
ATOM   7645 C CD2 . LEU C 1 251 ? 35.039 30.354  31.246  1.00 35.36 ? 251 LEU C CD2 1 
ATOM   7646 N N   . PHE C 1 252 ? 37.533 26.097  31.826  1.00 25.99 ? 252 PHE C N   1 
ATOM   7647 C CA  . PHE C 1 252 ? 36.898 24.958  32.501  1.00 20.79 ? 252 PHE C CA  1 
ATOM   7648 C C   . PHE C 1 252 ? 35.879 25.760  33.319  1.00 22.48 ? 252 PHE C C   1 
ATOM   7649 O O   . PHE C 1 252 ? 36.228 26.386  34.338  1.00 25.14 ? 252 PHE C O   1 
ATOM   7650 C CB  . PHE C 1 252 ? 37.901 24.262  33.425  1.00 16.47 ? 252 PHE C CB  1 
ATOM   7651 C CG  . PHE C 1 252 ? 37.452 22.908  33.948  1.00 18.23 ? 252 PHE C CG  1 
ATOM   7652 C CD1 . PHE C 1 252 ? 36.119 22.509  33.894  1.00 14.75 ? 252 PHE C CD1 1 
ATOM   7653 C CD2 . PHE C 1 252 ? 38.382 22.034  34.513  1.00 22.10 ? 252 PHE C CD2 1 
ATOM   7654 C CE1 . PHE C 1 252 ? 35.714 21.260  34.390  1.00 17.57 ? 252 PHE C CE1 1 
ATOM   7655 C CE2 . PHE C 1 252 ? 37.984 20.775  35.016  1.00 18.93 ? 252 PHE C CE2 1 
ATOM   7656 C CZ  . PHE C 1 252 ? 36.645 20.394  34.948  1.00 17.79 ? 252 PHE C CZ  1 
ATOM   7657 N N   . VAL C 1 253 ? 34.657 25.855  32.796  1.00 23.41 ? 253 VAL C N   1 
ATOM   7658 C CA  . VAL C 1 253 ? 33.582 26.630  33.432  1.00 24.15 ? 253 VAL C CA  1 
ATOM   7659 C C   . VAL C 1 253 ? 33.390 26.370  34.927  1.00 26.11 ? 253 VAL C C   1 
ATOM   7660 O O   . VAL C 1 253 ? 33.773 25.315  35.432  1.00 33.51 ? 253 VAL C O   1 
ATOM   7661 C CB  . VAL C 1 253 ? 32.228 26.425  32.713  1.00 24.53 ? 253 VAL C CB  1 
ATOM   7662 C CG1 . VAL C 1 253 ? 32.386 26.635  31.192  1.00 25.76 ? 253 VAL C CG1 1 
ATOM   7663 C CG2 . VAL C 1 253 ? 31.625 25.066  33.078  1.00 21.92 ? 253 VAL C CG2 1 
ATOM   7664 N N   . PRO C 1 254 ? 32.780 27.328  35.657  1.00 26.41 ? 254 PRO C N   1 
ATOM   7665 C CA  . PRO C 1 254 ? 32.546 27.173  37.099  1.00 20.44 ? 254 PRO C CA  1 
ATOM   7666 C C   . PRO C 1 254 ? 31.943 25.795  37.477  1.00 21.52 ? 254 PRO C C   1 
ATOM   7667 O O   . PRO C 1 254 ? 31.000 25.311  36.827  1.00 21.57 ? 254 PRO C O   1 
ATOM   7668 C CB  . PRO C 1 254 ? 31.564 28.319  37.399  1.00 22.06 ? 254 PRO C CB  1 
ATOM   7669 C CG  . PRO C 1 254 ? 31.950 29.372  36.421  1.00 20.95 ? 254 PRO C CG  1 
ATOM   7670 C CD  . PRO C 1 254 ? 32.151 28.569  35.157  1.00 21.44 ? 254 PRO C CD  1 
ATOM   7671 N N   . HIS C 1 255 ? 32.437 25.193  38.563  1.00 17.24 ? 255 HIS C N   1 
ATOM   7672 C CA  . HIS C 1 255 ? 31.959 23.878  38.992  1.00 12.77 ? 255 HIS C CA  1 
ATOM   7673 C C   . HIS C 1 255 ? 32.532 23.539  40.365  1.00 17.62 ? 255 HIS C C   1 
ATOM   7674 O O   . HIS C 1 255 ? 33.335 24.304  40.890  1.00 20.61 ? 255 HIS C O   1 
ATOM   7675 C CB  . HIS C 1 255 ? 32.480 22.840  38.024  1.00 12.08 ? 255 HIS C CB  1 
ATOM   7676 C CG  . HIS C 1 255 ? 33.972 22.674  38.067  1.00 8.47  ? 255 HIS C CG  1 
ATOM   7677 N ND1 . HIS C 1 255 ? 34.841 23.535  37.428  1.00 13.62 ? 255 HIS C ND1 1 
ATOM   7678 C CD2 . HIS C 1 255 ? 34.750 21.777  38.718  1.00 8.31  ? 255 HIS C CD2 1 
ATOM   7679 C CE1 . HIS C 1 255 ? 36.086 23.181  37.688  1.00 10.14 ? 255 HIS C CE1 1 
ATOM   7680 N NE2 . HIS C 1 255 ? 36.056 22.118  38.471  1.00 13.25 ? 255 HIS C NE2 1 
ATOM   7681 N N   . TYR C 1 256 ? 32.130 22.399  40.937  1.00 18.40 ? 256 TYR C N   1 
ATOM   7682 C CA  . TYR C 1 256 ? 32.675 21.949  42.226  1.00 18.78 ? 256 TYR C CA  1 
ATOM   7683 C C   . TYR C 1 256 ? 32.616 20.420  42.427  1.00 15.07 ? 256 TYR C C   1 
ATOM   7684 O O   . TYR C 1 256 ? 31.850 19.736  41.761  1.00 14.94 ? 256 TYR C O   1 
ATOM   7685 C CB  . TYR C 1 256 ? 32.043 22.718  43.419  1.00 16.23 ? 256 TYR C CB  1 
ATOM   7686 C CG  . TYR C 1 256 ? 30.621 22.348  43.777  1.00 12.78 ? 256 TYR C CG  1 
ATOM   7687 C CD1 . TYR C 1 256 ? 30.360 21.217  44.530  1.00 13.20 ? 256 TYR C CD1 1 
ATOM   7688 C CD2 . TYR C 1 256 ? 29.538 23.116  43.343  1.00 12.22 ? 256 TYR C CD2 1 
ATOM   7689 C CE1 . TYR C 1 256 ? 29.067 20.844  44.849  1.00 14.91 ? 256 TYR C CE1 1 
ATOM   7690 C CE2 . TYR C 1 256 ? 28.229 22.747  43.656  1.00 16.60 ? 256 TYR C CE2 1 
ATOM   7691 C CZ  . TYR C 1 256 ? 28.008 21.600  44.422  1.00 12.88 ? 256 TYR C CZ  1 
ATOM   7692 O OH  . TYR C 1 256 ? 26.740 21.235  44.822  1.00 21.51 ? 256 TYR C OH  1 
ATOM   7693 N N   . TYR C 1 257 ? 33.515 19.890  43.259  1.00 17.35 ? 257 TYR C N   1 
ATOM   7694 C CA  . TYR C 1 257 ? 33.561 18.454  43.593  1.00 17.77 ? 257 TYR C CA  1 
ATOM   7695 C C   . TYR C 1 257 ? 32.870 18.355  44.947  1.00 21.61 ? 257 TYR C C   1 
ATOM   7696 O O   . TYR C 1 257 ? 33.208 19.098  45.860  1.00 22.03 ? 257 TYR C O   1 
ATOM   7697 C CB  . TYR C 1 257 ? 35.016 17.937  43.664  1.00 18.36 ? 257 TYR C CB  1 
ATOM   7698 C CG  . TYR C 1 257 ? 35.633 17.698  42.293  1.00 22.63 ? 257 TYR C CG  1 
ATOM   7699 C CD1 . TYR C 1 257 ? 35.019 18.210  41.142  1.00 28.33 ? 257 TYR C CD1 1 
ATOM   7700 C CD2 . TYR C 1 257 ? 36.782 16.926  42.130  1.00 19.95 ? 257 TYR C CD2 1 
ATOM   7701 C CE1 . TYR C 1 257 ? 35.520 17.957  39.876  1.00 22.87 ? 257 TYR C CE1 1 
ATOM   7702 C CE2 . TYR C 1 257 ? 37.294 16.669  40.854  1.00 9.06  ? 257 TYR C CE2 1 
ATOM   7703 C CZ  . TYR C 1 257 ? 36.645 17.188  39.735  1.00 20.69 ? 257 TYR C CZ  1 
ATOM   7704 O OH  . TYR C 1 257 ? 37.064 16.922  38.449  1.00 26.45 ? 257 TYR C OH  1 
ATOM   7705 N N   . SER C 1 258 ? 31.880 17.473  45.053  1.00 23.97 ? 258 SER C N   1 
ATOM   7706 C CA  . SER C 1 258 ? 31.092 17.308  46.265  1.00 19.07 ? 258 SER C CA  1 
ATOM   7707 C C   . SER C 1 258 ? 31.819 16.999  47.568  1.00 21.50 ? 258 SER C C   1 
ATOM   7708 O O   . SER C 1 258 ? 31.500 17.589  48.613  1.00 24.72 ? 258 SER C O   1 
ATOM   7709 C CB  . SER C 1 258 ? 29.984 16.275  46.033  1.00 20.23 ? 258 SER C CB  1 
ATOM   7710 O OG  . SER C 1 258 ? 30.484 15.070  45.447  1.00 19.26 ? 258 SER C OG  1 
ATOM   7711 N N   . LYS C 1 259 ? 32.804 16.108  47.513  1.00 21.92 ? 259 LYS C N   1 
ATOM   7712 C CA  . LYS C 1 259 ? 33.529 15.710  48.710  1.00 21.64 ? 259 LYS C CA  1 
ATOM   7713 C C   . LYS C 1 259 ? 35.031 15.604  48.632  1.00 20.76 ? 259 LYS C C   1 
ATOM   7714 O O   . LYS C 1 259 ? 35.693 15.565  49.668  1.00 24.30 ? 259 LYS C O   1 
ATOM   7715 C CB  . LYS C 1 259 ? 32.981 14.380  49.207  1.00 28.46 ? 259 LYS C CB  1 
ATOM   7716 C CG  . LYS C 1 259 ? 32.832 13.340  48.125  1.00 31.54 ? 259 LYS C CG  1 
ATOM   7717 C CD  . LYS C 1 259 ? 31.758 12.358  48.520  1.00 44.88 ? 259 LYS C CD  1 
ATOM   7718 C CE  . LYS C 1 259 ? 30.438 13.069  48.936  1.00 54.52 ? 259 LYS C CE  1 
ATOM   7719 N NZ  . LYS C 1 259 ? 29.562 13.568  47.816  1.00 51.58 ? 259 LYS C NZ  1 
ATOM   7720 N N   . ALA C 1 260 ? 35.589 15.532  47.434  1.00 21.85 ? 260 ALA C N   1 
ATOM   7721 C CA  . ALA C 1 260 ? 37.044 15.425  47.313  1.00 22.29 ? 260 ALA C CA  1 
ATOM   7722 C C   . ALA C 1 260 ? 37.787 16.768  47.461  1.00 24.75 ? 260 ALA C C   1 
ATOM   7723 O O   . ALA C 1 260 ? 37.319 17.801  46.951  1.00 22.78 ? 260 ALA C O   1 
ATOM   7724 C CB  . ALA C 1 260 ? 37.406 14.775  45.974  1.00 27.61 ? 260 ALA C CB  1 
ATOM   7725 N N   . ILE C 1 261 ? 38.919 16.742  48.176  1.00 20.41 ? 261 ILE C N   1 
ATOM   7726 C CA  . ILE C 1 261 ? 39.795 17.901  48.360  1.00 18.11 ? 261 ILE C CA  1 
ATOM   7727 C C   . ILE C 1 261 ? 40.880 17.747  47.278  1.00 21.13 ? 261 ILE C C   1 
ATOM   7728 O O   . ILE C 1 261 ? 41.708 16.832  47.362  1.00 21.60 ? 261 ILE C O   1 
ATOM   7729 C CB  . ILE C 1 261 ? 40.470 17.872  49.741  1.00 12.13 ? 261 ILE C CB  1 
ATOM   7730 C CG1 . ILE C 1 261 ? 39.444 18.183  50.817  1.00 15.29 ? 261 ILE C CG1 1 
ATOM   7731 C CG2 . ILE C 1 261 ? 41.610 18.856  49.806  1.00 11.93 ? 261 ILE C CG2 1 
ATOM   7732 C CD1 . ILE C 1 261 ? 40.017 18.219  52.215  1.00 22.21 ? 261 ILE C CD1 1 
ATOM   7733 N N   . VAL C 1 262 ? 40.877 18.646  46.285  1.00 23.03 ? 262 VAL C N   1 
ATOM   7734 C CA  . VAL C 1 262 ? 41.811 18.594  45.149  1.00 19.40 ? 262 VAL C CA  1 
ATOM   7735 C C   . VAL C 1 262 ? 43.068 19.480  45.213  1.00 20.35 ? 262 VAL C C   1 
ATOM   7736 O O   . VAL C 1 262 ? 43.000 20.695  45.448  1.00 18.26 ? 262 VAL C O   1 
ATOM   7737 C CB  . VAL C 1 262 ? 41.053 18.866  43.784  1.00 24.68 ? 262 VAL C CB  1 
ATOM   7738 C CG1 . VAL C 1 262 ? 42.025 18.844  42.575  1.00 16.33 ? 262 VAL C CG1 1 
ATOM   7739 C CG2 . VAL C 1 262 ? 39.929 17.832  43.573  1.00 17.93 ? 262 VAL C CG2 1 
ATOM   7740 N N   . ILE C 1 263 ? 44.213 18.830  44.992  1.00 23.16 ? 263 ILE C N   1 
ATOM   7741 C CA  . ILE C 1 263 ? 45.552 19.443  44.965  1.00 20.84 ? 263 ILE C CA  1 
ATOM   7742 C C   . ILE C 1 263 ? 45.966 19.506  43.468  1.00 23.37 ? 263 ILE C C   1 
ATOM   7743 O O   . ILE C 1 263 ? 46.063 18.455  42.810  1.00 19.42 ? 263 ILE C O   1 
ATOM   7744 C CB  . ILE C 1 263 ? 46.567 18.542  45.699  1.00 15.66 ? 263 ILE C CB  1 
ATOM   7745 C CG1 . ILE C 1 263 ? 46.122 18.318  47.152  1.00 12.92 ? 263 ILE C CG1 1 
ATOM   7746 C CG2 . ILE C 1 263 ? 47.964 19.143  45.598  1.00 14.94 ? 263 ILE C CG2 1 
ATOM   7747 C CD1 . ILE C 1 263 ? 46.840 17.130  47.878  1.00 2.22  ? 263 ILE C CD1 1 
ATOM   7748 N N   . LEU C 1 264 ? 46.176 20.716  42.943  1.00 21.74 ? 264 LEU C N   1 
ATOM   7749 C CA  . LEU C 1 264 ? 46.538 20.931  41.528  1.00 23.99 ? 264 LEU C CA  1 
ATOM   7750 C C   . LEU C 1 264 ? 47.986 21.310  41.320  1.00 22.66 ? 264 LEU C C   1 
ATOM   7751 O O   . LEU C 1 264 ? 48.461 22.253  41.955  1.00 21.86 ? 264 LEU C O   1 
ATOM   7752 C CB  . LEU C 1 264 ? 45.746 22.103  40.961  1.00 25.56 ? 264 LEU C CB  1 
ATOM   7753 C CG  . LEU C 1 264 ? 44.659 21.976  39.905  1.00 23.67 ? 264 LEU C CG  1 
ATOM   7754 C CD1 . LEU C 1 264 ? 44.509 23.351  39.292  1.00 20.12 ? 264 LEU C CD1 1 
ATOM   7755 C CD2 . LEU C 1 264 ? 44.932 20.905  38.842  1.00 16.50 ? 264 LEU C CD2 1 
ATOM   7756 N N   . VAL C 1 265 ? 48.641 20.655  40.359  1.00 23.06 ? 265 VAL C N   1 
ATOM   7757 C CA  . VAL C 1 265 ? 50.047 20.931  40.031  1.00 21.97 ? 265 VAL C CA  1 
ATOM   7758 C C   . VAL C 1 265 ? 50.160 21.276  38.551  1.00 25.86 ? 265 VAL C C   1 
ATOM   7759 O O   . VAL C 1 265 ? 49.635 20.548  37.703  1.00 27.29 ? 265 VAL C O   1 
ATOM   7760 C CB  . VAL C 1 265 ? 50.947 19.707  40.285  1.00 18.64 ? 265 VAL C CB  1 
ATOM   7761 C CG1 . VAL C 1 265 ? 52.411 20.096  40.095  1.00 14.76 ? 265 VAL C CG1 1 
ATOM   7762 C CG2 . VAL C 1 265 ? 50.701 19.148  41.694  1.00 16.26 ? 265 VAL C CG2 1 
ATOM   7763 N N   . VAL C 1 266 ? 50.798 22.401  38.243  1.00 25.61 ? 266 VAL C N   1 
ATOM   7764 C CA  . VAL C 1 266 ? 50.962 22.826  36.857  1.00 23.66 ? 266 VAL C CA  1 
ATOM   7765 C C   . VAL C 1 266 ? 52.211 22.134  36.335  1.00 25.32 ? 266 VAL C C   1 
ATOM   7766 O O   . VAL C 1 266 ? 53.289 22.315  36.897  1.00 26.89 ? 266 VAL C O   1 
ATOM   7767 C CB  . VAL C 1 266 ? 51.125 24.372  36.749  1.00 19.10 ? 266 VAL C CB  1 
ATOM   7768 C CG1 . VAL C 1 266 ? 51.260 24.794  35.305  1.00 23.67 ? 266 VAL C CG1 1 
ATOM   7769 C CG2 . VAL C 1 266 ? 49.917 25.071  37.332  1.00 21.39 ? 266 VAL C CG2 1 
ATOM   7770 N N   . ASN C 1 267 ? 52.066 21.318  35.293  1.00 28.48 ? 267 ASN C N   1 
ATOM   7771 C CA  . ASN C 1 267 ? 53.212 20.606  34.727  1.00 31.06 ? 267 ASN C CA  1 
ATOM   7772 C C   . ASN C 1 267 ? 53.941 21.471  33.724  1.00 31.08 ? 267 ASN C C   1 
ATOM   7773 O O   . ASN C 1 267 ? 55.167 21.630  33.788  1.00 27.86 ? 267 ASN C O   1 
ATOM   7774 C CB  . ASN C 1 267 ? 52.778 19.299  34.070  1.00 33.98 ? 267 ASN C CB  1 
ATOM   7775 C CG  . ASN C 1 267 ? 52.268 18.281  35.084  1.00 33.78 ? 267 ASN C CG  1 
ATOM   7776 O OD1 . ASN C 1 267 ? 52.644 18.302  36.265  1.00 33.72 ? 267 ASN C OD1 1 
ATOM   7777 N ND2 . ASN C 1 267 ? 51.412 17.383  34.626  1.00 32.73 ? 267 ASN C ND2 1 
ATOM   7778 N N   . GLU C 1 268 ? 53.165 22.037  32.811  1.00 35.31 ? 268 GLU C N   1 
ATOM   7779 C CA  . GLU C 1 268 ? 53.662 22.926  31.775  1.00 36.98 ? 268 GLU C CA  1 
ATOM   7780 C C   . GLU C 1 268 ? 52.560 23.933  31.484  1.00 34.61 ? 268 GLU C C   1 
ATOM   7781 O O   . GLU C 1 268 ? 51.380 23.631  31.661  1.00 31.05 ? 268 GLU C O   1 
ATOM   7782 C CB  . GLU C 1 268 ? 54.004 22.144  30.499  1.00 44.61 ? 268 GLU C CB  1 
ATOM   7783 C CG  . GLU C 1 268 ? 55.379 21.463  30.511  1.00 63.84 ? 268 GLU C CG  1 
ATOM   7784 C CD  . GLU C 1 268 ? 55.333 19.930  30.328  1.00 74.01 ? 268 GLU C CD  1 
ATOM   7785 O OE1 . GLU C 1 268 ? 54.224 19.343  30.334  1.00 77.06 ? 268 GLU C OE1 1 
ATOM   7786 O OE2 . GLU C 1 268 ? 56.425 19.311  30.190  1.00 76.11 ? 268 GLU C OE2 1 
ATOM   7787 N N   . GLY C 1 269 ? 52.952 25.154  31.131  1.00 35.64 ? 269 GLY C N   1 
ATOM   7788 C CA  . GLY C 1 269 ? 51.983 26.185  30.779  1.00 36.93 ? 269 GLY C CA  1 
ATOM   7789 C C   . GLY C 1 269 ? 51.586 27.189  31.846  1.00 35.08 ? 269 GLY C C   1 
ATOM   7790 O O   . GLY C 1 269 ? 52.136 27.195  32.951  1.00 34.71 ? 269 GLY C O   1 
ATOM   7791 N N   . GLU C 1 270 ? 50.619 28.033  31.493  1.00 33.19 ? 270 GLU C N   1 
ATOM   7792 C CA  . GLU C 1 270 ? 50.094 29.069  32.369  1.00 29.16 ? 270 GLU C CA  1 
ATOM   7793 C C   . GLU C 1 270 ? 48.558 29.095  32.388  1.00 29.38 ? 270 GLU C C   1 
ATOM   7794 O O   . GLU C 1 270 ? 47.907 28.876  31.348  1.00 26.57 ? 270 GLU C O   1 
ATOM   7795 C CB  . GLU C 1 270 ? 50.640 30.426  31.940  1.00 31.90 ? 270 GLU C CB  1 
ATOM   7796 C CG  . GLU C 1 270 ? 51.984 30.721  32.536  1.00 41.57 ? 270 GLU C CG  1 
ATOM   7797 C CD  . GLU C 1 270 ? 53.018 31.173  31.538  1.00 52.78 ? 270 GLU C CD  1 
ATOM   7798 O OE1 . GLU C 1 270 ? 52.820 30.988  30.307  1.00 53.80 ? 270 GLU C OE1 1 
ATOM   7799 O OE2 . GLU C 1 270 ? 54.052 31.701  32.012  1.00 59.27 ? 270 GLU C OE2 1 
ATOM   7800 N N   . ALA C 1 271 ? 47.991 29.389  33.568  1.00 25.61 ? 271 ALA C N   1 
ATOM   7801 C CA  . ALA C 1 271 ? 46.539 29.443  33.761  1.00 19.62 ? 271 ALA C CA  1 
ATOM   7802 C C   . ALA C 1 271 ? 46.105 30.508  34.762  1.00 19.28 ? 271 ALA C C   1 
ATOM   7803 O O   . ALA C 1 271 ? 46.895 30.964  35.582  1.00 18.43 ? 271 ALA C O   1 
ATOM   7804 C CB  . ALA C 1 271 ? 46.026 28.076  34.222  1.00 14.36 ? 271 ALA C CB  1 
ATOM   7805 N N   . HIS C 1 272 ? 44.848 30.921  34.670  1.00 19.46 ? 272 HIS C N   1 
ATOM   7806 C CA  . HIS C 1 272 ? 44.293 31.891  35.597  1.00 20.81 ? 272 HIS C CA  1 
ATOM   7807 C C   . HIS C 1 272 ? 43.175 31.174  36.354  1.00 22.02 ? 272 HIS C C   1 
ATOM   7808 O O   . HIS C 1 272 ? 42.234 30.637  35.759  1.00 19.87 ? 272 HIS C O   1 
ATOM   7809 C CB  . HIS C 1 272 ? 43.740 33.107  34.867  1.00 26.11 ? 272 HIS C CB  1 
ATOM   7810 C CG  . HIS C 1 272 ? 42.795 33.922  35.692  1.00 24.47 ? 272 HIS C CG  1 
ATOM   7811 N ND1 . HIS C 1 272 ? 43.220 34.797  36.670  1.00 29.50 ? 272 HIS C ND1 1 
ATOM   7812 C CD2 . HIS C 1 272 ? 41.441 33.949  35.729  1.00 21.67 ? 272 HIS C CD2 1 
ATOM   7813 C CE1 . HIS C 1 272 ? 42.172 35.325  37.276  1.00 24.65 ? 272 HIS C CE1 1 
ATOM   7814 N NE2 . HIS C 1 272 ? 41.082 34.825  36.724  1.00 26.10 ? 272 HIS C NE2 1 
ATOM   7815 N N   . VAL C 1 273 ? 43.253 31.219  37.676  1.00 24.54 ? 273 VAL C N   1 
ATOM   7816 C CA  . VAL C 1 273 ? 42.281 30.529  38.506  1.00 23.67 ? 273 VAL C CA  1 
ATOM   7817 C C   . VAL C 1 273 ? 41.488 31.465  39.413  1.00 22.97 ? 273 VAL C C   1 
ATOM   7818 O O   . VAL C 1 273 ? 41.983 32.514  39.841  1.00 22.79 ? 273 VAL C O   1 
ATOM   7819 C CB  . VAL C 1 273 ? 42.988 29.364  39.309  1.00 19.88 ? 273 VAL C CB  1 
ATOM   7820 C CG1 . VAL C 1 273 ? 44.124 29.906  40.139  1.00 19.60 ? 273 VAL C CG1 1 
ATOM   7821 C CG2 . VAL C 1 273 ? 42.009 28.598  40.164  1.00 20.24 ? 273 VAL C CG2 1 
ATOM   7822 N N   . GLU C 1 274 ? 40.207 31.136  39.561  1.00 25.51 ? 274 GLU C N   1 
ATOM   7823 C CA  . GLU C 1 274 ? 39.292 31.871  40.410  1.00 22.63 ? 274 GLU C CA  1 
ATOM   7824 C C   . GLU C 1 274 ? 38.564 30.862  41.307  1.00 22.36 ? 274 GLU C C   1 
ATOM   7825 O O   . GLU C 1 274 ? 37.934 29.920  40.818  1.00 15.78 ? 274 GLU C O   1 
ATOM   7826 C CB  . GLU C 1 274 ? 38.323 32.698  39.563  1.00 24.68 ? 274 GLU C CB  1 
ATOM   7827 C CG  . GLU C 1 274 ? 38.877 34.057  39.121  1.00 25.66 ? 274 GLU C CG  1 
ATOM   7828 C CD  . GLU C 1 274 ? 37.904 34.845  38.256  1.00 27.67 ? 274 GLU C CD  1 
ATOM   7829 O OE1 . GLU C 1 274 ? 36.698 34.861  38.567  1.00 22.46 ? 274 GLU C OE1 1 
ATOM   7830 O OE2 . GLU C 1 274 ? 38.340 35.450  37.259  1.00 28.04 ? 274 GLU C OE2 1 
ATOM   7831 N N   . LEU C 1 275 ? 38.735 31.032  42.622  1.00 24.10 ? 275 LEU C N   1 
ATOM   7832 C CA  . LEU C 1 275 ? 38.143 30.155  43.638  1.00 22.60 ? 275 LEU C CA  1 
ATOM   7833 C C   . LEU C 1 275 ? 37.251 30.976  44.534  1.00 22.03 ? 275 LEU C C   1 
ATOM   7834 O O   . LEU C 1 275 ? 37.678 32.022  44.982  1.00 26.47 ? 275 LEU C O   1 
ATOM   7835 C CB  . LEU C 1 275 ? 39.239 29.544  44.513  1.00 20.07 ? 275 LEU C CB  1 
ATOM   7836 C CG  . LEU C 1 275 ? 38.797 28.480  45.525  1.00 22.48 ? 275 LEU C CG  1 
ATOM   7837 C CD1 . LEU C 1 275 ? 38.366 27.213  44.800  1.00 22.31 ? 275 LEU C CD1 1 
ATOM   7838 C CD2 . LEU C 1 275 ? 39.930 28.167  46.480  1.00 17.70 ? 275 LEU C CD2 1 
ATOM   7839 N N   . VAL C 1 276 ? 36.046 30.497  44.838  1.00 20.81 ? 276 VAL C N   1 
ATOM   7840 C CA  . VAL C 1 276 ? 35.133 31.243  45.707  1.00 22.25 ? 276 VAL C CA  1 
ATOM   7841 C C   . VAL C 1 276 ? 35.051 30.566  47.062  1.00 27.48 ? 276 VAL C C   1 
ATOM   7842 O O   . VAL C 1 276 ? 34.562 29.443  47.175  1.00 33.56 ? 276 VAL C O   1 
ATOM   7843 C CB  . VAL C 1 276 ? 33.713 31.354  45.110  1.00 22.08 ? 276 VAL C CB  1 
ATOM   7844 C CG1 . VAL C 1 276 ? 32.776 32.110  46.058  1.00 10.11 ? 276 VAL C CG1 1 
ATOM   7845 C CG2 . VAL C 1 276 ? 33.773 32.049  43.761  1.00 16.87 ? 276 VAL C CG2 1 
ATOM   7846 N N   . GLY C 1 277 ? 35.533 31.255  48.091  1.00 31.83 ? 277 GLY C N   1 
ATOM   7847 C CA  . GLY C 1 277 ? 35.519 30.700  49.423  1.00 31.71 ? 277 GLY C CA  1 
ATOM   7848 C C   . GLY C 1 277 ? 34.871 31.659  50.386  1.00 38.29 ? 277 GLY C C   1 
ATOM   7849 O O   . GLY C 1 277 ? 34.304 32.668  49.962  1.00 40.33 ? 277 GLY C O   1 
ATOM   7850 N N   . PRO C 1 278 ? 34.854 31.321  51.685  1.00 40.71 ? 278 PRO C N   1 
ATOM   7851 C CA  . PRO C 1 278 ? 34.256 32.181  52.713  1.00 41.57 ? 278 PRO C CA  1 
ATOM   7852 C C   . PRO C 1 278 ? 35.219 33.335  53.022  1.00 42.40 ? 278 PRO C C   1 
ATOM   7853 O O   . PRO C 1 278 ? 36.384 33.279  52.637  1.00 42.78 ? 278 PRO C O   1 
ATOM   7854 C CB  . PRO C 1 278 ? 34.120 31.222  53.897  1.00 42.05 ? 278 PRO C CB  1 
ATOM   7855 C CG  . PRO C 1 278 ? 35.341 30.331  53.735  1.00 38.48 ? 278 PRO C CG  1 
ATOM   7856 C CD  . PRO C 1 278 ? 35.317 30.041  52.260  1.00 37.15 ? 278 PRO C CD  1 
ATOM   7857 N N   . LYS C 1 279 ? 34.761 34.374  53.711  1.00 44.50 ? 279 LYS C N   1 
ATOM   7858 C CA  . LYS C 1 279 ? 35.670 35.471  54.021  1.00 49.71 ? 279 LYS C CA  1 
ATOM   7859 C C   . LYS C 1 279 ? 36.749 35.142  55.060  1.00 55.68 ? 279 LYS C C   1 
ATOM   7860 O O   . LYS C 1 279 ? 37.704 35.897  55.225  1.00 56.42 ? 279 LYS C O   1 
ATOM   7861 C CB  . LYS C 1 279 ? 34.909 36.733  54.405  1.00 47.13 ? 279 LYS C CB  1 
ATOM   7862 C CG  . LYS C 1 279 ? 34.783 37.696  53.245  1.00 50.81 ? 279 LYS C CG  1 
ATOM   7863 C CD  . LYS C 1 279 ? 34.030 38.958  53.597  1.00 55.79 ? 279 LYS C CD  1 
ATOM   7864 C CE  . LYS C 1 279 ? 34.842 39.885  54.482  1.00 62.99 ? 279 LYS C CE  1 
ATOM   7865 N NZ  . LYS C 1 279 ? 34.068 41.131  54.767  1.00 65.95 ? 279 LYS C NZ  1 
ATOM   7866 N N   . GLY C 1 280 ? 36.632 33.998  55.727  1.00 59.85 ? 280 GLY C N   1 
ATOM   7867 C CA  . GLY C 1 280 ? 37.632 33.641  56.715  1.00 62.74 ? 280 GLY C CA  1 
ATOM   7868 C C   . GLY C 1 280 ? 37.497 32.229  57.246  1.00 68.96 ? 280 GLY C C   1 
ATOM   7869 O O   . GLY C 1 280 ? 37.753 31.974  58.431  1.00 74.74 ? 280 GLY C O   1 
ATOM   7870 N N   . GLU C 1 283 ? 32.349 31.497  59.528  1.00 36.91 ? 283 GLU C N   1 
ATOM   7871 C CA  . GLU C 1 283 ? 30.993 31.021  59.247  1.00 38.73 ? 283 GLU C CA  1 
ATOM   7872 C C   . GLU C 1 283 ? 29.981 32.143  59.005  1.00 37.79 ? 283 GLU C C   1 
ATOM   7873 O O   . GLU C 1 283 ? 29.142 32.441  59.847  1.00 45.81 ? 283 GLU C O   1 
ATOM   7874 C CB  . GLU C 1 283 ? 30.500 30.112  60.378  1.00 37.94 ? 283 GLU C CB  1 
ATOM   7875 C CG  . GLU C 1 283 ? 31.156 28.760  60.400  1.00 41.79 ? 283 GLU C CG  1 
ATOM   7876 C CD  . GLU C 1 283 ? 31.132 28.089  61.756  1.00 45.87 ? 283 GLU C CD  1 
ATOM   7877 O OE1 . GLU C 1 283 ? 30.482 28.607  62.695  1.00 48.64 ? 283 GLU C OE1 1 
ATOM   7878 O OE2 . GLU C 1 283 ? 31.804 27.036  61.887  1.00 50.75 ? 283 GLU C OE2 1 
ATOM   7879 N N   . THR C 1 284 ? 30.057 32.776  57.851  1.00 35.76 ? 284 THR C N   1 
ATOM   7880 C CA  . THR C 1 284 ? 29.126 33.849  57.537  1.00 34.39 ? 284 THR C CA  1 
ATOM   7881 C C   . THR C 1 284 ? 28.503 33.400  56.251  1.00 28.90 ? 284 THR C C   1 
ATOM   7882 O O   . THR C 1 284 ? 28.726 32.283  55.824  1.00 33.92 ? 284 THR C O   1 
ATOM   7883 C CB  . THR C 1 284 ? 29.850 35.194  57.253  1.00 36.78 ? 284 THR C CB  1 
ATOM   7884 O OG1 . THR C 1 284 ? 30.673 35.070  56.075  1.00 31.77 ? 284 THR C OG1 1 
ATOM   7885 C CG2 . THR C 1 284 ? 30.710 35.598  58.431  1.00 40.82 ? 284 THR C CG2 1 
ATOM   7886 N N   . LEU C 1 285 ? 27.736 34.269  55.626  1.00 24.24 ? 285 LEU C N   1 
ATOM   7887 C CA  . LEU C 1 285 ? 27.141 33.927  54.367  1.00 26.12 ? 285 LEU C CA  1 
ATOM   7888 C C   . LEU C 1 285 ? 27.839 34.800  53.304  1.00 29.96 ? 285 LEU C C   1 
ATOM   7889 O O   . LEU C 1 285 ? 27.379 34.904  52.166  1.00 34.64 ? 285 LEU C O   1 
ATOM   7890 C CB  . LEU C 1 285 ? 25.605 34.105  54.426  1.00 20.85 ? 285 LEU C CB  1 
ATOM   7891 C CG  . LEU C 1 285 ? 24.835 33.152  55.374  1.00 14.86 ? 285 LEU C CG  1 
ATOM   7892 C CD1 . LEU C 1 285 ? 23.279 33.206  55.172  1.00 2.42  ? 285 LEU C CD1 1 
ATOM   7893 C CD2 . LEU C 1 285 ? 25.351 31.709  55.185  1.00 18.36 ? 285 LEU C CD2 1 
ATOM   7894 N N   . GLU C 1 286 ? 28.981 35.380  53.692  1.00 29.49 ? 286 GLU C N   1 
ATOM   7895 C CA  . GLU C 1 286 ? 29.806 36.232  52.837  1.00 28.63 ? 286 GLU C CA  1 
ATOM   7896 C C   . GLU C 1 286 ? 30.864 35.410  52.127  1.00 27.67 ? 286 GLU C C   1 
ATOM   7897 O O   . GLU C 1 286 ? 31.600 34.672  52.763  1.00 29.32 ? 286 GLU C O   1 
ATOM   7898 C CB  . GLU C 1 286 ? 30.561 37.251  53.673  1.00 33.32 ? 286 GLU C CB  1 
ATOM   7899 C CG  . GLU C 1 286 ? 29.730 38.199  54.485  1.00 44.53 ? 286 GLU C CG  1 
ATOM   7900 C CD  . GLU C 1 286 ? 30.587 39.302  55.063  1.00 54.22 ? 286 GLU C CD  1 
ATOM   7901 O OE1 . GLU C 1 286 ? 30.907 40.254  54.307  1.00 58.49 ? 286 GLU C OE1 1 
ATOM   7902 O OE2 . GLU C 1 286 ? 30.971 39.199  56.256  1.00 57.34 ? 286 GLU C OE2 1 
ATOM   7903 N N   . TYR C 1 287 ? 30.983 35.566  50.817  1.00 30.39 ? 287 TYR C N   1 
ATOM   7904 C CA  . TYR C 1 287 ? 31.993 34.825  50.069  1.00 30.22 ? 287 TYR C CA  1 
ATOM   7905 C C   . TYR C 1 287 ? 33.084 35.815  49.676  1.00 32.80 ? 287 TYR C C   1 
ATOM   7906 O O   . TYR C 1 287 ? 32.918 37.031  49.824  1.00 29.36 ? 287 TYR C O   1 
ATOM   7907 C CB  . TYR C 1 287 ? 31.370 34.135  48.840  1.00 31.72 ? 287 TYR C CB  1 
ATOM   7908 C CG  . TYR C 1 287 ? 30.137 33.373  49.229  1.00 29.95 ? 287 TYR C CG  1 
ATOM   7909 C CD1 . TYR C 1 287 ? 30.137 32.603  50.401  1.00 35.60 ? 287 TYR C CD1 1 
ATOM   7910 C CD2 . TYR C 1 287 ? 28.927 33.563  48.561  1.00 22.21 ? 287 TYR C CD2 1 
ATOM   7911 C CE1 . TYR C 1 287 ? 28.971 32.074  50.920  1.00 37.87 ? 287 TYR C CE1 1 
ATOM   7912 C CE2 . TYR C 1 287 ? 27.744 33.026  49.061  1.00 30.62 ? 287 TYR C CE2 1 
ATOM   7913 C CZ  . TYR C 1 287 ? 27.771 32.292  50.262  1.00 38.76 ? 287 TYR C CZ  1 
ATOM   7914 O OH  . TYR C 1 287 ? 26.606 31.870  50.886  1.00 45.26 ? 287 TYR C OH  1 
ATOM   7915 N N   . GLU C 1 288 ? 34.198 35.287  49.191  1.00 33.07 ? 288 GLU C N   1 
ATOM   7916 C CA  . GLU C 1 288 ? 35.316 36.107  48.788  1.00 35.71 ? 288 GLU C CA  1 
ATOM   7917 C C   . GLU C 1 288 ? 36.051 35.359  47.697  1.00 34.95 ? 288 GLU C C   1 
ATOM   7918 O O   . GLU C 1 288 ? 36.204 34.132  47.760  1.00 33.49 ? 288 GLU C O   1 
ATOM   7919 C CB  . GLU C 1 288 ? 36.235 36.350  49.975  1.00 36.70 ? 288 GLU C CB  1 
ATOM   7920 C CG  . GLU C 1 288 ? 37.145 37.529  49.830  1.00 46.15 ? 288 GLU C CG  1 
ATOM   7921 C CD  . GLU C 1 288 ? 37.760 37.890  51.152  1.00 56.86 ? 288 GLU C CD  1 
ATOM   7922 O OE1 . GLU C 1 288 ? 38.569 37.090  51.666  1.00 61.01 ? 288 GLU C OE1 1 
ATOM   7923 O OE2 . GLU C 1 288 ? 37.401 38.949  51.709  1.00 64.16 ? 288 GLU C OE2 1 
ATOM   7924 N N   . SER C 1 289 ? 36.481 36.109  46.688  1.00 34.98 ? 289 SER C N   1 
ATOM   7925 C CA  . SER C 1 289 ? 37.175 35.559  45.547  1.00 28.42 ? 289 SER C CA  1 
ATOM   7926 C C   . SER C 1 289 ? 38.670 35.474  45.778  1.00 28.11 ? 289 SER C C   1 
ATOM   7927 O O   . SER C 1 289 ? 39.306 36.469  46.093  1.00 30.60 ? 289 SER C O   1 
ATOM   7928 C CB  . SER C 1 289 ? 36.908 36.424  44.323  1.00 29.07 ? 289 SER C CB  1 
ATOM   7929 O OG  . SER C 1 289 ? 37.229 35.726  43.141  1.00 33.88 ? 289 SER C OG  1 
ATOM   7930 N N   . TYR C 1 290 ? 39.219 34.274  45.644  1.00 24.60 ? 290 TYR C N   1 
ATOM   7931 C CA  . TYR C 1 290 ? 40.642 34.043  45.786  1.00 22.43 ? 290 TYR C CA  1 
ATOM   7932 C C   . TYR C 1 290 ? 41.119 33.779  44.354  1.00 23.89 ? 290 TYR C C   1 
ATOM   7933 O O   . TYR C 1 290 ? 40.669 32.829  43.727  1.00 26.57 ? 290 TYR C O   1 
ATOM   7934 C CB  . TYR C 1 290 ? 40.869 32.824  46.682  1.00 22.63 ? 290 TYR C CB  1 
ATOM   7935 C CG  . TYR C 1 290 ? 40.381 33.037  48.099  1.00 26.03 ? 290 TYR C CG  1 
ATOM   7936 C CD1 . TYR C 1 290 ? 41.208 33.637  49.053  1.00 25.20 ? 290 TYR C CD1 1 
ATOM   7937 C CD2 . TYR C 1 290 ? 39.057 32.730  48.464  1.00 23.30 ? 290 TYR C CD2 1 
ATOM   7938 C CE1 . TYR C 1 290 ? 40.726 33.941  50.338  1.00 25.08 ? 290 TYR C CE1 1 
ATOM   7939 C CE2 . TYR C 1 290 ? 38.574 33.028  49.731  1.00 23.48 ? 290 TYR C CE2 1 
ATOM   7940 C CZ  . TYR C 1 290 ? 39.417 33.637  50.660  1.00 24.76 ? 290 TYR C CZ  1 
ATOM   7941 O OH  . TYR C 1 290 ? 38.953 33.959  51.904  1.00 30.42 ? 290 TYR C OH  1 
ATOM   7942 N N   . ARG C 1 291 ? 42.003 34.632  43.831  1.00 26.94 ? 291 ARG C N   1 
ATOM   7943 C CA  . ARG C 1 291 ? 42.508 34.501  42.455  1.00 24.31 ? 291 ARG C CA  1 
ATOM   7944 C C   . ARG C 1 291 ? 44.023 34.414  42.362  1.00 25.20 ? 291 ARG C C   1 
ATOM   7945 O O   . ARG C 1 291 ? 44.746 34.928  43.236  1.00 26.16 ? 291 ARG C O   1 
ATOM   7946 C CB  . ARG C 1 291 ? 42.033 35.690  41.609  1.00 22.65 ? 291 ARG C CB  1 
ATOM   7947 C CG  . ARG C 1 291 ? 40.559 35.935  41.736  1.00 23.45 ? 291 ARG C CG  1 
ATOM   7948 C CD  . ARG C 1 291 ? 40.023 37.065  40.898  1.00 26.17 ? 291 ARG C CD  1 
ATOM   7949 N NE  . ARG C 1 291 ? 38.561 37.044  40.967  1.00 20.51 ? 291 ARG C NE  1 
ATOM   7950 C CZ  . ARG C 1 291 ? 37.765 37.995  40.505  1.00 22.50 ? 291 ARG C CZ  1 
ATOM   7951 N NH1 . ARG C 1 291 ? 38.263 39.051  39.867  1.00 23.10 ? 291 ARG C NH1 1 
ATOM   7952 N NH2 . ARG C 1 291 ? 36.454 37.865  40.654  1.00 27.58 ? 291 ARG C NH2 1 
ATOM   7953 N N   . ALA C 1 292 ? 44.497 33.768  41.297  1.00 19.99 ? 292 ALA C N   1 
ATOM   7954 C CA  . ALA C 1 292 ? 45.927 33.620  41.049  1.00 21.77 ? 292 ALA C CA  1 
ATOM   7955 C C   . ALA C 1 292 ? 46.268 33.335  39.562  1.00 19.89 ? 292 ALA C C   1 
ATOM   7956 O O   . ALA C 1 292 ? 45.394 32.995  38.769  1.00 21.65 ? 292 ALA C O   1 
ATOM   7957 C CB  . ALA C 1 292 ? 46.533 32.525  41.982  1.00 20.17 ? 292 ALA C CB  1 
ATOM   7958 N N   . GLU C 1 293 ? 47.519 33.592  39.188  1.00 18.66 ? 293 GLU C N   1 
ATOM   7959 C CA  . GLU C 1 293 ? 48.032 33.328  37.853  1.00 19.88 ? 293 GLU C CA  1 
ATOM   7960 C C   . GLU C 1 293 ? 49.044 32.237  38.120  1.00 23.96 ? 293 GLU C C   1 
ATOM   7961 O O   . GLU C 1 293 ? 50.033 32.466  38.813  1.00 26.43 ? 293 GLU C O   1 
ATOM   7962 C CB  . GLU C 1 293 ? 48.730 34.550  37.275  1.00 21.32 ? 293 GLU C CB  1 
ATOM   7963 C CG  . GLU C 1 293 ? 47.871 35.807  37.274  1.00 30.39 ? 293 GLU C CG  1 
ATOM   7964 C CD  . GLU C 1 293 ? 46.555 35.650  36.527  1.00 36.20 ? 293 GLU C CD  1 
ATOM   7965 O OE1 . GLU C 1 293 ? 46.491 34.913  35.514  1.00 40.49 ? 293 GLU C OE1 1 
ATOM   7966 O OE2 . GLU C 1 293 ? 45.574 36.285  36.965  1.00 43.96 ? 293 GLU C OE2 1 
ATOM   7967 N N   . LEU C 1 294 ? 48.719 31.026  37.684  1.00 26.84 ? 294 LEU C N   1 
ATOM   7968 C CA  . LEU C 1 294 ? 49.563 29.856  37.877  1.00 25.68 ? 294 LEU C CA  1 
ATOM   7969 C C   . LEU C 1 294 ? 50.507 29.610  36.698  1.00 27.96 ? 294 LEU C C   1 
ATOM   7970 O O   . LEU C 1 294 ? 50.196 29.960  35.555  1.00 29.88 ? 294 LEU C O   1 
ATOM   7971 C CB  . LEU C 1 294 ? 48.672 28.630  38.021  1.00 20.13 ? 294 LEU C CB  1 
ATOM   7972 C CG  . LEU C 1 294 ? 48.005 28.177  39.318  1.00 18.59 ? 294 LEU C CG  1 
ATOM   7973 C CD1 . LEU C 1 294 ? 47.858 29.255  40.364  1.00 19.62 ? 294 LEU C CD1 1 
ATOM   7974 C CD2 . LEU C 1 294 ? 46.672 27.550  38.937  1.00 17.32 ? 294 LEU C CD2 1 
ATOM   7975 N N   . SER C 1 295 ? 51.644 28.990  36.999  1.00 28.49 ? 295 SER C N   1 
ATOM   7976 C CA  . SER C 1 295 ? 52.655 28.621  36.014  1.00 31.37 ? 295 SER C CA  1 
ATOM   7977 C C   . SER C 1 295 ? 53.430 27.426  36.570  1.00 32.86 ? 295 SER C C   1 
ATOM   7978 O O   . SER C 1 295 ? 53.296 27.091  37.751  1.00 31.11 ? 295 SER C O   1 
ATOM   7979 C CB  . SER C 1 295 ? 53.594 29.789  35.689  1.00 32.67 ? 295 SER C CB  1 
ATOM   7980 O OG  . SER C 1 295 ? 54.064 30.409  36.864  1.00 32.73 ? 295 SER C OG  1 
ATOM   7981 N N   . LYS C 1 296 ? 54.231 26.799  35.712  1.00 33.73 ? 296 LYS C N   1 
ATOM   7982 C CA  . LYS C 1 296 ? 55.026 25.613  36.044  1.00 35.55 ? 296 LYS C CA  1 
ATOM   7983 C C   . LYS C 1 296 ? 55.482 25.393  37.490  1.00 35.57 ? 296 LYS C C   1 
ATOM   7984 O O   . LYS C 1 296 ? 56.226 26.212  38.044  1.00 36.53 ? 296 LYS C O   1 
ATOM   7985 C CB  . LYS C 1 296 ? 56.233 25.507  35.128  1.00 38.48 ? 296 LYS C CB  1 
ATOM   7986 C CG  . LYS C 1 296 ? 56.913 24.163  35.226  1.00 44.94 ? 296 LYS C CG  1 
ATOM   7987 C CD  . LYS C 1 296 ? 58.189 24.124  34.425  1.00 52.80 ? 296 LYS C CD  1 
ATOM   7988 C CE  . LYS C 1 296 ? 58.902 22.811  34.641  1.00 58.25 ? 296 LYS C CE  1 
ATOM   7989 N NZ  . LYS C 1 296 ? 59.239 22.622  36.079  1.00 65.02 ? 296 LYS C NZ  1 
ATOM   7990 N N   . ASP C 1 297 ? 55.078 24.240  38.040  1.00 30.42 ? 297 ASP C N   1 
ATOM   7991 C CA  . ASP C 1 297 ? 55.391 23.793  39.399  1.00 27.84 ? 297 ASP C CA  1 
ATOM   7992 C C   . ASP C 1 297 ? 54.709 24.550  40.570  1.00 28.60 ? 297 ASP C C   1 
ATOM   7993 O O   . ASP C 1 297 ? 55.176 24.513  41.719  1.00 25.27 ? 297 ASP C O   1 
ATOM   7994 C CB  . ASP C 1 297 ? 56.915 23.704  39.609  1.00 28.37 ? 297 ASP C CB  1 
ATOM   7995 C CG  . ASP C 1 297 ? 57.579 22.589  38.801  1.00 20.64 ? 297 ASP C CG  1 
ATOM   7996 O OD1 . ASP C 1 297 ? 56.897 21.857  38.077  1.00 26.47 ? 297 ASP C OD1 1 
ATOM   7997 O OD2 . ASP C 1 297 ? 58.809 22.446  38.888  1.00 21.65 ? 297 ASP C OD2 1 
ATOM   7998 N N   . ASP C 1 298 ? 53.619 25.253  40.275  1.00 28.44 ? 298 ASP C N   1 
ATOM   7999 C CA  . ASP C 1 298 ? 52.852 25.959  41.307  1.00 25.58 ? 298 ASP C CA  1 
ATOM   8000 C C   . ASP C 1 298 ? 51.777 24.993  41.828  1.00 23.71 ? 298 ASP C C   1 
ATOM   8001 O O   . ASP C 1 298 ? 51.168 24.268  41.050  1.00 24.53 ? 298 ASP C O   1 
ATOM   8002 C CB  . ASP C 1 298 ? 52.124 27.164  40.707  1.00 19.23 ? 298 ASP C CB  1 
ATOM   8003 C CG  . ASP C 1 298 ? 52.969 28.414  40.661  1.00 25.59 ? 298 ASP C CG  1 
ATOM   8004 O OD1 . ASP C 1 298 ? 54.097 28.449  41.200  1.00 23.37 ? 298 ASP C OD1 1 
ATOM   8005 O OD2 . ASP C 1 298 ? 52.471 29.403  40.090  1.00 29.17 ? 298 ASP C OD2 1 
ATOM   8006 N N   . VAL C 1 299 ? 51.517 24.997  43.127  1.00 24.84 ? 299 VAL C N   1 
ATOM   8007 C CA  . VAL C 1 299 ? 50.481 24.123  43.675  1.00 24.47 ? 299 VAL C CA  1 
ATOM   8008 C C   . VAL C 1 299 ? 49.302 24.991  44.144  1.00 24.18 ? 299 VAL C C   1 
ATOM   8009 O O   . VAL C 1 299 ? 49.505 25.970  44.863  1.00 29.41 ? 299 VAL C O   1 
ATOM   8010 C CB  . VAL C 1 299 ? 51.019 23.281  44.887  1.00 21.40 ? 299 VAL C CB  1 
ATOM   8011 C CG1 . VAL C 1 299 ? 49.992 22.285  45.342  1.00 10.02 ? 299 VAL C CG1 1 
ATOM   8012 C CG2 . VAL C 1 299 ? 52.289 22.569  44.516  1.00 19.07 ? 299 VAL C CG2 1 
ATOM   8013 N N   . PHE C 1 300 ? 48.097 24.682  43.674  1.00 23.68 ? 300 PHE C N   1 
ATOM   8014 C CA  . PHE C 1 300 ? 46.893 25.404  44.086  1.00 22.26 ? 300 PHE C CA  1 
ATOM   8015 C C   . PHE C 1 300 ? 45.882 24.404  44.686  1.00 21.83 ? 300 PHE C C   1 
ATOM   8016 O O   . PHE C 1 300 ? 45.531 23.399  44.048  1.00 18.56 ? 300 PHE C O   1 
ATOM   8017 C CB  . PHE C 1 300 ? 46.264 26.173  42.909  1.00 22.71 ? 300 PHE C CB  1 
ATOM   8018 C CG  . PHE C 1 300 ? 45.123 27.103  43.314  1.00 25.60 ? 300 PHE C CG  1 
ATOM   8019 C CD1 . PHE C 1 300 ? 45.380 28.415  43.723  1.00 29.56 ? 300 PHE C CD1 1 
ATOM   8020 C CD2 . PHE C 1 300 ? 43.797 26.662  43.306  1.00 21.74 ? 300 PHE C CD2 1 
ATOM   8021 C CE1 . PHE C 1 300 ? 44.330 29.276  44.121  1.00 21.50 ? 300 PHE C CE1 1 
ATOM   8022 C CE2 . PHE C 1 300 ? 42.761 27.503  43.698  1.00 24.55 ? 300 PHE C CE2 1 
ATOM   8023 C CZ  . PHE C 1 300 ? 43.031 28.817  44.107  1.00 20.32 ? 300 PHE C CZ  1 
ATOM   8024 N N   . VAL C 1 301 ? 45.429 24.672  45.916  1.00 23.47 ? 301 VAL C N   1 
ATOM   8025 C CA  . VAL C 1 301 ? 44.466 23.796  46.603  1.00 18.81 ? 301 VAL C CA  1 
ATOM   8026 C C   . VAL C 1 301 ? 43.017 24.216  46.388  1.00 15.36 ? 301 VAL C C   1 
ATOM   8027 O O   . VAL C 1 301 ? 42.695 25.390  46.528  1.00 13.12 ? 301 VAL C O   1 
ATOM   8028 C CB  . VAL C 1 301 ? 44.721 23.745  48.133  1.00 18.66 ? 301 VAL C CB  1 
ATOM   8029 C CG1 . VAL C 1 301 ? 43.620 22.925  48.826  1.00 8.69  ? 301 VAL C CG1 1 
ATOM   8030 C CG2 . VAL C 1 301 ? 46.110 23.197  48.423  1.00 17.08 ? 301 VAL C CG2 1 
ATOM   8031 N N   . ILE C 1 302 ? 42.156 23.230  46.118  1.00 16.90 ? 302 ILE C N   1 
ATOM   8032 C CA  . ILE C 1 302 ? 40.699 23.415  45.874  1.00 20.65 ? 302 ILE C CA  1 
ATOM   8033 C C   . ILE C 1 302 ? 39.889 22.548  46.861  1.00 22.80 ? 302 ILE C C   1 
ATOM   8034 O O   . ILE C 1 302 ? 39.711 21.334  46.660  1.00 20.84 ? 302 ILE C O   1 
ATOM   8035 C CB  . ILE C 1 302 ? 40.286 23.009  44.411  1.00 19.51 ? 302 ILE C CB  1 
ATOM   8036 C CG1 . ILE C 1 302 ? 41.127 23.762  43.370  1.00 20.38 ? 302 ILE C CG1 1 
ATOM   8037 C CG2 . ILE C 1 302 ? 38.812 23.283  44.192  1.00 15.21 ? 302 ILE C CG2 1 
ATOM   8038 C CD1 . ILE C 1 302 ? 41.105 23.135  41.975  1.00 10.31 ? 302 ILE C CD1 1 
ATOM   8039 N N   . PRO C 1 303 ? 39.385 23.172  47.943  1.00 20.18 ? 303 PRO C N   1 
ATOM   8040 C CA  . PRO C 1 303 ? 38.606 22.545  49.000  1.00 16.80 ? 303 PRO C CA  1 
ATOM   8041 C C   . PRO C 1 303 ? 37.330 21.973  48.489  1.00 19.28 ? 303 PRO C C   1 
ATOM   8042 O O   . PRO C 1 303 ? 36.747 22.538  47.588  1.00 9.88  ? 303 PRO C O   1 
ATOM   8043 C CB  . PRO C 1 303 ? 38.306 23.710  49.915  1.00 11.78 ? 303 PRO C CB  1 
ATOM   8044 C CG  . PRO C 1 303 ? 39.489 24.577  49.758  1.00 9.28  ? 303 PRO C CG  1 
ATOM   8045 C CD  . PRO C 1 303 ? 39.581 24.595  48.256  1.00 20.41 ? 303 PRO C CD  1 
ATOM   8046 N N   . ALA C 1 304 ? 36.844 20.927  49.162  1.00 23.85 ? 304 ALA C N   1 
ATOM   8047 C CA  . ALA C 1 304 ? 35.606 20.245  48.787  1.00 21.03 ? 304 ALA C CA  1 
ATOM   8048 C C   . ALA C 1 304 ? 34.430 21.207  48.781  1.00 22.45 ? 304 ALA C C   1 
ATOM   8049 O O   . ALA C 1 304 ? 34.306 22.030  49.687  1.00 23.60 ? 304 ALA C O   1 
ATOM   8050 C CB  . ALA C 1 304 ? 35.333 19.115  49.744  1.00 23.24 ? 304 ALA C CB  1 
ATOM   8051 N N   . ALA C 1 305 ? 33.614 21.126  47.729  1.00 14.17 ? 305 ALA C N   1 
ATOM   8052 C CA  . ALA C 1 305 ? 32.415 21.927  47.542  1.00 13.27 ? 305 ALA C CA  1 
ATOM   8053 C C   . ALA C 1 305 ? 32.566 23.445  47.295  1.00 11.37 ? 305 ALA C C   1 
ATOM   8054 O O   . ALA C 1 305 ? 31.548 24.139  47.139  1.00 12.80 ? 305 ALA C O   1 
ATOM   8055 C CB  . ALA C 1 305 ? 31.432 21.658  48.658  1.00 13.55 ? 305 ALA C CB  1 
ATOM   8056 N N   . TYR C 1 306 ? 33.805 23.951  47.256  1.00 7.76  ? 306 TYR C N   1 
ATOM   8057 C CA  . TYR C 1 306 ? 34.078 25.382  46.979  1.00 12.21 ? 306 TYR C CA  1 
ATOM   8058 C C   . TYR C 1 306 ? 34.092 25.565  45.453  1.00 13.61 ? 306 TYR C C   1 
ATOM   8059 O O   . TYR C 1 306 ? 34.879 24.907  44.776  1.00 11.96 ? 306 TYR C O   1 
ATOM   8060 C CB  . TYR C 1 306 ? 35.463 25.800  47.481  1.00 15.04 ? 306 TYR C CB  1 
ATOM   8061 C CG  . TYR C 1 306 ? 35.613 25.995  48.973  1.00 17.66 ? 306 TYR C CG  1 
ATOM   8062 C CD1 . TYR C 1 306 ? 34.972 25.163  49.876  1.00 16.00 ? 306 TYR C CD1 1 
ATOM   8063 C CD2 . TYR C 1 306 ? 36.437 27.001  49.477  1.00 22.68 ? 306 TYR C CD2 1 
ATOM   8064 C CE1 . TYR C 1 306 ? 35.144 25.327  51.246  1.00 15.65 ? 306 TYR C CE1 1 
ATOM   8065 C CE2 . TYR C 1 306 ? 36.619 27.169  50.851  1.00 18.28 ? 306 TYR C CE2 1 
ATOM   8066 C CZ  . TYR C 1 306 ? 35.965 26.335  51.720  1.00 19.69 ? 306 TYR C CZ  1 
ATOM   8067 O OH  . TYR C 1 306 ? 36.083 26.537  53.079  1.00 28.41 ? 306 TYR C OH  1 
ATOM   8068 N N   . PRO C 1 307 ? 33.263 26.477  44.906  1.00 16.27 ? 307 PRO C N   1 
ATOM   8069 C CA  . PRO C 1 307 ? 33.178 26.743  43.451  1.00 18.03 ? 307 PRO C CA  1 
ATOM   8070 C C   . PRO C 1 307 ? 34.511 27.203  42.806  1.00 18.47 ? 307 PRO C C   1 
ATOM   8071 O O   . PRO C 1 307 ? 35.263 27.966  43.419  1.00 22.04 ? 307 PRO C O   1 
ATOM   8072 C CB  . PRO C 1 307 ? 32.090 27.821  43.378  1.00 12.20 ? 307 PRO C CB  1 
ATOM   8073 C CG  . PRO C 1 307 ? 31.252 27.541  44.584  1.00 10.11 ? 307 PRO C CG  1 
ATOM   8074 C CD  . PRO C 1 307 ? 32.276 27.289  45.633  1.00 8.32  ? 307 PRO C CD  1 
ATOM   8075 N N   . VAL C 1 308 ? 34.782 26.802  41.559  1.00 17.78 ? 308 VAL C N   1 
ATOM   8076 C CA  . VAL C 1 308 ? 36.050 27.180  40.910  1.00 10.55 ? 308 VAL C CA  1 
ATOM   8077 C C   . VAL C 1 308 ? 35.944 27.247  39.369  1.00 18.39 ? 308 VAL C C   1 
ATOM   8078 O O   . VAL C 1 308 ? 35.047 26.620  38.791  1.00 18.47 ? 308 VAL C O   1 
ATOM   8079 C CB  . VAL C 1 308 ? 37.153 26.171  41.329  1.00 8.19  ? 308 VAL C CB  1 
ATOM   8080 C CG1 . VAL C 1 308 ? 36.933 24.802  40.691  1.00 10.24 ? 308 VAL C CG1 1 
ATOM   8081 C CG2 . VAL C 1 308 ? 38.552 26.717  41.103  1.00 3.27  ? 308 VAL C CG2 1 
ATOM   8082 N N   . ALA C 1 309 ? 36.795 28.072  38.727  1.00 21.49 ? 309 ALA C N   1 
ATOM   8083 C CA  . ALA C 1 309 ? 36.849 28.230  37.248  1.00 15.12 ? 309 ALA C CA  1 
ATOM   8084 C C   . ALA C 1 309 ? 38.296 28.427  36.889  1.00 18.69 ? 309 ALA C C   1 
ATOM   8085 O O   . ALA C 1 309 ? 39.034 29.060  37.656  1.00 25.72 ? 309 ALA C O   1 
ATOM   8086 C CB  . ALA C 1 309 ? 36.075 29.425  36.803  1.00 12.20 ? 309 ALA C CB  1 
ATOM   8087 N N   . ILE C 1 310 ? 38.713 27.883  35.744  1.00 27.14 ? 310 ILE C N   1 
ATOM   8088 C CA  . ILE C 1 310 ? 40.112 27.987  35.282  1.00 24.42 ? 310 ILE C CA  1 
ATOM   8089 C C   . ILE C 1 310 ? 40.163 28.413  33.817  1.00 28.99 ? 310 ILE C C   1 
ATOM   8090 O O   . ILE C 1 310 ? 39.622 27.743  32.932  1.00 27.73 ? 310 ILE C O   1 
ATOM   8091 C CB  . ILE C 1 310 ? 40.908 26.628  35.432  1.00 25.45 ? 310 ILE C CB  1 
ATOM   8092 C CG1 . ILE C 1 310 ? 40.635 25.983  36.805  1.00 26.90 ? 310 ILE C CG1 1 
ATOM   8093 C CG2 . ILE C 1 310 ? 42.425 26.876  35.281  1.00 17.40 ? 310 ILE C CG2 1 
ATOM   8094 C CD1 . ILE C 1 310 ? 40.950 24.492  36.890  1.00 17.68 ? 310 ILE C CD1 1 
ATOM   8095 N N   . LYS C 1 311 ? 40.815 29.543  33.584  1.00 30.38 ? 311 LYS C N   1 
ATOM   8096 C CA  . LYS C 1 311 ? 40.987 30.122  32.265  1.00 27.47 ? 311 LYS C CA  1 
ATOM   8097 C C   . LYS C 1 311 ? 42.417 29.841  31.824  1.00 27.45 ? 311 LYS C C   1 
ATOM   8098 O O   . LYS C 1 311 ? 43.361 30.365  32.437  1.00 27.96 ? 311 LYS C O   1 
ATOM   8099 C CB  . LYS C 1 311 ? 40.796 31.634  32.369  1.00 30.32 ? 311 LYS C CB  1 
ATOM   8100 C CG  . LYS C 1 311 ? 41.052 32.382  31.101  1.00 30.76 ? 311 LYS C CG  1 
ATOM   8101 C CD  . LYS C 1 311 ? 39.759 32.698  30.415  1.00 41.09 ? 311 LYS C CD  1 
ATOM   8102 C CE  . LYS C 1 311 ? 40.004 32.870  28.945  1.00 49.93 ? 311 LYS C CE  1 
ATOM   8103 N NZ  . LYS C 1 311 ? 40.489 31.585  28.366  1.00 52.01 ? 311 LYS C NZ  1 
ATOM   8104 N N   . ALA C 1 312 ? 42.581 29.052  30.759  1.00 28.85 ? 312 ALA C N   1 
ATOM   8105 C CA  . ALA C 1 312 ? 43.909 28.704  30.222  1.00 27.52 ? 312 ALA C CA  1 
ATOM   8106 C C   . ALA C 1 312 ? 44.520 29.904  29.496  1.00 27.70 ? 312 ALA C C   1 
ATOM   8107 O O   . ALA C 1 312 ? 43.940 30.391  28.522  1.00 25.00 ? 312 ALA C O   1 
ATOM   8108 C CB  . ALA C 1 312 ? 43.795 27.511  29.278  1.00 24.39 ? 312 ALA C CB  1 
ATOM   8109 N N   . THR C 1 313 ? 45.664 30.402  29.970  1.00 28.72 ? 313 THR C N   1 
ATOM   8110 C CA  . THR C 1 313 ? 46.265 31.558  29.328  1.00 29.90 ? 313 THR C CA  1 
ATOM   8111 C C   . THR C 1 313 ? 47.351 31.203  28.358  1.00 31.25 ? 313 THR C C   1 
ATOM   8112 O O   . THR C 1 313 ? 47.885 32.056  27.673  1.00 36.32 ? 313 THR C O   1 
ATOM   8113 C CB  . THR C 1 313 ? 46.768 32.610  30.318  1.00 29.66 ? 313 THR C CB  1 
ATOM   8114 O OG1 . THR C 1 313 ? 47.609 31.999  31.293  1.00 34.13 ? 313 THR C OG1 1 
ATOM   8115 C CG2 . THR C 1 313 ? 45.598 33.289  30.982  1.00 25.40 ? 313 THR C CG2 1 
ATOM   8116 N N   . SER C 1 314 ? 47.684 29.932  28.307  1.00 32.75 ? 314 SER C N   1 
ATOM   8117 C CA  . SER C 1 314 ? 48.674 29.444  27.375  1.00 35.52 ? 314 SER C CA  1 
ATOM   8118 C C   . SER C 1 314 ? 48.342 27.973  27.326  1.00 36.93 ? 314 SER C C   1 
ATOM   8119 O O   . SER C 1 314 ? 47.526 27.514  28.118  1.00 43.87 ? 314 SER C O   1 
ATOM   8120 C CB  . SER C 1 314 ? 50.108 29.691  27.882  1.00 36.98 ? 314 SER C CB  1 
ATOM   8121 O OG  . SER C 1 314 ? 50.600 28.656  28.720  1.00 40.92 ? 314 SER C OG  1 
ATOM   8122 N N   . ASN C 1 315 ? 48.850 27.250  26.340  1.00 36.10 ? 315 ASN C N   1 
ATOM   8123 C CA  . ASN C 1 315 ? 48.573 25.826  26.301  1.00 35.83 ? 315 ASN C CA  1 
ATOM   8124 C C   . ASN C 1 315 ? 49.064 25.330  27.657  1.00 34.19 ? 315 ASN C C   1 
ATOM   8125 O O   . ASN C 1 315 ? 50.219 25.575  28.025  1.00 36.37 ? 315 ASN C O   1 
ATOM   8126 C CB  . ASN C 1 315 ? 49.334 25.176  25.145  1.00 41.67 ? 315 ASN C CB  1 
ATOM   8127 C CG  . ASN C 1 315 ? 48.568 25.256  23.838  1.00 39.53 ? 315 ASN C CG  1 
ATOM   8128 O OD1 . ASN C 1 315 ? 47.897 26.248  23.562  1.00 39.33 ? 315 ASN C OD1 1 
ATOM   8129 N ND2 . ASN C 1 315 ? 48.628 24.193  23.050  1.00 42.96 ? 315 ASN C ND2 1 
ATOM   8130 N N   . VAL C 1 316 ? 48.174 24.707  28.428  1.00 31.07 ? 316 VAL C N   1 
ATOM   8131 C CA  . VAL C 1 316 ? 48.541 24.265  29.768  1.00 25.36 ? 316 VAL C CA  1 
ATOM   8132 C C   . VAL C 1 316 ? 48.107 22.854  30.139  1.00 25.04 ? 316 VAL C C   1 
ATOM   8133 O O   . VAL C 1 316 ? 47.044 22.405  29.741  1.00 29.11 ? 316 VAL C O   1 
ATOM   8134 C CB  . VAL C 1 316 ? 47.921 25.236  30.792  1.00 26.38 ? 316 VAL C CB  1 
ATOM   8135 C CG1 . VAL C 1 316 ? 46.406 25.107  30.773  1.00 24.18 ? 316 VAL C CG1 1 
ATOM   8136 C CG2 . VAL C 1 316 ? 48.494 25.022  32.189  1.00 23.00 ? 316 VAL C CG2 1 
ATOM   8137 N N   . ASN C 1 317 ? 48.924 22.156  30.915  1.00 25.54 ? 317 ASN C N   1 
ATOM   8138 C CA  . ASN C 1 317 ? 48.547 20.832  31.378  1.00 26.91 ? 317 ASN C CA  1 
ATOM   8139 C C   . ASN C 1 317 ? 48.802 20.662  32.882  1.00 26.76 ? 317 ASN C C   1 
ATOM   8140 O O   . ASN C 1 317 ? 49.855 21.049  33.419  1.00 22.71 ? 317 ASN C O   1 
ATOM   8141 C CB  . ASN C 1 317 ? 49.178 19.716  30.540  1.00 38.89 ? 317 ASN C CB  1 
ATOM   8142 C CG  . ASN C 1 317 ? 50.672 19.816  30.464  1.00 50.32 ? 317 ASN C CG  1 
ATOM   8143 O OD1 . ASN C 1 317 ? 51.230 20.896  30.274  1.00 61.56 ? 317 ASN C OD1 1 
ATOM   8144 N ND2 . ASN C 1 317 ? 51.341 18.679  30.587  1.00 60.53 ? 317 ASN C ND2 1 
ATOM   8145 N N   . PHE C 1 318 ? 47.796 20.113  33.560  1.00 25.71 ? 318 PHE C N   1 
ATOM   8146 C CA  . PHE C 1 318 ? 47.834 19.907  34.998  1.00 23.26 ? 318 PHE C CA  1 
ATOM   8147 C C   . PHE C 1 318 ? 47.740 18.434  35.367  1.00 23.58 ? 318 PHE C C   1 
ATOM   8148 O O   . PHE C 1 318 ? 47.235 17.614  34.589  1.00 25.46 ? 318 PHE C O   1 
ATOM   8149 C CB  . PHE C 1 318 ? 46.606 20.551  35.651  1.00 22.70 ? 318 PHE C CB  1 
ATOM   8150 C CG  . PHE C 1 318 ? 46.300 21.954  35.196  1.00 22.74 ? 318 PHE C CG  1 
ATOM   8151 C CD1 . PHE C 1 318 ? 45.612 22.177  34.015  1.00 21.09 ? 318 PHE C CD1 1 
ATOM   8152 C CD2 . PHE C 1 318 ? 46.632 23.050  35.995  1.00 22.52 ? 318 PHE C CD2 1 
ATOM   8153 C CE1 . PHE C 1 318 ? 45.259 23.461  33.638  1.00 23.58 ? 318 PHE C CE1 1 
ATOM   8154 C CE2 . PHE C 1 318 ? 46.277 24.343  35.620  1.00 18.04 ? 318 PHE C CE2 1 
ATOM   8155 C CZ  . PHE C 1 318 ? 45.592 24.547  34.440  1.00 19.62 ? 318 PHE C CZ  1 
ATOM   8156 N N   . THR C 1 319 ? 48.229 18.119  36.563  1.00 22.03 ? 319 THR C N   1 
ATOM   8157 C CA  . THR C 1 319 ? 48.118 16.796  37.160  1.00 22.19 ? 319 THR C CA  1 
ATOM   8158 C C   . THR C 1 319 ? 47.628 17.127  38.572  1.00 24.32 ? 319 THR C C   1 
ATOM   8159 O O   . THR C 1 319 ? 48.122 18.051  39.213  1.00 20.83 ? 319 THR C O   1 
ATOM   8160 C CB  . THR C 1 319 ? 49.449 16.017  37.230  1.00 25.59 ? 319 THR C CB  1 
ATOM   8161 O OG1 . THR C 1 319 ? 49.790 15.527  35.927  1.00 32.78 ? 319 THR C OG1 1 
ATOM   8162 C CG2 . THR C 1 319 ? 49.313 14.810  38.155  1.00 25.62 ? 319 THR C CG2 1 
ATOM   8163 N N   . GLY C 1 320 ? 46.580 16.461  39.020  1.00 24.49 ? 320 GLY C N   1 
ATOM   8164 C CA  . GLY C 1 320 ? 46.093 16.759  40.347  1.00 25.70 ? 320 GLY C CA  1 
ATOM   8165 C C   . GLY C 1 320 ? 45.714 15.513  41.106  1.00 25.50 ? 320 GLY C C   1 
ATOM   8166 O O   . GLY C 1 320 ? 45.466 14.466  40.500  1.00 22.34 ? 320 GLY C O   1 
ATOM   8167 N N   . PHE C 1 321 ? 45.709 15.607  42.433  1.00 27.11 ? 321 PHE C N   1 
ATOM   8168 C CA  . PHE C 1 321 ? 45.319 14.474  43.253  1.00 21.26 ? 321 PHE C CA  1 
ATOM   8169 C C   . PHE C 1 321 ? 44.048 14.861  43.985  1.00 21.70 ? 321 PHE C C   1 
ATOM   8170 O O   . PHE C 1 321 ? 43.866 16.024  44.357  1.00 26.27 ? 321 PHE C O   1 
ATOM   8171 C CB  . PHE C 1 321 ? 46.420 14.131  44.239  1.00 22.89 ? 321 PHE C CB  1 
ATOM   8172 C CG  . PHE C 1 321 ? 47.787 14.005  43.611  1.00 24.91 ? 321 PHE C CG  1 
ATOM   8173 C CD1 . PHE C 1 321 ? 48.173 12.824  42.981  1.00 24.91 ? 321 PHE C CD1 1 
ATOM   8174 C CD2 . PHE C 1 321 ? 48.681 15.067  43.641  1.00 22.56 ? 321 PHE C CD2 1 
ATOM   8175 C CE1 . PHE C 1 321 ? 49.414 12.708  42.394  1.00 20.88 ? 321 PHE C CE1 1 
ATOM   8176 C CE2 . PHE C 1 321 ? 49.925 14.955  43.057  1.00 18.65 ? 321 PHE C CE2 1 
ATOM   8177 C CZ  . PHE C 1 321 ? 50.289 13.775  42.433  1.00 22.79 ? 321 PHE C CZ  1 
ATOM   8178 N N   . GLY C 1 322 ? 43.126 13.917  44.102  1.00 22.79 ? 322 GLY C N   1 
ATOM   8179 C CA  . GLY C 1 322 ? 41.886 14.167  44.813  1.00 22.63 ? 322 GLY C CA  1 
ATOM   8180 C C   . GLY C 1 322 ? 41.756 13.237  46.017  1.00 21.06 ? 322 GLY C C   1 
ATOM   8181 O O   . GLY C 1 322 ? 41.567 12.033  45.848  1.00 15.79 ? 322 GLY C O   1 
ATOM   8182 N N   . ILE C 1 323 ? 41.881 13.772  47.231  1.00 22.15 ? 323 ILE C N   1 
ATOM   8183 C CA  . ILE C 1 323 ? 41.762 12.939  48.426  1.00 24.37 ? 323 ILE C CA  1 
ATOM   8184 C C   . ILE C 1 323 ? 40.315 12.950  48.918  1.00 24.12 ? 323 ILE C C   1 
ATOM   8185 O O   . ILE C 1 323 ? 39.594 13.937  48.733  1.00 28.46 ? 323 ILE C O   1 
ATOM   8186 C CB  . ILE C 1 323 ? 42.721 13.381  49.585  1.00 25.57 ? 323 ILE C CB  1 
ATOM   8187 C CG1 . ILE C 1 323 ? 42.197 14.634  50.260  1.00 26.49 ? 323 ILE C CG1 1 
ATOM   8188 C CG2 . ILE C 1 323 ? 44.161 13.656  49.074  1.00 22.73 ? 323 ILE C CG2 1 
ATOM   8189 C CD1 . ILE C 1 323 ? 42.750 14.818  51.657  1.00 36.83 ? 323 ILE C CD1 1 
ATOM   8190 N N   . ASN C 1 324 ? 39.899 11.853  49.551  1.00 30.37 ? 324 ASN C N   1 
ATOM   8191 C CA  . ASN C 1 324 ? 38.531 11.684  50.065  1.00 29.95 ? 324 ASN C CA  1 
ATOM   8192 C C   . ASN C 1 324 ? 37.671 11.683  48.830  1.00 29.60 ? 324 ASN C C   1 
ATOM   8193 O O   . ASN C 1 324 ? 36.702 12.443  48.728  1.00 25.29 ? 324 ASN C O   1 
ATOM   8194 C CB  . ASN C 1 324 ? 38.115 12.847  50.966  1.00 35.73 ? 324 ASN C CB  1 
ATOM   8195 C CG  . ASN C 1 324 ? 36.821 12.572  51.699  1.00 41.39 ? 324 ASN C CG  1 
ATOM   8196 O OD1 . ASN C 1 324 ? 36.547 11.429  52.068  1.00 46.60 ? 324 ASN C OD1 1 
ATOM   8197 N ND2 . ASN C 1 324 ? 36.022 13.615  51.931  1.00 40.75 ? 324 ASN C ND2 1 
ATOM   8198 N N   . ALA C 1 325 ? 38.037 10.800  47.902  1.00 26.02 ? 325 ALA C N   1 
ATOM   8199 C CA  . ALA C 1 325 ? 37.375 10.705  46.614  1.00 23.72 ? 325 ALA C CA  1 
ATOM   8200 C C   . ALA C 1 325 ? 36.280 9.656   46.399  1.00 28.90 ? 325 ALA C C   1 
ATOM   8201 O O   . ALA C 1 325 ? 35.479 9.785   45.457  1.00 27.12 ? 325 ALA C O   1 
ATOM   8202 C CB  . ALA C 1 325 ? 38.424 10.580  45.552  1.00 20.48 ? 325 ALA C CB  1 
ATOM   8203 N N   . ASN C 1 326 ? 36.196 8.633   47.246  1.00 29.10 ? 326 ASN C N   1 
ATOM   8204 C CA  . ASN C 1 326 ? 35.166 7.626   46.999  1.00 31.68 ? 326 ASN C CA  1 
ATOM   8205 C C   . ASN C 1 326 ? 33.783 8.251   47.085  1.00 29.62 ? 326 ASN C C   1 
ATOM   8206 O O   . ASN C 1 326 ? 33.504 9.017   48.000  1.00 28.91 ? 326 ASN C O   1 
ATOM   8207 C CB  . ASN C 1 326 ? 35.327 6.383   47.894  1.00 41.79 ? 326 ASN C CB  1 
ATOM   8208 C CG  . ASN C 1 326 ? 36.584 5.516   47.515  1.00 50.15 ? 326 ASN C CG  1 
ATOM   8209 O OD1 . ASN C 1 326 ? 37.312 5.816   46.555  1.00 53.56 ? 326 ASN C OD1 1 
ATOM   8210 N ND2 . ASN C 1 326 ? 36.830 4.453   48.287  1.00 44.71 ? 326 ASN C ND2 1 
ATOM   8211 N N   . ASN C 1 327 ? 33.000 8.043   46.025  1.00 27.29 ? 327 ASN C N   1 
ATOM   8212 C CA  . ASN C 1 327 ? 31.634 8.565   45.882  1.00 29.51 ? 327 ASN C CA  1 
ATOM   8213 C C   . ASN C 1 327 ? 31.506 10.010  45.439  1.00 25.35 ? 327 ASN C C   1 
ATOM   8214 O O   . ASN C 1 327 ? 30.403 10.513  45.304  1.00 25.50 ? 327 ASN C O   1 
ATOM   8215 C CB  . ASN C 1 327 ? 30.821 8.387   47.160  1.00 40.11 ? 327 ASN C CB  1 
ATOM   8216 C CG  . ASN C 1 327 ? 30.064 7.090   47.179  1.00 52.79 ? 327 ASN C CG  1 
ATOM   8217 O OD1 . ASN C 1 327 ? 29.529 6.655   46.149  1.00 59.80 ? 327 ASN C OD1 1 
ATOM   8218 N ND2 . ASN C 1 327 ? 30.009 6.453   48.348  1.00 55.95 ? 327 ASN C ND2 1 
ATOM   8219 N N   . ASN C 1 328 ? 32.619 10.677  45.190  1.00 21.65 ? 328 ASN C N   1 
ATOM   8220 C CA  . ASN C 1 328 ? 32.568 12.073  44.785  1.00 22.03 ? 328 ASN C CA  1 
ATOM   8221 C C   . ASN C 1 328 ? 31.701 12.297  43.564  1.00 22.45 ? 328 ASN C C   1 
ATOM   8222 O O   . ASN C 1 328 ? 31.525 11.388  42.769  1.00 25.52 ? 328 ASN C O   1 
ATOM   8223 C CB  . ASN C 1 328 ? 33.975 12.581  44.502  1.00 15.93 ? 328 ASN C CB  1 
ATOM   8224 C CG  . ASN C 1 328 ? 34.004 14.064  44.181  1.00 20.59 ? 328 ASN C CG  1 
ATOM   8225 O OD1 . ASN C 1 328 ? 33.622 14.899  45.006  1.00 24.52 ? 328 ASN C OD1 1 
ATOM   8226 N ND2 . ASN C 1 328 ? 34.440 14.398  42.973  1.00 2.00  ? 328 ASN C ND2 1 
ATOM   8227 N N   . ASN C 1 329 ? 31.166 13.509  43.427  1.00 24.37 ? 329 ASN C N   1 
ATOM   8228 C CA  . ASN C 1 329 ? 30.348 13.908  42.281  1.00 22.47 ? 329 ASN C CA  1 
ATOM   8229 C C   . ASN C 1 329 ? 30.813 15.281  41.813  1.00 23.54 ? 329 ASN C C   1 
ATOM   8230 O O   . ASN C 1 329 ? 31.172 16.141  42.631  1.00 19.54 ? 329 ASN C O   1 
ATOM   8231 C CB  . ASN C 1 329 ? 28.871 14.027  42.647  1.00 21.73 ? 329 ASN C CB  1 
ATOM   8232 C CG  . ASN C 1 329 ? 28.112 12.718  42.525  1.00 30.07 ? 329 ASN C CG  1 
ATOM   8233 O OD1 . ASN C 1 329 ? 26.891 12.718  42.528  1.00 33.44 ? 329 ASN C OD1 1 
ATOM   8234 N ND2 . ASN C 1 329 ? 28.820 11.602  42.419  1.00 39.01 ? 329 ASN C ND2 1 
ATOM   8235 N N   . ARG C 1 330 ? 30.823 15.451  40.494  1.00 24.90 ? 330 ARG C N   1 
ATOM   8236 C CA  . ARG C 1 330 ? 31.192 16.694  39.810  1.00 25.14 ? 330 ARG C CA  1 
ATOM   8237 C C   . ARG C 1 330 ? 29.950 17.524  39.473  1.00 23.57 ? 330 ARG C C   1 
ATOM   8238 O O   . ARG C 1 330 ? 29.090 17.077  38.711  1.00 23.80 ? 330 ARG C O   1 
ATOM   8239 C CB  . ARG C 1 330 ? 31.908 16.357  38.517  1.00 21.98 ? 330 ARG C CB  1 
ATOM   8240 C CG  . ARG C 1 330 ? 33.289 15.880  38.722  1.00 17.26 ? 330 ARG C CG  1 
ATOM   8241 C CD  . ARG C 1 330 ? 34.014 15.931  37.433  1.00 21.53 ? 330 ARG C CD  1 
ATOM   8242 N NE  . ARG C 1 330 ? 33.555 14.836  36.608  1.00 28.43 ? 330 ARG C NE  1 
ATOM   8243 C CZ  . ARG C 1 330 ? 34.275 13.747  36.377  1.00 32.47 ? 330 ARG C CZ  1 
ATOM   8244 N NH1 . ARG C 1 330 ? 35.505 13.644  36.876  1.00 34.84 ? 330 ARG C NH1 1 
ATOM   8245 N NH2 . ARG C 1 330 ? 33.778 12.777  35.627  1.00 32.03 ? 330 ARG C NH2 1 
ATOM   8246 N N   . ASN C 1 331 ? 29.880 18.744  39.998  1.00 24.89 ? 331 ASN C N   1 
ATOM   8247 C CA  . ASN C 1 331 ? 28.722 19.615  39.770  1.00 20.65 ? 331 ASN C CA  1 
ATOM   8248 C C   . ASN C 1 331 ? 29.054 20.875  38.998  1.00 22.10 ? 331 ASN C C   1 
ATOM   8249 O O   . ASN C 1 331 ? 29.635 21.812  39.566  1.00 20.16 ? 331 ASN C O   1 
ATOM   8250 C CB  . ASN C 1 331 ? 28.105 20.036  41.109  1.00 25.69 ? 331 ASN C CB  1 
ATOM   8251 C CG  . ASN C 1 331 ? 27.464 18.888  41.836  1.00 11.11 ? 331 ASN C CG  1 
ATOM   8252 O OD1 . ASN C 1 331 ? 28.146 17.993  42.326  1.00 21.08 ? 331 ASN C OD1 1 
ATOM   8253 N ND2 . ASN C 1 331 ? 26.151 18.904  41.903  1.00 8.40  ? 331 ASN C ND2 1 
ATOM   8254 N N   . LEU C 1 332 ? 28.652 20.920  37.725  1.00 20.17 ? 332 LEU C N   1 
ATOM   8255 C CA  . LEU C 1 332 ? 28.903 22.075  36.885  1.00 16.50 ? 332 LEU C CA  1 
ATOM   8256 C C   . LEU C 1 332 ? 27.798 23.124  36.973  1.00 18.03 ? 332 LEU C C   1 
ATOM   8257 O O   . LEU C 1 332 ? 26.630 22.793  37.165  1.00 19.90 ? 332 LEU C O   1 
ATOM   8258 C CB  . LEU C 1 332 ? 29.155 21.617  35.450  1.00 19.29 ? 332 LEU C CB  1 
ATOM   8259 C CG  . LEU C 1 332 ? 30.527 20.951  35.348  1.00 13.79 ? 332 LEU C CG  1 
ATOM   8260 C CD1 . LEU C 1 332 ? 30.411 19.498  35.056  1.00 14.31 ? 332 LEU C CD1 1 
ATOM   8261 C CD2 . LEU C 1 332 ? 31.382 21.650  34.315  1.00 14.73 ? 332 LEU C CD2 1 
ATOM   8262 N N   . LEU C 1 333 ? 28.174 24.397  36.854  1.00 20.79 ? 333 LEU C N   1 
ATOM   8263 C CA  . LEU C 1 333 ? 27.214 25.496  36.956  1.00 20.33 ? 333 LEU C CA  1 
ATOM   8264 C C   . LEU C 1 333 ? 26.894 26.168  35.631  1.00 23.38 ? 333 LEU C C   1 
ATOM   8265 O O   . LEU C 1 333 ? 26.226 27.201  35.603  1.00 24.91 ? 333 LEU C O   1 
ATOM   8266 C CB  . LEU C 1 333 ? 27.731 26.520  37.966  1.00 17.76 ? 333 LEU C CB  1 
ATOM   8267 C CG  . LEU C 1 333 ? 28.024 25.878  39.336  1.00 13.10 ? 333 LEU C CG  1 
ATOM   8268 C CD1 . LEU C 1 333 ? 28.845 26.772  40.208  1.00 13.23 ? 333 LEU C CD1 1 
ATOM   8269 C CD2 . LEU C 1 333 ? 26.720 25.556  40.023  1.00 18.77 ? 333 LEU C CD2 1 
ATOM   8270 N N   . ALA C 1 334 ? 27.314 25.522  34.540  1.00 27.62 ? 334 ALA C N   1 
ATOM   8271 C CA  . ALA C 1 334 ? 27.116 25.998  33.176  1.00 21.92 ? 334 ALA C CA  1 
ATOM   8272 C C   . ALA C 1 334 ? 27.431 24.849  32.189  1.00 23.50 ? 334 ALA C C   1 
ATOM   8273 O O   . ALA C 1 334 ? 28.271 23.993  32.480  1.00 28.25 ? 334 ALA C O   1 
ATOM   8274 C CB  . ALA C 1 334 ? 28.022 27.169  32.928  1.00 10.82 ? 334 ALA C CB  1 
ATOM   8275 N N   . GLY C 1 335 ? 26.742 24.810  31.046  1.00 25.50 ? 335 GLY C N   1 
ATOM   8276 C CA  . GLY C 1 335 ? 26.985 23.766  30.051  1.00 18.23 ? 335 GLY C CA  1 
ATOM   8277 C C   . GLY C 1 335 ? 25.873 22.731  29.971  1.00 18.74 ? 335 GLY C C   1 
ATOM   8278 O O   . GLY C 1 335 ? 25.023 22.657  30.857  1.00 22.16 ? 335 GLY C O   1 
ATOM   8279 N N   . LYS C 1 336 ? 25.900 21.903  28.933  1.00 20.81 ? 336 LYS C N   1 
ATOM   8280 C CA  . LYS C 1 336 ? 24.879 20.883  28.717  1.00 21.65 ? 336 LYS C CA  1 
ATOM   8281 C C   . LYS C 1 336 ? 25.014 19.559  29.494  1.00 24.37 ? 336 LYS C C   1 
ATOM   8282 O O   . LYS C 1 336 ? 24.027 18.807  29.630  1.00 24.68 ? 336 LYS C O   1 
ATOM   8283 C CB  . LYS C 1 336 ? 24.739 20.604  27.231  1.00 21.98 ? 336 LYS C CB  1 
ATOM   8284 C CG  . LYS C 1 336 ? 23.488 21.229  26.616  1.00 31.96 ? 336 LYS C CG  1 
ATOM   8285 C CD  . LYS C 1 336 ? 23.638 21.313  25.111  1.00 42.68 ? 336 LYS C CD  1 
ATOM   8286 C CE  . LYS C 1 336 ? 24.138 19.985  24.549  1.00 49.77 ? 336 LYS C CE  1 
ATOM   8287 N NZ  . LYS C 1 336 ? 24.593 20.111  23.138  1.00 57.20 ? 336 LYS C NZ  1 
ATOM   8288 N N   . THR C 1 337 ? 26.217 19.267  29.987  1.00 24.83 ? 337 THR C N   1 
ATOM   8289 C CA  . THR C 1 337 ? 26.456 18.061  30.769  1.00 22.38 ? 337 THR C CA  1 
ATOM   8290 C C   . THR C 1 337 ? 26.668 18.464  32.256  1.00 22.02 ? 337 THR C C   1 
ATOM   8291 O O   . THR C 1 337 ? 27.168 19.553  32.543  1.00 22.25 ? 337 THR C O   1 
ATOM   8292 C CB  . THR C 1 337 ? 27.695 17.321  30.243  1.00 24.26 ? 337 THR C CB  1 
ATOM   8293 O OG1 . THR C 1 337 ? 27.644 17.249  28.812  1.00 26.53 ? 337 THR C OG1 1 
ATOM   8294 C CG2 . THR C 1 337 ? 27.766 15.931  30.819  1.00 17.93 ? 337 THR C CG2 1 
ATOM   8295 N N   . ASP C 1 338 ? 26.249 17.592  33.174  1.00 21.51 ? 338 ASP C N   1 
ATOM   8296 C CA  . ASP C 1 338 ? 26.358 17.776  34.648  1.00 22.76 ? 338 ASP C CA  1 
ATOM   8297 C C   . ASP C 1 338 ? 25.991 19.129  35.271  1.00 22.64 ? 338 ASP C C   1 
ATOM   8298 O O   . ASP C 1 338 ? 26.467 19.446  36.363  1.00 27.35 ? 338 ASP C O   1 
ATOM   8299 C CB  . ASP C 1 338 ? 27.742 17.353  35.169  1.00 19.82 ? 338 ASP C CB  1 
ATOM   8300 C CG  . ASP C 1 338 ? 28.045 15.903  34.917  1.00 15.77 ? 338 ASP C CG  1 
ATOM   8301 O OD1 . ASP C 1 338 ? 27.105 15.097  34.838  1.00 19.44 ? 338 ASP C OD1 1 
ATOM   8302 O OD2 . ASP C 1 338 ? 29.240 15.555  34.783  1.00 9.23  ? 338 ASP C OD2 1 
ATOM   8303 N N   . ASN C 1 339 ? 25.079 19.860  34.632  1.00 23.26 ? 339 ASN C N   1 
ATOM   8304 C CA  . ASN C 1 339 ? 24.641 21.168  35.091  1.00 20.95 ? 339 ASN C CA  1 
ATOM   8305 C C   . ASN C 1 339 ? 23.637 21.065  36.247  1.00 21.80 ? 339 ASN C C   1 
ATOM   8306 O O   . ASN C 1 339 ? 22.472 20.735  36.012  1.00 22.73 ? 339 ASN C O   1 
ATOM   8307 C CB  . ASN C 1 339 ? 24.036 21.940  33.918  1.00 14.99 ? 339 ASN C CB  1 
ATOM   8308 C CG  . ASN C 1 339 ? 23.757 23.407  34.245  1.00 21.14 ? 339 ASN C CG  1 
ATOM   8309 O OD1 . ASN C 1 339 ? 23.281 23.748  35.338  1.00 23.30 ? 339 ASN C OD1 1 
ATOM   8310 N ND2 . ASN C 1 339 ? 24.037 24.277  33.292  1.00 21.79 ? 339 ASN C ND2 1 
ATOM   8311 N N   . VAL C 1 340 ? 24.074 21.360  37.485  1.00 22.59 ? 340 VAL C N   1 
ATOM   8312 C CA  . VAL C 1 340 ? 23.164 21.296  38.642  1.00 21.84 ? 340 VAL C CA  1 
ATOM   8313 C C   . VAL C 1 340 ? 22.022 22.283  38.634  1.00 23.62 ? 340 VAL C C   1 
ATOM   8314 O O   . VAL C 1 340 ? 20.984 22.037  39.249  1.00 24.74 ? 340 VAL C O   1 
ATOM   8315 C CB  . VAL C 1 340 ? 23.818 21.517  40.041  1.00 22.56 ? 340 VAL C CB  1 
ATOM   8316 C CG1 . VAL C 1 340 ? 23.705 20.258  40.868  1.00 24.22 ? 340 VAL C CG1 1 
ATOM   8317 C CG2 . VAL C 1 340 ? 25.227 22.068  39.953  1.00 22.49 ? 340 VAL C CG2 1 
ATOM   8318 N N   . ILE C 1 341 ? 22.220 23.431  38.004  1.00 23.29 ? 341 ILE C N   1 
ATOM   8319 C CA  . ILE C 1 341 ? 21.163 24.426  37.987  1.00 18.68 ? 341 ILE C CA  1 
ATOM   8320 C C   . ILE C 1 341 ? 19.986 24.014  37.139  1.00 17.29 ? 341 ILE C C   1 
ATOM   8321 O O   . ILE C 1 341 ? 18.844 24.171  37.572  1.00 17.59 ? 341 ILE C O   1 
ATOM   8322 C CB  . ILE C 1 341 ? 21.685 25.789  37.627  1.00 21.73 ? 341 ILE C CB  1 
ATOM   8323 C CG1 . ILE C 1 341 ? 22.893 26.104  38.529  1.00 20.02 ? 341 ILE C CG1 1 
ATOM   8324 C CG2 . ILE C 1 341 ? 20.548 26.801  37.743  1.00 20.76 ? 341 ILE C CG2 1 
ATOM   8325 C CD1 . ILE C 1 341 ? 23.614 27.440  38.248  1.00 14.87 ? 341 ILE C CD1 1 
ATOM   8326 N N   . SER C 1 342 ? 20.245 23.405  35.983  1.00 13.23 ? 342 SER C N   1 
ATOM   8327 C CA  . SER C 1 342 ? 19.140 22.919  35.138  1.00 17.16 ? 342 SER C CA  1 
ATOM   8328 C C   . SER C 1 342 ? 18.506 21.723  35.841  1.00 12.70 ? 342 SER C C   1 
ATOM   8329 O O   . SER C 1 342 ? 17.306 21.493  35.748  1.00 12.77 ? 342 SER C O   1 
ATOM   8330 C CB  . SER C 1 342 ? 19.636 22.447  33.765  1.00 10.19 ? 342 SER C CB  1 
ATOM   8331 O OG  . SER C 1 342 ? 20.946 22.928  33.530  1.00 24.89 ? 342 SER C OG  1 
ATOM   8332 N N   . SER C 1 343 ? 19.325 20.955  36.539  1.00 16.17 ? 343 SER C N   1 
ATOM   8333 C CA  . SER C 1 343 ? 18.799 19.811  37.250  1.00 19.39 ? 343 SER C CA  1 
ATOM   8334 C C   . SER C 1 343 ? 17.788 20.249  38.292  1.00 19.52 ? 343 SER C C   1 
ATOM   8335 O O   . SER C 1 343 ? 16.887 19.488  38.578  1.00 23.78 ? 343 SER C O   1 
ATOM   8336 C CB  . SER C 1 343 ? 19.902 18.983  37.879  1.00 22.36 ? 343 SER C CB  1 
ATOM   8337 O OG  . SER C 1 343 ? 19.387 17.716  38.226  1.00 28.32 ? 343 SER C OG  1 
ATOM   8338 N N   . ILE C 1 344 ? 17.899 21.476  38.822  1.00 20.18 ? 344 ILE C N   1 
ATOM   8339 C CA  . ILE C 1 344 ? 16.915 21.989  39.807  1.00 20.92 ? 344 ILE C CA  1 
ATOM   8340 C C   . ILE C 1 344 ? 15.635 22.379  39.063  1.00 20.45 ? 344 ILE C C   1 
ATOM   8341 O O   . ILE C 1 344 ? 14.516 22.136  39.543  1.00 20.72 ? 344 ILE C O   1 
ATOM   8342 C CB  . ILE C 1 344 ? 17.415 23.264  40.581  1.00 23.76 ? 344 ILE C CB  1 
ATOM   8343 C CG1 . ILE C 1 344 ? 18.528 22.927  41.567  1.00 21.09 ? 344 ILE C CG1 1 
ATOM   8344 C CG2 . ILE C 1 344 ? 16.308 23.841  41.461  1.00 20.90 ? 344 ILE C CG2 1 
ATOM   8345 C CD1 . ILE C 1 344 ? 19.107 24.168  42.182  1.00 19.30 ? 344 ILE C CD1 1 
ATOM   8346 N N   . GLY C 1 345 ? 15.821 22.960  37.875  1.00 18.85 ? 345 GLY C N   1 
ATOM   8347 C CA  . GLY C 1 345 ? 14.719 23.404  37.048  1.00 14.08 ? 345 GLY C CA  1 
ATOM   8348 C C   . GLY C 1 345 ? 13.837 22.269  36.619  1.00 17.42 ? 345 GLY C C   1 
ATOM   8349 O O   . GLY C 1 345 ? 12.632 22.439  36.493  1.00 19.84 ? 345 GLY C O   1 
ATOM   8350 N N   . ARG C 1 346 ? 14.418 21.100  36.400  1.00 19.37 ? 346 ARG C N   1 
ATOM   8351 C CA  . ARG C 1 346 ? 13.616 19.946  36.012  1.00 21.85 ? 346 ARG C CA  1 
ATOM   8352 C C   . ARG C 1 346 ? 13.067 19.166  37.223  1.00 22.42 ? 346 ARG C C   1 
ATOM   8353 O O   . ARG C 1 346 ? 12.779 17.982  37.121  1.00 26.53 ? 346 ARG C O   1 
ATOM   8354 C CB  . ARG C 1 346 ? 14.422 19.015  35.107  1.00 23.25 ? 346 ARG C CB  1 
ATOM   8355 C CG  . ARG C 1 346 ? 15.492 19.737  34.313  1.00 26.32 ? 346 ARG C CG  1 
ATOM   8356 C CD  . ARG C 1 346 ? 15.387 19.511  32.844  1.00 33.13 ? 346 ARG C CD  1 
ATOM   8357 N NE  . ARG C 1 346 ? 15.337 18.102  32.500  1.00 39.93 ? 346 ARG C NE  1 
ATOM   8358 C CZ  . ARG C 1 346 ? 14.966 17.648  31.309  1.00 47.47 ? 346 ARG C CZ  1 
ATOM   8359 N NH1 . ARG C 1 346 ? 14.622 18.497  30.351  1.00 55.91 ? 346 ARG C NH1 1 
ATOM   8360 N NH2 . ARG C 1 346 ? 14.900 16.347  31.081  1.00 50.56 ? 346 ARG C NH2 1 
ATOM   8361 N N   . ALA C 1 347 ? 12.939 19.800  38.379  1.00 21.33 ? 347 ALA C N   1 
ATOM   8362 C CA  . ALA C 1 347 ? 12.413 19.081  39.515  1.00 21.08 ? 347 ALA C CA  1 
ATOM   8363 C C   . ALA C 1 347 ? 10.929 19.303  39.478  1.00 29.52 ? 347 ALA C C   1 
ATOM   8364 O O   . ALA C 1 347 ? 10.460 20.263  38.868  1.00 29.05 ? 347 ALA C O   1 
ATOM   8365 C CB  . ALA C 1 347 ? 12.993 19.609  40.804  1.00 23.60 ? 347 ALA C CB  1 
ATOM   8366 N N   . LEU C 1 348 ? 10.203 18.445  40.190  1.00 37.08 ? 348 LEU C N   1 
ATOM   8367 C CA  . LEU C 1 348 ? 8.744  18.478  40.298  1.00 39.68 ? 348 LEU C CA  1 
ATOM   8368 C C   . LEU C 1 348 ? 8.203  19.890  40.424  1.00 42.52 ? 348 LEU C C   1 
ATOM   8369 O O   . LEU C 1 348 ? 7.093  20.168  39.995  1.00 52.32 ? 348 LEU C O   1 
ATOM   8370 C CB  . LEU C 1 348 ? 8.298  17.632  41.501  1.00 38.22 ? 348 LEU C CB  1 
ATOM   8371 C CG  . LEU C 1 348 ? 6.825  17.321  41.778  1.00 36.87 ? 348 LEU C CG  1 
ATOM   8372 C CD1 . LEU C 1 348 ? 6.177  18.461  42.534  1.00 41.69 ? 348 LEU C CD1 1 
ATOM   8373 C CD2 . LEU C 1 348 ? 6.094  17.017  40.486  1.00 34.65 ? 348 LEU C CD2 1 
ATOM   8374 N N   . ASP C 1 349 ? 8.977  20.779  41.022  1.00 41.91 ? 349 ASP C N   1 
ATOM   8375 C CA  . ASP C 1 349 ? 8.560  22.166  41.181  1.00 43.56 ? 349 ASP C CA  1 
ATOM   8376 C C   . ASP C 1 349 ? 9.579  23.137  40.590  1.00 41.12 ? 349 ASP C C   1 
ATOM   8377 O O   . ASP C 1 349 ? 9.276  24.300  40.352  1.00 40.48 ? 349 ASP C O   1 
ATOM   8378 C CB  . ASP C 1 349 ? 8.330  22.479  42.658  1.00 48.78 ? 349 ASP C CB  1 
ATOM   8379 C CG  . ASP C 1 349 ? 9.439  21.931  43.568  1.00 50.67 ? 349 ASP C CG  1 
ATOM   8380 O OD1 . ASP C 1 349 ? 9.931  20.804  43.345  1.00 45.17 ? 349 ASP C OD1 1 
ATOM   8381 O OD2 . ASP C 1 349 ? 9.785  22.621  44.548  1.00 56.47 ? 349 ASP C OD2 1 
ATOM   8382 N N   . GLY C 1 350 ? 10.789 22.630  40.375  1.00 39.89 ? 350 GLY C N   1 
ATOM   8383 C CA  . GLY C 1 350 ? 11.906 23.389  39.831  1.00 33.48 ? 350 GLY C CA  1 
ATOM   8384 C C   . GLY C 1 350 ? 11.771 24.852  39.472  1.00 29.80 ? 350 GLY C C   1 
ATOM   8385 O O   . GLY C 1 350 ? 12.342 25.708  40.137  1.00 29.16 ? 350 GLY C O   1 
ATOM   8386 N N   . LYS C 1 351 ? 11.046 25.128  38.395  1.00 31.14 ? 351 LYS C N   1 
ATOM   8387 C CA  . LYS C 1 351 ? 10.827 26.480  37.885  1.00 28.24 ? 351 LYS C CA  1 
ATOM   8388 C C   . LYS C 1 351 ? 10.379 27.462  38.982  1.00 26.63 ? 351 LYS C C   1 
ATOM   8389 O O   . LYS C 1 351 ? 10.887 28.584  39.074  1.00 29.27 ? 351 LYS C O   1 
ATOM   8390 C CB  . LYS C 1 351 ? 9.793  26.376  36.772  1.00 33.99 ? 351 LYS C CB  1 
ATOM   8391 C CG  . LYS C 1 351 ? 9.672  27.545  35.835  1.00 36.99 ? 351 LYS C CG  1 
ATOM   8392 C CD  . LYS C 1 351 ? 8.730  27.157  34.705  1.00 38.55 ? 351 LYS C CD  1 
ATOM   8393 C CE  . LYS C 1 351 ? 9.473  26.401  33.607  1.00 41.38 ? 351 LYS C CE  1 
ATOM   8394 N NZ  . LYS C 1 351 ? 10.512 25.441  34.096  1.00 48.40 ? 351 LYS C NZ  1 
ATOM   8395 N N   . ASP C 1 352 ? 9.436  27.026  39.814  1.00 28.60 ? 352 ASP C N   1 
ATOM   8396 C CA  . ASP C 1 352 ? 8.934  27.830  40.934  1.00 30.49 ? 352 ASP C CA  1 
ATOM   8397 C C   . ASP C 1 352 ? 10.115 28.146  41.832  1.00 24.89 ? 352 ASP C C   1 
ATOM   8398 O O   . ASP C 1 352 ? 10.372 29.311  42.138  1.00 19.79 ? 352 ASP C O   1 
ATOM   8399 C CB  . ASP C 1 352 ? 7.897  27.046  41.752  1.00 38.24 ? 352 ASP C CB  1 
ATOM   8400 C CG  . ASP C 1 352 ? 6.551  26.929  41.045  1.00 48.82 ? 352 ASP C CG  1 
ATOM   8401 O OD1 . ASP C 1 352 ? 6.434  27.373  39.870  1.00 49.47 ? 352 ASP C OD1 1 
ATOM   8402 O OD2 . ASP C 1 352 ? 5.606  26.384  41.672  1.00 50.45 ? 352 ASP C OD2 1 
ATOM   8403 N N   . VAL C 1 353 ? 10.851 27.098  42.202  1.00 15.77 ? 353 VAL C N   1 
ATOM   8404 C CA  . VAL C 1 353 ? 12.031 27.212  43.050  1.00 17.18 ? 353 VAL C CA  1 
ATOM   8405 C C   . VAL C 1 353 ? 13.117 28.114  42.444  1.00 16.34 ? 353 VAL C C   1 
ATOM   8406 O O   . VAL C 1 353 ? 13.697 28.947  43.140  1.00 22.36 ? 353 VAL C O   1 
ATOM   8407 C CB  . VAL C 1 353 ? 12.564 25.805  43.401  1.00 13.16 ? 353 VAL C CB  1 
ATOM   8408 C CG1 . VAL C 1 353 ? 13.818 25.866  44.166  1.00 4.66  ? 353 VAL C CG1 1 
ATOM   8409 C CG2 . VAL C 1 353 ? 11.578 25.118  44.236  1.00 11.84 ? 353 VAL C CG2 1 
ATOM   8410 N N   . LEU C 1 354 ? 13.365 27.997  41.144  1.00 21.84 ? 354 LEU C N   1 
ATOM   8411 C CA  . LEU C 1 354 ? 14.375 28.829  40.473  1.00 21.10 ? 354 LEU C CA  1 
ATOM   8412 C C   . LEU C 1 354 ? 13.927 30.289  40.389  1.00 20.11 ? 354 LEU C C   1 
ATOM   8413 O O   . LEU C 1 354 ? 14.748 31.194  40.283  1.00 20.68 ? 354 LEU C O   1 
ATOM   8414 C CB  . LEU C 1 354 ? 14.640 28.330  39.048  1.00 23.13 ? 354 LEU C CB  1 
ATOM   8415 C CG  . LEU C 1 354 ? 15.635 27.214  38.735  1.00 21.42 ? 354 LEU C CG  1 
ATOM   8416 C CD1 . LEU C 1 354 ? 15.475 26.770  37.314  1.00 9.88  ? 354 LEU C CD1 1 
ATOM   8417 C CD2 . LEU C 1 354 ? 17.047 27.648  39.026  1.00 17.25 ? 354 LEU C CD2 1 
ATOM   8418 N N   . GLY C 1 355 ? 12.620 30.503  40.375  1.00 20.16 ? 355 GLY C N   1 
ATOM   8419 C CA  . GLY C 1 355 ? 12.098 31.850  40.313  1.00 19.75 ? 355 GLY C CA  1 
ATOM   8420 C C   . GLY C 1 355 ? 12.271 32.660  41.586  1.00 17.17 ? 355 GLY C C   1 
ATOM   8421 O O   . GLY C 1 355 ? 12.285 33.900  41.555  1.00 15.67 ? 355 GLY C O   1 
ATOM   8422 N N   . LEU C 1 356 ? 12.351 31.958  42.711  1.00 14.87 ? 356 LEU C N   1 
ATOM   8423 C CA  . LEU C 1 356 ? 12.520 32.588  44.026  1.00 16.04 ? 356 LEU C CA  1 
ATOM   8424 C C   . LEU C 1 356 ? 13.972 32.686  44.367  1.00 13.36 ? 356 LEU C C   1 
ATOM   8425 O O   . LEU C 1 356 ? 14.363 33.528  45.175  1.00 23.22 ? 356 LEU C O   1 
ATOM   8426 C CB  . LEU C 1 356 ? 11.838 31.780  45.125  1.00 14.36 ? 356 LEU C CB  1 
ATOM   8427 C CG  . LEU C 1 356 ? 10.326 31.796  45.074  1.00 15.73 ? 356 LEU C CG  1 
ATOM   8428 C CD1 . LEU C 1 356 ? 9.758  30.571  45.745  1.00 25.67 ? 356 LEU C CD1 1 
ATOM   8429 C CD2 . LEU C 1 356 ? 9.831  33.027  45.733  1.00 13.04 ? 356 LEU C CD2 1 
ATOM   8430 N N   . THR C 1 357 ? 14.770 31.802  43.782  1.00 12.97 ? 357 THR C N   1 
ATOM   8431 C CA  . THR C 1 357 ? 16.209 31.781  44.011  1.00 14.34 ? 357 THR C CA  1 
ATOM   8432 C C   . THR C 1 357 ? 16.952 32.960  43.379  1.00 19.50 ? 357 THR C C   1 
ATOM   8433 O O   . THR C 1 357 ? 17.817 33.592  44.009  1.00 15.53 ? 357 THR C O   1 
ATOM   8434 C CB  . THR C 1 357 ? 16.808 30.473  43.441  1.00 17.21 ? 357 THR C CB  1 
ATOM   8435 O OG1 . THR C 1 357 ? 16.249 29.363  44.147  1.00 23.39 ? 357 THR C OG1 1 
ATOM   8436 C CG2 . THR C 1 357 ? 18.320 30.442  43.557  1.00 10.28 ? 357 THR C CG2 1 
ATOM   8437 N N   . PHE C 1 358 ? 16.606 33.235  42.126  1.00 19.78 ? 358 PHE C N   1 
ATOM   8438 C CA  . PHE C 1 358 ? 17.250 34.276  41.350  1.00 19.91 ? 358 PHE C CA  1 
ATOM   8439 C C   . PHE C 1 358 ? 16.326 35.443  41.065  1.00 23.37 ? 358 PHE C C   1 
ATOM   8440 O O   . PHE C 1 358 ? 15.114 35.349  41.269  1.00 25.20 ? 358 PHE C O   1 
ATOM   8441 C CB  . PHE C 1 358 ? 17.747 33.668  40.046  1.00 18.71 ? 358 PHE C CB  1 
ATOM   8442 C CG  . PHE C 1 358 ? 18.891 32.678  40.219  1.00 18.09 ? 358 PHE C CG  1 
ATOM   8443 C CD1 . PHE C 1 358 ? 20.107 33.079  40.760  1.00 7.25  ? 358 PHE C CD1 1 
ATOM   8444 C CD2 . PHE C 1 358 ? 18.771 31.363  39.760  1.00 17.33 ? 358 PHE C CD2 1 
ATOM   8445 C CE1 . PHE C 1 358 ? 21.185 32.192  40.830  1.00 8.85  ? 358 PHE C CE1 1 
ATOM   8446 C CE2 . PHE C 1 358 ? 19.849 30.474  39.831  1.00 9.94  ? 358 PHE C CE2 1 
ATOM   8447 C CZ  . PHE C 1 358 ? 21.051 30.894  40.363  1.00 13.83 ? 358 PHE C CZ  1 
ATOM   8448 N N   . SER C 1 359 ? 16.892 36.541  40.567  1.00 27.90 ? 359 SER C N   1 
ATOM   8449 C CA  . SER C 1 359 ? 16.094 37.734  40.277  1.00 29.27 ? 359 SER C CA  1 
ATOM   8450 C C   . SER C 1 359 ? 14.991 37.595  39.203  1.00 28.00 ? 359 SER C C   1 
ATOM   8451 O O   . SER C 1 359 ? 13.861 38.057  39.403  1.00 25.17 ? 359 SER C O   1 
ATOM   8452 C CB  . SER C 1 359 ? 17.006 38.914  39.967  1.00 26.82 ? 359 SER C CB  1 
ATOM   8453 O OG  . SER C 1 359 ? 16.233 40.096  39.961  1.00 39.57 ? 359 SER C OG  1 
ATOM   8454 N N   . GLY C 1 360 ? 15.311 36.924  38.096  1.00 26.43 ? 360 GLY C N   1 
ATOM   8455 C CA  . GLY C 1 360 ? 14.356 36.742  37.019  1.00 21.33 ? 360 GLY C CA  1 
ATOM   8456 C C   . GLY C 1 360 ? 13.287 35.721  37.334  1.00 22.75 ? 360 GLY C C   1 
ATOM   8457 O O   . GLY C 1 360 ? 13.064 35.391  38.494  1.00 27.00 ? 360 GLY C O   1 
ATOM   8458 N N   . SER C 1 361 ? 12.585 35.247  36.311  1.00 19.62 ? 361 SER C N   1 
ATOM   8459 C CA  . SER C 1 361 ? 11.547 34.253  36.527  1.00 20.75 ? 361 SER C CA  1 
ATOM   8460 C C   . SER C 1 361 ? 12.150 32.911  36.174  1.00 20.79 ? 361 SER C C   1 
ATOM   8461 O O   . SER C 1 361 ? 13.210 32.858  35.553  1.00 28.26 ? 361 SER C O   1 
ATOM   8462 C CB  . SER C 1 361 ? 10.316 34.550  35.676  1.00 25.77 ? 361 SER C CB  1 
ATOM   8463 O OG  . SER C 1 361 ? 10.505 34.197  34.310  1.00 35.40 ? 361 SER C OG  1 
ATOM   8464 N N   . GLY C 1 362 ? 11.466 31.833  36.528  1.00 24.81 ? 362 GLY C N   1 
ATOM   8465 C CA  . GLY C 1 362 ? 11.972 30.488  36.275  1.00 25.97 ? 362 GLY C CA  1 
ATOM   8466 C C   . GLY C 1 362 ? 12.173 30.139  34.821  1.00 30.50 ? 362 GLY C C   1 
ATOM   8467 O O   . GLY C 1 362 ? 13.104 29.401  34.481  1.00 30.67 ? 362 GLY C O   1 
ATOM   8468 N N   . ASP C 1 363 ? 11.268 30.625  33.974  1.00 35.28 ? 363 ASP C N   1 
ATOM   8469 C CA  . ASP C 1 363 ? 11.349 30.398  32.529  1.00 38.11 ? 363 ASP C CA  1 
ATOM   8470 C C   . ASP C 1 363 ? 12.556 31.174  31.998  1.00 35.30 ? 363 ASP C C   1 
ATOM   8471 O O   . ASP C 1 363 ? 13.319 30.659  31.182  1.00 34.90 ? 363 ASP C O   1 
ATOM   8472 C CB  . ASP C 1 363 ? 10.077 30.891  31.825  1.00 47.92 ? 363 ASP C CB  1 
ATOM   8473 C CG  . ASP C 1 363 ? 8.840  30.055  32.168  1.00 61.50 ? 363 ASP C CG  1 
ATOM   8474 O OD1 . ASP C 1 363 ? 8.644  28.981  31.546  1.00 65.75 ? 363 ASP C OD1 1 
ATOM   8475 O OD2 . ASP C 1 363 ? 8.050  30.480  33.047  1.00 67.29 ? 363 ASP C OD2 1 
ATOM   8476 N N   . GLU C 1 364 ? 12.733 32.401  32.494  1.00 31.57 ? 364 GLU C N   1 
ATOM   8477 C CA  . GLU C 1 364 ? 13.844 33.266  32.099  1.00 31.42 ? 364 GLU C CA  1 
ATOM   8478 C C   . GLU C 1 364 ? 15.222 32.673  32.395  1.00 31.29 ? 364 GLU C C   1 
ATOM   8479 O O   . GLU C 1 364 ? 16.101 32.667  31.520  1.00 30.88 ? 364 GLU C O   1 
ATOM   8480 C CB  . GLU C 1 364 ? 13.735 34.623  32.783  1.00 30.17 ? 364 GLU C CB  1 
ATOM   8481 C CG  . GLU C 1 364 ? 12.638 35.491  32.255  1.00 39.48 ? 364 GLU C CG  1 
ATOM   8482 C CD  . GLU C 1 364 ? 12.575 36.835  32.955  1.00 49.06 ? 364 GLU C CD  1 
ATOM   8483 O OE1 . GLU C 1 364 ? 11.868 36.949  33.987  1.00 54.78 ? 364 GLU C OE1 1 
ATOM   8484 O OE2 . GLU C 1 364 ? 13.232 37.782  32.469  1.00 55.34 ? 364 GLU C OE2 1 
ATOM   8485 N N   . VAL C 1 365 ? 15.421 32.196  33.626  1.00 29.09 ? 365 VAL C N   1 
ATOM   8486 C CA  . VAL C 1 365 ? 16.707 31.608  33.999  1.00 26.11 ? 365 VAL C CA  1 
ATOM   8487 C C   . VAL C 1 365 ? 16.932 30.337  33.174  1.00 28.21 ? 365 VAL C C   1 
ATOM   8488 O O   . VAL C 1 365 ? 18.016 30.114  32.626  1.00 28.00 ? 365 VAL C O   1 
ATOM   8489 C CB  . VAL C 1 365 ? 16.804 31.276  35.536  1.00 22.50 ? 365 VAL C CB  1 
ATOM   8490 C CG1 . VAL C 1 365 ? 16.018 32.268  36.355  1.00 16.83 ? 365 VAL C CG1 1 
ATOM   8491 C CG2 . VAL C 1 365 ? 16.334 29.894  35.828  1.00 25.36 ? 365 VAL C CG2 1 
ATOM   8492 N N   . MET C 1 366 ? 15.876 29.537  33.056  1.00 29.16 ? 366 MET C N   1 
ATOM   8493 C CA  . MET C 1 366 ? 15.913 28.282  32.334  1.00 29.99 ? 366 MET C CA  1 
ATOM   8494 C C   . MET C 1 366 ? 16.281 28.543  30.848  1.00 28.99 ? 366 MET C C   1 
ATOM   8495 O O   . MET C 1 366 ? 16.969 27.746  30.212  1.00 25.12 ? 366 MET C O   1 
ATOM   8496 C CB  . MET C 1 366 ? 14.559 27.581  32.533  1.00 28.98 ? 366 MET C CB  1 
ATOM   8497 C CG  . MET C 1 366 ? 14.595 26.047  32.597  1.00 35.46 ? 366 MET C CG  1 
ATOM   8498 S SD  . MET C 1 366 ? 15.863 25.291  33.649  1.00 37.40 ? 366 MET C SD  1 
ATOM   8499 C CE  . MET C 1 366 ? 17.055 24.820  32.369  1.00 41.10 ? 366 MET C CE  1 
ATOM   8500 N N   . LYS C 1 367 ? 15.865 29.695  30.332  1.00 30.31 ? 367 LYS C N   1 
ATOM   8501 C CA  . LYS C 1 367 ? 16.184 30.092  28.974  1.00 31.30 ? 367 LYS C CA  1 
ATOM   8502 C C   . LYS C 1 367 ? 17.672 30.329  28.926  1.00 30.13 ? 367 LYS C C   1 
ATOM   8503 O O   . LYS C 1 367 ? 18.349 29.740  28.098  1.00 34.25 ? 367 LYS C O   1 
ATOM   8504 C CB  . LYS C 1 367 ? 15.480 31.397  28.602  1.00 40.46 ? 367 LYS C CB  1 
ATOM   8505 C CG  . LYS C 1 367 ? 14.323 31.240  27.622  1.00 53.03 ? 367 LYS C CG  1 
ATOM   8506 C CD  . LYS C 1 367 ? 13.406 32.460  27.628  1.00 60.45 ? 367 LYS C CD  1 
ATOM   8507 C CE  . LYS C 1 367 ? 14.179 33.753  27.365  1.00 66.59 ? 367 LYS C CE  1 
ATOM   8508 N NZ  . LYS C 1 367 ? 14.802 33.797  26.011  1.00 71.06 ? 367 LYS C NZ  1 
ATOM   8509 N N   . LEU C 1 368 ? 18.185 31.149  29.848  1.00 29.23 ? 368 LEU C N   1 
ATOM   8510 C CA  . LEU C 1 368 ? 19.619 31.490  29.906  1.00 28.48 ? 368 LEU C CA  1 
ATOM   8511 C C   . LEU C 1 368 ? 20.569 30.292  30.012  1.00 29.95 ? 368 LEU C C   1 
ATOM   8512 O O   . LEU C 1 368 ? 21.573 30.223  29.312  1.00 29.78 ? 368 LEU C O   1 
ATOM   8513 C CB  . LEU C 1 368 ? 19.885 32.463  31.055  1.00 26.41 ? 368 LEU C CB  1 
ATOM   8514 C CG  . LEU C 1 368 ? 21.325 32.928  31.273  1.00 27.39 ? 368 LEU C CG  1 
ATOM   8515 C CD1 . LEU C 1 368 ? 21.905 33.510  30.009  1.00 27.30 ? 368 LEU C CD1 1 
ATOM   8516 C CD2 . LEU C 1 368 ? 21.362 33.964  32.365  1.00 27.95 ? 368 LEU C CD2 1 
ATOM   8517 N N   . ILE C 1 369 ? 20.225 29.355  30.889  1.00 33.90 ? 369 ILE C N   1 
ATOM   8518 C CA  . ILE C 1 369 ? 20.986 28.127  31.143  1.00 33.29 ? 369 ILE C CA  1 
ATOM   8519 C C   . ILE C 1 369 ? 21.197 27.265  29.886  1.00 38.51 ? 369 ILE C C   1 
ATOM   8520 O O   . ILE C 1 369 ? 22.125 26.445  29.821  1.00 41.71 ? 369 ILE C O   1 
ATOM   8521 C CB  . ILE C 1 369 ? 20.255 27.280  32.243  1.00 33.63 ? 369 ILE C CB  1 
ATOM   8522 C CG1 . ILE C 1 369 ? 20.532 27.834  33.658  1.00 27.34 ? 369 ILE C CG1 1 
ATOM   8523 C CG2 . ILE C 1 369 ? 20.546 25.802  32.088  1.00 34.68 ? 369 ILE C CG2 1 
ATOM   8524 C CD1 . ILE C 1 369 ? 22.004 27.970  34.037  1.00 18.18 ? 369 ILE C CD1 1 
ATOM   8525 N N   . ASN C 1 370 ? 20.329 27.449  28.896  1.00 39.40 ? 370 ASN C N   1 
ATOM   8526 C CA  . ASN C 1 370 ? 20.416 26.678  27.672  1.00 38.19 ? 370 ASN C CA  1 
ATOM   8527 C C   . ASN C 1 370 ? 21.174 27.354  26.529  1.00 37.04 ? 370 ASN C C   1 
ATOM   8528 O O   . ASN C 1 370 ? 21.329 26.757  25.474  1.00 41.90 ? 370 ASN C O   1 
ATOM   8529 C CB  . ASN C 1 370 ? 19.017 26.260  27.204  1.00 42.74 ? 370 ASN C CB  1 
ATOM   8530 C CG  . ASN C 1 370 ? 18.203 25.594  28.299  1.00 49.51 ? 370 ASN C CG  1 
ATOM   8531 O OD1 . ASN C 1 370 ? 18.745 25.038  29.253  1.00 56.54 ? 370 ASN C OD1 1 
ATOM   8532 N ND2 . ASN C 1 370 ? 16.890 25.652  28.169  1.00 56.24 ? 370 ASN C ND2 1 
ATOM   8533 N N   . LYS C 1 371 ? 21.626 28.592  26.692  1.00 35.40 ? 371 LYS C N   1 
ATOM   8534 C CA  . LYS C 1 371 ? 22.375 29.236  25.615  1.00 31.72 ? 371 LYS C CA  1 
ATOM   8535 C C   . LYS C 1 371 ? 23.711 28.521  25.393  1.00 33.46 ? 371 LYS C C   1 
ATOM   8536 O O   . LYS C 1 371 ? 24.186 28.384  24.260  1.00 36.61 ? 371 LYS C O   1 
ATOM   8537 C CB  . LYS C 1 371 ? 22.646 30.693  25.930  1.00 31.04 ? 371 LYS C CB  1 
ATOM   8538 C CG  . LYS C 1 371 ? 21.474 31.600  25.784  1.00 31.36 ? 371 LYS C CG  1 
ATOM   8539 C CD  . LYS C 1 371 ? 21.987 32.989  25.470  1.00 36.86 ? 371 LYS C CD  1 
ATOM   8540 C CE  . LYS C 1 371 ? 20.865 34.015  25.448  1.00 45.09 ? 371 LYS C CE  1 
ATOM   8541 N NZ  . LYS C 1 371 ? 21.379 35.329  24.960  1.00 53.18 ? 371 LYS C NZ  1 
ATOM   8542 N N   . GLN C 1 372 ? 24.354 28.129  26.483  1.00 34.18 ? 372 GLN C N   1 
ATOM   8543 C CA  . GLN C 1 372 ? 25.622 27.409  26.403  1.00 33.89 ? 372 GLN C CA  1 
ATOM   8544 C C   . GLN C 1 372 ? 25.367 25.972  25.910  1.00 31.76 ? 372 GLN C C   1 
ATOM   8545 O O   . GLN C 1 372 ? 24.698 25.174  26.572  1.00 21.72 ? 372 GLN C O   1 
ATOM   8546 C CB  . GLN C 1 372 ? 26.318 27.409  27.775  1.00 35.91 ? 372 GLN C CB  1 
ATOM   8547 C CG  . GLN C 1 372 ? 27.740 26.880  27.780  1.00 32.36 ? 372 GLN C CG  1 
ATOM   8548 C CD  . GLN C 1 372 ? 28.607 27.571  26.761  1.00 33.41 ? 372 GLN C CD  1 
ATOM   8549 O OE1 . GLN C 1 372 ? 28.977 26.969  25.755  1.00 34.48 ? 372 GLN C OE1 1 
ATOM   8550 N NE2 . GLN C 1 372 ? 28.904 28.850  26.987  1.00 30.93 ? 372 GLN C NE2 1 
ATOM   8551 N N   . SER C 1 373 ? 25.873 25.676  24.715  1.00 34.67 ? 373 SER C N   1 
ATOM   8552 C CA  . SER C 1 373 ? 25.712 24.357  24.101  1.00 34.19 ? 373 SER C CA  1 
ATOM   8553 C C   . SER C 1 373 ? 26.914 23.478  24.375  1.00 29.18 ? 373 SER C C   1 
ATOM   8554 O O   . SER C 1 373 ? 26.867 22.265  24.160  1.00 27.10 ? 373 SER C O   1 
ATOM   8555 C CB  . SER C 1 373 ? 25.508 24.504  22.588  1.00 41.37 ? 373 SER C CB  1 
ATOM   8556 O OG  . SER C 1 373 ? 26.092 25.716  22.120  1.00 50.90 ? 373 SER C OG  1 
ATOM   8557 N N   . GLY C 1 374 ? 28.000 24.110  24.810  1.00 24.91 ? 374 GLY C N   1 
ATOM   8558 C CA  . GLY C 1 374 ? 29.209 23.378  25.125  1.00 22.65 ? 374 GLY C CA  1 
ATOM   8559 C C   . GLY C 1 374 ? 29.041 22.671  26.458  1.00 22.73 ? 374 GLY C C   1 
ATOM   8560 O O   . GLY C 1 374 ? 28.030 22.859  27.135  1.00 16.09 ? 374 GLY C O   1 
ATOM   8561 N N   . SER C 1 375 ? 30.032 21.856  26.807  1.00 23.90 ? 375 SER C N   1 
ATOM   8562 C CA  . SER C 1 375 ? 30.068 21.079  28.043  1.00 25.89 ? 375 SER C CA  1 
ATOM   8563 C C   . SER C 1 375 ? 31.500 21.011  28.613  1.00 27.71 ? 375 SER C C   1 
ATOM   8564 O O   . SER C 1 375 ? 32.450 20.747  27.862  1.00 29.27 ? 375 SER C O   1 
ATOM   8565 C CB  . SER C 1 375 ? 29.529 19.670  27.780  1.00 20.84 ? 375 SER C CB  1 
ATOM   8566 O OG  . SER C 1 375 ? 28.184 19.733  27.308  1.00 21.85 ? 375 SER C OG  1 
ATOM   8567 N N   . TYR C 1 376 ? 31.637 21.295  29.922  1.00 28.31 ? 376 TYR C N   1 
ATOM   8568 C CA  . TYR C 1 376 ? 32.913 21.310  30.669  1.00 19.18 ? 376 TYR C CA  1 
ATOM   8569 C C   . TYR C 1 376 ? 33.887 22.370  30.223  1.00 23.19 ? 376 TYR C C   1 
ATOM   8570 O O   . TYR C 1 376 ? 34.217 23.260  30.992  1.00 24.64 ? 376 TYR C O   1 
ATOM   8571 C CB  . TYR C 1 376 ? 33.639 19.979  30.623  1.00 18.42 ? 376 TYR C CB  1 
ATOM   8572 C CG  . TYR C 1 376 ? 33.134 18.964  31.589  1.00 18.46 ? 376 TYR C CG  1 
ATOM   8573 C CD1 . TYR C 1 376 ? 31.838 18.449  31.478  1.00 23.90 ? 376 TYR C CD1 1 
ATOM   8574 C CD2 . TYR C 1 376 ? 33.943 18.497  32.615  1.00 19.27 ? 376 TYR C CD2 1 
ATOM   8575 C CE1 . TYR C 1 376 ? 31.362 17.485  32.369  1.00 21.95 ? 376 TYR C CE1 1 
ATOM   8576 C CE2 . TYR C 1 376 ? 33.476 17.530  33.509  1.00 24.35 ? 376 TYR C CE2 1 
ATOM   8577 C CZ  . TYR C 1 376 ? 32.188 17.031  33.371  1.00 19.11 ? 376 TYR C CZ  1 
ATOM   8578 O OH  . TYR C 1 376 ? 31.752 16.024  34.192  1.00 31.93 ? 376 TYR C OH  1 
ATOM   8579 N N   . PHE C 1 377 ? 34.420 22.231  29.015  1.00 20.90 ? 377 PHE C N   1 
ATOM   8580 C CA  . PHE C 1 377 ? 35.373 23.200  28.518  1.00 22.83 ? 377 PHE C CA  1 
ATOM   8581 C C   . PHE C 1 377 ? 34.679 24.017  27.440  1.00 26.61 ? 377 PHE C C   1 
ATOM   8582 O O   . PHE C 1 377 ? 34.022 23.492  26.537  1.00 27.38 ? 377 PHE C O   1 
ATOM   8583 C CB  . PHE C 1 377 ? 36.655 22.526  28.037  1.00 24.09 ? 377 PHE C CB  1 
ATOM   8584 C CG  . PHE C 1 377 ? 37.284 21.598  29.050  1.00 23.24 ? 377 PHE C CG  1 
ATOM   8585 C CD1 . PHE C 1 377 ? 38.149 22.086  30.025  1.00 26.11 ? 377 PHE C CD1 1 
ATOM   8586 C CD2 . PHE C 1 377 ? 37.000 20.231  29.029  1.00 27.10 ? 377 PHE C CD2 1 
ATOM   8587 C CE1 . PHE C 1 377 ? 38.723 21.231  30.975  1.00 19.77 ? 377 PHE C CE1 1 
ATOM   8588 C CE2 . PHE C 1 377 ? 37.568 19.369  29.973  1.00 22.41 ? 377 PHE C CE2 1 
ATOM   8589 C CZ  . PHE C 1 377 ? 38.432 19.872  30.950  1.00 20.79 ? 377 PHE C CZ  1 
ATOM   8590 N N   . VAL C 1 378 ? 34.949 25.306  27.489  1.00 30.42 ? 378 VAL C N   1 
ATOM   8591 C CA  . VAL C 1 378 ? 34.290 26.306  26.666  1.00 28.89 ? 378 VAL C CA  1 
ATOM   8592 C C   . VAL C 1 378 ? 35.339 27.252  26.083  1.00 31.64 ? 378 VAL C C   1 
ATOM   8593 O O   . VAL C 1 378 ? 36.451 27.317  26.593  1.00 31.38 ? 378 VAL C O   1 
ATOM   8594 C CB  . VAL C 1 378 ? 33.328 27.029  27.675  1.00 31.42 ? 378 VAL C CB  1 
ATOM   8595 C CG1 . VAL C 1 378 ? 33.470 28.543  27.663  1.00 30.14 ? 378 VAL C CG1 1 
ATOM   8596 C CG2 . VAL C 1 378 ? 31.878 26.490  27.563  1.00 28.38 ? 378 VAL C CG2 1 
ATOM   8597 N N   . ASP C 1 379 ? 35.038 27.919  24.973  1.00 34.44 ? 379 ASP C N   1 
ATOM   8598 C CA  . ASP C 1 379 ? 36.020 28.852  24.427  1.00 36.86 ? 379 ASP C CA  1 
ATOM   8599 C C   . ASP C 1 379 ? 35.850 30.167  25.146  1.00 35.65 ? 379 ASP C C   1 
ATOM   8600 O O   . ASP C 1 379 ? 34.746 30.658  25.264  1.00 32.72 ? 379 ASP C O   1 
ATOM   8601 C CB  . ASP C 1 379 ? 35.820 29.091  22.932  1.00 41.08 ? 379 ASP C CB  1 
ATOM   8602 C CG  . ASP C 1 379 ? 36.844 30.073  22.356  1.00 46.89 ? 379 ASP C CG  1 
ATOM   8603 O OD1 . ASP C 1 379 ? 38.051 29.988  22.709  1.00 48.46 ? 379 ASP C OD1 1 
ATOM   8604 O OD2 . ASP C 1 379 ? 36.435 30.949  21.565  1.00 50.66 ? 379 ASP C OD2 1 
ATOM   8605 N N   . ALA C 1 380 ? 36.937 30.767  25.592  1.00 39.38 ? 380 ALA C N   1 
ATOM   8606 C CA  . ALA C 1 380 ? 36.795 32.034  26.281  1.00 46.99 ? 380 ALA C CA  1 
ATOM   8607 C C   . ALA C 1 380 ? 37.669 33.169  25.753  1.00 52.50 ? 380 ALA C C   1 
ATOM   8608 O O   . ALA C 1 380 ? 37.826 34.187  26.427  1.00 56.57 ? 380 ALA C O   1 
ATOM   8609 C CB  . ALA C 1 380 ? 36.988 31.846  27.782  1.00 46.41 ? 380 ALA C CB  1 
ATOM   8610 N N   . HIS C 1 381 ? 38.211 33.018  24.545  1.00 56.84 ? 381 HIS C N   1 
ATOM   8611 C CA  . HIS C 1 381 ? 39.047 34.062  23.935  1.00 59.97 ? 381 HIS C CA  1 
ATOM   8612 C C   . HIS C 1 381 ? 38.412 35.444  24.034  1.00 58.39 ? 381 HIS C C   1 
ATOM   8613 O O   . HIS C 1 381 ? 37.274 35.633  23.607  1.00 57.55 ? 381 HIS C O   1 
ATOM   8614 C CB  . HIS C 1 381 ? 39.298 33.755  22.460  1.00 63.12 ? 381 HIS C CB  1 
ATOM   8615 C CG  . HIS C 1 381 ? 40.486 32.884  22.215  1.00 66.91 ? 381 HIS C CG  1 
ATOM   8616 N ND1 . HIS C 1 381 ? 41.715 33.393  21.848  1.00 69.33 ? 381 HIS C ND1 1 
ATOM   8617 C CD2 . HIS C 1 381 ? 40.630 31.540  22.258  1.00 70.28 ? 381 HIS C CD2 1 
ATOM   8618 C CE1 . HIS C 1 381 ? 42.566 32.397  21.674  1.00 72.41 ? 381 HIS C CE1 1 
ATOM   8619 N NE2 . HIS C 1 381 ? 41.934 31.263  21.916  1.00 77.15 ? 381 HIS C NE2 1 
HETATM 8620 C C1  . NAG D 2 .   ? 5.882  6.643   76.559  1.00 53.79 ? 900 NAG A C1  1 
HETATM 8621 C C2  . NAG D 2 .   ? 4.566  6.133   77.279  1.00 59.01 ? 900 NAG A C2  1 
HETATM 8622 C C3  . NAG D 2 .   ? 3.663  7.217   77.755  1.00 58.22 ? 900 NAG A C3  1 
HETATM 8623 C C4  . NAG D 2 .   ? 4.512  8.194   78.556  1.00 55.15 ? 900 NAG A C4  1 
HETATM 8624 C C5  . NAG D 2 .   ? 5.556  8.794   77.766  1.00 53.82 ? 900 NAG A C5  1 
HETATM 8625 C C6  . NAG D 2 .   ? 6.287  9.823   78.634  1.00 56.18 ? 900 NAG A C6  1 
HETATM 8626 C C7  . NAG D 2 .   ? 3.931  4.323   75.704  1.00 62.21 ? 900 NAG A C7  1 
HETATM 8627 C C8  . NAG D 2 .   ? 2.804  3.523   75.103  1.00 60.37 ? 900 NAG A C8  1 
HETATM 8628 N N2  . NAG D 2 .   ? 3.601  5.255   76.590  1.00 62.86 ? 900 NAG A N2  1 
HETATM 8629 O O3  . NAG D 2 .   ? 2.606  6.605   78.518  1.00 53.74 ? 900 NAG A O3  1 
HETATM 8630 O O4  . NAG D 2 .   ? 3.710  9.276   78.982  1.00 67.88 ? 900 NAG A O4  1 
HETATM 8631 O O5  . NAG D 2 .   ? 6.424  7.745   77.339  1.00 55.21 ? 900 NAG A O5  1 
HETATM 8632 O O6  . NAG D 2 .   ? 6.474  9.417   79.989  1.00 57.27 ? 900 NAG A O6  1 
HETATM 8633 O O7  . NAG D 2 .   ? 5.094  4.093   75.381  1.00 64.00 ? 900 NAG A O7  1 
HETATM 8634 P P   . PO4 E 3 .   ? 13.950 26.684  68.385  1.00 45.14 ? 950 PO4 A P   1 
HETATM 8635 O O1  . PO4 E 3 .   ? 15.135 27.433  67.878  1.00 38.33 ? 950 PO4 A O1  1 
HETATM 8636 O O2  . PO4 E 3 .   ? 13.468 25.753  67.307  1.00 40.49 ? 950 PO4 A O2  1 
HETATM 8637 O O3  . PO4 E 3 .   ? 14.377 25.904  69.579  1.00 45.05 ? 950 PO4 A O3  1 
HETATM 8638 O O4  . PO4 E 3 .   ? 12.932 27.726  68.748  1.00 39.35 ? 950 PO4 A O4  1 
HETATM 8639 C C1  . NAG F 2 .   ? 64.476 -20.608 71.146  1.00 71.36 ? 901 NAG B C1  1 
HETATM 8640 C C2  . NAG F 2 .   ? 64.254 -21.914 70.340  1.00 74.72 ? 901 NAG B C2  1 
HETATM 8641 C C3  . NAG F 2 .   ? 64.595 -23.125 71.137  1.00 75.52 ? 901 NAG B C3  1 
HETATM 8642 C C4  . NAG F 2 .   ? 66.063 -23.007 71.561  1.00 76.49 ? 901 NAG B C4  1 
HETATM 8643 C C5  . NAG F 2 .   ? 66.196 -21.753 72.490  1.00 78.25 ? 901 NAG B C5  1 
HETATM 8644 C C6  . NAG F 2 .   ? 67.628 -21.475 72.939  1.00 83.69 ? 901 NAG B C6  1 
HETATM 8645 C C7  . NAG F 2 .   ? 61.814 -22.353 70.670  1.00 89.95 ? 901 NAG B C7  1 
HETATM 8646 C C8  . NAG F 2 .   ? 60.415 -22.485 70.057  1.00 88.29 ? 901 NAG B C8  1 
HETATM 8647 N N2  . NAG F 2 .   ? 62.869 -22.073 69.901  1.00 84.47 ? 901 NAG B N2  1 
HETATM 8648 O O3  . NAG F 2 .   ? 64.321 -24.266 70.361  1.00 75.84 ? 901 NAG B O3  1 
HETATM 8649 O O4  . NAG F 2 .   ? 66.432 -24.228 72.249  1.00 77.01 ? 901 NAG B O4  1 
HETATM 8650 O O5  . NAG F 2 .   ? 65.756 -20.561 71.818  1.00 73.20 ? 901 NAG B O5  1 
HETATM 8651 O O6  . NAG F 2 .   ? 68.460 -21.214 71.829  1.00 90.73 ? 901 NAG B O6  1 
HETATM 8652 O O7  . NAG F 2 .   ? 61.896 -22.508 71.892  1.00 94.40 ? 901 NAG B O7  1 
HETATM 8653 P P   . PO4 G 3 .   ? 56.941 -5.481  87.291  1.00 39.79 ? 951 PO4 B P   1 
HETATM 8654 O O1  . PO4 G 3 .   ? 56.217 -4.447  88.090  1.00 43.05 ? 951 PO4 B O1  1 
HETATM 8655 O O2  . PO4 G 3 .   ? 56.021 -6.602  87.134  1.00 41.50 ? 951 PO4 B O2  1 
HETATM 8656 O O3  . PO4 G 3 .   ? 57.448 -5.053  85.963  1.00 33.28 ? 951 PO4 B O3  1 
HETATM 8657 O O4  . PO4 G 3 .   ? 58.039 -5.900  88.190  1.00 43.49 ? 951 PO4 B O4  1 
HETATM 8658 C C1  . NAG H 2 .   ? 41.195 16.289  23.556  1.00 55.73 ? 902 NAG C C1  1 
HETATM 8659 C C2  . NAG H 2 .   ? 40.537 15.955  22.203  1.00 63.31 ? 902 NAG C C2  1 
HETATM 8660 C C3  . NAG H 2 .   ? 41.621 16.490  21.211  1.00 64.05 ? 902 NAG C C3  1 
HETATM 8661 C C4  . NAG H 2 .   ? 41.889 18.006  21.564  1.00 63.35 ? 902 NAG C C4  1 
HETATM 8662 C C5  . NAG H 2 .   ? 42.643 17.994  22.966  1.00 59.29 ? 902 NAG C C5  1 
HETATM 8663 C C6  . NAG H 2 .   ? 43.446 19.155  23.606  1.00 53.77 ? 902 NAG C C6  1 
HETATM 8664 C C7  . NAG H 2 .   ? 40.916 13.605  21.836  1.00 73.73 ? 902 NAG C C7  1 
HETATM 8665 C C8  . NAG H 2 .   ? 40.432 12.218  21.421  1.00 78.95 ? 902 NAG C C8  1 
HETATM 8666 N N2  . NAG H 2 .   ? 40.070 14.629  21.827  1.00 67.56 ? 902 NAG C N2  1 
HETATM 8667 O O3  . NAG H 2 .   ? 41.315 16.309  19.847  1.00 68.06 ? 902 NAG C O3  1 
HETATM 8668 O O4  . NAG H 2 .   ? 42.615 18.653  20.508  1.00 68.06 ? 902 NAG C O4  1 
HETATM 8669 O O5  . NAG H 2 .   ? 41.639 17.595  23.854  1.00 57.98 ? 902 NAG C O5  1 
HETATM 8670 O O6  . NAG H 2 .   ? 42.634 20.286  23.818  1.00 49.42 ? 902 NAG C O6  1 
HETATM 8671 O O7  . NAG H 2 .   ? 42.092 13.719  22.181  1.00 78.98 ? 902 NAG C O7  1 
HETATM 8672 P P   . PO4 I 3 .   ? 60.877 19.857  37.008  1.00 57.63 ? 952 PO4 C P   1 
HETATM 8673 O O1  . PO4 I 3 .   ? 59.734 19.032  37.482  1.00 65.75 ? 952 PO4 C O1  1 
HETATM 8674 O O2  . PO4 I 3 .   ? 60.878 19.983  35.558  1.00 60.71 ? 952 PO4 C O2  1 
HETATM 8675 O O3  . PO4 I 3 .   ? 60.963 21.209  37.593  1.00 62.91 ? 952 PO4 C O3  1 
HETATM 8676 O O4  . PO4 I 3 .   ? 62.091 19.179  37.520  1.00 65.34 ? 952 PO4 C O4  1 
HETATM 8677 O O   . HOH J 4 .   ? 11.763 14.311  39.367  1.00 14.35 ? 500 HOH A O   1 
HETATM 8678 O O   . HOH J 4 .   ? 37.449 13.796  80.977  1.00 15.97 ? 502 HOH A O   1 
HETATM 8679 O O   . HOH J 4 .   ? 25.563 18.289  52.811  1.00 16.49 ? 505 HOH A O   1 
HETATM 8680 O O   . HOH J 4 .   ? 11.222 26.131  55.761  1.00 22.78 ? 513 HOH A O   1 
HETATM 8681 O O   . HOH J 4 .   ? 22.611 41.150  47.438  1.00 46.79 ? 515 HOH A O   1 
HETATM 8682 O O   . HOH J 4 .   ? 33.598 20.843  67.395  1.00 16.65 ? 520 HOH A O   1 
HETATM 8683 O O   . HOH J 4 .   ? 21.615 8.813   77.814  1.00 18.85 ? 521 HOH A O   1 
HETATM 8684 O O   . HOH J 4 .   ? 27.590 7.725   76.584  1.00 28.64 ? 525 HOH A O   1 
HETATM 8685 O O   . HOH J 4 .   ? 19.355 23.585  57.304  1.00 33.37 ? 529 HOH A O   1 
HETATM 8686 O O   . HOH J 4 .   ? 41.895 20.792  54.069  1.00 29.46 ? 530 HOH A O   1 
HETATM 8687 O O   . HOH J 4 .   ? 35.082 21.752  56.184  1.00 33.04 ? 531 HOH A O   1 
HETATM 8688 O O   . HOH J 4 .   ? 31.335 -4.301  71.448  1.00 39.95 ? 533 HOH A O   1 
HETATM 8689 O O   . HOH J 4 .   ? 8.946  -0.691  83.363  1.00 54.17 ? 541 HOH A O   1 
HETATM 8690 O O   . HOH J 4 .   ? 15.840 36.039  45.222  1.00 21.34 ? 542 HOH A O   1 
HETATM 8691 O O   . HOH J 4 .   ? 28.339 28.571  57.226  1.00 44.15 ? 544 HOH A O   1 
HETATM 8692 O O   . HOH J 4 .   ? 29.405 22.114  67.660  1.00 16.13 ? 547 HOH A O   1 
HETATM 8693 O O   . HOH J 4 .   ? 9.940  8.826   72.455  1.00 27.92 ? 548 HOH A O   1 
HETATM 8694 O O   . HOH J 4 .   ? 22.901 23.632  56.993  1.00 40.30 ? 549 HOH A O   1 
HETATM 8695 O O   . HOH J 4 .   ? 24.145 18.239  43.719  1.00 17.08 ? 552 HOH A O   1 
HETATM 8696 O O   . HOH J 4 .   ? 8.453  39.362  52.105  1.00 49.24 ? 553 HOH A O   1 
HETATM 8697 O O   . HOH J 4 .   ? 37.282 28.702  57.165  1.00 57.86 ? 554 HOH A O   1 
HETATM 8698 O O   . HOH J 4 .   ? 33.777 -3.092  70.489  1.00 33.98 ? 564 HOH A O   1 
HETATM 8699 O O   . HOH J 4 .   ? 16.470 -1.158  84.411  1.00 32.29 ? 566 HOH A O   1 
HETATM 8700 O O   . HOH J 4 .   ? 17.803 -2.046  91.866  1.00 41.02 ? 568 HOH A O   1 
HETATM 8701 O O   . HOH K 4 .   ? 50.593 15.281  78.820  1.00 35.01 ? 506 HOH B O   1 
HETATM 8702 O O   . HOH K 4 .   ? 62.004 -0.552  61.845  1.00 21.93 ? 507 HOH B O   1 
HETATM 8703 O O   . HOH K 4 .   ? 62.638 -4.624  65.717  1.00 30.90 ? 508 HOH B O   1 
HETATM 8704 O O   . HOH K 4 .   ? 61.727 11.211  63.547  1.00 20.98 ? 509 HOH B O   1 
HETATM 8705 O O   . HOH K 4 .   ? 29.322 -4.656  80.874  1.00 20.78 ? 510 HOH B O   1 
HETATM 8706 O O   . HOH K 4 .   ? 66.433 -6.154  84.609  1.00 41.58 ? 514 HOH B O   1 
HETATM 8707 O O   . HOH K 4 .   ? 67.466 10.819  56.626  1.00 41.04 ? 516 HOH B O   1 
HETATM 8708 O O   . HOH K 4 .   ? 51.744 5.860   77.282  1.00 17.47 ? 517 HOH B O   1 
HETATM 8709 O O   . HOH K 4 .   ? 66.647 -12.626 51.285  1.00 30.60 ? 518 HOH B O   1 
HETATM 8710 O O   . HOH K 4 .   ? 50.253 8.609   74.090  1.00 21.39 ? 523 HOH B O   1 
HETATM 8711 O O   . HOH K 4 .   ? 61.717 -2.820  64.015  1.00 23.26 ? 524 HOH B O   1 
HETATM 8712 O O   . HOH K 4 .   ? 43.163 -0.698  82.534  1.00 56.55 ? 526 HOH B O   1 
HETATM 8713 O O   . HOH K 4 .   ? 69.135 -13.014 58.498  1.00 22.33 ? 535 HOH B O   1 
HETATM 8714 O O   . HOH K 4 .   ? 36.320 -1.813  80.659  1.00 27.83 ? 538 HOH B O   1 
HETATM 8715 O O   . HOH K 4 .   ? 43.136 6.123   85.318  1.00 32.80 ? 539 HOH B O   1 
HETATM 8716 O O   . HOH K 4 .   ? 27.673 -17.669 83.912  1.00 31.96 ? 543 HOH B O   1 
HETATM 8717 O O   . HOH K 4 .   ? 33.490 -15.263 90.048  1.00 25.83 ? 546 HOH B O   1 
HETATM 8718 O O   . HOH K 4 .   ? 34.331 4.028   100.452 1.00 35.27 ? 551 HOH B O   1 
HETATM 8719 O O   . HOH K 4 .   ? 59.065 -10.752 55.295  1.00 33.33 ? 556 HOH B O   1 
HETATM 8720 O O   . HOH K 4 .   ? 61.434 -6.694  66.665  1.00 38.75 ? 558 HOH B O   1 
HETATM 8721 O O   . HOH K 4 .   ? 75.037 -10.935 55.524  1.00 43.82 ? 559 HOH B O   1 
HETATM 8722 O O   . HOH K 4 .   ? 70.367 -19.654 62.120  1.00 48.14 ? 560 HOH B O   1 
HETATM 8723 O O   . HOH K 4 .   ? 10.308 4.252   95.826  1.00 43.36 ? 562 HOH B O   1 
HETATM 8724 O O   . HOH K 4 .   ? 44.072 -3.446  84.256  1.00 79.72 ? 565 HOH B O   1 
HETATM 8725 O O   . HOH L 4 .   ? 38.463 27.717  54.142  1.00 5.37  ? 501 HOH C O   1 
HETATM 8726 O O   . HOH L 4 .   ? 61.400 14.371  61.980  1.00 48.17 ? 503 HOH C O   1 
HETATM 8727 O O   . HOH L 4 .   ? 55.214 8.255   65.917  1.00 17.55 ? 504 HOH C O   1 
HETATM 8728 O O   . HOH L 4 .   ? 39.670 20.628  39.233  1.00 17.51 ? 511 HOH C O   1 
HETATM 8729 O O   . HOH L 4 .   ? 37.554 20.225  45.435  1.00 14.08 ? 512 HOH C O   1 
HETATM 8730 O O   . HOH L 4 .   ? 66.408 7.345   36.471  1.00 51.74 ? 519 HOH C O   1 
HETATM 8731 O O   . HOH L 4 .   ? 57.132 -8.742  36.704  1.00 33.53 ? 522 HOH C O   1 
HETATM 8732 O O   . HOH L 4 .   ? 61.705 9.734   44.117  1.00 30.00 ? 527 HOH C O   1 
HETATM 8733 O O   . HOH L 4 .   ? 61.903 -3.835  50.866  1.00 17.51 ? 528 HOH C O   1 
HETATM 8734 O O   . HOH L 4 .   ? 90.573 6.912   52.528  1.00 39.78 ? 532 HOH C O   1 
HETATM 8735 O O   . HOH L 4 .   ? 64.989 5.570   44.600  1.00 19.60 ? 534 HOH C O   1 
HETATM 8736 O O   . HOH L 4 .   ? 81.123 7.041   51.816  1.00 28.68 ? 536 HOH C O   1 
HETATM 8737 O O   . HOH L 4 .   ? 57.369 4.080   49.728  1.00 19.02 ? 537 HOH C O   1 
HETATM 8738 O O   . HOH L 4 .   ? 37.750 20.905  40.867  1.00 36.58 ? 540 HOH C O   1 
HETATM 8739 O O   . HOH L 4 .   ? 68.438 -3.795  37.654  1.00 30.79 ? 545 HOH C O   1 
HETATM 8740 O O   . HOH L 4 .   ? 80.926 2.454   62.627  1.00 39.30 ? 550 HOH C O   1 
HETATM 8741 O O   . HOH L 4 .   ? 59.401 15.647  63.159  1.00 41.93 ? 555 HOH C O   1 
HETATM 8742 O O   . HOH L 4 .   ? 60.617 9.530   47.787  1.00 51.89 ? 557 HOH C O   1 
HETATM 8743 O O   . HOH L 4 .   ? 59.609 2.795   50.544  1.00 21.62 ? 561 HOH C O   1 
HETATM 8744 O O   . HOH L 4 .   ? 79.813 5.294   62.417  1.00 65.56 ? 563 HOH C O   1 
HETATM 8745 O O   . HOH L 4 .   ? 53.619 18.905  51.172  1.00 22.73 ? 567 HOH C O   1 
HETATM 8746 O O   . HOH L 4 .   ? 24.242 29.125  29.316  1.00 29.62 ? 569 HOH C O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   THR 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LEU 3   3   ?   ?   ?   A . n 
A 1 4   ARG 4   4   ?   ?   ?   A . n 
A 1 5   GLU 5   5   ?   ?   ?   A . n 
A 1 6   GLU 6   6   ?   ?   ?   A . n 
A 1 7   GLU 7   7   ?   ?   ?   A . n 
A 1 8   GLU 8   8   ?   ?   ?   A . n 
A 1 9   SER 9   9   ?   ?   ?   A . n 
A 1 10  GLN 10  10  ?   ?   ?   A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  ASN 12  12  12  ASN ASN A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  PHE 14  14  14  PHE PHE A . n 
A 1 15  TYR 15  15  15  TYR TYR A . n 
A 1 16  PHE 16  16  16  PHE PHE A . n 
A 1 17  ASN 17  17  17  ASN ASN A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  TRP 22  22  22  TRP TRP A . n 
A 1 23  ASN 23  23  23  ASN ASN A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  LYS 27  27  27  LYS LYS A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  TYR 30  30  30  TYR TYR A . n 
A 1 31  GLY 31  31  31  GLY GLY A . n 
A 1 32  HIS 32  32  32  HIS HIS A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ARG 34  34  34  ARG ARG A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  LEU 36  36  36  LEU LEU A . n 
A 1 37  GLN 37  37  37  GLN GLN A . n 
A 1 38  ARG 38  38  38  ARG ARG A . n 
A 1 39  PHE 39  39  39  PHE PHE A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  GLN 41  41  41  GLN GLN A . n 
A 1 42  GLN 42  42  42  GLN GLN A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLN 47  47  47  GLN GLN A . n 
A 1 48  ASN 48  48  48  ASN ASN A . n 
A 1 49  LEU 49  49  49  LEU LEU A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  ASP 51  51  51  ASP ASP A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  GLU 56  56  56  GLU GLU A . n 
A 1 57  PHE 57  57  57  PHE PHE A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  PRO 61  61  61  PRO PRO A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  THR 63  63  63  THR THR A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  PRO 67  67  67  PRO PRO A . n 
A 1 68  GLN 68  68  68  GLN GLN A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ALA 72  72  72  ALA ALA A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  SER 82  82  82  SER SER A . n 
A 1 83  ALA 83  83  83  ALA ALA A . n 
A 1 84  ILE 84  84  84  ILE ILE A . n 
A 1 85  LEU 85  85  85  LEU LEU A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  ASP 91  91  91  ASP ASP A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  ARG 94  94  94  ARG ARG A . n 
A 1 95  GLU 95  95  95  GLU GLU A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  PHE 97  97  97  PHE PHE A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  LEU 99  99  99  LEU LEU A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 PRO 104 104 104 PRO PRO A . n 
A 1 105 ILE 105 105 105 ILE ILE A . n 
A 1 106 PHE 106 106 106 PHE PHE A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 HIS 109 109 109 HIS HIS A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLY 115 115 115 GLY GLY A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 ILE 117 117 117 ILE ILE A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 TYR 119 119 119 TYR TYR A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 PRO 123 123 123 PRO PRO A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 ARG 130 130 130 ARG ARG A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 ILE 132 132 132 ILE ILE A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 ALA 135 135 135 ALA ALA A . n 
A 1 136 MET 136 136 136 MET MET A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ASN 140 140 140 ASN ASN A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 GLN 142 142 142 GLN GLN A . n 
A 1 143 ILE 143 143 143 ILE ILE A . n 
A 1 144 HIS 144 144 144 HIS HIS A . n 
A 1 145 GLU 145 145 145 GLU GLU A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 PHE 147 147 147 PHE PHE A . n 
A 1 148 LEU 148 148 148 LEU LEU A . n 
A 1 149 SER 149 149 149 SER SER A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 THR 151 151 151 THR THR A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 ALA 153 153 153 ALA ALA A . n 
A 1 154 GLN 154 154 154 GLN GLN A . n 
A 1 155 GLN 155 155 155 GLN GLN A . n 
A 1 156 SER 156 156 156 SER SER A . n 
A 1 157 TYR 157 157 157 TYR TYR A . n 
A 1 158 LEU 158 158 158 LEU LEU A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 GLU 160 160 160 GLU GLU A . n 
A 1 161 PHE 161 161 161 PHE PHE A . n 
A 1 162 SER 162 162 162 SER SER A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 ILE 165 165 165 ILE ILE A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 GLU 167 167 167 GLU GLU A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 PHE 170 170 170 PHE PHE A . n 
A 1 171 ASN 171 171 171 ASN ASN A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 LYS 173 173 173 LYS LYS A . n 
A 1 174 PHE 174 174 174 PHE PHE A . n 
A 1 175 GLU 175 175 175 GLU GLU A . n 
A 1 176 GLU 176 176 176 GLU GLU A . n 
A 1 177 ILE 177 177 177 ILE ILE A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ARG 179 179 179 ARG ARG A . n 
A 1 180 VAL 180 180 180 VAL VAL A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 PHE 182 182 182 PHE PHE A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 GLU 184 184 184 GLU GLU A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 GLN 187 187 187 GLN GLN A . n 
A 1 188 GLN 188 188 188 GLN GLN A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 GLY 190 190 190 GLY GLY A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 VAL 193 193 193 VAL VAL A . n 
A 1 194 ASN 194 194 194 ASN ASN A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 ASP 196 196 196 ASP ASP A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 GLU 198 198 198 GLU GLU A . n 
A 1 199 GLN 199 199 199 GLN GLN A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 GLU 202 202 202 GLU GLU A . n 
A 1 203 LEU 203 203 203 LEU LEU 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 HIS 206 206 206 HIS HIS A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 LYS 208 208 208 LYS LYS A . n 
A 1 209 SER 209 209 209 SER SER A . n 
A 1 210 SER 210 210 210 SER SER A . n 
A 1 211 SER 211 211 ?   ?   ?   A . n 
A 1 212 ARG 212 212 ?   ?   ?   A . n 
A 1 213 LYS 213 213 ?   ?   ?   A . n 
A 1 214 SER 214 214 ?   ?   ?   A . n 
A 1 215 LEU 215 215 ?   ?   ?   A . n 
A 1 216 SER 216 216 ?   ?   ?   A . n 
A 1 217 LYS 217 217 ?   ?   ?   A . n 
A 1 218 GLN 218 218 ?   ?   ?   A . n 
A 1 219 ASP 219 219 ?   ?   ?   A . n 
A 1 220 ASN 220 220 220 ASN ASN A . n 
A 1 221 THR 221 221 221 THR THR A . n 
A 1 222 ILE 222 222 222 ILE ILE A . n 
A 1 223 GLY 223 223 223 GLY GLY A . n 
A 1 224 ASN 224 224 224 ASN ASN A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 PHE 226 226 226 PHE PHE A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 THR 230 230 230 THR THR A . n 
A 1 231 GLU 231 231 231 GLU GLU A . n 
A 1 232 ARG 232 232 232 ARG ARG A . n 
A 1 233 THR 233 233 233 THR THR A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 SER 242 242 242 SER SER A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 ILE 244 244 244 ILE ILE A . n 
A 1 245 GLU 245 245 245 GLU GLU A . n 
A 1 246 MET 246 246 246 MET MET A . n 
A 1 247 GLU 247 247 247 GLU GLU A . n 
A 1 248 GLU 248 248 248 GLU GLU A . n 
A 1 249 GLY 249 249 249 GLY GLY A . n 
A 1 250 ALA 250 250 250 ALA ALA A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 VAL 253 253 253 VAL VAL A . n 
A 1 254 PRO 254 254 254 PRO PRO A . n 
A 1 255 HIS 255 255 255 HIS HIS A . n 
A 1 256 TYR 256 256 256 TYR TYR A . n 
A 1 257 TYR 257 257 257 TYR TYR A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 LYS 259 259 259 LYS LYS A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 VAL 262 262 262 VAL VAL A . n 
A 1 263 ILE 263 263 263 ILE ILE A . n 
A 1 264 LEU 264 264 264 LEU LEU A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 VAL 266 266 266 VAL VAL A . n 
A 1 267 ASN 267 267 267 ASN ASN A . n 
A 1 268 GLU 268 268 268 GLU GLU A . n 
A 1 269 GLY 269 269 269 GLY GLY A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 HIS 272 272 272 HIS HIS A . n 
A 1 273 VAL 273 273 273 VAL VAL A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 GLY 277 277 277 GLY GLY A . n 
A 1 278 PRO 278 278 278 PRO PRO A . n 
A 1 279 LYS 279 279 279 LYS LYS A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 ASN 281 281 ?   ?   ?   A . n 
A 1 282 LYS 282 282 ?   ?   ?   A . n 
A 1 283 GLU 283 283 283 GLU GLU A . n 
A 1 284 THR 284 284 284 THR THR A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 GLU 286 286 286 GLU GLU A . n 
A 1 287 TYR 287 287 287 TYR TYR A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 SER 289 289 289 SER SER A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 ARG 291 291 291 ARG ARG A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 GLU 293 293 293 GLU GLU A . n 
A 1 294 LEU 294 294 294 LEU LEU A . n 
A 1 295 SER 295 295 295 SER SER A . n 
A 1 296 LYS 296 296 296 LYS LYS A . n 
A 1 297 ASP 297 297 297 ASP ASP A . n 
A 1 298 ASP 298 298 298 ASP ASP A . n 
A 1 299 VAL 299 299 299 VAL VAL A . n 
A 1 300 PHE 300 300 300 PHE PHE A . n 
A 1 301 VAL 301 301 301 VAL VAL A . n 
A 1 302 ILE 302 302 302 ILE ILE A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 ALA 304 304 304 ALA ALA A . n 
A 1 305 ALA 305 305 305 ALA ALA A . n 
A 1 306 TYR 306 306 306 TYR TYR A . n 
A 1 307 PRO 307 307 307 PRO PRO A . n 
A 1 308 VAL 308 308 308 VAL VAL A . n 
A 1 309 ALA 309 309 309 ALA ALA A . n 
A 1 310 ILE 310 310 310 ILE ILE A . n 
A 1 311 LYS 311 311 311 LYS LYS A . n 
A 1 312 ALA 312 312 312 ALA ALA A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 SER 314 314 314 SER SER A . n 
A 1 315 ASN 315 315 315 ASN ASN A . n 
A 1 316 VAL 316 316 316 VAL VAL A . n 
A 1 317 ASN 317 317 317 ASN ASN A . n 
A 1 318 PHE 318 318 318 PHE PHE A . n 
A 1 319 THR 319 319 319 THR THR A . n 
A 1 320 GLY 320 320 320 GLY GLY A . n 
A 1 321 PHE 321 321 321 PHE PHE A . n 
A 1 322 GLY 322 322 322 GLY GLY A . n 
A 1 323 ILE 323 323 323 ILE ILE A . n 
A 1 324 ASN 324 324 324 ASN ASN A . n 
A 1 325 ALA 325 325 325 ALA ALA A . n 
A 1 326 ASN 326 326 326 ASN ASN A . n 
A 1 327 ASN 327 327 327 ASN ASN A . n 
A 1 328 ASN 328 328 328 ASN ASN A . n 
A 1 329 ASN 329 329 329 ASN ASN A . n 
A 1 330 ARG 330 330 330 ARG ARG A . n 
A 1 331 ASN 331 331 331 ASN ASN A . n 
A 1 332 LEU 332 332 332 LEU LEU A . n 
A 1 333 LEU 333 333 333 LEU LEU A . n 
A 1 334 ALA 334 334 334 ALA ALA A . n 
A 1 335 GLY 335 335 335 GLY GLY A . n 
A 1 336 LYS 336 336 336 LYS LYS A . n 
A 1 337 THR 337 337 337 THR THR A . n 
A 1 338 ASP 338 338 338 ASP ASP A . n 
A 1 339 ASN 339 339 339 ASN ASN A . n 
A 1 340 VAL 340 340 340 VAL VAL A . n 
A 1 341 ILE 341 341 341 ILE ILE A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 SER 343 343 343 SER SER A . n 
A 1 344 ILE 344 344 344 ILE ILE A . n 
A 1 345 GLY 345 345 345 GLY GLY A . n 
A 1 346 ARG 346 346 346 ARG ARG A . n 
A 1 347 ALA 347 347 347 ALA ALA A . n 
A 1 348 LEU 348 348 348 LEU LEU A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 GLY 350 350 350 GLY GLY A . n 
A 1 351 LYS 351 351 351 LYS LYS A . n 
A 1 352 ASP 352 352 352 ASP ASP A . n 
A 1 353 VAL 353 353 353 VAL VAL A . n 
A 1 354 LEU 354 354 354 LEU LEU A . n 
A 1 355 GLY 355 355 355 GLY GLY A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 THR 357 357 357 THR THR A . n 
A 1 358 PHE 358 358 358 PHE PHE A . n 
A 1 359 SER 359 359 359 SER SER A . n 
A 1 360 GLY 360 360 360 GLY GLY A . n 
A 1 361 SER 361 361 361 SER SER A . n 
A 1 362 GLY 362 362 362 GLY GLY A . n 
A 1 363 ASP 363 363 363 ASP ASP A . n 
A 1 364 GLU 364 364 364 GLU GLU A . n 
A 1 365 VAL 365 365 365 VAL VAL A . n 
A 1 366 MET 366 366 366 MET MET A . n 
A 1 367 LYS 367 367 367 LYS LYS A . n 
A 1 368 LEU 368 368 368 LEU LEU A . n 
A 1 369 ILE 369 369 369 ILE ILE A . n 
A 1 370 ASN 370 370 370 ASN ASN A . n 
A 1 371 LYS 371 371 371 LYS LYS A . n 
A 1 372 GLN 372 372 372 GLN GLN A . n 
A 1 373 SER 373 373 373 SER SER A . n 
A 1 374 GLY 374 374 374 GLY GLY A . n 
A 1 375 SER 375 375 375 SER SER A . n 
A 1 376 TYR 376 376 376 TYR TYR A . n 
A 1 377 PHE 377 377 377 PHE PHE A . n 
A 1 378 VAL 378 378 378 VAL VAL A . n 
A 1 379 ASP 379 379 379 ASP ASP A . n 
A 1 380 ALA 380 380 380 ALA ALA A . n 
A 1 381 HIS 381 381 381 HIS HIS A . n 
A 1 382 HIS 382 382 ?   ?   ?   A . n 
A 1 383 HIS 383 383 ?   ?   ?   A . n 
A 1 384 GLN 384 384 ?   ?   ?   A . n 
A 1 385 GLN 385 385 ?   ?   ?   A . n 
A 1 386 GLU 386 386 ?   ?   ?   A . n 
A 1 387 GLN 387 387 ?   ?   ?   A . n 
A 1 388 GLN 388 388 ?   ?   ?   A . n 
A 1 389 LYS 389 389 ?   ?   ?   A . n 
A 1 390 GLY 390 390 ?   ?   ?   A . n 
A 1 391 ARG 391 391 ?   ?   ?   A . n 
A 1 392 LYS 392 392 ?   ?   ?   A . n 
A 1 393 GLY 393 393 ?   ?   ?   A . n 
A 1 394 ALA 394 394 ?   ?   ?   A . n 
A 1 395 PHE 395 395 ?   ?   ?   A . n 
A 1 396 VAL 396 396 ?   ?   ?   A . n 
A 1 397 TYR 397 397 ?   ?   ?   A . n 
B 1 1   THR 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LEU 3   3   ?   ?   ?   B . n 
B 1 4   ARG 4   4   ?   ?   ?   B . n 
B 1 5   GLU 5   5   ?   ?   ?   B . n 
B 1 6   GLU 6   6   ?   ?   ?   B . n 
B 1 7   GLU 7   7   ?   ?   ?   B . n 
B 1 8   GLU 8   8   ?   ?   ?   B . n 
B 1 9   SER 9   9   ?   ?   ?   B . n 
B 1 10  GLN 10  10  ?   ?   ?   B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  ASN 12  12  12  ASN ASN B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  PHE 14  14  14  PHE PHE B . n 
B 1 15  TYR 15  15  15  TYR TYR B . n 
B 1 16  PHE 16  16  16  PHE PHE B . n 
B 1 17  ASN 17  17  17  ASN ASN B . n 
B 1 18  SER 18  18  18  SER SER B . n 
B 1 19  ASP 19  19  19  ASP ASP B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  TRP 22  22  22  TRP TRP B . n 
B 1 23  ASN 23  23  23  ASN ASN B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  LYS 27  27  27  LYS LYS B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  GLN 29  29  29  GLN GLN B . n 
B 1 30  TYR 30  30  30  TYR TYR B . n 
B 1 31  GLY 31  31  31  GLY GLY B . n 
B 1 32  HIS 32  32  32  HIS HIS B . n 
B 1 33  ILE 33  33  33  ILE ILE B . n 
B 1 34  ARG 34  34  34  ARG ARG B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  LEU 36  36  36  LEU LEU B . n 
B 1 37  GLN 37  37  37  GLN GLN B . n 
B 1 38  ARG 38  38  38  ARG ARG B . n 
B 1 39  PHE 39  39  39  PHE PHE B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  GLN 41  41  41  GLN GLN B . n 
B 1 42  GLN 42  42  42  GLN GLN B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  ARG 45  45  45  ARG ARG B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  GLN 47  47  47  GLN GLN B . n 
B 1 48  ASN 48  48  48  ASN ASN B . n 
B 1 49  LEU 49  49  49  LEU LEU B . n 
B 1 50  GLU 50  50  50  GLU GLU B . n 
B 1 51  ASP 51  51  51  ASP ASP B . n 
B 1 52  TYR 52  52  52  TYR TYR B . n 
B 1 53  ARG 53  53  53  ARG ARG B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  GLU 56  56  56  GLU GLU B . n 
B 1 57  PHE 57  57  57  PHE PHE B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  LYS 60  60  60  LYS LYS B . n 
B 1 61  PRO 61  61  61  PRO PRO B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  THR 63  63  63  THR THR B . n 
B 1 64  LEU 64  64  64  LEU LEU B . n 
B 1 65  LEU 65  65  65  LEU LEU B . n 
B 1 66  LEU 66  66  66  LEU LEU B . n 
B 1 67  PRO 67  67  67  PRO PRO B . n 
B 1 68  GLN 68  68  68  GLN GLN B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  ALA 72  72  72  ALA ALA B . n 
B 1 73  GLU 73  73  73  GLU GLU B . n 
B 1 74  LEU 74  74  74  LEU LEU B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  VAL 78  78  78  VAL VAL B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  SER 82  82  82  SER SER B . n 
B 1 83  ALA 83  83  83  ALA ALA B . n 
B 1 84  ILE 84  84  84  ILE ILE B . n 
B 1 85  LEU 85  85  85  LEU LEU B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  LYS 89  89  89  LYS LYS B . n 
B 1 90  PRO 90  90  90  PRO PRO B . n 
B 1 91  ASP 91  91  91  ASP ASP B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  ARG 93  93  93  ARG ARG B . n 
B 1 94  ARG 94  94  94  ARG ARG B . n 
B 1 95  GLU 95  95  95  GLU GLU B . n 
B 1 96  TYR 96  96  96  TYR TYR B . n 
B 1 97  PHE 97  97  97  PHE PHE B . n 
B 1 98  PHE 98  98  98  PHE PHE B . n 
B 1 99  LEU 99  99  99  LEU LEU B . n 
B 1 100 THR 100 100 100 THR THR B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 ASN 103 103 103 ASN ASN B . n 
B 1 104 PRO 104 104 104 PRO PRO B . n 
B 1 105 ILE 105 105 105 ILE ILE B . n 
B 1 106 PHE 106 106 106 PHE PHE B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 ASP 108 108 108 ASP ASP B . n 
B 1 109 HIS 109 109 109 HIS HIS B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLY 115 115 115 GLY GLY B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 ILE 117 117 117 ILE ILE B . n 
B 1 118 PHE 118 118 118 PHE PHE B . n 
B 1 119 TYR 119 119 119 TYR TYR B . n 
B 1 120 LEU 120 120 120 LEU LEU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 ASN 122 122 122 ASN ASN B . n 
B 1 123 PRO 123 123 123 PRO PRO B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LYS 126 126 126 LYS LYS B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 ARG 130 130 130 ARG ARG B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 ILE 132 132 132 ILE ILE B . n 
B 1 133 GLN 133 133 133 GLN GLN B . n 
B 1 134 LEU 134 134 134 LEU LEU B . n 
B 1 135 ALA 135 135 135 ALA ALA B . n 
B 1 136 MET 136 136 136 MET MET B . n 
B 1 137 PRO 137 137 137 PRO PRO B . n 
B 1 138 VAL 138 138 138 VAL VAL B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ASN 140 140 140 ASN ASN B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 GLN 142 142 142 GLN GLN B . n 
B 1 143 ILE 143 143 143 ILE ILE B . n 
B 1 144 HIS 144 144 144 HIS HIS B . n 
B 1 145 GLU 145 145 145 GLU GLU B . n 
B 1 146 PHE 146 146 146 PHE PHE B . n 
B 1 147 PHE 147 147 147 PHE PHE B . n 
B 1 148 LEU 148 148 148 LEU LEU B . n 
B 1 149 SER 149 149 149 SER SER B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 THR 151 151 151 THR THR B . n 
B 1 152 GLU 152 152 152 GLU GLU B . n 
B 1 153 ALA 153 153 153 ALA ALA B . n 
B 1 154 GLN 154 154 154 GLN GLN B . n 
B 1 155 GLN 155 155 155 GLN GLN B . n 
B 1 156 SER 156 156 156 SER SER B . n 
B 1 157 TYR 157 157 157 TYR TYR B . n 
B 1 158 LEU 158 158 158 LEU LEU B . n 
B 1 159 GLN 159 159 159 GLN GLN B . n 
B 1 160 GLU 160 160 160 GLU GLU B . n 
B 1 161 PHE 161 161 161 PHE PHE B . n 
B 1 162 SER 162 162 162 SER SER B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 ILE 165 165 165 ILE ILE B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 GLU 167 167 167 GLU GLU B . n 
B 1 168 ALA 168 168 168 ALA ALA B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 PHE 170 170 170 PHE PHE B . n 
B 1 171 ASN 171 171 171 ASN ASN B . n 
B 1 172 SER 172 172 172 SER SER B . n 
B 1 173 LYS 173 173 173 LYS LYS B . n 
B 1 174 PHE 174 174 174 PHE PHE B . n 
B 1 175 GLU 175 175 175 GLU GLU B . n 
B 1 176 GLU 176 176 176 GLU GLU B . n 
B 1 177 ILE 177 177 177 ILE ILE B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ARG 179 179 179 ARG ARG B . n 
B 1 180 VAL 180 180 180 VAL VAL B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 PHE 182 182 182 PHE PHE B . n 
B 1 183 GLU 183 183 183 GLU GLU B . n 
B 1 184 GLU 184 184 184 GLU GLU B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 GLY 186 186 186 GLY GLY B . n 
B 1 187 GLN 187 187 187 GLN GLN B . n 
B 1 188 GLN 188 188 188 GLN GLN B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 GLY 190 190 190 GLY GLY B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 VAL 193 193 193 VAL VAL B . n 
B 1 194 ASN 194 194 194 ASN ASN B . n 
B 1 195 ILE 195 195 195 ILE ILE B . n 
B 1 196 ASP 196 196 196 ASP ASP B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 GLU 198 198 198 GLU GLU B . n 
B 1 199 GLN 199 199 199 GLN GLN B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 LYS 201 201 201 LYS LYS B . n 
B 1 202 GLU 202 202 202 GLU GLU B . n 
B 1 203 LEU 203 203 203 LEU LEU 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 HIS 206 206 206 HIS HIS B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 LYS 208 208 208 LYS LYS B . n 
B 1 209 SER 209 209 209 SER SER B . n 
B 1 210 SER 210 210 210 SER SER B . n 
B 1 211 SER 211 211 ?   ?   ?   B . n 
B 1 212 ARG 212 212 ?   ?   ?   B . n 
B 1 213 LYS 213 213 ?   ?   ?   B . n 
B 1 214 SER 214 214 ?   ?   ?   B . n 
B 1 215 LEU 215 215 ?   ?   ?   B . n 
B 1 216 SER 216 216 ?   ?   ?   B . n 
B 1 217 LYS 217 217 ?   ?   ?   B . n 
B 1 218 GLN 218 218 ?   ?   ?   B . n 
B 1 219 ASP 219 219 ?   ?   ?   B . n 
B 1 220 ASN 220 220 220 ASN ASN B . n 
B 1 221 THR 221 221 221 THR THR B . n 
B 1 222 ILE 222 222 222 ILE ILE B . n 
B 1 223 GLY 223 223 223 GLY GLY B . n 
B 1 224 ASN 224 224 224 ASN ASN B . n 
B 1 225 GLU 225 225 225 GLU GLU B . n 
B 1 226 PHE 226 226 226 PHE PHE B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 ASN 228 228 228 ASN ASN B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 THR 230 230 230 THR THR B . n 
B 1 231 GLU 231 231 231 GLU GLU B . n 
B 1 232 ARG 232 232 232 ARG ARG B . n 
B 1 233 THR 233 233 233 THR THR B . n 
B 1 234 ASP 234 234 234 ASP ASP B . n 
B 1 235 ASN 235 235 235 ASN ASN B . n 
B 1 236 SER 236 236 236 SER SER B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 VAL 239 239 239 VAL VAL B . n 
B 1 240 LEU 240 240 240 LEU LEU B . n 
B 1 241 ILE 241 241 241 ILE ILE B . n 
B 1 242 SER 242 242 242 SER SER B . n 
B 1 243 SER 243 243 243 SER SER B . n 
B 1 244 ILE 244 244 244 ILE ILE B . n 
B 1 245 GLU 245 245 245 GLU GLU B . n 
B 1 246 MET 246 246 246 MET MET B . n 
B 1 247 GLU 247 247 247 GLU GLU B . n 
B 1 248 GLU 248 248 248 GLU GLU B . n 
B 1 249 GLY 249 249 249 GLY GLY B . n 
B 1 250 ALA 250 250 250 ALA ALA B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 VAL 253 253 253 VAL VAL B . n 
B 1 254 PRO 254 254 254 PRO PRO B . n 
B 1 255 HIS 255 255 255 HIS HIS B . n 
B 1 256 TYR 256 256 256 TYR TYR B . n 
B 1 257 TYR 257 257 257 TYR TYR B . n 
B 1 258 SER 258 258 258 SER SER B . n 
B 1 259 LYS 259 259 259 LYS LYS B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 VAL 262 262 262 VAL VAL B . n 
B 1 263 ILE 263 263 263 ILE ILE B . n 
B 1 264 LEU 264 264 264 LEU LEU B . n 
B 1 265 VAL 265 265 265 VAL VAL B . n 
B 1 266 VAL 266 266 266 VAL VAL B . n 
B 1 267 ASN 267 267 267 ASN ASN B . n 
B 1 268 GLU 268 268 268 GLU GLU B . n 
B 1 269 GLY 269 269 269 GLY GLY B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 ALA 271 271 271 ALA ALA B . n 
B 1 272 HIS 272 272 272 HIS HIS B . n 
B 1 273 VAL 273 273 273 VAL VAL B . n 
B 1 274 GLU 274 274 274 GLU GLU B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 VAL 276 276 276 VAL VAL B . n 
B 1 277 GLY 277 277 277 GLY GLY B . n 
B 1 278 PRO 278 278 278 PRO PRO B . n 
B 1 279 LYS 279 279 279 LYS LYS B . n 
B 1 280 GLY 280 280 280 GLY GLY B . n 
B 1 281 ASN 281 281 ?   ?   ?   B . n 
B 1 282 LYS 282 282 ?   ?   ?   B . n 
B 1 283 GLU 283 283 283 GLU GLU B . n 
B 1 284 THR 284 284 284 THR THR B . n 
B 1 285 LEU 285 285 285 LEU LEU B . n 
B 1 286 GLU 286 286 286 GLU GLU B . n 
B 1 287 TYR 287 287 287 TYR TYR B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 SER 289 289 289 SER SER B . n 
B 1 290 TYR 290 290 290 TYR TYR B . n 
B 1 291 ARG 291 291 291 ARG ARG B . n 
B 1 292 ALA 292 292 292 ALA ALA B . n 
B 1 293 GLU 293 293 293 GLU GLU B . n 
B 1 294 LEU 294 294 294 LEU LEU B . n 
B 1 295 SER 295 295 295 SER SER B . n 
B 1 296 LYS 296 296 296 LYS LYS B . n 
B 1 297 ASP 297 297 297 ASP ASP B . n 
B 1 298 ASP 298 298 298 ASP ASP B . n 
B 1 299 VAL 299 299 299 VAL VAL B . n 
B 1 300 PHE 300 300 300 PHE PHE B . n 
B 1 301 VAL 301 301 301 VAL VAL B . n 
B 1 302 ILE 302 302 302 ILE ILE B . n 
B 1 303 PRO 303 303 303 PRO PRO B . n 
B 1 304 ALA 304 304 304 ALA ALA B . n 
B 1 305 ALA 305 305 305 ALA ALA B . n 
B 1 306 TYR 306 306 306 TYR TYR B . n 
B 1 307 PRO 307 307 307 PRO PRO B . n 
B 1 308 VAL 308 308 308 VAL VAL B . n 
B 1 309 ALA 309 309 309 ALA ALA B . n 
B 1 310 ILE 310 310 310 ILE ILE B . n 
B 1 311 LYS 311 311 311 LYS LYS B . n 
B 1 312 ALA 312 312 312 ALA ALA B . n 
B 1 313 THR 313 313 313 THR THR B . n 
B 1 314 SER 314 314 314 SER SER B . n 
B 1 315 ASN 315 315 315 ASN ASN B . n 
B 1 316 VAL 316 316 316 VAL VAL B . n 
B 1 317 ASN 317 317 317 ASN ASN B . n 
B 1 318 PHE 318 318 318 PHE PHE B . n 
B 1 319 THR 319 319 319 THR THR B . n 
B 1 320 GLY 320 320 320 GLY GLY B . n 
B 1 321 PHE 321 321 321 PHE PHE B . n 
B 1 322 GLY 322 322 322 GLY GLY B . n 
B 1 323 ILE 323 323 323 ILE ILE B . n 
B 1 324 ASN 324 324 324 ASN ASN B . n 
B 1 325 ALA 325 325 325 ALA ALA B . n 
B 1 326 ASN 326 326 326 ASN ASN B . n 
B 1 327 ASN 327 327 327 ASN ASN B . n 
B 1 328 ASN 328 328 328 ASN ASN B . n 
B 1 329 ASN 329 329 329 ASN ASN B . n 
B 1 330 ARG 330 330 330 ARG ARG B . n 
B 1 331 ASN 331 331 331 ASN ASN B . n 
B 1 332 LEU 332 332 332 LEU LEU B . n 
B 1 333 LEU 333 333 333 LEU LEU B . n 
B 1 334 ALA 334 334 334 ALA ALA B . n 
B 1 335 GLY 335 335 335 GLY GLY B . n 
B 1 336 LYS 336 336 336 LYS LYS B . n 
B 1 337 THR 337 337 337 THR THR B . n 
B 1 338 ASP 338 338 338 ASP ASP B . n 
B 1 339 ASN 339 339 339 ASN ASN B . n 
B 1 340 VAL 340 340 340 VAL VAL B . n 
B 1 341 ILE 341 341 341 ILE ILE B . n 
B 1 342 SER 342 342 342 SER SER B . n 
B 1 343 SER 343 343 343 SER SER B . n 
B 1 344 ILE 344 344 344 ILE ILE B . n 
B 1 345 GLY 345 345 345 GLY GLY B . n 
B 1 346 ARG 346 346 346 ARG ARG B . n 
B 1 347 ALA 347 347 347 ALA ALA B . n 
B 1 348 LEU 348 348 348 LEU LEU B . n 
B 1 349 ASP 349 349 349 ASP ASP B . n 
B 1 350 GLY 350 350 350 GLY GLY B . n 
B 1 351 LYS 351 351 351 LYS LYS B . n 
B 1 352 ASP 352 352 352 ASP ASP B . n 
B 1 353 VAL 353 353 353 VAL VAL B . n 
B 1 354 LEU 354 354 354 LEU LEU B . n 
B 1 355 GLY 355 355 355 GLY GLY B . n 
B 1 356 LEU 356 356 356 LEU LEU B . n 
B 1 357 THR 357 357 357 THR THR B . n 
B 1 358 PHE 358 358 358 PHE PHE B . n 
B 1 359 SER 359 359 359 SER SER B . n 
B 1 360 GLY 360 360 360 GLY GLY B . n 
B 1 361 SER 361 361 361 SER SER B . n 
B 1 362 GLY 362 362 362 GLY GLY B . n 
B 1 363 ASP 363 363 363 ASP ASP B . n 
B 1 364 GLU 364 364 364 GLU GLU B . n 
B 1 365 VAL 365 365 365 VAL VAL B . n 
B 1 366 MET 366 366 366 MET MET B . n 
B 1 367 LYS 367 367 367 LYS LYS B . n 
B 1 368 LEU 368 368 368 LEU LEU B . n 
B 1 369 ILE 369 369 369 ILE ILE B . n 
B 1 370 ASN 370 370 370 ASN ASN B . n 
B 1 371 LYS 371 371 371 LYS LYS B . n 
B 1 372 GLN 372 372 372 GLN GLN B . n 
B 1 373 SER 373 373 373 SER SER B . n 
B 1 374 GLY 374 374 374 GLY GLY B . n 
B 1 375 SER 375 375 375 SER SER B . n 
B 1 376 TYR 376 376 376 TYR TYR B . n 
B 1 377 PHE 377 377 377 PHE PHE B . n 
B 1 378 VAL 378 378 378 VAL VAL B . n 
B 1 379 ASP 379 379 379 ASP ASP B . n 
B 1 380 ALA 380 380 380 ALA ALA B . n 
B 1 381 HIS 381 381 381 HIS HIS B . n 
B 1 382 HIS 382 382 ?   ?   ?   B . n 
B 1 383 HIS 383 383 ?   ?   ?   B . n 
B 1 384 GLN 384 384 ?   ?   ?   B . n 
B 1 385 GLN 385 385 ?   ?   ?   B . n 
B 1 386 GLU 386 386 ?   ?   ?   B . n 
B 1 387 GLN 387 387 ?   ?   ?   B . n 
B 1 388 GLN 388 388 ?   ?   ?   B . n 
B 1 389 LYS 389 389 ?   ?   ?   B . n 
B 1 390 GLY 390 390 ?   ?   ?   B . n 
B 1 391 ARG 391 391 ?   ?   ?   B . n 
B 1 392 LYS 392 392 ?   ?   ?   B . n 
B 1 393 GLY 393 393 ?   ?   ?   B . n 
B 1 394 ALA 394 394 ?   ?   ?   B . n 
B 1 395 PHE 395 395 ?   ?   ?   B . n 
B 1 396 VAL 396 396 ?   ?   ?   B . n 
B 1 397 TYR 397 397 ?   ?   ?   B . n 
C 1 1   THR 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   LEU 3   3   ?   ?   ?   C . n 
C 1 4   ARG 4   4   ?   ?   ?   C . n 
C 1 5   GLU 5   5   ?   ?   ?   C . n 
C 1 6   GLU 6   6   ?   ?   ?   C . n 
C 1 7   GLU 7   7   ?   ?   ?   C . n 
C 1 8   GLU 8   8   ?   ?   ?   C . n 
C 1 9   SER 9   9   ?   ?   ?   C . n 
C 1 10  GLN 10  10  10  GLN GLN C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  ASN 12  12  12  ASN ASN C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  PHE 14  14  14  PHE PHE C . n 
C 1 15  TYR 15  15  15  TYR TYR C . n 
C 1 16  PHE 16  16  16  PHE PHE C . n 
C 1 17  ASN 17  17  17  ASN ASN C . n 
C 1 18  SER 18  18  18  SER SER C . n 
C 1 19  ASP 19  19  19  ASP ASP C . n 
C 1 20  ASN 20  20  20  ASN ASN C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  TRP 22  22  22  TRP TRP C . n 
C 1 23  ASN 23  23  23  ASN ASN C . n 
C 1 24  THR 24  24  24  THR THR C . n 
C 1 25  LEU 25  25  25  LEU LEU C . n 
C 1 26  PHE 26  26  26  PHE PHE C . n 
C 1 27  LYS 27  27  27  LYS LYS C . n 
C 1 28  ASN 28  28  28  ASN ASN C . n 
C 1 29  GLN 29  29  29  GLN GLN C . n 
C 1 30  TYR 30  30  30  TYR TYR C . n 
C 1 31  GLY 31  31  31  GLY GLY C . n 
C 1 32  HIS 32  32  32  HIS HIS C . n 
C 1 33  ILE 33  33  33  ILE ILE C . n 
C 1 34  ARG 34  34  34  ARG ARG C . n 
C 1 35  VAL 35  35  35  VAL VAL C . n 
C 1 36  LEU 36  36  36  LEU LEU C . n 
C 1 37  GLN 37  37  37  GLN GLN C . n 
C 1 38  ARG 38  38  38  ARG ARG C . n 
C 1 39  PHE 39  39  39  PHE PHE C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  GLN 41  41  41  GLN GLN C . n 
C 1 42  GLN 42  42  42  GLN GLN C . n 
C 1 43  SER 43  43  43  SER SER C . n 
C 1 44  LYS 44  44  44  LYS LYS C . n 
C 1 45  ARG 45  45  45  ARG ARG C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLN 47  47  47  GLN GLN C . n 
C 1 48  ASN 48  48  48  ASN ASN C . n 
C 1 49  LEU 49  49  49  LEU LEU C . n 
C 1 50  GLU 50  50  50  GLU GLU C . n 
C 1 51  ASP 51  51  51  ASP ASP C . n 
C 1 52  TYR 52  52  52  TYR TYR C . n 
C 1 53  ARG 53  53  53  ARG ARG C . n 
C 1 54  LEU 54  54  54  LEU LEU C . n 
C 1 55  VAL 55  55  55  VAL VAL C . n 
C 1 56  GLU 56  56  56  GLU GLU C . n 
C 1 57  PHE 57  57  57  PHE PHE C . n 
C 1 58  ARG 58  58  58  ARG ARG C . n 
C 1 59  SER 59  59  59  SER SER C . n 
C 1 60  LYS 60  60  60  LYS LYS C . n 
C 1 61  PRO 61  61  61  PRO PRO C . n 
C 1 62  GLU 62  62  62  GLU GLU C . n 
C 1 63  THR 63  63  63  THR THR C . n 
C 1 64  LEU 64  64  64  LEU LEU C . n 
C 1 65  LEU 65  65  65  LEU LEU C . n 
C 1 66  LEU 66  66  66  LEU LEU C . n 
C 1 67  PRO 67  67  67  PRO PRO C . n 
C 1 68  GLN 68  68  68  GLN GLN C . n 
C 1 69  GLN 69  69  69  GLN GLN C . n 
C 1 70  ALA 70  70  70  ALA ALA C . n 
C 1 71  ASP 71  71  71  ASP ASP C . n 
C 1 72  ALA 72  72  72  ALA ALA C . n 
C 1 73  GLU 73  73  73  GLU GLU C . n 
C 1 74  LEU 74  74  74  LEU LEU C . n 
C 1 75  LEU 75  75  75  LEU LEU C . n 
C 1 76  LEU 76  76  76  LEU LEU C . n 
C 1 77  VAL 77  77  77  VAL VAL C . n 
C 1 78  VAL 78  78  78  VAL VAL C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  SER 80  80  80  SER SER C . n 
C 1 81  GLY 81  81  81  GLY GLY C . n 
C 1 82  SER 82  82  82  SER SER C . n 
C 1 83  ALA 83  83  83  ALA ALA C . n 
C 1 84  ILE 84  84  84  ILE ILE C . n 
C 1 85  LEU 85  85  85  LEU LEU C . n 
C 1 86  VAL 86  86  86  VAL VAL C . n 
C 1 87  LEU 87  87  87  LEU LEU C . n 
C 1 88  VAL 88  88  88  VAL VAL C . n 
C 1 89  LYS 89  89  89  LYS LYS C . n 
C 1 90  PRO 90  90  90  PRO PRO C . n 
C 1 91  ASP 91  91  91  ASP ASP C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  ARG 93  93  93  ARG ARG C . n 
C 1 94  ARG 94  94  94  ARG ARG C . n 
C 1 95  GLU 95  95  95  GLU GLU C . n 
C 1 96  TYR 96  96  96  TYR TYR C . n 
C 1 97  PHE 97  97  97  PHE PHE C . n 
C 1 98  PHE 98  98  98  PHE PHE C . n 
C 1 99  LEU 99  99  99  LEU LEU C . n 
C 1 100 THR 100 100 100 THR THR C . n 
C 1 101 SER 101 101 101 SER SER C . n 
C 1 102 ASP 102 102 102 ASP ASP C . n 
C 1 103 ASN 103 103 103 ASN ASN C . n 
C 1 104 PRO 104 104 104 PRO PRO C . n 
C 1 105 ILE 105 105 105 ILE ILE C . n 
C 1 106 PHE 106 106 106 PHE PHE C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 ASP 108 108 108 ASP ASP C . n 
C 1 109 HIS 109 109 109 HIS HIS C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 LYS 111 111 111 LYS LYS C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 PRO 113 113 113 PRO PRO C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 GLY 115 115 115 GLY GLY C . n 
C 1 116 THR 116 116 116 THR THR C . n 
C 1 117 ILE 117 117 117 ILE ILE C . n 
C 1 118 PHE 118 118 118 PHE PHE C . n 
C 1 119 TYR 119 119 119 TYR TYR C . n 
C 1 120 LEU 120 120 120 LEU LEU C . n 
C 1 121 VAL 121 121 121 VAL VAL C . n 
C 1 122 ASN 122 122 122 ASN ASN C . n 
C 1 123 PRO 123 123 123 PRO PRO C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 PRO 125 125 125 PRO PRO C . n 
C 1 126 LYS 126 126 126 LYS LYS C . n 
C 1 127 GLU 127 127 127 GLU GLU C . n 
C 1 128 ASP 128 128 128 ASP ASP C . n 
C 1 129 LEU 129 129 129 LEU LEU C . n 
C 1 130 ARG 130 130 130 ARG ARG C . n 
C 1 131 ILE 131 131 131 ILE ILE C . n 
C 1 132 ILE 132 132 132 ILE ILE C . n 
C 1 133 GLN 133 133 133 GLN GLN C . n 
C 1 134 LEU 134 134 134 LEU LEU C . n 
C 1 135 ALA 135 135 135 ALA ALA C . n 
C 1 136 MET 136 136 136 MET MET C . n 
C 1 137 PRO 137 137 137 PRO PRO C . n 
C 1 138 VAL 138 138 138 VAL VAL C . n 
C 1 139 ASN 139 139 139 ASN ASN C . n 
C 1 140 ASN 140 140 140 ASN ASN C . n 
C 1 141 PRO 141 141 141 PRO PRO C . n 
C 1 142 GLN 142 142 142 GLN GLN C . n 
C 1 143 ILE 143 143 143 ILE ILE C . n 
C 1 144 HIS 144 144 144 HIS HIS C . n 
C 1 145 GLU 145 145 145 GLU GLU C . n 
C 1 146 PHE 146 146 146 PHE PHE C . n 
C 1 147 PHE 147 147 147 PHE PHE C . n 
C 1 148 LEU 148 148 148 LEU LEU C . n 
C 1 149 SER 149 149 149 SER SER C . n 
C 1 150 SER 150 150 150 SER SER C . n 
C 1 151 THR 151 151 151 THR THR C . n 
C 1 152 GLU 152 152 152 GLU GLU C . n 
C 1 153 ALA 153 153 153 ALA ALA C . n 
C 1 154 GLN 154 154 154 GLN GLN C . n 
C 1 155 GLN 155 155 155 GLN GLN C . n 
C 1 156 SER 156 156 156 SER SER C . n 
C 1 157 TYR 157 157 157 TYR TYR C . n 
C 1 158 LEU 158 158 158 LEU LEU C . n 
C 1 159 GLN 159 159 159 GLN GLN C . n 
C 1 160 GLU 160 160 160 GLU GLU C . n 
C 1 161 PHE 161 161 161 PHE PHE C . n 
C 1 162 SER 162 162 162 SER SER C . n 
C 1 163 LYS 163 163 163 LYS LYS C . n 
C 1 164 HIS 164 164 164 HIS HIS C . n 
C 1 165 ILE 165 165 165 ILE ILE C . n 
C 1 166 LEU 166 166 166 LEU LEU C . n 
C 1 167 GLU 167 167 167 GLU GLU C . n 
C 1 168 ALA 168 168 168 ALA ALA C . n 
C 1 169 SER 169 169 169 SER SER C . n 
C 1 170 PHE 170 170 170 PHE PHE C . n 
C 1 171 ASN 171 171 171 ASN ASN C . n 
C 1 172 SER 172 172 172 SER SER C . n 
C 1 173 LYS 173 173 173 LYS LYS C . n 
C 1 174 PHE 174 174 174 PHE PHE C . n 
C 1 175 GLU 175 175 175 GLU GLU C . n 
C 1 176 GLU 176 176 176 GLU GLU C . n 
C 1 177 ILE 177 177 177 ILE ILE C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ARG 179 179 179 ARG ARG C . n 
C 1 180 VAL 180 180 180 VAL VAL C . n 
C 1 181 LEU 181 181 181 LEU LEU C . n 
C 1 182 PHE 182 182 182 PHE PHE C . n 
C 1 183 GLU 183 183 183 GLU GLU C . n 
C 1 184 GLU 184 184 184 GLU GLU C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 GLY 186 186 186 GLY GLY C . n 
C 1 187 GLN 187 187 187 GLN GLN C . n 
C 1 188 GLN 188 188 188 GLN GLN C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 GLY 190 190 190 GLY GLY C . n 
C 1 191 VAL 191 191 191 VAL VAL C . n 
C 1 192 ILE 192 192 192 ILE ILE C . n 
C 1 193 VAL 193 193 193 VAL VAL C . n 
C 1 194 ASN 194 194 194 ASN ASN C . n 
C 1 195 ILE 195 195 195 ILE ILE C . n 
C 1 196 ASP 196 196 196 ASP ASP C . n 
C 1 197 SER 197 197 197 SER SER C . n 
C 1 198 GLU 198 198 198 GLU GLU C . n 
C 1 199 GLN 199 199 199 GLN GLN C . n 
C 1 200 ILE 200 200 200 ILE ILE C . n 
C 1 201 LYS 201 201 201 LYS LYS C . n 
C 1 202 GLU 202 202 202 GLU GLU C . n 
C 1 203 LEU 203 203 203 LEU LEU 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 HIS 206 206 206 HIS HIS C . n 
C 1 207 ALA 207 207 207 ALA ALA C . n 
C 1 208 LYS 208 208 208 LYS LYS C . n 
C 1 209 SER 209 209 209 SER SER C . n 
C 1 210 SER 210 210 210 SER SER C . n 
C 1 211 SER 211 211 ?   ?   ?   C . n 
C 1 212 ARG 212 212 ?   ?   ?   C . n 
C 1 213 LYS 213 213 ?   ?   ?   C . n 
C 1 214 SER 214 214 ?   ?   ?   C . n 
C 1 215 LEU 215 215 ?   ?   ?   C . n 
C 1 216 SER 216 216 ?   ?   ?   C . n 
C 1 217 LYS 217 217 ?   ?   ?   C . n 
C 1 218 GLN 218 218 ?   ?   ?   C . n 
C 1 219 ASP 219 219 ?   ?   ?   C . n 
C 1 220 ASN 220 220 220 ASN ASN C . n 
C 1 221 THR 221 221 221 THR THR C . n 
C 1 222 ILE 222 222 222 ILE ILE C . n 
C 1 223 GLY 223 223 223 GLY GLY C . n 
C 1 224 ASN 224 224 224 ASN ASN C . n 
C 1 225 GLU 225 225 225 GLU GLU C . n 
C 1 226 PHE 226 226 226 PHE PHE C . n 
C 1 227 GLY 227 227 227 GLY GLY C . n 
C 1 228 ASN 228 228 228 ASN ASN C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 THR 230 230 230 THR THR C . n 
C 1 231 GLU 231 231 231 GLU GLU C . n 
C 1 232 ARG 232 232 232 ARG ARG C . n 
C 1 233 THR 233 233 233 THR THR C . n 
C 1 234 ASP 234 234 234 ASP ASP C . n 
C 1 235 ASN 235 235 235 ASN ASN C . n 
C 1 236 SER 236 236 236 SER SER C . n 
C 1 237 LEU 237 237 237 LEU LEU C . n 
C 1 238 ASN 238 238 238 ASN ASN C . n 
C 1 239 VAL 239 239 239 VAL VAL C . n 
C 1 240 LEU 240 240 240 LEU LEU C . n 
C 1 241 ILE 241 241 241 ILE ILE C . n 
C 1 242 SER 242 242 242 SER SER C . n 
C 1 243 SER 243 243 243 SER SER C . n 
C 1 244 ILE 244 244 244 ILE ILE C . n 
C 1 245 GLU 245 245 245 GLU GLU C . n 
C 1 246 MET 246 246 246 MET MET C . n 
C 1 247 GLU 247 247 247 GLU GLU C . n 
C 1 248 GLU 248 248 248 GLU GLU C . n 
C 1 249 GLY 249 249 249 GLY GLY C . n 
C 1 250 ALA 250 250 250 ALA ALA C . n 
C 1 251 LEU 251 251 251 LEU LEU C . n 
C 1 252 PHE 252 252 252 PHE PHE C . n 
C 1 253 VAL 253 253 253 VAL VAL C . n 
C 1 254 PRO 254 254 254 PRO PRO C . n 
C 1 255 HIS 255 255 255 HIS HIS C . n 
C 1 256 TYR 256 256 256 TYR TYR C . n 
C 1 257 TYR 257 257 257 TYR TYR C . n 
C 1 258 SER 258 258 258 SER SER C . n 
C 1 259 LYS 259 259 259 LYS LYS C . n 
C 1 260 ALA 260 260 260 ALA ALA C . n 
C 1 261 ILE 261 261 261 ILE ILE C . n 
C 1 262 VAL 262 262 262 VAL VAL C . n 
C 1 263 ILE 263 263 263 ILE ILE C . n 
C 1 264 LEU 264 264 264 LEU LEU C . n 
C 1 265 VAL 265 265 265 VAL VAL C . n 
C 1 266 VAL 266 266 266 VAL VAL C . n 
C 1 267 ASN 267 267 267 ASN ASN C . n 
C 1 268 GLU 268 268 268 GLU GLU C . n 
C 1 269 GLY 269 269 269 GLY GLY C . n 
C 1 270 GLU 270 270 270 GLU GLU C . n 
C 1 271 ALA 271 271 271 ALA ALA C . n 
C 1 272 HIS 272 272 272 HIS HIS C . n 
C 1 273 VAL 273 273 273 VAL VAL C . n 
C 1 274 GLU 274 274 274 GLU GLU C . n 
C 1 275 LEU 275 275 275 LEU LEU C . n 
C 1 276 VAL 276 276 276 VAL VAL C . n 
C 1 277 GLY 277 277 277 GLY GLY C . n 
C 1 278 PRO 278 278 278 PRO PRO C . n 
C 1 279 LYS 279 279 279 LYS LYS C . n 
C 1 280 GLY 280 280 280 GLY GLY C . n 
C 1 281 ASN 281 281 ?   ?   ?   C . n 
C 1 282 LYS 282 282 ?   ?   ?   C . n 
C 1 283 GLU 283 283 283 GLU GLU C . n 
C 1 284 THR 284 284 284 THR THR C . n 
C 1 285 LEU 285 285 285 LEU LEU C . n 
C 1 286 GLU 286 286 286 GLU GLU C . n 
C 1 287 TYR 287 287 287 TYR TYR C . n 
C 1 288 GLU 288 288 288 GLU GLU C . n 
C 1 289 SER 289 289 289 SER SER C . n 
C 1 290 TYR 290 290 290 TYR TYR C . n 
C 1 291 ARG 291 291 291 ARG ARG C . n 
C 1 292 ALA 292 292 292 ALA ALA C . n 
C 1 293 GLU 293 293 293 GLU GLU C . n 
C 1 294 LEU 294 294 294 LEU LEU C . n 
C 1 295 SER 295 295 295 SER SER C . n 
C 1 296 LYS 296 296 296 LYS LYS C . n 
C 1 297 ASP 297 297 297 ASP ASP C . n 
C 1 298 ASP 298 298 298 ASP ASP C . n 
C 1 299 VAL 299 299 299 VAL VAL C . n 
C 1 300 PHE 300 300 300 PHE PHE C . n 
C 1 301 VAL 301 301 301 VAL VAL C . n 
C 1 302 ILE 302 302 302 ILE ILE C . n 
C 1 303 PRO 303 303 303 PRO PRO C . n 
C 1 304 ALA 304 304 304 ALA ALA C . n 
C 1 305 ALA 305 305 305 ALA ALA C . n 
C 1 306 TYR 306 306 306 TYR TYR C . n 
C 1 307 PRO 307 307 307 PRO PRO C . n 
C 1 308 VAL 308 308 308 VAL VAL C . n 
C 1 309 ALA 309 309 309 ALA ALA C . n 
C 1 310 ILE 310 310 310 ILE ILE C . n 
C 1 311 LYS 311 311 311 LYS LYS C . n 
C 1 312 ALA 312 312 312 ALA ALA C . n 
C 1 313 THR 313 313 313 THR THR C . n 
C 1 314 SER 314 314 314 SER SER C . n 
C 1 315 ASN 315 315 315 ASN ASN C . n 
C 1 316 VAL 316 316 316 VAL VAL C . n 
C 1 317 ASN 317 317 317 ASN ASN C . n 
C 1 318 PHE 318 318 318 PHE PHE C . n 
C 1 319 THR 319 319 319 THR THR C . n 
C 1 320 GLY 320 320 320 GLY GLY C . n 
C 1 321 PHE 321 321 321 PHE PHE C . n 
C 1 322 GLY 322 322 322 GLY GLY C . n 
C 1 323 ILE 323 323 323 ILE ILE C . n 
C 1 324 ASN 324 324 324 ASN ASN C . n 
C 1 325 ALA 325 325 325 ALA ALA C . n 
C 1 326 ASN 326 326 326 ASN ASN C . n 
C 1 327 ASN 327 327 327 ASN ASN C . n 
C 1 328 ASN 328 328 328 ASN ASN C . n 
C 1 329 ASN 329 329 329 ASN ASN C . n 
C 1 330 ARG 330 330 330 ARG ARG C . n 
C 1 331 ASN 331 331 331 ASN ASN C . n 
C 1 332 LEU 332 332 332 LEU LEU C . n 
C 1 333 LEU 333 333 333 LEU LEU C . n 
C 1 334 ALA 334 334 334 ALA ALA C . n 
C 1 335 GLY 335 335 335 GLY GLY C . n 
C 1 336 LYS 336 336 336 LYS LYS C . n 
C 1 337 THR 337 337 337 THR THR C . n 
C 1 338 ASP 338 338 338 ASP ASP C . n 
C 1 339 ASN 339 339 339 ASN ASN C . n 
C 1 340 VAL 340 340 340 VAL VAL C . n 
C 1 341 ILE 341 341 341 ILE ILE C . n 
C 1 342 SER 342 342 342 SER SER C . n 
C 1 343 SER 343 343 343 SER SER C . n 
C 1 344 ILE 344 344 344 ILE ILE C . n 
C 1 345 GLY 345 345 345 GLY GLY C . n 
C 1 346 ARG 346 346 346 ARG ARG C . n 
C 1 347 ALA 347 347 347 ALA ALA C . n 
C 1 348 LEU 348 348 348 LEU LEU C . n 
C 1 349 ASP 349 349 349 ASP ASP C . n 
C 1 350 GLY 350 350 350 GLY GLY C . n 
C 1 351 LYS 351 351 351 LYS LYS C . n 
C 1 352 ASP 352 352 352 ASP ASP C . n 
C 1 353 VAL 353 353 353 VAL VAL C . n 
C 1 354 LEU 354 354 354 LEU LEU C . n 
C 1 355 GLY 355 355 355 GLY GLY C . n 
C 1 356 LEU 356 356 356 LEU LEU C . n 
C 1 357 THR 357 357 357 THR THR C . n 
C 1 358 PHE 358 358 358 PHE PHE C . n 
C 1 359 SER 359 359 359 SER SER C . n 
C 1 360 GLY 360 360 360 GLY GLY C . n 
C 1 361 SER 361 361 361 SER SER C . n 
C 1 362 GLY 362 362 362 GLY GLY C . n 
C 1 363 ASP 363 363 363 ASP ASP C . n 
C 1 364 GLU 364 364 364 GLU GLU C . n 
C 1 365 VAL 365 365 365 VAL VAL C . n 
C 1 366 MET 366 366 366 MET MET C . n 
C 1 367 LYS 367 367 367 LYS LYS C . n 
C 1 368 LEU 368 368 368 LEU LEU C . n 
C 1 369 ILE 369 369 369 ILE ILE C . n 
C 1 370 ASN 370 370 370 ASN ASN C . n 
C 1 371 LYS 371 371 371 LYS LYS C . n 
C 1 372 GLN 372 372 372 GLN GLN C . n 
C 1 373 SER 373 373 373 SER SER C . n 
C 1 374 GLY 374 374 374 GLY GLY C . n 
C 1 375 SER 375 375 375 SER SER C . n 
C 1 376 TYR 376 376 376 TYR TYR C . n 
C 1 377 PHE 377 377 377 PHE PHE C . n 
C 1 378 VAL 378 378 378 VAL VAL C . n 
C 1 379 ASP 379 379 379 ASP ASP C . n 
C 1 380 ALA 380 380 380 ALA ALA C . n 
C 1 381 HIS 381 381 381 HIS HIS C . n 
C 1 382 HIS 382 382 ?   ?   ?   C . n 
C 1 383 HIS 383 383 ?   ?   ?   C . n 
C 1 384 GLN 384 384 ?   ?   ?   C . n 
C 1 385 GLN 385 385 ?   ?   ?   C . n 
C 1 386 GLU 386 386 ?   ?   ?   C . n 
C 1 387 GLN 387 387 ?   ?   ?   C . n 
C 1 388 GLN 388 388 ?   ?   ?   C . n 
C 1 389 LYS 389 389 ?   ?   ?   C . n 
C 1 390 GLY 390 390 ?   ?   ?   C . n 
C 1 391 ARG 391 391 ?   ?   ?   C . n 
C 1 392 LYS 392 392 ?   ?   ?   C . n 
C 1 393 GLY 393 393 ?   ?   ?   C . n 
C 1 394 ALA 394 394 ?   ?   ?   C . n 
C 1 395 PHE 395 395 ?   ?   ?   C . n 
C 1 396 VAL 396 396 ?   ?   ?   C . n 
C 1 397 TYR 397 397 ?   ?   ?   C . n 
# 
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 NAG 1  900 900 NAG NAG A . 
E 3 PO4 1  950 950 PO4 PO4 A . 
F 2 NAG 1  901 901 NAG NAG B . 
G 3 PO4 1  951 951 PO4 PO4 B . 
H 2 NAG 1  902 902 NAG NAG C . 
I 3 PO4 1  952 952 PO4 PO4 C . 
J 4 HOH 1  500 500 HOH HOH A . 
J 4 HOH 2  502 502 HOH HOH A . 
J 4 HOH 3  505 505 HOH HOH A . 
J 4 HOH 4  513 513 HOH HOH A . 
J 4 HOH 5  515 515 HOH HOH A . 
J 4 HOH 6  520 520 HOH HOH A . 
J 4 HOH 7  521 521 HOH HOH A . 
J 4 HOH 8  525 525 HOH HOH A . 
J 4 HOH 9  529 529 HOH HOH A . 
J 4 HOH 10 530 530 HOH HOH A . 
J 4 HOH 11 531 531 HOH HOH A . 
J 4 HOH 12 533 533 HOH HOH A . 
J 4 HOH 13 541 541 HOH HOH A . 
J 4 HOH 14 542 542 HOH HOH A . 
J 4 HOH 15 544 544 HOH HOH A . 
J 4 HOH 16 547 547 HOH HOH A . 
J 4 HOH 17 548 548 HOH HOH A . 
J 4 HOH 18 549 549 HOH HOH A . 
J 4 HOH 19 552 552 HOH HOH A . 
J 4 HOH 20 553 553 HOH HOH A . 
J 4 HOH 21 554 554 HOH HOH A . 
J 4 HOH 22 564 564 HOH HOH A . 
J 4 HOH 23 566 566 HOH HOH A . 
J 4 HOH 24 568 568 HOH HOH A . 
K 4 HOH 1  506 506 HOH HOH B . 
K 4 HOH 2  507 507 HOH HOH B . 
K 4 HOH 3  508 508 HOH HOH B . 
K 4 HOH 4  509 509 HOH HOH B . 
K 4 HOH 5  510 510 HOH HOH B . 
K 4 HOH 6  514 514 HOH HOH B . 
K 4 HOH 7  516 516 HOH HOH B . 
K 4 HOH 8  517 517 HOH HOH B . 
K 4 HOH 9  518 518 HOH HOH B . 
K 4 HOH 10 523 523 HOH HOH B . 
K 4 HOH 11 524 524 HOH HOH B . 
K 4 HOH 12 526 526 HOH HOH B . 
K 4 HOH 13 535 535 HOH HOH B . 
K 4 HOH 14 538 538 HOH HOH B . 
K 4 HOH 15 539 539 HOH HOH B . 
K 4 HOH 16 543 543 HOH HOH B . 
K 4 HOH 17 546 546 HOH HOH B . 
K 4 HOH 18 551 551 HOH HOH B . 
K 4 HOH 19 556 556 HOH HOH B . 
K 4 HOH 20 558 558 HOH HOH B . 
K 4 HOH 21 559 559 HOH HOH B . 
K 4 HOH 22 560 560 HOH HOH B . 
K 4 HOH 23 562 562 HOH HOH B . 
K 4 HOH 24 565 565 HOH HOH B . 
L 4 HOH 1  501 501 HOH HOH C . 
L 4 HOH 2  503 503 HOH HOH C . 
L 4 HOH 3  504 504 HOH HOH C . 
L 4 HOH 4  511 511 HOH HOH C . 
L 4 HOH 5  512 512 HOH HOH C . 
L 4 HOH 6  519 519 HOH HOH C . 
L 4 HOH 7  522 522 HOH HOH C . 
L 4 HOH 8  527 527 HOH HOH C . 
L 4 HOH 9  528 528 HOH HOH C . 
L 4 HOH 10 532 532 HOH HOH C . 
L 4 HOH 11 534 534 HOH HOH C . 
L 4 HOH 12 536 536 HOH HOH C . 
L 4 HOH 13 537 537 HOH HOH C . 
L 4 HOH 14 540 540 HOH HOH C . 
L 4 HOH 15 545 545 HOH HOH C . 
L 4 HOH 16 550 550 HOH HOH C . 
L 4 HOH 17 555 555 HOH HOH C . 
L 4 HOH 18 557 557 HOH HOH C . 
L 4 HOH 19 561 561 HOH HOH C . 
L 4 HOH 20 563 563 HOH HOH C . 
L 4 HOH 21 567 567 HOH HOH C . 
L 4 HOH 22 569 569 HOH HOH C . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A ASN 228 A ASN 228 ? ASN 'GLYCOSYLATION SITE' 
2 B ASN 228 B ASN 228 ? ASN 'GLYCOSYLATION SITE' 
3 C ASN 228 C ASN 228 ? ASN 'GLYCOSYLATION SITE' 
# 
_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 
# 
_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 
# 
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)' 18040 ? 
1 MORE         -114  ? 
1 'SSA (A^2)'  39770 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_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 1994-09-30 
2 'Structure model' 1 1 2008-03-24 
3 'Structure model' 1 2 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Non-polymer description'   
3 3 'Structure model' 'Version format compliance' 
# 
_software.name             X-PLOR 
_software.classification   refinement 
_software.version          . 
_software.citation_id      ? 
_software.pdbx_ordinal     1 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;SHEET
THERE ARE SEVERAL BIFURCATED SHEETS IN THIS STRUCTURE.
THESE ARE REPRESENTED BY TWO SHEETS WHICH HAVE ONE OR MORE
IDENTICAL STRANDS.  SHEETS *N2A* AND *N2B* REPRESENT ONE
BIFURCATED SHEET.  SHEETS *C2A* AND *C2B* ALSO REPRESENT
ONE BIFURCATED SHEET.
;
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   ND2 
_pdbx_validate_close_contact.auth_asym_id_1   C 
_pdbx_validate_close_contact.auth_comp_id_1   ASN 
_pdbx_validate_close_contact.auth_seq_id_1    228 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O5 
_pdbx_validate_close_contact.auth_asym_id_2   C 
_pdbx_validate_close_contact.auth_comp_id_2   NAG 
_pdbx_validate_close_contact.auth_seq_id_2    902 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.12 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C B ASN 103 ? ? N B PRO 104 ? ? CA B PRO 104 ? ? 130.04 119.30 10.74 1.50 Y 
2 1 C C ASN 103 ? ? N C PRO 104 ? ? CA C PRO 104 ? ? 128.49 119.30 9.19  1.50 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 20  ? ? -149.41 32.49   
2  1 GLN A 29  ? ? -43.83  -7.89   
3  1 LEU A 46  ? ? -85.77  30.66   
4  1 ASP A 71  ? ? -86.34  42.81   
5  1 PRO A 104 ? ? -66.82  14.57   
6  1 LYS A 126 ? ? -133.36 -31.37  
7  1 ASN A 140 ? ? -172.39 -174.62 
8  1 GLU A 183 ? ? -38.83  123.74  
9  1 GLU A 185 ? ? -67.34  92.59   
10 1 ASN A 224 ? ? -172.39 -154.45 
11 1 VAL A 253 ? ? -48.43  158.05  
12 1 ALA A 292 ? ? -170.81 147.22  
13 1 ALA A 305 ? ? 84.07   -1.89   
14 1 ASN A 324 ? ? 70.44   61.10   
15 1 ASN A 327 ? ? 80.67   11.52   
16 1 TYR A 376 ? ? 68.21   -69.95  
17 1 ALA A 380 ? ? -150.93 45.90   
18 1 ASP B 19  ? ? -67.70  5.17    
19 1 ASN B 20  ? ? -143.45 -46.14  
20 1 LYS B 27  ? ? -170.06 141.54  
21 1 GLU B 62  ? ? 48.78   73.63   
22 1 ASP B 71  ? ? -94.10  43.84   
23 1 SER B 80  ? ? 174.54  128.63  
24 1 ASP B 91  ? ? -106.30 47.53   
25 1 ASP B 102 ? ? -109.88 -69.36  
26 1 ASN B 103 ? ? -37.42  112.88  
27 1 PRO B 104 ? ? -56.28  10.62   
28 1 PRO B 141 ? ? -64.16  10.80   
29 1 ASN B 224 ? ? -155.85 -158.39 
30 1 ASN B 238 ? ? 70.03   31.82   
31 1 GLU B 248 ? ? -32.72  128.03  
32 1 LYS B 279 ? ? -63.88  86.84   
33 1 TYR B 290 ? ? -117.11 75.44   
34 1 LYS B 296 ? ? -35.93  134.77  
35 1 ASN B 324 ? ? 84.53   32.37   
36 1 ASN B 327 ? ? 78.15   41.28   
37 1 TYR B 376 ? ? 63.87   -75.80  
38 1 LEU C 46  ? ? -84.96  41.86   
39 1 ASP C 71  ? ? -93.28  38.74   
40 1 SER C 80  ? ? 166.19  139.23  
41 1 ASP C 91  ? ? -86.80  37.83   
42 1 PRO C 104 ? ? -43.76  -0.18   
43 1 LYS C 126 ? ? -130.91 -30.95  
44 1 GLN C 159 ? ? -56.36  -7.13   
45 1 ARG C 179 ? ? -57.18  -74.69  
46 1 GLU C 185 ? ? -82.97  47.96   
47 1 ILE C 200 ? ? -76.14  22.73   
48 1 ASN C 224 ? ? -147.49 -154.01 
49 1 VAL C 253 ? ? -48.09  157.59  
50 1 LYS C 296 ? ? -27.76  122.01  
51 1 ASN C 327 ? ? 80.66   1.38    
52 1 ASP C 338 ? ? 44.46   28.65   
53 1 TYR C 376 ? ? 64.82   -68.01  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 TYR A 287 ? ? 0.071 'SIDE CHAIN' 
2 1 TYR C 287 ? ? 0.092 'SIDE CHAIN' 
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    C1 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    C 
_pdbx_validate_chiral.auth_comp_id    NAG 
_pdbx_validate_chiral.auth_seq_id     902 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         PLANAR 
_pdbx_validate_chiral.omega           . 
# 
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 THR 1   ? A THR 1   
2   1 Y 1 A SER 2   ? A SER 2   
3   1 Y 1 A LEU 3   ? A LEU 3   
4   1 Y 1 A ARG 4   ? A ARG 4   
5   1 Y 1 A GLU 5   ? A GLU 5   
6   1 Y 1 A GLU 6   ? A GLU 6   
7   1 Y 1 A GLU 7   ? A GLU 7   
8   1 Y 1 A GLU 8   ? A GLU 8   
9   1 Y 1 A SER 9   ? A SER 9   
10  1 Y 1 A GLN 10  ? A GLN 10  
11  1 Y 1 A SER 211 ? A SER 211 
12  1 Y 1 A ARG 212 ? A ARG 212 
13  1 Y 1 A LYS 213 ? A LYS 213 
14  1 Y 1 A SER 214 ? A SER 214 
15  1 Y 1 A LEU 215 ? A LEU 215 
16  1 Y 1 A SER 216 ? A SER 216 
17  1 Y 1 A LYS 217 ? A LYS 217 
18  1 Y 1 A GLN 218 ? A GLN 218 
19  1 Y 1 A ASP 219 ? A ASP 219 
20  1 Y 1 A ASN 281 ? A ASN 281 
21  1 Y 1 A LYS 282 ? A LYS 282 
22  1 Y 1 A HIS 382 ? A HIS 382 
23  1 Y 1 A HIS 383 ? A HIS 383 
24  1 Y 1 A GLN 384 ? A GLN 384 
25  1 Y 1 A GLN 385 ? A GLN 385 
26  1 Y 1 A GLU 386 ? A GLU 386 
27  1 Y 1 A GLN 387 ? A GLN 387 
28  1 Y 1 A GLN 388 ? A GLN 388 
29  1 Y 1 A LYS 389 ? A LYS 389 
30  1 Y 1 A GLY 390 ? A GLY 390 
31  1 Y 1 A ARG 391 ? A ARG 391 
32  1 Y 1 A LYS 392 ? A LYS 392 
33  1 Y 1 A GLY 393 ? A GLY 393 
34  1 Y 1 A ALA 394 ? A ALA 394 
35  1 Y 1 A PHE 395 ? A PHE 395 
36  1 Y 1 A VAL 396 ? A VAL 396 
37  1 Y 1 A TYR 397 ? A TYR 397 
38  1 Y 1 B THR 1   ? B THR 1   
39  1 Y 1 B SER 2   ? B SER 2   
40  1 Y 1 B LEU 3   ? B LEU 3   
41  1 Y 1 B ARG 4   ? B ARG 4   
42  1 Y 1 B GLU 5   ? B GLU 5   
43  1 Y 1 B GLU 6   ? B GLU 6   
44  1 Y 1 B GLU 7   ? B GLU 7   
45  1 Y 1 B GLU 8   ? B GLU 8   
46  1 Y 1 B SER 9   ? B SER 9   
47  1 Y 1 B GLN 10  ? B GLN 10  
48  1 Y 1 B SER 211 ? B SER 211 
49  1 Y 1 B ARG 212 ? B ARG 212 
50  1 Y 1 B LYS 213 ? B LYS 213 
51  1 Y 1 B SER 214 ? B SER 214 
52  1 Y 1 B LEU 215 ? B LEU 215 
53  1 Y 1 B SER 216 ? B SER 216 
54  1 Y 1 B LYS 217 ? B LYS 217 
55  1 Y 1 B GLN 218 ? B GLN 218 
56  1 Y 1 B ASP 219 ? B ASP 219 
57  1 Y 1 B ASN 281 ? B ASN 281 
58  1 Y 1 B LYS 282 ? B LYS 282 
59  1 Y 1 B HIS 382 ? B HIS 382 
60  1 Y 1 B HIS 383 ? B HIS 383 
61  1 Y 1 B GLN 384 ? B GLN 384 
62  1 Y 1 B GLN 385 ? B GLN 385 
63  1 Y 1 B GLU 386 ? B GLU 386 
64  1 Y 1 B GLN 387 ? B GLN 387 
65  1 Y 1 B GLN 388 ? B GLN 388 
66  1 Y 1 B LYS 389 ? B LYS 389 
67  1 Y 1 B GLY 390 ? B GLY 390 
68  1 Y 1 B ARG 391 ? B ARG 391 
69  1 Y 1 B LYS 392 ? B LYS 392 
70  1 Y 1 B GLY 393 ? B GLY 393 
71  1 Y 1 B ALA 394 ? B ALA 394 
72  1 Y 1 B PHE 395 ? B PHE 395 
73  1 Y 1 B VAL 396 ? B VAL 396 
74  1 Y 1 B TYR 397 ? B TYR 397 
75  1 Y 1 C THR 1   ? C THR 1   
76  1 Y 1 C SER 2   ? C SER 2   
77  1 Y 1 C LEU 3   ? C LEU 3   
78  1 Y 1 C ARG 4   ? C ARG 4   
79  1 Y 1 C GLU 5   ? C GLU 5   
80  1 Y 1 C GLU 6   ? C GLU 6   
81  1 Y 1 C GLU 7   ? C GLU 7   
82  1 Y 1 C GLU 8   ? C GLU 8   
83  1 Y 1 C SER 9   ? C SER 9   
84  1 Y 1 C SER 211 ? C SER 211 
85  1 Y 1 C ARG 212 ? C ARG 212 
86  1 Y 1 C LYS 213 ? C LYS 213 
87  1 Y 1 C SER 214 ? C SER 214 
88  1 Y 1 C LEU 215 ? C LEU 215 
89  1 Y 1 C SER 216 ? C SER 216 
90  1 Y 1 C LYS 217 ? C LYS 217 
91  1 Y 1 C GLN 218 ? C GLN 218 
92  1 Y 1 C ASP 219 ? C ASP 219 
93  1 Y 1 C ASN 281 ? C ASN 281 
94  1 Y 1 C LYS 282 ? C LYS 282 
95  1 Y 1 C HIS 382 ? C HIS 382 
96  1 Y 1 C HIS 383 ? C HIS 383 
97  1 Y 1 C GLN 384 ? C GLN 384 
98  1 Y 1 C GLN 385 ? C GLN 385 
99  1 Y 1 C GLU 386 ? C GLU 386 
100 1 Y 1 C GLN 387 ? C GLN 387 
101 1 Y 1 C GLN 388 ? C GLN 388 
102 1 Y 1 C LYS 389 ? C LYS 389 
103 1 Y 1 C GLY 390 ? C GLY 390 
104 1 Y 1 C ARG 391 ? C ARG 391 
105 1 Y 1 C LYS 392 ? C LYS 392 
106 1 Y 1 C GLY 393 ? C GLY 393 
107 1 Y 1 C ALA 394 ? C ALA 394 
108 1 Y 1 C PHE 395 ? C PHE 395 
109 1 Y 1 C VAL 396 ? C VAL 396 
110 1 Y 1 C TYR 397 ? C TYR 397 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 'PHOSPHATE ION'        PO4 
4 water                  HOH 
# 
