data_4MC7
# 
_entry.id   4MC7 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4MC7         
RCSB  RCSB081728   
WWPDB D_1000081728 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4K3Y . unspecified 
PDB 4MC4 . unspecified 
PDB 4MC5 . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4MC7 
_pdbx_database_status.recvd_initial_deposition_date   2013-08-21 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Yang, H.'     1 
'Carney, P.J.' 2 
'Chang, J.C.'  3 
'Guo, Z.'      4 
'Stevens, J.'  5 
# 
_citation.id                        primary 
_citation.title                     'New world bats harbor diverse influenza a viruses.' 
_citation.journal_abbrev            'Plos Pathog.' 
_citation.journal_volume            9 
_citation.page_first                e1003657 
_citation.page_last                 e1003657 
_citation.year                      2013 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1553-7366 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   24130481 
_citation.pdbx_database_id_DOI      10.1371/journal.ppat.1003657 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Tong, S.'        1  
primary 'Zhu, X.'         2  
primary 'Li, Y.'          3  
primary 'Shi, M.'         4  
primary 'Zhang, J.'       5  
primary 'Bourgeois, M.'   6  
primary 'Yang, H.'        7  
primary 'Chen, X.'        8  
primary 'Recuenco, S.'    9  
primary 'Gomez, J.'       10 
primary 'Chen, L.M.'      11 
primary 'Johnson, A.'     12 
primary 'Tao, Y.'         13 
primary 'Dreyfus, C.'     14 
primary 'Yu, W.'          15 
primary 'McBride, R.'     16 
primary 'Carney, P.J.'    17 
primary 'Gilbert, A.T.'   18 
primary 'Chang, J.'       19 
primary 'Guo, Z.'         20 
primary 'Davis, C.T.'     21 
primary 'Paulson, J.C.'   22 
primary 'Stevens, J.'     23 
primary 'Rupprecht, C.E.' 24 
primary 'Holmes, E.C.'    25 
primary 'Wilson, I.A.'    26 
primary 'Donis, R.O.'     27 
# 
_cell.entry_id           4MC7 
_cell.length_a           123.374 
_cell.length_b           164.358 
_cell.length_c           214.912 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              32 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4MC7 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            ? 
# 
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 NEURAMINIDASE          40624.199 4 ? ? ? ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208   4 ? ? ? ? 
3 non-polymer syn 'CALCIUM ION'          40.078    5 ? ? ? ? 
# 
_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       
;GSGDSGSPGIATPLVLGENLCSINGWVPTYRGEGTTGKIPDEQMLTRQNFVSCSDKECRRFFVSMGYGTTTNFADLIVSE
QMNVYSVKLGDPPTPDKLKFEAVGWSASSCHDGFQWTVLSVAGDGFVSILYGGIITDTIHPTNGGPLRTQASSCICNDGT
CYTIIADGTTYTASSHRLYRLVNGTSAGWKALDTTGFNFEFPTCYYTSGKVKCTGTNLWNDAKRPFLEFDQSFTYTFKEP
CLGFLGDTPRGIDTTNYCDKTTTEGEGGIQGFMIEGSNSWIGRIINPGSKKGFEIYKFLGTLFSVQTVGNRNYQLLSNST
IGRSGLYQPAYESRDCQELCFWIEIAATTKAGLSSNDLITFCGTGGSMPDVNWG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSGDSGSPGIATPLVLGENLCSINGWVPTYRGEGTTGKIPDEQMLTRQNFVSCSDKECRRFFVSMGYGTTTNFADLIVSE
QMNVYSVKLGDPPTPDKLKFEAVGWSASSCHDGFQWTVLSVAGDGFVSILYGGIITDTIHPTNGGPLRTQASSCICNDGT
CYTIIADGTTYTASSHRLYRLVNGTSAGWKALDTTGFNFEFPTCYYTSGKVKCTGTNLWNDAKRPFLEFDQSFTYTFKEP
CLGFLGDTPRGIDTTNYCDKTTTEGEGGIQGFMIEGSNSWIGRIINPGSKKGFEIYKFLGTLFSVQTVGNRNYQLLSNST
IGRSGLYQPAYESRDCQELCFWIEIAATTKAGLSSNDLITFCGTGGSMPDVNWG
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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   GLY n 
1 2   SER n 
1 3   GLY n 
1 4   ASP n 
1 5   SER n 
1 6   GLY n 
1 7   SER n 
1 8   PRO n 
1 9   GLY n 
1 10  ILE n 
1 11  ALA n 
1 12  THR n 
1 13  PRO n 
1 14  LEU n 
1 15  VAL n 
1 16  LEU n 
1 17  GLY n 
1 18  GLU n 
1 19  ASN n 
1 20  LEU n 
1 21  CYS n 
1 22  SER n 
1 23  ILE n 
1 24  ASN n 
1 25  GLY n 
1 26  TRP n 
1 27  VAL n 
1 28  PRO n 
1 29  THR n 
1 30  TYR n 
1 31  ARG n 
1 32  GLY n 
1 33  GLU n 
1 34  GLY n 
1 35  THR n 
1 36  THR n 
1 37  GLY n 
1 38  LYS n 
1 39  ILE n 
1 40  PRO n 
1 41  ASP n 
1 42  GLU n 
1 43  GLN n 
1 44  MET n 
1 45  LEU n 
1 46  THR n 
1 47  ARG n 
1 48  GLN n 
1 49  ASN n 
1 50  PHE n 
1 51  VAL n 
1 52  SER n 
1 53  CYS n 
1 54  SER n 
1 55  ASP n 
1 56  LYS n 
1 57  GLU n 
1 58  CYS n 
1 59  ARG n 
1 60  ARG n 
1 61  PHE n 
1 62  PHE n 
1 63  VAL n 
1 64  SER n 
1 65  MET n 
1 66  GLY n 
1 67  TYR n 
1 68  GLY n 
1 69  THR n 
1 70  THR n 
1 71  THR n 
1 72  ASN n 
1 73  PHE n 
1 74  ALA n 
1 75  ASP n 
1 76  LEU n 
1 77  ILE n 
1 78  VAL n 
1 79  SER n 
1 80  GLU n 
1 81  GLN n 
1 82  MET n 
1 83  ASN n 
1 84  VAL n 
1 85  TYR n 
1 86  SER n 
1 87  VAL n 
1 88  LYS n 
1 89  LEU n 
1 90  GLY n 
1 91  ASP n 
1 92  PRO n 
1 93  PRO n 
1 94  THR n 
1 95  PRO n 
1 96  ASP n 
1 97  LYS n 
1 98  LEU n 
1 99  LYS n 
1 100 PHE n 
1 101 GLU n 
1 102 ALA n 
1 103 VAL n 
1 104 GLY n 
1 105 TRP n 
1 106 SER n 
1 107 ALA n 
1 108 SER n 
1 109 SER n 
1 110 CYS n 
1 111 HIS n 
1 112 ASP n 
1 113 GLY n 
1 114 PHE n 
1 115 GLN n 
1 116 TRP n 
1 117 THR n 
1 118 VAL n 
1 119 LEU n 
1 120 SER n 
1 121 VAL n 
1 122 ALA n 
1 123 GLY n 
1 124 ASP n 
1 125 GLY n 
1 126 PHE n 
1 127 VAL n 
1 128 SER n 
1 129 ILE n 
1 130 LEU n 
1 131 TYR n 
1 132 GLY n 
1 133 GLY n 
1 134 ILE n 
1 135 ILE n 
1 136 THR n 
1 137 ASP n 
1 138 THR n 
1 139 ILE n 
1 140 HIS n 
1 141 PRO n 
1 142 THR n 
1 143 ASN n 
1 144 GLY n 
1 145 GLY n 
1 146 PRO n 
1 147 LEU n 
1 148 ARG n 
1 149 THR n 
1 150 GLN n 
1 151 ALA n 
1 152 SER n 
1 153 SER n 
1 154 CYS n 
1 155 ILE n 
1 156 CYS n 
1 157 ASN n 
1 158 ASP n 
1 159 GLY n 
1 160 THR n 
1 161 CYS n 
1 162 TYR n 
1 163 THR n 
1 164 ILE n 
1 165 ILE n 
1 166 ALA n 
1 167 ASP n 
1 168 GLY n 
1 169 THR n 
1 170 THR n 
1 171 TYR n 
1 172 THR n 
1 173 ALA n 
1 174 SER n 
1 175 SER n 
1 176 HIS n 
1 177 ARG n 
1 178 LEU n 
1 179 TYR n 
1 180 ARG n 
1 181 LEU n 
1 182 VAL n 
1 183 ASN n 
1 184 GLY n 
1 185 THR n 
1 186 SER n 
1 187 ALA n 
1 188 GLY n 
1 189 TRP n 
1 190 LYS n 
1 191 ALA n 
1 192 LEU n 
1 193 ASP n 
1 194 THR n 
1 195 THR n 
1 196 GLY n 
1 197 PHE n 
1 198 ASN n 
1 199 PHE n 
1 200 GLU n 
1 201 PHE n 
1 202 PRO n 
1 203 THR n 
1 204 CYS n 
1 205 TYR n 
1 206 TYR n 
1 207 THR n 
1 208 SER n 
1 209 GLY n 
1 210 LYS n 
1 211 VAL n 
1 212 LYS n 
1 213 CYS n 
1 214 THR n 
1 215 GLY n 
1 216 THR n 
1 217 ASN n 
1 218 LEU n 
1 219 TRP n 
1 220 ASN n 
1 221 ASP n 
1 222 ALA n 
1 223 LYS n 
1 224 ARG n 
1 225 PRO n 
1 226 PHE n 
1 227 LEU n 
1 228 GLU n 
1 229 PHE n 
1 230 ASP n 
1 231 GLN n 
1 232 SER n 
1 233 PHE n 
1 234 THR n 
1 235 TYR n 
1 236 THR n 
1 237 PHE n 
1 238 LYS n 
1 239 GLU n 
1 240 PRO n 
1 241 CYS n 
1 242 LEU n 
1 243 GLY n 
1 244 PHE n 
1 245 LEU n 
1 246 GLY n 
1 247 ASP n 
1 248 THR n 
1 249 PRO n 
1 250 ARG n 
1 251 GLY n 
1 252 ILE n 
1 253 ASP n 
1 254 THR n 
1 255 THR n 
1 256 ASN n 
1 257 TYR n 
1 258 CYS n 
1 259 ASP n 
1 260 LYS n 
1 261 THR n 
1 262 THR n 
1 263 THR n 
1 264 GLU n 
1 265 GLY n 
1 266 GLU n 
1 267 GLY n 
1 268 GLY n 
1 269 ILE n 
1 270 GLN n 
1 271 GLY n 
1 272 PHE n 
1 273 MET n 
1 274 ILE n 
1 275 GLU n 
1 276 GLY n 
1 277 SER n 
1 278 ASN n 
1 279 SER n 
1 280 TRP n 
1 281 ILE n 
1 282 GLY n 
1 283 ARG n 
1 284 ILE n 
1 285 ILE n 
1 286 ASN n 
1 287 PRO n 
1 288 GLY n 
1 289 SER n 
1 290 LYS n 
1 291 LYS n 
1 292 GLY n 
1 293 PHE n 
1 294 GLU n 
1 295 ILE n 
1 296 TYR n 
1 297 LYS n 
1 298 PHE n 
1 299 LEU n 
1 300 GLY n 
1 301 THR n 
1 302 LEU n 
1 303 PHE n 
1 304 SER n 
1 305 VAL n 
1 306 GLN n 
1 307 THR n 
1 308 VAL n 
1 309 GLY n 
1 310 ASN n 
1 311 ARG n 
1 312 ASN n 
1 313 TYR n 
1 314 GLN n 
1 315 LEU n 
1 316 LEU n 
1 317 SER n 
1 318 ASN n 
1 319 SER n 
1 320 THR n 
1 321 ILE n 
1 322 GLY n 
1 323 ARG n 
1 324 SER n 
1 325 GLY n 
1 326 LEU n 
1 327 TYR n 
1 328 GLN n 
1 329 PRO n 
1 330 ALA n 
1 331 TYR n 
1 332 GLU n 
1 333 SER n 
1 334 ARG n 
1 335 ASP n 
1 336 CYS n 
1 337 GLN n 
1 338 GLU n 
1 339 LEU n 
1 340 CYS n 
1 341 PHE n 
1 342 TRP n 
1 343 ILE n 
1 344 GLU n 
1 345 ILE n 
1 346 ALA n 
1 347 ALA n 
1 348 THR n 
1 349 THR n 
1 350 LYS n 
1 351 ALA n 
1 352 GLY n 
1 353 LEU n 
1 354 SER n 
1 355 SER n 
1 356 ASN n 
1 357 ASP n 
1 358 LEU n 
1 359 ILE n 
1 360 THR n 
1 361 PHE n 
1 362 CYS n 
1 363 GLY n 
1 364 THR n 
1 365 GLY n 
1 366 GLY n 
1 367 SER n 
1 368 MET n 
1 369 PRO n 
1 370 ASP n 
1 371 VAL n 
1 372 ASN n 
1 373 TRP n 
1 374 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_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                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    'A/flat-faced bat/Peru/033/2010 (H18N11)' 
_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      'Influenza A virus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     11320 
_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               'cabbage looper' 
_entity_src_gen.pdbx_host_org_scientific_name      'Trichoplusia ni' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     7111 
_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          baculovirus 
_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                    PDB 
_struct_ref.db_code                    4MC7 
_struct_ref.pdbx_db_accession          4MC7 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;GSGDSGSPGIATPLVLGENLCSINGWVPTYRGEGTTGKIPDEQMLTRQNFVSCSDKECRRFFVSMGYGTTTNFADLIVSE
QMNVYSVKLGDPPTPDKLKFEAVGWSASSCHDGFQWTVLSVAGDGFVSILYGGIITDTIHPTNGGPLRTQASSCICNDGT
CYTIIADGTTYTASSHRLYRLVNGTSAGWKALDTTGFNFEFPTCYYTSGKVKCTGTNLWNDAKRPFLEFDQSFTYTFKEP
CLGFLGDTPRGIDTTNYCDKTTTEGEGGIQGFMIEGSNSWIGRIINPGSKKGFEIYKFLGTLFSVQTVGNRNYQLLSNST
IGRSGLYQPAYESRDCQELCFWIEIAATTKAGLSSNDLITFCGTGGSMPDVNWG
;
_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 4MC7 A 1 ? 374 ? 4MC7 65 ? 438 ? 65 438 
2 1 4MC7 B 1 ? 374 ? 4MC7 65 ? 438 ? 65 438 
3 1 4MC7 C 1 ? 374 ? 4MC7 65 ? 438 ? 65 438 
4 1 4MC7 D 1 ? 374 ? 4MC7 65 ? 438 ? 65 438 
# 
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 
CA  non-polymer         . 'CALCIUM ION'          ? 'Ca 2'           40.078  
CYS 'L-peptide linking' y CYSTEINE               ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE              ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'        ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE              ? 'C6 H10 N3 O2 1' 156.162 
ILE 'L-peptide linking' y ISOLEUCINE             ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                 ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE             ? 'C5 H11 N O2 S'  149.211 
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 
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          4MC7 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.35 
_exptl_crystal.density_percent_sol   63.31 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    
'0.2 mM calcium acetate, 10% PEG8000, 0.1 M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MARMOSAIC 300 mm CCD' 
_diffrn_detector.pdbx_collection_date   2012-04-27 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'double crystal Si(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 22-ID' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   22-ID 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0 
# 
_reflns.entry_id                     4MC7 
_reflns.observed_criterion_sigma_I   2 
_reflns.observed_criterion_sigma_F   2 
_reflns.d_resolution_low             44.835 
_reflns.d_resolution_high            2.99 
_reflns.number_obs                   39587 
_reflns.number_all                   39587 
_reflns.percent_possible_obs         94.5 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.99 
_reflns_shell.d_res_low              3.11 
_reflns_shell.percent_possible_all   93.0 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 4MC7 
_refine.ls_number_reflns_obs                     39587 
_refine.ls_number_reflns_all                     39587 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             44.835 
_refine.ls_d_res_high                            2.99 
_refine.ls_percent_reflns_obs                    93.58 
_refine.ls_R_factor_obs                          0.21667 
_refine.ls_R_factor_all                          0.220 
_refine.ls_R_factor_R_work                       0.21431 
_refine.ls_R_factor_R_free                       0.26009 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  2121 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.927 
_refine.correlation_coeff_Fo_to_Fc_free          0.898 
_refine.B_iso_mean                               80.133 
_refine.aniso_B[1][1]                            4.01 
_refine.aniso_B[2][2]                            -0.31 
_refine.aniso_B[3][3]                            -3.70 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.431 
_refine.overall_SU_ML                            0.338 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             42.396 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_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        11164 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         61 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               11225 
_refine_hist.d_res_high                       2.99 
_refine_hist.d_res_low                        44.835 
# 
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_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d       0.014  0.022  ? 11528 ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg    1.422  1.945  ? 15684 ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg 7.372  5.000  ? 1448  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg 31.853 24.160 ? 500   ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg 17.560 15.000 ? 1780  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg 14.965 15.000 ? 52    ? 'X-RAY DIFFRACTION' 
r_chiral_restr         0.091  0.200  ? 1712  ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined   0.006  0.021  ? 8832  ? 'X-RAY DIFFRACTION' 
# 
loop_
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.pdbx_ens_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.weight_B_iso 
1 'X-RAY DIFFRACTION' 1 1 'TIGHT POSITIONAL' A 2791 0.050  0.050 ? ? ? 
2 'X-RAY DIFFRACTION' 1 2 'TIGHT POSITIONAL' B 2791 0.060  0.050 ? ? ? 
3 'X-RAY DIFFRACTION' 1 3 'TIGHT POSITIONAL' C 2791 0.050  0.050 ? ? ? 
4 'X-RAY DIFFRACTION' 1 4 'TIGHT POSITIONAL' D 2791 0.050  0.050 ? ? ? 
5 'X-RAY DIFFRACTION' 1 1 'TIGHT THERMAL'    A 2791 11.050 0.050 ? ? ? 
6 'X-RAY DIFFRACTION' 1 2 'TIGHT THERMAL'    B 2791 12.580 0.050 ? ? ? 
7 'X-RAY DIFFRACTION' 1 3 'TIGHT THERMAL'    C 2791 10.220 0.050 ? ? ? 
8 'X-RAY DIFFRACTION' 1 4 'TIGHT THERMAL'    D 2791 10.600 0.050 ? ? ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.990 
_refine_ls_shell.d_res_low                        3.067 
_refine_ls_shell.number_reflns_R_work             2638 
_refine_ls_shell.R_factor_R_work                  0.339 
_refine_ls_shell.percent_reflns_obs               88.45 
_refine_ls_shell.R_factor_R_free                  0.426 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             111 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
1 1 A 
1 2 B 
1 3 C 
1 4 D 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.selection_details 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
1 1 1 1 A 75 A 437 ? . . . . . . . . 
1 2 1 1 B 75 B 437 ? . . . . . . . . 
1 3 1 1 C 75 C 437 ? . . . . . . . . 
1 4 1 1 D 75 D 437 ? . . . . . . . . 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                  4MC7 
_struct.title                     
'Crystal structure of a subtype N11 neuraminidase-like protein of A/flat-faced bat/Peru/033/2010 (H18N11)' 
_struct.pdbx_descriptor           NEURAMINIDASE 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4MC7 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'bat, influenza, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 3 ? 
G N N 3 ? 
H N N 2 ? 
I N N 3 ? 
J N N 2 ? 
K N N 3 ? 
L N N 2 ? 
M N N 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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  1  GLU A 33  ? THR A 36  ? GLU A 97  THR A 100 5 ? 4 
HELX_P HELX_P2  2  VAL A 78  ? GLN A 81  ? VAL A 142 GLN A 145 5 ? 4 
HELX_P HELX_P3  3  THR A 170 ? SER A 174 ? THR A 234 SER A 238 5 ? 5 
HELX_P HELX_P4  4  GLU B 33  ? THR B 36  ? GLU B 97  THR B 100 5 ? 4 
HELX_P HELX_P5  5  VAL B 78  ? GLN B 81  ? VAL B 142 GLN B 145 5 ? 4 
HELX_P HELX_P6  6  THR B 170 ? SER B 174 ? THR B 234 SER B 238 5 ? 5 
HELX_P HELX_P7  7  GLU C 33  ? THR C 36  ? GLU C 97  THR C 100 5 ? 4 
HELX_P HELX_P8  8  VAL C 78  ? GLN C 81  ? VAL C 142 GLN C 145 5 ? 4 
HELX_P HELX_P9  9  THR C 170 ? SER C 174 ? THR C 234 SER C 238 5 ? 5 
HELX_P HELX_P10 10 GLU D 33  ? THR D 36  ? GLU D 97  THR D 100 5 ? 4 
HELX_P HELX_P11 11 VAL D 78  ? GLN D 81  ? VAL D 142 GLN D 145 5 ? 4 
HELX_P HELX_P12 12 THR D 170 ? SER D 174 ? THR D 234 SER D 238 5 ? 5 
# 
_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 
disulf1  disulf ? ? A CYS 21  SG  ? ? ? 1_555 A CYS 336 SG ? ? A CYS 85  A CYS 400 1_555 ? ? ? ? ? ? ? 2.018 ? 
disulf2  disulf ? ? A CYS 53  SG  ? ? ? 1_555 A CYS 58  SG ? ? A CYS 117 A CYS 122 1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf3  disulf ? ? A CYS 110 SG  ? ? ? 1_555 A CYS 154 SG ? ? A CYS 174 A CYS 218 1_555 ? ? ? ? ? ? ? 2.052 ? 
disulf4  disulf ? ? A CYS 156 SG  ? ? ? 1_555 A CYS 161 SG ? ? A CYS 220 A CYS 225 1_555 ? ? ? ? ? ? ? 2.085 ? 
disulf5  disulf ? ? A CYS 204 SG  ? ? ? 1_555 A CYS 213 SG ? ? A CYS 268 A CYS 277 1_555 ? ? ? ? ? ? ? 2.023 ? 
disulf6  disulf ? ? A CYS 241 SG  ? ? ? 1_555 A CYS 258 SG ? ? A CYS 305 A CYS 322 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf7  disulf ? ? A CYS 340 SG  ? ? ? 1_555 A CYS 362 SG ? ? A CYS 404 A CYS 426 1_555 ? ? ? ? ? ? ? 2.071 ? 
disulf8  disulf ? ? B CYS 21  SG  ? ? ? 1_555 B CYS 336 SG ? ? B CYS 85  B CYS 400 1_555 ? ? ? ? ? ? ? 2.021 ? 
disulf9  disulf ? ? B CYS 53  SG  ? ? ? 1_555 B CYS 58  SG ? ? B CYS 117 B CYS 122 1_555 ? ? ? ? ? ? ? 2.026 ? 
disulf10 disulf ? ? B CYS 110 SG  ? ? ? 1_555 B CYS 154 SG ? ? B CYS 174 B CYS 218 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf11 disulf ? ? B CYS 156 SG  ? ? ? 1_555 B CYS 161 SG ? ? B CYS 220 B CYS 225 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf12 disulf ? ? B CYS 204 SG  ? ? ? 1_555 B CYS 213 SG ? ? B CYS 268 B CYS 277 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf13 disulf ? ? B CYS 241 SG  ? ? ? 1_555 B CYS 258 SG ? ? B CYS 305 B CYS 322 1_555 ? ? ? ? ? ? ? 2.056 ? 
disulf14 disulf ? ? B CYS 340 SG  ? ? ? 1_555 B CYS 362 SG ? ? B CYS 404 B CYS 426 1_555 ? ? ? ? ? ? ? 2.070 ? 
disulf15 disulf ? ? C CYS 21  SG  ? ? ? 1_555 C CYS 336 SG ? ? C CYS 85  C CYS 400 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf16 disulf ? ? C CYS 53  SG  ? ? ? 1_555 C CYS 58  SG ? ? C CYS 117 C CYS 122 1_555 ? ? ? ? ? ? ? 2.060 ? 
disulf17 disulf ? ? C CYS 110 SG  ? ? ? 1_555 C CYS 154 SG ? ? C CYS 174 C CYS 218 1_555 ? ? ? ? ? ? ? 2.057 ? 
disulf18 disulf ? ? C CYS 156 SG  ? ? ? 1_555 C CYS 161 SG ? ? C CYS 220 C CYS 225 1_555 ? ? ? ? ? ? ? 2.064 ? 
disulf19 disulf ? ? C CYS 204 SG  ? ? ? 1_555 C CYS 213 SG ? ? C CYS 268 C CYS 277 1_555 ? ? ? ? ? ? ? 2.086 ? 
disulf20 disulf ? ? C CYS 241 SG  ? ? ? 1_555 C CYS 258 SG ? ? C CYS 305 C CYS 322 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf21 disulf ? ? C CYS 340 SG  ? ? ? 1_555 C CYS 362 SG ? ? C CYS 404 C CYS 426 1_555 ? ? ? ? ? ? ? 2.062 ? 
disulf22 disulf ? ? D CYS 21  SG  ? ? ? 1_555 D CYS 336 SG ? ? D CYS 85  D CYS 400 1_555 ? ? ? ? ? ? ? 2.023 ? 
disulf23 disulf ? ? D CYS 53  SG  ? ? ? 1_555 D CYS 58  SG ? ? D CYS 117 D CYS 122 1_555 ? ? ? ? ? ? ? 2.032 ? 
disulf24 disulf ? ? D CYS 110 SG  ? ? ? 1_555 D CYS 154 SG ? ? D CYS 174 D CYS 218 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf25 disulf ? ? D CYS 156 SG  ? ? ? 1_555 D CYS 161 SG ? ? D CYS 220 D CYS 225 1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf26 disulf ? ? D CYS 204 SG  ? ? ? 1_555 D CYS 213 SG ? ? D CYS 268 D CYS 277 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf27 disulf ? ? D CYS 241 SG  ? ? ? 1_555 D CYS 258 SG ? ? D CYS 305 D CYS 322 1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf28 disulf ? ? D CYS 340 SG  ? ? ? 1_555 D CYS 362 SG ? ? D CYS 404 D CYS 426 1_555 ? ? ? ? ? ? ? 2.062 ? 
covale1  covale ? ? D ASN 183 ND2 ? ? ? 1_555 L NAG .   C1 ? ? D ASN 247 D NAG 501 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale2  covale ? ? B ASN 183 ND2 ? ? ? 1_555 H NAG .   C1 ? ? B ASN 247 B NAG 501 1_555 ? ? ? ? ? ? ? 1.458 ? 
covale3  covale ? ? A ASN 183 ND2 ? ? ? 1_555 E NAG .   C1 ? ? A ASN 247 A NAG 501 1_555 ? ? ? ? ? ? ? 1.471 ? 
covale4  covale ? ? C ASN 183 ND2 ? ? ? 1_555 J NAG .   C1 ? ? C ASN 247 C NAG 501 1_555 ? ? ? ? ? ? ? 1.488 ? 
metalc1  metalc ? ? D ASP 96  OD2 ? ? ? 1_555 G CA  .   CA ? ? D ASP 160 A CA  503 1_555 ? ? ? ? ? ? ? 2.058 ? 
metalc2  metalc ? ? A ASP 96  OD2 ? ? ? 1_555 G CA  .   CA ? ? A ASP 160 A CA  503 1_555 ? ? ? ? ? ? ? 2.108 ? 
metalc3  metalc ? ? B ASP 96  OD2 ? ? ? 1_555 G CA  .   CA ? ? B ASP 160 A CA  503 1_555 ? ? ? ? ? ? ? 2.141 ? 
metalc4  metalc ? ? C ASP 96  OD2 ? ? ? 1_555 G CA  .   CA ? ? C ASP 160 A CA  503 1_555 ? ? ? ? ? ? ? 2.185 ? 
metalc5  metalc ? ? C GLY 265 O   ? ? ? 1_555 K CA  .   CA ? ? C GLY 329 C CA  502 1_555 ? ? ? ? ? ? ? 2.256 ? 
metalc6  metalc ? ? B GLY 267 O   ? ? ? 1_555 I CA  .   CA ? ? B GLY 331 B CA  502 1_555 ? ? ? ? ? ? ? 2.263 ? 
metalc7  metalc ? ? A GLY 267 O   ? ? ? 1_555 F CA  .   CA ? ? A GLY 331 A CA  502 1_555 ? ? ? ? ? ? ? 2.317 ? 
metalc8  metalc ? ? A GLY 265 O   ? ? ? 1_555 F CA  .   CA ? ? A GLY 329 A CA  502 1_555 ? ? ? ? ? ? ? 2.320 ? 
metalc9  metalc ? ? C ASN 217 O   ? ? ? 1_555 K CA  .   CA ? ? C ASN 281 C CA  502 1_555 ? ? ? ? ? ? ? 2.355 ? 
metalc10 metalc ? ? D GLY 267 O   ? ? ? 1_555 M CA  .   CA ? ? D GLY 331 D CA  502 1_555 ? ? ? ? ? ? ? 2.362 ? 
metalc11 metalc ? ? C GLY 267 O   ? ? ? 1_555 K CA  .   CA ? ? C GLY 331 C CA  502 1_555 ? ? ? ? ? ? ? 2.394 ? 
metalc12 metalc ? ? D GLY 265 O   ? ? ? 1_555 M CA  .   CA ? ? D GLY 329 D CA  502 1_555 ? ? ? ? ? ? ? 2.409 ? 
metalc13 metalc ? ? C ASP 221 O   ? ? ? 1_555 K CA  .   CA ? ? C ASP 285 C CA  502 1_555 ? ? ? ? ? ? ? 2.429 ? 
metalc14 metalc ? ? A ASP 221 O   ? ? ? 1_555 F CA  .   CA ? ? A ASP 285 A CA  502 1_555 ? ? ? ? ? ? ? 2.440 ? 
metalc15 metalc ? ? B GLY 265 O   ? ? ? 1_555 I CA  .   CA ? ? B GLY 329 B CA  502 1_555 ? ? ? ? ? ? ? 2.448 ? 
metalc16 metalc ? ? D ASP 221 O   ? ? ? 1_555 M CA  .   CA ? ? D ASP 285 D CA  502 1_555 ? ? ? ? ? ? ? 2.458 ? 
metalc17 metalc ? ? A ASN 217 O   ? ? ? 1_555 F CA  .   CA ? ? A ASN 281 A CA  502 1_555 ? ? ? ? ? ? ? 2.615 ? 
metalc18 metalc ? ? B ASN 217 O   ? ? ? 1_555 I CA  .   CA ? ? B ASN 281 B CA  502 1_555 ? ? ? ? ? ? ? 2.615 ? 
metalc19 metalc ? ? B ASP 221 O   ? ? ? 1_555 I CA  .   CA ? ? B ASP 285 B CA  502 1_555 ? ? ? ? ? ? ? 2.627 ? 
metalc20 metalc ? ? D ASN 217 O   ? ? ? 1_555 M CA  .   CA ? ? D ASN 281 D CA  502 1_555 ? ? ? ? ? ? ? 2.658 ? 
metalc21 metalc ? ? C ASP 247 OD2 ? ? ? 1_555 K CA  .   CA ? ? C ASP 311 C CA  502 1_555 ? ? ? ? ? ? ? 2.738 ? 
metalc22 metalc ? ? D ASP 247 OD2 ? ? ? 1_555 M CA  .   CA ? ? D ASP 311 D CA  502 1_555 ? ? ? ? ? ? ? 2.774 ? 
metalc23 metalc ? ? A ASP 247 OD2 ? ? ? 1_555 F CA  .   CA ? ? A ASP 311 A CA  502 1_555 ? ? ? ? ? ? ? 2.806 ? 
metalc24 metalc ? ? B ASP 247 OD2 ? ? ? 1_555 I CA  .   CA ? ? B ASP 311 B CA  502 1_555 ? ? ? ? ? ? ? 2.809 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 THR 248 A . ? THR 312 A PRO 249 A ? PRO 313 A 1 3.64 
2 THR 248 B . ? THR 312 B PRO 249 B ? PRO 313 B 1 6.39 
3 THR 248 C . ? THR 312 C PRO 249 C ? PRO 313 C 1 4.32 
4 THR 248 D . ? THR 312 D PRO 249 D ? PRO 313 D 1 5.05 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 2 ? 
B ? 7 ? 
C ? 4 ? 
D ? 4 ? 
E ? 4 ? 
F ? 4 ? 
G ? 2 ? 
H ? 7 ? 
I ? 4 ? 
J ? 4 ? 
K ? 4 ? 
L ? 4 ? 
M ? 2 ? 
N ? 7 ? 
O ? 4 ? 
P ? 4 ? 
Q ? 4 ? 
R ? 4 ? 
S ? 2 ? 
T ? 7 ? 
U ? 4 ? 
V ? 4 ? 
W ? 4 ? 
X ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? parallel      
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
B 4 5 ? anti-parallel 
B 5 6 ? anti-parallel 
B 6 7 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? parallel      
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
H 4 5 ? anti-parallel 
H 5 6 ? anti-parallel 
H 6 7 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
K 1 2 ? anti-parallel 
K 2 3 ? anti-parallel 
K 3 4 ? anti-parallel 
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
M 1 2 ? parallel      
N 1 2 ? anti-parallel 
N 2 3 ? anti-parallel 
N 3 4 ? anti-parallel 
N 4 5 ? anti-parallel 
N 5 6 ? anti-parallel 
N 6 7 ? anti-parallel 
O 1 2 ? anti-parallel 
O 2 3 ? anti-parallel 
O 3 4 ? anti-parallel 
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? anti-parallel 
Q 1 2 ? anti-parallel 
Q 2 3 ? anti-parallel 
Q 3 4 ? anti-parallel 
R 1 2 ? anti-parallel 
R 2 3 ? anti-parallel 
R 3 4 ? anti-parallel 
S 1 2 ? parallel      
T 1 2 ? anti-parallel 
T 2 3 ? anti-parallel 
T 3 4 ? anti-parallel 
T 4 5 ? anti-parallel 
T 5 6 ? anti-parallel 
T 6 7 ? anti-parallel 
U 1 2 ? anti-parallel 
U 2 3 ? anti-parallel 
U 3 4 ? anti-parallel 
V 1 2 ? anti-parallel 
V 2 3 ? anti-parallel 
V 3 4 ? anti-parallel 
W 1 2 ? anti-parallel 
W 2 3 ? anti-parallel 
W 3 4 ? anti-parallel 
X 1 2 ? anti-parallel 
X 2 3 ? anti-parallel 
X 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ASN A 19  ? LEU A 20  ? ASN A 83  LEU A 84  
A 2 CYS A 336 ? GLN A 337 ? CYS A 400 GLN A 401 
B 1 GLY A 25  ? ARG A 31  ? GLY A 89  ARG A 95  
B 2 ASN A 356 ? THR A 364 ? ASN A 420 THR A 428 
B 3 CYS A 340 ? ALA A 346 ? CYS A 404 ALA A 410 
B 4 GLY A 309 ? TYR A 327 ? GLY A 373 TYR A 391 
B 5 LYS A 291 ? LEU A 299 ? LYS A 355 LEU A 363 
B 6 ASN A 278 ? ASN A 286 ? ASN A 342 ASN A 350 
B 7 MET A 273 ? ILE A 274 ? MET A 337 ILE A 338 
C 1 MET A 44  ? CYS A 53  ? MET A 108 CYS A 117 
C 2 CYS A 58  ? TYR A 67  ? CYS A 122 TYR A 131 
C 3 ASN A 83  ? LYS A 88  ? ASN A 147 LYS A 152 
C 4 LYS A 99  ? VAL A 103 ? LYS A 163 VAL A 167 
D 1 SER A 106 ? HIS A 111 ? SER A 170 HIS A 175 
D 2 TRP A 116 ? ALA A 122 ? TRP A 180 ALA A 186 
D 3 PHE A 126 ? TYR A 131 ? PHE A 190 TYR A 195 
D 4 ILE A 134 ? ILE A 139 ? ILE A 198 ILE A 203 
E 1 ILE A 155 ? ASN A 157 ? ILE A 219 ASN A 221 
E 2 THR A 160 ? ASP A 167 ? THR A 224 ASP A 231 
E 3 SER A 175 ? VAL A 182 ? SER A 239 VAL A 246 
E 4 THR A 185 ? LEU A 192 ? THR A 249 LEU A 256 
F 1 GLU A 200 ? THR A 207 ? GLU A 264 THR A 271 
F 2 LYS A 210 ? THR A 216 ? LYS A 274 THR A 280 
F 3 PHE A 226 ? PHE A 229 ? PHE A 290 PHE A 293 
F 4 TYR A 235 ? LYS A 238 ? TYR A 299 LYS A 302 
G 1 ASN B 19  ? LEU B 20  ? ASN B 83  LEU B 84  
G 2 CYS B 336 ? GLN B 337 ? CYS B 400 GLN B 401 
H 1 GLY B 25  ? ARG B 31  ? GLY B 89  ARG B 95  
H 2 ASN B 356 ? THR B 364 ? ASN B 420 THR B 428 
H 3 CYS B 340 ? ALA B 346 ? CYS B 404 ALA B 410 
H 4 GLY B 309 ? TYR B 327 ? GLY B 373 TYR B 391 
H 5 LYS B 291 ? LEU B 299 ? LYS B 355 LEU B 363 
H 6 ASN B 278 ? ASN B 286 ? ASN B 342 ASN B 350 
H 7 MET B 273 ? ILE B 274 ? MET B 337 ILE B 338 
I 1 MET B 44  ? CYS B 53  ? MET B 108 CYS B 117 
I 2 CYS B 58  ? TYR B 67  ? CYS B 122 TYR B 131 
I 3 ASN B 83  ? LYS B 88  ? ASN B 147 LYS B 152 
I 4 LYS B 99  ? VAL B 103 ? LYS B 163 VAL B 167 
J 1 SER B 106 ? HIS B 111 ? SER B 170 HIS B 175 
J 2 TRP B 116 ? ALA B 122 ? TRP B 180 ALA B 186 
J 3 PHE B 126 ? TYR B 131 ? PHE B 190 TYR B 195 
J 4 ILE B 134 ? ILE B 139 ? ILE B 198 ILE B 203 
K 1 ILE B 155 ? ASN B 157 ? ILE B 219 ASN B 221 
K 2 THR B 160 ? ASP B 167 ? THR B 224 ASP B 231 
K 3 SER B 175 ? VAL B 182 ? SER B 239 VAL B 246 
K 4 THR B 185 ? LEU B 192 ? THR B 249 LEU B 256 
L 1 GLU B 200 ? THR B 207 ? GLU B 264 THR B 271 
L 2 LYS B 210 ? THR B 216 ? LYS B 274 THR B 280 
L 3 PHE B 226 ? PHE B 229 ? PHE B 290 PHE B 293 
L 4 TYR B 235 ? LYS B 238 ? TYR B 299 LYS B 302 
M 1 ASN C 19  ? LEU C 20  ? ASN C 83  LEU C 84  
M 2 CYS C 336 ? GLN C 337 ? CYS C 400 GLN C 401 
N 1 GLY C 25  ? ARG C 31  ? GLY C 89  ARG C 95  
N 2 ASN C 356 ? THR C 364 ? ASN C 420 THR C 428 
N 3 CYS C 340 ? ALA C 346 ? CYS C 404 ALA C 410 
N 4 GLY C 309 ? TYR C 327 ? GLY C 373 TYR C 391 
N 5 LYS C 291 ? LEU C 299 ? LYS C 355 LEU C 363 
N 6 ASN C 278 ? ASN C 286 ? ASN C 342 ASN C 350 
N 7 MET C 273 ? ILE C 274 ? MET C 337 ILE C 338 
O 1 MET C 44  ? CYS C 53  ? MET C 108 CYS C 117 
O 2 CYS C 58  ? TYR C 67  ? CYS C 122 TYR C 131 
O 3 ASN C 83  ? LYS C 88  ? ASN C 147 LYS C 152 
O 4 LYS C 99  ? VAL C 103 ? LYS C 163 VAL C 167 
P 1 SER C 106 ? HIS C 111 ? SER C 170 HIS C 175 
P 2 TRP C 116 ? ALA C 122 ? TRP C 180 ALA C 186 
P 3 PHE C 126 ? TYR C 131 ? PHE C 190 TYR C 195 
P 4 ILE C 134 ? ILE C 139 ? ILE C 198 ILE C 203 
Q 1 ILE C 155 ? ASN C 157 ? ILE C 219 ASN C 221 
Q 2 THR C 160 ? ASP C 167 ? THR C 224 ASP C 231 
Q 3 SER C 175 ? VAL C 182 ? SER C 239 VAL C 246 
Q 4 THR C 185 ? LEU C 192 ? THR C 249 LEU C 256 
R 1 GLU C 200 ? THR C 207 ? GLU C 264 THR C 271 
R 2 LYS C 210 ? THR C 216 ? LYS C 274 THR C 280 
R 3 PHE C 226 ? PHE C 229 ? PHE C 290 PHE C 293 
R 4 TYR C 235 ? LYS C 238 ? TYR C 299 LYS C 302 
S 1 ASN D 19  ? LEU D 20  ? ASN D 83  LEU D 84  
S 2 CYS D 336 ? GLN D 337 ? CYS D 400 GLN D 401 
T 1 GLY D 25  ? ARG D 31  ? GLY D 89  ARG D 95  
T 2 ASN D 356 ? THR D 364 ? ASN D 420 THR D 428 
T 3 CYS D 340 ? ALA D 346 ? CYS D 404 ALA D 410 
T 4 GLY D 309 ? TYR D 327 ? GLY D 373 TYR D 391 
T 5 LYS D 291 ? LEU D 299 ? LYS D 355 LEU D 363 
T 6 ASN D 278 ? ASN D 286 ? ASN D 342 ASN D 350 
T 7 MET D 273 ? ILE D 274 ? MET D 337 ILE D 338 
U 1 MET D 44  ? CYS D 53  ? MET D 108 CYS D 117 
U 2 CYS D 58  ? TYR D 67  ? CYS D 122 TYR D 131 
U 3 ASN D 83  ? LYS D 88  ? ASN D 147 LYS D 152 
U 4 LYS D 99  ? VAL D 103 ? LYS D 163 VAL D 167 
V 1 SER D 106 ? HIS D 111 ? SER D 170 HIS D 175 
V 2 TRP D 116 ? ALA D 122 ? TRP D 180 ALA D 186 
V 3 PHE D 126 ? TYR D 131 ? PHE D 190 TYR D 195 
V 4 ILE D 134 ? ILE D 139 ? ILE D 198 ILE D 203 
W 1 ILE D 155 ? ASN D 157 ? ILE D 219 ASN D 221 
W 2 THR D 160 ? ASP D 167 ? THR D 224 ASP D 231 
W 3 SER D 175 ? VAL D 182 ? SER D 239 VAL D 246 
W 4 THR D 185 ? LEU D 192 ? THR D 249 LEU D 256 
X 1 GLU D 200 ? THR D 207 ? GLU D 264 THR D 271 
X 2 LYS D 210 ? THR D 216 ? LYS D 274 THR D 280 
X 3 PHE D 226 ? PHE D 229 ? PHE D 290 PHE D 293 
X 4 TYR D 235 ? LYS D 238 ? TYR D 299 LYS D 302 
# 
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 
A 1 2 N ASN A 19  ? N ASN A 83  O GLN A 337 ? O GLN A 401 
B 1 2 N VAL A 27  ? N VAL A 91  O CYS A 362 ? O CYS A 426 
B 2 3 O ASP A 357 ? O ASP A 421 N ILE A 345 ? N ILE A 409 
B 3 4 O GLU A 344 ? O GLU A 408 N ARG A 323 ? N ARG A 387 
B 4 5 O TYR A 313 ? O TYR A 377 N ILE A 295 ? N ILE A 359 
B 5 6 O GLU A 294 ? O GLU A 358 N ARG A 283 ? N ARG A 347 
B 6 7 O TRP A 280 ? O TRP A 344 N ILE A 274 ? N ILE A 338 
C 1 2 N SER A 52  ? N SER A 116 O ARG A 59  ? O ARG A 123 
C 2 3 N SER A 64  ? N SER A 128 O ASN A 83  ? O ASN A 147 
C 3 4 N VAL A 84  ? N VAL A 148 O ALA A 102 ? O ALA A 166 
D 1 2 N SER A 108 ? N SER A 172 O LEU A 119 ? O LEU A 183 
D 2 3 N VAL A 118 ? N VAL A 182 O LEU A 130 ? O LEU A 194 
D 3 4 N ILE A 129 ? N ILE A 193 O ASP A 137 ? O ASP A 201 
E 1 2 N ILE A 155 ? N ILE A 219 O TYR A 162 ? O TYR A 226 
E 2 3 N CYS A 161 ? N CYS A 225 O LEU A 181 ? O LEU A 245 
E 3 4 N ARG A 180 ? N ARG A 244 O ALA A 187 ? O ALA A 251 
F 1 2 N THR A 203 ? N THR A 267 O THR A 214 ? O THR A 278 
F 2 3 N VAL A 211 ? N VAL A 275 O PHE A 229 ? O PHE A 293 
F 3 4 N PHE A 226 ? N PHE A 290 O LYS A 238 ? O LYS A 302 
G 1 2 N ASN B 19  ? N ASN B 83  O GLN B 337 ? O GLN B 401 
H 1 2 N VAL B 27  ? N VAL B 91  O CYS B 362 ? O CYS B 426 
H 2 3 O PHE B 361 ? O PHE B 425 N PHE B 341 ? N PHE B 405 
H 3 4 O GLU B 344 ? O GLU B 408 N ARG B 323 ? N ARG B 387 
H 4 5 O ARG B 311 ? O ARG B 375 N LYS B 297 ? N LYS B 361 
H 5 6 O PHE B 298 ? O PHE B 362 N SER B 279 ? N SER B 343 
H 6 7 O TRP B 280 ? O TRP B 344 N ILE B 274 ? N ILE B 338 
I 1 2 N LEU B 45  ? N LEU B 109 O GLY B 66  ? O GLY B 130 
I 2 3 N ARG B 60  ? N ARG B 124 O VAL B 87  ? O VAL B 151 
I 3 4 N VAL B 84  ? N VAL B 148 O ALA B 102 ? O ALA B 166 
J 1 2 N SER B 108 ? N SER B 172 O LEU B 119 ? O LEU B 183 
J 2 3 N VAL B 118 ? N VAL B 182 O LEU B 130 ? O LEU B 194 
J 3 4 N ILE B 129 ? N ILE B 193 O ASP B 137 ? O ASP B 201 
K 1 2 N ILE B 155 ? N ILE B 219 O TYR B 162 ? O TYR B 226 
K 2 3 N CYS B 161 ? N CYS B 225 O LEU B 181 ? O LEU B 245 
K 3 4 N ARG B 180 ? N ARG B 244 O ALA B 187 ? O ALA B 251 
L 1 2 N TYR B 205 ? N TYR B 269 O LYS B 212 ? O LYS B 276 
L 2 3 N VAL B 211 ? N VAL B 275 O PHE B 229 ? O PHE B 293 
L 3 4 N PHE B 226 ? N PHE B 290 O LYS B 238 ? O LYS B 302 
M 1 2 N ASN C 19  ? N ASN C 83  O GLN C 337 ? O GLN C 401 
N 1 2 N VAL C 27  ? N VAL C 91  O CYS C 362 ? O CYS C 426 
N 2 3 O ASP C 357 ? O ASP C 421 N ILE C 345 ? N ILE C 409 
N 3 4 O GLU C 344 ? O GLU C 408 N ARG C 323 ? N ARG C 387 
N 4 5 O ARG C 311 ? O ARG C 375 N LYS C 297 ? N LYS C 361 
N 5 6 O GLU C 294 ? O GLU C 358 N ARG C 283 ? N ARG C 347 
N 6 7 O TRP C 280 ? O TRP C 344 N ILE C 274 ? N ILE C 338 
O 1 2 N ARG C 47  ? N ARG C 111 O VAL C 63  ? O VAL C 127 
O 2 3 N SER C 64  ? N SER C 128 O ASN C 83  ? O ASN C 147 
O 3 4 N VAL C 84  ? N VAL C 148 O ALA C 102 ? O ALA C 166 
P 1 2 N SER C 108 ? N SER C 172 O LEU C 119 ? O LEU C 183 
P 2 3 N VAL C 118 ? N VAL C 182 O LEU C 130 ? O LEU C 194 
P 3 4 N VAL C 127 ? N VAL C 191 O ILE C 139 ? O ILE C 203 
Q 1 2 N ILE C 155 ? N ILE C 219 O TYR C 162 ? O TYR C 226 
Q 2 3 N CYS C 161 ? N CYS C 225 O LEU C 181 ? O LEU C 245 
Q 3 4 N ARG C 180 ? N ARG C 244 O ALA C 187 ? O ALA C 251 
R 1 2 N THR C 203 ? N THR C 267 O THR C 214 ? O THR C 278 
R 2 3 N VAL C 211 ? N VAL C 275 O PHE C 229 ? O PHE C 293 
R 3 4 N PHE C 226 ? N PHE C 290 O LYS C 238 ? O LYS C 302 
S 1 2 N ASN D 19  ? N ASN D 83  O GLN D 337 ? O GLN D 401 
T 1 2 N VAL D 27  ? N VAL D 91  O CYS D 362 ? O CYS D 426 
T 2 3 O ASP D 357 ? O ASP D 421 N ILE D 345 ? N ILE D 409 
T 3 4 O GLU D 344 ? O GLU D 408 N ARG D 323 ? N ARG D 387 
T 4 5 O ARG D 311 ? O ARG D 375 N LYS D 297 ? N LYS D 361 
T 5 6 O GLU D 294 ? O GLU D 358 N ARG D 283 ? N ARG D 347 
T 6 7 O TRP D 280 ? O TRP D 344 N ILE D 274 ? N ILE D 338 
U 1 2 N ARG D 47  ? N ARG D 111 O VAL D 63  ? O VAL D 127 
U 2 3 N SER D 64  ? N SER D 128 O ASN D 83  ? O ASN D 147 
U 3 4 N VAL D 84  ? N VAL D 148 O ALA D 102 ? O ALA D 166 
V 1 2 N SER D 108 ? N SER D 172 O LEU D 119 ? O LEU D 183 
V 2 3 N VAL D 118 ? N VAL D 182 O LEU D 130 ? O LEU D 194 
V 3 4 N ILE D 129 ? N ILE D 193 O ASP D 137 ? O ASP D 201 
W 1 2 N ILE D 155 ? N ILE D 219 O TYR D 162 ? O TYR D 226 
W 2 3 N CYS D 161 ? N CYS D 225 O LEU D 181 ? O LEU D 245 
W 3 4 N ARG D 180 ? N ARG D 244 O ALA D 187 ? O ALA D 251 
X 1 2 N THR D 203 ? N THR D 267 O THR D 214 ? O THR D 278 
X 2 3 N VAL D 211 ? N VAL D 275 O PHE D 229 ? O PHE D 293 
X 3 4 N PHE D 226 ? N PHE D 290 O LYS D 238 ? O LYS D 302 
# 
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 ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA A 502'                             
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CA A 503'                             
AC3 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA B 502'                             
AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA C 502'                             
AC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CA D 502'                             
AC6 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG A 501 BOUND TO ASN A 247' 
AC7 Software ? ? ? ? 3 'BINDING SITE FOR MONO-SACCHARIDE NAG B 501 BOUND TO ASN B 247' 
AC8 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG C 501 BOUND TO ASN C 247' 
AC9 Software ? ? ? ? 2 'BINDING SITE FOR MONO-SACCHARIDE NAG D 501 BOUND TO ASN D 247' 
# 
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 5 ASN A 217 ? ASN A 281 . ? 1_555 ? 
2  AC1 5 ASP A 221 ? ASP A 285 . ? 1_555 ? 
3  AC1 5 ASP A 247 ? ASP A 311 . ? 1_555 ? 
4  AC1 5 GLY A 265 ? GLY A 329 . ? 1_555 ? 
5  AC1 5 GLY A 267 ? GLY A 331 . ? 1_555 ? 
6  AC2 4 ASP A 96  ? ASP A 160 . ? 1_555 ? 
7  AC2 4 ASP B 96  ? ASP B 160 . ? 1_555 ? 
8  AC2 4 ASP C 96  ? ASP C 160 . ? 1_555 ? 
9  AC2 4 ASP D 96  ? ASP D 160 . ? 1_555 ? 
10 AC3 5 ASN B 217 ? ASN B 281 . ? 1_555 ? 
11 AC3 5 ASP B 221 ? ASP B 285 . ? 1_555 ? 
12 AC3 5 ASP B 247 ? ASP B 311 . ? 1_555 ? 
13 AC3 5 GLY B 265 ? GLY B 329 . ? 1_555 ? 
14 AC3 5 GLY B 267 ? GLY B 331 . ? 1_555 ? 
15 AC4 5 ASN C 217 ? ASN C 281 . ? 1_555 ? 
16 AC4 5 ASP C 221 ? ASP C 285 . ? 1_555 ? 
17 AC4 5 ASP C 247 ? ASP C 311 . ? 1_555 ? 
18 AC4 5 GLY C 265 ? GLY C 329 . ? 1_555 ? 
19 AC4 5 GLY C 267 ? GLY C 331 . ? 1_555 ? 
20 AC5 5 ASN D 217 ? ASN D 281 . ? 1_555 ? 
21 AC5 5 ASP D 221 ? ASP D 285 . ? 1_555 ? 
22 AC5 5 ASP D 247 ? ASP D 311 . ? 1_555 ? 
23 AC5 5 GLY D 265 ? GLY D 329 . ? 1_555 ? 
24 AC5 5 GLY D 267 ? GLY D 331 . ? 1_555 ? 
25 AC6 2 PHE A 114 ? PHE A 178 . ? 1_555 ? 
26 AC6 2 ASN A 183 ? ASN A 247 . ? 1_555 ? 
27 AC7 3 PHE B 114 ? PHE B 178 . ? 1_555 ? 
28 AC7 3 VAL B 182 ? VAL B 246 . ? 1_555 ? 
29 AC7 3 ASN B 183 ? ASN B 247 . ? 1_555 ? 
30 AC8 2 PHE C 114 ? PHE C 178 . ? 1_555 ? 
31 AC8 2 ASN C 183 ? ASN C 247 . ? 1_555 ? 
32 AC9 2 PHE D 114 ? PHE D 178 . ? 1_555 ? 
33 AC9 2 ASN D 183 ? ASN D 247 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4MC7 
_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                    4MC7 
_atom_sites.fract_transf_matrix[1][1]   0.008105 
_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]   0.006084 
_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]   0.004653 
_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  
CA 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . ALA A 1 11  ? 63.280 47.668 67.702  1.00 68.44  ? 75  ALA A N   1 
ATOM   2     C  CA  . ALA A 1 11  ? 63.357 46.354 68.429  1.00 87.97  ? 75  ALA A CA  1 
ATOM   3     C  C   . ALA A 1 11  ? 64.777 45.758 68.468  1.00 102.21 ? 75  ALA A C   1 
ATOM   4     O  O   . ALA A 1 11  ? 65.558 45.893 67.532  1.00 79.16  ? 75  ALA A O   1 
ATOM   5     C  CB  . ALA A 1 11  ? 62.350 45.329 67.867  1.00 52.76  ? 75  ALA A CB  1 
ATOM   6     N  N   . THR A 1 12  ? 65.090 45.085 69.568  1.00 126.51 ? 76  THR A N   1 
ATOM   7     C  CA  . THR A 1 12  ? 66.434 44.587 69.825  1.00 106.56 ? 76  THR A CA  1 
ATOM   8     C  C   . THR A 1 12  ? 66.347 43.132 70.233  1.00 81.57  ? 76  THR A C   1 
ATOM   9     O  O   . THR A 1 12  ? 65.474 42.775 71.024  1.00 99.43  ? 76  THR A O   1 
ATOM   10    C  CB  . THR A 1 12  ? 67.095 45.402 70.965  1.00 124.36 ? 76  THR A CB  1 
ATOM   11    O  OG1 . THR A 1 12  ? 67.166 46.775 70.571  1.00 131.19 ? 76  THR A OG1 1 
ATOM   12    C  CG2 . THR A 1 12  ? 68.511 44.894 71.300  1.00 120.43 ? 76  THR A CG2 1 
ATOM   13    N  N   . PRO A 1 13  ? 67.263 42.290 69.717  1.00 76.81  ? 77  PRO A N   1 
ATOM   14    C  CA  . PRO A 1 13  ? 67.309 40.864 70.094  1.00 70.56  ? 77  PRO A CA  1 
ATOM   15    C  C   . PRO A 1 13  ? 67.224 40.669 71.603  1.00 76.09  ? 77  PRO A C   1 
ATOM   16    O  O   . PRO A 1 13  ? 67.971 41.308 72.357  1.00 91.01  ? 77  PRO A O   1 
ATOM   17    C  CB  . PRO A 1 13  ? 68.679 40.406 69.597  1.00 58.79  ? 77  PRO A CB  1 
ATOM   18    C  CG  . PRO A 1 13  ? 69.002 41.323 68.473  1.00 66.19  ? 77  PRO A CG  1 
ATOM   19    C  CD  . PRO A 1 13  ? 68.366 42.655 68.809  1.00 75.87  ? 77  PRO A CD  1 
ATOM   20    N  N   . LEU A 1 14  ? 66.303 39.810 72.031  1.00 73.24  ? 78  LEU A N   1 
ATOM   21    C  CA  . LEU A 1 14  ? 66.135 39.503 73.438  1.00 73.16  ? 78  LEU A CA  1 
ATOM   22    C  C   . LEU A 1 14  ? 67.413 38.918 74.030  1.00 80.22  ? 78  LEU A C   1 
ATOM   23    O  O   . LEU A 1 14  ? 67.917 37.894 73.568  1.00 79.71  ? 78  LEU A O   1 
ATOM   24    C  CB  . LEU A 1 14  ? 64.971 38.540 73.657  1.00 78.69  ? 78  LEU A CB  1 
ATOM   25    C  CG  . LEU A 1 14  ? 64.665 38.270 75.136  1.00 92.53  ? 78  LEU A CG  1 
ATOM   26    C  CD1 . LEU A 1 14  ? 63.907 39.440 75.735  1.00 129.56 ? 78  LEU A CD1 1 
ATOM   27    C  CD2 . LEU A 1 14  ? 63.882 37.003 75.331  1.00 111.81 ? 78  LEU A CD2 1 
ATOM   28    N  N   . VAL A 1 15  ? 67.934 39.607 75.040  1.00 94.52  ? 79  VAL A N   1 
ATOM   29    C  CA  . VAL A 1 15  ? 69.098 39.161 75.797  1.00 84.23  ? 79  VAL A CA  1 
ATOM   30    C  C   . VAL A 1 15  ? 68.645 38.889 77.219  1.00 88.91  ? 79  VAL A C   1 
ATOM   31    O  O   . VAL A 1 15  ? 67.990 39.727 77.848  1.00 100.83 ? 79  VAL A O   1 
ATOM   32    C  CB  . VAL A 1 15  ? 70.244 40.219 75.773  1.00 69.87  ? 79  VAL A CB  1 
ATOM   33    C  CG1 . VAL A 1 15  ? 70.967 40.323 77.130  1.00 75.51  ? 79  VAL A CG1 1 
ATOM   34    C  CG2 . VAL A 1 15  ? 71.231 39.934 74.649  1.00 49.73  ? 79  VAL A CG2 1 
ATOM   35    N  N   . LEU A 1 16  ? 68.979 37.707 77.717  1.00 86.05  ? 80  LEU A N   1 
ATOM   36    C  CA  . LEU A 1 16  ? 68.660 37.362 79.088  1.00 82.64  ? 80  LEU A CA  1 
ATOM   37    C  C   . LEU A 1 16  ? 69.857 37.639 79.989  1.00 81.43  ? 80  LEU A C   1 
ATOM   38    O  O   . LEU A 1 16  ? 71.020 37.596 79.526  1.00 75.79  ? 80  LEU A O   1 
ATOM   39    C  CB  . LEU A 1 16  ? 68.226 35.892 79.177  1.00 77.66  ? 80  LEU A CB  1 
ATOM   40    C  CG  . LEU A 1 16  ? 66.877 35.572 78.539  1.00 80.29  ? 80  LEU A CG  1 
ATOM   41    C  CD1 . LEU A 1 16  ? 66.723 34.087 78.378  1.00 108.66 ? 80  LEU A CD1 1 
ATOM   42    C  CD2 . LEU A 1 16  ? 65.705 36.161 79.339  1.00 87.50  ? 80  LEU A CD2 1 
ATOM   43    N  N   . GLY A 1 17  ? 69.566 37.929 81.263  1.00 64.52  ? 81  GLY A N   1 
ATOM   44    C  CA  . GLY A 1 17  ? 70.612 38.073 82.292  1.00 77.81  ? 81  GLY A CA  1 
ATOM   45    C  C   . GLY A 1 17  ? 71.436 36.807 82.547  1.00 76.18  ? 81  GLY A C   1 
ATOM   46    O  O   . GLY A 1 17  ? 70.901 35.680 82.652  1.00 61.46  ? 81  GLY A O   1 
ATOM   47    N  N   . GLU A 1 18  ? 72.748 36.987 82.649  1.00 79.81  ? 82  GLU A N   1 
ATOM   48    C  CA  . GLU A 1 18  ? 73.643 35.855 82.836  1.00 80.71  ? 82  GLU A CA  1 
ATOM   49    C  C   . GLU A 1 18  ? 73.533 35.305 84.254  1.00 86.67  ? 82  GLU A C   1 
ATOM   50    O  O   . GLU A 1 18  ? 73.660 34.091 84.477  1.00 92.82  ? 82  GLU A O   1 
ATOM   51    C  CB  . GLU A 1 18  ? 75.078 36.248 82.511  1.00 68.85  ? 82  GLU A CB  1 
ATOM   52    C  CG  . GLU A 1 18  ? 75.840 35.163 81.763  1.00 99.87  ? 82  GLU A CG  1 
ATOM   53    C  CD  . GLU A 1 18  ? 75.337 34.945 80.339  1.00 118.09 ? 82  GLU A CD  1 
ATOM   54    O  OE1 . GLU A 1 18  ? 74.719 35.862 79.738  1.00 114.19 ? 82  GLU A OE1 1 
ATOM   55    O  OE2 . GLU A 1 18  ? 75.573 33.840 79.818  1.00 132.64 ? 82  GLU A OE2 1 
ATOM   56    N  N   . ASN A 1 19  ? 73.257 36.206 85.197  1.00 80.11  ? 83  ASN A N   1 
ATOM   57    C  CA  . ASN A 1 19  ? 73.176 35.857 86.601  1.00 78.79  ? 83  ASN A CA  1 
ATOM   58    C  C   . ASN A 1 19  ? 71.747 35.797 87.126  1.00 75.25  ? 83  ASN A C   1 
ATOM   59    O  O   . ASN A 1 19  ? 70.966 36.709 86.898  1.00 71.05  ? 83  ASN A O   1 
ATOM   60    C  CB  . ASN A 1 19  ? 74.040 36.818 87.416  1.00 91.16  ? 83  ASN A CB  1 
ATOM   61    C  CG  . ASN A 1 19  ? 75.528 36.641 87.124  1.00 116.82 ? 83  ASN A CG  1 
ATOM   62    O  OD1 . ASN A 1 19  ? 75.998 35.539 86.802  1.00 115.54 ? 83  ASN A OD1 1 
ATOM   63    N  ND2 . ASN A 1 19  ? 76.274 37.728 87.231  1.00 116.13 ? 83  ASN A ND2 1 
ATOM   64    N  N   . LEU A 1 20  ? 71.416 34.709 87.818  1.00 70.97  ? 84  LEU A N   1 
ATOM   65    C  CA  . LEU A 1 20  ? 70.094 34.516 88.372  1.00 52.87  ? 84  LEU A CA  1 
ATOM   66    C  C   . LEU A 1 20  ? 69.880 35.276 89.695  1.00 61.36  ? 84  LEU A C   1 
ATOM   67    O  O   . LEU A 1 20  ? 70.792 35.366 90.512  1.00 64.08  ? 84  LEU A O   1 
ATOM   68    C  CB  . LEU A 1 20  ? 69.889 33.029 88.589  1.00 48.36  ? 84  LEU A CB  1 
ATOM   69    C  CG  . LEU A 1 20  ? 68.519 32.480 88.213  1.00 55.79  ? 84  LEU A CG  1 
ATOM   70    C  CD1 . LEU A 1 20  ? 68.258 32.652 86.720  1.00 59.36  ? 84  LEU A CD1 1 
ATOM   71    C  CD2 . LEU A 1 20  ? 68.410 31.019 88.626  1.00 48.62  ? 84  LEU A CD2 1 
ATOM   72    N  N   . CYS A 1 21  ? 68.675 35.817 89.894  1.00 77.74  ? 85  CYS A N   1 
ATOM   73    C  CA  . CYS A 1 21  ? 68.257 36.421 91.162  1.00 79.70  ? 85  CYS A CA  1 
ATOM   74    C  C   . CYS A 1 21  ? 68.333 35.370 92.241  1.00 98.50  ? 85  CYS A C   1 
ATOM   75    O  O   . CYS A 1 21  ? 68.037 34.199 91.977  1.00 141.70 ? 85  CYS A O   1 
ATOM   76    C  CB  . CYS A 1 21  ? 66.813 36.926 91.065  1.00 106.34 ? 85  CYS A CB  1 
ATOM   77    S  SG  . CYS A 1 21  ? 66.731 38.470 90.227  1.00 225.50 ? 85  CYS A SG  1 
ATOM   78    N  N   . SER A 1 22  ? 68.746 35.770 93.442  1.00 78.27  ? 86  SER A N   1 
ATOM   79    C  CA  . SER A 1 22  ? 68.647 34.893 94.596  1.00 76.60  ? 86  SER A CA  1 
ATOM   80    C  C   . SER A 1 22  ? 67.180 34.745 94.926  1.00 81.86  ? 86  SER A C   1 
ATOM   81    O  O   . SER A 1 22  ? 66.449 35.730 95.003  1.00 81.46  ? 86  SER A O   1 
ATOM   82    C  CB  . SER A 1 22  ? 69.384 35.451 95.796  1.00 84.62  ? 86  SER A CB  1 
ATOM   83    O  OG  . SER A 1 22  ? 70.768 35.565 95.522  1.00 154.15 ? 86  SER A OG  1 
ATOM   84    N  N   . ILE A 1 23  ? 66.751 33.501 95.084  1.00 80.77  ? 87  ILE A N   1 
ATOM   85    C  CA  . ILE A 1 23  ? 65.374 33.201 95.376  1.00 61.67  ? 87  ILE A CA  1 
ATOM   86    C  C   . ILE A 1 23  ? 65.353 32.539 96.741  1.00 63.68  ? 87  ILE A C   1 
ATOM   87    O  O   . ILE A 1 23  ? 66.034 31.518 96.974  1.00 58.53  ? 87  ILE A O   1 
ATOM   88    C  CB  . ILE A 1 23  ? 64.772 32.310 94.267  1.00 64.61  ? 87  ILE A CB  1 
ATOM   89    C  CG1 . ILE A 1 23  ? 64.631 33.139 92.999  1.00 83.87  ? 87  ILE A CG1 1 
ATOM   90    C  CG2 . ILE A 1 23  ? 63.404 31.752 94.657  1.00 67.23  ? 87  ILE A CG2 1 
ATOM   91    C  CD1 . ILE A 1 23  ? 65.003 32.419 91.743  1.00 98.92  ? 87  ILE A CD1 1 
ATOM   92    N  N   . ASN A 1 24  ? 64.608 33.154 97.657  1.00 54.55  ? 88  ASN A N   1 
ATOM   93    C  CA  . ASN A 1 24  ? 64.377 32.527 98.954  1.00 61.70  ? 88  ASN A CA  1 
ATOM   94    C  C   . ASN A 1 24  ? 62.906 32.294 99.262  1.00 55.75  ? 88  ASN A C   1 
ATOM   95    O  O   . ASN A 1 24  ? 62.579 31.694 100.281 1.00 49.77  ? 88  ASN A O   1 
ATOM   96    C  CB  . ASN A 1 24  ? 65.060 33.319 100.065 1.00 69.85  ? 88  ASN A CB  1 
ATOM   97    C  CG  . ASN A 1 24  ? 66.565 33.229 99.983  1.00 89.63  ? 88  ASN A CG  1 
ATOM   98    O  OD1 . ASN A 1 24  ? 67.165 32.215 100.362 1.00 75.13  ? 88  ASN A OD1 1 
ATOM   99    N  ND2 . ASN A 1 24  ? 67.189 34.282 99.462  1.00 98.14  ? 88  ASN A ND2 1 
ATOM   100   N  N   . GLY A 1 25  ? 62.029 32.764 98.373  1.00 46.51  ? 89  GLY A N   1 
ATOM   101   C  CA  . GLY A 1 25  ? 60.589 32.622 98.546  1.00 45.34  ? 89  GLY A CA  1 
ATOM   102   C  C   . GLY A 1 25  ? 59.804 32.788 97.244  1.00 49.68  ? 89  GLY A C   1 
ATOM   103   O  O   . GLY A 1 25  ? 60.367 32.989 96.163  1.00 42.09  ? 89  GLY A O   1 
ATOM   104   N  N   . TRP A 1 26  ? 58.487 32.681 97.327  1.00 44.66  ? 90  TRP A N   1 
ATOM   105   C  CA  . TRP A 1 26  ? 57.669 32.790 96.142  1.00 36.56  ? 90  TRP A CA  1 
ATOM   106   C  C   . TRP A 1 26  ? 56.415 33.559 96.445  1.00 46.12  ? 90  TRP A C   1 
ATOM   107   O  O   . TRP A 1 26  ? 55.694 33.300 97.444  1.00 45.42  ? 90  TRP A O   1 
ATOM   108   C  CB  . TRP A 1 26  ? 57.311 31.399 95.628  1.00 38.91  ? 90  TRP A CB  1 
ATOM   109   C  CG  . TRP A 1 26  ? 58.526 30.554 95.326  1.00 43.86  ? 90  TRP A CG  1 
ATOM   110   C  CD1 . TRP A 1 26  ? 59.153 29.625 96.157  1.00 47.67  ? 90  TRP A CD1 1 
ATOM   111   C  CD2 . TRP A 1 26  ? 59.321 30.557 94.101  1.00 42.08  ? 90  TRP A CD2 1 
ATOM   112   N  NE1 . TRP A 1 26  ? 60.246 29.070 95.547  1.00 49.68  ? 90  TRP A NE1 1 
ATOM   113   C  CE2 . TRP A 1 26  ? 60.410 29.595 94.307  1.00 50.02  ? 90  TRP A CE2 1 
ATOM   114   C  CE3 . TRP A 1 26  ? 59.255 31.237 92.917  1.00 43.71  ? 90  TRP A CE3 1 
ATOM   115   C  CZ2 . TRP A 1 26  ? 61.373 29.346 93.329  1.00 39.29  ? 90  TRP A CZ2 1 
ATOM   116   C  CZ3 . TRP A 1 26  ? 60.242 30.986 91.955  1.00 42.37  ? 90  TRP A CZ3 1 
ATOM   117   C  CH2 . TRP A 1 26  ? 61.274 30.065 92.162  1.00 33.59  ? 90  TRP A CH2 1 
ATOM   118   N  N   . VAL A 1 27  ? 56.119 34.530 95.591  1.00 41.40  ? 91  VAL A N   1 
ATOM   119   C  CA  . VAL A 1 27  ? 54.846 35.225 95.703  1.00 44.73  ? 91  VAL A CA  1 
ATOM   120   C  C   . VAL A 1 27  ? 54.090 35.132 94.408  1.00 43.17  ? 91  VAL A C   1 
ATOM   121   O  O   . VAL A 1 27  ? 54.673 35.281 93.331  1.00 45.84  ? 91  VAL A O   1 
ATOM   122   C  CB  . VAL A 1 27  ? 54.992 36.688 96.164  1.00 47.11  ? 91  VAL A CB  1 
ATOM   123   C  CG1 . VAL A 1 27  ? 56.226 36.830 97.041  1.00 59.67  ? 91  VAL A CG1 1 
ATOM   124   C  CG2 . VAL A 1 27  ? 55.097 37.592 95.006  1.00 46.91  ? 91  VAL A CG2 1 
ATOM   125   N  N   . PRO A 1 28  ? 52.791 34.864 94.507  1.00 41.31  ? 92  PRO A N   1 
ATOM   126   C  CA  . PRO A 1 28  ? 51.963 34.743 93.333  1.00 48.89  ? 92  PRO A CA  1 
ATOM   127   C  C   . PRO A 1 28  ? 51.822 36.116 92.634  1.00 51.45  ? 92  PRO A C   1 
ATOM   128   O  O   . PRO A 1 28  ? 51.643 37.126 93.290  1.00 54.79  ? 92  PRO A O   1 
ATOM   129   C  CB  . PRO A 1 28  ? 50.632 34.261 93.905  1.00 42.13  ? 92  PRO A CB  1 
ATOM   130   C  CG  . PRO A 1 28  ? 50.632 34.771 95.294  1.00 48.57  ? 92  PRO A CG  1 
ATOM   131   C  CD  . PRO A 1 28  ? 52.027 34.737 95.751  1.00 38.54  ? 92  PRO A CD  1 
ATOM   132   N  N   . THR A 1 29  ? 51.944 36.138 91.316  1.00 51.75  ? 93  THR A N   1 
ATOM   133   C  CA  . THR A 1 29  ? 51.816 37.361 90.555  1.00 48.36  ? 93  THR A CA  1 
ATOM   134   C  C   . THR A 1 29  ? 50.517 37.314 89.749  1.00 56.08  ? 93  THR A C   1 
ATOM   135   O  O   . THR A 1 29  ? 50.053 38.330 89.238  1.00 64.51  ? 93  THR A O   1 
ATOM   136   C  CB  . THR A 1 29  ? 53.056 37.620 89.599  1.00 45.90  ? 93  THR A CB  1 
ATOM   137   O  OG1 . THR A 1 29  ? 53.415 36.440 88.878  1.00 47.65  ? 93  THR A OG1 1 
ATOM   138   C  CG2 . THR A 1 29  ? 54.255 38.072 90.376  1.00 54.97  ? 93  THR A CG2 1 
ATOM   139   N  N   . TYR A 1 30  ? 49.944 36.127 89.606  1.00 45.34  ? 94  TYR A N   1 
ATOM   140   C  CA  . TYR A 1 30  ? 48.691 35.999 88.899  1.00 42.43  ? 94  TYR A CA  1 
ATOM   141   C  C   . TYR A 1 30  ? 47.955 34.732 89.255  1.00 55.33  ? 94  TYR A C   1 
ATOM   142   O  O   . TYR A 1 30  ? 48.538 33.649 89.531  1.00 46.24  ? 94  TYR A O   1 
ATOM   143   C  CB  . TYR A 1 30  ? 48.916 35.972 87.412  1.00 47.33  ? 94  TYR A CB  1 
ATOM   144   C  CG  . TYR A 1 30  ? 47.670 35.613 86.608  1.00 69.25  ? 94  TYR A CG  1 
ATOM   145   C  CD1 . TYR A 1 30  ? 46.678 36.560 86.360  1.00 57.60  ? 94  TYR A CD1 1 
ATOM   146   C  CD2 . TYR A 1 30  ? 47.488 34.320 86.096  1.00 75.96  ? 94  TYR A CD2 1 
ATOM   147   C  CE1 . TYR A 1 30  ? 45.562 36.240 85.639  1.00 63.84  ? 94  TYR A CE1 1 
ATOM   148   C  CE2 . TYR A 1 30  ? 46.353 33.992 85.358  1.00 65.66  ? 94  TYR A CE2 1 
ATOM   149   C  CZ  . TYR A 1 30  ? 45.403 34.957 85.139  1.00 71.17  ? 94  TYR A CZ  1 
ATOM   150   O  OH  . TYR A 1 30  ? 44.280 34.643 84.423  1.00 89.53  ? 94  TYR A OH  1 
ATOM   151   N  N   . ARG A 1 31  ? 46.644 34.865 89.191  1.00 54.10  ? 95  ARG A N   1 
ATOM   152   C  CA  . ARG A 1 31  ? 45.770 33.779 89.524  1.00 62.90  ? 95  ARG A CA  1 
ATOM   153   C  C   . ARG A 1 31  ? 44.480 33.909 88.710  1.00 85.02  ? 95  ARG A C   1 
ATOM   154   O  O   . ARG A 1 31  ? 43.784 34.949 88.742  1.00 60.42  ? 95  ARG A O   1 
ATOM   155   C  CB  . ARG A 1 31  ? 45.523 33.810 91.015  1.00 55.07  ? 95  ARG A CB  1 
ATOM   156   C  CG  . ARG A 1 31  ? 44.463 32.909 91.501  1.00 67.93  ? 95  ARG A CG  1 
ATOM   157   C  CD  . ARG A 1 31  ? 44.456 32.880 93.027  1.00 81.10  ? 95  ARG A CD  1 
ATOM   158   N  NE  . ARG A 1 31  ? 44.125 34.169 93.637  1.00 73.30  ? 95  ARG A NE  1 
ATOM   159   C  CZ  . ARG A 1 31  ? 43.777 34.320 94.905  1.00 66.51  ? 95  ARG A CZ  1 
ATOM   160   N  NH1 . ARG A 1 31  ? 43.708 33.262 95.707  1.00 69.02  ? 95  ARG A NH1 1 
ATOM   161   N  NH2 . ARG A 1 31  ? 43.492 35.526 95.367  1.00 80.37  ? 95  ARG A NH2 1 
ATOM   162   N  N   . GLY A 1 32  ? 44.189 32.842 87.962  1.00 94.16  ? 96  GLY A N   1 
ATOM   163   C  CA  . GLY A 1 32  ? 43.007 32.777 87.117  1.00 86.87  ? 96  GLY A CA  1 
ATOM   164   C  C   . GLY A 1 32  ? 41.752 32.778 87.960  1.00 65.56  ? 96  GLY A C   1 
ATOM   165   O  O   . GLY A 1 32  ? 41.787 32.404 89.114  1.00 58.22  ? 96  GLY A O   1 
ATOM   166   N  N   . GLU A 1 33  ? 40.638 33.203 87.383  1.00 71.62  ? 97  GLU A N   1 
ATOM   167   C  CA  . GLU A 1 33  ? 39.424 33.296 88.165  1.00 86.68  ? 97  GLU A CA  1 
ATOM   168   C  C   . GLU A 1 33  ? 38.832 31.921 88.431  1.00 85.04  ? 97  GLU A C   1 
ATOM   169   O  O   . GLU A 1 33  ? 38.040 31.754 89.353  1.00 75.03  ? 97  GLU A O   1 
ATOM   170   C  CB  . GLU A 1 33  ? 38.415 34.241 87.516  1.00 89.06  ? 97  GLU A CB  1 
ATOM   171   C  CG  . GLU A 1 33  ? 37.556 35.002 88.552  1.00 132.19 ? 97  GLU A CG  1 
ATOM   172   C  CD  . GLU A 1 33  ? 38.350 35.963 89.458  1.00 122.71 ? 97  GLU A CD  1 
ATOM   173   O  OE1 . GLU A 1 33  ? 39.283 36.634 88.973  1.00 127.76 ? 97  GLU A OE1 1 
ATOM   174   O  OE2 . GLU A 1 33  ? 38.023 36.059 90.661  1.00 105.18 ? 97  GLU A OE2 1 
ATOM   175   N  N   . GLY A 1 34  ? 39.253 30.936 87.641  1.00 85.93  ? 98  GLY A N   1 
ATOM   176   C  CA  . GLY A 1 34  ? 38.849 29.549 87.861  1.00 88.80  ? 98  GLY A CA  1 
ATOM   177   C  C   . GLY A 1 34  ? 39.618 28.816 88.960  1.00 73.57  ? 98  GLY A C   1 
ATOM   178   O  O   . GLY A 1 34  ? 39.360 27.631 89.251  1.00 60.62  ? 98  GLY A O   1 
ATOM   179   N  N   . THR A 1 35  ? 40.560 29.512 89.584  1.00 56.63  ? 99  THR A N   1 
ATOM   180   C  CA  . THR A 1 35  ? 41.389 28.885 90.595  1.00 57.80  ? 99  THR A CA  1 
ATOM   181   C  C   . THR A 1 35  ? 40.676 28.998 91.931  1.00 63.93  ? 99  THR A C   1 
ATOM   182   O  O   . THR A 1 35  ? 41.097 28.420 92.945  1.00 69.80  ? 99  THR A O   1 
ATOM   183   C  CB  . THR A 1 35  ? 42.759 29.566 90.689  1.00 57.06  ? 99  THR A CB  1 
ATOM   184   O  OG1 . THR A 1 35  ? 42.572 30.905 91.118  1.00 65.05  ? 99  THR A OG1 1 
ATOM   185   C  CG2 . THR A 1 35  ? 43.431 29.623 89.338  1.00 70.81  ? 99  THR A CG2 1 
ATOM   186   N  N   . THR A 1 36  ? 39.593 29.766 91.927  1.00 66.43  ? 100 THR A N   1 
ATOM   187   C  CA  . THR A 1 36  ? 38.841 30.058 93.150  1.00 85.00  ? 100 THR A CA  1 
ATOM   188   C  C   . THR A 1 36  ? 37.359 29.738 92.946  1.00 89.10  ? 100 THR A C   1 
ATOM   189   O  O   . THR A 1 36  ? 36.836 28.834 93.583  1.00 111.58 ? 100 THR A O   1 
ATOM   190   C  CB  . THR A 1 36  ? 39.040 31.536 93.624  1.00 82.21  ? 100 THR A CB  1 
ATOM   191   O  OG1 . THR A 1 36  ? 38.911 32.426 92.506  1.00 113.48 ? 100 THR A OG1 1 
ATOM   192   C  CG2 . THR A 1 36  ? 40.417 31.735 94.225  1.00 66.69  ? 100 THR A CG2 1 
ATOM   193   N  N   . GLY A 1 37  ? 36.698 30.467 92.045  1.00 91.00  ? 101 GLY A N   1 
ATOM   194   C  CA  . GLY A 1 37  ? 35.308 30.193 91.669  1.00 85.13  ? 101 GLY A CA  1 
ATOM   195   C  C   . GLY A 1 37  ? 35.184 29.287 90.442  1.00 86.18  ? 101 GLY A C   1 
ATOM   196   O  O   . GLY A 1 37  ? 36.144 28.639 90.022  1.00 95.25  ? 101 GLY A O   1 
ATOM   197   N  N   . LYS A 1 38  ? 33.986 29.239 89.875  1.00 75.37  ? 102 LYS A N   1 
ATOM   198   C  CA  . LYS A 1 38  ? 33.728 28.505 88.645  1.00 68.55  ? 102 LYS A CA  1 
ATOM   199   C  C   . LYS A 1 38  ? 33.911 29.373 87.398  1.00 73.43  ? 102 LYS A C   1 
ATOM   200   O  O   . LYS A 1 38  ? 33.919 30.608 87.470  1.00 87.43  ? 102 LYS A O   1 
ATOM   201   C  CB  . LYS A 1 38  ? 32.312 27.964 88.676  1.00 76.46  ? 102 LYS A CB  1 
ATOM   202   C  CG  . LYS A 1 38  ? 32.117 26.877 89.686  1.00 86.90  ? 102 LYS A CG  1 
ATOM   203   C  CD  . LYS A 1 38  ? 30.871 26.110 89.342  1.00 119.33 ? 102 LYS A CD  1 
ATOM   204   C  CE  . LYS A 1 38  ? 30.919 24.704 89.891  1.00 110.27 ? 102 LYS A CE  1 
ATOM   205   N  NZ  . LYS A 1 38  ? 29.886 23.888 89.204  1.00 134.21 ? 102 LYS A NZ  1 
ATOM   206   N  N   . ILE A 1 39  ? 34.044 28.727 86.243  1.00 66.90  ? 103 ILE A N   1 
ATOM   207   C  CA  . ILE A 1 39  ? 34.313 29.463 85.015  1.00 61.48  ? 103 ILE A CA  1 
ATOM   208   C  C   . ILE A 1 39  ? 33.019 29.789 84.291  1.00 77.43  ? 103 ILE A C   1 
ATOM   209   O  O   . ILE A 1 39  ? 32.144 28.924 84.161  1.00 86.27  ? 103 ILE A O   1 
ATOM   210   C  CB  . ILE A 1 39  ? 35.221 28.664 84.078  1.00 56.53  ? 103 ILE A CB  1 
ATOM   211   C  CG1 . ILE A 1 39  ? 36.363 27.990 84.855  1.00 58.91  ? 103 ILE A CG1 1 
ATOM   212   C  CG2 . ILE A 1 39  ? 35.706 29.533 82.882  1.00 43.49  ? 103 ILE A CG2 1 
ATOM   213   C  CD1 . ILE A 1 39  ? 37.692 28.668 84.769  1.00 55.47  ? 103 ILE A CD1 1 
ATOM   214   N  N   . PRO A 1 40  ? 32.887 31.042 83.820  1.00 85.49  ? 104 PRO A N   1 
ATOM   215   C  CA  . PRO A 1 40  ? 31.750 31.446 82.968  1.00 93.36  ? 104 PRO A CA  1 
ATOM   216   C  C   . PRO A 1 40  ? 31.684 30.643 81.663  1.00 84.56  ? 104 PRO A C   1 
ATOM   217   O  O   . PRO A 1 40  ? 32.699 30.425 81.012  1.00 98.43  ? 104 PRO A O   1 
ATOM   218   C  CB  . PRO A 1 40  ? 32.043 32.918 82.665  1.00 101.24 ? 104 PRO A CB  1 
ATOM   219   C  CG  . PRO A 1 40  ? 32.954 33.365 83.765  1.00 89.34  ? 104 PRO A CG  1 
ATOM   220   C  CD  . PRO A 1 40  ? 33.761 32.177 84.179  1.00 67.52  ? 104 PRO A CD  1 
ATOM   221   N  N   . ASP A 1 41  ? 30.489 30.233 81.275  1.00 88.39  ? 105 ASP A N   1 
ATOM   222   C  CA  . ASP A 1 41  ? 30.324 29.307 80.166  1.00 94.03  ? 105 ASP A CA  1 
ATOM   223   C  C   . ASP A 1 41  ? 30.802 29.855 78.833  1.00 91.31  ? 105 ASP A C   1 
ATOM   224   O  O   . ASP A 1 41  ? 31.172 29.083 77.951  1.00 117.14 ? 105 ASP A O   1 
ATOM   225   C  CB  . ASP A 1 41  ? 28.866 28.840 80.074  1.00 111.18 ? 105 ASP A CB  1 
ATOM   226   C  CG  . ASP A 1 41  ? 28.367 28.232 81.382  1.00 126.40 ? 105 ASP A CG  1 
ATOM   227   O  OD1 . ASP A 1 41  ? 28.940 28.564 82.432  1.00 169.93 ? 105 ASP A OD1 1 
ATOM   228   O  OD2 . ASP A 1 41  ? 27.413 27.430 81.379  1.00 122.36 ? 105 ASP A OD2 1 
ATOM   229   N  N   . GLU A 1 42  ? 30.804 31.177 78.686  1.00 78.40  ? 106 GLU A N   1 
ATOM   230   C  CA  . GLU A 1 42  ? 31.198 31.784 77.411  1.00 97.73  ? 106 GLU A CA  1 
ATOM   231   C  C   . GLU A 1 42  ? 32.709 31.738 77.166  1.00 101.51 ? 106 GLU A C   1 
ATOM   232   O  O   . GLU A 1 42  ? 33.156 31.929 76.030  1.00 114.43 ? 106 GLU A O   1 
ATOM   233   C  CB  . GLU A 1 42  ? 30.671 33.215 77.251  1.00 106.76 ? 106 GLU A CB  1 
ATOM   234   C  CG  . GLU A 1 42  ? 31.271 34.226 78.213  1.00 145.00 ? 106 GLU A CG  1 
ATOM   235   C  CD  . GLU A 1 42  ? 30.308 34.605 79.316  1.00 170.03 ? 106 GLU A CD  1 
ATOM   236   O  OE1 . GLU A 1 42  ? 29.690 33.693 79.920  1.00 138.51 ? 106 GLU A OE1 1 
ATOM   237   O  OE2 . GLU A 1 42  ? 30.166 35.823 79.568  1.00 192.31 ? 106 GLU A OE2 1 
ATOM   238   N  N   . GLN A 1 43  ? 33.490 31.492 78.218  1.00 68.87  ? 107 GLN A N   1 
ATOM   239   C  CA  . GLN A 1 43  ? 34.923 31.374 78.060  1.00 51.74  ? 107 GLN A CA  1 
ATOM   240   C  C   . GLN A 1 43  ? 35.312 30.136 77.262  1.00 62.09  ? 107 GLN A C   1 
ATOM   241   O  O   . GLN A 1 43  ? 34.602 29.130 77.261  1.00 59.85  ? 107 GLN A O   1 
ATOM   242   C  CB  . GLN A 1 43  ? 35.615 31.375 79.403  1.00 48.55  ? 107 GLN A CB  1 
ATOM   243   C  CG  . GLN A 1 43  ? 35.678 32.748 80.050  1.00 71.15  ? 107 GLN A CG  1 
ATOM   244   C  CD  . GLN A 1 43  ? 36.708 32.832 81.169  1.00 82.21  ? 107 GLN A CD  1 
ATOM   245   O  OE1 . GLN A 1 43  ? 37.725 32.109 81.162  1.00 77.00  ? 107 GLN A OE1 1 
ATOM   246   N  NE2 . GLN A 1 43  ? 36.450 33.717 82.146  1.00 68.58  ? 107 GLN A NE2 1 
ATOM   247   N  N   . MET A 1 44  ? 36.435 30.247 76.554  1.00 76.13  ? 108 MET A N   1 
ATOM   248   C  CA  . MET A 1 44  ? 37.063 29.137 75.857  1.00 64.41  ? 108 MET A CA  1 
ATOM   249   C  C   . MET A 1 44  ? 37.564 28.159 76.910  1.00 56.97  ? 108 MET A C   1 
ATOM   250   O  O   . MET A 1 44  ? 38.150 28.590 77.888  1.00 62.25  ? 108 MET A O   1 
ATOM   251   C  CB  . MET A 1 44  ? 38.238 29.680 75.053  1.00 70.49  ? 108 MET A CB  1 
ATOM   252   C  CG  . MET A 1 44  ? 38.962 28.642 74.226  1.00 84.67  ? 108 MET A CG  1 
ATOM   253   S  SD  . MET A 1 44  ? 37.928 28.004 72.911  1.00 97.48  ? 108 MET A SD  1 
ATOM   254   C  CE  . MET A 1 44  ? 38.214 29.151 71.554  1.00 85.14  ? 108 MET A CE  1 
ATOM   255   N  N   . LEU A 1 45  ? 37.307 26.865 76.744  1.00 49.75  ? 109 LEU A N   1 
ATOM   256   C  CA  . LEU A 1 45  ? 37.880 25.842 77.638  1.00 52.52  ? 109 LEU A CA  1 
ATOM   257   C  C   . LEU A 1 45  ? 39.346 25.670 77.256  1.00 54.71  ? 109 LEU A C   1 
ATOM   258   O  O   . LEU A 1 45  ? 39.640 25.529 76.060  1.00 57.05  ? 109 LEU A O   1 
ATOM   259   C  CB  . LEU A 1 45  ? 37.183 24.494 77.464  1.00 51.04  ? 109 LEU A CB  1 
ATOM   260   C  CG  . LEU A 1 45  ? 35.671 24.453 77.658  1.00 63.99  ? 109 LEU A CG  1 
ATOM   261   C  CD1 . LEU A 1 45  ? 35.085 23.145 77.184  1.00 66.88  ? 109 LEU A CD1 1 
ATOM   262   C  CD2 . LEU A 1 45  ? 35.339 24.671 79.083  1.00 73.22  ? 109 LEU A CD2 1 
ATOM   263   N  N   . THR A 1 46  ? 40.259 25.695 78.236  1.00 45.03  ? 110 THR A N   1 
ATOM   264   C  CA  . THR A 1 46  ? 41.693 25.581 77.907  1.00 48.89  ? 110 THR A CA  1 
ATOM   265   C  C   . THR A 1 46  ? 42.392 24.328 78.406  1.00 50.52  ? 110 THR A C   1 
ATOM   266   O  O   . THR A 1 46  ? 41.947 23.681 79.341  1.00 61.81  ? 110 THR A O   1 
ATOM   267   C  CB  . THR A 1 46  ? 42.482 26.710 78.437  1.00 40.89  ? 110 THR A CB  1 
ATOM   268   O  OG1 . THR A 1 46  ? 42.445 26.614 79.849  1.00 56.88  ? 110 THR A OG1 1 
ATOM   269   C  CG2 . THR A 1 46  ? 41.881 28.001 78.006  1.00 44.48  ? 110 THR A CG2 1 
ATOM   270   N  N   . ARG A 1 47  ? 43.488 23.983 77.748  1.00 46.29  ? 111 ARG A N   1 
ATOM   271   C  CA  . ARG A 1 47  ? 44.311 22.858 78.166  1.00 45.18  ? 111 ARG A CA  1 
ATOM   272   C  C   . ARG A 1 47  ? 45.707 23.067 77.653  1.00 38.49  ? 111 ARG A C   1 
ATOM   273   O  O   . ARG A 1 47  ? 45.920 23.810 76.691  1.00 44.57  ? 111 ARG A O   1 
ATOM   274   C  CB  . ARG A 1 47  ? 43.761 21.525 77.673  1.00 47.33  ? 111 ARG A CB  1 
ATOM   275   C  CG  . ARG A 1 47  ? 44.340 21.018 76.398  1.00 41.23  ? 111 ARG A CG  1 
ATOM   276   C  CD  . ARG A 1 47  ? 44.204 19.538 76.332  1.00 45.87  ? 111 ARG A CD  1 
ATOM   277   N  NE  . ARG A 1 47  ? 44.912 19.066 75.148  1.00 67.02  ? 111 ARG A NE  1 
ATOM   278   C  CZ  . ARG A 1 47  ? 46.223 18.857 75.086  1.00 73.65  ? 111 ARG A CZ  1 
ATOM   279   N  NH1 . ARG A 1 47  ? 46.988 19.080 76.145  1.00 83.39  ? 111 ARG A NH1 1 
ATOM   280   N  NH2 . ARG A 1 47  ? 46.774 18.417 73.962  1.00 109.26 ? 111 ARG A NH2 1 
ATOM   281   N  N   . GLN A 1 48  ? 46.655 22.425 78.308  1.00 31.02  ? 112 GLN A N   1 
ATOM   282   C  CA  . GLN A 1 48  ? 48.064 22.637 77.992  1.00 36.90  ? 112 GLN A CA  1 
ATOM   283   C  C   . GLN A 1 48  ? 48.560 24.105 78.149  1.00 35.48  ? 112 GLN A C   1 
ATOM   284   O  O   . GLN A 1 48  ? 49.482 24.570 77.451  1.00 42.59  ? 112 GLN A O   1 
ATOM   285   C  CB  . GLN A 1 48  ? 48.437 22.009 76.628  1.00 31.07  ? 112 GLN A CB  1 
ATOM   286   C  CG  . GLN A 1 48  ? 49.390 22.875 75.875  1.00 45.02  ? 112 GLN A CG  1 
ATOM   287   C  CD  . GLN A 1 48  ? 50.551 22.149 75.314  1.00 55.74  ? 112 GLN A CD  1 
ATOM   288   O  OE1 . GLN A 1 48  ? 51.391 22.862 74.577  1.00 90.89  ? 112 GLN A OE1 1 
ATOM   289   N  NE2 . GLN A 1 48  ? 50.696 20.953 75.512  1.00 54.78  ? 112 GLN A NE2 1 
ATOM   290   N  N   . ASN A 1 49  ? 47.970 24.818 79.096  1.00 37.78  ? 113 ASN A N   1 
ATOM   291   C  CA  . ASN A 1 49  ? 48.406 26.191 79.405  1.00 37.04  ? 113 ASN A CA  1 
ATOM   292   C  C   . ASN A 1 49  ? 49.877 26.295 79.702  1.00 32.99  ? 113 ASN A C   1 
ATOM   293   O  O   . ASN A 1 49  ? 50.432 25.447 80.377  1.00 36.62  ? 113 ASN A O   1 
ATOM   294   C  CB  . ASN A 1 49  ? 47.641 26.723 80.603  1.00 36.13  ? 113 ASN A CB  1 
ATOM   295   C  CG  . ASN A 1 49  ? 46.134 26.823 80.328  1.00 58.27  ? 113 ASN A CG  1 
ATOM   296   O  OD1 . ASN A 1 49  ? 45.615 27.955 80.138  1.00 44.81  ? 113 ASN A OD1 1 
ATOM   297   N  ND2 . ASN A 1 49  ? 45.415 25.638 80.281  1.00 34.84  ? 113 ASN A ND2 1 
ATOM   298   N  N   . PHE A 1 50  ? 50.518 27.321 79.179  1.00 30.24  ? 114 PHE A N   1 
ATOM   299   C  CA  . PHE A 1 50  ? 51.787 27.686 79.725  1.00 31.74  ? 114 PHE A CA  1 
ATOM   300   C  C   . PHE A 1 50  ? 52.003 29.171 79.601  1.00 34.20  ? 114 PHE A C   1 
ATOM   301   O  O   . PHE A 1 50  ? 51.104 29.897 79.161  1.00 51.85  ? 114 PHE A O   1 
ATOM   302   C  CB  . PHE A 1 50  ? 52.891 26.892 79.047  1.00 51.78  ? 114 PHE A CB  1 
ATOM   303   C  CG  . PHE A 1 50  ? 53.051 27.170 77.584  1.00 56.89  ? 114 PHE A CG  1 
ATOM   304   C  CD1 . PHE A 1 50  ? 52.342 26.425 76.659  1.00 59.26  ? 114 PHE A CD1 1 
ATOM   305   C  CD2 . PHE A 1 50  ? 53.950 28.150 77.132  1.00 44.01  ? 114 PHE A CD2 1 
ATOM   306   C  CE1 . PHE A 1 50  ? 52.493 26.671 75.302  1.00 64.34  ? 114 PHE A CE1 1 
ATOM   307   C  CE2 . PHE A 1 50  ? 54.110 28.389 75.778  1.00 55.32  ? 114 PHE A CE2 1 
ATOM   308   C  CZ  . PHE A 1 50  ? 53.376 27.652 74.857  1.00 52.40  ? 114 PHE A CZ  1 
ATOM   309   N  N   . VAL A 1 51  ? 53.181 29.642 80.000  1.00 28.65  ? 115 VAL A N   1 
ATOM   310   C  CA  . VAL A 1 51  ? 53.463 31.052 79.966  1.00 27.77  ? 115 VAL A CA  1 
ATOM   311   C  C   . VAL A 1 51  ? 54.789 31.232 79.277  1.00 31.25  ? 115 VAL A C   1 
ATOM   312   O  O   . VAL A 1 51  ? 55.674 30.418 79.411  1.00 44.67  ? 115 VAL A O   1 
ATOM   313   C  CB  . VAL A 1 51  ? 53.454 31.682 81.356  1.00 28.49  ? 115 VAL A CB  1 
ATOM   314   C  CG1 . VAL A 1 51  ? 53.881 33.157 81.299  1.00 36.25  ? 115 VAL A CG1 1 
ATOM   315   C  CG2 . VAL A 1 51  ? 52.073 31.619 81.941  1.00 28.57  ? 115 VAL A CG2 1 
ATOM   316   N  N   . SER A 1 52  ? 54.896 32.304 78.509  1.00 37.34  ? 116 SER A N   1 
ATOM   317   C  CA  . SER A 1 52  ? 56.116 32.683 77.840  1.00 36.75  ? 116 SER A CA  1 
ATOM   318   C  C   . SER A 1 52  ? 56.099 34.203 77.754  1.00 51.65  ? 116 SER A C   1 
ATOM   319   O  O   . SER A 1 52  ? 55.012 34.815 77.535  1.00 43.16  ? 116 SER A O   1 
ATOM   320   C  CB  . SER A 1 52  ? 56.168 32.090 76.452  1.00 36.95  ? 116 SER A CB  1 
ATOM   321   O  OG  . SER A 1 52  ? 57.325 32.546 75.779  1.00 67.77  ? 116 SER A OG  1 
ATOM   322   N  N   . CYS A 1 53  ? 57.281 34.810 77.933  1.00 41.24  ? 117 CYS A N   1 
ATOM   323   C  CA  . CYS A 1 53  ? 57.312 36.247 77.984  1.00 46.09  ? 117 CYS A CA  1 
ATOM   324   C  C   . CYS A 1 53  ? 58.078 36.903 76.834  1.00 42.72  ? 117 CYS A C   1 
ATOM   325   O  O   . CYS A 1 53  ? 59.078 36.370 76.381  1.00 71.40  ? 117 CYS A O   1 
ATOM   326   C  CB  . CYS A 1 53  ? 57.813 36.708 79.339  1.00 53.71  ? 117 CYS A CB  1 
ATOM   327   S  SG  . CYS A 1 53  ? 56.804 36.180 80.740  1.00 114.17 ? 117 CYS A SG  1 
ATOM   328   N  N   . SER A 1 54  ? 57.569 38.042 76.354  1.00 53.04  ? 118 SER A N   1 
ATOM   329   C  CA  . SER A 1 54  ? 58.292 38.957 75.450  1.00 52.85  ? 118 SER A CA  1 
ATOM   330   C  C   . SER A 1 54  ? 58.960 40.033 76.292  1.00 57.60  ? 118 SER A C   1 
ATOM   331   O  O   . SER A 1 54  ? 58.914 39.983 77.521  1.00 79.67  ? 118 SER A O   1 
ATOM   332   C  CB  . SER A 1 54  ? 57.355 39.581 74.385  1.00 58.78  ? 118 SER A CB  1 
ATOM   333   O  OG  . SER A 1 54  ? 56.571 40.672 74.866  1.00 60.79  ? 118 SER A OG  1 
ATOM   334   N  N   . ASP A 1 55  ? 59.604 40.991 75.643  1.00 61.53  ? 119 ASP A N   1 
ATOM   335   C  CA  . ASP A 1 55  ? 60.265 42.079 76.368  1.00 84.68  ? 119 ASP A CA  1 
ATOM   336   C  C   . ASP A 1 55  ? 59.248 43.164 76.751  1.00 86.22  ? 119 ASP A C   1 
ATOM   337   O  O   . ASP A 1 55  ? 59.556 44.109 77.483  1.00 95.79  ? 119 ASP A O   1 
ATOM   338   C  CB  . ASP A 1 55  ? 61.410 42.664 75.528  1.00 94.41  ? 119 ASP A CB  1 
ATOM   339   C  CG  . ASP A 1 55  ? 60.981 43.020 74.097  1.00 134.16 ? 119 ASP A CG  1 
ATOM   340   O  OD1 . ASP A 1 55  ? 59.765 43.148 73.827  1.00 157.42 ? 119 ASP A OD1 1 
ATOM   341   O  OD2 . ASP A 1 55  ? 61.873 43.181 73.235  1.00 129.73 ? 119 ASP A OD2 1 
ATOM   342   N  N   . LYS A 1 56  ? 58.033 42.986 76.247  1.00 70.60  ? 120 LYS A N   1 
ATOM   343   C  CA  . LYS A 1 56  ? 56.965 43.935 76.360  1.00 68.25  ? 120 LYS A CA  1 
ATOM   344   C  C   . LYS A 1 56  ? 55.950 43.436 77.363  1.00 69.67  ? 120 LYS A C   1 
ATOM   345   O  O   . LYS A 1 56  ? 55.349 44.239 78.067  1.00 115.79 ? 120 LYS A O   1 
ATOM   346   C  CB  . LYS A 1 56  ? 56.311 44.074 75.000  1.00 71.85  ? 120 LYS A CB  1 
ATOM   347   C  CG  . LYS A 1 56  ? 55.097 44.988 74.940  1.00 118.46 ? 120 LYS A CG  1 
ATOM   348   C  CD  . LYS A 1 56  ? 54.403 44.914 73.572  1.00 157.70 ? 120 LYS A CD  1 
ATOM   349   C  CE  . LYS A 1 56  ? 55.270 45.479 72.441  1.00 188.88 ? 120 LYS A CE  1 
ATOM   350   N  NZ  . LYS A 1 56  ? 56.218 44.475 71.866  1.00 239.52 ? 120 LYS A NZ  1 
ATOM   351   N  N   . GLU A 1 57  ? 55.778 42.115 77.435  1.00 69.70  ? 121 GLU A N   1 
ATOM   352   C  CA  . GLU A 1 57  ? 54.660 41.483 78.163  1.00 69.25  ? 121 GLU A CA  1 
ATOM   353   C  C   . GLU A 1 57  ? 54.771 39.960 78.230  1.00 58.58  ? 121 GLU A C   1 
ATOM   354   O  O   . GLU A 1 57  ? 55.482 39.351 77.459  1.00 58.34  ? 121 GLU A O   1 
ATOM   355   C  CB  . GLU A 1 57  ? 53.347 41.801 77.452  1.00 55.28  ? 121 GLU A CB  1 
ATOM   356   C  CG  . GLU A 1 57  ? 53.085 40.914 76.300  1.00 51.95  ? 121 GLU A CG  1 
ATOM   357   C  CD  . GLU A 1 57  ? 51.963 41.382 75.382  1.00 88.06  ? 121 GLU A CD  1 
ATOM   358   O  OE1 . GLU A 1 57  ? 51.075 42.144 75.827  1.00 110.28 ? 121 GLU A OE1 1 
ATOM   359   O  OE2 . GLU A 1 57  ? 51.966 40.962 74.197  1.00 113.82 ? 121 GLU A OE2 1 
ATOM   360   N  N   . CYS A 1 58  ? 54.009 39.352 79.120  1.00 57.90  ? 122 CYS A N   1 
ATOM   361   C  CA  . CYS A 1 58  ? 53.948 37.905 79.228  1.00 48.59  ? 122 CYS A CA  1 
ATOM   362   C  C   . CYS A 1 58  ? 52.625 37.443 78.675  1.00 45.48  ? 122 CYS A C   1 
ATOM   363   O  O   . CYS A 1 58  ? 51.576 38.082 78.901  1.00 47.51  ? 122 CYS A O   1 
ATOM   364   C  CB  . CYS A 1 58  ? 54.070 37.474 80.689  1.00 61.41  ? 122 CYS A CB  1 
ATOM   365   S  SG  . CYS A 1 58  ? 55.715 37.801 81.368  1.00 101.12 ? 122 CYS A SG  1 
ATOM   366   N  N   . ARG A 1 59  ? 52.668 36.342 77.932  1.00 40.98  ? 123 ARG A N   1 
ATOM   367   C  CA  . ARG A 1 59  ? 51.446 35.797 77.349  1.00 32.10  ? 123 ARG A CA  1 
ATOM   368   C  C   . ARG A 1 59  ? 51.184 34.427 77.870  1.00 31.51  ? 123 ARG A C   1 
ATOM   369   O  O   . ARG A 1 59  ? 52.111 33.707 78.224  1.00 40.09  ? 123 ARG A O   1 
ATOM   370   C  CB  . ARG A 1 59  ? 51.511 35.798 75.840  1.00 28.86  ? 123 ARG A CB  1 
ATOM   371   C  CG  . ARG A 1 59  ? 51.629 37.213 75.276  1.00 33.80  ? 123 ARG A CG  1 
ATOM   372   C  CD  . ARG A 1 59  ? 51.482 37.267 73.755  1.00 39.13  ? 123 ARG A CD  1 
ATOM   373   N  NE  . ARG A 1 59  ? 50.122 36.947 73.350  1.00 49.75  ? 123 ARG A NE  1 
ATOM   374   C  CZ  . ARG A 1 59  ? 49.116 37.793 73.427  1.00 49.07  ? 123 ARG A CZ  1 
ATOM   375   N  NH1 . ARG A 1 59  ? 49.336 39.019 73.878  1.00 57.06  ? 123 ARG A NH1 1 
ATOM   376   N  NH2 . ARG A 1 59  ? 47.911 37.409 73.035  1.00 56.37  ? 123 ARG A NH2 1 
ATOM   377   N  N   . ARG A 1 60  ? 49.909 34.088 77.961  1.00 29.71  ? 124 ARG A N   1 
ATOM   378   C  CA  . ARG A 1 60  ? 49.493 32.750 78.348  1.00 31.31  ? 124 ARG A CA  1 
ATOM   379   C  C   . ARG A 1 60  ? 49.093 31.984 77.111  1.00 35.74  ? 124 ARG A C   1 
ATOM   380   O  O   . ARG A 1 60  ? 48.163 32.368 76.422  1.00 62.91  ? 124 ARG A O   1 
ATOM   381   C  CB  . ARG A 1 60  ? 48.305 32.903 79.267  1.00 31.34  ? 124 ARG A CB  1 
ATOM   382   C  CG  . ARG A 1 60  ? 47.344 31.724 79.291  1.00 35.58  ? 124 ARG A CG  1 
ATOM   383   C  CD  . ARG A 1 60  ? 46.494 31.800 80.578  1.00 35.27  ? 124 ARG A CD  1 
ATOM   384   N  NE  . ARG A 1 60  ? 45.484 30.757 80.642  1.00 43.37  ? 124 ARG A NE  1 
ATOM   385   C  CZ  . ARG A 1 60  ? 44.297 30.899 81.231  1.00 65.23  ? 124 ARG A CZ  1 
ATOM   386   N  NH1 . ARG A 1 60  ? 43.981 32.049 81.817  1.00 67.42  ? 124 ARG A NH1 1 
ATOM   387   N  NH2 . ARG A 1 60  ? 43.413 29.895 81.231  1.00 60.36  ? 124 ARG A NH2 1 
ATOM   388   N  N   . PHE A 1 61  ? 49.818 30.939 76.768  1.00 36.15  ? 125 PHE A N   1 
ATOM   389   C  CA  . PHE A 1 61  ? 49.401 30.087 75.605  1.00 41.13  ? 125 PHE A CA  1 
ATOM   390   C  C   . PHE A 1 61  ? 48.569 28.925 76.076  1.00 37.49  ? 125 PHE A C   1 
ATOM   391   O  O   . PHE A 1 61  ? 48.707 28.453 77.211  1.00 40.25  ? 125 PHE A O   1 
ATOM   392   C  CB  . PHE A 1 61  ? 50.596 29.597 74.755  1.00 28.02  ? 125 PHE A CB  1 
ATOM   393   C  CG  . PHE A 1 61  ? 51.314 30.724 74.074  1.00 30.35  ? 125 PHE A CG  1 
ATOM   394   C  CD1 . PHE A 1 61  ? 52.061 31.638 74.820  1.00 32.56  ? 125 PHE A CD1 1 
ATOM   395   C  CD2 . PHE A 1 61  ? 51.172 30.942 72.721  1.00 29.79  ? 125 PHE A CD2 1 
ATOM   396   C  CE1 . PHE A 1 61  ? 52.722 32.729 74.220  1.00 35.55  ? 125 PHE A CE1 1 
ATOM   397   C  CE2 . PHE A 1 61  ? 51.835 32.013 72.097  1.00 40.07  ? 125 PHE A CE2 1 
ATOM   398   C  CZ  . PHE A 1 61  ? 52.625 32.920 72.859  1.00 34.14  ? 125 PHE A CZ  1 
ATOM   399   N  N   . PHE A 1 62  ? 47.698 28.451 75.217  1.00 32.13  ? 126 PHE A N   1 
ATOM   400   C  CA  . PHE A 1 62  ? 46.990 27.244 75.581  1.00 47.91  ? 126 PHE A CA  1 
ATOM   401   C  C   . PHE A 1 62  ? 46.394 26.571 74.378  1.00 41.72  ? 126 PHE A C   1 
ATOM   402   O  O   . PHE A 1 62  ? 46.560 27.054 73.272  1.00 58.97  ? 126 PHE A O   1 
ATOM   403   C  CB  . PHE A 1 62  ? 45.918 27.566 76.619  1.00 70.21  ? 126 PHE A CB  1 
ATOM   404   C  CG  . PHE A 1 62  ? 44.909 28.551 76.152  1.00 52.73  ? 126 PHE A CG  1 
ATOM   405   C  CD1 . PHE A 1 62  ? 43.754 28.122 75.538  1.00 43.98  ? 126 PHE A CD1 1 
ATOM   406   C  CD2 . PHE A 1 62  ? 45.118 29.905 76.339  1.00 47.52  ? 126 PHE A CD2 1 
ATOM   407   C  CE1 . PHE A 1 62  ? 42.814 29.033 75.110  1.00 64.09  ? 126 PHE A CE1 1 
ATOM   408   C  CE2 . PHE A 1 62  ? 44.184 30.829 75.903  1.00 51.11  ? 126 PHE A CE2 1 
ATOM   409   C  CZ  . PHE A 1 62  ? 43.031 30.396 75.295  1.00 70.58  ? 126 PHE A CZ  1 
ATOM   410   N  N   . VAL A 1 63  ? 45.705 25.456 74.586  1.00 39.51  ? 127 VAL A N   1 
ATOM   411   C  CA  . VAL A 1 63  ? 45.097 24.731 73.472  1.00 42.36  ? 127 VAL A CA  1 
ATOM   412   C  C   . VAL A 1 63  ? 43.609 24.695 73.753  1.00 46.97  ? 127 VAL A C   1 
ATOM   413   O  O   . VAL A 1 63  ? 43.222 24.293 74.840  1.00 68.70  ? 127 VAL A O   1 
ATOM   414   C  CB  . VAL A 1 63  ? 45.697 23.300 73.334  1.00 41.02  ? 127 VAL A CB  1 
ATOM   415   C  CG1 . VAL A 1 63  ? 44.771 22.380 72.587  1.00 47.57  ? 127 VAL A CG1 1 
ATOM   416   C  CG2 . VAL A 1 63  ? 47.069 23.315 72.652  1.00 34.39  ? 127 VAL A CG2 1 
ATOM   417   N  N   . SER A 1 64  ? 42.787 25.149 72.803  1.00 51.62  ? 128 SER A N   1 
ATOM   418   C  CA  . SER A 1 64  ? 41.323 25.229 72.973  1.00 51.90  ? 128 SER A CA  1 
ATOM   419   C  C   . SER A 1 64  ? 40.640 23.867 72.913  1.00 50.78  ? 128 SER A C   1 
ATOM   420   O  O   . SER A 1 64  ? 41.002 23.025 72.094  1.00 66.07  ? 128 SER A O   1 
ATOM   421   C  CB  . SER A 1 64  ? 40.721 26.098 71.881  1.00 64.16  ? 128 SER A CB  1 
ATOM   422   O  OG  . SER A 1 64  ? 40.770 25.417 70.632  1.00 97.89  ? 128 SER A OG  1 
ATOM   423   N  N   . MET A 1 65  ? 39.656 23.670 73.783  1.00 47.59  ? 129 MET A N   1 
ATOM   424   C  CA  . MET A 1 65  ? 38.710 22.559 73.670  1.00 61.87  ? 129 MET A CA  1 
ATOM   425   C  C   . MET A 1 65  ? 37.339 22.985 73.096  1.00 69.45  ? 129 MET A C   1 
ATOM   426   O  O   . MET A 1 65  ? 36.415 22.170 73.005  1.00 76.62  ? 129 MET A O   1 
ATOM   427   C  CB  . MET A 1 65  ? 38.531 21.837 75.015  1.00 59.74  ? 129 MET A CB  1 
ATOM   428   C  CG  . MET A 1 65  ? 39.463 20.642 75.220  1.00 67.84  ? 129 MET A CG  1 
ATOM   429   S  SD  . MET A 1 65  ? 40.650 20.793 76.577  1.00 109.59 ? 129 MET A SD  1 
ATOM   430   C  CE  . MET A 1 65  ? 39.612 20.519 78.036  1.00 66.37  ? 129 MET A CE  1 
ATOM   431   N  N   . GLY A 1 66  ? 37.227 24.244 72.679  1.00 63.12  ? 130 GLY A N   1 
ATOM   432   C  CA  . GLY A 1 66  ? 35.943 24.823 72.277  1.00 62.35  ? 130 GLY A CA  1 
ATOM   433   C  C   . GLY A 1 66  ? 35.362 25.663 73.397  1.00 68.65  ? 130 GLY A C   1 
ATOM   434   O  O   . GLY A 1 66  ? 35.909 25.692 74.499  1.00 71.53  ? 130 GLY A O   1 
ATOM   435   N  N   . TYR A 1 67  ? 34.275 26.373 73.107  1.00 80.68  ? 131 TYR A N   1 
ATOM   436   C  CA  . TYR A 1 67  ? 33.633 27.228 74.097  1.00 76.77  ? 131 TYR A CA  1 
ATOM   437   C  C   . TYR A 1 67  ? 32.856 26.345 75.046  1.00 74.19  ? 131 TYR A C   1 
ATOM   438   O  O   . TYR A 1 67  ? 32.355 25.300 74.655  1.00 76.64  ? 131 TYR A O   1 
ATOM   439   C  CB  . TYR A 1 67  ? 32.707 28.240 73.417  1.00 83.55  ? 131 TYR A CB  1 
ATOM   440   C  CG  . TYR A 1 67  ? 33.405 29.152 72.426  1.00 83.51  ? 131 TYR A CG  1 
ATOM   441   C  CD1 . TYR A 1 67  ? 34.302 30.136 72.854  1.00 83.57  ? 131 TYR A CD1 1 
ATOM   442   C  CD2 . TYR A 1 67  ? 33.165 29.034 71.063  1.00 80.48  ? 131 TYR A CD2 1 
ATOM   443   C  CE1 . TYR A 1 67  ? 34.944 30.976 71.937  1.00 79.41  ? 131 TYR A CE1 1 
ATOM   444   C  CE2 . TYR A 1 67  ? 33.792 29.867 70.144  1.00 86.88  ? 131 TYR A CE2 1 
ATOM   445   C  CZ  . TYR A 1 67  ? 34.682 30.835 70.582  1.00 84.30  ? 131 TYR A CZ  1 
ATOM   446   O  OH  . TYR A 1 67  ? 35.300 31.667 69.662  1.00 81.08  ? 131 TYR A OH  1 
ATOM   447   N  N   . GLY A 1 68  ? 32.750 26.775 76.295  1.00 90.92  ? 132 GLY A N   1 
ATOM   448   C  CA  . GLY A 1 68  ? 32.041 26.010 77.317  1.00 92.83  ? 132 GLY A CA  1 
ATOM   449   C  C   . GLY A 1 68  ? 30.534 25.949 77.135  1.00 83.60  ? 132 GLY A C   1 
ATOM   450   O  O   . GLY A 1 68  ? 29.889 25.040 77.636  1.00 101.56 ? 132 GLY A O   1 
ATOM   451   N  N   . THR A 1 69  ? 29.974 26.915 76.418  1.00 78.49  ? 133 THR A N   1 
ATOM   452   C  CA  . THR A 1 69  ? 28.534 26.978 76.205  1.00 86.98  ? 133 THR A CA  1 
ATOM   453   C  C   . THR A 1 69  ? 28.099 26.128 74.991  1.00 102.50 ? 133 THR A C   1 
ATOM   454   O  O   . THR A 1 69  ? 26.976 25.614 74.951  1.00 100.22 ? 133 THR A O   1 
ATOM   455   C  CB  . THR A 1 69  ? 28.065 28.447 76.079  1.00 87.91  ? 133 THR A CB  1 
ATOM   456   O  OG1 . THR A 1 69  ? 26.688 28.479 75.698  1.00 131.21 ? 133 THR A OG1 1 
ATOM   457   C  CG2 . THR A 1 69  ? 28.908 29.206 75.041  1.00 78.77  ? 133 THR A CG2 1 
ATOM   458   N  N   . THR A 1 70  ? 29.003 25.969 74.024  1.00 109.09 ? 134 THR A N   1 
ATOM   459   C  CA  . THR A 1 70  ? 28.706 25.254 72.791  1.00 104.08 ? 134 THR A CA  1 
ATOM   460   C  C   . THR A 1 70  ? 29.151 23.797 72.907  1.00 109.74 ? 134 THR A C   1 
ATOM   461   O  O   . THR A 1 70  ? 28.876 22.979 72.021  1.00 119.55 ? 134 THR A O   1 
ATOM   462   C  CB  . THR A 1 70  ? 29.409 25.903 71.583  1.00 135.22 ? 134 THR A CB  1 
ATOM   463   O  OG1 . THR A 1 70  ? 30.802 25.558 71.594  1.00 188.10 ? 134 THR A OG1 1 
ATOM   464   C  CG2 . THR A 1 70  ? 29.272 27.411 71.621  1.00 154.80 ? 134 THR A CG2 1 
ATOM   465   N  N   . THR A 1 71  ? 29.848 23.485 73.998  1.00 95.41  ? 135 THR A N   1 
ATOM   466   C  CA  . THR A 1 71  ? 30.326 22.128 74.259  1.00 104.43 ? 135 THR A CA  1 
ATOM   467   C  C   . THR A 1 71  ? 29.360 21.418 75.204  1.00 123.43 ? 135 THR A C   1 
ATOM   468   O  O   . THR A 1 71  ? 29.025 21.946 76.264  1.00 159.05 ? 135 THR A O   1 
ATOM   469   C  CB  . THR A 1 71  ? 31.765 22.139 74.872  1.00 99.31  ? 135 THR A CB  1 
ATOM   470   O  OG1 . THR A 1 71  ? 32.706 22.668 73.926  1.00 89.29  ? 135 THR A OG1 1 
ATOM   471   C  CG2 . THR A 1 71  ? 32.216 20.746 75.281  1.00 81.81  ? 135 THR A CG2 1 
ATOM   472   N  N   . ASN A 1 72  ? 28.904 20.230 74.814  1.00 131.37 ? 136 ASN A N   1 
ATOM   473   C  CA  . ASN A 1 72  ? 28.100 19.394 75.699  1.00 126.73 ? 136 ASN A CA  1 
ATOM   474   C  C   . ASN A 1 72  ? 28.964 18.344 76.400  1.00 131.68 ? 136 ASN A C   1 
ATOM   475   O  O   . ASN A 1 72  ? 29.921 17.847 75.806  1.00 161.27 ? 136 ASN A O   1 
ATOM   476   C  CB  . ASN A 1 72  ? 26.957 18.736 74.935  1.00 130.80 ? 136 ASN A CB  1 
ATOM   477   C  CG  . ASN A 1 72  ? 25.881 18.185 75.860  1.00 167.51 ? 136 ASN A CG  1 
ATOM   478   O  OD1 . ASN A 1 72  ? 25.760 18.604 77.015  1.00 156.90 ? 136 ASN A OD1 1 
ATOM   479   N  ND2 . ASN A 1 72  ? 25.093 17.243 75.356  1.00 176.45 ? 136 ASN A ND2 1 
ATOM   480   N  N   . PHE A 1 73  ? 28.625 18.016 77.653  1.00 136.92 ? 137 PHE A N   1 
ATOM   481   C  CA  . PHE A 1 73  ? 29.437 17.119 78.505  1.00 142.72 ? 137 PHE A CA  1 
ATOM   482   C  C   . PHE A 1 73  ? 29.631 15.705 77.953  1.00 152.37 ? 137 PHE A C   1 
ATOM   483   O  O   . PHE A 1 73  ? 30.730 15.152 78.043  1.00 141.42 ? 137 PHE A O   1 
ATOM   484   C  CB  . PHE A 1 73  ? 28.876 17.039 79.937  1.00 146.93 ? 137 PHE A CB  1 
ATOM   485   C  CG  . PHE A 1 73  ? 29.688 16.154 80.865  1.00 172.23 ? 137 PHE A CG  1 
ATOM   486   C  CD1 . PHE A 1 73  ? 30.937 16.575 81.344  1.00 173.93 ? 137 PHE A CD1 1 
ATOM   487   C  CD2 . PHE A 1 73  ? 29.207 14.903 81.260  1.00 160.22 ? 137 PHE A CD2 1 
ATOM   488   C  CE1 . PHE A 1 73  ? 31.698 15.763 82.200  1.00 151.45 ? 137 PHE A CE1 1 
ATOM   489   C  CE2 . PHE A 1 73  ? 29.960 14.086 82.115  1.00 173.88 ? 137 PHE A CE2 1 
ATOM   490   C  CZ  . PHE A 1 73  ? 31.210 14.521 82.585  1.00 162.56 ? 137 PHE A CZ  1 
ATOM   491   N  N   . ALA A 1 74  ? 28.561 15.134 77.396  1.00 170.99 ? 138 ALA A N   1 
ATOM   492   C  CA  . ALA A 1 74  ? 28.563 13.765 76.860  1.00 158.97 ? 138 ALA A CA  1 
ATOM   493   C  C   . ALA A 1 74  ? 29.622 13.514 75.778  1.00 159.46 ? 138 ALA A C   1 
ATOM   494   O  O   . ALA A 1 74  ? 30.076 12.381 75.617  1.00 137.44 ? 138 ALA A O   1 
ATOM   495   C  CB  . ALA A 1 74  ? 27.172 13.393 76.346  1.00 136.63 ? 138 ALA A CB  1 
ATOM   496   N  N   . ASP A 1 75  ? 29.995 14.569 75.046  1.00 206.26 ? 139 ASP A N   1 
ATOM   497   C  CA  . ASP A 1 75  ? 31.095 14.523 74.070  1.00 183.30 ? 139 ASP A CA  1 
ATOM   498   C  C   . ASP A 1 75  ? 32.432 14.451 74.767  1.00 172.36 ? 139 ASP A C   1 
ATOM   499   O  O   . ASP A 1 75  ? 32.666 15.129 75.768  1.00 187.34 ? 139 ASP A O   1 
ATOM   500   C  CB  . ASP A 1 75  ? 31.127 15.776 73.181  1.00 159.03 ? 139 ASP A CB  1 
ATOM   501   C  CG  . ASP A 1 75  ? 29.958 15.859 72.227  1.00 168.70 ? 139 ASP A CG  1 
ATOM   502   O  OD1 . ASP A 1 75  ? 29.286 14.835 71.994  1.00 204.90 ? 139 ASP A OD1 1 
ATOM   503   O  OD2 . ASP A 1 75  ? 29.713 16.962 71.701  1.00 138.88 ? 139 ASP A OD2 1 
ATOM   504   N  N   . LEU A 1 76  ? 33.310 13.623 74.231  1.00 176.49 ? 140 LEU A N   1 
ATOM   505   C  CA  . LEU A 1 76  ? 34.720 13.760 74.519  1.00 188.26 ? 140 LEU A CA  1 
ATOM   506   C  C   . LEU A 1 76  ? 35.260 14.421 73.265  1.00 142.96 ? 140 LEU A C   1 
ATOM   507   O  O   . LEU A 1 76  ? 34.869 14.042 72.162  1.00 87.68  ? 140 LEU A O   1 
ATOM   508   C  CB  . LEU A 1 76  ? 35.372 12.397 74.803  1.00 216.90 ? 140 LEU A CB  1 
ATOM   509   C  CG  . LEU A 1 76  ? 35.298 11.847 76.244  1.00 206.04 ? 140 LEU A CG  1 
ATOM   510   C  CD1 . LEU A 1 76  ? 33.882 11.412 76.662  1.00 179.32 ? 140 LEU A CD1 1 
ATOM   511   C  CD2 . LEU A 1 76  ? 36.286 10.704 76.457  1.00 171.55 ? 140 LEU A CD2 1 
ATOM   512   N  N   . ILE A 1 77  ? 36.093 15.447 73.431  1.00 151.35 ? 141 ILE A N   1 
ATOM   513   C  CA  . ILE A 1 77  ? 36.681 16.132 72.276  1.00 146.07 ? 141 ILE A CA  1 
ATOM   514   C  C   . ILE A 1 77  ? 38.090 15.631 71.968  1.00 130.44 ? 141 ILE A C   1 
ATOM   515   O  O   . ILE A 1 77  ? 38.784 15.077 72.825  1.00 140.53 ? 141 ILE A O   1 
ATOM   516   C  CB  . ILE A 1 77  ? 36.637 17.679 72.385  1.00 167.64 ? 141 ILE A CB  1 
ATOM   517   C  CG1 . ILE A 1 77  ? 36.930 18.318 71.012  1.00 154.09 ? 141 ILE A CG1 1 
ATOM   518   C  CG2 . ILE A 1 77  ? 37.602 18.167 73.463  1.00 149.68 ? 141 ILE A CG2 1 
ATOM   519   C  CD1 . ILE A 1 77  ? 36.233 19.644 70.742  1.00 154.50 ? 141 ILE A CD1 1 
ATOM   520   N  N   . VAL A 1 78  ? 38.504 15.871 70.735  1.00 96.63  ? 142 VAL A N   1 
ATOM   521   C  CA  . VAL A 1 78  ? 39.584 15.126 70.142  1.00 74.98  ? 142 VAL A CA  1 
ATOM   522   C  C   . VAL A 1 78  ? 40.647 16.051 69.555  1.00 77.79  ? 142 VAL A C   1 
ATOM   523   O  O   . VAL A 1 78  ? 40.315 17.120 69.022  1.00 66.24  ? 142 VAL A O   1 
ATOM   524   C  CB  . VAL A 1 78  ? 39.010 14.202 69.063  1.00 74.27  ? 142 VAL A CB  1 
ATOM   525   C  CG1 . VAL A 1 78  ? 38.149 14.977 68.058  1.00 72.25  ? 142 VAL A CG1 1 
ATOM   526   C  CG2 . VAL A 1 78  ? 40.115 13.414 68.379  1.00 94.89  ? 142 VAL A CG2 1 
ATOM   527   N  N   . SER A 1 79  ? 41.909 15.615 69.642  1.00 66.73  ? 143 SER A N   1 
ATOM   528   C  CA  . SER A 1 79  ? 43.089 16.399 69.264  1.00 55.82  ? 143 SER A CA  1 
ATOM   529   C  C   . SER A 1 79  ? 43.027 17.095 67.897  1.00 59.93  ? 143 SER A C   1 
ATOM   530   O  O   . SER A 1 79  ? 43.599 18.182 67.705  1.00 85.64  ? 143 SER A O   1 
ATOM   531   C  CB  . SER A 1 79  ? 44.338 15.521 69.338  1.00 69.74  ? 143 SER A CB  1 
ATOM   532   O  OG  . SER A 1 79  ? 44.392 14.831 70.578  1.00 98.29  ? 143 SER A OG  1 
ATOM   533   N  N   . GLU A 1 80  ? 42.339 16.486 66.945  1.00 54.55  ? 144 GLU A N   1 
ATOM   534   C  CA  . GLU A 1 80  ? 42.296 17.042 65.590  1.00 69.73  ? 144 GLU A CA  1 
ATOM   535   C  C   . GLU A 1 80  ? 41.448 18.311 65.496  1.00 64.75  ? 144 GLU A C   1 
ATOM   536   O  O   . GLU A 1 80  ? 41.556 19.066 64.545  1.00 74.63  ? 144 GLU A O   1 
ATOM   537   C  CB  . GLU A 1 80  ? 41.800 16.004 64.575  1.00 77.77  ? 144 GLU A CB  1 
ATOM   538   C  CG  . GLU A 1 80  ? 42.776 14.848 64.294  1.00 86.92  ? 144 GLU A CG  1 
ATOM   539   C  CD  . GLU A 1 80  ? 42.928 13.877 65.469  1.00 93.97  ? 144 GLU A CD  1 
ATOM   540   O  OE1 . GLU A 1 80  ? 42.046 13.812 66.354  1.00 94.86  ? 144 GLU A OE1 1 
ATOM   541   O  OE2 . GLU A 1 80  ? 43.951 13.173 65.506  1.00 121.17 ? 144 GLU A OE2 1 
ATOM   542   N  N   . GLN A 1 81  ? 40.608 18.548 66.481  1.00 53.38  ? 145 GLN A N   1 
ATOM   543   C  CA  . GLN A 1 81  ? 39.723 19.688 66.440  1.00 57.30  ? 145 GLN A CA  1 
ATOM   544   C  C   . GLN A 1 81  ? 40.352 20.875 67.154  1.00 58.58  ? 145 GLN A C   1 
ATOM   545   O  O   . GLN A 1 81  ? 39.762 21.953 67.224  1.00 65.12  ? 145 GLN A O   1 
ATOM   546   C  CB  . GLN A 1 81  ? 38.394 19.328 67.101  1.00 72.34  ? 145 GLN A CB  1 
ATOM   547   C  CG  . GLN A 1 81  ? 37.616 18.233 66.368  1.00 75.15  ? 145 GLN A CG  1 
ATOM   548   C  CD  . GLN A 1 81  ? 36.186 18.090 66.858  1.00 97.26  ? 145 GLN A CD  1 
ATOM   549   O  OE1 . GLN A 1 81  ? 35.926 17.628 67.973  1.00 120.09 ? 145 GLN A OE1 1 
ATOM   550   N  NE2 . GLN A 1 81  ? 35.247 18.489 66.017  1.00 117.72 ? 145 GLN A NE2 1 
ATOM   551   N  N   . MET A 1 82  ? 41.565 20.681 67.654  1.00 50.08  ? 146 MET A N   1 
ATOM   552   C  CA  . MET A 1 82  ? 42.162 21.591 68.626  1.00 42.56  ? 146 MET A CA  1 
ATOM   553   C  C   . MET A 1 82  ? 43.041 22.637 67.963  1.00 41.88  ? 146 MET A C   1 
ATOM   554   O  O   . MET A 1 82  ? 43.712 22.371 66.969  1.00 54.13  ? 146 MET A O   1 
ATOM   555   C  CB  . MET A 1 82  ? 42.972 20.803 69.664  1.00 38.50  ? 146 MET A CB  1 
ATOM   556   C  CG  . MET A 1 82  ? 42.153 20.097 70.694  1.00 40.29  ? 146 MET A CG  1 
ATOM   557   S  SD  . MET A 1 82  ? 43.116 18.993 71.730  1.00 69.54  ? 146 MET A SD  1 
ATOM   558   C  CE  . MET A 1 82  ? 41.845 18.521 72.924  1.00 43.61  ? 146 MET A CE  1 
ATOM   559   N  N   . ASN A 1 83  ? 43.048 23.816 68.567  1.00 41.58  ? 147 ASN A N   1 
ATOM   560   C  CA  . ASN A 1 83  ? 43.724 25.010 68.059  1.00 42.47  ? 147 ASN A CA  1 
ATOM   561   C  C   . ASN A 1 83  ? 44.525 25.715 69.157  1.00 46.19  ? 147 ASN A C   1 
ATOM   562   O  O   . ASN A 1 83  ? 44.144 25.748 70.329  1.00 54.05  ? 147 ASN A O   1 
ATOM   563   C  CB  . ASN A 1 83  ? 42.693 26.036 67.570  1.00 44.18  ? 147 ASN A CB  1 
ATOM   564   C  CG  . ASN A 1 83  ? 42.063 25.659 66.268  1.00 45.54  ? 147 ASN A CG  1 
ATOM   565   O  OD1 . ASN A 1 83  ? 42.716 25.162 65.361  1.00 61.61  ? 147 ASN A OD1 1 
ATOM   566   N  ND2 . ASN A 1 83  ? 40.773 25.888 66.169  1.00 52.88  ? 147 ASN A ND2 1 
ATOM   567   N  N   . VAL A 1 84  ? 45.614 26.344 68.765  1.00 36.78  ? 148 VAL A N   1 
ATOM   568   C  CA  . VAL A 1 84  ? 46.469 26.973 69.736  1.00 33.83  ? 148 VAL A CA  1 
ATOM   569   C  C   . VAL A 1 84  ? 46.175 28.453 69.794  1.00 32.60  ? 148 VAL A C   1 
ATOM   570   O  O   . VAL A 1 84  ? 46.436 29.191 68.840  1.00 46.26  ? 148 VAL A O   1 
ATOM   571   C  CB  . VAL A 1 84  ? 47.971 26.794 69.373  1.00 33.65  ? 148 VAL A CB  1 
ATOM   572   C  CG1 . VAL A 1 84  ? 48.855 27.488 70.428  1.00 29.86  ? 148 VAL A CG1 1 
ATOM   573   C  CG2 . VAL A 1 84  ? 48.342 25.334 69.180  1.00 24.20  ? 148 VAL A CG2 1 
ATOM   574   N  N   . TYR A 1 85  ? 45.667 28.890 70.928  1.00 32.38  ? 149 TYR A N   1 
ATOM   575   C  CA  . TYR A 1 85  ? 45.472 30.314 71.185  1.00 36.71  ? 149 TYR A CA  1 
ATOM   576   C  C   . TYR A 1 85  ? 46.411 30.935 72.170  1.00 32.93  ? 149 TYR A C   1 
ATOM   577   O  O   . TYR A 1 85  ? 47.039 30.278 72.959  1.00 54.52  ? 149 TYR A O   1 
ATOM   578   C  CB  . TYR A 1 85  ? 44.090 30.565 71.691  1.00 37.85  ? 149 TYR A CB  1 
ATOM   579   C  CG  . TYR A 1 85  ? 43.022 30.273 70.685  1.00 46.80  ? 149 TYR A CG  1 
ATOM   580   C  CD1 . TYR A 1 85  ? 42.562 31.278 69.856  1.00 52.59  ? 149 TYR A CD1 1 
ATOM   581   C  CD2 . TYR A 1 85  ? 42.445 28.995 70.584  1.00 50.71  ? 149 TYR A CD2 1 
ATOM   582   C  CE1 . TYR A 1 85  ? 41.551 31.049 68.955  1.00 75.56  ? 149 TYR A CE1 1 
ATOM   583   C  CE2 . TYR A 1 85  ? 41.420 28.750 69.681  1.00 63.17  ? 149 TYR A CE2 1 
ATOM   584   C  CZ  . TYR A 1 85  ? 40.979 29.793 68.869  1.00 77.88  ? 149 TYR A CZ  1 
ATOM   585   O  OH  . TYR A 1 85  ? 39.991 29.603 67.938  1.00 94.92  ? 149 TYR A OH  1 
ATOM   586   N  N   . SER A 1 86  ? 46.472 32.241 72.106  1.00 41.72  ? 150 SER A N   1 
ATOM   587   C  CA  . SER A 1 86  ? 47.283 33.059 72.982  1.00 52.30  ? 150 SER A CA  1 
ATOM   588   C  C   . SER A 1 86  ? 46.354 34.109 73.631  1.00 41.86  ? 150 SER A C   1 
ATOM   589   O  O   . SER A 1 86  ? 45.277 34.376 73.131  1.00 61.46  ? 150 SER A O   1 
ATOM   590   C  CB  . SER A 1 86  ? 48.394 33.718 72.152  1.00 40.45  ? 150 SER A CB  1 
ATOM   591   O  OG  . SER A 1 86  ? 49.092 34.630 72.947  1.00 71.37  ? 150 SER A OG  1 
ATOM   592   N  N   . VAL A 1 87  ? 46.773 34.695 74.736  1.00 40.36  ? 151 VAL A N   1 
ATOM   593   C  CA  . VAL A 1 87  ? 46.013 35.740 75.442  1.00 44.47  ? 151 VAL A CA  1 
ATOM   594   C  C   . VAL A 1 87  ? 47.058 36.462 76.287  1.00 49.65  ? 151 VAL A C   1 
ATOM   595   O  O   . VAL A 1 87  ? 48.161 35.925 76.480  1.00 67.55  ? 151 VAL A O   1 
ATOM   596   C  CB  . VAL A 1 87  ? 44.928 35.134 76.345  1.00 45.64  ? 151 VAL A CB  1 
ATOM   597   C  CG1 . VAL A 1 87  ? 45.553 34.555 77.618  1.00 51.78  ? 151 VAL A CG1 1 
ATOM   598   C  CG2 . VAL A 1 87  ? 43.950 36.130 76.716  1.00 45.59  ? 151 VAL A CG2 1 
ATOM   599   N  N   . LYS A 1 88  ? 46.760 37.664 76.774  1.00 43.79  ? 152 LYS A N   1 
ATOM   600   C  CA  . LYS A 1 88  ? 47.773 38.379 77.549  1.00 51.80  ? 152 LYS A CA  1 
ATOM   601   C  C   . LYS A 1 88  ? 47.667 37.862 78.977  1.00 62.30  ? 152 LYS A C   1 
ATOM   602   O  O   . LYS A 1 88  ? 46.548 37.725 79.487  1.00 65.97  ? 152 LYS A O   1 
ATOM   603   C  CB  . LYS A 1 88  ? 47.566 39.888 77.515  1.00 51.12  ? 152 LYS A CB  1 
ATOM   604   C  CG  . LYS A 1 88  ? 48.804 40.661 78.023  1.00 76.96  ? 152 LYS A CG  1 
ATOM   605   C  CD  . LYS A 1 88  ? 48.485 42.005 78.689  1.00 71.65  ? 152 LYS A CD  1 
ATOM   606   C  CE  . LYS A 1 88  ? 48.102 41.810 80.163  1.00 84.25  ? 152 LYS A CE  1 
ATOM   607   N  NZ  . LYS A 1 88  ? 47.518 43.045 80.762  1.00 144.14 ? 152 LYS A NZ  1 
ATOM   608   N  N   . LEU A 1 89  ? 48.793 37.561 79.629  1.00 40.25  ? 153 LEU A N   1 
ATOM   609   C  CA  . LEU A 1 89  ? 48.686 36.975 80.950  1.00 35.58  ? 153 LEU A CA  1 
ATOM   610   C  C   . LEU A 1 89  ? 48.045 37.991 81.855  1.00 45.60  ? 153 LEU A C   1 
ATOM   611   O  O   . LEU A 1 89  ? 48.518 39.139 81.987  1.00 56.62  ? 153 LEU A O   1 
ATOM   612   C  CB  . LEU A 1 89  ? 50.038 36.541 81.509  1.00 41.32  ? 153 LEU A CB  1 
ATOM   613   C  CG  . LEU A 1 89  ? 50.061 36.047 82.974  1.00 44.13  ? 153 LEU A CG  1 
ATOM   614   C  CD1 . LEU A 1 89  ? 49.294 34.729 83.142  1.00 42.85  ? 153 LEU A CD1 1 
ATOM   615   C  CD2 . LEU A 1 89  ? 51.468 35.901 83.528  1.00 37.56  ? 153 LEU A CD2 1 
ATOM   616   N  N   . GLY A 1 90  ? 46.958 37.558 82.483  1.00 61.38  ? 154 GLY A N   1 
ATOM   617   C  CA  . GLY A 1 90  ? 46.161 38.426 83.332  1.00 53.63  ? 154 GLY A CA  1 
ATOM   618   C  C   . GLY A 1 90  ? 44.826 38.685 82.690  1.00 47.85  ? 154 GLY A C   1 
ATOM   619   O  O   . GLY A 1 90  ? 43.925 39.219 83.308  1.00 64.85  ? 154 GLY A O   1 
ATOM   620   N  N   . ASP A 1 91  ? 44.700 38.323 81.428  1.00 56.02  ? 155 ASP A N   1 
ATOM   621   C  CA  . ASP A 1 91  ? 43.417 38.442 80.764  1.00 73.14  ? 155 ASP A CA  1 
ATOM   622   C  C   . ASP A 1 91  ? 42.760 37.087 80.793  1.00 63.42  ? 155 ASP A C   1 
ATOM   623   O  O   . ASP A 1 91  ? 43.438 36.076 80.780  1.00 78.56  ? 155 ASP A O   1 
ATOM   624   C  CB  . ASP A 1 91  ? 43.558 38.981 79.330  1.00 77.57  ? 155 ASP A CB  1 
ATOM   625   C  CG  . ASP A 1 91  ? 43.783 40.493 79.285  1.00 109.57 ? 155 ASP A CG  1 
ATOM   626   O  OD1 . ASP A 1 91  ? 43.495 41.188 80.293  1.00 133.02 ? 155 ASP A OD1 1 
ATOM   627   O  OD2 . ASP A 1 91  ? 44.242 40.984 78.230  1.00 116.44 ? 155 ASP A OD2 1 
ATOM   628   N  N   . PRO A 1 92  ? 41.436 37.060 80.882  1.00 62.57  ? 156 PRO A N   1 
ATOM   629   C  CA  . PRO A 1 92  ? 40.731 35.800 80.844  1.00 52.56  ? 156 PRO A CA  1 
ATOM   630   C  C   . PRO A 1 92  ? 40.514 35.390 79.398  1.00 50.67  ? 156 PRO A C   1 
ATOM   631   O  O   . PRO A 1 92  ? 40.420 36.264 78.548  1.00 70.89  ? 156 PRO A O   1 
ATOM   632   C  CB  . PRO A 1 92  ? 39.412 36.147 81.521  1.00 52.46  ? 156 PRO A CB  1 
ATOM   633   C  CG  . PRO A 1 92  ? 39.175 37.568 81.144  1.00 77.27  ? 156 PRO A CG  1 
ATOM   634   C  CD  . PRO A 1 92  ? 40.541 38.184 81.211  1.00 83.86  ? 156 PRO A CD  1 
ATOM   635   N  N   . PRO A 1 93  ? 40.442 34.077 79.113  1.00 47.02  ? 157 PRO A N   1 
ATOM   636   C  CA  . PRO A 1 93  ? 40.135 33.587 77.744  1.00 50.13  ? 157 PRO A CA  1 
ATOM   637   C  C   . PRO A 1 93  ? 38.687 33.782 77.260  1.00 49.12  ? 157 PRO A C   1 
ATOM   638   O  O   . PRO A 1 93  ? 38.020 32.827 76.902  1.00 54.05  ? 157 PRO A O   1 
ATOM   639   C  CB  . PRO A 1 93  ? 40.524 32.097 77.788  1.00 42.06  ? 157 PRO A CB  1 
ATOM   640   C  CG  . PRO A 1 93  ? 40.458 31.743 79.259  1.00 48.49  ? 157 PRO A CG  1 
ATOM   641   C  CD  . PRO A 1 93  ? 40.920 32.992 79.988  1.00 45.38  ? 157 PRO A CD  1 
ATOM   642   N  N   . THR A 1 94  ? 38.228 35.028 77.226  1.00 74.71  ? 158 THR A N   1 
ATOM   643   C  CA  . THR A 1 94  ? 37.001 35.386 76.507  1.00 72.52  ? 158 THR A CA  1 
ATOM   644   C  C   . THR A 1 94  ? 37.281 35.425 75.015  1.00 68.88  ? 158 THR A C   1 
ATOM   645   O  O   . THR A 1 94  ? 38.397 35.716 74.582  1.00 67.75  ? 158 THR A O   1 
ATOM   646   C  CB  . THR A 1 94  ? 36.418 36.759 76.933  1.00 69.92  ? 158 THR A CB  1 
ATOM   647   O  OG1 . THR A 1 94  ? 37.472 37.721 77.026  1.00 87.48  ? 158 THR A OG1 1 
ATOM   648   C  CG2 . THR A 1 94  ? 35.724 36.655 78.278  1.00 101.19 ? 158 THR A CG2 1 
ATOM   649   N  N   . PRO A 1 95  ? 36.256 35.138 74.215  1.00 66.35  ? 159 PRO A N   1 
ATOM   650   C  CA  . PRO A 1 95  ? 36.368 35.151 72.758  1.00 67.32  ? 159 PRO A CA  1 
ATOM   651   C  C   . PRO A 1 95  ? 37.010 36.434 72.220  1.00 83.37  ? 159 PRO A C   1 
ATOM   652   O  O   . PRO A 1 95  ? 37.739 36.395 71.226  1.00 95.47  ? 159 PRO A O   1 
ATOM   653   C  CB  . PRO A 1 95  ? 34.922 35.070 72.313  1.00 58.14  ? 159 PRO A CB  1 
ATOM   654   C  CG  . PRO A 1 95  ? 34.228 34.381 73.443  1.00 50.62  ? 159 PRO A CG  1 
ATOM   655   C  CD  . PRO A 1 95  ? 34.902 34.794 74.676  1.00 53.19  ? 159 PRO A CD  1 
ATOM   656   N  N   . ASP A 1 96  ? 36.754 37.550 72.897  1.00 78.44  ? 160 ASP A N   1 
ATOM   657   C  CA  . ASP A 1 96  ? 37.262 38.837 72.476  1.00 77.10  ? 160 ASP A CA  1 
ATOM   658   C  C   . ASP A 1 96  ? 38.737 39.013 72.797  1.00 72.14  ? 160 ASP A C   1 
ATOM   659   O  O   . ASP A 1 96  ? 39.444 39.767 72.129  1.00 68.42  ? 160 ASP A O   1 
ATOM   660   C  CB  . ASP A 1 96  ? 36.435 39.926 73.127  1.00 88.77  ? 160 ASP A CB  1 
ATOM   661   C  CG  . ASP A 1 96  ? 34.963 39.744 72.878  1.00 93.92  ? 160 ASP A CG  1 
ATOM   662   O  OD1 . ASP A 1 96  ? 34.593 39.053 71.907  1.00 100.35 ? 160 ASP A OD1 1 
ATOM   663   O  OD2 . ASP A 1 96  ? 34.171 40.298 73.655  1.00 113.71 ? 160 ASP A OD2 1 
ATOM   664   N  N   . LYS A 1 97  ? 39.207 38.302 73.808  1.00 62.44  ? 161 LYS A N   1 
ATOM   665   C  CA  . LYS A 1 97  ? 40.604 38.415 74.189  1.00 59.54  ? 161 LYS A CA  1 
ATOM   666   C  C   . LYS A 1 97  ? 41.520 37.464 73.431  1.00 62.36  ? 161 LYS A C   1 
ATOM   667   O  O   . LYS A 1 97  ? 42.736 37.666 73.390  1.00 76.14  ? 161 LYS A O   1 
ATOM   668   C  CB  . LYS A 1 97  ? 40.763 38.180 75.677  1.00 55.02  ? 161 LYS A CB  1 
ATOM   669   C  CG  . LYS A 1 97  ? 40.304 39.330 76.549  1.00 64.71  ? 161 LYS A CG  1 
ATOM   670   C  CD  . LYS A 1 97  ? 40.984 40.616 76.172  1.00 74.48  ? 161 LYS A CD  1 
ATOM   671   C  CE  . LYS A 1 97  ? 40.676 41.685 77.205  1.00 78.89  ? 161 LYS A CE  1 
ATOM   672   N  NZ  . LYS A 1 97  ? 41.254 42.969 76.744  1.00 104.30 ? 161 LYS A NZ  1 
ATOM   673   N  N   . LEU A 1 98  ? 40.951 36.426 72.833  1.00 67.89  ? 162 LEU A N   1 
ATOM   674   C  CA  . LEU A 1 98  ? 41.784 35.373 72.245  1.00 56.85  ? 162 LEU A CA  1 
ATOM   675   C  C   . LEU A 1 98  ? 42.556 35.886 71.056  1.00 49.86  ? 162 LEU A C   1 
ATOM   676   O  O   . LEU A 1 98  ? 42.066 36.709 70.287  1.00 72.73  ? 162 LEU A O   1 
ATOM   677   C  CB  . LEU A 1 98  ? 40.943 34.177 71.822  1.00 64.90  ? 162 LEU A CB  1 
ATOM   678   C  CG  . LEU A 1 98  ? 40.269 33.410 72.948  1.00 78.99  ? 162 LEU A CG  1 
ATOM   679   C  CD1 . LEU A 1 98  ? 39.935 32.022 72.442  1.00 100.00 ? 162 LEU A CD1 1 
ATOM   680   C  CD2 . LEU A 1 98  ? 41.195 33.344 74.155  1.00 70.69  ? 162 LEU A CD2 1 
ATOM   681   N  N   . LYS A 1 99  ? 43.784 35.422 70.923  1.00 44.48  ? 163 LYS A N   1 
ATOM   682   C  CA  . LYS A 1 99  ? 44.521 35.573 69.661  1.00 48.93  ? 163 LYS A CA  1 
ATOM   683   C  C   . LYS A 1 99  ? 44.830 34.221 68.995  1.00 42.25  ? 163 LYS A C   1 
ATOM   684   O  O   . LYS A 1 99  ? 45.572 33.418 69.515  1.00 48.87  ? 163 LYS A O   1 
ATOM   685   C  CB  . LYS A 1 99  ? 45.808 36.340 69.881  1.00 42.65  ? 163 LYS A CB  1 
ATOM   686   C  CG  . LYS A 1 99  ? 46.702 36.286 68.674  1.00 40.27  ? 163 LYS A CG  1 
ATOM   687   C  CD  . LYS A 1 99  ? 47.609 37.464 68.706  1.00 64.13  ? 163 LYS A CD  1 
ATOM   688   C  CE  . LYS A 1 99  ? 48.970 37.145 68.136  1.00 65.18  ? 163 LYS A CE  1 
ATOM   689   N  NZ  . LYS A 1 99  ? 49.025 37.497 66.689  1.00 102.09 ? 163 LYS A NZ  1 
ATOM   690   N  N   . PHE A 1 100 ? 44.230 33.942 67.863  1.00 44.08  ? 164 PHE A N   1 
ATOM   691   C  CA  . PHE A 1 100 ? 44.492 32.663 67.244  1.00 46.63  ? 164 PHE A CA  1 
ATOM   692   C  C   . PHE A 1 100 ? 45.989 32.587 66.938  1.00 43.14  ? 164 PHE A C   1 
ATOM   693   O  O   . PHE A 1 100 ? 46.568 33.563 66.435  1.00 46.23  ? 164 PHE A O   1 
ATOM   694   C  CB  . PHE A 1 100 ? 43.669 32.519 65.968  1.00 44.09  ? 164 PHE A CB  1 
ATOM   695   C  CG  . PHE A 1 100 ? 43.789 31.190 65.355  1.00 42.56  ? 164 PHE A CG  1 
ATOM   696   C  CD1 . PHE A 1 100 ? 44.938 30.830 64.656  1.00 43.04  ? 164 PHE A CD1 1 
ATOM   697   C  CD2 . PHE A 1 100 ? 42.762 30.266 65.501  1.00 41.64  ? 164 PHE A CD2 1 
ATOM   698   C  CE1 . PHE A 1 100 ? 45.048 29.553 64.094  1.00 41.36  ? 164 PHE A CE1 1 
ATOM   699   C  CE2 . PHE A 1 100 ? 42.849 28.993 64.943  1.00 36.27  ? 164 PHE A CE2 1 
ATOM   700   C  CZ  . PHE A 1 100 ? 43.989 28.628 64.250  1.00 40.75  ? 164 PHE A CZ  1 
ATOM   701   N  N   . GLU A 1 101 ? 46.613 31.450 67.252  1.00 38.78  ? 165 GLU A N   1 
ATOM   702   C  CA  . GLU A 1 101 ? 48.057 31.323 67.079  1.00 42.04  ? 165 GLU A CA  1 
ATOM   703   C  C   . GLU A 1 101 ? 48.449 30.326 66.023  1.00 46.90  ? 165 GLU A C   1 
ATOM   704   O  O   . GLU A 1 101 ? 49.274 30.623 65.142  1.00 52.79  ? 165 GLU A O   1 
ATOM   705   C  CB  . GLU A 1 101 ? 48.756 31.031 68.381  1.00 45.28  ? 165 GLU A CB  1 
ATOM   706   C  CG  . GLU A 1 101 ? 48.947 32.305 69.282  1.00 72.12  ? 165 GLU A CG  1 
ATOM   707   C  CD  . GLU A 1 101 ? 50.026 33.306 68.791  1.00 67.42  ? 165 GLU A CD  1 
ATOM   708   O  OE1 . GLU A 1 101 ? 50.471 33.196 67.631  1.00 82.39  ? 165 GLU A OE1 1 
ATOM   709   O  OE2 . GLU A 1 101 ? 50.420 34.214 69.568  1.00 89.19  ? 165 GLU A OE2 1 
ATOM   710   N  N   . ALA A 1 102 ? 47.836 29.156 66.085  1.00 41.35  ? 166 ALA A N   1 
ATOM   711   C  CA  . ALA A 1 102 ? 48.006 28.157 65.033  1.00 38.08  ? 166 ALA A CA  1 
ATOM   712   C  C   . ALA A 1 102 ? 46.981 27.022 65.174  1.00 42.61  ? 166 ALA A C   1 
ATOM   713   O  O   . ALA A 1 102 ? 46.211 27.021 66.136  1.00 41.24  ? 166 ALA A O   1 
ATOM   714   C  CB  . ALA A 1 102 ? 49.393 27.612 65.079  1.00 32.69  ? 166 ALA A CB  1 
ATOM   715   N  N   . VAL A 1 103 ? 46.969 26.061 64.234  1.00 39.35  ? 167 VAL A N   1 
ATOM   716   C  CA  . VAL A 1 103 ? 46.155 24.845 64.423  1.00 41.58  ? 167 VAL A CA  1 
ATOM   717   C  C   . VAL A 1 103 ? 47.030 23.755 64.962  1.00 47.01  ? 167 VAL A C   1 
ATOM   718   O  O   . VAL A 1 103 ? 48.106 23.495 64.423  1.00 67.87  ? 167 VAL A O   1 
ATOM   719   C  CB  . VAL A 1 103 ? 45.568 24.320 63.143  1.00 47.24  ? 167 VAL A CB  1 
ATOM   720   C  CG1 . VAL A 1 103 ? 44.486 25.271 62.621  1.00 61.87  ? 167 VAL A CG1 1 
ATOM   721   C  CG2 . VAL A 1 103 ? 46.668 24.184 62.132  1.00 79.85  ? 167 VAL A CG2 1 
ATOM   722   N  N   . GLY A 1 104 ? 46.578 23.109 66.023  1.00 46.29  ? 168 GLY A N   1 
ATOM   723   C  CA  . GLY A 1 104 ? 47.346 22.026 66.612  1.00 40.62  ? 168 GLY A CA  1 
ATOM   724   C  C   . GLY A 1 104 ? 46.813 21.647 67.965  1.00 44.94  ? 168 GLY A C   1 
ATOM   725   O  O   . GLY A 1 104 ? 45.974 22.362 68.539  1.00 36.20  ? 168 GLY A O   1 
ATOM   726   N  N   . TRP A 1 105 ? 47.301 20.523 68.482  1.00 53.06  ? 169 TRP A N   1 
ATOM   727   C  CA  . TRP A 1 105 ? 46.885 20.037 69.798  1.00 49.51  ? 169 TRP A CA  1 
ATOM   728   C  C   . TRP A 1 105 ? 48.004 20.131 70.794  1.00 44.59  ? 169 TRP A C   1 
ATOM   729   O  O   . TRP A 1 105 ? 47.887 19.660 71.905  1.00 48.93  ? 169 TRP A O   1 
ATOM   730   C  CB  . TRP A 1 105 ? 46.389 18.610 69.693  1.00 40.94  ? 169 TRP A CB  1 
ATOM   731   C  CG  . TRP A 1 105 ? 47.442 17.661 69.197  1.00 41.20  ? 169 TRP A CG  1 
ATOM   732   C  CD1 . TRP A 1 105 ? 48.554 17.185 69.882  1.00 48.21  ? 169 TRP A CD1 1 
ATOM   733   C  CD2 . TRP A 1 105 ? 47.503 17.028 67.893  1.00 39.37  ? 169 TRP A CD2 1 
ATOM   734   N  NE1 . TRP A 1 105 ? 49.283 16.329 69.090  1.00 56.91  ? 169 TRP A NE1 1 
ATOM   735   C  CE2 . TRP A 1 105 ? 48.702 16.191 67.892  1.00 48.94  ? 169 TRP A CE2 1 
ATOM   736   C  CE3 . TRP A 1 105 ? 46.723 17.066 66.779  1.00 46.50  ? 169 TRP A CE3 1 
ATOM   737   C  CZ2 . TRP A 1 105 ? 49.071 15.441 66.798  1.00 58.92  ? 169 TRP A CZ2 1 
ATOM   738   C  CZ3 . TRP A 1 105 ? 47.103 16.314 65.667  1.00 60.75  ? 169 TRP A CZ3 1 
ATOM   739   C  CH2 . TRP A 1 105 ? 48.253 15.519 65.677  1.00 66.13  ? 169 TRP A CH2 1 
ATOM   740   N  N   . SER A 1 106 ? 49.117 20.714 70.387  1.00 41.63  ? 170 SER A N   1 
ATOM   741   C  CA  . SER A 1 106 ? 50.255 20.862 71.289  1.00 51.62  ? 170 SER A CA  1 
ATOM   742   C  C   . SER A 1 106 ? 51.220 21.928 70.764  1.00 54.19  ? 170 SER A C   1 
ATOM   743   O  O   . SER A 1 106 ? 51.474 22.050 69.551  1.00 52.39  ? 170 SER A O   1 
ATOM   744   C  CB  . SER A 1 106 ? 50.963 19.522 71.575  1.00 54.49  ? 170 SER A CB  1 
ATOM   745   O  OG  . SER A 1 106 ? 52.326 19.716 71.945  1.00 72.92  ? 170 SER A OG  1 
ATOM   746   N  N   . ALA A 1 107 ? 51.742 22.719 71.694  1.00 40.49  ? 171 ALA A N   1 
ATOM   747   C  CA  . ALA A 1 107 ? 52.376 23.955 71.318  1.00 38.71  ? 171 ALA A CA  1 
ATOM   748   C  C   . ALA A 1 107 ? 53.413 24.405 72.317  1.00 42.28  ? 171 ALA A C   1 
ATOM   749   O  O   . ALA A 1 107 ? 53.296 24.166 73.486  1.00 51.48  ? 171 ALA A O   1 
ATOM   750   C  CB  . ALA A 1 107 ? 51.319 25.065 71.137  1.00 32.63  ? 171 ALA A CB  1 
ATOM   751   N  N   . SER A 1 108 ? 54.419 25.094 71.815  1.00 43.10  ? 172 SER A N   1 
ATOM   752   C  CA  . SER A 1 108 ? 55.411 25.750 72.603  1.00 40.32  ? 172 SER A CA  1 
ATOM   753   C  C   . SER A 1 108 ? 55.754 27.072 71.899  1.00 44.92  ? 172 SER A C   1 
ATOM   754   O  O   . SER A 1 108 ? 55.564 27.198 70.675  1.00 47.51  ? 172 SER A O   1 
ATOM   755   C  CB  . SER A 1 108 ? 56.639 24.846 72.686  1.00 51.29  ? 172 SER A CB  1 
ATOM   756   O  OG  . SER A 1 108 ? 57.846 25.594 72.680  1.00 64.16  ? 172 SER A OG  1 
ATOM   757   N  N   . SER A 1 109 ? 56.277 28.046 72.647  1.00 38.53  ? 173 SER A N   1 
ATOM   758   C  CA  . SER A 1 109 ? 56.532 29.358 72.065  1.00 37.84  ? 173 SER A CA  1 
ATOM   759   C  C   . SER A 1 109 ? 57.502 30.182 72.867  1.00 40.39  ? 173 SER A C   1 
ATOM   760   O  O   . SER A 1 109 ? 57.766 29.894 74.029  1.00 46.55  ? 173 SER A O   1 
ATOM   761   C  CB  . SER A 1 109 ? 55.218 30.152 71.903  1.00 53.17  ? 173 SER A CB  1 
ATOM   762   O  OG  . SER A 1 109 ? 54.660 30.555 73.152  1.00 46.75  ? 173 SER A OG  1 
ATOM   763   N  N   . CYS A 1 110 ? 58.016 31.225 72.232  1.00 37.56  ? 174 CYS A N   1 
ATOM   764   C  CA  . CYS A 1 110 ? 59.069 32.038 72.789  1.00 41.78  ? 174 CYS A CA  1 
ATOM   765   C  C   . CYS A 1 110 ? 59.277 33.202 71.866  1.00 49.79  ? 174 CYS A C   1 
ATOM   766   O  O   . CYS A 1 110 ? 59.188 33.059 70.635  1.00 51.81  ? 174 CYS A O   1 
ATOM   767   C  CB  . CYS A 1 110 ? 60.380 31.255 72.930  1.00 49.37  ? 174 CYS A CB  1 
ATOM   768   S  SG  . CYS A 1 110 ? 60.758 30.103 71.590  1.00 71.88  ? 174 CYS A SG  1 
ATOM   769   N  N   . HIS A 1 111 ? 59.562 34.357 72.463  1.00 44.32  ? 175 HIS A N   1 
ATOM   770   C  CA  . HIS A 1 111 ? 59.736 35.568 71.705  1.00 40.18  ? 175 HIS A CA  1 
ATOM   771   C  C   . HIS A 1 111 ? 61.182 35.935 71.608  1.00 44.12  ? 175 HIS A C   1 
ATOM   772   O  O   . HIS A 1 111 ? 61.834 36.077 72.619  1.00 66.62  ? 175 HIS A O   1 
ATOM   773   C  CB  . HIS A 1 111 ? 58.988 36.660 72.403  1.00 54.24  ? 175 HIS A CB  1 
ATOM   774   C  CG  . HIS A 1 111 ? 58.844 37.903 71.591  1.00 56.66  ? 175 HIS A CG  1 
ATOM   775   N  ND1 . HIS A 1 111 ? 59.809 38.826 71.507  1.00 57.63  ? 175 HIS A ND1 1 
ATOM   776   C  CD2 . HIS A 1 111 ? 57.790 38.355 70.815  1.00 60.95  ? 175 HIS A CD2 1 
ATOM   777   C  CE1 . HIS A 1 111 ? 59.397 39.822 70.708  1.00 74.93  ? 175 HIS A CE1 1 
ATOM   778   N  NE2 . HIS A 1 111 ? 58.159 39.530 70.281  1.00 52.86  ? 175 HIS A NE2 1 
ATOM   779   N  N   . ASP A 1 112 ? 61.705 36.113 70.400  1.00 51.07  ? 176 ASP A N   1 
ATOM   780   C  CA  . ASP A 1 112 ? 63.139 36.435 70.220  1.00 50.82  ? 176 ASP A CA  1 
ATOM   781   C  C   . ASP A 1 112 ? 63.551 37.882 70.360  1.00 54.73  ? 176 ASP A C   1 
ATOM   782   O  O   . ASP A 1 112 ? 64.743 38.160 70.365  1.00 61.33  ? 176 ASP A O   1 
ATOM   783   C  CB  . ASP A 1 112 ? 63.674 35.920 68.892  1.00 51.60  ? 176 ASP A CB  1 
ATOM   784   C  CG  . ASP A 1 112 ? 63.021 36.567 67.691  1.00 61.18  ? 176 ASP A CG  1 
ATOM   785   O  OD1 . ASP A 1 112 ? 62.197 37.508 67.837  1.00 70.53  ? 176 ASP A OD1 1 
ATOM   786   O  OD2 . ASP A 1 112 ? 63.355 36.105 66.574  1.00 77.86  ? 176 ASP A OD2 1 
ATOM   787   N  N   . GLY A 1 113 ? 62.578 38.785 70.482  1.00 62.91  ? 177 GLY A N   1 
ATOM   788   C  CA  . GLY A 1 113 ? 62.844 40.225 70.532  1.00 58.94  ? 177 GLY A CA  1 
ATOM   789   C  C   . GLY A 1 113 ? 62.287 40.941 69.314  1.00 63.47  ? 177 GLY A C   1 
ATOM   790   O  O   . GLY A 1 113 ? 62.223 42.170 69.271  1.00 93.29  ? 177 GLY A O   1 
ATOM   791   N  N   . PHE A 1 114 ? 61.868 40.155 68.329  1.00 68.46  ? 178 PHE A N   1 
ATOM   792   C  CA  . PHE A 1 114 ? 61.271 40.670 67.115  1.00 60.43  ? 178 PHE A CA  1 
ATOM   793   C  C   . PHE A 1 114 ? 59.865 40.158 66.930  1.00 66.23  ? 178 PHE A C   1 
ATOM   794   O  O   . PHE A 1 114 ? 58.916 40.953 66.951  1.00 76.89  ? 178 PHE A O   1 
ATOM   795   C  CB  . PHE A 1 114 ? 62.108 40.250 65.927  1.00 65.46  ? 178 PHE A CB  1 
ATOM   796   C  CG  . PHE A 1 114 ? 63.491 40.774 65.973  1.00 76.05  ? 178 PHE A CG  1 
ATOM   797   C  CD1 . PHE A 1 114 ? 63.742 42.142 65.777  1.00 73.64  ? 178 PHE A CD1 1 
ATOM   798   C  CD2 . PHE A 1 114 ? 64.553 39.912 66.213  1.00 73.79  ? 178 PHE A CD2 1 
ATOM   799   C  CE1 . PHE A 1 114 ? 65.039 42.637 65.821  1.00 72.55  ? 178 PHE A CE1 1 
ATOM   800   C  CE2 . PHE A 1 114 ? 65.851 40.394 66.261  1.00 81.88  ? 178 PHE A CE2 1 
ATOM   801   C  CZ  . PHE A 1 114 ? 66.099 41.762 66.059  1.00 71.92  ? 178 PHE A CZ  1 
ATOM   802   N  N   . GLN A 1 115 ? 59.737 38.838 66.735  1.00 51.64  ? 179 GLN A N   1 
ATOM   803   C  CA  . GLN A 1 115 ? 58.424 38.213 66.563  1.00 49.49  ? 179 GLN A CA  1 
ATOM   804   C  C   . GLN A 1 115 ? 58.210 37.017 67.481  1.00 40.98  ? 179 GLN A C   1 
ATOM   805   O  O   . GLN A 1 115 ? 59.113 36.576 68.148  1.00 48.08  ? 179 GLN A O   1 
ATOM   806   C  CB  . GLN A 1 115 ? 58.267 37.799 65.125  1.00 60.65  ? 179 GLN A CB  1 
ATOM   807   C  CG  . GLN A 1 115 ? 58.310 38.967 64.148  1.00 58.47  ? 179 GLN A CG  1 
ATOM   808   C  CD  . GLN A 1 115 ? 57.068 39.794 64.219  1.00 66.49  ? 179 GLN A CD  1 
ATOM   809   O  OE1 . GLN A 1 115 ? 56.098 39.449 64.912  1.00 91.69  ? 179 GLN A OE1 1 
ATOM   810   N  NE2 . GLN A 1 115 ? 57.084 40.901 63.522  1.00 82.17  ? 179 GLN A NE2 1 
ATOM   811   N  N   . TRP A 1 116 ? 56.997 36.523 67.582  1.00 41.24  ? 180 TRP A N   1 
ATOM   812   C  CA  . TRP A 1 116 ? 56.808 35.325 68.388  1.00 36.44  ? 180 TRP A CA  1 
ATOM   813   C  C   . TRP A 1 116 ? 57.059 34.137 67.540  1.00 41.03  ? 180 TRP A C   1 
ATOM   814   O  O   . TRP A 1 116 ? 56.593 34.029 66.387  1.00 43.15  ? 180 TRP A O   1 
ATOM   815   C  CB  . TRP A 1 116 ? 55.383 35.215 68.890  1.00 41.67  ? 180 TRP A CB  1 
ATOM   816   C  CG  . TRP A 1 116 ? 55.088 36.041 70.091  1.00 41.98  ? 180 TRP A CG  1 
ATOM   817   C  CD1 . TRP A 1 116 ? 54.486 37.288 70.146  1.00 46.52  ? 180 TRP A CD1 1 
ATOM   818   C  CD2 . TRP A 1 116 ? 55.363 35.682 71.464  1.00 45.71  ? 180 TRP A CD2 1 
ATOM   819   N  NE1 . TRP A 1 116 ? 54.358 37.708 71.438  1.00 54.75  ? 180 TRP A NE1 1 
ATOM   820   C  CE2 . TRP A 1 116 ? 54.874 36.785 72.281  1.00 48.16  ? 180 TRP A CE2 1 
ATOM   821   C  CE3 . TRP A 1 116 ? 55.922 34.585 72.077  1.00 46.77  ? 180 TRP A CE3 1 
ATOM   822   C  CZ2 . TRP A 1 116 ? 54.969 36.774 73.653  1.00 50.48  ? 180 TRP A CZ2 1 
ATOM   823   C  CZ3 . TRP A 1 116 ? 56.012 34.579 73.451  1.00 51.24  ? 180 TRP A CZ3 1 
ATOM   824   C  CH2 . TRP A 1 116 ? 55.541 35.649 74.229  1.00 48.26  ? 180 TRP A CH2 1 
ATOM   825   N  N   . THR A 1 117 ? 57.778 33.188 68.099  1.00 41.62  ? 181 THR A N   1 
ATOM   826   C  CA  . THR A 1 117 ? 57.944 31.948 67.391  1.00 38.31  ? 181 THR A CA  1 
ATOM   827   C  C   . THR A 1 117 ? 56.990 30.988 68.046  1.00 39.86  ? 181 THR A C   1 
ATOM   828   O  O   . THR A 1 117 ? 56.955 30.924 69.273  1.00 52.94  ? 181 THR A O   1 
ATOM   829   C  CB  . THR A 1 117 ? 59.375 31.471 67.486  1.00 37.44  ? 181 THR A CB  1 
ATOM   830   O  OG1 . THR A 1 117 ? 60.253 32.461 66.900  1.00 47.44  ? 181 THR A OG1 1 
ATOM   831   C  CG2 . THR A 1 117 ? 59.529 30.124 66.806  1.00 27.36  ? 181 THR A CG2 1 
ATOM   832   N  N   . VAL A 1 118 ? 56.183 30.291 67.240  1.00 38.59  ? 182 VAL A N   1 
ATOM   833   C  CA  . VAL A 1 118 ? 55.276 29.264 67.748  1.00 40.40  ? 182 VAL A CA  1 
ATOM   834   C  C   . VAL A 1 118 ? 55.399 27.900 67.048  1.00 48.83  ? 182 VAL A C   1 
ATOM   835   O  O   . VAL A 1 118 ? 55.255 27.820 65.830  1.00 74.34  ? 182 VAL A O   1 
ATOM   836   C  CB  . VAL A 1 118 ? 53.809 29.721 67.682  1.00 32.34  ? 182 VAL A CB  1 
ATOM   837   C  CG1 . VAL A 1 118 ? 52.863 28.553 68.121  1.00 36.89  ? 182 VAL A CG1 1 
ATOM   838   C  CG2 . VAL A 1 118 ? 53.599 30.905 68.568  1.00 28.90  ? 182 VAL A CG2 1 
ATOM   839   N  N   . LEU A 1 119 ? 55.617 26.842 67.831  1.00 36.31  ? 183 LEU A N   1 
ATOM   840   C  CA  . LEU A 1 119 ? 55.677 25.472 67.314  1.00 40.97  ? 183 LEU A CA  1 
ATOM   841   C  C   . LEU A 1 119 ? 54.427 24.737 67.672  1.00 43.45  ? 183 LEU A C   1 
ATOM   842   O  O   . LEU A 1 119 ? 54.126 24.530 68.834  1.00 61.98  ? 183 LEU A O   1 
ATOM   843   C  CB  . LEU A 1 119 ? 56.874 24.664 67.859  1.00 36.91  ? 183 LEU A CB  1 
ATOM   844   C  CG  . LEU A 1 119 ? 58.231 25.344 67.734  1.00 41.31  ? 183 LEU A CG  1 
ATOM   845   C  CD1 . LEU A 1 119 ? 58.888 25.615 69.114  1.00 51.93  ? 183 LEU A CD1 1 
ATOM   846   C  CD2 . LEU A 1 119 ? 59.095 24.518 66.855  1.00 42.35  ? 183 LEU A CD2 1 
ATOM   847   N  N   . SER A 1 120 ? 53.716 24.301 66.656  1.00 49.22  ? 184 SER A N   1 
ATOM   848   C  CA  . SER A 1 120 ? 52.494 23.560 66.848  1.00 50.78  ? 184 SER A CA  1 
ATOM   849   C  C   . SER A 1 120 ? 52.562 22.167 66.217  1.00 50.10  ? 184 SER A C   1 
ATOM   850   O  O   . SER A 1 120 ? 53.253 21.945 65.224  1.00 69.87  ? 184 SER A O   1 
ATOM   851   C  CB  . SER A 1 120 ? 51.342 24.360 66.259  1.00 66.48  ? 184 SER A CB  1 
ATOM   852   O  OG  . SER A 1 120 ? 50.117 23.663 66.385  1.00 108.42 ? 184 SER A OG  1 
ATOM   853   N  N   . VAL A 1 121 ? 51.841 21.230 66.808  1.00 37.94  ? 185 VAL A N   1 
ATOM   854   C  CA  . VAL A 1 121 ? 51.753 19.893 66.290  1.00 38.10  ? 185 VAL A CA  1 
ATOM   855   C  C   . VAL A 1 121 ? 50.324 19.704 65.819  1.00 45.54  ? 185 VAL A C   1 
ATOM   856   O  O   . VAL A 1 121 ? 49.404 19.921 66.601  1.00 49.77  ? 185 VAL A O   1 
ATOM   857   C  CB  . VAL A 1 121 ? 51.996 18.903 67.401  1.00 38.15  ? 185 VAL A CB  1 
ATOM   858   C  CG1 . VAL A 1 121 ? 51.789 17.484 66.910  1.00 39.65  ? 185 VAL A CG1 1 
ATOM   859   C  CG2 . VAL A 1 121 ? 53.383 19.082 67.975  1.00 42.95  ? 185 VAL A CG2 1 
ATOM   860   N  N   . ALA A 1 122 ? 50.136 19.275 64.570  1.00 43.96  ? 186 ALA A N   1 
ATOM   861   C  CA  . ALA A 1 122 ? 48.794 19.109 63.979  1.00 40.20  ? 186 ALA A CA  1 
ATOM   862   C  C   . ALA A 1 122 ? 48.670 17.953 62.977  1.00 47.54  ? 186 ALA A C   1 
ATOM   863   O  O   . ALA A 1 122 ? 49.662 17.281 62.638  1.00 42.65  ? 186 ALA A O   1 
ATOM   864   C  CB  . ALA A 1 122 ? 48.378 20.394 63.299  1.00 50.18  ? 186 ALA A CB  1 
ATOM   865   N  N   . GLY A 1 123 ? 47.444 17.753 62.485  1.00 54.29  ? 187 GLY A N   1 
ATOM   866   C  CA  . GLY A 1 123 ? 47.118 16.686 61.509  1.00 51.64  ? 187 GLY A CA  1 
ATOM   867   C  C   . GLY A 1 123 ? 47.786 15.323 61.668  1.00 53.37  ? 187 GLY A C   1 
ATOM   868   O  O   . GLY A 1 123 ? 47.493 14.561 62.590  1.00 47.32  ? 187 GLY A O   1 
ATOM   869   N  N   . ASP A 1 124 ? 48.682 15.017 60.737  1.00 75.95  ? 188 ASP A N   1 
ATOM   870   C  CA  . ASP A 1 124 ? 49.485 13.787 60.749  1.00 82.66  ? 188 ASP A CA  1 
ATOM   871   C  C   . ASP A 1 124 ? 50.198 13.581 62.089  1.00 70.56  ? 188 ASP A C   1 
ATOM   872   O  O   . ASP A 1 124 ? 50.369 12.456 62.515  1.00 69.05  ? 188 ASP A O   1 
ATOM   873   C  CB  . ASP A 1 124 ? 50.493 13.847 59.586  1.00 96.78  ? 188 ASP A CB  1 
ATOM   874   C  CG  . ASP A 1 124 ? 51.614 12.827 59.702  1.00 139.59 ? 188 ASP A CG  1 
ATOM   875   O  OD1 . ASP A 1 124 ? 51.321 11.624 59.875  1.00 187.61 ? 188 ASP A OD1 1 
ATOM   876   O  OD2 . ASP A 1 124 ? 52.796 13.230 59.587  1.00 167.34 ? 188 ASP A OD2 1 
ATOM   877   N  N   . GLY A 1 125 ? 50.563 14.674 62.756  1.00 57.33  ? 189 GLY A N   1 
ATOM   878   C  CA  . GLY A 1 125 ? 51.402 14.628 63.937  1.00 46.01  ? 189 GLY A CA  1 
ATOM   879   C  C   . GLY A 1 125 ? 52.734 15.320 63.655  1.00 52.29  ? 189 GLY A C   1 
ATOM   880   O  O   . GLY A 1 125 ? 53.707 15.111 64.384  1.00 56.24  ? 189 GLY A O   1 
ATOM   881   N  N   . PHE A 1 126 ? 52.795 16.128 62.595  1.00 38.27  ? 190 PHE A N   1 
ATOM   882   C  CA  . PHE A 1 126 ? 53.956 16.987 62.363  1.00 41.09  ? 190 PHE A CA  1 
ATOM   883   C  C   . PHE A 1 126 ? 53.918 18.382 63.054  1.00 57.40  ? 190 PHE A C   1 
ATOM   884   O  O   . PHE A 1 126 ? 52.913 18.796 63.686  1.00 42.45  ? 190 PHE A O   1 
ATOM   885   C  CB  . PHE A 1 126 ? 54.136 17.227 60.887  1.00 47.42  ? 190 PHE A CB  1 
ATOM   886   C  CG  . PHE A 1 126 ? 53.125 18.181 60.293  1.00 55.05  ? 190 PHE A CG  1 
ATOM   887   C  CD1 . PHE A 1 126 ? 53.508 19.441 59.868  1.00 75.39  ? 190 PHE A CD1 1 
ATOM   888   C  CD2 . PHE A 1 126 ? 51.794 17.804 60.119  1.00 73.40  ? 190 PHE A CD2 1 
ATOM   889   C  CE1 . PHE A 1 126 ? 52.573 20.321 59.304  1.00 72.85  ? 190 PHE A CE1 1 
ATOM   890   C  CE2 . PHE A 1 126 ? 50.857 18.680 59.545  1.00 68.08  ? 190 PHE A CE2 1 
ATOM   891   C  CZ  . PHE A 1 126 ? 51.248 19.932 59.146  1.00 60.92  ? 190 PHE A CZ  1 
ATOM   892   N  N   . VAL A 1 127 ? 55.027 19.109 62.886  1.00 49.84  ? 191 VAL A N   1 
ATOM   893   C  CA  . VAL A 1 127 ? 55.229 20.400 63.524  1.00 43.62  ? 191 VAL A CA  1 
ATOM   894   C  C   . VAL A 1 127 ? 55.275 21.555 62.518  1.00 51.41  ? 191 VAL A C   1 
ATOM   895   O  O   . VAL A 1 127 ? 56.089 21.574 61.598  1.00 54.51  ? 191 VAL A O   1 
ATOM   896   C  CB  . VAL A 1 127 ? 56.507 20.381 64.368  1.00 50.48  ? 191 VAL A CB  1 
ATOM   897   C  CG1 . VAL A 1 127 ? 57.057 21.765 64.558  1.00 53.85  ? 191 VAL A CG1 1 
ATOM   898   C  CG2 . VAL A 1 127 ? 56.215 19.781 65.695  1.00 46.95  ? 191 VAL A CG2 1 
ATOM   899   N  N   . SER A 1 128 ? 54.362 22.505 62.674  1.00 52.82  ? 192 SER A N   1 
ATOM   900   C  CA  . SER A 1 128 ? 54.446 23.752 61.954  1.00 48.44  ? 192 SER A CA  1 
ATOM   901   C  C   . SER A 1 128 ? 55.229 24.660 62.851  1.00 50.24  ? 192 SER A C   1 
ATOM   902   O  O   . SER A 1 128 ? 55.112 24.601 64.060  1.00 76.95  ? 192 SER A O   1 
ATOM   903   C  CB  . SER A 1 128 ? 53.072 24.371 61.776  1.00 58.27  ? 192 SER A CB  1 
ATOM   904   O  OG  . SER A 1 128 ? 52.341 23.672 60.812  1.00 67.51  ? 192 SER A OG  1 
ATOM   905   N  N   . ILE A 1 129 ? 56.013 25.520 62.251  1.00 43.89  ? 193 ILE A N   1 
ATOM   906   C  CA  . ILE A 1 129 ? 56.731 26.526 62.982  1.00 42.49  ? 193 ILE A CA  1 
ATOM   907   C  C   . ILE A 1 129 ? 56.229 27.861 62.450  1.00 45.18  ? 193 ILE A C   1 
ATOM   908   O  O   . ILE A 1 129 ? 56.340 28.119 61.250  1.00 52.41  ? 193 ILE A O   1 
ATOM   909   C  CB  . ILE A 1 129 ? 58.246 26.407 62.715  1.00 42.85  ? 193 ILE A CB  1 
ATOM   910   C  CG1 . ILE A 1 129 ? 58.791 25.179 63.427  1.00 47.74  ? 193 ILE A CG1 1 
ATOM   911   C  CG2 . ILE A 1 129 ? 58.978 27.657 63.176  1.00 43.40  ? 193 ILE A CG2 1 
ATOM   912   C  CD1 . ILE A 1 129 ? 60.223 24.853 63.062  1.00 60.45  ? 193 ILE A CD1 1 
ATOM   913   N  N   . LEU A 1 130 ? 55.668 28.715 63.303  1.00 39.55  ? 194 LEU A N   1 
ATOM   914   C  CA  . LEU A 1 130 ? 55.295 30.015 62.780  1.00 45.02  ? 194 LEU A CA  1 
ATOM   915   C  C   . LEU A 1 130 ? 55.838 31.246 63.473  1.00 49.39  ? 194 LEU A C   1 
ATOM   916   O  O   . LEU A 1 130 ? 55.821 31.374 64.706  1.00 74.97  ? 194 LEU A O   1 
ATOM   917   C  CB  . LEU A 1 130 ? 53.810 30.107 62.423  1.00 49.90  ? 194 LEU A CB  1 
ATOM   918   C  CG  . LEU A 1 130 ? 52.786 29.658 63.425  1.00 68.10  ? 194 LEU A CG  1 
ATOM   919   C  CD1 . LEU A 1 130 ? 52.080 30.915 63.998  1.00 82.61  ? 194 LEU A CD1 1 
ATOM   920   C  CD2 . LEU A 1 130 ? 51.858 28.760 62.684  1.00 56.77  ? 194 LEU A CD2 1 
ATOM   921   N  N   . TYR A 1 131 ? 56.325 32.150 62.628  1.00 44.70  ? 195 TYR A N   1 
ATOM   922   C  CA  . TYR A 1 131 ? 57.097 33.293 63.070  1.00 54.31  ? 195 TYR A CA  1 
ATOM   923   C  C   . TYR A 1 131 ? 56.278 34.521 62.784  1.00 53.87  ? 195 TYR A C   1 
ATOM   924   O  O   . TYR A 1 131 ? 56.035 34.867 61.638  1.00 50.15  ? 195 TYR A O   1 
ATOM   925   C  CB  . TYR A 1 131 ? 58.463 33.351 62.355  1.00 43.75  ? 195 TYR A CB  1 
ATOM   926   C  CG  . TYR A 1 131 ? 59.423 34.358 62.930  1.00 41.40  ? 195 TYR A CG  1 
ATOM   927   C  CD1 . TYR A 1 131 ? 60.064 34.136 64.156  1.00 41.04  ? 195 TYR A CD1 1 
ATOM   928   C  CD2 . TYR A 1 131 ? 59.699 35.538 62.256  1.00 41.73  ? 195 TYR A CD2 1 
ATOM   929   C  CE1 . TYR A 1 131 ? 60.959 35.091 64.694  1.00 42.56  ? 195 TYR A CE1 1 
ATOM   930   C  CE2 . TYR A 1 131 ? 60.600 36.492 62.790  1.00 48.15  ? 195 TYR A CE2 1 
ATOM   931   C  CZ  . TYR A 1 131 ? 61.216 36.261 63.998  1.00 48.26  ? 195 TYR A CZ  1 
ATOM   932   O  OH  . TYR A 1 131 ? 62.078 37.218 64.483  1.00 76.20  ? 195 TYR A OH  1 
ATOM   933   N  N   . GLY A 1 132 ? 55.827 35.171 63.842  1.00 61.88  ? 196 GLY A N   1 
ATOM   934   C  CA  . GLY A 1 132 ? 54.944 36.316 63.697  1.00 63.85  ? 196 GLY A CA  1 
ATOM   935   C  C   . GLY A 1 132 ? 53.644 35.975 62.995  1.00 57.12  ? 196 GLY A C   1 
ATOM   936   O  O   . GLY A 1 132 ? 53.139 36.763 62.210  1.00 76.38  ? 196 GLY A O   1 
ATOM   937   N  N   . GLY A 1 133 ? 53.113 34.788 63.260  1.00 56.52  ? 197 GLY A N   1 
ATOM   938   C  CA  . GLY A 1 133 ? 51.814 34.399 62.720  1.00 72.80  ? 197 GLY A CA  1 
ATOM   939   C  C   . GLY A 1 133 ? 51.801 33.756 61.343  1.00 66.89  ? 197 GLY A C   1 
ATOM   940   O  O   . GLY A 1 133 ? 50.769 33.242 60.907  1.00 86.35  ? 197 GLY A O   1 
ATOM   941   N  N   . ILE A 1 134 ? 52.930 33.790 60.645  1.00 54.85  ? 198 ILE A N   1 
ATOM   942   C  CA  . ILE A 1 134 ? 53.004 33.191 59.311  1.00 65.92  ? 198 ILE A CA  1 
ATOM   943   C  C   . ILE A 1 134 ? 53.853 31.950 59.337  1.00 61.47  ? 198 ILE A C   1 
ATOM   944   O  O   . ILE A 1 134 ? 54.753 31.858 60.156  1.00 78.52  ? 198 ILE A O   1 
ATOM   945   C  CB  . ILE A 1 134 ? 53.500 34.200 58.234  1.00 63.12  ? 198 ILE A CB  1 
ATOM   946   C  CG1 . ILE A 1 134 ? 54.945 34.593 58.453  1.00 84.59  ? 198 ILE A CG1 1 
ATOM   947   C  CG2 . ILE A 1 134 ? 52.642 35.471 58.270  1.00 69.77  ? 198 ILE A CG2 1 
ATOM   948   C  CD1 . ILE A 1 134 ? 55.489 35.519 57.391  1.00 85.80  ? 198 ILE A CD1 1 
ATOM   949   N  N   . ILE A 1 135 ? 53.570 30.998 58.452  1.00 75.44  ? 199 ILE A N   1 
ATOM   950   C  CA  . ILE A 1 135 ? 54.270 29.691 58.466  1.00 67.08  ? 199 ILE A CA  1 
ATOM   951   C  C   . ILE A 1 135 ? 55.618 29.750 57.790  1.00 57.11  ? 199 ILE A C   1 
ATOM   952   O  O   . ILE A 1 135 ? 55.686 29.914 56.587  1.00 57.89  ? 199 ILE A O   1 
ATOM   953   C  CB  . ILE A 1 135 ? 53.453 28.552 57.803  1.00 56.93  ? 199 ILE A CB  1 
ATOM   954   C  CG1 . ILE A 1 135 ? 52.070 28.461 58.456  1.00 64.25  ? 199 ILE A CG1 1 
ATOM   955   C  CG2 . ILE A 1 135 ? 54.212 27.257 57.894  1.00 51.62  ? 199 ILE A CG2 1 
ATOM   956   C  CD1 . ILE A 1 135 ? 51.741 27.136 59.127  1.00 50.68  ? 199 ILE A CD1 1 
ATOM   957   N  N   . THR A 1 136 ? 56.682 29.592 58.573  1.00 57.65  ? 200 THR A N   1 
ATOM   958   C  CA  . THR A 1 136 ? 58.045 29.690 58.058  1.00 63.67  ? 200 THR A CA  1 
ATOM   959   C  C   . THR A 1 136 ? 58.711 28.327 57.815  1.00 64.21  ? 200 THR A C   1 
ATOM   960   O  O   . THR A 1 136 ? 59.665 28.221 57.037  1.00 63.29  ? 200 THR A O   1 
ATOM   961   C  CB  . THR A 1 136 ? 58.927 30.530 58.984  1.00 54.80  ? 200 THR A CB  1 
ATOM   962   O  OG1 . THR A 1 136 ? 58.751 30.066 60.319  1.00 63.02  ? 200 THR A OG1 1 
ATOM   963   C  CG2 . THR A 1 136 ? 58.507 31.970 58.917  1.00 65.49  ? 200 THR A CG2 1 
ATOM   964   N  N   . ASP A 1 137 ? 58.207 27.287 58.466  1.00 64.46  ? 201 ASP A N   1 
ATOM   965   C  CA  . ASP A 1 137 ? 58.848 25.973 58.407  1.00 74.23  ? 201 ASP A CA  1 
ATOM   966   C  C   . ASP A 1 137 ? 57.977 24.845 58.961  1.00 59.27  ? 201 ASP A C   1 
ATOM   967   O  O   . ASP A 1 137 ? 57.094 25.060 59.781  1.00 61.89  ? 201 ASP A O   1 
ATOM   968   C  CB  . ASP A 1 137 ? 60.214 25.987 59.136  1.00 99.75  ? 201 ASP A CB  1 
ATOM   969   C  CG  . ASP A 1 137 ? 61.238 24.992 58.529  1.00 96.67  ? 201 ASP A CG  1 
ATOM   970   O  OD1 . ASP A 1 137 ? 60.862 23.868 58.136  1.00 101.98 ? 201 ASP A OD1 1 
ATOM   971   O  OD2 . ASP A 1 137 ? 62.437 25.330 58.450  1.00 91.09  ? 201 ASP A OD2 1 
ATOM   972   N  N   . THR A 1 138 ? 58.236 23.632 58.486  1.00 65.44  ? 202 THR A N   1 
ATOM   973   C  CA  . THR A 1 138 ? 57.619 22.438 59.045  1.00 63.94  ? 202 THR A CA  1 
ATOM   974   C  C   . THR A 1 138 ? 58.663 21.380 59.331  1.00 56.29  ? 202 THR A C   1 
ATOM   975   O  O   . THR A 1 138 ? 59.705 21.341 58.708  1.00 79.37  ? 202 THR A O   1 
ATOM   976   C  CB  . THR A 1 138 ? 56.577 21.834 58.117  1.00 61.23  ? 202 THR A CB  1 
ATOM   977   O  OG1 . THR A 1 138 ? 57.204 21.482 56.888  1.00 81.11  ? 202 THR A OG1 1 
ATOM   978   C  CG2 . THR A 1 138 ? 55.485 22.832 57.832  1.00 68.57  ? 202 THR A CG2 1 
ATOM   979   N  N   . ILE A 1 139 ? 58.350 20.520 60.280  1.00 61.22  ? 203 ILE A N   1 
ATOM   980   C  CA  . ILE A 1 139 ? 59.227 19.461 60.714  1.00 59.35  ? 203 ILE A CA  1 
ATOM   981   C  C   . ILE A 1 139 ? 58.398 18.188 60.764  1.00 67.18  ? 203 ILE A C   1 
ATOM   982   O  O   . ILE A 1 139 ? 57.330 18.173 61.393  1.00 59.15  ? 203 ILE A O   1 
ATOM   983   C  CB  . ILE A 1 139 ? 59.762 19.725 62.125  1.00 50.66  ? 203 ILE A CB  1 
ATOM   984   C  CG1 . ILE A 1 139 ? 60.656 20.971 62.150  1.00 50.51  ? 203 ILE A CG1 1 
ATOM   985   C  CG2 . ILE A 1 139 ? 60.522 18.512 62.606  1.00 47.50  ? 203 ILE A CG2 1 
ATOM   986   C  CD1 . ILE A 1 139 ? 61.175 21.343 63.588  1.00 49.28  ? 203 ILE A CD1 1 
ATOM   987   N  N   . HIS A 1 140 ? 58.899 17.126 60.129  1.00 66.45  ? 204 HIS A N   1 
ATOM   988   C  CA  . HIS A 1 140 ? 58.172 15.855 60.045  1.00 48.48  ? 204 HIS A CA  1 
ATOM   989   C  C   . HIS A 1 140 ? 58.827 14.696 60.759  1.00 65.01  ? 204 HIS A C   1 
ATOM   990   O  O   . HIS A 1 140 ? 60.064 14.652 60.926  1.00 68.31  ? 204 HIS A O   1 
ATOM   991   C  CB  . HIS A 1 140 ? 57.951 15.497 58.622  1.00 49.92  ? 204 HIS A CB  1 
ATOM   992   C  CG  . HIS A 1 140 ? 57.306 16.588 57.813  1.00 74.97  ? 204 HIS A CG  1 
ATOM   993   N  ND1 . HIS A 1 140 ? 55.981 16.658 57.634  1.00 76.60  ? 204 HIS A ND1 1 
ATOM   994   C  CD2 . HIS A 1 140 ? 57.857 17.651 57.095  1.00 96.58  ? 204 HIS A CD2 1 
ATOM   995   C  CE1 . HIS A 1 140 ? 55.688 17.722 56.859  1.00 75.94  ? 204 HIS A CE1 1 
ATOM   996   N  NE2 . HIS A 1 140 ? 56.833 18.325 56.526  1.00 78.69  ? 204 HIS A NE2 1 
ATOM   997   N  N   . PRO A 1 141 ? 57.997 13.728 61.193  1.00 62.00  ? 205 PRO A N   1 
ATOM   998   C  CA  . PRO A 1 141 ? 58.467 12.629 62.044  1.00 72.22  ? 205 PRO A CA  1 
ATOM   999   C  C   . PRO A 1 141 ? 59.176 11.538 61.257  1.00 81.05  ? 205 PRO A C   1 
ATOM   1000  O  O   . PRO A 1 141 ? 58.637 11.044 60.269  1.00 60.37  ? 205 PRO A O   1 
ATOM   1001  C  CB  . PRO A 1 141 ? 57.187 12.070 62.647  1.00 57.39  ? 205 PRO A CB  1 
ATOM   1002  C  CG  . PRO A 1 141 ? 56.062 12.929 62.107  1.00 54.86  ? 205 PRO A CG  1 
ATOM   1003  C  CD  . PRO A 1 141 ? 56.553 13.647 60.929  1.00 48.41  ? 205 PRO A CD  1 
ATOM   1004  N  N   . THR A 1 142 ? 60.383 11.198 61.703  1.00 101.19 ? 206 THR A N   1 
ATOM   1005  C  CA  . THR A 1 142 ? 61.170 10.121 61.132  1.00 98.74  ? 206 THR A CA  1 
ATOM   1006  C  C   . THR A 1 142 ? 60.822 8.860  61.923  1.00 118.41 ? 206 THR A C   1 
ATOM   1007  O  O   . THR A 1 142 ? 60.201 7.929  61.399  1.00 85.20  ? 206 THR A O   1 
ATOM   1008  C  CB  . THR A 1 142 ? 62.718 10.410 61.223  1.00 134.85 ? 206 THR A CB  1 
ATOM   1009  O  OG1 . THR A 1 142 ? 63.149 10.416 62.594  1.00 160.25 ? 206 THR A OG1 1 
ATOM   1010  C  CG2 . THR A 1 142 ? 63.096 11.751 60.565  1.00 96.66  ? 206 THR A CG2 1 
ATOM   1011  N  N   . ASN A 1 143 ? 61.203 8.839  63.197  1.00 146.77 ? 207 ASN A N   1 
ATOM   1012  C  CA  . ASN A 1 143 ? 61.007 7.668  64.055  1.00 121.61 ? 207 ASN A CA  1 
ATOM   1013  C  C   . ASN A 1 143 ? 59.567 7.149  64.166  1.00 120.03 ? 207 ASN A C   1 
ATOM   1014  O  O   . ASN A 1 143 ? 59.302 6.203  64.908  1.00 96.05  ? 207 ASN A O   1 
ATOM   1015  C  CB  . ASN A 1 143 ? 61.569 7.937  65.454  1.00 133.41 ? 207 ASN A CB  1 
ATOM   1016  C  CG  . ASN A 1 143 ? 62.531 6.859  65.912  1.00 127.77 ? 207 ASN A CG  1 
ATOM   1017  O  OD1 . ASN A 1 143 ? 63.221 6.241  65.102  1.00 126.17 ? 207 ASN A OD1 1 
ATOM   1018  N  ND2 . ASN A 1 143 ? 62.581 6.627  67.219  1.00 105.32 ? 207 ASN A ND2 1 
ATOM   1019  N  N   . GLY A 1 144 ? 58.646 7.764  63.432  1.00 139.05 ? 208 GLY A N   1 
ATOM   1020  C  CA  . GLY A 1 144 ? 57.232 7.351  63.445  1.00 101.47 ? 208 GLY A CA  1 
ATOM   1021  C  C   . GLY A 1 144 ? 56.381 7.975  64.543  1.00 109.48 ? 208 GLY A C   1 
ATOM   1022  O  O   . GLY A 1 144 ? 56.905 8.620  65.462  1.00 119.81 ? 208 GLY A O   1 
ATOM   1023  N  N   . GLY A 1 145 ? 55.061 7.790  64.446  1.00 95.37  ? 209 GLY A N   1 
ATOM   1024  C  CA  . GLY A 1 145 ? 54.115 8.330  65.435  1.00 94.78  ? 209 GLY A CA  1 
ATOM   1025  C  C   . GLY A 1 145 ? 54.267 9.835  65.603  1.00 75.27  ? 209 GLY A C   1 
ATOM   1026  O  O   . GLY A 1 145 ? 55.233 10.414 65.097  1.00 65.07  ? 209 GLY A O   1 
ATOM   1027  N  N   . PRO A 1 146 ? 53.354 10.473 66.364  1.00 75.98  ? 210 PRO A N   1 
ATOM   1028  C  CA  . PRO A 1 146 ? 53.270 11.946 66.398  1.00 60.36  ? 210 PRO A CA  1 
ATOM   1029  C  C   . PRO A 1 146 ? 54.484 12.582 67.099  1.00 55.17  ? 210 PRO A C   1 
ATOM   1030  O  O   . PRO A 1 146 ? 55.025 12.016 68.061  1.00 64.47  ? 210 PRO A O   1 
ATOM   1031  C  CB  . PRO A 1 146 ? 52.017 12.187 67.232  1.00 56.81  ? 210 PRO A CB  1 
ATOM   1032  C  CG  . PRO A 1 146 ? 52.046 11.074 68.249  1.00 72.40  ? 210 PRO A CG  1 
ATOM   1033  C  CD  . PRO A 1 146 ? 52.654 9.866  67.516  1.00 86.48  ? 210 PRO A CD  1 
ATOM   1034  N  N   . LEU A 1 147 ? 54.924 13.733 66.615  1.00 39.09  ? 211 LEU A N   1 
ATOM   1035  C  CA  . LEU A 1 147 ? 55.899 14.509 67.366  1.00 46.78  ? 211 LEU A CA  1 
ATOM   1036  C  C   . LEU A 1 147 ? 55.222 15.224 68.550  1.00 62.35  ? 211 LEU A C   1 
ATOM   1037  O  O   . LEU A 1 147 ? 53.965 15.278 68.684  1.00 51.13  ? 211 LEU A O   1 
ATOM   1038  C  CB  . LEU A 1 147 ? 56.585 15.546 66.494  1.00 51.27  ? 211 LEU A CB  1 
ATOM   1039  C  CG  . LEU A 1 147 ? 57.345 15.167 65.236  1.00 53.41  ? 211 LEU A CG  1 
ATOM   1040  C  CD1 . LEU A 1 147 ? 57.290 16.338 64.271  1.00 48.56  ? 211 LEU A CD1 1 
ATOM   1041  C  CD2 . LEU A 1 147 ? 58.746 14.900 65.585  1.00 59.15  ? 211 LEU A CD2 1 
ATOM   1042  N  N   . ARG A 1 148 ? 56.068 15.781 69.412  1.00 58.73  ? 212 ARG A N   1 
ATOM   1043  C  CA  . ARG A 1 148 ? 55.612 16.334 70.668  1.00 56.98  ? 212 ARG A CA  1 
ATOM   1044  C  C   . ARG A 1 148 ? 56.505 17.496 71.032  1.00 54.83  ? 212 ARG A C   1 
ATOM   1045  O  O   . ARG A 1 148 ? 57.739 17.386 70.893  1.00 51.38  ? 212 ARG A O   1 
ATOM   1046  C  CB  . ARG A 1 148 ? 55.677 15.244 71.742  1.00 62.38  ? 212 ARG A CB  1 
ATOM   1047  C  CG  . ARG A 1 148 ? 54.712 14.053 71.506  1.00 70.84  ? 212 ARG A CG  1 
ATOM   1048  C  CD  . ARG A 1 148 ? 54.714 13.040 72.666  1.00 81.29  ? 212 ARG A CD  1 
ATOM   1049  N  NE  . ARG A 1 148 ? 56.009 12.380 72.845  1.00 90.75  ? 212 ARG A NE  1 
ATOM   1050  C  CZ  . ARG A 1 148 ? 56.433 11.342 72.125  1.00 84.73  ? 212 ARG A CZ  1 
ATOM   1051  N  NH1 . ARG A 1 148 ? 55.670 10.828 71.164  1.00 80.57  ? 212 ARG A NH1 1 
ATOM   1052  N  NH2 . ARG A 1 148 ? 57.627 10.820 72.365  1.00 62.46  ? 212 ARG A NH2 1 
ATOM   1053  N  N   . THR A 1 149 ? 55.885 18.605 71.461  1.00 61.15  ? 213 THR A N   1 
ATOM   1054  C  CA  . THR A 1 149 ? 56.633 19.842 71.804  1.00 77.11  ? 213 THR A CA  1 
ATOM   1055  C  C   . THR A 1 149 ? 56.851 19.895 73.296  1.00 56.34  ? 213 THR A C   1 
ATOM   1056  O  O   . THR A 1 149 ? 56.211 19.129 74.008  1.00 58.35  ? 213 THR A O   1 
ATOM   1057  C  CB  . THR A 1 149 ? 55.879 21.130 71.418  1.00 67.58  ? 213 THR A CB  1 
ATOM   1058  O  OG1 . THR A 1 149 ? 54.563 21.081 71.971  1.00 76.85  ? 213 THR A OG1 1 
ATOM   1059  C  CG2 . THR A 1 149 ? 55.795 21.312 69.920  1.00 44.74  ? 213 THR A CG2 1 
ATOM   1060  N  N   . GLN A 1 150 ? 57.737 20.783 73.765  1.00 38.81  ? 214 GLN A N   1 
ATOM   1061  C  CA  . GLN A 1 150 ? 57.891 21.012 75.205  1.00 42.61  ? 214 GLN A CA  1 
ATOM   1062  C  C   . GLN A 1 150 ? 56.597 21.316 75.939  1.00 50.56  ? 214 GLN A C   1 
ATOM   1063  O  O   . GLN A 1 150 ? 56.502 21.034 77.130  1.00 70.83  ? 214 GLN A O   1 
ATOM   1064  C  CB  . GLN A 1 150 ? 58.825 22.176 75.472  1.00 54.48  ? 214 GLN A CB  1 
ATOM   1065  C  CG  . GLN A 1 150 ? 60.103 21.979 74.779  1.00 86.04  ? 214 GLN A CG  1 
ATOM   1066  C  CD  . GLN A 1 150 ? 61.010 23.107 75.005  1.00 67.43  ? 214 GLN A CD  1 
ATOM   1067  O  OE1 . GLN A 1 150 ? 60.558 24.214 75.130  1.00 70.22  ? 214 GLN A OE1 1 
ATOM   1068  N  NE2 . GLN A 1 150 ? 62.307 22.843 75.080  1.00 96.82  ? 214 GLN A NE2 1 
ATOM   1069  N  N   . ALA A 1 151 ? 55.610 21.922 75.272  1.00 39.19  ? 215 ALA A N   1 
ATOM   1070  C  CA  . ALA A 1 151 ? 54.411 22.324 76.011  1.00 38.19  ? 215 ALA A CA  1 
ATOM   1071  C  C   . ALA A 1 151 ? 54.866 23.226 77.155  1.00 37.33  ? 215 ALA A C   1 
ATOM   1072  O  O   . ALA A 1 151 ? 54.426 23.111 78.274  1.00 45.23  ? 215 ALA A O   1 
ATOM   1073  C  CB  . ALA A 1 151 ? 53.667 21.123 76.540  1.00 26.42  ? 215 ALA A CB  1 
ATOM   1074  N  N   . SER A 1 152 ? 55.801 24.092 76.834  1.00 33.93  ? 216 SER A N   1 
ATOM   1075  C  CA  . SER A 1 152 ? 56.395 24.993 77.744  1.00 40.66  ? 216 SER A CA  1 
ATOM   1076  C  C   . SER A 1 152 ? 57.077 26.029 76.863  1.00 48.83  ? 216 SER A C   1 
ATOM   1077  O  O   . SER A 1 152 ? 57.484 25.744 75.744  1.00 63.12  ? 216 SER A O   1 
ATOM   1078  C  CB  . SER A 1 152 ? 57.455 24.250 78.562  1.00 48.20  ? 216 SER A CB  1 
ATOM   1079  O  OG  . SER A 1 152 ? 58.338 25.152 79.256  1.00 72.07  ? 216 SER A OG  1 
ATOM   1080  N  N   . SER A 1 153 ? 57.233 27.228 77.374  1.00 39.22  ? 217 SER A N   1 
ATOM   1081  C  CA  . SER A 1 153 ? 58.064 28.191 76.709  1.00 49.71  ? 217 SER A CA  1 
ATOM   1082  C  C   . SER A 1 153 ? 59.437 27.611 76.258  1.00 52.15  ? 217 SER A C   1 
ATOM   1083  O  O   . SER A 1 153 ? 60.153 26.935 77.036  1.00 52.51  ? 217 SER A O   1 
ATOM   1084  C  CB  . SER A 1 153 ? 58.263 29.376 77.655  1.00 45.62  ? 217 SER A CB  1 
ATOM   1085  O  OG  . SER A 1 153 ? 59.320 30.196 77.206  1.00 49.51  ? 217 SER A OG  1 
ATOM   1086  N  N   . CYS A 1 154 ? 59.798 27.883 75.007  1.00 41.05  ? 218 CYS A N   1 
ATOM   1087  C  CA  . CYS A 1 154 ? 61.137 27.607 74.541  1.00 39.55  ? 218 CYS A CA  1 
ATOM   1088  C  C   . CYS A 1 154 ? 62.014 28.791 74.921  1.00 49.31  ? 218 CYS A C   1 
ATOM   1089  O  O   . CYS A 1 154 ? 61.519 29.774 75.432  1.00 42.38  ? 218 CYS A O   1 
ATOM   1090  C  CB  . CYS A 1 154 ? 61.135 27.390 73.032  1.00 50.12  ? 218 CYS A CB  1 
ATOM   1091  S  SG  . CYS A 1 154 ? 59.862 28.337 72.129  1.00 87.45  ? 218 CYS A SG  1 
ATOM   1092  N  N   . ILE A 1 155 ? 63.314 28.709 74.679  1.00 51.25  ? 219 ILE A N   1 
ATOM   1093  C  CA  . ILE A 1 155 ? 64.209 29.716 75.179  1.00 42.58  ? 219 ILE A CA  1 
ATOM   1094  C  C   . ILE A 1 155 ? 64.853 30.464 74.052  1.00 45.43  ? 219 ILE A C   1 
ATOM   1095  O  O   . ILE A 1 155 ? 65.498 29.862 73.202  1.00 62.74  ? 219 ILE A O   1 
ATOM   1096  C  CB  . ILE A 1 155 ? 65.290 29.063 76.021  1.00 50.74  ? 219 ILE A CB  1 
ATOM   1097  C  CG1 . ILE A 1 155 ? 64.696 28.642 77.348  1.00 62.49  ? 219 ILE A CG1 1 
ATOM   1098  C  CG2 . ILE A 1 155 ? 66.432 30.024 76.282  1.00 59.15  ? 219 ILE A CG2 1 
ATOM   1099  C  CD1 . ILE A 1 155 ? 63.744 27.466 77.243  1.00 86.70  ? 219 ILE A CD1 1 
ATOM   1100  N  N   . CYS A 1 156 ? 64.694 31.782 74.040  1.00 54.01  ? 220 CYS A N   1 
ATOM   1101  C  CA  . CYS A 1 156 ? 65.391 32.602 73.048  1.00 60.69  ? 220 CYS A CA  1 
ATOM   1102  C  C   . CYS A 1 156 ? 66.454 33.421 73.741  1.00 65.09  ? 220 CYS A C   1 
ATOM   1103  O  O   . CYS A 1 156 ? 66.226 33.973 74.816  1.00 71.64  ? 220 CYS A O   1 
ATOM   1104  C  CB  . CYS A 1 156 ? 64.432 33.513 72.267  1.00 54.05  ? 220 CYS A CB  1 
ATOM   1105  S  SG  . CYS A 1 156 ? 63.100 32.660 71.413  1.00 88.16  ? 220 CYS A SG  1 
ATOM   1106  N  N   . ASN A 1 157 ? 67.623 33.472 73.123  1.00 57.22  ? 221 ASN A N   1 
ATOM   1107  C  CA  . ASN A 1 157 ? 68.699 34.314 73.588  1.00 64.56  ? 221 ASN A CA  1 
ATOM   1108  C  C   . ASN A 1 157 ? 69.518 34.780 72.396  1.00 70.34  ? 221 ASN A C   1 
ATOM   1109  O  O   . ASN A 1 157 ? 70.026 33.954 71.634  1.00 62.63  ? 221 ASN A O   1 
ATOM   1110  C  CB  . ASN A 1 157 ? 69.580 33.570 74.591  1.00 77.42  ? 221 ASN A CB  1 
ATOM   1111  C  CG  . ASN A 1 157 ? 70.355 34.521 75.507  1.00 96.83  ? 221 ASN A CG  1 
ATOM   1112  O  OD1 . ASN A 1 157 ? 69.821 35.519 76.011  1.00 84.92  ? 221 ASN A OD1 1 
ATOM   1113  N  ND2 . ASN A 1 157 ? 71.621 34.206 75.729  1.00 107.99 ? 221 ASN A ND2 1 
ATOM   1114  N  N   . ASP A 1 158 ? 69.630 36.101 72.228  1.00 74.98  ? 222 ASP A N   1 
ATOM   1115  C  CA  . ASP A 1 158 ? 70.390 36.706 71.119  1.00 85.69  ? 222 ASP A CA  1 
ATOM   1116  C  C   . ASP A 1 158 ? 69.838 36.342 69.746  1.00 85.86  ? 222 ASP A C   1 
ATOM   1117  O  O   . ASP A 1 158 ? 70.605 36.147 68.799  1.00 83.41  ? 222 ASP A O   1 
ATOM   1118  C  CB  . ASP A 1 158 ? 71.886 36.344 71.172  1.00 100.26 ? 222 ASP A CB  1 
ATOM   1119  C  CG  . ASP A 1 158 ? 72.612 36.988 72.335  1.00 136.12 ? 222 ASP A CG  1 
ATOM   1120  O  OD1 . ASP A 1 158 ? 72.111 37.987 72.883  1.00 165.59 ? 222 ASP A OD1 1 
ATOM   1121  O  OD2 . ASP A 1 158 ? 73.698 36.493 72.704  1.00 170.30 ? 222 ASP A OD2 1 
ATOM   1122  N  N   . GLY A 1 159 ? 68.514 36.237 69.645  1.00 86.99  ? 223 GLY A N   1 
ATOM   1123  C  CA  . GLY A 1 159 ? 67.871 36.127 68.340  1.00 97.71  ? 223 GLY A CA  1 
ATOM   1124  C  C   . GLY A 1 159 ? 67.777 34.738 67.750  1.00 78.79  ? 223 GLY A C   1 
ATOM   1125  O  O   . GLY A 1 159 ? 67.103 34.552 66.722  1.00 78.11  ? 223 GLY A O   1 
ATOM   1126  N  N   . THR A 1 160 ? 68.461 33.779 68.390  1.00 71.71  ? 224 THR A N   1 
ATOM   1127  C  CA  . THR A 1 160 ? 68.288 32.340 68.108  1.00 59.04  ? 224 THR A CA  1 
ATOM   1128  C  C   . THR A 1 160 ? 67.476 31.662 69.212  1.00 50.22  ? 224 THR A C   1 
ATOM   1129  O  O   . THR A 1 160 ? 67.596 32.020 70.386  1.00 45.74  ? 224 THR A O   1 
ATOM   1130  C  CB  . THR A 1 160 ? 69.639 31.611 67.869  1.00 56.71  ? 224 THR A CB  1 
ATOM   1131  O  OG1 . THR A 1 160 ? 70.397 31.623 69.059  1.00 61.53  ? 224 THR A OG1 1 
ATOM   1132  C  CG2 . THR A 1 160 ? 70.477 32.314 66.773  1.00 69.57  ? 224 THR A CG2 1 
ATOM   1133  N  N   . CYS A 1 161 ? 66.605 30.726 68.845  1.00 53.55  ? 225 CYS A N   1 
ATOM   1134  C  CA  . CYS A 1 161 ? 65.735 30.091 69.851  1.00 57.06  ? 225 CYS A CA  1 
ATOM   1135  C  C   . CYS A 1 161 ? 66.017 28.625 69.886  1.00 52.92  ? 225 CYS A C   1 
ATOM   1136  O  O   . CYS A 1 161 ? 66.332 28.054 68.864  1.00 91.86  ? 225 CYS A O   1 
ATOM   1137  C  CB  . CYS A 1 161 ? 64.243 30.342 69.570  1.00 50.15  ? 225 CYS A CB  1 
ATOM   1138  S  SG  . CYS A 1 161 ? 63.813 32.102 69.535  1.00 91.36  ? 225 CYS A SG  1 
ATOM   1139  N  N   . TYR A 1 162 ? 65.913 28.023 71.058  1.00 45.76  ? 226 TYR A N   1 
ATOM   1140  C  CA  . TYR A 1 162 ? 66.189 26.592 71.242  1.00 42.64  ? 226 TYR A CA  1 
ATOM   1141  C  C   . TYR A 1 162 ? 64.935 25.884 71.740  1.00 43.69  ? 226 TYR A C   1 
ATOM   1142  O  O   . TYR A 1 162 ? 64.253 26.348 72.669  1.00 36.83  ? 226 TYR A O   1 
ATOM   1143  C  CB  . TYR A 1 162 ? 67.332 26.392 72.235  1.00 34.38  ? 226 TYR A CB  1 
ATOM   1144  C  CG  . TYR A 1 162 ? 68.526 27.221 71.926  1.00 46.09  ? 226 TYR A CG  1 
ATOM   1145  C  CD1 . TYR A 1 162 ? 69.585 26.682 71.233  1.00 64.05  ? 226 TYR A CD1 1 
ATOM   1146  C  CD2 . TYR A 1 162 ? 68.609 28.554 72.317  1.00 54.78  ? 226 TYR A CD2 1 
ATOM   1147  C  CE1 . TYR A 1 162 ? 70.717 27.441 70.935  1.00 78.00  ? 226 TYR A CE1 1 
ATOM   1148  C  CE2 . TYR A 1 162 ? 69.733 29.326 72.027  1.00 56.42  ? 226 TYR A CE2 1 
ATOM   1149  C  CZ  . TYR A 1 162 ? 70.786 28.762 71.332  1.00 69.25  ? 226 TYR A CZ  1 
ATOM   1150  O  OH  . TYR A 1 162 ? 71.917 29.498 71.031  1.00 70.13  ? 226 TYR A OH  1 
ATOM   1151  N  N   . THR A 1 163 ? 64.611 24.763 71.121  1.00 40.94  ? 227 THR A N   1 
ATOM   1152  C  CA  . THR A 1 163 ? 63.476 24.003 71.623  1.00 49.47  ? 227 THR A CA  1 
ATOM   1153  C  C   . THR A 1 163 ? 63.773 22.528 71.513  1.00 45.86  ? 227 THR A C   1 
ATOM   1154  O  O   . THR A 1 163 ? 64.668 22.151 70.760  1.00 51.47  ? 227 THR A O   1 
ATOM   1155  C  CB  . THR A 1 163 ? 62.131 24.388 70.941  1.00 38.60  ? 227 THR A CB  1 
ATOM   1156  O  OG1 . THR A 1 163 ? 61.077 23.619 71.537  1.00 75.07  ? 227 THR A OG1 1 
ATOM   1157  C  CG2 . THR A 1 163 ? 62.166 24.116 69.483  1.00 27.22  ? 227 THR A CG2 1 
ATOM   1158  N  N   . ILE A 1 164 ? 63.055 21.710 72.288  1.00 36.20  ? 228 ILE A N   1 
ATOM   1159  C  CA  . ILE A 1 164 ? 63.243 20.268 72.245  1.00 33.76  ? 228 ILE A CA  1 
ATOM   1160  C  C   . ILE A 1 164 ? 62.024 19.549 71.695  1.00 37.83  ? 228 ILE A C   1 
ATOM   1161  O  O   . ILE A 1 164 ? 60.893 19.816 72.090  1.00 70.84  ? 228 ILE A O   1 
ATOM   1162  C  CB  . ILE A 1 164 ? 63.653 19.720 73.609  1.00 30.60  ? 228 ILE A CB  1 
ATOM   1163  C  CG1 . ILE A 1 164 ? 65.019 20.267 74.005  1.00 29.17  ? 228 ILE A CG1 1 
ATOM   1164  C  CG2 . ILE A 1 164 ? 63.777 18.175 73.576  1.00 43.66  ? 228 ILE A CG2 1 
ATOM   1165  C  CD1 . ILE A 1 164 ? 65.277 20.192 75.496  1.00 30.00  ? 228 ILE A CD1 1 
ATOM   1166  N  N   . ILE A 1 165 ? 62.262 18.622 70.776  1.00 52.87  ? 229 ILE A N   1 
ATOM   1167  C  CA  . ILE A 1 165 ? 61.175 17.862 70.138  1.00 49.27  ? 229 ILE A CA  1 
ATOM   1168  C  C   . ILE A 1 165 ? 61.303 16.345 70.251  1.00 52.18  ? 229 ILE A C   1 
ATOM   1169  O  O   . ILE A 1 165 ? 62.351 15.765 69.903  1.00 49.08  ? 229 ILE A O   1 
ATOM   1170  C  CB  . ILE A 1 165 ? 61.056 18.210 68.679  1.00 42.09  ? 229 ILE A CB  1 
ATOM   1171  C  CG1 . ILE A 1 165 ? 61.111 19.734 68.526  1.00 50.52  ? 229 ILE A CG1 1 
ATOM   1172  C  CG2 . ILE A 1 165 ? 59.807 17.615 68.149  1.00 39.04  ? 229 ILE A CG2 1 
ATOM   1173  C  CD1 . ILE A 1 165 ? 59.978 20.369 67.787  1.00 56.52  ? 229 ILE A CD1 1 
ATOM   1174  N  N   . ALA A 1 166 ? 60.209 15.722 70.703  1.00 50.21  ? 230 ALA A N   1 
ATOM   1175  C  CA  . ALA A 1 166 ? 60.128 14.260 70.920  1.00 49.12  ? 230 ALA A CA  1 
ATOM   1176  C  C   . ALA A 1 166 ? 59.469 13.519 69.790  1.00 56.12  ? 230 ALA A C   1 
ATOM   1177  O  O   . ALA A 1 166 ? 58.446 13.964 69.265  1.00 68.35  ? 230 ALA A O   1 
ATOM   1178  C  CB  . ALA A 1 166 ? 59.379 13.941 72.164  1.00 40.31  ? 230 ALA A CB  1 
ATOM   1179  N  N   . ASP A 1 167 ? 60.054 12.368 69.459  1.00 61.67  ? 231 ASP A N   1 
ATOM   1180  C  CA  . ASP A 1 167 ? 59.542 11.459 68.444  1.00 60.33  ? 231 ASP A CA  1 
ATOM   1181  C  C   . ASP A 1 167 ? 59.368 10.057 69.032  1.00 64.60  ? 231 ASP A C   1 
ATOM   1182  O  O   . ASP A 1 167 ? 60.063 9.690  69.982  1.00 71.06  ? 231 ASP A O   1 
ATOM   1183  C  CB  . ASP A 1 167 ? 60.544 11.392 67.304  1.00 78.40  ? 231 ASP A CB  1 
ATOM   1184  C  CG  . ASP A 1 167 ? 59.890 11.105 65.959  1.00 122.16 ? 231 ASP A CG  1 
ATOM   1185  O  OD1 . ASP A 1 167 ? 58.670 10.786 65.933  1.00 123.74 ? 231 ASP A OD1 1 
ATOM   1186  O  OD2 . ASP A 1 167 ? 60.607 11.205 64.925  1.00 97.22  ? 231 ASP A OD2 1 
ATOM   1187  N  N   . GLY A 1 168 ? 58.447 9.271  68.484  1.00 54.62  ? 232 GLY A N   1 
ATOM   1188  C  CA  . GLY A 1 168 ? 58.371 7.861  68.864  1.00 68.45  ? 232 GLY A CA  1 
ATOM   1189  C  C   . GLY A 1 168 ? 57.007 7.321  69.252  1.00 81.06  ? 232 GLY A C   1 
ATOM   1190  O  O   . GLY A 1 168 ? 56.135 8.062  69.711  1.00 70.77  ? 232 GLY A O   1 
ATOM   1191  N  N   . THR A 1 169 ? 56.838 6.012  69.072  1.00 96.05  ? 233 THR A N   1 
ATOM   1192  C  CA  . THR A 1 169 ? 55.543 5.356  69.230  1.00 85.91  ? 233 THR A CA  1 
ATOM   1193  C  C   . THR A 1 169 ? 55.197 5.224  70.693  1.00 88.01  ? 233 THR A C   1 
ATOM   1194  O  O   . THR A 1 169 ? 54.030 5.343  71.071  1.00 88.96  ? 233 THR A O   1 
ATOM   1195  C  CB  . THR A 1 169 ? 55.557 3.958  68.616  1.00 83.36  ? 233 THR A CB  1 
ATOM   1196  O  OG1 . THR A 1 169 ? 55.963 4.047  67.252  1.00 87.74  ? 233 THR A OG1 1 
ATOM   1197  C  CG2 . THR A 1 169 ? 54.183 3.338  68.676  1.00 110.13 ? 233 THR A CG2 1 
ATOM   1198  N  N   . THR A 1 170 ? 56.219 4.962  71.506  1.00 91.04  ? 234 THR A N   1 
ATOM   1199  C  CA  . THR A 1 170 ? 56.047 4.790  72.946  1.00 106.07 ? 234 THR A CA  1 
ATOM   1200  C  C   . THR A 1 170 ? 57.292 5.267  73.685  1.00 91.32  ? 234 THR A C   1 
ATOM   1201  O  O   . THR A 1 170 ? 58.337 5.468  73.075  1.00 121.10 ? 234 THR A O   1 
ATOM   1202  C  CB  . THR A 1 170 ? 55.687 3.323  73.321  1.00 96.98  ? 234 THR A CB  1 
ATOM   1203  O  OG1 . THR A 1 170 ? 55.512 3.207  74.741  1.00 105.88 ? 234 THR A OG1 1 
ATOM   1204  C  CG2 . THR A 1 170 ? 56.765 2.376  72.861  1.00 62.67  ? 234 THR A CG2 1 
ATOM   1205  N  N   . TYR A 1 171 ? 57.164 5.441  74.995  1.00 72.15  ? 235 TYR A N   1 
ATOM   1206  C  CA  . TYR A 1 171 ? 58.161 6.136  75.792  1.00 76.17  ? 235 TYR A CA  1 
ATOM   1207  C  C   . TYR A 1 171 ? 59.368 5.263  76.019  1.00 86.12  ? 235 TYR A C   1 
ATOM   1208  O  O   . TYR A 1 171 ? 60.487 5.766  76.187  1.00 83.38  ? 235 TYR A O   1 
ATOM   1209  C  CB  . TYR A 1 171 ? 57.527 6.615  77.090  1.00 69.26  ? 235 TYR A CB  1 
ATOM   1210  C  CG  . TYR A 1 171 ? 56.248 7.391  76.828  1.00 86.58  ? 235 TYR A CG  1 
ATOM   1211  C  CD1 . TYR A 1 171 ? 56.277 8.623  76.153  1.00 100.87 ? 235 TYR A CD1 1 
ATOM   1212  C  CD2 . TYR A 1 171 ? 55.008 6.889  77.217  1.00 107.37 ? 235 TYR A CD2 1 
ATOM   1213  C  CE1 . TYR A 1 171 ? 55.112 9.337  75.888  1.00 111.59 ? 235 TYR A CE1 1 
ATOM   1214  C  CE2 . TYR A 1 171 ? 53.837 7.604  76.957  1.00 120.95 ? 235 TYR A CE2 1 
ATOM   1215  C  CZ  . TYR A 1 171 ? 53.908 8.824  76.294  1.00 132.21 ? 235 TYR A CZ  1 
ATOM   1216  O  OH  . TYR A 1 171 ? 52.773 9.533  76.030  1.00 151.95 ? 235 TYR A OH  1 
ATOM   1217  N  N   . THR A 1 172 ? 59.126 3.952  75.979  1.00 89.68  ? 236 THR A N   1 
ATOM   1218  C  CA  . THR A 1 172 ? 60.180 2.954  75.977  1.00 77.37  ? 236 THR A CA  1 
ATOM   1219  C  C   . THR A 1 172 ? 61.101 3.242  74.785  1.00 63.06  ? 236 THR A C   1 
ATOM   1220  O  O   . THR A 1 172 ? 62.310 3.054  74.852  1.00 71.72  ? 236 THR A O   1 
ATOM   1221  C  CB  . THR A 1 172 ? 59.600 1.504  75.919  1.00 73.50  ? 236 THR A CB  1 
ATOM   1222  O  OG1 . THR A 1 172 ? 59.181 1.201  74.591  1.00 92.56  ? 236 THR A OG1 1 
ATOM   1223  C  CG2 . THR A 1 172 ? 58.404 1.343  76.846  1.00 63.40  ? 236 THR A CG2 1 
ATOM   1224  N  N   . ALA A 1 173 ? 60.518 3.757  73.713  1.00 70.20  ? 237 ALA A N   1 
ATOM   1225  C  CA  . ALA A 1 173 ? 61.218 3.903  72.426  1.00 98.65  ? 237 ALA A CA  1 
ATOM   1226  C  C   . ALA A 1 173 ? 61.458 5.355  71.956  1.00 85.64  ? 237 ALA A C   1 
ATOM   1227  O  O   . ALA A 1 173 ? 61.712 5.591  70.772  1.00 79.40  ? 237 ALA A O   1 
ATOM   1228  C  CB  . ALA A 1 173 ? 60.444 3.120  71.338  1.00 156.46 ? 237 ALA A CB  1 
ATOM   1229  N  N   . SER A 1 174 ? 61.374 6.324  72.865  1.00 74.02  ? 238 SER A N   1 
ATOM   1230  C  CA  . SER A 1 174 ? 61.397 7.733  72.465  1.00 69.09  ? 238 SER A CA  1 
ATOM   1231  C  C   . SER A 1 174 ? 62.758 8.249  71.970  1.00 59.69  ? 238 SER A C   1 
ATOM   1232  O  O   . SER A 1 174 ? 63.803 7.789  72.393  1.00 70.90  ? 238 SER A O   1 
ATOM   1233  C  CB  . SER A 1 174 ? 60.880 8.614  73.597  1.00 89.54  ? 238 SER A CB  1 
ATOM   1234  O  OG  . SER A 1 174 ? 61.729 8.530  74.732  1.00 121.53 ? 238 SER A OG  1 
ATOM   1235  N  N   . SER A 1 175 ? 62.720 9.213  71.061  1.00 61.28  ? 239 SER A N   1 
ATOM   1236  C  CA  . SER A 1 175 ? 63.907 9.854  70.546  1.00 60.72  ? 239 SER A CA  1 
ATOM   1237  C  C   . SER A 1 175 ? 63.741 11.354 70.747  1.00 81.11  ? 239 SER A C   1 
ATOM   1238  O  O   . SER A 1 175 ? 62.622 11.877 70.567  1.00 80.16  ? 239 SER A O   1 
ATOM   1239  C  CB  . SER A 1 175 ? 64.017 9.559  69.063  1.00 64.09  ? 239 SER A CB  1 
ATOM   1240  O  OG  . SER A 1 175 ? 65.117 10.241 68.495  1.00 107.74 ? 239 SER A OG  1 
ATOM   1241  N  N   . HIS A 1 176 ? 64.826 12.053 71.104  1.00 58.51  ? 240 HIS A N   1 
ATOM   1242  C  CA  . HIS A 1 176 ? 64.713 13.504 71.313  1.00 53.20  ? 240 HIS A CA  1 
ATOM   1243  C  C   . HIS A 1 176 ? 65.746 14.313 70.585  1.00 51.57  ? 240 HIS A C   1 
ATOM   1244  O  O   . HIS A 1 176 ? 66.947 14.081 70.721  1.00 69.22  ? 240 HIS A O   1 
ATOM   1245  C  CB  . HIS A 1 176 ? 64.717 13.829 72.795  1.00 46.59  ? 240 HIS A CB  1 
ATOM   1246  C  CG  . HIS A 1 176 ? 63.665 13.087 73.572  1.00 50.29  ? 240 HIS A CG  1 
ATOM   1247  N  ND1 . HIS A 1 176 ? 62.386 13.452 73.958  1.00 65.01  ? 240 HIS A ND1 1 
ATOM   1248  C  CD2 . HIS A 1 176 ? 63.858 11.839 74.028  1.00 62.11  ? 240 HIS A CD2 1 
ATOM   1249  C  CE1 . HIS A 1 176 ? 61.858 12.408 74.641  1.00 65.55  ? 240 HIS A CE1 1 
ATOM   1250  N  NE2 . HIS A 1 176 ? 62.765 11.421 74.687  1.00 84.95  ? 240 HIS A NE2 1 
ATOM   1251  N  N   . ARG A 1 177 ? 65.276 15.269 69.792  1.00 39.90  ? 241 ARG A N   1 
ATOM   1252  C  CA  . ARG A 1 177 ? 66.144 16.259 69.158  1.00 40.69  ? 241 ARG A CA  1 
ATOM   1253  C  C   . ARG A 1 177 ? 66.019 17.671 69.750  1.00 47.15  ? 241 ARG A C   1 
ATOM   1254  O  O   . ARG A 1 177 ? 64.953 18.163 70.128  1.00 48.47  ? 241 ARG A O   1 
ATOM   1255  C  CB  . ARG A 1 177 ? 65.879 16.324 67.665  1.00 47.35  ? 241 ARG A CB  1 
ATOM   1256  C  CG  . ARG A 1 177 ? 66.030 14.968 67.021  1.00 104.04 ? 241 ARG A CG  1 
ATOM   1257  C  CD  . ARG A 1 177 ? 64.877 14.697 66.105  1.00 112.42 ? 241 ARG A CD  1 
ATOM   1258  N  NE  . ARG A 1 177 ? 65.143 15.204 64.771  1.00 85.86  ? 241 ARG A NE  1 
ATOM   1259  C  CZ  . ARG A 1 177 ? 65.696 14.481 63.810  1.00 70.96  ? 241 ARG A CZ  1 
ATOM   1260  N  NH1 . ARG A 1 177 ? 66.073 13.227 64.032  1.00 53.92  ? 241 ARG A NH1 1 
ATOM   1261  N  NH2 . ARG A 1 177 ? 65.887 15.029 62.631  1.00 85.22  ? 241 ARG A NH2 1 
ATOM   1262  N  N   . LEU A 1 178 ? 67.152 18.322 69.818  1.00 42.61  ? 242 LEU A N   1 
ATOM   1263  C  CA  . LEU A 1 178 ? 67.247 19.637 70.333  1.00 43.26  ? 242 LEU A CA  1 
ATOM   1264  C  C   . LEU A 1 178 ? 67.387 20.464 69.084  1.00 43.30  ? 242 LEU A C   1 
ATOM   1265  O  O   . LEU A 1 178 ? 68.369 20.336 68.372  1.00 49.75  ? 242 LEU A O   1 
ATOM   1266  C  CB  . LEU A 1 178 ? 68.513 19.703 71.173  1.00 57.78  ? 242 LEU A CB  1 
ATOM   1267  C  CG  . LEU A 1 178 ? 69.186 20.999 71.588  1.00 63.49  ? 242 LEU A CG  1 
ATOM   1268  C  CD1 . LEU A 1 178 ? 68.215 21.832 72.374  1.00 62.45  ? 242 LEU A CD1 1 
ATOM   1269  C  CD2 . LEU A 1 178 ? 70.379 20.617 72.441  1.00 67.39  ? 242 LEU A CD2 1 
ATOM   1270  N  N   . TYR A 1 179 ? 66.379 21.268 68.782  1.00 40.13  ? 243 TYR A N   1 
ATOM   1271  C  CA  . TYR A 1 179 ? 66.417 22.128 67.612  1.00 33.51  ? 243 TYR A CA  1 
ATOM   1272  C  C   . TYR A 1 179 ? 66.885 23.511 67.910  1.00 36.12  ? 243 TYR A C   1 
ATOM   1273  O  O   . TYR A 1 179 ? 66.654 24.028 69.013  1.00 59.59  ? 243 TYR A O   1 
ATOM   1274  C  CB  . TYR A 1 179 ? 65.027 22.239 67.051  1.00 34.03  ? 243 TYR A CB  1 
ATOM   1275  C  CG  . TYR A 1 179 ? 64.696 21.069 66.200  1.00 35.12  ? 243 TYR A CG  1 
ATOM   1276  C  CD1 . TYR A 1 179 ? 64.103 19.922 66.743  1.00 32.64  ? 243 TYR A CD1 1 
ATOM   1277  C  CD2 . TYR A 1 179 ? 65.000 21.096 64.842  1.00 35.85  ? 243 TYR A CD2 1 
ATOM   1278  C  CE1 . TYR A 1 179 ? 63.799 18.830 65.934  1.00 44.61  ? 243 TYR A CE1 1 
ATOM   1279  C  CE2 . TYR A 1 179 ? 64.707 20.016 64.025  1.00 48.21  ? 243 TYR A CE2 1 
ATOM   1280  C  CZ  . TYR A 1 179 ? 64.118 18.879 64.570  1.00 55.11  ? 243 TYR A CZ  1 
ATOM   1281  O  OH  . TYR A 1 179 ? 63.857 17.815 63.728  1.00 62.94  ? 243 TYR A OH  1 
ATOM   1282  N  N   . ARG A 1 180 ? 67.500 24.117 66.908  1.00 30.31  ? 244 ARG A N   1 
ATOM   1283  C  CA  . ARG A 1 180 ? 67.843 25.537 66.918  1.00 35.59  ? 244 ARG A CA  1 
ATOM   1284  C  C   . ARG A 1 180 ? 67.088 26.299 65.835  1.00 37.88  ? 244 ARG A C   1 
ATOM   1285  O  O   . ARG A 1 180 ? 67.097 25.901 64.702  1.00 58.45  ? 244 ARG A O   1 
ATOM   1286  C  CB  . ARG A 1 180 ? 69.343 25.665 66.734  1.00 45.21  ? 244 ARG A CB  1 
ATOM   1287  C  CG  . ARG A 1 180 ? 69.855 26.987 66.284  1.00 56.41  ? 244 ARG A CG  1 
ATOM   1288  C  CD  . ARG A 1 180 ? 71.366 26.901 66.221  1.00 54.50  ? 244 ARG A CD  1 
ATOM   1289  N  NE  . ARG A 1 180 ? 71.855 27.743 65.149  1.00 57.20  ? 244 ARG A NE  1 
ATOM   1290  C  CZ  . ARG A 1 180 ? 72.616 28.812 65.324  1.00 67.86  ? 244 ARG A CZ  1 
ATOM   1291  N  NH1 . ARG A 1 180 ? 73.008 29.145 66.556  1.00 70.98  ? 244 ARG A NH1 1 
ATOM   1292  N  NH2 . ARG A 1 180 ? 72.996 29.533 64.263  1.00 82.15  ? 244 ARG A NH2 1 
ATOM   1293  N  N   . LEU A 1 181 ? 66.420 27.391 66.177  1.00 46.24  ? 245 LEU A N   1 
ATOM   1294  C  CA  . LEU A 1 181 ? 65.628 28.141 65.200  1.00 39.83  ? 245 LEU A CA  1 
ATOM   1295  C  C   . LEU A 1 181 ? 66.110 29.556 65.129  1.00 45.94  ? 245 LEU A C   1 
ATOM   1296  O  O   . LEU A 1 181 ? 66.532 30.116 66.157  1.00 58.59  ? 245 LEU A O   1 
ATOM   1297  C  CB  . LEU A 1 181 ? 64.177 28.167 65.639  1.00 39.32  ? 245 LEU A CB  1 
ATOM   1298  C  CG  . LEU A 1 181 ? 63.636 26.816 66.092  1.00 44.04  ? 245 LEU A CG  1 
ATOM   1299  C  CD1 . LEU A 1 181 ? 62.423 27.011 67.002  1.00 47.40  ? 245 LEU A CD1 1 
ATOM   1300  C  CD2 . LEU A 1 181 ? 63.315 25.939 64.909  1.00 40.03  ? 245 LEU A CD2 1 
ATOM   1301  N  N   . VAL A 1 182 ? 66.038 30.142 63.933  1.00 47.20  ? 246 VAL A N   1 
ATOM   1302  C  CA  . VAL A 1 182 ? 66.318 31.583 63.730  1.00 46.05  ? 246 VAL A CA  1 
ATOM   1303  C  C   . VAL A 1 182 ? 65.278 32.242 62.827  1.00 46.52  ? 246 VAL A C   1 
ATOM   1304  O  O   . VAL A 1 182 ? 65.038 31.769 61.707  1.00 38.46  ? 246 VAL A O   1 
ATOM   1305  C  CB  . VAL A 1 182 ? 67.668 31.796 63.071  1.00 39.20  ? 246 VAL A CB  1 
ATOM   1306  C  CG1 . VAL A 1 182 ? 68.010 33.241 63.092  1.00 45.61  ? 246 VAL A CG1 1 
ATOM   1307  C  CG2 . VAL A 1 182 ? 68.730 30.965 63.772  1.00 34.97  ? 246 VAL A CG2 1 
ATOM   1308  N  N   . ASN A 1 183 ? 64.680 33.339 63.300  1.00 48.88  ? 247 ASN A N   1 
ATOM   1309  C  CA  . ASN A 1 183 ? 63.655 34.025 62.524  1.00 45.50  ? 247 ASN A CA  1 
ATOM   1310  C  C   . ASN A 1 183 ? 62.690 32.970 61.905  1.00 48.01  ? 247 ASN A C   1 
ATOM   1311  O  O   . ASN A 1 183 ? 62.170 33.128 60.789  1.00 50.21  ? 247 ASN A O   1 
ATOM   1312  C  CB  . ASN A 1 183 ? 64.289 34.944 61.476  1.00 45.02  ? 247 ASN A CB  1 
ATOM   1313  C  CG  . ASN A 1 183 ? 65.107 36.084 62.095  1.00 59.96  ? 247 ASN A CG  1 
ATOM   1314  O  OD1 . ASN A 1 183 ? 65.197 36.203 63.320  1.00 72.71  ? 247 ASN A OD1 1 
ATOM   1315  N  ND2 . ASN A 1 183 ? 65.710 36.937 61.235  1.00 67.12  ? 247 ASN A ND2 1 
ATOM   1316  N  N   . GLY A 1 184 ? 62.481 31.881 62.650  1.00 36.78  ? 248 GLY A N   1 
ATOM   1317  C  CA  . GLY A 1 184 ? 61.425 30.953 62.351  1.00 42.31  ? 248 GLY A CA  1 
ATOM   1318  C  C   . GLY A 1 184 ? 61.793 29.797 61.437  1.00 48.99  ? 248 GLY A C   1 
ATOM   1319  O  O   . GLY A 1 184 ? 60.979 28.928 61.124  1.00 65.96  ? 248 GLY A O   1 
ATOM   1320  N  N   . THR A 1 185 ? 63.017 29.773 60.981  1.00 48.01  ? 249 THR A N   1 
ATOM   1321  C  CA  . THR A 1 185 ? 63.443 28.628 60.225  1.00 52.54  ? 249 THR A CA  1 
ATOM   1322  C  C   . THR A 1 185 ? 64.416 27.841 61.068  1.00 55.31  ? 249 THR A C   1 
ATOM   1323  O  O   . THR A 1 185 ? 65.110 28.411 61.904  1.00 86.79  ? 249 THR A O   1 
ATOM   1324  C  CB  . THR A 1 185 ? 64.072 29.059 58.940  1.00 68.30  ? 249 THR A CB  1 
ATOM   1325  O  OG1 . THR A 1 185 ? 64.987 30.118 59.227  1.00 91.50  ? 249 THR A OG1 1 
ATOM   1326  C  CG2 . THR A 1 185 ? 62.983 29.575 57.981  1.00 107.61 ? 249 THR A CG2 1 
ATOM   1327  N  N   . SER A 1 186 ? 64.437 26.526 60.899  1.00 58.37  ? 250 SER A N   1 
ATOM   1328  C  CA  . SER A 1 186 ? 65.380 25.712 61.658  1.00 65.22  ? 250 SER A CA  1 
ATOM   1329  C  C   . SER A 1 186 ? 66.808 26.025 61.178  1.00 52.68  ? 250 SER A C   1 
ATOM   1330  O  O   . SER A 1 186 ? 67.059 26.161 60.010  1.00 54.50  ? 250 SER A O   1 
ATOM   1331  C  CB  . SER A 1 186 ? 65.042 24.210 61.600  1.00 53.92  ? 250 SER A CB  1 
ATOM   1332  O  OG  . SER A 1 186 ? 64.985 23.747 60.270  1.00 62.75  ? 250 SER A OG  1 
ATOM   1333  N  N   . ALA A 1 187 ? 67.712 26.212 62.116  1.00 65.95  ? 251 ALA A N   1 
ATOM   1334  C  CA  . ALA A 1 187 ? 69.117 26.418 61.834  1.00 58.35  ? 251 ALA A CA  1 
ATOM   1335  C  C   . ALA A 1 187 ? 69.890 25.189 62.354  1.00 54.09  ? 251 ALA A C   1 
ATOM   1336  O  O   . ALA A 1 187 ? 70.978 25.298 62.901  1.00 54.41  ? 251 ALA A O   1 
ATOM   1337  C  CB  . ALA A 1 187 ? 69.582 27.680 62.535  1.00 75.55  ? 251 ALA A CB  1 
ATOM   1338  N  N   . GLY A 1 188 ? 69.309 24.011 62.216  1.00 44.19  ? 252 GLY A N   1 
ATOM   1339  C  CA  . GLY A 1 188 ? 70.016 22.829 62.636  1.00 45.13  ? 252 GLY A CA  1 
ATOM   1340  C  C   . GLY A 1 188 ? 69.577 22.261 63.963  1.00 50.77  ? 252 GLY A C   1 
ATOM   1341  O  O   . GLY A 1 188 ? 68.831 22.892 64.721  1.00 68.54  ? 252 GLY A O   1 
ATOM   1342  N  N   . TRP A 1 189 ? 70.047 21.051 64.239  1.00 39.89  ? 253 TRP A N   1 
ATOM   1343  C  CA  . TRP A 1 189 ? 69.695 20.382 65.465  1.00 36.92  ? 253 TRP A CA  1 
ATOM   1344  C  C   . TRP A 1 189 ? 70.721 19.351 65.869  1.00 37.11  ? 253 TRP A C   1 
ATOM   1345  O  O   . TRP A 1 189 ? 71.658 19.079 65.141  1.00 41.11  ? 253 TRP A O   1 
ATOM   1346  C  CB  . TRP A 1 189 ? 68.322 19.772 65.295  1.00 36.53  ? 253 TRP A CB  1 
ATOM   1347  C  CG  . TRP A 1 189 ? 68.250 18.845 64.131  1.00 41.11  ? 253 TRP A CG  1 
ATOM   1348  C  CD1 . TRP A 1 189 ? 67.847 19.123 62.840  1.00 44.21  ? 253 TRP A CD1 1 
ATOM   1349  C  CD2 . TRP A 1 189 ? 68.620 17.435 64.119  1.00 51.09  ? 253 TRP A CD2 1 
ATOM   1350  N  NE1 . TRP A 1 189 ? 67.915 18.001 62.058  1.00 41.34  ? 253 TRP A NE1 1 
ATOM   1351  C  CE2 . TRP A 1 189 ? 68.391 16.965 62.764  1.00 42.61  ? 253 TRP A CE2 1 
ATOM   1352  C  CE3 . TRP A 1 189 ? 69.085 16.540 65.078  1.00 53.81  ? 253 TRP A CE3 1 
ATOM   1353  C  CZ2 . TRP A 1 189 ? 68.613 15.664 62.409  1.00 36.54  ? 253 TRP A CZ2 1 
ATOM   1354  C  CZ3 . TRP A 1 189 ? 69.325 15.227 64.703  1.00 43.12  ? 253 TRP A CZ3 1 
ATOM   1355  C  CH2 . TRP A 1 189 ? 69.095 14.800 63.406  1.00 37.40  ? 253 TRP A CH2 1 
ATOM   1356  N  N   . LYS A 1 190 ? 70.538 18.757 67.034  1.00 36.32  ? 254 LYS A N   1 
ATOM   1357  C  CA  . LYS A 1 190 ? 71.410 17.705 67.519  1.00 35.51  ? 254 LYS A CA  1 
ATOM   1358  C  C   . LYS A 1 190 ? 70.562 16.622 68.161  1.00 35.82  ? 254 LYS A C   1 
ATOM   1359  O  O   . LYS A 1 190 ? 69.576 16.910 68.786  1.00 47.26  ? 254 LYS A O   1 
ATOM   1360  C  CB  . LYS A 1 190 ? 72.388 18.265 68.538  1.00 37.35  ? 254 LYS A CB  1 
ATOM   1361  C  CG  . LYS A 1 190 ? 73.222 17.205 69.183  1.00 44.55  ? 254 LYS A CG  1 
ATOM   1362  C  CD  . LYS A 1 190 ? 74.641 17.660 69.471  1.00 48.11  ? 254 LYS A CD  1 
ATOM   1363  C  CE  . LYS A 1 190 ? 75.436 16.522 70.106  1.00 57.82  ? 254 LYS A CE  1 
ATOM   1364  N  NZ  . LYS A 1 190 ? 76.852 16.912 70.302  1.00 99.10  ? 254 LYS A NZ  1 
ATOM   1365  N  N   . ALA A 1 191 ? 70.919 15.365 67.982  1.00 48.08  ? 255 ALA A N   1 
ATOM   1366  C  CA  . ALA A 1 191 ? 70.188 14.304 68.656  1.00 54.67  ? 255 ALA A CA  1 
ATOM   1367  C  C   . ALA A 1 191 ? 70.677 14.288 70.077  1.00 61.76  ? 255 ALA A C   1 
ATOM   1368  O  O   . ALA A 1 191 ? 71.871 14.430 70.342  1.00 64.47  ? 255 ALA A O   1 
ATOM   1369  C  CB  . ALA A 1 191 ? 70.413 12.972 68.008  1.00 46.39  ? 255 ALA A CB  1 
ATOM   1370  N  N   . LEU A 1 192 ? 69.737 14.161 70.996  1.00 57.10  ? 256 LEU A N   1 
ATOM   1371  C  CA  . LEU A 1 192 ? 70.089 13.987 72.376  1.00 56.70  ? 256 LEU A CA  1 
ATOM   1372  C  C   . LEU A 1 192 ? 70.072 12.496 72.680  1.00 59.65  ? 256 LEU A C   1 
ATOM   1373  O  O   . LEU A 1 192 ? 69.078 11.816 72.347  1.00 41.79  ? 256 LEU A O   1 
ATOM   1374  C  CB  . LEU A 1 192 ? 69.078 14.713 73.244  1.00 51.09  ? 256 LEU A CB  1 
ATOM   1375  C  CG  . LEU A 1 192 ? 69.081 16.236 73.178  1.00 47.90  ? 256 LEU A CG  1 
ATOM   1376  C  CD1 . LEU A 1 192 ? 67.878 16.813 73.965  1.00 39.43  ? 256 LEU A CD1 1 
ATOM   1377  C  CD2 . LEU A 1 192 ? 70.440 16.809 73.685  1.00 40.74  ? 256 LEU A CD2 1 
ATOM   1378  N  N   . ASP A 1 193 ? 71.157 12.015 73.306  1.00 58.62  ? 257 ASP A N   1 
ATOM   1379  C  CA  . ASP A 1 193 ? 71.283 10.623 73.737  1.00 71.63  ? 257 ASP A CA  1 
ATOM   1380  C  C   . ASP A 1 193 ? 70.452 10.325 74.980  1.00 54.07  ? 257 ASP A C   1 
ATOM   1381  O  O   . ASP A 1 193 ? 70.856 10.635 76.093  1.00 54.52  ? 257 ASP A O   1 
ATOM   1382  C  CB  . ASP A 1 193 ? 72.747 10.250 73.986  1.00 82.16  ? 257 ASP A CB  1 
ATOM   1383  C  CG  . ASP A 1 193 ? 72.926 8.790  74.369  1.00 87.72  ? 257 ASP A CG  1 
ATOM   1384  O  OD1 . ASP A 1 193 ? 71.947 8.011  74.347  1.00 110.10 ? 257 ASP A OD1 1 
ATOM   1385  O  OD2 . ASP A 1 193 ? 74.062 8.418  74.694  1.00 115.19 ? 257 ASP A OD2 1 
ATOM   1386  N  N   . THR A 1 194 ? 69.323 9.673  74.752  1.00 57.44  ? 258 THR A N   1 
ATOM   1387  C  CA  . THR A 1 194 ? 68.314 9.412  75.760  1.00 91.88  ? 258 THR A CA  1 
ATOM   1388  C  C   . THR A 1 194 ? 68.355 7.952  76.258  1.00 88.34  ? 258 THR A C   1 
ATOM   1389  O  O   . THR A 1 194 ? 67.742 7.620  77.283  1.00 77.64  ? 258 THR A O   1 
ATOM   1390  C  CB  . THR A 1 194 ? 66.904 9.724  75.174  1.00 92.49  ? 258 THR A CB  1 
ATOM   1391  O  OG1 . THR A 1 194 ? 65.922 9.712  76.213  1.00 96.32  ? 258 THR A OG1 1 
ATOM   1392  C  CG2 . THR A 1 194 ? 66.515 8.695  74.104  1.00 105.34 ? 258 THR A CG2 1 
ATOM   1393  N  N   . THR A 1 195 ? 69.084 7.097  75.539  1.00 83.75  ? 259 THR A N   1 
ATOM   1394  C  CA  . THR A 1 195 ? 68.893 5.640  75.662  1.00 104.28 ? 259 THR A CA  1 
ATOM   1395  C  C   . THR A 1 195 ? 68.883 5.172  77.111  1.00 84.61  ? 259 THR A C   1 
ATOM   1396  O  O   . THR A 1 195 ? 69.682 5.619  77.938  1.00 62.41  ? 259 THR A O   1 
ATOM   1397  C  CB  . THR A 1 195 ? 69.900 4.776  74.826  1.00 89.56  ? 259 THR A CB  1 
ATOM   1398  O  OG1 . THR A 1 195 ? 71.235 5.106  75.199  1.00 99.72  ? 259 THR A OG1 1 
ATOM   1399  C  CG2 . THR A 1 195 ? 69.714 4.965  73.300  1.00 89.36  ? 259 THR A CG2 1 
ATOM   1400  N  N   . GLY A 1 196 ? 67.943 4.288  77.409  1.00 82.56  ? 260 GLY A N   1 
ATOM   1401  C  CA  . GLY A 1 196 ? 67.829 3.768  78.746  1.00 76.66  ? 260 GLY A CA  1 
ATOM   1402  C  C   . GLY A 1 196 ? 66.797 4.532  79.523  1.00 70.95  ? 260 GLY A C   1 
ATOM   1403  O  O   . GLY A 1 196 ? 66.277 4.017  80.505  1.00 83.99  ? 260 GLY A O   1 
ATOM   1404  N  N   . PHE A 1 197 ? 66.499 5.756  79.094  1.00 67.50  ? 261 PHE A N   1 
ATOM   1405  C  CA  . PHE A 1 197 ? 65.449 6.553  79.744  1.00 64.08  ? 261 PHE A CA  1 
ATOM   1406  C  C   . PHE A 1 197 ? 64.592 7.383  78.765  1.00 57.37  ? 261 PHE A C   1 
ATOM   1407  O  O   . PHE A 1 197 ? 64.640 7.165  77.543  1.00 59.77  ? 261 PHE A O   1 
ATOM   1408  C  CB  . PHE A 1 197 ? 66.020 7.403  80.901  1.00 64.70  ? 261 PHE A CB  1 
ATOM   1409  C  CG  . PHE A 1 197 ? 66.815 8.596  80.457  1.00 77.58  ? 261 PHE A CG  1 
ATOM   1410  C  CD1 . PHE A 1 197 ? 66.234 9.861  80.421  1.00 68.57  ? 261 PHE A CD1 1 
ATOM   1411  C  CD2 . PHE A 1 197 ? 68.152 8.457  80.093  1.00 88.39  ? 261 PHE A CD2 1 
ATOM   1412  C  CE1 . PHE A 1 197 ? 66.969 10.965 80.011  1.00 85.99  ? 261 PHE A CE1 1 
ATOM   1413  C  CE2 . PHE A 1 197 ? 68.897 9.557  79.684  1.00 82.33  ? 261 PHE A CE2 1 
ATOM   1414  C  CZ  . PHE A 1 197 ? 68.306 10.814 79.642  1.00 90.20  ? 261 PHE A CZ  1 
ATOM   1415  N  N   . ASN A 1 198 ? 63.822 8.325  79.319  1.00 53.19  ? 262 ASN A N   1 
ATOM   1416  C  CA  . ASN A 1 198 ? 62.831 9.107  78.583  1.00 54.08  ? 262 ASN A CA  1 
ATOM   1417  C  C   . ASN A 1 198 ? 62.657 10.521 79.179  1.00 61.31  ? 262 ASN A C   1 
ATOM   1418  O  O   . ASN A 1 198 ? 62.704 10.712 80.393  1.00 60.20  ? 262 ASN A O   1 
ATOM   1419  C  CB  . ASN A 1 198 ? 61.513 8.323  78.526  1.00 60.36  ? 262 ASN A CB  1 
ATOM   1420  C  CG  . ASN A 1 198 ? 60.304 9.203  78.361  1.00 68.66  ? 262 ASN A CG  1 
ATOM   1421  O  OD1 . ASN A 1 198 ? 59.513 9.375  79.296  1.00 87.02  ? 262 ASN A OD1 1 
ATOM   1422  N  ND2 . ASN A 1 198 ? 60.155 9.776  77.180  1.00 56.80  ? 262 ASN A ND2 1 
ATOM   1423  N  N   . PHE A 1 199 ? 62.426 11.501 78.310  1.00 66.12  ? 263 PHE A N   1 
ATOM   1424  C  CA  . PHE A 1 199 ? 62.616 12.924 78.643  1.00 53.23  ? 263 PHE A CA  1 
ATOM   1425  C  C   . PHE A 1 199 ? 61.598 13.779 77.939  1.00 55.57  ? 263 PHE A C   1 
ATOM   1426  O  O   . PHE A 1 199 ? 61.820 14.282 76.839  1.00 74.40  ? 263 PHE A O   1 
ATOM   1427  C  CB  . PHE A 1 199 ? 63.991 13.342 78.157  1.00 49.60  ? 263 PHE A CB  1 
ATOM   1428  C  CG  . PHE A 1 199 ? 64.382 14.718 78.507  1.00 35.73  ? 263 PHE A CG  1 
ATOM   1429  C  CD1 . PHE A 1 199 ? 64.680 15.053 79.796  1.00 49.09  ? 263 PHE A CD1 1 
ATOM   1430  C  CD2 . PHE A 1 199 ? 64.551 15.655 77.534  1.00 50.30  ? 263 PHE A CD2 1 
ATOM   1431  C  CE1 . PHE A 1 199 ? 65.102 16.333 80.125  1.00 56.43  ? 263 PHE A CE1 1 
ATOM   1432  C  CE2 . PHE A 1 199 ? 64.987 16.951 77.843  1.00 52.54  ? 263 PHE A CE2 1 
ATOM   1433  C  CZ  . PHE A 1 199 ? 65.261 17.286 79.136  1.00 46.49  ? 263 PHE A CZ  1 
ATOM   1434  N  N   . GLU A 1 200 ? 60.477 13.966 78.593  1.00 60.94  ? 264 GLU A N   1 
ATOM   1435  C  CA  . GLU A 1 200 ? 59.352 14.600 77.952  1.00 62.83  ? 264 GLU A CA  1 
ATOM   1436  C  C   . GLU A 1 200 ? 59.000 15.914 78.609  1.00 56.73  ? 264 GLU A C   1 
ATOM   1437  O  O   . GLU A 1 200 ? 59.219 16.111 79.796  1.00 62.38  ? 264 GLU A O   1 
ATOM   1438  C  CB  . GLU A 1 200 ? 58.151 13.660 77.992  1.00 57.78  ? 264 GLU A CB  1 
ATOM   1439  C  CG  . GLU A 1 200 ? 58.378 12.391 77.204  1.00 75.81  ? 264 GLU A CG  1 
ATOM   1440  C  CD  . GLU A 1 200 ? 57.850 12.481 75.773  1.00 93.81  ? 264 GLU A CD  1 
ATOM   1441  O  OE1 . GLU A 1 200 ? 57.059 13.411 75.478  1.00 88.77  ? 264 GLU A OE1 1 
ATOM   1442  O  OE2 . GLU A 1 200 ? 58.212 11.616 74.938  1.00 72.74  ? 264 GLU A OE2 1 
ATOM   1443  N  N   . PHE A 1 201 ? 58.439 16.814 77.823  1.00 46.47  ? 265 PHE A N   1 
ATOM   1444  C  CA  . PHE A 1 201 ? 57.897 18.028 78.381  1.00 41.05  ? 265 PHE A CA  1 
ATOM   1445  C  C   . PHE A 1 201 ? 58.947 18.830 79.121  1.00 30.44  ? 265 PHE A C   1 
ATOM   1446  O  O   . PHE A 1 201 ? 58.644 19.390 80.161  1.00 33.27  ? 265 PHE A O   1 
ATOM   1447  C  CB  . PHE A 1 201 ? 56.704 17.705 79.311  1.00 35.96  ? 265 PHE A CB  1 
ATOM   1448  C  CG  . PHE A 1 201 ? 55.646 16.853 78.660  1.00 59.62  ? 265 PHE A CG  1 
ATOM   1449  C  CD1 . PHE A 1 201 ? 54.983 17.270 77.489  1.00 67.89  ? 265 PHE A CD1 1 
ATOM   1450  C  CD2 . PHE A 1 201 ? 55.309 15.627 79.216  1.00 69.75  ? 265 PHE A CD2 1 
ATOM   1451  C  CE1 . PHE A 1 201 ? 54.006 16.474 76.893  1.00 76.71  ? 265 PHE A CE1 1 
ATOM   1452  C  CE2 . PHE A 1 201 ? 54.329 14.828 78.635  1.00 66.95  ? 265 PHE A CE2 1 
ATOM   1453  C  CZ  . PHE A 1 201 ? 53.679 15.248 77.458  1.00 79.70  ? 265 PHE A CZ  1 
ATOM   1454  N  N   . PRO A 1 202 ? 60.176 18.901 78.598  1.00 29.85  ? 266 PRO A N   1 
ATOM   1455  C  CA  . PRO A 1 202 ? 61.224 19.704 79.283  1.00 37.12  ? 266 PRO A CA  1 
ATOM   1456  C  C   . PRO A 1 202 ? 60.767 21.119 79.535  1.00 33.22  ? 266 PRO A C   1 
ATOM   1457  O  O   . PRO A 1 202 ? 60.128 21.718 78.692  1.00 41.99  ? 266 PRO A O   1 
ATOM   1458  C  CB  . PRO A 1 202 ? 62.371 19.766 78.279  1.00 29.76  ? 266 PRO A CB  1 
ATOM   1459  C  CG  . PRO A 1 202 ? 61.717 19.504 76.997  1.00 35.14  ? 266 PRO A CG  1 
ATOM   1460  C  CD  . PRO A 1 202 ? 60.593 18.522 77.254  1.00 33.32  ? 266 PRO A CD  1 
ATOM   1461  N  N   . THR A 1 203 ? 61.086 21.623 80.707  1.00 38.79  ? 267 THR A N   1 
ATOM   1462  C  CA  . THR A 1 203 ? 60.769 22.974 81.069  1.00 45.54  ? 267 THR A CA  1 
ATOM   1463  C  C   . THR A 1 203 ? 62.098 23.629 81.458  1.00 54.76  ? 267 THR A C   1 
ATOM   1464  O  O   . THR A 1 203 ? 62.863 23.097 82.284  1.00 49.94  ? 267 THR A O   1 
ATOM   1465  C  CB  . THR A 1 203 ? 59.717 23.022 82.163  1.00 51.97  ? 267 THR A CB  1 
ATOM   1466  O  OG1 . THR A 1 203 ? 59.382 24.388 82.418  1.00 63.56  ? 267 THR A OG1 1 
ATOM   1467  C  CG2 . THR A 1 203 ? 60.217 22.380 83.431  1.00 77.34  ? 267 THR A CG2 1 
ATOM   1468  N  N   . CYS A 1 204 ? 62.385 24.764 80.824  1.00 54.49  ? 268 CYS A N   1 
ATOM   1469  C  CA  . CYS A 1 204 ? 63.747 25.267 80.757  1.00 40.51  ? 268 CYS A CA  1 
ATOM   1470  C  C   . CYS A 1 204 ? 63.957 26.701 81.237  1.00 46.11  ? 268 CYS A C   1 
ATOM   1471  O  O   . CYS A 1 204 ? 63.027 27.509 81.224  1.00 73.10  ? 268 CYS A O   1 
ATOM   1472  C  CB  . CYS A 1 204 ? 64.177 25.162 79.335  1.00 47.76  ? 268 CYS A CB  1 
ATOM   1473  S  SG  . CYS A 1 204 ? 63.930 23.519 78.699  1.00 111.79 ? 268 CYS A SG  1 
ATOM   1474  N  N   . TYR A 1 205 ? 65.176 27.016 81.669  1.00 43.27  ? 269 TYR A N   1 
ATOM   1475  C  CA  . TYR A 1 205 ? 65.575 28.421 81.842  1.00 44.66  ? 269 TYR A CA  1 
ATOM   1476  C  C   . TYR A 1 205 ? 67.024 28.610 81.490  1.00 51.25  ? 269 TYR A C   1 
ATOM   1477  O  O   . TYR A 1 205 ? 67.702 27.661 81.104  1.00 58.69  ? 269 TYR A O   1 
ATOM   1478  C  CB  . TYR A 1 205 ? 65.339 28.914 83.247  1.00 47.98  ? 269 TYR A CB  1 
ATOM   1479  C  CG  . TYR A 1 205 ? 66.128 28.134 84.253  1.00 66.19  ? 269 TYR A CG  1 
ATOM   1480  C  CD1 . TYR A 1 205 ? 67.221 28.717 84.891  1.00 58.01  ? 269 TYR A CD1 1 
ATOM   1481  C  CD2 . TYR A 1 205 ? 65.797 26.794 84.557  1.00 49.29  ? 269 TYR A CD2 1 
ATOM   1482  C  CE1 . TYR A 1 205 ? 67.976 28.011 85.833  1.00 55.60  ? 269 TYR A CE1 1 
ATOM   1483  C  CE2 . TYR A 1 205 ? 66.541 26.077 85.487  1.00 51.20  ? 269 TYR A CE2 1 
ATOM   1484  C  CZ  . TYR A 1 205 ? 67.638 26.693 86.127  1.00 59.65  ? 269 TYR A CZ  1 
ATOM   1485  O  OH  . TYR A 1 205 ? 68.392 25.997 87.056  1.00 49.05  ? 269 TYR A OH  1 
ATOM   1486  N  N   . TYR A 1 206 ? 67.490 29.847 81.597  1.00 55.04  ? 270 TYR A N   1 
ATOM   1487  C  CA  . TYR A 1 206 ? 68.811 30.170 81.105  1.00 59.28  ? 270 TYR A CA  1 
ATOM   1488  C  C   . TYR A 1 206 ? 69.577 30.911 82.139  1.00 61.07  ? 270 TYR A C   1 
ATOM   1489  O  O   . TYR A 1 206 ? 69.107 31.925 82.657  1.00 75.14  ? 270 TYR A O   1 
ATOM   1490  C  CB  . TYR A 1 206 ? 68.750 31.029 79.844  1.00 57.67  ? 270 TYR A CB  1 
ATOM   1491  C  CG  . TYR A 1 206 ? 70.108 31.561 79.425  1.00 60.24  ? 270 TYR A CG  1 
ATOM   1492  C  CD1 . TYR A 1 206 ? 70.415 32.894 79.565  1.00 61.56  ? 270 TYR A CD1 1 
ATOM   1493  C  CD2 . TYR A 1 206 ? 71.092 30.711 78.919  1.00 83.99  ? 270 TYR A CD2 1 
ATOM   1494  C  CE1 . TYR A 1 206 ? 71.659 33.390 79.206  1.00 77.37  ? 270 TYR A CE1 1 
ATOM   1495  C  CE2 . TYR A 1 206 ? 72.343 31.201 78.551  1.00 90.60  ? 270 TYR A CE2 1 
ATOM   1496  C  CZ  . TYR A 1 206 ? 72.613 32.550 78.705  1.00 66.84  ? 270 TYR A CZ  1 
ATOM   1497  O  OH  . TYR A 1 206 ? 73.819 33.090 78.348  1.00 64.53  ? 270 TYR A OH  1 
ATOM   1498  N  N   . THR A 1 207 ? 70.776 30.414 82.416  1.00 58.22  ? 271 THR A N   1 
ATOM   1499  C  CA  . THR A 1 207 ? 71.711 31.116 83.282  1.00 69.44  ? 271 THR A CA  1 
ATOM   1500  C  C   . THR A 1 207 ? 73.160 30.752 82.984  1.00 75.12  ? 271 THR A C   1 
ATOM   1501  O  O   . THR A 1 207 ? 73.443 29.675 82.453  1.00 70.05  ? 271 THR A O   1 
ATOM   1502  C  CB  . THR A 1 207 ? 71.424 30.850 84.753  1.00 70.27  ? 271 THR A CB  1 
ATOM   1503  O  OG1 . THR A 1 207 ? 72.263 31.701 85.557  1.00 93.52  ? 271 THR A OG1 1 
ATOM   1504  C  CG2 . THR A 1 207 ? 71.637 29.331 85.083  1.00 64.29  ? 271 THR A CG2 1 
ATOM   1505  N  N   . SER A 1 208 ? 74.071 31.668 83.313  1.00 70.32  ? 272 SER A N   1 
ATOM   1506  C  CA  . SER A 1 208 ? 75.484 31.371 83.268  1.00 75.87  ? 272 SER A CA  1 
ATOM   1507  C  C   . SER A 1 208 ? 75.850 30.631 81.958  1.00 90.26  ? 272 SER A C   1 
ATOM   1508  O  O   . SER A 1 208 ? 76.541 29.595 81.959  1.00 92.72  ? 272 SER A O   1 
ATOM   1509  C  CB  . SER A 1 208 ? 75.862 30.560 84.514  1.00 66.29  ? 272 SER A CB  1 
ATOM   1510  O  OG  . SER A 1 208 ? 77.266 30.488 84.681  1.00 108.78 ? 272 SER A OG  1 
ATOM   1511  N  N   . GLY A 1 209 ? 75.351 31.161 80.844  1.00 76.95  ? 273 GLY A N   1 
ATOM   1512  C  CA  . GLY A 1 209 ? 75.722 30.663 79.526  1.00 71.92  ? 273 GLY A CA  1 
ATOM   1513  C  C   . GLY A 1 209 ? 75.207 29.287 79.187  1.00 60.68  ? 273 GLY A C   1 
ATOM   1514  O  O   . GLY A 1 209 ? 75.657 28.677 78.221  1.00 82.45  ? 273 GLY A O   1 
ATOM   1515  N  N   . LYS A 1 210 ? 74.271 28.787 79.977  1.00 49.41  ? 274 LYS A N   1 
ATOM   1516  C  CA  . LYS A 1 210 ? 73.709 27.465 79.715  1.00 53.15  ? 274 LYS A CA  1 
ATOM   1517  C  C   . LYS A 1 210 ? 72.181 27.415 79.852  1.00 54.36  ? 274 LYS A C   1 
ATOM   1518  O  O   . LYS A 1 210 ? 71.569 28.101 80.667  1.00 54.08  ? 274 LYS A O   1 
ATOM   1519  C  CB  . LYS A 1 210 ? 74.391 26.397 80.584  1.00 51.87  ? 274 LYS A CB  1 
ATOM   1520  C  CG  . LYS A 1 210 ? 75.808 26.071 80.089  1.00 77.02  ? 274 LYS A CG  1 
ATOM   1521  C  CD  . LYS A 1 210 ? 76.560 25.061 80.940  1.00 100.06 ? 274 LYS A CD  1 
ATOM   1522  C  CE  . LYS A 1 210 ? 77.139 25.719 82.192  1.00 127.83 ? 274 LYS A CE  1 
ATOM   1523  N  NZ  . LYS A 1 210 ? 78.456 25.135 82.570  1.00 140.23 ? 274 LYS A NZ  1 
ATOM   1524  N  N   . VAL A 1 211 ? 71.554 26.610 79.021  1.00 60.00  ? 275 VAL A N   1 
ATOM   1525  C  CA  . VAL A 1 211 ? 70.156 26.355 79.211  1.00 54.61  ? 275 VAL A CA  1 
ATOM   1526  C  C   . VAL A 1 211 ? 70.001 25.077 80.009  1.00 51.32  ? 275 VAL A C   1 
ATOM   1527  O  O   . VAL A 1 211 ? 70.711 24.102 79.783  1.00 75.03  ? 275 VAL A O   1 
ATOM   1528  C  CB  . VAL A 1 211 ? 69.431 26.265 77.897  1.00 42.21  ? 275 VAL A CB  1 
ATOM   1529  C  CG1 . VAL A 1 211 ? 67.991 25.867 78.134  1.00 40.98  ? 275 VAL A CG1 1 
ATOM   1530  C  CG2 . VAL A 1 211 ? 69.458 27.599 77.273  1.00 39.69  ? 275 VAL A CG2 1 
ATOM   1531  N  N   . LYS A 1 212 ? 69.060 25.101 80.940  1.00 54.00  ? 276 LYS A N   1 
ATOM   1532  C  CA  . LYS A 1 212 ? 68.874 24.040 81.904  1.00 51.46  ? 276 LYS A CA  1 
ATOM   1533  C  C   . LYS A 1 212 ? 67.425 23.669 81.890  1.00 47.19  ? 276 LYS A C   1 
ATOM   1534  O  O   . LYS A 1 212 ? 66.559 24.495 82.142  1.00 47.52  ? 276 LYS A O   1 
ATOM   1535  C  CB  . LYS A 1 212 ? 69.301 24.513 83.289  1.00 59.99  ? 276 LYS A CB  1 
ATOM   1536  C  CG  . LYS A 1 212 ? 70.745 25.016 83.316  1.00 93.41  ? 276 LYS A CG  1 
ATOM   1537  C  CD  . LYS A 1 212 ? 71.210 25.436 84.699  1.00 87.97  ? 276 LYS A CD  1 
ATOM   1538  C  CE  . LYS A 1 212 ? 72.638 25.934 84.644  1.00 81.66  ? 276 LYS A CE  1 
ATOM   1539  N  NZ  . LYS A 1 212 ? 73.162 26.157 85.994  1.00 96.89  ? 276 LYS A NZ  1 
ATOM   1540  N  N   . CYS A 1 213 ? 67.176 22.416 81.554  1.00 59.64  ? 277 CYS A N   1 
ATOM   1541  C  CA  . CYS A 1 213 ? 65.835 21.901 81.347  1.00 57.33  ? 277 CYS A CA  1 
ATOM   1542  C  C   . CYS A 1 213 ? 65.524 20.712 82.239  1.00 54.27  ? 277 CYS A C   1 
ATOM   1543  O  O   . CYS A 1 213 ? 66.287 19.751 82.290  1.00 53.98  ? 277 CYS A O   1 
ATOM   1544  C  CB  . CYS A 1 213 ? 65.687 21.439 79.912  1.00 58.15  ? 277 CYS A CB  1 
ATOM   1545  S  SG  . CYS A 1 213 ? 65.792 22.728 78.729  1.00 99.85  ? 277 CYS A SG  1 
ATOM   1546  N  N   . THR A 1 214 ? 64.372 20.770 82.895  1.00 53.85  ? 278 THR A N   1 
ATOM   1547  C  CA  . THR A 1 214 ? 63.846 19.660 83.694  1.00 54.21  ? 278 THR A CA  1 
ATOM   1548  C  C   . THR A 1 214 ? 62.806 18.823 82.932  1.00 53.30  ? 278 THR A C   1 
ATOM   1549  O  O   . THR A 1 214 ? 61.682 19.259 82.697  1.00 58.40  ? 278 THR A O   1 
ATOM   1550  C  CB  . THR A 1 214 ? 63.177 20.201 84.965  1.00 61.55  ? 278 THR A CB  1 
ATOM   1551  O  OG1 . THR A 1 214 ? 64.069 21.099 85.647  1.00 70.96  ? 278 THR A OG1 1 
ATOM   1552  C  CG2 . THR A 1 214 ? 62.768 19.066 85.865  1.00 47.32  ? 278 THR A CG2 1 
ATOM   1553  N  N   . GLY A 1 215 ? 63.158 17.607 82.557  1.00 54.60  ? 279 GLY A N   1 
ATOM   1554  C  CA  . GLY A 1 215 ? 62.181 16.779 81.862  1.00 61.00  ? 279 GLY A CA  1 
ATOM   1555  C  C   . GLY A 1 215 ? 61.299 15.961 82.804  1.00 51.86  ? 279 GLY A C   1 
ATOM   1556  O  O   . GLY A 1 215 ? 61.322 16.152 84.015  1.00 52.12  ? 279 GLY A O   1 
ATOM   1557  N  N   . THR A 1 216 ? 60.546 15.029 82.225  1.00 41.00  ? 280 THR A N   1 
ATOM   1558  C  CA  . THR A 1 216 ? 59.648 14.140 82.926  1.00 41.47  ? 280 THR A CA  1 
ATOM   1559  C  C   . THR A 1 216 ? 59.793 12.740 82.314  1.00 53.30  ? 280 THR A C   1 
ATOM   1560  O  O   . THR A 1 216 ? 59.624 12.532 81.106  1.00 52.50  ? 280 THR A O   1 
ATOM   1561  C  CB  . THR A 1 216 ? 58.218 14.680 82.814  1.00 47.94  ? 280 THR A CB  1 
ATOM   1562  O  OG1 . THR A 1 216 ? 58.012 15.681 83.830  1.00 61.95  ? 280 THR A OG1 1 
ATOM   1563  C  CG2 . THR A 1 216 ? 57.193 13.601 82.980  1.00 44.26  ? 280 THR A CG2 1 
ATOM   1564  N  N   . ASN A 1 217 ? 60.154 11.773 83.137  1.00 53.95  ? 281 ASN A N   1 
ATOM   1565  C  CA  . ASN A 1 217 ? 60.389 10.444 82.611  1.00 47.95  ? 281 ASN A CA  1 
ATOM   1566  C  C   . ASN A 1 217 ? 59.136 9.638  82.831  1.00 59.63  ? 281 ASN A C   1 
ATOM   1567  O  O   . ASN A 1 217 ? 58.776 9.305  83.993  1.00 52.93  ? 281 ASN A O   1 
ATOM   1568  C  CB  . ASN A 1 217 ? 61.575 9.804  83.311  1.00 58.05  ? 281 ASN A CB  1 
ATOM   1569  C  CG  . ASN A 1 217 ? 61.964 8.456  82.728  1.00 73.22  ? 281 ASN A CG  1 
ATOM   1570  O  OD1 . ASN A 1 217 ? 61.122 7.638  82.315  1.00 56.79  ? 281 ASN A OD1 1 
ATOM   1571  N  ND2 . ASN A 1 217 ? 63.268 8.202  82.728  1.00 87.08  ? 281 ASN A ND2 1 
ATOM   1572  N  N   . LEU A 1 218 ? 58.466 9.345  81.711  1.00 52.74  ? 282 LEU A N   1 
ATOM   1573  C  CA  . LEU A 1 218 ? 57.192 8.639  81.745  1.00 58.07  ? 282 LEU A CA  1 
ATOM   1574  C  C   . LEU A 1 218 ? 57.356 7.141  81.711  1.00 69.40  ? 282 LEU A C   1 
ATOM   1575  O  O   . LEU A 1 218 ? 56.357 6.408  81.731  1.00 76.41  ? 282 LEU A O   1 
ATOM   1576  C  CB  . LEU A 1 218 ? 56.284 9.060  80.605  1.00 51.11  ? 282 LEU A CB  1 
ATOM   1577  C  CG  . LEU A 1 218 ? 55.607 10.414 80.727  1.00 56.28  ? 282 LEU A CG  1 
ATOM   1578  C  CD1 . LEU A 1 218 ? 56.437 11.357 79.946  1.00 66.71  ? 282 LEU A CD1 1 
ATOM   1579  C  CD2 . LEU A 1 218 ? 54.227 10.345 80.128  1.00 64.82  ? 282 LEU A CD2 1 
ATOM   1580  N  N   . TRP A 1 219 ? 58.612 6.698  81.692  1.00 63.18  ? 283 TRP A N   1 
ATOM   1581  C  CA  . TRP A 1 219 ? 58.933 5.295  81.539  1.00 59.81  ? 283 TRP A CA  1 
ATOM   1582  C  C   . TRP A 1 219 ? 59.435 4.652  82.796  1.00 60.98  ? 283 TRP A C   1 
ATOM   1583  O  O   . TRP A 1 219 ? 58.694 3.932  83.453  1.00 61.69  ? 283 TRP A O   1 
ATOM   1584  C  CB  . TRP A 1 219 ? 59.939 5.165  80.415  1.00 72.43  ? 283 TRP A CB  1 
ATOM   1585  C  CG  . TRP A 1 219 ? 60.459 3.778  80.168  1.00 92.76  ? 283 TRP A CG  1 
ATOM   1586  C  CD1 . TRP A 1 219 ? 59.871 2.561  80.507  1.00 104.97 ? 283 TRP A CD1 1 
ATOM   1587  C  CD2 . TRP A 1 219 ? 61.689 3.427  79.472  1.00 83.50  ? 283 TRP A CD2 1 
ATOM   1588  N  NE1 . TRP A 1 219 ? 60.654 1.523  80.101  1.00 104.78 ? 283 TRP A NE1 1 
ATOM   1589  C  CE2 . TRP A 1 219 ? 61.757 1.976  79.471  1.00 80.66  ? 283 TRP A CE2 1 
ATOM   1590  C  CE3 . TRP A 1 219 ? 62.710 4.153  78.874  1.00 81.09  ? 283 TRP A CE3 1 
ATOM   1591  C  CZ2 . TRP A 1 219 ? 62.804 1.302  78.892  1.00 82.89  ? 283 TRP A CZ2 1 
ATOM   1592  C  CZ3 . TRP A 1 219 ? 63.766 3.457  78.293  1.00 79.17  ? 283 TRP A CZ3 1 
ATOM   1593  C  CH2 . TRP A 1 219 ? 63.808 2.064  78.305  1.00 78.66  ? 283 TRP A CH2 1 
ATOM   1594  N  N   . ASN A 1 220 ? 60.690 4.924  83.147  1.00 66.35  ? 284 ASN A N   1 
ATOM   1595  C  CA  . ASN A 1 220 ? 61.388 4.148  84.161  1.00 64.65  ? 284 ASN A CA  1 
ATOM   1596  C  C   . ASN A 1 220 ? 61.882 4.962  85.344  1.00 65.45  ? 284 ASN A C   1 
ATOM   1597  O  O   . ASN A 1 220 ? 62.821 4.555  86.027  1.00 102.06 ? 284 ASN A O   1 
ATOM   1598  C  CB  . ASN A 1 220 ? 62.563 3.405  83.523  1.00 68.45  ? 284 ASN A CB  1 
ATOM   1599  C  CG  . ASN A 1 220 ? 63.460 4.315  82.778  1.00 68.44  ? 284 ASN A CG  1 
ATOM   1600  O  OD1 . ASN A 1 220 ? 63.369 5.532  82.935  1.00 72.35  ? 284 ASN A OD1 1 
ATOM   1601  N  ND2 . ASN A 1 220 ? 64.314 3.752  81.929  1.00 71.94  ? 284 ASN A ND2 1 
ATOM   1602  N  N   . ASP A 1 221 ? 61.228 6.081  85.617  1.00 57.99  ? 285 ASP A N   1 
ATOM   1603  C  CA  . ASP A 1 221 ? 61.758 7.023  86.598  1.00 63.96  ? 285 ASP A CA  1 
ATOM   1604  C  C   . ASP A 1 221 ? 60.715 7.909  87.340  1.00 53.77  ? 285 ASP A C   1 
ATOM   1605  O  O   . ASP A 1 221 ? 59.795 8.509  86.754  1.00 46.54  ? 285 ASP A O   1 
ATOM   1606  C  CB  . ASP A 1 221 ? 62.862 7.867  85.925  1.00 79.68  ? 285 ASP A CB  1 
ATOM   1607  C  CG  . ASP A 1 221 ? 63.750 8.627  86.912  1.00 92.65  ? 285 ASP A CG  1 
ATOM   1608  O  OD1 . ASP A 1 221 ? 63.577 8.498  88.156  1.00 59.70  ? 285 ASP A OD1 1 
ATOM   1609  O  OD2 . ASP A 1 221 ? 64.646 9.361  86.413  1.00 114.76 ? 285 ASP A OD2 1 
ATOM   1610  N  N   . ALA A 1 222 ? 60.903 7.983  88.653  1.00 52.28  ? 286 ALA A N   1 
ATOM   1611  C  CA  . ALA A 1 222 ? 60.101 8.826  89.541  1.00 67.94  ? 286 ALA A CA  1 
ATOM   1612  C  C   . ALA A 1 222 ? 60.823 10.124 89.942  1.00 62.45  ? 286 ALA A C   1 
ATOM   1613  O  O   . ALA A 1 222 ? 60.278 10.983 90.617  1.00 62.65  ? 286 ALA A O   1 
ATOM   1614  C  CB  . ALA A 1 222 ? 59.694 8.045  90.786  1.00 73.48  ? 286 ALA A CB  1 
ATOM   1615  N  N   . LYS A 1 223 ? 62.071 10.245 89.545  1.00 63.06  ? 287 LYS A N   1 
ATOM   1616  C  CA  . LYS A 1 223 ? 62.768 11.490 89.651  1.00 52.42  ? 287 LYS A CA  1 
ATOM   1617  C  C   . LYS A 1 223 ? 62.652 12.190 88.302  1.00 58.72  ? 287 LYS A C   1 
ATOM   1618  O  O   . LYS A 1 223 ? 61.993 11.690 87.382  1.00 87.77  ? 287 LYS A O   1 
ATOM   1619  C  CB  . LYS A 1 223 ? 64.223 11.216 89.942  1.00 70.40  ? 287 LYS A CB  1 
ATOM   1620  C  CG  . LYS A 1 223 ? 64.513 10.469 91.240  1.00 79.55  ? 287 LYS A CG  1 
ATOM   1621  C  CD  . LYS A 1 223 ? 66.037 10.501 91.459  1.00 109.59 ? 287 LYS A CD  1 
ATOM   1622  C  CE  . LYS A 1 223 ? 66.548 9.589  92.556  1.00 86.54  ? 287 LYS A CE  1 
ATOM   1623  N  NZ  . LYS A 1 223 ? 67.965 9.910  92.862  1.00 90.99  ? 287 LYS A NZ  1 
ATOM   1624  N  N   . ARG A 1 224 ? 63.280 13.350 88.172  1.00 57.64  ? 288 ARG A N   1 
ATOM   1625  C  CA  . ARG A 1 224 ? 63.199 14.091 86.914  1.00 58.31  ? 288 ARG A CA  1 
ATOM   1626  C  C   . ARG A 1 224 ? 64.572 14.236 86.265  1.00 50.27  ? 288 ARG A C   1 
ATOM   1627  O  O   . ARG A 1 224 ? 65.503 14.785 86.848  1.00 45.86  ? 288 ARG A O   1 
ATOM   1628  C  CB  . ARG A 1 224 ? 62.537 15.466 87.083  1.00 61.23  ? 288 ARG A CB  1 
ATOM   1629  C  CG  . ARG A 1 224 ? 61.355 15.498 88.030  1.00 68.06  ? 288 ARG A CG  1 
ATOM   1630  C  CD  . ARG A 1 224 ? 60.573 16.780 87.867  1.00 65.87  ? 288 ARG A CD  1 
ATOM   1631  N  NE  . ARG A 1 224 ? 59.436 16.504 87.013  1.00 67.55  ? 288 ARG A NE  1 
ATOM   1632  C  CZ  . ARG A 1 224 ? 58.186 16.489 87.444  1.00 66.48  ? 288 ARG A CZ  1 
ATOM   1633  N  NH1 . ARG A 1 224 ? 57.925 16.779 88.715  1.00 79.49  ? 288 ARG A NH1 1 
ATOM   1634  N  NH2 . ARG A 1 224 ? 57.205 16.214 86.594  1.00 50.60  ? 288 ARG A NH2 1 
ATOM   1635  N  N   . PRO A 1 225 ? 64.694 13.752 85.030  1.00 49.02  ? 289 PRO A N   1 
ATOM   1636  C  CA  . PRO A 1 225 ? 65.955 13.931 84.345  1.00 47.10  ? 289 PRO A CA  1 
ATOM   1637  C  C   . PRO A 1 225 ? 66.238 15.413 84.270  1.00 45.90  ? 289 PRO A C   1 
ATOM   1638  O  O   . PRO A 1 225 ? 65.321 16.233 84.412  1.00 53.42  ? 289 PRO A O   1 
ATOM   1639  C  CB  . PRO A 1 225 ? 65.660 13.389 82.940  1.00 53.06  ? 289 PRO A CB  1 
ATOM   1640  C  CG  . PRO A 1 225 ? 64.464 12.475 83.127  1.00 60.72  ? 289 PRO A CG  1 
ATOM   1641  C  CD  . PRO A 1 225 ? 63.657 13.145 84.165  1.00 44.06  ? 289 PRO A CD  1 
ATOM   1642  N  N   . PHE A 1 226 ? 67.493 15.759 84.038  1.00 43.15  ? 290 PHE A N   1 
ATOM   1643  C  CA  . PHE A 1 226 ? 67.864 17.141 83.935  1.00 42.95  ? 290 PHE A CA  1 
ATOM   1644  C  C   . PHE A 1 226 ? 68.918 17.332 82.873  1.00 55.76  ? 290 PHE A C   1 
ATOM   1645  O  O   . PHE A 1 226 ? 69.819 16.505 82.720  1.00 64.03  ? 290 PHE A O   1 
ATOM   1646  C  CB  . PHE A 1 226 ? 68.372 17.609 85.261  1.00 46.93  ? 290 PHE A CB  1 
ATOM   1647  C  CG  . PHE A 1 226 ? 68.488 19.091 85.386  1.00 63.09  ? 290 PHE A CG  1 
ATOM   1648  C  CD1 . PHE A 1 226 ? 67.451 19.824 85.969  1.00 54.22  ? 290 PHE A CD1 1 
ATOM   1649  C  CD2 . PHE A 1 226 ? 69.661 19.755 84.987  1.00 69.05  ? 290 PHE A CD2 1 
ATOM   1650  C  CE1 . PHE A 1 226 ? 67.562 21.185 86.142  1.00 48.18  ? 290 PHE A CE1 1 
ATOM   1651  C  CE2 . PHE A 1 226 ? 69.775 21.120 85.150  1.00 67.66  ? 290 PHE A CE2 1 
ATOM   1652  C  CZ  . PHE A 1 226 ? 68.717 21.838 85.729  1.00 53.92  ? 290 PHE A CZ  1 
ATOM   1653  N  N   . LEU A 1 227 ? 68.801 18.451 82.160  1.00 58.26  ? 291 LEU A N   1 
ATOM   1654  C  CA  . LEU A 1 227 ? 69.553 18.687 80.960  1.00 46.68  ? 291 LEU A CA  1 
ATOM   1655  C  C   . LEU A 1 227 ? 70.196 20.041 80.957  1.00 50.44  ? 291 LEU A C   1 
ATOM   1656  O  O   . LEU A 1 227 ? 69.555 21.040 81.244  1.00 51.68  ? 291 LEU A O   1 
ATOM   1657  C  CB  . LEU A 1 227 ? 68.638 18.597 79.766  1.00 48.89  ? 291 LEU A CB  1 
ATOM   1658  C  CG  . LEU A 1 227 ? 69.369 18.829 78.440  1.00 63.95  ? 291 LEU A CG  1 
ATOM   1659  C  CD1 . LEU A 1 227 ? 70.459 17.769 78.198  1.00 79.33  ? 291 LEU A CD1 1 
ATOM   1660  C  CD2 . LEU A 1 227 ? 68.381 18.865 77.285  1.00 62.15  ? 291 LEU A CD2 1 
ATOM   1661  N  N   . GLU A 1 228 ? 71.473 20.061 80.597  1.00 58.63  ? 292 GLU A N   1 
ATOM   1662  C  CA  . GLU A 1 228 ? 72.235 21.278 80.481  1.00 54.27  ? 292 GLU A CA  1 
ATOM   1663  C  C   . GLU A 1 228 ? 72.753 21.272 79.063  1.00 63.32  ? 292 GLU A C   1 
ATOM   1664  O  O   . GLU A 1 228 ? 73.173 20.215 78.564  1.00 78.07  ? 292 GLU A O   1 
ATOM   1665  C  CB  . GLU A 1 228 ? 73.399 21.214 81.450  1.00 76.70  ? 292 GLU A CB  1 
ATOM   1666  C  CG  . GLU A 1 228 ? 73.715 22.516 82.155  1.00 100.70 ? 292 GLU A CG  1 
ATOM   1667  C  CD  . GLU A 1 228 ? 75.028 22.451 82.938  1.00 130.75 ? 292 GLU A CD  1 
ATOM   1668  O  OE1 . GLU A 1 228 ? 75.008 22.719 84.157  1.00 135.13 ? 292 GLU A OE1 1 
ATOM   1669  O  OE2 . GLU A 1 228 ? 76.080 22.128 82.341  1.00 164.18 ? 292 GLU A OE2 1 
ATOM   1670  N  N   . PHE A 1 229 ? 72.696 22.428 78.398  1.00 57.87  ? 293 PHE A N   1 
ATOM   1671  C  CA  . PHE A 1 229 ? 73.321 22.592 77.074  1.00 61.26  ? 293 PHE A CA  1 
ATOM   1672  C  C   . PHE A 1 229 ? 73.540 24.041 76.812  1.00 63.31  ? 293 PHE A C   1 
ATOM   1673  O  O   . PHE A 1 229 ? 72.851 24.870 77.405  1.00 63.66  ? 293 PHE A O   1 
ATOM   1674  C  CB  . PHE A 1 229 ? 72.471 22.015 75.943  1.00 52.33  ? 293 PHE A CB  1 
ATOM   1675  C  CG  . PHE A 1 229 ? 71.152 22.713 75.730  1.00 46.94  ? 293 PHE A CG  1 
ATOM   1676  C  CD1 . PHE A 1 229 ? 71.073 23.887 74.993  1.00 52.70  ? 293 PHE A CD1 1 
ATOM   1677  C  CD2 . PHE A 1 229 ? 69.976 22.160 76.212  1.00 45.28  ? 293 PHE A CD2 1 
ATOM   1678  C  CE1 . PHE A 1 229 ? 69.831 24.516 74.762  1.00 50.12  ? 293 PHE A CE1 1 
ATOM   1679  C  CE2 . PHE A 1 229 ? 68.731 22.790 75.992  1.00 51.47  ? 293 PHE A CE2 1 
ATOM   1680  C  CZ  . PHE A 1 229 ? 68.667 23.974 75.273  1.00 39.30  ? 293 PHE A CZ  1 
ATOM   1681  N  N   . ASP A 1 230 ? 74.463 24.338 75.900  1.00 58.05  ? 294 ASP A N   1 
ATOM   1682  C  CA  . ASP A 1 230 ? 74.842 25.716 75.612  1.00 58.37  ? 294 ASP A CA  1 
ATOM   1683  C  C   . ASP A 1 230 ? 74.640 26.015 74.148  1.00 65.28  ? 294 ASP A C   1 
ATOM   1684  O  O   . ASP A 1 230 ? 74.098 25.179 73.424  1.00 52.88  ? 294 ASP A O   1 
ATOM   1685  C  CB  . ASP A 1 230 ? 76.295 25.953 75.984  1.00 72.92  ? 294 ASP A CB  1 
ATOM   1686  C  CG  . ASP A 1 230 ? 77.249 25.046 75.231  1.00 103.92 ? 294 ASP A CG  1 
ATOM   1687  O  OD1 . ASP A 1 230 ? 76.827 24.379 74.252  1.00 121.88 ? 294 ASP A OD1 1 
ATOM   1688  O  OD2 . ASP A 1 230 ? 78.434 25.015 75.622  1.00 130.60 ? 294 ASP A OD2 1 
ATOM   1689  N  N   . GLN A 1 231 ? 75.102 27.189 73.706  1.00 72.67  ? 295 GLN A N   1 
ATOM   1690  C  CA  . GLN A 1 231 ? 74.838 27.600 72.338  1.00 67.18  ? 295 GLN A CA  1 
ATOM   1691  C  C   . GLN A 1 231 ? 75.452 26.659 71.319  1.00 61.75  ? 295 GLN A C   1 
ATOM   1692  O  O   . GLN A 1 231 ? 74.885 26.503 70.247  1.00 64.32  ? 295 GLN A O   1 
ATOM   1693  C  CB  . GLN A 1 231 ? 75.165 29.074 72.070  1.00 80.34  ? 295 GLN A CB  1 
ATOM   1694  C  CG  . GLN A 1 231 ? 76.594 29.531 72.304  1.00 104.39 ? 295 GLN A CG  1 
ATOM   1695  C  CD  . GLN A 1 231 ? 76.746 31.020 72.049  1.00 115.81 ? 295 GLN A CD  1 
ATOM   1696  O  OE1 . GLN A 1 231 ? 75.769 31.771 72.080  1.00 162.10 ? 295 GLN A OE1 1 
ATOM   1697  N  NE2 . GLN A 1 231 ? 77.971 31.454 71.798  1.00 155.60 ? 295 GLN A NE2 1 
ATOM   1698  N  N   . SER A 1 232 ? 76.566 26.004 71.655  1.00 72.57  ? 296 SER A N   1 
ATOM   1699  C  CA  . SER A 1 232 ? 77.235 25.115 70.691  1.00 81.98  ? 296 SER A CA  1 
ATOM   1700  C  C   . SER A 1 232 ? 76.715 23.689 70.711  1.00 68.93  ? 296 SER A C   1 
ATOM   1701  O  O   . SER A 1 232 ? 77.335 22.803 70.118  1.00 83.73  ? 296 SER A O   1 
ATOM   1702  C  CB  . SER A 1 232 ? 78.730 25.102 70.922  1.00 90.17  ? 296 SER A CB  1 
ATOM   1703  O  OG  . SER A 1 232 ? 79.001 24.448 72.143  1.00 132.05 ? 296 SER A OG  1 
ATOM   1704  N  N   . PHE A 1 233 ? 75.575 23.488 71.374  1.00 61.50  ? 297 PHE A N   1 
ATOM   1705  C  CA  . PHE A 1 233 ? 74.914 22.171 71.536  1.00 69.87  ? 297 PHE A CA  1 
ATOM   1706  C  C   . PHE A 1 233 ? 75.731 21.101 72.257  1.00 74.06  ? 297 PHE A C   1 
ATOM   1707  O  O   . PHE A 1 233 ? 75.416 19.916 72.143  1.00 93.44  ? 297 PHE A O   1 
ATOM   1708  C  CB  . PHE A 1 233 ? 74.401 21.572 70.215  1.00 69.72  ? 297 PHE A CB  1 
ATOM   1709  C  CG  . PHE A 1 233 ? 73.182 22.234 69.668  1.00 76.07  ? 297 PHE A CG  1 
ATOM   1710  C  CD1 . PHE A 1 233 ? 72.207 22.725 70.502  1.00 78.98  ? 297 PHE A CD1 1 
ATOM   1711  C  CD2 . PHE A 1 233 ? 73.002 22.339 68.298  1.00 100.61 ? 297 PHE A CD2 1 
ATOM   1712  C  CE1 . PHE A 1 233 ? 71.077 23.338 69.989  1.00 100.13 ? 297 PHE A CE1 1 
ATOM   1713  C  CE2 . PHE A 1 233 ? 71.873 22.950 67.774  1.00 102.66 ? 297 PHE A CE2 1 
ATOM   1714  C  CZ  . PHE A 1 233 ? 70.910 23.450 68.624  1.00 99.87  ? 297 PHE A CZ  1 
ATOM   1715  N  N   . THR A 1 234 ? 76.775 21.488 72.981  1.00 67.31  ? 298 THR A N   1 
ATOM   1716  C  CA  . THR A 1 234 ? 77.414 20.529 73.879  1.00 68.70  ? 298 THR A CA  1 
ATOM   1717  C  C   . THR A 1 234 ? 76.475 20.416 75.092  1.00 60.34  ? 298 THR A C   1 
ATOM   1718  O  O   . THR A 1 234 ? 76.009 21.428 75.649  1.00 61.75  ? 298 THR A O   1 
ATOM   1719  C  CB  . THR A 1 234 ? 78.918 20.865 74.217  1.00 60.95  ? 298 THR A CB  1 
ATOM   1720  O  OG1 . THR A 1 234 ? 79.031 22.211 74.669  1.00 83.95  ? 298 THR A OG1 1 
ATOM   1721  C  CG2 . THR A 1 234 ? 79.796 20.736 72.985  1.00 75.12  ? 298 THR A CG2 1 
ATOM   1722  N  N   . TYR A 1 235 ? 76.135 19.185 75.448  1.00 48.29  ? 299 TYR A N   1 
ATOM   1723  C  CA  . TYR A 1 235 ? 75.099 18.975 76.439  1.00 54.46  ? 299 TYR A CA  1 
ATOM   1724  C  C   . TYR A 1 235 ? 75.467 17.817 77.318  1.00 65.36  ? 299 TYR A C   1 
ATOM   1725  O  O   . TYR A 1 235 ? 76.192 16.921 76.883  1.00 104.17 ? 299 TYR A O   1 
ATOM   1726  C  CB  . TYR A 1 235 ? 73.785 18.648 75.753  1.00 51.40  ? 299 TYR A CB  1 
ATOM   1727  C  CG  . TYR A 1 235 ? 73.727 17.243 75.182  1.00 62.56  ? 299 TYR A CG  1 
ATOM   1728  C  CD1 . TYR A 1 235 ? 74.212 16.947 73.910  1.00 68.58  ? 299 TYR A CD1 1 
ATOM   1729  C  CD2 . TYR A 1 235 ? 73.195 16.204 75.919  1.00 58.19  ? 299 TYR A CD2 1 
ATOM   1730  C  CE1 . TYR A 1 235 ? 74.152 15.632 73.396  1.00 75.21  ? 299 TYR A CE1 1 
ATOM   1731  C  CE2 . TYR A 1 235 ? 73.138 14.901 75.409  1.00 59.09  ? 299 TYR A CE2 1 
ATOM   1732  C  CZ  . TYR A 1 235 ? 73.607 14.622 74.161  1.00 62.17  ? 299 TYR A CZ  1 
ATOM   1733  O  OH  . TYR A 1 235 ? 73.518 13.331 73.697  1.00 71.25  ? 299 TYR A OH  1 
ATOM   1734  N  N   . THR A 1 236 ? 74.959 17.829 78.549  1.00 61.67  ? 300 THR A N   1 
ATOM   1735  C  CA  . THR A 1 236 ? 75.040 16.669 79.446  1.00 66.91  ? 300 THR A CA  1 
ATOM   1736  C  C   . THR A 1 236 ? 73.720 16.476 80.207  1.00 57.20  ? 300 THR A C   1 
ATOM   1737  O  O   . THR A 1 236 ? 73.075 17.425 80.632  1.00 54.70  ? 300 THR A O   1 
ATOM   1738  C  CB  . THR A 1 236 ? 76.188 16.767 80.488  1.00 73.71  ? 300 THR A CB  1 
ATOM   1739  O  OG1 . THR A 1 236 ? 75.793 17.659 81.530  1.00 110.45 ? 300 THR A OG1 1 
ATOM   1740  C  CG2 . THR A 1 236 ? 77.536 17.251 79.874  1.00 72.90  ? 300 THR A CG2 1 
ATOM   1741  N  N   . PHE A 1 237 ? 73.311 15.237 80.374  1.00 59.82  ? 301 PHE A N   1 
ATOM   1742  C  CA  . PHE A 1 237 ? 72.171 14.966 81.192  1.00 48.93  ? 301 PHE A CA  1 
ATOM   1743  C  C   . PHE A 1 237 ? 72.720 14.724 82.564  1.00 53.93  ? 301 PHE A C   1 
ATOM   1744  O  O   . PHE A 1 237 ? 73.755 14.063 82.722  1.00 73.28  ? 301 PHE A O   1 
ATOM   1745  C  CB  . PHE A 1 237 ? 71.475 13.695 80.723  1.00 62.97  ? 301 PHE A CB  1 
ATOM   1746  C  CG  . PHE A 1 237 ? 70.552 13.893 79.567  1.00 63.37  ? 301 PHE A CG  1 
ATOM   1747  C  CD1 . PHE A 1 237 ? 70.983 13.664 78.279  1.00 62.24  ? 301 PHE A CD1 1 
ATOM   1748  C  CD2 . PHE A 1 237 ? 69.231 14.274 79.779  1.00 78.13  ? 301 PHE A CD2 1 
ATOM   1749  C  CE1 . PHE A 1 237 ? 70.121 13.828 77.207  1.00 83.41  ? 301 PHE A CE1 1 
ATOM   1750  C  CE2 . PHE A 1 237 ? 68.357 14.439 78.725  1.00 70.65  ? 301 PHE A CE2 1 
ATOM   1751  C  CZ  . PHE A 1 237 ? 68.806 14.210 77.430  1.00 94.42  ? 301 PHE A CZ  1 
ATOM   1752  N  N   . LYS A 1 238 ? 72.019 15.250 83.560  1.00 63.19  ? 302 LYS A N   1 
ATOM   1753  C  CA  . LYS A 1 238 ? 72.315 14.968 84.971  1.00 67.90  ? 302 LYS A CA  1 
ATOM   1754  C  C   . LYS A 1 238 ? 71.082 14.344 85.612  1.00 75.53  ? 302 LYS A C   1 
ATOM   1755  O  O   . LYS A 1 238 ? 69.961 14.644 85.207  1.00 71.79  ? 302 LYS A O   1 
ATOM   1756  C  CB  . LYS A 1 238 ? 72.708 16.254 85.710  1.00 57.66  ? 302 LYS A CB  1 
ATOM   1757  C  CG  . LYS A 1 238 ? 73.837 17.046 85.022  1.00 61.55  ? 302 LYS A CG  1 
ATOM   1758  C  CD  . LYS A 1 238 ? 74.167 18.302 85.752  1.00 69.76  ? 302 LYS A CD  1 
ATOM   1759  C  CE  . LYS A 1 238 ? 75.632 18.616 85.690  1.00 67.42  ? 302 LYS A CE  1 
ATOM   1760  N  NZ  . LYS A 1 238 ? 76.043 19.323 86.945  1.00 87.00  ? 302 LYS A NZ  1 
ATOM   1761  N  N   . GLU A 1 239 ? 71.289 13.460 86.584  1.00 81.41  ? 303 GLU A N   1 
ATOM   1762  C  CA  . GLU A 1 239 ? 70.188 12.929 87.383  1.00 85.96  ? 303 GLU A CA  1 
ATOM   1763  C  C   . GLU A 1 239 ? 70.322 13.417 88.823  1.00 77.42  ? 303 GLU A C   1 
ATOM   1764  O  O   . GLU A 1 239 ? 71.376 13.263 89.426  1.00 82.46  ? 303 GLU A O   1 
ATOM   1765  C  CB  . GLU A 1 239 ? 70.182 11.402 87.339  1.00 89.88  ? 303 GLU A CB  1 
ATOM   1766  C  CG  . GLU A 1 239 ? 69.160 10.738 88.268  1.00 95.69  ? 303 GLU A CG  1 
ATOM   1767  C  CD  . GLU A 1 239 ? 67.765 10.514 87.639  1.00 116.21 ? 303 GLU A CD  1 
ATOM   1768  O  OE1 . GLU A 1 239 ? 67.569 10.711 86.415  1.00 113.41 ? 303 GLU A OE1 1 
ATOM   1769  O  OE2 . GLU A 1 239 ? 66.847 10.113 88.383  1.00 125.78 ? 303 GLU A OE2 1 
ATOM   1770  N  N   . PRO A 1 240 ? 69.251 13.993 89.382  1.00 65.88  ? 304 PRO A N   1 
ATOM   1771  C  CA  . PRO A 1 240 ? 69.324 14.554 90.718  1.00 66.26  ? 304 PRO A CA  1 
ATOM   1772  C  C   . PRO A 1 240 ? 69.498 13.455 91.751  1.00 80.52  ? 304 PRO A C   1 
ATOM   1773  O  O   . PRO A 1 240 ? 68.872 12.396 91.644  1.00 70.88  ? 304 PRO A O   1 
ATOM   1774  C  CB  . PRO A 1 240 ? 67.972 15.248 90.887  1.00 61.22  ? 304 PRO A CB  1 
ATOM   1775  C  CG  . PRO A 1 240 ? 67.059 14.519 90.003  1.00 68.65  ? 304 PRO A CG  1 
ATOM   1776  C  CD  . PRO A 1 240 ? 67.875 13.974 88.863  1.00 65.52  ? 304 PRO A CD  1 
ATOM   1777  N  N   . CYS A 1 241 ? 70.371 13.720 92.722  1.00 111.38 ? 305 CYS A N   1 
ATOM   1778  C  CA  . CYS A 1 241 ? 70.753 12.762 93.754  1.00 100.59 ? 305 CYS A CA  1 
ATOM   1779  C  C   . CYS A 1 241 ? 70.069 13.110 95.059  1.00 106.07 ? 305 CYS A C   1 
ATOM   1780  O  O   . CYS A 1 241 ? 70.747 13.350 96.060  1.00 146.53 ? 305 CYS A O   1 
ATOM   1781  C  CB  . CYS A 1 241 ? 72.274 12.788 93.978  1.00 97.72  ? 305 CYS A CB  1 
ATOM   1782  S  SG  . CYS A 1 241 ? 73.314 12.669 92.492  1.00 176.76 ? 305 CYS A SG  1 
ATOM   1783  N  N   . LEU A 1 242 ? 68.737 13.152 95.058  1.00 89.66  ? 306 LEU A N   1 
ATOM   1784  C  CA  . LEU A 1 242 ? 67.990 13.539 96.260  1.00 84.76  ? 306 LEU A CA  1 
ATOM   1785  C  C   . LEU A 1 242 ? 66.724 12.712 96.459  1.00 96.18  ? 306 LEU A C   1 
ATOM   1786  O  O   . LEU A 1 242 ? 65.948 12.511 95.513  1.00 82.43  ? 306 LEU A O   1 
ATOM   1787  C  CB  . LEU A 1 242 ? 67.648 15.041 96.236  1.00 64.78  ? 306 LEU A CB  1 
ATOM   1788  C  CG  . LEU A 1 242 ? 68.798 16.040 96.381  1.00 61.00  ? 306 LEU A CG  1 
ATOM   1789  C  CD1 . LEU A 1 242 ? 68.261 17.426 96.174  1.00 64.95  ? 306 LEU A CD1 1 
ATOM   1790  C  CD2 . LEU A 1 242 ? 69.536 15.949 97.730  1.00 64.79  ? 306 LEU A CD2 1 
ATOM   1791  N  N   . GLY A 1 243 ? 66.514 12.253 97.697  1.00 88.39  ? 307 GLY A N   1 
ATOM   1792  C  CA  . GLY A 1 243 ? 65.349 11.435 98.052  1.00 87.69  ? 307 GLY A CA  1 
ATOM   1793  C  C   . GLY A 1 243 ? 63.989 12.081 97.828  1.00 103.85 ? 307 GLY A C   1 
ATOM   1794  O  O   . GLY A 1 243 ? 62.958 11.439 98.031  1.00 125.25 ? 307 GLY A O   1 
ATOM   1795  N  N   . PHE A 1 244 ? 63.992 13.351 97.409  1.00 123.24 ? 308 PHE A N   1 
ATOM   1796  C  CA  . PHE A 1 244 ? 62.775 14.124 97.097  1.00 82.29  ? 308 PHE A CA  1 
ATOM   1797  C  C   . PHE A 1 244 ? 62.334 13.867 95.658  1.00 76.64  ? 308 PHE A C   1 
ATOM   1798  O  O   . PHE A 1 244 ? 62.999 14.256 94.668  1.00 75.82  ? 308 PHE A O   1 
ATOM   1799  C  CB  . PHE A 1 244 ? 63.028 15.611 97.311  1.00 74.80  ? 308 PHE A CB  1 
ATOM   1800  C  CG  . PHE A 1 244 ? 61.801 16.396 97.656  1.00 70.38  ? 308 PHE A CG  1 
ATOM   1801  C  CD1 . PHE A 1 244 ? 61.227 16.289 98.923  1.00 68.89  ? 308 PHE A CD1 1 
ATOM   1802  C  CD2 . PHE A 1 244 ? 61.243 17.278 96.733  1.00 57.22  ? 308 PHE A CD2 1 
ATOM   1803  C  CE1 . PHE A 1 244 ? 60.100 17.031 99.270  1.00 64.65  ? 308 PHE A CE1 1 
ATOM   1804  C  CE2 . PHE A 1 244 ? 60.117 18.007 97.056  1.00 50.98  ? 308 PHE A CE2 1 
ATOM   1805  C  CZ  . PHE A 1 244 ? 59.542 17.889 98.346  1.00 61.44  ? 308 PHE A CZ  1 
ATOM   1806  N  N   . LEU A 1 245 ? 61.208 13.187 95.541  1.00 60.07  ? 309 LEU A N   1 
ATOM   1807  C  CA  . LEU A 1 245 ? 60.839 12.665 94.259  1.00 66.88  ? 309 LEU A CA  1 
ATOM   1808  C  C   . LEU A 1 245 ? 59.969 13.681 93.593  1.00 62.44  ? 309 LEU A C   1 
ATOM   1809  O  O   . LEU A 1 245 ? 58.930 14.006 94.133  1.00 87.51  ? 309 LEU A O   1 
ATOM   1810  C  CB  . LEU A 1 245 ? 60.115 11.337 94.432  1.00 75.63  ? 309 LEU A CB  1 
ATOM   1811  C  CG  . LEU A 1 245 ? 60.920 10.151 94.975  1.00 73.89  ? 309 LEU A CG  1 
ATOM   1812  C  CD1 . LEU A 1 245 ? 60.227 8.843  94.539  1.00 102.43 ? 309 LEU A CD1 1 
ATOM   1813  C  CD2 . LEU A 1 245 ? 62.365 10.179 94.493  1.00 56.69  ? 309 LEU A CD2 1 
ATOM   1814  N  N   . GLY A 1 246 ? 60.407 14.204 92.450  1.00 56.03  ? 310 GLY A N   1 
ATOM   1815  C  CA  . GLY A 1 246 ? 59.657 15.240 91.737  1.00 60.72  ? 310 GLY A CA  1 
ATOM   1816  C  C   . GLY A 1 246 ? 58.365 14.773 91.082  1.00 57.33  ? 310 GLY A C   1 
ATOM   1817  O  O   . GLY A 1 246 ? 57.309 15.437 91.166  1.00 58.62  ? 310 GLY A O   1 
ATOM   1818  N  N   . ASP A 1 247 ? 58.453 13.615 90.442  1.00 59.90  ? 311 ASP A N   1 
ATOM   1819  C  CA  . ASP A 1 247 ? 57.443 13.141 89.480  1.00 74.27  ? 311 ASP A CA  1 
ATOM   1820  C  C   . ASP A 1 247 ? 56.162 12.723 90.179  1.00 73.49  ? 311 ASP A C   1 
ATOM   1821  O  O   . ASP A 1 247 ? 56.100 12.731 91.407  1.00 58.37  ? 311 ASP A O   1 
ATOM   1822  C  CB  . ASP A 1 247 ? 57.998 11.954 88.660  1.00 85.73  ? 311 ASP A CB  1 
ATOM   1823  C  CG  . ASP A 1 247 ? 57.554 11.975 87.195  1.00 86.95  ? 311 ASP A CG  1 
ATOM   1824  O  OD1 . ASP A 1 247 ? 56.447 12.519 86.920  1.00 63.98  ? 311 ASP A OD1 1 
ATOM   1825  O  OD2 . ASP A 1 247 ? 58.323 11.442 86.332  1.00 73.82  ? 311 ASP A OD2 1 
ATOM   1826  N  N   . THR A 1 248 ? 55.153 12.360 89.382  1.00 76.85  ? 312 THR A N   1 
ATOM   1827  C  CA  . THR A 1 248 ? 53.842 11.916 89.866  1.00 66.86  ? 312 THR A CA  1 
ATOM   1828  C  C   . THR A 1 248 ? 53.153 11.033 88.823  1.00 77.66  ? 312 THR A C   1 
ATOM   1829  O  O   . THR A 1 248 ? 53.003 11.444 87.671  1.00 115.62 ? 312 THR A O   1 
ATOM   1830  C  CB  . THR A 1 248 ? 52.926 13.104 90.190  1.00 74.36  ? 312 THR A CB  1 
ATOM   1831  O  OG1 . THR A 1 248 ? 53.516 13.924 91.223  1.00 91.72  ? 312 THR A OG1 1 
ATOM   1832  C  CG2 . THR A 1 248 ? 51.543 12.606 90.626  1.00 67.96  ? 312 THR A CG2 1 
ATOM   1833  N  N   . PRO A 1 249 ? 52.712 9.823  89.219  1.00 83.52  ? 313 PRO A N   1 
ATOM   1834  C  CA  . PRO A 1 249 ? 52.790 9.354  90.592  1.00 78.09  ? 313 PRO A CA  1 
ATOM   1835  C  C   . PRO A 1 249 ? 54.196 8.906  90.930  1.00 75.38  ? 313 PRO A C   1 
ATOM   1836  O  O   . PRO A 1 249 ? 55.087 8.934  90.058  1.00 74.27  ? 313 PRO A O   1 
ATOM   1837  C  CB  . PRO A 1 249 ? 51.827 8.168  90.610  1.00 110.37 ? 313 PRO A CB  1 
ATOM   1838  C  CG  . PRO A 1 249 ? 51.883 7.624  89.217  1.00 112.96 ? 313 PRO A CG  1 
ATOM   1839  C  CD  . PRO A 1 249 ? 52.156 8.794  88.311  1.00 83.10  ? 313 PRO A CD  1 
ATOM   1840  N  N   . ARG A 1 250 ? 54.370 8.512  92.193  1.00 69.20  ? 314 ARG A N   1 
ATOM   1841  C  CA  . ARG A 1 250 ? 55.658 8.127  92.776  1.00 65.73  ? 314 ARG A CA  1 
ATOM   1842  C  C   . ARG A 1 250 ? 55.384 7.324  94.027  1.00 74.67  ? 314 ARG A C   1 
ATOM   1843  O  O   . ARG A 1 250 ? 54.277 7.342  94.554  1.00 99.76  ? 314 ARG A O   1 
ATOM   1844  C  CB  . ARG A 1 250 ? 56.489 9.352  93.136  1.00 62.24  ? 314 ARG A CB  1 
ATOM   1845  C  CG  . ARG A 1 250 ? 55.705 10.391 93.919  1.00 68.02  ? 314 ARG A CG  1 
ATOM   1846  C  CD  . ARG A 1 250 ? 56.591 11.491 94.430  1.00 72.21  ? 314 ARG A CD  1 
ATOM   1847  N  NE  . ARG A 1 250 ? 55.858 12.737 94.650  1.00 80.44  ? 314 ARG A NE  1 
ATOM   1848  C  CZ  . ARG A 1 250 ? 55.283 13.081 95.795  1.00 72.95  ? 314 ARG A CZ  1 
ATOM   1849  N  NH1 . ARG A 1 250 ? 55.338 12.267 96.837  1.00 98.83  ? 314 ARG A NH1 1 
ATOM   1850  N  NH2 . ARG A 1 250 ? 54.656 14.241 95.902  1.00 68.93  ? 314 ARG A NH2 1 
ATOM   1851  N  N   . GLY A 1 251 ? 56.389 6.623  94.512  1.00 77.87  ? 315 GLY A N   1 
ATOM   1852  C  CA  . GLY A 1 251 ? 56.150 5.699  95.596  1.00 123.78 ? 315 GLY A CA  1 
ATOM   1853  C  C   . GLY A 1 251 ? 56.214 6.347  96.959  1.00 137.51 ? 315 GLY A C   1 
ATOM   1854  O  O   . GLY A 1 251 ? 55.215 6.430  97.677  1.00 160.29 ? 315 GLY A O   1 
ATOM   1855  N  N   . ILE A 1 252 ? 57.405 6.821  97.297  1.00 117.20 ? 316 ILE A N   1 
ATOM   1856  C  CA  . ILE A 1 252 ? 57.762 7.124  98.668  1.00 94.54  ? 316 ILE A CA  1 
ATOM   1857  C  C   . ILE A 1 252 ? 59.115 7.784  98.632  1.00 90.99  ? 316 ILE A C   1 
ATOM   1858  O  O   . ILE A 1 252 ? 59.879 7.570  97.691  1.00 112.45 ? 316 ILE A O   1 
ATOM   1859  C  CB  . ILE A 1 252 ? 57.866 5.829  99.510  1.00 101.15 ? 316 ILE A CB  1 
ATOM   1860  C  CG1 . ILE A 1 252 ? 57.587 6.119  100.981 1.00 92.97  ? 316 ILE A CG1 1 
ATOM   1861  C  CG2 . ILE A 1 252 ? 59.215 5.099  99.296  1.00 108.49 ? 316 ILE A CG2 1 
ATOM   1862  C  CD1 . ILE A 1 252 ? 56.115 6.218  101.303 1.00 75.96  ? 316 ILE A CD1 1 
ATOM   1863  N  N   . ASP A 1 253 ? 59.433 8.570  99.652  1.00 92.30  ? 317 ASP A N   1 
ATOM   1864  C  CA  . ASP A 1 253 ? 60.714 9.264  99.657  1.00 98.12  ? 317 ASP A CA  1 
ATOM   1865  C  C   . ASP A 1 253 ? 61.813 8.307  100.070 1.00 85.77  ? 317 ASP A C   1 
ATOM   1866  O  O   . ASP A 1 253 ? 61.580 7.402  100.864 1.00 85.78  ? 317 ASP A O   1 
ATOM   1867  C  CB  . ASP A 1 253 ? 60.677 10.524 100.522 1.00 103.62 ? 317 ASP A CB  1 
ATOM   1868  C  CG  . ASP A 1 253 ? 59.881 11.656 99.870  1.00 113.96 ? 317 ASP A CG  1 
ATOM   1869  O  OD1 . ASP A 1 253 ? 59.841 11.760 98.611  1.00 93.39  ? 317 ASP A OD1 1 
ATOM   1870  O  OD2 . ASP A 1 253 ? 59.288 12.446 100.634 1.00 125.36 ? 317 ASP A OD2 1 
ATOM   1871  N  N   . THR A 1 254 ? 62.993 8.493  99.487  1.00 85.31  ? 318 THR A N   1 
ATOM   1872  C  CA  . THR A 1 254 ? 64.085 7.529  99.593  1.00 99.95  ? 318 THR A CA  1 
ATOM   1873  C  C   . THR A 1 254 ? 65.270 8.172  100.274 1.00 83.22  ? 318 THR A C   1 
ATOM   1874  O  O   . THR A 1 254 ? 65.188 9.305  100.696 1.00 58.11  ? 318 THR A O   1 
ATOM   1875  C  CB  . THR A 1 254 ? 64.561 6.992  98.191  1.00 106.81 ? 318 THR A CB  1 
ATOM   1876  O  OG1 . THR A 1 254 ? 64.996 8.083  97.361  1.00 111.70 ? 318 THR A OG1 1 
ATOM   1877  C  CG2 . THR A 1 254 ? 63.459 6.192  97.484  1.00 92.77  ? 318 THR A CG2 1 
ATOM   1878  N  N   . THR A 1 255 ? 66.360 7.414  100.390 1.00 112.06 ? 319 THR A N   1 
ATOM   1879  C  CA  . THR A 1 255 ? 67.664 7.952  100.750 1.00 104.71 ? 319 THR A CA  1 
ATOM   1880  C  C   . THR A 1 255 ? 68.215 8.642  99.490  1.00 87.45  ? 319 THR A C   1 
ATOM   1881  O  O   . THR A 1 255 ? 67.687 8.447  98.385  1.00 79.10  ? 319 THR A O   1 
ATOM   1882  C  CB  . THR A 1 255 ? 68.620 6.817  101.265 1.00 104.02 ? 319 THR A CB  1 
ATOM   1883  O  OG1 . THR A 1 255 ? 68.765 5.805  100.264 1.00 102.09 ? 319 THR A OG1 1 
ATOM   1884  C  CG2 . THR A 1 255 ? 68.070 6.143  102.514 1.00 83.95  ? 319 THR A CG2 1 
ATOM   1885  N  N   . ASN A 1 256 ? 69.263 9.443  99.637  1.00 78.45  ? 320 ASN A N   1 
ATOM   1886  C  CA  . ASN A 1 256 ? 69.874 10.057 98.459  1.00 106.36 ? 320 ASN A CA  1 
ATOM   1887  C  C   . ASN A 1 256 ? 70.777 9.112  97.689  1.00 104.47 ? 320 ASN A C   1 
ATOM   1888  O  O   . ASN A 1 256 ? 71.580 8.411  98.285  1.00 112.51 ? 320 ASN A O   1 
ATOM   1889  C  CB  . ASN A 1 256 ? 70.677 11.284 98.857  1.00 106.99 ? 320 ASN A CB  1 
ATOM   1890  C  CG  . ASN A 1 256 ? 69.864 12.271 99.614  1.00 93.39  ? 320 ASN A CG  1 
ATOM   1891  O  OD1 . ASN A 1 256 ? 68.704 12.019 99.933  1.00 92.52  ? 320 ASN A OD1 1 
ATOM   1892  N  ND2 . ASN A 1 256 ? 70.458 13.411 99.911  1.00 98.69  ? 320 ASN A ND2 1 
ATOM   1893  N  N   . TYR A 1 257 ? 70.648 9.103  96.367  1.00 108.61 ? 321 TYR A N   1 
ATOM   1894  C  CA  . TYR A 1 257 ? 71.600 8.392  95.511  1.00 121.42 ? 321 TYR A CA  1 
ATOM   1895  C  C   . TYR A 1 257 ? 71.527 8.849  94.055  1.00 130.53 ? 321 TYR A C   1 
ATOM   1896  O  O   . TYR A 1 257 ? 70.463 9.254  93.572  1.00 109.02 ? 321 TYR A O   1 
ATOM   1897  C  CB  . TYR A 1 257 ? 71.401 6.885  95.601  1.00 108.17 ? 321 TYR A CB  1 
ATOM   1898  C  CG  . TYR A 1 257 ? 69.986 6.433  95.351  1.00 102.30 ? 321 TYR A CG  1 
ATOM   1899  C  CD1 . TYR A 1 257 ? 69.530 6.166  94.055  1.00 97.56  ? 321 TYR A CD1 1 
ATOM   1900  C  CD2 . TYR A 1 257 ? 69.107 6.252  96.413  1.00 97.87  ? 321 TYR A CD2 1 
ATOM   1901  C  CE1 . TYR A 1 257 ? 68.229 5.735  93.830  1.00 100.23 ? 321 TYR A CE1 1 
ATOM   1902  C  CE2 . TYR A 1 257 ? 67.807 5.815  96.203  1.00 100.94 ? 321 TYR A CE2 1 
ATOM   1903  C  CZ  . TYR A 1 257 ? 67.374 5.556  94.915  1.00 97.87  ? 321 TYR A CZ  1 
ATOM   1904  O  OH  . TYR A 1 257 ? 66.080 5.117  94.731  1.00 90.15  ? 321 TYR A OH  1 
ATOM   1905  N  N   . CYS A 1 258 ? 72.657 8.751  93.355  1.00 122.11 ? 322 CYS A N   1 
ATOM   1906  C  CA  . CYS A 1 258 ? 72.790 9.351  92.032  1.00 107.08 ? 322 CYS A CA  1 
ATOM   1907  C  C   . CYS A 1 258 ? 72.267 8.473  90.903  1.00 114.69 ? 322 CYS A C   1 
ATOM   1908  O  O   . CYS A 1 258 ? 72.399 8.802  89.718  1.00 109.50 ? 322 CYS A O   1 
ATOM   1909  C  CB  . CYS A 1 258 ? 74.226 9.825  91.801  1.00 112.41 ? 322 CYS A CB  1 
ATOM   1910  S  SG  . CYS A 1 258 ? 74.679 11.200 92.906  1.00 187.31 ? 322 CYS A SG  1 
ATOM   1911  N  N   . ASP A 1 259 ? 71.649 7.363  91.289  1.00 132.27 ? 323 ASP A N   1 
ATOM   1912  C  CA  . ASP A 1 259 ? 70.962 6.495  90.347  1.00 130.54 ? 323 ASP A CA  1 
ATOM   1913  C  C   . ASP A 1 259 ? 69.527 7.025  90.121  1.00 85.41  ? 323 ASP A C   1 
ATOM   1914  O  O   . ASP A 1 259 ? 69.102 8.015  90.727  1.00 75.99  ? 323 ASP A O   1 
ATOM   1915  C  CB  . ASP A 1 259 ? 70.985 5.039  90.871  1.00 134.07 ? 323 ASP A CB  1 
ATOM   1916  C  CG  . ASP A 1 259 ? 70.905 3.993  89.760  1.00 125.76 ? 323 ASP A CG  1 
ATOM   1917  O  OD1 . ASP A 1 259 ? 71.452 4.214  88.661  1.00 115.11 ? 323 ASP A OD1 1 
ATOM   1918  O  OD2 . ASP A 1 259 ? 70.295 2.931  89.997  1.00 153.62 ? 323 ASP A OD2 1 
ATOM   1919  N  N   . LYS A 1 260 ? 68.801 6.353  89.240  1.00 65.62  ? 324 LYS A N   1 
ATOM   1920  C  CA  . LYS A 1 260 ? 67.409 6.647  88.935  1.00 71.22  ? 324 LYS A CA  1 
ATOM   1921  C  C   . LYS A 1 260 ? 66.393 5.733  89.689  1.00 83.92  ? 324 LYS A C   1 
ATOM   1922  O  O   . LYS A 1 260 ? 66.541 4.502  89.730  1.00 77.28  ? 324 LYS A O   1 
ATOM   1923  C  CB  . LYS A 1 260 ? 67.272 6.548  87.412  1.00 62.29  ? 324 LYS A CB  1 
ATOM   1924  C  CG  . LYS A 1 260 ? 65.947 6.123  86.855  1.00 69.42  ? 324 LYS A CG  1 
ATOM   1925  C  CD  . LYS A 1 260 ? 66.131 5.406  85.524  1.00 93.15  ? 324 LYS A CD  1 
ATOM   1926  C  CE  . LYS A 1 260 ? 67.226 6.034  84.693  1.00 90.07  ? 324 LYS A CE  1 
ATOM   1927  N  NZ  . LYS A 1 260 ? 67.429 5.239  83.461  1.00 89.07  ? 324 LYS A NZ  1 
ATOM   1928  N  N   . THR A 1 261 ? 65.362 6.339  90.275  1.00 76.36  ? 325 THR A N   1 
ATOM   1929  C  CA  . THR A 1 261 ? 64.364 5.596  91.065  1.00 71.32  ? 325 THR A CA  1 
ATOM   1930  C  C   . THR A 1 261 ? 63.297 4.888  90.238  1.00 67.47  ? 325 THR A C   1 
ATOM   1931  O  O   . THR A 1 261 ? 62.328 5.499  89.824  1.00 78.27  ? 325 THR A O   1 
ATOM   1932  C  CB  . THR A 1 261 ? 63.640 6.535  92.026  1.00 64.83  ? 325 THR A CB  1 
ATOM   1933  O  OG1 . THR A 1 261 ? 64.599 7.167  92.876  1.00 78.88  ? 325 THR A OG1 1 
ATOM   1934  C  CG2 . THR A 1 261 ? 62.617 5.767  92.872  1.00 66.55  ? 325 THR A CG2 1 
ATOM   1935  N  N   . THR A 1 262 ? 63.437 3.589  90.041  1.00 77.45  ? 326 THR A N   1 
ATOM   1936  C  CA  . THR A 1 262 ? 62.582 2.903  89.068  1.00 83.45  ? 326 THR A CA  1 
ATOM   1937  C  C   . THR A 1 262 ? 61.214 2.529  89.621  1.00 78.62  ? 326 THR A C   1 
ATOM   1938  O  O   . THR A 1 262 ? 60.359 2.082  88.869  1.00 85.52  ? 326 THR A O   1 
ATOM   1939  C  CB  . THR A 1 262 ? 63.237 1.629  88.514  1.00 84.07  ? 326 THR A CB  1 
ATOM   1940  O  OG1 . THR A 1 262 ? 63.064 0.573  89.468  1.00 150.53 ? 326 THR A OG1 1 
ATOM   1941  C  CG2 . THR A 1 262 ? 64.729 1.838  88.267  1.00 77.58  ? 326 THR A CG2 1 
ATOM   1942  N  N   . THR A 1 263 ? 61.013 2.697  90.924  1.00 79.40  ? 327 THR A N   1 
ATOM   1943  C  CA  . THR A 1 263 ? 59.780 2.251  91.561  1.00 77.18  ? 327 THR A CA  1 
ATOM   1944  C  C   . THR A 1 263 ? 58.695 3.279  91.358  1.00 73.07  ? 327 THR A C   1 
ATOM   1945  O  O   . THR A 1 263 ? 58.866 4.437  91.725  1.00 75.36  ? 327 THR A O   1 
ATOM   1946  C  CB  . THR A 1 263 ? 59.952 2.036  93.063  1.00 80.10  ? 327 THR A CB  1 
ATOM   1947  O  OG1 . THR A 1 263 ? 61.250 1.494  93.323  1.00 88.47  ? 327 THR A OG1 1 
ATOM   1948  C  CG2 . THR A 1 263 ? 58.877 1.086  93.585  1.00 77.42  ? 327 THR A CG2 1 
ATOM   1949  N  N   . GLU A 1 264 ? 57.571 2.822  90.811  1.00 71.05  ? 328 GLU A N   1 
ATOM   1950  C  CA  . GLU A 1 264 ? 56.480 3.677  90.345  1.00 72.32  ? 328 GLU A CA  1 
ATOM   1951  C  C   . GLU A 1 264 ? 56.968 4.731  89.327  1.00 85.61  ? 328 GLU A C   1 
ATOM   1952  O  O   . GLU A 1 264 ? 56.391 5.811  89.169  1.00 113.51 ? 328 GLU A O   1 
ATOM   1953  C  CB  . GLU A 1 264 ? 55.731 4.310  91.520  1.00 60.45  ? 328 GLU A CB  1 
ATOM   1954  C  CG  . GLU A 1 264 ? 54.724 3.396  92.189  1.00 73.83  ? 328 GLU A CG  1 
ATOM   1955  C  CD  . GLU A 1 264 ? 53.420 4.127  92.539  1.00 108.54 ? 328 GLU A CD  1 
ATOM   1956  O  OE1 . GLU A 1 264 ? 52.669 4.492  91.601  1.00 113.94 ? 328 GLU A OE1 1 
ATOM   1957  O  OE2 . GLU A 1 264 ? 53.141 4.338  93.746  1.00 105.90 ? 328 GLU A OE2 1 
ATOM   1958  N  N   . GLY A 1 265 ? 58.034 4.408  88.619  1.00 79.02  ? 329 GLY A N   1 
ATOM   1959  C  CA  . GLY A 1 265 ? 58.624 5.369  87.704  1.00 71.05  ? 329 GLY A CA  1 
ATOM   1960  C  C   . GLY A 1 265 ? 57.769 5.611  86.493  1.00 68.75  ? 329 GLY A C   1 
ATOM   1961  O  O   . GLY A 1 265 ? 58.003 6.570  85.771  1.00 96.41  ? 329 GLY A O   1 
ATOM   1962  N  N   . GLU A 1 266 ? 56.781 4.744  86.273  1.00 68.37  ? 330 GLU A N   1 
ATOM   1963  C  CA  . GLU A 1 266 ? 55.952 4.811  85.076  1.00 81.92  ? 330 GLU A CA  1 
ATOM   1964  C  C   . GLU A 1 266 ? 54.760 5.743  85.254  1.00 84.46  ? 330 GLU A C   1 
ATOM   1965  O  O   . GLU A 1 266 ? 54.150 5.780  86.324  1.00 78.92  ? 330 GLU A O   1 
ATOM   1966  C  CB  . GLU A 1 266 ? 55.480 3.428  84.624  1.00 82.92  ? 330 GLU A CB  1 
ATOM   1967  C  CG  . GLU A 1 266 ? 54.787 3.496  83.271  1.00 143.28 ? 330 GLU A CG  1 
ATOM   1968  C  CD  . GLU A 1 266 ? 54.633 2.156  82.604  1.00 192.43 ? 330 GLU A CD  1 
ATOM   1969  O  OE1 . GLU A 1 266 ? 55.066 1.146  83.194  1.00 194.35 ? 330 GLU A OE1 1 
ATOM   1970  O  OE2 . GLU A 1 266 ? 54.079 2.116  81.484  1.00 263.44 ? 330 GLU A OE2 1 
ATOM   1971  N  N   . GLY A 1 267 ? 54.422 6.455  84.175  1.00 71.83  ? 331 GLY A N   1 
ATOM   1972  C  CA  . GLY A 1 267 ? 53.500 7.577  84.230  1.00 72.69  ? 331 GLY A CA  1 
ATOM   1973  C  C   . GLY A 1 267 ? 54.294 8.822  84.611  1.00 86.61  ? 331 GLY A C   1 
ATOM   1974  O  O   . GLY A 1 267 ? 55.504 8.771  84.906  1.00 75.41  ? 331 GLY A O   1 
ATOM   1975  N  N   . GLY A 1 268 ? 53.620 9.956  84.623  1.00 72.98  ? 332 GLY A N   1 
ATOM   1976  C  CA  . GLY A 1 268 ? 54.311 11.189 84.904  1.00 63.02  ? 332 GLY A CA  1 
ATOM   1977  C  C   . GLY A 1 268 ? 53.495 12.398 84.498  1.00 72.68  ? 332 GLY A C   1 
ATOM   1978  O  O   . GLY A 1 268 ? 52.521 12.296 83.742  1.00 80.26  ? 332 GLY A O   1 
ATOM   1979  N  N   . ILE A 1 269 ? 53.880 13.551 85.029  1.00 48.47  ? 333 ILE A N   1 
ATOM   1980  C  CA  . ILE A 1 269 ? 53.298 14.773 84.575  1.00 55.09  ? 333 ILE A CA  1 
ATOM   1981  C  C   . ILE A 1 269 ? 54.374 15.852 84.590  1.00 55.95  ? 333 ILE A C   1 
ATOM   1982  O  O   . ILE A 1 269 ? 55.297 15.744 85.380  1.00 41.50  ? 333 ILE A O   1 
ATOM   1983  C  CB  . ILE A 1 269 ? 52.162 15.139 85.454  1.00 54.64  ? 333 ILE A CB  1 
ATOM   1984  C  CG1 . ILE A 1 269 ? 51.274 16.210 84.774  1.00 74.63  ? 333 ILE A CG1 1 
ATOM   1985  C  CG2 . ILE A 1 269 ? 52.734 15.501 86.766  1.00 37.69  ? 333 ILE A CG2 1 
ATOM   1986  C  CD1 . ILE A 1 269 ? 49.851 16.347 85.347  1.00 73.16  ? 333 ILE A CD1 1 
ATOM   1987  N  N   . GLN A 1 270 ? 54.238 16.858 83.707  1.00 46.91  ? 334 GLN A N   1 
ATOM   1988  C  CA  . GLN A 1 270 ? 55.220 17.921 83.504  1.00 42.09  ? 334 GLN A CA  1 
ATOM   1989  C  C   . GLN A 1 270 ? 55.469 18.713 84.757  1.00 50.35  ? 334 GLN A C   1 
ATOM   1990  O  O   . GLN A 1 270 ? 54.516 19.127 85.458  1.00 64.36  ? 334 GLN A O   1 
ATOM   1991  C  CB  . GLN A 1 270 ? 54.714 18.882 82.435  1.00 55.09  ? 334 GLN A CB  1 
ATOM   1992  C  CG  . GLN A 1 270 ? 55.724 19.953 82.041  1.00 59.90  ? 334 GLN A CG  1 
ATOM   1993  C  CD  . GLN A 1 270 ? 55.251 20.780 80.867  1.00 63.52  ? 334 GLN A CD  1 
ATOM   1994  O  OE1 . GLN A 1 270 ? 54.067 20.752 80.505  1.00 52.30  ? 334 GLN A OE1 1 
ATOM   1995  N  NE2 . GLN A 1 270 ? 56.176 21.527 80.262  1.00 66.88  ? 334 GLN A NE2 1 
ATOM   1996  N  N   . GLY A 1 271 ? 56.743 18.946 85.042  1.00 45.08  ? 335 GLY A N   1 
ATOM   1997  C  CA  . GLY A 1 271 ? 57.118 19.714 86.246  1.00 47.18  ? 335 GLY A CA  1 
ATOM   1998  C  C   . GLY A 1 271 ? 58.571 20.123 86.200  1.00 53.36  ? 335 GLY A C   1 
ATOM   1999  O  O   . GLY A 1 271 ? 59.305 19.736 85.281  1.00 65.80  ? 335 GLY A O   1 
ATOM   2000  N  N   . PHE A 1 272 ? 58.999 20.891 87.191  1.00 57.47  ? 336 PHE A N   1 
ATOM   2001  C  CA  . PHE A 1 272 ? 60.340 21.483 87.135  1.00 54.23  ? 336 PHE A CA  1 
ATOM   2002  C  C   . PHE A 1 272 ? 61.237 21.218 88.333  1.00 56.72  ? 336 PHE A C   1 
ATOM   2003  O  O   . PHE A 1 272 ? 60.818 20.634 89.345  1.00 85.25  ? 336 PHE A O   1 
ATOM   2004  C  CB  . PHE A 1 272 ? 60.227 22.986 86.950  1.00 62.25  ? 336 PHE A CB  1 
ATOM   2005  C  CG  . PHE A 1 272 ? 59.471 23.656 88.035  1.00 56.04  ? 336 PHE A CG  1 
ATOM   2006  C  CD1 . PHE A 1 272 ? 60.139 24.316 89.051  1.00 42.95  ? 336 PHE A CD1 1 
ATOM   2007  C  CD2 . PHE A 1 272 ? 58.076 23.612 88.055  1.00 64.43  ? 336 PHE A CD2 1 
ATOM   2008  C  CE1 . PHE A 1 272 ? 59.423 24.939 90.052  1.00 45.77  ? 336 PHE A CE1 1 
ATOM   2009  C  CE2 . PHE A 1 272 ? 57.360 24.230 89.080  1.00 50.98  ? 336 PHE A CE2 1 
ATOM   2010  C  CZ  . PHE A 1 272 ? 58.026 24.891 90.066  1.00 35.41  ? 336 PHE A CZ  1 
ATOM   2011  N  N   . MET A 1 273 ? 62.488 21.627 88.159  1.00 43.75  ? 337 MET A N   1 
ATOM   2012  C  CA  . MET A 1 273 ? 63.484 21.736 89.221  1.00 48.85  ? 337 MET A CA  1 
ATOM   2013  C  C   . MET A 1 273 ? 64.339 22.934 88.859  1.00 55.31  ? 337 MET A C   1 
ATOM   2014  O  O   . MET A 1 273 ? 64.499 23.264 87.691  1.00 89.02  ? 337 MET A O   1 
ATOM   2015  C  CB  . MET A 1 273 ? 64.384 20.509 89.302  1.00 49.69  ? 337 MET A CB  1 
ATOM   2016  C  CG  . MET A 1 273 ? 63.676 19.234 89.744  1.00 68.89  ? 337 MET A CG  1 
ATOM   2017  S  SD  . MET A 1 273 ? 64.677 17.726 89.771  1.00 71.10  ? 337 MET A SD  1 
ATOM   2018  C  CE  . MET A 1 273 ? 65.516 17.760 88.191  1.00 56.90  ? 337 MET A CE  1 
ATOM   2019  N  N   . ILE A 1 274 ? 64.899 23.576 89.858  1.00 44.59  ? 338 ILE A N   1 
ATOM   2020  C  CA  . ILE A 1 274 ? 65.705 24.735 89.622  1.00 44.59  ? 338 ILE A CA  1 
ATOM   2021  C  C   . ILE A 1 274 ? 67.079 24.438 90.195  1.00 46.20  ? 338 ILE A C   1 
ATOM   2022  O  O   . ILE A 1 274 ? 67.206 23.973 91.308  1.00 56.15  ? 338 ILE A O   1 
ATOM   2023  C  CB  . ILE A 1 274 ? 65.076 25.970 90.294  1.00 37.68  ? 338 ILE A CB  1 
ATOM   2024  C  CG1 . ILE A 1 274 ? 63.600 26.068 89.920  1.00 42.19  ? 338 ILE A CG1 1 
ATOM   2025  C  CG2 . ILE A 1 274 ? 65.768 27.209 89.842  1.00 31.05  ? 338 ILE A CG2 1 
ATOM   2026  C  CD1 . ILE A 1 274 ? 63.013 27.463 90.170  1.00 49.98  ? 338 ILE A CD1 1 
ATOM   2027  N  N   . GLU A 1 275 ? 68.111 24.671 89.418  1.00 50.58  ? 339 GLU A N   1 
ATOM   2028  C  CA  . GLU A 1 275 ? 69.462 24.528 89.924  1.00 62.12  ? 339 GLU A CA  1 
ATOM   2029  C  C   . GLU A 1 275 ? 70.094 25.930 90.076  1.00 60.52  ? 339 GLU A C   1 
ATOM   2030  O  O   . GLU A 1 275 ? 70.017 26.758 89.166  1.00 69.36  ? 339 GLU A O   1 
ATOM   2031  C  CB  . GLU A 1 275 ? 70.250 23.581 88.999  1.00 62.98  ? 339 GLU A CB  1 
ATOM   2032  C  CG  . GLU A 1 275 ? 71.764 23.626 89.097  1.00 91.67  ? 339 GLU A CG  1 
ATOM   2033  C  CD  . GLU A 1 275 ? 72.328 22.891 90.310  1.00 104.73 ? 339 GLU A CD  1 
ATOM   2034  O  OE1 . GLU A 1 275 ? 71.589 22.099 90.940  1.00 74.58  ? 339 GLU A OE1 1 
ATOM   2035  O  OE2 . GLU A 1 275 ? 73.524 23.106 90.628  1.00 113.76 ? 339 GLU A OE2 1 
ATOM   2036  N  N   . GLY A 1 276 ? 70.687 26.198 91.235  1.00 60.47  ? 340 GLY A N   1 
ATOM   2037  C  CA  . GLY A 1 276 ? 71.329 27.489 91.496  1.00 81.51  ? 340 GLY A CA  1 
ATOM   2038  C  C   . GLY A 1 276 ? 72.167 27.453 92.761  1.00 99.31  ? 340 GLY A C   1 
ATOM   2039  O  O   . GLY A 1 276 ? 72.598 26.371 93.202  1.00 93.97  ? 340 GLY A O   1 
ATOM   2040  N  N   . SER A 1 277 ? 72.407 28.637 93.329  1.00 82.83  ? 341 SER A N   1 
ATOM   2041  C  CA  . SER A 1 277 ? 73.007 28.770 94.658  1.00 90.25  ? 341 SER A CA  1 
ATOM   2042  C  C   . SER A 1 277 ? 72.121 28.029 95.665  1.00 82.84  ? 341 SER A C   1 
ATOM   2043  O  O   . SER A 1 277 ? 72.540 27.050 96.305  1.00 91.71  ? 341 SER A O   1 
ATOM   2044  C  CB  . SER A 1 277 ? 73.133 30.248 95.060  1.00 100.34 ? 341 SER A CB  1 
ATOM   2045  O  OG  . SER A 1 277 ? 74.165 30.897 94.344  1.00 100.81 ? 341 SER A OG  1 
ATOM   2046  N  N   . ASN A 1 278 ? 70.904 28.541 95.817  1.00 64.13  ? 342 ASN A N   1 
ATOM   2047  C  CA  . ASN A 1 278 ? 69.794 27.775 96.339  1.00 60.27  ? 342 ASN A CA  1 
ATOM   2048  C  C   . ASN A 1 278 ? 69.225 26.940 95.203  1.00 59.79  ? 342 ASN A C   1 
ATOM   2049  O  O   . ASN A 1 278 ? 69.208 27.383 94.055  1.00 69.32  ? 342 ASN A O   1 
ATOM   2050  C  CB  . ASN A 1 278 ? 68.691 28.698 96.822  1.00 61.12  ? 342 ASN A CB  1 
ATOM   2051  C  CG  . ASN A 1 278 ? 69.046 29.408 98.071  1.00 69.82  ? 342 ASN A CG  1 
ATOM   2052  O  OD1 . ASN A 1 278 ? 69.522 28.801 99.034  1.00 81.77  ? 342 ASN A OD1 1 
ATOM   2053  N  ND2 . ASN A 1 278 ? 68.800 30.711 98.089  1.00 89.20  ? 342 ASN A ND2 1 
ATOM   2054  N  N   . SER A 1 279 ? 68.758 25.742 95.524  1.00 56.33  ? 343 SER A N   1 
ATOM   2055  C  CA  . SER A 1 279 ? 68.091 24.875 94.548  1.00 65.65  ? 343 SER A CA  1 
ATOM   2056  C  C   . SER A 1 279 ? 66.652 24.568 94.979  1.00 44.28  ? 343 SER A C   1 
ATOM   2057  O  O   . SER A 1 279 ? 66.344 24.559 96.141  1.00 53.18  ? 343 SER A O   1 
ATOM   2058  C  CB  . SER A 1 279 ? 68.919 23.589 94.269  1.00 62.19  ? 343 SER A CB  1 
ATOM   2059  O  OG  . SER A 1 279 ? 70.150 23.897 93.599  1.00 56.73  ? 343 SER A OG  1 
ATOM   2060  N  N   . TRP A 1 280 ? 65.767 24.334 94.027  1.00 53.36  ? 344 TRP A N   1 
ATOM   2061  C  CA  . TRP A 1 280 ? 64.360 24.069 94.330  1.00 51.99  ? 344 TRP A CA  1 
ATOM   2062  C  C   . TRP A 1 280 ? 63.837 22.848 93.651  1.00 55.47  ? 344 TRP A C   1 
ATOM   2063  O  O   . TRP A 1 280 ? 64.174 22.590 92.494  1.00 67.98  ? 344 TRP A O   1 
ATOM   2064  C  CB  . TRP A 1 280 ? 63.502 25.250 93.928  1.00 40.94  ? 344 TRP A CB  1 
ATOM   2065  C  CG  . TRP A 1 280 ? 63.878 26.510 94.664  1.00 36.22  ? 344 TRP A CG  1 
ATOM   2066  C  CD1 . TRP A 1 280 ? 64.888 27.409 94.342  1.00 42.52  ? 344 TRP A CD1 1 
ATOM   2067  C  CD2 . TRP A 1 280 ? 63.256 27.051 95.855  1.00 36.23  ? 344 TRP A CD2 1 
ATOM   2068  N  NE1 . TRP A 1 280 ? 64.932 28.453 95.219  1.00 38.66  ? 344 TRP A NE1 1 
ATOM   2069  C  CE2 . TRP A 1 280 ? 63.981 28.307 96.160  1.00 44.83  ? 344 TRP A CE2 1 
ATOM   2070  C  CE3 . TRP A 1 280 ? 62.203 26.650 96.679  1.00 38.28  ? 344 TRP A CE3 1 
ATOM   2071  C  CZ2 . TRP A 1 280 ? 63.653 29.109 97.260  1.00 45.04  ? 344 TRP A CZ2 1 
ATOM   2072  C  CZ3 . TRP A 1 280 ? 61.903 27.439 97.790  1.00 44.96  ? 344 TRP A CZ3 1 
ATOM   2073  C  CH2 . TRP A 1 280 ? 62.612 28.646 98.073  1.00 51.32  ? 344 TRP A CH2 1 
ATOM   2074  N  N   . ILE A 1 281 ? 63.020 22.076 94.367  1.00 47.48  ? 345 ILE A N   1 
ATOM   2075  C  CA  . ILE A 1 281 ? 62.152 21.074 93.727  1.00 47.29  ? 345 ILE A CA  1 
ATOM   2076  C  C   . ILE A 1 281 ? 60.704 21.323 94.079  1.00 54.74  ? 345 ILE A C   1 
ATOM   2077  O  O   . ILE A 1 281 ? 60.352 21.400 95.251  1.00 68.23  ? 345 ILE A O   1 
ATOM   2078  C  CB  . ILE A 1 281 ? 62.479 19.658 94.118  1.00 48.03  ? 345 ILE A CB  1 
ATOM   2079  C  CG1 . ILE A 1 281 ? 63.858 19.305 93.593  1.00 54.51  ? 345 ILE A CG1 1 
ATOM   2080  C  CG2 . ILE A 1 281 ? 61.456 18.720 93.510  1.00 36.90  ? 345 ILE A CG2 1 
ATOM   2081  C  CD1 . ILE A 1 281 ? 64.394 18.011 94.099  1.00 70.31  ? 345 ILE A CD1 1 
ATOM   2082  N  N   . GLY A 1 282 ? 59.872 21.470 93.058  1.00 54.71  ? 346 GLY A N   1 
ATOM   2083  C  CA  . GLY A 1 282 ? 58.439 21.633 93.259  1.00 55.17  ? 346 GLY A CA  1 
ATOM   2084  C  C   . GLY A 1 282 ? 57.805 20.291 92.991  1.00 49.51  ? 346 GLY A C   1 
ATOM   2085  O  O   . GLY A 1 282 ? 58.338 19.509 92.192  1.00 45.28  ? 346 GLY A O   1 
ATOM   2086  N  N   . ARG A 1 283 ? 56.697 20.005 93.667  1.00 39.62  ? 347 ARG A N   1 
ATOM   2087  C  CA  . ARG A 1 283 ? 55.978 18.799 93.357  1.00 44.74  ? 347 ARG A CA  1 
ATOM   2088  C  C   . ARG A 1 283 ? 54.543 18.811 93.853  1.00 45.46  ? 347 ARG A C   1 
ATOM   2089  O  O   . ARG A 1 283 ? 54.191 19.612 94.721  1.00 39.99  ? 347 ARG A O   1 
ATOM   2090  C  CB  . ARG A 1 283 ? 56.728 17.597 93.899  1.00 45.43  ? 347 ARG A CB  1 
ATOM   2091  C  CG  . ARG A 1 283 ? 56.469 17.330 95.325  1.00 52.72  ? 347 ARG A CG  1 
ATOM   2092  C  CD  . ARG A 1 283 ? 57.442 16.302 95.796  1.00 65.19  ? 347 ARG A CD  1 
ATOM   2093  N  NE  . ARG A 1 283 ? 57.107 15.791 97.119  1.00 61.63  ? 347 ARG A NE  1 
ATOM   2094  C  CZ  . ARG A 1 283 ? 57.763 14.808 97.709  1.00 63.07  ? 347 ARG A CZ  1 
ATOM   2095  N  NH1 . ARG A 1 283 ? 58.787 14.196 97.104  1.00 80.72  ? 347 ARG A NH1 1 
ATOM   2096  N  NH2 . ARG A 1 283 ? 57.378 14.431 98.901  1.00 65.94  ? 347 ARG A NH2 1 
ATOM   2097  N  N   . ILE A 1 284 ? 53.727 17.921 93.277  1.00 46.14  ? 348 ILE A N   1 
ATOM   2098  C  CA  . ILE A 1 284 ? 52.365 17.701 93.745  1.00 45.40  ? 348 ILE A CA  1 
ATOM   2099  C  C   . ILE A 1 284 ? 52.429 16.958 95.077  1.00 53.25  ? 348 ILE A C   1 
ATOM   2100  O  O   . ILE A 1 284 ? 53.203 16.007 95.245  1.00 74.18  ? 348 ILE A O   1 
ATOM   2101  C  CB  . ILE A 1 284 ? 51.552 16.909 92.726  1.00 44.87  ? 348 ILE A CB  1 
ATOM   2102  C  CG1 . ILE A 1 284 ? 51.695 17.577 91.350  1.00 60.74  ? 348 ILE A CG1 1 
ATOM   2103  C  CG2 . ILE A 1 284 ? 50.092 16.751 93.163  1.00 44.17  ? 348 ILE A CG2 1 
ATOM   2104  C  CD1 . ILE A 1 284 ? 50.541 17.397 90.349  1.00 50.16  ? 348 ILE A CD1 1 
ATOM   2105  N  N   . ILE A 1 285 ? 51.625 17.407 96.029  1.00 54.32  ? 349 ILE A N   1 
ATOM   2106  C  CA  . ILE A 1 285 ? 51.751 16.913 97.390  1.00 64.51  ? 349 ILE A CA  1 
ATOM   2107  C  C   . ILE A 1 285 ? 51.226 15.499 97.572  1.00 57.45  ? 349 ILE A C   1 
ATOM   2108  O  O   . ILE A 1 285 ? 51.935 14.637 98.058  1.00 51.05  ? 349 ILE A O   1 
ATOM   2109  C  CB  . ILE A 1 285 ? 51.112 17.875 98.402  1.00 58.27  ? 349 ILE A CB  1 
ATOM   2110  C  CG1 . ILE A 1 285 ? 51.872 19.220 98.387  1.00 54.02  ? 349 ILE A CG1 1 
ATOM   2111  C  CG2 . ILE A 1 285 ? 51.135 17.234 99.761  1.00 49.56  ? 349 ILE A CG2 1 
ATOM   2112  C  CD1 . ILE A 1 285 ? 51.441 20.226 99.424  1.00 49.42  ? 349 ILE A CD1 1 
ATOM   2113  N  N   . ASN A 1 286 ? 49.989 15.279 97.159  1.00 64.41  ? 350 ASN A N   1 
ATOM   2114  C  CA  . ASN A 1 286 ? 49.311 14.021 97.362  1.00 72.11  ? 350 ASN A CA  1 
ATOM   2115  C  C   . ASN A 1 286 ? 49.061 13.317 96.043  1.00 72.95  ? 350 ASN A C   1 
ATOM   2116  O  O   . ASN A 1 286 ? 47.999 13.493 95.448  1.00 87.88  ? 350 ASN A O   1 
ATOM   2117  C  CB  . ASN A 1 286 ? 47.988 14.248 98.088  1.00 79.83  ? 350 ASN A CB  1 
ATOM   2118  C  CG  . ASN A 1 286 ? 48.183 14.710 99.493  1.00 91.41  ? 350 ASN A CG  1 
ATOM   2119  O  OD1 . ASN A 1 286 ? 48.314 15.901 99.752  1.00 98.60  ? 350 ASN A OD1 1 
ATOM   2120  N  ND2 . ASN A 1 286 ? 48.210 13.768 100.422 1.00 120.66 ? 350 ASN A ND2 1 
ATOM   2121  N  N   . PRO A 1 287 ? 50.015 12.476 95.607  1.00 69.74  ? 351 PRO A N   1 
ATOM   2122  C  CA  . PRO A 1 287 ? 49.999 11.870 94.271  1.00 77.40  ? 351 PRO A CA  1 
ATOM   2123  C  C   . PRO A 1 287 ? 48.748 11.029 93.979  1.00 78.97  ? 351 PRO A C   1 
ATOM   2124  O  O   . PRO A 1 287 ? 48.380 10.857 92.810  1.00 70.39  ? 351 PRO A O   1 
ATOM   2125  C  CB  . PRO A 1 287 ? 51.249 10.986 94.275  1.00 66.05  ? 351 PRO A CB  1 
ATOM   2126  C  CG  . PRO A 1 287 ? 52.075 11.524 95.368  1.00 68.40  ? 351 PRO A CG  1 
ATOM   2127  C  CD  . PRO A 1 287 ? 51.105 11.918 96.419  1.00 63.23  ? 351 PRO A CD  1 
ATOM   2128  N  N   . GLY A 1 288 ? 48.109 10.515 95.028  1.00 69.30  ? 352 GLY A N   1 
ATOM   2129  C  CA  . GLY A 1 288 ? 46.826 9.854  94.875  1.00 74.25  ? 352 GLY A CA  1 
ATOM   2130  C  C   . GLY A 1 288 ? 45.769 10.808 94.349  1.00 77.64  ? 352 GLY A C   1 
ATOM   2131  O  O   . GLY A 1 288 ? 45.280 10.652 93.231  1.00 99.07  ? 352 GLY A O   1 
ATOM   2132  N  N   . SER A 1 289 ? 45.434 11.810 95.154  1.00 77.40  ? 353 SER A N   1 
ATOM   2133  C  CA  . SER A 1 289 ? 44.333 12.723 94.841  1.00 90.50  ? 353 SER A CA  1 
ATOM   2134  C  C   . SER A 1 289 ? 44.728 13.884 93.937  1.00 74.89  ? 353 SER A C   1 
ATOM   2135  O  O   . SER A 1 289 ? 43.874 14.646 93.489  1.00 78.72  ? 353 SER A O   1 
ATOM   2136  C  CB  . SER A 1 289 ? 43.694 13.251 96.133  1.00 118.98 ? 353 SER A CB  1 
ATOM   2137  O  OG  . SER A 1 289 ? 44.675 13.541 97.114  1.00 120.67 ? 353 SER A OG  1 
ATOM   2138  N  N   . LYS A 1 290 ? 46.025 14.009 93.679  1.00 78.14  ? 354 LYS A N   1 
ATOM   2139  C  CA  . LYS A 1 290 ? 46.595 15.119 92.901  1.00 73.11  ? 354 LYS A CA  1 
ATOM   2140  C  C   . LYS A 1 290 ? 46.401 16.485 93.577  1.00 67.12  ? 354 LYS A C   1 
ATOM   2141  O  O   . LYS A 1 290 ? 46.443 17.524 92.925  1.00 66.82  ? 354 LYS A O   1 
ATOM   2142  C  CB  . LYS A 1 290 ? 46.028 15.120 91.481  1.00 89.39  ? 354 LYS A CB  1 
ATOM   2143  C  CG  . LYS A 1 290 ? 46.297 13.851 90.705  1.00 88.48  ? 354 LYS A CG  1 
ATOM   2144  C  CD  . LYS A 1 290 ? 47.745 13.794 90.262  1.00 91.15  ? 354 LYS A CD  1 
ATOM   2145  C  CE  . LYS A 1 290 ? 48.051 12.463 89.602  1.00 113.85 ? 354 LYS A CE  1 
ATOM   2146  N  NZ  . LYS A 1 290 ? 47.321 12.304 88.318  1.00 113.79 ? 354 LYS A NZ  1 
ATOM   2147  N  N   . LYS A 1 291 ? 46.200 16.464 94.891  1.00 66.64  ? 355 LYS A N   1 
ATOM   2148  C  CA  . LYS A 1 291 ? 45.912 17.654 95.671  1.00 68.71  ? 355 LYS A CA  1 
ATOM   2149  C  C   . LYS A 1 291 ? 47.181 18.300 96.199  1.00 62.51  ? 355 LYS A C   1 
ATOM   2150  O  O   . LYS A 1 291 ? 48.078 17.625 96.688  1.00 64.97  ? 355 LYS A O   1 
ATOM   2151  C  CB  . LYS A 1 291 ? 44.996 17.292 96.846  1.00 88.57  ? 355 LYS A CB  1 
ATOM   2152  C  CG  . LYS A 1 291 ? 43.521 17.119 96.491  1.00 112.38 ? 355 LYS A CG  1 
ATOM   2153  C  CD  . LYS A 1 291 ? 42.672 18.277 97.032  1.00 122.52 ? 355 LYS A CD  1 
ATOM   2154  C  CE  . LYS A 1 291 ? 41.183 17.961 96.968  1.00 110.99 ? 355 LYS A CE  1 
ATOM   2155  N  NZ  . LYS A 1 291 ? 40.862 16.665 97.632  1.00 123.81 ? 355 LYS A NZ  1 
ATOM   2156  N  N   . GLY A 1 292 ? 47.245 19.621 96.116  1.00 66.29  ? 356 GLY A N   1 
ATOM   2157  C  CA  . GLY A 1 292 ? 48.329 20.373 96.747  1.00 59.68  ? 356 GLY A CA  1 
ATOM   2158  C  C   . GLY A 1 292 ? 49.627 20.454 95.964  1.00 59.60  ? 356 GLY A C   1 
ATOM   2159  O  O   . GLY A 1 292 ? 50.012 19.532 95.234  1.00 59.75  ? 356 GLY A O   1 
ATOM   2160  N  N   . PHE A 1 293 ? 50.299 21.585 96.112  1.00 52.37  ? 357 PHE A N   1 
ATOM   2161  C  CA  . PHE A 1 293 ? 51.583 21.779 95.474  1.00 54.09  ? 357 PHE A CA  1 
ATOM   2162  C  C   . PHE A 1 293 ? 52.569 22.350 96.491  1.00 66.62  ? 357 PHE A C   1 
ATOM   2163  O  O   . PHE A 1 293 ? 52.287 23.377 97.150  1.00 59.31  ? 357 PHE A O   1 
ATOM   2164  C  CB  . PHE A 1 293 ? 51.443 22.714 94.284  1.00 44.67  ? 357 PHE A CB  1 
ATOM   2165  C  CG  . PHE A 1 293 ? 52.706 22.885 93.506  1.00 45.79  ? 357 PHE A CG  1 
ATOM   2166  C  CD1 . PHE A 1 293 ? 53.620 23.874 93.840  1.00 50.31  ? 357 PHE A CD1 1 
ATOM   2167  C  CD2 . PHE A 1 293 ? 53.002 22.045 92.451  1.00 58.46  ? 357 PHE A CD2 1 
ATOM   2168  C  CE1 . PHE A 1 293 ? 54.816 24.043 93.118  1.00 51.74  ? 357 PHE A CE1 1 
ATOM   2169  C  CE2 . PHE A 1 293 ? 54.203 22.198 91.726  1.00 64.78  ? 357 PHE A CE2 1 
ATOM   2170  C  CZ  . PHE A 1 293 ? 55.110 23.209 92.059  1.00 45.45  ? 357 PHE A CZ  1 
ATOM   2171  N  N   . GLU A 1 294 ? 53.711 21.670 96.620  1.00 55.93  ? 358 GLU A N   1 
ATOM   2172  C  CA  . GLU A 1 294 ? 54.782 22.100 97.504  1.00 50.25  ? 358 GLU A CA  1 
ATOM   2173  C  C   . GLU A 1 294 ? 56.087 22.331 96.731  1.00 47.54  ? 358 GLU A C   1 
ATOM   2174  O  O   . GLU A 1 294 ? 56.388 21.617 95.759  1.00 51.28  ? 358 GLU A O   1 
ATOM   2175  C  CB  . GLU A 1 294 ? 54.978 21.085 98.635  1.00 70.28  ? 358 GLU A CB  1 
ATOM   2176  C  CG  . GLU A 1 294 ? 55.534 19.696 98.244  1.00 80.25  ? 358 GLU A CG  1 
ATOM   2177  C  CD  . GLU A 1 294 ? 55.589 18.702 99.423  1.00 105.85 ? 358 GLU A CD  1 
ATOM   2178  O  OE1 . GLU A 1 294 ? 55.665 19.154 100.591 1.00 111.80 ? 358 GLU A OE1 1 
ATOM   2179  O  OE2 . GLU A 1 294 ? 55.558 17.466 99.184  1.00 101.81 ? 358 GLU A OE2 1 
ATOM   2180  N  N   . ILE A 1 295 ? 56.842 23.341 97.159  1.00 36.88  ? 359 ILE A N   1 
ATOM   2181  C  CA  . ILE A 1 295 ? 58.171 23.615 96.626  1.00 38.37  ? 359 ILE A CA  1 
ATOM   2182  C  C   . ILE A 1 295 ? 59.177 23.701 97.764  1.00 43.00  ? 359 ILE A C   1 
ATOM   2183  O  O   . ILE A 1 295 ? 58.882 24.213 98.837  1.00 49.73  ? 359 ILE A O   1 
ATOM   2184  C  CB  . ILE A 1 295 ? 58.232 24.908 95.867  1.00 37.64  ? 359 ILE A CB  1 
ATOM   2185  C  CG1 . ILE A 1 295 ? 59.559 25.002 95.111  1.00 43.65  ? 359 ILE A CG1 1 
ATOM   2186  C  CG2 . ILE A 1 295 ? 58.180 26.060 96.822  1.00 35.47  ? 359 ILE A CG2 1 
ATOM   2187  C  CD1 . ILE A 1 295 ? 59.564 26.109 94.080  1.00 55.11  ? 359 ILE A CD1 1 
ATOM   2188  N  N   . TYR A 1 296 ? 60.386 23.230 97.507  1.00 48.98  ? 360 TYR A N   1 
ATOM   2189  C  CA  . TYR A 1 296 ? 61.246 22.784 98.577  1.00 54.84  ? 360 TYR A CA  1 
ATOM   2190  C  C   . TYR A 1 296 ? 62.664 23.202 98.261  1.00 55.56  ? 360 TYR A C   1 
ATOM   2191  O  O   . TYR A 1 296 ? 63.165 22.945 97.174  1.00 62.66  ? 360 TYR A O   1 
ATOM   2192  C  CB  . TYR A 1 296 ? 61.087 21.259 98.737  1.00 55.89  ? 360 TYR A CB  1 
ATOM   2193  C  CG  . TYR A 1 296 ? 61.808 20.661 99.897  1.00 63.11  ? 360 TYR A CG  1 
ATOM   2194  C  CD1 . TYR A 1 296 ? 61.326 20.791 101.173 1.00 80.01  ? 360 TYR A CD1 1 
ATOM   2195  C  CD2 . TYR A 1 296 ? 62.966 19.949 99.711  1.00 84.09  ? 360 TYR A CD2 1 
ATOM   2196  C  CE1 . TYR A 1 296 ? 61.996 20.250 102.256 1.00 98.04  ? 360 TYR A CE1 1 
ATOM   2197  C  CE2 . TYR A 1 296 ? 63.641 19.391 100.777 1.00 121.21 ? 360 TYR A CE2 1 
ATOM   2198  C  CZ  . TYR A 1 296 ? 63.149 19.554 102.055 1.00 108.38 ? 360 TYR A CZ  1 
ATOM   2199  O  OH  . TYR A 1 296 ? 63.800 19.020 103.140 1.00 105.93 ? 360 TYR A OH  1 
ATOM   2200  N  N   . LYS A 1 297 ? 63.289 23.876 99.214  1.00 51.49  ? 361 LYS A N   1 
ATOM   2201  C  CA  . LYS A 1 297 ? 64.589 24.489 99.031  1.00 48.62  ? 361 LYS A CA  1 
ATOM   2202  C  C   . LYS A 1 297 ? 65.751 23.553 99.440  1.00 51.30  ? 361 LYS A C   1 
ATOM   2203  O  O   . LYS A 1 297 ? 65.602 22.662 100.264 1.00 61.66  ? 361 LYS A O   1 
ATOM   2204  C  CB  . LYS A 1 297 ? 64.588 25.745 99.872  1.00 55.44  ? 361 LYS A CB  1 
ATOM   2205  C  CG  . LYS A 1 297 ? 65.707 26.735 99.657  1.00 60.40  ? 361 LYS A CG  1 
ATOM   2206  C  CD  . LYS A 1 297 ? 65.369 27.902 100.554 1.00 59.15  ? 361 LYS A CD  1 
ATOM   2207  C  CE  . LYS A 1 297 ? 66.538 28.744 100.883 1.00 64.23  ? 361 LYS A CE  1 
ATOM   2208  N  NZ  . LYS A 1 297 ? 66.050 29.919 101.659 1.00 69.19  ? 361 LYS A NZ  1 
ATOM   2209  N  N   . PHE A 1 298 ? 66.908 23.762 98.847  1.00 48.29  ? 362 PHE A N   1 
ATOM   2210  C  CA  . PHE A 1 298 ? 68.094 22.992 99.150  1.00 50.45  ? 362 PHE A CA  1 
ATOM   2211  C  C   . PHE A 1 298 ? 69.318 23.870 99.037  1.00 63.86  ? 362 PHE A C   1 
ATOM   2212  O  O   . PHE A 1 298 ? 69.446 24.673 98.101  1.00 76.42  ? 362 PHE A O   1 
ATOM   2213  C  CB  . PHE A 1 298 ? 68.258 21.923 98.111  1.00 54.34  ? 362 PHE A CB  1 
ATOM   2214  C  CG  . PHE A 1 298 ? 67.246 20.853 98.184  1.00 57.49  ? 362 PHE A CG  1 
ATOM   2215  C  CD1 . PHE A 1 298 ? 67.472 19.716 98.956  1.00 64.60  ? 362 PHE A CD1 1 
ATOM   2216  C  CD2 . PHE A 1 298 ? 66.090 20.942 97.451  1.00 50.37  ? 362 PHE A CD2 1 
ATOM   2217  C  CE1 . PHE A 1 298 ? 66.535 18.694 99.002  1.00 57.83  ? 362 PHE A CE1 1 
ATOM   2218  C  CE2 . PHE A 1 298 ? 65.161 19.916 97.476  1.00 60.47  ? 362 PHE A CE2 1 
ATOM   2219  C  CZ  . PHE A 1 298 ? 65.383 18.793 98.257  1.00 54.89  ? 362 PHE A CZ  1 
ATOM   2220  N  N   . LEU A 1 299 ? 70.249 23.702 99.960  1.00 63.67  ? 363 LEU A N   1 
ATOM   2221  C  CA  . LEU A 1 299 ? 71.500 24.415 99.831  1.00 74.84  ? 363 LEU A CA  1 
ATOM   2222  C  C   . LEU A 1 299 ? 72.411 23.691 98.841  1.00 88.44  ? 363 LEU A C   1 
ATOM   2223  O  O   . LEU A 1 299 ? 72.590 22.469 98.938  1.00 92.46  ? 363 LEU A O   1 
ATOM   2224  C  CB  . LEU A 1 299 ? 72.161 24.568 101.190 1.00 90.41  ? 363 LEU A CB  1 
ATOM   2225  C  CG  . LEU A 1 299 ? 71.604 25.725 102.026 1.00 93.27  ? 363 LEU A CG  1 
ATOM   2226  C  CD1 . LEU A 1 299 ? 71.447 26.990 101.156 1.00 89.30  ? 363 LEU A CD1 1 
ATOM   2227  C  CD2 . LEU A 1 299 ? 70.290 25.345 102.771 1.00 64.11  ? 363 LEU A CD2 1 
ATOM   2228  N  N   . GLY A 1 300 ? 72.956 24.441 97.876  1.00 78.55  ? 364 GLY A N   1 
ATOM   2229  C  CA  . GLY A 1 300 ? 73.821 23.869 96.849  1.00 78.17  ? 364 GLY A CA  1 
ATOM   2230  C  C   . GLY A 1 300 ? 73.089 22.982 95.842  1.00 82.59  ? 364 GLY A C   1 
ATOM   2231  O  O   . GLY A 1 300 ? 71.857 22.997 95.765  1.00 105.67 ? 364 GLY A O   1 
ATOM   2232  N  N   . THR A 1 301 ? 73.856 22.196 95.086  1.00 70.50  ? 365 THR A N   1 
ATOM   2233  C  CA  . THR A 1 301 ? 73.347 21.490 93.911  1.00 66.51  ? 365 THR A CA  1 
ATOM   2234  C  C   . THR A 1 301 ? 72.363 20.388 94.254  1.00 64.83  ? 365 THR A C   1 
ATOM   2235  O  O   . THR A 1 301 ? 72.305 19.923 95.387  1.00 73.19  ? 365 THR A O   1 
ATOM   2236  C  CB  . THR A 1 301 ? 74.504 20.934 93.026  1.00 76.51  ? 365 THR A CB  1 
ATOM   2237  O  OG1 . THR A 1 301 ? 73.960 20.315 91.855  1.00 95.95  ? 365 THR A OG1 1 
ATOM   2238  C  CG2 . THR A 1 301 ? 75.343 19.920 93.769  1.00 59.54  ? 365 THR A CG2 1 
ATOM   2239  N  N   . LEU A 1 302 ? 71.583 19.984 93.262  1.00 62.89  ? 366 LEU A N   1 
ATOM   2240  C  CA  . LEU A 1 302 ? 70.690 18.848 93.399  1.00 59.29  ? 366 LEU A CA  1 
ATOM   2241  C  C   . LEU A 1 302 ? 71.421 17.584 92.995  1.00 70.71  ? 366 LEU A C   1 
ATOM   2242  O  O   . LEU A 1 302 ? 70.876 16.491 93.086  1.00 79.82  ? 366 LEU A O   1 
ATOM   2243  C  CB  . LEU A 1 302 ? 69.509 19.023 92.476  1.00 58.76  ? 366 LEU A CB  1 
ATOM   2244  C  CG  . LEU A 1 302 ? 68.737 20.316 92.635  1.00 67.23  ? 366 LEU A CG  1 
ATOM   2245  C  CD1 . LEU A 1 302 ? 69.068 21.248 91.500  1.00 81.61  ? 366 LEU A CD1 1 
ATOM   2246  C  CD2 . LEU A 1 302 ? 67.310 19.978 92.589  1.00 74.38  ? 366 LEU A CD2 1 
ATOM   2247  N  N   . PHE A 1 303 ? 72.662 17.742 92.547  1.00 84.16  ? 367 PHE A N   1 
ATOM   2248  C  CA  . PHE A 1 303 ? 73.407 16.647 91.950  1.00 83.75  ? 367 PHE A CA  1 
ATOM   2249  C  C   . PHE A 1 303 ? 74.507 16.106 92.856  1.00 101.26 ? 367 PHE A C   1 
ATOM   2250  O  O   . PHE A 1 303 ? 75.250 15.205 92.469  1.00 108.88 ? 367 PHE A O   1 
ATOM   2251  C  CB  . PHE A 1 303 ? 73.945 17.089 90.596  1.00 97.00  ? 367 PHE A CB  1 
ATOM   2252  C  CG  . PHE A 1 303 ? 72.891 17.661 89.711  1.00 91.75  ? 367 PHE A CG  1 
ATOM   2253  C  CD1 . PHE A 1 303 ? 71.730 16.928 89.445  1.00 80.40  ? 367 PHE A CD1 1 
ATOM   2254  C  CD2 . PHE A 1 303 ? 73.040 18.932 89.158  1.00 80.04  ? 367 PHE A CD2 1 
ATOM   2255  C  CE1 . PHE A 1 303 ? 70.732 17.445 88.645  1.00 73.01  ? 367 PHE A CE1 1 
ATOM   2256  C  CE2 . PHE A 1 303 ? 72.041 19.462 88.347  1.00 98.77  ? 367 PHE A CE2 1 
ATOM   2257  C  CZ  . PHE A 1 303 ? 70.884 18.713 88.090  1.00 78.61  ? 367 PHE A CZ  1 
ATOM   2258  N  N   . SER A 1 304 ? 74.604 16.665 94.058  1.00 96.27  ? 368 SER A N   1 
ATOM   2259  C  CA  . SER A 1 304 ? 75.433 16.095 95.099  1.00 98.83  ? 368 SER A CA  1 
ATOM   2260  C  C   . SER A 1 304 ? 74.534 15.314 96.047  1.00 105.72 ? 368 SER A C   1 
ATOM   2261  O  O   . SER A 1 304 ? 73.432 15.747 96.371  1.00 122.75 ? 368 SER A O   1 
ATOM   2262  C  CB  . SER A 1 304 ? 76.192 17.182 95.860  1.00 104.38 ? 368 SER A CB  1 
ATOM   2263  O  OG  . SER A 1 304 ? 77.138 16.607 96.748  1.00 117.75 ? 368 SER A OG  1 
ATOM   2264  N  N   . VAL A 1 305 ? 75.008 14.157 96.488  1.00 101.70 ? 369 VAL A N   1 
ATOM   2265  C  CA  . VAL A 1 305 ? 74.279 13.336 97.439  1.00 82.24  ? 369 VAL A CA  1 
ATOM   2266  C  C   . VAL A 1 305 ? 74.408 13.969 98.828  1.00 88.92  ? 369 VAL A C   1 
ATOM   2267  O  O   . VAL A 1 305 ? 73.671 13.635 99.763  1.00 86.76  ? 369 VAL A O   1 
ATOM   2268  C  CB  . VAL A 1 305 ? 74.833 11.894 97.399  1.00 79.42  ? 369 VAL A CB  1 
ATOM   2269  C  CG1 . VAL A 1 305 ? 76.296 11.869 97.849  1.00 93.76  ? 369 VAL A CG1 1 
ATOM   2270  C  CG2 . VAL A 1 305 ? 73.971 10.945 98.211  1.00 78.34  ? 369 VAL A CG2 1 
ATOM   2271  N  N   . GLN A 1 306 ? 75.347 14.905 98.926  1.00 98.09  ? 370 GLN A N   1 
ATOM   2272  C  CA  . GLN A 1 306 ? 75.693 15.604 100.158 1.00 97.04  ? 370 GLN A CA  1 
ATOM   2273  C  C   . GLN A 1 306 ? 74.639 16.587 100.650 1.00 79.35  ? 370 GLN A C   1 
ATOM   2274  O  O   . GLN A 1 306 ? 74.600 16.906 101.831 1.00 89.08  ? 370 GLN A O   1 
ATOM   2275  C  CB  . GLN A 1 306 ? 76.993 16.390 99.931  1.00 134.75 ? 370 GLN A CB  1 
ATOM   2276  C  CG  . GLN A 1 306 ? 78.268 15.554 99.914  1.00 139.71 ? 370 GLN A CG  1 
ATOM   2277  C  CD  . GLN A 1 306 ? 78.731 15.191 101.313 1.00 130.17 ? 370 GLN A CD  1 
ATOM   2278  O  OE1 . GLN A 1 306 ? 78.225 14.250 101.921 1.00 128.69 ? 370 GLN A OE1 1 
ATOM   2279  N  NE2 . GLN A 1 306 ? 79.698 15.940 101.830 1.00 130.95 ? 370 GLN A NE2 1 
ATOM   2280  N  N   . THR A 1 307 ? 73.799 17.072 99.739  1.00 81.73  ? 371 THR A N   1 
ATOM   2281  C  CA  . THR A 1 307 ? 73.049 18.314 99.963  1.00 81.53  ? 371 THR A CA  1 
ATOM   2282  C  C   . THR A 1 307 ? 71.740 18.147 100.722 1.00 74.76  ? 371 THR A C   1 
ATOM   2283  O  O   . THR A 1 307 ? 71.082 17.119 100.652 1.00 75.23  ? 371 THR A O   1 
ATOM   2284  C  CB  . THR A 1 307 ? 72.836 19.086 98.668  1.00 79.67  ? 371 THR A CB  1 
ATOM   2285  O  OG1 . THR A 1 307 ? 72.234 18.214 97.719  1.00 99.94  ? 371 THR A OG1 1 
ATOM   2286  C  CG2 . THR A 1 307 ? 74.191 19.576 98.122  1.00 85.82  ? 371 THR A CG2 1 
ATOM   2287  N  N   . VAL A 1 308 ? 71.378 19.210 101.426 1.00 81.56  ? 372 VAL A N   1 
ATOM   2288  C  CA  . VAL A 1 308 ? 70.499 19.161 102.583 1.00 71.29  ? 372 VAL A CA  1 
ATOM   2289  C  C   . VAL A 1 308 ? 69.199 19.911 102.333 1.00 78.54  ? 372 VAL A C   1 
ATOM   2290  O  O   . VAL A 1 308 ? 69.202 21.062 101.872 1.00 69.08  ? 372 VAL A O   1 
ATOM   2291  C  CB  . VAL A 1 308 ? 71.201 19.853 103.770 1.00 77.51  ? 372 VAL A CB  1 
ATOM   2292  C  CG1 . VAL A 1 308 ? 70.390 19.734 105.024 1.00 91.31  ? 372 VAL A CG1 1 
ATOM   2293  C  CG2 . VAL A 1 308 ? 72.585 19.284 103.993 1.00 85.79  ? 372 VAL A CG2 1 
ATOM   2294  N  N   . GLY A 1 309 ? 68.086 19.267 102.659 1.00 86.91  ? 373 GLY A N   1 
ATOM   2295  C  CA  . GLY A 1 309 ? 66.801 19.958 102.664 1.00 84.16  ? 373 GLY A CA  1 
ATOM   2296  C  C   . GLY A 1 309 ? 66.855 21.103 103.650 1.00 72.93  ? 373 GLY A C   1 
ATOM   2297  O  O   . GLY A 1 309 ? 67.560 21.028 104.647 1.00 87.40  ? 373 GLY A O   1 
ATOM   2298  N  N   . ASN A 1 310 ? 66.128 22.174 103.378 1.00 67.37  ? 374 ASN A N   1 
ATOM   2299  C  CA  . ASN A 1 310 ? 66.217 23.345 104.230 1.00 67.88  ? 374 ASN A CA  1 
ATOM   2300  C  C   . ASN A 1 310 ? 64.839 23.836 104.536 1.00 67.63  ? 374 ASN A C   1 
ATOM   2301  O  O   . ASN A 1 310 ? 64.433 23.842 105.678 1.00 115.82 ? 374 ASN A O   1 
ATOM   2302  C  CB  . ASN A 1 310 ? 67.052 24.464 103.587 1.00 74.40  ? 374 ASN A CB  1 
ATOM   2303  C  CG  . ASN A 1 310 ? 67.052 25.736 104.406 1.00 74.02  ? 374 ASN A CG  1 
ATOM   2304  O  OD1 . ASN A 1 310 ? 66.288 26.651 104.155 1.00 83.74  ? 374 ASN A OD1 1 
ATOM   2305  N  ND2 . ASN A 1 310 ? 67.889 25.781 105.409 1.00 89.44  ? 374 ASN A ND2 1 
ATOM   2306  N  N   . ARG A 1 311 ? 64.117 24.258 103.513 1.00 70.20  ? 375 ARG A N   1 
ATOM   2307  C  CA  . ARG A 1 311 ? 62.819 24.878 103.725 1.00 66.41  ? 375 ARG A CA  1 
ATOM   2308  C  C   . ARG A 1 311 ? 61.733 24.400 102.775 1.00 67.83  ? 375 ARG A C   1 
ATOM   2309  O  O   . ARG A 1 311 ? 61.872 24.477 101.547 1.00 66.11  ? 375 ARG A O   1 
ATOM   2310  C  CB  . ARG A 1 311 ? 62.935 26.378 103.594 1.00 54.98  ? 375 ARG A CB  1 
ATOM   2311  C  CG  . ARG A 1 311 ? 61.608 27.074 103.747 1.00 51.01  ? 375 ARG A CG  1 
ATOM   2312  C  CD  . ARG A 1 311 ? 61.266 27.141 105.175 1.00 61.44  ? 375 ARG A CD  1 
ATOM   2313  N  NE  . ARG A 1 311 ? 60.044 27.888 105.444 1.00 76.65  ? 375 ARG A NE  1 
ATOM   2314  C  CZ  . ARG A 1 311 ? 60.008 29.193 105.688 1.00 81.97  ? 375 ARG A CZ  1 
ATOM   2315  N  NH1 . ARG A 1 311 ? 61.132 29.893 105.652 1.00 97.67  ? 375 ARG A NH1 1 
ATOM   2316  N  NH2 . ARG A 1 311 ? 58.852 29.800 105.953 1.00 72.45  ? 375 ARG A NH2 1 
ATOM   2317  N  N   . ASN A 1 312 ? 60.634 23.937 103.345 1.00 57.48  ? 376 ASN A N   1 
ATOM   2318  C  CA  . ASN A 1 312 ? 59.526 23.475 102.533 1.00 59.16  ? 376 ASN A CA  1 
ATOM   2319  C  C   . ASN A 1 312 ? 58.365 24.465 102.532 1.00 64.30  ? 376 ASN A C   1 
ATOM   2320  O  O   . ASN A 1 312 ? 57.767 24.724 103.585 1.00 72.68  ? 376 ASN A O   1 
ATOM   2321  C  CB  . ASN A 1 312 ? 59.064 22.122 103.050 1.00 63.87  ? 376 ASN A CB  1 
ATOM   2322  C  CG  . ASN A 1 312 ? 57.750 21.702 102.479 1.00 75.18  ? 376 ASN A CG  1 
ATOM   2323  O  OD1 . ASN A 1 312 ? 56.685 21.930 103.082 1.00 102.92 ? 376 ASN A OD1 1 
ATOM   2324  N  ND2 . ASN A 1 312 ? 57.799 21.091 101.304 1.00 64.47  ? 376 ASN A ND2 1 
ATOM   2325  N  N   . TYR A 1 313 ? 58.055 25.018 101.359 1.00 47.71  ? 377 TYR A N   1 
ATOM   2326  C  CA  . TYR A 1 313 ? 56.854 25.853 101.176 1.00 49.06  ? 377 TYR A CA  1 
ATOM   2327  C  C   . TYR A 1 313 ? 55.677 25.059 100.602 1.00 52.40  ? 377 TYR A C   1 
ATOM   2328  O  O   . TYR A 1 313 ? 55.714 24.594 99.476  1.00 69.07  ? 377 TYR A O   1 
ATOM   2329  C  CB  . TYR A 1 313 ? 57.136 27.030 100.239 1.00 39.55  ? 377 TYR A CB  1 
ATOM   2330  C  CG  . TYR A 1 313 ? 58.121 28.039 100.774 1.00 49.83  ? 377 TYR A CG  1 
ATOM   2331  C  CD1 . TYR A 1 313 ? 59.446 28.048 100.339 1.00 44.51  ? 377 TYR A CD1 1 
ATOM   2332  C  CD2 . TYR A 1 313 ? 57.731 28.990 101.722 1.00 56.94  ? 377 TYR A CD2 1 
ATOM   2333  C  CE1 . TYR A 1 313 ? 60.350 28.989 100.822 1.00 49.95  ? 377 TYR A CE1 1 
ATOM   2334  C  CE2 . TYR A 1 313 ? 58.635 29.927 102.227 1.00 63.67  ? 377 TYR A CE2 1 
ATOM   2335  C  CZ  . TYR A 1 313 ? 59.940 29.928 101.774 1.00 59.10  ? 377 TYR A CZ  1 
ATOM   2336  O  OH  . TYR A 1 313 ? 60.814 30.869 102.278 1.00 55.20  ? 377 TYR A OH  1 
ATOM   2337  N  N   . GLN A 1 314 ? 54.617 24.908 101.358 1.00 52.29  ? 378 GLN A N   1 
ATOM   2338  C  CA  . GLN A 1 314 ? 53.428 24.296 100.803 1.00 55.85  ? 378 GLN A CA  1 
ATOM   2339  C  C   . GLN A 1 314 ? 52.568 25.394 100.230 1.00 53.54  ? 378 GLN A C   1 
ATOM   2340  O  O   . GLN A 1 314 ? 51.782 26.002 100.943 1.00 69.61  ? 378 GLN A O   1 
ATOM   2341  C  CB  . GLN A 1 314 ? 52.649 23.542 101.883 1.00 66.61  ? 378 GLN A CB  1 
ATOM   2342  C  CG  . GLN A 1 314 ? 53.376 22.324 102.391 1.00 72.35  ? 378 GLN A CG  1 
ATOM   2343  C  CD  . GLN A 1 314 ? 52.432 21.313 102.950 1.00 88.26  ? 378 GLN A CD  1 
ATOM   2344  O  OE1 . GLN A 1 314 ? 51.138 21.628 102.926 1.00 120.90 ? 378 GLN A OE1 1 
ATOM   2345  N  NE2 . GLN A 1 314 ? 52.850 20.253 103.400 1.00 99.08  ? 378 GLN A NE2 1 
ATOM   2346  N  N   . LEU A 1 315 ? 52.703 25.647 98.940  1.00 50.57  ? 379 LEU A N   1 
ATOM   2347  C  CA  . LEU A 1 315 ? 52.025 26.794 98.348  1.00 46.33  ? 379 LEU A CA  1 
ATOM   2348  C  C   . LEU A 1 315 ? 50.552 26.594 98.146  1.00 52.37  ? 379 LEU A C   1 
ATOM   2349  O  O   . LEU A 1 315 ? 49.779 27.540 98.304  1.00 62.71  ? 379 LEU A O   1 
ATOM   2350  C  CB  . LEU A 1 315 ? 52.662 27.170 97.027  1.00 50.19  ? 379 LEU A CB  1 
ATOM   2351  C  CG  . LEU A 1 315 ? 54.122 27.619 97.093  1.00 50.00  ? 379 LEU A CG  1 
ATOM   2352  C  CD1 . LEU A 1 315 ? 54.618 27.924 95.686  1.00 55.49  ? 379 LEU A CD1 1 
ATOM   2353  C  CD2 . LEU A 1 315 ? 54.260 28.827 97.992  1.00 40.58  ? 379 LEU A CD2 1 
ATOM   2354  N  N   . LEU A 1 316 ? 50.158 25.375 97.783  1.00 54.47  ? 380 LEU A N   1 
ATOM   2355  C  CA  . LEU A 1 316 ? 48.752 25.102 97.490  1.00 60.75  ? 380 LEU A CA  1 
ATOM   2356  C  C   . LEU A 1 316 ? 48.345 23.872 98.230  1.00 64.65  ? 380 LEU A C   1 
ATOM   2357  O  O   . LEU A 1 316 ? 49.116 22.902 98.261  1.00 71.04  ? 380 LEU A O   1 
ATOM   2358  C  CB  . LEU A 1 316 ? 48.511 24.902 95.978  1.00 61.51  ? 380 LEU A CB  1 
ATOM   2359  C  CG  . LEU A 1 316 ? 48.830 26.040 94.992  1.00 50.88  ? 380 LEU A CG  1 
ATOM   2360  C  CD1 . LEU A 1 316 ? 48.120 25.818 93.737  1.00 63.59  ? 380 LEU A CD1 1 
ATOM   2361  C  CD2 . LEU A 1 316 ? 48.430 27.397 95.529  1.00 61.17  ? 380 LEU A CD2 1 
ATOM   2362  N  N   . SER A 1 317 ? 47.140 23.903 98.807  1.00 59.59  ? 381 SER A N   1 
ATOM   2363  C  CA  . SER A 1 317 ? 46.631 22.765 99.575  1.00 58.33  ? 381 SER A CA  1 
ATOM   2364  C  C   . SER A 1 317 ? 45.288 22.302 99.095  1.00 69.58  ? 381 SER A C   1 
ATOM   2365  O  O   . SER A 1 317 ? 45.074 21.110 98.872  1.00 99.46  ? 381 SER A O   1 
ATOM   2366  C  CB  . SER A 1 317 ? 46.534 23.122 101.031 1.00 61.55  ? 381 SER A CB  1 
ATOM   2367  O  OG  . SER A 1 317 ? 47.750 23.697 101.470 1.00 106.36 ? 381 SER A OG  1 
ATOM   2368  N  N   . ASN A 1 318 ? 44.380 23.249 98.920  1.00 78.11  ? 382 ASN A N   1 
ATOM   2369  C  CA  . ASN A 1 318 ? 43.022 22.905 98.542  1.00 105.31 ? 382 ASN A CA  1 
ATOM   2370  C  C   . ASN A 1 318 ? 42.756 22.597 97.051  1.00 85.69  ? 382 ASN A C   1 
ATOM   2371  O  O   . ASN A 1 318 ? 41.631 22.270 96.679  1.00 118.71 ? 382 ASN A O   1 
ATOM   2372  C  CB  . ASN A 1 318 ? 42.052 23.961 99.090  1.00 118.37 ? 382 ASN A CB  1 
ATOM   2373  C  CG  . ASN A 1 318 ? 41.242 23.450 100.274 1.00 172.68 ? 382 ASN A CG  1 
ATOM   2374  O  OD1 . ASN A 1 318 ? 41.157 22.241 100.519 1.00 222.89 ? 382 ASN A OD1 1 
ATOM   2375  N  ND2 . ASN A 1 318 ? 40.625 24.369 101.002 1.00 174.17 ? 382 ASN A ND2 1 
ATOM   2376  N  N   . SER A 1 319 ? 43.777 22.668 96.208  1.00 61.35  ? 383 SER A N   1 
ATOM   2377  C  CA  . SER A 1 319 ? 43.536 22.721 94.769  1.00 67.90  ? 383 SER A CA  1 
ATOM   2378  C  C   . SER A 1 319 ? 44.059 21.505 94.028  1.00 69.08  ? 383 SER A C   1 
ATOM   2379  O  O   . SER A 1 319 ? 45.164 21.066 94.279  1.00 87.81  ? 383 SER A O   1 
ATOM   2380  C  CB  . SER A 1 319 ? 44.127 24.005 94.183  1.00 53.73  ? 383 SER A CB  1 
ATOM   2381  O  OG  . SER A 1 319 ? 44.272 24.982 95.209  1.00 70.16  ? 383 SER A OG  1 
ATOM   2382  N  N   . THR A 1 320 ? 43.261 20.968 93.113  1.00 63.99  ? 384 THR A N   1 
ATOM   2383  C  CA  . THR A 1 320 ? 43.704 19.864 92.268  1.00 66.13  ? 384 THR A CA  1 
ATOM   2384  C  C   . THR A 1 320 ? 44.735 20.294 91.211  1.00 62.55  ? 384 THR A C   1 
ATOM   2385  O  O   . THR A 1 320 ? 44.446 21.126 90.331  1.00 67.74  ? 384 THR A O   1 
ATOM   2386  C  CB  . THR A 1 320 ? 42.513 19.140 91.618  1.00 68.17  ? 384 THR A CB  1 
ATOM   2387  O  OG1 . THR A 1 320 ? 41.654 18.636 92.655  1.00 75.74  ? 384 THR A OG1 1 
ATOM   2388  C  CG2 . THR A 1 320 ? 43.013 17.974 90.754  1.00 62.90  ? 384 THR A CG2 1 
ATOM   2389  N  N   . ILE A 1 321 ? 45.928 19.701 91.297  1.00 48.29  ? 385 ILE A N   1 
ATOM   2390  C  CA  . ILE A 1 321 ? 47.086 20.150 90.511  1.00 45.49  ? 385 ILE A CA  1 
ATOM   2391  C  C   . ILE A 1 321 ? 47.454 19.208 89.382  1.00 47.67  ? 385 ILE A C   1 
ATOM   2392  O  O   . ILE A 1 321 ? 47.105 18.039 89.401  1.00 60.19  ? 385 ILE A O   1 
ATOM   2393  C  CB  . ILE A 1 321 ? 48.340 20.342 91.388  1.00 46.65  ? 385 ILE A CB  1 
ATOM   2394  C  CG1 . ILE A 1 321 ? 48.007 21.123 92.657  1.00 56.42  ? 385 ILE A CG1 1 
ATOM   2395  C  CG2 . ILE A 1 321 ? 49.410 21.105 90.654  1.00 34.67  ? 385 ILE A CG2 1 
ATOM   2396  C  CD1 . ILE A 1 321 ? 47.749 22.602 92.433  1.00 46.08  ? 385 ILE A CD1 1 
ATOM   2397  N  N   . GLY A 1 322 ? 48.156 19.760 88.392  1.00 57.73  ? 386 GLY A N   1 
ATOM   2398  C  CA  . GLY A 1 322 ? 48.593 19.057 87.190  1.00 45.14  ? 386 GLY A CA  1 
ATOM   2399  C  C   . GLY A 1 322 ? 49.950 19.569 86.759  1.00 58.87  ? 386 GLY A C   1 
ATOM   2400  O  O   . GLY A 1 322 ? 50.937 19.477 87.519  1.00 62.37  ? 386 GLY A O   1 
ATOM   2401  N  N   . ARG A 1 323 ? 50.031 20.110 85.546  1.00 62.43  ? 387 ARG A N   1 
ATOM   2402  C  CA  . ARG A 1 323 ? 51.353 20.515 85.013  1.00 50.85  ? 387 ARG A CA  1 
ATOM   2403  C  C   . ARG A 1 323 ? 51.847 21.773 85.693  1.00 36.26  ? 387 ARG A C   1 
ATOM   2404  O  O   . ARG A 1 323 ? 51.064 22.562 86.242  1.00 39.14  ? 387 ARG A O   1 
ATOM   2405  C  CB  . ARG A 1 323 ? 51.344 20.698 83.489  1.00 42.88  ? 387 ARG A CB  1 
ATOM   2406  C  CG  . ARG A 1 323 ? 50.555 19.649 82.755  1.00 41.44  ? 387 ARG A CG  1 
ATOM   2407  C  CD  . ARG A 1 323 ? 50.100 20.116 81.412  1.00 47.15  ? 387 ARG A CD  1 
ATOM   2408  N  NE  . ARG A 1 323 ? 51.180 20.778 80.702  1.00 62.01  ? 387 ARG A NE  1 
ATOM   2409  C  CZ  . ARG A 1 323 ? 51.204 22.080 80.432  1.00 54.11  ? 387 ARG A CZ  1 
ATOM   2410  N  NH1 . ARG A 1 323 ? 50.197 22.882 80.789  1.00 40.93  ? 387 ARG A NH1 1 
ATOM   2411  N  NH2 . ARG A 1 323 ? 52.249 22.575 79.802  1.00 51.96  ? 387 ARG A NH2 1 
ATOM   2412  N  N   . SER A 1 324 ? 53.155 21.929 85.657  1.00 29.33  ? 388 SER A N   1 
ATOM   2413  C  CA  . SER A 1 324 ? 53.854 23.053 86.264  1.00 40.13  ? 388 SER A CA  1 
ATOM   2414  C  C   . SER A 1 324 ? 55.036 23.355 85.357  1.00 40.62  ? 388 SER A C   1 
ATOM   2415  O  O   . SER A 1 324 ? 55.619 22.452 84.795  1.00 54.42  ? 388 SER A O   1 
ATOM   2416  C  CB  . SER A 1 324 ? 54.340 22.725 87.700  1.00 38.34  ? 388 SER A CB  1 
ATOM   2417  O  OG  . SER A 1 324 ? 54.791 21.360 87.879  1.00 43.25  ? 388 SER A OG  1 
ATOM   2418  N  N   . GLY A 1 325 ? 55.393 24.608 85.178  1.00 35.10  ? 389 GLY A N   1 
ATOM   2419  C  CA  . GLY A 1 325 ? 56.519 24.873 84.317  1.00 37.75  ? 389 GLY A CA  1 
ATOM   2420  C  C   . GLY A 1 325 ? 57.153 26.187 84.691  1.00 42.23  ? 389 GLY A C   1 
ATOM   2421  O  O   . GLY A 1 325 ? 56.545 26.966 85.444  1.00 39.58  ? 389 GLY A O   1 
ATOM   2422  N  N   . LEU A 1 326 ? 58.368 26.427 84.182  1.00 31.19  ? 390 LEU A N   1 
ATOM   2423  C  CA  . LEU A 1 326 ? 59.075 27.672 84.440  1.00 35.54  ? 390 LEU A CA  1 
ATOM   2424  C  C   . LEU A 1 326 ? 58.887 28.674 83.308  1.00 40.22  ? 390 LEU A C   1 
ATOM   2425  O  O   . LEU A 1 326 ? 58.424 28.320 82.224  1.00 56.16  ? 390 LEU A O   1 
ATOM   2426  C  CB  . LEU A 1 326 ? 60.548 27.401 84.585  1.00 32.22  ? 390 LEU A CB  1 
ATOM   2427  C  CG  . LEU A 1 326 ? 60.938 26.469 85.700  1.00 30.15  ? 390 LEU A CG  1 
ATOM   2428  C  CD1 . LEU A 1 326 ? 62.187 25.877 85.281  1.00 38.58  ? 390 LEU A CD1 1 
ATOM   2429  C  CD2 . LEU A 1 326 ? 61.189 27.283 86.884  1.00 42.83  ? 390 LEU A CD2 1 
ATOM   2430  N  N   . TYR A 1 327 ? 59.216 29.934 83.590  1.00 45.52  ? 391 TYR A N   1 
ATOM   2431  C  CA  . TYR A 1 327 ? 59.320 30.999 82.574  1.00 46.39  ? 391 TYR A CA  1 
ATOM   2432  C  C   . TYR A 1 327 ? 60.120 32.170 83.091  1.00 45.20  ? 391 TYR A C   1 
ATOM   2433  O  O   . TYR A 1 327 ? 60.028 32.511 84.266  1.00 63.78  ? 391 TYR A O   1 
ATOM   2434  C  CB  . TYR A 1 327 ? 57.947 31.482 82.079  1.00 32.76  ? 391 TYR A CB  1 
ATOM   2435  C  CG  . TYR A 1 327 ? 57.081 32.248 83.043  1.00 38.02  ? 391 TYR A CG  1 
ATOM   2436  C  CD1 . TYR A 1 327 ? 57.109 33.639 83.091  1.00 42.14  ? 391 TYR A CD1 1 
ATOM   2437  C  CD2 . TYR A 1 327 ? 56.195 31.589 83.875  1.00 53.50  ? 391 TYR A CD2 1 
ATOM   2438  C  CE1 . TYR A 1 327 ? 56.286 34.354 83.945  1.00 42.73  ? 391 TYR A CE1 1 
ATOM   2439  C  CE2 . TYR A 1 327 ? 55.375 32.295 84.741  1.00 60.24  ? 391 TYR A CE2 1 
ATOM   2440  C  CZ  . TYR A 1 327 ? 55.423 33.686 84.759  1.00 51.33  ? 391 TYR A CZ  1 
ATOM   2441  O  OH  . TYR A 1 327 ? 54.612 34.400 85.615  1.00 50.70  ? 391 TYR A OH  1 
ATOM   2442  N  N   . GLN A 1 328 ? 60.900 32.792 82.221  1.00 49.52  ? 392 GLN A N   1 
ATOM   2443  C  CA  . GLN A 1 328 ? 61.647 33.987 82.630  1.00 47.25  ? 392 GLN A CA  1 
ATOM   2444  C  C   . GLN A 1 328 ? 61.072 35.196 81.935  1.00 51.69  ? 392 GLN A C   1 
ATOM   2445  O  O   . GLN A 1 328 ? 61.069 35.276 80.703  1.00 104.57 ? 392 GLN A O   1 
ATOM   2446  C  CB  . GLN A 1 328 ? 63.127 33.860 82.295  1.00 40.24  ? 392 GLN A CB  1 
ATOM   2447  C  CG  . GLN A 1 328 ? 63.696 32.559 82.720  1.00 44.86  ? 392 GLN A CG  1 
ATOM   2448  C  CD  . GLN A 1 328 ? 65.138 32.425 82.365  1.00 56.13  ? 392 GLN A CD  1 
ATOM   2449  O  OE1 . GLN A 1 328 ? 65.474 32.020 81.255  1.00 73.22  ? 392 GLN A OE1 1 
ATOM   2450  N  NE2 . GLN A 1 328 ? 66.015 32.739 83.314  1.00 69.88  ? 392 GLN A NE2 1 
ATOM   2451  N  N   . PRO A 1 329 ? 60.543 36.124 82.716  1.00 38.87  ? 393 PRO A N   1 
ATOM   2452  C  CA  . PRO A 1 329 ? 60.143 37.413 82.191  1.00 43.46  ? 393 PRO A CA  1 
ATOM   2453  C  C   . PRO A 1 329 ? 61.400 38.236 81.887  1.00 52.30  ? 393 PRO A C   1 
ATOM   2454  O  O   . PRO A 1 329 ? 62.437 38.031 82.523  1.00 60.20  ? 393 PRO A O   1 
ATOM   2455  C  CB  . PRO A 1 329 ? 59.312 37.995 83.324  1.00 43.32  ? 393 PRO A CB  1 
ATOM   2456  C  CG  . PRO A 1 329 ? 59.833 37.316 84.558  1.00 42.94  ? 393 PRO A CG  1 
ATOM   2457  C  CD  . PRO A 1 329 ? 60.251 35.969 84.146  1.00 44.16  ? 393 PRO A CD  1 
ATOM   2458  N  N   . ALA A 1 330 ? 61.327 39.134 80.909  1.00 71.28  ? 394 ALA A N   1 
ATOM   2459  C  CA  . ALA A 1 330 ? 62.502 39.930 80.544  1.00 84.03  ? 394 ALA A CA  1 
ATOM   2460  C  C   . ALA A 1 330 ? 62.243 41.420 80.688  1.00 110.21 ? 394 ALA A C   1 
ATOM   2461  O  O   . ALA A 1 330 ? 61.290 41.945 80.106  1.00 137.79 ? 394 ALA A O   1 
ATOM   2462  C  CB  . ALA A 1 330 ? 62.925 39.611 79.144  1.00 82.51  ? 394 ALA A CB  1 
ATOM   2463  N  N   . TYR A 1 331 ? 63.078 42.085 81.487  1.00 115.87 ? 395 TYR A N   1 
ATOM   2464  C  CA  . TYR A 1 331 ? 63.072 43.547 81.594  1.00 142.06 ? 395 TYR A CA  1 
ATOM   2465  C  C   . TYR A 1 331 ? 64.505 44.032 81.710  1.00 160.66 ? 395 TYR A C   1 
ATOM   2466  O  O   . TYR A 1 331 ? 65.438 43.220 81.751  1.00 169.94 ? 395 TYR A O   1 
ATOM   2467  C  CB  . TYR A 1 331 ? 62.282 44.036 82.816  1.00 143.11 ? 395 TYR A CB  1 
ATOM   2468  C  CG  . TYR A 1 331 ? 61.109 43.171 83.209  1.00 145.88 ? 395 TYR A CG  1 
ATOM   2469  C  CD1 . TYR A 1 331 ? 59.882 43.273 82.542  1.00 155.92 ? 395 TYR A CD1 1 
ATOM   2470  C  CD2 . TYR A 1 331 ? 61.225 42.248 84.260  1.00 118.70 ? 395 TYR A CD2 1 
ATOM   2471  C  CE1 . TYR A 1 331 ? 58.797 42.469 82.904  1.00 160.14 ? 395 TYR A CE1 1 
ATOM   2472  C  CE2 . TYR A 1 331 ? 60.147 41.437 84.639  1.00 96.33  ? 395 TYR A CE2 1 
ATOM   2473  C  CZ  . TYR A 1 331 ? 58.937 41.553 83.956  1.00 136.41 ? 395 TYR A CZ  1 
ATOM   2474  O  OH  . TYR A 1 331 ? 57.875 40.755 84.330  1.00 110.91 ? 395 TYR A OH  1 
ATOM   2475  N  N   . GLU A 1 332 ? 64.676 45.353 81.758  1.00 165.70 ? 396 GLU A N   1 
ATOM   2476  C  CA  . GLU A 1 332 ? 65.965 45.945 82.086  1.00 194.36 ? 396 GLU A CA  1 
ATOM   2477  C  C   . GLU A 1 332 ? 66.341 45.509 83.500  1.00 230.18 ? 396 GLU A C   1 
ATOM   2478  O  O   . GLU A 1 332 ? 67.451 45.015 83.723  1.00 285.12 ? 396 GLU A O   1 
ATOM   2479  C  CB  . GLU A 1 332 ? 65.913 47.474 81.971  1.00 188.63 ? 396 GLU A CB  1 
ATOM   2480  C  CG  . GLU A 1 332 ? 67.268 48.178 82.120  1.00 178.32 ? 396 GLU A CG  1 
ATOM   2481  C  CD  . GLU A 1 332 ? 67.701 48.329 83.566  1.00 185.40 ? 396 GLU A CD  1 
ATOM   2482  O  OE1 . GLU A 1 332 ? 66.887 48.804 84.383  1.00 201.42 ? 396 GLU A OE1 1 
ATOM   2483  O  OE2 . GLU A 1 332 ? 68.855 47.970 83.886  1.00 180.71 ? 396 GLU A OE2 1 
ATOM   2484  N  N   . SER A 1 333 ? 65.397 45.670 84.434  1.00 210.29 ? 397 SER A N   1 
ATOM   2485  C  CA  . SER A 1 333 ? 65.587 45.329 85.851  1.00 198.19 ? 397 SER A CA  1 
ATOM   2486  C  C   . SER A 1 333 ? 67.013 45.629 86.294  1.00 213.32 ? 397 SER A C   1 
ATOM   2487  O  O   . SER A 1 333 ? 67.393 46.794 86.401  1.00 278.06 ? 397 SER A O   1 
ATOM   2488  C  CB  . SER A 1 333 ? 65.227 43.866 86.121  1.00 196.35 ? 397 SER A CB  1 
ATOM   2489  O  OG  . SER A 1 333 ? 63.853 43.633 85.882  1.00 198.93 ? 397 SER A OG  1 
ATOM   2490  N  N   . ARG A 1 334 ? 67.799 44.581 86.534  1.00 169.58 ? 398 ARG A N   1 
ATOM   2491  C  CA  . ARG A 1 334 ? 69.233 44.731 86.796  1.00 177.87 ? 398 ARG A CA  1 
ATOM   2492  C  C   . ARG A 1 334 ? 70.000 43.468 86.435  1.00 158.00 ? 398 ARG A C   1 
ATOM   2493  O  O   . ARG A 1 334 ? 69.446 42.575 85.796  1.00 167.07 ? 398 ARG A O   1 
ATOM   2494  C  CB  . ARG A 1 334 ? 69.503 45.146 88.249  1.00 172.72 ? 398 ARG A CB  1 
ATOM   2495  C  CG  . ARG A 1 334 ? 68.773 44.344 89.313  1.00 124.99 ? 398 ARG A CG  1 
ATOM   2496  C  CD  . ARG A 1 334 ? 69.286 44.717 90.695  1.00 148.53 ? 398 ARG A CD  1 
ATOM   2497  N  NE  . ARG A 1 334 ? 69.432 46.164 90.866  1.00 167.30 ? 398 ARG A NE  1 
ATOM   2498  C  CZ  . ARG A 1 334 ? 69.830 46.756 91.989  1.00 170.84 ? 398 ARG A CZ  1 
ATOM   2499  N  NH1 . ARG A 1 334 ? 70.125 46.031 93.060  1.00 176.67 ? 398 ARG A NH1 1 
ATOM   2500  N  NH2 . ARG A 1 334 ? 69.931 48.079 92.042  1.00 169.33 ? 398 ARG A NH2 1 
ATOM   2501  N  N   . ASP A 1 335 ? 71.270 43.404 86.841  1.00 175.46 ? 399 ASP A N   1 
ATOM   2502  C  CA  . ASP A 1 335 ? 72.146 42.246 86.583  1.00 187.54 ? 399 ASP A CA  1 
ATOM   2503  C  C   . ASP A 1 335 ? 71.436 40.923 86.841  1.00 153.80 ? 399 ASP A C   1 
ATOM   2504  O  O   . ASP A 1 335 ? 71.806 39.874 86.294  1.00 147.65 ? 399 ASP A O   1 
ATOM   2505  C  CB  . ASP A 1 335 ? 73.405 42.325 87.454  1.00 204.40 ? 399 ASP A CB  1 
ATOM   2506  C  CG  . ASP A 1 335 ? 74.289 43.517 87.112  1.00 208.74 ? 399 ASP A CG  1 
ATOM   2507  O  OD1 . ASP A 1 335 ? 74.118 44.109 86.025  1.00 212.74 ? 399 ASP A OD1 1 
ATOM   2508  O  OD2 . ASP A 1 335 ? 75.164 43.859 87.934  1.00 205.15 ? 399 ASP A OD2 1 
ATOM   2509  N  N   . CYS A 1 336 ? 70.405 41.015 87.673  1.00 106.96 ? 400 CYS A N   1 
ATOM   2510  C  CA  . CYS A 1 336 ? 69.593 39.901 88.100  1.00 83.17  ? 400 CYS A CA  1 
ATOM   2511  C  C   . CYS A 1 336 ? 68.558 39.429 87.059  1.00 82.77  ? 400 CYS A C   1 
ATOM   2512  O  O   . CYS A 1 336 ? 67.731 40.214 86.581  1.00 86.81  ? 400 CYS A O   1 
ATOM   2513  C  CB  . CYS A 1 336 ? 68.862 40.338 89.351  1.00 110.21 ? 400 CYS A CB  1 
ATOM   2514  S  SG  . CYS A 1 336 ? 68.646 39.044 90.502  1.00 186.06 ? 400 CYS A SG  1 
ATOM   2515  N  N   . GLN A 1 337 ? 68.592 38.136 86.733  1.00 85.50  ? 401 GLN A N   1 
ATOM   2516  C  CA  . GLN A 1 337 ? 67.552 37.496 85.899  1.00 72.60  ? 401 GLN A CA  1 
ATOM   2517  C  C   . GLN A 1 337 ? 66.404 36.887 86.692  1.00 61.14  ? 401 GLN A C   1 
ATOM   2518  O  O   . GLN A 1 337 ? 66.566 35.868 87.346  1.00 94.07  ? 401 GLN A O   1 
ATOM   2519  C  CB  . GLN A 1 337 ? 68.137 36.424 84.965  1.00 60.28  ? 401 GLN A CB  1 
ATOM   2520  C  CG  . GLN A 1 337 ? 67.124 35.830 84.000  1.00 63.66  ? 401 GLN A CG  1 
ATOM   2521  C  CD  . GLN A 1 337 ? 66.121 36.850 83.424  1.00 77.28  ? 401 GLN A CD  1 
ATOM   2522  O  OE1 . GLN A 1 337 ? 66.504 37.872 82.833  1.00 105.52 ? 401 GLN A OE1 1 
ATOM   2523  N  NE2 . GLN A 1 337 ? 64.832 36.563 83.593  1.00 73.57  ? 401 GLN A NE2 1 
ATOM   2524  N  N   . GLU A 1 338 ? 65.233 37.495 86.593  1.00 67.69  ? 402 GLU A N   1 
ATOM   2525  C  CA  . GLU A 1 338 ? 64.065 37.015 87.304  1.00 68.55  ? 402 GLU A CA  1 
ATOM   2526  C  C   . GLU A 1 338 ? 63.658 35.612 86.831  1.00 66.04  ? 402 GLU A C   1 
ATOM   2527  O  O   . GLU A 1 338 ? 63.819 35.269 85.657  1.00 63.03  ? 402 GLU A O   1 
ATOM   2528  C  CB  . GLU A 1 338 ? 62.912 38.007 87.128  1.00 88.34  ? 402 GLU A CB  1 
ATOM   2529  C  CG  . GLU A 1 338 ? 61.683 37.744 88.017  1.00 136.20 ? 402 GLU A CG  1 
ATOM   2530  C  CD  . GLU A 1 338 ? 61.640 38.578 89.295  1.00 161.70 ? 402 GLU A CD  1 
ATOM   2531  O  OE1 . GLU A 1 338 ? 61.995 39.775 89.246  1.00 185.51 ? 402 GLU A OE1 1 
ATOM   2532  O  OE2 . GLU A 1 338 ? 61.221 38.037 90.344  1.00 144.75 ? 402 GLU A OE2 1 
ATOM   2533  N  N   . LEU A 1 339 ? 63.152 34.806 87.763  1.00 54.30  ? 403 LEU A N   1 
ATOM   2534  C  CA  . LEU A 1 339 ? 62.616 33.477 87.449  1.00 45.56  ? 403 LEU A CA  1 
ATOM   2535  C  C   . LEU A 1 339 ? 61.239 33.225 88.061  1.00 43.32  ? 403 LEU A C   1 
ATOM   2536  O  O   . LEU A 1 339 ? 61.010 33.437 89.241  1.00 57.39  ? 403 LEU A O   1 
ATOM   2537  C  CB  . LEU A 1 339 ? 63.575 32.402 87.915  1.00 41.75  ? 403 LEU A CB  1 
ATOM   2538  C  CG  . LEU A 1 339 ? 63.191 30.963 87.643  1.00 41.20  ? 403 LEU A CG  1 
ATOM   2539  C  CD1 . LEU A 1 339 ? 63.029 30.706 86.158  1.00 49.13  ? 403 LEU A CD1 1 
ATOM   2540  C  CD2 . LEU A 1 339 ? 64.319 30.125 88.129  1.00 54.95  ? 403 LEU A CD2 1 
ATOM   2541  N  N   . CYS A 1 340 ? 60.317 32.770 87.240  1.00 48.23  ? 404 CYS A N   1 
ATOM   2542  C  CA  . CYS A 1 340 ? 58.950 32.550 87.666  1.00 49.74  ? 404 CYS A CA  1 
ATOM   2543  C  C   . CYS A 1 340 ? 58.490 31.157 87.266  1.00 44.94  ? 404 CYS A C   1 
ATOM   2544  O  O   . CYS A 1 340 ? 59.092 30.516 86.389  1.00 57.29  ? 404 CYS A O   1 
ATOM   2545  C  CB  . CYS A 1 340 ? 58.039 33.608 87.031  1.00 51.83  ? 404 CYS A CB  1 
ATOM   2546  S  SG  . CYS A 1 340 ? 58.453 35.230 87.579  1.00 76.86  ? 404 CYS A SG  1 
ATOM   2547  N  N   . PHE A 1 341 ? 57.421 30.679 87.884  1.00 29.69  ? 405 PHE A N   1 
ATOM   2548  C  CA  . PHE A 1 341 ? 56.834 29.474 87.368  1.00 31.60  ? 405 PHE A CA  1 
ATOM   2549  C  C   . PHE A 1 341 ? 55.325 29.523 87.471  1.00 33.43  ? 405 PHE A C   1 
ATOM   2550  O  O   . PHE A 1 341 ? 54.765 30.257 88.289  1.00 38.87  ? 405 PHE A O   1 
ATOM   2551  C  CB  . PHE A 1 341 ? 57.432 28.239 88.058  1.00 36.54  ? 405 PHE A CB  1 
ATOM   2552  C  CG  . PHE A 1 341 ? 57.007 28.069 89.507  1.00 40.76  ? 405 PHE A CG  1 
ATOM   2553  C  CD1 . PHE A 1 341 ? 57.725 28.637 90.530  1.00 55.63  ? 405 PHE A CD1 1 
ATOM   2554  C  CD2 . PHE A 1 341 ? 55.897 27.332 89.838  1.00 47.46  ? 405 PHE A CD2 1 
ATOM   2555  C  CE1 . PHE A 1 341 ? 57.342 28.503 91.853  1.00 40.73  ? 405 PHE A CE1 1 
ATOM   2556  C  CE2 . PHE A 1 341 ? 55.517 27.201 91.152  1.00 45.96  ? 405 PHE A CE2 1 
ATOM   2557  C  CZ  . PHE A 1 341 ? 56.244 27.803 92.153  1.00 43.56  ? 405 PHE A CZ  1 
ATOM   2558  N  N   . TRP A 1 342 ? 54.679 28.718 86.638  1.00 34.62  ? 406 TRP A N   1 
ATOM   2559  C  CA  . TRP A 1 342 ? 53.238 28.602 86.610  1.00 37.12  ? 406 TRP A CA  1 
ATOM   2560  C  C   . TRP A 1 342 ? 52.867 27.221 86.997  1.00 46.08  ? 406 TRP A C   1 
ATOM   2561  O  O   . TRP A 1 342 ? 53.690 26.302 86.926  1.00 58.48  ? 406 TRP A O   1 
ATOM   2562  C  CB  . TRP A 1 342 ? 52.692 28.891 85.210  1.00 38.77  ? 406 TRP A CB  1 
ATOM   2563  C  CG  . TRP A 1 342 ? 53.332 28.056 84.126  1.00 39.60  ? 406 TRP A CG  1 
ATOM   2564  C  CD1 . TRP A 1 342 ? 54.382 28.420 83.258  1.00 40.53  ? 406 TRP A CD1 1 
ATOM   2565  C  CD2 . TRP A 1 342 ? 52.993 26.694 83.755  1.00 38.28  ? 406 TRP A CD2 1 
ATOM   2566  N  NE1 . TRP A 1 342 ? 54.704 27.392 82.410  1.00 31.97  ? 406 TRP A NE1 1 
ATOM   2567  C  CE2 . TRP A 1 342 ? 53.897 26.325 82.657  1.00 38.52  ? 406 TRP A CE2 1 
ATOM   2568  C  CE3 . TRP A 1 342 ? 52.058 25.769 84.195  1.00 49.31  ? 406 TRP A CE3 1 
ATOM   2569  C  CZ2 . TRP A 1 342 ? 53.837 25.083 82.057  1.00 37.86  ? 406 TRP A CZ2 1 
ATOM   2570  C  CZ3 . TRP A 1 342 ? 52.010 24.507 83.571  1.00 40.12  ? 406 TRP A CZ3 1 
ATOM   2571  C  CH2 . TRP A 1 342 ? 52.874 24.182 82.533  1.00 37.01  ? 406 TRP A CH2 1 
ATOM   2572  N  N   . ILE A 1 343 ? 51.606 27.070 87.392  1.00 54.64  ? 407 ILE A N   1 
ATOM   2573  C  CA  . ILE A 1 343 ? 51.028 25.796 87.768  1.00 45.28  ? 407 ILE A CA  1 
ATOM   2574  C  C   . ILE A 1 343 ? 49.594 25.754 87.272  1.00 54.09  ? 407 ILE A C   1 
ATOM   2575  O  O   . ILE A 1 343 ? 48.782 26.659 87.530  1.00 63.13  ? 407 ILE A O   1 
ATOM   2576  C  CB  . ILE A 1 343 ? 50.969 25.639 89.258  1.00 43.13  ? 407 ILE A CB  1 
ATOM   2577  C  CG1 . ILE A 1 343 ? 52.325 25.927 89.890  1.00 50.23  ? 407 ILE A CG1 1 
ATOM   2578  C  CG2 . ILE A 1 343 ? 50.514 24.242 89.588  1.00 42.28  ? 407 ILE A CG2 1 
ATOM   2579  C  CD1 . ILE A 1 343 ? 52.295 25.891 91.406  1.00 63.86  ? 407 ILE A CD1 1 
ATOM   2580  N  N   . GLU A 1 344 ? 49.283 24.669 86.590  1.00 47.42  ? 408 GLU A N   1 
ATOM   2581  C  CA  . GLU A 1 344 ? 47.989 24.482 86.020  1.00 46.45  ? 408 GLU A CA  1 
ATOM   2582  C  C   . GLU A 1 344 ? 47.049 23.735 87.000  1.00 54.82  ? 408 GLU A C   1 
ATOM   2583  O  O   . GLU A 1 344 ? 47.419 22.742 87.644  1.00 49.35  ? 408 GLU A O   1 
ATOM   2584  C  CB  . GLU A 1 344 ? 48.185 23.764 84.700  1.00 45.56  ? 408 GLU A CB  1 
ATOM   2585  C  CG  . GLU A 1 344 ? 46.958 23.611 83.806  1.00 75.77  ? 408 GLU A CG  1 
ATOM   2586  C  CD  . GLU A 1 344 ? 47.210 22.648 82.647  1.00 89.08  ? 408 GLU A CD  1 
ATOM   2587  O  OE1 . GLU A 1 344 ? 47.057 23.070 81.476  1.00 76.87  ? 408 GLU A OE1 1 
ATOM   2588  O  OE2 . GLU A 1 344 ? 47.584 21.478 82.917  1.00 96.44  ? 408 GLU A OE2 1 
ATOM   2589  N  N   . ILE A 1 345 ? 45.820 24.220 87.094  1.00 55.11  ? 409 ILE A N   1 
ATOM   2590  C  CA  . ILE A 1 345 ? 44.900 23.805 88.135  1.00 45.66  ? 409 ILE A CA  1 
ATOM   2591  C  C   . ILE A 1 345 ? 43.582 23.433 87.521  1.00 50.17  ? 409 ILE A C   1 
ATOM   2592  O  O   . ILE A 1 345 ? 43.069 24.186 86.705  1.00 65.48  ? 409 ILE A O   1 
ATOM   2593  C  CB  . ILE A 1 345 ? 44.648 25.007 89.013  1.00 45.32  ? 409 ILE A CB  1 
ATOM   2594  C  CG1 . ILE A 1 345 ? 45.908 25.310 89.834  1.00 45.05  ? 409 ILE A CG1 1 
ATOM   2595  C  CG2 . ILE A 1 345 ? 43.419 24.810 89.852  1.00 48.08  ? 409 ILE A CG2 1 
ATOM   2596  C  CD1 . ILE A 1 345 ? 45.658 26.274 90.977  1.00 60.04  ? 409 ILE A CD1 1 
ATOM   2597  N  N   . ALA A 1 346 ? 43.028 22.289 87.911  1.00 53.90  ? 410 ALA A N   1 
ATOM   2598  C  CA  . ALA A 1 346 ? 41.677 21.876 87.492  1.00 47.74  ? 410 ALA A CA  1 
ATOM   2599  C  C   . ALA A 1 346 ? 40.611 22.938 87.841  1.00 60.08  ? 410 ALA A C   1 
ATOM   2600  O  O   . ALA A 1 346 ? 40.590 23.484 88.956  1.00 52.70  ? 410 ALA A O   1 
ATOM   2601  C  CB  . ALA A 1 346 ? 41.311 20.576 88.161  1.00 41.78  ? 410 ALA A CB  1 
ATOM   2602  N  N   . ALA A 1 347 ? 39.730 23.232 86.891  1.00 69.19  ? 411 ALA A N   1 
ATOM   2603  C  CA  . ALA A 1 347 ? 38.596 24.112 87.159  1.00 70.56  ? 411 ALA A CA  1 
ATOM   2604  C  C   . ALA A 1 347 ? 37.343 23.371 86.774  1.00 73.04  ? 411 ALA A C   1 
ATOM   2605  O  O   . ALA A 1 347 ? 37.393 22.181 86.457  1.00 86.80  ? 411 ALA A O   1 
ATOM   2606  C  CB  . ALA A 1 347 ? 38.713 25.400 86.353  1.00 86.73  ? 411 ALA A CB  1 
ATOM   2607  N  N   . THR A 1 348 ? 36.221 24.075 86.810  1.00 72.16  ? 412 THR A N   1 
ATOM   2608  C  CA  . THR A 1 348 ? 35.001 23.603 86.179  1.00 73.51  ? 412 THR A CA  1 
ATOM   2609  C  C   . THR A 1 348 ? 34.238 24.819 85.630  1.00 73.80  ? 412 THR A C   1 
ATOM   2610  O  O   . THR A 1 348 ? 34.311 25.933 86.161  1.00 67.88  ? 412 THR A O   1 
ATOM   2611  C  CB  . THR A 1 348 ? 34.108 22.696 87.139  1.00 73.93  ? 412 THR A CB  1 
ATOM   2612  O  OG1 . THR A 1 348 ? 33.757 23.411 88.321  1.00 82.92  ? 412 THR A OG1 1 
ATOM   2613  C  CG2 . THR A 1 348 ? 34.816 21.408 87.581  1.00 63.15  ? 412 THR A CG2 1 
ATOM   2614  N  N   . THR A 1 349 ? 33.521 24.610 84.545  1.00 73.83  ? 413 THR A N   1 
ATOM   2615  C  CA  . THR A 1 349 ? 32.614 25.622 84.055  1.00 74.61  ? 413 THR A CA  1 
ATOM   2616  C  C   . THR A 1 349 ? 31.424 25.768 85.007  1.00 79.96  ? 413 THR A C   1 
ATOM   2617  O  O   . THR A 1 349 ? 31.226 24.942 85.898  1.00 69.35  ? 413 THR A O   1 
ATOM   2618  C  CB  . THR A 1 349 ? 32.191 25.233 82.658  1.00 87.90  ? 413 THR A CB  1 
ATOM   2619  O  OG1 . THR A 1 349 ? 33.364 25.261 81.836  1.00 119.99 ? 413 THR A OG1 1 
ATOM   2620  C  CG2 . THR A 1 349 ? 31.131 26.165 82.079  1.00 108.48 ? 413 THR A CG2 1 
ATOM   2621  N  N   . LYS A 1 350 ? 30.662 26.844 84.841  1.00 95.03  ? 414 LYS A N   1 
ATOM   2622  C  CA  . LYS A 1 350 ? 29.431 27.074 85.588  1.00 95.41  ? 414 LYS A CA  1 
ATOM   2623  C  C   . LYS A 1 350 ? 28.516 25.842 85.584  1.00 94.91  ? 414 LYS A C   1 
ATOM   2624  O  O   . LYS A 1 350 ? 27.696 25.675 86.479  1.00 103.65 ? 414 LYS A O   1 
ATOM   2625  C  CB  . LYS A 1 350 ? 28.700 28.291 85.011  1.00 138.19 ? 414 LYS A CB  1 
ATOM   2626  C  CG  . LYS A 1 350 ? 27.429 28.740 85.733  1.00 161.88 ? 414 LYS A CG  1 
ATOM   2627  C  CD  . LYS A 1 350 ? 26.655 29.749 84.883  1.00 180.87 ? 414 LYS A CD  1 
ATOM   2628  C  CE  . LYS A 1 350 ? 25.340 30.151 85.542  1.00 214.41 ? 414 LYS A CE  1 
ATOM   2629  N  NZ  . LYS A 1 350 ? 24.640 31.242 84.795  1.00 252.66 ? 414 LYS A NZ  1 
ATOM   2630  N  N   . ALA A 1 351 ? 28.651 24.978 84.586  1.00 91.89  ? 415 ALA A N   1 
ATOM   2631  C  CA  . ALA A 1 351 ? 27.907 23.729 84.593  1.00 90.53  ? 415 ALA A CA  1 
ATOM   2632  C  C   . ALA A 1 351 ? 28.738 22.573 84.040  1.00 101.98 ? 415 ALA A C   1 
ATOM   2633  O  O   . ALA A 1 351 ? 28.736 22.350 82.835  1.00 124.64 ? 415 ALA A O   1 
ATOM   2634  C  CB  . ALA A 1 351 ? 26.632 23.894 83.797  1.00 101.33 ? 415 ALA A CB  1 
ATOM   2635  N  N   . GLY A 1 352 ? 29.447 21.848 84.915  1.00 104.92 ? 416 GLY A N   1 
ATOM   2636  C  CA  . GLY A 1 352 ? 30.326 20.714 84.520  1.00 81.59  ? 416 GLY A CA  1 
ATOM   2637  C  C   . GLY A 1 352 ? 31.549 21.168 83.752  1.00 90.26  ? 416 GLY A C   1 
ATOM   2638  O  O   . GLY A 1 352 ? 31.848 22.365 83.726  1.00 121.35 ? 416 GLY A O   1 
ATOM   2639  N  N   . LEU A 1 353 ? 32.262 20.228 83.125  1.00 95.24  ? 417 LEU A N   1 
ATOM   2640  C  CA  . LEU A 1 353 ? 33.395 20.547 82.208  1.00 85.36  ? 417 LEU A CA  1 
ATOM   2641  C  C   . LEU A 1 353 ? 34.698 20.873 82.943  1.00 77.17  ? 417 LEU A C   1 
ATOM   2642  O  O   . LEU A 1 353 ? 34.679 21.514 83.983  1.00 85.96  ? 417 LEU A O   1 
ATOM   2643  C  CB  . LEU A 1 353 ? 33.029 21.681 81.233  1.00 74.42  ? 417 LEU A CB  1 
ATOM   2644  C  CG  . LEU A 1 353 ? 31.547 21.738 80.790  1.00 74.19  ? 417 LEU A CG  1 
ATOM   2645  C  CD1 . LEU A 1 353 ? 31.110 23.079 80.179  1.00 81.44  ? 417 LEU A CD1 1 
ATOM   2646  C  CD2 . LEU A 1 353 ? 31.200 20.610 79.861  1.00 64.56  ? 417 LEU A CD2 1 
ATOM   2647  N  N   . SER A 1 354 ? 35.827 20.448 82.388  1.00 70.06  ? 418 SER A N   1 
ATOM   2648  C  CA  . SER A 1 354 ? 37.066 20.487 83.123  1.00 82.77  ? 418 SER A CA  1 
ATOM   2649  C  C   . SER A 1 354 ? 38.102 21.373 82.453  1.00 90.37  ? 418 SER A C   1 
ATOM   2650  O  O   . SER A 1 354 ? 39.155 20.910 82.034  1.00 148.21 ? 418 SER A O   1 
ATOM   2651  C  CB  . SER A 1 354 ? 37.601 19.066 83.289  1.00 111.53 ? 418 SER A CB  1 
ATOM   2652  O  OG  . SER A 1 354 ? 37.783 18.453 82.019  1.00 142.45 ? 418 SER A OG  1 
ATOM   2653  N  N   . SER A 1 355 ? 37.814 22.655 82.342  1.00 97.65  ? 419 SER A N   1 
ATOM   2654  C  CA  . SER A 1 355 ? 38.846 23.584 81.918  1.00 97.59  ? 419 SER A CA  1 
ATOM   2655  C  C   . SER A 1 355 ? 39.914 23.614 83.026  1.00 85.85  ? 419 SER A C   1 
ATOM   2656  O  O   . SER A 1 355 ? 39.696 23.132 84.144  1.00 82.39  ? 419 SER A O   1 
ATOM   2657  C  CB  . SER A 1 355 ? 38.252 24.980 81.622  1.00 106.82 ? 419 SER A CB  1 
ATOM   2658  O  OG  . SER A 1 355 ? 39.164 25.836 80.935  1.00 97.76  ? 419 SER A OG  1 
ATOM   2659  N  N   . ASN A 1 356 ? 41.082 24.139 82.691  1.00 75.99  ? 420 ASN A N   1 
ATOM   2660  C  CA  . ASN A 1 356 ? 42.119 24.369 83.665  1.00 68.90  ? 420 ASN A CA  1 
ATOM   2661  C  C   . ASN A 1 356 ? 42.399 25.851 83.769  1.00 70.58  ? 420 ASN A C   1 
ATOM   2662  O  O   . ASN A 1 356 ? 42.197 26.584 82.800  1.00 103.18 ? 420 ASN A O   1 
ATOM   2663  C  CB  . ASN A 1 356 ? 43.404 23.642 83.256  1.00 82.42  ? 420 ASN A CB  1 
ATOM   2664  C  CG  . ASN A 1 356 ? 43.152 22.246 82.780  1.00 73.73  ? 420 ASN A CG  1 
ATOM   2665  O  OD1 . ASN A 1 356 ? 42.619 22.038 81.694  1.00 83.92  ? 420 ASN A OD1 1 
ATOM   2666  N  ND2 . ASN A 1 356 ? 43.538 21.273 83.589  1.00 82.48  ? 420 ASN A ND2 1 
ATOM   2667  N  N   . ASP A 1 357 ? 42.863 26.298 84.938  1.00 74.75  ? 421 ASP A N   1 
ATOM   2668  C  CA  . ASP A 1 357 ? 43.394 27.654 85.061  1.00 76.27  ? 421 ASP A CA  1 
ATOM   2669  C  C   . ASP A 1 357 ? 44.797 27.708 85.616  1.00 64.32  ? 421 ASP A C   1 
ATOM   2670  O  O   . ASP A 1 357 ? 45.358 26.706 86.033  1.00 58.61  ? 421 ASP A O   1 
ATOM   2671  C  CB  . ASP A 1 357 ? 42.476 28.586 85.849  1.00 74.50  ? 421 ASP A CB  1 
ATOM   2672  C  CG  . ASP A 1 357 ? 42.269 29.942 85.140  1.00 116.19 ? 421 ASP A CG  1 
ATOM   2673  O  OD1 . ASP A 1 357 ? 43.248 30.537 84.608  1.00 91.58  ? 421 ASP A OD1 1 
ATOM   2674  O  OD2 . ASP A 1 357 ? 41.110 30.413 85.110  1.00 126.49 ? 421 ASP A OD2 1 
ATOM   2675  N  N   . LEU A 1 358 ? 45.347 28.912 85.610  1.00 68.73  ? 422 LEU A N   1 
ATOM   2676  C  CA  . LEU A 1 358 ? 46.733 29.134 85.907  1.00 55.29  ? 422 LEU A CA  1 
ATOM   2677  C  C   . LEU A 1 358 ? 46.872 29.913 87.174  1.00 66.70  ? 422 LEU A C   1 
ATOM   2678  O  O   . LEU A 1 358 ? 46.008 30.743 87.513  1.00 72.71  ? 422 LEU A O   1 
ATOM   2679  C  CB  . LEU A 1 358 ? 47.363 29.951 84.791  1.00 50.88  ? 422 LEU A CB  1 
ATOM   2680  C  CG  . LEU A 1 358 ? 47.960 29.150 83.675  1.00 48.26  ? 422 LEU A CG  1 
ATOM   2681  C  CD1 . LEU A 1 358 ? 48.955 30.020 82.949  1.00 55.86  ? 422 LEU A CD1 1 
ATOM   2682  C  CD2 . LEU A 1 358 ? 48.657 28.014 84.352  1.00 49.66  ? 422 LEU A CD2 1 
ATOM   2683  N  N   . ILE A 1 359 ? 47.972 29.637 87.867  1.00 60.69  ? 423 ILE A N   1 
ATOM   2684  C  CA  . ILE A 1 359 ? 48.476 30.525 88.894  1.00 53.27  ? 423 ILE A CA  1 
ATOM   2685  C  C   . ILE A 1 359 ? 49.959 30.592 88.661  1.00 47.29  ? 423 ILE A C   1 
ATOM   2686  O  O   . ILE A 1 359 ? 50.554 29.616 88.229  1.00 46.28  ? 423 ILE A O   1 
ATOM   2687  C  CB  . ILE A 1 359 ? 48.120 30.061 90.318  1.00 47.85  ? 423 ILE A CB  1 
ATOM   2688  C  CG1 . ILE A 1 359 ? 48.838 30.942 91.327  1.00 56.68  ? 423 ILE A CG1 1 
ATOM   2689  C  CG2 . ILE A 1 359 ? 48.457 28.593 90.543  1.00 35.53  ? 423 ILE A CG2 1 
ATOM   2690  C  CD1 . ILE A 1 359 ? 48.067 31.132 92.588  1.00 71.70  ? 423 ILE A CD1 1 
ATOM   2691  N  N   . THR A 1 360 ? 50.547 31.751 88.913  1.00 47.19  ? 424 THR A N   1 
ATOM   2692  C  CA  . THR A 1 360 ? 51.959 31.937 88.650  1.00 45.13  ? 424 THR A CA  1 
ATOM   2693  C  C   . THR A 1 360 ? 52.615 32.559 89.874  1.00 46.84  ? 424 THR A C   1 
ATOM   2694  O  O   . THR A 1 360 ? 52.008 33.407 90.553  1.00 43.76  ? 424 THR A O   1 
ATOM   2695  C  CB  . THR A 1 360 ? 52.168 32.886 87.465  1.00 51.27  ? 424 THR A CB  1 
ATOM   2696  O  OG1 . THR A 1 360 ? 52.069 34.240 87.916  1.00 71.19  ? 424 THR A OG1 1 
ATOM   2697  C  CG2 . THR A 1 360 ? 51.096 32.684 86.456  1.00 55.40  ? 424 THR A CG2 1 
ATOM   2698  N  N   . PHE A 1 361 ? 53.858 32.154 90.121  1.00 38.49  ? 425 PHE A N   1 
ATOM   2699  C  CA  . PHE A 1 361 ? 54.651 32.613 91.248  1.00 36.70  ? 425 PHE A CA  1 
ATOM   2700  C  C   . PHE A 1 361 ? 55.922 33.200 90.747  1.00 43.63  ? 425 PHE A C   1 
ATOM   2701  O  O   . PHE A 1 361 ? 56.521 32.660 89.833  1.00 46.02  ? 425 PHE A O   1 
ATOM   2702  C  CB  . PHE A 1 361 ? 55.004 31.421 92.151  1.00 29.53  ? 425 PHE A CB  1 
ATOM   2703  C  CG  . PHE A 1 361 ? 53.819 30.896 92.891  1.00 33.61  ? 425 PHE A CG  1 
ATOM   2704  C  CD1 . PHE A 1 361 ? 53.082 29.844 92.374  1.00 27.32  ? 425 PHE A CD1 1 
ATOM   2705  C  CD2 . PHE A 1 361 ? 53.365 31.519 94.052  1.00 32.67  ? 425 PHE A CD2 1 
ATOM   2706  C  CE1 . PHE A 1 361 ? 51.954 29.372 93.027  1.00 27.94  ? 425 PHE A CE1 1 
ATOM   2707  C  CE2 . PHE A 1 361 ? 52.246 31.040 94.698  1.00 35.84  ? 425 PHE A CE2 1 
ATOM   2708  C  CZ  . PHE A 1 361 ? 51.541 29.956 94.178  1.00 31.68  ? 425 PHE A CZ  1 
ATOM   2709  N  N   . CYS A 1 362 ? 56.363 34.288 91.355  1.00 53.80  ? 426 CYS A N   1 
ATOM   2710  C  CA  . CYS A 1 362 ? 57.695 34.783 91.077  1.00 52.54  ? 426 CYS A CA  1 
ATOM   2711  C  C   . CYS A 1 362 ? 58.539 34.717 92.306  1.00 49.65  ? 426 CYS A C   1 
ATOM   2712  O  O   . CYS A 1 362 ? 58.032 34.759 93.420  1.00 64.62  ? 426 CYS A O   1 
ATOM   2713  C  CB  . CYS A 1 362 ? 57.653 36.168 90.444  1.00 54.36  ? 426 CYS A CB  1 
ATOM   2714  S  SG  . CYS A 1 362 ? 56.936 35.949 88.792  1.00 124.35 ? 426 CYS A SG  1 
ATOM   2715  N  N   . GLY A 1 363 ? 59.838 34.569 92.099  1.00 52.25  ? 427 GLY A N   1 
ATOM   2716  C  CA  . GLY A 1 363 ? 60.774 34.453 93.214  1.00 51.26  ? 427 GLY A CA  1 
ATOM   2717  C  C   . GLY A 1 363 ? 61.130 35.801 93.787  1.00 57.73  ? 427 GLY A C   1 
ATOM   2718  O  O   . GLY A 1 363 ? 61.290 36.767 93.041  1.00 80.12  ? 427 GLY A O   1 
ATOM   2719  N  N   . THR A 1 364 ? 61.215 35.864 95.114  1.00 67.85  ? 428 THR A N   1 
ATOM   2720  C  CA  . THR A 1 364 ? 61.793 37.008 95.802  1.00 91.30  ? 428 THR A CA  1 
ATOM   2721  C  C   . THR A 1 364 ? 63.066 36.567 96.521  1.00 90.77  ? 428 THR A C   1 
ATOM   2722  O  O   . THR A 1 364 ? 63.253 35.356 96.790  1.00 55.48  ? 428 THR A O   1 
ATOM   2723  C  CB  . THR A 1 364 ? 60.792 37.721 96.761  1.00 96.88  ? 428 THR A CB  1 
ATOM   2724  O  OG1 . THR A 1 364 ? 61.373 38.941 97.257  1.00 114.77 ? 428 THR A OG1 1 
ATOM   2725  C  CG2 . THR A 1 364 ? 60.423 36.825 97.923  1.00 64.46  ? 428 THR A CG2 1 
ATOM   2726  N  N   . GLY A 1 365 ? 63.935 37.558 96.774  1.00 98.98  ? 429 GLY A N   1 
ATOM   2727  C  CA  . GLY A 1 365 ? 65.212 37.381 97.465  1.00 75.64  ? 429 GLY A CA  1 
ATOM   2728  C  C   . GLY A 1 365 ? 64.971 37.124 98.935  1.00 76.88  ? 429 GLY A C   1 
ATOM   2729  O  O   . GLY A 1 365 ? 65.742 36.420 99.608  1.00 85.74  ? 429 GLY A O   1 
ATOM   2730  N  N   . GLY A 1 366 ? 63.877 37.683 99.433  1.00 67.85  ? 430 GLY A N   1 
ATOM   2731  C  CA  . GLY A 1 366 ? 63.551 37.552 100.843 1.00 89.28  ? 430 GLY A CA  1 
ATOM   2732  C  C   . GLY A 1 366 ? 62.989 36.177 101.181 1.00 74.55  ? 430 GLY A C   1 
ATOM   2733  O  O   . GLY A 1 366 ? 62.451 35.470 100.344 1.00 50.85  ? 430 GLY A O   1 
ATOM   2734  N  N   . SER A 1 367 ? 63.102 35.788 102.432 1.00 81.77  ? 431 SER A N   1 
ATOM   2735  C  CA  . SER A 1 367 ? 62.353 34.637 102.873 1.00 57.37  ? 431 SER A CA  1 
ATOM   2736  C  C   . SER A 1 367 ? 60.895 35.035 103.033 1.00 58.24  ? 431 SER A C   1 
ATOM   2737  O  O   . SER A 1 367 ? 60.555 36.207 103.215 1.00 98.56  ? 431 SER A O   1 
ATOM   2738  C  CB  . SER A 1 367 ? 62.918 34.129 104.190 1.00 65.81  ? 431 SER A CB  1 
ATOM   2739  O  OG  . SER A 1 367 ? 62.198 33.002 104.614 1.00 60.84  ? 431 SER A OG  1 
ATOM   2740  N  N   . MET A 1 368 ? 60.024 34.054 102.980 1.00 59.47  ? 432 MET A N   1 
ATOM   2741  C  CA  . MET A 1 368 ? 58.610 34.338 103.047 1.00 63.63  ? 432 MET A CA  1 
ATOM   2742  C  C   . MET A 1 368 ? 57.924 33.451 104.046 1.00 68.12  ? 432 MET A C   1 
ATOM   2743  O  O   . MET A 1 368 ? 58.356 32.318 104.256 1.00 62.96  ? 432 MET A O   1 
ATOM   2744  C  CB  . MET A 1 368 ? 57.989 34.120 101.690 1.00 57.02  ? 432 MET A CB  1 
ATOM   2745  C  CG  . MET A 1 368 ? 58.302 35.230 100.699 1.00 64.86  ? 432 MET A CG  1 
ATOM   2746  S  SD  . MET A 1 368 ? 57.016 36.472 100.660 1.00 67.18  ? 432 MET A SD  1 
ATOM   2747  C  CE  . MET A 1 368 ? 55.509 35.521 100.837 1.00 60.58  ? 432 MET A CE  1 
ATOM   2748  N  N   . PRO A 1 369 ? 56.844 33.960 104.663 1.00 80.50  ? 433 PRO A N   1 
ATOM   2749  C  CA  . PRO A 1 369 ? 56.080 33.217 105.651 1.00 70.02  ? 433 PRO A CA  1 
ATOM   2750  C  C   . PRO A 1 369 ? 55.286 32.075 105.009 1.00 65.83  ? 433 PRO A C   1 
ATOM   2751  O  O   . PRO A 1 369 ? 55.136 32.022 103.789 1.00 56.59  ? 433 PRO A O   1 
ATOM   2752  C  CB  . PRO A 1 369 ? 55.112 34.273 106.183 1.00 80.55  ? 433 PRO A CB  1 
ATOM   2753  C  CG  . PRO A 1 369 ? 54.860 35.131 105.006 1.00 85.85  ? 433 PRO A CG  1 
ATOM   2754  C  CD  . PRO A 1 369 ? 56.209 35.257 104.360 1.00 90.43  ? 433 PRO A CD  1 
ATOM   2755  N  N   . ASP A 1 370 ? 54.776 31.174 105.841 1.00 79.44  ? 434 ASP A N   1 
ATOM   2756  C  CA  . ASP A 1 370 ? 53.978 30.055 105.370 1.00 70.04  ? 434 ASP A CA  1 
ATOM   2757  C  C   . ASP A 1 370 ? 52.617 30.569 104.952 1.00 77.65  ? 434 ASP A C   1 
ATOM   2758  O  O   . ASP A 1 370 ? 51.944 31.270 105.723 1.00 78.69  ? 434 ASP A O   1 
ATOM   2759  C  CB  . ASP A 1 370 ? 53.838 28.990 106.456 1.00 62.87  ? 434 ASP A CB  1 
ATOM   2760  C  CG  . ASP A 1 370 ? 55.157 28.361 106.815 1.00 86.05  ? 434 ASP A CG  1 
ATOM   2761  O  OD1 . ASP A 1 370 ? 56.038 28.272 105.927 1.00 94.54  ? 434 ASP A OD1 1 
ATOM   2762  O  OD2 . ASP A 1 370 ? 55.320 27.959 107.990 1.00 107.01 ? 434 ASP A OD2 1 
ATOM   2763  N  N   . VAL A 1 371 ? 52.226 30.246 103.720 1.00 63.99  ? 435 VAL A N   1 
ATOM   2764  C  CA  . VAL A 1 371 ? 50.920 30.633 103.232 1.00 55.91  ? 435 VAL A CA  1 
ATOM   2765  C  C   . VAL A 1 371 ? 50.363 29.555 102.311 1.00 64.14  ? 435 VAL A C   1 
ATOM   2766  O  O   . VAL A 1 371 ? 51.058 29.013 101.441 1.00 54.66  ? 435 VAL A O   1 
ATOM   2767  C  CB  . VAL A 1 371 ? 50.969 31.968 102.435 1.00 61.72  ? 435 VAL A CB  1 
ATOM   2768  C  CG1 . VAL A 1 371 ? 49.585 32.435 102.133 1.00 79.57  ? 435 VAL A CG1 1 
ATOM   2769  C  CG2 . VAL A 1 371 ? 51.750 33.055 103.168 1.00 54.68  ? 435 VAL A CG2 1 
ATOM   2770  N  N   . ASN A 1 372 ? 49.088 29.261 102.513 1.00 67.95  ? 436 ASN A N   1 
ATOM   2771  C  CA  . ASN A 1 372 ? 48.308 28.460 101.598 1.00 57.37  ? 436 ASN A CA  1 
ATOM   2772  C  C   . ASN A 1 372 ? 47.491 29.415 100.714 1.00 60.41  ? 436 ASN A C   1 
ATOM   2773  O  O   . ASN A 1 372 ? 46.551 30.039 101.200 1.00 76.90  ? 436 ASN A O   1 
ATOM   2774  C  CB  . ASN A 1 372 ? 47.386 27.547 102.420 1.00 56.12  ? 436 ASN A CB  1 
ATOM   2775  C  CG  . ASN A 1 372 ? 46.392 26.768 101.568 1.00 79.20  ? 436 ASN A CG  1 
ATOM   2776  O  OD1 . ASN A 1 372 ? 46.284 26.933 100.340 1.00 84.44  ? 436 ASN A OD1 1 
ATOM   2777  N  ND2 . ASN A 1 372 ? 45.648 25.904 102.230 1.00 111.34 ? 436 ASN A ND2 1 
ATOM   2778  N  N   . TRP A 1 373 ? 47.841 29.525 99.433  1.00 48.31  ? 437 TRP A N   1 
ATOM   2779  C  CA  . TRP A 1 373 ? 47.086 30.341 98.448  1.00 56.85  ? 437 TRP A CA  1 
ATOM   2780  C  C   . TRP A 1 373 ? 45.793 29.752 97.876  1.00 62.02  ? 437 TRP A C   1 
ATOM   2781  O  O   . TRP A 1 373 ? 45.541 28.535 97.918  1.00 64.17  ? 437 TRP A O   1 
ATOM   2782  C  CB  . TRP A 1 373 ? 48.010 30.760 97.308  1.00 53.02  ? 437 TRP A CB  1 
ATOM   2783  C  CG  . TRP A 1 373 ? 49.224 31.485 97.810  1.00 54.45  ? 437 TRP A CG  1 
ATOM   2784  C  CD1 . TRP A 1 373 ? 50.487 30.965 98.082  1.00 65.40  ? 437 TRP A CD1 1 
ATOM   2785  C  CD2 . TRP A 1 373 ? 49.312 32.877 98.182  1.00 56.60  ? 437 TRP A CD2 1 
ATOM   2786  N  NE1 . TRP A 1 373 ? 51.331 31.938 98.572  1.00 50.47  ? 437 TRP A NE1 1 
ATOM   2787  C  CE2 . TRP A 1 373 ? 50.690 33.095 98.662  1.00 59.05  ? 437 TRP A CE2 1 
ATOM   2788  C  CE3 . TRP A 1 373 ? 48.430 33.935 98.168  1.00 57.88  ? 437 TRP A CE3 1 
ATOM   2789  C  CZ2 . TRP A 1 373 ? 51.128 34.328 99.076  1.00 66.28  ? 437 TRP A CZ2 1 
ATOM   2790  C  CZ3 . TRP A 1 373 ? 48.882 35.178 98.594  1.00 48.97  ? 437 TRP A CZ3 1 
ATOM   2791  C  CH2 . TRP A 1 373 ? 50.199 35.373 99.028  1.00 52.52  ? 437 TRP A CH2 1 
ATOM   2792  N  N   . ALA B 1 11  ? 47.542 68.406 67.235  1.00 109.66 ? 75  ALA B N   1 
ATOM   2793  C  CA  . ALA B 1 11  ? 46.088 68.735 66.983  1.00 111.89 ? 75  ALA B CA  1 
ATOM   2794  C  C   . ALA B 1 11  ? 45.868 70.198 66.582  1.00 128.21 ? 75  ALA B C   1 
ATOM   2795  O  O   . ALA B 1 11  ? 46.572 71.105 67.045  1.00 138.70 ? 75  ALA B O   1 
ATOM   2796  C  CB  . ALA B 1 11  ? 45.184 68.361 68.190  1.00 88.63  ? 75  ALA B CB  1 
ATOM   2797  N  N   . THR B 1 12  ? 44.871 70.406 65.723  1.00 130.83 ? 76  THR B N   1 
ATOM   2798  C  CA  . THR B 1 12  ? 44.589 71.699 65.108  1.00 121.94 ? 76  THR B CA  1 
ATOM   2799  C  C   . THR B 1 12  ? 43.106 72.026 65.247  1.00 122.17 ? 76  THR B C   1 
ATOM   2800  O  O   . THR B 1 12  ? 42.259 71.149 65.048  1.00 116.08 ? 76  THR B O   1 
ATOM   2801  C  CB  . THR B 1 12  ? 44.978 71.680 63.610  1.00 133.16 ? 76  THR B CB  1 
ATOM   2802  O  OG1 . THR B 1 12  ? 46.378 71.400 63.492  1.00 200.10 ? 76  THR B OG1 1 
ATOM   2803  C  CG2 . THR B 1 12  ? 44.668 73.013 62.915  1.00 128.22 ? 76  THR B CG2 1 
ATOM   2804  N  N   . PRO B 1 13  ? 42.783 73.292 65.585  1.00 128.42 ? 77  PRO B N   1 
ATOM   2805  C  CA  . PRO B 1 13  ? 41.386 73.704 65.698  1.00 113.58 ? 77  PRO B CA  1 
ATOM   2806  C  C   . PRO B 1 13  ? 40.604 73.240 64.481  1.00 116.44 ? 77  PRO B C   1 
ATOM   2807  O  O   . PRO B 1 13  ? 41.054 73.438 63.349  1.00 124.33 ? 77  PRO B O   1 
ATOM   2808  C  CB  . PRO B 1 13  ? 41.468 75.234 65.722  1.00 103.00 ? 77  PRO B CB  1 
ATOM   2809  C  CG  . PRO B 1 13  ? 42.802 75.534 66.278  1.00 107.26 ? 77  PRO B CG  1 
ATOM   2810  C  CD  . PRO B 1 13  ? 43.710 74.410 65.851  1.00 121.15 ? 77  PRO B CD  1 
ATOM   2811  N  N   . LEU B 1 14  ? 39.460 72.603 64.727  1.00 130.62 ? 78  LEU B N   1 
ATOM   2812  C  CA  . LEU B 1 14  ? 38.575 72.141 63.659  1.00 118.03 ? 78  LEU B CA  1 
ATOM   2813  C  C   . LEU B 1 14  ? 38.049 73.297 62.814  1.00 108.84 ? 78  LEU B C   1 
ATOM   2814  O  O   . LEU B 1 14  ? 37.398 74.228 63.323  1.00 117.64 ? 78  LEU B O   1 
ATOM   2815  C  CB  . LEU B 1 14  ? 37.402 71.339 64.224  1.00 120.98 ? 78  LEU B CB  1 
ATOM   2816  C  CG  . LEU B 1 14  ? 36.468 70.751 63.164  1.00 103.01 ? 78  LEU B CG  1 
ATOM   2817  C  CD1 . LEU B 1 14  ? 37.105 69.499 62.576  1.00 89.41  ? 78  LEU B CD1 1 
ATOM   2818  C  CD2 . LEU B 1 14  ? 35.084 70.464 63.750  1.00 82.59  ? 78  LEU B CD2 1 
ATOM   2819  N  N   . VAL B 1 15  ? 38.354 73.218 61.523  1.00 87.58  ? 79  VAL B N   1 
ATOM   2820  C  CA  . VAL B 1 15  ? 37.918 74.196 60.549  1.00 92.24  ? 79  VAL B CA  1 
ATOM   2821  C  C   . VAL B 1 15  ? 36.950 73.503 59.593  1.00 94.65  ? 79  VAL B C   1 
ATOM   2822  O  O   . VAL B 1 15  ? 37.257 72.448 59.043  1.00 94.04  ? 79  VAL B O   1 
ATOM   2823  C  CB  . VAL B 1 15  ? 39.131 74.815 59.790  1.00 87.06  ? 79  VAL B CB  1 
ATOM   2824  C  CG1 . VAL B 1 15  ? 38.770 75.160 58.339  1.00 107.08 ? 79  VAL B CG1 1 
ATOM   2825  C  CG2 . VAL B 1 15  ? 39.658 76.038 60.518  1.00 91.38  ? 79  VAL B CG2 1 
ATOM   2826  N  N   . LEU B 1 16  ? 35.771 74.080 59.409  1.00 90.05  ? 80  LEU B N   1 
ATOM   2827  C  CA  . LEU B 1 16  ? 34.836 73.524 58.449  1.00 90.74  ? 80  LEU B CA  1 
ATOM   2828  C  C   . LEU B 1 16  ? 34.934 74.249 57.110  1.00 106.98 ? 80  LEU B C   1 
ATOM   2829  O  O   . LEU B 1 16  ? 35.350 75.423 57.056  1.00 107.34 ? 80  LEU B O   1 
ATOM   2830  C  CB  . LEU B 1 16  ? 33.417 73.587 58.990  1.00 95.63  ? 80  LEU B CB  1 
ATOM   2831  C  CG  . LEU B 1 16  ? 33.132 72.695 60.194  1.00 112.34 ? 80  LEU B CG  1 
ATOM   2832  C  CD1 . LEU B 1 16  ? 31.827 73.107 60.852  1.00 107.15 ? 80  LEU B CD1 1 
ATOM   2833  C  CD2 . LEU B 1 16  ? 33.102 71.227 59.801  1.00 134.76 ? 80  LEU B CD2 1 
ATOM   2834  N  N   . GLY B 1 17  ? 34.563 73.538 56.039  1.00 87.72  ? 81  GLY B N   1 
ATOM   2835  C  CA  . GLY B 1 17  ? 34.532 74.101 54.686  1.00 77.87  ? 81  GLY B CA  1 
ATOM   2836  C  C   . GLY B 1 17  ? 33.522 75.235 54.560  1.00 83.74  ? 81  GLY B C   1 
ATOM   2837  O  O   . GLY B 1 17  ? 32.376 75.156 55.055  1.00 87.11  ? 81  GLY B O   1 
ATOM   2838  N  N   . GLU B 1 18  ? 33.931 76.305 53.896  1.00 95.87  ? 82  GLU B N   1 
ATOM   2839  C  CA  . GLU B 1 18  ? 33.027 77.435 53.719  1.00 112.18 ? 82  GLU B CA  1 
ATOM   2840  C  C   . GLU B 1 18  ? 31.912 77.093 52.725  1.00 108.93 ? 82  GLU B C   1 
ATOM   2841  O  O   . GLU B 1 18  ? 30.777 77.528 52.887  1.00 98.95  ? 82  GLU B O   1 
ATOM   2842  C  CB  . GLU B 1 18  ? 33.804 78.684 53.298  1.00 115.36 ? 82  GLU B CB  1 
ATOM   2843  C  CG  . GLU B 1 18  ? 33.329 79.964 53.982  1.00 132.58 ? 82  GLU B CG  1 
ATOM   2844  C  CD  . GLU B 1 18  ? 33.643 80.007 55.479  1.00 127.14 ? 82  GLU B CD  1 
ATOM   2845  O  OE1 . GLU B 1 18  ? 34.609 79.357 55.932  1.00 116.57 ? 82  GLU B OE1 1 
ATOM   2846  O  OE2 . GLU B 1 18  ? 32.918 80.706 56.209  1.00 134.66 ? 82  GLU B OE2 1 
ATOM   2847  N  N   . ASN B 1 19  ? 32.250 76.278 51.725  1.00 115.70 ? 83  ASN B N   1 
ATOM   2848  C  CA  . ASN B 1 19  ? 31.340 75.938 50.645  1.00 104.63 ? 83  ASN B CA  1 
ATOM   2849  C  C   . ASN B 1 19  ? 30.800 74.539 50.781  1.00 97.17  ? 83  ASN B C   1 
ATOM   2850  O  O   . ASN B 1 19  ? 31.553 73.596 50.988  1.00 121.96 ? 83  ASN B O   1 
ATOM   2851  C  CB  . ASN B 1 19  ? 32.031 76.129 49.293  1.00 109.10 ? 83  ASN B CB  1 
ATOM   2852  C  CG  . ASN B 1 19  ? 32.307 77.595 48.989  1.00 133.42 ? 83  ASN B CG  1 
ATOM   2853  O  OD1 . ASN B 1 19  ? 31.556 78.482 49.407  1.00 132.48 ? 83  ASN B OD1 1 
ATOM   2854  N  ND2 . ASN B 1 19  ? 33.386 77.856 48.261  1.00 145.90 ? 83  ASN B ND2 1 
ATOM   2855  N  N   . LEU B 1 20  ? 29.488 74.410 50.658  1.00 94.18  ? 84  LEU B N   1 
ATOM   2856  C  CA  . LEU B 1 20  ? 28.814 73.115 50.757  1.00 87.17  ? 84  LEU B CA  1 
ATOM   2857  C  C   . LEU B 1 20  ? 28.903 72.297 49.473  1.00 85.47  ? 84  LEU B C   1 
ATOM   2858  O  O   . LEU B 1 20  ? 28.844 72.852 48.378  1.00 116.71 ? 84  LEU B O   1 
ATOM   2859  C  CB  . LEU B 1 20  ? 27.342 73.347 51.082  1.00 79.85  ? 84  LEU B CB  1 
ATOM   2860  C  CG  . LEU B 1 20  ? 26.712 72.479 52.165  1.00 74.42  ? 84  LEU B CG  1 
ATOM   2861  C  CD1 . LEU B 1 20  ? 27.446 72.626 53.470  1.00 81.04  ? 84  LEU B CD1 1 
ATOM   2862  C  CD2 . LEU B 1 20  ? 25.247 72.837 52.343  1.00 69.98  ? 84  LEU B CD2 1 
ATOM   2863  N  N   . CYS B 1 21  ? 29.028 70.980 49.619  1.00 90.08  ? 85  CYS B N   1 
ATOM   2864  C  CA  . CYS B 1 21  ? 28.962 70.040 48.496  1.00 88.11  ? 85  CYS B CA  1 
ATOM   2865  C  C   . CYS B 1 21  ? 27.630 70.168 47.828  1.00 77.07  ? 85  CYS B C   1 
ATOM   2866  O  O   . CYS B 1 21  ? 26.651 70.451 48.515  1.00 76.93  ? 85  CYS B O   1 
ATOM   2867  C  CB  . CYS B 1 21  ? 29.123 68.614 49.007  1.00 102.46 ? 85  CYS B CB  1 
ATOM   2868  S  SG  . CYS B 1 21  ? 30.822 68.248 49.260  1.00 236.62 ? 85  CYS B SG  1 
ATOM   2869  N  N   . SER B 1 22  ? 27.585 69.989 46.505  1.00 70.16  ? 86  SER B N   1 
ATOM   2870  C  CA  . SER B 1 22  ? 26.300 69.942 45.815  1.00 87.39  ? 86  SER B CA  1 
ATOM   2871  C  C   . SER B 1 22  ? 25.718 68.605 46.164  1.00 89.61  ? 86  SER B C   1 
ATOM   2872  O  O   . SER B 1 22  ? 26.425 67.597 46.085  1.00 94.38  ? 86  SER B O   1 
ATOM   2873  C  CB  . SER B 1 22  ? 26.458 70.045 44.305  1.00 98.74  ? 86  SER B CB  1 
ATOM   2874  O  OG  . SER B 1 22  ? 26.935 71.323 43.936  1.00 137.96 ? 86  SER B OG  1 
ATOM   2875  N  N   . ILE B 1 23  ? 24.455 68.602 46.588  1.00 71.16  ? 87  ILE B N   1 
ATOM   2876  C  CA  . ILE B 1 23  ? 23.786 67.378 46.971  1.00 62.19  ? 87  ILE B CA  1 
ATOM   2877  C  C   . ILE B 1 23  ? 22.621 67.154 46.016  1.00 69.24  ? 87  ILE B C   1 
ATOM   2878  O  O   . ILE B 1 23  ? 21.718 68.012 45.919  1.00 69.37  ? 87  ILE B O   1 
ATOM   2879  C  CB  . ILE B 1 23  ? 23.323 67.463 48.412  1.00 68.03  ? 87  ILE B CB  1 
ATOM   2880  C  CG1 . ILE B 1 23  ? 24.538 67.381 49.316  1.00 73.21  ? 87  ILE B CG1 1 
ATOM   2881  C  CG2 . ILE B 1 23  ? 22.386 66.312 48.748  1.00 111.26 ? 87  ILE B CG2 1 
ATOM   2882  C  CD1 . ILE B 1 23  ? 24.489 68.324 50.479  1.00 109.06 ? 87  ILE B CD1 1 
ATOM   2883  N  N   . ASN B 1 24  ? 22.665 66.035 45.282  1.00 48.88  ? 88  ASN B N   1 
ATOM   2884  C  CA  . ASN B 1 24  ? 21.542 65.693 44.446  1.00 50.40  ? 88  ASN B CA  1 
ATOM   2885  C  C   . ASN B 1 24  ? 20.912 64.365 44.789  1.00 52.94  ? 88  ASN B C   1 
ATOM   2886  O  O   . ASN B 1 24  ? 19.951 63.943 44.144  1.00 59.24  ? 88  ASN B O   1 
ATOM   2887  C  CB  . ASN B 1 24  ? 21.911 65.753 42.983  1.00 55.03  ? 88  ASN B CB  1 
ATOM   2888  C  CG  . ASN B 1 24  ? 22.173 67.180 42.505  1.00 62.97  ? 88  ASN B CG  1 
ATOM   2889  O  OD1 . ASN B 1 24  ? 21.264 67.927 42.153  1.00 59.60  ? 88  ASN B OD1 1 
ATOM   2890  N  ND2 . ASN B 1 24  ? 23.431 67.551 42.487  1.00 83.57  ? 88  ASN B ND2 1 
ATOM   2891  N  N   . GLY B 1 25  ? 21.445 63.710 45.814  1.00 48.83  ? 89  GLY B N   1 
ATOM   2892  C  CA  . GLY B 1 25  ? 20.928 62.406 46.223  1.00 54.09  ? 89  GLY B CA  1 
ATOM   2893  C  C   . GLY B 1 25  ? 21.418 62.022 47.594  1.00 56.03  ? 89  GLY B C   1 
ATOM   2894  O  O   . GLY B 1 25  ? 22.220 62.740 48.182  1.00 62.77  ? 89  GLY B O   1 
ATOM   2895  N  N   . TRP B 1 26  ? 20.934 60.904 48.125  1.00 48.95  ? 90  TRP B N   1 
ATOM   2896  C  CA  . TRP B 1 26  ? 21.399 60.486 49.436  1.00 45.27  ? 90  TRP B CA  1 
ATOM   2897  C  C   . TRP B 1 26  ? 21.705 59.030 49.496  1.00 49.63  ? 90  TRP B C   1 
ATOM   2898  O  O   . TRP B 1 26  ? 20.892 58.217 49.048  1.00 49.87  ? 90  TRP B O   1 
ATOM   2899  C  CB  . TRP B 1 26  ? 20.349 60.824 50.449  1.00 46.73  ? 90  TRP B CB  1 
ATOM   2900  C  CG  . TRP B 1 26  ? 20.001 62.281 50.467  1.00 43.21  ? 90  TRP B CG  1 
ATOM   2901  C  CD1 . TRP B 1 26  ? 18.959 62.930 49.790  1.00 44.08  ? 90  TRP B CD1 1 
ATOM   2902  C  CD2 . TRP B 1 26  ? 20.673 63.324 51.215  1.00 45.09  ? 90  TRP B CD2 1 
ATOM   2903  N  NE1 . TRP B 1 26  ? 18.944 64.277 50.073  1.00 44.82  ? 90  TRP B NE1 1 
ATOM   2904  C  CE2 . TRP B 1 26  ? 19.953 64.583 50.920  1.00 52.10  ? 90  TRP B CE2 1 
ATOM   2905  C  CE3 . TRP B 1 26  ? 21.745 63.356 52.070  1.00 43.49  ? 90  TRP B CE3 1 
ATOM   2906  C  CZ2 . TRP B 1 26  ? 20.329 65.789 51.485  1.00 45.04  ? 90  TRP B CZ2 1 
ATOM   2907  C  CZ3 . TRP B 1 26  ? 22.122 64.593 52.622  1.00 44.09  ? 90  TRP B CZ3 1 
ATOM   2908  C  CH2 . TRP B 1 26  ? 21.433 65.769 52.345  1.00 39.82  ? 90  TRP B CH2 1 
ATOM   2909  N  N   . VAL B 1 27  ? 22.876 58.667 50.028  1.00 46.86  ? 91  VAL B N   1 
ATOM   2910  C  CA  . VAL B 1 27  ? 23.151 57.240 50.232  1.00 53.45  ? 91  VAL B CA  1 
ATOM   2911  C  C   . VAL B 1 27  ? 23.421 56.945 51.693  1.00 50.41  ? 91  VAL B C   1 
ATOM   2912  O  O   . VAL B 1 27  ? 24.129 57.714 52.339  1.00 57.09  ? 91  VAL B O   1 
ATOM   2913  C  CB  . VAL B 1 27  ? 24.297 56.736 49.349  1.00 64.92  ? 91  VAL B CB  1 
ATOM   2914  C  CG1 . VAL B 1 27  ? 24.289 57.470 48.034  1.00 84.18  ? 91  VAL B CG1 1 
ATOM   2915  C  CG2 . VAL B 1 27  ? 25.622 56.964 50.029  1.00 66.96  ? 91  VAL B CG2 1 
ATOM   2916  N  N   . PRO B 1 28  ? 22.846 55.843 52.224  1.00 50.47  ? 92  PRO B N   1 
ATOM   2917  C  CA  . PRO B 1 28  ? 23.055 55.464 53.624  1.00 46.17  ? 92  PRO B CA  1 
ATOM   2918  C  C   . PRO B 1 28  ? 24.495 55.083 53.849  1.00 49.22  ? 92  PRO B C   1 
ATOM   2919  O  O   . PRO B 1 28  ? 25.056 54.351 53.031  1.00 64.30  ? 92  PRO B O   1 
ATOM   2920  C  CB  . PRO B 1 28  ? 22.163 54.241 53.794  1.00 42.65  ? 92  PRO B CB  1 
ATOM   2921  C  CG  . PRO B 1 28  ? 22.036 53.680 52.428  1.00 48.88  ? 92  PRO B CG  1 
ATOM   2922  C  CD  . PRO B 1 28  ? 21.970 54.881 51.534  1.00 48.44  ? 92  PRO B CD  1 
ATOM   2923  N  N   . THR B 1 29  ? 25.091 55.585 54.927  1.00 45.90  ? 93  THR B N   1 
ATOM   2924  C  CA  . THR B 1 29  ? 26.465 55.258 55.225  1.00 55.41  ? 93  THR B CA  1 
ATOM   2925  C  C   . THR B 1 29  ? 26.524 54.286 56.403  1.00 60.53  ? 93  THR B C   1 
ATOM   2926  O  O   . THR B 1 29  ? 27.511 53.589 56.607  1.00 56.35  ? 93  THR B O   1 
ATOM   2927  C  CB  . THR B 1 29  ? 27.295 56.524 55.487  1.00 64.70  ? 93  THR B CB  1 
ATOM   2928  O  OG1 . THR B 1 29  ? 26.537 57.431 56.297  1.00 69.04  ? 93  THR B OG1 1 
ATOM   2929  C  CG2 . THR B 1 29  ? 27.655 57.202 54.171  1.00 62.65  ? 93  THR B CG2 1 
ATOM   2930  N  N   . TYR B 1 30  ? 25.447 54.241 57.173  1.00 67.68  ? 94  TYR B N   1 
ATOM   2931  C  CA  . TYR B 1 30  ? 25.388 53.363 58.332  1.00 60.23  ? 94  TYR B CA  1 
ATOM   2932  C  C   . TYR B 1 30  ? 23.960 53.021 58.676  1.00 59.46  ? 94  TYR B C   1 
ATOM   2933  O  O   . TYR B 1 30  ? 23.026 53.820 58.475  1.00 49.62  ? 94  TYR B O   1 
ATOM   2934  C  CB  . TYR B 1 30  ? 26.020 54.017 59.547  1.00 58.27  ? 94  TYR B CB  1 
ATOM   2935  C  CG  . TYR B 1 30  ? 25.741 53.276 60.838  1.00 66.03  ? 94  TYR B CG  1 
ATOM   2936  C  CD1 . TYR B 1 30  ? 26.448 52.134 61.154  1.00 62.87  ? 94  TYR B CD1 1 
ATOM   2937  C  CD2 . TYR B 1 30  ? 24.760 53.721 61.743  1.00 77.54  ? 94  TYR B CD2 1 
ATOM   2938  C  CE1 . TYR B 1 30  ? 26.214 51.443 62.322  1.00 72.41  ? 94  TYR B CE1 1 
ATOM   2939  C  CE2 . TYR B 1 30  ? 24.514 53.026 62.934  1.00 73.26  ? 94  TYR B CE2 1 
ATOM   2940  C  CZ  . TYR B 1 30  ? 25.257 51.883 63.209  1.00 83.84  ? 94  TYR B CZ  1 
ATOM   2941  O  OH  . TYR B 1 30  ? 25.065 51.162 64.365  1.00 116.28 ? 94  TYR B OH  1 
ATOM   2942  N  N   . ARG B 1 31  ? 23.806 51.836 59.241  1.00 52.69  ? 95  ARG B N   1 
ATOM   2943  C  CA  . ARG B 1 31  ? 22.500 51.376 59.610  1.00 56.32  ? 95  ARG B CA  1 
ATOM   2944  C  C   . ARG B 1 31  ? 22.699 50.445 60.767  1.00 51.35  ? 95  ARG B C   1 
ATOM   2945  O  O   . ARG B 1 31  ? 23.531 49.548 60.697  1.00 44.15  ? 95  ARG B O   1 
ATOM   2946  C  CB  . ARG B 1 31  ? 21.878 50.685 58.414  1.00 55.62  ? 95  ARG B CB  1 
ATOM   2947  C  CG  . ARG B 1 31  ? 20.696 49.871 58.722  1.00 76.90  ? 95  ARG B CG  1 
ATOM   2948  C  CD  . ARG B 1 31  ? 20.025 49.403 57.455  1.00 88.52  ? 95  ARG B CD  1 
ATOM   2949  N  NE  . ARG B 1 31  ? 20.846 48.485 56.655  1.00 72.14  ? 95  ARG B NE  1 
ATOM   2950  C  CZ  . ARG B 1 31  ? 20.373 47.819 55.609  1.00 61.53  ? 95  ARG B CZ  1 
ATOM   2951  N  NH1 . ARG B 1 31  ? 19.100 47.940 55.270  1.00 78.78  ? 95  ARG B NH1 1 
ATOM   2952  N  NH2 . ARG B 1 31  ? 21.147 47.016 54.915  1.00 64.08  ? 95  ARG B NH2 1 
ATOM   2953  N  N   . GLY B 1 32  ? 21.971 50.706 61.848  1.00 65.31  ? 96  GLY B N   1 
ATOM   2954  C  CA  . GLY B 1 32  ? 22.084 49.901 63.066  1.00 67.53  ? 96  GLY B CA  1 
ATOM   2955  C  C   . GLY B 1 32  ? 21.424 48.559 62.850  1.00 58.96  ? 96  GLY B C   1 
ATOM   2956  O  O   . GLY B 1 32  ? 20.605 48.398 61.956  1.00 55.61  ? 96  GLY B O   1 
ATOM   2957  N  N   . GLU B 1 33  ? 21.764 47.590 63.678  1.00 61.82  ? 97  GLU B N   1 
ATOM   2958  C  CA  . GLU B 1 33  ? 21.252 46.255 63.458  1.00 67.82  ? 97  GLU B CA  1 
ATOM   2959  C  C   . GLU B 1 33  ? 19.782 46.138 63.874  1.00 68.56  ? 97  GLU B C   1 
ATOM   2960  O  O   . GLU B 1 33  ? 19.049 45.255 63.388  1.00 55.38  ? 97  GLU B O   1 
ATOM   2961  C  CB  . GLU B 1 33  ? 22.134 45.217 64.153  1.00 74.51  ? 97  GLU B CB  1 
ATOM   2962  C  CG  . GLU B 1 33  ? 22.233 43.901 63.367  1.00 109.35 ? 97  GLU B CG  1 
ATOM   2963  C  CD  . GLU B 1 33  ? 22.872 44.044 61.964  1.00 113.72 ? 97  GLU B CD  1 
ATOM   2964  O  OE1 . GLU B 1 33  ? 23.854 44.799 61.801  1.00 104.70 ? 97  GLU B OE1 1 
ATOM   2965  O  OE2 . GLU B 1 33  ? 22.399 43.375 61.018  1.00 116.31 ? 97  GLU B OE2 1 
ATOM   2966  N  N   . GLY B 1 34  ? 19.352 47.051 64.746  1.00 66.44  ? 98  GLY B N   1 
ATOM   2967  C  CA  . GLY B 1 34  ? 17.959 47.112 65.173  1.00 56.74  ? 98  GLY B CA  1 
ATOM   2968  C  C   . GLY B 1 34  ? 17.036 47.731 64.140  1.00 65.12  ? 98  GLY B C   1 
ATOM   2969  O  O   . GLY B 1 34  ? 15.813 47.732 64.326  1.00 77.62  ? 98  GLY B O   1 
ATOM   2970  N  N   . THR B 1 35  ? 17.607 48.254 63.053  1.00 52.77  ? 99  THR B N   1 
ATOM   2971  C  CA  . THR B 1 35  ? 16.809 48.890 62.018  1.00 62.89  ? 99  THR B CA  1 
ATOM   2972  C  C   . THR B 1 35  ? 16.184 47.822 61.105  1.00 66.28  ? 99  THR B C   1 
ATOM   2973  O  O   . THR B 1 35  ? 15.370 48.121 60.231  1.00 61.34  ? 99  THR B O   1 
ATOM   2974  C  CB  . THR B 1 35  ? 17.683 49.805 61.177  1.00 63.11  ? 99  THR B CB  1 
ATOM   2975  O  OG1 . THR B 1 35  ? 18.671 49.014 60.545  1.00 74.73  ? 99  THR B OG1 1 
ATOM   2976  C  CG2 . THR B 1 35  ? 18.419 50.785 62.022  1.00 54.73  ? 99  THR B CG2 1 
ATOM   2977  N  N   . THR B 1 36  ? 16.601 46.577 61.313  1.00 73.40  ? 100 THR B N   1 
ATOM   2978  C  CA  . THR B 1 36  ? 16.220 45.467 60.450  1.00 82.69  ? 100 THR B CA  1 
ATOM   2979  C  C   . THR B 1 36  ? 15.746 44.308 61.306  1.00 79.85  ? 100 THR B C   1 
ATOM   2980  O  O   . THR B 1 36  ? 14.580 43.907 61.233  1.00 116.64 ? 100 THR B O   1 
ATOM   2981  C  CB  . THR B 1 36  ? 17.394 45.004 59.542  1.00 78.35  ? 100 THR B CB  1 
ATOM   2982  O  OG1 . THR B 1 36  ? 18.598 44.900 60.319  1.00 78.44  ? 100 THR B OG1 1 
ATOM   2983  C  CG2 . THR B 1 36  ? 17.612 45.985 58.373  1.00 69.99  ? 100 THR B CG2 1 
ATOM   2984  N  N   . GLY B 1 37  ? 16.650 43.792 62.132  1.00 67.98  ? 101 GLY B N   1 
ATOM   2985  C  CA  . GLY B 1 37  ? 16.313 42.739 63.087  1.00 84.12  ? 101 GLY B CA  1 
ATOM   2986  C  C   . GLY B 1 37  ? 15.965 43.265 64.473  1.00 72.03  ? 101 GLY B C   1 
ATOM   2987  O  O   . GLY B 1 37  ? 15.760 44.471 64.658  1.00 79.73  ? 101 GLY B O   1 
ATOM   2988  N  N   . LYS B 1 38  ? 15.886 42.347 65.438  1.00 56.64  ? 102 LYS B N   1 
ATOM   2989  C  CA  . LYS B 1 38  ? 15.661 42.681 66.835  1.00 55.88  ? 102 LYS B CA  1 
ATOM   2990  C  C   . LYS B 1 38  ? 16.983 42.913 67.547  1.00 60.19  ? 102 LYS B C   1 
ATOM   2991  O  O   . LYS B 1 38  ? 18.017 42.472 67.088  1.00 74.67  ? 102 LYS B O   1 
ATOM   2992  C  CB  . LYS B 1 38  ? 14.882 41.566 67.526  1.00 67.12  ? 102 LYS B CB  1 
ATOM   2993  C  CG  . LYS B 1 38  ? 13.440 41.489 67.078  1.00 89.96  ? 102 LYS B CG  1 
ATOM   2994  C  CD  . LYS B 1 38  ? 12.617 40.783 68.123  1.00 106.82 ? 102 LYS B CD  1 
ATOM   2995  C  CE  . LYS B 1 38  ? 11.152 41.179 68.042  1.00 101.08 ? 102 LYS B CE  1 
ATOM   2996  N  NZ  . LYS B 1 38  ? 10.457 40.702 69.268  1.00 139.07 ? 102 LYS B NZ  1 
ATOM   2997  N  N   . ILE B 1 39  ? 16.944 43.619 68.668  1.00 67.07  ? 103 ILE B N   1 
ATOM   2998  C  CA  . ILE B 1 39  ? 18.148 43.981 69.414  1.00 57.44  ? 103 ILE B CA  1 
ATOM   2999  C  C   . ILE B 1 39  ? 18.424 42.922 70.474  1.00 71.13  ? 103 ILE B C   1 
ATOM   3000  O  O   . ILE B 1 39  ? 17.530 42.522 71.221  1.00 69.83  ? 103 ILE B O   1 
ATOM   3001  C  CB  . ILE B 1 39  ? 17.962 45.324 70.156  1.00 52.27  ? 103 ILE B CB  1 
ATOM   3002  C  CG1 . ILE B 1 39  ? 17.314 46.365 69.242  1.00 51.03  ? 103 ILE B CG1 1 
ATOM   3003  C  CG2 . ILE B 1 39  ? 19.263 45.816 70.790  1.00 51.06  ? 103 ILE B CG2 1 
ATOM   3004  C  CD1 . ILE B 1 39  ? 18.231 47.236 68.520  1.00 44.96  ? 103 ILE B CD1 1 
ATOM   3005  N  N   . PRO B 1 40  ? 19.676 42.468 70.550  1.00 74.86  ? 104 PRO B N   1 
ATOM   3006  C  CA  . PRO B 1 40  ? 20.090 41.542 71.593  1.00 60.97  ? 104 PRO B CA  1 
ATOM   3007  C  C   . PRO B 1 40  ? 19.904 42.182 72.972  1.00 80.66  ? 104 PRO B C   1 
ATOM   3008  O  O   . PRO B 1 40  ? 20.096 43.396 73.133  1.00 72.10  ? 104 PRO B O   1 
ATOM   3009  C  CB  . PRO B 1 40  ? 21.549 41.310 71.280  1.00 63.66  ? 104 PRO B CB  1 
ATOM   3010  C  CG  . PRO B 1 40  ? 21.709 41.674 69.833  1.00 60.46  ? 104 PRO B CG  1 
ATOM   3011  C  CD  . PRO B 1 40  ? 20.747 42.755 69.574  1.00 66.66  ? 104 PRO B CD  1 
ATOM   3012  N  N   . ASP B 1 41  ? 19.519 41.363 73.948  1.00 102.88 ? 105 ASP B N   1 
ATOM   3013  C  CA  . ASP B 1 41  ? 19.089 41.858 75.248  1.00 93.31  ? 105 ASP B CA  1 
ATOM   3014  C  C   . ASP B 1 41  ? 20.238 42.478 76.034  1.00 100.48 ? 105 ASP B C   1 
ATOM   3015  O  O   . ASP B 1 41  ? 20.009 43.338 76.889  1.00 118.48 ? 105 ASP B O   1 
ATOM   3016  C  CB  . ASP B 1 41  ? 18.405 40.744 76.058  1.00 114.53 ? 105 ASP B CB  1 
ATOM   3017  C  CG  . ASP B 1 41  ? 17.216 40.138 75.333  1.00 146.09 ? 105 ASP B CG  1 
ATOM   3018  O  OD1 . ASP B 1 41  ? 17.211 40.186 74.092  1.00 215.29 ? 105 ASP B OD1 1 
ATOM   3019  O  OD2 . ASP B 1 41  ? 16.292 39.610 75.987  1.00 153.08 ? 105 ASP B OD2 1 
ATOM   3020  N  N   . GLU B 1 42  ? 21.469 42.058 75.745  1.00 88.43  ? 106 GLU B N   1 
ATOM   3021  C  CA  . GLU B 1 42  ? 22.621 42.554 76.501  1.00 91.96  ? 106 GLU B CA  1 
ATOM   3022  C  C   . GLU B 1 42  ? 23.023 43.966 76.111  1.00 90.18  ? 106 GLU B C   1 
ATOM   3023  O  O   . GLU B 1 42  ? 23.792 44.608 76.838  1.00 112.10 ? 106 GLU B O   1 
ATOM   3024  C  CB  . GLU B 1 42  ? 23.831 41.619 76.416  1.00 110.50 ? 106 GLU B CB  1 
ATOM   3025  C  CG  . GLU B 1 42  ? 24.472 41.525 75.044  1.00 138.79 ? 106 GLU B CG  1 
ATOM   3026  C  CD  . GLU B 1 42  ? 24.142 40.220 74.343  1.00 179.56 ? 106 GLU B CD  1 
ATOM   3027  O  OE1 . GLU B 1 42  ? 22.953 39.824 74.321  1.00 186.83 ? 106 GLU B OE1 1 
ATOM   3028  O  OE2 . GLU B 1 42  ? 25.081 39.587 73.814  1.00 185.25 ? 106 GLU B OE2 1 
ATOM   3029  N  N   . GLN B 1 43  ? 22.508 44.455 74.982  1.00 65.87  ? 107 GLN B N   1 
ATOM   3030  C  CA  . GLN B 1 43  ? 22.776 45.834 74.583  1.00 56.93  ? 107 GLN B CA  1 
ATOM   3031  C  C   . GLN B 1 43  ? 22.082 46.866 75.476  1.00 59.96  ? 107 GLN B C   1 
ATOM   3032  O  O   . GLN B 1 43  ? 21.022 46.619 76.055  1.00 59.89  ? 107 GLN B O   1 
ATOM   3033  C  CB  . GLN B 1 43  ? 22.417 46.072 73.140  1.00 50.11  ? 107 GLN B CB  1 
ATOM   3034  C  CG  . GLN B 1 43  ? 23.323 45.367 72.173  1.00 59.62  ? 107 GLN B CG  1 
ATOM   3035  C  CD  . GLN B 1 43  ? 23.227 45.963 70.780  1.00 88.95  ? 107 GLN B CD  1 
ATOM   3036  O  OE1 . GLN B 1 43  ? 22.831 47.133 70.626  1.00 94.22  ? 107 GLN B OE1 1 
ATOM   3037  N  NE2 . GLN B 1 43  ? 23.584 45.164 69.750  1.00 67.84  ? 107 GLN B NE2 1 
ATOM   3038  N  N   . MET B 1 44  ? 22.726 48.018 75.607  1.00 66.60  ? 108 MET B N   1 
ATOM   3039  C  CA  . MET B 1 44  ? 22.171 49.142 76.330  1.00 73.36  ? 108 MET B CA  1 
ATOM   3040  C  C   . MET B 1 44  ? 20.950 49.677 75.558  1.00 72.83  ? 108 MET B C   1 
ATOM   3041  O  O   . MET B 1 44  ? 21.006 49.804 74.340  1.00 67.23  ? 108 MET B O   1 
ATOM   3042  C  CB  . MET B 1 44  ? 23.258 50.211 76.444  1.00 74.41  ? 108 MET B CB  1 
ATOM   3043  C  CG  . MET B 1 44  ? 22.852 51.452 77.182  1.00 75.49  ? 108 MET B CG  1 
ATOM   3044  S  SD  . MET B 1 44  ? 22.564 51.102 78.897  1.00 101.56 ? 108 MET B SD  1 
ATOM   3045  C  CE  . MET B 1 44  ? 24.203 51.378 79.586  1.00 116.83 ? 108 MET B CE  1 
ATOM   3046  N  N   . LEU B 1 45  ? 19.846 49.969 76.246  1.00 64.82  ? 109 LEU B N   1 
ATOM   3047  C  CA  . LEU B 1 45  ? 18.694 50.576 75.569  1.00 66.87  ? 109 LEU B CA  1 
ATOM   3048  C  C   . LEU B 1 45  ? 18.997 52.049 75.373  1.00 62.91  ? 109 LEU B C   1 
ATOM   3049  O  O   . LEU B 1 45  ? 19.392 52.705 76.327  1.00 78.22  ? 109 LEU B O   1 
ATOM   3050  C  CB  . LEU B 1 45  ? 17.412 50.434 76.391  1.00 57.25  ? 109 LEU B CB  1 
ATOM   3051  C  CG  . LEU B 1 45  ? 16.998 49.030 76.806  1.00 51.08  ? 109 LEU B CG  1 
ATOM   3052  C  CD1 . LEU B 1 45  ? 15.950 49.156 77.878  1.00 60.05  ? 109 LEU B CD1 1 
ATOM   3053  C  CD2 . LEU B 1 45  ? 16.457 48.314 75.658  1.00 45.21  ? 109 LEU B CD2 1 
ATOM   3054  N  N   . THR B 1 46  ? 18.832 52.567 74.156  1.00 49.40  ? 110 THR B N   1 
ATOM   3055  C  CA  . THR B 1 46  ? 19.187 53.953 73.887  1.00 46.49  ? 110 THR B CA  1 
ATOM   3056  C  C   . THR B 1 46  ? 17.994 54.845 73.588  1.00 48.33  ? 110 THR B C   1 
ATOM   3057  O  O   . THR B 1 46  ? 16.949 54.391 73.136  1.00 60.46  ? 110 THR B O   1 
ATOM   3058  C  CB  . THR B 1 46  ? 20.185 54.080 72.739  1.00 48.26  ? 110 THR B CB  1 
ATOM   3059  O  OG1 . THR B 1 46  ? 19.525 53.824 71.511  1.00 70.83  ? 110 THR B OG1 1 
ATOM   3060  C  CG2 . THR B 1 46  ? 21.310 53.088 72.883  1.00 51.31  ? 110 THR B CG2 1 
ATOM   3061  N  N   . ARG B 1 47  ? 18.148 56.127 73.870  1.00 45.66  ? 111 ARG B N   1 
ATOM   3062  C  CA  . ARG B 1 47  ? 17.171 57.101 73.441  1.00 40.99  ? 111 ARG B CA  1 
ATOM   3063  C  C   . ARG B 1 47  ? 17.895 58.396 73.179  1.00 43.17  ? 111 ARG B C   1 
ATOM   3064  O  O   . ARG B 1 47  ? 19.020 58.561 73.634  1.00 54.82  ? 111 ARG B O   1 
ATOM   3065  C  CB  . ARG B 1 47  ? 16.044 57.257 74.446  1.00 35.80  ? 111 ARG B CB  1 
ATOM   3066  C  CG  . ARG B 1 47  ? 16.279 58.252 75.464  1.00 43.10  ? 111 ARG B CG  1 
ATOM   3067  C  CD  . ARG B 1 47  ? 14.940 58.755 76.051  1.00 61.60  ? 111 ARG B CD  1 
ATOM   3068  N  NE  . ARG B 1 47  ? 15.151 59.891 76.962  1.00 68.63  ? 111 ARG B NE  1 
ATOM   3069  C  CZ  . ARG B 1 47  ? 15.257 61.161 76.574  1.00 74.52  ? 111 ARG B CZ  1 
ATOM   3070  N  NH1 . ARG B 1 47  ? 15.143 61.493 75.292  1.00 69.18  ? 111 ARG B NH1 1 
ATOM   3071  N  NH2 . ARG B 1 47  ? 15.461 62.110 77.473  1.00 98.06  ? 111 ARG B NH2 1 
ATOM   3072  N  N   . GLN B 1 48  ? 17.266 59.294 72.418  1.00 43.65  ? 112 GLN B N   1 
ATOM   3073  C  CA  . GLN B 1 48  ? 17.866 60.585 72.072  1.00 48.56  ? 112 GLN B CA  1 
ATOM   3074  C  C   . GLN B 1 48  ? 19.220 60.423 71.350  1.00 47.62  ? 112 GLN B C   1 
ATOM   3075  O  O   . GLN B 1 48  ? 20.165 61.192 71.562  1.00 55.83  ? 112 GLN B O   1 
ATOM   3076  C  CB  . GLN B 1 48  ? 17.973 61.516 73.302  1.00 44.95  ? 112 GLN B CB  1 
ATOM   3077  C  CG  . GLN B 1 48  ? 19.301 62.271 73.357  1.00 54.28  ? 112 GLN B CG  1 
ATOM   3078  C  CD  . GLN B 1 48  ? 19.135 63.733 73.612  1.00 67.62  ? 112 GLN B CD  1 
ATOM   3079  O  OE1 . GLN B 1 48  ? 20.259 64.422 73.715  1.00 78.29  ? 112 GLN B OE1 1 
ATOM   3080  N  NE2 . GLN B 1 48  ? 18.007 64.252 73.730  1.00 52.68  ? 112 GLN B NE2 1 
ATOM   3081  N  N   . ASN B 1 49  ? 19.300 59.423 70.491  1.00 41.87  ? 113 ASN B N   1 
ATOM   3082  C  CA  . ASN B 1 49  ? 20.482 59.260 69.662  1.00 47.07  ? 113 ASN B CA  1 
ATOM   3083  C  C   . ASN B 1 49  ? 20.806 60.490 68.811  1.00 47.49  ? 113 ASN B C   1 
ATOM   3084  O  O   . ASN B 1 49  ? 19.919 61.172 68.302  1.00 49.44  ? 113 ASN B O   1 
ATOM   3085  C  CB  . ASN B 1 49  ? 20.310 58.045 68.768  1.00 41.47  ? 113 ASN B CB  1 
ATOM   3086  C  CG  . ASN B 1 49  ? 20.223 56.765 69.565  1.00 55.30  ? 113 ASN B CG  1 
ATOM   3087  O  OD1 . ASN B 1 49  ? 21.192 55.985 69.645  1.00 45.87  ? 113 ASN B OD1 1 
ATOM   3088  N  ND2 . ASN B 1 49  ? 19.062 56.545 70.196  1.00 64.10  ? 113 ASN B ND2 1 
ATOM   3089  N  N   . PHE B 1 50  ? 22.082 60.802 68.688  1.00 44.40  ? 114 PHE B N   1 
ATOM   3090  C  CA  . PHE B 1 50  ? 22.496 61.686 67.617  1.00 47.95  ? 114 PHE B CA  1 
ATOM   3091  C  C   . PHE B 1 50  ? 23.918 61.399 67.177  1.00 44.25  ? 114 PHE B C   1 
ATOM   3092  O  O   . PHE B 1 50  ? 24.579 60.475 67.661  1.00 49.57  ? 114 PHE B O   1 
ATOM   3093  C  CB  . PHE B 1 50  ? 22.298 63.167 67.966  1.00 59.80  ? 114 PHE B CB  1 
ATOM   3094  C  CG  . PHE B 1 50  ? 23.153 63.646 69.084  1.00 52.41  ? 114 PHE B CG  1 
ATOM   3095  C  CD1 . PHE B 1 50  ? 22.728 63.534 70.377  1.00 54.59  ? 114 PHE B CD1 1 
ATOM   3096  C  CD2 . PHE B 1 50  ? 24.371 64.238 68.832  1.00 53.69  ? 114 PHE B CD2 1 
ATOM   3097  C  CE1 . PHE B 1 50  ? 23.515 63.965 71.395  1.00 59.88  ? 114 PHE B CE1 1 
ATOM   3098  C  CE2 . PHE B 1 50  ? 25.157 64.704 69.851  1.00 51.01  ? 114 PHE B CE2 1 
ATOM   3099  C  CZ  . PHE B 1 50  ? 24.736 64.558 71.132  1.00 52.70  ? 114 PHE B CZ  1 
ATOM   3100  N  N   . VAL B 1 51  ? 24.385 62.169 66.217  1.00 39.81  ? 115 VAL B N   1 
ATOM   3101  C  CA  . VAL B 1 51  ? 25.692 61.926 65.693  1.00 43.04  ? 115 VAL B CA  1 
ATOM   3102  C  C   . VAL B 1 51  ? 26.416 63.232 65.672  1.00 42.14  ? 115 VAL B C   1 
ATOM   3103  O  O   . VAL B 1 51  ? 25.846 64.239 65.372  1.00 55.82  ? 115 VAL B O   1 
ATOM   3104  C  CB  . VAL B 1 51  ? 25.648 61.342 64.284  1.00 45.91  ? 115 VAL B CB  1 
ATOM   3105  C  CG1 . VAL B 1 51  ? 27.083 61.151 63.752  1.00 47.43  ? 115 VAL B CG1 1 
ATOM   3106  C  CG2 . VAL B 1 51  ? 24.896 60.013 64.271  1.00 45.70  ? 115 VAL B CG2 1 
ATOM   3107  N  N   . SER B 1 52  ? 27.688 63.193 65.998  1.00 47.95  ? 116 SER B N   1 
ATOM   3108  C  CA  . SER B 1 52  ? 28.541 64.342 65.928  1.00 49.91  ? 116 SER B CA  1 
ATOM   3109  C  C   . SER B 1 52  ? 29.917 63.821 65.565  1.00 56.36  ? 116 SER B C   1 
ATOM   3110  O  O   . SER B 1 52  ? 30.340 62.740 66.032  1.00 54.51  ? 116 SER B O   1 
ATOM   3111  C  CB  . SER B 1 52  ? 28.573 65.061 67.257  1.00 49.67  ? 116 SER B CB  1 
ATOM   3112  O  OG  . SER B 1 52  ? 29.546 66.088 67.176  1.00 60.30  ? 116 SER B OG  1 
ATOM   3113  N  N   . CYS B 1 53  ? 30.617 64.576 64.730  1.00 59.38  ? 117 CYS B N   1 
ATOM   3114  C  CA  . CYS B 1 53  ? 31.904 64.099 64.263  1.00 69.19  ? 117 CYS B CA  1 
ATOM   3115  C  C   . CYS B 1 53  ? 33.114 64.876 64.777  1.00 71.36  ? 117 CYS B C   1 
ATOM   3116  O  O   . CYS B 1 53  ? 33.062 66.103 64.935  1.00 83.07  ? 117 CYS B O   1 
ATOM   3117  C  CB  . CYS B 1 53  ? 31.908 64.028 62.740  1.00 85.64  ? 117 CYS B CB  1 
ATOM   3118  S  SG  . CYS B 1 53  ? 30.619 62.945 62.089  1.00 131.46 ? 117 CYS B SG  1 
ATOM   3119  N  N   . SER B 1 54  ? 34.196 64.141 65.047  1.00 77.90  ? 118 SER B N   1 
ATOM   3120  C  CA  . SER B 1 54  ? 35.529 64.732 65.237  1.00 79.03  ? 118 SER B CA  1 
ATOM   3121  C  C   . SER B 1 54  ? 36.271 64.731 63.905  1.00 71.37  ? 118 SER B C   1 
ATOM   3122  O  O   . SER B 1 54  ? 35.705 64.347 62.879  1.00 74.10  ? 118 SER B O   1 
ATOM   3123  C  CB  . SER B 1 54  ? 36.326 64.005 66.350  1.00 85.60  ? 118 SER B CB  1 
ATOM   3124  O  OG  . SER B 1 54  ? 37.022 62.832 65.928  1.00 71.55  ? 118 SER B OG  1 
ATOM   3125  N  N   . ASP B 1 55  ? 37.528 65.172 63.915  1.00 93.58  ? 119 ASP B N   1 
ATOM   3126  C  CA  . ASP B 1 55  ? 38.351 65.185 62.697  1.00 95.59  ? 119 ASP B CA  1 
ATOM   3127  C  C   . ASP B 1 55  ? 38.918 63.799 62.434  1.00 90.85  ? 119 ASP B C   1 
ATOM   3128  O  O   . ASP B 1 55  ? 39.491 63.536 61.379  1.00 106.10 ? 119 ASP B O   1 
ATOM   3129  C  CB  . ASP B 1 55  ? 39.466 66.234 62.798  1.00 102.84 ? 119 ASP B CB  1 
ATOM   3130  C  CG  . ASP B 1 55  ? 40.258 66.143 64.103  1.00 141.25 ? 119 ASP B CG  1 
ATOM   3131  O  OD1 . ASP B 1 55  ? 40.212 65.098 64.789  1.00 146.14 ? 119 ASP B OD1 1 
ATOM   3132  O  OD2 . ASP B 1 55  ? 40.946 67.131 64.439  1.00 174.26 ? 119 ASP B OD2 1 
ATOM   3133  N  N   . LYS B 1 56  ? 38.716 62.924 63.415  1.00 82.16  ? 120 LYS B N   1 
ATOM   3134  C  CA  . LYS B 1 56  ? 39.235 61.580 63.439  1.00 79.33  ? 120 LYS B CA  1 
ATOM   3135  C  C   . LYS B 1 56  ? 38.160 60.560 63.045  1.00 76.34  ? 120 LYS B C   1 
ATOM   3136  O  O   . LYS B 1 56  ? 38.452 59.553 62.405  1.00 121.40 ? 120 LYS B O   1 
ATOM   3137  C  CB  . LYS B 1 56  ? 39.751 61.297 64.853  1.00 88.23  ? 120 LYS B CB  1 
ATOM   3138  C  CG  . LYS B 1 56  ? 40.475 59.945 65.089  1.00 100.45 ? 120 LYS B CG  1 
ATOM   3139  C  CD  . LYS B 1 56  ? 40.859 59.725 66.573  1.00 112.35 ? 120 LYS B CD  1 
ATOM   3140  C  CE  . LYS B 1 56  ? 41.981 60.665 67.044  1.00 173.77 ? 120 LYS B CE  1 
ATOM   3141  N  NZ  . LYS B 1 56  ? 41.523 62.026 67.486  1.00 180.95 ? 120 LYS B NZ  1 
ATOM   3142  N  N   . GLU B 1 57  ? 36.921 60.824 63.423  1.00 64.97  ? 121 GLU B N   1 
ATOM   3143  C  CA  . GLU B 1 57  ? 35.867 59.813 63.445  1.00 63.76  ? 121 GLU B CA  1 
ATOM   3144  C  C   . GLU B 1 57  ? 34.542 60.471 63.835  1.00 66.82  ? 121 GLU B C   1 
ATOM   3145  O  O   . GLU B 1 57  ? 34.510 61.566 64.405  1.00 70.62  ? 121 GLU B O   1 
ATOM   3146  C  CB  . GLU B 1 57  ? 36.177 58.728 64.495  1.00 66.21  ? 121 GLU B CB  1 
ATOM   3147  C  CG  . GLU B 1 57  ? 35.733 59.135 65.920  1.00 77.16  ? 121 GLU B CG  1 
ATOM   3148  C  CD  . GLU B 1 57  ? 36.279 58.280 67.047  1.00 101.92 ? 121 GLU B CD  1 
ATOM   3149  O  OE1 . GLU B 1 57  ? 36.652 57.107 66.808  1.00 137.64 ? 121 GLU B OE1 1 
ATOM   3150  O  OE2 . GLU B 1 57  ? 36.318 58.797 68.191  1.00 119.06 ? 121 GLU B OE2 1 
ATOM   3151  N  N   . CYS B 1 58  ? 33.449 59.774 63.571  1.00 68.71  ? 122 CYS B N   1 
ATOM   3152  C  CA  . CYS B 1 58  ? 32.128 60.214 64.002  1.00 56.87  ? 122 CYS B CA  1 
ATOM   3153  C  C   . CYS B 1 58  ? 31.662 59.338 65.138  1.00 56.96  ? 122 CYS B C   1 
ATOM   3154  O  O   . CYS B 1 58  ? 31.878 58.115 65.139  1.00 63.52  ? 122 CYS B O   1 
ATOM   3155  C  CB  . CYS B 1 58  ? 31.147 60.123 62.854  1.00 61.80  ? 122 CYS B CB  1 
ATOM   3156  S  SG  . CYS B 1 58  ? 31.582 61.244 61.555  1.00 103.55 ? 122 CYS B SG  1 
ATOM   3157  N  N   . ARG B 1 59  ? 31.023 59.962 66.115  1.00 51.67  ? 123 ARG B N   1 
ATOM   3158  C  CA  . ARG B 1 59  ? 30.554 59.214 67.256  1.00 50.36  ? 123 ARG B CA  1 
ATOM   3159  C  C   . ARG B 1 59  ? 29.054 59.281 67.350  1.00 52.90  ? 123 ARG B C   1 
ATOM   3160  O  O   . ARG B 1 59  ? 28.430 60.251 66.867  1.00 49.44  ? 123 ARG B O   1 
ATOM   3161  C  CB  . ARG B 1 59  ? 31.201 59.765 68.512  1.00 54.08  ? 123 ARG B CB  1 
ATOM   3162  C  CG  . ARG B 1 59  ? 32.699 59.545 68.566  1.00 50.41  ? 123 ARG B CG  1 
ATOM   3163  C  CD  . ARG B 1 59  ? 33.274 59.807 69.940  1.00 53.62  ? 123 ARG B CD  1 
ATOM   3164  N  NE  . ARG B 1 59  ? 32.886 58.789 70.916  1.00 53.34  ? 123 ARG B NE  1 
ATOM   3165  C  CZ  . ARG B 1 59  ? 33.356 57.554 70.930  1.00 49.52  ? 123 ARG B CZ  1 
ATOM   3166  N  NH1 . ARG B 1 59  ? 34.247 57.192 70.037  1.00 58.40  ? 123 ARG B NH1 1 
ATOM   3167  N  NH2 . ARG B 1 59  ? 32.952 56.697 71.846  1.00 50.27  ? 123 ARG B NH2 1 
ATOM   3168  N  N   . ARG B 1 60  ? 28.469 58.240 67.945  1.00 48.97  ? 124 ARG B N   1 
ATOM   3169  C  CA  . ARG B 1 60  ? 27.013 58.235 68.160  1.00 50.27  ? 124 ARG B CA  1 
ATOM   3170  C  C   . ARG B 1 60  ? 26.716 58.486 69.623  1.00 49.34  ? 124 ARG B C   1 
ATOM   3171  O  O   . ARG B 1 60  ? 27.102 57.692 70.466  1.00 68.83  ? 124 ARG B O   1 
ATOM   3172  C  CB  . ARG B 1 60  ? 26.432 56.905 67.710  1.00 44.10  ? 124 ARG B CB  1 
ATOM   3173  C  CG  . ARG B 1 60  ? 25.179 56.476 68.422  1.00 47.99  ? 124 ARG B CG  1 
ATOM   3174  C  CD  . ARG B 1 60  ? 24.576 55.308 67.696  1.00 51.46  ? 124 ARG B CD  1 
ATOM   3175  N  NE  . ARG B 1 60  ? 23.404 54.748 68.359  1.00 59.51  ? 124 ARG B NE  1 
ATOM   3176  C  CZ  . ARG B 1 60  ? 23.016 53.483 68.225  1.00 68.95  ? 124 ARG B CZ  1 
ATOM   3177  N  NH1 . ARG B 1 60  ? 23.726 52.661 67.465  1.00 64.75  ? 124 ARG B NH1 1 
ATOM   3178  N  NH2 . ARG B 1 60  ? 21.938 53.033 68.864  1.00 66.86  ? 124 ARG B NH2 1 
ATOM   3179  N  N   . PHE B 1 61  ? 26.092 59.607 69.940  1.00 40.91  ? 125 PHE B N   1 
ATOM   3180  C  CA  . PHE B 1 61  ? 25.760 59.891 71.339  1.00 43.91  ? 125 PHE B CA  1 
ATOM   3181  C  C   . PHE B 1 61  ? 24.359 59.418 71.630  1.00 47.07  ? 125 PHE B C   1 
ATOM   3182  O  O   . PHE B 1 61  ? 23.499 59.407 70.732  1.00 53.20  ? 125 PHE B O   1 
ATOM   3183  C  CB  . PHE B 1 61  ? 25.912 61.385 71.663  1.00 38.31  ? 125 PHE B CB  1 
ATOM   3184  C  CG  . PHE B 1 61  ? 27.328 61.837 71.644  1.00 38.51  ? 125 PHE B CG  1 
ATOM   3185  C  CD1 . PHE B 1 61  ? 27.986 61.951 70.444  1.00 39.80  ? 125 PHE B CD1 1 
ATOM   3186  C  CD2 . PHE B 1 61  ? 28.024 62.080 72.824  1.00 40.72  ? 125 PHE B CD2 1 
ATOM   3187  C  CE1 . PHE B 1 61  ? 29.308 62.350 70.401  1.00 48.12  ? 125 PHE B CE1 1 
ATOM   3188  C  CE2 . PHE B 1 61  ? 29.341 62.481 72.813  1.00 46.06  ? 125 PHE B CE2 1 
ATOM   3189  C  CZ  . PHE B 1 61  ? 30.002 62.616 71.599  1.00 50.24  ? 125 PHE B CZ  1 
ATOM   3190  N  N   . PHE B 1 62  ? 24.114 59.016 72.871  1.00 43.95  ? 126 PHE B N   1 
ATOM   3191  C  CA  . PHE B 1 62  ? 22.748 58.681 73.245  1.00 53.87  ? 126 PHE B CA  1 
ATOM   3192  C  C   . PHE B 1 62  ? 22.538 58.743 74.746  1.00 50.54  ? 126 PHE B C   1 
ATOM   3193  O  O   . PHE B 1 62  ? 23.461 59.030 75.482  1.00 58.76  ? 126 PHE B O   1 
ATOM   3194  C  CB  . PHE B 1 62  ? 22.347 57.315 72.673  1.00 46.45  ? 126 PHE B CB  1 
ATOM   3195  C  CG  . PHE B 1 62  ? 23.178 56.234 73.157  1.00 45.59  ? 126 PHE B CG  1 
ATOM   3196  C  CD1 . PHE B 1 62  ? 22.832 55.555 74.300  1.00 54.88  ? 126 PHE B CD1 1 
ATOM   3197  C  CD2 . PHE B 1 62  ? 24.355 55.911 72.505  1.00 52.88  ? 126 PHE B CD2 1 
ATOM   3198  C  CE1 . PHE B 1 62  ? 23.638 54.523 74.771  1.00 69.17  ? 126 PHE B CE1 1 
ATOM   3199  C  CE2 . PHE B 1 62  ? 25.189 54.889 72.971  1.00 54.51  ? 126 PHE B CE2 1 
ATOM   3200  C  CZ  . PHE B 1 62  ? 24.824 54.189 74.102  1.00 63.49  ? 126 PHE B CZ  1 
ATOM   3201  N  N   . VAL B 1 63  ? 21.313 58.487 75.182  1.00 46.76  ? 127 VAL B N   1 
ATOM   3202  C  CA  . VAL B 1 63  ? 20.976 58.514 76.580  1.00 47.62  ? 127 VAL B CA  1 
ATOM   3203  C  C   . VAL B 1 63  ? 20.487 57.123 76.938  1.00 47.58  ? 127 VAL B C   1 
ATOM   3204  O  O   . VAL B 1 63  ? 19.599 56.606 76.275  1.00 58.80  ? 127 VAL B O   1 
ATOM   3205  C  CB  . VAL B 1 63  ? 19.900 59.573 76.835  1.00 49.37  ? 127 VAL B CB  1 
ATOM   3206  C  CG1 . VAL B 1 63  ? 19.228 59.357 78.161  1.00 57.70  ? 127 VAL B CG1 1 
ATOM   3207  C  CG2 . VAL B 1 63  ? 20.501 60.958 76.770  1.00 48.16  ? 127 VAL B CG2 1 
ATOM   3208  N  N   . SER B 1 64  ? 21.067 56.530 77.980  1.00 49.25  ? 128 SER B N   1 
ATOM   3209  C  CA  . SER B 1 64  ? 20.768 55.154 78.384  1.00 55.51  ? 128 SER B CA  1 
ATOM   3210  C  C   . SER B 1 64  ? 19.437 55.029 79.091  1.00 64.29  ? 128 SER B C   1 
ATOM   3211  O  O   . SER B 1 64  ? 19.047 55.911 79.846  1.00 76.80  ? 128 SER B O   1 
ATOM   3212  C  CB  . SER B 1 64  ? 21.841 54.618 79.318  1.00 63.25  ? 128 SER B CB  1 
ATOM   3213  O  OG  . SER B 1 64  ? 21.754 55.217 80.599  1.00 91.10  ? 128 SER B OG  1 
ATOM   3214  N  N   . MET B 1 65  ? 18.740 53.926 78.832  1.00 67.98  ? 129 MET B N   1 
ATOM   3215  C  CA  . MET B 1 65  ? 17.600 53.538 79.651  1.00 76.74  ? 129 MET B CA  1 
ATOM   3216  C  C   . MET B 1 65  ? 17.946 52.336 80.539  1.00 67.08  ? 129 MET B C   1 
ATOM   3217  O  O   . MET B 1 65  ? 17.082 51.778 81.199  1.00 91.89  ? 129 MET B O   1 
ATOM   3218  C  CB  . MET B 1 65  ? 16.340 53.268 78.806  1.00 75.32  ? 129 MET B CB  1 
ATOM   3219  C  CG  . MET B 1 65  ? 15.409 54.475 78.627  1.00 66.66  ? 129 MET B CG  1 
ATOM   3220  S  SD  . MET B 1 65  ? 15.226 55.037 76.927  1.00 109.04 ? 129 MET B SD  1 
ATOM   3221  C  CE  . MET B 1 65  ? 14.134 53.795 76.187  1.00 90.13  ? 129 MET B CE  1 
ATOM   3222  N  N   . GLY B 1 66  ? 19.212 51.957 80.578  1.00 61.54  ? 130 GLY B N   1 
ATOM   3223  C  CA  . GLY B 1 66  ? 19.613 50.699 81.218  1.00 67.38  ? 130 GLY B CA  1 
ATOM   3224  C  C   . GLY B 1 66  ? 19.793 49.567 80.213  1.00 75.15  ? 130 GLY B C   1 
ATOM   3225  O  O   . GLY B 1 66  ? 19.502 49.733 79.010  1.00 74.03  ? 130 GLY B O   1 
ATOM   3226  N  N   . TYR B 1 67  ? 20.289 48.422 80.695  1.00 71.87  ? 131 TYR B N   1 
ATOM   3227  C  CA  . TYR B 1 67  ? 20.474 47.250 79.840  1.00 77.11  ? 131 TYR B CA  1 
ATOM   3228  C  C   . TYR B 1 67  ? 19.163 46.521 79.597  1.00 89.56  ? 131 TYR B C   1 
ATOM   3229  O  O   . TYR B 1 67  ? 18.299 46.478 80.468  1.00 84.12  ? 131 TYR B O   1 
ATOM   3230  C  CB  . TYR B 1 67  ? 21.465 46.294 80.457  1.00 82.80  ? 131 TYR B CB  1 
ATOM   3231  C  CG  . TYR B 1 67  ? 22.811 46.905 80.739  1.00 79.09  ? 131 TYR B CG  1 
ATOM   3232  C  CD1 . TYR B 1 67  ? 23.714 47.185 79.711  1.00 68.49  ? 131 TYR B CD1 1 
ATOM   3233  C  CD2 . TYR B 1 67  ? 23.188 47.187 82.044  1.00 84.17  ? 131 TYR B CD2 1 
ATOM   3234  C  CE1 . TYR B 1 67  ? 24.958 47.743 79.992  1.00 76.05  ? 131 TYR B CE1 1 
ATOM   3235  C  CE2 . TYR B 1 67  ? 24.426 47.730 82.339  1.00 86.91  ? 131 TYR B CE2 1 
ATOM   3236  C  CZ  . TYR B 1 67  ? 25.309 48.011 81.319  1.00 89.11  ? 131 TYR B CZ  1 
ATOM   3237  O  OH  . TYR B 1 67  ? 26.539 48.553 81.649  1.00 97.02  ? 131 TYR B OH  1 
ATOM   3238  N  N   . GLY B 1 68  ? 19.025 45.938 78.412  1.00 87.59  ? 132 GLY B N   1 
ATOM   3239  C  CA  . GLY B 1 68  ? 17.767 45.324 78.017  1.00 98.39  ? 132 GLY B CA  1 
ATOM   3240  C  C   . GLY B 1 68  ? 17.440 44.097 78.834  1.00 101.11 ? 132 GLY B C   1 
ATOM   3241  O  O   . GLY B 1 68  ? 16.275 43.709 78.949  1.00 123.85 ? 132 GLY B O   1 
ATOM   3242  N  N   . THR B 1 69  ? 18.479 43.496 79.406  1.00 99.02  ? 133 THR B N   1 
ATOM   3243  C  CA  . THR B 1 69  ? 18.335 42.239 80.131  1.00 113.80 ? 133 THR B CA  1 
ATOM   3244  C  C   . THR B 1 69  ? 17.976 42.482 81.584  1.00 99.43  ? 133 THR B C   1 
ATOM   3245  O  O   . THR B 1 69  ? 17.291 41.671 82.205  1.00 113.47 ? 133 THR B O   1 
ATOM   3246  C  CB  . THR B 1 69  ? 19.598 41.332 80.009  1.00 100.21 ? 133 THR B CB  1 
ATOM   3247  O  OG1 . THR B 1 69  ? 19.453 40.194 80.866  1.00 122.69 ? 133 THR B OG1 1 
ATOM   3248  C  CG2 . THR B 1 69  ? 20.875 42.094 80.372  1.00 87.63  ? 133 THR B CG2 1 
ATOM   3249  N  N   . THR B 1 70  ? 18.431 43.615 82.106  1.00 108.85 ? 134 THR B N   1 
ATOM   3250  C  CA  . THR B 1 70  ? 18.225 43.969 83.510  1.00 128.40 ? 134 THR B CA  1 
ATOM   3251  C  C   . THR B 1 70  ? 16.996 44.870 83.680  1.00 117.78 ? 134 THR B C   1 
ATOM   3252  O  O   . THR B 1 70  ? 16.653 45.267 84.797  1.00 115.54 ? 134 THR B O   1 
ATOM   3253  C  CB  . THR B 1 70  ? 19.455 44.688 84.100  1.00 126.79 ? 134 THR B CB  1 
ATOM   3254  O  OG1 . THR B 1 70  ? 19.437 46.065 83.701  1.00 176.17 ? 134 THR B OG1 1 
ATOM   3255  C  CG2 . THR B 1 70  ? 20.749 44.038 83.624  1.00 107.30 ? 134 THR B CG2 1 
ATOM   3256  N  N   . THR B 1 71  ? 16.353 45.199 82.563  1.00 109.62 ? 135 THR B N   1 
ATOM   3257  C  CA  . THR B 1 71  ? 15.159 46.032 82.560  1.00 112.37 ? 135 THR B CA  1 
ATOM   3258  C  C   . THR B 1 71  ? 13.933 45.154 82.336  1.00 119.82 ? 135 THR B C   1 
ATOM   3259  O  O   . THR B 1 71  ? 13.880 44.362 81.386  1.00 113.23 ? 135 THR B O   1 
ATOM   3260  C  CB  . THR B 1 71  ? 15.239 47.133 81.460  1.00 117.94 ? 135 THR B CB  1 
ATOM   3261  O  OG1 . THR B 1 71  ? 16.299 48.049 81.763  1.00 97.69  ? 135 THR B OG1 1 
ATOM   3262  C  CG2 . THR B 1 71  ? 13.931 47.909 81.348  1.00 120.37 ? 135 THR B CG2 1 
ATOM   3263  N  N   . ASN B 1 72  ? 12.954 45.289 83.224  1.00 124.56 ? 136 ASN B N   1 
ATOM   3264  C  CA  . ASN B 1 72  ? 11.677 44.622 83.039  1.00 153.57 ? 136 ASN B CA  1 
ATOM   3265  C  C   . ASN B 1 72  ? 10.653 45.570 82.398  1.00 171.97 ? 136 ASN B C   1 
ATOM   3266  O  O   . ASN B 1 72  ? 10.685 46.780 82.652  1.00 148.82 ? 136 ASN B O   1 
ATOM   3267  C  CB  . ASN B 1 72  ? 11.165 44.056 84.363  1.00 140.73 ? 136 ASN B CB  1 
ATOM   3268  C  CG  . ASN B 1 72  ? 10.071 43.030 84.168  1.00 170.83 ? 136 ASN B CG  1 
ATOM   3269  O  OD1 . ASN B 1 72  ? 9.931  42.444 83.091  1.00 203.76 ? 136 ASN B OD1 1 
ATOM   3270  N  ND2 . ASN B 1 72  ? 9.284  42.807 85.211  1.00 181.62 ? 136 ASN B ND2 1 
ATOM   3271  N  N   . PHE B 1 73  ? 9.761  45.013 81.570  1.00 187.36 ? 137 PHE B N   1 
ATOM   3272  C  CA  . PHE B 1 73  ? 8.793  45.796 80.776  1.00 166.40 ? 137 PHE B CA  1 
ATOM   3273  C  C   . PHE B 1 73  ? 7.814  46.626 81.604  1.00 167.86 ? 137 PHE B C   1 
ATOM   3274  O  O   . PHE B 1 73  ? 7.513  47.771 81.244  1.00 122.26 ? 137 PHE B O   1 
ATOM   3275  C  CB  . PHE B 1 73  ? 8.004  44.902 79.803  1.00 157.58 ? 137 PHE B CB  1 
ATOM   3276  C  CG  . PHE B 1 73  ? 7.013  45.663 78.948  1.00 160.67 ? 137 PHE B CG  1 
ATOM   3277  C  CD1 . PHE B 1 73  ? 7.454  46.491 77.911  1.00 180.93 ? 137 PHE B CD1 1 
ATOM   3278  C  CD2 . PHE B 1 73  ? 5.643  45.560 79.182  1.00 131.68 ? 137 PHE B CD2 1 
ATOM   3279  C  CE1 . PHE B 1 73  ? 6.547  47.204 77.118  1.00 159.81 ? 137 PHE B CE1 1 
ATOM   3280  C  CE2 . PHE B 1 73  ? 4.725  46.270 78.396  1.00 139.07 ? 137 PHE B CE2 1 
ATOM   3281  C  CZ  . PHE B 1 73  ? 5.180  47.094 77.362  1.00 143.75 ? 137 PHE B CZ  1 
ATOM   3282  N  N   . ALA B 1 74  ? 7.318  46.035 82.696  1.00 197.51 ? 138 ALA B N   1 
ATOM   3283  C  CA  . ALA B 1 74  ? 6.319  46.664 83.578  1.00 177.14 ? 138 ALA B CA  1 
ATOM   3284  C  C   . ALA B 1 74  ? 6.781  47.997 84.173  1.00 189.93 ? 138 ALA B C   1 
ATOM   3285  O  O   . ALA B 1 74  ? 5.953  48.854 84.491  1.00 204.16 ? 138 ALA B O   1 
ATOM   3286  C  CB  . ALA B 1 74  ? 5.883  45.696 84.691  1.00 111.37 ? 138 ALA B CB  1 
ATOM   3287  N  N   . ASP B 1 75  ? 8.098  48.159 84.319  1.00 200.49 ? 139 ASP B N   1 
ATOM   3288  C  CA  . ASP B 1 75  ? 8.700  49.424 84.738  1.00 162.15 ? 139 ASP B CA  1 
ATOM   3289  C  C   . ASP B 1 75  ? 8.641  50.441 83.632  1.00 146.33 ? 139 ASP B C   1 
ATOM   3290  O  O   . ASP B 1 75  ? 8.885  50.123 82.469  1.00 150.95 ? 139 ASP B O   1 
ATOM   3291  C  CB  . ASP B 1 75  ? 10.175 49.244 85.096  1.00 150.36 ? 139 ASP B CB  1 
ATOM   3292  C  CG  . ASP B 1 75  ? 10.381 48.430 86.351  1.00 164.24 ? 139 ASP B CG  1 
ATOM   3293  O  OD1 . ASP B 1 75  ? 9.416  48.240 87.119  1.00 185.78 ? 139 ASP B OD1 1 
ATOM   3294  O  OD2 . ASP B 1 75  ? 11.523 47.980 86.572  1.00 175.64 ? 139 ASP B OD2 1 
ATOM   3295  N  N   . LEU B 1 76  ? 8.304  51.665 84.000  1.00 157.22 ? 140 LEU B N   1 
ATOM   3296  C  CA  . LEU B 1 76  ? 8.598  52.802 83.157  1.00 176.73 ? 140 LEU B CA  1 
ATOM   3297  C  C   . LEU B 1 76  ? 9.812  53.415 83.830  1.00 151.05 ? 140 LEU B C   1 
ATOM   3298  O  O   . LEU B 1 76  ? 9.847  53.516 85.054  1.00 123.03 ? 140 LEU B O   1 
ATOM   3299  C  CB  . LEU B 1 76  ? 7.406  53.776 83.072  1.00 192.18 ? 140 LEU B CB  1 
ATOM   3300  C  CG  . LEU B 1 76  ? 6.315  53.504 82.013  1.00 185.07 ? 140 LEU B CG  1 
ATOM   3301  C  CD1 . LEU B 1 76  ? 5.459  52.262 82.333  1.00 163.50 ? 140 LEU B CD1 1 
ATOM   3302  C  CD2 . LEU B 1 76  ? 5.419  54.731 81.792  1.00 154.82 ? 140 LEU B CD2 1 
ATOM   3303  N  N   . ILE B 1 77  ? 10.831 53.753 83.042  1.00 171.17 ? 141 ILE B N   1 
ATOM   3304  C  CA  . ILE B 1 77  ? 12.043 54.369 83.591  1.00 153.28 ? 141 ILE B CA  1 
ATOM   3305  C  C   . ILE B 1 77  ? 12.046 55.895 83.451  1.00 117.91 ? 141 ILE B C   1 
ATOM   3306  O  O   . ILE B 1 77  ? 11.379 56.474 82.586  1.00 110.76 ? 141 ILE B O   1 
ATOM   3307  C  CB  . ILE B 1 77  ? 13.357 53.731 83.045  1.00 165.36 ? 141 ILE B CB  1 
ATOM   3308  C  CG1 . ILE B 1 77  ? 14.554 54.158 83.913  1.00 131.93 ? 141 ILE B CG1 1 
ATOM   3309  C  CG2 . ILE B 1 77  ? 13.558 54.083 81.570  1.00 174.46 ? 141 ILE B CG2 1 
ATOM   3310  C  CD1 . ILE B 1 77  ? 15.648 53.125 84.056  1.00 115.81 ? 141 ILE B CD1 1 
ATOM   3311  N  N   . VAL B 1 78  ? 12.839 56.526 84.304  1.00 87.60  ? 142 VAL B N   1 
ATOM   3312  C  CA  . VAL B 1 78  ? 12.662 57.918 84.616  1.00 86.88  ? 142 VAL B CA  1 
ATOM   3313  C  C   . VAL B 1 78  ? 13.942 58.722 84.409  1.00 84.18  ? 142 VAL B C   1 
ATOM   3314  O  O   . VAL B 1 78  ? 15.025 58.236 84.709  1.00 84.02  ? 142 VAL B O   1 
ATOM   3315  C  CB  . VAL B 1 78  ? 12.160 58.033 86.061  1.00 86.26  ? 142 VAL B CB  1 
ATOM   3316  C  CG1 . VAL B 1 78  ? 13.128 57.372 87.024  1.00 74.76  ? 142 VAL B CG1 1 
ATOM   3317  C  CG2 . VAL B 1 78  ? 11.889 59.474 86.430  1.00 104.84 ? 142 VAL B CG2 1 
ATOM   3318  N  N   . SER B 1 79  ? 13.793 59.950 83.907  1.00 88.47  ? 143 SER B N   1 
ATOM   3319  C  CA  . SER B 1 79  ? 14.906 60.851 83.556  1.00 83.98  ? 143 SER B CA  1 
ATOM   3320  C  C   . SER B 1 79  ? 16.066 60.933 84.570  1.00 81.45  ? 143 SER B C   1 
ATOM   3321  O  O   . SER B 1 79  ? 17.251 61.010 84.194  1.00 79.63  ? 143 SER B O   1 
ATOM   3322  C  CB  . SER B 1 79  ? 14.370 62.254 83.276  1.00 82.34  ? 143 SER B CB  1 
ATOM   3323  O  OG  . SER B 1 79  ? 13.261 62.188 82.405  1.00 99.34  ? 143 SER B OG  1 
ATOM   3324  N  N   . GLU B 1 80  ? 15.743 60.908 85.854  1.00 71.86  ? 144 GLU B N   1 
ATOM   3325  C  CA  . GLU B 1 80  ? 16.792 61.044 86.863  1.00 87.14  ? 144 GLU B CA  1 
ATOM   3326  C  C   . GLU B 1 80  ? 17.772 59.888 86.850  1.00 86.60  ? 144 GLU B C   1 
ATOM   3327  O  O   . GLU B 1 80  ? 18.865 60.020 87.369  1.00 90.23  ? 144 GLU B O   1 
ATOM   3328  C  CB  . GLU B 1 80  ? 16.211 61.222 88.266  1.00 89.88  ? 144 GLU B CB  1 
ATOM   3329  C  CG  . GLU B 1 80  ? 15.486 62.553 88.485  1.00 115.89 ? 144 GLU B CG  1 
ATOM   3330  C  CD  . GLU B 1 80  ? 14.197 62.690 87.665  1.00 146.17 ? 144 GLU B CD  1 
ATOM   3331  O  OE1 . GLU B 1 80  ? 13.596 61.662 87.286  1.00 163.40 ? 144 GLU B OE1 1 
ATOM   3332  O  OE2 . GLU B 1 80  ? 13.783 63.836 87.395  1.00 153.54 ? 144 GLU B OE2 1 
ATOM   3333  N  N   . GLN B 1 81  ? 17.374 58.767 86.255  1.00 79.53  ? 145 GLN B N   1 
ATOM   3334  C  CA  . GLN B 1 81  ? 18.175 57.561 86.275  1.00 75.44  ? 145 GLN B CA  1 
ATOM   3335  C  C   . GLN B 1 81  ? 19.067 57.514 85.041  1.00 69.80  ? 145 GLN B C   1 
ATOM   3336  O  O   . GLN B 1 81  ? 19.950 56.667 84.921  1.00 69.46  ? 145 GLN B O   1 
ATOM   3337  C  CB  . GLN B 1 81  ? 17.273 56.325 86.352  1.00 85.20  ? 145 GLN B CB  1 
ATOM   3338  C  CG  . GLN B 1 81  ? 16.495 56.167 87.668  1.00 96.42  ? 145 GLN B CG  1 
ATOM   3339  C  CD  . GLN B 1 81  ? 15.901 54.763 87.858  1.00 118.14 ? 145 GLN B CD  1 
ATOM   3340  O  OE1 . GLN B 1 81  ? 14.981 54.346 87.144  1.00 142.06 ? 145 GLN B OE1 1 
ATOM   3341  N  NE2 . GLN B 1 81  ? 16.429 54.037 88.831  1.00 113.28 ? 145 GLN B NE2 1 
ATOM   3342  N  N   . MET B 1 82  ? 18.869 58.470 84.151  1.00 63.92  ? 146 MET B N   1 
ATOM   3343  C  CA  . MET B 1 82  ? 19.484 58.411 82.846  1.00 59.25  ? 146 MET B CA  1 
ATOM   3344  C  C   . MET B 1 82  ? 20.877 59.008 82.789  1.00 65.14  ? 146 MET B C   1 
ATOM   3345  O  O   . MET B 1 82  ? 21.166 60.025 83.453  1.00 73.84  ? 146 MET B O   1 
ATOM   3346  C  CB  . MET B 1 82  ? 18.585 59.113 81.853  1.00 56.92  ? 146 MET B CB  1 
ATOM   3347  C  CG  . MET B 1 82  ? 17.313 58.349 81.585  1.00 66.12  ? 146 MET B CG  1 
ATOM   3348  S  SD  . MET B 1 82  ? 16.139 59.254 80.566  1.00 80.40  ? 146 MET B SD  1 
ATOM   3349  C  CE  . MET B 1 82  ? 14.934 57.984 80.249  1.00 68.62  ? 146 MET B CE  1 
ATOM   3350  N  N   . ASN B 1 83  ? 21.710 58.379 81.957  1.00 58.66  ? 147 ASN B N   1 
ATOM   3351  C  CA  . ASN B 1 83  ? 23.115 58.756 81.746  1.00 64.22  ? 147 ASN B CA  1 
ATOM   3352  C  C   . ASN B 1 83  ? 23.458 58.961 80.296  1.00 65.71  ? 147 ASN B C   1 
ATOM   3353  O  O   . ASN B 1 83  ? 22.873 58.313 79.432  1.00 81.49  ? 147 ASN B O   1 
ATOM   3354  C  CB  . ASN B 1 83  ? 24.035 57.660 82.257  1.00 61.97  ? 147 ASN B CB  1 
ATOM   3355  C  CG  . ASN B 1 83  ? 24.072 57.601 83.734  1.00 67.34  ? 147 ASN B CG  1 
ATOM   3356  O  OD1 . ASN B 1 83  ? 24.107 58.625 84.405  1.00 85.54  ? 147 ASN B OD1 1 
ATOM   3357  N  ND2 . ASN B 1 83  ? 24.046 56.400 84.270  1.00 77.56  ? 147 ASN B ND2 1 
ATOM   3358  N  N   . VAL B 1 84  ? 24.427 59.834 80.027  1.00 58.09  ? 148 VAL B N   1 
ATOM   3359  C  CA  . VAL B 1 84  ? 24.833 60.081 78.643  1.00 55.55  ? 148 VAL B CA  1 
ATOM   3360  C  C   . VAL B 1 84  ? 26.080 59.272 78.233  1.00 54.11  ? 148 VAL B C   1 
ATOM   3361  O  O   . VAL B 1 84  ? 27.183 59.499 78.754  1.00 49.54  ? 148 VAL B O   1 
ATOM   3362  C  CB  . VAL B 1 84  ? 25.063 61.567 78.350  1.00 48.99  ? 148 VAL B CB  1 
ATOM   3363  C  CG1 . VAL B 1 84  ? 25.385 61.748 76.893  1.00 44.79  ? 148 VAL B CG1 1 
ATOM   3364  C  CG2 . VAL B 1 84  ? 23.836 62.364 78.686  1.00 47.83  ? 148 VAL B CG2 1 
ATOM   3365  N  N   . TYR B 1 85  ? 25.882 58.365 77.275  1.00 48.74  ? 149 TYR B N   1 
ATOM   3366  C  CA  . TYR B 1 85  ? 26.945 57.580 76.700  1.00 47.99  ? 149 TYR B CA  1 
ATOM   3367  C  C   . TYR B 1 85  ? 27.307 57.953 75.286  1.00 46.38  ? 149 TYR B C   1 
ATOM   3368  O  O   . TYR B 1 85  ? 26.544 58.540 74.554  1.00 57.79  ? 149 TYR B O   1 
ATOM   3369  C  CB  . TYR B 1 85  ? 26.554 56.121 76.716  1.00 48.77  ? 149 TYR B CB  1 
ATOM   3370  C  CG  . TYR B 1 85  ? 26.528 55.533 78.097  1.00 51.89  ? 149 TYR B CG  1 
ATOM   3371  C  CD1 . TYR B 1 85  ? 27.696 55.063 78.691  1.00 49.71  ? 149 TYR B CD1 1 
ATOM   3372  C  CD2 . TYR B 1 85  ? 25.332 55.446 78.810  1.00 48.31  ? 149 TYR B CD2 1 
ATOM   3373  C  CE1 . TYR B 1 85  ? 27.669 54.513 79.953  1.00 52.30  ? 149 TYR B CE1 1 
ATOM   3374  C  CE2 . TYR B 1 85  ? 25.289 54.888 80.062  1.00 52.38  ? 149 TYR B CE2 1 
ATOM   3375  C  CZ  . TYR B 1 85  ? 26.470 54.426 80.631  1.00 57.16  ? 149 TYR B CZ  1 
ATOM   3376  O  OH  . TYR B 1 85  ? 26.470 53.877 81.885  1.00 66.68  ? 149 TYR B OH  1 
ATOM   3377  N  N   . SER B 1 86  ? 28.491 57.545 74.902  1.00 49.85  ? 150 SER B N   1 
ATOM   3378  C  CA  . SER B 1 86  ? 28.988 57.712 73.562  1.00 57.78  ? 150 SER B CA  1 
ATOM   3379  C  C   . SER B 1 86  ? 29.443 56.329 73.041  1.00 53.03  ? 150 SER B C   1 
ATOM   3380  O  O   . SER B 1 86  ? 29.651 55.404 73.811  1.00 62.52  ? 150 SER B O   1 
ATOM   3381  C  CB  . SER B 1 86  ? 30.145 58.711 73.608  1.00 68.74  ? 150 SER B CB  1 
ATOM   3382  O  OG  . SER B 1 86  ? 30.774 58.862 72.363  1.00 106.89 ? 150 SER B OG  1 
ATOM   3383  N  N   . VAL B 1 87  ? 29.590 56.199 71.734  1.00 49.97  ? 151 VAL B N   1 
ATOM   3384  C  CA  . VAL B 1 87  ? 30.072 54.981 71.080  1.00 54.83  ? 151 VAL B CA  1 
ATOM   3385  C  C   . VAL B 1 87  ? 30.599 55.444 69.705  1.00 58.63  ? 151 VAL B C   1 
ATOM   3386  O  O   . VAL B 1 87  ? 30.256 56.557 69.249  1.00 63.34  ? 151 VAL B O   1 
ATOM   3387  C  CB  . VAL B 1 87  ? 28.946 53.908 70.940  1.00 51.60  ? 151 VAL B CB  1 
ATOM   3388  C  CG1 . VAL B 1 87  ? 27.986 54.295 69.836  1.00 59.18  ? 151 VAL B CG1 1 
ATOM   3389  C  CG2 . VAL B 1 87  ? 29.517 52.599 70.594  1.00 49.67  ? 151 VAL B CG2 1 
ATOM   3390  N  N   . LYS B 1 88  ? 31.413 54.634 69.030  1.00 53.00  ? 152 LYS B N   1 
ATOM   3391  C  CA  . LYS B 1 88  ? 31.946 55.088 67.742  1.00 56.05  ? 152 LYS B CA  1 
ATOM   3392  C  C   . LYS B 1 88  ? 30.935 54.729 66.700  1.00 55.82  ? 152 LYS B C   1 
ATOM   3393  O  O   . LYS B 1 88  ? 30.470 53.603 66.691  1.00 74.20  ? 152 LYS B O   1 
ATOM   3394  C  CB  . LYS B 1 88  ? 33.255 54.409 67.400  1.00 72.62  ? 152 LYS B CB  1 
ATOM   3395  C  CG  . LYS B 1 88  ? 33.971 55.043 66.216  1.00 89.85  ? 152 LYS B CG  1 
ATOM   3396  C  CD  . LYS B 1 88  ? 34.824 54.039 65.432  1.00 109.04 ? 152 LYS B CD  1 
ATOM   3397  C  CE  . LYS B 1 88  ? 34.003 53.357 64.339  1.00 117.77 ? 152 LYS B CE  1 
ATOM   3398  N  NZ  . LYS B 1 88  ? 34.736 52.250 63.663  1.00 153.64 ? 152 LYS B NZ  1 
ATOM   3399  N  N   . LEU B 1 89  ? 30.561 55.672 65.838  1.00 57.57  ? 153 LEU B N   1 
ATOM   3400  C  CA  . LEU B 1 89  ? 29.498 55.398 64.857  1.00 57.94  ? 153 LEU B CA  1 
ATOM   3401  C  C   . LEU B 1 89  ? 29.832 54.169 64.008  1.00 68.80  ? 153 LEU B C   1 
ATOM   3402  O  O   . LEU B 1 89  ? 30.872 54.134 63.348  1.00 77.43  ? 153 LEU B O   1 
ATOM   3403  C  CB  . LEU B 1 89  ? 29.228 56.600 63.953  1.00 48.49  ? 153 LEU B CB  1 
ATOM   3404  C  CG  . LEU B 1 89  ? 28.206 56.365 62.814  1.00 46.51  ? 153 LEU B CG  1 
ATOM   3405  C  CD1 . LEU B 1 89  ? 26.803 55.973 63.282  1.00 44.58  ? 153 LEU B CD1 1 
ATOM   3406  C  CD2 . LEU B 1 89  ? 28.109 57.579 61.911  1.00 38.74  ? 153 LEU B CD2 1 
ATOM   3407  N  N   . GLY B 1 90  ? 28.957 53.171 64.033  1.00 59.79  ? 154 GLY B N   1 
ATOM   3408  C  CA  . GLY B 1 90  ? 29.277 51.906 63.391  1.00 60.72  ? 154 GLY B CA  1 
ATOM   3409  C  C   . GLY B 1 90  ? 29.493 50.795 64.392  1.00 71.62  ? 154 GLY B C   1 
ATOM   3410  O  O   . GLY B 1 90  ? 29.510 49.624 64.033  1.00 107.46 ? 154 GLY B O   1 
ATOM   3411  N  N   . ASP B 1 91  ? 29.678 51.157 65.653  1.00 71.00  ? 155 ASP B N   1 
ATOM   3412  C  CA  . ASP B 1 91  ? 29.763 50.165 66.716  1.00 67.38  ? 155 ASP B CA  1 
ATOM   3413  C  C   . ASP B 1 91  ? 28.391 50.065 67.377  1.00 70.70  ? 155 ASP B C   1 
ATOM   3414  O  O   . ASP B 1 91  ? 27.616 51.038 67.355  1.00 71.72  ? 155 ASP B O   1 
ATOM   3415  C  CB  . ASP B 1 91  ? 30.869 50.507 67.730  1.00 78.90  ? 155 ASP B CB  1 
ATOM   3416  C  CG  . ASP B 1 91  ? 32.289 50.158 67.215  1.00 97.48  ? 155 ASP B CG  1 
ATOM   3417  O  OD1 . ASP B 1 91  ? 32.421 49.407 66.220  1.00 103.21 ? 155 ASP B OD1 1 
ATOM   3418  O  OD2 . ASP B 1 91  ? 33.280 50.635 67.814  1.00 87.22  ? 155 ASP B OD2 1 
ATOM   3419  N  N   . PRO B 1 92  ? 28.052 48.866 67.890  1.00 68.82  ? 156 PRO B N   1 
ATOM   3420  C  CA  . PRO B 1 92  ? 26.818 48.666 68.623  1.00 62.46  ? 156 PRO B CA  1 
ATOM   3421  C  C   . PRO B 1 92  ? 26.995 49.027 70.097  1.00 59.54  ? 156 PRO B C   1 
ATOM   3422  O  O   . PRO B 1 92  ? 28.065 48.833 70.642  1.00 64.88  ? 156 PRO B O   1 
ATOM   3423  C  CB  . PRO B 1 92  ? 26.571 47.170 68.465  1.00 58.14  ? 156 PRO B CB  1 
ATOM   3424  C  CG  . PRO B 1 92  ? 27.913 46.596 68.406  1.00 67.59  ? 156 PRO B CG  1 
ATOM   3425  C  CD  . PRO B 1 92  ? 28.709 47.580 67.598  1.00 74.36  ? 156 PRO B CD  1 
ATOM   3426  N  N   . PRO B 1 93  ? 25.946 49.563 70.736  1.00 64.75  ? 157 PRO B N   1 
ATOM   3427  C  CA  . PRO B 1 93  ? 26.006 49.854 72.160  1.00 60.26  ? 157 PRO B CA  1 
ATOM   3428  C  C   . PRO B 1 93  ? 26.045 48.606 73.082  1.00 66.43  ? 157 PRO B C   1 
ATOM   3429  O  O   . PRO B 1 93  ? 25.147 48.402 73.924  1.00 65.20  ? 157 PRO B O   1 
ATOM   3430  C  CB  . PRO B 1 93  ? 24.749 50.720 72.393  1.00 52.77  ? 157 PRO B CB  1 
ATOM   3431  C  CG  . PRO B 1 93  ? 23.838 50.379 71.296  1.00 56.05  ? 157 PRO B CG  1 
ATOM   3432  C  CD  . PRO B 1 93  ? 24.707 50.085 70.117  1.00 64.37  ? 157 PRO B CD  1 
ATOM   3433  N  N   . THR B 1 94  ? 27.086 47.786 72.914  1.00 74.14  ? 158 THR B N   1 
ATOM   3434  C  CA  . THR B 1 94  ? 27.415 46.718 73.874  1.00 77.85  ? 158 THR B CA  1 
ATOM   3435  C  C   . THR B 1 94  ? 28.121 47.367 75.043  1.00 82.57  ? 158 THR B C   1 
ATOM   3436  O  O   . THR B 1 94  ? 28.729 48.429 74.888  1.00 90.44  ? 158 THR B O   1 
ATOM   3437  C  CB  . THR B 1 94  ? 28.333 45.574 73.294  1.00 77.19  ? 158 THR B CB  1 
ATOM   3438  O  OG1 . THR B 1 94  ? 29.407 46.118 72.515  1.00 63.89  ? 158 THR B OG1 1 
ATOM   3439  C  CG2 . THR B 1 94  ? 27.531 44.620 72.424  1.00 88.97  ? 158 THR B CG2 1 
ATOM   3440  N  N   . PRO B 1 95  ? 28.043 46.735 76.219  1.00 82.53  ? 159 PRO B N   1 
ATOM   3441  C  CA  . PRO B 1 95  ? 28.648 47.249 77.449  1.00 89.84  ? 159 PRO B CA  1 
ATOM   3442  C  C   . PRO B 1 95  ? 30.124 47.562 77.288  1.00 86.45  ? 159 PRO B C   1 
ATOM   3443  O  O   . PRO B 1 95  ? 30.621 48.523 77.882  1.00 123.03 ? 159 PRO B O   1 
ATOM   3444  C  CB  . PRO B 1 95  ? 28.464 46.094 78.425  1.00 82.59  ? 159 PRO B CB  1 
ATOM   3445  C  CG  . PRO B 1 95  ? 27.212 45.438 77.960  1.00 77.02  ? 159 PRO B CG  1 
ATOM   3446  C  CD  . PRO B 1 95  ? 27.234 45.531 76.467  1.00 71.18  ? 159 PRO B CD  1 
ATOM   3447  N  N   . ASP B 1 96  ? 30.801 46.764 76.469  1.00 87.54  ? 160 ASP B N   1 
ATOM   3448  C  CA  . ASP B 1 96  ? 32.238 46.919 76.206  1.00 101.03 ? 160 ASP B CA  1 
ATOM   3449  C  C   . ASP B 1 96  ? 32.605 48.049 75.226  1.00 88.82  ? 160 ASP B C   1 
ATOM   3450  O  O   . ASP B 1 96  ? 33.737 48.545 75.232  1.00 91.60  ? 160 ASP B O   1 
ATOM   3451  C  CB  . ASP B 1 96  ? 32.811 45.595 75.715  1.00 112.40 ? 160 ASP B CB  1 
ATOM   3452  C  CG  . ASP B 1 96  ? 32.355 44.418 76.555  1.00 136.24 ? 160 ASP B CG  1 
ATOM   3453  O  OD1 . ASP B 1 96  ? 31.978 44.609 77.731  1.00 144.69 ? 160 ASP B OD1 1 
ATOM   3454  O  OD2 . ASP B 1 96  ? 32.369 43.289 76.033  1.00 166.09 ? 160 ASP B OD2 1 
ATOM   3455  N  N   . LYS B 1 97  ? 31.651 48.453 74.392  1.00 71.63  ? 161 LYS B N   1 
ATOM   3456  C  CA  . LYS B 1 97  ? 31.851 49.582 73.490  1.00 61.07  ? 161 LYS B CA  1 
ATOM   3457  C  C   . LYS B 1 97  ? 31.512 50.931 74.102  1.00 61.89  ? 161 LYS B C   1 
ATOM   3458  O  O   . LYS B 1 97  ? 32.001 51.963 73.638  1.00 72.50  ? 161 LYS B O   1 
ATOM   3459  C  CB  . LYS B 1 97  ? 31.028 49.411 72.227  1.00 57.13  ? 161 LYS B CB  1 
ATOM   3460  C  CG  . LYS B 1 97  ? 31.569 48.373 71.275  1.00 70.98  ? 161 LYS B CG  1 
ATOM   3461  C  CD  . LYS B 1 97  ? 33.043 48.599 70.999  1.00 81.23  ? 161 LYS B CD  1 
ATOM   3462  C  CE  . LYS B 1 97  ? 33.522 47.671 69.907  1.00 95.96  ? 161 LYS B CE  1 
ATOM   3463  N  NZ  . LYS B 1 97  ? 34.976 47.817 69.703  1.00 118.61 ? 161 LYS B NZ  1 
ATOM   3464  N  N   . LEU B 1 98  ? 30.679 50.935 75.134  1.00 60.85  ? 162 LEU B N   1 
ATOM   3465  C  CA  . LEU B 1 98  ? 30.164 52.190 75.662  1.00 57.87  ? 162 LEU B CA  1 
ATOM   3466  C  C   . LEU B 1 98  ? 31.273 53.029 76.234  1.00 58.43  ? 162 LEU B C   1 
ATOM   3467  O  O   . LEU B 1 98  ? 32.211 52.509 76.837  1.00 68.73  ? 162 LEU B O   1 
ATOM   3468  C  CB  . LEU B 1 98  ? 29.114 51.937 76.738  1.00 59.12  ? 162 LEU B CB  1 
ATOM   3469  C  CG  . LEU B 1 98  ? 27.803 51.334 76.283  1.00 61.81  ? 162 LEU B CG  1 
ATOM   3470  C  CD1 . LEU B 1 98  ? 26.755 51.757 77.284  1.00 87.12  ? 162 LEU B CD1 1 
ATOM   3471  C  CD2 . LEU B 1 98  ? 27.430 51.828 74.912  1.00 52.44  ? 162 LEU B CD2 1 
ATOM   3472  N  N   . LYS B 1 99  ? 31.171 54.331 76.029  1.00 54.77  ? 163 LYS B N   1 
ATOM   3473  C  CA  . LYS B 1 99  ? 31.981 55.293 76.799  1.00 61.92  ? 163 LYS B CA  1 
ATOM   3474  C  C   . LYS B 1 99  ? 31.095 56.225 77.634  1.00 60.10  ? 163 LYS B C   1 
ATOM   3475  O  O   . LYS B 1 99  ? 30.248 56.940 77.121  1.00 56.63  ? 163 LYS B O   1 
ATOM   3476  C  CB  . LYS B 1 99  ? 32.887 56.106 75.879  1.00 58.86  ? 163 LYS B CB  1 
ATOM   3477  C  CG  . LYS B 1 99  ? 33.571 57.266 76.543  1.00 59.13  ? 163 LYS B CG  1 
ATOM   3478  C  CD  . LYS B 1 99  ? 34.779 57.645 75.721  1.00 68.68  ? 163 LYS B CD  1 
ATOM   3479  C  CE  . LYS B 1 99  ? 35.015 59.129 75.759  1.00 77.91  ? 163 LYS B CE  1 
ATOM   3480  N  NZ  . LYS B 1 99  ? 35.889 59.503 76.912  1.00 114.96 ? 163 LYS B NZ  1 
ATOM   3481  N  N   . PHE B 1 100 ? 31.270 56.196 78.939  1.00 71.89  ? 164 PHE B N   1 
ATOM   3482  C  CA  . PHE B 1 100 ? 30.477 57.073 79.782  1.00 68.72  ? 164 PHE B CA  1 
ATOM   3483  C  C   . PHE B 1 100 ? 30.841 58.517 79.494  1.00 69.34  ? 164 PHE B C   1 
ATOM   3484  O  O   . PHE B 1 100 ? 32.019 58.864 79.481  1.00 74.80  ? 164 PHE B O   1 
ATOM   3485  C  CB  . PHE B 1 100 ? 30.709 56.778 81.250  1.00 57.35  ? 164 PHE B CB  1 
ATOM   3486  C  CG  . PHE B 1 100 ? 29.776 57.503 82.133  1.00 62.33  ? 164 PHE B CG  1 
ATOM   3487  C  CD1 . PHE B 1 100 ? 30.001 58.844 82.466  1.00 66.49  ? 164 PHE B CD1 1 
ATOM   3488  C  CD2 . PHE B 1 100 ? 28.645 56.875 82.632  1.00 64.22  ? 164 PHE B CD2 1 
ATOM   3489  C  CE1 . PHE B 1 100 ? 29.122 59.544 83.311  1.00 56.76  ? 164 PHE B CE1 1 
ATOM   3490  C  CE2 . PHE B 1 100 ? 27.758 57.576 83.471  1.00 60.12  ? 164 PHE B CE2 1 
ATOM   3491  C  CZ  . PHE B 1 100 ? 28.006 58.909 83.801  1.00 55.64  ? 164 PHE B CZ  1 
ATOM   3492  N  N   . GLU B 1 101 ? 29.833 59.355 79.267  1.00 64.91  ? 165 GLU B N   1 
ATOM   3493  C  CA  . GLU B 1 101 ? 30.099 60.725 78.871  1.00 63.31  ? 165 GLU B CA  1 
ATOM   3494  C  C   . GLU B 1 101 ? 29.725 61.747 79.923  1.00 65.69  ? 165 GLU B C   1 
ATOM   3495  O  O   . GLU B 1 101 ? 30.510 62.656 80.173  1.00 67.04  ? 165 GLU B O   1 
ATOM   3496  C  CB  . GLU B 1 101 ? 29.439 61.042 77.541  1.00 63.66  ? 165 GLU B CB  1 
ATOM   3497  C  CG  . GLU B 1 101 ? 30.192 60.519 76.316  1.00 65.88  ? 165 GLU B CG  1 
ATOM   3498  C  CD  . GLU B 1 101 ? 31.500 61.248 75.998  1.00 78.05  ? 165 GLU B CD  1 
ATOM   3499  O  OE1 . GLU B 1 101 ? 32.029 61.997 76.879  1.00 107.87 ? 165 GLU B OE1 1 
ATOM   3500  O  OE2 . GLU B 1 101 ? 31.998 61.054 74.848  1.00 80.90  ? 165 GLU B OE2 1 
ATOM   3501  N  N   . ALA B 1 102 ? 28.539 61.592 80.521  1.00 64.42  ? 166 ALA B N   1 
ATOM   3502  C  CA  . ALA B 1 102 ? 28.100 62.388 81.682  1.00 60.81  ? 166 ALA B CA  1 
ATOM   3503  C  C   . ALA B 1 102 ? 26.775 61.873 82.243  1.00 59.31  ? 166 ALA B C   1 
ATOM   3504  O  O   . ALA B 1 102 ? 26.133 61.019 81.618  1.00 62.44  ? 166 ALA B O   1 
ATOM   3505  C  CB  . ALA B 1 102 ? 27.937 63.804 81.287  1.00 78.12  ? 166 ALA B CB  1 
ATOM   3506  N  N   . VAL B 1 103 ? 26.346 62.407 83.395  1.00 55.96  ? 167 VAL B N   1 
ATOM   3507  C  CA  . VAL B 1 103 ? 25.020 62.050 83.959  1.00 56.79  ? 167 VAL B CA  1 
ATOM   3508  C  C   . VAL B 1 103 ? 24.004 63.050 83.491  1.00 61.09  ? 167 VAL B C   1 
ATOM   3509  O  O   . VAL B 1 103 ? 24.239 64.251 83.598  1.00 77.01  ? 167 VAL B O   1 
ATOM   3510  C  CB  . VAL B 1 103 ? 24.974 62.102 85.462  1.00 54.49  ? 167 VAL B CB  1 
ATOM   3511  C  CG1 . VAL B 1 103 ? 25.855 61.005 86.075  1.00 59.00  ? 167 VAL B CG1 1 
ATOM   3512  C  CG2 . VAL B 1 103 ? 25.473 63.431 85.886  1.00 58.80  ? 167 VAL B CG2 1 
ATOM   3513  N  N   . GLY B 1 104 ? 22.882 62.563 82.969  1.00 56.35  ? 168 GLY B N   1 
ATOM   3514  C  CA  . GLY B 1 104 ? 21.868 63.440 82.447  1.00 55.51  ? 168 GLY B CA  1 
ATOM   3515  C  C   . GLY B 1 104 ? 20.898 62.712 81.555  1.00 64.07  ? 168 GLY B C   1 
ATOM   3516  O  O   . GLY B 1 104 ? 21.145 61.555 81.177  1.00 56.56  ? 168 GLY B O   1 
ATOM   3517  N  N   . TRP B 1 105 ? 19.798 63.397 81.219  1.00 64.86  ? 169 TRP B N   1 
ATOM   3518  C  CA  . TRP B 1 105 ? 18.709 62.807 80.455  1.00 57.93  ? 169 TRP B CA  1 
ATOM   3519  C  C   . TRP B 1 105 ? 18.600 63.482 79.152  1.00 59.75  ? 169 TRP B C   1 
ATOM   3520  O  O   . TRP B 1 105 ? 17.740 63.123 78.353  1.00 65.38  ? 169 TRP B O   1 
ATOM   3521  C  CB  . TRP B 1 105 ? 17.372 62.910 81.193  1.00 61.66  ? 169 TRP B CB  1 
ATOM   3522  C  CG  . TRP B 1 105 ? 16.945 64.321 81.502  1.00 61.58  ? 169 TRP B CG  1 
ATOM   3523  C  CD1 . TRP B 1 105 ? 16.458 65.278 80.617  1.00 62.22  ? 169 TRP B CD1 1 
ATOM   3524  C  CD2 . TRP B 1 105 ? 16.941 64.971 82.800  1.00 60.21  ? 169 TRP B CD2 1 
ATOM   3525  N  NE1 . TRP B 1 105 ? 16.170 66.447 81.271  1.00 67.86  ? 169 TRP B NE1 1 
ATOM   3526  C  CE2 . TRP B 1 105 ? 16.444 66.331 82.580  1.00 68.27  ? 169 TRP B CE2 1 
ATOM   3527  C  CE3 . TRP B 1 105 ? 17.305 64.594 84.065  1.00 77.61  ? 169 TRP B CE3 1 
ATOM   3528  C  CZ2 . TRP B 1 105 ? 16.330 67.247 83.611  1.00 74.39  ? 169 TRP B CZ2 1 
ATOM   3529  C  CZ3 . TRP B 1 105 ? 17.186 65.526 85.108  1.00 93.35  ? 169 TRP B CZ3 1 
ATOM   3530  C  CH2 . TRP B 1 105 ? 16.709 66.821 84.883  1.00 87.03  ? 169 TRP B CH2 1 
ATOM   3531  N  N   . SER B 1 106 ? 19.441 64.491 78.930  1.00 59.79  ? 170 SER B N   1 
ATOM   3532  C  CA  . SER B 1 106 ? 19.489 65.177 77.628  1.00 56.70  ? 170 SER B CA  1 
ATOM   3533  C  C   . SER B 1 106 ? 20.864 65.746 77.365  1.00 51.18  ? 170 SER B C   1 
ATOM   3534  O  O   . SER B 1 106 ? 21.539 66.212 78.284  1.00 53.74  ? 170 SER B O   1 
ATOM   3535  C  CB  . SER B 1 106 ? 18.428 66.274 77.542  1.00 65.19  ? 170 SER B CB  1 
ATOM   3536  O  OG  . SER B 1 106 ? 18.750 67.264 76.572  1.00 61.79  ? 170 SER B OG  1 
ATOM   3537  N  N   . ALA B 1 107 ? 21.286 65.702 76.113  1.00 45.19  ? 171 ALA B N   1 
ATOM   3538  C  CA  . ALA B 1 107 ? 22.679 65.976 75.816  1.00 48.44  ? 171 ALA B CA  1 
ATOM   3539  C  C   . ALA B 1 107 ? 22.895 66.448 74.421  1.00 46.71  ? 171 ALA B C   1 
ATOM   3540  O  O   . ALA B 1 107 ? 22.191 66.058 73.533  1.00 57.84  ? 171 ALA B O   1 
ATOM   3541  C  CB  . ALA B 1 107 ? 23.564 64.729 76.076  1.00 47.50  ? 171 ALA B CB  1 
ATOM   3542  N  N   . SER B 1 108 ? 23.910 67.270 74.253  1.00 50.62  ? 172 SER B N   1 
ATOM   3543  C  CA  . SER B 1 108 ? 24.417 67.679 72.967  1.00 54.58  ? 172 SER B CA  1 
ATOM   3544  C  C   . SER B 1 108 ? 25.964 67.677 72.997  1.00 57.46  ? 172 SER B C   1 
ATOM   3545  O  O   . SER B 1 108 ? 26.566 67.825 74.061  1.00 71.52  ? 172 SER B O   1 
ATOM   3546  C  CB  . SER B 1 108 ? 23.853 69.064 72.638  1.00 56.64  ? 172 SER B CB  1 
ATOM   3547  O  OG  . SER B 1 108 ? 24.755 69.801 71.835  1.00 64.58  ? 172 SER B OG  1 
ATOM   3548  N  N   . SER B 1 109 ? 26.615 67.499 71.855  1.00 54.32  ? 173 SER B N   1 
ATOM   3549  C  CA  . SER B 1 109 ? 28.069 67.462 71.864  1.00 61.61  ? 173 SER B CA  1 
ATOM   3550  C  C   . SER B 1 109 ? 28.677 67.839 70.530  1.00 64.01  ? 173 SER B C   1 
ATOM   3551  O  O   . SER B 1 109 ? 27.989 67.812 69.504  1.00 60.48  ? 173 SER B O   1 
ATOM   3552  C  CB  . SER B 1 109 ? 28.561 66.088 72.285  1.00 62.14  ? 173 SER B CB  1 
ATOM   3553  O  OG  . SER B 1 109 ? 28.265 65.160 71.270  1.00 66.48  ? 173 SER B OG  1 
ATOM   3554  N  N   . CYS B 1 110 ? 29.960 68.211 70.565  1.00 61.48  ? 174 CYS B N   1 
ATOM   3555  C  CA  . CYS B 1 110 ? 30.677 68.669 69.381  1.00 65.43  ? 174 CYS B CA  1 
ATOM   3556  C  C   . CYS B 1 110 ? 32.129 68.662 69.725  1.00 68.52  ? 174 CYS B C   1 
ATOM   3557  O  O   . CYS B 1 110 ? 32.489 68.868 70.876  1.00 79.52  ? 174 CYS B O   1 
ATOM   3558  C  CB  . CYS B 1 110 ? 30.236 70.077 68.947  1.00 68.50  ? 174 CYS B CB  1 
ATOM   3559  S  SG  . CYS B 1 110 ? 29.830 71.252 70.294  1.00 89.55  ? 174 CYS B SG  1 
ATOM   3560  N  N   . HIS B 1 111 ? 32.963 68.417 68.721  1.00 76.81  ? 175 HIS B N   1 
ATOM   3561  C  CA  . HIS B 1 111 ? 34.418 68.323 68.907  1.00 68.36  ? 175 HIS B CA  1 
ATOM   3562  C  C   . HIS B 1 111 ? 35.107 69.516 68.325  1.00 68.38  ? 175 HIS B C   1 
ATOM   3563  O  O   . HIS B 1 111 ? 34.994 69.770 67.128  1.00 81.99  ? 175 HIS B O   1 
ATOM   3564  C  CB  . HIS B 1 111 ? 34.940 67.060 68.241  1.00 60.13  ? 175 HIS B CB  1 
ATOM   3565  C  CG  . HIS B 1 111 ? 36.328 66.709 68.646  1.00 66.76  ? 175 HIS B CG  1 
ATOM   3566  N  ND1 . HIS B 1 111 ? 37.406 67.212 68.023  1.00 71.42  ? 175 HIS B ND1 1 
ATOM   3567  C  CD2 . HIS B 1 111 ? 36.806 65.891 69.675  1.00 72.07  ? 175 HIS B CD2 1 
ATOM   3568  C  CE1 . HIS B 1 111 ? 38.529 66.732 68.612  1.00 76.52  ? 175 HIS B CE1 1 
ATOM   3569  N  NE2 . HIS B 1 111 ? 38.160 65.922 69.620  1.00 75.29  ? 175 HIS B NE2 1 
ATOM   3570  N  N   . ASP B 1 112 ? 35.834 70.263 69.143  1.00 68.44  ? 176 ASP B N   1 
ATOM   3571  C  CA  . ASP B 1 112 ? 36.473 71.482 68.638  1.00 79.55  ? 176 ASP B CA  1 
ATOM   3572  C  C   . ASP B 1 112 ? 37.795 71.279 67.881  1.00 82.36  ? 176 ASP B C   1 
ATOM   3573  O  O   . ASP B 1 112 ? 38.304 72.217 67.278  1.00 110.41 ? 176 ASP B O   1 
ATOM   3574  C  CB  . ASP B 1 112 ? 36.655 72.507 69.759  1.00 79.32  ? 176 ASP B CB  1 
ATOM   3575  C  CG  . ASP B 1 112 ? 37.608 72.036 70.839  1.00 86.37  ? 176 ASP B CG  1 
ATOM   3576  O  OD1 . ASP B 1 112 ? 38.165 70.923 70.726  1.00 109.00 ? 176 ASP B OD1 1 
ATOM   3577  O  OD2 . ASP B 1 112 ? 37.797 72.785 71.816  1.00 88.72  ? 176 ASP B OD2 1 
ATOM   3578  N  N   . GLY B 1 113 ? 38.347 70.076 67.908  1.00 70.33  ? 177 GLY B N   1 
ATOM   3579  C  CA  . GLY B 1 113 ? 39.678 69.859 67.346  1.00 81.74  ? 177 GLY B CA  1 
ATOM   3580  C  C   . GLY B 1 113 ? 40.683 69.417 68.394  1.00 79.74  ? 177 GLY B C   1 
ATOM   3581  O  O   . GLY B 1 113 ? 41.766 68.914 68.080  1.00 96.86  ? 177 GLY B O   1 
ATOM   3582  N  N   . PHE B 1 114 ? 40.303 69.580 69.648  1.00 76.97  ? 178 PHE B N   1 
ATOM   3583  C  CA  . PHE B 1 114 ? 41.154 69.202 70.751  1.00 83.71  ? 178 PHE B CA  1 
ATOM   3584  C  C   . PHE B 1 114 ? 40.479 68.156 71.608  1.00 86.01  ? 178 PHE B C   1 
ATOM   3585  O  O   . PHE B 1 114 ? 41.001 67.056 71.760  1.00 97.52  ? 178 PHE B O   1 
ATOM   3586  C  CB  . PHE B 1 114 ? 41.496 70.433 71.581  1.00 88.27  ? 178 PHE B CB  1 
ATOM   3587  C  CG  . PHE B 1 114 ? 42.182 71.495 70.799  1.00 95.23  ? 178 PHE B CG  1 
ATOM   3588  C  CD1 . PHE B 1 114 ? 43.500 71.333 70.429  1.00 102.38 ? 178 PHE B CD1 1 
ATOM   3589  C  CD2 . PHE B 1 114 ? 41.510 72.649 70.413  1.00 112.56 ? 178 PHE B CD2 1 
ATOM   3590  C  CE1 . PHE B 1 114 ? 44.159 72.304 69.693  1.00 118.76 ? 178 PHE B CE1 1 
ATOM   3591  C  CE2 . PHE B 1 114 ? 42.165 73.635 69.677  1.00 128.98 ? 178 PHE B CE2 1 
ATOM   3592  C  CZ  . PHE B 1 114 ? 43.498 73.458 69.318  1.00 113.25 ? 178 PHE B CZ  1 
ATOM   3593  N  N   . GLN B 1 115 ? 39.320 68.501 72.162  1.00 75.87  ? 179 GLN B N   1 
ATOM   3594  C  CA  . GLN B 1 115 ? 38.588 67.599 73.028  1.00 73.71  ? 179 GLN B CA  1 
ATOM   3595  C  C   . GLN B 1 115 ? 37.127 67.587 72.607  1.00 74.79  ? 179 GLN B C   1 
ATOM   3596  O  O   . GLN B 1 115 ? 36.712 68.403 71.787  1.00 67.65  ? 179 GLN B O   1 
ATOM   3597  C  CB  . GLN B 1 115 ? 38.730 68.048 74.482  1.00 83.93  ? 179 GLN B CB  1 
ATOM   3598  C  CG  . GLN B 1 115 ? 40.157 67.990 75.034  1.00 97.80  ? 179 GLN B CG  1 
ATOM   3599  C  CD  . GLN B 1 115 ? 40.645 66.574 75.209  1.00 96.22  ? 179 GLN B CD  1 
ATOM   3600  O  OE1 . GLN B 1 115 ? 39.857 65.633 75.228  1.00 113.72 ? 179 GLN B OE1 1 
ATOM   3601  N  NE2 . GLN B 1 115 ? 41.946 66.412 75.334  1.00 109.73 ? 179 GLN B NE2 1 
ATOM   3602  N  N   . TRP B 1 116 ? 36.356 66.639 73.137  1.00 86.73  ? 180 TRP B N   1 
ATOM   3603  C  CA  . TRP B 1 116 ? 34.895 66.671 73.016  1.00 71.21  ? 180 TRP B CA  1 
ATOM   3604  C  C   . TRP B 1 116 ? 34.291 67.556 74.046  1.00 71.07  ? 180 TRP B C   1 
ATOM   3605  O  O   . TRP B 1 116 ? 34.570 67.415 75.238  1.00 73.80  ? 180 TRP B O   1 
ATOM   3606  C  CB  . TRP B 1 116 ? 34.313 65.316 73.272  1.00 68.35  ? 180 TRP B CB  1 
ATOM   3607  C  CG  . TRP B 1 116 ? 34.439 64.423 72.114  1.00 72.80  ? 180 TRP B CG  1 
ATOM   3608  C  CD1 . TRP B 1 116 ? 35.357 63.410 71.932  1.00 71.06  ? 180 TRP B CD1 1 
ATOM   3609  C  CD2 . TRP B 1 116 ? 33.601 64.417 70.927  1.00 80.23  ? 180 TRP B CD2 1 
ATOM   3610  N  NE1 . TRP B 1 116 ? 35.147 62.776 70.745  1.00 76.64  ? 180 TRP B NE1 1 
ATOM   3611  C  CE2 . TRP B 1 116 ? 34.111 63.341 70.080  1.00 80.32  ? 180 TRP B CE2 1 
ATOM   3612  C  CE3 . TRP B 1 116 ? 32.511 65.168 70.491  1.00 76.19  ? 180 TRP B CE3 1 
ATOM   3613  C  CZ2 . TRP B 1 116 ? 33.556 63.054 68.838  1.00 79.95  ? 180 TRP B CZ2 1 
ATOM   3614  C  CZ3 . TRP B 1 116 ? 31.952 64.866 69.246  1.00 70.19  ? 180 TRP B CZ3 1 
ATOM   3615  C  CH2 . TRP B 1 116 ? 32.469 63.836 68.436  1.00 77.85  ? 180 TRP B CH2 1 
ATOM   3616  N  N   . THR B 1 117 ? 33.434 68.459 73.601  1.00 67.50  ? 181 THR B N   1 
ATOM   3617  C  CA  . THR B 1 117 ? 32.608 69.240 74.495  1.00 62.04  ? 181 THR B CA  1 
ATOM   3618  C  C   . THR B 1 117 ? 31.238 68.545 74.584  1.00 60.26  ? 181 THR B C   1 
ATOM   3619  O  O   . THR B 1 117 ? 30.635 68.206 73.552  1.00 62.25  ? 181 THR B O   1 
ATOM   3620  C  CB  . THR B 1 117 ? 32.500 70.682 73.976  1.00 63.11  ? 181 THR B CB  1 
ATOM   3621  O  OG1 . THR B 1 117 ? 33.816 71.228 73.821  1.00 61.22  ? 181 THR B OG1 1 
ATOM   3622  C  CG2 . THR B 1 117 ? 31.709 71.539 74.930  1.00 64.49  ? 181 THR B CG2 1 
ATOM   3623  N  N   . VAL B 1 118 ? 30.765 68.308 75.808  1.00 58.81  ? 182 VAL B N   1 
ATOM   3624  C  CA  . VAL B 1 118 ? 29.450 67.682 76.034  1.00 57.81  ? 182 VAL B CA  1 
ATOM   3625  C  C   . VAL B 1 118 ? 28.613 68.445 77.042  1.00 59.57  ? 182 VAL B C   1 
ATOM   3626  O  O   . VAL B 1 118 ? 29.048 68.676 78.170  1.00 68.67  ? 182 VAL B O   1 
ATOM   3627  C  CB  . VAL B 1 118 ? 29.567 66.226 76.516  1.00 53.71  ? 182 VAL B CB  1 
ATOM   3628  C  CG1 . VAL B 1 118 ? 28.206 65.692 76.885  1.00 55.06  ? 182 VAL B CG1 1 
ATOM   3629  C  CG2 . VAL B 1 118 ? 30.133 65.397 75.436  1.00 51.17  ? 182 VAL B CG2 1 
ATOM   3630  N  N   . LEU B 1 119 ? 27.406 68.815 76.623  1.00 61.40  ? 183 LEU B N   1 
ATOM   3631  C  CA  . LEU B 1 119 ? 26.446 69.545 77.462  1.00 60.65  ? 183 LEU B CA  1 
ATOM   3632  C  C   . LEU B 1 119 ? 25.375 68.586 77.892  1.00 58.38  ? 183 LEU B C   1 
ATOM   3633  O  O   . LEU B 1 119 ? 24.716 67.986 77.057  1.00 66.27  ? 183 LEU B O   1 
ATOM   3634  C  CB  . LEU B 1 119 ? 25.786 70.670 76.672  1.00 61.19  ? 183 LEU B CB  1 
ATOM   3635  C  CG  . LEU B 1 119 ? 26.695 71.732 76.062  1.00 63.45  ? 183 LEU B CG  1 
ATOM   3636  C  CD1 . LEU B 1 119 ? 26.404 71.902 74.620  1.00 64.81  ? 183 LEU B CD1 1 
ATOM   3637  C  CD2 . LEU B 1 119 ? 26.507 73.032 76.738  1.00 78.17  ? 183 LEU B CD2 1 
ATOM   3638  N  N   . SER B 1 120 ? 25.185 68.462 79.193  1.00 61.29  ? 184 SER B N   1 
ATOM   3639  C  CA  . SER B 1 120 ? 24.228 67.510 79.742  1.00 66.96  ? 184 SER B CA  1 
ATOM   3640  C  C   . SER B 1 120 ? 23.267 68.228 80.667  1.00 62.53  ? 184 SER B C   1 
ATOM   3641  O  O   . SER B 1 120 ? 23.623 69.195 81.313  1.00 80.19  ? 184 SER B O   1 
ATOM   3642  C  CB  . SER B 1 120 ? 24.970 66.378 80.489  1.00 71.95  ? 184 SER B CB  1 
ATOM   3643  O  OG  . SER B 1 120 ? 24.076 65.483 81.129  1.00 71.59  ? 184 SER B OG  1 
ATOM   3644  N  N   . VAL B 1 121 ? 22.047 67.744 80.723  1.00 56.41  ? 185 VAL B N   1 
ATOM   3645  C  CA  . VAL B 1 121 ? 21.033 68.265 81.626  1.00 59.33  ? 185 VAL B CA  1 
ATOM   3646  C  C   . VAL B 1 121 ? 20.713 67.210 82.694  1.00 63.59  ? 185 VAL B C   1 
ATOM   3647  O  O   . VAL B 1 121 ? 20.272 66.106 82.372  1.00 84.93  ? 185 VAL B O   1 
ATOM   3648  C  CB  . VAL B 1 121 ? 19.742 68.551 80.841  1.00 56.07  ? 185 VAL B CB  1 
ATOM   3649  C  CG1 . VAL B 1 121 ? 18.625 69.013 81.756  1.00 56.49  ? 185 VAL B CG1 1 
ATOM   3650  C  CG2 . VAL B 1 121 ? 19.998 69.560 79.767  1.00 53.14  ? 185 VAL B CG2 1 
ATOM   3651  N  N   . ALA B 1 122 ? 20.892 67.552 83.959  1.00 64.40  ? 186 ALA B N   1 
ATOM   3652  C  CA  . ALA B 1 122 ? 20.691 66.585 85.052  1.00 68.83  ? 186 ALA B CA  1 
ATOM   3653  C  C   . ALA B 1 122 ? 20.065 67.173 86.336  1.00 69.74  ? 186 ALA B C   1 
ATOM   3654  O  O   . ALA B 1 122 ? 19.930 68.398 86.498  1.00 56.98  ? 186 ALA B O   1 
ATOM   3655  C  CB  . ALA B 1 122 ? 22.003 65.886 85.389  1.00 63.52  ? 186 ALA B CB  1 
ATOM   3656  N  N   . GLY B 1 123 ? 19.702 66.261 87.238  1.00 75.58  ? 187 GLY B N   1 
ATOM   3657  C  CA  . GLY B 1 123 ? 19.130 66.579 88.545  1.00 80.99  ? 187 GLY B CA  1 
ATOM   3658  C  C   . GLY B 1 123 ? 18.000 67.594 88.575  1.00 86.70  ? 187 GLY B C   1 
ATOM   3659  O  O   . GLY B 1 123 ? 16.874 67.318 88.159  1.00 89.69  ? 187 GLY B O   1 
ATOM   3660  N  N   . ASP B 1 124 ? 18.320 68.770 89.100  1.00 94.05  ? 188 ASP B N   1 
ATOM   3661  C  CA  . ASP B 1 124 ? 17.419 69.912 89.160  1.00 101.48 ? 188 ASP B CA  1 
ATOM   3662  C  C   . ASP B 1 124 ? 16.821 70.192 87.772  1.00 90.91  ? 188 ASP B C   1 
ATOM   3663  O  O   . ASP B 1 124 ? 15.659 70.555 87.656  1.00 103.78 ? 188 ASP B O   1 
ATOM   3664  C  CB  . ASP B 1 124 ? 18.196 71.132 89.735  1.00 129.78 ? 188 ASP B CB  1 
ATOM   3665  C  CG  . ASP B 1 124 ? 17.470 72.482 89.544  1.00 140.98 ? 188 ASP B CG  1 
ATOM   3666  O  OD1 . ASP B 1 124 ? 16.259 72.575 89.843  1.00 156.82 ? 188 ASP B OD1 1 
ATOM   3667  O  OD2 . ASP B 1 124 ? 18.129 73.463 89.115  1.00 116.76 ? 188 ASP B OD2 1 
ATOM   3668  N  N   . GLY B 1 125 ? 17.608 69.976 86.726  1.00 72.82  ? 189 GLY B N   1 
ATOM   3669  C  CA  . GLY B 1 125 ? 17.258 70.454 85.407  1.00 60.84  ? 189 GLY B CA  1 
ATOM   3670  C  C   . GLY B 1 125 ? 18.293 71.437 84.877  1.00 59.63  ? 189 GLY B C   1 
ATOM   3671  O  O   . GLY B 1 125 ? 18.022 72.155 83.938  1.00 58.71  ? 189 GLY B O   1 
ATOM   3672  N  N   . PHE B 1 126 ? 19.486 71.474 85.465  1.00 67.67  ? 190 PHE B N   1 
ATOM   3673  C  CA  . PHE B 1 126 ? 20.558 72.366 84.995  1.00 70.17  ? 190 PHE B CA  1 
ATOM   3674  C  C   . PHE B 1 126 ? 21.459 71.678 83.966  1.00 74.94  ? 190 PHE B C   1 
ATOM   3675  O  O   . PHE B 1 126 ? 21.299 70.492 83.651  1.00 69.34  ? 190 PHE B O   1 
ATOM   3676  C  CB  . PHE B 1 126 ? 21.401 72.872 86.171  1.00 80.33  ? 190 PHE B CB  1 
ATOM   3677  C  CG  . PHE B 1 126 ? 22.291 71.806 86.796  1.00 92.07  ? 190 PHE B CG  1 
ATOM   3678  C  CD1 . PHE B 1 126 ? 23.670 71.827 86.607  1.00 97.27  ? 190 PHE B CD1 1 
ATOM   3679  C  CD2 . PHE B 1 126 ? 21.749 70.789 87.574  1.00 95.07  ? 190 PHE B CD2 1 
ATOM   3680  C  CE1 . PHE B 1 126 ? 24.487 70.845 87.174  1.00 92.56  ? 190 PHE B CE1 1 
ATOM   3681  C  CE2 . PHE B 1 126 ? 22.558 69.816 88.139  1.00 93.37  ? 190 PHE B CE2 1 
ATOM   3682  C  CZ  . PHE B 1 126 ? 23.925 69.845 87.939  1.00 88.03  ? 190 PHE B CZ  1 
ATOM   3683  N  N   . VAL B 1 127 ? 22.423 72.437 83.463  1.00 76.06  ? 191 VAL B N   1 
ATOM   3684  C  CA  . VAL B 1 127 ? 23.342 71.952 82.458  1.00 68.41  ? 191 VAL B CA  1 
ATOM   3685  C  C   . VAL B 1 127 ? 24.783 71.894 82.952  1.00 76.78  ? 191 VAL B C   1 
ATOM   3686  O  O   . VAL B 1 127 ? 25.335 72.914 83.367  1.00 87.34  ? 191 VAL B O   1 
ATOM   3687  C  CB  . VAL B 1 127 ? 23.265 72.858 81.254  1.00 68.47  ? 191 VAL B CB  1 
ATOM   3688  C  CG1 . VAL B 1 127 ? 24.545 72.828 80.441  1.00 80.80  ? 191 VAL B CG1 1 
ATOM   3689  C  CG2 . VAL B 1 127 ? 22.163 72.428 80.435  1.00 63.86  ? 191 VAL B CG2 1 
ATOM   3690  N  N   . SER B 1 128 ? 25.375 70.696 82.919  1.00 75.08  ? 192 SER B N   1 
ATOM   3691  C  CA  . SER B 1 128 ? 26.821 70.518 83.085  1.00 73.69  ? 192 SER B CA  1 
ATOM   3692  C  C   . SER B 1 128 ? 27.461 70.639 81.730  1.00 73.85  ? 192 SER B C   1 
ATOM   3693  O  O   . SER B 1 128 ? 26.903 70.185 80.728  1.00 91.82  ? 192 SER B O   1 
ATOM   3694  C  CB  . SER B 1 128 ? 27.138 69.128 83.614  1.00 76.60  ? 192 SER B CB  1 
ATOM   3695  O  OG  . SER B 1 128 ? 26.538 68.951 84.872  1.00 85.52  ? 192 SER B OG  1 
ATOM   3696  N  N   . ILE B 1 129 ? 28.629 71.249 81.683  1.00 65.10  ? 193 ILE B N   1 
ATOM   3697  C  CA  . ILE B 1 129 ? 29.366 71.307 80.446  1.00 66.36  ? 193 ILE B CA  1 
ATOM   3698  C  C   . ILE B 1 129 ? 30.642 70.574 80.723  1.00 71.74  ? 193 ILE B C   1 
ATOM   3699  O  O   . ILE B 1 129 ? 31.393 70.966 81.623  1.00 75.47  ? 193 ILE B O   1 
ATOM   3700  C  CB  . ILE B 1 129 ? 29.690 72.753 80.059  1.00 72.16  ? 193 ILE B CB  1 
ATOM   3701  C  CG1 . ILE B 1 129 ? 28.428 73.464 79.590  1.00 81.05  ? 193 ILE B CG1 1 
ATOM   3702  C  CG2 . ILE B 1 129 ? 30.698 72.811 78.940  1.00 69.12  ? 193 ILE B CG2 1 
ATOM   3703  C  CD1 . ILE B 1 129 ? 28.568 74.970 79.494  1.00 81.50  ? 193 ILE B CD1 1 
ATOM   3704  N  N   . LEU B 1 130 ? 30.903 69.496 79.989  1.00 72.08  ? 194 LEU B N   1 
ATOM   3705  C  CA  . LEU B 1 130 ? 32.205 68.867 80.161  1.00 78.08  ? 194 LEU B CA  1 
ATOM   3706  C  C   . LEU B 1 130 ? 33.103 68.742 78.951  1.00 77.70  ? 194 LEU B C   1 
ATOM   3707  O  O   . LEU B 1 130 ? 32.695 68.277 77.894  1.00 102.70 ? 194 LEU B O   1 
ATOM   3708  C  CB  . LEU B 1 130 ? 32.137 67.584 80.982  1.00 77.98  ? 194 LEU B CB  1 
ATOM   3709  C  CG  . LEU B 1 130 ? 31.087 66.570 80.676  1.00 84.22  ? 194 LEU B CG  1 
ATOM   3710  C  CD1 . LEU B 1 130 ? 31.826 65.375 80.069  1.00 111.65 ? 194 LEU B CD1 1 
ATOM   3711  C  CD2 . LEU B 1 130 ? 30.419 66.228 81.977  1.00 78.16  ? 194 LEU B CD2 1 
ATOM   3712  N  N   . TYR B 1 131 ? 34.340 69.184 79.156  1.00 73.17  ? 195 TYR B N   1 
ATOM   3713  C  CA  . TYR B 1 131 ? 35.353 69.260 78.128  1.00 69.32  ? 195 TYR B CA  1 
ATOM   3714  C  C   . TYR B 1 131 ? 36.363 68.167 78.374  1.00 69.98  ? 195 TYR B C   1 
ATOM   3715  O  O   . TYR B 1 131 ? 37.028 68.132 79.409  1.00 69.46  ? 195 TYR B O   1 
ATOM   3716  C  CB  . TYR B 1 131 ? 36.018 70.632 78.159  1.00 71.55  ? 195 TYR B CB  1 
ATOM   3717  C  CG  . TYR B 1 131 ? 36.873 70.953 76.960  1.00 75.55  ? 195 TYR B CG  1 
ATOM   3718  C  CD1 . TYR B 1 131 ? 36.301 71.284 75.734  1.00 77.04  ? 195 TYR B CD1 1 
ATOM   3719  C  CD2 . TYR B 1 131 ? 38.253 70.951 77.055  1.00 84.59  ? 195 TYR B CD2 1 
ATOM   3720  C  CE1 . TYR B 1 131 ? 37.087 71.597 74.637  1.00 80.19  ? 195 TYR B CE1 1 
ATOM   3721  C  CE2 . TYR B 1 131 ? 39.048 71.264 75.970  1.00 89.44  ? 195 TYR B CE2 1 
ATOM   3722  C  CZ  . TYR B 1 131 ? 38.463 71.584 74.765  1.00 92.17  ? 195 TYR B CZ  1 
ATOM   3723  O  OH  . TYR B 1 131 ? 39.267 71.894 73.696  1.00 117.97 ? 195 TYR B OH  1 
ATOM   3724  N  N   . GLY B 1 132 ? 36.449 67.245 77.428  1.00 74.57  ? 196 GLY B N   1 
ATOM   3725  C  CA  . GLY B 1 132 ? 37.379 66.131 77.544  1.00 72.59  ? 196 GLY B CA  1 
ATOM   3726  C  C   . GLY B 1 132 ? 37.094 65.305 78.770  1.00 68.21  ? 196 GLY B C   1 
ATOM   3727  O  O   . GLY B 1 132 ? 38.011 64.768 79.359  1.00 69.41  ? 196 GLY B O   1 
ATOM   3728  N  N   . GLY B 1 133 ? 35.821 65.227 79.156  1.00 71.88  ? 197 GLY B N   1 
ATOM   3729  C  CA  . GLY B 1 133 ? 35.387 64.311 80.202  1.00 85.31  ? 197 GLY B CA  1 
ATOM   3730  C  C   . GLY B 1 133 ? 35.475 64.854 81.609  1.00 79.48  ? 197 GLY B C   1 
ATOM   3731  O  O   . GLY B 1 133 ? 35.168 64.152 82.568  1.00 82.21  ? 197 GLY B O   1 
ATOM   3732  N  N   . ILE B 1 134 ? 35.897 66.103 81.743  1.00 81.19  ? 198 ILE B N   1 
ATOM   3733  C  CA  . ILE B 1 134 ? 35.978 66.726 83.068  1.00 86.32  ? 198 ILE B CA  1 
ATOM   3734  C  C   . ILE B 1 134 ? 35.104 67.937 83.113  1.00 84.81  ? 198 ILE B C   1 
ATOM   3735  O  O   . ILE B 1 134 ? 34.900 68.559 82.076  1.00 91.44  ? 198 ILE B O   1 
ATOM   3736  C  CB  . ILE B 1 134 ? 37.400 67.131 83.415  1.00 96.26  ? 198 ILE B CB  1 
ATOM   3737  C  CG1 . ILE B 1 134 ? 37.905 68.219 82.458  1.00 87.10  ? 198 ILE B CG1 1 
ATOM   3738  C  CG2 . ILE B 1 134 ? 38.290 65.883 83.408  1.00 119.39 ? 198 ILE B CG2 1 
ATOM   3739  C  CD1 . ILE B 1 134 ? 39.229 68.808 82.824  1.00 103.55 ? 198 ILE B CD1 1 
ATOM   3740  N  N   . ILE B 1 135 ? 34.593 68.280 84.299  1.00 88.42  ? 199 ILE B N   1 
ATOM   3741  C  CA  . ILE B 1 135 ? 33.536 69.309 84.391  1.00 97.90  ? 199 ILE B CA  1 
ATOM   3742  C  C   . ILE B 1 135 ? 34.100 70.689 84.422  1.00 87.65  ? 199 ILE B C   1 
ATOM   3743  O  O   . ILE B 1 135 ? 34.690 71.073 85.399  1.00 86.73  ? 199 ILE B O   1 
ATOM   3744  C  CB  . ILE B 1 135 ? 32.600 69.146 85.602  1.00 98.32  ? 199 ILE B CB  1 
ATOM   3745  C  CG1 . ILE B 1 135 ? 31.997 67.740 85.577  1.00 121.49 ? 199 ILE B CG1 1 
ATOM   3746  C  CG2 . ILE B 1 135 ? 31.528 70.261 85.601  1.00 85.00  ? 199 ILE B CG2 1 
ATOM   3747  C  CD1 . ILE B 1 135 ? 30.490 67.671 85.523  1.00 134.95 ? 199 ILE B CD1 1 
ATOM   3748  N  N   . THR B 1 136 ? 33.878 71.437 83.353  1.00 87.71  ? 200 THR B N   1 
ATOM   3749  C  CA  . THR B 1 136 ? 34.479 72.751 83.203  1.00 92.90  ? 200 THR B CA  1 
ATOM   3750  C  C   . THR B 1 136 ? 33.523 73.908 83.545  1.00 92.73  ? 200 THR B C   1 
ATOM   3751  O  O   . THR B 1 136 ? 33.976 75.010 83.866  1.00 104.44 ? 200 THR B O   1 
ATOM   3752  C  CB  . THR B 1 136 ? 35.058 72.931 81.776  1.00 89.39  ? 200 THR B CB  1 
ATOM   3753  O  OG1 . THR B 1 136 ? 34.068 72.574 80.805  1.00 87.54  ? 200 THR B OG1 1 
ATOM   3754  C  CG2 . THR B 1 136 ? 36.279 72.049 81.574  1.00 79.37  ? 200 THR B CG2 1 
ATOM   3755  N  N   . ASP B 1 137 ? 32.217 73.658 83.481  1.00 82.97  ? 201 ASP B N   1 
ATOM   3756  C  CA  . ASP B 1 137 ? 31.230 74.711 83.708  1.00 86.62  ? 201 ASP B CA  1 
ATOM   3757  C  C   . ASP B 1 137 ? 29.804 74.179 83.856  1.00 82.26  ? 201 ASP B C   1 
ATOM   3758  O  O   . ASP B 1 137 ? 29.451 73.125 83.323  1.00 82.79  ? 201 ASP B O   1 
ATOM   3759  C  CB  . ASP B 1 137 ? 31.271 75.731 82.566  1.00 106.89 ? 201 ASP B CB  1 
ATOM   3760  C  CG  . ASP B 1 137 ? 30.846 77.137 83.003  1.00 127.85 ? 201 ASP B CG  1 
ATOM   3761  O  OD1 . ASP B 1 137 ? 29.903 77.285 83.803  1.00 152.45 ? 201 ASP B OD1 1 
ATOM   3762  O  OD2 . ASP B 1 137 ? 31.451 78.119 82.533  1.00 146.11 ? 201 ASP B OD2 1 
ATOM   3763  N  N   . THR B 1 138 ? 28.987 74.930 84.585  1.00 78.95  ? 202 THR B N   1 
ATOM   3764  C  CA  . THR B 1 138 ? 27.565 74.635 84.731  1.00 83.05  ? 202 THR B CA  1 
ATOM   3765  C  C   . THR B 1 138 ? 26.700 75.838 84.387  1.00 82.14  ? 202 THR B C   1 
ATOM   3766  O  O   . THR B 1 138 ? 27.101 76.984 84.574  1.00 92.51  ? 202 THR B O   1 
ATOM   3767  C  CB  . THR B 1 138 ? 27.192 74.180 86.150  1.00 92.90  ? 202 THR B CB  1 
ATOM   3768  O  OG1 . THR B 1 138 ? 27.527 75.211 87.090  1.00 134.60 ? 202 THR B OG1 1 
ATOM   3769  C  CG2 . THR B 1 138 ? 27.917 72.898 86.515  1.00 88.25  ? 202 THR B CG2 1 
ATOM   3770  N  N   . ILE B 1 139 ? 25.504 75.554 83.890  1.00 81.67  ? 203 ILE B N   1 
ATOM   3771  C  CA  . ILE B 1 139 ? 24.555 76.582 83.550  1.00 81.47  ? 203 ILE B CA  1 
ATOM   3772  C  C   . ILE B 1 139 ? 23.241 76.316 84.267  1.00 87.25  ? 203 ILE B C   1 
ATOM   3773  O  O   . ILE B 1 139 ? 22.729 75.187 84.222  1.00 84.30  ? 203 ILE B O   1 
ATOM   3774  C  CB  . ILE B 1 139 ? 24.322 76.612 82.051  1.00 73.23  ? 203 ILE B CB  1 
ATOM   3775  C  CG1 . ILE B 1 139 ? 25.630 76.913 81.313  1.00 72.32  ? 203 ILE B CG1 1 
ATOM   3776  C  CG2 . ILE B 1 139 ? 23.279 77.666 81.714  1.00 76.63  ? 203 ILE B CG2 1 
ATOM   3777  C  CD1 . ILE B 1 139 ? 25.469 76.964 79.789  1.00 75.18  ? 203 ILE B CD1 1 
ATOM   3778  N  N   . HIS B 1 140 ? 22.692 77.351 84.911  1.00 85.57  ? 204 HIS B N   1 
ATOM   3779  C  CA  . HIS B 1 140 ? 21.434 77.206 85.645  1.00 88.23  ? 204 HIS B CA  1 
ATOM   3780  C  C   . HIS B 1 140 ? 20.236 77.925 85.067  1.00 98.07  ? 204 HIS B C   1 
ATOM   3781  O  O   . HIS B 1 140 ? 20.373 78.941 84.387  1.00 98.47  ? 204 HIS B O   1 
ATOM   3782  C  CB  . HIS B 1 140 ? 21.660 77.573 87.080  1.00 84.95  ? 204 HIS B CB  1 
ATOM   3783  C  CG  . HIS B 1 140 ? 22.792 76.831 87.679  1.00 91.70  ? 204 HIS B CG  1 
ATOM   3784  N  ND1 . HIS B 1 140 ? 22.638 75.633 88.242  1.00 94.29  ? 204 HIS B ND1 1 
ATOM   3785  C  CD2 . HIS B 1 140 ? 24.146 77.131 87.743  1.00 107.58 ? 204 HIS B CD2 1 
ATOM   3786  C  CE1 . HIS B 1 140 ? 23.835 75.189 88.677  1.00 109.47 ? 204 HIS B CE1 1 
ATOM   3787  N  NE2 . HIS B 1 140 ? 24.755 76.111 88.371  1.00 109.77 ? 204 HIS B NE2 1 
ATOM   3788  N  N   . PRO B 1 141 ? 19.033 77.392 85.326  1.00 100.25 ? 205 PRO B N   1 
ATOM   3789  C  CA  . PRO B 1 141 ? 17.827 77.964 84.760  1.00 104.27 ? 205 PRO B CA  1 
ATOM   3790  C  C   . PRO B 1 141 ? 17.410 79.231 85.490  1.00 126.99 ? 205 PRO B C   1 
ATOM   3791  O  O   . PRO B 1 141 ? 17.363 79.252 86.721  1.00 139.02 ? 205 PRO B O   1 
ATOM   3792  C  CB  . PRO B 1 141 ? 16.775 76.878 85.002  1.00 115.60 ? 205 PRO B CB  1 
ATOM   3793  C  CG  . PRO B 1 141 ? 17.493 75.723 85.664  1.00 102.53 ? 205 PRO B CG  1 
ATOM   3794  C  CD  . PRO B 1 141 ? 18.735 76.267 86.231  1.00 101.39 ? 205 PRO B CD  1 
ATOM   3795  N  N   . THR B 1 142 ? 17.121 80.277 84.725  1.00 140.48 ? 206 THR B N   1 
ATOM   3796  C  CA  . THR B 1 142 ? 16.557 81.509 85.262  1.00 147.22 ? 206 THR B CA  1 
ATOM   3797  C  C   . THR B 1 142 ? 15.038 81.433 85.108  1.00 145.86 ? 206 THR B C   1 
ATOM   3798  O  O   . THR B 1 142 ? 14.293 81.433 86.092  1.00 149.54 ? 206 THR B O   1 
ATOM   3799  C  CB  . THR B 1 142 ? 17.098 82.753 84.512  1.00 141.47 ? 206 THR B CB  1 
ATOM   3800  O  OG1 . THR B 1 142 ? 16.656 82.717 83.148  1.00 125.41 ? 206 THR B OG1 1 
ATOM   3801  C  CG2 . THR B 1 142 ? 18.630 82.796 84.543  1.00 118.29 ? 206 THR B CG2 1 
ATOM   3802  N  N   . ASN B 1 143 ? 14.606 81.325 83.852  1.00 134.93 ? 207 ASN B N   1 
ATOM   3803  C  CA  . ASN B 1 143 ? 13.201 81.282 83.463  1.00 115.71 ? 207 ASN B CA  1 
ATOM   3804  C  C   . ASN B 1 143 ? 12.403 80.128 84.075  1.00 105.44 ? 207 ASN B C   1 
ATOM   3805  O  O   . ASN B 1 143 ? 11.257 79.903 83.686  1.00 89.38  ? 207 ASN B O   1 
ATOM   3806  C  CB  . ASN B 1 143 ? 13.105 81.323 81.935  1.00 101.20 ? 207 ASN B CB  1 
ATOM   3807  C  CG  . ASN B 1 143 ? 12.058 82.284 81.444  1.00 126.35 ? 207 ASN B CG  1 
ATOM   3808  O  OD1 . ASN B 1 143 ? 11.875 83.371 81.999  1.00 150.69 ? 207 ASN B OD1 1 
ATOM   3809  N  ND2 . ASN B 1 143 ? 11.370 81.902 80.382  1.00 144.42 ? 207 ASN B ND2 1 
ATOM   3810  N  N   . GLY B 1 144 ? 13.028 79.396 85.007  1.00 122.52 ? 208 GLY B N   1 
ATOM   3811  C  CA  . GLY B 1 144 ? 12.403 78.275 85.725  1.00 128.26 ? 208 GLY B CA  1 
ATOM   3812  C  C   . GLY B 1 144 ? 12.275 76.997 84.913  1.00 153.56 ? 208 GLY B C   1 
ATOM   3813  O  O   . GLY B 1 144 ? 12.544 76.986 83.708  1.00 173.40 ? 208 GLY B O   1 
ATOM   3814  N  N   . GLY B 1 145 ? 11.854 75.914 85.568  1.00 148.23 ? 209 GLY B N   1 
ATOM   3815  C  CA  . GLY B 1 145 ? 11.640 74.632 84.885  1.00 117.81 ? 209 GLY B CA  1 
ATOM   3816  C  C   . GLY B 1 145 ? 12.928 74.204 84.230  1.00 104.81 ? 209 GLY B C   1 
ATOM   3817  O  O   . GLY B 1 145 ? 13.860 74.999 84.165  1.00 101.51 ? 209 GLY B O   1 
ATOM   3818  N  N   . PRO B 1 146 ? 12.987 72.962 83.715  1.00 103.68 ? 210 PRO B N   1 
ATOM   3819  C  CA  . PRO B 1 146 ? 14.278 72.362 83.312  1.00 74.48  ? 210 PRO B CA  1 
ATOM   3820  C  C   . PRO B 1 146 ? 14.799 73.029 82.052  1.00 73.09  ? 210 PRO B C   1 
ATOM   3821  O  O   . PRO B 1 146 ? 13.993 73.479 81.222  1.00 90.43  ? 210 PRO B O   1 
ATOM   3822  C  CB  . PRO B 1 146 ? 13.907 70.926 83.007  1.00 68.39  ? 210 PRO B CB  1 
ATOM   3823  C  CG  . PRO B 1 146 ? 12.489 71.037 82.463  1.00 89.11  ? 210 PRO B CG  1 
ATOM   3824  C  CD  . PRO B 1 146 ? 11.833 72.208 83.191  1.00 95.31  ? 210 PRO B CD  1 
ATOM   3825  N  N   . LEU B 1 147 ? 16.118 73.145 81.927  1.00 62.93  ? 211 LEU B N   1 
ATOM   3826  C  CA  . LEU B 1 147 ? 16.722 73.523 80.656  1.00 61.19  ? 211 LEU B CA  1 
ATOM   3827  C  C   . LEU B 1 147 ? 16.708 72.335 79.687  1.00 76.48  ? 211 LEU B C   1 
ATOM   3828  O  O   . LEU B 1 147 ? 16.460 71.164 80.065  1.00 74.11  ? 211 LEU B O   1 
ATOM   3829  C  CB  . LEU B 1 147 ? 18.153 73.994 80.829  1.00 57.77  ? 211 LEU B CB  1 
ATOM   3830  C  CG  . LEU B 1 147 ? 18.435 75.146 81.768  1.00 70.59  ? 211 LEU B CG  1 
ATOM   3831  C  CD1 . LEU B 1 147 ? 19.835 75.000 82.298  1.00 93.79  ? 211 LEU B CD1 1 
ATOM   3832  C  CD2 . LEU B 1 147 ? 18.320 76.431 81.022  1.00 89.53  ? 211 LEU B CD2 1 
ATOM   3833  N  N   . ARG B 1 148 ? 16.987 72.647 78.428  1.00 75.43  ? 212 ARG B N   1 
ATOM   3834  C  CA  . ARG B 1 148 ? 16.941 71.662 77.379  1.00 69.18  ? 212 ARG B CA  1 
ATOM   3835  C  C   . ARG B 1 148 ? 18.041 71.956 76.356  1.00 71.99  ? 212 ARG B C   1 
ATOM   3836  O  O   . ARG B 1 148 ? 18.282 73.109 76.004  1.00 83.60  ? 212 ARG B O   1 
ATOM   3837  C  CB  . ARG B 1 148 ? 15.554 71.677 76.738  1.00 74.62  ? 212 ARG B CB  1 
ATOM   3838  C  CG  . ARG B 1 148 ? 14.403 71.335 77.704  1.00 81.49  ? 212 ARG B CG  1 
ATOM   3839  C  CD  . ARG B 1 148 ? 13.012 71.425 77.042  1.00 107.26 ? 212 ARG B CD  1 
ATOM   3840  N  NE  . ARG B 1 148 ? 12.659 72.775 76.599  1.00 110.64 ? 212 ARG B NE  1 
ATOM   3841  C  CZ  . ARG B 1 148 ? 12.125 73.714 77.377  1.00 109.48 ? 212 ARG B CZ  1 
ATOM   3842  N  NH1 . ARG B 1 148 ? 11.864 73.480 78.662  1.00 97.65  ? 212 ARG B NH1 1 
ATOM   3843  N  NH2 . ARG B 1 148 ? 11.854 74.900 76.864  1.00 118.88 ? 212 ARG B NH2 1 
ATOM   3844  N  N   . THR B 1 149 ? 18.717 70.906 75.903  1.00 81.89  ? 213 THR B N   1 
ATOM   3845  C  CA  . THR B 1 149 ? 19.777 71.029 74.896  1.00 72.77  ? 213 THR B CA  1 
ATOM   3846  C  C   . THR B 1 149 ? 19.240 70.723 73.514  1.00 66.14  ? 213 THR B C   1 
ATOM   3847  O  O   . THR B 1 149 ? 18.118 70.198 73.366  1.00 60.24  ? 213 THR B O   1 
ATOM   3848  C  CB  . THR B 1 149 ? 20.954 70.041 75.152  1.00 70.74  ? 213 THR B CB  1 
ATOM   3849  O  OG1 . THR B 1 149 ? 20.462 68.695 75.211  1.00 55.91  ? 213 THR B OG1 1 
ATOM   3850  C  CG2 . THR B 1 149 ? 21.660 70.367 76.443  1.00 71.33  ? 213 THR B CG2 1 
ATOM   3851  N  N   . GLN B 1 150 ? 20.060 71.004 72.504  1.00 61.51  ? 214 GLN B N   1 
ATOM   3852  C  CA  . GLN B 1 150 ? 19.674 70.742 71.116  1.00 54.36  ? 214 GLN B CA  1 
ATOM   3853  C  C   . GLN B 1 150 ? 19.332 69.308 70.841  1.00 51.81  ? 214 GLN B C   1 
ATOM   3854  O  O   . GLN B 1 150 ? 18.620 69.035 69.895  1.00 57.59  ? 214 GLN B O   1 
ATOM   3855  C  CB  . GLN B 1 150 ? 20.796 71.129 70.175  1.00 63.74  ? 214 GLN B CB  1 
ATOM   3856  C  CG  . GLN B 1 150 ? 21.225 72.536 70.322  1.00 72.08  ? 214 GLN B CG  1 
ATOM   3857  C  CD  . GLN B 1 150 ? 22.277 72.886 69.340  1.00 68.68  ? 214 GLN B CD  1 
ATOM   3858  O  OE1 . GLN B 1 150 ? 23.126 72.086 69.041  1.00 61.56  ? 214 GLN B OE1 1 
ATOM   3859  N  NE2 . GLN B 1 150 ? 22.231 74.098 68.821  1.00 119.05 ? 214 GLN B NE2 1 
ATOM   3860  N  N   . ALA B 1 151 ? 19.875 68.384 71.631  1.00 50.96  ? 215 ALA B N   1 
ATOM   3861  C  CA  . ALA B 1 151 ? 19.679 66.963 71.376  1.00 45.59  ? 215 ALA B CA  1 
ATOM   3862  C  C   . ALA B 1 151 ? 20.166 66.629 69.960  1.00 47.06  ? 215 ALA B C   1 
ATOM   3863  O  O   . ALA B 1 151 ? 19.544 65.858 69.221  1.00 45.08  ? 215 ALA B O   1 
ATOM   3864  C  CB  . ALA B 1 151 ? 18.229 66.591 71.564  1.00 40.03  ? 215 ALA B CB  1 
ATOM   3865  N  N   . SER B 1 152 ? 21.291 67.241 69.615  1.00 47.31  ? 216 SER B N   1 
ATOM   3866  C  CA  . SER B 1 152 ? 21.847 67.222 68.296  1.00 55.25  ? 216 SER B CA  1 
ATOM   3867  C  C   . SER B 1 152 ? 23.238 67.772 68.482  1.00 57.64  ? 216 SER B C   1 
ATOM   3868  O  O   . SER B 1 152 ? 23.474 68.537 69.405  1.00 62.69  ? 216 SER B O   1 
ATOM   3869  C  CB  . SER B 1 152 ? 21.056 68.179 67.383  1.00 59.76  ? 216 SER B CB  1 
ATOM   3870  O  OG  . SER B 1 152 ? 21.746 68.490 66.169  1.00 82.51  ? 216 SER B OG  1 
ATOM   3871  N  N   . SER B 1 153 ? 24.148 67.387 67.595  1.00 56.52  ? 217 SER B N   1 
ATOM   3872  C  CA  . SER B 1 153 ? 25.470 67.973 67.512  1.00 52.20  ? 217 SER B CA  1 
ATOM   3873  C  C   . SER B 1 153 ? 25.424 69.513 67.541  1.00 56.29  ? 217 SER B C   1 
ATOM   3874  O  O   . SER B 1 153 ? 24.636 70.129 66.802  1.00 60.26  ? 217 SER B O   1 
ATOM   3875  C  CB  . SER B 1 153 ? 26.116 67.490 66.221  1.00 45.37  ? 217 SER B CB  1 
ATOM   3876  O  OG  . SER B 1 153 ? 27.304 68.199 65.916  1.00 53.20  ? 217 SER B OG  1 
ATOM   3877  N  N   . CYS B 1 154 ? 26.243 70.117 68.407  1.00 51.25  ? 218 CYS B N   1 
ATOM   3878  C  CA  . CYS B 1 154 ? 26.470 71.551 68.368  1.00 56.54  ? 218 CYS B CA  1 
ATOM   3879  C  C   . CYS B 1 154 ? 27.527 71.816 67.306  1.00 64.02  ? 218 CYS B C   1 
ATOM   3880  O  O   . CYS B 1 154 ? 28.056 70.879 66.711  1.00 61.98  ? 218 CYS B O   1 
ATOM   3881  C  CB  . CYS B 1 154 ? 26.915 72.079 69.733  1.00 68.40  ? 218 CYS B CB  1 
ATOM   3882  S  SG  . CYS B 1 154 ? 27.858 70.901 70.719  1.00 100.66 ? 218 CYS B SG  1 
ATOM   3883  N  N   . ILE B 1 155 ? 27.840 73.083 67.056  1.00 68.76  ? 219 ILE B N   1 
ATOM   3884  C  CA  . ILE B 1 155 ? 28.733 73.424 65.960  1.00 62.81  ? 219 ILE B CA  1 
ATOM   3885  C  C   . ILE B 1 155 ? 30.023 74.031 66.440  1.00 65.99  ? 219 ILE B C   1 
ATOM   3886  O  O   . ILE B 1 155 ? 30.005 75.042 67.136  1.00 85.11  ? 219 ILE B O   1 
ATOM   3887  C  CB  . ILE B 1 155 ? 28.048 74.371 64.995  1.00 60.31  ? 219 ILE B CB  1 
ATOM   3888  C  CG1 . ILE B 1 155 ? 27.019 73.590 64.194  1.00 72.09  ? 219 ILE B CG1 1 
ATOM   3889  C  CG2 . ILE B 1 155 ? 29.057 74.974 64.032  1.00 55.66  ? 219 ILE B CG2 1 
ATOM   3890  C  CD1 . ILE B 1 155 ? 25.851 73.100 64.985  1.00 98.67  ? 219 ILE B CD1 1 
ATOM   3891  N  N   . CYS B 1 156 ? 31.148 73.416 66.087  1.00 71.37  ? 220 CYS B N   1 
ATOM   3892  C  CA  . CYS B 1 156 ? 32.438 74.014 66.418  1.00 72.35  ? 220 CYS B CA  1 
ATOM   3893  C  C   . CYS B 1 156 ? 33.100 74.457 65.145  1.00 72.99  ? 220 CYS B C   1 
ATOM   3894  O  O   . CYS B 1 156 ? 33.024 73.779 64.133  1.00 89.42  ? 220 CYS B O   1 
ATOM   3895  C  CB  . CYS B 1 156 ? 33.341 73.074 67.218  1.00 75.31  ? 220 CYS B CB  1 
ATOM   3896  S  SG  . CYS B 1 156 ? 32.608 72.461 68.753  1.00 129.62 ? 220 CYS B SG  1 
ATOM   3897  N  N   . ASN B 1 157 ? 33.710 75.630 65.198  1.00 89.96  ? 221 ASN B N   1 
ATOM   3898  C  CA  . ASN B 1 157 ? 34.478 76.168 64.097  1.00 94.89  ? 221 ASN B CA  1 
ATOM   3899  C  C   . ASN B 1 157 ? 35.542 77.093 64.663  1.00 99.50  ? 221 ASN B C   1 
ATOM   3900  O  O   . ASN B 1 157 ? 35.221 78.068 65.349  1.00 115.62 ? 221 ASN B O   1 
ATOM   3901  C  CB  . ASN B 1 157 ? 33.572 76.929 63.122  1.00 93.13  ? 221 ASN B CB  1 
ATOM   3902  C  CG  . ASN B 1 157 ? 34.193 77.057 61.743  1.00 97.11  ? 221 ASN B CG  1 
ATOM   3903  O  OD1 . ASN B 1 157 ? 34.800 76.111 61.234  1.00 91.76  ? 221 ASN B OD1 1 
ATOM   3904  N  ND2 . ASN B 1 157 ? 34.053 78.226 61.136  1.00 98.98  ? 221 ASN B ND2 1 
ATOM   3905  N  N   . ASP B 1 158 ? 36.802 76.777 64.389  1.00 94.94  ? 222 ASP B N   1 
ATOM   3906  C  CA  . ASP B 1 158 ? 37.938 77.586 64.857  1.00 104.40 ? 222 ASP B CA  1 
ATOM   3907  C  C   . ASP B 1 158 ? 38.038 77.617 66.375  1.00 104.81 ? 222 ASP B C   1 
ATOM   3908  O  O   . ASP B 1 158 ? 38.386 78.648 66.955  1.00 113.06 ? 222 ASP B O   1 
ATOM   3909  C  CB  . ASP B 1 158 ? 37.876 79.030 64.332  1.00 116.25 ? 222 ASP B CB  1 
ATOM   3910  C  CG  . ASP B 1 158 ? 38.149 79.132 62.852  1.00 140.99 ? 222 ASP B CG  1 
ATOM   3911  O  OD1 . ASP B 1 158 ? 38.752 78.200 62.289  1.00 143.26 ? 222 ASP B OD1 1 
ATOM   3912  O  OD2 . ASP B 1 158 ? 37.763 80.157 62.250  1.00 166.49 ? 222 ASP B OD2 1 
ATOM   3913  N  N   . GLY B 1 159 ? 37.702 76.502 67.019  1.00 97.53  ? 223 GLY B N   1 
ATOM   3914  C  CA  . GLY B 1 159 ? 38.006 76.335 68.438  1.00 107.11 ? 223 GLY B CA  1 
ATOM   3915  C  C   . GLY B 1 159 ? 36.997 76.899 69.411  1.00 95.48  ? 223 GLY B C   1 
ATOM   3916  O  O   . GLY B 1 159 ? 37.109 76.666 70.622  1.00 95.93  ? 223 GLY B O   1 
ATOM   3917  N  N   . THR B 1 160 ? 36.035 77.656 68.882  1.00 88.39  ? 224 THR B N   1 
ATOM   3918  C  CA  . THR B 1 160 ? 34.860 78.102 69.642  1.00 88.32  ? 224 THR B CA  1 
ATOM   3919  C  C   . THR B 1 160 ? 33.616 77.297 69.195  1.00 81.91  ? 224 THR B C   1 
ATOM   3920  O  O   . THR B 1 160 ? 33.468 76.994 68.021  1.00 82.10  ? 224 THR B O   1 
ATOM   3921  C  CB  . THR B 1 160 ? 34.627 79.653 69.524  1.00 90.38  ? 224 THR B CB  1 
ATOM   3922  O  OG1 . THR B 1 160 ? 34.322 80.009 68.171  1.00 81.72  ? 224 THR B OG1 1 
ATOM   3923  C  CG2 . THR B 1 160 ? 35.864 80.455 69.991  1.00 82.43  ? 224 THR B CG2 1 
ATOM   3924  N  N   . CYS B 1 161 ? 32.741 76.921 70.123  1.00 81.06  ? 225 CYS B N   1 
ATOM   3925  C  CA  . CYS B 1 161 ? 31.576 76.114 69.770  1.00 72.00  ? 225 CYS B CA  1 
ATOM   3926  C  C   . CYS B 1 161 ? 30.327 76.874 70.119  1.00 68.42  ? 225 CYS B C   1 
ATOM   3927  O  O   . CYS B 1 161 ? 30.321 77.643 71.065  1.00 88.84  ? 225 CYS B O   1 
ATOM   3928  C  CB  . CYS B 1 161 ? 31.596 74.777 70.507  1.00 86.43  ? 225 CYS B CB  1 
ATOM   3929  S  SG  . CYS B 1 161 ? 33.105 73.812 70.208  1.00 121.00 ? 225 CYS B SG  1 
ATOM   3930  N  N   . TYR B 1 162 ? 29.271 76.658 69.356  1.00 63.90  ? 226 TYR B N   1 
ATOM   3931  C  CA  . TYR B 1 162 ? 27.999 77.371 69.529  1.00 59.61  ? 226 TYR B CA  1 
ATOM   3932  C  C   . TYR B 1 162 ? 26.905 76.363 69.787  1.00 59.13  ? 226 TYR B C   1 
ATOM   3933  O  O   . TYR B 1 162 ? 26.798 75.362 69.080  1.00 75.06  ? 226 TYR B O   1 
ATOM   3934  C  CB  . TYR B 1 162 ? 27.647 78.169 68.267  1.00 58.62  ? 226 TYR B CB  1 
ATOM   3935  C  CG  . TYR B 1 162 ? 28.767 79.063 67.809  1.00 66.23  ? 226 TYR B CG  1 
ATOM   3936  C  CD1 . TYR B 1 162 ? 28.801 80.402 68.180  1.00 68.10  ? 226 TYR B CD1 1 
ATOM   3937  C  CD2 . TYR B 1 162 ? 29.823 78.559 67.038  1.00 73.82  ? 226 TYR B CD2 1 
ATOM   3938  C  CE1 . TYR B 1 162 ? 29.854 81.234 67.783  1.00 83.97  ? 226 TYR B CE1 1 
ATOM   3939  C  CE2 . TYR B 1 162 ? 30.878 79.376 66.631  1.00 90.91  ? 226 TYR B CE2 1 
ATOM   3940  C  CZ  . TYR B 1 162 ? 30.888 80.715 67.010  1.00 101.88 ? 226 TYR B CZ  1 
ATOM   3941  O  OH  . TYR B 1 162 ? 31.924 81.539 66.626  1.00 101.54 ? 226 TYR B OH  1 
ATOM   3942  N  N   . THR B 1 163 ? 26.097 76.608 70.804  1.00 53.29  ? 227 THR B N   1 
ATOM   3943  C  CA  . THR B 1 163 ? 24.963 75.739 71.058  1.00 60.11  ? 227 THR B CA  1 
ATOM   3944  C  C   . THR B 1 163 ? 23.759 76.548 71.515  1.00 62.63  ? 227 THR B C   1 
ATOM   3945  O  O   . THR B 1 163 ? 23.908 77.674 71.963  1.00 69.42  ? 227 THR B O   1 
ATOM   3946  C  CB  . THR B 1 163 ? 25.275 74.601 72.061  1.00 63.34  ? 227 THR B CB  1 
ATOM   3947  O  OG1 . THR B 1 163 ? 24.131 73.729 72.173  1.00 74.32  ? 227 THR B OG1 1 
ATOM   3948  C  CG2 . THR B 1 163 ? 25.607 75.171 73.423  1.00 65.51  ? 227 THR B CG2 1 
ATOM   3949  N  N   . ILE B 1 164 ? 22.568 75.962 71.391  1.00 63.14  ? 228 ILE B N   1 
ATOM   3950  C  CA  . ILE B 1 164 ? 21.334 76.636 71.754  1.00 60.85  ? 228 ILE B CA  1 
ATOM   3951  C  C   . ILE B 1 164 ? 20.619 75.938 72.909  1.00 68.36  ? 228 ILE B C   1 
ATOM   3952  O  O   . ILE B 1 164 ? 20.347 74.735 72.856  1.00 80.11  ? 228 ILE B O   1 
ATOM   3953  C  CB  . ILE B 1 164 ? 20.405 76.789 70.546  1.00 55.02  ? 228 ILE B CB  1 
ATOM   3954  C  CG1 . ILE B 1 164 ? 21.039 77.721 69.532  1.00 53.88  ? 228 ILE B CG1 1 
ATOM   3955  C  CG2 . ILE B 1 164 ? 19.065 77.407 70.942  1.00 70.47  ? 228 ILE B CG2 1 
ATOM   3956  C  CD1 . ILE B 1 164 ? 20.424 77.605 68.194  1.00 53.93  ? 228 ILE B CD1 1 
ATOM   3957  N  N   . ILE B 1 165 ? 20.297 76.728 73.936  1.00 73.95  ? 229 ILE B N   1 
ATOM   3958  C  CA  . ILE B 1 165 ? 19.671 76.229 75.147  1.00 66.37  ? 229 ILE B CA  1 
ATOM   3959  C  C   . ILE B 1 165 ? 18.314 76.856 75.438  1.00 68.36  ? 229 ILE B C   1 
ATOM   3960  O  O   . ILE B 1 165 ? 18.150 78.089 75.436  1.00 67.28  ? 229 ILE B O   1 
ATOM   3961  C  CB  . ILE B 1 165 ? 20.585 76.405 76.350  1.00 76.09  ? 229 ILE B CB  1 
ATOM   3962  C  CG1 . ILE B 1 165 ? 21.993 75.937 75.977  1.00 92.06  ? 229 ILE B CG1 1 
ATOM   3963  C  CG2 . ILE B 1 165 ? 20.037 75.638 77.531  1.00 74.97  ? 229 ILE B CG2 1 
ATOM   3964  C  CD1 . ILE B 1 165 ? 22.566 74.871 76.869  1.00 100.26 ? 229 ILE B CD1 1 
ATOM   3965  N  N   . ALA B 1 166 ? 17.359 75.968 75.710  1.00 67.97  ? 230 ALA B N   1 
ATOM   3966  C  CA  . ALA B 1 166 ? 15.979 76.325 75.985  1.00 77.66  ? 230 ALA B CA  1 
ATOM   3967  C  C   . ALA B 1 166 ? 15.654 76.318 77.470  1.00 82.35  ? 230 ALA B C   1 
ATOM   3968  O  O   . ALA B 1 166 ? 16.086 75.425 78.202  1.00 89.49  ? 230 ALA B O   1 
ATOM   3969  C  CB  . ALA B 1 166 ? 15.047 75.378 75.248  1.00 72.17  ? 230 ALA B CB  1 
ATOM   3970  N  N   . ASP B 1 167 ? 14.861 77.305 77.883  1.00 73.95  ? 231 ASP B N   1 
ATOM   3971  C  CA  . ASP B 1 167 ? 14.380 77.450 79.249  1.00 72.33  ? 231 ASP B CA  1 
ATOM   3972  C  C   . ASP B 1 167 ? 12.838 77.628 79.265  1.00 77.71  ? 231 ASP B C   1 
ATOM   3973  O  O   . ASP B 1 167 ? 12.227 78.087 78.279  1.00 75.81  ? 231 ASP B O   1 
ATOM   3974  C  CB  . ASP B 1 167 ? 15.071 78.674 79.850  1.00 87.90  ? 231 ASP B CB  1 
ATOM   3975  C  CG  . ASP B 1 167 ? 15.167 78.624 81.357  1.00 112.15 ? 231 ASP B CG  1 
ATOM   3976  O  OD1 . ASP B 1 167 ? 14.566 77.719 81.971  1.00 149.46 ? 231 ASP B OD1 1 
ATOM   3977  O  OD2 . ASP B 1 167 ? 15.848 79.502 81.934  1.00 120.34 ? 231 ASP B OD2 1 
ATOM   3978  N  N   . GLY B 1 168 ? 12.199 77.270 80.370  1.00 72.84  ? 232 GLY B N   1 
ATOM   3979  C  CA  . GLY B 1 168 ? 10.787 77.596 80.516  1.00 82.12  ? 232 GLY B CA  1 
ATOM   3980  C  C   . GLY B 1 168 ? 9.866  76.437 80.828  1.00 98.95  ? 232 GLY B C   1 
ATOM   3981  O  O   . GLY B 1 168 ? 10.134 75.287 80.466  1.00 89.61  ? 232 GLY B O   1 
ATOM   3982  N  N   . THR B 1 169 ? 8.764  76.773 81.494  1.00 108.58 ? 233 THR B N   1 
ATOM   3983  C  CA  . THR B 1 169 ? 7.811  75.805 82.022  1.00 99.20  ? 233 THR B CA  1 
ATOM   3984  C  C   . THR B 1 169 ? 7.071  75.110 80.894  1.00 83.24  ? 233 THR B C   1 
ATOM   3985  O  O   . THR B 1 169 ? 6.870  73.908 80.931  1.00 75.61  ? 233 THR B O   1 
ATOM   3986  C  CB  . THR B 1 169 ? 6.793  76.502 82.972  1.00 116.66 ? 233 THR B CB  1 
ATOM   3987  O  OG1 . THR B 1 169 ? 7.504  77.270 83.944  1.00 122.33 ? 233 THR B OG1 1 
ATOM   3988  C  CG2 . THR B 1 169 ? 5.902  75.493 83.699  1.00 118.40 ? 233 THR B CG2 1 
ATOM   3989  N  N   . THR B 1 170 ? 6.659  75.887 79.899  1.00 109.44 ? 234 THR B N   1 
ATOM   3990  C  CA  . THR B 1 170 ? 5.886  75.370 78.777  1.00 104.61 ? 234 THR B CA  1 
ATOM   3991  C  C   . THR B 1 170 ? 6.231  76.111 77.497  1.00 88.94  ? 234 THR B C   1 
ATOM   3992  O  O   . THR B 1 170 ? 6.886  77.163 77.542  1.00 123.09 ? 234 THR B O   1 
ATOM   3993  C  CB  . THR B 1 170 ? 4.365  75.422 79.048  1.00 114.92 ? 234 THR B CB  1 
ATOM   3994  O  OG1 . THR B 1 170 ? 3.671  74.927 77.899  1.00 149.84 ? 234 THR B OG1 1 
ATOM   3995  C  CG2 . THR B 1 170 ? 3.898  76.835 79.366  1.00 81.36  ? 234 THR B CG2 1 
ATOM   3996  N  N   . TYR B 1 171 ? 5.774  75.563 76.371  1.00 76.08  ? 235 TYR B N   1 
ATOM   3997  C  CA  . TYR B 1 171 ? 6.231  75.986 75.041  1.00 82.00  ? 235 TYR B CA  1 
ATOM   3998  C  C   . TYR B 1 171 ? 5.633  77.293 74.609  1.00 78.47  ? 235 TYR B C   1 
ATOM   3999  O  O   . TYR B 1 171 ? 6.229  78.056 73.848  1.00 97.31  ? 235 TYR B O   1 
ATOM   4000  C  CB  . TYR B 1 171 ? 5.977  74.880 74.035  1.00 86.04  ? 235 TYR B CB  1 
ATOM   4001  C  CG  . TYR B 1 171 ? 6.545  73.568 74.541  1.00 149.44 ? 235 TYR B CG  1 
ATOM   4002  C  CD1 . TYR B 1 171 ? 7.937  73.396 74.749  1.00 155.25 ? 235 TYR B CD1 1 
ATOM   4003  C  CD2 . TYR B 1 171 ? 5.700  72.510 74.852  1.00 162.78 ? 235 TYR B CD2 1 
ATOM   4004  C  CE1 . TYR B 1 171 ? 8.461  72.184 75.232  1.00 145.44 ? 235 TYR B CE1 1 
ATOM   4005  C  CE2 . TYR B 1 171 ? 6.213  71.294 75.329  1.00 190.44 ? 235 TYR B CE2 1 
ATOM   4006  C  CZ  . TYR B 1 171 ? 7.590  71.137 75.515  1.00 164.06 ? 235 TYR B CZ  1 
ATOM   4007  O  OH  . TYR B 1 171 ? 8.086  69.941 75.981  1.00 159.89 ? 235 TYR B OH  1 
ATOM   4008  N  N   . THR B 1 172 ? 4.456  77.554 75.145  1.00 75.77  ? 236 THR B N   1 
ATOM   4009  C  CA  . THR B 1 172 ? 3.860  78.858 75.090  1.00 74.90  ? 236 THR B CA  1 
ATOM   4010  C  C   . THR B 1 172 ? 4.819  79.918 75.684  1.00 74.08  ? 236 THR B C   1 
ATOM   4011  O  O   . THR B 1 172 ? 4.872  81.054 75.211  1.00 103.66 ? 236 THR B O   1 
ATOM   4012  C  CB  . THR B 1 172 ? 2.515  78.837 75.845  1.00 83.76  ? 236 THR B CB  1 
ATOM   4013  O  OG1 . THR B 1 172 ? 2.745  78.942 77.247  1.00 95.79  ? 236 THR B OG1 1 
ATOM   4014  C  CG2 . THR B 1 172 ? 1.782  77.539 75.592  1.00 66.95  ? 236 THR B CG2 1 
ATOM   4015  N  N   . ALA B 1 173 ? 5.601  79.519 76.682  1.00 70.03  ? 237 ALA B N   1 
ATOM   4016  C  CA  . ALA B 1 173 ? 6.408  80.432 77.497  1.00 89.56  ? 237 ALA B CA  1 
ATOM   4017  C  C   . ALA B 1 173 ? 7.924  80.241 77.389  1.00 86.93  ? 237 ALA B C   1 
ATOM   4018  O  O   . ALA B 1 173 ? 8.672  80.743 78.221  1.00 110.66 ? 237 ALA B O   1 
ATOM   4019  C  CB  . ALA B 1 173 ? 5.986  80.323 78.970  1.00 96.59  ? 237 ALA B CB  1 
ATOM   4020  N  N   . SER B 1 174 ? 8.386  79.541 76.370  1.00 76.77  ? 238 SER B N   1 
ATOM   4021  C  CA  . SER B 1 174 ? 9.814  79.229 76.270  1.00 79.29  ? 238 SER B CA  1 
ATOM   4022  C  C   . SER B 1 174 ? 10.729 80.443 75.991  1.00 75.76  ? 238 SER B C   1 
ATOM   4023  O  O   . SER B 1 174 ? 10.308 81.468 75.436  1.00 86.52  ? 238 SER B O   1 
ATOM   4024  C  CB  . SER B 1 174 ? 10.042 78.145 75.214  1.00 72.44  ? 238 SER B CB  1 
ATOM   4025  O  OG  . SER B 1 174 ? 9.696  78.618 73.918  1.00 102.42 ? 238 SER B OG  1 
ATOM   4026  N  N   . SER B 1 175 ? 11.987 80.292 76.385  1.00 65.13  ? 239 SER B N   1 
ATOM   4027  C  CA  . SER B 1 175 ? 13.026 81.283 76.166  1.00 69.17  ? 239 SER B CA  1 
ATOM   4028  C  C   . SER B 1 175 ? 14.231 80.551 75.631  1.00 73.55  ? 239 SER B C   1 
ATOM   4029  O  O   . SER B 1 175 ? 14.507 79.443 76.070  1.00 89.63  ? 239 SER B O   1 
ATOM   4030  C  CB  . SER B 1 175 ? 13.409 81.915 77.495  1.00 84.28  ? 239 SER B CB  1 
ATOM   4031  O  OG  . SER B 1 175 ? 14.540 82.755 77.356  1.00 127.44 ? 239 SER B OG  1 
ATOM   4032  N  N   . HIS B 1 176 ? 14.972 81.153 74.708  1.00 73.84  ? 240 HIS B N   1 
ATOM   4033  C  CA  . HIS B 1 176 ? 16.126 80.473 74.102  1.00 59.09  ? 240 HIS B CA  1 
ATOM   4034  C  C   . HIS B 1 176 ? 17.317 81.331 74.041  1.00 59.47  ? 240 HIS B C   1 
ATOM   4035  O  O   . HIS B 1 176 ? 17.274 82.444 73.523  1.00 70.80  ? 240 HIS B O   1 
ATOM   4036  C  CB  . HIS B 1 176 ? 15.786 80.004 72.703  1.00 61.62  ? 240 HIS B CB  1 
ATOM   4037  C  CG  . HIS B 1 176 ? 14.575 79.108 72.654  1.00 63.63  ? 240 HIS B CG  1 
ATOM   4038  N  ND1 . HIS B 1 176 ? 14.459 77.725 72.695  1.00 67.27  ? 240 HIS B ND1 1 
ATOM   4039  C  CD2 . HIS B 1 176 ? 13.331 79.590 72.614  1.00 67.07  ? 240 HIS B CD2 1 
ATOM   4040  C  CE1 . HIS B 1 176 ? 13.148 77.434 72.643  1.00 75.53  ? 240 HIS B CE1 1 
ATOM   4041  N  NE2 . HIS B 1 176 ? 12.457 78.579 72.592  1.00 79.68  ? 240 HIS B NE2 1 
ATOM   4042  N  N   . ARG B 1 177 ? 18.410 80.824 74.578  1.00 61.90  ? 241 ARG B N   1 
ATOM   4043  C  CA  . ARG B 1 177 ? 19.666 81.537 74.454  1.00 60.51  ? 241 ARG B CA  1 
ATOM   4044  C  C   . ARG B 1 177 ? 20.633 80.757 73.572  1.00 64.33  ? 241 ARG B C   1 
ATOM   4045  O  O   . ARG B 1 177 ? 20.672 79.521 73.540  1.00 57.06  ? 241 ARG B O   1 
ATOM   4046  C  CB  . ARG B 1 177 ? 20.284 81.842 75.813  1.00 63.21  ? 241 ARG B CB  1 
ATOM   4047  C  CG  . ARG B 1 177 ? 19.382 82.585 76.753  1.00 75.81  ? 241 ARG B CG  1 
ATOM   4048  C  CD  . ARG B 1 177 ? 19.301 81.903 78.098  1.00 87.12  ? 241 ARG B CD  1 
ATOM   4049  N  NE  . ARG B 1 177 ? 20.372 82.354 78.980  1.00 93.05  ? 241 ARG B NE  1 
ATOM   4050  C  CZ  . ARG B 1 177 ? 20.271 83.386 79.814  1.00 81.90  ? 241 ARG B CZ  1 
ATOM   4051  N  NH1 . ARG B 1 177 ? 19.142 84.089 79.885  1.00 70.14  ? 241 ARG B NH1 1 
ATOM   4052  N  NH2 . ARG B 1 177 ? 21.304 83.705 80.580  1.00 72.48  ? 241 ARG B NH2 1 
ATOM   4053  N  N   . LEU B 1 178 ? 21.418 81.525 72.852  1.00 64.87  ? 242 LEU B N   1 
ATOM   4054  C  CA  . LEU B 1 178 ? 22.426 81.001 72.000  1.00 65.91  ? 242 LEU B CA  1 
ATOM   4055  C  C   . LEU B 1 178 ? 23.736 81.185 72.764  1.00 73.72  ? 242 LEU B C   1 
ATOM   4056  O  O   . LEU B 1 178 ? 24.136 82.321 73.027  1.00 74.19  ? 242 LEU B O   1 
ATOM   4057  C  CB  . LEU B 1 178 ? 22.377 81.842 70.740  1.00 73.36  ? 242 LEU B CB  1 
ATOM   4058  C  CG  . LEU B 1 178 ? 23.502 81.905 69.731  1.00 96.90  ? 242 LEU B CG  1 
ATOM   4059  C  CD1 . LEU B 1 178 ? 23.758 80.521 69.170  1.00 132.73 ? 242 LEU B CD1 1 
ATOM   4060  C  CD2 . LEU B 1 178 ? 23.053 82.860 68.637  1.00 87.43  ? 242 LEU B CD2 1 
ATOM   4061  N  N   . TYR B 1 179 ? 24.364 80.075 73.167  1.00 68.55  ? 243 TYR B N   1 
ATOM   4062  C  CA  . TYR B 1 179 ? 25.627 80.099 73.932  1.00 63.98  ? 243 TYR B CA  1 
ATOM   4063  C  C   . TYR B 1 179 ? 26.859 79.943 73.096  1.00 65.83  ? 243 TYR B C   1 
ATOM   4064  O  O   . TYR B 1 179 ? 26.856 79.240 72.094  1.00 84.85  ? 243 TYR B O   1 
ATOM   4065  C  CB  . TYR B 1 179 ? 25.649 78.972 74.950  1.00 66.40  ? 243 TYR B CB  1 
ATOM   4066  C  CG  . TYR B 1 179 ? 24.903 79.339 76.171  1.00 69.73  ? 243 TYR B CG  1 
ATOM   4067  C  CD1 . TYR B 1 179 ? 23.526 79.098 76.264  1.00 72.79  ? 243 TYR B CD1 1 
ATOM   4068  C  CD2 . TYR B 1 179 ? 25.551 79.982 77.223  1.00 63.96  ? 243 TYR B CD2 1 
ATOM   4069  C  CE1 . TYR B 1 179 ? 22.814 79.470 77.412  1.00 76.70  ? 243 TYR B CE1 1 
ATOM   4070  C  CE2 . TYR B 1 179 ? 24.855 80.371 78.358  1.00 70.43  ? 243 TYR B CE2 1 
ATOM   4071  C  CZ  . TYR B 1 179 ? 23.485 80.116 78.452  1.00 68.94  ? 243 TYR B CZ  1 
ATOM   4072  O  OH  . TYR B 1 179 ? 22.790 80.485 79.580  1.00 68.39  ? 243 TYR B OH  1 
ATOM   4073  N  N   . ARG B 1 180 ? 27.933 80.568 73.535  1.00 67.44  ? 244 ARG B N   1 
ATOM   4074  C  CA  . ARG B 1 180 ? 29.237 80.390 72.904  1.00 69.51  ? 244 ARG B CA  1 
ATOM   4075  C  C   . ARG B 1 180 ? 30.143 79.757 73.914  1.00 63.44  ? 244 ARG B C   1 
ATOM   4076  O  O   . ARG B 1 180 ? 30.210 80.218 75.046  1.00 70.18  ? 244 ARG B O   1 
ATOM   4077  C  CB  . ARG B 1 180 ? 29.756 81.759 72.448  1.00 82.16  ? 244 ARG B CB  1 
ATOM   4078  C  CG  . ARG B 1 180 ? 31.193 81.897 72.015  1.00 82.15  ? 244 ARG B CG  1 
ATOM   4079  C  CD  . ARG B 1 180 ? 31.439 83.360 71.602  1.00 94.68  ? 244 ARG B CD  1 
ATOM   4080  N  NE  . ARG B 1 180 ? 32.734 83.806 72.121  1.00 189.08 ? 244 ARG B NE  1 
ATOM   4081  C  CZ  . ARG B 1 180 ? 33.809 84.073 71.378  1.00 226.81 ? 244 ARG B CZ  1 
ATOM   4082  N  NH1 . ARG B 1 180 ? 33.752 83.974 70.055  1.00 238.46 ? 244 ARG B NH1 1 
ATOM   4083  N  NH2 . ARG B 1 180 ? 34.942 84.459 71.961  1.00 213.61 ? 244 ARG B NH2 1 
ATOM   4084  N  N   . LEU B 1 181 ? 30.832 78.696 73.524  1.00 64.39  ? 245 LEU B N   1 
ATOM   4085  C  CA  . LEU B 1 181 ? 31.746 78.008 74.449  1.00 75.70  ? 245 LEU B CA  1 
ATOM   4086  C  C   . LEU B 1 181 ? 33.149 77.950 73.896  1.00 87.60  ? 245 LEU B C   1 
ATOM   4087  O  O   . LEU B 1 181 ? 33.314 77.851 72.679  1.00 98.01  ? 245 LEU B O   1 
ATOM   4088  C  CB  . LEU B 1 181 ? 31.278 76.586 74.703  1.00 66.40  ? 245 LEU B CB  1 
ATOM   4089  C  CG  . LEU B 1 181 ? 29.792 76.451 74.973  1.00 62.55  ? 245 LEU B CG  1 
ATOM   4090  C  CD1 . LEU B 1 181 ? 29.330 75.073 74.540  1.00 68.04  ? 245 LEU B CD1 1 
ATOM   4091  C  CD2 . LEU B 1 181 ? 29.526 76.677 76.407  1.00 60.31  ? 245 LEU B CD2 1 
ATOM   4092  N  N   . VAL B 1 182 ? 34.148 78.002 74.785  1.00 90.95  ? 246 VAL B N   1 
ATOM   4093  C  CA  . VAL B 1 182 ? 35.562 77.824 74.412  1.00 88.70  ? 246 VAL B CA  1 
ATOM   4094  C  C   . VAL B 1 182 ? 36.268 76.930 75.420  1.00 84.51  ? 246 VAL B C   1 
ATOM   4095  O  O   . VAL B 1 182 ? 36.204 77.183 76.622  1.00 79.66  ? 246 VAL B O   1 
ATOM   4096  C  CB  . VAL B 1 182 ? 36.342 79.171 74.360  1.00 93.27  ? 246 VAL B CB  1 
ATOM   4097  C  CG1 . VAL B 1 182 ? 37.721 78.969 73.725  1.00 95.31  ? 246 VAL B CG1 1 
ATOM   4098  C  CG2 . VAL B 1 182 ? 35.550 80.261 73.625  1.00 78.64  ? 246 VAL B CG2 1 
ATOM   4099  N  N   . ASN B 1 183 ? 36.966 75.907 74.927  1.00 92.60  ? 247 ASN B N   1 
ATOM   4100  C  CA  . ASN B 1 183 ? 37.677 74.957 75.784  1.00 78.52  ? 247 ASN B CA  1 
ATOM   4101  C  C   . ASN B 1 183 ? 36.811 74.558 76.986  1.00 77.41  ? 247 ASN B C   1 
ATOM   4102  O  O   . ASN B 1 183 ? 37.318 74.269 78.056  1.00 80.09  ? 247 ASN B O   1 
ATOM   4103  C  CB  . ASN B 1 183 ? 39.053 75.507 76.184  1.00 79.66  ? 247 ASN B CB  1 
ATOM   4104  C  CG  . ASN B 1 183 ? 39.997 75.654 74.987  1.00 87.84  ? 247 ASN B CG  1 
ATOM   4105  O  OD1 . ASN B 1 183 ? 39.605 75.356 73.859  1.00 91.81  ? 247 ASN B OD1 1 
ATOM   4106  N  ND2 . ASN B 1 183 ? 41.245 76.104 75.227  1.00 87.33  ? 247 ASN B ND2 1 
ATOM   4107  N  N   . GLY B 1 184 ? 35.491 74.577 76.788  1.00 75.65  ? 248 GLY B N   1 
ATOM   4108  C  CA  . GLY B 1 184 ? 34.547 74.052 77.761  1.00 77.15  ? 248 GLY B CA  1 
ATOM   4109  C  C   . GLY B 1 184 ? 33.921 75.054 78.708  1.00 81.16  ? 248 GLY B C   1 
ATOM   4110  O  O   . GLY B 1 184 ? 33.054 74.709 79.511  1.00 81.24  ? 248 GLY B O   1 
ATOM   4111  N  N   . THR B 1 185 ? 34.367 76.296 78.641  1.00 90.17  ? 249 THR B N   1 
ATOM   4112  C  CA  . THR B 1 185 ? 33.794 77.341 79.485  1.00 103.75 ? 249 THR B CA  1 
ATOM   4113  C  C   . THR B 1 185 ? 32.945 78.285 78.627  1.00 100.60 ? 249 THR B C   1 
ATOM   4114  O  O   . THR B 1 185 ? 33.224 78.484 77.441  1.00 107.50 ? 249 THR B O   1 
ATOM   4115  C  CB  . THR B 1 185 ? 34.889 78.102 80.264  1.00 113.54 ? 249 THR B CB  1 
ATOM   4116  O  OG1 . THR B 1 185 ? 35.942 78.470 79.366  1.00 126.25 ? 249 THR B OG1 1 
ATOM   4117  C  CG2 . THR B 1 185 ? 35.479 77.220 81.387  1.00 112.53 ? 249 THR B CG2 1 
ATOM   4118  N  N   . SER B 1 186 ? 31.883 78.836 79.199  1.00 90.68  ? 250 SER B N   1 
ATOM   4119  C  CA  . SER B 1 186 ? 31.011 79.698 78.414  1.00 88.52  ? 250 SER B CA  1 
ATOM   4120  C  C   . SER B 1 186 ? 31.723 81.002 78.176  1.00 85.41  ? 250 SER B C   1 
ATOM   4121  O  O   . SER B 1 186 ? 32.300 81.554 79.085  1.00 81.28  ? 250 SER B O   1 
ATOM   4122  C  CB  . SER B 1 186 ? 29.677 79.937 79.108  1.00 90.51  ? 250 SER B CB  1 
ATOM   4123  O  OG  . SER B 1 186 ? 29.849 80.571 80.367  1.00 102.50 ? 250 SER B OG  1 
ATOM   4124  N  N   . ALA B 1 187 ? 31.707 81.459 76.934  1.00 90.63  ? 251 ALA B N   1 
ATOM   4125  C  CA  . ALA B 1 187 ? 32.332 82.713 76.559  1.00 89.35  ? 251 ALA B CA  1 
ATOM   4126  C  C   . ALA B 1 187 ? 31.228 83.654 76.167  1.00 86.55  ? 251 ALA B C   1 
ATOM   4127  O  O   . ALA B 1 187 ? 31.341 84.399 75.202  1.00 93.33  ? 251 ALA B O   1 
ATOM   4128  C  CB  . ALA B 1 187 ? 33.297 82.508 75.403  1.00 106.46 ? 251 ALA B CB  1 
ATOM   4129  N  N   . GLY B 1 188 ? 30.136 83.609 76.913  1.00 86.72  ? 252 GLY B N   1 
ATOM   4130  C  CA  . GLY B 1 188 ? 29.037 84.533 76.666  1.00 84.46  ? 252 GLY B CA  1 
ATOM   4131  C  C   . GLY B 1 188 ? 27.878 83.947 75.875  1.00 85.10  ? 252 GLY B C   1 
ATOM   4132  O  O   . GLY B 1 188 ? 27.956 82.833 75.328  1.00 91.11  ? 252 GLY B O   1 
ATOM   4133  N  N   . TRP B 1 189 ? 26.787 84.703 75.823  1.00 75.28  ? 253 TRP B N   1 
ATOM   4134  C  CA  . TRP B 1 189 ? 25.603 84.269 75.098  1.00 80.27  ? 253 TRP B CA  1 
ATOM   4135  C  C   . TRP B 1 189 ? 24.743 85.420 74.636  1.00 80.99  ? 253 TRP B C   1 
ATOM   4136  O  O   . TRP B 1 189 ? 25.010 86.580 74.955  1.00 95.61  ? 253 TRP B O   1 
ATOM   4137  C  CB  . TRP B 1 189 ? 24.801 83.313 75.962  1.00 86.49  ? 253 TRP B CB  1 
ATOM   4138  C  CG  . TRP B 1 189 ? 24.489 83.953 77.266  1.00 89.22  ? 253 TRP B CG  1 
ATOM   4139  C  CD1 . TRP B 1 189 ? 25.239 83.920 78.435  1.00 102.45 ? 253 TRP B CD1 1 
ATOM   4140  C  CD2 . TRP B 1 189 ? 23.350 84.807 77.564  1.00 100.41 ? 253 TRP B CD2 1 
ATOM   4141  N  NE1 . TRP B 1 189 ? 24.643 84.673 79.415  1.00 104.14 ? 253 TRP B NE1 1 
ATOM   4142  C  CE2 . TRP B 1 189 ? 23.507 85.233 78.960  1.00 96.28  ? 253 TRP B CE2 1 
ATOM   4143  C  CE3 . TRP B 1 189 ? 22.245 85.242 76.845  1.00 121.39 ? 253 TRP B CE3 1 
ATOM   4144  C  CZ2 . TRP B 1 189 ? 22.585 86.059 79.585  1.00 85.45  ? 253 TRP B CZ2 1 
ATOM   4145  C  CZ3 . TRP B 1 189 ? 21.322 86.077 77.486  1.00 121.89 ? 253 TRP B CZ3 1 
ATOM   4146  C  CH2 . TRP B 1 189 ? 21.490 86.472 78.827  1.00 86.48  ? 253 TRP B CH2 1 
ATOM   4147  N  N   . LYS B 1 190 ? 23.710 85.100 73.860  1.00 76.54  ? 254 LYS B N   1 
ATOM   4148  C  CA  . LYS B 1 190 ? 22.748 86.079 73.400  1.00 66.62  ? 254 LYS B CA  1 
ATOM   4149  C  C   . LYS B 1 190 ? 21.347 85.500 73.529  1.00 64.93  ? 254 LYS B C   1 
ATOM   4150  O  O   . LYS B 1 190 ? 21.117 84.334 73.228  1.00 60.60  ? 254 LYS B O   1 
ATOM   4151  C  CB  . LYS B 1 190 ? 23.037 86.482 71.951  1.00 70.24  ? 254 LYS B CB  1 
ATOM   4152  C  CG  . LYS B 1 190 ? 22.042 87.508 71.389  1.00 75.00  ? 254 LYS B CG  1 
ATOM   4153  C  CD  . LYS B 1 190 ? 22.673 88.546 70.483  1.00 79.07  ? 254 LYS B CD  1 
ATOM   4154  C  CE  . LYS B 1 190 ? 21.593 89.389 69.839  1.00 100.85 ? 254 LYS B CE  1 
ATOM   4155  N  NZ  . LYS B 1 190 ? 22.135 90.521 69.044  1.00 122.06 ? 254 LYS B NZ  1 
ATOM   4156  N  N   . ALA B 1 191 ? 20.412 86.308 74.017  1.00 74.59  ? 255 ALA B N   1 
ATOM   4157  C  CA  . ALA B 1 191 ? 19.001 85.925 74.007  1.00 68.72  ? 255 ALA B CA  1 
ATOM   4158  C  C   . ALA B 1 191 ? 18.502 85.979 72.597  1.00 67.03  ? 255 ALA B C   1 
ATOM   4159  O  O   . ALA B 1 191 ? 18.752 86.938 71.883  1.00 72.16  ? 255 ALA B O   1 
ATOM   4160  C  CB  . ALA B 1 191 ? 18.188 86.840 74.846  1.00 66.13  ? 255 ALA B CB  1 
ATOM   4161  N  N   . LEU B 1 192 ? 17.815 84.927 72.190  1.00 67.91  ? 256 LEU B N   1 
ATOM   4162  C  CA  . LEU B 1 192 ? 17.188 84.913 70.893  1.00 63.67  ? 256 LEU B CA  1 
ATOM   4163  C  C   . LEU B 1 192 ? 15.764 85.364 71.110  1.00 63.24  ? 256 LEU B C   1 
ATOM   4164  O  O   . LEU B 1 192 ? 15.139 84.924 72.069  1.00 60.23  ? 256 LEU B O   1 
ATOM   4165  C  CB  . LEU B 1 192 ? 17.233 83.514 70.295  1.00 65.43  ? 256 LEU B CB  1 
ATOM   4166  C  CG  . LEU B 1 192 ? 18.619 83.015 69.901  1.00 74.23  ? 256 LEU B CG  1 
ATOM   4167  C  CD1 . LEU B 1 192 ? 18.448 81.607 69.410  1.00 93.82  ? 256 LEU B CD1 1 
ATOM   4168  C  CD2 . LEU B 1 192 ? 19.303 83.874 68.834  1.00 67.61  ? 256 LEU B CD2 1 
ATOM   4169  N  N   . ASP B 1 193 ? 15.274 86.256 70.240  1.00 71.71  ? 257 ASP B N   1 
ATOM   4170  C  CA  . ASP B 1 193 ? 13.892 86.757 70.288  1.00 78.90  ? 257 ASP B CA  1 
ATOM   4171  C  C   . ASP B 1 193 ? 12.936 85.759 69.640  1.00 79.70  ? 257 ASP B C   1 
ATOM   4172  O  O   . ASP B 1 193 ? 12.859 85.626 68.405  1.00 60.94  ? 257 ASP B O   1 
ATOM   4173  C  CB  . ASP B 1 193 ? 13.779 88.128 69.607  1.00 108.15 ? 257 ASP B CB  1 
ATOM   4174  C  CG  . ASP B 1 193 ? 12.369 88.724 69.691  1.00 119.37 ? 257 ASP B CG  1 
ATOM   4175  O  OD1 . ASP B 1 193 ? 11.497 88.136 70.365  1.00 149.57 ? 257 ASP B OD1 1 
ATOM   4176  O  OD2 . ASP B 1 193 ? 12.129 89.789 69.080  1.00 105.19 ? 257 ASP B OD2 1 
ATOM   4177  N  N   . THR B 1 194 ? 12.198 85.069 70.497  1.00 82.23  ? 258 THR B N   1 
ATOM   4178  C  CA  . THR B 1 194 ? 11.378 83.953 70.079  1.00 95.45  ? 258 THR B CA  1 
ATOM   4179  C  C   . THR B 1 194 ? 9.905  84.326 70.086  1.00 102.41 ? 258 THR B C   1 
ATOM   4180  O  O   . THR B 1 194 ? 9.079  83.611 69.523  1.00 115.81 ? 258 THR B O   1 
ATOM   4181  C  CB  . THR B 1 194 ? 11.580 82.769 71.033  1.00 102.83 ? 258 THR B CB  1 
ATOM   4182  O  OG1 . THR B 1 194 ? 10.952 81.608 70.484  1.00 160.91 ? 258 THR B OG1 1 
ATOM   4183  C  CG2 . THR B 1 194 ? 10.977 83.069 72.421  1.00 99.26  ? 258 THR B CG2 1 
ATOM   4184  N  N   . THR B 1 195 ? 9.590  85.454 70.723  1.00 132.84 ? 259 THR B N   1 
ATOM   4185  C  CA  . THR B 1 195 ? 8.212  85.773 71.121  1.00 107.44 ? 259 THR B CA  1 
ATOM   4186  C  C   . THR B 1 195 ? 7.226  85.488 70.029  1.00 75.40  ? 259 THR B C   1 
ATOM   4187  O  O   . THR B 1 195 ? 7.440  85.831 68.855  1.00 66.49  ? 259 THR B O   1 
ATOM   4188  C  CB  . THR B 1 195 ? 8.005  87.240 71.656  1.00 114.27 ? 259 THR B CB  1 
ATOM   4189  O  OG1 . THR B 1 195 ? 8.411  88.197 70.667  1.00 101.05 ? 259 THR B OG1 1 
ATOM   4190  C  CG2 . THR B 1 195 ? 8.774  87.473 72.974  1.00 140.57 ? 259 THR B CG2 1 
ATOM   4191  N  N   . GLY B 1 196 ? 6.153  84.826 70.432  1.00 69.74  ? 260 GLY B N   1 
ATOM   4192  C  CA  . GLY B 1 196 ? 5.077  84.512 69.515  1.00 75.97  ? 260 GLY B CA  1 
ATOM   4193  C  C   . GLY B 1 196 ? 5.224  83.131 68.929  1.00 53.35  ? 260 GLY B C   1 
ATOM   4194  O  O   . GLY B 1 196 ? 4.288  82.596 68.376  1.00 50.65  ? 260 GLY B O   1 
ATOM   4195  N  N   . PHE B 1 197 ? 6.409  82.553 69.019  1.00 57.44  ? 261 PHE B N   1 
ATOM   4196  C  CA  . PHE B 1 197 ? 6.572  81.169 68.598  1.00 55.73  ? 261 PHE B CA  1 
ATOM   4197  C  C   . PHE B 1 197 ? 7.466  80.359 69.525  1.00 60.43  ? 261 PHE B C   1 
ATOM   4198  O  O   . PHE B 1 197 ? 7.798  80.809 70.620  1.00 67.42  ? 261 PHE B O   1 
ATOM   4199  C  CB  . PHE B 1 197 ? 7.007  81.077 67.129  1.00 64.91  ? 261 PHE B CB  1 
ATOM   4200  C  CG  . PHE B 1 197 ? 8.426  81.532 66.852  1.00 67.94  ? 261 PHE B CG  1 
ATOM   4201  C  CD1 . PHE B 1 197 ? 9.454  80.592 66.735  1.00 70.56  ? 261 PHE B CD1 1 
ATOM   4202  C  CD2 . PHE B 1 197 ? 8.721  82.878 66.637  1.00 59.69  ? 261 PHE B CD2 1 
ATOM   4203  C  CE1 . PHE B 1 197 ? 10.765 80.992 66.455  1.00 82.39  ? 261 PHE B CE1 1 
ATOM   4204  C  CE2 . PHE B 1 197 ? 10.012 83.283 66.351  1.00 67.67  ? 261 PHE B CE2 1 
ATOM   4205  C  CZ  . PHE B 1 197 ? 11.046 82.335 66.262  1.00 78.80  ? 261 PHE B CZ  1 
ATOM   4206  N  N   . ASN B 1 198 ? 7.848  79.160 69.086  1.00 63.64  ? 262 ASN B N   1 
ATOM   4207  C  CA  . ASN B 1 198 ? 8.688  78.278 69.886  1.00 51.93  ? 262 ASN B CA  1 
ATOM   4208  C  C   . ASN B 1 198 ? 9.715  77.517 69.042  1.00 55.35  ? 262 ASN B C   1 
ATOM   4209  O  O   . ASN B 1 198 ? 9.433  77.185 67.903  1.00 88.13  ? 262 ASN B O   1 
ATOM   4210  C  CB  . ASN B 1 198 ? 7.765  77.373 70.681  1.00 53.00  ? 262 ASN B CB  1 
ATOM   4211  C  CG  . ASN B 1 198 ? 8.396  76.050 71.045  1.00 57.23  ? 262 ASN B CG  1 
ATOM   4212  O  OD1 . ASN B 1 198 ? 7.997  75.003 70.520  1.00 60.32  ? 262 ASN B OD1 1 
ATOM   4213  N  ND2 . ASN B 1 198 ? 9.381  76.079 71.942  1.00 49.46  ? 262 ASN B ND2 1 
ATOM   4214  N  N   . PHE B 1 199 ? 10.903 77.242 69.592  1.00 58.56  ? 263 PHE B N   1 
ATOM   4215  C  CA  . PHE B 1 199 ? 12.068 76.820 68.785  1.00 50.86  ? 263 PHE B CA  1 
ATOM   4216  C  C   . PHE B 1 199 ? 12.891 75.782 69.530  1.00 54.73  ? 263 PHE B C   1 
ATOM   4217  O  O   . PHE B 1 199 ? 13.816 76.086 70.283  1.00 72.26  ? 263 PHE B O   1 
ATOM   4218  C  CB  . PHE B 1 199 ? 12.920 78.068 68.501  1.00 53.41  ? 263 PHE B CB  1 
ATOM   4219  C  CG  . PHE B 1 199 ? 14.083 77.835 67.597  1.00 44.45  ? 263 PHE B CG  1 
ATOM   4220  C  CD1 . PHE B 1 199 ? 13.901 77.593 66.273  1.00 48.02  ? 263 PHE B CD1 1 
ATOM   4221  C  CD2 . PHE B 1 199 ? 15.366 77.887 68.081  1.00 56.19  ? 263 PHE B CD2 1 
ATOM   4222  C  CE1 . PHE B 1 199 ? 14.993 77.396 65.433  1.00 59.78  ? 263 PHE B CE1 1 
ATOM   4223  C  CE2 . PHE B 1 199 ? 16.461 77.693 67.258  1.00 56.06  ? 263 PHE B CE2 1 
ATOM   4224  C  CZ  . PHE B 1 199 ? 16.281 77.449 65.940  1.00 53.61  ? 263 PHE B CZ  1 
ATOM   4225  N  N   . GLU B 1 200 ? 12.567 74.529 69.317  1.00 62.22  ? 264 GLU B N   1 
ATOM   4226  C  CA  . GLU B 1 200 ? 13.147 73.485 70.148  1.00 58.30  ? 264 GLU B CA  1 
ATOM   4227  C  C   . GLU B 1 200 ? 13.944 72.503 69.345  1.00 54.98  ? 264 GLU B C   1 
ATOM   4228  O  O   . GLU B 1 200 ? 13.631 72.250 68.173  1.00 59.12  ? 264 GLU B O   1 
ATOM   4229  C  CB  . GLU B 1 200 ? 12.043 72.734 70.864  1.00 50.60  ? 264 GLU B CB  1 
ATOM   4230  C  CG  . GLU B 1 200 ? 11.289 73.591 71.829  1.00 74.51  ? 264 GLU B CG  1 
ATOM   4231  C  CD  . GLU B 1 200 ? 11.812 73.489 73.256  1.00 125.18 ? 264 GLU B CD  1 
ATOM   4232  O  OE1 . GLU B 1 200 ? 12.678 72.617 73.527  1.00 140.87 ? 264 GLU B OE1 1 
ATOM   4233  O  OE2 . GLU B 1 200 ? 11.339 74.274 74.114  1.00 116.28 ? 264 GLU B OE2 1 
ATOM   4234  N  N   . PHE B 1 201 ? 14.952 71.923 69.989  1.00 46.30  ? 265 PHE B N   1 
ATOM   4235  C  CA  . PHE B 1 201 ? 15.756 70.882 69.360  1.00 44.56  ? 265 PHE B CA  1 
ATOM   4236  C  C   . PHE B 1 201 ? 16.321 71.326 68.018  1.00 41.25  ? 265 PHE B C   1 
ATOM   4237  O  O   . PHE B 1 201 ? 16.159 70.603 67.032  1.00 44.57  ? 265 PHE B O   1 
ATOM   4238  C  CB  . PHE B 1 201 ? 14.923 69.610 69.163  1.00 41.75  ? 265 PHE B CB  1 
ATOM   4239  C  CG  . PHE B 1 201 ? 14.151 69.200 70.374  1.00 46.19  ? 265 PHE B CG  1 
ATOM   4240  C  CD1 . PHE B 1 201 ? 14.822 68.786 71.519  1.00 60.74  ? 265 PHE B CD1 1 
ATOM   4241  C  CD2 . PHE B 1 201 ? 12.756 69.180 70.356  1.00 50.01  ? 265 PHE B CD2 1 
ATOM   4242  C  CE1 . PHE B 1 201 ? 14.123 68.383 72.650  1.00 80.18  ? 265 PHE B CE1 1 
ATOM   4243  C  CE2 . PHE B 1 201 ? 12.026 68.770 71.478  1.00 54.24  ? 265 PHE B CE2 1 
ATOM   4244  C  CZ  . PHE B 1 201 ? 12.715 68.381 72.635  1.00 80.66  ? 265 PHE B CZ  1 
ATOM   4245  N  N   . PRO B 1 202 ? 16.942 72.528 67.958  1.00 41.84  ? 266 PRO B N   1 
ATOM   4246  C  CA  . PRO B 1 202 ? 17.559 72.962 66.701  1.00 44.90  ? 266 PRO B CA  1 
ATOM   4247  C  C   . PRO B 1 202 ? 18.597 71.970 66.222  1.00 41.28  ? 266 PRO B C   1 
ATOM   4248  O  O   . PRO B 1 202 ? 19.259 71.365 67.012  1.00 51.41  ? 266 PRO B O   1 
ATOM   4249  C  CB  . PRO B 1 202 ? 18.237 74.285 67.071  1.00 41.45  ? 266 PRO B CB  1 
ATOM   4250  C  CG  . PRO B 1 202 ? 18.300 74.280 68.531  1.00 45.00  ? 266 PRO B CG  1 
ATOM   4251  C  CD  . PRO B 1 202 ? 17.061 73.584 68.972  1.00 44.98  ? 266 PRO B CD  1 
ATOM   4252  N  N   . THR B 1 203 ? 18.703 71.809 64.922  1.00 47.01  ? 267 THR B N   1 
ATOM   4253  C  CA  . THR B 1 203 ? 19.656 70.924 64.305  1.00 51.07  ? 267 THR B CA  1 
ATOM   4254  C  C   . THR B 1 203 ? 20.364 71.738 63.210  1.00 55.25  ? 267 THR B C   1 
ATOM   4255  O  O   . THR B 1 203 ? 19.737 72.420 62.369  1.00 60.89  ? 267 THR B O   1 
ATOM   4256  C  CB  . THR B 1 203 ? 18.971 69.631 63.791  1.00 63.64  ? 267 THR B CB  1 
ATOM   4257  O  OG1 . THR B 1 203 ? 19.976 68.728 63.314  1.00 70.63  ? 267 THR B OG1 1 
ATOM   4258  C  CG2 . THR B 1 203 ? 17.913 69.917 62.693  1.00 52.66  ? 267 THR B CG2 1 
ATOM   4259  N  N   . CYS B 1 204 ? 21.682 71.717 63.259  1.00 64.54  ? 268 CYS B N   1 
ATOM   4260  C  CA  . CYS B 1 204 ? 22.436 72.808 62.663  1.00 65.70  ? 268 CYS B CA  1 
ATOM   4261  C  C   . CYS B 1 204 ? 23.567 72.352 61.764  1.00 67.13  ? 268 CYS B C   1 
ATOM   4262  O  O   . CYS B 1 204 ? 24.119 71.251 61.937  1.00 72.99  ? 268 CYS B O   1 
ATOM   4263  C  CB  . CYS B 1 204 ? 23.001 73.679 63.775  1.00 60.06  ? 268 CYS B CB  1 
ATOM   4264  S  SG  . CYS B 1 204 ? 21.786 74.232 64.939  1.00 100.31 ? 268 CYS B SG  1 
ATOM   4265  N  N   . TYR B 1 205 ? 23.921 73.214 60.818  1.00 56.30  ? 269 TYR B N   1 
ATOM   4266  C  CA  . TYR B 1 205 ? 25.151 73.046 60.065  1.00 54.84  ? 269 TYR B CA  1 
ATOM   4267  C  C   . TYR B 1 205 ? 25.757 74.406 59.785  1.00 60.09  ? 269 TYR B C   1 
ATOM   4268  O  O   . TYR B 1 205 ? 25.179 75.446 60.177  1.00 50.34  ? 269 TYR B O   1 
ATOM   4269  C  CB  . TYR B 1 205 ? 24.897 72.279 58.775  1.00 57.77  ? 269 TYR B CB  1 
ATOM   4270  C  CG  . TYR B 1 205 ? 23.971 72.999 57.830  1.00 61.31  ? 269 TYR B CG  1 
ATOM   4271  C  CD1 . TYR B 1 205 ? 24.465 73.589 56.665  1.00 61.29  ? 269 TYR B CD1 1 
ATOM   4272  C  CD2 . TYR B 1 205 ? 22.601 73.120 58.114  1.00 55.32  ? 269 TYR B CD2 1 
ATOM   4273  C  CE1 . TYR B 1 205 ? 23.631 74.277 55.793  1.00 56.22  ? 269 TYR B CE1 1 
ATOM   4274  C  CE2 . TYR B 1 205 ? 21.745 73.812 57.259  1.00 52.07  ? 269 TYR B CE2 1 
ATOM   4275  C  CZ  . TYR B 1 205 ? 22.265 74.393 56.087  1.00 58.27  ? 269 TYR B CZ  1 
ATOM   4276  O  OH  . TYR B 1 205 ? 21.427 75.076 55.200  1.00 48.52  ? 269 TYR B OH  1 
ATOM   4277  N  N   . TYR B 1 206 ? 26.921 74.390 59.124  1.00 67.07  ? 270 TYR B N   1 
ATOM   4278  C  CA  . TYR B 1 206 ? 27.681 75.613 58.868  1.00 64.46  ? 270 TYR B CA  1 
ATOM   4279  C  C   . TYR B 1 206 ? 28.034 75.729 57.421  1.00 62.38  ? 270 TYR B C   1 
ATOM   4280  O  O   . TYR B 1 206 ? 28.520 74.770 56.811  1.00 66.94  ? 270 TYR B O   1 
ATOM   4281  C  CB  . TYR B 1 206 ? 28.952 75.659 59.700  1.00 63.23  ? 270 TYR B CB  1 
ATOM   4282  C  CG  . TYR B 1 206 ? 29.864 76.804 59.350  1.00 82.38  ? 270 TYR B CG  1 
ATOM   4283  C  CD1 . TYR B 1 206 ? 31.076 76.570 58.713  1.00 110.51 ? 270 TYR B CD1 1 
ATOM   4284  C  CD2 . TYR B 1 206 ? 29.528 78.117 59.661  1.00 84.71  ? 270 TYR B CD2 1 
ATOM   4285  C  CE1 . TYR B 1 206 ? 31.939 77.614 58.393  1.00 117.35 ? 270 TYR B CE1 1 
ATOM   4286  C  CE2 . TYR B 1 206 ? 30.382 79.168 59.340  1.00 91.87  ? 270 TYR B CE2 1 
ATOM   4287  C  CZ  . TYR B 1 206 ? 31.587 78.906 58.702  1.00 105.02 ? 270 TYR B CZ  1 
ATOM   4288  O  OH  . TYR B 1 206 ? 32.456 79.921 58.372  1.00 101.17 ? 270 TYR B OH  1 
ATOM   4289  N  N   . THR B 1 207 ? 27.784 76.916 56.883  1.00 58.93  ? 271 THR B N   1 
ATOM   4290  C  CA  . THR B 1 207 ? 28.195 77.249 55.532  1.00 73.69  ? 271 THR B CA  1 
ATOM   4291  C  C   . THR B 1 207 ? 28.290 78.747 55.325  1.00 72.38  ? 271 THR B C   1 
ATOM   4292  O  O   . THR B 1 207 ? 27.542 79.507 55.937  1.00 66.20  ? 271 THR B O   1 
ATOM   4293  C  CB  . THR B 1 207 ? 27.264 76.630 54.464  1.00 77.95  ? 271 THR B CB  1 
ATOM   4294  O  OG1 . THR B 1 207 ? 27.817 76.864 53.158  1.00 115.72 ? 271 THR B OG1 1 
ATOM   4295  C  CG2 . THR B 1 207 ? 25.849 77.214 54.551  1.00 64.43  ? 271 THR B CG2 1 
ATOM   4296  N  N   . SER B 1 208 ? 29.228 79.161 54.471  1.00 92.32  ? 272 SER B N   1 
ATOM   4297  C  CA  . SER B 1 208 ? 29.295 80.539 53.998  1.00 103.73 ? 272 SER B CA  1 
ATOM   4298  C  C   . SER B 1 208 ? 29.287 81.510 55.185  1.00 96.21  ? 272 SER B C   1 
ATOM   4299  O  O   . SER B 1 208 ? 28.519 82.481 55.229  1.00 101.59 ? 272 SER B O   1 
ATOM   4300  C  CB  . SER B 1 208 ? 28.126 80.811 53.032  1.00 110.08 ? 272 SER B CB  1 
ATOM   4301  O  OG  . SER B 1 208 ? 28.286 82.038 52.345  1.00 139.20 ? 272 SER B OG  1 
ATOM   4302  N  N   . GLY B 1 209 ? 30.126 81.211 56.168  1.00 77.79  ? 273 GLY B N   1 
ATOM   4303  C  CA  . GLY B 1 209 ? 30.268 82.070 57.334  1.00 82.85  ? 273 GLY B CA  1 
ATOM   4304  C  C   . GLY B 1 209 ? 29.069 82.214 58.249  1.00 80.07  ? 273 GLY B C   1 
ATOM   4305  O  O   . GLY B 1 209 ? 29.048 83.115 59.108  1.00 89.51  ? 273 GLY B O   1 
ATOM   4306  N  N   . LYS B 1 210 ? 28.073 81.345 58.085  1.00 65.56  ? 274 LYS B N   1 
ATOM   4307  C  CA  . LYS B 1 210 ? 26.911 81.376 58.971  1.00 63.39  ? 274 LYS B CA  1 
ATOM   4308  C  C   . LYS B 1 210 ? 26.523 80.006 59.456  1.00 61.56  ? 274 LYS B C   1 
ATOM   4309  O  O   . LYS B 1 210 ? 26.669 79.030 58.733  1.00 75.42  ? 274 LYS B O   1 
ATOM   4310  C  CB  . LYS B 1 210 ? 25.738 82.074 58.285  1.00 62.53  ? 274 LYS B CB  1 
ATOM   4311  C  CG  . LYS B 1 210 ? 25.937 83.600 58.264  1.00 84.14  ? 274 LYS B CG  1 
ATOM   4312  C  CD  . LYS B 1 210 ? 24.874 84.384 57.517  1.00 96.15  ? 274 LYS B CD  1 
ATOM   4313  C  CE  . LYS B 1 210 ? 25.078 84.299 56.006  1.00 114.18 ? 274 LYS B CE  1 
ATOM   4314  N  NZ  . LYS B 1 210 ? 24.727 85.585 55.351  1.00 135.69 ? 274 LYS B NZ  1 
ATOM   4315  N  N   . VAL B 1 211 ? 26.059 79.917 60.693  1.00 57.55  ? 275 VAL B N   1 
ATOM   4316  C  CA  . VAL B 1 211 ? 25.410 78.680 61.151  1.00 59.69  ? 275 VAL B CA  1 
ATOM   4317  C  C   . VAL B 1 211 ? 23.894 78.705 60.931  1.00 57.00  ? 275 VAL B C   1 
ATOM   4318  O  O   . VAL B 1 211 ? 23.233 79.711 61.170  1.00 69.38  ? 275 VAL B O   1 
ATOM   4319  C  CB  . VAL B 1 211 ? 25.734 78.378 62.601  1.00 64.53  ? 275 VAL B CB  1 
ATOM   4320  C  CG1 . VAL B 1 211 ? 24.952 77.162 63.103  1.00 52.89  ? 275 VAL B CG1 1 
ATOM   4321  C  CG2 . VAL B 1 211 ? 27.239 78.148 62.735  1.00 64.88  ? 275 VAL B CG2 1 
ATOM   4322  N  N   . LYS B 1 212 ? 23.359 77.587 60.462  1.00 56.65  ? 276 LYS B N   1 
ATOM   4323  C  CA  . LYS B 1 212 ? 21.986 77.531 60.019  1.00 56.68  ? 276 LYS B CA  1 
ATOM   4324  C  C   . LYS B 1 212 ? 21.302 76.408 60.742  1.00 50.48  ? 276 LYS B C   1 
ATOM   4325  O  O   . LYS B 1 212 ? 21.719 75.276 60.644  1.00 68.14  ? 276 LYS B O   1 
ATOM   4326  C  CB  . LYS B 1 212 ? 21.952 77.358 58.502  1.00 61.35  ? 276 LYS B CB  1 
ATOM   4327  C  CG  . LYS B 1 212 ? 22.708 78.482 57.777  1.00 68.71  ? 276 LYS B CG  1 
ATOM   4328  C  CD  . LYS B 1 212 ? 22.572 78.414 56.286  1.00 78.93  ? 276 LYS B CD  1 
ATOM   4329  C  CE  . LYS B 1 212 ? 23.302 79.568 55.628  1.00 81.21  ? 276 LYS B CE  1 
ATOM   4330  N  NZ  . LYS B 1 212 ? 23.056 79.559 54.163  1.00 108.80 ? 276 LYS B NZ  1 
ATOM   4331  N  N   . CYS B 1 213 ? 20.272 76.737 61.503  1.00 54.08  ? 277 CYS B N   1 
ATOM   4332  C  CA  . CYS B 1 213 ? 19.588 75.769 62.362  1.00 61.72  ? 277 CYS B CA  1 
ATOM   4333  C  C   . CYS B 1 213 ? 18.091 75.631 62.074  1.00 62.22  ? 277 CYS B C   1 
ATOM   4334  O  O   . CYS B 1 213 ? 17.357 76.615 61.898  1.00 56.11  ? 277 CYS B O   1 
ATOM   4335  C  CB  . CYS B 1 213 ? 19.758 76.147 63.820  1.00 67.56  ? 277 CYS B CB  1 
ATOM   4336  S  SG  . CYS B 1 213 ? 21.434 76.140 64.326  1.00 130.00 ? 277 CYS B SG  1 
ATOM   4337  N  N   . THR B 1 214 ? 17.645 74.389 62.049  1.00 49.77  ? 278 THR B N   1 
ATOM   4338  C  CA  . THR B 1 214 ? 16.245 74.095 61.852  1.00 46.23  ? 278 THR B CA  1 
ATOM   4339  C  C   . THR B 1 214 ? 15.574 73.668 63.136  1.00 46.15  ? 278 THR B C   1 
ATOM   4340  O  O   . THR B 1 214 ? 15.739 72.540 63.587  1.00 47.86  ? 278 THR B O   1 
ATOM   4341  C  CB  . THR B 1 214 ? 16.104 72.946 60.896  1.00 49.39  ? 278 THR B CB  1 
ATOM   4342  O  OG1 . THR B 1 214 ? 16.820 73.252 59.686  1.00 70.31  ? 278 THR B OG1 1 
ATOM   4343  C  CG2 . THR B 1 214 ? 14.633 72.675 60.611  1.00 40.44  ? 278 THR B CG2 1 
ATOM   4344  N  N   . GLY B 1 215 ? 14.781 74.546 63.720  1.00 47.66  ? 279 GLY B N   1 
ATOM   4345  C  CA  . GLY B 1 215 ? 14.105 74.168 64.944  1.00 50.16  ? 279 GLY B CA  1 
ATOM   4346  C  C   . GLY B 1 215 ? 12.783 73.438 64.735  1.00 50.01  ? 279 GLY B C   1 
ATOM   4347  O  O   . GLY B 1 215 ? 12.413 73.114 63.628  1.00 55.63  ? 279 GLY B O   1 
ATOM   4348  N  N   . THR B 1 216 ? 12.073 73.205 65.831  1.00 51.55  ? 280 THR B N   1 
ATOM   4349  C  CA  . THR B 1 216 ? 10.817 72.518 65.857  1.00 44.27  ? 280 THR B CA  1 
ATOM   4350  C  C   . THR B 1 216 ? 9.866  73.308 66.762  1.00 56.85  ? 280 THR B C   1 
ATOM   4351  O  O   . THR B 1 216 ? 10.157 73.572 67.939  1.00 54.43  ? 280 THR B O   1 
ATOM   4352  C  CB  . THR B 1 216 ? 11.061 71.106 66.361  1.00 54.76  ? 280 THR B CB  1 
ATOM   4353  O  OG1 . THR B 1 216 ? 11.513 70.294 65.257  1.00 60.08  ? 280 THR B OG1 1 
ATOM   4354  C  CG2 . THR B 1 216 ? 9.808  70.510 66.999  1.00 56.10  ? 280 THR B CG2 1 
ATOM   4355  N  N   . ASN B 1 217 ? 8.738  73.728 66.203  1.00 68.01  ? 281 ASN B N   1 
ATOM   4356  C  CA  . ASN B 1 217 ? 7.787  74.548 66.963  1.00 56.09  ? 281 ASN B CA  1 
ATOM   4357  C  C   . ASN B 1 217 ? 6.719  73.657 67.540  1.00 58.68  ? 281 ASN B C   1 
ATOM   4358  O  O   . ASN B 1 217 ? 5.836  73.136 66.798  1.00 62.17  ? 281 ASN B O   1 
ATOM   4359  C  CB  . ASN B 1 217 ? 7.186  75.628 66.074  1.00 44.31  ? 281 ASN B CB  1 
ATOM   4360  C  CG  . ASN B 1 217 ? 6.307  76.577 66.817  1.00 53.69  ? 281 ASN B CG  1 
ATOM   4361  O  OD1 . ASN B 1 217 ? 5.582  76.188 67.731  1.00 53.55  ? 281 ASN B OD1 1 
ATOM   4362  N  ND2 . ASN B 1 217 ? 6.347  77.855 66.414  1.00 63.00  ? 281 ASN B ND2 1 
ATOM   4363  N  N   . LEU B 1 218 ? 6.814  73.458 68.856  1.00 42.70  ? 282 LEU B N   1 
ATOM   4364  C  CA  . LEU B 1 218 ? 5.865  72.557 69.528  1.00 51.93  ? 282 LEU B CA  1 
ATOM   4365  C  C   . LEU B 1 218 ? 4.590  73.227 69.975  1.00 52.29  ? 282 LEU B C   1 
ATOM   4366  O  O   . LEU B 1 218 ? 3.758  72.581 70.575  1.00 48.88  ? 282 LEU B O   1 
ATOM   4367  C  CB  . LEU B 1 218 ? 6.479  71.874 70.730  1.00 59.09  ? 282 LEU B CB  1 
ATOM   4368  C  CG  . LEU B 1 218 ? 7.521  70.792 70.518  1.00 57.97  ? 282 LEU B CG  1 
ATOM   4369  C  CD1 . LEU B 1 218 ? 8.871  71.427 70.632  1.00 63.69  ? 282 LEU B CD1 1 
ATOM   4370  C  CD2 . LEU B 1 218 ? 7.367  69.826 71.633  1.00 64.86  ? 282 LEU B CD2 1 
ATOM   4371  N  N   . TRP B 1 219 ? 4.437  74.507 69.641  1.00 65.16  ? 283 TRP B N   1 
ATOM   4372  C  CA  . TRP B 1 219 ? 3.327  75.317 70.088  1.00 50.70  ? 283 TRP B CA  1 
ATOM   4373  C  C   . TRP B 1 219 ? 2.351  75.630 69.005  1.00 53.60  ? 283 TRP B C   1 
ATOM   4374  O  O   . TRP B 1 219 ? 1.283  75.044 68.966  1.00 53.46  ? 283 TRP B O   1 
ATOM   4375  C  CB  . TRP B 1 219 ? 3.893  76.596 70.658  1.00 63.31  ? 283 TRP B CB  1 
ATOM   4376  C  CG  . TRP B 1 219 ? 2.881  77.602 71.144  1.00 69.03  ? 283 TRP B CG  1 
ATOM   4377  C  CD1 . TRP B 1 219 ? 1.551  77.390 71.482  1.00 65.91  ? 283 TRP B CD1 1 
ATOM   4378  C  CD2 . TRP B 1 219 ? 3.122  79.015 71.416  1.00 66.54  ? 283 TRP B CD2 1 
ATOM   4379  N  NE1 . TRP B 1 219 ? 0.973  78.550 71.905  1.00 72.87  ? 283 TRP B NE1 1 
ATOM   4380  C  CE2 . TRP B 1 219 ? 1.864  79.560 71.889  1.00 72.58  ? 283 TRP B CE2 1 
ATOM   4381  C  CE3 . TRP B 1 219 ? 4.219  79.851 71.310  1.00 67.84  ? 283 TRP B CE3 1 
ATOM   4382  C  CZ2 . TRP B 1 219 ? 1.730  80.885 72.229  1.00 77.72  ? 283 TRP B CZ2 1 
ATOM   4383  C  CZ3 . TRP B 1 219 ? 4.074  81.185 71.651  1.00 54.84  ? 283 TRP B CZ3 1 
ATOM   4384  C  CH2 . TRP B 1 219 ? 2.862  81.687 72.104  1.00 71.50  ? 283 TRP B CH2 1 
ATOM   4385  N  N   . ASN B 1 220 ? 2.713  76.550 68.111  1.00 61.52  ? 284 ASN B N   1 
ATOM   4386  C  CA  . ASN B 1 220 ? 1.755  77.173 67.207  1.00 56.42  ? 284 ASN B CA  1 
ATOM   4387  C  C   . ASN B 1 220 ? 2.089  76.992 65.737  1.00 62.77  ? 284 ASN B C   1 
ATOM   4388  O  O   . ASN B 1 220 ? 1.585  77.738 64.894  1.00 85.92  ? 284 ASN B O   1 
ATOM   4389  C  CB  . ASN B 1 220 ? 1.641  78.669 67.542  1.00 59.70  ? 284 ASN B CB  1 
ATOM   4390  C  CG  . ASN B 1 220 ? 2.958  79.346 67.573  1.00 61.58  ? 284 ASN B CG  1 
ATOM   4391  O  OD1 . ASN B 1 220 ? 3.960  78.820 67.084  1.00 81.96  ? 284 ASN B OD1 1 
ATOM   4392  N  ND2 . ASN B 1 220 ? 2.985  80.525 68.147  1.00 84.78  ? 284 ASN B ND2 1 
ATOM   4393  N  N   . ASP B 1 221 ? 2.916  75.996 65.420  1.00 61.84  ? 285 ASP B N   1 
ATOM   4394  C  CA  . ASP B 1 221 ? 3.417  75.873 64.057  1.00 52.60  ? 285 ASP B CA  1 
ATOM   4395  C  C   . ASP B 1 221 ? 3.653  74.447 63.554  1.00 44.55  ? 285 ASP B C   1 
ATOM   4396  O  O   . ASP B 1 221 ? 4.274  73.623 64.242  1.00 52.13  ? 285 ASP B O   1 
ATOM   4397  C  CB  . ASP B 1 221 ? 4.673  76.741 63.931  1.00 54.42  ? 285 ASP B CB  1 
ATOM   4398  C  CG  . ASP B 1 221 ? 5.099  76.995 62.484  1.00 83.05  ? 285 ASP B CG  1 
ATOM   4399  O  OD1 . ASP B 1 221 ? 4.406  76.538 61.523  1.00 67.07  ? 285 ASP B OD1 1 
ATOM   4400  O  OD2 . ASP B 1 221 ? 6.151  77.678 62.324  1.00 107.36 ? 285 ASP B OD2 1 
ATOM   4401  N  N   . ALA B 1 222 ? 3.162  74.190 62.338  1.00 43.99  ? 286 ALA B N   1 
ATOM   4402  C  CA  . ALA B 1 222 ? 3.387  72.926 61.599  1.00 51.86  ? 286 ALA B CA  1 
ATOM   4403  C  C   . ALA B 1 222 ? 4.532  72.985 60.568  1.00 58.67  ? 286 ALA B C   1 
ATOM   4404  O  O   . ALA B 1 222 ? 4.849  71.997 59.918  1.00 85.13  ? 286 ALA B O   1 
ATOM   4405  C  CB  . ALA B 1 222 ? 2.100  72.482 60.915  1.00 47.75  ? 286 ALA B CB  1 
ATOM   4406  N  N   . LYS B 1 223 ? 5.115  74.159 60.386  1.00 56.00  ? 287 LYS B N   1 
ATOM   4407  C  CA  . LYS B 1 223 ? 6.342  74.310 59.644  1.00 39.88  ? 287 LYS B CA  1 
ATOM   4408  C  C   . LYS B 1 223 ? 7.514  74.342 60.645  1.00 55.20  ? 287 LYS B C   1 
ATOM   4409  O  O   . LYS B 1 223 ? 7.351  74.174 61.865  1.00 62.16  ? 287 LYS B O   1 
ATOM   4410  C  CB  . LYS B 1 223 ? 6.298  75.628 58.919  1.00 39.49  ? 287 LYS B CB  1 
ATOM   4411  C  CG  . LYS B 1 223 ? 5.133  75.844 57.978  1.00 48.08  ? 287 LYS B CG  1 
ATOM   4412  C  CD  . LYS B 1 223 ? 5.444  77.113 57.142  1.00 51.29  ? 287 LYS B CD  1 
ATOM   4413  C  CE  . LYS B 1 223 ? 4.316  77.538 56.245  1.00 50.69  ? 287 LYS B CE  1 
ATOM   4414  N  NZ  . LYS B 1 223 ? 4.761  78.562 55.289  1.00 58.24  ? 287 LYS B NZ  1 
ATOM   4415  N  N   . ARG B 1 224 ? 8.720  74.550 60.161  1.00 52.90  ? 288 ARG B N   1 
ATOM   4416  C  CA  . ARG B 1 224 ? 9.819  74.543 61.097  1.00 41.96  ? 288 ARG B CA  1 
ATOM   4417  C  C   . ARG B 1 224 ? 10.502 75.843 61.041  1.00 42.87  ? 288 ARG B C   1 
ATOM   4418  O  O   . ARG B 1 224 ? 10.919 76.271 59.974  1.00 83.74  ? 288 ARG B O   1 
ATOM   4419  C  CB  . ARG B 1 224 ? 10.833 73.456 60.754  1.00 47.64  ? 288 ARG B CB  1 
ATOM   4420  C  CG  . ARG B 1 224 ? 10.225 72.128 60.451  1.00 49.12  ? 288 ARG B CG  1 
ATOM   4421  C  CD  . ARG B 1 224 ? 11.261 71.065 60.555  1.00 55.12  ? 288 ARG B CD  1 
ATOM   4422  N  NE  . ARG B 1 224 ? 11.101 70.362 61.815  1.00 53.26  ? 288 ARG B NE  1 
ATOM   4423  C  CZ  . ARG B 1 224 ? 10.625 69.127 61.904  1.00 59.20  ? 288 ARG B CZ  1 
ATOM   4424  N  NH1 . ARG B 1 224 ? 10.295 68.449 60.791  1.00 75.53  ? 288 ARG B NH1 1 
ATOM   4425  N  NH2 . ARG B 1 224 ? 10.506 68.570 63.102  1.00 42.25  ? 288 ARG B NH2 1 
ATOM   4426  N  N   . PRO B 1 225 ? 10.662 76.483 62.186  1.00 41.10  ? 289 PRO B N   1 
ATOM   4427  C  CA  . PRO B 1 225 ? 11.388 77.742 62.237  1.00 46.01  ? 289 PRO B CA  1 
ATOM   4428  C  C   . PRO B 1 225 ? 12.804 77.526 61.767  1.00 50.62  ? 289 PRO B C   1 
ATOM   4429  O  O   . PRO B 1 225 ? 13.338 76.428 61.881  1.00 59.55  ? 289 PRO B O   1 
ATOM   4430  C  CB  . PRO B 1 225 ? 11.414 78.058 63.721  1.00 47.63  ? 289 PRO B CB  1 
ATOM   4431  C  CG  . PRO B 1 225 ? 10.250 77.309 64.270  1.00 57.63  ? 289 PRO B CG  1 
ATOM   4432  C  CD  . PRO B 1 225 ? 10.234 76.048 63.514  1.00 43.43  ? 289 PRO B CD  1 
ATOM   4433  N  N   . PHE B 1 226 ? 13.409 78.570 61.239  1.00 51.53  ? 290 PHE B N   1 
ATOM   4434  C  CA  . PHE B 1 226 ? 14.757 78.463 60.766  1.00 52.88  ? 290 PHE B CA  1 
ATOM   4435  C  C   . PHE B 1 226 ? 15.563 79.634 61.287  1.00 58.56  ? 290 PHE B C   1 
ATOM   4436  O  O   . PHE B 1 226 ? 15.036 80.730 61.429  1.00 67.12  ? 290 PHE B O   1 
ATOM   4437  C  CB  . PHE B 1 226 ? 14.742 78.446 59.271  1.00 46.22  ? 290 PHE B CB  1 
ATOM   4438  C  CG  . PHE B 1 226 ? 16.010 77.988 58.663  1.00 54.61  ? 290 PHE B CG  1 
ATOM   4439  C  CD1 . PHE B 1 226 ? 16.189 76.664 58.347  1.00 47.27  ? 290 PHE B CD1 1 
ATOM   4440  C  CD2 . PHE B 1 226 ? 17.022 78.898 58.358  1.00 63.87  ? 290 PHE B CD2 1 
ATOM   4441  C  CE1 . PHE B 1 226 ? 17.353 76.244 57.741  1.00 54.25  ? 290 PHE B CE1 1 
ATOM   4442  C  CE2 . PHE B 1 226 ? 18.203 78.478 57.764  1.00 64.37  ? 290 PHE B CE2 1 
ATOM   4443  C  CZ  . PHE B 1 226 ? 18.366 77.152 57.447  1.00 52.97  ? 290 PHE B CZ  1 
ATOM   4444  N  N   . LEU B 1 227 ? 16.837 79.373 61.581  1.00 72.90  ? 291 LEU B N   1 
ATOM   4445  C  CA  . LEU B 1 227 ? 17.714 80.317 62.263  1.00 57.72  ? 291 LEU B CA  1 
ATOM   4446  C  C   . LEU B 1 227 ? 19.082 80.444 61.574  1.00 55.10  ? 291 LEU B C   1 
ATOM   4447  O  O   . LEU B 1 227 ? 19.689 79.455 61.185  1.00 50.06  ? 291 LEU B O   1 
ATOM   4448  C  CB  . LEU B 1 227 ? 17.893 79.881 63.702  1.00 52.21  ? 291 LEU B CB  1 
ATOM   4449  C  CG  . LEU B 1 227 ? 18.777 80.826 64.488  1.00 66.07  ? 291 LEU B CG  1 
ATOM   4450  C  CD1 . LEU B 1 227 ? 18.118 82.221 64.532  1.00 60.63  ? 291 LEU B CD1 1 
ATOM   4451  C  CD2 . LEU B 1 227 ? 19.100 80.264 65.874  1.00 55.15  ? 291 LEU B CD2 1 
ATOM   4452  N  N   . GLU B 1 228 ? 19.530 81.681 61.398  1.00 58.99  ? 292 GLU B N   1 
ATOM   4453  C  CA  . GLU B 1 228 ? 20.804 81.983 60.796  1.00 54.97  ? 292 GLU B CA  1 
ATOM   4454  C  C   . GLU B 1 228 ? 21.474 82.839 61.824  1.00 55.77  ? 292 GLU B C   1 
ATOM   4455  O  O   . GLU B 1 228 ? 20.834 83.760 62.346  1.00 65.92  ? 292 GLU B O   1 
ATOM   4456  C  CB  . GLU B 1 228 ? 20.601 82.833 59.543  1.00 65.11  ? 292 GLU B CB  1 
ATOM   4457  C  CG  . GLU B 1 228 ? 21.505 82.434 58.379  1.00 129.09 ? 292 GLU B CG  1 
ATOM   4458  C  CD  . GLU B 1 228 ? 21.409 83.378 57.184  1.00 170.88 ? 292 GLU B CD  1 
ATOM   4459  O  OE1 . GLU B 1 228 ? 21.147 82.904 56.051  1.00 162.67 ? 292 GLU B OE1 1 
ATOM   4460  O  OE2 . GLU B 1 228 ? 21.601 84.599 57.379  1.00 205.59 ? 292 GLU B OE2 1 
ATOM   4461  N  N   . PHE B 1 229 ? 22.734 82.533 62.145  1.00 54.96  ? 293 PHE B N   1 
ATOM   4462  C  CA  . PHE B 1 229 ? 23.591 83.433 62.926  1.00 59.77  ? 293 PHE B CA  1 
ATOM   4463  C  C   . PHE B 1 229 ? 25.039 83.242 62.599  1.00 64.30  ? 293 PHE B C   1 
ATOM   4464  O  O   . PHE B 1 229 ? 25.442 82.193 62.092  1.00 64.28  ? 293 PHE B O   1 
ATOM   4465  C  CB  . PHE B 1 229 ? 23.393 83.237 64.426  1.00 64.78  ? 293 PHE B CB  1 
ATOM   4466  C  CG  . PHE B 1 229 ? 23.769 81.866 64.930  1.00 59.12  ? 293 PHE B CG  1 
ATOM   4467  C  CD1 . PHE B 1 229 ? 25.084 81.592 65.300  1.00 66.30  ? 293 PHE B CD1 1 
ATOM   4468  C  CD2 . PHE B 1 229 ? 22.811 80.878 65.103  1.00 52.62  ? 293 PHE B CD2 1 
ATOM   4469  C  CE1 . PHE B 1 229 ? 25.462 80.333 65.806  1.00 70.13  ? 293 PHE B CE1 1 
ATOM   4470  C  CE2 . PHE B 1 229 ? 23.182 79.611 65.608  1.00 71.42  ? 293 PHE B CE2 1 
ATOM   4471  C  CZ  . PHE B 1 229 ? 24.515 79.334 65.949  1.00 65.95  ? 293 PHE B CZ  1 
ATOM   4472  N  N   . ASP B 1 230 ? 25.843 84.238 62.932  1.00 72.73  ? 294 ASP B N   1 
ATOM   4473  C  CA  . ASP B 1 230 ? 27.265 84.162 62.605  1.00 89.76  ? 294 ASP B CA  1 
ATOM   4474  C  C   . ASP B 1 230 ? 28.094 84.287 63.865  1.00 80.87  ? 294 ASP B C   1 
ATOM   4475  O  O   . ASP B 1 230 ? 27.519 84.319 64.948  1.00 60.66  ? 294 ASP B O   1 
ATOM   4476  C  CB  . ASP B 1 230 ? 27.639 85.256 61.611  1.00 107.41 ? 294 ASP B CB  1 
ATOM   4477  C  CG  . ASP B 1 230 ? 27.389 86.639 62.159  1.00 104.23 ? 294 ASP B CG  1 
ATOM   4478  O  OD1 . ASP B 1 230 ? 27.144 86.771 63.379  1.00 108.02 ? 294 ASP B OD1 1 
ATOM   4479  O  OD2 . ASP B 1 230 ? 27.443 87.595 61.364  1.00 109.42 ? 294 ASP B OD2 1 
ATOM   4480  N  N   . GLN B 1 231 ? 29.425 84.380 63.721  1.00 91.30  ? 295 GLN B N   1 
ATOM   4481  C  CA  . GLN B 1 231 ? 30.309 84.404 64.880  1.00 79.34  ? 295 GLN B CA  1 
ATOM   4482  C  C   . GLN B 1 231 ? 30.034 85.556 65.830  1.00 81.69  ? 295 GLN B C   1 
ATOM   4483  O  O   . GLN B 1 231 ? 30.192 85.407 67.033  1.00 86.52  ? 295 GLN B O   1 
ATOM   4484  C  CB  . GLN B 1 231 ? 31.791 84.279 64.502  1.00 97.58  ? 295 GLN B CB  1 
ATOM   4485  C  CG  . GLN B 1 231 ? 32.392 85.301 63.549  1.00 102.88 ? 295 GLN B CG  1 
ATOM   4486  C  CD  . GLN B 1 231 ? 33.855 84.979 63.234  1.00 122.86 ? 295 GLN B CD  1 
ATOM   4487  O  OE1 . GLN B 1 231 ? 34.297 83.830 63.346  1.00 123.35 ? 295 GLN B OE1 1 
ATOM   4488  N  NE2 . GLN B 1 231 ? 34.611 85.996 62.845  1.00 134.62 ? 295 GLN B NE2 1 
ATOM   4489  N  N   . SER B 1 232 ? 29.561 86.681 65.304  1.00 86.81  ? 296 SER B N   1 
ATOM   4490  C  CA  . SER B 1 232 ? 29.304 87.857 66.138  1.00 89.08  ? 296 SER B CA  1 
ATOM   4491  C  C   . SER B 1 232 ? 27.929 87.838 66.818  1.00 74.82  ? 296 SER B C   1 
ATOM   4492  O  O   . SER B 1 232 ? 27.508 88.830 67.414  1.00 85.82  ? 296 SER B O   1 
ATOM   4493  C  CB  . SER B 1 232 ? 29.480 89.139 65.310  1.00 121.76 ? 296 SER B CB  1 
ATOM   4494  O  OG  . SER B 1 232 ? 28.525 89.218 64.257  1.00 131.57 ? 296 SER B OG  1 
ATOM   4495  N  N   . PHE B 1 233 ? 27.235 86.711 66.723  1.00 66.08  ? 297 PHE B N   1 
ATOM   4496  C  CA  . PHE B 1 233 ? 25.840 86.562 67.196  1.00 64.59  ? 297 PHE B CA  1 
ATOM   4497  C  C   . PHE B 1 233 ? 24.765 87.434 66.542  1.00 67.03  ? 297 PHE B C   1 
ATOM   4498  O  O   . PHE B 1 233 ? 23.670 87.566 67.098  1.00 68.92  ? 297 PHE B O   1 
ATOM   4499  C  CB  . PHE B 1 233 ? 25.716 86.711 68.711  1.00 70.15  ? 297 PHE B CB  1 
ATOM   4500  C  CG  . PHE B 1 233 ? 26.269 85.570 69.469  1.00 89.36  ? 297 PHE B CG  1 
ATOM   4501  C  CD1 . PHE B 1 233 ? 26.134 84.277 68.991  1.00 84.16  ? 297 PHE B CD1 1 
ATOM   4502  C  CD2 . PHE B 1 233 ? 26.929 85.780 70.675  1.00 103.33 ? 297 PHE B CD2 1 
ATOM   4503  C  CE1 . PHE B 1 233 ? 26.653 83.200 69.689  1.00 94.33  ? 297 PHE B CE1 1 
ATOM   4504  C  CE2 . PHE B 1 233 ? 27.452 84.710 71.385  1.00 115.06 ? 297 PHE B CE2 1 
ATOM   4505  C  CZ  . PHE B 1 233 ? 27.306 83.412 70.888  1.00 114.86 ? 297 PHE B CZ  1 
ATOM   4506  N  N   . THR B 1 234 ? 25.051 88.045 65.396  1.00 70.65  ? 298 THR B N   1 
ATOM   4507  C  CA  . THR B 1 234 ? 23.980 88.693 64.645  1.00 77.52  ? 298 THR B CA  1 
ATOM   4508  C  C   . THR B 1 234 ? 23.185 87.540 63.999  1.00 80.14  ? 298 THR B C   1 
ATOM   4509  O  O   . THR B 1 234 ? 23.751 86.583 63.436  1.00 72.49  ? 298 THR B O   1 
ATOM   4510  C  CB  . THR B 1 234 ? 24.479 89.821 63.672  1.00 83.30  ? 298 THR B CB  1 
ATOM   4511  O  OG1 . THR B 1 234 ? 25.521 89.321 62.839  1.00 111.89 ? 298 THR B OG1 1 
ATOM   4512  C  CG2 . THR B 1 234 ? 25.051 91.020 64.447  1.00 96.24  ? 298 THR B CG2 1 
ATOM   4513  N  N   . TYR B 1 235 ? 21.870 87.585 64.176  1.00 85.15  ? 299 TYR B N   1 
ATOM   4514  C  CA  . TYR B 1 235 ? 21.029 86.437 63.845  1.00 72.02  ? 299 TYR B CA  1 
ATOM   4515  C  C   . TYR B 1 235 ? 19.705 86.905 63.306  1.00 68.25  ? 299 TYR B C   1 
ATOM   4516  O  O   . TYR B 1 235 ? 19.199 87.956 63.718  1.00 89.91  ? 299 TYR B O   1 
ATOM   4517  C  CB  . TYR B 1 235 ? 20.775 85.593 65.100  1.00 64.25  ? 299 TYR B CB  1 
ATOM   4518  C  CG  . TYR B 1 235 ? 19.742 86.198 66.039  1.00 66.74  ? 299 TYR B CG  1 
ATOM   4519  C  CD1 . TYR B 1 235 ? 20.095 87.129 67.013  1.00 68.76  ? 299 TYR B CD1 1 
ATOM   4520  C  CD2 . TYR B 1 235 ? 18.401 85.854 65.930  1.00 67.78  ? 299 TYR B CD2 1 
ATOM   4521  C  CE1 . TYR B 1 235 ? 19.124 87.682 67.862  1.00 76.01  ? 299 TYR B CE1 1 
ATOM   4522  C  CE2 . TYR B 1 235 ? 17.439 86.401 66.761  1.00 59.08  ? 299 TYR B CE2 1 
ATOM   4523  C  CZ  . TYR B 1 235 ? 17.794 87.294 67.719  1.00 64.07  ? 299 TYR B CZ  1 
ATOM   4524  O  OH  . TYR B 1 235 ? 16.788 87.798 68.503  1.00 63.70  ? 299 TYR B OH  1 
ATOM   4525  N  N   . THR B 1 236 ? 19.137 86.128 62.394  1.00 63.73  ? 300 THR B N   1 
ATOM   4526  C  CA  . THR B 1 236 ? 17.736 86.341 61.969  1.00 84.29  ? 300 THR B CA  1 
ATOM   4527  C  C   . THR B 1 236 ? 16.961 85.020 61.943  1.00 66.24  ? 300 THR B C   1 
ATOM   4528  O  O   . THR B 1 236 ? 17.499 83.955 61.629  1.00 67.13  ? 300 THR B O   1 
ATOM   4529  C  CB  . THR B 1 236 ? 17.576 87.057 60.576  1.00 92.31  ? 300 THR B CB  1 
ATOM   4530  O  OG1 . THR B 1 236 ? 17.826 86.125 59.520  1.00 106.30 ? 300 THR B OG1 1 
ATOM   4531  C  CG2 . THR B 1 236 ? 18.506 88.299 60.424  1.00 102.01 ? 300 THR B CG2 1 
ATOM   4532  N  N   . PHE B 1 237 ? 15.694 85.091 62.301  1.00 61.74  ? 301 PHE B N   1 
ATOM   4533  C  CA  . PHE B 1 237 ? 14.810 83.959 62.129  1.00 58.09  ? 301 PHE B CA  1 
ATOM   4534  C  C   . PHE B 1 237 ? 14.109 84.095 60.777  1.00 66.93  ? 301 PHE B C   1 
ATOM   4535  O  O   . PHE B 1 237 ? 13.646 85.173 60.392  1.00 92.25  ? 301 PHE B O   1 
ATOM   4536  C  CB  . PHE B 1 237 ? 13.759 83.898 63.235  1.00 54.72  ? 301 PHE B CB  1 
ATOM   4537  C  CG  . PHE B 1 237 ? 14.248 83.321 64.535  1.00 59.56  ? 301 PHE B CG  1 
ATOM   4538  C  CD1 . PHE B 1 237 ? 14.665 84.157 65.568  1.00 60.83  ? 301 PHE B CD1 1 
ATOM   4539  C  CD2 . PHE B 1 237 ? 14.243 81.947 64.754  1.00 66.04  ? 301 PHE B CD2 1 
ATOM   4540  C  CE1 . PHE B 1 237 ? 15.093 83.624 66.796  1.00 64.19  ? 301 PHE B CE1 1 
ATOM   4541  C  CE2 . PHE B 1 237 ? 14.675 81.408 65.971  1.00 57.66  ? 301 PHE B CE2 1 
ATOM   4542  C  CZ  . PHE B 1 237 ? 15.095 82.249 66.991  1.00 61.95  ? 301 PHE B CZ  1 
ATOM   4543  N  N   . LYS B 1 238 ? 14.040 82.989 60.058  1.00 62.54  ? 302 LYS B N   1 
ATOM   4544  C  CA  . LYS B 1 238 ? 13.347 82.936 58.799  1.00 53.92  ? 302 LYS B CA  1 
ATOM   4545  C  C   . LYS B 1 238 ? 12.289 81.882 58.978  1.00 56.89  ? 302 LYS B C   1 
ATOM   4546  O  O   . LYS B 1 238 ? 12.452 80.988 59.795  1.00 67.56  ? 302 LYS B O   1 
ATOM   4547  C  CB  . LYS B 1 238 ? 14.305 82.552 57.674  1.00 43.55  ? 302 LYS B CB  1 
ATOM   4548  C  CG  . LYS B 1 238 ? 15.498 83.508 57.522  1.00 57.39  ? 302 LYS B CG  1 
ATOM   4549  C  CD  . LYS B 1 238 ? 16.368 83.143 56.325  1.00 70.90  ? 302 LYS B CD  1 
ATOM   4550  C  CE  . LYS B 1 238 ? 16.947 84.363 55.642  1.00 86.36  ? 302 LYS B CE  1 
ATOM   4551  N  NZ  . LYS B 1 238 ? 17.095 84.139 54.177  1.00 83.45  ? 302 LYS B NZ  1 
ATOM   4552  N  N   . GLU B 1 239 ? 11.189 82.018 58.249  1.00 62.47  ? 303 GLU B N   1 
ATOM   4553  C  CA  . GLU B 1 239 ? 10.163 80.995 58.190  1.00 55.17  ? 303 GLU B CA  1 
ATOM   4554  C  C   . GLU B 1 239 ? 10.038 80.569 56.744  1.00 55.11  ? 303 GLU B C   1 
ATOM   4555  O  O   . GLU B 1 239 ? 9.863  81.404 55.858  1.00 71.26  ? 303 GLU B O   1 
ATOM   4556  C  CB  . GLU B 1 239 ? 8.831  81.555 58.691  1.00 68.19  ? 303 GLU B CB  1 
ATOM   4557  C  CG  . GLU B 1 239 ? 7.612  80.654 58.492  1.00 73.63  ? 303 GLU B CG  1 
ATOM   4558  C  CD  . GLU B 1 239 ? 7.339  79.685 59.661  1.00 89.94  ? 303 GLU B CD  1 
ATOM   4559  O  OE1 . GLU B 1 239 ? 7.984  79.773 60.735  1.00 102.23 ? 303 GLU B OE1 1 
ATOM   4560  O  OE2 . GLU B 1 239 ? 6.450  78.823 59.498  1.00 110.14 ? 303 GLU B OE2 1 
ATOM   4561  N  N   . PRO B 1 240 ? 10.117 79.262 56.494  1.00 57.95  ? 304 PRO B N   1 
ATOM   4562  C  CA  . PRO B 1 240 ? 10.047 78.725 55.138  1.00 57.07  ? 304 PRO B CA  1 
ATOM   4563  C  C   . PRO B 1 240 ? 8.683  78.943 54.508  1.00 51.56  ? 304 PRO B C   1 
ATOM   4564  O  O   . PRO B 1 240 ? 7.670  78.756 55.181  1.00 47.53  ? 304 PRO B O   1 
ATOM   4565  C  CB  . PRO B 1 240 ? 10.314 77.241 55.339  1.00 48.42  ? 304 PRO B CB  1 
ATOM   4566  C  CG  . PRO B 1 240 ? 9.876  76.963 56.714  1.00 45.55  ? 304 PRO B CG  1 
ATOM   4567  C  CD  . PRO B 1 240 ? 10.073 78.202 57.511  1.00 50.77  ? 304 PRO B CD  1 
ATOM   4568  N  N   . CYS B 1 241 ? 8.692  79.341 53.235  1.00 61.57  ? 305 CYS B N   1 
ATOM   4569  C  CA  . CYS B 1 241 ? 7.511  79.766 52.507  1.00 67.90  ? 305 CYS B CA  1 
ATOM   4570  C  C   . CYS B 1 241 ? 7.072  78.677 51.571  1.00 64.81  ? 305 CYS B C   1 
ATOM   4571  O  O   . CYS B 1 241 ? 6.961  78.916 50.377  1.00 94.80  ? 305 CYS B O   1 
ATOM   4572  C  CB  . CYS B 1 241 ? 7.838  81.025 51.688  1.00 74.46  ? 305 CYS B CB  1 
ATOM   4573  S  SG  . CYS B 1 241 ? 8.530  82.419 52.625  1.00 105.91 ? 305 CYS B SG  1 
ATOM   4574  N  N   . LEU B 1 242 ? 6.850  77.471 52.084  1.00 52.47  ? 306 LEU B N   1 
ATOM   4575  C  CA  . LEU B 1 242 ? 6.542  76.351 51.191  1.00 55.59  ? 306 LEU B CA  1 
ATOM   4576  C  C   . LEU B 1 242 ? 5.487  75.468 51.792  1.00 63.53  ? 306 LEU B C   1 
ATOM   4577  O  O   . LEU B 1 242 ? 5.542  75.187 52.999  1.00 62.47  ? 306 LEU B O   1 
ATOM   4578  C  CB  . LEU B 1 242 ? 7.795  75.520 50.889  1.00 52.44  ? 306 LEU B CB  1 
ATOM   4579  C  CG  . LEU B 1 242 ? 8.859  76.144 49.989  1.00 61.04  ? 306 LEU B CG  1 
ATOM   4580  C  CD1 . LEU B 1 242 ? 10.091 75.270 49.958  1.00 71.83  ? 306 LEU B CD1 1 
ATOM   4581  C  CD2 . LEU B 1 242 ? 8.354  76.400 48.568  1.00 80.36  ? 306 LEU B CD2 1 
ATOM   4582  N  N   . GLY B 1 243 ? 4.548  75.027 50.945  1.00 55.84  ? 307 GLY B N   1 
ATOM   4583  C  CA  . GLY B 1 243 ? 3.404  74.207 51.359  1.00 65.81  ? 307 GLY B CA  1 
ATOM   4584  C  C   . GLY B 1 243 ? 3.743  72.835 51.883  1.00 69.38  ? 307 GLY B C   1 
ATOM   4585  O  O   . GLY B 1 243 ? 2.848  72.097 52.310  1.00 111.59 ? 307 GLY B O   1 
ATOM   4586  N  N   . PHE B 1 244 ? 5.039  72.507 51.853  1.00 83.79  ? 308 PHE B N   1 
ATOM   4587  C  CA  . PHE B 1 244 ? 5.589  71.231 52.338  1.00 77.29  ? 308 PHE B CA  1 
ATOM   4588  C  C   . PHE B 1 244 ? 5.869  71.365 53.835  1.00 69.84  ? 308 PHE B C   1 
ATOM   4589  O  O   . PHE B 1 244 ? 6.787  72.094 54.272  1.00 90.70  ? 308 PHE B O   1 
ATOM   4590  C  CB  . PHE B 1 244 ? 6.849  70.876 51.545  1.00 81.89  ? 308 PHE B CB  1 
ATOM   4591  C  CG  . PHE B 1 244 ? 7.140  69.403 51.461  1.00 157.59 ? 308 PHE B CG  1 
ATOM   4592  C  CD1 . PHE B 1 244 ? 6.396  68.570 50.629  1.00 179.85 ? 308 PHE B CD1 1 
ATOM   4593  C  CD2 . PHE B 1 244 ? 8.200  68.843 52.178  1.00 178.27 ? 308 PHE B CD2 1 
ATOM   4594  C  CE1 . PHE B 1 244 ? 6.685  67.176 50.529  1.00 168.08 ? 308 PHE B CE1 1 
ATOM   4595  C  CE2 . PHE B 1 244 ? 8.499  67.453 52.082  1.00 166.62 ? 308 PHE B CE2 1 
ATOM   4596  C  CZ  . PHE B 1 244 ? 7.736  66.619 51.243  1.00 119.30 ? 308 PHE B CZ  1 
ATOM   4597  N  N   . LEU B 1 245 ? 5.042  70.689 54.619  1.00 47.08  ? 309 LEU B N   1 
ATOM   4598  C  CA  . LEU B 1 245 ? 5.058  70.887 56.045  1.00 49.39  ? 309 LEU B CA  1 
ATOM   4599  C  C   . LEU B 1 245 ? 6.027  69.909 56.635  1.00 53.41  ? 309 LEU B C   1 
ATOM   4600  O  O   . LEU B 1 245 ? 5.859  68.703 56.438  1.00 76.81  ? 309 LEU B O   1 
ATOM   4601  C  CB  . LEU B 1 245 ? 3.667  70.641 56.607  1.00 63.23  ? 309 LEU B CB  1 
ATOM   4602  C  CG  . LEU B 1 245 ? 2.527  71.568 56.183  1.00 56.79  ? 309 LEU B CG  1 
ATOM   4603  C  CD1 . LEU B 1 245 ? 1.364  71.506 57.199  1.00 40.94  ? 309 LEU B CD1 1 
ATOM   4604  C  CD2 . LEU B 1 245 ? 3.063  72.976 56.069  1.00 58.12  ? 309 LEU B CD2 1 
ATOM   4605  N  N   . GLY B 1 246 ? 7.040  70.423 57.337  1.00 50.03  ? 310 GLY B N   1 
ATOM   4606  C  CA  . GLY B 1 246 ? 8.115  69.596 57.920  1.00 58.46  ? 310 GLY B CA  1 
ATOM   4607  C  C   . GLY B 1 246 ? 7.740  68.799 59.162  1.00 52.02  ? 310 GLY B C   1 
ATOM   4608  O  O   . GLY B 1 246 ? 8.077  67.620 59.312  1.00 51.85  ? 310 GLY B O   1 
ATOM   4609  N  N   . ASP B 1 247 ? 7.011  69.456 60.048  1.00 66.08  ? 311 ASP B N   1 
ATOM   4610  C  CA  . ASP B 1 247 ? 6.764  68.992 61.419  1.00 61.22  ? 311 ASP B CA  1 
ATOM   4611  C  C   . ASP B 1 247 ? 5.820  67.808 61.397  1.00 56.06  ? 311 ASP B C   1 
ATOM   4612  O  O   . ASP B 1 247 ? 5.340  67.424 60.325  1.00 45.05  ? 311 ASP B O   1 
ATOM   4613  C  CB  . ASP B 1 247 ? 6.143  70.134 62.247  1.00 64.03  ? 311 ASP B CB  1 
ATOM   4614  C  CG  . ASP B 1 247 ? 6.637  70.170 63.669  1.00 61.36  ? 311 ASP B CG  1 
ATOM   4615  O  OD1 . ASP B 1 247 ? 6.915  69.075 64.211  1.00 50.03  ? 311 ASP B OD1 1 
ATOM   4616  O  OD2 . ASP B 1 247 ? 6.729  71.300 64.245  1.00 62.59  ? 311 ASP B OD2 1 
ATOM   4617  N  N   . THR B 1 248 ? 5.569  67.254 62.589  1.00 61.89  ? 312 THR B N   1 
ATOM   4618  C  CA  . THR B 1 248 ? 4.723  66.063 62.829  1.00 51.96  ? 312 THR B CA  1 
ATOM   4619  C  C   . THR B 1 248 ? 4.220  66.091 64.276  1.00 60.38  ? 312 THR B C   1 
ATOM   4620  O  O   . THR B 1 248 ? 5.034  66.123 65.206  1.00 102.74 ? 312 THR B O   1 
ATOM   4621  C  CB  . THR B 1 248 ? 5.502  64.721 62.598  1.00 52.68  ? 312 THR B CB  1 
ATOM   4622  O  OG1 . THR B 1 248 ? 5.934  64.599 61.226  1.00 64.18  ? 312 THR B OG1 1 
ATOM   4623  C  CG2 . THR B 1 248 ? 4.627  63.537 62.919  1.00 54.98  ? 312 THR B CG2 1 
ATOM   4624  N  N   . PRO B 1 249 ? 2.890  66.072 64.483  1.00 56.85  ? 313 PRO B N   1 
ATOM   4625  C  CA  . PRO B 1 249 ? 1.946  65.892 63.413  1.00 77.94  ? 313 PRO B CA  1 
ATOM   4626  C  C   . PRO B 1 249 ? 1.700  67.208 62.699  1.00 81.33  ? 313 PRO B C   1 
ATOM   4627  O  O   . PRO B 1 249 ? 2.234  68.268 63.102  1.00 61.00  ? 313 PRO B O   1 
ATOM   4628  C  CB  . PRO B 1 249 ? 0.683  65.417 64.140  1.00 100.85 ? 313 PRO B CB  1 
ATOM   4629  C  CG  . PRO B 1 249 ? 0.749  66.151 65.450  1.00 94.18  ? 313 PRO B CG  1 
ATOM   4630  C  CD  . PRO B 1 249 ? 2.211  66.377 65.760  1.00 56.09  ? 313 PRO B CD  1 
ATOM   4631  N  N   . ARG B 1 250 ? 0.891  67.105 61.645  1.00 85.88  ? 314 ARG B N   1 
ATOM   4632  C  CA  . ARG B 1 250 ? 0.577  68.202 60.747  1.00 69.33  ? 314 ARG B CA  1 
ATOM   4633  C  C   . ARG B 1 250 ? -0.687 67.837 60.005  1.00 73.79  ? 314 ARG B C   1 
ATOM   4634  O  O   . ARG B 1 250 ? -1.111 66.660 60.006  1.00 75.91  ? 314 ARG B O   1 
ATOM   4635  C  CB  . ARG B 1 250 ? 1.699  68.411 59.752  1.00 61.05  ? 314 ARG B CB  1 
ATOM   4636  C  CG  . ARG B 1 250 ? 2.081  67.129 59.030  1.00 72.10  ? 314 ARG B CG  1 
ATOM   4637  C  CD  . ARG B 1 250 ? 3.057  67.395 57.933  1.00 62.00  ? 314 ARG B CD  1 
ATOM   4638  N  NE  . ARG B 1 250 ? 3.926  66.257 57.693  1.00 56.04  ? 314 ARG B NE  1 
ATOM   4639  C  CZ  . ARG B 1 250 ? 3.640  65.274 56.863  1.00 55.90  ? 314 ARG B CZ  1 
ATOM   4640  N  NH1 . ARG B 1 250 ? 2.487  65.279 56.206  1.00 86.46  ? 314 ARG B NH1 1 
ATOM   4641  N  NH2 . ARG B 1 250 ? 4.510  64.298 56.690  1.00 48.91  ? 314 ARG B NH2 1 
ATOM   4642  N  N   . GLY B 1 251 ? -1.276 68.837 59.364  1.00 56.25  ? 315 GLY B N   1 
ATOM   4643  C  CA  . GLY B 1 251 ? -2.609 68.662 58.851  1.00 102.30 ? 315 GLY B CA  1 
ATOM   4644  C  C   . GLY B 1 251 ? -2.582 68.086 57.465  1.00 95.80  ? 315 GLY B C   1 
ATOM   4645  O  O   . GLY B 1 251 ? -3.010 66.956 57.230  1.00 147.81 ? 315 GLY B O   1 
ATOM   4646  N  N   . ILE B 1 252 ? -2.047 68.883 56.555  1.00 80.77  ? 316 ILE B N   1 
ATOM   4647  C  CA  . ILE B 1 252 ? -2.283 68.742 55.127  1.00 83.38  ? 316 ILE B CA  1 
ATOM   4648  C  C   . ILE B 1 252 ? -1.427 69.769 54.434  1.00 69.00  ? 316 ILE B C   1 
ATOM   4649  O  O   . ILE B 1 252 ? -1.102 70.811 55.006  1.00 99.17  ? 316 ILE B O   1 
ATOM   4650  C  CB  . ILE B 1 252 ? -3.761 69.049 54.740  1.00 105.43 ? 316 ILE B CB  1 
ATOM   4651  C  CG1 . ILE B 1 252 ? -4.145 68.302 53.457  1.00 64.14  ? 316 ILE B CG1 1 
ATOM   4652  C  CG2 . ILE B 1 252 ? -4.041 70.578 54.667  1.00 106.42 ? 316 ILE B CG2 1 
ATOM   4653  C  CD1 . ILE B 1 252 ? -4.542 66.898 53.736  1.00 61.26  ? 316 ILE B CD1 1 
ATOM   4654  N  N   . ASP B 1 253 ? -1.059 69.484 53.196  1.00 79.24  ? 317 ASP B N   1 
ATOM   4655  C  CA  . ASP B 1 253 ? -0.154 70.381 52.495  1.00 95.34  ? 317 ASP B CA  1 
ATOM   4656  C  C   . ASP B 1 253 ? -0.923 71.587 52.013  1.00 76.15  ? 317 ASP B C   1 
ATOM   4657  O  O   . ASP B 1 253 ? -2.105 71.478 51.694  1.00 84.96  ? 317 ASP B O   1 
ATOM   4658  C  CB  . ASP B 1 253 ? 0.582  69.665 51.363  1.00 103.17 ? 317 ASP B CB  1 
ATOM   4659  C  CG  . ASP B 1 253 ? 1.708  68.769 51.875  1.00 105.90 ? 317 ASP B CG  1 
ATOM   4660  O  OD1 . ASP B 1 253 ? 2.339  69.088 52.926  1.00 72.45  ? 317 ASP B OD1 1 
ATOM   4661  O  OD2 . ASP B 1 253 ? 1.957  67.739 51.214  1.00 121.22 ? 317 ASP B OD2 1 
ATOM   4662  N  N   . THR B 1 254 ? -0.258 72.739 52.006  1.00 64.21  ? 318 THR B N   1 
ATOM   4663  C  CA  . THR B 1 254 ? -0.939 74.010 51.743  1.00 97.28  ? 318 THR B CA  1 
ATOM   4664  C  C   . THR B 1 254 ? -0.415 74.687 50.486  1.00 80.25  ? 318 THR B C   1 
ATOM   4665  O  O   . THR B 1 254 ? 0.411  74.128 49.778  1.00 55.04  ? 318 THR B O   1 
ATOM   4666  C  CB  . THR B 1 254 ? -0.747 74.995 52.899  1.00 80.97  ? 318 THR B CB  1 
ATOM   4667  O  OG1 . THR B 1 254 ? 0.656  75.154 53.126  1.00 105.31 ? 318 THR B OG1 1 
ATOM   4668  C  CG2 . THR B 1 254 ? -1.421 74.489 54.171  1.00 73.94  ? 318 THR B CG2 1 
ATOM   4669  N  N   . THR B 1 255 ? -0.911 75.892 50.205  1.00 78.78  ? 319 THR B N   1 
ATOM   4670  C  CA  . THR B 1 255 ? -0.290 76.731 49.181  1.00 83.76  ? 319 THR B CA  1 
ATOM   4671  C  C   . THR B 1 255 ? 0.946  77.330 49.834  1.00 65.34  ? 319 THR B C   1 
ATOM   4672  O  O   . THR B 1 255 ? 1.123  77.193 51.039  1.00 68.36  ? 319 THR B O   1 
ATOM   4673  C  CB  . THR B 1 255 ? -1.233 77.838 48.682  1.00 75.00  ? 319 THR B CB  1 
ATOM   4674  O  OG1 . THR B 1 255 ? -1.658 78.633 49.795  1.00 100.30 ? 319 THR B OG1 1 
ATOM   4675  C  CG2 . THR B 1 255 ? -2.465 77.227 47.983  1.00 111.08 ? 319 THR B CG2 1 
ATOM   4676  N  N   . ASN B 1 256 ? 1.811  77.971 49.061  1.00 57.31  ? 320 ASN B N   1 
ATOM   4677  C  CA  . ASN B 1 256 ? 3.005  78.594 49.650  1.00 60.02  ? 320 ASN B CA  1 
ATOM   4678  C  C   . ASN B 1 256 ? 2.747  79.963 50.178  1.00 47.80  ? 320 ASN B C   1 
ATOM   4679  O  O   . ASN B 1 256 ? 2.173  80.774 49.469  1.00 67.97  ? 320 ASN B O   1 
ATOM   4680  C  CB  . ASN B 1 256 ? 4.119  78.730 48.623  1.00 69.31  ? 320 ASN B CB  1 
ATOM   4681  C  CG  . ASN B 1 256 ? 4.503  77.416 48.007  1.00 64.67  ? 320 ASN B CG  1 
ATOM   4682  O  OD1 . ASN B 1 256 ? 3.882  76.381 48.258  1.00 88.53  ? 320 ASN B OD1 1 
ATOM   4683  N  ND2 . ASN B 1 256 ? 5.508  77.449 47.170  1.00 60.99  ? 320 ASN B ND2 1 
ATOM   4684  N  N   . TYR B 1 257 ? 3.171  80.235 51.409  1.00 56.59  ? 321 TYR B N   1 
ATOM   4685  C  CA  . TYR B 1 257 ? 3.090  81.607 51.982  1.00 60.04  ? 321 TYR B CA  1 
ATOM   4686  C  C   . TYR B 1 257 ? 4.109  81.784 53.076  1.00 63.17  ? 321 TYR B C   1 
ATOM   4687  O  O   . TYR B 1 257 ? 4.520  80.803 53.693  1.00 68.61  ? 321 TYR B O   1 
ATOM   4688  C  CB  . TYR B 1 257 ? 1.703  81.961 52.523  1.00 39.95  ? 321 TYR B CB  1 
ATOM   4689  C  CG  . TYR B 1 257 ? 1.101  80.913 53.432  1.00 58.10  ? 321 TYR B CG  1 
ATOM   4690  C  CD1 . TYR B 1 257 ? 1.282  80.975 54.811  1.00 42.54  ? 321 TYR B CD1 1 
ATOM   4691  C  CD2 . TYR B 1 257 ? 0.320  79.874 52.909  1.00 76.62  ? 321 TYR B CD2 1 
ATOM   4692  C  CE1 . TYR B 1 257 ? 0.744  80.002 55.648  1.00 51.14  ? 321 TYR B CE1 1 
ATOM   4693  C  CE2 . TYR B 1 257 ? -0.229 78.900 53.734  1.00 88.96  ? 321 TYR B CE2 1 
ATOM   4694  C  CZ  . TYR B 1 257 ? -0.008 78.965 55.102  1.00 61.79  ? 321 TYR B CZ  1 
ATOM   4695  O  OH  . TYR B 1 257 ? -0.568 78.012 55.927  1.00 67.41  ? 321 TYR B OH  1 
ATOM   4696  N  N   . CYS B 1 258 ? 4.498  83.032 53.328  1.00 65.79  ? 322 CYS B N   1 
ATOM   4697  C  CA  . CYS B 1 258 ? 5.596  83.308 54.258  1.00 66.33  ? 322 CYS B CA  1 
ATOM   4698  C  C   . CYS B 1 258 ? 5.170  83.489 55.713  1.00 69.61  ? 322 CYS B C   1 
ATOM   4699  O  O   . CYS B 1 258 ? 5.966  83.788 56.592  1.00 71.94  ? 322 CYS B O   1 
ATOM   4700  C  CB  . CYS B 1 258 ? 6.458  84.461 53.753  1.00 81.34  ? 322 CYS B CB  1 
ATOM   4701  S  SG  . CYS B 1 258 ? 7.319  84.024 52.194  1.00 203.71 ? 322 CYS B SG  1 
ATOM   4702  N  N   . ASP B 1 259 ? 3.902  83.254 55.978  1.00 95.20  ? 323 ASP B N   1 
ATOM   4703  C  CA  . ASP B 1 259 ? 3.428  83.176 57.346  1.00 87.56  ? 323 ASP B CA  1 
ATOM   4704  C  C   . ASP B 1 259 ? 3.677  81.760 57.930  1.00 67.90  ? 323 ASP B C   1 
ATOM   4705  O  O   . ASP B 1 259 ? 4.254  80.884 57.289  1.00 77.24  ? 323 ASP B O   1 
ATOM   4706  C  CB  . ASP B 1 259 ? 1.943  83.531 57.361  1.00 126.25 ? 323 ASP B CB  1 
ATOM   4707  C  CG  . ASP B 1 259 ? 1.484  84.093 58.680  1.00 109.73 ? 323 ASP B CG  1 
ATOM   4708  O  OD1 . ASP B 1 259 ? 2.262  84.798 59.354  1.00 78.32  ? 323 ASP B OD1 1 
ATOM   4709  O  OD2 . ASP B 1 259 ? 0.324  83.819 59.034  1.00 166.10 ? 323 ASP B OD2 1 
ATOM   4710  N  N   . LYS B 1 260 ? 3.227  81.545 59.153  1.00 53.76  ? 324 LYS B N   1 
ATOM   4711  C  CA  . LYS B 1 260 ? 3.379  80.279 59.853  1.00 50.55  ? 324 LYS B CA  1 
ATOM   4712  C  C   . LYS B 1 260 ? 2.065  79.481 59.929  1.00 54.39  ? 324 LYS B C   1 
ATOM   4713  O  O   . LYS B 1 260 ? 1.013  80.048 60.247  1.00 105.20 ? 324 LYS B O   1 
ATOM   4714  C  CB  . LYS B 1 260 ? 3.913  80.604 61.249  1.00 53.36  ? 324 LYS B CB  1 
ATOM   4715  C  CG  . LYS B 1 260 ? 3.290  79.842 62.409  1.00 63.79  ? 324 LYS B CG  1 
ATOM   4716  C  CD  . LYS B 1 260 ? 3.213  80.679 63.704  1.00 55.14  ? 324 LYS B CD  1 
ATOM   4717  C  CE  . LYS B 1 260 ? 4.424  81.539 63.882  1.00 64.33  ? 324 LYS B CE  1 
ATOM   4718  N  NZ  . LYS B 1 260 ? 4.298  82.243 65.188  1.00 63.07  ? 324 LYS B NZ  1 
ATOM   4719  N  N   . THR B 1 261 ? 2.134  78.180 59.668  1.00 45.64  ? 325 THR B N   1 
ATOM   4720  C  CA  . THR B 1 261 ? 0.937  77.317 59.583  1.00 61.00  ? 325 THR B CA  1 
ATOM   4721  C  C   . THR B 1 261 ? 0.367  76.817 60.909  1.00 57.59  ? 325 THR B C   1 
ATOM   4722  O  O   . THR B 1 261 ? 0.836  75.809 61.442  1.00 41.81  ? 325 THR B O   1 
ATOM   4723  C  CB  . THR B 1 261 ? 1.211  76.069 58.739  1.00 53.97  ? 325 THR B CB  1 
ATOM   4724  O  OG1 . THR B 1 261 ? 1.584  76.466 57.420  1.00 63.58  ? 325 THR B OG1 1 
ATOM   4725  C  CG2 . THR B 1 261 ? -0.024 75.200 58.671  1.00 45.23  ? 325 THR B CG2 1 
ATOM   4726  N  N   . THR B 1 262 ? -0.687 77.473 61.391  1.00 68.74  ? 326 THR B N   1 
ATOM   4727  C  CA  . THR B 1 262 ? -1.111 77.277 62.769  1.00 90.70  ? 326 THR B CA  1 
ATOM   4728  C  C   . THR B 1 262 ? -1.929 76.001 62.975  1.00 73.62  ? 326 THR B C   1 
ATOM   4729  O  O   . THR B 1 262 ? -2.150 75.583 64.111  1.00 67.77  ? 326 THR B O   1 
ATOM   4730  C  CB  . THR B 1 262 ? -1.906 78.490 63.305  1.00 78.36  ? 326 THR B CB  1 
ATOM   4731  O  OG1 . THR B 1 262 ? -3.242 78.392 62.837  1.00 73.94  ? 326 THR B OG1 1 
ATOM   4732  C  CG2 . THR B 1 262 ? -1.321 79.808 62.831  1.00 69.63  ? 326 THR B CG2 1 
ATOM   4733  N  N   . THR B 1 263 ? -2.350 75.379 61.882  1.00 57.15  ? 327 THR B N   1 
ATOM   4734  C  CA  . THR B 1 263 ? -3.267 74.262 61.964  1.00 60.09  ? 327 THR B CA  1 
ATOM   4735  C  C   . THR B 1 263 ? -2.523 72.999 62.271  1.00 68.36  ? 327 THR B C   1 
ATOM   4736  O  O   . THR B 1 263 ? -1.603 72.604 61.535  1.00 64.77  ? 327 THR B O   1 
ATOM   4737  C  CB  . THR B 1 263 ? -4.026 74.068 60.665  1.00 68.45  ? 327 THR B CB  1 
ATOM   4738  O  OG1 . THR B 1 263 ? -4.401 75.356 60.159  1.00 109.91 ? 327 THR B OG1 1 
ATOM   4739  C  CG2 . THR B 1 263 ? -5.271 73.228 60.902  1.00 64.13  ? 327 THR B CG2 1 
ATOM   4740  N  N   . GLU B 1 264 ? -2.949 72.346 63.350  1.00 71.15  ? 328 GLU B N   1 
ATOM   4741  C  CA  . GLU B 1 264 ? -2.213 71.211 63.909  1.00 67.89  ? 328 GLU B CA  1 
ATOM   4742  C  C   . GLU B 1 264 ? -0.754 71.575 64.248  1.00 60.76  ? 328 GLU B C   1 
ATOM   4743  O  O   . GLU B 1 264 ? 0.153  70.739 64.183  1.00 61.28  ? 328 GLU B O   1 
ATOM   4744  C  CB  . GLU B 1 264 ? -2.300 69.994 62.986  1.00 65.33  ? 328 GLU B CB  1 
ATOM   4745  C  CG  . GLU B 1 264 ? -3.640 69.228 63.068  1.00 82.43  ? 328 GLU B CG  1 
ATOM   4746  C  CD  . GLU B 1 264 ? -3.470 67.699 63.108  1.00 105.44 ? 328 GLU B CD  1 
ATOM   4747  O  OE1 . GLU B 1 264 ? -2.938 67.181 64.121  1.00 136.34 ? 328 GLU B OE1 1 
ATOM   4748  O  OE2 . GLU B 1 264 ? -3.876 67.018 62.135  1.00 104.73 ? 328 GLU B OE2 1 
ATOM   4749  N  N   . GLY B 1 265 ? -0.566 72.833 64.660  1.00 72.09  ? 329 GLY B N   1 
ATOM   4750  C  CA  . GLY B 1 265 ? 0.750  73.408 64.954  1.00 48.37  ? 329 GLY B CA  1 
ATOM   4751  C  C   . GLY B 1 265 ? 1.328  72.884 66.240  1.00 48.55  ? 329 GLY B C   1 
ATOM   4752  O  O   . GLY B 1 265 ? 2.544  72.900 66.451  1.00 78.83  ? 329 GLY B O   1 
ATOM   4753  N  N   . GLU B 1 266 ? 0.459  72.373 67.090  1.00 45.22  ? 330 GLU B N   1 
ATOM   4754  C  CA  . GLU B 1 266 ? 0.882  71.861 68.378  1.00 52.24  ? 330 GLU B CA  1 
ATOM   4755  C  C   . GLU B 1 266 ? 1.351  70.424 68.335  1.00 50.93  ? 330 GLU B C   1 
ATOM   4756  O  O   . GLU B 1 266 ? 0.798  69.582 67.603  1.00 48.22  ? 330 GLU B O   1 
ATOM   4757  C  CB  . GLU B 1 266 ? -0.241 71.990 69.389  1.00 60.91  ? 330 GLU B CB  1 
ATOM   4758  C  CG  . GLU B 1 266 ? 0.204  71.753 70.800  1.00 101.37 ? 330 GLU B CG  1 
ATOM   4759  C  CD  . GLU B 1 266 ? -0.771 72.275 71.840  1.00 154.28 ? 330 GLU B CD  1 
ATOM   4760  O  OE1 . GLU B 1 266 ? -1.825 72.826 71.461  1.00 193.96 ? 330 GLU B OE1 1 
ATOM   4761  O  OE2 . GLU B 1 266 ? -0.473 72.137 73.048  1.00 178.29 ? 330 GLU B OE2 1 
ATOM   4762  N  N   . GLY B 1 267 ? 2.324  70.159 69.200  1.00 48.51  ? 331 GLY B N   1 
ATOM   4763  C  CA  . GLY B 1 267 ? 3.074  68.935 69.180  1.00 66.32  ? 331 GLY B CA  1 
ATOM   4764  C  C   . GLY B 1 267 ? 4.203  69.147 68.208  1.00 63.20  ? 331 GLY B C   1 
ATOM   4765  O  O   . GLY B 1 267 ? 4.270  70.192 67.546  1.00 68.36  ? 331 GLY B O   1 
ATOM   4766  N  N   . GLY B 1 268 ? 5.081  68.158 68.117  1.00 55.47  ? 332 GLY B N   1 
ATOM   4767  C  CA  . GLY B 1 268 ? 6.186  68.209 67.174  1.00 53.59  ? 332 GLY B CA  1 
ATOM   4768  C  C   . GLY B 1 268 ? 7.260  67.197 67.499  1.00 54.48  ? 332 GLY B C   1 
ATOM   4769  O  O   . GLY B 1 268 ? 7.244  66.560 68.549  1.00 67.83  ? 332 GLY B O   1 
ATOM   4770  N  N   . ILE B 1 269 ? 8.188  67.043 66.578  1.00 40.45  ? 333 ILE B N   1 
ATOM   4771  C  CA  . ILE B 1 269 ? 9.317  66.192 66.798  1.00 51.65  ? 333 ILE B CA  1 
ATOM   4772  C  C   . ILE B 1 269 ? 10.500 66.737 65.994  1.00 53.87  ? 333 ILE B C   1 
ATOM   4773  O  O   . ILE B 1 269 ? 10.305 67.354 64.951  1.00 36.90  ? 333 ILE B O   1 
ATOM   4774  C  CB  . ILE B 1 269 ? 9.017  64.767 66.387  1.00 50.52  ? 333 ILE B CB  1 
ATOM   4775  C  CG1 . ILE B 1 269 ? 10.064 63.816 67.010  1.00 71.04  ? 333 ILE B CG1 1 
ATOM   4776  C  CG2 . ILE B 1 269 ? 8.965  64.717 64.897  1.00 33.04  ? 333 ILE B CG2 1 
ATOM   4777  C  CD1 . ILE B 1 269 ? 9.668  62.353 67.038  1.00 90.77  ? 333 ILE B CD1 1 
ATOM   4778  N  N   . GLN B 1 270 ? 11.710 66.504 66.512  1.00 51.94  ? 334 GLN B N   1 
ATOM   4779  C  CA  . GLN B 1 270 ? 12.934 67.036 65.956  1.00 48.67  ? 334 GLN B CA  1 
ATOM   4780  C  C   . GLN B 1 270 ? 13.106 66.626 64.499  1.00 53.79  ? 334 GLN B C   1 
ATOM   4781  O  O   . GLN B 1 270 ? 12.967 65.434 64.135  1.00 56.57  ? 334 GLN B O   1 
ATOM   4782  C  CB  . GLN B 1 270 ? 14.138 66.559 66.785  1.00 59.45  ? 334 GLN B CB  1 
ATOM   4783  C  CG  . GLN B 1 270 ? 15.475 67.200 66.401  1.00 62.98  ? 334 GLN B CG  1 
ATOM   4784  C  CD  . GLN B 1 270 ? 16.584 66.802 67.328  1.00 59.56  ? 334 GLN B CD  1 
ATOM   4785  O  OE1 . GLN B 1 270 ? 16.429 65.879 68.121  1.00 68.04  ? 334 GLN B OE1 1 
ATOM   4786  N  NE2 . GLN B 1 270 ? 17.711 67.503 67.250  1.00 61.12  ? 334 GLN B NE2 1 
ATOM   4787  N  N   . GLY B 1 271 ? 13.413 67.624 63.672  1.00 53.28  ? 335 GLY B N   1 
ATOM   4788  C  CA  . GLY B 1 271 ? 13.739 67.387 62.270  1.00 52.17  ? 335 GLY B CA  1 
ATOM   4789  C  C   . GLY B 1 271 ? 14.474 68.545 61.630  1.00 54.00  ? 335 GLY B C   1 
ATOM   4790  O  O   . GLY B 1 271 ? 14.669 69.595 62.273  1.00 68.76  ? 335 GLY B O   1 
ATOM   4791  N  N   . PHE B 1 272 ? 14.860 68.364 60.363  1.00 44.30  ? 336 PHE B N   1 
ATOM   4792  C  CA  . PHE B 1 272 ? 15.699 69.344 59.685  1.00 39.79  ? 336 PHE B CA  1 
ATOM   4793  C  C   . PHE B 1 272 ? 15.169 69.873 58.374  1.00 36.60  ? 336 PHE B C   1 
ATOM   4794  O  O   . PHE B 1 272 ? 14.177 69.374 57.841  1.00 46.63  ? 336 PHE B O   1 
ATOM   4795  C  CB  . PHE B 1 272 ? 17.087 68.769 59.452  1.00 39.85  ? 336 PHE B CB  1 
ATOM   4796  C  CG  . PHE B 1 272 ? 17.069 67.576 58.619  1.00 42.48  ? 336 PHE B CG  1 
ATOM   4797  C  CD1 . PHE B 1 272 ? 17.375 67.660 57.268  1.00 38.06  ? 336 PHE B CD1 1 
ATOM   4798  C  CD2 . PHE B 1 272 ? 16.699 66.354 59.167  1.00 46.00  ? 336 PHE B CD2 1 
ATOM   4799  C  CE1 . PHE B 1 272 ? 17.323 66.529 56.470  1.00 41.86  ? 336 PHE B CE1 1 
ATOM   4800  C  CE2 . PHE B 1 272 ? 16.659 65.220 58.374  1.00 49.54  ? 336 PHE B CE2 1 
ATOM   4801  C  CZ  . PHE B 1 272 ? 16.978 65.303 57.021  1.00 39.74  ? 336 PHE B CZ  1 
ATOM   4802  N  N   . MET B 1 273 ? 15.848 70.920 57.904  1.00 33.57  ? 337 MET B N   1 
ATOM   4803  C  CA  . MET B 1 273 ? 15.755 71.463 56.561  1.00 39.11  ? 337 MET B CA  1 
ATOM   4804  C  C   . MET B 1 273 ? 17.164 71.878 56.175  1.00 41.97  ? 337 MET B C   1 
ATOM   4805  O  O   . MET B 1 273 ? 17.963 72.294 57.000  1.00 68.35  ? 337 MET B O   1 
ATOM   4806  C  CB  . MET B 1 273 ? 14.824 72.689 56.488  1.00 38.76  ? 337 MET B CB  1 
ATOM   4807  C  CG  . MET B 1 273 ? 13.362 72.371 56.687  1.00 47.07  ? 337 MET B CG  1 
ATOM   4808  S  SD  . MET B 1 273 ? 12.257 73.810 56.729  1.00 71.10  ? 337 MET B SD  1 
ATOM   4809  C  CE  . MET B 1 273 ? 13.055 74.952 57.844  1.00 56.79  ? 337 MET B CE  1 
ATOM   4810  N  N   . ILE B 1 274 ? 17.477 71.785 54.910  1.00 42.47  ? 338 ILE B N   1 
ATOM   4811  C  CA  . ILE B 1 274 ? 18.747 72.271 54.429  1.00 49.32  ? 338 ILE B CA  1 
ATOM   4812  C  C   . ILE B 1 274 ? 18.510 73.461 53.469  1.00 53.34  ? 338 ILE B C   1 
ATOM   4813  O  O   . ILE B 1 274 ? 17.655 73.425 52.578  1.00 57.10  ? 338 ILE B O   1 
ATOM   4814  C  CB  . ILE B 1 274 ? 19.493 71.103 53.717  1.00 51.10  ? 338 ILE B CB  1 
ATOM   4815  C  CG1 . ILE B 1 274 ? 19.471 69.856 54.593  1.00 44.22  ? 338 ILE B CG1 1 
ATOM   4816  C  CG2 . ILE B 1 274 ? 20.917 71.472 53.394  1.00 40.48  ? 338 ILE B CG2 1 
ATOM   4817  C  CD1 . ILE B 1 274 ? 20.343 68.802 54.072  1.00 38.00  ? 338 ILE B CD1 1 
ATOM   4818  N  N   . GLU B 1 275 ? 19.265 74.522 53.650  1.00 55.53  ? 339 GLU B N   1 
ATOM   4819  C  CA  . GLU B 1 275 ? 19.188 75.637 52.723  1.00 69.47  ? 339 GLU B CA  1 
ATOM   4820  C  C   . GLU B 1 275 ? 20.472 75.668 51.900  1.00 63.01  ? 339 GLU B C   1 
ATOM   4821  O  O   . GLU B 1 275 ? 21.560 75.625 52.463  1.00 73.78  ? 339 GLU B O   1 
ATOM   4822  C  CB  . GLU B 1 275 ? 18.966 76.940 53.512  1.00 76.93  ? 339 GLU B CB  1 
ATOM   4823  C  CG  . GLU B 1 275 ? 19.292 78.244 52.772  1.00 106.80 ? 339 GLU B CG  1 
ATOM   4824  C  CD  . GLU B 1 275 ? 18.261 78.645 51.716  1.00 115.15 ? 339 GLU B CD  1 
ATOM   4825  O  OE1 . GLU B 1 275 ? 17.131 78.118 51.734  1.00 142.33 ? 339 GLU B OE1 1 
ATOM   4826  O  OE2 . GLU B 1 275 ? 18.588 79.500 50.859  1.00 92.25  ? 339 GLU B OE2 1 
ATOM   4827  N  N   . GLY B 1 276 ? 20.347 75.731 50.577  1.00 57.34  ? 340 GLY B N   1 
ATOM   4828  C  CA  . GLY B 1 276 ? 21.521 75.788 49.691  1.00 73.73  ? 340 GLY B CA  1 
ATOM   4829  C  C   . GLY B 1 276 ? 21.172 76.156 48.261  1.00 78.17  ? 340 GLY B C   1 
ATOM   4830  O  O   . GLY B 1 276 ? 20.110 76.744 48.010  1.00 80.30  ? 340 GLY B O   1 
ATOM   4831  N  N   . SER B 1 277 ? 22.064 75.815 47.325  1.00 75.87  ? 341 SER B N   1 
ATOM   4832  C  CA  . SER B 1 277 ? 21.769 75.950 45.900  1.00 80.94  ? 341 SER B CA  1 
ATOM   4833  C  C   . SER B 1 277 ? 20.520 75.128 45.633  1.00 82.48  ? 341 SER B C   1 
ATOM   4834  O  O   . SER B 1 277 ? 19.462 75.650 45.250  1.00 104.71 ? 341 SER B O   1 
ATOM   4835  C  CB  . SER B 1 277 ? 22.931 75.425 45.068  1.00 98.55  ? 341 SER B CB  1 
ATOM   4836  O  OG  . SER B 1 277 ? 24.042 76.303 45.130  1.00 144.95 ? 341 SER B OG  1 
ATOM   4837  N  N   . ASN B 1 278 ? 20.666 73.829 45.851  1.00 71.22  ? 342 ASN B N   1 
ATOM   4838  C  CA  . ASN B 1 278 ? 19.539 72.951 46.057  1.00 55.15  ? 342 ASN B CA  1 
ATOM   4839  C  C   . ASN B 1 278 ? 19.127 73.054 47.511  1.00 47.38  ? 342 ASN B C   1 
ATOM   4840  O  O   . ASN B 1 278 ? 19.972 73.100 48.375  1.00 50.23  ? 342 ASN B O   1 
ATOM   4841  C  CB  . ASN B 1 278 ? 19.940 71.510 45.765  1.00 51.66  ? 342 ASN B CB  1 
ATOM   4842  C  CG  . ASN B 1 278 ? 20.069 71.221 44.275  1.00 54.35  ? 342 ASN B CG  1 
ATOM   4843  O  OD1 . ASN B 1 278 ? 19.229 71.618 43.475  1.00 83.19  ? 342 ASN B OD1 1 
ATOM   4844  N  ND2 . ASN B 1 278 ? 21.102 70.491 43.907  1.00 63.92  ? 342 ASN B ND2 1 
ATOM   4845  N  N   . SER B 1 279 ? 17.832 73.080 47.787  1.00 50.62  ? 343 SER B N   1 
ATOM   4846  C  CA  . SER B 1 279 ? 17.356 73.015 49.168  1.00 59.50  ? 343 SER B CA  1 
ATOM   4847  C  C   . SER B 1 279 ? 16.550 71.743 49.451  1.00 50.02  ? 343 SER B C   1 
ATOM   4848  O  O   . SER B 1 279 ? 15.928 71.204 48.538  1.00 59.46  ? 343 SER B O   1 
ATOM   4849  C  CB  . SER B 1 279 ? 16.551 74.270 49.505  1.00 65.98  ? 343 SER B CB  1 
ATOM   4850  O  OG  . SER B 1 279 ? 17.380 75.425 49.469  1.00 63.39  ? 343 SER B OG  1 
ATOM   4851  N  N   . TRP B 1 280 ? 16.575 71.272 50.704  1.00 45.12  ? 344 TRP B N   1 
ATOM   4852  C  CA  . TRP B 1 280 ? 15.886 70.034 51.086  1.00 41.92  ? 344 TRP B CA  1 
ATOM   4853  C  C   . TRP B 1 280 ? 14.987 70.143 52.281  1.00 42.61  ? 344 TRP B C   1 
ATOM   4854  O  O   . TRP B 1 280 ? 15.320 70.814 53.251  1.00 43.29  ? 344 TRP B O   1 
ATOM   4855  C  CB  . TRP B 1 280 ? 16.880 68.969 51.368  1.00 35.02  ? 344 TRP B CB  1 
ATOM   4856  C  CG  . TRP B 1 280 ? 17.784 68.660 50.221  1.00 35.62  ? 344 TRP B CG  1 
ATOM   4857  C  CD1 . TRP B 1 280 ? 18.979 69.289 49.883  1.00 35.32  ? 344 TRP B CD1 1 
ATOM   4858  C  CD2 . TRP B 1 280 ? 17.620 67.589 49.240  1.00 35.80  ? 344 TRP B CD2 1 
ATOM   4859  N  NE1 . TRP B 1 280 ? 19.550 68.704 48.779  1.00 36.36  ? 344 TRP B NE1 1 
ATOM   4860  C  CE2 . TRP B 1 280 ? 18.795 67.659 48.357  1.00 37.26  ? 344 TRP B CE2 1 
ATOM   4861  C  CE3 . TRP B 1 280 ? 16.646 66.624 49.001  1.00 33.94  ? 344 TRP B CE3 1 
ATOM   4862  C  CZ2 . TRP B 1 280 ? 18.965 66.787 47.299  1.00 37.87  ? 344 TRP B CZ2 1 
ATOM   4863  C  CZ3 . TRP B 1 280 ? 16.827 65.752 47.927  1.00 34.06  ? 344 TRP B CZ3 1 
ATOM   4864  C  CH2 . TRP B 1 280 ? 17.955 65.836 47.095  1.00 39.48  ? 344 TRP B CH2 1 
ATOM   4865  N  N   . ILE B 1 281 ? 13.826 69.495 52.213  1.00 38.71  ? 345 ILE B N   1 
ATOM   4866  C  CA  . ILE B 1 281 ? 13.034 69.212 53.400  1.00 38.29  ? 345 ILE B CA  1 
ATOM   4867  C  C   . ILE B 1 281 ? 12.822 67.717 53.585  1.00 43.78  ? 345 ILE B C   1 
ATOM   4868  O  O   . ILE B 1 281 ? 12.366 67.034 52.678  1.00 70.28  ? 345 ILE B O   1 
ATOM   4869  C  CB  . ILE B 1 281 ? 11.704 69.871 53.350  1.00 37.79  ? 345 ILE B CB  1 
ATOM   4870  C  CG1 . ILE B 1 281 ? 11.892 71.370 53.432  1.00 44.85  ? 345 ILE B CG1 1 
ATOM   4871  C  CG2 . ILE B 1 281 ? 10.865 69.408 54.539  1.00 31.15  ? 345 ILE B CG2 1 
ATOM   4872  C  CD1 . ILE B 1 281 ? 10.631 72.157 53.124  1.00 60.94  ? 345 ILE B CD1 1 
ATOM   4873  N  N   . GLY B 1 282 ? 13.218 67.200 54.741  1.00 44.39  ? 346 GLY B N   1 
ATOM   4874  C  CA  . GLY B 1 282 ? 12.939 65.814 55.107  1.00 40.65  ? 346 GLY B CA  1 
ATOM   4875  C  C   . GLY B 1 282 ? 11.732 65.764 56.024  1.00 40.86  ? 346 GLY B C   1 
ATOM   4876  O  O   . GLY B 1 282 ? 11.451 66.720 56.753  1.00 68.03  ? 346 GLY B O   1 
ATOM   4877  N  N   . ARG B 1 283 ? 10.999 64.665 55.995  1.00 35.34  ? 347 ARG B N   1 
ATOM   4878  C  CA  . ARG B 1 283 ? 9.840  64.564 56.854  1.00 46.66  ? 347 ARG B CA  1 
ATOM   4879  C  C   . ARG B 1 283 ? 9.310  63.163 56.966  1.00 41.49  ? 347 ARG B C   1 
ATOM   4880  O  O   . ARG B 1 283 ? 9.544  62.338 56.096  1.00 46.49  ? 347 ARG B O   1 
ATOM   4881  C  CB  . ARG B 1 283 ? 8.713  65.523 56.405  1.00 44.82  ? 347 ARG B CB  1 
ATOM   4882  C  CG  . ARG B 1 283 ? 7.780  64.969 55.403  1.00 36.25  ? 347 ARG B CG  1 
ATOM   4883  C  CD  . ARG B 1 283 ? 6.980  66.095 54.904  1.00 47.01  ? 347 ARG B CD  1 
ATOM   4884  N  NE  . ARG B 1 283 ? 5.924  65.625 54.025  1.00 56.14  ? 347 ARG B NE  1 
ATOM   4885  C  CZ  . ARG B 1 283 ? 4.951  66.401 53.571  1.00 57.76  ? 347 ARG B CZ  1 
ATOM   4886  N  NH1 . ARG B 1 283 ? 4.874  67.691 53.929  1.00 56.31  ? 347 ARG B NH1 1 
ATOM   4887  N  NH2 . ARG B 1 283 ? 4.038  65.876 52.779  1.00 92.39  ? 347 ARG B NH2 1 
ATOM   4888  N  N   . ILE B 1 284 ? 8.581  62.919 58.053  1.00 51.92  ? 348 ILE B N   1 
ATOM   4889  C  CA  . ILE B 1 284 ? 7.899  61.654 58.267  1.00 51.52  ? 348 ILE B CA  1 
ATOM   4890  C  C   . ILE B 1 284 ? 6.713  61.628 57.340  1.00 45.32  ? 348 ILE B C   1 
ATOM   4891  O  O   . ILE B 1 284 ? 5.960  62.604 57.244  1.00 57.24  ? 348 ILE B O   1 
ATOM   4892  C  CB  . ILE B 1 284 ? 7.441  61.447 59.727  1.00 51.12  ? 348 ILE B CB  1 
ATOM   4893  C  CG1 . ILE B 1 284 ? 8.572  61.782 60.702  1.00 60.63  ? 348 ILE B CG1 1 
ATOM   4894  C  CG2 . ILE B 1 284 ? 6.950  60.011 59.927  1.00 52.73  ? 348 ILE B CG2 1 
ATOM   4895  C  CD1 . ILE B 1 284 ? 8.514  61.087 62.081  1.00 47.72  ? 348 ILE B CD1 1 
ATOM   4896  N  N   . ILE B 1 285 ? 6.575  60.505 56.655  1.00 38.93  ? 349 ILE B N   1 
ATOM   4897  C  CA  . ILE B 1 285 ? 5.623  60.382 55.582  1.00 35.32  ? 349 ILE B CA  1 
ATOM   4898  C  C   . ILE B 1 285 ? 4.204  60.327 56.078  1.00 40.10  ? 349 ILE B C   1 
ATOM   4899  O  O   . ILE B 1 285 ? 3.378  61.075 55.586  1.00 35.49  ? 349 ILE B O   1 
ATOM   4900  C  CB  . ILE B 1 285 ? 5.930  59.171 54.756  1.00 34.49  ? 349 ILE B CB  1 
ATOM   4901  C  CG1 . ILE B 1 285 ? 7.300  59.366 54.117  1.00 38.77  ? 349 ILE B CG1 1 
ATOM   4902  C  CG2 . ILE B 1 285 ? 4.908  58.984 53.716  1.00 24.38  ? 349 ILE B CG2 1 
ATOM   4903  C  CD1 . ILE B 1 285 ? 7.660  58.263 53.182  1.00 35.72  ? 349 ILE B CD1 1 
ATOM   4904  N  N   . ASN B 1 286 ? 3.930  59.449 57.042  1.00 54.16  ? 350 ASN B N   1 
ATOM   4905  C  CA  . ASN B 1 286 ? 2.575  59.219 57.517  1.00 51.82  ? 350 ASN B CA  1 
ATOM   4906  C  C   . ASN B 1 286 ? 2.451  59.595 58.967  1.00 51.26  ? 350 ASN B C   1 
ATOM   4907  O  O   . ASN B 1 286 ? 2.675  58.758 59.839  1.00 61.01  ? 350 ASN B O   1 
ATOM   4908  C  CB  . ASN B 1 286 ? 2.183  57.765 57.323  1.00 55.90  ? 350 ASN B CB  1 
ATOM   4909  C  CG  . ASN B 1 286 ? 2.040  57.411 55.897  1.00 50.59  ? 350 ASN B CG  1 
ATOM   4910  O  OD1 . ASN B 1 286 ? 2.987  56.951 55.284  1.00 69.09  ? 350 ASN B OD1 1 
ATOM   4911  N  ND2 . ASN B 1 286 ? 0.853  57.624 55.342  1.00 75.41  ? 350 ASN B ND2 1 
ATOM   4912  N  N   . PRO B 1 287 ? 2.056  60.854 59.232  1.00 57.41  ? 351 PRO B N   1 
ATOM   4913  C  CA  . PRO B 1 287 ? 2.070  61.425 60.581  1.00 51.74  ? 351 PRO B CA  1 
ATOM   4914  C  C   . PRO B 1 287 ? 1.210  60.645 61.578  1.00 60.92  ? 351 PRO B C   1 
ATOM   4915  O  O   . PRO B 1 287 ? 1.500  60.659 62.779  1.00 73.82  ? 351 PRO B O   1 
ATOM   4916  C  CB  . PRO B 1 287 ? 1.490  62.815 60.361  1.00 45.42  ? 351 PRO B CB  1 
ATOM   4917  C  CG  . PRO B 1 287 ? 1.715  63.076 58.893  1.00 51.67  ? 351 PRO B CG  1 
ATOM   4918  C  CD  . PRO B 1 287 ? 1.432  61.778 58.272  1.00 45.52  ? 351 PRO B CD  1 
ATOM   4919  N  N   . GLY B 1 288 ? 0.181  59.954 61.083  1.00 60.03  ? 352 GLY B N   1 
ATOM   4920  C  CA  . GLY B 1 288 ? -0.645 59.105 61.936  1.00 61.04  ? 352 GLY B CA  1 
ATOM   4921  C  C   . GLY B 1 288 ? 0.175  57.986 62.526  1.00 71.54  ? 352 GLY B C   1 
ATOM   4922  O  O   . GLY B 1 288 ? 0.468  57.976 63.718  1.00 83.42  ? 352 GLY B O   1 
ATOM   4923  N  N   . SER B 1 289 ? 0.579  57.062 61.662  1.00 75.75  ? 353 SER B N   1 
ATOM   4924  C  CA  . SER B 1 289 ? 1.351  55.896 62.066  1.00 57.68  ? 353 SER B CA  1 
ATOM   4925  C  C   . SER B 1 289 ? 2.836  56.132 62.344  1.00 50.73  ? 353 SER B C   1 
ATOM   4926  O  O   . SER B 1 289 ? 3.522  55.255 62.874  1.00 78.51  ? 353 SER B O   1 
ATOM   4927  C  CB  . SER B 1 289 ? 1.178  54.774 61.040  1.00 71.97  ? 353 SER B CB  1 
ATOM   4928  O  OG  . SER B 1 289 ? 1.190  55.256 59.715  1.00 86.14  ? 353 SER B OG  1 
ATOM   4929  N  N   . LYS B 1 290 ? 3.327  57.310 61.991  1.00 47.48  ? 354 LYS B N   1 
ATOM   4930  C  CA  . LYS B 1 290 ? 4.745  57.656 62.100  1.00 50.82  ? 354 LYS B CA  1 
ATOM   4931  C  C   . LYS B 1 290 ? 5.629  56.777 61.215  1.00 57.16  ? 354 LYS B C   1 
ATOM   4932  O  O   . LYS B 1 290 ? 6.810  56.617 61.487  1.00 65.32  ? 354 LYS B O   1 
ATOM   4933  C  CB  . LYS B 1 290 ? 5.209  57.575 63.547  1.00 61.58  ? 354 LYS B CB  1 
ATOM   4934  C  CG  . LYS B 1 290 ? 4.430  58.455 64.512  1.00 70.12  ? 354 LYS B CG  1 
ATOM   4935  C  CD  . LYS B 1 290 ? 4.884  59.882 64.400  1.00 94.47  ? 354 LYS B CD  1 
ATOM   4936  C  CE  . LYS B 1 290 ? 4.016  60.795 65.234  1.00 128.91 ? 354 LYS B CE  1 
ATOM   4937  N  NZ  . LYS B 1 290 ? 4.281  60.586 66.673  1.00 143.96 ? 354 LYS B NZ  1 
ATOM   4938  N  N   . LYS B 1 291 ? 5.041  56.215 60.159  1.00 56.57  ? 355 LYS B N   1 
ATOM   4939  C  CA  . LYS B 1 291 ? 5.733  55.324 59.232  1.00 50.37  ? 355 LYS B CA  1 
ATOM   4940  C  C   . LYS B 1 291 ? 6.360  56.080 58.063  1.00 62.56  ? 355 LYS B C   1 
ATOM   4941  O  O   . LYS B 1 291 ? 5.736  56.991 57.462  1.00 55.11  ? 355 LYS B O   1 
ATOM   4942  C  CB  . LYS B 1 291 ? 4.754  54.300 58.684  1.00 54.42  ? 355 LYS B CB  1 
ATOM   4943  C  CG  . LYS B 1 291 ? 4.428  53.171 59.643  1.00 76.16  ? 355 LYS B CG  1 
ATOM   4944  C  CD  . LYS B 1 291 ? 5.084  51.857 59.219  1.00 83.82  ? 355 LYS B CD  1 
ATOM   4945  C  CE  . LYS B 1 291 ? 4.486  50.678 59.959  1.00 88.52  ? 355 LYS B CE  1 
ATOM   4946  N  NZ  . LYS B 1 291 ? 2.986  50.649 59.865  1.00 142.47 ? 355 LYS B NZ  1 
ATOM   4947  N  N   . GLY B 1 292 ? 7.596  55.704 57.730  1.00 49.87  ? 356 GLY B N   1 
ATOM   4948  C  CA  . GLY B 1 292 ? 8.229  56.271 56.533  1.00 45.58  ? 356 GLY B CA  1 
ATOM   4949  C  C   . GLY B 1 292 ? 8.858  57.654 56.633  1.00 44.78  ? 356 GLY B C   1 
ATOM   4950  O  O   . GLY B 1 292 ? 8.445  58.525 57.396  1.00 55.69  ? 356 GLY B O   1 
ATOM   4951  N  N   . PHE B 1 293 ? 9.901  57.842 55.858  1.00 41.59  ? 357 PHE B N   1 
ATOM   4952  C  CA  . PHE B 1 293 ? 10.593 59.094 55.833  1.00 42.46  ? 357 PHE B CA  1 
ATOM   4953  C  C   . PHE B 1 293 ? 10.882 59.434 54.391  1.00 58.41  ? 357 PHE B C   1 
ATOM   4954  O  O   . PHE B 1 293 ? 11.426 58.588 53.634  1.00 55.88  ? 357 PHE B O   1 
ATOM   4955  C  CB  . PHE B 1 293 ? 11.895 58.967 56.570  1.00 36.55  ? 357 PHE B CB  1 
ATOM   4956  C  CG  . PHE B 1 293 ? 12.637 60.254 56.723  1.00 32.01  ? 357 PHE B CG  1 
ATOM   4957  C  CD1 . PHE B 1 293 ? 13.574 60.620 55.808  1.00 32.42  ? 357 PHE B CD1 1 
ATOM   4958  C  CD2 . PHE B 1 293 ? 12.416 61.078 57.809  1.00 35.21  ? 357 PHE B CD2 1 
ATOM   4959  C  CE1 . PHE B 1 293 ? 14.312 61.776 55.960  1.00 38.52  ? 357 PHE B CE1 1 
ATOM   4960  C  CE2 . PHE B 1 293 ? 13.127 62.244 57.954  1.00 38.34  ? 357 PHE B CE2 1 
ATOM   4961  C  CZ  . PHE B 1 293 ? 14.094 62.587 57.029  1.00 36.36  ? 357 PHE B CZ  1 
ATOM   4962  N  N   . GLU B 1 294 ? 10.499 60.657 54.014  1.00 45.81  ? 358 GLU B N   1 
ATOM   4963  C  CA  . GLU B 1 294 ? 10.750 61.176 52.679  1.00 37.70  ? 358 GLU B CA  1 
ATOM   4964  C  C   . GLU B 1 294 ? 11.522 62.483 52.756  1.00 38.81  ? 358 GLU B C   1 
ATOM   4965  O  O   . GLU B 1 294 ? 11.345 63.252 53.699  1.00 50.58  ? 358 GLU B O   1 
ATOM   4966  C  CB  . GLU B 1 294 ? 9.435  61.384 51.947  1.00 45.80  ? 358 GLU B CB  1 
ATOM   4967  C  CG  . GLU B 1 294 ? 8.462  62.407 52.568  1.00 82.98  ? 358 GLU B CG  1 
ATOM   4968  C  CD  . GLU B 1 294 ? 7.132  62.570 51.786  1.00 97.10  ? 358 GLU B CD  1 
ATOM   4969  O  OE1 . GLU B 1 294 ? 7.075  62.180 50.600  1.00 118.20 ? 358 GLU B OE1 1 
ATOM   4970  O  OE2 . GLU B 1 294 ? 6.141  63.096 52.354  1.00 81.38  ? 358 GLU B OE2 1 
ATOM   4971  N  N   . ILE B 1 295 ? 12.383 62.728 51.780  1.00 33.07  ? 359 ILE B N   1 
ATOM   4972  C  CA  . ILE B 1 295 ? 13.107 63.987 51.694  1.00 34.66  ? 359 ILE B CA  1 
ATOM   4973  C  C   . ILE B 1 295 ? 12.891 64.533 50.332  1.00 37.02  ? 359 ILE B C   1 
ATOM   4974  O  O   . ILE B 1 295 ? 12.819 63.804 49.368  1.00 43.39  ? 359 ILE B O   1 
ATOM   4975  C  CB  . ILE B 1 295 ? 14.588 63.799 51.872  1.00 39.78  ? 359 ILE B CB  1 
ATOM   4976  C  CG1 . ILE B 1 295 ? 15.268 65.154 52.072  1.00 42.00  ? 359 ILE B CG1 1 
ATOM   4977  C  CG2 . ILE B 1 295 ? 15.179 63.012 50.694  1.00 30.65  ? 359 ILE B CG2 1 
ATOM   4978  C  CD1 . ILE B 1 295 ? 16.701 64.969 52.599  1.00 62.04  ? 359 ILE B CD1 1 
ATOM   4979  N  N   . TYR B 1 296 ? 12.849 65.836 50.237  1.00 45.67  ? 360 TYR B N   1 
ATOM   4980  C  CA  . TYR B 1 296 ? 12.216 66.452 49.104  1.00 47.40  ? 360 TYR B CA  1 
ATOM   4981  C  C   . TYR B 1 296 ? 13.040 67.665 48.629  1.00 45.11  ? 360 TYR B C   1 
ATOM   4982  O  O   . TYR B 1 296 ? 13.466 68.467 49.434  1.00 71.42  ? 360 TYR B O   1 
ATOM   4983  C  CB  . TYR B 1 296 ? 10.786 66.794 49.535  1.00 60.48  ? 360 TYR B CB  1 
ATOM   4984  C  CG  . TYR B 1 296 ? 9.957  67.306 48.437  1.00 100.45 ? 360 TYR B CG  1 
ATOM   4985  C  CD1 . TYR B 1 296 ? 9.526  66.478 47.423  1.00 181.58 ? 360 TYR B CD1 1 
ATOM   4986  C  CD2 . TYR B 1 296 ? 9.639  68.641 48.373  1.00 168.59 ? 360 TYR B CD2 1 
ATOM   4987  C  CE1 . TYR B 1 296 ? 8.785  66.980 46.379  1.00 234.19 ? 360 TYR B CE1 1 
ATOM   4988  C  CE2 . TYR B 1 296 ? 8.887  69.157 47.343  1.00 229.73 ? 360 TYR B CE2 1 
ATOM   4989  C  CZ  . TYR B 1 296 ? 8.461  68.335 46.349  1.00 238.92 ? 360 TYR B CZ  1 
ATOM   4990  O  OH  . TYR B 1 296 ? 7.708  68.893 45.335  1.00 223.28 ? 360 TYR B OH  1 
ATOM   4991  N  N   . LYS B 1 297 ? 13.291 67.771 47.331  1.00 41.43  ? 361 LYS B N   1 
ATOM   4992  C  CA  . LYS B 1 297 ? 14.307 68.667 46.784  1.00 40.54  ? 361 LYS B CA  1 
ATOM   4993  C  C   . LYS B 1 297 ? 13.678 69.904 46.196  1.00 40.89  ? 361 LYS B C   1 
ATOM   4994  O  O   . LYS B 1 297 ? 12.603 69.839 45.610  1.00 53.06  ? 361 LYS B O   1 
ATOM   4995  C  CB  . LYS B 1 297 ? 15.093 67.912 45.716  1.00 39.69  ? 361 LYS B CB  1 
ATOM   4996  C  CG  . LYS B 1 297 ? 16.294 68.619 45.147  1.00 45.78  ? 361 LYS B CG  1 
ATOM   4997  C  CD  . LYS B 1 297 ? 16.956 67.658 44.160  1.00 44.03  ? 361 LYS B CD  1 
ATOM   4998  C  CE  . LYS B 1 297 ? 17.892 68.357 43.179  1.00 48.23  ? 361 LYS B CE  1 
ATOM   4999  N  NZ  . LYS B 1 297 ? 18.449 67.343 42.250  1.00 56.73  ? 361 LYS B NZ  1 
ATOM   5000  N  N   . PHE B 1 298 ? 14.359 71.033 46.340  1.00 52.85  ? 362 PHE B N   1 
ATOM   5001  C  CA  . PHE B 1 298 ? 13.845 72.303 45.833  1.00 54.59  ? 362 PHE B CA  1 
ATOM   5002  C  C   . PHE B 1 298 ? 14.918 73.092 45.152  1.00 56.08  ? 362 PHE B C   1 
ATOM   5003  O  O   . PHE B 1 298 ? 16.018 73.179 45.666  1.00 71.69  ? 362 PHE B O   1 
ATOM   5004  C  CB  . PHE B 1 298 ? 13.342 73.143 46.970  1.00 38.72  ? 362 PHE B CB  1 
ATOM   5005  C  CG  . PHE B 1 298 ? 12.138 72.607 47.620  1.00 37.32  ? 362 PHE B CG  1 
ATOM   5006  C  CD1 . PHE B 1 298 ? 10.876 72.909 47.138  1.00 47.09  ? 362 PHE B CD1 1 
ATOM   5007  C  CD2 . PHE B 1 298 ? 12.263 71.826 48.736  1.00 36.32  ? 362 PHE B CD2 1 
ATOM   5008  C  CE1 . PHE B 1 298 ? 9.741  72.426 47.785  1.00 78.78  ? 362 PHE B CE1 1 
ATOM   5009  C  CE2 . PHE B 1 298 ? 11.142 71.341 49.401  1.00 54.13  ? 362 PHE B CE2 1 
ATOM   5010  C  CZ  . PHE B 1 298 ? 9.878  71.641 48.929  1.00 63.60  ? 362 PHE B CZ  1 
ATOM   5011  N  N   . LEU B 1 299 ? 14.603 73.685 44.006  1.00 67.68  ? 363 LEU B N   1 
ATOM   5012  C  CA  . LEU B 1 299 ? 15.536 74.605 43.384  1.00 75.63  ? 363 LEU B CA  1 
ATOM   5013  C  C   . LEU B 1 299 ? 15.458 75.927 44.115  1.00 88.05  ? 363 LEU B C   1 
ATOM   5014  O  O   . LEU B 1 299 ? 14.359 76.469 44.338  1.00 111.68 ? 363 LEU B O   1 
ATOM   5015  C  CB  . LEU B 1 299 ? 15.225 74.773 41.905  1.00 102.26 ? 363 LEU B CB  1 
ATOM   5016  C  CG  . LEU B 1 299 ? 15.769 73.641 41.027  1.00 130.70 ? 363 LEU B CG  1 
ATOM   5017  C  CD1 . LEU B 1 299 ? 17.187 73.264 41.456  1.00 103.14 ? 363 LEU B CD1 1 
ATOM   5018  C  CD2 . LEU B 1 299 ? 14.847 72.413 41.020  1.00 154.90 ? 363 LEU B CD2 1 
ATOM   5019  N  N   . GLY B 1 300 ? 16.622 76.412 44.532  1.00 68.29  ? 364 GLY B N   1 
ATOM   5020  C  CA  . GLY B 1 300 ? 16.707 77.705 45.217  1.00 91.53  ? 364 GLY B CA  1 
ATOM   5021  C  C   . GLY B 1 300 ? 16.190 77.681 46.642  1.00 67.51  ? 364 GLY B C   1 
ATOM   5022  O  O   . GLY B 1 300 ? 15.986 76.611 47.199  1.00 80.09  ? 364 GLY B O   1 
ATOM   5023  N  N   . THR B 1 301 ? 15.975 78.864 47.218  1.00 57.81  ? 365 THR B N   1 
ATOM   5024  C  CA  . THR B 1 301 ? 15.706 78.997 48.641  1.00 55.83  ? 365 THR B CA  1 
ATOM   5025  C  C   . THR B 1 301 ? 14.347 78.465 49.076  1.00 52.25  ? 365 THR B C   1 
ATOM   5026  O  O   . THR B 1 301 ? 13.413 78.373 48.295  1.00 57.09  ? 365 THR B O   1 
ATOM   5027  C  CB  . THR B 1 301 ? 15.858 80.465 49.116  1.00 59.49  ? 365 THR B CB  1 
ATOM   5028  O  OG1 . THR B 1 301 ? 15.612 80.542 50.525  1.00 67.40  ? 365 THR B OG1 1 
ATOM   5029  C  CG2 . THR B 1 301 ? 14.884 81.375 48.406  1.00 67.96  ? 365 THR B CG2 1 
ATOM   5030  N  N   . LEU B 1 302 ? 14.270 78.121 50.351  1.00 56.67  ? 366 LEU B N   1 
ATOM   5031  C  CA  . LEU B 1 302 ? 13.045 77.731 50.994  1.00 56.21  ? 366 LEU B CA  1 
ATOM   5032  C  C   . LEU B 1 302 ? 12.262 78.953 51.404  1.00 53.17  ? 366 LEU B C   1 
ATOM   5033  O  O   . LEU B 1 302 ? 11.131 78.833 51.901  1.00 91.69  ? 366 LEU B O   1 
ATOM   5034  C  CB  . LEU B 1 302 ? 13.371 76.938 52.247  1.00 55.04  ? 366 LEU B CB  1 
ATOM   5035  C  CG  . LEU B 1 302 ? 14.184 75.690 52.003  1.00 64.21  ? 366 LEU B CG  1 
ATOM   5036  C  CD1 . LEU B 1 302 ? 15.522 75.953 52.586  1.00 94.21  ? 366 LEU B CD1 1 
ATOM   5037  C  CD2 . LEU B 1 302 ? 13.564 74.554 52.714  1.00 67.25  ? 366 LEU B CD2 1 
ATOM   5038  N  N   . PHE B 1 303 ? 12.860 80.126 51.199  1.00 52.18  ? 367 PHE B N   1 
ATOM   5039  C  CA  . PHE B 1 303 ? 12.323 81.363 51.750  1.00 58.91  ? 367 PHE B CA  1 
ATOM   5040  C  C   . PHE B 1 303 ? 11.704 82.289 50.722  1.00 62.58  ? 367 PHE B C   1 
ATOM   5041  O  O   . PHE B 1 303 ? 11.253 83.380 51.045  1.00 87.89  ? 367 PHE B O   1 
ATOM   5042  C  CB  . PHE B 1 303 ? 13.369 82.045 52.598  1.00 51.66  ? 367 PHE B CB  1 
ATOM   5043  C  CG  . PHE B 1 303 ? 13.969 81.130 53.618  1.00 61.78  ? 367 PHE B CG  1 
ATOM   5044  C  CD1 . PHE B 1 303 ? 13.165 80.465 54.553  1.00 60.46  ? 367 PHE B CD1 1 
ATOM   5045  C  CD2 . PHE B 1 303 ? 15.335 80.897 53.627  1.00 69.16  ? 367 PHE B CD2 1 
ATOM   5046  C  CE1 . PHE B 1 303 ? 13.730 79.589 55.491  1.00 54.84  ? 367 PHE B CE1 1 
ATOM   5047  C  CE2 . PHE B 1 303 ? 15.904 80.030 54.557  1.00 65.79  ? 367 PHE B CE2 1 
ATOM   5048  C  CZ  . PHE B 1 303 ? 15.098 79.376 55.489  1.00 51.90  ? 367 PHE B CZ  1 
ATOM   5049  N  N   . SER B 1 304 ? 11.658 81.817 49.489  1.00 55.15  ? 368 SER B N   1 
ATOM   5050  C  CA  . SER B 1 304 ? 10.878 82.450 48.466  1.00 66.33  ? 368 SER B CA  1 
ATOM   5051  C  C   . SER B 1 304 ? 9.607  81.646 48.228  1.00 84.41  ? 368 SER B C   1 
ATOM   5052  O  O   . SER B 1 304 ? 9.628  80.415 48.218  1.00 74.57  ? 368 SER B O   1 
ATOM   5053  C  CB  . SER B 1 304 ? 11.678 82.560 47.178  1.00 71.22  ? 368 SER B CB  1 
ATOM   5054  O  OG  . SER B 1 304 ? 10.980 83.337 46.221  1.00 83.83  ? 368 SER B OG  1 
ATOM   5055  N  N   . VAL B 1 305 ? 8.501  82.357 48.039  1.00 91.97  ? 369 VAL B N   1 
ATOM   5056  C  CA  . VAL B 1 305 ? 7.231  81.722 47.712  1.00 85.34  ? 369 VAL B CA  1 
ATOM   5057  C  C   . VAL B 1 305 ? 7.249  81.213 46.246  1.00 66.37  ? 369 VAL B C   1 
ATOM   5058  O  O   . VAL B 1 305 ? 6.358  80.479 45.791  1.00 63.64  ? 369 VAL B O   1 
ATOM   5059  C  CB  . VAL B 1 305 ? 6.087  82.706 47.981  1.00 66.79  ? 369 VAL B CB  1 
ATOM   5060  C  CG1 . VAL B 1 305 ? 6.176  83.875 47.026  1.00 88.54  ? 369 VAL B CG1 1 
ATOM   5061  C  CG2 . VAL B 1 305 ? 4.738  82.010 47.890  1.00 99.60  ? 369 VAL B CG2 1 
ATOM   5062  N  N   . GLN B 1 306 ? 8.299  81.604 45.535  1.00 62.06  ? 370 GLN B N   1 
ATOM   5063  C  CA  . GLN B 1 306 ? 8.440  81.361 44.106  1.00 81.91  ? 370 GLN B CA  1 
ATOM   5064  C  C   . GLN B 1 306 ? 8.892  79.938 43.781  1.00 84.46  ? 370 GLN B C   1 
ATOM   5065  O  O   . GLN B 1 306 ? 8.727  79.465 42.660  1.00 81.59  ? 370 GLN B O   1 
ATOM   5066  C  CB  . GLN B 1 306 ? 9.489  82.325 43.545  1.00 109.66 ? 370 GLN B CB  1 
ATOM   5067  C  CG  . GLN B 1 306 ? 9.027  83.741 43.317  1.00 100.55 ? 370 GLN B CG  1 
ATOM   5068  C  CD  . GLN B 1 306 ? 8.245  83.849 42.045  1.00 102.16 ? 370 GLN B CD  1 
ATOM   5069  O  OE1 . GLN B 1 306 ? 7.048  83.542 42.004  1.00 106.99 ? 370 GLN B OE1 1 
ATOM   5070  N  NE2 . GLN B 1 306 ? 8.919  84.269 40.981  1.00 82.95  ? 370 GLN B NE2 1 
ATOM   5071  N  N   . THR B 1 307 ? 9.475  79.272 44.767  1.00 79.35  ? 371 THR B N   1 
ATOM   5072  C  CA  . THR B 1 307 ? 10.320 78.130 44.500  1.00 73.12  ? 371 THR B CA  1 
ATOM   5073  C  C   . THR B 1 307 ? 9.548  76.828 44.433  1.00 79.23  ? 371 THR B C   1 
ATOM   5074  O  O   . THR B 1 307 ? 8.496  76.671 45.063  1.00 60.33  ? 371 THR B O   1 
ATOM   5075  C  CB  . THR B 1 307 ? 11.484 78.060 45.490  1.00 78.30  ? 371 THR B CB  1 
ATOM   5076  O  OG1 . THR B 1 307 ? 10.968 78.106 46.817  1.00 97.91  ? 371 THR B OG1 1 
ATOM   5077  C  CG2 . THR B 1 307 ? 12.396 79.275 45.292  1.00 68.46  ? 371 THR B CG2 1 
ATOM   5078  N  N   . VAL B 1 308 ? 10.117 75.900 43.671  1.00 89.43  ? 372 VAL B N   1 
ATOM   5079  C  CA  . VAL B 1 308 ? 9.395  74.803 43.053  1.00 78.75  ? 372 VAL B CA  1 
ATOM   5080  C  C   . VAL B 1 308 ? 9.908  73.470 43.602  1.00 93.50  ? 372 VAL B C   1 
ATOM   5081  O  O   . VAL B 1 308 ? 11.126 73.228 43.620  1.00 143.40 ? 372 VAL B O   1 
ATOM   5082  C  CB  . VAL B 1 308 ? 9.688  74.844 41.524  1.00 116.99 ? 372 VAL B CB  1 
ATOM   5083  C  CG1 . VAL B 1 308 ? 8.890  73.809 40.763  1.00 126.79 ? 372 VAL B CG1 1 
ATOM   5084  C  CG2 . VAL B 1 308 ? 9.428  76.229 40.959  1.00 133.76 ? 372 VAL B CG2 1 
ATOM   5085  N  N   . GLY B 1 309 ? 8.995  72.604 44.038  1.00 55.30  ? 373 GLY B N   1 
ATOM   5086  C  CA  . GLY B 1 309 ? 9.350  71.200 44.293  1.00 50.41  ? 373 GLY B CA  1 
ATOM   5087  C  C   . GLY B 1 309 ? 9.911  70.511 43.050  1.00 51.87  ? 373 GLY B C   1 
ATOM   5088  O  O   . GLY B 1 309 ? 9.479  70.780 41.942  1.00 72.00  ? 373 GLY B O   1 
ATOM   5089  N  N   . ASN B 1 310 ? 10.901 69.648 43.211  1.00 44.96  ? 374 ASN B N   1 
ATOM   5090  C  CA  . ASN B 1 310 ? 11.552 69.115 42.050  1.00 49.30  ? 374 ASN B CA  1 
ATOM   5091  C  C   . ASN B 1 310 ? 11.526 67.622 42.160  1.00 47.91  ? 374 ASN B C   1 
ATOM   5092  O  O   . ASN B 1 310 ? 11.069 66.947 41.252  1.00 70.59  ? 374 ASN B O   1 
ATOM   5093  C  CB  . ASN B 1 310 ? 12.994 69.668 41.891  1.00 53.60  ? 374 ASN B CB  1 
ATOM   5094  C  CG  . ASN B 1 310 ? 13.789 68.948 40.778  1.00 79.51  ? 374 ASN B CG  1 
ATOM   5095  O  OD1 . ASN B 1 310 ? 14.541 67.995 41.025  1.00 68.38  ? 374 ASN B OD1 1 
ATOM   5096  N  ND2 . ASN B 1 310 ? 13.594 69.389 39.547  1.00 122.41 ? 374 ASN B ND2 1 
ATOM   5097  N  N   . ARG B 1 311 ? 12.015 67.098 43.273  1.00 47.93  ? 375 ARG B N   1 
ATOM   5098  C  CA  . ARG B 1 311 ? 12.254 65.671 43.339  1.00 62.85  ? 375 ARG B CA  1 
ATOM   5099  C  C   . ARG B 1 311 ? 11.942 65.230 44.727  1.00 63.83  ? 375 ARG B C   1 
ATOM   5100  O  O   . ARG B 1 311 ? 12.390 65.839 45.677  1.00 90.60  ? 375 ARG B O   1 
ATOM   5101  C  CB  . ARG B 1 311 ? 13.701 65.298 42.942  1.00 53.88  ? 375 ARG B CB  1 
ATOM   5102  C  CG  . ARG B 1 311 ? 14.036 63.808 43.018  1.00 44.92  ? 375 ARG B CG  1 
ATOM   5103  C  CD  . ARG B 1 311 ? 13.406 63.074 41.875  1.00 50.26  ? 375 ARG B CD  1 
ATOM   5104  N  NE  . ARG B 1 311 ? 13.645 61.626 41.900  1.00 61.90  ? 375 ARG B NE  1 
ATOM   5105  C  CZ  . ARG B 1 311 ? 14.712 61.056 41.366  1.00 95.37  ? 375 ARG B CZ  1 
ATOM   5106  N  NH1 . ARG B 1 311 ? 15.632 61.816 40.774  1.00 126.69 ? 375 ARG B NH1 1 
ATOM   5107  N  NH2 . ARG B 1 311 ? 14.865 59.738 41.426  1.00 129.52 ? 375 ARG B NH2 1 
ATOM   5108  N  N   . ASN B 1 312 ? 11.162 64.169 44.836  1.00 58.77  ? 376 ASN B N   1 
ATOM   5109  C  CA  . ASN B 1 312 ? 10.878 63.570 46.118  1.00 48.22  ? 376 ASN B CA  1 
ATOM   5110  C  C   . ASN B 1 312 ? 11.440 62.169 46.221  1.00 43.40  ? 376 ASN B C   1 
ATOM   5111  O  O   . ASN B 1 312 ? 11.041 61.267 45.468  1.00 49.45  ? 376 ASN B O   1 
ATOM   5112  C  CB  . ASN B 1 312 ? 9.373  63.521 46.314  1.00 55.96  ? 376 ASN B CB  1 
ATOM   5113  C  CG  . ASN B 1 312 ? 8.963  62.586 47.433  1.00 58.31  ? 376 ASN B CG  1 
ATOM   5114  O  OD1 . ASN B 1 312 ? 8.723  61.394 47.229  1.00 82.66  ? 376 ASN B OD1 1 
ATOM   5115  N  ND2 . ASN B 1 312 ? 8.880  63.127 48.625  1.00 67.75  ? 376 ASN B ND2 1 
ATOM   5116  N  N   . TYR B 1 313 ? 12.350 61.988 47.162  1.00 43.20  ? 377 TYR B N   1 
ATOM   5117  C  CA  . TYR B 1 313 ? 12.914 60.688 47.460  1.00 42.34  ? 377 TYR B CA  1 
ATOM   5118  C  C   . TYR B 1 313 ? 12.207 60.098 48.664  1.00 43.73  ? 377 TYR B C   1 
ATOM   5119  O  O   . TYR B 1 313 ? 12.226 60.697 49.741  1.00 57.55  ? 377 TYR B O   1 
ATOM   5120  C  CB  . TYR B 1 313 ? 14.377 60.836 47.786  1.00 38.44  ? 377 TYR B CB  1 
ATOM   5121  C  CG  . TYR B 1 313 ? 15.253 61.218 46.640  1.00 48.58  ? 377 TYR B CG  1 
ATOM   5122  C  CD1 . TYR B 1 313 ? 15.738 62.512 46.522  1.00 55.55  ? 377 TYR B CD1 1 
ATOM   5123  C  CD2 . TYR B 1 313 ? 15.656 60.277 45.711  1.00 59.64  ? 377 TYR B CD2 1 
ATOM   5124  C  CE1 . TYR B 1 313 ? 16.598 62.865 45.493  1.00 71.52  ? 377 TYR B CE1 1 
ATOM   5125  C  CE2 . TYR B 1 313 ? 16.506 60.621 44.678  1.00 76.30  ? 377 TYR B CE2 1 
ATOM   5126  C  CZ  . TYR B 1 313 ? 16.974 61.918 44.572  1.00 77.55  ? 377 TYR B CZ  1 
ATOM   5127  O  OH  . TYR B 1 313 ? 17.822 62.275 43.550  1.00 105.97 ? 377 TYR B OH  1 
ATOM   5128  N  N   . GLN B 1 314 ? 11.612 58.918 48.498  1.00 46.38  ? 378 GLN B N   1 
ATOM   5129  C  CA  . GLN B 1 314 ? 11.069 58.174 49.629  1.00 53.23  ? 378 GLN B CA  1 
ATOM   5130  C  C   . GLN B 1 314 ? 12.078 57.220 50.182  1.00 48.54  ? 378 GLN B C   1 
ATOM   5131  O  O   . GLN B 1 314 ? 12.172 56.130 49.682  1.00 77.65  ? 378 GLN B O   1 
ATOM   5132  C  CB  . GLN B 1 314 ? 9.824  57.420 49.215  1.00 56.77  ? 378 GLN B CB  1 
ATOM   5133  C  CG  . GLN B 1 314 ? 8.672  58.402 49.000  1.00 131.08 ? 378 GLN B CG  1 
ATOM   5134  C  CD  . GLN B 1 314 ? 7.314  57.785 49.202  1.00 184.88 ? 378 GLN B CD  1 
ATOM   5135  O  OE1 . GLN B 1 314 ? 7.294  56.525 49.636  1.00 207.99 ? 378 GLN B OE1 1 
ATOM   5136  N  NE2 . GLN B 1 314 ? 6.285  58.429 48.970  1.00 188.91 ? 378 GLN B NE2 1 
ATOM   5137  N  N   . LEU B 1 315 ? 12.834 57.628 51.196  1.00 41.52  ? 379 LEU B N   1 
ATOM   5138  C  CA  . LEU B 1 315 ? 13.968 56.855 51.642  1.00 42.79  ? 379 LEU B CA  1 
ATOM   5139  C  C   . LEU B 1 315 ? 13.541 55.633 52.454  1.00 52.69  ? 379 LEU B C   1 
ATOM   5140  O  O   . LEU B 1 315 ? 14.082 54.539 52.284  1.00 46.90  ? 379 LEU B O   1 
ATOM   5141  C  CB  . LEU B 1 315 ? 14.920 57.725 52.451  1.00 36.58  ? 379 LEU B CB  1 
ATOM   5142  C  CG  . LEU B 1 315 ? 15.583 58.848 51.678  1.00 40.71  ? 379 LEU B CG  1 
ATOM   5143  C  CD1 . LEU B 1 315 ? 16.589 59.634 52.572  1.00 47.25  ? 379 LEU B CD1 1 
ATOM   5144  C  CD2 . LEU B 1 315 ? 16.261 58.301 50.432  1.00 39.67  ? 379 LEU B CD2 1 
ATOM   5145  N  N   . LEU B 1 316 ? 12.575 55.822 53.348  1.00 57.85  ? 380 LEU B N   1 
ATOM   5146  C  CA  . LEU B 1 316 ? 12.137 54.732 54.218  1.00 50.75  ? 380 LEU B CA  1 
ATOM   5147  C  C   . LEU B 1 316 ? 10.632 54.616 54.152  1.00 49.99  ? 380 LEU B C   1 
ATOM   5148  O  O   . LEU B 1 316 ? 9.933  55.626 54.127  1.00 57.40  ? 380 LEU B O   1 
ATOM   5149  C  CB  . LEU B 1 316 ? 12.535 54.997 55.663  1.00 67.24  ? 380 LEU B CB  1 
ATOM   5150  C  CG  . LEU B 1 316 ? 14.010 55.177 56.004  1.00 76.53  ? 380 LEU B CG  1 
ATOM   5151  C  CD1 . LEU B 1 316 ? 14.191 55.000 57.481  1.00 100.45 ? 380 LEU B CD1 1 
ATOM   5152  C  CD2 . LEU B 1 316 ? 14.885 54.192 55.237  1.00 65.26  ? 380 LEU B CD2 1 
ATOM   5153  N  N   . SER B 1 317 ? 10.141 53.385 54.124  1.00 56.36  ? 381 SER B N   1 
ATOM   5154  C  CA  . SER B 1 317 ? 8.716  53.098 53.978  1.00 51.99  ? 381 SER B CA  1 
ATOM   5155  C  C   . SER B 1 317 ? 8.199  52.238 55.098  1.00 57.09  ? 381 SER B C   1 
ATOM   5156  O  O   . SER B 1 317 ? 7.201  52.571 55.711  1.00 60.14  ? 381 SER B O   1 
ATOM   5157  C  CB  . SER B 1 317 ? 8.468  52.364 52.677  1.00 59.96  ? 381 SER B CB  1 
ATOM   5158  O  OG  . SER B 1 317 ? 9.047  53.081 51.603  1.00 132.40 ? 381 SER B OG  1 
ATOM   5159  N  N   . ASN B 1 318 ? 8.891  51.133 55.364  1.00 68.37  ? 382 ASN B N   1 
ATOM   5160  C  CA  . ASN B 1 318 ? 8.446  50.144 56.340  1.00 74.31  ? 382 ASN B CA  1 
ATOM   5161  C  C   . ASN B 1 318 ? 8.788  50.404 57.799  1.00 69.53  ? 382 ASN B C   1 
ATOM   5162  O  O   . ASN B 1 318 ? 8.409  49.620 58.649  1.00 89.18  ? 382 ASN B O   1 
ATOM   5163  C  CB  . ASN B 1 318 ? 8.980  48.764 55.955  1.00 111.01 ? 382 ASN B CB  1 
ATOM   5164  C  CG  . ASN B 1 318 ? 7.899  47.852 55.496  1.00 117.12 ? 382 ASN B CG  1 
ATOM   5165  O  OD1 . ASN B 1 318 ? 6.726  48.128 55.731  1.00 132.72 ? 382 ASN B OD1 1 
ATOM   5166  N  ND2 . ASN B 1 318 ? 8.272  46.750 54.841  1.00 150.40 ? 382 ASN B ND2 1 
ATOM   5167  N  N   . SER B 1 319 ? 9.493  51.493 58.092  1.00 70.84  ? 383 SER B N   1 
ATOM   5168  C  CA  . SER B 1 319 ? 10.059 51.726 59.436  1.00 68.93  ? 383 SER B CA  1 
ATOM   5169  C  C   . SER B 1 319 ? 9.362  52.855 60.204  1.00 60.85  ? 383 SER B C   1 
ATOM   5170  O  O   . SER B 1 319 ? 9.024  53.906 59.654  1.00 69.72  ? 383 SER B O   1 
ATOM   5171  C  CB  . SER B 1 319 ? 11.565 51.996 59.342  1.00 58.10  ? 383 SER B CB  1 
ATOM   5172  O  OG  . SER B 1 319 ? 12.064 51.481 58.116  1.00 94.76  ? 383 SER B OG  1 
ATOM   5173  N  N   . THR B 1 320 ? 9.137  52.628 61.484  1.00 51.15  ? 384 THR B N   1 
ATOM   5174  C  CA  . THR B 1 320 ? 8.562  53.647 62.341  1.00 54.16  ? 384 THR B CA  1 
ATOM   5175  C  C   . THR B 1 320 ? 9.599  54.696 62.766  1.00 55.74  ? 384 THR B C   1 
ATOM   5176  O  O   . THR B 1 320 ? 10.569 54.413 63.497  1.00 72.28  ? 384 THR B O   1 
ATOM   5177  C  CB  . THR B 1 320 ? 7.907  53.020 63.559  1.00 67.59  ? 384 THR B CB  1 
ATOM   5178  O  OG1 . THR B 1 320 ? 6.904  52.114 63.104  1.00 82.14  ? 384 THR B OG1 1 
ATOM   5179  C  CG2 . THR B 1 320 ? 7.251  54.085 64.436  1.00 62.44  ? 384 THR B CG2 1 
ATOM   5180  N  N   . ILE B 1 321 ? 9.349  55.921 62.324  1.00 42.36  ? 385 ILE B N   1 
ATOM   5181  C  CA  . ILE B 1 321 ? 10.294 57.013 62.452  1.00 40.78  ? 385 ILE B CA  1 
ATOM   5182  C  C   . ILE B 1 321 ? 10.016 57.991 63.594  1.00 53.72  ? 385 ILE B C   1 
ATOM   5183  O  O   . ILE B 1 321 ? 8.882  58.102 64.101  1.00 54.40  ? 385 ILE B O   1 
ATOM   5184  C  CB  . ILE B 1 321 ? 10.345 57.798 61.184  1.00 39.52  ? 385 ILE B CB  1 
ATOM   5185  C  CG1 . ILE B 1 321 ? 10.517 56.840 60.013  1.00 47.36  ? 385 ILE B CG1 1 
ATOM   5186  C  CG2 . ILE B 1 321 ? 11.476 58.765 61.206  1.00 34.30  ? 385 ILE B CG2 1 
ATOM   5187  C  CD1 . ILE B 1 321 ? 11.856 56.236 59.942  1.00 35.14  ? 385 ILE B CD1 1 
ATOM   5188  N  N   . GLY B 1 322 ? 11.092 58.686 63.987  1.00 52.49  ? 386 GLY B N   1 
ATOM   5189  C  CA  . GLY B 1 322 ? 11.090 59.620 65.088  1.00 47.03  ? 386 GLY B CA  1 
ATOM   5190  C  C   . GLY B 1 322 ? 11.942 60.829 64.788  1.00 55.66  ? 386 GLY B C   1 
ATOM   5191  O  O   . GLY B 1 322 ? 11.649 61.627 63.865  1.00 62.22  ? 386 GLY B O   1 
ATOM   5192  N  N   . ARG B 1 323 ? 13.000 60.994 65.568  1.00 45.97  ? 387 ARG B N   1 
ATOM   5193  C  CA  . ARG B 1 323 ? 13.783 62.204 65.401  1.00 50.48  ? 387 ARG B CA  1 
ATOM   5194  C  C   . ARG B 1 323 ? 14.678 62.026 64.180  1.00 43.73  ? 387 ARG B C   1 
ATOM   5195  O  O   . ARG B 1 323 ? 14.984 60.882 63.773  1.00 32.40  ? 387 ARG B O   1 
ATOM   5196  C  CB  . ARG B 1 323 ? 14.594 62.536 66.668  1.00 59.35  ? 387 ARG B CB  1 
ATOM   5197  C  CG  . ARG B 1 323 ? 13.772 62.686 67.951  1.00 43.97  ? 387 ARG B CG  1 
ATOM   5198  C  CD  . ARG B 1 323 ? 14.609 62.471 69.171  1.00 39.22  ? 387 ARG B CD  1 
ATOM   5199  N  NE  . ARG B 1 323 ? 15.784 63.332 69.167  1.00 61.13  ? 387 ARG B NE  1 
ATOM   5200  C  CZ  . ARG B 1 323 ? 17.050 62.935 68.979  1.00 56.63  ? 387 ARG B CZ  1 
ATOM   5201  N  NH1 . ARG B 1 323 ? 17.342 61.648 68.759  1.00 40.80  ? 387 ARG B NH1 1 
ATOM   5202  N  NH2 . ARG B 1 323 ? 18.025 63.853 69.012  1.00 47.81  ? 387 ARG B NH2 1 
ATOM   5203  N  N   . SER B 1 324 ? 15.077 63.160 63.602  1.00 40.02  ? 388 SER B N   1 
ATOM   5204  C  CA  . SER B 1 324 ? 16.025 63.208 62.475  1.00 43.43  ? 388 SER B CA  1 
ATOM   5205  C  C   . SER B 1 324 ? 16.863 64.457 62.679  1.00 42.22  ? 388 SER B C   1 
ATOM   5206  O  O   . SER B 1 324 ? 16.352 65.417 63.235  1.00 42.44  ? 388 SER B O   1 
ATOM   5207  C  CB  . SER B 1 324 ? 15.253 63.329 61.177  1.00 39.70  ? 388 SER B CB  1 
ATOM   5208  O  OG  . SER B 1 324 ? 13.976 63.959 61.403  1.00 59.70  ? 388 SER B OG  1 
ATOM   5209  N  N   . GLY B 1 325 ? 18.130 64.444 62.270  1.00 38.19  ? 389 GLY B N   1 
ATOM   5210  C  CA  . GLY B 1 325 ? 19.021 65.569 62.523  1.00 34.77  ? 389 GLY B CA  1 
ATOM   5211  C  C   . GLY B 1 325 ? 20.185 65.575 61.569  1.00 37.82  ? 389 GLY B C   1 
ATOM   5212  O  O   . GLY B 1 325 ? 20.477 64.586 60.944  1.00 40.84  ? 389 GLY B O   1 
ATOM   5213  N  N   . LEU B 1 326 ? 20.858 66.699 61.439  1.00 39.99  ? 390 LEU B N   1 
ATOM   5214  C  CA  . LEU B 1 326 ? 22.027 66.774 60.586  1.00 39.73  ? 390 LEU B CA  1 
ATOM   5215  C  C   . LEU B 1 326 ? 23.330 66.551 61.341  1.00 42.53  ? 390 LEU B C   1 
ATOM   5216  O  O   . LEU B 1 326 ? 23.362 66.503 62.568  1.00 48.07  ? 390 LEU B O   1 
ATOM   5217  C  CB  . LEU B 1 326 ? 22.096 68.152 59.983  1.00 41.12  ? 390 LEU B CB  1 
ATOM   5218  C  CG  . LEU B 1 326 ? 20.901 68.546 59.165  1.00 46.14  ? 390 LEU B CG  1 
ATOM   5219  C  CD1 . LEU B 1 326 ? 20.827 70.044 59.216  1.00 71.11  ? 390 LEU B CD1 1 
ATOM   5220  C  CD2 . LEU B 1 326 ? 21.093 68.096 57.763  1.00 50.59  ? 390 LEU B CD2 1 
ATOM   5221  N  N   . TYR B 1 327 ? 24.409 66.396 60.583  1.00 46.35  ? 391 TYR B N   1 
ATOM   5222  C  CA  . TYR B 1 327 ? 25.776 66.437 61.125  1.00 56.01  ? 391 TYR B CA  1 
ATOM   5223  C  C   . TYR B 1 327 ? 26.759 66.584 59.998  1.00 58.85  ? 391 TYR B C   1 
ATOM   5224  O  O   . TYR B 1 327 ? 26.502 66.102 58.906  1.00 63.35  ? 391 TYR B O   1 
ATOM   5225  C  CB  . TYR B 1 327 ? 26.142 65.208 61.972  1.00 44.73  ? 391 TYR B CB  1 
ATOM   5226  C  CG  . TYR B 1 327 ? 26.247 63.887 61.234  1.00 53.28  ? 391 TYR B CG  1 
ATOM   5227  C  CD1 . TYR B 1 327 ? 27.476 63.400 60.767  1.00 52.94  ? 391 TYR B CD1 1 
ATOM   5228  C  CD2 . TYR B 1 327 ? 25.120 63.089 61.046  1.00 58.98  ? 391 TYR B CD2 1 
ATOM   5229  C  CE1 . TYR B 1 327 ? 27.563 62.153 60.132  1.00 52.67  ? 391 TYR B CE1 1 
ATOM   5230  C  CE2 . TYR B 1 327 ? 25.200 61.858 60.398  1.00 57.47  ? 391 TYR B CE2 1 
ATOM   5231  C  CZ  . TYR B 1 327 ? 26.416 61.391 59.959  1.00 56.15  ? 391 TYR B CZ  1 
ATOM   5232  O  OH  . TYR B 1 327 ? 26.449 60.173 59.325  1.00 58.85  ? 391 TYR B OH  1 
ATOM   5233  N  N   . GLN B 1 328 ? 27.877 67.256 60.265  1.00 59.71  ? 392 GLN B N   1 
ATOM   5234  C  CA  . GLN B 1 328 ? 28.901 67.426 59.252  1.00 56.67  ? 392 GLN B CA  1 
ATOM   5235  C  C   . GLN B 1 328 ? 30.133 66.699 59.684  1.00 58.69  ? 392 GLN B C   1 
ATOM   5236  O  O   . GLN B 1 328 ? 30.724 67.014 60.730  1.00 89.48  ? 392 GLN B O   1 
ATOM   5237  C  CB  . GLN B 1 328 ? 29.219 68.899 59.001  1.00 70.47  ? 392 GLN B CB  1 
ATOM   5238  C  CG  . GLN B 1 328 ? 28.007 69.711 58.651  1.00 80.53  ? 392 GLN B CG  1 
ATOM   5239  C  CD  . GLN B 1 328 ? 28.332 71.148 58.458  1.00 80.01  ? 392 GLN B CD  1 
ATOM   5240  O  OE1 . GLN B 1 328 ? 28.492 71.889 59.422  1.00 80.08  ? 392 GLN B OE1 1 
ATOM   5241  N  NE2 . GLN B 1 328 ? 28.410 71.567 57.205  1.00 80.56  ? 392 GLN B NE2 1 
ATOM   5242  N  N   . PRO B 1 329 ? 30.513 65.691 58.900  1.00 51.24  ? 393 PRO B N   1 
ATOM   5243  C  CA  . PRO B 1 329 ? 31.790 65.032 59.084  1.00 53.54  ? 393 PRO B CA  1 
ATOM   5244  C  C   . PRO B 1 329 ? 32.921 65.938 58.604  1.00 63.46  ? 393 PRO B C   1 
ATOM   5245  O  O   . PRO B 1 329 ? 32.713 66.729 57.677  1.00 62.11  ? 393 PRO B O   1 
ATOM   5246  C  CB  . PRO B 1 329 ? 31.661 63.791 58.211  1.00 46.56  ? 393 PRO B CB  1 
ATOM   5247  C  CG  . PRO B 1 329 ? 30.595 64.081 57.263  1.00 42.57  ? 393 PRO B CG  1 
ATOM   5248  C  CD  . PRO B 1 329 ? 29.668 65.014 57.908  1.00 43.05  ? 393 PRO B CD  1 
ATOM   5249  N  N   . ALA B 1 330 ? 34.094 65.837 59.235  1.00 75.85  ? 394 ALA B N   1 
ATOM   5250  C  CA  . ALA B 1 330 ? 35.218 66.699 58.888  1.00 87.69  ? 394 ALA B CA  1 
ATOM   5251  C  C   . ALA B 1 330 ? 36.414 65.904 58.400  1.00 92.84  ? 394 ALA B C   1 
ATOM   5252  O  O   . ALA B 1 330 ? 36.893 65.022 59.104  1.00 96.13  ? 394 ALA B O   1 
ATOM   5253  C  CB  . ALA B 1 330 ? 35.601 67.566 60.073  1.00 91.41  ? 394 ALA B CB  1 
ATOM   5254  N  N   . TYR B 1 331 ? 36.866 66.209 57.182  1.00 139.97 ? 395 TYR B N   1 
ATOM   5255  C  CA  . TYR B 1 331 ? 38.117 65.672 56.622  1.00 175.42 ? 395 TYR B CA  1 
ATOM   5256  C  C   . TYR B 1 331 ? 38.797 66.756 55.797  1.00 203.48 ? 395 TYR B C   1 
ATOM   5257  O  O   . TYR B 1 331 ? 38.258 67.860 55.636  1.00 209.69 ? 395 TYR B O   1 
ATOM   5258  C  CB  . TYR B 1 331 ? 37.883 64.439 55.727  1.00 170.37 ? 395 TYR B CB  1 
ATOM   5259  C  CG  . TYR B 1 331 ? 36.708 63.576 56.117  1.00 177.78 ? 395 TYR B CG  1 
ATOM   5260  C  CD1 . TYR B 1 331 ? 36.813 62.647 57.162  1.00 154.89 ? 395 TYR B CD1 1 
ATOM   5261  C  CD2 . TYR B 1 331 ? 35.488 63.686 55.438  1.00 174.01 ? 395 TYR B CD2 1 
ATOM   5262  C  CE1 . TYR B 1 331 ? 35.729 61.858 57.529  1.00 164.73 ? 395 TYR B CE1 1 
ATOM   5263  C  CE2 . TYR B 1 331 ? 34.399 62.902 55.791  1.00 170.00 ? 395 TYR B CE2 1 
ATOM   5264  C  CZ  . TYR B 1 331 ? 34.527 61.990 56.836  1.00 191.81 ? 395 TYR B CZ  1 
ATOM   5265  O  OH  . TYR B 1 331 ? 33.453 61.209 57.187  1.00 191.37 ? 395 TYR B OH  1 
ATOM   5266  N  N   . GLU B 1 332 ? 39.982 66.438 55.277  1.00 211.29 ? 396 GLU B N   1 
ATOM   5267  C  CA  . GLU B 1 332 ? 40.640 67.293 54.301  1.00 229.99 ? 396 GLU B CA  1 
ATOM   5268  C  C   . GLU B 1 332 ? 39.746 67.374 53.067  1.00 246.81 ? 396 GLU B C   1 
ATOM   5269  O  O   . GLU B 1 332 ? 39.444 68.472 52.586  1.00 268.89 ? 396 GLU B O   1 
ATOM   5270  C  CB  . GLU B 1 332 ? 42.028 66.746 53.945  1.00 213.37 ? 396 GLU B CB  1 
ATOM   5271  C  CG  . GLU B 1 332 ? 42.871 67.664 53.054  1.00 215.73 ? 396 GLU B CG  1 
ATOM   5272  C  CD  . GLU B 1 332 ? 42.500 67.575 51.581  1.00 208.87 ? 396 GLU B CD  1 
ATOM   5273  O  OE1 . GLU B 1 332 ? 42.421 66.445 51.053  1.00 218.80 ? 396 GLU B OE1 1 
ATOM   5274  O  OE2 . GLU B 1 332 ? 42.290 68.635 50.952  1.00 185.01 ? 396 GLU B OE2 1 
ATOM   5275  N  N   . SER B 1 333 ? 39.308 66.207 52.588  1.00 222.60 ? 397 SER B N   1 
ATOM   5276  C  CA  . SER B 1 333 ? 38.456 66.093 51.403  1.00 208.34 ? 397 SER B CA  1 
ATOM   5277  C  C   . SER B 1 333 ? 38.856 67.131 50.359  1.00 207.78 ? 397 SER B C   1 
ATOM   5278  O  O   . SER B 1 333 ? 39.925 67.024 49.756  1.00 214.39 ? 397 SER B O   1 
ATOM   5279  C  CB  . SER B 1 333 ? 36.975 66.225 51.778  1.00 207.55 ? 397 SER B CB  1 
ATOM   5280  O  OG  . SER B 1 333 ? 36.563 65.155 52.610  1.00 217.91 ? 397 SER B OG  1 
ATOM   5281  N  N   . ARG B 1 334 ? 38.007 68.138 50.167  1.00 184.24 ? 398 ARG B N   1 
ATOM   5282  C  CA  . ARG B 1 334 ? 38.341 69.285 49.321  1.00 195.89 ? 398 ARG B CA  1 
ATOM   5283  C  C   . ARG B 1 334 ? 37.553 70.520 49.733  1.00 168.02 ? 398 ARG B C   1 
ATOM   5284  O  O   . ARG B 1 334 ? 36.942 70.533 50.802  1.00 135.94 ? 398 ARG B O   1 
ATOM   5285  C  CB  . ARG B 1 334 ? 38.151 68.969 47.827  1.00 221.95 ? 398 ARG B CB  1 
ATOM   5286  C  CG  . ARG B 1 334 ? 36.836 68.286 47.446  1.00 210.11 ? 398 ARG B CG  1 
ATOM   5287  C  CD  . ARG B 1 334 ? 36.686 68.205 45.928  1.00 214.95 ? 398 ARG B CD  1 
ATOM   5288  N  NE  . ARG B 1 334 ? 37.920 67.772 45.270  1.00 219.36 ? 398 ARG B NE  1 
ATOM   5289  C  CZ  . ARG B 1 334 ? 38.062 67.593 43.959  1.00 195.44 ? 398 ARG B CZ  1 
ATOM   5290  N  NH1 . ARG B 1 334 ? 37.042 67.800 43.136  1.00 180.78 ? 398 ARG B NH1 1 
ATOM   5291  N  NH2 . ARG B 1 334 ? 39.231 67.200 43.471  1.00 207.22 ? 398 ARG B NH2 1 
ATOM   5292  N  N   . ASP B 1 335 ? 37.581 71.551 48.885  1.00 181.73 ? 399 ASP B N   1 
ATOM   5293  C  CA  . ASP B 1 335 ? 36.837 72.800 49.109  1.00 196.73 ? 399 ASP B CA  1 
ATOM   5294  C  C   . ASP B 1 335 ? 35.407 72.543 49.592  1.00 166.87 ? 399 ASP B C   1 
ATOM   5295  O  O   . ASP B 1 335 ? 34.780 73.384 50.247  1.00 153.63 ? 399 ASP B O   1 
ATOM   5296  C  CB  . ASP B 1 335 ? 36.805 73.633 47.821  1.00 208.18 ? 399 ASP B CB  1 
ATOM   5297  C  CG  . ASP B 1 335 ? 38.178 74.125 47.405  1.00 207.63 ? 399 ASP B CG  1 
ATOM   5298  O  OD1 . ASP B 1 335 ? 39.116 74.073 48.231  1.00 198.31 ? 399 ASP B OD1 1 
ATOM   5299  O  OD2 . ASP B 1 335 ? 38.317 74.570 46.247  1.00 256.63 ? 399 ASP B OD2 1 
ATOM   5300  N  N   . CYS B 1 336 ? 34.927 71.352 49.263  1.00 131.70 ? 400 CYS B N   1 
ATOM   5301  C  CA  . CYS B 1 336 ? 33.583 70.904 49.530  1.00 92.52  ? 400 CYS B CA  1 
ATOM   5302  C  C   . CYS B 1 336 ? 33.374 70.456 50.979  1.00 87.33  ? 400 CYS B C   1 
ATOM   5303  O  O   . CYS B 1 336 ? 34.064 69.556 51.472  1.00 91.49  ? 400 CYS B O   1 
ATOM   5304  C  CB  . CYS B 1 336 ? 33.306 69.734 48.592  1.00 122.28 ? 400 CYS B CB  1 
ATOM   5305  S  SG  . CYS B 1 336 ? 31.641 69.636 48.040  1.00 197.50 ? 400 CYS B SG  1 
ATOM   5306  N  N   . GLN B 1 337 ? 32.399 71.063 51.655  1.00 88.16  ? 401 GLN B N   1 
ATOM   5307  C  CA  . GLN B 1 337 ? 31.972 70.580 52.978  1.00 90.80  ? 401 GLN B CA  1 
ATOM   5308  C  C   . GLN B 1 337 ? 30.843 69.542 52.923  1.00 88.45  ? 401 GLN B C   1 
ATOM   5309  O  O   . GLN B 1 337 ? 29.712 69.862 52.553  1.00 75.47  ? 401 GLN B O   1 
ATOM   5310  C  CB  . GLN B 1 337 ? 31.556 71.739 53.885  1.00 88.79  ? 401 GLN B CB  1 
ATOM   5311  C  CG  . GLN B 1 337 ? 31.154 71.313 55.305  1.00 93.91  ? 401 GLN B CG  1 
ATOM   5312  C  CD  . GLN B 1 337 ? 32.046 70.227 55.884  1.00 91.26  ? 401 GLN B CD  1 
ATOM   5313  O  OE1 . GLN B 1 337 ? 33.270 70.346 55.892  1.00 135.55 ? 401 GLN B OE1 1 
ATOM   5314  N  NE2 . GLN B 1 337 ? 31.432 69.162 56.367  1.00 90.00  ? 401 GLN B NE2 1 
ATOM   5315  N  N   . GLU B 1 338 ? 31.160 68.309 53.318  1.00 86.53  ? 402 GLU B N   1 
ATOM   5316  C  CA  . GLU B 1 338 ? 30.186 67.220 53.305  1.00 81.48  ? 402 GLU B CA  1 
ATOM   5317  C  C   . GLU B 1 338 ? 29.047 67.460 54.309  1.00 64.91  ? 402 GLU B C   1 
ATOM   5318  O  O   . GLU B 1 338 ? 29.249 68.090 55.339  1.00 68.15  ? 402 GLU B O   1 
ATOM   5319  C  CB  . GLU B 1 338 ? 30.882 65.880 53.566  1.00 95.75  ? 402 GLU B CB  1 
ATOM   5320  C  CG  . GLU B 1 338 ? 29.996 64.634 53.362  1.00 125.18 ? 402 GLU B CG  1 
ATOM   5321  C  CD  . GLU B 1 338 ? 30.228 63.916 52.031  1.00 155.40 ? 402 GLU B CD  1 
ATOM   5322  O  OE1 . GLU B 1 338 ? 31.395 63.849 51.581  1.00 187.98 ? 402 GLU B OE1 1 
ATOM   5323  O  OE2 . GLU B 1 338 ? 29.246 63.393 51.449  1.00 127.01 ? 402 GLU B OE2 1 
ATOM   5324  N  N   . LEU B 1 339 ? 27.848 66.977 53.981  1.00 57.82  ? 403 LEU B N   1 
ATOM   5325  C  CA  . LEU B 1 339 ? 26.657 67.120 54.836  1.00 51.85  ? 403 LEU B CA  1 
ATOM   5326  C  C   . LEU B 1 339 ? 25.830 65.821 54.912  1.00 52.40  ? 403 LEU B C   1 
ATOM   5327  O  O   . LEU B 1 339 ? 25.439 65.271 53.891  1.00 75.51  ? 403 LEU B O   1 
ATOM   5328  C  CB  . LEU B 1 339 ? 25.785 68.281 54.357  1.00 47.59  ? 403 LEU B CB  1 
ATOM   5329  C  CG  . LEU B 1 339 ? 24.571 68.581 55.230  1.00 46.66  ? 403 LEU B CG  1 
ATOM   5330  C  CD1 . LEU B 1 339 ? 25.004 68.913 56.634  1.00 51.89  ? 403 LEU B CD1 1 
ATOM   5331  C  CD2 . LEU B 1 339 ? 23.821 69.730 54.662  1.00 41.67  ? 403 LEU B CD2 1 
ATOM   5332  N  N   . CYS B 1 340 ? 25.593 65.322 56.120  1.00 50.77  ? 404 CYS B N   1 
ATOM   5333  C  CA  . CYS B 1 340 ? 24.930 64.032 56.331  1.00 46.31  ? 404 CYS B CA  1 
ATOM   5334  C  C   . CYS B 1 340 ? 23.811 64.241 57.324  1.00 47.12  ? 404 CYS B C   1 
ATOM   5335  O  O   . CYS B 1 340 ? 23.769 65.244 58.045  1.00 55.69  ? 404 CYS B O   1 
ATOM   5336  C  CB  . CYS B 1 340 ? 25.899 62.986 56.874  1.00 43.55  ? 404 CYS B CB  1 
ATOM   5337  S  SG  . CYS B 1 340 ? 27.299 62.743 55.819  1.00 82.27  ? 404 CYS B SG  1 
ATOM   5338  N  N   . PHE B 1 341 ? 22.897 63.297 57.380  1.00 38.00  ? 405 PHE B N   1 
ATOM   5339  C  CA  . PHE B 1 341 ? 21.902 63.373 58.437  1.00 46.88  ? 405 PHE B CA  1 
ATOM   5340  C  C   . PHE B 1 341 ? 21.537 61.981 58.920  1.00 47.07  ? 405 PHE B C   1 
ATOM   5341  O  O   . PHE B 1 341 ? 21.721 61.000 58.205  1.00 65.03  ? 405 PHE B O   1 
ATOM   5342  C  CB  . PHE B 1 341 ? 20.646 64.146 57.998  1.00 49.22  ? 405 PHE B CB  1 
ATOM   5343  C  CG  . PHE B 1 341 ? 19.810 63.411 56.965  1.00 56.19  ? 405 PHE B CG  1 
ATOM   5344  C  CD1 . PHE B 1 341 ? 20.060 63.561 55.605  1.00 66.88  ? 405 PHE B CD1 1 
ATOM   5345  C  CD2 . PHE B 1 341 ? 18.806 62.545 57.345  1.00 54.35  ? 405 PHE B CD2 1 
ATOM   5346  C  CE1 . PHE B 1 341 ? 19.328 62.856 54.657  1.00 57.68  ? 405 PHE B CE1 1 
ATOM   5347  C  CE2 . PHE B 1 341 ? 18.062 61.837 56.377  1.00 54.54  ? 405 PHE B CE2 1 
ATOM   5348  C  CZ  . PHE B 1 341 ? 18.335 61.984 55.054  1.00 53.59  ? 405 PHE B CZ  1 
ATOM   5349  N  N   . TRP B 1 342 ? 21.016 61.915 60.136  1.00 43.41  ? 406 TRP B N   1 
ATOM   5350  C  CA  . TRP B 1 342 ? 20.630 60.670 60.790  1.00 45.38  ? 406 TRP B CA  1 
ATOM   5351  C  C   . TRP B 1 342 ? 19.151 60.681 61.056  1.00 54.16  ? 406 TRP B C   1 
ATOM   5352  O  O   . TRP B 1 342 ? 18.496 61.738 61.136  1.00 59.45  ? 406 TRP B O   1 
ATOM   5353  C  CB  . TRP B 1 342 ? 21.368 60.474 62.111  1.00 36.58  ? 406 TRP B CB  1 
ATOM   5354  C  CG  . TRP B 1 342 ? 21.225 61.655 63.048  1.00 42.09  ? 406 TRP B CG  1 
ATOM   5355  C  CD1 . TRP B 1 342 ? 22.120 62.724 63.245  1.00 50.41  ? 406 TRP B CD1 1 
ATOM   5356  C  CD2 . TRP B 1 342 ? 20.108 61.939 63.939  1.00 47.39  ? 406 TRP B CD2 1 
ATOM   5357  N  NE1 . TRP B 1 342 ? 21.642 63.603 64.174  1.00 46.85  ? 406 TRP B NE1 1 
ATOM   5358  C  CE2 . TRP B 1 342 ? 20.435 63.181 64.636  1.00 45.63  ? 406 TRP B CE2 1 
ATOM   5359  C  CE3 . TRP B 1 342 ? 18.913 61.306 64.232  1.00 59.06  ? 406 TRP B CE3 1 
ATOM   5360  C  CZ2 . TRP B 1 342 ? 19.586 63.732 65.580  1.00 42.23  ? 406 TRP B CZ2 1 
ATOM   5361  C  CZ3 . TRP B 1 342 ? 18.066 61.885 65.189  1.00 45.75  ? 406 TRP B CZ3 1 
ATOM   5362  C  CH2 . TRP B 1 342 ? 18.403 63.065 65.840  1.00 38.37  ? 406 TRP B CH2 1 
ATOM   5363  N  N   . ILE B 1 343 ? 18.620 59.483 61.220  1.00 44.03  ? 407 ILE B N   1 
ATOM   5364  C  CA  . ILE B 1 343 ? 17.239 59.293 61.511  1.00 44.13  ? 407 ILE B CA  1 
ATOM   5365  C  C   . ILE B 1 343 ? 17.146 58.178 62.523  1.00 45.05  ? 407 ILE B C   1 
ATOM   5366  O  O   . ILE B 1 343 ? 17.714 57.097 62.350  1.00 50.62  ? 407 ILE B O   1 
ATOM   5367  C  CB  . ILE B 1 343 ? 16.494 58.835 60.270  1.00 47.86  ? 407 ILE B CB  1 
ATOM   5368  C  CG1 . ILE B 1 343 ? 16.737 59.801 59.117  1.00 46.96  ? 407 ILE B CG1 1 
ATOM   5369  C  CG2 . ILE B 1 343 ? 14.996 58.673 60.566  1.00 45.20  ? 407 ILE B CG2 1 
ATOM   5370  C  CD1 . ILE B 1 343 ? 15.997 59.408 57.847  1.00 52.19  ? 407 ILE B CD1 1 
ATOM   5371  N  N   . GLU B 1 344 ? 16.387 58.439 63.568  1.00 48.74  ? 408 GLU B N   1 
ATOM   5372  C  CA  . GLU B 1 344 ? 16.208 57.502 64.661  1.00 46.46  ? 408 GLU B CA  1 
ATOM   5373  C  C   . GLU B 1 344 ? 14.950 56.684 64.402  1.00 56.56  ? 408 GLU B C   1 
ATOM   5374  O  O   . GLU B 1 344 ? 13.901 57.181 63.942  1.00 60.72  ? 408 GLU B O   1 
ATOM   5375  C  CB  . GLU B 1 344 ? 16.084 58.300 65.946  1.00 50.44  ? 408 GLU B CB  1 
ATOM   5376  C  CG  . GLU B 1 344 ? 16.048 57.534 67.233  1.00 69.84  ? 408 GLU B CG  1 
ATOM   5377  C  CD  . GLU B 1 344 ? 15.706 58.452 68.408  1.00 99.26  ? 408 GLU B CD  1 
ATOM   5378  O  OE1 . GLU B 1 344 ? 16.505 58.529 69.386  1.00 98.13  ? 408 GLU B OE1 1 
ATOM   5379  O  OE2 . GLU B 1 344 ? 14.639 59.113 68.318  1.00 85.35  ? 408 GLU B OE2 1 
ATOM   5380  N  N   . ILE B 1 345 ? 15.054 55.410 64.699  1.00 53.72  ? 409 ILE B N   1 
ATOM   5381  C  CA  . ILE B 1 345 ? 14.047 54.469 64.269  1.00 51.60  ? 409 ILE B CA  1 
ATOM   5382  C  C   . ILE B 1 345 ? 13.661 53.602 65.427  1.00 48.94  ? 409 ILE B C   1 
ATOM   5383  O  O   . ILE B 1 345 ? 14.537 53.091 66.108  1.00 52.64  ? 409 ILE B O   1 
ATOM   5384  C  CB  . ILE B 1 345 ? 14.678 53.572 63.218  1.00 61.11  ? 409 ILE B CB  1 
ATOM   5385  C  CG1 . ILE B 1 345 ? 14.833 54.347 61.907  1.00 54.88  ? 409 ILE B CG1 1 
ATOM   5386  C  CG2 . ILE B 1 345 ? 13.895 52.281 63.048  1.00 64.79  ? 409 ILE B CG2 1 
ATOM   5387  C  CD1 . ILE B 1 345 ? 15.322 53.482 60.775  1.00 71.44  ? 409 ILE B CD1 1 
ATOM   5388  N  N   . ALA B 1 346 ? 12.366 53.429 65.664  1.00 48.35  ? 410 ALA B N   1 
ATOM   5389  C  CA  . ALA B 1 346 ? 11.904 52.467 66.681  1.00 48.52  ? 410 ALA B CA  1 
ATOM   5390  C  C   . ALA B 1 346 ? 12.523 51.059 66.491  1.00 42.99  ? 410 ALA B C   1 
ATOM   5391  O  O   . ALA B 1 346 ? 12.589 50.546 65.396  1.00 43.37  ? 410 ALA B O   1 
ATOM   5392  C  CB  . ALA B 1 346 ? 10.407 52.365 66.641  1.00 47.73  ? 410 ALA B CB  1 
ATOM   5393  N  N   . ALA B 1 347 ? 12.985 50.448 67.565  1.00 46.24  ? 411 ALA B N   1 
ATOM   5394  C  CA  . ALA B 1 347 ? 13.433 49.064 67.534  1.00 54.50  ? 411 ALA B CA  1 
ATOM   5395  C  C   . ALA B 1 347 ? 12.638 48.302 68.577  1.00 64.36  ? 411 ALA B C   1 
ATOM   5396  O  O   . ALA B 1 347 ? 11.665 48.824 69.134  1.00 73.06  ? 411 ALA B O   1 
ATOM   5397  C  CB  . ALA B 1 347 ? 14.925 48.978 67.845  1.00 57.04  ? 411 ALA B CB  1 
ATOM   5398  N  N   . THR B 1 348 ? 13.035 47.057 68.809  1.00 74.53  ? 412 THR B N   1 
ATOM   5399  C  CA  . THR B 1 348 ? 12.566 46.291 69.960  1.00 80.09  ? 412 THR B CA  1 
ATOM   5400  C  C   . THR B 1 348 ? 13.674 45.321 70.341  1.00 69.29  ? 412 THR B C   1 
ATOM   5401  O  O   . THR B 1 348 ? 14.406 44.833 69.487  1.00 67.31  ? 412 THR B O   1 
ATOM   5402  C  CB  . THR B 1 348 ? 11.181 45.531 69.734  1.00 78.87  ? 412 THR B CB  1 
ATOM   5403  O  OG1 . THR B 1 348 ? 11.289 44.596 68.659  1.00 88.00  ? 412 THR B OG1 1 
ATOM   5404  C  CG2 . THR B 1 348 ? 9.983  46.495 69.444  1.00 71.83  ? 412 THR B CG2 1 
ATOM   5405  N  N   . THR B 1 349 ? 13.811 45.067 71.631  1.00 70.76  ? 413 THR B N   1 
ATOM   5406  C  CA  . THR B 1 349 ? 14.719 44.047 72.124  1.00 61.80  ? 413 THR B CA  1 
ATOM   5407  C  C   . THR B 1 349 ? 14.183 42.670 71.767  1.00 64.69  ? 413 THR B C   1 
ATOM   5408  O  O   . THR B 1 349 ? 13.010 42.527 71.453  1.00 70.41  ? 413 THR B O   1 
ATOM   5409  C  CB  . THR B 1 349 ? 14.886 44.228 73.635  1.00 66.36  ? 413 THR B CB  1 
ATOM   5410  O  OG1 . THR B 1 349 ? 15.570 45.465 73.849  1.00 70.74  ? 413 THR B OG1 1 
ATOM   5411  C  CG2 . THR B 1 349 ? 15.695 43.112 74.290  1.00 105.91 ? 413 THR B CG2 1 
ATOM   5412  N  N   . LYS B 1 350 ? 15.055 41.663 71.796  1.00 101.55 ? 414 LYS B N   1 
ATOM   5413  C  CA  . LYS B 1 350 ? 14.683 40.256 71.587  1.00 111.64 ? 414 LYS B CA  1 
ATOM   5414  C  C   . LYS B 1 350 ? 13.405 39.870 72.339  1.00 109.94 ? 414 LYS B C   1 
ATOM   5415  O  O   . LYS B 1 350 ? 12.705 38.958 71.915  1.00 109.54 ? 414 LYS B O   1 
ATOM   5416  C  CB  . LYS B 1 350 ? 15.848 39.337 71.991  1.00 115.96 ? 414 LYS B CB  1 
ATOM   5417  C  CG  . LYS B 1 350 ? 15.664 37.843 71.757  1.00 105.59 ? 414 LYS B CG  1 
ATOM   5418  C  CD  . LYS B 1 350 ? 16.739 37.048 72.502  1.00 138.30 ? 414 LYS B CD  1 
ATOM   5419  C  CE  . LYS B 1 350 ? 16.534 35.541 72.360  1.00 135.85 ? 414 LYS B CE  1 
ATOM   5420  N  NZ  . LYS B 1 350 ? 17.672 34.742 72.912  1.00 138.51 ? 414 LYS B NZ  1 
ATOM   5421  N  N   . ALA B 1 351 ? 13.097 40.564 73.436  1.00 99.15  ? 415 ALA B N   1 
ATOM   5422  C  CA  . ALA B 1 351 ? 11.837 40.345 74.134  1.00 94.88  ? 415 ALA B CA  1 
ATOM   5423  C  C   . ALA B 1 351 ? 11.199 41.651 74.595  1.00 102.09 ? 415 ALA B C   1 
ATOM   5424  O  O   . ALA B 1 351 ? 11.428 42.054 75.730  1.00 129.50 ? 415 ALA B O   1 
ATOM   5425  C  CB  . ALA B 1 351 ? 12.071 39.437 75.311  1.00 84.47  ? 415 ALA B CB  1 
ATOM   5426  N  N   . GLY B 1 352 ? 10.418 42.308 73.724  1.00 86.25  ? 416 GLY B N   1 
ATOM   5427  C  CA  . GLY B 1 352 ? 9.724  43.583 74.052  1.00 79.61  ? 416 GLY B CA  1 
ATOM   5428  C  C   . GLY B 1 352 ? 10.693 44.737 74.128  1.00 79.39  ? 416 GLY B C   1 
ATOM   5429  O  O   . GLY B 1 352 ? 11.816 44.602 73.671  1.00 93.63  ? 416 GLY B O   1 
ATOM   5430  N  N   . LEU B 1 353 ? 10.274 45.871 74.698  1.00 95.97  ? 417 LEU B N   1 
ATOM   5431  C  CA  . LEU B 1 353 ? 11.168 47.036 74.960  1.00 89.50  ? 417 LEU B CA  1 
ATOM   5432  C  C   . LEU B 1 353 ? 11.423 47.879 73.712  1.00 98.51  ? 417 LEU B C   1 
ATOM   5433  O  O   . LEU B 1 353 ? 11.548 47.339 72.623  1.00 113.82 ? 417 LEU B O   1 
ATOM   5434  C  CB  . LEU B 1 353 ? 12.502 46.604 75.605  1.00 69.27  ? 417 LEU B CB  1 
ATOM   5435  C  CG  . LEU B 1 353 ? 12.430 45.397 76.570  1.00 72.33  ? 417 LEU B CG  1 
ATOM   5436  C  CD1 . LEU B 1 353 ? 13.780 44.794 76.916  1.00 88.29  ? 417 LEU B CD1 1 
ATOM   5437  C  CD2 . LEU B 1 353 ? 11.720 45.686 77.857  1.00 70.28  ? 417 LEU B CD2 1 
ATOM   5438  N  N   . SER B 1 354 ? 11.514 49.197 73.870  1.00 88.63  ? 418 SER B N   1 
ATOM   5439  C  CA  . SER B 1 354 ? 11.508 50.080 72.716  1.00 93.34  ? 418 SER B CA  1 
ATOM   5440  C  C   . SER B 1 354 ? 12.797 50.870 72.622  1.00 89.76  ? 418 SER B C   1 
ATOM   5441  O  O   . SER B 1 354 ? 12.794 52.091 72.707  1.00 151.96 ? 418 SER B O   1 
ATOM   5442  C  CB  . SER B 1 354 ? 10.289 51.012 72.760  1.00 104.43 ? 418 SER B CB  1 
ATOM   5443  O  OG  . SER B 1 354 ? 10.295 51.793 73.945  1.00 163.51 ? 418 SER B OG  1 
ATOM   5444  N  N   . SER B 1 355 ? 13.908 50.185 72.438  1.00 89.54  ? 419 SER B N   1 
ATOM   5445  C  CA  . SER B 1 355 ? 15.118 50.899 72.091  1.00 95.73  ? 419 SER B CA  1 
ATOM   5446  C  C   . SER B 1 355 ? 14.917 51.549 70.705  1.00 74.20  ? 419 SER B C   1 
ATOM   5447  O  O   . SER B 1 355 ? 14.034 51.160 69.952  1.00 93.15  ? 419 SER B O   1 
ATOM   5448  C  CB  . SER B 1 355 ? 16.322 49.948 72.128  1.00 106.29 ? 419 SER B CB  1 
ATOM   5449  O  OG  . SER B 1 355 ? 17.555 50.648 72.036  1.00 110.04 ? 419 SER B OG  1 
ATOM   5450  N  N   . ASN B 1 356 ? 15.712 52.564 70.399  1.00 63.37  ? 420 ASN B N   1 
ATOM   5451  C  CA  . ASN B 1 356 ? 15.764 53.135 69.066  1.00 57.24  ? 420 ASN B CA  1 
ATOM   5452  C  C   . ASN B 1 356 ? 17.115 52.829 68.414  1.00 56.82  ? 420 ASN B C   1 
ATOM   5453  O  O   . ASN B 1 356 ? 18.105 52.696 69.108  1.00 71.82  ? 420 ASN B O   1 
ATOM   5454  C  CB  . ASN B 1 356 ? 15.577 54.654 69.118  1.00 58.50  ? 420 ASN B CB  1 
ATOM   5455  C  CG  . ASN B 1 356 ? 14.540 55.077 70.095  1.00 62.79  ? 420 ASN B CG  1 
ATOM   5456  O  OD1 . ASN B 1 356 ? 14.754 55.027 71.281  1.00 58.66  ? 420 ASN B OD1 1 
ATOM   5457  N  ND2 . ASN B 1 356 ? 13.409 55.515 69.603  1.00 69.41  ? 420 ASN B ND2 1 
ATOM   5458  N  N   . ASP B 1 357 ? 17.144 52.691 67.088  1.00 57.30  ? 421 ASP B N   1 
ATOM   5459  C  CA  . ASP B 1 357 ? 18.406 52.682 66.350  1.00 61.25  ? 421 ASP B CA  1 
ATOM   5460  C  C   . ASP B 1 357 ? 18.564 53.807 65.299  1.00 61.41  ? 421 ASP B C   1 
ATOM   5461  O  O   . ASP B 1 357 ? 17.646 54.609 65.047  1.00 67.84  ? 421 ASP B O   1 
ATOM   5462  C  CB  . ASP B 1 357 ? 18.704 51.314 65.749  1.00 54.66  ? 421 ASP B CB  1 
ATOM   5463  C  CG  . ASP B 1 357 ? 20.152 50.873 66.014  1.00 96.07  ? 421 ASP B CG  1 
ATOM   5464  O  OD1 . ASP B 1 357 ? 21.081 51.714 65.928  1.00 110.83 ? 421 ASP B OD1 1 
ATOM   5465  O  OD2 . ASP B 1 357 ? 20.367 49.681 66.325  1.00 110.30 ? 421 ASP B OD2 1 
ATOM   5466  N  N   . LEU B 1 358 ? 19.741 53.852 64.690  1.00 49.85  ? 422 LEU B N   1 
ATOM   5467  C  CA  . LEU B 1 358 ? 20.088 54.916 63.781  1.00 45.54  ? 422 LEU B CA  1 
ATOM   5468  C  C   . LEU B 1 358 ? 20.296 54.393 62.393  1.00 51.06  ? 422 LEU B C   1 
ATOM   5469  O  O   . LEU B 1 358 ? 20.741 53.241 62.184  1.00 46.93  ? 422 LEU B O   1 
ATOM   5470  C  CB  . LEU B 1 358 ? 21.394 55.555 64.197  1.00 51.09  ? 422 LEU B CB  1 
ATOM   5471  C  CG  . LEU B 1 358 ? 21.284 56.632 65.226  1.00 48.72  ? 422 LEU B CG  1 
ATOM   5472  C  CD1 . LEU B 1 358 ? 22.575 57.374 65.244  1.00 60.45  ? 422 LEU B CD1 1 
ATOM   5473  C  CD2 . LEU B 1 358 ? 20.182 57.516 64.759  1.00 62.09  ? 422 LEU B CD2 1 
ATOM   5474  N  N   . ILE B 1 359 ? 19.955 55.263 61.449  1.00 47.82  ? 423 ILE B N   1 
ATOM   5475  C  CA  . ILE B 1 359 ? 20.391 55.128 60.079  1.00 46.24  ? 423 ILE B CA  1 
ATOM   5476  C  C   . ILE B 1 359 ? 20.848 56.500 59.619  1.00 48.03  ? 423 ILE B C   1 
ATOM   5477  O  O   . ILE B 1 359 ? 20.261 57.505 59.974  1.00 53.80  ? 423 ILE B O   1 
ATOM   5478  C  CB  . ILE B 1 359 ? 19.310 54.561 59.204  1.00 40.66  ? 423 ILE B CB  1 
ATOM   5479  C  CG1 . ILE B 1 359 ? 19.731 54.638 57.754  1.00 50.19  ? 423 ILE B CG1 1 
ATOM   5480  C  CG2 . ILE B 1 359 ? 18.078 55.326 59.396  1.00 43.55  ? 423 ILE B CG2 1 
ATOM   5481  C  CD1 . ILE B 1 359 ? 19.230 53.483 56.934  1.00 56.81  ? 423 ILE B CD1 1 
ATOM   5482  N  N   . THR B 1 360 ? 21.948 56.543 58.888  1.00 55.08  ? 424 THR B N   1 
ATOM   5483  C  CA  . THR B 1 360 ? 22.535 57.803 58.506  1.00 51.90  ? 424 THR B CA  1 
ATOM   5484  C  C   . THR B 1 360 ? 22.686 57.788 57.003  1.00 57.41  ? 424 THR B C   1 
ATOM   5485  O  O   . THR B 1 360 ? 23.057 56.752 56.416  1.00 63.16  ? 424 THR B O   1 
ATOM   5486  C  CB  . THR B 1 360 ? 23.932 57.985 59.107  1.00 56.04  ? 424 THR B CB  1 
ATOM   5487  O  OG1 . THR B 1 360 ? 24.879 57.260 58.315  1.00 67.25  ? 424 THR B OG1 1 
ATOM   5488  C  CG2 . THR B 1 360 ? 23.987 57.447 60.497  1.00 68.70  ? 424 THR B CG2 1 
ATOM   5489  N  N   . PHE B 1 361 ? 22.410 58.945 56.403  1.00 44.92  ? 425 PHE B N   1 
ATOM   5490  C  CA  . PHE B 1 361 ? 22.587 59.184 54.987  1.00 42.18  ? 425 PHE B CA  1 
ATOM   5491  C  C   . PHE B 1 361 ? 23.574 60.308 54.713  1.00 49.59  ? 425 PHE B C   1 
ATOM   5492  O  O   . PHE B 1 361 ? 23.578 61.345 55.420  1.00 55.52  ? 425 PHE B O   1 
ATOM   5493  C  CB  . PHE B 1 361 ? 21.262 59.610 54.413  1.00 40.26  ? 425 PHE B CB  1 
ATOM   5494  C  CG  . PHE B 1 361 ? 20.260 58.543 54.398  1.00 42.03  ? 425 PHE B CG  1 
ATOM   5495  C  CD1 . PHE B 1 361 ? 19.361 58.434 55.450  1.00 41.90  ? 425 PHE B CD1 1 
ATOM   5496  C  CD2 . PHE B 1 361 ? 20.198 57.623 53.331  1.00 41.18  ? 425 PHE B CD2 1 
ATOM   5497  C  CE1 . PHE B 1 361 ? 18.383 57.402 55.458  1.00 41.93  ? 425 PHE B CE1 1 
ATOM   5498  C  CE2 . PHE B 1 361 ? 19.228 56.583 53.318  1.00 41.82  ? 425 PHE B CE2 1 
ATOM   5499  C  CZ  . PHE B 1 361 ? 18.304 56.484 54.367  1.00 39.17  ? 425 PHE B CZ  1 
ATOM   5500  N  N   . CYS B 1 362 ? 24.393 60.121 53.683  1.00 47.68  ? 426 CYS B N   1 
ATOM   5501  C  CA  . CYS B 1 362 ? 25.273 61.189 53.230  1.00 59.31  ? 426 CYS B CA  1 
ATOM   5502  C  C   . CYS B 1 362 ? 24.885 61.633 51.844  1.00 53.02  ? 426 CYS B C   1 
ATOM   5503  O  O   . CYS B 1 362 ? 24.356 60.847 51.039  1.00 63.45  ? 426 CYS B O   1 
ATOM   5504  C  CB  . CYS B 1 362 ? 26.767 60.818 53.362  1.00 60.81  ? 426 CYS B CB  1 
ATOM   5505  S  SG  . CYS B 1 362 ? 27.225 60.786 55.149  1.00 141.40 ? 426 CYS B SG  1 
ATOM   5506  N  N   . GLY B 1 363 ? 25.111 62.907 51.582  1.00 43.72  ? 427 GLY B N   1 
ATOM   5507  C  CA  . GLY B 1 363 ? 24.817 63.457 50.284  1.00 52.55  ? 427 GLY B CA  1 
ATOM   5508  C  C   . GLY B 1 363 ? 25.841 63.108 49.226  1.00 63.77  ? 427 GLY B C   1 
ATOM   5509  O  O   . GLY B 1 363 ? 27.049 63.093 49.492  1.00 80.38  ? 427 GLY B O   1 
ATOM   5510  N  N   . THR B 1 364 ? 25.345 62.809 48.027  1.00 86.03  ? 428 THR B N   1 
ATOM   5511  C  CA  . THR B 1 364 ? 26.180 62.727 46.834  1.00 99.28  ? 428 THR B CA  1 
ATOM   5512  C  C   . THR B 1 364 ? 25.768 63.796 45.801  1.00 93.85  ? 428 THR B C   1 
ATOM   5513  O  O   . THR B 1 364 ? 24.618 64.283 45.791  1.00 81.87  ? 428 THR B O   1 
ATOM   5514  C  CB  . THR B 1 364 ? 26.216 61.289 46.227  1.00 93.52  ? 428 THR B CB  1 
ATOM   5515  O  OG1 . THR B 1 364 ? 27.191 61.227 45.169  1.00 115.55 ? 428 THR B OG1 1 
ATOM   5516  C  CG2 . THR B 1 364 ? 24.849 60.882 45.719  1.00 65.54  ? 428 THR B CG2 1 
ATOM   5517  N  N   . GLY B 1 365 ? 26.735 64.158 44.956  1.00 95.99  ? 429 GLY B N   1 
ATOM   5518  C  CA  . GLY B 1 365 ? 26.568 65.174 43.926  1.00 82.79  ? 429 GLY B CA  1 
ATOM   5519  C  C   . GLY B 1 365 ? 25.729 64.623 42.819  1.00 75.93  ? 429 GLY B C   1 
ATOM   5520  O  O   . GLY B 1 365 ? 25.011 65.367 42.172  1.00 86.21  ? 429 GLY B O   1 
ATOM   5521  N  N   . GLY B 1 366 ? 25.819 63.304 42.625  1.00 81.00  ? 430 GLY B N   1 
ATOM   5522  C  CA  . GLY B 1 366 ? 25.044 62.597 41.605  1.00 83.53  ? 430 GLY B CA  1 
ATOM   5523  C  C   . GLY B 1 366 ? 23.571 62.455 41.948  1.00 80.16  ? 430 GLY B C   1 
ATOM   5524  O  O   . GLY B 1 366 ? 23.199 62.385 43.115  1.00 64.51  ? 430 GLY B O   1 
ATOM   5525  N  N   . SER B 1 367 ? 22.720 62.422 40.930  1.00 82.73  ? 431 SER B N   1 
ATOM   5526  C  CA  . SER B 1 367 ? 21.345 62.044 41.164  1.00 81.27  ? 431 SER B CA  1 
ATOM   5527  C  C   . SER B 1 367 ? 21.316 60.553 41.495  1.00 84.02  ? 431 SER B C   1 
ATOM   5528  O  O   . SER B 1 367 ? 22.230 59.802 41.133  1.00 77.52  ? 431 SER B O   1 
ATOM   5529  C  CB  . SER B 1 367 ? 20.497 62.345 39.947  1.00 75.15  ? 431 SER B CB  1 
ATOM   5530  O  OG  . SER B 1 367 ? 19.161 62.017 40.226  1.00 89.90  ? 431 SER B OG  1 
ATOM   5531  N  N   . MET B 1 368 ? 20.282 60.131 42.211  1.00 84.77  ? 432 MET B N   1 
ATOM   5532  C  CA  . MET B 1 368 ? 20.188 58.743 42.639  1.00 76.66  ? 432 MET B CA  1 
ATOM   5533  C  C   . MET B 1 368 ? 18.870 58.142 42.245  1.00 76.46  ? 432 MET B C   1 
ATOM   5534  O  O   . MET B 1 368 ? 17.883 58.857 42.103  1.00 81.22  ? 432 MET B O   1 
ATOM   5535  C  CB  . MET B 1 368 ? 20.348 58.663 44.139  1.00 68.10  ? 432 MET B CB  1 
ATOM   5536  C  CG  . MET B 1 368 ? 21.788 58.822 44.577  1.00 96.70  ? 432 MET B CG  1 
ATOM   5537  S  SD  . MET B 1 368 ? 22.655 57.254 44.632  1.00 95.40  ? 432 MET B SD  1 
ATOM   5538  C  CE  . MET B 1 368 ? 21.467 56.237 45.535  1.00 102.45 ? 432 MET B CE  1 
ATOM   5539  N  N   . PRO B 1 369 ? 18.841 56.820 42.063  1.00 79.85  ? 433 PRO B N   1 
ATOM   5540  C  CA  . PRO B 1 369 ? 17.587 56.138 41.764  1.00 83.66  ? 433 PRO B CA  1 
ATOM   5541  C  C   . PRO B 1 369 ? 16.659 56.058 42.998  1.00 79.85  ? 433 PRO B C   1 
ATOM   5542  O  O   . PRO B 1 369 ? 17.085 56.288 44.143  1.00 71.01  ? 433 PRO B O   1 
ATOM   5543  C  CB  . PRO B 1 369 ? 18.060 54.744 41.350  1.00 73.86  ? 433 PRO B CB  1 
ATOM   5544  C  CG  . PRO B 1 369 ? 19.289 54.529 42.189  1.00 70.41  ? 433 PRO B CG  1 
ATOM   5545  C  CD  . PRO B 1 369 ? 19.968 55.878 42.173  1.00 71.92  ? 433 PRO B CD  1 
ATOM   5546  N  N   . ASP B 1 370 ? 15.395 55.752 42.751  1.00 66.13  ? 434 ASP B N   1 
ATOM   5547  C  CA  . ASP B 1 370 ? 14.459 55.528 43.813  1.00 54.77  ? 434 ASP B CA  1 
ATOM   5548  C  C   . ASP B 1 370 ? 14.801 54.244 44.569  1.00 50.40  ? 434 ASP B C   1 
ATOM   5549  O  O   . ASP B 1 370 ? 14.910 53.156 43.982  1.00 70.27  ? 434 ASP B O   1 
ATOM   5550  C  CB  . ASP B 1 370 ? 13.052 55.457 43.238  1.00 82.37  ? 434 ASP B CB  1 
ATOM   5551  C  CG  . ASP B 1 370 ? 12.630 56.744 42.529  1.00 104.38 ? 434 ASP B CG  1 
ATOM   5552  O  OD1 . ASP B 1 370 ? 13.153 57.820 42.866  1.00 101.65 ? 434 ASP B OD1 1 
ATOM   5553  O  OD2 . ASP B 1 370 ? 11.753 56.682 41.640  1.00 142.33 ? 434 ASP B OD2 1 
ATOM   5554  N  N   . VAL B 1 371 ? 14.963 54.368 45.880  1.00 41.07  ? 435 VAL B N   1 
ATOM   5555  C  CA  . VAL B 1 371 ? 15.209 53.207 46.723  1.00 46.68  ? 435 VAL B CA  1 
ATOM   5556  C  C   . VAL B 1 371 ? 14.466 53.287 48.066  1.00 59.43  ? 435 VAL B C   1 
ATOM   5557  O  O   . VAL B 1 371 ? 14.433 54.335 48.710  1.00 82.90  ? 435 VAL B O   1 
ATOM   5558  C  CB  . VAL B 1 371 ? 16.723 53.012 46.965  1.00 42.70  ? 435 VAL B CB  1 
ATOM   5559  C  CG1 . VAL B 1 371 ? 17.005 51.703 47.672  1.00 55.41  ? 435 VAL B CG1 1 
ATOM   5560  C  CG2 . VAL B 1 371 ? 17.469 53.085 45.651  1.00 36.43  ? 435 VAL B CG2 1 
ATOM   5561  N  N   . ASN B 1 372 ? 13.871 52.166 48.468  1.00 67.42  ? 436 ASN B N   1 
ATOM   5562  C  CA  . ASN B 1 372 ? 13.329 52.001 49.801  1.00 64.09  ? 436 ASN B CA  1 
ATOM   5563  C  C   . ASN B 1 372 ? 14.324 51.187 50.638  1.00 59.70  ? 436 ASN B C   1 
ATOM   5564  O  O   . ASN B 1 372 ? 14.429 49.990 50.470  1.00 81.13  ? 436 ASN B O   1 
ATOM   5565  C  CB  . ASN B 1 372 ? 11.971 51.293 49.724  1.00 57.71  ? 436 ASN B CB  1 
ATOM   5566  C  CG  . ASN B 1 372 ? 11.407 50.968 51.083  1.00 90.00  ? 436 ASN B CG  1 
ATOM   5567  O  OD1 . ASN B 1 372 ? 12.060 51.136 52.119  1.00 135.56 ? 436 ASN B OD1 1 
ATOM   5568  N  ND2 . ASN B 1 372 ? 10.186 50.475 51.090  1.00 102.27 ? 436 ASN B ND2 1 
ATOM   5569  N  N   . TRP B 1 373 ? 15.040 51.836 51.544  1.00 50.66  ? 437 TRP B N   1 
ATOM   5570  C  CA  . TRP B 1 373 ? 16.019 51.163 52.415  1.00 58.24  ? 437 TRP B CA  1 
ATOM   5571  C  C   . TRP B 1 373 ? 15.465 50.384 53.590  1.00 52.98  ? 437 TRP B C   1 
ATOM   5572  O  O   . TRP B 1 373 ? 14.314 50.563 53.999  1.00 63.38  ? 437 TRP B O   1 
ATOM   5573  C  CB  . TRP B 1 373 ? 17.025 52.194 52.899  1.00 54.41  ? 437 TRP B CB  1 
ATOM   5574  C  CG  . TRP B 1 373 ? 17.724 52.868 51.741  1.00 48.72  ? 437 TRP B CG  1 
ATOM   5575  C  CD1 . TRP B 1 373 ? 17.405 54.075 51.132  1.00 55.02  ? 437 TRP B CD1 1 
ATOM   5576  C  CD2 . TRP B 1 373 ? 18.857 52.369 51.003  1.00 44.63  ? 437 TRP B CD2 1 
ATOM   5577  N  NE1 . TRP B 1 373 ? 18.252 54.341 50.090  1.00 45.93  ? 437 TRP B NE1 1 
ATOM   5578  C  CE2 . TRP B 1 373 ? 19.148 53.366 49.968  1.00 47.87  ? 437 TRP B CE2 1 
ATOM   5579  C  CE3 . TRP B 1 373 ? 19.647 51.247 51.095  1.00 46.06  ? 437 TRP B CE3 1 
ATOM   5580  C  CZ2 . TRP B 1 373 ? 20.184 53.220 49.090  1.00 53.54  ? 437 TRP B CZ2 1 
ATOM   5581  C  CZ3 . TRP B 1 373 ? 20.700 51.108 50.201  1.00 56.14  ? 437 TRP B CZ3 1 
ATOM   5582  C  CH2 . TRP B 1 373 ? 20.962 52.072 49.222  1.00 58.79  ? 437 TRP B CH2 1 
ATOM   5583  N  N   . ALA C 1 11  ? 57.370 60.751 79.125  1.00 110.00 ? 75  ALA C N   1 
ATOM   5584  C  CA  . ALA C 1 11  ? 56.685 60.816 80.453  1.00 128.20 ? 75  ALA C CA  1 
ATOM   5585  C  C   . ALA C 1 11  ? 57.432 61.675 81.483  1.00 134.00 ? 75  ALA C C   1 
ATOM   5586  O  O   . ALA C 1 11  ? 58.663 61.707 81.531  1.00 100.20 ? 75  ALA C O   1 
ATOM   5587  C  CB  . ALA C 1 11  ? 56.415 59.407 81.009  1.00 110.62 ? 75  ALA C CB  1 
ATOM   5588  N  N   . THR C 1 12  ? 56.655 62.357 82.317  1.00 161.88 ? 76  THR C N   1 
ATOM   5589  C  CA  . THR C 1 12  ? 57.168 63.328 83.282  1.00 144.65 ? 76  THR C CA  1 
ATOM   5590  C  C   . THR C 1 12  ? 56.602 63.039 84.679  1.00 111.99 ? 76  THR C C   1 
ATOM   5591  O  O   . THR C 1 12  ? 55.413 62.747 84.816  1.00 108.95 ? 76  THR C O   1 
ATOM   5592  C  CB  . THR C 1 12  ? 56.807 64.776 82.835  1.00 132.96 ? 76  THR C CB  1 
ATOM   5593  O  OG1 . THR C 1 12  ? 57.361 65.018 81.537  1.00 129.38 ? 76  THR C OG1 1 
ATOM   5594  C  CG2 . THR C 1 12  ? 57.323 65.839 83.822  1.00 115.09 ? 76  THR C CG2 1 
ATOM   5595  N  N   . PRO C 1 13  ? 57.452 63.135 85.720  1.00 93.64  ? 77  PRO C N   1 
ATOM   5596  C  CA  . PRO C 1 13  ? 56.993 62.955 87.083  1.00 97.74  ? 77  PRO C CA  1 
ATOM   5597  C  C   . PRO C 1 13  ? 55.718 63.747 87.341  1.00 115.17 ? 77  PRO C C   1 
ATOM   5598  O  O   . PRO C 1 13  ? 55.667 64.943 87.049  1.00 135.57 ? 77  PRO C O   1 
ATOM   5599  C  CB  . PRO C 1 13  ? 58.144 63.533 87.919  1.00 97.51  ? 77  PRO C CB  1 
ATOM   5600  C  CG  . PRO C 1 13  ? 59.351 63.337 87.093  1.00 91.03  ? 77  PRO C CG  1 
ATOM   5601  C  CD  . PRO C 1 13  ? 58.886 63.493 85.670  1.00 102.47 ? 77  PRO C CD  1 
ATOM   5602  N  N   . LEU C 1 14  ? 54.698 63.072 87.865  1.00 130.42 ? 78  LEU C N   1 
ATOM   5603  C  CA  . LEU C 1 14  ? 53.442 63.717 88.215  1.00 107.56 ? 78  LEU C CA  1 
ATOM   5604  C  C   . LEU C 1 14  ? 53.673 64.793 89.271  1.00 115.63 ? 78  LEU C C   1 
ATOM   5605  O  O   . LEU C 1 14  ? 54.207 64.533 90.356  1.00 119.25 ? 78  LEU C O   1 
ATOM   5606  C  CB  . LEU C 1 14  ? 52.419 62.696 88.718  1.00 111.42 ? 78  LEU C CB  1 
ATOM   5607  C  CG  . LEU C 1 14  ? 51.034 63.264 89.026  1.00 107.10 ? 78  LEU C CG  1 
ATOM   5608  C  CD1 . LEU C 1 14  ? 50.292 63.453 87.733  1.00 101.76 ? 78  LEU C CD1 1 
ATOM   5609  C  CD2 . LEU C 1 14  ? 50.234 62.379 89.979  1.00 126.83 ? 78  LEU C CD2 1 
ATOM   5610  N  N   . VAL C 1 15  ? 53.283 66.008 88.915  1.00 125.35 ? 79  VAL C N   1 
ATOM   5611  C  CA  . VAL C 1 15  ? 53.347 67.153 89.806  1.00 124.42 ? 79  VAL C CA  1 
ATOM   5612  C  C   . VAL C 1 15  ? 51.921 67.615 90.074  1.00 114.79 ? 79  VAL C C   1 
ATOM   5613  O  O   . VAL C 1 15  ? 51.122 67.789 89.147  1.00 113.42 ? 79  VAL C O   1 
ATOM   5614  C  CB  . VAL C 1 15  ? 54.209 68.293 89.194  1.00 127.24 ? 79  VAL C CB  1 
ATOM   5615  C  CG1 . VAL C 1 15  ? 53.645 69.684 89.536  1.00 120.73 ? 79  VAL C CG1 1 
ATOM   5616  C  CG2 . VAL C 1 15  ? 55.673 68.152 89.626  1.00 105.26 ? 79  VAL C CG2 1 
ATOM   5617  N  N   . LEU C 1 16  ? 51.592 67.788 91.344  1.00 94.21  ? 80  LEU C N   1 
ATOM   5618  C  CA  . LEU C 1 16  ? 50.267 68.265 91.683  1.00 105.81 ? 80  LEU C CA  1 
ATOM   5619  C  C   . LEU C 1 16  ? 50.307 69.755 91.946  1.00 117.72 ? 80  LEU C C   1 
ATOM   5620  O  O   . LEU C 1 16  ? 51.355 70.289 92.350  1.00 109.05 ? 80  LEU C O   1 
ATOM   5621  C  CB  . LEU C 1 16  ? 49.720 67.515 92.893  1.00 94.98  ? 80  LEU C CB  1 
ATOM   5622  C  CG  . LEU C 1 16  ? 49.382 66.044 92.639  1.00 93.80  ? 80  LEU C CG  1 
ATOM   5623  C  CD1 . LEU C 1 16  ? 49.221 65.276 93.938  1.00 92.86  ? 80  LEU C CD1 1 
ATOM   5624  C  CD2 . LEU C 1 16  ? 48.131 65.943 91.778  1.00 97.58  ? 80  LEU C CD2 1 
ATOM   5625  N  N   . GLY C 1 17  ? 49.169 70.414 91.705  1.00 112.21 ? 81  GLY C N   1 
ATOM   5626  C  CA  . GLY C 1 17  ? 49.019 71.854 91.962  1.00 124.50 ? 81  GLY C CA  1 
ATOM   5627  C  C   . GLY C 1 17  ? 49.130 72.231 93.431  1.00 110.01 ? 81  GLY C C   1 
ATOM   5628  O  O   . GLY C 1 17  ? 48.542 71.578 94.308  1.00 97.15  ? 81  GLY C O   1 
ATOM   5629  N  N   . GLU C 1 18  ? 49.878 73.293 93.707  1.00 106.44 ? 82  GLU C N   1 
ATOM   5630  C  CA  . GLU C 1 18  ? 50.120 73.676 95.090  1.00 117.03 ? 82  GLU C CA  1 
ATOM   5631  C  C   . GLU C 1 18  ? 48.862 74.278 95.717  1.00 109.52 ? 82  GLU C C   1 
ATOM   5632  O  O   . GLU C 1 18  ? 48.606 74.098 96.914  1.00 119.98 ? 82  GLU C O   1 
ATOM   5633  C  CB  . GLU C 1 18  ? 51.319 74.624 95.190  1.00 119.41 ? 82  GLU C CB  1 
ATOM   5634  C  CG  . GLU C 1 18  ? 52.235 74.364 96.403  1.00 143.57 ? 82  GLU C CG  1 
ATOM   5635  C  CD  . GLU C 1 18  ? 53.028 73.058 96.312  1.00 144.10 ? 82  GLU C CD  1 
ATOM   5636  O  OE1 . GLU C 1 18  ? 53.275 72.546 95.197  1.00 127.88 ? 82  GLU C OE1 1 
ATOM   5637  O  OE2 . GLU C 1 18  ? 53.414 72.543 97.376  1.00 162.30 ? 82  GLU C OE2 1 
ATOM   5638  N  N   . ASN C 1 19  ? 48.069 74.963 94.893  1.00 112.77 ? 83  ASN C N   1 
ATOM   5639  C  CA  . ASN C 1 19  ? 46.873 75.675 95.360  1.00 90.72  ? 83  ASN C CA  1 
ATOM   5640  C  C   . ASN C 1 19  ? 45.605 74.992 94.934  1.00 78.76  ? 83  ASN C C   1 
ATOM   5641  O  O   . ASN C 1 19  ? 45.458 74.646 93.775  1.00 75.99  ? 83  ASN C O   1 
ATOM   5642  C  CB  . ASN C 1 19  ? 46.881 77.114 94.860  1.00 95.60  ? 83  ASN C CB  1 
ATOM   5643  C  CG  . ASN C 1 19  ? 47.997 77.938 95.482  1.00 110.74 ? 83  ASN C CG  1 
ATOM   5644  O  OD1 . ASN C 1 19  ? 48.374 77.733 96.644  1.00 105.16 ? 83  ASN C OD1 1 
ATOM   5645  N  ND2 . ASN C 1 19  ? 48.534 78.877 94.710  1.00 115.57 ? 83  ASN C ND2 1 
ATOM   5646  N  N   . LEU C 1 20  ? 44.690 74.798 95.877  1.00 82.41  ? 84  LEU C N   1 
ATOM   5647  C  CA  . LEU C 1 20  ? 43.435 74.082 95.620  1.00 75.61  ? 84  LEU C CA  1 
ATOM   5648  C  C   . LEU C 1 20  ? 42.375 74.970 95.002  1.00 77.33  ? 84  LEU C C   1 
ATOM   5649  O  O   . LEU C 1 20  ? 42.250 76.150 95.336  1.00 81.69  ? 84  LEU C O   1 
ATOM   5650  C  CB  . LEU C 1 20  ? 42.888 73.545 96.928  1.00 81.62  ? 84  LEU C CB  1 
ATOM   5651  C  CG  . LEU C 1 20  ? 42.334 72.138 96.941  1.00 91.85  ? 84  LEU C CG  1 
ATOM   5652  C  CD1 . LEU C 1 20  ? 43.444 71.169 96.622  1.00 112.43 ? 84  LEU C CD1 1 
ATOM   5653  C  CD2 . LEU C 1 20  ? 41.780 71.839 98.311  1.00 120.55 ? 84  LEU C CD2 1 
ATOM   5654  N  N   . CYS C 1 21  ? 41.598 74.387 94.104  1.00 91.44  ? 85  CYS C N   1 
ATOM   5655  C  CA  . CYS C 1 21  ? 40.425 75.041 93.544  1.00 95.74  ? 85  CYS C CA  1 
ATOM   5656  C  C   . CYS C 1 21  ? 39.502 75.463 94.662  1.00 97.60  ? 85  CYS C C   1 
ATOM   5657  O  O   . CYS C 1 21  ? 39.407 74.751 95.656  1.00 108.55 ? 85  CYS C O   1 
ATOM   5658  C  CB  . CYS C 1 21  ? 39.710 74.071 92.607  1.00 116.54 ? 85  CYS C CB  1 
ATOM   5659  S  SG  . CYS C 1 21  ? 40.541 74.037 91.043  1.00 244.17 ? 85  CYS C SG  1 
ATOM   5660  N  N   . SER C 1 22  ? 38.857 76.625 94.530  1.00 98.16  ? 86  SER C N   1 
ATOM   5661  C  CA  . SER C 1 22  ? 37.784 76.996 95.461  1.00 97.50  ? 86  SER C CA  1 
ATOM   5662  C  C   . SER C 1 22  ? 36.611 76.102 95.133  1.00 97.05  ? 86  SER C C   1 
ATOM   5663  O  O   . SER C 1 22  ? 36.240 75.950 93.971  1.00 96.13  ? 86  SER C O   1 
ATOM   5664  C  CB  . SER C 1 22  ? 37.355 78.458 95.321  1.00 102.83 ? 86  SER C CB  1 
ATOM   5665  O  OG  . SER C 1 22  ? 38.410 79.343 95.632  1.00 127.02 ? 86  SER C OG  1 
ATOM   5666  N  N   . ILE C 1 23  ? 36.036 75.498 96.156  1.00 90.70  ? 87  ILE C N   1 
ATOM   5667  C  CA  . ILE C 1 23  ? 34.925 74.595 95.952  1.00 81.98  ? 87  ILE C CA  1 
ATOM   5668  C  C   . ILE C 1 23  ? 33.748 75.192 96.694  1.00 77.79  ? 87  ILE C C   1 
ATOM   5669  O  O   . ILE C 1 23  ? 33.838 75.507 97.885  1.00 66.19  ? 87  ILE C O   1 
ATOM   5670  C  CB  . ILE C 1 23  ? 35.271 73.173 96.443  1.00 83.02  ? 87  ILE C CB  1 
ATOM   5671  C  CG1 . ILE C 1 23  ? 36.327 72.555 95.521  1.00 89.62  ? 87  ILE C CG1 1 
ATOM   5672  C  CG2 . ILE C 1 23  ? 34.026 72.294 96.480  1.00 84.25  ? 87  ILE C CG2 1 
ATOM   5673  C  CD1 . ILE C 1 23  ? 37.413 71.794 96.242  1.00 81.88  ? 87  ILE C CD1 1 
ATOM   5674  N  N   . ASN C 1 24  ? 32.661 75.396 95.969  1.00 76.85  ? 88  ASN C N   1 
ATOM   5675  C  CA  . ASN C 1 24  ? 31.440 75.841 96.597  1.00 79.24  ? 88  ASN C CA  1 
ATOM   5676  C  C   . ASN C 1 24  ? 30.254 74.912 96.341  1.00 92.83  ? 88  ASN C C   1 
ATOM   5677  O  O   . ASN C 1 24  ? 29.177 75.105 96.903  1.00 99.18  ? 88  ASN C O   1 
ATOM   5678  C  CB  . ASN C 1 24  ? 31.130 77.269 96.187  1.00 77.12  ? 88  ASN C CB  1 
ATOM   5679  C  CG  . ASN C 1 24  ? 32.104 78.271 96.792  1.00 88.54  ? 88  ASN C CG  1 
ATOM   5680  O  OD1 . ASN C 1 24  ? 31.981 78.675 97.960  1.00 71.99  ? 88  ASN C OD1 1 
ATOM   5681  N  ND2 . ASN C 1 24  ? 33.073 78.693 95.988  1.00 110.02 ? 88  ASN C ND2 1 
ATOM   5682  N  N   . GLY C 1 25  ? 30.454 73.890 95.514  1.00 86.00  ? 89  GLY C N   1 
ATOM   5683  C  CA  . GLY C 1 25  ? 29.391 72.931 95.251  1.00 71.49  ? 89  GLY C CA  1 
ATOM   5684  C  C   . GLY C 1 25  ? 29.935 71.661 94.668  1.00 65.47  ? 89  GLY C C   1 
ATOM   5685  O  O   . GLY C 1 25  ? 31.139 71.525 94.512  1.00 87.97  ? 89  GLY C O   1 
ATOM   5686  N  N   . TRP C 1 26  ? 29.053 70.722 94.351  1.00 58.22  ? 90  TRP C N   1 
ATOM   5687  C  CA  . TRP C 1 26  ? 29.505 69.439 93.826  1.00 59.21  ? 90  TRP C CA  1 
ATOM   5688  C  C   . TRP C 1 26  ? 28.664 68.967 92.678  1.00 64.32  ? 90  TRP C C   1 
ATOM   5689  O  O   . TRP C 1 26  ? 27.420 69.076 92.696  1.00 61.42  ? 90  TRP C O   1 
ATOM   5690  C  CB  . TRP C 1 26  ? 29.586 68.383 94.943  1.00 57.86  ? 90  TRP C CB  1 
ATOM   5691  C  CG  . TRP C 1 26  ? 30.480 68.816 96.092  1.00 59.80  ? 90  TRP C CG  1 
ATOM   5692  C  CD1 . TRP C 1 26  ? 30.117 69.538 97.226  1.00 59.01  ? 90  TRP C CD1 1 
ATOM   5693  C  CD2 . TRP C 1 26  ? 31.923 68.611 96.228  1.00 59.04  ? 90  TRP C CD2 1 
ATOM   5694  N  NE1 . TRP C 1 26  ? 31.193 69.768 98.030  1.00 57.96  ? 90  TRP C NE1 1 
ATOM   5695  C  CE2 . TRP C 1 26  ? 32.306 69.235 97.495  1.00 63.49  ? 90  TRP C CE2 1 
ATOM   5696  C  CE3 . TRP C 1 26  ? 32.894 67.992 95.461  1.00 58.39  ? 90  TRP C CE3 1 
ATOM   5697  C  CZ2 . TRP C 1 26  ? 33.609 69.212 97.958  1.00 71.12  ? 90  TRP C CZ2 1 
ATOM   5698  C  CZ3 . TRP C 1 26  ? 34.206 67.982 95.932  1.00 64.76  ? 90  TRP C CZ3 1 
ATOM   5699  C  CH2 . TRP C 1 26  ? 34.555 68.584 97.148  1.00 69.20  ? 90  TRP C CH2 1 
ATOM   5700  N  N   . VAL C 1 27  ? 29.327 68.458 91.643  1.00 62.39  ? 91  VAL C N   1 
ATOM   5701  C  CA  . VAL C 1 27  ? 28.591 67.843 90.561  1.00 63.76  ? 91  VAL C CA  1 
ATOM   5702  C  C   . VAL C 1 27  ? 29.146 66.460 90.293  1.00 56.86  ? 91  VAL C C   1 
ATOM   5703  O  O   . VAL C 1 27  ? 30.363 66.259 90.353  1.00 52.17  ? 91  VAL C O   1 
ATOM   5704  C  CB  . VAL C 1 27  ? 28.544 68.722 89.285  1.00 67.66  ? 91  VAL C CB  1 
ATOM   5705  C  CG1 . VAL C 1 27  ? 28.609 70.199 89.644  1.00 69.16  ? 91  VAL C CG1 1 
ATOM   5706  C  CG2 . VAL C 1 27  ? 29.665 68.391 88.385  1.00 67.53  ? 91  VAL C CG2 1 
ATOM   5707  N  N   . PRO C 1 28  ? 28.244 65.499 90.020  1.00 59.09  ? 92  PRO C N   1 
ATOM   5708  C  CA  . PRO C 1 28  ? 28.645 64.119 89.723  1.00 55.71  ? 92  PRO C CA  1 
ATOM   5709  C  C   . PRO C 1 28  ? 29.313 64.048 88.382  1.00 52.85  ? 92  PRO C C   1 
ATOM   5710  O  O   . PRO C 1 28  ? 28.855 64.662 87.443  1.00 65.54  ? 92  PRO C O   1 
ATOM   5711  C  CB  . PRO C 1 28  ? 27.323 63.350 89.710  1.00 48.32  ? 92  PRO C CB  1 
ATOM   5712  C  CG  . PRO C 1 28  ? 26.281 64.384 89.502  1.00 51.76  ? 92  PRO C CG  1 
ATOM   5713  C  CD  . PRO C 1 28  ? 26.781 65.657 90.061  1.00 54.89  ? 92  PRO C CD  1 
ATOM   5714  N  N   . THR C 1 29  ? 30.416 63.335 88.306  1.00 55.34  ? 93  THR C N   1 
ATOM   5715  C  CA  . THR C 1 29  ? 31.129 63.171 87.044  1.00 62.23  ? 93  THR C CA  1 
ATOM   5716  C  C   . THR C 1 29  ? 30.974 61.745 86.519  1.00 58.58  ? 93  THR C C   1 
ATOM   5717  O  O   . THR C 1 29  ? 31.231 61.471 85.358  1.00 63.74  ? 93  THR C O   1 
ATOM   5718  C  CB  . THR C 1 29  ? 32.646 63.556 87.160  1.00 69.43  ? 93  THR C CB  1 
ATOM   5719  O  OG1 . THR C 1 29  ? 33.228 62.985 88.344  1.00 68.73  ? 93  THR C OG1 1 
ATOM   5720  C  CG2 . THR C 1 29  ? 32.822 65.065 87.227  1.00 71.85  ? 93  THR C CG2 1 
ATOM   5721  N  N   . TYR C 1 30  ? 30.553 60.833 87.378  1.00 55.34  ? 94  TYR C N   1 
ATOM   5722  C  CA  . TYR C 1 30  ? 30.384 59.451 86.979  1.00 52.59  ? 94  TYR C CA  1 
ATOM   5723  C  C   . TYR C 1 30  ? 29.459 58.735 87.928  1.00 56.89  ? 94  TYR C C   1 
ATOM   5724  O  O   . TYR C 1 30  ? 29.398 59.062 89.113  1.00 77.16  ? 94  TYR C O   1 
ATOM   5725  C  CB  . TYR C 1 30  ? 31.717 58.704 86.992  1.00 58.42  ? 94  TYR C CB  1 
ATOM   5726  C  CG  . TYR C 1 30  ? 31.526 57.203 86.838  1.00 63.14  ? 94  TYR C CG  1 
ATOM   5727  C  CD1 . TYR C 1 30  ? 31.270 56.641 85.599  1.00 74.30  ? 94  TYR C CD1 1 
ATOM   5728  C  CD2 . TYR C 1 30  ? 31.528 56.358 87.935  1.00 61.85  ? 94  TYR C CD2 1 
ATOM   5729  C  CE1 . TYR C 1 30  ? 31.049 55.271 85.452  1.00 72.27  ? 94  TYR C CE1 1 
ATOM   5730  C  CE2 . TYR C 1 30  ? 31.303 54.984 87.794  1.00 63.42  ? 94  TYR C CE2 1 
ATOM   5731  C  CZ  . TYR C 1 30  ? 31.072 54.454 86.557  1.00 70.41  ? 94  TYR C CZ  1 
ATOM   5732  O  OH  . TYR C 1 30  ? 30.882 53.100 86.422  1.00 88.70  ? 94  TYR C OH  1 
ATOM   5733  N  N   . ARG C 1 31  ? 28.774 57.726 87.411  1.00 48.58  ? 95  ARG C N   1 
ATOM   5734  C  CA  . ARG C 1 31  ? 27.772 57.019 88.168  1.00 52.66  ? 95  ARG C CA  1 
ATOM   5735  C  C   . ARG C 1 31  ? 27.721 55.656 87.562  1.00 56.99  ? 95  ARG C C   1 
ATOM   5736  O  O   . ARG C 1 31  ? 27.565 55.509 86.365  1.00 66.41  ? 95  ARG C O   1 
ATOM   5737  C  CB  . ARG C 1 31  ? 26.417 57.726 88.039  1.00 59.16  ? 95  ARG C CB  1 
ATOM   5738  C  CG  . ARG C 1 31  ? 25.263 56.993 88.647  1.00 79.57  ? 95  ARG C CG  1 
ATOM   5739  C  CD  . ARG C 1 31  ? 24.096 57.931 88.882  1.00 90.65  ? 95  ARG C CD  1 
ATOM   5740  N  NE  . ARG C 1 31  ? 23.604 58.469 87.622  1.00 89.93  ? 95  ARG C NE  1 
ATOM   5741  C  CZ  . ARG C 1 31  ? 22.427 59.050 87.477  1.00 65.99  ? 95  ARG C CZ  1 
ATOM   5742  N  NH1 . ARG C 1 31  ? 21.628 59.155 88.521  1.00 72.26  ? 95  ARG C NH1 1 
ATOM   5743  N  NH2 . ARG C 1 31  ? 22.055 59.500 86.286  1.00 62.05  ? 95  ARG C NH2 1 
ATOM   5744  N  N   . GLY C 1 32  ? 27.897 54.643 88.383  1.00 65.37  ? 96  GLY C N   1 
ATOM   5745  C  CA  . GLY C 1 32  ? 27.813 53.273 87.906  1.00 74.56  ? 96  GLY C CA  1 
ATOM   5746  C  C   . GLY C 1 32  ? 26.386 52.895 87.578  1.00 67.25  ? 96  GLY C C   1 
ATOM   5747  O  O   . GLY C 1 32  ? 25.438 53.528 88.057  1.00 77.68  ? 96  GLY C O   1 
ATOM   5748  N  N   . GLU C 1 33  ? 26.222 51.861 86.768  1.00 62.03  ? 97  GLU C N   1 
ATOM   5749  C  CA  . GLU C 1 33  ? 24.885 51.493 86.365  1.00 83.50  ? 97  GLU C CA  1 
ATOM   5750  C  C   . GLU C 1 33  ? 24.135 50.783 87.491  1.00 89.51  ? 97  GLU C C   1 
ATOM   5751  O  O   . GLU C 1 33  ? 22.913 50.683 87.467  1.00 118.17 ? 97  GLU C O   1 
ATOM   5752  C  CB  . GLU C 1 33  ? 24.897 50.669 85.075  1.00 102.19 ? 97  GLU C CB  1 
ATOM   5753  C  CG  . GLU C 1 33  ? 23.675 50.927 84.173  1.00 125.82 ? 97  GLU C CG  1 
ATOM   5754  C  CD  . GLU C 1 33  ? 23.609 52.362 83.597  1.00 148.68 ? 97  GLU C CD  1 
ATOM   5755  O  OE1 . GLU C 1 33  ? 24.670 52.925 83.258  1.00 166.16 ? 97  GLU C OE1 1 
ATOM   5756  O  OE2 . GLU C 1 33  ? 22.493 52.927 83.463  1.00 112.88 ? 97  GLU C OE2 1 
ATOM   5757  N  N   . GLY C 1 34  ? 24.865 50.312 88.491  1.00 77.96  ? 98  GLY C N   1 
ATOM   5758  C  CA  . GLY C 1 34  ? 24.232 49.668 89.635  1.00 79.90  ? 98  GLY C CA  1 
ATOM   5759  C  C   . GLY C 1 34  ? 23.701 50.648 90.662  1.00 78.15  ? 98  GLY C C   1 
ATOM   5760  O  O   . GLY C 1 34  ? 23.098 50.249 91.666  1.00 76.29  ? 98  GLY C O   1 
ATOM   5761  N  N   . THR C 1 35  ? 23.909 51.936 90.407  1.00 76.95  ? 99  THR C N   1 
ATOM   5762  C  CA  . THR C 1 35  ? 23.540 52.962 91.379  1.00 82.05  ? 99  THR C CA  1 
ATOM   5763  C  C   . THR C 1 35  ? 22.101 53.298 91.164  1.00 79.48  ? 99  THR C C   1 
ATOM   5764  O  O   . THR C 1 35  ? 21.523 54.047 91.950  1.00 97.05  ? 99  THR C O   1 
ATOM   5765  C  CB  . THR C 1 35  ? 24.346 54.257 91.211  1.00 72.66  ? 99  THR C CB  1 
ATOM   5766  O  OG1 . THR C 1 35  ? 24.103 54.787 89.904  1.00 80.43  ? 99  THR C OG1 1 
ATOM   5767  C  CG2 . THR C 1 35  ? 25.833 53.992 91.384  1.00 80.17  ? 99  THR C CG2 1 
ATOM   5768  N  N   . THR C 1 36  ? 21.538 52.753 90.086  1.00 70.09  ? 100 THR C N   1 
ATOM   5769  C  CA  . THR C 1 36  ? 20.162 53.061 89.681  1.00 93.83  ? 100 THR C CA  1 
ATOM   5770  C  C   . THR C 1 36  ? 19.364 51.776 89.442  1.00 99.71  ? 100 THR C C   1 
ATOM   5771  O  O   . THR C 1 36  ? 18.409 51.483 90.156  1.00 101.77 ? 100 THR C O   1 
ATOM   5772  C  CB  . THR C 1 36  ? 20.116 53.977 88.420  1.00 95.45  ? 100 THR C CB  1 
ATOM   5773  O  OG1 . THR C 1 36  ? 21.035 53.487 87.445  1.00 111.99 ? 100 THR C OG1 1 
ATOM   5774  C  CG2 . THR C 1 36  ? 20.515 55.408 88.764  1.00 102.15 ? 100 THR C CG2 1 
ATOM   5775  N  N   . GLY C 1 37  ? 19.767 51.010 88.437  1.00 100.65 ? 101 GLY C N   1 
ATOM   5776  C  CA  . GLY C 1 37  ? 19.208 49.685 88.214  1.00 93.79  ? 101 GLY C CA  1 
ATOM   5777  C  C   . GLY C 1 37  ? 20.008 48.556 88.862  1.00 103.23 ? 101 GLY C C   1 
ATOM   5778  O  O   . GLY C 1 37  ? 20.861 48.775 89.746  1.00 85.58  ? 101 GLY C O   1 
ATOM   5779  N  N   . LYS C 1 38  ? 19.716 47.337 88.417  1.00 96.03  ? 102 LYS C N   1 
ATOM   5780  C  CA  . LYS C 1 38  ? 20.396 46.151 88.905  1.00 83.10  ? 102 LYS C CA  1 
ATOM   5781  C  C   . LYS C 1 38  ? 21.613 45.827 88.044  1.00 77.10  ? 102 LYS C C   1 
ATOM   5782  O  O   . LYS C 1 38  ? 21.717 46.281 86.915  1.00 81.28  ? 102 LYS C O   1 
ATOM   5783  C  CB  . LYS C 1 38  ? 19.427 44.982 88.933  1.00 86.19  ? 102 LYS C CB  1 
ATOM   5784  C  CG  . LYS C 1 38  ? 18.402 45.071 90.040  1.00 108.37 ? 102 LYS C CG  1 
ATOM   5785  C  CD  . LYS C 1 38  ? 17.796 43.707 90.303  1.00 129.49 ? 102 LYS C CD  1 
ATOM   5786  C  CE  . LYS C 1 38  ? 17.242 43.603 91.708  1.00 122.93 ? 102 LYS C CE  1 
ATOM   5787  N  NZ  . LYS C 1 38  ? 17.018 42.175 92.048  1.00 128.49 ? 102 LYS C NZ  1 
ATOM   5788  N  N   . ILE C 1 39  ? 22.543 45.058 88.587  1.00 73.58  ? 103 ILE C N   1 
ATOM   5789  C  CA  . ILE C 1 39  ? 23.761 44.709 87.871  1.00 69.95  ? 103 ILE C CA  1 
ATOM   5790  C  C   . ILE C 1 39  ? 23.554 43.412 87.086  1.00 82.32  ? 103 ILE C C   1 
ATOM   5791  O  O   . ILE C 1 39  ? 22.997 42.446 87.613  1.00 82.23  ? 103 ILE C O   1 
ATOM   5792  C  CB  . ILE C 1 39  ? 24.918 44.455 88.853  1.00 70.05  ? 103 ILE C CB  1 
ATOM   5793  C  CG1 . ILE C 1 39  ? 24.948 45.517 89.957  1.00 57.43  ? 103 ILE C CG1 1 
ATOM   5794  C  CG2 . ILE C 1 39  ? 26.261 44.261 88.103  1.00 68.42  ? 103 ILE C CG2 1 
ATOM   5795  C  CD1 . ILE C 1 39  ? 25.947 46.617 89.760  1.00 48.08  ? 103 ILE C CD1 1 
ATOM   5796  N  N   . PRO C 1 40  ? 24.022 43.385 85.826  1.00 90.97  ? 104 PRO C N   1 
ATOM   5797  C  CA  . PRO C 1 40  ? 24.081 42.175 84.980  1.00 82.58  ? 104 PRO C CA  1 
ATOM   5798  C  C   . PRO C 1 40  ? 24.945 41.069 85.584  1.00 85.33  ? 104 PRO C C   1 
ATOM   5799  O  O   . PRO C 1 40  ? 26.046 41.344 86.099  1.00 84.09  ? 104 PRO C O   1 
ATOM   5800  C  CB  . PRO C 1 40  ? 24.739 42.681 83.698  1.00 81.31  ? 104 PRO C CB  1 
ATOM   5801  C  CG  . PRO C 1 40  ? 24.500 44.162 83.689  1.00 71.65  ? 104 PRO C CG  1 
ATOM   5802  C  CD  . PRO C 1 40  ? 24.505 44.585 85.115  1.00 81.41  ? 104 PRO C CD  1 
ATOM   5803  N  N   . ASP C 1 41  ? 24.460 39.830 85.508  1.00 89.81  ? 105 ASP C N   1 
ATOM   5804  C  CA  . ASP C 1 41  ? 25.084 38.716 86.238  1.00 106.86 ? 105 ASP C CA  1 
ATOM   5805  C  C   . ASP C 1 41  ? 26.494 38.405 85.772  1.00 106.93 ? 105 ASP C C   1 
ATOM   5806  O  O   . ASP C 1 41  ? 27.288 37.854 86.536  1.00 138.44 ? 105 ASP C O   1 
ATOM   5807  C  CB  . ASP C 1 41  ? 24.216 37.457 86.199  1.00 111.48 ? 105 ASP C CB  1 
ATOM   5808  C  CG  . ASP C 1 41  ? 22.812 37.703 86.722  1.00 142.18 ? 105 ASP C CG  1 
ATOM   5809  O  OD1 . ASP C 1 41  ? 22.371 38.864 86.693  1.00 145.42 ? 105 ASP C OD1 1 
ATOM   5810  O  OD2 . ASP C 1 41  ? 22.143 36.743 87.153  1.00 179.05 ? 105 ASP C OD2 1 
ATOM   5811  N  N   . GLU C 1 42  ? 26.807 38.773 84.530  1.00 92.53  ? 106 GLU C N   1 
ATOM   5812  C  CA  . GLU C 1 42  ? 28.129 38.505 83.968  1.00 83.30  ? 106 GLU C CA  1 
ATOM   5813  C  C   . GLU C 1 42  ? 29.211 39.422 84.497  1.00 86.98  ? 106 GLU C C   1 
ATOM   5814  O  O   . GLU C 1 42  ? 30.398 39.103 84.381  1.00 104.51 ? 106 GLU C O   1 
ATOM   5815  C  CB  . GLU C 1 42  ? 28.141 38.526 82.443  1.00 84.34  ? 106 GLU C CB  1 
ATOM   5816  C  CG  . GLU C 1 42  ? 27.888 39.869 81.798  1.00 111.62 ? 106 GLU C CG  1 
ATOM   5817  C  CD  . GLU C 1 42  ? 26.486 39.965 81.201  1.00 174.52 ? 106 GLU C CD  1 
ATOM   5818  O  OE1 . GLU C 1 42  ? 25.502 39.620 81.895  1.00 216.24 ? 106 GLU C OE1 1 
ATOM   5819  O  OE2 . GLU C 1 42  ? 26.368 40.385 80.028  1.00 190.24 ? 106 GLU C OE2 1 
ATOM   5820  N  N   . GLN C 1 43  ? 28.819 40.549 85.083  1.00 73.93  ? 107 GLN C N   1 
ATOM   5821  C  CA  . GLN C 1 43  ? 29.809 41.445 85.672  1.00 65.72  ? 107 GLN C CA  1 
ATOM   5822  C  C   . GLN C 1 43  ? 30.507 40.832 86.881  1.00 66.24  ? 107 GLN C C   1 
ATOM   5823  O  O   . GLN C 1 43  ? 29.976 39.943 87.552  1.00 83.50  ? 107 GLN C O   1 
ATOM   5824  C  CB  . GLN C 1 43  ? 29.181 42.774 86.040  1.00 71.10  ? 107 GLN C CB  1 
ATOM   5825  C  CG  . GLN C 1 43  ? 28.837 43.624 84.841  1.00 79.28  ? 107 GLN C CG  1 
ATOM   5826  C  CD  . GLN C 1 43  ? 28.645 45.075 85.200  1.00 85.00  ? 107 GLN C CD  1 
ATOM   5827  O  OE1 . GLN C 1 43  ? 29.194 45.561 86.192  1.00 99.15  ? 107 GLN C OE1 1 
ATOM   5828  N  NE2 . GLN C 1 43  ? 27.868 45.783 84.393  1.00 95.68  ? 107 GLN C NE2 1 
ATOM   5829  N  N   . MET C 1 44  ? 31.727 41.284 87.116  1.00 68.94  ? 108 MET C N   1 
ATOM   5830  C  CA  . MET C 1 44  ? 32.492 40.919 88.293  1.00 64.40  ? 108 MET C CA  1 
ATOM   5831  C  C   . MET C 1 44  ? 31.834 41.627 89.508  1.00 62.20  ? 108 MET C C   1 
ATOM   5832  O  O   . MET C 1 44  ? 31.403 42.782 89.424  1.00 54.10  ? 108 MET C O   1 
ATOM   5833  C  CB  . MET C 1 44  ? 33.941 41.358 88.078  1.00 57.95  ? 108 MET C CB  1 
ATOM   5834  C  CG  . MET C 1 44  ? 34.869 41.039 89.216  1.00 83.32  ? 108 MET C CG  1 
ATOM   5835  S  SD  . MET C 1 44  ? 35.178 39.276 89.322  1.00 100.57 ? 108 MET C SD  1 
ATOM   5836  C  CE  . MET C 1 44  ? 36.580 39.061 88.213  1.00 72.19  ? 108 MET C CE  1 
ATOM   5837  N  N   . LEU C 1 45  ? 31.697 40.911 90.616  1.00 64.19  ? 109 LEU C N   1 
ATOM   5838  C  CA  . LEU C 1 45  ? 31.207 41.509 91.860  1.00 64.80  ? 109 LEU C CA  1 
ATOM   5839  C  C   . LEU C 1 45  ? 32.362 42.261 92.503  1.00 62.84  ? 109 LEU C C   1 
ATOM   5840  O  O   . LEU C 1 45  ? 33.459 41.719 92.629  1.00 76.10  ? 109 LEU C O   1 
ATOM   5841  C  CB  . LEU C 1 45  ? 30.722 40.421 92.826  1.00 64.91  ? 109 LEU C CB  1 
ATOM   5842  C  CG  . LEU C 1 45  ? 29.614 39.471 92.365  1.00 63.71  ? 109 LEU C CG  1 
ATOM   5843  C  CD1 . LEU C 1 45  ? 29.518 38.322 93.356  1.00 65.53  ? 109 LEU C CD1 1 
ATOM   5844  C  CD2 . LEU C 1 45  ? 28.281 40.198 92.223  1.00 54.02  ? 109 LEU C CD2 1 
ATOM   5845  N  N   . THR C 1 46  ? 32.139 43.502 92.911  1.00 63.34  ? 110 THR C N   1 
ATOM   5846  C  CA  . THR C 1 46  ? 33.251 44.309 93.421  1.00 56.53  ? 110 THR C CA  1 
ATOM   5847  C  C   . THR C 1 46  ? 33.064 44.696 94.855  1.00 62.35  ? 110 THR C C   1 
ATOM   5848  O  O   . THR C 1 46  ? 31.943 44.794 95.366  1.00 66.41  ? 110 THR C O   1 
ATOM   5849  C  CB  . THR C 1 46  ? 33.439 45.635 92.658  1.00 56.69  ? 110 THR C CB  1 
ATOM   5850  O  OG1 . THR C 1 46  ? 32.321 46.483 92.907  1.00 66.10  ? 110 THR C OG1 1 
ATOM   5851  C  CG2 . THR C 1 46  ? 33.550 45.419 91.174  1.00 75.95  ? 110 THR C CG2 1 
ATOM   5852  N  N   . ARG C 1 47  ? 34.188 44.947 95.503  1.00 65.69  ? 111 ARG C N   1 
ATOM   5853  C  CA  . ARG C 1 47  ? 34.174 45.479 96.841  1.00 53.74  ? 111 ARG C CA  1 
ATOM   5854  C  C   . ARG C 1 47  ? 35.419 46.292 97.028  1.00 47.33  ? 111 ARG C C   1 
ATOM   5855  O  O   . ARG C 1 47  ? 36.413 46.070 96.348  1.00 60.32  ? 111 ARG C O   1 
ATOM   5856  C  CB  . ARG C 1 47  ? 34.076 44.332 97.852  1.00 54.45  ? 111 ARG C CB  1 
ATOM   5857  C  CG  . ARG C 1 47  ? 35.359 43.778 98.400  1.00 48.16  ? 111 ARG C CG  1 
ATOM   5858  C  CD  . ARG C 1 47  ? 35.120 43.202 99.808  1.00 51.86  ? 111 ARG C CD  1 
ATOM   5859  N  NE  . ARG C 1 47  ? 36.373 42.818 100.448 1.00 65.52  ? 111 ARG C NE  1 
ATOM   5860  C  CZ  . ARG C 1 47  ? 37.216 43.659 101.053 1.00 71.73  ? 111 ARG C CZ  1 
ATOM   5861  N  NH1 . ARG C 1 47  ? 36.946 44.951 101.131 1.00 58.90  ? 111 ARG C NH1 1 
ATOM   5862  N  NH2 . ARG C 1 47  ? 38.342 43.202 101.593 1.00 87.26  ? 111 ARG C NH2 1 
ATOM   5863  N  N   . GLN C 1 48  ? 35.365 47.231 97.953  1.00 46.43  ? 112 GLN C N   1 
ATOM   5864  C  CA  . GLN C 1 48  ? 36.530 48.064 98.317  1.00 49.33  ? 112 GLN C CA  1 
ATOM   5865  C  C   . GLN C 1 48  ? 36.952 48.928 97.150  1.00 47.80  ? 112 GLN C C   1 
ATOM   5866  O  O   . GLN C 1 48  ? 38.132 49.279 97.003  1.00 52.80  ? 112 GLN C O   1 
ATOM   5867  C  CB  . GLN C 1 48  ? 37.723 47.267 98.893  1.00 44.92  ? 112 GLN C CB  1 
ATOM   5868  C  CG  . GLN C 1 48  ? 39.055 47.804 98.353  1.00 69.29  ? 112 GLN C CG  1 
ATOM   5869  C  CD  . GLN C 1 48  ? 40.130 48.016 99.381  1.00 72.95  ? 112 GLN C CD  1 
ATOM   5870  O  OE1 . GLN C 1 48  ? 41.329 48.343 98.910  1.00 74.08  ? 112 GLN C OE1 1 
ATOM   5871  N  NE2 . GLN C 1 48  ? 39.899 47.886 100.579 1.00 59.56  ? 112 GLN C NE2 1 
ATOM   5872  N  N   . ASN C 1 49  ? 35.971 49.272 96.324  1.00 49.76  ? 113 ASN C N   1 
ATOM   5873  C  CA  . ASN C 1 49  ? 36.164 50.257 95.260  1.00 47.86  ? 113 ASN C CA  1 
ATOM   5874  C  C   . ASN C 1 49  ? 36.854 51.544 95.694  1.00 47.90  ? 113 ASN C C   1 
ATOM   5875  O  O   . ASN C 1 49  ? 36.567 52.126 96.780  1.00 42.72  ? 113 ASN C O   1 
ATOM   5876  C  CB  . ASN C 1 49  ? 34.825 50.599 94.642  1.00 47.94  ? 113 ASN C CB  1 
ATOM   5877  C  CG  . ASN C 1 49  ? 34.174 49.387 93.981  1.00 60.13  ? 113 ASN C CG  1 
ATOM   5878  O  OD1 . ASN C 1 49  ? 34.256 49.209 92.740  1.00 53.52  ? 113 ASN C OD1 1 
ATOM   5879  N  ND2 . ASN C 1 49  ? 33.537 48.531 94.806  1.00 52.79  ? 113 ASN C ND2 1 
ATOM   5880  N  N   . PHE C 1 50  ? 37.789 51.985 94.858  1.00 46.21  ? 114 PHE C N   1 
ATOM   5881  C  CA  . PHE C 1 50  ? 38.231 53.372 94.964  1.00 50.89  ? 114 PHE C CA  1 
ATOM   5882  C  C   . PHE C 1 50  ? 38.679 53.933 93.649  1.00 46.54  ? 114 PHE C C   1 
ATOM   5883  O  O   . PHE C 1 50  ? 38.601 53.266 92.634  1.00 63.44  ? 114 PHE C O   1 
ATOM   5884  C  CB  . PHE C 1 50  ? 39.307 53.509 96.002  1.00 54.46  ? 114 PHE C CB  1 
ATOM   5885  C  CG  . PHE C 1 50  ? 40.558 52.786 95.674  1.00 50.10  ? 114 PHE C CG  1 
ATOM   5886  C  CD1 . PHE C 1 50  ? 40.725 51.457 96.051  1.00 54.46  ? 114 PHE C CD1 1 
ATOM   5887  C  CD2 . PHE C 1 50  ? 41.594 53.451 95.030  1.00 47.86  ? 114 PHE C CD2 1 
ATOM   5888  C  CE1 . PHE C 1 50  ? 41.903 50.799 95.781  1.00 59.81  ? 114 PHE C CE1 1 
ATOM   5889  C  CE2 . PHE C 1 50  ? 42.782 52.813 94.760  1.00 55.78  ? 114 PHE C CE2 1 
ATOM   5890  C  CZ  . PHE C 1 50  ? 42.941 51.477 95.130  1.00 57.86  ? 114 PHE C CZ  1 
ATOM   5891  N  N   . VAL C 1 51  ? 39.134 55.162 93.646  1.00 41.07  ? 115 VAL C N   1 
ATOM   5892  C  CA  . VAL C 1 51  ? 39.524 55.777 92.394  1.00 40.74  ? 115 VAL C CA  1 
ATOM   5893  C  C   . VAL C 1 51  ? 40.837 56.414 92.621  1.00 42.72  ? 115 VAL C C   1 
ATOM   5894  O  O   . VAL C 1 51  ? 41.086 57.020 93.682  1.00 55.41  ? 115 VAL C O   1 
ATOM   5895  C  CB  . VAL C 1 51  ? 38.518 56.867 91.956  1.00 38.79  ? 115 VAL C CB  1 
ATOM   5896  C  CG1 . VAL C 1 51  ? 39.003 57.614 90.740  1.00 35.78  ? 115 VAL C CG1 1 
ATOM   5897  C  CG2 . VAL C 1 51  ? 37.230 56.226 91.628  1.00 42.74  ? 115 VAL C CG2 1 
ATOM   5898  N  N   . SER C 1 52  ? 41.667 56.280 91.613  1.00 42.21  ? 116 SER C N   1 
ATOM   5899  C  CA  . SER C 1 52  ? 42.983 56.886 91.576  1.00 54.61  ? 116 SER C CA  1 
ATOM   5900  C  C   . SER C 1 52  ? 43.249 57.386 90.159  1.00 53.34  ? 116 SER C C   1 
ATOM   5901  O  O   . SER C 1 52  ? 42.912 56.708 89.190  1.00 49.89  ? 116 SER C O   1 
ATOM   5902  C  CB  . SER C 1 52  ? 44.061 55.860 91.985  1.00 56.40  ? 116 SER C CB  1 
ATOM   5903  O  OG  . SER C 1 52  ? 45.364 56.447 91.971  1.00 74.22  ? 116 SER C OG  1 
ATOM   5904  N  N   . CYS C 1 53  ? 43.862 58.553 90.026  1.00 57.12  ? 117 CYS C N   1 
ATOM   5905  C  CA  . CYS C 1 53  ? 44.097 59.075 88.698  1.00 63.06  ? 117 CYS C CA  1 
ATOM   5906  C  C   . CYS C 1 53  ? 45.564 59.076 88.269  1.00 62.51  ? 117 CYS C C   1 
ATOM   5907  O  O   . CYS C 1 53  ? 46.449 59.293 89.083  1.00 87.07  ? 117 CYS C O   1 
ATOM   5908  C  CB  . CYS C 1 53  ? 43.450 60.450 88.555  1.00 68.13  ? 117 CYS C CB  1 
ATOM   5909  S  SG  . CYS C 1 53  ? 41.689 60.372 88.865  1.00 100.75 ? 117 CYS C SG  1 
ATOM   5910  N  N   . SER C 1 54  ? 45.799 58.800 86.988  1.00 62.35  ? 118 SER C N   1 
ATOM   5911  C  CA  . SER C 1 54  ? 47.075 59.092 86.328  1.00 62.15  ? 118 SER C CA  1 
ATOM   5912  C  C   . SER C 1 54  ? 46.953 60.445 85.630  1.00 75.61  ? 118 SER C C   1 
ATOM   5913  O  O   . SER C 1 54  ? 45.954 61.160 85.801  1.00 93.11  ? 118 SER C O   1 
ATOM   5914  C  CB  . SER C 1 54  ? 47.482 57.978 85.339  1.00 63.86  ? 118 SER C CB  1 
ATOM   5915  O  OG  . SER C 1 54  ? 46.822 58.038 84.075  1.00 72.95  ? 118 SER C OG  1 
ATOM   5916  N  N   . ASP C 1 55  ? 47.965 60.805 84.849  1.00 80.49  ? 119 ASP C N   1 
ATOM   5917  C  CA  . ASP C 1 55  ? 47.958 62.084 84.143  1.00 94.38  ? 119 ASP C CA  1 
ATOM   5918  C  C   . ASP C 1 55  ? 47.192 61.957 82.845  1.00 92.87  ? 119 ASP C C   1 
ATOM   5919  O  O   . ASP C 1 55  ? 46.925 62.941 82.158  1.00 127.51 ? 119 ASP C O   1 
ATOM   5920  C  CB  . ASP C 1 55  ? 49.395 62.569 83.892  1.00 137.15 ? 119 ASP C CB  1 
ATOM   5921  C  CG  . ASP C 1 55  ? 50.302 61.484 83.308  1.00 152.44 ? 119 ASP C CG  1 
ATOM   5922  O  OD1 . ASP C 1 55  ? 49.801 60.483 82.746  1.00 157.04 ? 119 ASP C OD1 1 
ATOM   5923  O  OD2 . ASP C 1 55  ? 51.536 61.644 83.409  1.00 167.76 ? 119 ASP C OD2 1 
ATOM   5924  N  N   . LYS C 1 56  ? 46.841 60.716 82.538  1.00 96.22  ? 120 LYS C N   1 
ATOM   5925  C  CA  . LYS C 1 56  ? 46.233 60.315 81.287  1.00 86.62  ? 120 LYS C CA  1 
ATOM   5926  C  C   . LYS C 1 56  ? 44.742 60.034 81.487  1.00 81.38  ? 120 LYS C C   1 
ATOM   5927  O  O   . LYS C 1 56  ? 43.940 60.300 80.600  1.00 97.22  ? 120 LYS C O   1 
ATOM   5928  C  CB  . LYS C 1 56  ? 46.956 59.058 80.786  1.00 102.07 ? 120 LYS C CB  1 
ATOM   5929  C  CG  . LYS C 1 56  ? 46.385 58.397 79.509  1.00 138.24 ? 120 LYS C CG  1 
ATOM   5930  C  CD  . LYS C 1 56  ? 47.027 57.031 79.189  1.00 119.20 ? 120 LYS C CD  1 
ATOM   5931  C  CE  . LYS C 1 56  ? 48.526 57.153 78.893  1.00 166.76 ? 120 LYS C CE  1 
ATOM   5932  N  NZ  . LYS C 1 56  ? 49.392 57.183 80.120  1.00 196.58 ? 120 LYS C NZ  1 
ATOM   5933  N  N   . GLU C 1 57  ? 44.376 59.517 82.662  1.00 80.12  ? 121 GLU C N   1 
ATOM   5934  C  CA  . GLU C 1 57  ? 43.036 58.965 82.901  1.00 78.74  ? 121 GLU C CA  1 
ATOM   5935  C  C   . GLU C 1 57  ? 42.849 58.589 84.354  1.00 75.45  ? 121 GLU C C   1 
ATOM   5936  O  O   . GLU C 1 57  ? 43.837 58.426 85.083  1.00 66.43  ? 121 GLU C O   1 
ATOM   5937  C  CB  . GLU C 1 57  ? 42.867 57.682 82.102  1.00 82.66  ? 121 GLU C CB  1 
ATOM   5938  C  CG  . GLU C 1 57  ? 43.469 56.468 82.810  1.00 88.53  ? 121 GLU C CG  1 
ATOM   5939  C  CD  . GLU C 1 57  ? 43.603 55.234 81.934  1.00 98.81  ? 121 GLU C CD  1 
ATOM   5940  O  OE1 . GLU C 1 57  ? 42.908 55.127 80.892  1.00 112.15 ? 121 GLU C OE1 1 
ATOM   5941  O  OE2 . GLU C 1 57  ? 44.410 54.358 82.317  1.00 89.08  ? 121 GLU C OE2 1 
ATOM   5942  N  N   . CYS C 1 58  ? 41.587 58.398 84.748  1.00 68.64  ? 122 CYS C N   1 
ATOM   5943  C  CA  . CYS C 1 58  ? 41.254 57.952 86.104  1.00 63.19  ? 122 CYS C CA  1 
ATOM   5944  C  C   . CYS C 1 58  ? 40.832 56.506 86.069  1.00 50.53  ? 122 CYS C C   1 
ATOM   5945  O  O   . CYS C 1 58  ? 40.093 56.107 85.159  1.00 49.70  ? 122 CYS C O   1 
ATOM   5946  C  CB  . CYS C 1 58  ? 40.160 58.823 86.727  1.00 62.45  ? 122 CYS C CB  1 
ATOM   5947  S  SG  . CYS C 1 58  ? 40.766 60.460 87.025  1.00 105.15 ? 122 CYS C SG  1 
ATOM   5948  N  N   . ARG C 1 59  ? 41.302 55.722 87.044  1.00 43.99  ? 123 ARG C N   1 
ATOM   5949  C  CA  . ARG C 1 59  ? 40.988 54.296 87.057  1.00 43.05  ? 123 ARG C CA  1 
ATOM   5950  C  C   . ARG C 1 59  ? 40.220 53.952 88.268  1.00 42.54  ? 123 ARG C C   1 
ATOM   5951  O  O   . ARG C 1 59  ? 40.376 54.611 89.311  1.00 49.00  ? 123 ARG C O   1 
ATOM   5952  C  CB  . ARG C 1 59  ? 42.245 53.465 86.974  1.00 44.15  ? 123 ARG C CB  1 
ATOM   5953  C  CG  . ARG C 1 59  ? 42.970 53.667 85.650  1.00 51.67  ? 123 ARG C CG  1 
ATOM   5954  C  CD  . ARG C 1 59  ? 44.011 52.615 85.368  1.00 55.90  ? 123 ARG C CD  1 
ATOM   5955  N  NE  . ARG C 1 59  ? 43.424 51.281 85.177  1.00 57.54  ? 123 ARG C NE  1 
ATOM   5956  C  CZ  . ARG C 1 59  ? 42.875 50.846 84.058  1.00 47.03  ? 123 ARG C CZ  1 
ATOM   5957  N  NH1 . ARG C 1 59  ? 42.820 51.616 82.990  1.00 51.77  ? 123 ARG C NH1 1 
ATOM   5958  N  NH2 . ARG C 1 59  ? 42.389 49.632 84.022  1.00 47.74  ? 123 ARG C NH2 1 
ATOM   5959  N  N   . ARG C 1 60  ? 39.362 52.942 88.135  1.00 38.81  ? 124 ARG C N   1 
ATOM   5960  C  CA  . ARG C 1 60  ? 38.621 52.456 89.294  1.00 41.70  ? 124 ARG C CA  1 
ATOM   5961  C  C   . ARG C 1 60  ? 39.225 51.151 89.777  1.00 49.50  ? 124 ARG C C   1 
ATOM   5962  O  O   . ARG C 1 60  ? 39.226 50.186 89.043  1.00 76.17  ? 124 ARG C O   1 
ATOM   5963  C  CB  . ARG C 1 60  ? 37.186 52.271 88.941  1.00 35.80  ? 124 ARG C CB  1 
ATOM   5964  C  CG  . ARG C 1 60  ? 36.438 51.253 89.770  1.00 41.21  ? 124 ARG C CG  1 
ATOM   5965  C  CD  . ARG C 1 60  ? 34.946 51.415 89.530  1.00 47.36  ? 124 ARG C CD  1 
ATOM   5966  N  NE  . ARG C 1 60  ? 34.131 50.383 90.133  1.00 50.38  ? 124 ARG C NE  1 
ATOM   5967  C  CZ  . ARG C 1 60  ? 32.956 50.000 89.639  1.00 69.51  ? 124 ARG C CZ  1 
ATOM   5968  N  NH1 . ARG C 1 60  ? 32.475 50.572 88.523  1.00 69.57  ? 124 ARG C NH1 1 
ATOM   5969  N  NH2 . ARG C 1 60  ? 32.259 49.047 90.258  1.00 64.72  ? 124 ARG C NH2 1 
ATOM   5970  N  N   . PHE C 1 61  ? 39.779 51.118 90.984  1.00 45.89  ? 125 PHE C N   1 
ATOM   5971  C  CA  . PHE C 1 61  ? 40.330 49.875 91.507  1.00 49.77  ? 125 PHE C CA  1 
ATOM   5972  C  C   . PHE C 1 61  ? 39.313 49.206 92.365  1.00 54.99  ? 125 PHE C C   1 
ATOM   5973  O  O   . PHE C 1 61  ? 38.498 49.882 93.000  1.00 79.06  ? 125 PHE C O   1 
ATOM   5974  C  CB  . PHE C 1 61  ? 41.588 50.143 92.306  1.00 41.43  ? 125 PHE C CB  1 
ATOM   5975  C  CG  . PHE C 1 61  ? 42.725 50.601 91.459  1.00 44.80  ? 125 PHE C CG  1 
ATOM   5976  C  CD1 . PHE C 1 61  ? 42.701 51.870 90.888  1.00 39.54  ? 125 PHE C CD1 1 
ATOM   5977  C  CD2 . PHE C 1 61  ? 43.807 49.757 91.193  1.00 45.00  ? 125 PHE C CD2 1 
ATOM   5978  C  CE1 . PHE C 1 61  ? 43.753 52.315 90.093  1.00 40.87  ? 125 PHE C CE1 1 
ATOM   5979  C  CE2 . PHE C 1 61  ? 44.864 50.191 90.411  1.00 43.30  ? 125 PHE C CE2 1 
ATOM   5980  C  CZ  . PHE C 1 61  ? 44.832 51.474 89.844  1.00 40.93  ? 125 PHE C CZ  1 
ATOM   5981  N  N   . PHE C 1 62  ? 39.345 47.887 92.403  1.00 42.72  ? 126 PHE C N   1 
ATOM   5982  C  CA  . PHE C 1 62  ? 38.481 47.217 93.349  1.00 50.47  ? 126 PHE C CA  1 
ATOM   5983  C  C   . PHE C 1 62  ? 38.978 45.802 93.672  1.00 51.19  ? 126 PHE C C   1 
ATOM   5984  O  O   . PHE C 1 62  ? 39.983 45.350 93.135  1.00 56.07  ? 126 PHE C O   1 
ATOM   5985  C  CB  . PHE C 1 62  ? 37.047 47.221 92.811  1.00 57.73  ? 126 PHE C CB  1 
ATOM   5986  C  CG  . PHE C 1 62  ? 36.912 46.515 91.524  1.00 65.37  ? 126 PHE C CG  1 
ATOM   5987  C  CD1 . PHE C 1 62  ? 36.709 45.132 91.481  1.00 68.23  ? 126 PHE C CD1 1 
ATOM   5988  C  CD2 . PHE C 1 62  ? 37.056 47.205 90.348  1.00 73.13  ? 126 PHE C CD2 1 
ATOM   5989  C  CE1 . PHE C 1 62  ? 36.618 44.458 90.270  1.00 60.34  ? 126 PHE C CE1 1 
ATOM   5990  C  CE2 . PHE C 1 62  ? 36.966 46.544 89.134  1.00 74.88  ? 126 PHE C CE2 1 
ATOM   5991  C  CZ  . PHE C 1 62  ? 36.746 45.167 89.099  1.00 71.88  ? 126 PHE C CZ  1 
ATOM   5992  N  N   . VAL C 1 63  ? 38.282 45.121 94.567  1.00 45.02  ? 127 VAL C N   1 
ATOM   5993  C  CA  . VAL C 1 63  ? 38.615 43.777 94.922  1.00 47.18  ? 127 VAL C CA  1 
ATOM   5994  C  C   . VAL C 1 63  ? 37.462 42.884 94.447  1.00 51.72  ? 127 VAL C C   1 
ATOM   5995  O  O   . VAL C 1 63  ? 36.297 43.185 94.718  1.00 51.16  ? 127 VAL C O   1 
ATOM   5996  C  CB  . VAL C 1 63  ? 38.822 43.691 96.440  1.00 51.96  ? 127 VAL C CB  1 
ATOM   5997  C  CG1 . VAL C 1 63  ? 38.879 42.243 96.932  1.00 54.42  ? 127 VAL C CG1 1 
ATOM   5998  C  CG2 . VAL C 1 63  ? 40.076 44.431 96.848  1.00 57.09  ? 127 VAL C CG2 1 
ATOM   5999  N  N   . SER C 1 64  ? 37.792 41.797 93.741  1.00 55.91  ? 128 SER C N   1 
ATOM   6000  C  CA  . SER C 1 64  ? 36.791 40.892 93.179  1.00 64.67  ? 128 SER C CA  1 
ATOM   6001  C  C   . SER C 1 64  ? 36.213 39.952 94.215  1.00 72.13  ? 128 SER C C   1 
ATOM   6002  O  O   . SER C 1 64  ? 36.918 39.479 95.117  1.00 91.07  ? 128 SER C O   1 
ATOM   6003  C  CB  . SER C 1 64  ? 37.387 40.050 92.058  1.00 76.33  ? 128 SER C CB  1 
ATOM   6004  O  OG  . SER C 1 64  ? 38.319 39.120 92.577  1.00 98.92  ? 128 SER C OG  1 
ATOM   6005  N  N   . MET C 1 65  ? 34.923 39.685 94.073  1.00 66.08  ? 129 MET C N   1 
ATOM   6006  C  CA  . MET C 1 65  ? 34.287 38.596 94.795  1.00 88.00  ? 129 MET C CA  1 
ATOM   6007  C  C   . MET C 1 65  ? 33.956 37.410 93.860  1.00 99.14  ? 129 MET C C   1 
ATOM   6008  O  O   . MET C 1 65  ? 33.350 36.417 94.286  1.00 115.48 ? 129 MET C O   1 
ATOM   6009  C  CB  . MET C 1 65  ? 33.035 39.075 95.545  1.00 90.46  ? 129 MET C CB  1 
ATOM   6010  C  CG  . MET C 1 65  ? 33.273 39.503 96.989  1.00 87.36  ? 129 MET C CG  1 
ATOM   6011  S  SD  . MET C 1 65  ? 32.867 41.233 97.328  1.00 103.08 ? 129 MET C SD  1 
ATOM   6012  C  CE  . MET C 1 65  ? 31.070 41.169 97.494  1.00 76.56  ? 129 MET C CE  1 
ATOM   6013  N  N   . GLY C 1 66  ? 34.379 37.492 92.601  1.00 79.50  ? 130 GLY C N   1 
ATOM   6014  C  CA  . GLY C 1 66  ? 33.989 36.478 91.623  1.00 74.01  ? 130 GLY C CA  1 
ATOM   6015  C  C   . GLY C 1 66  ? 32.909 37.033 90.711  1.00 79.16  ? 130 GLY C C   1 
ATOM   6016  O  O   . GLY C 1 66  ? 32.396 38.129 90.936  1.00 82.20  ? 130 GLY C O   1 
ATOM   6017  N  N   . TYR C 1 67  ? 32.578 36.299 89.658  1.00 77.31  ? 131 TYR C N   1 
ATOM   6018  C  CA  . TYR C 1 67  ? 31.541 36.744 88.745  1.00 76.40  ? 131 TYR C CA  1 
ATOM   6019  C  C   . TYR C 1 67  ? 30.182 36.469 89.359  1.00 80.49  ? 131 TYR C C   1 
ATOM   6020  O  O   . TYR C 1 67  ? 30.015 35.507 90.109  1.00 87.30  ? 131 TYR C O   1 
ATOM   6021  C  CB  . TYR C 1 67  ? 31.657 36.009 87.429  1.00 81.29  ? 131 TYR C CB  1 
ATOM   6022  C  CG  . TYR C 1 67  ? 32.985 36.188 86.745  1.00 96.20  ? 131 TYR C CG  1 
ATOM   6023  C  CD1 . TYR C 1 67  ? 33.333 37.402 86.156  1.00 100.98 ? 131 TYR C CD1 1 
ATOM   6024  C  CD2 . TYR C 1 67  ? 33.890 35.137 86.665  1.00 105.72 ? 131 TYR C CD2 1 
ATOM   6025  C  CE1 . TYR C 1 67  ? 34.558 37.559 85.506  1.00 85.30  ? 131 TYR C CE1 1 
ATOM   6026  C  CE2 . TYR C 1 67  ? 35.106 35.282 86.010  1.00 99.73  ? 131 TYR C CE2 1 
ATOM   6027  C  CZ  . TYR C 1 67  ? 35.433 36.494 85.439  1.00 83.65  ? 131 TYR C CZ  1 
ATOM   6028  O  OH  . TYR C 1 67  ? 36.638 36.623 84.792  1.00 92.48  ? 131 TYR C OH  1 
ATOM   6029  N  N   . GLY C 1 68  ? 29.210 37.314 89.040  1.00 77.17  ? 132 GLY C N   1 
ATOM   6030  C  CA  . GLY C 1 68  ? 27.870 37.192 89.615  1.00 96.47  ? 132 GLY C CA  1 
ATOM   6031  C  C   . GLY C 1 68  ? 27.092 35.968 89.155  1.00 100.61 ? 132 GLY C C   1 
ATOM   6032  O  O   . GLY C 1 68  ? 26.170 35.514 89.831  1.00 121.85 ? 132 GLY C O   1 
ATOM   6033  N  N   . THR C 1 69  ? 27.468 35.438 88.001  1.00 80.72  ? 133 THR C N   1 
ATOM   6034  C  CA  . THR C 1 69  ? 26.811 34.274 87.440  1.00 100.01 ? 133 THR C CA  1 
ATOM   6035  C  C   . THR C 1 69  ? 27.362 32.948 87.989  1.00 111.80 ? 133 THR C C   1 
ATOM   6036  O  O   . THR C 1 69  ? 26.633 31.948 88.096  1.00 122.03 ? 133 THR C O   1 
ATOM   6037  C  CB  . THR C 1 69  ? 26.850 34.296 85.882  1.00 103.38 ? 133 THR C CB  1 
ATOM   6038  O  OG1 . THR C 1 69  ? 26.311 33.074 85.375  1.00 151.81 ? 133 THR C OG1 1 
ATOM   6039  C  CG2 . THR C 1 69  ? 28.262 34.486 85.324  1.00 71.26  ? 133 THR C CG2 1 
ATOM   6040  N  N   . THR C 1 70  ? 28.644 32.954 88.341  1.00 106.37 ? 134 THR C N   1 
ATOM   6041  C  CA  . THR C 1 70  ? 29.325 31.753 88.804  1.00 107.08 ? 134 THR C CA  1 
ATOM   6042  C  C   . THR C 1 70  ? 29.276 31.670 90.323  1.00 113.99 ? 134 THR C C   1 
ATOM   6043  O  O   . THR C 1 70  ? 29.716 30.670 90.905  1.00 122.44 ? 134 THR C O   1 
ATOM   6044  C  CB  . THR C 1 70  ? 30.794 31.729 88.338  1.00 111.57 ? 134 THR C CB  1 
ATOM   6045  O  OG1 . THR C 1 70  ? 31.589 32.593 89.167  1.00 105.76 ? 134 THR C OG1 1 
ATOM   6046  C  CG2 . THR C 1 70  ? 30.899 32.179 86.887  1.00 127.01 ? 134 THR C CG2 1 
ATOM   6047  N  N   . THR C 1 71  ? 28.745 32.725 90.950  1.00 89.61  ? 135 THR C N   1 
ATOM   6048  C  CA  . THR C 1 71  ? 28.661 32.814 92.404  1.00 100.47 ? 135 THR C CA  1 
ATOM   6049  C  C   . THR C 1 71  ? 27.247 32.497 92.864  1.00 113.06 ? 135 THR C C   1 
ATOM   6050  O  O   . THR C 1 71  ? 26.297 33.108 92.391  1.00 129.26 ? 135 THR C O   1 
ATOM   6051  C  CB  . THR C 1 71  ? 29.068 34.225 92.919  1.00 94.50  ? 135 THR C CB  1 
ATOM   6052  O  OG1 . THR C 1 71  ? 30.452 34.471 92.630  1.00 76.02  ? 135 THR C OG1 1 
ATOM   6053  C  CG2 . THR C 1 71  ? 28.828 34.359 94.431  1.00 90.84  ? 135 THR C CG2 1 
ATOM   6054  N  N   . ASN C 1 72  ? 27.117 31.538 93.780  1.00 135.75 ? 136 ASN C N   1 
ATOM   6055  C  CA  . ASN C 1 72  ? 25.826 31.210 94.383  1.00 154.13 ? 136 ASN C CA  1 
ATOM   6056  C  C   . ASN C 1 72  ? 25.660 31.944 95.716  1.00 166.07 ? 136 ASN C C   1 
ATOM   6057  O  O   . ASN C 1 72  ? 26.638 32.143 96.438  1.00 148.50 ? 136 ASN C O   1 
ATOM   6058  C  CB  . ASN C 1 72  ? 25.659 29.689 94.549  1.00 135.74 ? 136 ASN C CB  1 
ATOM   6059  C  CG  . ASN C 1 72  ? 24.218 29.283 94.789  1.00 134.85 ? 136 ASN C CG  1 
ATOM   6060  O  OD1 . ASN C 1 72  ? 23.286 30.023 94.464  1.00 158.66 ? 136 ASN C OD1 1 
ATOM   6061  N  ND2 . ASN C 1 72  ? 24.027 28.103 95.364  1.00 118.33 ? 136 ASN C ND2 1 
ATOM   6062  N  N   . PHE C 1 73  ? 24.424 32.347 96.025  1.00 184.52 ? 137 PHE C N   1 
ATOM   6063  C  CA  . PHE C 1 73  ? 24.120 33.164 97.209  1.00 170.15 ? 137 PHE C CA  1 
ATOM   6064  C  C   . PHE C 1 73  ? 24.472 32.502 98.544  1.00 199.77 ? 137 PHE C C   1 
ATOM   6065  O  O   . PHE C 1 73  ? 24.988 33.168 99.448  1.00 198.74 ? 137 PHE C O   1 
ATOM   6066  C  CB  . PHE C 1 73  ? 22.646 33.605 97.221  1.00 150.55 ? 137 PHE C CB  1 
ATOM   6067  C  CG  . PHE C 1 73  ? 22.282 34.473 98.402  1.00 170.15 ? 137 PHE C CG  1 
ATOM   6068  C  CD1 . PHE C 1 73  ? 22.718 35.800 98.471  1.00 164.50 ? 137 PHE C CD1 1 
ATOM   6069  C  CD2 . PHE C 1 73  ? 21.517 33.962 99.453  1.00 174.34 ? 137 PHE C CD2 1 
ATOM   6070  C  CE1 . PHE C 1 73  ? 22.394 36.606 99.566  1.00 167.48 ? 137 PHE C CE1 1 
ATOM   6071  C  CE2 . PHE C 1 73  ? 21.186 34.761 100.557 1.00 172.50 ? 137 PHE C CE2 1 
ATOM   6072  C  CZ  . PHE C 1 73  ? 21.623 36.085 100.611 1.00 172.88 ? 137 PHE C CZ  1 
ATOM   6073  N  N   . ALA C 1 74  ? 24.186 31.200 98.654  1.00 211.85 ? 138 ALA C N   1 
ATOM   6074  C  CA  . ALA C 1 74  ? 24.407 30.418 99.884  1.00 180.71 ? 138 ALA C CA  1 
ATOM   6075  C  C   . ALA C 1 74  ? 25.863 30.431 100.373 1.00 180.17 ? 138 ALA C C   1 
ATOM   6076  O  O   . ALA C 1 74  ? 26.116 30.296 101.574 1.00 158.89 ? 138 ALA C O   1 
ATOM   6077  C  CB  . ALA C 1 74  ? 23.902 28.975 99.710  1.00 138.28 ? 138 ALA C CB  1 
ATOM   6078  N  N   . ASP C 1 75  ? 26.803 30.595 99.438  1.00 202.24 ? 139 ASP C N   1 
ATOM   6079  C  CA  . ASP C 1 75  ? 28.222 30.780 99.762  1.00 184.95 ? 139 ASP C CA  1 
ATOM   6080  C  C   . ASP C 1 75  ? 28.484 32.147 100.352 1.00 171.91 ? 139 ASP C C   1 
ATOM   6081  O  O   . ASP C 1 75  ? 27.941 33.154 99.896  1.00 176.80 ? 139 ASP C O   1 
ATOM   6082  C  CB  . ASP C 1 75  ? 29.103 30.654 98.516  1.00 156.34 ? 139 ASP C CB  1 
ATOM   6083  C  CG  . ASP C 1 75  ? 29.134 29.252 97.953  1.00 160.07 ? 139 ASP C CG  1 
ATOM   6084  O  OD1 . ASP C 1 75  ? 28.733 28.300 98.653  1.00 162.45 ? 139 ASP C OD1 1 
ATOM   6085  O  OD2 . ASP C 1 75  ? 29.573 29.099 96.798  1.00 167.92 ? 139 ASP C OD2 1 
ATOM   6086  N  N   . LEU C 1 76  ? 29.313 32.173 101.381 1.00 174.13 ? 140 LEU C N   1 
ATOM   6087  C  CA  . LEU C 1 76  ? 29.969 33.398 101.763 1.00 183.12 ? 140 LEU C CA  1 
ATOM   6088  C  C   . LEU C 1 76  ? 31.367 33.217 101.192 1.00 163.80 ? 140 LEU C C   1 
ATOM   6089  O  O   . LEU C 1 76  ? 31.934 32.124 101.272 1.00 136.27 ? 140 LEU C O   1 
ATOM   6090  C  CB  . LEU C 1 76  ? 29.949 33.606 103.292 1.00 182.92 ? 140 LEU C CB  1 
ATOM   6091  C  CG  . LEU C 1 76  ? 28.706 34.285 103.912 1.00 169.94 ? 140 LEU C CG  1 
ATOM   6092  C  CD1 . LEU C 1 76  ? 27.454 33.389 103.885 1.00 178.18 ? 140 LEU C CD1 1 
ATOM   6093  C  CD2 . LEU C 1 76  ? 28.978 34.769 105.335 1.00 133.72 ? 140 LEU C CD2 1 
ATOM   6094  N  N   . ILE C 1 77  ? 31.886 34.256 100.543 1.00 156.56 ? 141 ILE C N   1 
ATOM   6095  C  CA  . ILE C 1 77  ? 33.238 34.204 99.995  1.00 137.93 ? 141 ILE C CA  1 
ATOM   6096  C  C   . ILE C 1 77  ? 34.266 34.888 100.908 1.00 127.43 ? 141 ILE C C   1 
ATOM   6097  O  O   . ILE C 1 77  ? 33.942 35.764 101.722 1.00 106.24 ? 141 ILE C O   1 
ATOM   6098  C  CB  . ILE C 1 77  ? 33.323 34.740 98.545  1.00 138.86 ? 141 ILE C CB  1 
ATOM   6099  C  CG1 . ILE C 1 77  ? 34.641 34.280 97.896  1.00 141.07 ? 141 ILE C CG1 1 
ATOM   6100  C  CG2 . ILE C 1 77  ? 33.153 36.272 98.525  1.00 106.96 ? 141 ILE C CG2 1 
ATOM   6101  C  CD1 . ILE C 1 77  ? 34.585 34.025 96.393  1.00 119.96 ? 141 ILE C CD1 1 
ATOM   6102  N  N   . VAL C 1 78  ? 35.515 34.490 100.723 1.00 103.37 ? 142 VAL C N   1 
ATOM   6103  C  CA  . VAL C 1 78  ? 36.525 34.653 101.734 1.00 81.47  ? 142 VAL C CA  1 
ATOM   6104  C  C   . VAL C 1 78  ? 37.749 35.398 101.185 1.00 78.38  ? 142 VAL C C   1 
ATOM   6105  O  O   . VAL C 1 78  ? 38.098 35.244 100.014 1.00 78.62  ? 142 VAL C O   1 
ATOM   6106  C  CB  . VAL C 1 78  ? 36.877 33.256 102.300 1.00 77.89  ? 142 VAL C CB  1 
ATOM   6107  C  CG1 . VAL C 1 78  ? 37.240 32.262 101.179 1.00 76.79  ? 142 VAL C CG1 1 
ATOM   6108  C  CG2 . VAL C 1 78  ? 37.975 33.351 103.347 1.00 94.80  ? 142 VAL C CG2 1 
ATOM   6109  N  N   . SER C 1 79  ? 38.388 36.197 102.040 1.00 69.72  ? 143 SER C N   1 
ATOM   6110  C  CA  . SER C 1 79  ? 39.533 37.049 101.667 1.00 81.90  ? 143 SER C CA  1 
ATOM   6111  C  C   . SER C 1 79  ? 40.662 36.381 100.851 1.00 79.19  ? 143 SER C C   1 
ATOM   6112  O  O   . SER C 1 79  ? 41.295 37.005 99.989  1.00 90.08  ? 143 SER C O   1 
ATOM   6113  C  CB  . SER C 1 79  ? 40.128 37.703 102.923 1.00 89.85  ? 143 SER C CB  1 
ATOM   6114  O  OG  . SER C 1 79  ? 39.120 38.293 103.729 1.00 111.93 ? 143 SER C OG  1 
ATOM   6115  N  N   . GLU C 1 80  ? 40.918 35.114 101.124 1.00 75.07  ? 144 GLU C N   1 
ATOM   6116  C  CA  . GLU C 1 80  ? 42.009 34.413 100.461 1.00 85.43  ? 144 GLU C CA  1 
ATOM   6117  C  C   . GLU C 1 80  ? 41.737 34.162 99.002  1.00 71.69  ? 144 GLU C C   1 
ATOM   6118  O  O   . GLU C 1 80  ? 42.656 33.851 98.249  1.00 72.00  ? 144 GLU C O   1 
ATOM   6119  C  CB  . GLU C 1 80  ? 42.308 33.081 101.150 1.00 105.57 ? 144 GLU C CB  1 
ATOM   6120  C  CG  . GLU C 1 80  ? 42.963 33.228 102.527 1.00 153.35 ? 144 GLU C CG  1 
ATOM   6121  C  CD  . GLU C 1 80  ? 42.013 33.773 103.591 1.00 152.59 ? 144 GLU C CD  1 
ATOM   6122  O  OE1 . GLU C 1 80  ? 40.777 33.636 103.430 1.00 117.85 ? 144 GLU C OE1 1 
ATOM   6123  O  OE2 . GLU C 1 80  ? 42.509 34.338 104.591 1.00 161.67 ? 144 GLU C OE2 1 
ATOM   6124  N  N   . GLN C 1 81  ? 40.476 34.290 98.610  1.00 66.16  ? 145 GLN C N   1 
ATOM   6125  C  CA  . GLN C 1 81  ? 40.071 34.022 97.238  1.00 67.16  ? 145 GLN C CA  1 
ATOM   6126  C  C   . GLN C 1 81  ? 40.045 35.283 96.425  1.00 68.88  ? 145 GLN C C   1 
ATOM   6127  O  O   . GLN C 1 81  ? 39.798 35.249 95.230  1.00 91.92  ? 145 GLN C O   1 
ATOM   6128  C  CB  . GLN C 1 81  ? 38.702 33.355 97.194  1.00 72.43  ? 145 GLN C CB  1 
ATOM   6129  C  CG  . GLN C 1 81  ? 38.664 31.966 97.847  1.00 92.63  ? 145 GLN C CG  1 
ATOM   6130  C  CD  . GLN C 1 81  ? 37.408 31.179 97.508  1.00 94.51  ? 145 GLN C CD  1 
ATOM   6131  O  OE1 . GLN C 1 81  ? 36.315 31.470 98.001  1.00 91.62  ? 145 GLN C OE1 1 
ATOM   6132  N  NE2 . GLN C 1 81  ? 37.565 30.168 96.665  1.00 113.22 ? 145 GLN C NE2 1 
ATOM   6133  N  N   . MET C 1 82  ? 40.345 36.399 97.069  1.00 69.78  ? 146 MET C N   1 
ATOM   6134  C  CA  . MET C 1 82  ? 40.123 37.691 96.461  1.00 56.20  ? 146 MET C CA  1 
ATOM   6135  C  C   . MET C 1 82  ? 41.336 38.229 95.718  1.00 54.11  ? 146 MET C C   1 
ATOM   6136  O  O   . MET C 1 82  ? 42.485 38.013 96.118  1.00 71.82  ? 146 MET C O   1 
ATOM   6137  C  CB  . MET C 1 82  ? 39.705 38.658 97.534  1.00 61.25  ? 146 MET C CB  1 
ATOM   6138  C  CG  . MET C 1 82  ? 38.299 38.467 98.026  1.00 68.55  ? 146 MET C CG  1 
ATOM   6139  S  SD  . MET C 1 82  ? 37.933 39.575 99.410  1.00 88.84  ? 146 MET C SD  1 
ATOM   6140  C  CE  . MET C 1 82  ? 36.197 39.210 99.639  1.00 72.12  ? 146 MET C CE  1 
ATOM   6141  N  N   . ASN C 1 83  ? 41.055 38.958 94.652  1.00 46.61  ? 147 ASN C N   1 
ATOM   6142  C  CA  . ASN C 1 83  ? 42.063 39.500 93.770  1.00 49.17  ? 147 ASN C CA  1 
ATOM   6143  C  C   . ASN C 1 83  ? 41.795 40.964 93.503  1.00 48.89  ? 147 ASN C C   1 
ATOM   6144  O  O   . ASN C 1 83  ? 40.656 41.402 93.581  1.00 55.77  ? 147 ASN C O   1 
ATOM   6145  C  CB  . ASN C 1 83  ? 41.974 38.795 92.436  1.00 57.04  ? 147 ASN C CB  1 
ATOM   6146  C  CG  . ASN C 1 83  ? 42.564 37.447 92.461  1.00 54.68  ? 147 ASN C CG  1 
ATOM   6147  O  OD1 . ASN C 1 83  ? 43.589 37.233 93.080  1.00 70.38  ? 147 ASN C OD1 1 
ATOM   6148  N  ND2 . ASN C 1 83  ? 41.938 36.516 91.762  1.00 71.08  ? 147 ASN C ND2 1 
ATOM   6149  N  N   . VAL C 1 84  ? 42.838 41.699 93.145  1.00 43.07  ? 148 VAL C N   1 
ATOM   6150  C  CA  . VAL C 1 84  ? 42.710 43.125 92.929  1.00 47.46  ? 148 VAL C CA  1 
ATOM   6151  C  C   . VAL C 1 84  ? 42.677 43.416 91.463  1.00 44.86  ? 148 VAL C C   1 
ATOM   6152  O  O   . VAL C 1 84  ? 43.654 43.157 90.762  1.00 52.24  ? 148 VAL C O   1 
ATOM   6153  C  CB  . VAL C 1 84  ? 43.895 43.917 93.531  1.00 45.11  ? 148 VAL C CB  1 
ATOM   6154  C  CG1 . VAL C 1 84  ? 43.694 45.404 93.307  1.00 40.13  ? 148 VAL C CG1 1 
ATOM   6155  C  CG2 . VAL C 1 84  ? 44.064 43.583 95.001  1.00 39.30  ? 148 VAL C CG2 1 
ATOM   6156  N  N   . TYR C 1 85  ? 41.560 43.984 91.019  1.00 46.86  ? 149 TYR C N   1 
ATOM   6157  C  CA  . TYR C 1 85  ? 41.381 44.435 89.631  1.00 47.40  ? 149 TYR C CA  1 
ATOM   6158  C  C   . TYR C 1 85  ? 41.338 45.934 89.448  1.00 52.26  ? 149 TYR C C   1 
ATOM   6159  O  O   . TYR C 1 85  ? 41.043 46.706 90.374  1.00 69.61  ? 149 TYR C O   1 
ATOM   6160  C  CB  . TYR C 1 85  ? 40.120 43.840 89.049  1.00 40.38  ? 149 TYR C CB  1 
ATOM   6161  C  CG  . TYR C 1 85  ? 40.246 42.353 88.825  1.00 46.88  ? 149 TYR C CG  1 
ATOM   6162  C  CD1 . TYR C 1 85  ? 40.895 41.840 87.695  1.00 46.12  ? 149 TYR C CD1 1 
ATOM   6163  C  CD2 . TYR C 1 85  ? 39.727 41.456 89.744  1.00 51.79  ? 149 TYR C CD2 1 
ATOM   6164  C  CE1 . TYR C 1 85  ? 41.014 40.491 87.495  1.00 53.30  ? 149 TYR C CE1 1 
ATOM   6165  C  CE2 . TYR C 1 85  ? 39.827 40.091 89.543  1.00 61.29  ? 149 TYR C CE2 1 
ATOM   6166  C  CZ  . TYR C 1 85  ? 40.476 39.613 88.422  1.00 64.29  ? 149 TYR C CZ  1 
ATOM   6167  O  OH  . TYR C 1 85  ? 40.593 38.253 88.241  1.00 75.41  ? 149 TYR C OH  1 
ATOM   6168  N  N   . SER C 1 86  ? 41.628 46.335 88.225  1.00 54.85  ? 150 SER C N   1 
ATOM   6169  C  CA  . SER C 1 86  ? 41.526 47.725 87.819  1.00 60.62  ? 150 SER C CA  1 
ATOM   6170  C  C   . SER C 1 86  ? 40.609 47.818 86.588  1.00 49.48  ? 150 SER C C   1 
ATOM   6171  O  O   . SER C 1 86  ? 40.403 46.838 85.897  1.00 69.96  ? 150 SER C O   1 
ATOM   6172  C  CB  . SER C 1 86  ? 42.925 48.237 87.501  1.00 61.90  ? 150 SER C CB  1 
ATOM   6173  O  OG  . SER C 1 86  ? 42.853 49.454 86.823  1.00 81.51  ? 150 SER C OG  1 
ATOM   6174  N  N   . VAL C 1 87  ? 40.055 48.985 86.318  1.00 45.80  ? 151 VAL C N   1 
ATOM   6175  C  CA  . VAL C 1 87  ? 39.178 49.228 85.152  1.00 43.93  ? 151 VAL C CA  1 
ATOM   6176  C  C   . VAL C 1 87  ? 39.301 50.719 84.882  1.00 46.78  ? 151 VAL C C   1 
ATOM   6177  O  O   . VAL C 1 87  ? 39.799 51.463 85.759  1.00 62.12  ? 151 VAL C O   1 
ATOM   6178  C  CB  . VAL C 1 87  ? 37.719 48.848 85.437  1.00 42.45  ? 151 VAL C CB  1 
ATOM   6179  C  CG1 . VAL C 1 87  ? 37.022 49.922 86.248  1.00 38.81  ? 151 VAL C CG1 1 
ATOM   6180  C  CG2 . VAL C 1 87  ? 36.983 48.672 84.184  1.00 51.79  ? 151 VAL C CG2 1 
ATOM   6181  N  N   . LYS C 1 88  ? 38.909 51.183 83.699  1.00 45.00  ? 152 LYS C N   1 
ATOM   6182  C  CA  . LYS C 1 88  ? 38.994 52.639 83.450  1.00 50.55  ? 152 LYS C CA  1 
ATOM   6183  C  C   . LYS C 1 88  ? 37.747 53.285 84.023  1.00 47.08  ? 152 LYS C C   1 
ATOM   6184  O  O   . LYS C 1 88  ? 36.673 52.722 83.843  1.00 47.91  ? 152 LYS C O   1 
ATOM   6185  C  CB  . LYS C 1 88  ? 39.125 52.973 81.981  1.00 46.59  ? 152 LYS C CB  1 
ATOM   6186  C  CG  . LYS C 1 88  ? 39.539 54.399 81.751  1.00 52.26  ? 152 LYS C CG  1 
ATOM   6187  C  CD  . LYS C 1 88  ? 39.059 54.960 80.419  1.00 71.31  ? 152 LYS C CD  1 
ATOM   6188  C  CE  . LYS C 1 88  ? 37.656 55.575 80.555  1.00 113.32 ? 152 LYS C CE  1 
ATOM   6189  N  NZ  . LYS C 1 88  ? 37.004 55.910 79.240  1.00 111.28 ? 152 LYS C NZ  1 
ATOM   6190  N  N   . LEU C 1 89  ? 37.878 54.410 84.747  1.00 43.40  ? 153 LEU C N   1 
ATOM   6191  C  CA  . LEU C 1 89  ? 36.709 54.992 85.412  1.00 44.58  ? 153 LEU C CA  1 
ATOM   6192  C  C   . LEU C 1 89  ? 35.701 55.397 84.350  1.00 60.01  ? 153 LEU C C   1 
ATOM   6193  O  O   . LEU C 1 89  ? 36.006 56.212 83.456  1.00 63.90  ? 153 LEU C O   1 
ATOM   6194  C  CB  . LEU C 1 89  ? 37.052 56.206 86.252  1.00 38.46  ? 153 LEU C CB  1 
ATOM   6195  C  CG  . LEU C 1 89  ? 35.830 56.954 86.819  1.00 38.94  ? 153 LEU C CG  1 
ATOM   6196  C  CD1 . LEU C 1 89  ? 34.971 56.102 87.764  1.00 48.79  ? 153 LEU C CD1 1 
ATOM   6197  C  CD2 . LEU C 1 89  ? 36.250 58.122 87.591  1.00 38.16  ? 153 LEU C CD2 1 
ATOM   6198  N  N   . GLY C 1 90  ? 34.506 54.822 84.440  1.00 55.98  ? 154 GLY C N   1 
ATOM   6199  C  CA  . GLY C 1 90  ? 33.521 55.019 83.392  1.00 62.47  ? 154 GLY C CA  1 
ATOM   6200  C  C   . GLY C 1 90  ? 33.233 53.768 82.604  1.00 64.12  ? 154 GLY C C   1 
ATOM   6201  O  O   . GLY C 1 90  ? 32.261 53.706 81.863  1.00 84.03  ? 154 GLY C O   1 
ATOM   6202  N  N   . ASP C 1 91  ? 34.099 52.777 82.745  1.00 64.38  ? 155 ASP C N   1 
ATOM   6203  C  CA  . ASP C 1 91  ? 33.865 51.478 82.174  1.00 63.97  ? 155 ASP C CA  1 
ATOM   6204  C  C   . ASP C 1 91  ? 33.277 50.557 83.228  1.00 73.46  ? 155 ASP C C   1 
ATOM   6205  O  O   . ASP C 1 91  ? 33.547 50.738 84.419  1.00 89.18  ? 155 ASP C O   1 
ATOM   6206  C  CB  . ASP C 1 91  ? 35.147 50.913 81.613  1.00 75.18  ? 155 ASP C CB  1 
ATOM   6207  C  CG  . ASP C 1 91  ? 35.507 51.530 80.293  1.00 106.65 ? 155 ASP C CG  1 
ATOM   6208  O  OD1 . ASP C 1 91  ? 34.626 52.164 79.671  1.00 132.12 ? 155 ASP C OD1 1 
ATOM   6209  O  OD2 . ASP C 1 91  ? 36.671 51.375 79.871  1.00 135.81 ? 155 ASP C OD2 1 
ATOM   6210  N  N   . PRO C 1 92  ? 32.424 49.602 82.798  1.00 66.24  ? 156 PRO C N   1 
ATOM   6211  C  CA  . PRO C 1 92  ? 31.806 48.680 83.741  1.00 55.16  ? 156 PRO C CA  1 
ATOM   6212  C  C   . PRO C 1 92  ? 32.711 47.478 83.924  1.00 55.45  ? 156 PRO C C   1 
ATOM   6213  O  O   . PRO C 1 92  ? 33.466 47.152 83.015  1.00 71.02  ? 156 PRO C O   1 
ATOM   6214  C  CB  . PRO C 1 92  ? 30.530 48.290 83.031  1.00 57.26  ? 156 PRO C CB  1 
ATOM   6215  C  CG  . PRO C 1 92  ? 30.894 48.364 81.584  1.00 58.83  ? 156 PRO C CG  1 
ATOM   6216  C  CD  . PRO C 1 92  ? 31.836 49.491 81.448  1.00 56.11  ? 156 PRO C CD  1 
ATOM   6217  N  N   . PRO C 1 93  ? 32.670 46.838 85.099  1.00 50.80  ? 157 PRO C N   1 
ATOM   6218  C  CA  . PRO C 1 93  ? 33.555 45.704 85.331  1.00 54.23  ? 157 PRO C CA  1 
ATOM   6219  C  C   . PRO C 1 93  ? 33.097 44.439 84.635  1.00 54.61  ? 157 PRO C C   1 
ATOM   6220  O  O   . PRO C 1 93  ? 32.764 43.464 85.286  1.00 65.79  ? 157 PRO C O   1 
ATOM   6221  C  CB  . PRO C 1 93  ? 33.535 45.545 86.858  1.00 51.38  ? 157 PRO C CB  1 
ATOM   6222  C  CG  . PRO C 1 93  ? 32.294 46.211 87.285  1.00 53.67  ? 157 PRO C CG  1 
ATOM   6223  C  CD  . PRO C 1 93  ? 32.083 47.339 86.352  1.00 51.69  ? 157 PRO C CD  1 
ATOM   6224  N  N   . THR C 1 94  ? 33.059 44.475 83.311  1.00 60.78  ? 158 THR C N   1 
ATOM   6225  C  CA  . THR C 1 94  ? 32.859 43.274 82.510  1.00 63.61  ? 158 THR C CA  1 
ATOM   6226  C  C   . THR C 1 94  ? 34.195 42.573 82.432  1.00 63.43  ? 158 THR C C   1 
ATOM   6227  O  O   . THR C 1 94  ? 35.230 43.220 82.625  1.00 56.00  ? 158 THR C O   1 
ATOM   6228  C  CB  . THR C 1 94  ? 32.374 43.584 81.073  1.00 73.42  ? 158 THR C CB  1 
ATOM   6229  O  OG1 . THR C 1 94  ? 33.136 44.663 80.514  1.00 69.32  ? 158 THR C OG1 1 
ATOM   6230  C  CG2 . THR C 1 94  ? 30.868 43.931 81.058  1.00 84.50  ? 158 THR C CG2 1 
ATOM   6231  N  N   . PRO C 1 95  ? 34.183 41.251 82.171  1.00 71.18  ? 159 PRO C N   1 
ATOM   6232  C  CA  . PRO C 1 95  ? 35.392 40.409 82.086  1.00 71.72  ? 159 PRO C CA  1 
ATOM   6233  C  C   . PRO C 1 95  ? 36.397 40.912 81.071  1.00 71.88  ? 159 PRO C C   1 
ATOM   6234  O  O   . PRO C 1 95  ? 37.611 40.819 81.293  1.00 77.09  ? 159 PRO C O   1 
ATOM   6235  C  CB  . PRO C 1 95  ? 34.850 39.062 81.635  1.00 66.10  ? 159 PRO C CB  1 
ATOM   6236  C  CG  . PRO C 1 95  ? 33.468 39.031 82.190  1.00 80.02  ? 159 PRO C CG  1 
ATOM   6237  C  CD  . PRO C 1 95  ? 32.955 40.441 82.093  1.00 78.52  ? 159 PRO C CD  1 
ATOM   6238  N  N   . ASP C 1 96  ? 35.887 41.465 79.981  1.00 66.67  ? 160 ASP C N   1 
ATOM   6239  C  CA  . ASP C 1 96  ? 36.735 42.024 78.940  1.00 74.26  ? 160 ASP C CA  1 
ATOM   6240  C  C   . ASP C 1 96  ? 37.386 43.362 79.298  1.00 71.20  ? 160 ASP C C   1 
ATOM   6241  O  O   . ASP C 1 96  ? 38.428 43.692 78.750  1.00 79.98  ? 160 ASP C O   1 
ATOM   6242  C  CB  . ASP C 1 96  ? 35.931 42.155 77.662  1.00 97.06  ? 160 ASP C CB  1 
ATOM   6243  C  CG  . ASP C 1 96  ? 35.116 40.922 77.375  1.00 120.15 ? 160 ASP C CG  1 
ATOM   6244  O  OD1 . ASP C 1 96  ? 35.480 39.849 77.885  1.00 122.10 ? 160 ASP C OD1 1 
ATOM   6245  O  OD2 . ASP C 1 96  ? 34.109 41.018 76.647  1.00 156.26 ? 160 ASP C OD2 1 
ATOM   6246  N  N   . LYS C 1 97  ? 36.779 44.124 80.206  1.00 64.74  ? 161 LYS C N   1 
ATOM   6247  C  CA  . LYS C 1 97  ? 37.327 45.408 80.625  1.00 59.96  ? 161 LYS C CA  1 
ATOM   6248  C  C   . LYS C 1 97  ? 38.356 45.271 81.758  1.00 65.89  ? 161 LYS C C   1 
ATOM   6249  O  O   . LYS C 1 97  ? 39.194 46.166 81.961  1.00 60.56  ? 161 LYS C O   1 
ATOM   6250  C  CB  . LYS C 1 97  ? 36.202 46.344 81.075  1.00 59.40  ? 161 LYS C CB  1 
ATOM   6251  C  CG  . LYS C 1 97  ? 35.425 46.947 79.966  1.00 63.95  ? 161 LYS C CG  1 
ATOM   6252  C  CD  . LYS C 1 97  ? 36.345 47.543 78.929  1.00 68.26  ? 161 LYS C CD  1 
ATOM   6253  C  CE  . LYS C 1 97  ? 35.521 48.328 77.928  1.00 85.02  ? 161 LYS C CE  1 
ATOM   6254  N  NZ  . LYS C 1 97  ? 36.378 48.820 76.829  1.00 97.66  ? 161 LYS C NZ  1 
ATOM   6255  N  N   . LEU C 1 98  ? 38.290 44.163 82.498  1.00 67.57  ? 162 LEU C N   1 
ATOM   6256  C  CA  . LEU C 1 98  ? 39.085 44.012 83.722  1.00 57.73  ? 162 LEU C CA  1 
ATOM   6257  C  C   . LEU C 1 98  ? 40.548 43.947 83.431  1.00 50.84  ? 162 LEU C C   1 
ATOM   6258  O  O   . LEU C 1 98  ? 40.966 43.420 82.415  1.00 62.29  ? 162 LEU C O   1 
ATOM   6259  C  CB  . LEU C 1 98  ? 38.697 42.759 84.487  1.00 56.80  ? 162 LEU C CB  1 
ATOM   6260  C  CG  . LEU C 1 98  ? 37.317 42.743 85.124  1.00 69.70  ? 162 LEU C CG  1 
ATOM   6261  C  CD1 . LEU C 1 98  ? 37.367 41.773 86.258  1.00 84.50  ? 162 LEU C CD1 1 
ATOM   6262  C  CD2 . LEU C 1 98  ? 36.872 44.116 85.632  1.00 69.40  ? 162 LEU C CD2 1 
ATOM   6263  N  N   . LYS C 1 99  ? 41.322 44.533 84.317  1.00 49.34  ? 163 LYS C N   1 
ATOM   6264  C  CA  . LYS C 1 99  ? 42.766 44.444 84.251  1.00 55.81  ? 163 LYS C CA  1 
ATOM   6265  C  C   . LYS C 1 99  ? 43.243 43.918 85.578  1.00 59.45  ? 163 LYS C C   1 
ATOM   6266  O  O   . LYS C 1 99  ? 43.125 44.608 86.622  1.00 52.46  ? 163 LYS C O   1 
ATOM   6267  C  CB  . LYS C 1 99  ? 43.437 45.799 83.949  1.00 54.35  ? 163 LYS C CB  1 
ATOM   6268  C  CG  . LYS C 1 99  ? 44.956 45.744 84.121  1.00 62.69  ? 163 LYS C CG  1 
ATOM   6269  C  CD  . LYS C 1 99  ? 45.655 46.818 83.321  1.00 73.80  ? 163 LYS C CD  1 
ATOM   6270  C  CE  . LYS C 1 99  ? 46.865 47.354 84.083  1.00 89.18  ? 163 LYS C CE  1 
ATOM   6271  N  NZ  . LYS C 1 99  ? 48.112 46.632 83.709  1.00 137.26 ? 163 LYS C NZ  1 
ATOM   6272  N  N   . PHE C 1 100 ? 43.768 42.696 85.546  1.00 55.23  ? 164 PHE C N   1 
ATOM   6273  C  CA  . PHE C 1 100 ? 44.293 42.093 86.756  1.00 49.85  ? 164 PHE C CA  1 
ATOM   6274  C  C   . PHE C 1 100 ? 45.435 42.942 87.275  1.00 52.07  ? 164 PHE C C   1 
ATOM   6275  O  O   . PHE C 1 100 ? 46.345 43.316 86.505  1.00 54.34  ? 164 PHE C O   1 
ATOM   6276  C  CB  . PHE C 1 100 ? 44.801 40.694 86.477  1.00 51.97  ? 164 PHE C CB  1 
ATOM   6277  C  CG  . PHE C 1 100 ? 45.135 39.924 87.716  1.00 47.10  ? 164 PHE C CG  1 
ATOM   6278  C  CD1 . PHE C 1 100 ? 46.372 40.089 88.329  1.00 44.97  ? 164 PHE C CD1 1 
ATOM   6279  C  CD2 . PHE C 1 100 ? 44.217 39.028 88.261  1.00 45.19  ? 164 PHE C CD2 1 
ATOM   6280  C  CE1 . PHE C 1 100 ? 46.688 39.402 89.476  1.00 45.90  ? 164 PHE C CE1 1 
ATOM   6281  C  CE2 . PHE C 1 100 ? 44.521 38.323 89.409  1.00 46.72  ? 164 PHE C CE2 1 
ATOM   6282  C  CZ  . PHE C 1 100 ? 45.761 38.513 90.026  1.00 49.00  ? 164 PHE C CZ  1 
ATOM   6283  N  N   . GLU C 1 101 ? 45.402 43.243 88.572  1.00 45.98  ? 165 GLU C N   1 
ATOM   6284  C  CA  . GLU C 1 101 ? 46.401 44.133 89.130  1.00 46.14  ? 165 GLU C CA  1 
ATOM   6285  C  C   . GLU C 1 101 ? 47.305 43.435 90.099  1.00 50.71  ? 165 GLU C C   1 
ATOM   6286  O  O   . GLU C 1 101 ? 48.514 43.654 90.058  1.00 59.66  ? 165 GLU C O   1 
ATOM   6287  C  CB  . GLU C 1 101 ? 45.764 45.358 89.771  1.00 53.08  ? 165 GLU C CB  1 
ATOM   6288  C  CG  . GLU C 1 101 ? 45.282 46.430 88.749  1.00 78.45  ? 165 GLU C CG  1 
ATOM   6289  C  CD  . GLU C 1 101 ? 46.417 47.214 88.059  1.00 88.82  ? 165 GLU C CD  1 
ATOM   6290  O  OE1 . GLU C 1 101 ? 47.603 46.869 88.283  1.00 98.08  ? 165 GLU C OE1 1 
ATOM   6291  O  OE2 . GLU C 1 101 ? 46.110 48.171 87.287  1.00 83.78  ? 165 GLU C OE2 1 
ATOM   6292  N  N   . ALA C 1 102 ? 46.717 42.599 90.962  1.00 51.02  ? 166 ALA C N   1 
ATOM   6293  C  CA  . ALA C 1 102 ? 47.457 41.760 91.945  1.00 50.21  ? 166 ALA C CA  1 
ATOM   6294  C  C   . ALA C 1 102 ? 46.543 40.794 92.720  1.00 50.14  ? 166 ALA C C   1 
ATOM   6295  O  O   . ALA C 1 102 ? 45.319 40.857 92.567  1.00 52.98  ? 166 ALA C O   1 
ATOM   6296  C  CB  . ALA C 1 102 ? 48.243 42.623 92.919  1.00 42.33  ? 166 ALA C CB  1 
ATOM   6297  N  N   . VAL C 1 103 ? 47.125 39.916 93.549  1.00 45.96  ? 167 VAL C N   1 
ATOM   6298  C  CA  . VAL C 1 103 ? 46.316 38.978 94.352  1.00 49.21  ? 167 VAL C CA  1 
ATOM   6299  C  C   . VAL C 1 103 ? 46.294 39.560 95.708  1.00 56.88  ? 167 VAL C C   1 
ATOM   6300  O  O   . VAL C 1 103 ? 47.352 39.921 96.221  1.00 88.43  ? 167 VAL C O   1 
ATOM   6301  C  CB  . VAL C 1 103 ? 46.935 37.571 94.516  1.00 49.79  ? 167 VAL C CB  1 
ATOM   6302  C  CG1 . VAL C 1 103 ? 46.863 36.797 93.245  1.00 58.66  ? 167 VAL C CG1 1 
ATOM   6303  C  CG2 . VAL C 1 103 ? 48.380 37.695 94.938  1.00 62.97  ? 167 VAL C CG2 1 
ATOM   6304  N  N   . GLY C 1 104 ? 45.111 39.630 96.309  1.00 56.16  ? 168 GLY C N   1 
ATOM   6305  C  CA  . GLY C 1 104 ? 44.952 40.254 97.622  1.00 49.97  ? 168 GLY C CA  1 
ATOM   6306  C  C   . GLY C 1 104 ? 43.524 40.675 97.895  1.00 55.53  ? 168 GLY C C   1 
ATOM   6307  O  O   . GLY C 1 104 ? 42.710 40.704 96.993  1.00 60.77  ? 168 GLY C O   1 
ATOM   6308  N  N   . TRP C 1 105 ? 43.219 41.008 99.143  1.00 61.20  ? 169 TRP C N   1 
ATOM   6309  C  CA  . TRP C 1 105 ? 41.860 41.310 99.553  1.00 51.06  ? 169 TRP C CA  1 
ATOM   6310  C  C   . TRP C 1 105 ? 41.776 42.753 99.907  1.00 54.26  ? 169 TRP C C   1 
ATOM   6311  O  O   . TRP C 1 105 ? 40.725 43.246 100.262 1.00 70.32  ? 169 TRP C O   1 
ATOM   6312  C  CB  . TRP C 1 105 ? 41.439 40.414 100.731 1.00 51.12  ? 169 TRP C CB  1 
ATOM   6313  C  CG  . TRP C 1 105 ? 42.314 40.539 101.958 1.00 56.32  ? 169 TRP C CG  1 
ATOM   6314  C  CD1 . TRP C 1 105 ? 42.366 41.600 102.874 1.00 53.06  ? 169 TRP C CD1 1 
ATOM   6315  C  CD2 . TRP C 1 105 ? 43.302 39.572 102.442 1.00 62.98  ? 169 TRP C CD2 1 
ATOM   6316  N  NE1 . TRP C 1 105 ? 43.294 41.358 103.851 1.00 55.04  ? 169 TRP C NE1 1 
ATOM   6317  C  CE2 . TRP C 1 105 ? 43.890 40.152 103.654 1.00 70.07  ? 169 TRP C CE2 1 
ATOM   6318  C  CE3 . TRP C 1 105 ? 43.751 38.339 102.005 1.00 75.04  ? 169 TRP C CE3 1 
ATOM   6319  C  CZ2 . TRP C 1 105 ? 44.873 39.488 104.384 1.00 80.13  ? 169 TRP C CZ2 1 
ATOM   6320  C  CZ3 . TRP C 1 105 ? 44.747 37.684 102.747 1.00 77.11  ? 169 TRP C CZ3 1 
ATOM   6321  C  CH2 . TRP C 1 105 ? 45.291 38.244 103.904 1.00 74.61  ? 169 TRP C CH2 1 
ATOM   6322  N  N   . SER C 1 106 ? 42.898 43.448 99.836  1.00 52.92  ? 170 SER C N   1 
ATOM   6323  C  CA  . SER C 1 106 ? 42.904 44.872 100.126 1.00 57.70  ? 170 SER C CA  1 
ATOM   6324  C  C   . SER C 1 106 ? 44.043 45.585 99.411  1.00 51.19  ? 170 SER C C   1 
ATOM   6325  O  O   . SER C 1 106 ? 45.184 45.111 99.394  1.00 53.16  ? 170 SER C O   1 
ATOM   6326  C  CB  . SER C 1 106 ? 43.011 45.108 101.627 1.00 60.92  ? 170 SER C CB  1 
ATOM   6327  O  OG  . SER C 1 106 ? 43.470 46.419 101.899 1.00 77.68  ? 170 SER C OG  1 
ATOM   6328  N  N   . ALA C 1 107 ? 43.725 46.742 98.845  1.00 42.60  ? 171 ALA C N   1 
ATOM   6329  C  CA  . ALA C 1 107 ? 44.645 47.404 97.941  1.00 41.61  ? 171 ALA C CA  1 
ATOM   6330  C  C   . ALA C 1 107 ? 44.529 48.900 97.929  1.00 49.35  ? 171 ALA C C   1 
ATOM   6331  O  O   . ALA C 1 107 ? 43.473 49.448 98.175  1.00 60.94  ? 171 ALA C O   1 
ATOM   6332  C  CB  . ALA C 1 107 ? 44.440 46.927 96.580  1.00 38.43  ? 171 ALA C CB  1 
ATOM   6333  N  N   . SER C 1 108 ? 45.641 49.539 97.596  1.00 49.07  ? 172 SER C N   1 
ATOM   6334  C  CA  . SER C 1 108 ? 45.708 50.957 97.385  1.00 48.06  ? 172 SER C CA  1 
ATOM   6335  C  C   . SER C 1 108 ? 46.631 51.202 96.184  1.00 51.24  ? 172 SER C C   1 
ATOM   6336  O  O   . SER C 1 108 ? 47.479 50.346 95.832  1.00 47.97  ? 172 SER C O   1 
ATOM   6337  C  CB  . SER C 1 108 ? 46.242 51.620 98.643  1.00 57.82  ? 172 SER C CB  1 
ATOM   6338  O  OG  . SER C 1 108 ? 46.868 52.855 98.359  1.00 67.54  ? 172 SER C OG  1 
ATOM   6339  N  N   . SER C 1 109 ? 46.473 52.352 95.527  1.00 48.06  ? 173 SER C N   1 
ATOM   6340  C  CA  . SER C 1 109 ? 47.289 52.597 94.338  1.00 51.52  ? 173 SER C CA  1 
ATOM   6341  C  C   . SER C 1 109 ? 47.355 54.054 93.967  1.00 57.26  ? 173 SER C C   1 
ATOM   6342  O  O   . SER C 1 109 ? 46.500 54.850 94.362  1.00 50.09  ? 173 SER C O   1 
ATOM   6343  C  CB  . SER C 1 109 ? 46.771 51.811 93.141  1.00 60.65  ? 173 SER C CB  1 
ATOM   6344  O  OG  . SER C 1 109 ? 45.553 52.370 92.663  1.00 66.40  ? 173 SER C OG  1 
ATOM   6345  N  N   . CYS C 1 110 ? 48.390 54.384 93.197  1.00 63.53  ? 174 CYS C N   1 
ATOM   6346  C  CA  . CYS C 1 110 ? 48.682 55.758 92.816  1.00 62.51  ? 174 CYS C CA  1 
ATOM   6347  C  C   . CYS C 1 110 ? 49.669 55.719 91.686  1.00 68.95  ? 174 CYS C C   1 
ATOM   6348  O  O   . CYS C 1 110 ? 50.509 54.814 91.609  1.00 73.83  ? 174 CYS C O   1 
ATOM   6349  C  CB  . CYS C 1 110 ? 49.261 56.567 93.977  1.00 65.37  ? 174 CYS C CB  1 
ATOM   6350  S  SG  . CYS C 1 110 ? 50.403 55.696 95.082  1.00 105.72 ? 174 CYS C SG  1 
ATOM   6351  N  N   . HIS C 1 111 ? 49.548 56.704 90.798  1.00 72.02  ? 175 HIS C N   1 
ATOM   6352  C  CA  . HIS C 1 111 ? 50.384 56.782 89.617  1.00 62.98  ? 175 HIS C CA  1 
ATOM   6353  C  C   . HIS C 1 111 ? 51.378 57.880 89.733  1.00 69.80  ? 175 HIS C C   1 
ATOM   6354  O  O   . HIS C 1 111 ? 51.001 59.033 89.884  1.00 83.53  ? 175 HIS C O   1 
ATOM   6355  C  CB  . HIS C 1 111 ? 49.536 57.027 88.401  1.00 68.73  ? 175 HIS C CB  1 
ATOM   6356  C  CG  . HIS C 1 111 ? 50.262 56.767 87.111  1.00 80.52  ? 175 HIS C CG  1 
ATOM   6357  N  ND1 . HIS C 1 111 ? 51.051 57.690 86.533  1.00 74.76  ? 175 HIS C ND1 1 
ATOM   6358  C  CD2 . HIS C 1 111 ? 50.314 55.629 86.298  1.00 65.71  ? 175 HIS C CD2 1 
ATOM   6359  C  CE1 . HIS C 1 111 ? 51.579 57.178 85.408  1.00 71.47  ? 175 HIS C CE1 1 
ATOM   6360  N  NE2 . HIS C 1 111 ? 51.125 55.918 85.266  1.00 66.91  ? 175 HIS C NE2 1 
ATOM   6361  N  N   . ASP C 1 112 ? 52.658 57.532 89.671  1.00 73.93  ? 176 ASP C N   1 
ATOM   6362  C  CA  . ASP C 1 112 ? 53.723 58.520 89.842  1.00 75.70  ? 176 ASP C CA  1 
ATOM   6363  C  C   . ASP C 1 112 ? 54.072 59.374 88.610  1.00 74.34  ? 176 ASP C C   1 
ATOM   6364  O  O   . ASP C 1 112 ? 54.853 60.324 88.736  1.00 73.76  ? 176 ASP C O   1 
ATOM   6365  C  CB  . ASP C 1 112 ? 54.990 57.862 90.407  1.00 82.54  ? 176 ASP C CB  1 
ATOM   6366  C  CG  . ASP C 1 112 ? 55.635 56.849 89.450  1.00 93.84  ? 176 ASP C CG  1 
ATOM   6367  O  OD1 . ASP C 1 112 ? 55.135 56.593 88.327  1.00 79.14  ? 176 ASP C OD1 1 
ATOM   6368  O  OD2 . ASP C 1 112 ? 56.682 56.296 89.852  1.00 108.86 ? 176 ASP C OD2 1 
ATOM   6369  N  N   . GLY C 1 113 ? 53.493 59.050 87.450  1.00 65.17  ? 177 GLY C N   1 
ATOM   6370  C  CA  . GLY C 1 113 ? 53.827 59.710 86.186  1.00 66.78  ? 177 GLY C CA  1 
ATOM   6371  C  C   . GLY C 1 113 ? 54.550 58.790 85.208  1.00 76.51  ? 177 GLY C C   1 
ATOM   6372  O  O   . GLY C 1 113 ? 54.720 59.114 84.024  1.00 85.39  ? 177 GLY C O   1 
ATOM   6373  N  N   . PHE C 1 114 ? 54.987 57.639 85.709  1.00 78.52  ? 178 PHE C N   1 
ATOM   6374  C  CA  . PHE C 1 114 ? 55.650 56.634 84.885  1.00 69.90  ? 178 PHE C CA  1 
ATOM   6375  C  C   . PHE C 1 114 ? 54.868 55.345 84.859  1.00 64.72  ? 178 PHE C C   1 
ATOM   6376  O  O   . PHE C 1 114 ? 54.430 54.936 83.805  1.00 60.93  ? 178 PHE C O   1 
ATOM   6377  C  CB  . PHE C 1 114 ? 57.042 56.378 85.392  1.00 66.31  ? 178 PHE C CB  1 
ATOM   6378  C  CG  . PHE C 1 114 ? 57.889 57.601 85.415  1.00 87.42  ? 178 PHE C CG  1 
ATOM   6379  C  CD1 . PHE C 1 114 ? 58.398 58.121 84.230  1.00 89.15  ? 178 PHE C CD1 1 
ATOM   6380  C  CD2 . PHE C 1 114 ? 58.186 58.252 86.622  1.00 100.71 ? 178 PHE C CD2 1 
ATOM   6381  C  CE1 . PHE C 1 114 ? 59.206 59.268 84.240  1.00 83.86  ? 178 PHE C CE1 1 
ATOM   6382  C  CE2 . PHE C 1 114 ? 59.000 59.400 86.644  1.00 76.18  ? 178 PHE C CE2 1 
ATOM   6383  C  CZ  . PHE C 1 114 ? 59.512 59.898 85.450  1.00 76.77  ? 178 PHE C CZ  1 
ATOM   6384  N  N   . GLN C 1 115 ? 54.679 54.722 86.021  1.00 61.10  ? 179 GLN C N   1 
ATOM   6385  C  CA  . GLN C 1 115 ? 53.905 53.503 86.107  1.00 54.75  ? 179 GLN C CA  1 
ATOM   6386  C  C   . GLN C 1 115 ? 52.875 53.618 87.215  1.00 52.05  ? 179 GLN C C   1 
ATOM   6387  O  O   . GLN C 1 115 ? 52.897 54.574 87.984  1.00 53.46  ? 179 GLN C O   1 
ATOM   6388  C  CB  . GLN C 1 115 ? 54.846 52.332 86.367  1.00 60.54  ? 179 GLN C CB  1 
ATOM   6389  C  CG  . GLN C 1 115 ? 55.862 52.087 85.282  1.00 61.72  ? 179 GLN C CG  1 
ATOM   6390  C  CD  . GLN C 1 115 ? 55.217 51.507 84.074  1.00 67.47  ? 179 GLN C CD  1 
ATOM   6391  O  OE1 . GLN C 1 115 ? 54.065 51.075 84.126  1.00 70.86  ? 179 GLN C OE1 1 
ATOM   6392  N  NE2 . GLN C 1 115 ? 55.934 51.510 82.963  1.00 81.98  ? 179 GLN C NE2 1 
ATOM   6393  N  N   . TRP C 1 116 ? 51.978 52.641 87.301  1.00 53.18  ? 180 TRP C N   1 
ATOM   6394  C  CA  . TRP C 1 116 ? 51.144 52.486 88.495  1.00 55.71  ? 180 TRP C CA  1 
ATOM   6395  C  C   . TRP C 1 116 ? 51.816 51.722 89.608  1.00 61.00  ? 180 TRP C C   1 
ATOM   6396  O  O   . TRP C 1 116 ? 52.404 50.635 89.411  1.00 58.54  ? 180 TRP C O   1 
ATOM   6397  C  CB  . TRP C 1 116 ? 49.897 51.728 88.159  1.00 66.78  ? 180 TRP C CB  1 
ATOM   6398  C  CG  . TRP C 1 116 ? 48.882 52.535 87.437  1.00 58.97  ? 180 TRP C CG  1 
ATOM   6399  C  CD1 . TRP C 1 116 ? 48.639 52.552 86.087  1.00 61.67  ? 180 TRP C CD1 1 
ATOM   6400  C  CD2 . TRP C 1 116 ? 47.921 53.445 88.010  1.00 61.81  ? 180 TRP C CD2 1 
ATOM   6401  N  NE1 . TRP C 1 116 ? 47.628 53.393 85.784  1.00 61.90  ? 180 TRP C NE1 1 
ATOM   6402  C  CE2 . TRP C 1 116 ? 47.144 53.965 86.896  1.00 64.44  ? 180 TRP C CE2 1 
ATOM   6403  C  CE3 . TRP C 1 116 ? 47.622 53.867 89.293  1.00 70.03  ? 180 TRP C CE3 1 
ATOM   6404  C  CZ2 . TRP C 1 116 ? 46.110 54.874 87.077  1.00 58.05  ? 180 TRP C CZ2 1 
ATOM   6405  C  CZ3 . TRP C 1 116 ? 46.574 54.787 89.463  1.00 66.10  ? 180 TRP C CZ3 1 
ATOM   6406  C  CH2 . TRP C 1 116 ? 45.845 55.279 88.378  1.00 52.40  ? 180 TRP C CH2 1 
ATOM   6407  N  N   . THR C 1 117 ? 51.713 52.283 90.804  1.00 67.95  ? 181 THR C N   1 
ATOM   6408  C  CA  . THR C 1 117 ? 52.173 51.608 91.999  1.00 58.83  ? 181 THR C CA  1 
ATOM   6409  C  C   . THR C 1 117 ? 50.920 51.061 92.659  1.00 58.18  ? 181 THR C C   1 
ATOM   6410  O  O   . THR C 1 117 ? 49.924 51.792 92.859  1.00 57.46  ? 181 THR C O   1 
ATOM   6411  C  CB  . THR C 1 117 ? 52.924 52.575 92.955  1.00 55.73  ? 181 THR C CB  1 
ATOM   6412  O  OG1 . THR C 1 117 ? 54.095 53.115 92.312  1.00 57.74  ? 181 THR C OG1 1 
ATOM   6413  C  CG2 . THR C 1 117 ? 53.359 51.847 94.181  1.00 49.91  ? 181 THR C CG2 1 
ATOM   6414  N  N   . VAL C 1 118 ? 50.962 49.771 92.973  1.00 52.35  ? 182 VAL C N   1 
ATOM   6415  C  CA  . VAL C 1 118 ? 49.872 49.135 93.692  1.00 52.27  ? 182 VAL C CA  1 
ATOM   6416  C  C   . VAL C 1 118 ? 50.353 48.337 94.903  1.00 59.80  ? 182 VAL C C   1 
ATOM   6417  O  O   . VAL C 1 118 ? 51.268 47.497 94.820  1.00 67.25  ? 182 VAL C O   1 
ATOM   6418  C  CB  . VAL C 1 118 ? 49.090 48.215 92.786  1.00 48.62  ? 182 VAL C CB  1 
ATOM   6419  C  CG1 . VAL C 1 118 ? 48.051 47.437 93.602  1.00 52.34  ? 182 VAL C CG1 1 
ATOM   6420  C  CG2 . VAL C 1 118 ? 48.448 49.013 91.685  1.00 43.27  ? 182 VAL C CG2 1 
ATOM   6421  N  N   . LEU C 1 119 ? 49.703 48.606 96.026  1.00 60.03  ? 183 LEU C N   1 
ATOM   6422  C  CA  . LEU C 1 119 ? 49.945 47.880 97.272  1.00 64.31  ? 183 LEU C CA  1 
ATOM   6423  C  C   . LEU C 1 119 ? 48.790 46.934 97.569  1.00 54.18  ? 183 LEU C C   1 
ATOM   6424  O  O   . LEU C 1 119 ? 47.643 47.344 97.703  1.00 49.22  ? 183 LEU C O   1 
ATOM   6425  C  CB  . LEU C 1 119 ? 50.086 48.858 98.435  1.00 65.49  ? 183 LEU C CB  1 
ATOM   6426  C  CG  . LEU C 1 119 ? 51.135 49.938 98.245  1.00 65.00  ? 183 LEU C CG  1 
ATOM   6427  C  CD1 . LEU C 1 119 ? 50.470 51.266 98.437  1.00 63.13  ? 183 LEU C CD1 1 
ATOM   6428  C  CD2 . LEU C 1 119 ? 52.283 49.738 99.198  1.00 59.49  ? 183 LEU C CD2 1 
ATOM   6429  N  N   . SER C 1 120 ? 49.112 45.665 97.700  1.00 53.02  ? 184 SER C N   1 
ATOM   6430  C  CA  . SER C 1 120 ? 48.108 44.690 97.987  1.00 56.10  ? 184 SER C CA  1 
ATOM   6431  C  C   . SER C 1 120 ? 48.444 43.877 99.226  1.00 63.25  ? 184 SER C C   1 
ATOM   6432  O  O   . SER C 1 120 ? 49.610 43.649 99.552  1.00 72.20  ? 184 SER C O   1 
ATOM   6433  C  CB  . SER C 1 120 ? 47.962 43.765 96.807  1.00 69.39  ? 184 SER C CB  1 
ATOM   6434  O  OG  . SER C 1 120 ? 46.999 42.775 97.103  1.00 105.92 ? 184 SER C OG  1 
ATOM   6435  N  N   . VAL C 1 121 ? 47.399 43.432 99.910  1.00 57.93  ? 185 VAL C N   1 
ATOM   6436  C  CA  . VAL C 1 121 ? 47.550 42.625 101.096 1.00 51.41  ? 185 VAL C CA  1 
ATOM   6437  C  C   . VAL C 1 121 ? 47.054 41.241 100.802 1.00 48.25  ? 185 VAL C C   1 
ATOM   6438  O  O   . VAL C 1 121 ? 45.889 41.122 100.465 1.00 51.80  ? 185 VAL C O   1 
ATOM   6439  C  CB  . VAL C 1 121 ? 46.672 43.182 102.187 1.00 50.43  ? 185 VAL C CB  1 
ATOM   6440  C  CG1 . VAL C 1 121 ? 46.765 42.333 103.428 1.00 46.82  ? 185 VAL C CG1 1 
ATOM   6441  C  CG2 . VAL C 1 121 ? 47.099 44.585 102.504 1.00 61.78  ? 185 VAL C CG2 1 
ATOM   6442  N  N   . ALA C 1 122 ? 47.901 40.214 100.961 1.00 43.42  ? 186 ALA C N   1 
ATOM   6443  C  CA  . ALA C 1 122 ? 47.520 38.841 100.606 1.00 41.93  ? 186 ALA C CA  1 
ATOM   6444  C  C   . ALA C 1 122 ? 48.013 37.788 101.570 1.00 50.89  ? 186 ALA C C   1 
ATOM   6445  O  O   . ALA C 1 122 ? 48.765 38.097 102.491 1.00 58.24  ? 186 ALA C O   1 
ATOM   6446  C  CB  . ALA C 1 122 ? 47.999 38.526 99.255  1.00 40.92  ? 186 ALA C CB  1 
ATOM   6447  N  N   . GLY C 1 123 ? 47.563 36.550 101.338 1.00 62.11  ? 187 GLY C N   1 
ATOM   6448  C  CA  . GLY C 1 123 ? 47.942 35.349 102.100 1.00 68.59  ? 187 GLY C CA  1 
ATOM   6449  C  C   . GLY C 1 123 ? 48.052 35.441 103.612 1.00 72.55  ? 187 GLY C C   1 
ATOM   6450  O  O   . GLY C 1 123 ? 47.043 35.514 104.309 1.00 64.65  ? 187 GLY C O   1 
ATOM   6451  N  N   . ASP C 1 124 ? 49.295 35.402 104.105 1.00 98.71  ? 188 ASP C N   1 
ATOM   6452  C  CA  . ASP C 1 124 ? 49.628 35.600 105.520 1.00 101.14 ? 188 ASP C CA  1 
ATOM   6453  C  C   . ASP C 1 124 ? 48.954 36.883 106.066 1.00 98.36  ? 188 ASP C C   1 
ATOM   6454  O  O   . ASP C 1 124 ? 48.537 36.940 107.217 1.00 89.53  ? 188 ASP C O   1 
ATOM   6455  C  CB  . ASP C 1 124 ? 51.169 35.652 105.666 1.00 121.30 ? 188 ASP C CB  1 
ATOM   6456  C  CG  . ASP C 1 124 ? 51.642 36.158 107.041 1.00 147.74 ? 188 ASP C CG  1 
ATOM   6457  O  OD1 . ASP C 1 124 ? 51.157 35.639 108.070 1.00 182.94 ? 188 ASP C OD1 1 
ATOM   6458  O  OD2 . ASP C 1 124 ? 52.520 37.062 107.093 1.00 109.08 ? 188 ASP C OD2 1 
ATOM   6459  N  N   . GLY C 1 125 ? 48.814 37.893 105.215 1.00 82.00  ? 189 GLY C N   1 
ATOM   6460  C  CA  . GLY C 1 125 ? 48.413 39.210 105.648 1.00 62.27  ? 189 GLY C CA  1 
ATOM   6461  C  C   . GLY C 1 125 ? 49.544 40.207 105.441 1.00 66.80  ? 189 GLY C C   1 
ATOM   6462  O  O   . GLY C 1 125 ? 49.590 41.229 106.131 1.00 61.51  ? 189 GLY C O   1 
ATOM   6463  N  N   . PHE C 1 126 ? 50.460 39.917 104.508 1.00 55.33  ? 190 PHE C N   1 
ATOM   6464  C  CA  . PHE C 1 126 ? 51.561 40.840 104.167 1.00 51.53  ? 190 PHE C CA  1 
ATOM   6465  C  C   . PHE C 1 126 ? 51.207 41.691 102.943 1.00 59.12  ? 190 PHE C C   1 
ATOM   6466  O  O   . PHE C 1 126 ? 50.179 41.486 102.280 1.00 60.14  ? 190 PHE C O   1 
ATOM   6467  C  CB  . PHE C 1 126 ? 52.875 40.086 103.910 1.00 48.37  ? 190 PHE C CB  1 
ATOM   6468  C  CG  . PHE C 1 126 ? 52.882 39.303 102.619 1.00 57.97  ? 190 PHE C CG  1 
ATOM   6469  C  CD1 . PHE C 1 126 ? 53.580 39.767 101.516 1.00 70.31  ? 190 PHE C CD1 1 
ATOM   6470  C  CD2 . PHE C 1 126 ? 52.181 38.095 102.511 1.00 60.22  ? 190 PHE C CD2 1 
ATOM   6471  C  CE1 . PHE C 1 126 ? 53.571 39.055 100.331 1.00 86.48  ? 190 PHE C CE1 1 
ATOM   6472  C  CE2 . PHE C 1 126 ? 52.165 37.385 101.341 1.00 57.99  ? 190 PHE C CE2 1 
ATOM   6473  C  CZ  . PHE C 1 126 ? 52.861 37.861 100.246 1.00 78.66  ? 190 PHE C CZ  1 
ATOM   6474  N  N   . VAL C 1 127 ? 52.092 42.623 102.632 1.00 55.30  ? 191 VAL C N   1 
ATOM   6475  C  CA  . VAL C 1 127 ? 51.893 43.527 101.533 1.00 56.06  ? 191 VAL C CA  1 
ATOM   6476  C  C   . VAL C 1 127 ? 52.899 43.272 100.414 1.00 55.25  ? 191 VAL C C   1 
ATOM   6477  O  O   . VAL C 1 127 ? 54.110 43.318 100.631 1.00 57.80  ? 191 VAL C O   1 
ATOM   6478  C  CB  . VAL C 1 127 ? 51.989 44.990 102.040 1.00 72.04  ? 191 VAL C CB  1 
ATOM   6479  C  CG1 . VAL C 1 127 ? 52.417 45.933 100.957 1.00 96.28  ? 191 VAL C CG1 1 
ATOM   6480  C  CG2 . VAL C 1 127 ? 50.668 45.444 102.561 1.00 62.33  ? 191 VAL C CG2 1 
ATOM   6481  N  N   . SER C 1 128 ? 52.379 42.979 99.227  1.00 64.96  ? 192 SER C N   1 
ATOM   6482  C  CA  . SER C 1 128 ? 53.131 43.094 97.976  1.00 66.40  ? 192 SER C CA  1 
ATOM   6483  C  C   . SER C 1 128 ? 53.021 44.532 97.445  1.00 72.66  ? 192 SER C C   1 
ATOM   6484  O  O   . SER C 1 128 ? 51.971 45.209 97.555  1.00 60.83  ? 192 SER C O   1 
ATOM   6485  C  CB  . SER C 1 128 ? 52.565 42.145 96.930  1.00 75.25  ? 192 SER C CB  1 
ATOM   6486  O  OG  . SER C 1 128 ? 52.604 40.826 97.418  1.00 86.03  ? 192 SER C OG  1 
ATOM   6487  N  N   . ILE C 1 129 ? 54.112 45.009 96.869  1.00 66.47  ? 193 ILE C N   1 
ATOM   6488  C  CA  . ILE C 1 129 ? 54.115 46.317 96.237  1.00 59.61  ? 193 ILE C CA  1 
ATOM   6489  C  C   . ILE C 1 129 ? 54.418 46.033 94.791  1.00 60.70  ? 193 ILE C C   1 
ATOM   6490  O  O   . ILE C 1 129 ? 55.488 45.486 94.486  1.00 66.76  ? 193 ILE C O   1 
ATOM   6491  C  CB  . ILE C 1 129 ? 55.223 47.212 96.828  1.00 54.09  ? 193 ILE C CB  1 
ATOM   6492  C  CG1 . ILE C 1 129 ? 54.860 47.594 98.247  1.00 56.00  ? 193 ILE C CG1 1 
ATOM   6493  C  CG2 . ILE C 1 129 ? 55.419 48.461 96.012  1.00 48.00  ? 193 ILE C CG2 1 
ATOM   6494  C  CD1 . ILE C 1 129 ? 55.968 48.246 99.009  1.00 63.46  ? 193 ILE C CD1 1 
ATOM   6495  N  N   . LEU C 1 130 ? 53.497 46.367 93.887  1.00 57.45  ? 194 LEU C N   1 
ATOM   6496  C  CA  . LEU C 1 130 ? 53.864 46.230 92.478  1.00 63.93  ? 194 LEU C CA  1 
ATOM   6497  C  C   . LEU C 1 130 ? 53.834 47.478 91.580  1.00 62.89  ? 194 LEU C C   1 
ATOM   6498  O  O   . LEU C 1 130 ? 52.859 48.234 91.534  1.00 82.29  ? 194 LEU C O   1 
ATOM   6499  C  CB  . LEU C 1 130 ? 53.255 44.984 91.841  1.00 62.12  ? 194 LEU C CB  1 
ATOM   6500  C  CG  . LEU C 1 130 ? 51.796 44.733 92.071  1.00 66.45  ? 194 LEU C CG  1 
ATOM   6501  C  CD1 . LEU C 1 130 ? 51.047 45.015 90.755  1.00 87.88  ? 194 LEU C CD1 1 
ATOM   6502  C  CD2 . LEU C 1 130 ? 51.723 43.312 92.459  1.00 52.18  ? 194 LEU C CD2 1 
ATOM   6503  N  N   . TYR C 1 131 ? 54.951 47.669 90.887  1.00 55.90  ? 195 TYR C N   1 
ATOM   6504  C  CA  . TYR C 1 131 ? 55.166 48.841 90.080  1.00 54.29  ? 195 TYR C CA  1 
ATOM   6505  C  C   . TYR C 1 131 ? 55.034 48.424 88.645  1.00 55.99  ? 195 TYR C C   1 
ATOM   6506  O  O   . TYR C 1 131 ? 55.830 47.625 88.132  1.00 59.69  ? 195 TYR C O   1 
ATOM   6507  C  CB  . TYR C 1 131 ? 56.562 49.373 90.328  1.00 55.58  ? 195 TYR C CB  1 
ATOM   6508  C  CG  . TYR C 1 131 ? 56.819 50.739 89.755  1.00 61.74  ? 195 TYR C CG  1 
ATOM   6509  C  CD1 . TYR C 1 131 ? 56.194 51.886 90.296  1.00 67.14  ? 195 TYR C CD1 1 
ATOM   6510  C  CD2 . TYR C 1 131 ? 57.704 50.904 88.688  1.00 59.77  ? 195 TYR C CD2 1 
ATOM   6511  C  CE1 . TYR C 1 131 ? 56.447 53.164 89.770  1.00 70.17  ? 195 TYR C CE1 1 
ATOM   6512  C  CE2 . TYR C 1 131 ? 57.964 52.173 88.152  1.00 71.74  ? 195 TYR C CE2 1 
ATOM   6513  C  CZ  . TYR C 1 131 ? 57.338 53.298 88.692  1.00 78.79  ? 195 TYR C CZ  1 
ATOM   6514  O  OH  . TYR C 1 131 ? 57.625 54.529 88.139  1.00 77.43  ? 195 TYR C OH  1 
ATOM   6515  N  N   . GLY C 1 132 ? 54.004 48.943 87.999  1.00 52.20  ? 196 GLY C N   1 
ATOM   6516  C  CA  . GLY C 1 132 ? 53.790 48.648 86.594  1.00 60.65  ? 196 GLY C CA  1 
ATOM   6517  C  C   . GLY C 1 132 ? 53.529 47.184 86.328  1.00 56.38  ? 196 GLY C C   1 
ATOM   6518  O  O   . GLY C 1 132 ? 53.955 46.657 85.318  1.00 57.41  ? 196 GLY C O   1 
ATOM   6519  N  N   . GLY C 1 133 ? 52.831 46.530 87.247  1.00 64.61  ? 197 GLY C N   1 
ATOM   6520  C  CA  . GLY C 1 133 ? 52.448 45.132 87.059  1.00 67.02  ? 197 GLY C CA  1 
ATOM   6521  C  C   . GLY C 1 133 ? 53.465 44.094 87.520  1.00 70.43  ? 197 GLY C C   1 
ATOM   6522  O  O   . GLY C 1 133 ? 53.159 42.901 87.514  1.00 99.25  ? 197 GLY C O   1 
ATOM   6523  N  N   . ILE C 1 134 ? 54.662 44.522 87.915  1.00 54.82  ? 198 ILE C N   1 
ATOM   6524  C  CA  . ILE C 1 134 ? 55.662 43.575 88.411  1.00 74.26  ? 198 ILE C CA  1 
ATOM   6525  C  C   . ILE C 1 134 ? 55.999 43.811 89.886  1.00 75.74  ? 198 ILE C C   1 
ATOM   6526  O  O   . ILE C 1 134 ? 55.975 44.952 90.353  1.00 72.38  ? 198 ILE C O   1 
ATOM   6527  C  CB  . ILE C 1 134 ? 56.933 43.572 87.540  1.00 73.42  ? 198 ILE C CB  1 
ATOM   6528  C  CG1 . ILE C 1 134 ? 57.698 44.881 87.699  1.00 91.94  ? 198 ILE C CG1 1 
ATOM   6529  C  CG2 . ILE C 1 134 ? 56.547 43.339 86.080  1.00 89.32  ? 198 ILE C CG2 1 
ATOM   6530  C  CD1 . ILE C 1 134 ? 59.018 44.931 86.975  1.00 108.25 ? 198 ILE C CD1 1 
ATOM   6531  N  N   . ILE C 1 135 ? 56.315 42.734 90.604  1.00 72.89  ? 199 ILE C N   1 
ATOM   6532  C  CA  . ILE C 1 135 ? 56.556 42.796 92.046  1.00 64.56  ? 199 ILE C CA  1 
ATOM   6533  C  C   . ILE C 1 135 ? 57.931 43.327 92.396  1.00 66.64  ? 199 ILE C C   1 
ATOM   6534  O  O   . ILE C 1 135 ? 58.940 42.634 92.226  1.00 73.10  ? 199 ILE C O   1 
ATOM   6535  C  CB  . ILE C 1 135 ? 56.416 41.418 92.706  1.00 76.42  ? 199 ILE C CB  1 
ATOM   6536  C  CG1 . ILE C 1 135 ? 55.070 40.809 92.327  1.00 70.47  ? 199 ILE C CG1 1 
ATOM   6537  C  CG2 . ILE C 1 135 ? 56.611 41.542 94.218  1.00 85.84  ? 199 ILE C CG2 1 
ATOM   6538  C  CD1 . ILE C 1 135 ? 54.197 40.454 93.490  1.00 61.98  ? 199 ILE C CD1 1 
ATOM   6539  N  N   . THR C 1 136 ? 57.961 44.541 92.923  1.00 72.49  ? 200 THR C N   1 
ATOM   6540  C  CA  . THR C 1 136 ? 59.213 45.227 93.223  1.00 76.50  ? 200 THR C CA  1 
ATOM   6541  C  C   . THR C 1 136 ? 59.602 45.132 94.697  1.00 78.08  ? 200 THR C C   1 
ATOM   6542  O  O   . THR C 1 136 ? 60.779 45.311 95.032  1.00 106.08 ? 200 THR C O   1 
ATOM   6543  C  CB  . THR C 1 136 ? 59.144 46.718 92.811  1.00 80.56  ? 200 THR C CB  1 
ATOM   6544  O  OG1 . THR C 1 136 ? 57.963 47.305 93.370  1.00 67.55  ? 200 THR C OG1 1 
ATOM   6545  C  CG2 . THR C 1 136 ? 59.102 46.863 91.289  1.00 90.41  ? 200 THR C CG2 1 
ATOM   6546  N  N   . ASP C 1 137 ? 58.626 44.862 95.569  1.00 60.94  ? 201 ASP C N   1 
ATOM   6547  C  CA  . ASP C 1 137 ? 58.862 44.888 97.022  1.00 77.86  ? 201 ASP C CA  1 
ATOM   6548  C  C   . ASP C 1 137 ? 57.732 44.283 97.868  1.00 65.47  ? 201 ASP C C   1 
ATOM   6549  O  O   . ASP C 1 137 ? 56.571 44.349 97.498  1.00 68.13  ? 201 ASP C O   1 
ATOM   6550  C  CB  . ASP C 1 137 ? 59.153 46.323 97.505  1.00 82.14  ? 201 ASP C CB  1 
ATOM   6551  C  CG  . ASP C 1 137 ? 60.071 46.366 98.727  1.00 97.48  ? 201 ASP C CG  1 
ATOM   6552  O  OD1 . ASP C 1 137 ? 59.950 45.512 99.640  1.00 119.23 ? 201 ASP C OD1 1 
ATOM   6553  O  OD2 . ASP C 1 137 ? 60.930 47.272 98.772  1.00 120.22 ? 201 ASP C OD2 1 
ATOM   6554  N  N   . THR C 1 138 ? 58.098 43.681 99.001  1.00 67.46  ? 202 THR C N   1 
ATOM   6555  C  CA  . THR C 1 138 ? 57.132 43.175 99.982  1.00 61.82  ? 202 THR C CA  1 
ATOM   6556  C  C   . THR C 1 138 ? 57.384 43.782 101.363 1.00 67.02  ? 202 THR C C   1 
ATOM   6557  O  O   . THR C 1 138 ? 58.535 44.105 101.739 1.00 78.20  ? 202 THR C O   1 
ATOM   6558  C  CB  . THR C 1 138 ? 57.158 41.635 100.117 1.00 62.15  ? 202 THR C CB  1 
ATOM   6559  O  OG1 . THR C 1 138 ? 58.456 41.224 100.538 1.00 106.81 ? 202 THR C OG1 1 
ATOM   6560  C  CG2 . THR C 1 138 ? 56.873 40.966 98.804  1.00 59.66  ? 202 THR C CG2 1 
ATOM   6561  N  N   . ILE C 1 139 ? 56.294 43.933 102.106 1.00 53.97  ? 203 ILE C N   1 
ATOM   6562  C  CA  . ILE C 1 139 ? 56.329 44.448 103.468 1.00 57.74  ? 203 ILE C CA  1 
ATOM   6563  C  C   . ILE C 1 139 ? 55.637 43.458 104.425 1.00 65.46  ? 203 ILE C C   1 
ATOM   6564  O  O   . ILE C 1 139 ? 54.535 42.994 104.149 1.00 75.43  ? 203 ILE C O   1 
ATOM   6565  C  CB  . ILE C 1 139 ? 55.634 45.797 103.548 1.00 53.97  ? 203 ILE C CB  1 
ATOM   6566  C  CG1 . ILE C 1 139 ? 56.361 46.822 102.688 1.00 47.87  ? 203 ILE C CG1 1 
ATOM   6567  C  CG2 . ILE C 1 139 ? 55.561 46.278 104.984 1.00 55.23  ? 203 ILE C CG2 1 
ATOM   6568  C  CD1 . ILE C 1 139 ? 55.645 48.144 102.636 1.00 54.87  ? 203 ILE C CD1 1 
ATOM   6569  N  N   . HIS C 1 140 ? 56.287 43.144 105.542 1.00 68.09  ? 204 HIS C N   1 
ATOM   6570  C  CA  . HIS C 1 140 ? 55.789 42.132 106.459 1.00 66.36  ? 204 HIS C CA  1 
ATOM   6571  C  C   . HIS C 1 140 ? 55.416 42.690 107.807 1.00 76.76  ? 204 HIS C C   1 
ATOM   6572  O  O   . HIS C 1 140 ? 56.022 43.655 108.278 1.00 102.41 ? 204 HIS C O   1 
ATOM   6573  C  CB  . HIS C 1 140 ? 56.814 41.023 106.597 1.00 62.00  ? 204 HIS C CB  1 
ATOM   6574  C  CG  . HIS C 1 140 ? 57.176 40.394 105.295 1.00 69.58  ? 204 HIS C CG  1 
ATOM   6575  N  ND1 . HIS C 1 140 ? 56.450 39.405 104.744 1.00 68.04  ? 204 HIS C ND1 1 
ATOM   6576  C  CD2 . HIS C 1 140 ? 58.219 40.663 104.415 1.00 75.75  ? 204 HIS C CD2 1 
ATOM   6577  C  CE1 . HIS C 1 140 ? 57.005 39.048 103.570 1.00 80.82  ? 204 HIS C CE1 1 
ATOM   6578  N  NE2 . HIS C 1 140 ? 58.085 39.823 103.368 1.00 94.76  ? 204 HIS C NE2 1 
ATOM   6579  N  N   . PRO C 1 141 ? 54.410 42.084 108.457 1.00 72.26  ? 205 PRO C N   1 
ATOM   6580  C  CA  . PRO C 1 141 ? 53.918 42.554 109.742 1.00 71.13  ? 205 PRO C CA  1 
ATOM   6581  C  C   . PRO C 1 141 ? 54.893 42.251 110.877 1.00 81.56  ? 205 PRO C C   1 
ATOM   6582  O  O   . PRO C 1 141 ? 55.400 41.125 110.989 1.00 82.66  ? 205 PRO C O   1 
ATOM   6583  C  CB  . PRO C 1 141 ? 52.641 41.729 109.953 1.00 69.21  ? 205 PRO C CB  1 
ATOM   6584  C  CG  . PRO C 1 141 ? 52.455 40.908 108.735 1.00 62.90  ? 205 PRO C CG  1 
ATOM   6585  C  CD  . PRO C 1 141 ? 53.774 40.813 108.074 1.00 74.85  ? 205 PRO C CD  1 
ATOM   6586  N  N   . THR C 1 142 ? 55.150 43.259 111.704 1.00 92.57  ? 206 THR C N   1 
ATOM   6587  C  CA  . THR C 1 142 ? 55.923 43.086 112.933 1.00 102.02 ? 206 THR C CA  1 
ATOM   6588  C  C   . THR C 1 142 ? 54.934 42.920 114.089 1.00 116.42 ? 206 THR C C   1 
ATOM   6589  O  O   . THR C 1 142 ? 54.911 41.891 114.775 1.00 134.64 ? 206 THR C O   1 
ATOM   6590  C  CB  . THR C 1 142 ? 56.858 44.296 113.209 1.00 93.34  ? 206 THR C CB  1 
ATOM   6591  O  OG1 . THR C 1 142 ? 56.072 45.462 113.491 1.00 136.98 ? 206 THR C OG1 1 
ATOM   6592  C  CG2 . THR C 1 142 ? 57.775 44.575 112.013 1.00 76.06  ? 206 THR C CG2 1 
ATOM   6593  N  N   . ASN C 1 143 ? 54.086 43.934 114.247 1.00 113.62 ? 207 ASN C N   1 
ATOM   6594  C  CA  . ASN C 1 143 ? 53.107 44.034 115.320 1.00 91.65  ? 207 ASN C CA  1 
ATOM   6595  C  C   . ASN C 1 143 ? 51.995 42.971 115.243 1.00 89.18  ? 207 ASN C C   1 
ATOM   6596  O  O   . ASN C 1 143 ? 50.943 43.112 115.889 1.00 69.62  ? 207 ASN C O   1 
ATOM   6597  C  CB  . ASN C 1 143 ? 52.511 45.442 115.293 1.00 85.84  ? 207 ASN C CB  1 
ATOM   6598  C  CG  . ASN C 1 143 ? 52.407 46.055 116.647 1.00 95.31  ? 207 ASN C CG  1 
ATOM   6599  O  OD1 . ASN C 1 143 ? 53.300 45.909 117.471 1.00 124.22 ? 207 ASN C OD1 1 
ATOM   6600  N  ND2 . ASN C 1 143 ? 51.322 46.775 116.887 1.00 125.17 ? 207 ASN C ND2 1 
ATOM   6601  N  N   . GLY C 1 144 ? 52.235 41.928 114.442 1.00 94.96  ? 208 GLY C N   1 
ATOM   6602  C  CA  . GLY C 1 144 ? 51.360 40.751 114.338 1.00 87.74  ? 208 GLY C CA  1 
ATOM   6603  C  C   . GLY C 1 144 ? 50.072 41.006 113.584 1.00 97.99  ? 208 GLY C C   1 
ATOM   6604  O  O   . GLY C 1 144 ? 49.748 42.149 113.266 1.00 99.97  ? 208 GLY C O   1 
ATOM   6605  N  N   . GLY C 1 145 ? 49.328 39.940 113.294 1.00 104.08 ? 209 GLY C N   1 
ATOM   6606  C  CA  . GLY C 1 145 ? 48.027 40.077 112.630 1.00 98.17  ? 209 GLY C CA  1 
ATOM   6607  C  C   . GLY C 1 145 ? 48.180 40.813 111.317 1.00 84.87  ? 209 GLY C C   1 
ATOM   6608  O  O   . GLY C 1 145 ? 49.242 41.359 111.058 1.00 87.74  ? 209 GLY C O   1 
ATOM   6609  N  N   . PRO C 1 146 ? 47.118 40.860 110.490 1.00 89.81  ? 210 PRO C N   1 
ATOM   6610  C  CA  . PRO C 1 146 ? 47.265 41.271 109.081 1.00 80.79  ? 210 PRO C CA  1 
ATOM   6611  C  C   . PRO C 1 146 ? 47.549 42.761 108.971 1.00 59.26  ? 210 PRO C C   1 
ATOM   6612  O  O   . PRO C 1 146 ? 47.018 43.524 109.758 1.00 70.70  ? 210 PRO C O   1 
ATOM   6613  C  CB  . PRO C 1 146 ? 45.884 40.979 108.497 1.00 65.72  ? 210 PRO C CB  1 
ATOM   6614  C  CG  . PRO C 1 146 ? 44.969 41.282 109.639 1.00 64.79  ? 210 PRO C CG  1 
ATOM   6615  C  CD  . PRO C 1 146 ? 45.702 40.827 110.895 1.00 80.37  ? 210 PRO C CD  1 
ATOM   6616  N  N   . LEU C 1 147 ? 48.384 43.172 108.029 1.00 45.87  ? 211 LEU C N   1 
ATOM   6617  C  CA  . LEU C 1 147 ? 48.475 44.584 107.699 1.00 46.10  ? 211 LEU C CA  1 
ATOM   6618  C  C   . LEU C 1 147 ? 47.241 45.058 106.940 1.00 55.75  ? 211 LEU C C   1 
ATOM   6619  O  O   . LEU C 1 147 ? 46.382 44.275 106.486 1.00 58.72  ? 211 LEU C O   1 
ATOM   6620  C  CB  . LEU C 1 147 ? 49.697 44.882 106.855 1.00 45.13  ? 211 LEU C CB  1 
ATOM   6621  C  CG  . LEU C 1 147 ? 51.047 44.459 107.375 1.00 46.86  ? 211 LEU C CG  1 
ATOM   6622  C  CD1 . LEU C 1 147 ? 51.962 44.212 106.192 1.00 66.29  ? 211 LEU C CD1 1 
ATOM   6623  C  CD2 . LEU C 1 147 ? 51.557 45.556 108.164 1.00 59.93  ? 211 LEU C CD2 1 
ATOM   6624  N  N   . ARG C 1 148 ? 47.161 46.367 106.785 1.00 61.29  ? 212 ARG C N   1 
ATOM   6625  C  CA  . ARG C 1 148 ? 45.994 46.980 106.171 1.00 63.72  ? 212 ARG C CA  1 
ATOM   6626  C  C   . ARG C 1 148 ? 46.391 48.216 105.392 1.00 60.59  ? 212 ARG C C   1 
ATOM   6627  O  O   . ARG C 1 148 ? 47.156 49.029 105.908 1.00 65.20  ? 212 ARG C O   1 
ATOM   6628  C  CB  . ARG C 1 148 ? 45.009 47.345 107.269 1.00 61.65  ? 212 ARG C CB  1 
ATOM   6629  C  CG  . ARG C 1 148 ? 44.461 46.107 107.987 1.00 85.89  ? 212 ARG C CG  1 
ATOM   6630  C  CD  . ARG C 1 148 ? 43.453 46.435 109.078 1.00 87.69  ? 212 ARG C CD  1 
ATOM   6631  N  NE  . ARG C 1 148 ? 44.053 47.231 110.144 1.00 85.99  ? 212 ARG C NE  1 
ATOM   6632  C  CZ  . ARG C 1 148 ? 44.703 46.735 111.195 1.00 90.78  ? 212 ARG C CZ  1 
ATOM   6633  N  NH1 . ARG C 1 148 ? 44.861 45.423 111.340 1.00 104.40 ? 212 ARG C NH1 1 
ATOM   6634  N  NH2 . ARG C 1 148 ? 45.203 47.557 112.106 1.00 73.97  ? 212 ARG C NH2 1 
ATOM   6635  N  N   . THR C 1 149 ? 45.906 48.346 104.152 1.00 57.82  ? 213 THR C N   1 
ATOM   6636  C  CA  . THR C 1 149 ? 46.250 49.499 103.288 1.00 55.15  ? 213 THR C CA  1 
ATOM   6637  C  C   . THR C 1 149 ? 45.186 50.551 103.422 1.00 55.64  ? 213 THR C C   1 
ATOM   6638  O  O   . THR C 1 149 ? 44.085 50.266 103.923 1.00 60.57  ? 213 THR C O   1 
ATOM   6639  C  CB  . THR C 1 149 ? 46.289 49.138 101.796 1.00 57.45  ? 213 THR C CB  1 
ATOM   6640  O  OG1 . THR C 1 149 ? 45.044 48.546 101.408 1.00 71.45  ? 213 THR C OG1 1 
ATOM   6641  C  CG2 . THR C 1 149 ? 47.379 48.178 101.495 1.00 63.42  ? 213 THR C CG2 1 
ATOM   6642  N  N   . GLN C 1 150 ? 45.487 51.751 102.939 1.00 47.16  ? 214 GLN C N   1 
ATOM   6643  C  CA  . GLN C 1 150 ? 44.490 52.824 102.922 1.00 54.46  ? 214 GLN C CA  1 
ATOM   6644  C  C   . GLN C 1 150 ? 43.151 52.483 102.270 1.00 57.24  ? 214 GLN C C   1 
ATOM   6645  O  O   . GLN C 1 150 ? 42.136 53.094 102.594 1.00 70.46  ? 214 GLN C O   1 
ATOM   6646  C  CB  . GLN C 1 150 ? 45.040 54.031 102.201 1.00 65.94  ? 214 GLN C CB  1 
ATOM   6647  C  CG  . GLN C 1 150 ? 46.283 54.538 102.832 1.00 76.34  ? 214 GLN C CG  1 
ATOM   6648  C  CD  . GLN C 1 150 ? 46.872 55.688 102.091 1.00 77.54  ? 214 GLN C CD  1 
ATOM   6649  O  OE1 . GLN C 1 150 ? 46.785 55.779 100.876 1.00 75.37  ? 214 GLN C OE1 1 
ATOM   6650  N  NE2 . GLN C 1 150 ? 47.490 56.591 102.826 1.00 156.35 ? 214 GLN C NE2 1 
ATOM   6651  N  N   . ALA C 1 151 ? 43.135 51.536 101.342 1.00 51.71  ? 215 ALA C N   1 
ATOM   6652  C  CA  . ALA C 1 151 ? 41.919 51.252 100.606 1.00 53.67  ? 215 ALA C CA  1 
ATOM   6653  C  C   . ALA C 1 151 ? 41.410 52.556 100.017 1.00 54.03  ? 215 ALA C C   1 
ATOM   6654  O  O   . ALA C 1 151 ? 40.236 52.875 100.108 1.00 58.66  ? 215 ALA C O   1 
ATOM   6655  C  CB  . ALA C 1 151 ? 40.867 50.620 101.500 1.00 57.62  ? 215 ALA C CB  1 
ATOM   6656  N  N   . SER C 1 152 ? 42.328 53.296 99.415  1.00 58.33  ? 216 SER C N   1 
ATOM   6657  C  CA  . SER C 1 152 ? 42.083 54.600 98.852  1.00 55.29  ? 216 SER C CA  1 
ATOM   6658  C  C   . SER C 1 152 ? 43.352 54.870 98.088  1.00 54.22  ? 216 SER C C   1 
ATOM   6659  O  O   . SER C 1 152 ? 44.418 54.319 98.403  1.00 70.84  ? 216 SER C O   1 
ATOM   6660  C  CB  . SER C 1 152 ? 41.954 55.627 99.982  1.00 82.28  ? 216 SER C CB  1 
ATOM   6661  O  OG  . SER C 1 152 ? 42.116 56.968 99.530  1.00 130.98 ? 216 SER C OG  1 
ATOM   6662  N  N   . SER C 1 153 ? 43.251 55.724 97.090  1.00 43.70  ? 217 SER C N   1 
ATOM   6663  C  CA  . SER C 1 153 ? 44.426 56.220 96.386  1.00 45.67  ? 217 SER C CA  1 
ATOM   6664  C  C   . SER C 1 153 ? 45.527 56.774 97.315  1.00 48.55  ? 217 SER C C   1 
ATOM   6665  O  O   . SER C 1 153 ? 45.249 57.559 98.228  1.00 69.27  ? 217 SER C O   1 
ATOM   6666  C  CB  . SER C 1 153 ? 43.985 57.291 95.405  1.00 43.37  ? 217 SER C CB  1 
ATOM   6667  O  OG  . SER C 1 153 ? 45.089 58.051 94.988  1.00 57.51  ? 217 SER C OG  1 
ATOM   6668  N  N   . CYS C 1 154 ? 46.765 56.347 97.087  1.00 52.21  ? 218 CYS C N   1 
ATOM   6669  C  CA  . CYS C 1 154 ? 47.915 56.910 97.791  1.00 59.75  ? 218 CYS C CA  1 
ATOM   6670  C  C   . CYS C 1 154 ? 48.321 58.137 97.011  1.00 57.75  ? 218 CYS C C   1 
ATOM   6671  O  O   . CYS C 1 154 ? 47.736 58.411 95.976  1.00 48.19  ? 218 CYS C O   1 
ATOM   6672  C  CB  . CYS C 1 154 ? 49.078 55.917 97.882  1.00 76.12  ? 218 CYS C CB  1 
ATOM   6673  S  SG  . CYS C 1 154 ? 49.213 54.787 96.493  1.00 100.37 ? 218 CYS C SG  1 
ATOM   6674  N  N   . ILE C 1 155 ? 49.309 58.881 97.501  1.00 63.78  ? 219 ILE C N   1 
ATOM   6675  C  CA  . ILE C 1 155 ? 49.611 60.195 96.932  1.00 62.24  ? 219 ILE C CA  1 
ATOM   6676  C  C   . ILE C 1 155 ? 50.994 60.213 96.317  1.00 57.09  ? 219 ILE C C   1 
ATOM   6677  O  O   . ILE C 1 155 ? 51.991 59.914 96.964  1.00 64.23  ? 219 ILE C O   1 
ATOM   6678  C  CB  . ILE C 1 155 ? 49.464 61.317 97.996  1.00 57.88  ? 219 ILE C CB  1 
ATOM   6679  C  CG1 . ILE C 1 155 ? 47.997 61.557 98.302  1.00 68.64  ? 219 ILE C CG1 1 
ATOM   6680  C  CG2 . ILE C 1 155 ? 50.024 62.614 97.488  1.00 59.39  ? 219 ILE C CG2 1 
ATOM   6681  C  CD1 . ILE C 1 155 ? 47.335 60.460 99.093  1.00 89.88  ? 219 ILE C CD1 1 
ATOM   6682  N  N   . CYS C 1 156 ? 51.064 60.556 95.056  1.00 58.68  ? 220 CYS C N   1 
ATOM   6683  C  CA  . CYS C 1 156 ? 52.365 60.672 94.429  1.00 72.76  ? 220 CYS C CA  1 
ATOM   6684  C  C   . CYS C 1 156 ? 52.582 62.110 94.049  1.00 78.55  ? 220 CYS C C   1 
ATOM   6685  O  O   . CYS C 1 156 ? 51.654 62.809 93.614  1.00 79.83  ? 220 CYS C O   1 
ATOM   6686  C  CB  . CYS C 1 156 ? 52.496 59.754 93.210  1.00 81.74  ? 220 CYS C CB  1 
ATOM   6687  S  SG  . CYS C 1 156 ? 52.211 57.997 93.607  1.00 125.13 ? 220 CYS C SG  1 
ATOM   6688  N  N   . ASN C 1 157 ? 53.812 62.552 94.257  1.00 81.49  ? 221 ASN C N   1 
ATOM   6689  C  CA  . ASN C 1 157 ? 54.209 63.912 93.958  1.00 87.50  ? 221 ASN C CA  1 
ATOM   6690  C  C   . ASN C 1 157 ? 55.705 63.962 93.722  1.00 80.66  ? 221 ASN C C   1 
ATOM   6691  O  O   . ASN C 1 157 ? 56.504 63.732 94.623  1.00 74.70  ? 221 ASN C O   1 
ATOM   6692  C  CB  . ASN C 1 157 ? 53.805 64.892 95.078  1.00 86.48  ? 221 ASN C CB  1 
ATOM   6693  C  CG  . ASN C 1 157 ? 53.698 66.326 94.583  1.00 83.56  ? 221 ASN C CG  1 
ATOM   6694  O  OD1 . ASN C 1 157 ? 53.119 66.597 93.515  1.00 83.65  ? 221 ASN C OD1 1 
ATOM   6695  N  ND2 . ASN C 1 157 ? 54.260 67.250 95.349  1.00 80.15  ? 221 ASN C ND2 1 
ATOM   6696  N  N   . ASP C 1 158 ? 56.077 64.273 92.493  1.00 91.57  ? 222 ASP C N   1 
ATOM   6697  C  CA  . ASP C 1 158 ? 57.478 64.374 92.120  1.00 103.41 ? 222 ASP C CA  1 
ATOM   6698  C  C   . ASP C 1 158 ? 58.153 63.013 92.162  1.00 92.08  ? 222 ASP C C   1 
ATOM   6699  O  O   . ASP C 1 158 ? 59.311 62.906 92.551  1.00 84.54  ? 222 ASP C O   1 
ATOM   6700  C  CB  . ASP C 1 158 ? 58.234 65.365 93.020  1.00 126.23 ? 222 ASP C CB  1 
ATOM   6701  C  CG  . ASP C 1 158 ? 57.872 66.812 92.746  1.00 173.32 ? 222 ASP C CG  1 
ATOM   6702  O  OD1 . ASP C 1 158 ? 57.308 67.116 91.673  1.00 188.06 ? 222 ASP C OD1 1 
ATOM   6703  O  OD2 . ASP C 1 158 ? 58.166 67.658 93.616  1.00 215.84 ? 222 ASP C OD2 1 
ATOM   6704  N  N   . GLY C 1 159 ? 57.423 61.973 91.775  1.00 91.51  ? 223 GLY C N   1 
ATOM   6705  C  CA  . GLY C 1 159 ? 58.045 60.672 91.556  1.00 94.78  ? 223 GLY C CA  1 
ATOM   6706  C  C   . GLY C 1 159 ? 58.286 59.801 92.782  1.00 92.42  ? 223 GLY C C   1 
ATOM   6707  O  O   . GLY C 1 159 ? 58.732 58.648 92.650  1.00 92.53  ? 223 GLY C O   1 
ATOM   6708  N  N   . THR C 1 160 ? 58.021 60.352 93.968  1.00 76.96  ? 224 THR C N   1 
ATOM   6709  C  CA  . THR C 1 160 ? 57.928 59.552 95.198  1.00 69.42  ? 224 THR C CA  1 
ATOM   6710  C  C   . THR C 1 160 ? 56.460 59.436 95.641  1.00 64.44  ? 224 THR C C   1 
ATOM   6711  O  O   . THR C 1 160 ? 55.685 60.377 95.510  1.00 66.90  ? 224 THR C O   1 
ATOM   6712  C  CB  . THR C 1 160 ? 58.809 60.105 96.354  1.00 62.35  ? 224 THR C CB  1 
ATOM   6713  O  OG1 . THR C 1 160 ? 58.314 61.380 96.752  1.00 75.49  ? 224 THR C OG1 1 
ATOM   6714  C  CG2 . THR C 1 160 ? 60.247 60.264 95.906  1.00 69.47  ? 224 THR C CG2 1 
ATOM   6715  N  N   . CYS C 1 161 ? 56.067 58.269 96.132  1.00 63.45  ? 225 CYS C N   1 
ATOM   6716  C  CA  . CYS C 1 161 ? 54.683 58.075 96.573  1.00 69.34  ? 225 CYS C CA  1 
ATOM   6717  C  C   . CYS C 1 161 ? 54.591 57.828 98.060  1.00 67.09  ? 225 CYS C C   1 
ATOM   6718  O  O   . CYS C 1 161 ? 55.471 57.174 98.619  1.00 73.36  ? 225 CYS C O   1 
ATOM   6719  C  CB  . CYS C 1 161 ? 54.027 56.918 95.833  1.00 61.35  ? 225 CYS C CB  1 
ATOM   6720  S  SG  . CYS C 1 161 ? 54.052 57.204 94.099  1.00 104.69 ? 225 CYS C SG  1 
ATOM   6721  N  N   . TYR C 1 162 ? 53.517 58.334 98.676  1.00 50.46  ? 226 TYR C N   1 
ATOM   6722  C  CA  . TYR C 1 162 ? 53.296 58.205 100.113 1.00 49.48  ? 226 TYR C CA  1 
ATOM   6723  C  C   . TYR C 1 162 ? 52.049 57.374 100.403 1.00 48.30  ? 226 TYR C C   1 
ATOM   6724  O  O   . TYR C 1 162 ? 50.993 57.588 99.814  1.00 50.00  ? 226 TYR C O   1 
ATOM   6725  C  CB  . TYR C 1 162 ? 53.203 59.582 100.784 1.00 44.81  ? 226 TYR C CB  1 
ATOM   6726  C  CG  . TYR C 1 162 ? 54.330 60.507 100.401 1.00 53.15  ? 226 TYR C CG  1 
ATOM   6727  C  CD1 . TYR C 1 162 ? 55.500 60.560 101.151 1.00 66.06  ? 226 TYR C CD1 1 
ATOM   6728  C  CD2 . TYR C 1 162 ? 54.237 61.328 99.282  1.00 57.14  ? 226 TYR C CD2 1 
ATOM   6729  C  CE1 . TYR C 1 162 ? 56.539 61.422 100.796 1.00 73.95  ? 226 TYR C CE1 1 
ATOM   6730  C  CE2 . TYR C 1 162 ? 55.270 62.182 98.916  1.00 59.53  ? 226 TYR C CE2 1 
ATOM   6731  C  CZ  . TYR C 1 162 ? 56.407 62.228 99.677  1.00 68.34  ? 226 TYR C CZ  1 
ATOM   6732  O  OH  . TYR C 1 162 ? 57.420 63.084 99.334  1.00 83.92  ? 226 TYR C OH  1 
ATOM   6733  N  N   . THR C 1 163 ? 52.173 56.413 101.302 1.00 46.30  ? 227 THR C N   1 
ATOM   6734  C  CA  . THR C 1 163 ? 51.014 55.664 101.729 1.00 53.76  ? 227 THR C CA  1 
ATOM   6735  C  C   . THR C 1 163 ? 51.101 55.274 103.206 1.00 52.92  ? 227 THR C C   1 
ATOM   6736  O  O   . THR C 1 163 ? 52.176 55.219 103.781 1.00 65.64  ? 227 THR C O   1 
ATOM   6737  C  CB  . THR C 1 163 ? 50.834 54.408 100.864 1.00 69.88  ? 227 THR C CB  1 
ATOM   6738  O  OG1 . THR C 1 163 ? 49.595 53.752 101.212 1.00 95.81  ? 227 THR C OG1 1 
ATOM   6739  C  CG2 . THR C 1 163 ? 52.048 53.462 101.038 1.00 56.11  ? 227 THR C CG2 1 
ATOM   6740  N  N   . ILE C 1 164 ? 49.961 54.972 103.803 1.00 47.27  ? 228 ILE C N   1 
ATOM   6741  C  CA  . ILE C 1 164 ? 49.902 54.646 105.211 1.00 46.08  ? 228 ILE C CA  1 
ATOM   6742  C  C   . ILE C 1 164 ? 49.475 53.216 105.446 1.00 43.97  ? 228 ILE C C   1 
ATOM   6743  O  O   . ILE C 1 164 ? 48.467 52.767 104.933 1.00 59.78  ? 228 ILE C O   1 
ATOM   6744  C  CB  . ILE C 1 164 ? 48.951 55.616 105.922 1.00 47.12  ? 228 ILE C CB  1 
ATOM   6745  C  CG1 . ILE C 1 164 ? 49.537 57.015 105.841 1.00 45.08  ? 228 ILE C CG1 1 
ATOM   6746  C  CG2 . ILE C 1 164 ? 48.660 55.189 107.371 1.00 46.66  ? 228 ILE C CG2 1 
ATOM   6747  C  CD1 . ILE C 1 164 ? 48.522 58.061 105.979 1.00 44.59  ? 228 ILE C CD1 1 
ATOM   6748  N  N   . ILE C 1 165 ? 50.257 52.504 106.242 1.00 46.94  ? 229 ILE C N   1 
ATOM   6749  C  CA  . ILE C 1 165 ? 50.014 51.094 106.522 1.00 49.71  ? 229 ILE C CA  1 
ATOM   6750  C  C   . ILE C 1 165 ? 49.726 50.821 107.991 1.00 49.19  ? 229 ILE C C   1 
ATOM   6751  O  O   . ILE C 1 165 ? 50.484 51.235 108.865 1.00 54.25  ? 229 ILE C O   1 
ATOM   6752  C  CB  . ILE C 1 165 ? 51.204 50.239 106.064 1.00 49.78  ? 229 ILE C CB  1 
ATOM   6753  C  CG1 . ILE C 1 165 ? 51.588 50.642 104.639 1.00 56.86  ? 229 ILE C CG1 1 
ATOM   6754  C  CG2 . ILE C 1 165 ? 50.875 48.733 106.198 1.00 50.69  ? 229 ILE C CG2 1 
ATOM   6755  C  CD1 . ILE C 1 165 ? 51.350 49.616 103.575 1.00 56.68  ? 229 ILE C CD1 1 
ATOM   6756  N  N   . ALA C 1 166 ? 48.632 50.111 108.252 1.00 56.47  ? 230 ALA C N   1 
ATOM   6757  C  CA  . ALA C 1 166 ? 48.266 49.691 109.613 1.00 63.19  ? 230 ALA C CA  1 
ATOM   6758  C  C   . ALA C 1 166 ? 48.674 48.240 109.948 1.00 71.39  ? 230 ALA C C   1 
ATOM   6759  O  O   . ALA C 1 166 ? 48.650 47.340 109.086 1.00 77.58  ? 230 ALA C O   1 
ATOM   6760  C  CB  . ALA C 1 166 ? 46.777 49.887 109.836 1.00 55.45  ? 230 ALA C CB  1 
ATOM   6761  N  N   . ASP C 1 167 ? 49.018 48.044 111.218 1.00 70.00  ? 231 ASP C N   1 
ATOM   6762  C  CA  . ASP C 1 167 ? 49.401 46.756 111.797 1.00 76.25  ? 231 ASP C CA  1 
ATOM   6763  C  C   . ASP C 1 167 ? 48.626 46.533 113.109 1.00 75.12  ? 231 ASP C C   1 
ATOM   6764  O  O   . ASP C 1 167 ? 48.154 47.481 113.739 1.00 76.48  ? 231 ASP C O   1 
ATOM   6765  C  CB  . ASP C 1 167 ? 50.911 46.774 112.087 1.00 96.77  ? 231 ASP C CB  1 
ATOM   6766  C  CG  . ASP C 1 167 ? 51.543 45.385 112.075 1.00 97.75  ? 231 ASP C CG  1 
ATOM   6767  O  OD1 . ASP C 1 167 ? 50.803 44.386 112.040 1.00 117.47 ? 231 ASP C OD1 1 
ATOM   6768  O  OD2 . ASP C 1 167 ? 52.794 45.287 112.103 1.00 91.30  ? 231 ASP C OD2 1 
ATOM   6769  N  N   . GLY C 1 168 ? 48.481 45.286 113.529 1.00 68.67  ? 232 GLY C N   1 
ATOM   6770  C  CA  . GLY C 1 168 ? 47.919 45.028 114.855 1.00 69.62  ? 232 GLY C CA  1 
ATOM   6771  C  C   . GLY C 1 168 ? 46.689 44.155 114.903 1.00 74.15  ? 232 GLY C C   1 
ATOM   6772  O  O   . GLY C 1 168 ? 45.894 44.128 113.961 1.00 77.77  ? 232 GLY C O   1 
ATOM   6773  N  N   . THR C 1 169 ? 46.536 43.458 116.026 1.00 89.66  ? 233 THR C N   1 
ATOM   6774  C  CA  . THR C 1 169 ? 45.506 42.431 116.206 1.00 95.07  ? 233 THR C CA  1 
ATOM   6775  C  C   . THR C 1 169 ? 44.118 43.052 116.328 1.00 93.86  ? 233 THR C C   1 
ATOM   6776  O  O   . THR C 1 169 ? 43.135 42.508 115.815 1.00 94.39  ? 233 THR C O   1 
ATOM   6777  C  CB  . THR C 1 169 ? 45.802 41.575 117.460 1.00 95.28  ? 233 THR C CB  1 
ATOM   6778  O  OG1 . THR C 1 169 ? 47.141 41.088 117.383 1.00 115.72 ? 233 THR C OG1 1 
ATOM   6779  C  CG2 . THR C 1 169 ? 44.846 40.388 117.574 1.00 98.07  ? 233 THR C CG2 1 
ATOM   6780  N  N   . THR C 1 170 ? 44.052 44.187 117.014 1.00 86.46  ? 234 THR C N   1 
ATOM   6781  C  CA  . THR C 1 170 ? 42.799 44.892 117.223 1.00 97.21  ? 234 THR C CA  1 
ATOM   6782  C  C   . THR C 1 170 ? 43.049 46.393 117.312 1.00 98.46  ? 234 THR C C   1 
ATOM   6783  O  O   . THR C 1 170 ? 44.186 46.826 117.491 1.00 102.19 ? 234 THR C O   1 
ATOM   6784  C  CB  . THR C 1 170 ? 42.071 44.392 118.486 1.00 112.95 ? 234 THR C CB  1 
ATOM   6785  O  OG1 . THR C 1 170 ? 40.827 45.090 118.628 1.00 123.78 ? 234 THR C OG1 1 
ATOM   6786  C  CG2 . THR C 1 170 ? 42.932 44.599 119.738 1.00 102.09 ? 234 THR C CG2 1 
ATOM   6787  N  N   . TYR C 1 171 ? 41.973 47.169 117.213 1.00 104.84 ? 235 TYR C N   1 
ATOM   6788  C  CA  . TYR C 1 171 ? 42.039 48.619 117.021 1.00 103.54 ? 235 TYR C CA  1 
ATOM   6789  C  C   . TYR C 1 171 ? 42.451 49.354 118.277 1.00 95.06  ? 235 TYR C C   1 
ATOM   6790  O  O   . TYR C 1 171 ? 43.071 50.420 118.224 1.00 105.52 ? 235 TYR C O   1 
ATOM   6791  C  CB  . TYR C 1 171 ? 40.705 49.117 116.481 1.00 121.38 ? 235 TYR C CB  1 
ATOM   6792  C  CG  . TYR C 1 171 ? 40.260 48.295 115.294 1.00 161.87 ? 235 TYR C CG  1 
ATOM   6793  C  CD1 . TYR C 1 171 ? 40.995 48.300 114.096 1.00 171.53 ? 235 TYR C CD1 1 
ATOM   6794  C  CD2 . TYR C 1 171 ? 39.133 47.482 115.372 1.00 172.64 ? 235 TYR C CD2 1 
ATOM   6795  C  CE1 . TYR C 1 171 ? 40.601 47.527 112.998 1.00 153.81 ? 235 TYR C CE1 1 
ATOM   6796  C  CE2 . TYR C 1 171 ? 38.732 46.709 114.278 1.00 189.62 ? 235 TYR C CE2 1 
ATOM   6797  C  CZ  . TYR C 1 171 ? 39.471 46.739 113.098 1.00 157.29 ? 235 TYR C CZ  1 
ATOM   6798  O  OH  . TYR C 1 171 ? 39.081 45.983 112.021 1.00 165.52 ? 235 TYR C OH  1 
ATOM   6799  N  N   . THR C 1 172 ? 42.121 48.756 119.408 1.00 86.38  ? 236 THR C N   1 
ATOM   6800  C  CA  . THR C 1 172 ? 42.685 49.149 120.685 1.00 94.62  ? 236 THR C CA  1 
ATOM   6801  C  C   . THR C 1 172 ? 44.226 49.169 120.610 1.00 90.35  ? 236 THR C C   1 
ATOM   6802  O  O   . THR C 1 172 ? 44.867 50.006 121.226 1.00 86.85  ? 236 THR C O   1 
ATOM   6803  C  CB  . THR C 1 172 ? 42.207 48.185 121.811 1.00 108.86 ? 236 THR C CB  1 
ATOM   6804  O  OG1 . THR C 1 172 ? 42.965 46.970 121.776 1.00 118.52 ? 236 THR C OG1 1 
ATOM   6805  C  CG2 . THR C 1 172 ? 40.733 47.826 121.648 1.00 113.55 ? 236 THR C CG2 1 
ATOM   6806  N  N   . ALA C 1 173 ? 44.800 48.259 119.822 1.00 102.03 ? 237 ALA C N   1 
ATOM   6807  C  CA  . ALA C 1 173 ? 46.244 48.000 119.822 1.00 90.89  ? 237 ALA C CA  1 
ATOM   6808  C  C   . ALA C 1 173 ? 46.957 48.347 118.510 1.00 81.88  ? 237 ALA C C   1 
ATOM   6809  O  O   . ALA C 1 173 ? 48.085 47.915 118.289 1.00 95.13  ? 237 ALA C O   1 
ATOM   6810  C  CB  . ALA C 1 173 ? 46.500 46.530 120.187 1.00 103.51 ? 237 ALA C CB  1 
ATOM   6811  N  N   . SER C 1 174 ? 46.319 49.134 117.650 1.00 78.44  ? 238 SER C N   1 
ATOM   6812  C  CA  . SER C 1 174 ? 46.869 49.422 116.301 1.00 74.90  ? 238 SER C CA  1 
ATOM   6813  C  C   . SER C 1 174 ? 48.163 50.248 116.257 1.00 69.21  ? 238 SER C C   1 
ATOM   6814  O  O   . SER C 1 174 ? 48.454 51.047 117.137 1.00 71.74  ? 238 SER C O   1 
ATOM   6815  C  CB  . SER C 1 174 ? 45.810 50.048 115.376 1.00 73.20  ? 238 SER C CB  1 
ATOM   6816  O  OG  . SER C 1 174 ? 45.385 51.327 115.824 1.00 70.05  ? 238 SER C OG  1 
ATOM   6817  N  N   . SER C 1 175 ? 48.927 50.028 115.202 1.00 74.35  ? 239 SER C N   1 
ATOM   6818  C  CA  . SER C 1 175 ? 50.176 50.709 114.942 1.00 70.46  ? 239 SER C CA  1 
ATOM   6819  C  C   . SER C 1 175 ? 50.098 51.172 113.493 1.00 71.97  ? 239 SER C C   1 
ATOM   6820  O  O   . SER C 1 175 ? 49.616 50.434 112.643 1.00 96.39  ? 239 SER C O   1 
ATOM   6821  C  CB  . SER C 1 175 ? 51.333 49.719 115.092 1.00 69.16  ? 239 SER C CB  1 
ATOM   6822  O  OG  . SER C 1 175 ? 52.555 50.301 114.683 1.00 96.84  ? 239 SER C OG  1 
ATOM   6823  N  N   . HIS C 1 176 ? 50.561 52.382 113.191 1.00 61.84  ? 240 HIS C N   1 
ATOM   6824  C  CA  . HIS C 1 176 ? 50.519 52.879 111.816 1.00 51.20  ? 240 HIS C CA  1 
ATOM   6825  C  C   . HIS C 1 176 ? 51.841 53.443 111.415 1.00 55.34  ? 240 HIS C C   1 
ATOM   6826  O  O   . HIS C 1 176 ? 52.440 54.261 112.119 1.00 56.39  ? 240 HIS C O   1 
ATOM   6827  C  CB  . HIS C 1 176 ? 49.432 53.919 111.661 1.00 54.39  ? 240 HIS C CB  1 
ATOM   6828  C  CG  . HIS C 1 176 ? 48.089 53.442 112.132 1.00 62.58  ? 240 HIS C CG  1 
ATOM   6829  N  ND1 . HIS C 1 176 ? 47.058 52.827 111.446 1.00 58.74  ? 240 HIS C ND1 1 
ATOM   6830  C  CD2 . HIS C 1 176 ? 47.693 53.525 113.417 1.00 77.02  ? 240 HIS C CD2 1 
ATOM   6831  C  CE1 . HIS C 1 176 ? 46.079 52.563 112.340 1.00 61.34  ? 240 HIS C CE1 1 
ATOM   6832  N  NE2 . HIS C 1 176 ? 46.472 52.991 113.545 1.00 75.11  ? 240 HIS C NE2 1 
ATOM   6833  N  N   . ARG C 1 177 ? 52.323 52.996 110.269 1.00 52.98  ? 241 ARG C N   1 
ATOM   6834  C  CA  . ARG C 1 177 ? 53.524 53.565 109.693 1.00 53.43  ? 241 ARG C CA  1 
ATOM   6835  C  C   . ARG C 1 177 ? 53.162 54.344 108.445 1.00 51.78  ? 241 ARG C C   1 
ATOM   6836  O  O   . ARG C 1 177 ? 52.212 54.044 107.741 1.00 61.65  ? 241 ARG C O   1 
ATOM   6837  C  CB  . ARG C 1 177 ? 54.556 52.471 109.396 1.00 57.51  ? 241 ARG C CB  1 
ATOM   6838  C  CG  . ARG C 1 177 ? 54.974 51.736 110.645 1.00 66.25  ? 241 ARG C CG  1 
ATOM   6839  C  CD  . ARG C 1 177 ? 54.968 50.275 110.437 1.00 68.75  ? 241 ARG C CD  1 
ATOM   6840  N  NE  . ARG C 1 177 ? 56.244 49.824 109.901 1.00 83.53  ? 241 ARG C NE  1 
ATOM   6841  C  CZ  . ARG C 1 177 ? 57.242 49.370 110.651 1.00 75.56  ? 241 ARG C CZ  1 
ATOM   6842  N  NH1 . ARG C 1 177 ? 57.119 49.325 111.977 1.00 52.89  ? 241 ARG C NH1 1 
ATOM   6843  N  NH2 . ARG C 1 177 ? 58.364 48.966 110.069 1.00 79.59  ? 241 ARG C NH2 1 
ATOM   6844  N  N   . LEU C 1 178 ? 53.941 55.362 108.190 1.00 51.48  ? 242 LEU C N   1 
ATOM   6845  C  CA  . LEU C 1 178 ? 53.805 56.169 107.016 1.00 56.81  ? 242 LEU C CA  1 
ATOM   6846  C  C   . LEU C 1 178 ? 54.966 55.802 106.096 1.00 56.44  ? 242 LEU C C   1 
ATOM   6847  O  O   . LEU C 1 178 ? 56.107 56.059 106.422 1.00 64.84  ? 242 LEU C O   1 
ATOM   6848  C  CB  . LEU C 1 178 ? 53.871 57.619 107.468 1.00 59.13  ? 242 LEU C CB  1 
ATOM   6849  C  CG  . LEU C 1 178 ? 54.134 58.763 106.521 1.00 70.59  ? 242 LEU C CG  1 
ATOM   6850  C  CD1 . LEU C 1 178 ? 53.075 58.796 105.477 1.00 87.72  ? 242 LEU C CD1 1 
ATOM   6851  C  CD2 . LEU C 1 178 ? 54.086 60.037 107.338 1.00 71.11  ? 242 LEU C CD2 1 
ATOM   6852  N  N   . TYR C 1 179 ? 54.664 55.154 104.972 1.00 59.35  ? 243 TYR C N   1 
ATOM   6853  C  CA  . TYR C 1 179 ? 55.677 54.681 104.022 1.00 51.93  ? 243 TYR C CA  1 
ATOM   6854  C  C   . TYR C 1 179 ? 55.958 55.658 102.900 1.00 52.04  ? 243 TYR C C   1 
ATOM   6855  O  O   . TYR C 1 179 ? 55.088 56.395 102.470 1.00 57.95  ? 243 TYR C O   1 
ATOM   6856  C  CB  . TYR C 1 179 ? 55.248 53.348 103.426 1.00 48.05  ? 243 TYR C CB  1 
ATOM   6857  C  CG  . TYR C 1 179 ? 55.595 52.199 104.326 1.00 53.90  ? 243 TYR C CG  1 
ATOM   6858  C  CD1 . TYR C 1 179 ? 54.682 51.743 105.277 1.00 54.80  ? 243 TYR C CD1 1 
ATOM   6859  C  CD2 . TYR C 1 179 ? 56.850 51.594 104.258 1.00 52.59  ? 243 TYR C CD2 1 
ATOM   6860  C  CE1 . TYR C 1 179 ? 54.993 50.697 106.124 1.00 69.38  ? 243 TYR C CE1 1 
ATOM   6861  C  CE2 . TYR C 1 179 ? 57.172 50.545 105.094 1.00 68.22  ? 243 TYR C CE2 1 
ATOM   6862  C  CZ  . TYR C 1 179 ? 56.244 50.095 106.035 1.00 83.63  ? 243 TYR C CZ  1 
ATOM   6863  O  OH  . TYR C 1 179 ? 56.572 49.040 106.877 1.00 99.97  ? 243 TYR C OH  1 
ATOM   6864  N  N   . ARG C 1 180 ? 57.192 55.652 102.429 1.00 52.78  ? 244 ARG C N   1 
ATOM   6865  C  CA  . ARG C 1 180 ? 57.589 56.409 101.248 1.00 60.83  ? 244 ARG C CA  1 
ATOM   6866  C  C   . ARG C 1 180 ? 58.133 55.416 100.183 1.00 64.83  ? 244 ARG C C   1 
ATOM   6867  O  O   . ARG C 1 180 ? 58.945 54.555 100.476 1.00 82.65  ? 244 ARG C O   1 
ATOM   6868  C  CB  . ARG C 1 180 ? 58.591 57.486 101.656 1.00 65.18  ? 244 ARG C CB  1 
ATOM   6869  C  CG  . ARG C 1 180 ? 59.508 58.018 100.599 1.00 90.72  ? 244 ARG C CG  1 
ATOM   6870  C  CD  . ARG C 1 180 ? 60.538 58.975 101.248 1.00 112.13 ? 244 ARG C CD  1 
ATOM   6871  N  NE  . ARG C 1 180 ? 61.801 58.929 100.512 1.00 158.16 ? 244 ARG C NE  1 
ATOM   6872  C  CZ  . ARG C 1 180 ? 62.291 59.914 99.760  1.00 175.83 ? 244 ARG C CZ  1 
ATOM   6873  N  NH1 . ARG C 1 180 ? 61.646 61.071 99.653  1.00 172.78 ? 244 ARG C NH1 1 
ATOM   6874  N  NH2 . ARG C 1 180 ? 63.447 59.742 99.126  1.00 179.68 ? 244 ARG C NH2 1 
ATOM   6875  N  N   . LEU C 1 181 ? 57.637 55.516 98.958  1.00 66.56  ? 245 LEU C N   1 
ATOM   6876  C  CA  . LEU C 1 181 ? 57.979 54.578 97.903  1.00 55.01  ? 245 LEU C CA  1 
ATOM   6877  C  C   . LEU C 1 181 ? 58.497 55.327 96.693  1.00 58.24  ? 245 LEU C C   1 
ATOM   6878  O  O   . LEU C 1 181 ? 58.001 56.410 96.358  1.00 57.75  ? 245 LEU C O   1 
ATOM   6879  C  CB  . LEU C 1 181 ? 56.734 53.826 97.463  1.00 49.71  ? 245 LEU C CB  1 
ATOM   6880  C  CG  . LEU C 1 181 ? 55.894 53.224 98.574  1.00 52.15  ? 245 LEU C CG  1 
ATOM   6881  C  CD1 . LEU C 1 181 ? 54.509 52.956 98.097  1.00 60.29  ? 245 LEU C CD1 1 
ATOM   6882  C  CD2 . LEU C 1 181 ? 56.524 51.967 99.069  1.00 54.21  ? 245 LEU C CD2 1 
ATOM   6883  N  N   . VAL C 1 182 ? 59.480 54.745 96.020  1.00 54.39  ? 246 VAL C N   1 
ATOM   6884  C  CA  . VAL C 1 182 ? 59.989 55.323 94.790  1.00 54.25  ? 246 VAL C CA  1 
ATOM   6885  C  C   . VAL C 1 182 ? 60.133 54.186 93.788  1.00 58.98  ? 246 VAL C C   1 
ATOM   6886  O  O   . VAL C 1 182 ? 60.688 53.138 94.119  1.00 51.26  ? 246 VAL C O   1 
ATOM   6887  C  CB  . VAL C 1 182 ? 61.376 55.964 94.978  1.00 57.52  ? 246 VAL C CB  1 
ATOM   6888  C  CG1 . VAL C 1 182 ? 61.724 56.797 93.758  1.00 62.38  ? 246 VAL C CG1 1 
ATOM   6889  C  CG2 . VAL C 1 182 ? 61.452 56.801 96.243  1.00 54.19  ? 246 VAL C CG2 1 
ATOM   6890  N  N   . ASN C 1 183 ? 59.645 54.401 92.563  1.00 66.70  ? 247 ASN C N   1 
ATOM   6891  C  CA  . ASN C 1 183 ? 59.701 53.400 91.502  1.00 53.63  ? 247 ASN C CA  1 
ATOM   6892  C  C   . ASN C 1 183 ? 59.412 52.012 92.096  1.00 52.91  ? 247 ASN C C   1 
ATOM   6893  O  O   . ASN C 1 183 ? 59.983 51.005 91.664  1.00 72.62  ? 247 ASN C O   1 
ATOM   6894  C  CB  . ASN C 1 183 ? 61.059 53.448 90.753  1.00 61.93  ? 247 ASN C CB  1 
ATOM   6895  C  CG  . ASN C 1 183 ? 61.336 54.804 90.052  1.00 81.53  ? 247 ASN C CG  1 
ATOM   6896  O  OD1 . ASN C 1 183 ? 60.478 55.700 90.031  1.00 120.62 ? 247 ASN C OD1 1 
ATOM   6897  N  ND2 . ASN C 1 183 ? 62.565 54.939 89.463  1.00 78.95  ? 247 ASN C ND2 1 
ATOM   6898  N  N   . GLY C 1 184 ? 58.549 51.966 93.114  1.00 44.80  ? 248 GLY C N   1 
ATOM   6899  C  CA  . GLY C 1 184 ? 57.993 50.712 93.602  1.00 44.49  ? 248 GLY C CA  1 
ATOM   6900  C  C   . GLY C 1 184 ? 58.706 50.024 94.739  1.00 55.00  ? 248 GLY C C   1 
ATOM   6901  O  O   . GLY C 1 184 ? 58.246 49.010 95.250  1.00 57.38  ? 248 GLY C O   1 
ATOM   6902  N  N   . THR C 1 185 ? 59.840 50.572 95.144  1.00 72.00  ? 249 THR C N   1 
ATOM   6903  C  CA  . THR C 1 185 ? 60.573 50.056 96.291  1.00 61.95  ? 249 THR C CA  1 
ATOM   6904  C  C   . THR C 1 185 ? 60.377 51.038 97.460  1.00 62.61  ? 249 THR C C   1 
ATOM   6905  O  O   . THR C 1 185 ? 60.093 52.224 97.247  1.00 63.70  ? 249 THR C O   1 
ATOM   6906  C  CB  . THR C 1 185 ? 62.073 49.811 95.937  1.00 70.18  ? 249 THR C CB  1 
ATOM   6907  O  OG1 . THR C 1 185 ? 62.627 50.946 95.254  1.00 81.40  ? 249 THR C OG1 1 
ATOM   6908  C  CG2 . THR C 1 185 ? 62.202 48.618 95.023  1.00 80.06  ? 249 THR C CG2 1 
ATOM   6909  N  N   . SER C 1 186 ? 60.486 50.550 98.690  1.00 70.48  ? 250 SER C N   1 
ATOM   6910  C  CA  . SER C 1 186 ? 60.307 51.433 99.841  1.00 76.09  ? 250 SER C CA  1 
ATOM   6911  C  C   . SER C 1 186 ? 61.571 52.244 100.019 1.00 64.24  ? 250 SER C C   1 
ATOM   6912  O  O   . SER C 1 186 ? 62.659 51.730 99.894  1.00 60.01  ? 250 SER C O   1 
ATOM   6913  C  CB  . SER C 1 186 ? 59.942 50.674 101.127 1.00 87.80  ? 250 SER C CB  1 
ATOM   6914  O  OG  . SER C 1 186 ? 60.908 49.695 101.458 1.00 108.82 ? 250 SER C OG  1 
ATOM   6915  N  N   . ALA C 1 187 ? 61.400 53.536 100.240 1.00 76.78  ? 251 ALA C N   1 
ATOM   6916  C  CA  . ALA C 1 187 ? 62.505 54.456 100.422 1.00 70.54  ? 251 ALA C CA  1 
ATOM   6917  C  C   . ALA C 1 187 ? 62.416 54.913 101.834 1.00 64.89  ? 251 ALA C C   1 
ATOM   6918  O  O   . ALA C 1 187 ? 62.868 56.007 102.170 1.00 87.32  ? 251 ALA C O   1 
ATOM   6919  C  CB  . ALA C 1 187 ? 62.396 55.651 99.467  1.00 72.47  ? 251 ALA C CB  1 
ATOM   6920  N  N   . GLY C 1 188 ? 61.795 54.080 102.657 1.00 58.72  ? 252 GLY C N   1 
ATOM   6921  C  CA  . GLY C 1 188 ? 61.794 54.316 104.102 1.00 78.46  ? 252 GLY C CA  1 
ATOM   6922  C  C   . GLY C 1 188 ? 60.429 54.618 104.654 1.00 73.20  ? 252 GLY C C   1 
ATOM   6923  O  O   . GLY C 1 188 ? 59.466 54.717 103.888 1.00 71.79  ? 252 GLY C O   1 
ATOM   6924  N  N   . TRP C 1 189 ? 60.348 54.765 105.977 1.00 64.74  ? 253 TRP C N   1 
ATOM   6925  C  CA  . TRP C 1 189 ? 59.079 55.082 106.623 1.00 59.50  ? 253 TRP C CA  1 
ATOM   6926  C  C   . TRP C 1 189 ? 59.287 55.773 107.936 1.00 58.50  ? 253 TRP C C   1 
ATOM   6927  O  O   . TRP C 1 189 ? 60.424 56.022 108.347 1.00 67.23  ? 253 TRP C O   1 
ATOM   6928  C  CB  . TRP C 1 189 ? 58.236 53.823 106.771 1.00 53.62  ? 253 TRP C CB  1 
ATOM   6929  C  CG  . TRP C 1 189 ? 59.004 52.759 107.505 1.00 64.21  ? 253 TRP C CG  1 
ATOM   6930  C  CD1 . TRP C 1 189 ? 59.859 51.789 106.976 1.00 66.67  ? 253 TRP C CD1 1 
ATOM   6931  C  CD2 . TRP C 1 189 ? 59.051 52.552 108.946 1.00 53.45  ? 253 TRP C CD2 1 
ATOM   6932  N  NE1 . TRP C 1 189 ? 60.369 50.994 107.967 1.00 52.89  ? 253 TRP C NE1 1 
ATOM   6933  C  CE2 . TRP C 1 189 ? 59.937 51.404 109.169 1.00 52.80  ? 253 TRP C CE2 1 
ATOM   6934  C  CE3 . TRP C 1 189 ? 58.447 53.153 110.021 1.00 52.31  ? 253 TRP C CE3 1 
ATOM   6935  C  CZ2 . TRP C 1 189 ? 60.201 50.918 110.429 1.00 55.02  ? 253 TRP C CZ2 1 
ATOM   6936  C  CZ3 . TRP C 1 189 ? 58.712 52.665 111.294 1.00 58.27  ? 253 TRP C CZ3 1 
ATOM   6937  C  CH2 . TRP C 1 189 ? 59.574 51.573 111.496 1.00 59.37  ? 253 TRP C CH2 1 
ATOM   6938  N  N   . LYS C 1 190 ? 58.179 56.132 108.575 1.00 55.80  ? 254 LYS C N   1 
ATOM   6939  C  CA  . LYS C 1 190 ? 58.190 56.740 109.899 1.00 57.82  ? 254 LYS C CA  1 
ATOM   6940  C  C   . LYS C 1 190 ? 57.027 56.169 110.707 1.00 58.96  ? 254 LYS C C   1 
ATOM   6941  O  O   . LYS C 1 190 ? 55.951 55.958 110.177 1.00 65.96  ? 254 LYS C O   1 
ATOM   6942  C  CB  . LYS C 1 190 ? 58.117 58.259 109.796 1.00 58.96  ? 254 LYS C CB  1 
ATOM   6943  C  CG  . LYS C 1 190 ? 58.017 58.957 111.138 1.00 71.68  ? 254 LYS C CG  1 
ATOM   6944  C  CD  . LYS C 1 190 ? 58.578 60.376 111.126 1.00 66.31  ? 254 LYS C CD  1 
ATOM   6945  C  CE  . LYS C 1 190 ? 58.362 60.996 112.489 1.00 87.42  ? 254 LYS C CE  1 
ATOM   6946  N  NZ  . LYS C 1 190 ? 59.175 62.225 112.744 1.00 112.56 ? 254 LYS C NZ  1 
ATOM   6947  N  N   . ALA C 1 191 ? 57.252 55.853 111.975 1.00 64.70  ? 255 ALA C N   1 
ATOM   6948  C  CA  . ALA C 1 191 ? 56.138 55.455 112.808 1.00 67.74  ? 255 ALA C CA  1 
ATOM   6949  C  C   . ALA C 1 191 ? 55.333 56.697 113.159 1.00 59.00  ? 255 ALA C C   1 
ATOM   6950  O  O   . ALA C 1 191 ? 55.879 57.733 113.482 1.00 61.52  ? 255 ALA C O   1 
ATOM   6951  C  CB  . ALA C 1 191 ? 56.611 54.752 114.039 1.00 83.68  ? 255 ALA C CB  1 
ATOM   6952  N  N   . LEU C 1 192 ? 54.027 56.583 113.042 1.00 59.73  ? 256 LEU C N   1 
ATOM   6953  C  CA  . LEU C 1 192 ? 53.136 57.628 113.441 1.00 66.26  ? 256 LEU C CA  1 
ATOM   6954  C  C   . LEU C 1 192 ? 52.683 57.340 114.880 1.00 78.13  ? 256 LEU C C   1 
ATOM   6955  O  O   . LEU C 1 192 ? 52.309 56.193 115.212 1.00 71.99  ? 256 LEU C O   1 
ATOM   6956  C  CB  . LEU C 1 192 ? 51.935 57.671 112.480 1.00 82.84  ? 256 LEU C CB  1 
ATOM   6957  C  CG  . LEU C 1 192 ? 52.145 58.114 111.029 1.00 71.83  ? 256 LEU C CG  1 
ATOM   6958  C  CD1 . LEU C 1 192 ? 50.863 57.957 110.306 1.00 77.85  ? 256 LEU C CD1 1 
ATOM   6959  C  CD2 . LEU C 1 192 ? 52.602 59.553 110.941 1.00 62.86  ? 256 LEU C CD2 1 
ATOM   6960  N  N   . ASP C 1 193 ? 52.717 58.378 115.726 1.00 76.95  ? 257 ASP C N   1 
ATOM   6961  C  CA  . ASP C 1 193 ? 52.268 58.260 117.105 1.00 79.36  ? 257 ASP C CA  1 
ATOM   6962  C  C   . ASP C 1 193 ? 50.745 58.308 117.233 1.00 86.15  ? 257 ASP C C   1 
ATOM   6963  O  O   . ASP C 1 193 ? 50.144 59.367 117.205 1.00 101.14 ? 257 ASP C O   1 
ATOM   6964  C  CB  . ASP C 1 193 ? 52.909 59.326 117.966 1.00 79.30  ? 257 ASP C CB  1 
ATOM   6965  C  CG  . ASP C 1 193 ? 52.579 59.164 119.443 1.00 95.93  ? 257 ASP C CG  1 
ATOM   6966  O  OD1 . ASP C 1 193 ? 51.830 58.233 119.816 1.00 124.71 ? 257 ASP C OD1 1 
ATOM   6967  O  OD2 . ASP C 1 193 ? 53.082 59.974 120.244 1.00 93.41  ? 257 ASP C OD2 1 
ATOM   6968  N  N   . THR C 1 194 ? 50.149 57.134 117.398 1.00 113.68 ? 258 THR C N   1 
ATOM   6969  C  CA  . THR C 1 194 ? 48.714 56.950 117.376 1.00 108.43 ? 258 THR C CA  1 
ATOM   6970  C  C   . THR C 1 194 ? 48.141 56.792 118.792 1.00 124.64 ? 258 THR C C   1 
ATOM   6971  O  O   . THR C 1 194 ? 46.928 56.900 118.981 1.00 136.42 ? 258 THR C O   1 
ATOM   6972  C  CB  . THR C 1 194 ? 48.372 55.692 116.552 1.00 110.91 ? 258 THR C CB  1 
ATOM   6973  O  OG1 . THR C 1 194 ? 46.964 55.646 116.322 1.00 156.55 ? 258 THR C OG1 1 
ATOM   6974  C  CG2 . THR C 1 194 ? 48.819 54.395 117.290 1.00 104.82 ? 258 THR C CG2 1 
ATOM   6975  N  N   . THR C 1 195 ? 49.014 56.549 119.776 1.00 125.71 ? 259 THR C N   1 
ATOM   6976  C  CA  . THR C 1 195 ? 48.594 56.038 121.097 1.00 124.61 ? 259 THR C CA  1 
ATOM   6977  C  C   . THR C 1 195 ? 47.402 56.765 121.707 1.00 98.03  ? 259 THR C C   1 
ATOM   6978  O  O   . THR C 1 195 ? 47.325 58.000 121.719 1.00 78.82  ? 259 THR C O   1 
ATOM   6979  C  CB  . THR C 1 195 ? 49.746 55.970 122.147 1.00 134.75 ? 259 THR C CB  1 
ATOM   6980  O  OG1 . THR C 1 195 ? 50.310 57.274 122.335 1.00 116.22 ? 259 THR C OG1 1 
ATOM   6981  C  CG2 . THR C 1 195 ? 50.836 54.958 121.733 1.00 128.33 ? 259 THR C CG2 1 
ATOM   6982  N  N   . GLY C 1 196 ? 46.469 55.970 122.205 1.00 93.53  ? 260 GLY C N   1 
ATOM   6983  C  CA  . GLY C 1 196 ? 45.257 56.511 122.772 1.00 105.43 ? 260 GLY C CA  1 
ATOM   6984  C  C   . GLY C 1 196 ? 44.125 56.564 121.773 1.00 104.76 ? 260 GLY C C   1 
ATOM   6985  O  O   . GLY C 1 196 ? 42.967 56.673 122.159 1.00 121.77 ? 260 GLY C O   1 
ATOM   6986  N  N   . PHE C 1 197 ? 44.450 56.499 120.486 1.00 94.08  ? 261 PHE C N   1 
ATOM   6987  C  CA  . PHE C 1 197 ? 43.414 56.422 119.462 1.00 88.97  ? 261 PHE C CA  1 
ATOM   6988  C  C   . PHE C 1 197 ? 43.752 55.454 118.311 1.00 85.67  ? 261 PHE C C   1 
ATOM   6989  O  O   . PHE C 1 197 ? 44.685 54.658 118.418 1.00 106.41 ? 261 PHE C O   1 
ATOM   6990  C  CB  . PHE C 1 197 ? 43.012 57.819 118.979 1.00 78.32  ? 261 PHE C CB  1 
ATOM   6991  C  CG  . PHE C 1 197 ? 44.025 58.481 118.107 1.00 78.95  ? 261 PHE C CG  1 
ATOM   6992  C  CD1 . PHE C 1 197 ? 43.878 58.472 116.732 1.00 78.34  ? 261 PHE C CD1 1 
ATOM   6993  C  CD2 . PHE C 1 197 ? 45.104 59.155 118.657 1.00 84.55  ? 261 PHE C CD2 1 
ATOM   6994  C  CE1 . PHE C 1 197 ? 44.805 59.108 115.916 1.00 82.42  ? 261 PHE C CE1 1 
ATOM   6995  C  CE2 . PHE C 1 197 ? 46.039 59.790 117.845 1.00 78.95  ? 261 PHE C CE2 1 
ATOM   6996  C  CZ  . PHE C 1 197 ? 45.887 59.769 116.476 1.00 75.22  ? 261 PHE C CZ  1 
ATOM   6997  N  N   . ASN C 1 198 ? 42.970 55.505 117.236 1.00 75.48  ? 262 ASN C N   1 
ATOM   6998  C  CA  . ASN C 1 198 ? 43.118 54.587 116.109 1.00 72.38  ? 262 ASN C CA  1 
ATOM   6999  C  C   . ASN C 1 198 ? 42.798 55.298 114.775 1.00 86.35  ? 262 ASN C C   1 
ATOM   7000  O  O   . ASN C 1 198 ? 41.910 56.163 114.708 1.00 101.08 ? 262 ASN C O   1 
ATOM   7001  C  CB  . ASN C 1 198 ? 42.271 53.328 116.370 1.00 74.33  ? 262 ASN C CB  1 
ATOM   7002  C  CG  . ASN C 1 198 ? 41.825 52.628 115.110 1.00 88.09  ? 262 ASN C CG  1 
ATOM   7003  O  OD1 . ASN C 1 198 ? 40.653 52.719 114.719 1.00 103.11 ? 262 ASN C OD1 1 
ATOM   7004  N  ND2 . ASN C 1 198 ? 42.747 51.915 114.467 1.00 82.27  ? 262 ASN C ND2 1 
ATOM   7005  N  N   . PHE C 1 199 ? 43.530 54.934 113.722 1.00 76.73  ? 263 PHE C N   1 
ATOM   7006  C  CA  . PHE C 1 199 ? 43.585 55.725 112.495 1.00 69.00  ? 263 PHE C CA  1 
ATOM   7007  C  C   . PHE C 1 199 ? 43.577 54.839 111.255 1.00 64.73  ? 263 PHE C C   1 
ATOM   7008  O  O   . PHE C 1 199 ? 44.630 54.490 110.722 1.00 81.96  ? 263 PHE C O   1 
ATOM   7009  C  CB  . PHE C 1 199 ? 44.858 56.568 112.543 1.00 62.38  ? 263 PHE C CB  1 
ATOM   7010  C  CG  . PHE C 1 199 ? 44.994 57.545 111.427 1.00 61.38  ? 263 PHE C CG  1 
ATOM   7011  C  CD1 . PHE C 1 199 ? 44.140 58.631 111.314 1.00 67.25  ? 263 PHE C CD1 1 
ATOM   7012  C  CD2 . PHE C 1 199 ? 45.997 57.393 110.504 1.00 68.51  ? 263 PHE C CD2 1 
ATOM   7013  C  CE1 . PHE C 1 199 ? 44.283 59.541 110.282 1.00 70.77  ? 263 PHE C CE1 1 
ATOM   7014  C  CE2 . PHE C 1 199 ? 46.151 58.298 109.461 1.00 83.24  ? 263 PHE C CE2 1 
ATOM   7015  C  CZ  . PHE C 1 199 ? 45.288 59.371 109.344 1.00 78.32  ? 263 PHE C CZ  1 
ATOM   7016  N  N   . GLU C 1 200 ? 42.387 54.493 110.781 1.00 68.06  ? 264 GLU C N   1 
ATOM   7017  C  CA  . GLU C 1 200 ? 42.260 53.496 109.711 1.00 68.99  ? 264 GLU C CA  1 
ATOM   7018  C  C   . GLU C 1 200 ? 41.691 54.038 108.419 1.00 66.35  ? 264 GLU C C   1 
ATOM   7019  O  O   . GLU C 1 200 ? 40.900 54.977 108.403 1.00 79.34  ? 264 GLU C O   1 
ATOM   7020  C  CB  . GLU C 1 200 ? 41.372 52.365 110.176 1.00 61.77  ? 264 GLU C CB  1 
ATOM   7021  C  CG  . GLU C 1 200 ? 41.884 51.671 111.395 1.00 71.70  ? 264 GLU C CG  1 
ATOM   7022  C  CD  . GLU C 1 200 ? 42.706 50.471 111.034 1.00 94.73  ? 264 GLU C CD  1 
ATOM   7023  O  OE1 . GLU C 1 200 ? 42.685 50.099 109.817 1.00 92.53  ? 264 GLU C OE1 1 
ATOM   7024  O  OE2 . GLU C 1 200 ? 43.355 49.919 111.970 1.00 84.74  ? 264 GLU C OE2 1 
ATOM   7025  N  N   . PHE C 1 201 ? 42.093 53.429 107.327 1.00 59.47  ? 265 PHE C N   1 
ATOM   7026  C  CA  . PHE C 1 201 ? 41.576 53.824 106.048 1.00 54.51  ? 265 PHE C CA  1 
ATOM   7027  C  C   . PHE C 1 201 ? 41.731 55.319 105.796 1.00 46.88  ? 265 PHE C C   1 
ATOM   7028  O  O   . PHE C 1 201 ? 40.758 55.997 105.443 1.00 72.98  ? 265 PHE C O   1 
ATOM   7029  C  CB  . PHE C 1 201 ? 40.102 53.393 105.954 1.00 57.69  ? 265 PHE C CB  1 
ATOM   7030  C  CG  . PHE C 1 201 ? 39.858 51.981 106.385 1.00 58.06  ? 265 PHE C CG  1 
ATOM   7031  C  CD1 . PHE C 1 201 ? 40.411 50.914 105.675 1.00 67.08  ? 265 PHE C CD1 1 
ATOM   7032  C  CD2 . PHE C 1 201 ? 39.061 51.711 107.476 1.00 55.87  ? 265 PHE C CD2 1 
ATOM   7033  C  CE1 . PHE C 1 201 ? 40.190 49.586 106.075 1.00 76.40  ? 265 PHE C CE1 1 
ATOM   7034  C  CE2 . PHE C 1 201 ? 38.824 50.382 107.882 1.00 61.23  ? 265 PHE C CE2 1 
ATOM   7035  C  CZ  . PHE C 1 201 ? 39.403 49.323 107.192 1.00 63.62  ? 265 PHE C CZ  1 
ATOM   7036  N  N   . PRO C 1 202 ? 42.936 55.856 105.969 1.00 42.58  ? 266 PRO C N   1 
ATOM   7037  C  CA  . PRO C 1 202 ? 43.117 57.291 105.681 1.00 49.95  ? 266 PRO C CA  1 
ATOM   7038  C  C   . PRO C 1 202 ? 42.886 57.623 104.224 1.00 50.73  ? 266 PRO C C   1 
ATOM   7039  O  O   . PRO C 1 202 ? 43.256 56.871 103.349 1.00 61.44  ? 266 PRO C O   1 
ATOM   7040  C  CB  . PRO C 1 202 ? 44.581 57.545 106.028 1.00 46.82  ? 266 PRO C CB  1 
ATOM   7041  C  CG  . PRO C 1 202 ? 45.200 56.218 105.984 1.00 47.46  ? 266 PRO C CG  1 
ATOM   7042  C  CD  . PRO C 1 202 ? 44.169 55.265 106.471 1.00 43.98  ? 266 PRO C CD  1 
ATOM   7043  N  N   . THR C 1 203 ? 42.246 58.740 103.980 1.00 59.33  ? 267 THR C N   1 
ATOM   7044  C  CA  . THR C 1 203 ? 41.932 59.148 102.639 1.00 63.22  ? 267 THR C CA  1 
ATOM   7045  C  C   . THR C 1 203 ? 42.516 60.561 102.505 1.00 60.71  ? 267 THR C C   1 
ATOM   7046  O  O   . THR C 1 203 ? 42.313 61.425 103.358 1.00 66.40  ? 267 THR C O   1 
ATOM   7047  C  CB  . THR C 1 203 ? 40.420 59.052 102.391 1.00 65.44  ? 267 THR C CB  1 
ATOM   7048  O  OG1 . THR C 1 203 ? 40.149 59.276 101.007 1.00 80.13  ? 267 THR C OG1 1 
ATOM   7049  C  CG2 . THR C 1 203 ? 39.657 60.070 103.237 1.00 71.61  ? 267 THR C CG2 1 
ATOM   7050  N  N   . CYS C 1 204 ? 43.284 60.780 101.453 1.00 58.25  ? 268 CYS C N   1 
ATOM   7051  C  CA  . CYS C 1 204 ? 44.245 61.863 101.459 1.00 53.24  ? 268 CYS C CA  1 
ATOM   7052  C  C   . CYS C 1 204 ? 44.225 62.765 100.249 1.00 48.66  ? 268 CYS C C   1 
ATOM   7053  O  O   . CYS C 1 204 ? 43.802 62.370 99.183  1.00 79.28  ? 268 CYS C O   1 
ATOM   7054  C  CB  . CYS C 1 204 ? 45.623 61.225 101.550 1.00 65.78  ? 268 CYS C CB  1 
ATOM   7055  S  SG  . CYS C 1 204 ? 45.808 60.122 102.925 1.00 91.19  ? 268 CYS C SG  1 
ATOM   7056  N  N   . TYR C 1 205 ? 44.730 63.968 100.391 1.00 49.88  ? 269 TYR C N   1 
ATOM   7057  C  CA  . TYR C 1 205 ? 45.002 64.816 99.230  1.00 54.34  ? 269 TYR C CA  1 
ATOM   7058  C  C   . TYR C 1 205 ? 46.199 65.683 99.500  1.00 63.34  ? 269 TYR C C   1 
ATOM   7059  O  O   . TYR C 1 205 ? 46.755 65.654 100.596 1.00 77.51  ? 269 TYR C O   1 
ATOM   7060  C  CB  . TYR C 1 205 ? 43.795 65.692 98.859  1.00 53.41  ? 269 TYR C CB  1 
ATOM   7061  C  CG  . TYR C 1 205 ? 43.368 66.620 99.921  1.00 52.57  ? 269 TYR C CG  1 
ATOM   7062  C  CD1 . TYR C 1 205 ? 43.620 67.985 99.798  1.00 64.16  ? 269 TYR C CD1 1 
ATOM   7063  C  CD2 . TYR C 1 205 ? 42.728 66.147 101.069 1.00 56.27  ? 269 TYR C CD2 1 
ATOM   7064  C  CE1 . TYR C 1 205 ? 43.243 68.881 100.790 1.00 67.11  ? 269 TYR C CE1 1 
ATOM   7065  C  CE2 . TYR C 1 205 ? 42.350 67.022 102.072 1.00 73.48  ? 269 TYR C CE2 1 
ATOM   7066  C  CZ  . TYR C 1 205 ? 42.615 68.394 101.925 1.00 71.17  ? 269 TYR C CZ  1 
ATOM   7067  O  OH  . TYR C 1 205 ? 42.255 69.279 102.902 1.00 76.31  ? 269 TYR C OH  1 
ATOM   7068  N  N   . TYR C 1 206 ? 46.590 66.473 98.510  1.00 65.99  ? 270 TYR C N   1 
ATOM   7069  C  CA  . TYR C 1 206 ? 47.803 67.257 98.634  1.00 64.36  ? 270 TYR C CA  1 
ATOM   7070  C  C   . TYR C 1 206 ? 47.514 68.685 98.329  1.00 66.91  ? 270 TYR C C   1 
ATOM   7071  O  O   . TYR C 1 206 ? 46.909 68.981 97.306  1.00 70.69  ? 270 TYR C O   1 
ATOM   7072  C  CB  . TYR C 1 206 ? 48.894 66.735 97.691  1.00 60.64  ? 270 TYR C CB  1 
ATOM   7073  C  CG  . TYR C 1 206 ? 50.105 67.620 97.632  1.00 66.11  ? 270 TYR C CG  1 
ATOM   7074  C  CD1 . TYR C 1 206 ? 50.346 68.411 96.525  1.00 83.32  ? 270 TYR C CD1 1 
ATOM   7075  C  CD2 . TYR C 1 206 ? 50.993 67.696 98.694  1.00 81.12  ? 270 TYR C CD2 1 
ATOM   7076  C  CE1 . TYR C 1 206 ? 51.454 69.251 96.454  1.00 84.22  ? 270 TYR C CE1 1 
ATOM   7077  C  CE2 . TYR C 1 206 ? 52.106 68.536 98.640  1.00 95.06  ? 270 TYR C CE2 1 
ATOM   7078  C  CZ  . TYR C 1 206 ? 52.323 69.307 97.508  1.00 87.48  ? 270 TYR C CZ  1 
ATOM   7079  O  OH  . TYR C 1 206 ? 53.407 70.138 97.420  1.00 102.11 ? 270 TYR C OH  1 
ATOM   7080  N  N   . THR C 1 207 ? 47.946 69.566 99.225  1.00 69.41  ? 271 THR C N   1 
ATOM   7081  C  CA  . THR C 1 207 ? 47.916 71.002 98.968  1.00 78.48  ? 271 THR C CA  1 
ATOM   7082  C  C   . THR C 1 207 ? 48.986 71.748 99.762  1.00 76.09  ? 271 THR C C   1 
ATOM   7083  O  O   . THR C 1 207 ? 49.401 71.296 100.833 1.00 85.20  ? 271 THR C O   1 
ATOM   7084  C  CB  . THR C 1 207 ? 46.513 71.604 99.232  1.00 84.84  ? 271 THR C CB  1 
ATOM   7085  O  OG1 . THR C 1 207 ? 46.520 72.990 98.874  1.00 135.28 ? 271 THR C OG1 1 
ATOM   7086  C  CG2 . THR C 1 207 ? 46.122 71.456 100.696 1.00 80.74  ? 271 THR C CG2 1 
ATOM   7087  N  N   . SER C 1 208 ? 49.440 72.878 99.225  1.00 78.33  ? 272 SER C N   1 
ATOM   7088  C  CA  . SER C 1 208 ? 50.295 73.796 99.963  1.00 91.57  ? 272 SER C CA  1 
ATOM   7089  C  C   . SER C 1 208 ? 51.465 73.055 100.642 1.00 82.82  ? 272 SER C C   1 
ATOM   7090  O  O   . SER C 1 208 ? 51.769 73.259 101.824 1.00 83.69  ? 272 SER C O   1 
ATOM   7091  C  CB  . SER C 1 208 ? 49.445 74.582 100.971 1.00 106.18 ? 272 SER C CB  1 
ATOM   7092  O  OG  . SER C 1 208 ? 50.188 75.644 101.539 1.00 148.84 ? 272 SER C OG  1 
ATOM   7093  N  N   . GLY C 1 209 ? 52.100 72.174 99.878  1.00 70.33  ? 273 GLY C N   1 
ATOM   7094  C  CA  . GLY C 1 209 ? 53.259 71.439 100.352 1.00 73.36  ? 273 GLY C CA  1 
ATOM   7095  C  C   . GLY C 1 209 ? 53.009 70.417 101.440 1.00 76.36  ? 273 GLY C C   1 
ATOM   7096  O  O   . GLY C 1 209 ? 53.966 69.936 102.060 1.00 86.93  ? 273 GLY C O   1 
ATOM   7097  N  N   . LYS C 1 210 ? 51.740 70.081 101.680 1.00 66.92  ? 274 LYS C N   1 
ATOM   7098  C  CA  . LYS C 1 210 ? 51.399 69.122 102.724 1.00 71.87  ? 274 LYS C CA  1 
ATOM   7099  C  C   . LYS C 1 210 ? 50.345 68.155 102.304 1.00 76.03  ? 274 LYS C C   1 
ATOM   7100  O  O   . LYS C 1 210 ? 49.433 68.514 101.580 1.00 104.15 ? 274 LYS C O   1 
ATOM   7101  C  CB  . LYS C 1 210 ? 50.974 69.823 104.009 1.00 83.12  ? 274 LYS C CB  1 
ATOM   7102  C  CG  . LYS C 1 210 ? 52.193 70.359 104.785 1.00 123.31 ? 274 LYS C CG  1 
ATOM   7103  C  CD  . LYS C 1 210 ? 51.854 71.113 106.065 1.00 125.46 ? 274 LYS C CD  1 
ATOM   7104  C  CE  . LYS C 1 210 ? 51.354 72.518 105.773 1.00 128.63 ? 274 LYS C CE  1 
ATOM   7105  N  NZ  . LYS C 1 210 ? 51.780 73.477 106.821 1.00 120.33 ? 274 LYS C NZ  1 
ATOM   7106  N  N   . VAL C 1 211 ? 50.485 66.907 102.738 1.00 76.98  ? 275 VAL C N   1 
ATOM   7107  C  CA  . VAL C 1 211 ? 49.477 65.897 102.474 1.00 59.50  ? 275 VAL C CA  1 
ATOM   7108  C  C   . VAL C 1 211 ? 48.589 65.839 103.675 1.00 60.93  ? 275 VAL C C   1 
ATOM   7109  O  O   . VAL C 1 211 ? 49.063 65.855 104.791 1.00 84.27  ? 275 VAL C O   1 
ATOM   7110  C  CB  . VAL C 1 211 ? 50.066 64.529 102.197 1.00 51.24  ? 275 VAL C CB  1 
ATOM   7111  C  CG1 . VAL C 1 211 ? 48.935 63.513 102.163 1.00 47.14  ? 275 VAL C CG1 1 
ATOM   7112  C  CG2 . VAL C 1 211 ? 50.850 64.565 100.868 1.00 46.92  ? 275 VAL C CG2 1 
ATOM   7113  N  N   . LYS C 1 212 ? 47.291 65.771 103.426 1.00 63.30  ? 276 LYS C N   1 
ATOM   7114  C  CA  . LYS C 1 212 ? 46.289 65.887 104.463 1.00 59.71  ? 276 LYS C CA  1 
ATOM   7115  C  C   . LYS C 1 212 ? 45.360 64.709 104.358 1.00 60.18  ? 276 LYS C C   1 
ATOM   7116  O  O   . LYS C 1 212 ? 44.691 64.531 103.349 1.00 69.81  ? 276 LYS C O   1 
ATOM   7117  C  CB  . LYS C 1 212 ? 45.530 67.203 104.315 1.00 61.99  ? 276 LYS C CB  1 
ATOM   7118  C  CG  . LYS C 1 212 ? 46.453 68.394 104.321 1.00 70.82  ? 276 LYS C CG  1 
ATOM   7119  C  CD  . LYS C 1 212 ? 45.715 69.686 104.220 1.00 85.95  ? 276 LYS C CD  1 
ATOM   7120  C  CE  . LYS C 1 212 ? 46.710 70.837 104.302 1.00 111.72 ? 276 LYS C CE  1 
ATOM   7121  N  NZ  . LYS C 1 212 ? 46.020 72.152 104.347 1.00 117.84 ? 276 LYS C NZ  1 
ATOM   7122  N  N   . CYS C 1 213 ? 45.335 63.915 105.421 1.00 66.03  ? 277 CYS C N   1 
ATOM   7123  C  CA  . CYS C 1 213 ? 44.640 62.643 105.466 1.00 62.84  ? 277 CYS C CA  1 
ATOM   7124  C  C   . CYS C 1 213 ? 43.527 62.603 106.509 1.00 57.81  ? 277 CYS C C   1 
ATOM   7125  O  O   . CYS C 1 213 ? 43.730 62.938 107.661 1.00 53.82  ? 277 CYS C O   1 
ATOM   7126  C  CB  . CYS C 1 213 ? 45.662 61.527 105.736 1.00 63.10  ? 277 CYS C CB  1 
ATOM   7127  S  SG  . CYS C 1 213 ? 46.802 61.296 104.334 1.00 110.74 ? 277 CYS C SG  1 
ATOM   7128  N  N   . THR C 1 214 ? 42.352 62.155 106.104 1.00 59.57  ? 278 THR C N   1 
ATOM   7129  C  CA  . THR C 1 214 ? 41.268 61.928 107.043 1.00 62.80  ? 278 THR C CA  1 
ATOM   7130  C  C   . THR C 1 214 ? 41.127 60.443 107.380 1.00 58.70  ? 278 THR C C   1 
ATOM   7131  O  O   . THR C 1 214 ? 40.722 59.644 106.551 1.00 84.49  ? 278 THR C O   1 
ATOM   7132  C  CB  . THR C 1 214 ? 39.958 62.426 106.444 1.00 73.76  ? 278 THR C CB  1 
ATOM   7133  O  OG1 . THR C 1 214 ? 40.112 63.789 106.019 1.00 75.06  ? 278 THR C OG1 1 
ATOM   7134  C  CG2 . THR C 1 214 ? 38.845 62.328 107.462 1.00 77.18  ? 278 THR C CG2 1 
ATOM   7135  N  N   . GLY C 1 215 ? 41.444 60.064 108.601 1.00 59.80  ? 279 GLY C N   1 
ATOM   7136  C  CA  . GLY C 1 215 ? 41.299 58.668 109.003 1.00 58.53  ? 279 GLY C CA  1 
ATOM   7137  C  C   . GLY C 1 215 ? 39.941 58.336 109.594 1.00 65.80  ? 279 GLY C C   1 
ATOM   7138  O  O   . GLY C 1 215 ? 39.005 59.164 109.616 1.00 57.58  ? 279 GLY C O   1 
ATOM   7139  N  N   . THR C 1 216 ? 39.848 57.111 110.097 1.00 66.05  ? 280 THR C N   1 
ATOM   7140  C  CA  . THR C 1 216 ? 38.613 56.602 110.663 1.00 71.03  ? 280 THR C CA  1 
ATOM   7141  C  C   . THR C 1 216 ? 38.966 55.893 111.953 1.00 81.63  ? 280 THR C C   1 
ATOM   7142  O  O   . THR C 1 216 ? 39.789 54.981 111.940 1.00 78.89  ? 280 THR C O   1 
ATOM   7143  C  CB  . THR C 1 216 ? 37.950 55.657 109.676 1.00 63.98  ? 280 THR C CB  1 
ATOM   7144  O  OG1 . THR C 1 216 ? 37.216 56.438 108.719 1.00 83.02  ? 280 THR C OG1 1 
ATOM   7145  C  CG2 . THR C 1 216 ? 37.042 54.665 110.378 1.00 57.01  ? 280 THR C CG2 1 
ATOM   7146  N  N   . ASN C 1 217 ? 38.379 56.346 113.065 1.00 91.09  ? 281 ASN C N   1 
ATOM   7147  C  CA  . ASN C 1 217 ? 38.645 55.767 114.390 1.00 77.91  ? 281 ASN C CA  1 
ATOM   7148  C  C   . ASN C 1 217 ? 37.597 54.715 114.759 1.00 76.91  ? 281 ASN C C   1 
ATOM   7149  O  O   . ASN C 1 217 ? 36.432 55.033 115.073 1.00 70.71  ? 281 ASN C O   1 
ATOM   7150  C  CB  . ASN C 1 217 ? 38.720 56.862 115.459 1.00 83.50  ? 281 ASN C CB  1 
ATOM   7151  C  CG  . ASN C 1 217 ? 39.260 56.357 116.797 1.00 79.21  ? 281 ASN C CG  1 
ATOM   7152  O  OD1 . ASN C 1 217 ? 39.033 55.213 117.181 1.00 84.23  ? 281 ASN C OD1 1 
ATOM   7153  N  ND2 . ASN C 1 217 ? 39.969 57.225 117.515 1.00 70.95  ? 281 ASN C ND2 1 
ATOM   7154  N  N   . LEU C 1 218 ? 38.019 53.459 114.721 1.00 66.00  ? 282 LEU C N   1 
ATOM   7155  C  CA  . LEU C 1 218 ? 37.091 52.364 114.926 1.00 75.26  ? 282 LEU C CA  1 
ATOM   7156  C  C   . LEU C 1 218 ? 37.047 51.964 116.365 1.00 80.66  ? 282 LEU C C   1 
ATOM   7157  O  O   . LEU C 1 218 ? 36.389 50.972 116.714 1.00 92.01  ? 282 LEU C O   1 
ATOM   7158  C  CB  . LEU C 1 218 ? 37.495 51.132 114.130 1.00 83.60  ? 282 LEU C CB  1 
ATOM   7159  C  CG  . LEU C 1 218 ? 37.241 51.146 112.642 1.00 83.57  ? 282 LEU C CG  1 
ATOM   7160  C  CD1 . LEU C 1 218 ? 38.523 51.549 111.983 1.00 91.42  ? 282 LEU C CD1 1 
ATOM   7161  C  CD2 . LEU C 1 218 ? 36.856 49.746 112.218 1.00 99.82  ? 282 LEU C CD2 1 
ATOM   7162  N  N   . TRP C 1 219 ? 37.754 52.723 117.197 1.00 77.13  ? 283 TRP C N   1 
ATOM   7163  C  CA  . TRP C 1 219 ? 37.886 52.405 118.619 1.00 82.35  ? 283 TRP C CA  1 
ATOM   7164  C  C   . TRP C 1 219 ? 37.099 53.309 119.556 1.00 86.00  ? 283 TRP C C   1 
ATOM   7165  O  O   . TRP C 1 219 ? 36.034 52.944 120.043 1.00 81.49  ? 283 TRP C O   1 
ATOM   7166  C  CB  . TRP C 1 219 ? 39.364 52.388 118.969 1.00 76.17  ? 283 TRP C CB  1 
ATOM   7167  C  CG  . TRP C 1 219 ? 39.686 52.137 120.409 1.00 77.76  ? 283 TRP C CG  1 
ATOM   7168  C  CD1 . TRP C 1 219 ? 38.907 51.495 121.354 1.00 87.28  ? 283 TRP C CD1 1 
ATOM   7169  C  CD2 . TRP C 1 219 ? 40.928 52.484 121.103 1.00 84.11  ? 283 TRP C CD2 1 
ATOM   7170  N  NE1 . TRP C 1 219 ? 39.558 51.434 122.553 1.00 101.28 ? 283 TRP C NE1 1 
ATOM   7171  C  CE2 . TRP C 1 219 ? 40.779 52.004 122.470 1.00 92.46  ? 283 TRP C CE2 1 
ATOM   7172  C  CE3 . TRP C 1 219 ? 42.116 53.110 120.734 1.00 91.93  ? 283 TRP C CE3 1 
ATOM   7173  C  CZ2 . TRP C 1 219 ? 41.782 52.165 123.422 1.00 90.87  ? 283 TRP C CZ2 1 
ATOM   7174  C  CZ3 . TRP C 1 219 ? 43.119 53.267 121.699 1.00 90.14  ? 283 TRP C CZ3 1 
ATOM   7175  C  CH2 . TRP C 1 219 ? 42.951 52.806 123.013 1.00 88.15  ? 283 TRP C CH2 1 
ATOM   7176  N  N   . ASN C 1 220 ? 37.611 54.509 119.798 1.00 87.56  ? 284 ASN C N   1 
ATOM   7177  C  CA  . ASN C 1 220 ? 37.119 55.359 120.859 1.00 77.03  ? 284 ASN C CA  1 
ATOM   7178  C  C   . ASN C 1 220 ? 36.643 56.728 120.349 1.00 96.28  ? 284 ASN C C   1 
ATOM   7179  O  O   . ASN C 1 220 ? 36.633 57.699 121.110 1.00 117.66 ? 284 ASN C O   1 
ATOM   7180  C  CB  . ASN C 1 220 ? 38.261 55.554 121.846 1.00 75.48  ? 284 ASN C CB  1 
ATOM   7181  C  CG  . ASN C 1 220 ? 39.547 56.023 121.166 1.00 81.13  ? 284 ASN C CG  1 
ATOM   7182  O  OD1 . ASN C 1 220 ? 39.533 56.493 120.023 1.00 102.16 ? 284 ASN C OD1 1 
ATOM   7183  N  ND2 . ASN C 1 220 ? 40.659 55.897 121.864 1.00 81.19  ? 284 ASN C ND2 1 
ATOM   7184  N  N   . ASP C 1 221 ? 36.250 56.816 119.075 1.00 96.73  ? 285 ASP C N   1 
ATOM   7185  C  CA  . ASP C 1 221 ? 35.949 58.119 118.452 1.00 91.84  ? 285 ASP C CA  1 
ATOM   7186  C  C   . ASP C 1 221 ? 34.892 58.124 117.311 1.00 90.40  ? 285 ASP C C   1 
ATOM   7187  O  O   . ASP C 1 221 ? 34.944 57.317 116.351 1.00 78.02  ? 285 ASP C O   1 
ATOM   7188  C  CB  . ASP C 1 221 ? 37.258 58.757 117.984 1.00 104.68 ? 285 ASP C CB  1 
ATOM   7189  C  CG  . ASP C 1 221 ? 37.118 60.218 117.648 1.00 126.78 ? 285 ASP C CG  1 
ATOM   7190  O  OD1 . ASP C 1 221 ? 36.030 60.794 117.866 1.00 122.99 ? 285 ASP C OD1 1 
ATOM   7191  O  OD2 . ASP C 1 221 ? 38.120 60.793 117.170 1.00 154.67 ? 285 ASP C OD2 1 
ATOM   7192  N  N   . ALA C 1 222 ? 33.945 59.058 117.441 1.00 82.67  ? 286 ALA C N   1 
ATOM   7193  C  CA  . ALA C 1 222 ? 32.865 59.278 116.471 1.00 87.29  ? 286 ALA C CA  1 
ATOM   7194  C  C   . ALA C 1 222 ? 33.149 60.478 115.571 1.00 92.06  ? 286 ALA C C   1 
ATOM   7195  O  O   . ALA C 1 222 ? 32.360 60.803 114.676 1.00 97.02  ? 286 ALA C O   1 
ATOM   7196  C  CB  . ALA C 1 222 ? 31.542 59.472 117.183 1.00 103.68 ? 286 ALA C CB  1 
ATOM   7197  N  N   . LYS C 1 223 ? 34.265 61.147 115.830 1.00 87.32  ? 287 LYS C N   1 
ATOM   7198  C  CA  . LYS C 1 223 ? 34.812 62.115 114.898 1.00 89.19  ? 287 LYS C CA  1 
ATOM   7199  C  C   . LYS C 1 223 ? 35.911 61.427 114.074 1.00 93.50  ? 287 LYS C C   1 
ATOM   7200  O  O   . LYS C 1 223 ? 36.232 60.248 114.290 1.00 86.96  ? 287 LYS C O   1 
ATOM   7201  C  CB  . LYS C 1 223 ? 35.407 63.303 115.643 1.00 85.33  ? 287 LYS C CB  1 
ATOM   7202  C  CG  . LYS C 1 223 ? 34.481 64.058 116.561 1.00 89.87  ? 287 LYS C CG  1 
ATOM   7203  C  CD  . LYS C 1 223 ? 35.219 65.316 117.010 1.00 98.86  ? 287 LYS C CD  1 
ATOM   7204  C  CE  . LYS C 1 223 ? 34.545 66.054 118.144 1.00 105.65 ? 287 LYS C CE  1 
ATOM   7205  N  NZ  . LYS C 1 223 ? 35.144 67.408 118.295 1.00 112.71 ? 287 LYS C NZ  1 
ATOM   7206  N  N   . ARG C 1 224 ? 36.500 62.159 113.135 1.00 95.32  ? 288 ARG C N   1 
ATOM   7207  C  CA  . ARG C 1 224 ? 37.548 61.571 112.325 1.00 81.09  ? 288 ARG C CA  1 
ATOM   7208  C  C   . ARG C 1 224 ? 38.871 62.235 112.637 1.00 79.28  ? 288 ARG C C   1 
ATOM   7209  O  O   . ARG C 1 224 ? 38.993 63.462 112.569 1.00 73.05  ? 288 ARG C O   1 
ATOM   7210  C  CB  . ARG C 1 224 ? 37.226 61.672 110.837 1.00 79.49  ? 288 ARG C CB  1 
ATOM   7211  C  CG  . ARG C 1 224 ? 35.756 61.477 110.508 1.00 81.39  ? 288 ARG C CG  1 
ATOM   7212  C  CD  . ARG C 1 224 ? 35.557 61.144 109.065 1.00 73.55  ? 288 ARG C CD  1 
ATOM   7213  N  NE  . ARG C 1 224 ? 35.458 59.705 108.911 1.00 77.77  ? 288 ARG C NE  1 
ATOM   7214  C  CZ  . ARG C 1 224 ? 34.348 59.087 108.545 1.00 75.13  ? 288 ARG C CZ  1 
ATOM   7215  N  NH1 . ARG C 1 224 ? 33.265 59.796 108.268 1.00 113.16 ? 288 ARG C NH1 1 
ATOM   7216  N  NH2 . ARG C 1 224 ? 34.325 57.775 108.424 1.00 63.65  ? 288 ARG C NH2 1 
ATOM   7217  N  N   . PRO C 1 225 ? 39.867 61.422 113.002 1.00 72.77  ? 289 PRO C N   1 
ATOM   7218  C  CA  . PRO C 1 225 ? 41.230 61.903 113.141 1.00 69.16  ? 289 PRO C CA  1 
ATOM   7219  C  C   . PRO C 1 225 ? 41.700 62.513 111.837 1.00 70.09  ? 289 PRO C C   1 
ATOM   7220  O  O   . PRO C 1 225 ? 41.244 62.107 110.766 1.00 84.92  ? 289 PRO C O   1 
ATOM   7221  C  CB  . PRO C 1 225 ? 42.013 60.629 113.396 1.00 61.68  ? 289 PRO C CB  1 
ATOM   7222  C  CG  . PRO C 1 225 ? 41.016 59.731 114.015 1.00 65.33  ? 289 PRO C CG  1 
ATOM   7223  C  CD  . PRO C 1 225 ? 39.763 59.989 113.288 1.00 66.05  ? 289 PRO C CD  1 
ATOM   7224  N  N   . PHE C 1 226 ? 42.596 63.487 111.929 1.00 61.34  ? 290 PHE C N   1 
ATOM   7225  C  CA  . PHE C 1 226 ? 43.122 64.139 110.760 1.00 55.41  ? 290 PHE C CA  1 
ATOM   7226  C  C   . PHE C 1 226 ? 44.617 64.262 110.863 1.00 59.24  ? 290 PHE C C   1 
ATOM   7227  O  O   . PHE C 1 226 ? 45.138 64.479 111.923 1.00 70.20  ? 290 PHE C O   1 
ATOM   7228  C  CB  . PHE C 1 226 ? 42.512 65.489 110.639 1.00 56.35  ? 290 PHE C CB  1 
ATOM   7229  C  CG  . PHE C 1 226 ? 42.682 66.108 109.302 1.00 62.10  ? 290 PHE C CG  1 
ATOM   7230  C  CD1 . PHE C 1 226 ? 41.714 65.934 108.320 1.00 63.70  ? 290 PHE C CD1 1 
ATOM   7231  C  CD2 . PHE C 1 226 ? 43.792 66.901 109.025 1.00 65.58  ? 290 PHE C CD2 1 
ATOM   7232  C  CE1 . PHE C 1 226 ? 41.853 66.534 107.077 1.00 61.86  ? 290 PHE C CE1 1 
ATOM   7233  C  CE2 . PHE C 1 226 ? 43.935 67.511 107.776 1.00 68.53  ? 290 PHE C CE2 1 
ATOM   7234  C  CZ  . PHE C 1 226 ? 42.966 67.338 106.807 1.00 59.50  ? 290 PHE C CZ  1 
ATOM   7235  N  N   . LEU C 1 227 ? 45.305 64.131 109.742 1.00 63.69  ? 291 LEU C N   1 
ATOM   7236  C  CA  . LEU C 1 227 ? 46.741 64.011 109.734 1.00 53.89  ? 291 LEU C CA  1 
ATOM   7237  C  C   . LEU C 1 227 ? 47.337 64.871 108.672 1.00 64.34  ? 291 LEU C C   1 
ATOM   7238  O  O   . LEU C 1 227 ? 46.878 64.861 107.530 1.00 94.36  ? 291 LEU C O   1 
ATOM   7239  C  CB  . LEU C 1 227 ? 47.103 62.585 109.436 1.00 54.27  ? 291 LEU C CB  1 
ATOM   7240  C  CG  . LEU C 1 227 ? 48.592 62.307 109.257 1.00 60.22  ? 291 LEU C CG  1 
ATOM   7241  C  CD1 . LEU C 1 227 ? 49.362 62.682 110.535 1.00 62.74  ? 291 LEU C CD1 1 
ATOM   7242  C  CD2 . LEU C 1 227 ? 48.831 60.821 108.838 1.00 50.44  ? 291 LEU C CD2 1 
ATOM   7243  N  N   . GLU C 1 228 ? 48.369 65.612 109.048 1.00 72.72  ? 292 GLU C N   1 
ATOM   7244  C  CA  . GLU C 1 228 ? 49.097 66.484 108.130 1.00 73.41  ? 292 GLU C CA  1 
ATOM   7245  C  C   . GLU C 1 228 ? 50.521 65.984 108.132 1.00 66.06  ? 292 GLU C C   1 
ATOM   7246  O  O   . GLU C 1 228 ? 51.021 65.634 109.186 1.00 88.99  ? 292 GLU C O   1 
ATOM   7247  C  CB  . GLU C 1 228 ? 49.040 67.918 108.646 1.00 85.67  ? 292 GLU C CB  1 
ATOM   7248  C  CG  . GLU C 1 228 ? 48.897 68.999 107.585 1.00 124.27 ? 292 GLU C CG  1 
ATOM   7249  C  CD  . GLU C 1 228 ? 49.033 70.406 108.160 1.00 160.60 ? 292 GLU C CD  1 
ATOM   7250  O  OE1 . GLU C 1 228 ? 48.085 71.207 108.017 1.00 177.88 ? 292 GLU C OE1 1 
ATOM   7251  O  OE2 . GLU C 1 228 ? 50.088 70.712 108.761 1.00 180.89 ? 292 GLU C OE2 1 
ATOM   7252  N  N   . PHE C 1 229 ? 51.149 65.879 106.966 1.00 62.16  ? 293 PHE C N   1 
ATOM   7253  C  CA  . PHE C 1 229 ? 52.581 65.585 106.878 1.00 67.60  ? 293 PHE C CA  1 
ATOM   7254  C  C   . PHE C 1 229 ? 53.138 66.142 105.607 1.00 61.59  ? 293 PHE C C   1 
ATOM   7255  O  O   . PHE C 1 229 ? 52.394 66.388 104.699 1.00 62.87  ? 293 PHE C O   1 
ATOM   7256  C  CB  . PHE C 1 229 ? 52.894 64.078 106.997 1.00 70.28  ? 293 PHE C CB  1 
ATOM   7257  C  CG  . PHE C 1 229 ? 52.358 63.231 105.885 1.00 66.34  ? 293 PHE C CG  1 
ATOM   7258  C  CD1 . PHE C 1 229 ? 53.050 63.113 104.677 1.00 70.33  ? 293 PHE C CD1 1 
ATOM   7259  C  CD2 . PHE C 1 229 ? 51.192 62.499 106.059 1.00 69.29  ? 293 PHE C CD2 1 
ATOM   7260  C  CE1 . PHE C 1 229 ? 52.554 62.318 103.611 1.00 62.40  ? 293 PHE C CE1 1 
ATOM   7261  C  CE2 . PHE C 1 229 ? 50.685 61.689 105.016 1.00 68.71  ? 293 PHE C CE2 1 
ATOM   7262  C  CZ  . PHE C 1 229 ? 51.373 61.601 103.786 1.00 60.09  ? 293 PHE C CZ  1 
ATOM   7263  N  N   . ASP C 1 230 ? 54.445 66.315 105.538 1.00 64.28  ? 294 ASP C N   1 
ATOM   7264  C  CA  . ASP C 1 230 ? 55.085 66.839 104.339 1.00 72.39  ? 294 ASP C CA  1 
ATOM   7265  C  C   . ASP C 1 230 ? 56.149 65.877 103.836 1.00 77.32  ? 294 ASP C C   1 
ATOM   7266  O  O   . ASP C 1 230 ? 56.262 64.754 104.355 1.00 86.06  ? 294 ASP C O   1 
ATOM   7267  C  CB  . ASP C 1 230 ? 55.719 68.184 104.634 1.00 87.46  ? 294 ASP C CB  1 
ATOM   7268  C  CG  . ASP C 1 230 ? 56.781 68.108 105.719 1.00 94.61  ? 294 ASP C CG  1 
ATOM   7269  O  OD1 . ASP C 1 230 ? 57.228 66.998 106.099 1.00 105.57 ? 294 ASP C OD1 1 
ATOM   7270  O  OD2 . ASP C 1 230 ? 57.167 69.187 106.196 1.00 105.95 ? 294 ASP C OD2 1 
ATOM   7271  N  N   . GLN C 1 231 ? 56.953 66.318 102.864 1.00 72.02  ? 295 GLN C N   1 
ATOM   7272  C  CA  . GLN C 1 231 ? 57.921 65.407 102.267 1.00 82.23  ? 295 GLN C CA  1 
ATOM   7273  C  C   . GLN C 1 231 ? 58.968 64.885 103.253 1.00 90.03  ? 295 GLN C C   1 
ATOM   7274  O  O   . GLN C 1 231 ? 59.385 63.739 103.141 1.00 104.65 ? 295 GLN C O   1 
ATOM   7275  C  CB  . GLN C 1 231 ? 58.542 65.952 100.975 1.00 87.99  ? 295 GLN C CB  1 
ATOM   7276  C  CG  . GLN C 1 231 ? 59.229 67.313 101.045 1.00 109.17 ? 295 GLN C CG  1 
ATOM   7277  C  CD  . GLN C 1 231 ? 59.737 67.761 99.674  1.00 114.69 ? 295 GLN C CD  1 
ATOM   7278  O  OE1 . GLN C 1 231 ? 59.247 67.302 98.644  1.00 145.31 ? 295 GLN C OE1 1 
ATOM   7279  N  NE2 . GLN C 1 231 ? 60.724 68.649 99.659  1.00 115.34 ? 295 GLN C NE2 1 
ATOM   7280  N  N   . SER C 1 232 ? 59.347 65.696 104.237 1.00 85.50  ? 296 SER C N   1 
ATOM   7281  C  CA  . SER C 1 232 ? 60.334 65.269 105.225 1.00 89.33  ? 296 SER C CA  1 
ATOM   7282  C  C   . SER C 1 232 ? 59.754 64.379 106.349 1.00 88.48  ? 296 SER C C   1 
ATOM   7283  O  O   . SER C 1 232 ? 60.458 64.040 107.305 1.00 103.30 ? 296 SER C O   1 
ATOM   7284  C  CB  . SER C 1 232 ? 61.019 66.496 105.817 1.00 88.87  ? 296 SER C CB  1 
ATOM   7285  O  OG  . SER C 1 232 ? 60.116 67.248 106.610 1.00 89.86  ? 296 SER C OG  1 
ATOM   7286  N  N   . PHE C 1 233 ? 58.479 64.007 106.223 1.00 72.79  ? 297 PHE C N   1 
ATOM   7287  C  CA  . PHE C 1 233 ? 57.757 63.226 107.233 1.00 76.91  ? 297 PHE C CA  1 
ATOM   7288  C  C   . PHE C 1 233 ? 57.517 63.916 108.570 1.00 74.41  ? 297 PHE C C   1 
ATOM   7289  O  O   . PHE C 1 233 ? 57.185 63.244 109.551 1.00 97.63  ? 297 PHE C O   1 
ATOM   7290  C  CB  . PHE C 1 233 ? 58.429 61.866 107.510 1.00 118.25 ? 297 PHE C CB  1 
ATOM   7291  C  CG  . PHE C 1 233 ? 58.222 60.847 106.433 1.00 123.56 ? 297 PHE C CG  1 
ATOM   7292  C  CD1 . PHE C 1 233 ? 57.039 60.826 105.697 1.00 90.66  ? 297 PHE C CD1 1 
ATOM   7293  C  CD2 . PHE C 1 233 ? 59.207 59.895 106.165 1.00 146.60 ? 297 PHE C CD2 1 
ATOM   7294  C  CE1 . PHE C 1 233 ? 56.834 59.892 104.703 1.00 74.66  ? 297 PHE C CE1 1 
ATOM   7295  C  CE2 . PHE C 1 233 ? 59.013 58.959 105.167 1.00 132.54 ? 297 PHE C CE2 1 
ATOM   7296  C  CZ  . PHE C 1 233 ? 57.808 58.958 104.440 1.00 94.30  ? 297 PHE C CZ  1 
ATOM   7297  N  N   . THR C 1 234 ? 57.691 65.229 108.647 1.00 70.11  ? 298 THR C N   1 
ATOM   7298  C  CA  . THR C 1 234 ? 57.267 65.925 109.872 1.00 81.63  ? 298 THR C CA  1 
ATOM   7299  C  C   . THR C 1 234 ? 55.742 66.005 109.808 1.00 84.69  ? 298 THR C C   1 
ATOM   7300  O  O   . THR C 1 234 ? 55.179 66.397 108.791 1.00 104.97 ? 298 THR C O   1 
ATOM   7301  C  CB  . THR C 1 234 ? 57.948 67.316 110.103 1.00 77.65  ? 298 THR C CB  1 
ATOM   7302  O  OG1 . THR C 1 234 ? 57.869 68.099 108.916 1.00 82.35  ? 298 THR C OG1 1 
ATOM   7303  C  CG2 . THR C 1 234 ? 59.414 67.150 110.466 1.00 81.00  ? 298 THR C CG2 1 
ATOM   7304  N  N   . TYR C 1 235 ? 55.083 65.572 110.873 1.00 75.19  ? 299 TYR C N   1 
ATOM   7305  C  CA  . TYR C 1 235 ? 53.659 65.337 110.839 1.00 67.91  ? 299 TYR C CA  1 
ATOM   7306  C  C   . TYR C 1 235 ? 53.019 65.751 112.132 1.00 74.34  ? 299 TYR C C   1 
ATOM   7307  O  O   . TYR C 1 235 ? 53.629 65.621 113.187 1.00 113.93 ? 299 TYR C O   1 
ATOM   7308  C  CB  . TYR C 1 235 ? 53.392 63.851 110.628 1.00 58.75  ? 299 TYR C CB  1 
ATOM   7309  C  CG  . TYR C 1 235 ? 53.578 63.000 111.865 1.00 61.54  ? 299 TYR C CG  1 
ATOM   7310  C  CD1 . TYR C 1 235 ? 54.797 62.393 112.143 1.00 66.75  ? 299 TYR C CD1 1 
ATOM   7311  C  CD2 . TYR C 1 235 ? 52.528 62.780 112.749 1.00 61.63  ? 299 TYR C CD2 1 
ATOM   7312  C  CE1 . TYR C 1 235 ? 54.966 61.583 113.285 1.00 71.91  ? 299 TYR C CE1 1 
ATOM   7313  C  CE2 . TYR C 1 235 ? 52.687 61.977 113.893 1.00 64.17  ? 299 TYR C CE2 1 
ATOM   7314  C  CZ  . TYR C 1 235 ? 53.906 61.379 114.159 1.00 68.79  ? 299 TYR C CZ  1 
ATOM   7315  O  OH  . TYR C 1 235 ? 54.070 60.581 115.291 1.00 65.33  ? 299 TYR C OH  1 
ATOM   7316  N  N   . THR C 1 236 ? 51.779 66.226 112.061 1.00 78.41  ? 300 THR C N   1 
ATOM   7317  C  CA  . THR C 1 236 ? 50.957 66.406 113.266 1.00 87.27  ? 300 THR C CA  1 
ATOM   7318  C  C   . THR C 1 236 ? 49.554 65.804 113.090 1.00 93.48  ? 300 THR C C   1 
ATOM   7319  O  O   . THR C 1 236 ? 48.964 65.901 112.009 1.00 118.76 ? 300 THR C O   1 
ATOM   7320  C  CB  . THR C 1 236 ? 50.784 67.892 113.658 1.00 78.62  ? 300 THR C CB  1 
ATOM   7321  O  OG1 . THR C 1 236 ? 49.865 68.489 112.754 1.00 75.82  ? 300 THR C OG1 1 
ATOM   7322  C  CG2 . THR C 1 236 ? 52.125 68.676 113.651 1.00 94.07  ? 300 THR C CG2 1 
ATOM   7323  N  N   . PHE C 1 237 ? 49.030 65.184 114.149 1.00 79.38  ? 301 PHE C N   1 
ATOM   7324  C  CA  . PHE C 1 237 ? 47.615 64.837 114.203 1.00 71.68  ? 301 PHE C CA  1 
ATOM   7325  C  C   . PHE C 1 237 ? 46.788 66.011 114.724 1.00 77.31  ? 301 PHE C C   1 
ATOM   7326  O  O   . PHE C 1 237 ? 47.185 66.705 115.650 1.00 88.41  ? 301 PHE C O   1 
ATOM   7327  C  CB  . PHE C 1 237 ? 47.389 63.612 115.074 1.00 73.40  ? 301 PHE C CB  1 
ATOM   7328  C  CG  . PHE C 1 237 ? 47.761 62.306 114.406 1.00 77.77  ? 301 PHE C CG  1 
ATOM   7329  C  CD1 . PHE C 1 237 ? 49.031 61.756 114.588 1.00 77.18  ? 301 PHE C CD1 1 
ATOM   7330  C  CD2 . PHE C 1 237 ? 46.839 61.619 113.611 1.00 71.34  ? 301 PHE C CD2 1 
ATOM   7331  C  CE1 . PHE C 1 237 ? 49.395 60.541 113.992 1.00 68.70  ? 301 PHE C CE1 1 
ATOM   7332  C  CE2 . PHE C 1 237 ? 47.192 60.417 113.007 1.00 87.38  ? 301 PHE C CE2 1 
ATOM   7333  C  CZ  . PHE C 1 237 ? 48.480 59.874 113.208 1.00 84.17  ? 301 PHE C CZ  1 
ATOM   7334  N  N   . LYS C 1 238 ? 45.651 66.254 114.097 1.00 83.10  ? 302 LYS C N   1 
ATOM   7335  C  CA  . LYS C 1 238 ? 44.716 67.275 114.541 1.00 81.25  ? 302 LYS C CA  1 
ATOM   7336  C  C   . LYS C 1 238 ? 43.373 66.578 114.720 1.00 79.40  ? 302 LYS C C   1 
ATOM   7337  O  O   . LYS C 1 238 ? 43.053 65.628 114.020 1.00 88.33  ? 302 LYS C O   1 
ATOM   7338  C  CB  . LYS C 1 238 ? 44.594 68.405 113.503 1.00 94.56  ? 302 LYS C CB  1 
ATOM   7339  C  CG  . LYS C 1 238 ? 45.911 69.088 113.085 1.00 98.71  ? 302 LYS C CG  1 
ATOM   7340  C  CD  . LYS C 1 238 ? 45.666 70.157 112.024 1.00 100.75 ? 302 LYS C CD  1 
ATOM   7341  C  CE  . LYS C 1 238 ? 46.628 71.308 112.196 1.00 105.84 ? 302 LYS C CE  1 
ATOM   7342  N  NZ  . LYS C 1 238 ? 45.986 72.576 111.750 1.00 114.05 ? 302 LYS C NZ  1 
ATOM   7343  N  N   . GLU C 1 239 ? 42.587 67.039 115.672 1.00 86.30  ? 303 GLU C N   1 
ATOM   7344  C  CA  . GLU C 1 239 ? 41.239 66.539 115.826 1.00 90.84  ? 303 GLU C CA  1 
ATOM   7345  C  C   . GLU C 1 239 ? 40.290 67.695 115.523 1.00 102.05 ? 303 GLU C C   1 
ATOM   7346  O  O   . GLU C 1 239 ? 40.453 68.792 116.071 1.00 123.01 ? 303 GLU C O   1 
ATOM   7347  C  CB  . GLU C 1 239 ? 41.054 66.030 117.255 1.00 102.16 ? 303 GLU C CB  1 
ATOM   7348  C  CG  . GLU C 1 239 ? 39.625 65.663 117.651 1.00 123.73 ? 303 GLU C CG  1 
ATOM   7349  C  CD  . GLU C 1 239 ? 39.244 64.220 117.337 1.00 128.62 ? 303 GLU C CD  1 
ATOM   7350  O  OE1 . GLU C 1 239 ? 40.115 63.428 116.927 1.00 167.79 ? 303 GLU C OE1 1 
ATOM   7351  O  OE2 . GLU C 1 239 ? 38.060 63.869 117.515 1.00 118.41 ? 303 GLU C OE2 1 
ATOM   7352  N  N   . PRO C 1 240 ? 39.295 67.459 114.656 1.00 84.48  ? 304 PRO C N   1 
ATOM   7353  C  CA  . PRO C 1 240 ? 38.352 68.512 114.296 1.00 90.71  ? 304 PRO C CA  1 
ATOM   7354  C  C   . PRO C 1 240 ? 37.487 68.936 115.487 1.00 100.93 ? 304 PRO C C   1 
ATOM   7355  O  O   . PRO C 1 240 ? 37.000 68.086 116.240 1.00 102.14 ? 304 PRO C O   1 
ATOM   7356  C  CB  . PRO C 1 240 ? 37.499 67.863 113.205 1.00 87.96  ? 304 PRO C CB  1 
ATOM   7357  C  CG  . PRO C 1 240 ? 37.556 66.423 113.492 1.00 92.12  ? 304 PRO C CG  1 
ATOM   7358  C  CD  . PRO C 1 240 ? 38.884 66.145 114.147 1.00 82.49  ? 304 PRO C CD  1 
ATOM   7359  N  N   . CYS C 1 241 ? 37.312 70.246 115.646 1.00 105.66 ? 305 CYS C N   1 
ATOM   7360  C  CA  . CYS C 1 241 ? 36.591 70.816 116.778 1.00 106.25 ? 305 CYS C CA  1 
ATOM   7361  C  C   . CYS C 1 241 ? 35.185 71.245 116.388 1.00 99.72  ? 305 CYS C C   1 
ATOM   7362  O  O   . CYS C 1 241 ? 34.850 72.424 116.498 1.00 111.26 ? 305 CYS C O   1 
ATOM   7363  C  CB  . CYS C 1 241 ? 37.347 72.041 117.284 1.00 134.75 ? 305 CYS C CB  1 
ATOM   7364  S  SG  . CYS C 1 241 ? 39.108 71.768 117.597 1.00 196.47 ? 305 CYS C SG  1 
ATOM   7365  N  N   . LEU C 1 242 ? 34.368 70.305 115.929 1.00 93.52  ? 306 LEU C N   1 
ATOM   7366  C  CA  . LEU C 1 242 ? 33.043 70.643 115.419 1.00 98.38  ? 306 LEU C CA  1 
ATOM   7367  C  C   . LEU C 1 242 ? 32.020 69.572 115.776 1.00 103.14 ? 306 LEU C C   1 
ATOM   7368  O  O   . LEU C 1 242 ? 32.312 68.377 115.701 1.00 101.76 ? 306 LEU C O   1 
ATOM   7369  C  CB  . LEU C 1 242 ? 33.080 70.878 113.900 1.00 94.17  ? 306 LEU C CB  1 
ATOM   7370  C  CG  . LEU C 1 242 ? 33.833 72.110 113.381 1.00 96.88  ? 306 LEU C CG  1 
ATOM   7371  C  CD1 . LEU C 1 242 ? 33.921 72.066 111.861 1.00 122.30 ? 306 LEU C CD1 1 
ATOM   7372  C  CD2 . LEU C 1 242 ? 33.192 73.428 113.851 1.00 104.17 ? 306 LEU C CD2 1 
ATOM   7373  N  N   . GLY C 1 243 ? 30.825 70.018 116.165 1.00 102.73 ? 307 GLY C N   1 
ATOM   7374  C  CA  . GLY C 1 243 ? 29.737 69.136 116.589 1.00 100.35 ? 307 GLY C CA  1 
ATOM   7375  C  C   . GLY C 1 243 ? 29.156 68.256 115.494 1.00 114.79 ? 307 GLY C C   1 
ATOM   7376  O  O   . GLY C 1 243 ? 28.263 67.448 115.758 1.00 140.22 ? 307 GLY C O   1 
ATOM   7377  N  N   . PHE C 1 244 ? 29.658 68.414 114.268 1.00 100.59 ? 308 PHE C N   1 
ATOM   7378  C  CA  . PHE C 1 244 ? 29.280 67.580 113.111 1.00 99.18  ? 308 PHE C CA  1 
ATOM   7379  C  C   . PHE C 1 244 ? 30.114 66.291 113.069 1.00 91.83  ? 308 PHE C C   1 
ATOM   7380  O  O   . PHE C 1 244 ? 31.330 66.288 112.800 1.00 86.74  ? 308 PHE C O   1 
ATOM   7381  C  CB  . PHE C 1 244 ? 29.480 68.378 111.823 1.00 106.77 ? 308 PHE C CB  1 
ATOM   7382  C  CG  . PHE C 1 244 ? 28.581 67.978 110.696 1.00 89.07  ? 308 PHE C CG  1 
ATOM   7383  C  CD1 . PHE C 1 244 ? 27.231 68.303 110.715 1.00 90.70  ? 308 PHE C CD1 1 
ATOM   7384  C  CD2 . PHE C 1 244 ? 29.088 67.331 109.587 1.00 88.28  ? 308 PHE C CD2 1 
ATOM   7385  C  CE1 . PHE C 1 244 ? 26.385 67.963 109.657 1.00 76.74  ? 308 PHE C CE1 1 
ATOM   7386  C  CE2 . PHE C 1 244 ? 28.251 66.995 108.530 1.00 87.02  ? 308 PHE C CE2 1 
ATOM   7387  C  CZ  . PHE C 1 244 ? 26.892 67.315 108.575 1.00 76.83  ? 308 PHE C CZ  1 
ATOM   7388  N  N   . LEU C 1 245 ? 29.449 65.189 113.355 1.00 86.97  ? 309 LEU C N   1 
ATOM   7389  C  CA  . LEU C 1 245 ? 30.146 63.945 113.574 1.00 89.58  ? 309 LEU C CA  1 
ATOM   7390  C  C   . LEU C 1 245 ? 30.283 63.212 112.277 1.00 85.45  ? 309 LEU C C   1 
ATOM   7391  O  O   . LEU C 1 245 ? 29.270 62.838 111.698 1.00 104.29 ? 309 LEU C O   1 
ATOM   7392  C  CB  . LEU C 1 245 ? 29.366 63.087 114.558 1.00 86.81  ? 309 LEU C CB  1 
ATOM   7393  C  CG  . LEU C 1 245 ? 29.299 63.594 115.992 1.00 78.12  ? 309 LEU C CG  1 
ATOM   7394  C  CD1 . LEU C 1 245 ? 29.032 62.412 116.911 1.00 81.63  ? 309 LEU C CD1 1 
ATOM   7395  C  CD2 . LEU C 1 245 ? 30.603 64.302 116.378 1.00 73.45  ? 309 LEU C CD2 1 
ATOM   7396  N  N   . GLY C 1 246 ? 31.524 63.014 111.825 1.00 75.94  ? 310 GLY C N   1 
ATOM   7397  C  CA  . GLY C 1 246 ? 31.787 62.405 110.517 1.00 82.93  ? 310 GLY C CA  1 
ATOM   7398  C  C   . GLY C 1 246 ? 31.508 60.914 110.432 1.00 80.97  ? 310 GLY C C   1 
ATOM   7399  O  O   . GLY C 1 246 ? 30.947 60.431 109.446 1.00 100.29 ? 310 GLY C O   1 
ATOM   7400  N  N   . ASP C 1 247 ? 31.888 60.198 111.487 1.00 78.70  ? 311 ASP C N   1 
ATOM   7401  C  CA  . ASP C 1 247 ? 31.916 58.737 111.504 1.00 75.93  ? 311 ASP C CA  1 
ATOM   7402  C  C   . ASP C 1 247 ? 30.530 58.127 111.527 1.00 80.09  ? 311 ASP C C   1 
ATOM   7403  O  O   . ASP C 1 247 ? 29.527 58.841 111.588 1.00 83.62  ? 311 ASP C O   1 
ATOM   7404  C  CB  . ASP C 1 247 ? 32.698 58.241 112.729 1.00 78.20  ? 311 ASP C CB  1 
ATOM   7405  C  CG  . ASP C 1 247 ? 33.561 57.001 112.440 1.00 74.97  ? 311 ASP C CG  1 
ATOM   7406  O  OD1 . ASP C 1 247 ? 33.215 56.193 111.556 1.00 67.49  ? 311 ASP C OD1 1 
ATOM   7407  O  OD2 . ASP C 1 247 ? 34.602 56.836 113.116 1.00 73.06  ? 311 ASP C OD2 1 
ATOM   7408  N  N   . THR C 1 248 ? 30.497 56.796 111.475 1.00 84.25  ? 312 THR C N   1 
ATOM   7409  C  CA  . THR C 1 248 ? 29.272 56.003 111.469 1.00 84.60  ? 312 THR C CA  1 
ATOM   7410  C  C   . THR C 1 248 ? 29.580 54.583 111.984 1.00 100.14 ? 312 THR C C   1 
ATOM   7411  O  O   . THR C 1 248 ? 30.446 53.910 111.444 1.00 105.00 ? 312 THR C O   1 
ATOM   7412  C  CB  . THR C 1 248 ? 28.643 55.922 110.062 1.00 80.39  ? 312 THR C CB  1 
ATOM   7413  O  OG1 . THR C 1 248 ? 28.338 57.239 109.573 1.00 92.03  ? 312 THR C OG1 1 
ATOM   7414  C  CG2 . THR C 1 248 ? 27.375 55.067 110.080 1.00 82.42  ? 312 THR C CG2 1 
ATOM   7415  N  N   . PRO C 1 249 ? 28.851 54.118 113.016 1.00 114.05 ? 313 PRO C N   1 
ATOM   7416  C  CA  . PRO C 1 249 ? 27.738 54.849 113.601 1.00 119.09 ? 313 PRO C CA  1 
ATOM   7417  C  C   . PRO C 1 249 ? 28.239 55.935 114.530 1.00 100.80 ? 313 PRO C C   1 
ATOM   7418  O  O   . PRO C 1 249 ? 29.454 56.057 114.755 1.00 93.43  ? 313 PRO C O   1 
ATOM   7419  C  CB  . PRO C 1 249 ? 26.991 53.772 114.380 1.00 112.69 ? 313 PRO C CB  1 
ATOM   7420  C  CG  . PRO C 1 249 ? 28.073 52.881 114.841 1.00 97.35  ? 313 PRO C CG  1 
ATOM   7421  C  CD  . PRO C 1 249 ? 29.110 52.864 113.742 1.00 96.25  ? 313 PRO C CD  1 
ATOM   7422  N  N   . ARG C 1 250 ? 27.289 56.717 115.033 1.00 89.66  ? 314 ARG C N   1 
ATOM   7423  C  CA  . ARG C 1 250 ? 27.550 57.865 115.876 1.00 87.93  ? 314 ARG C CA  1 
ATOM   7424  C  C   . ARG C 1 250 ? 26.288 58.166 116.647 1.00 106.11 ? 314 ARG C C   1 
ATOM   7425  O  O   . ARG C 1 250 ? 25.203 57.708 116.283 1.00 124.39 ? 314 ARG C O   1 
ATOM   7426  C  CB  . ARG C 1 250 ? 27.929 59.065 115.028 1.00 86.91  ? 314 ARG C CB  1 
ATOM   7427  C  CG  . ARG C 1 250 ? 27.015 59.301 113.830 1.00 77.57  ? 314 ARG C CG  1 
ATOM   7428  C  CD  . ARG C 1 250 ? 27.374 60.602 113.162 1.00 76.86  ? 314 ARG C CD  1 
ATOM   7429  N  NE  . ARG C 1 250 ? 26.908 60.662 111.791 1.00 71.19  ? 314 ARG C NE  1 
ATOM   7430  C  CZ  . ARG C 1 250 ? 25.700 61.093 111.434 1.00 82.86  ? 314 ARG C CZ  1 
ATOM   7431  N  NH1 . ARG C 1 250 ? 24.813 61.488 112.345 1.00 82.89  ? 314 ARG C NH1 1 
ATOM   7432  N  NH2 . ARG C 1 250 ? 25.370 61.129 110.156 1.00 94.19  ? 314 ARG C NH2 1 
ATOM   7433  N  N   . GLY C 1 251 ? 26.420 58.941 117.711 1.00 112.94 ? 315 GLY C N   1 
ATOM   7434  C  CA  . GLY C 1 251 ? 25.292 59.149 118.599 1.00 127.23 ? 315 GLY C CA  1 
ATOM   7435  C  C   . GLY C 1 251 ? 24.365 60.246 118.133 1.00 126.05 ? 315 GLY C C   1 
ATOM   7436  O  O   . GLY C 1 251 ? 23.220 59.996 117.757 1.00 140.01 ? 315 GLY C O   1 
ATOM   7437  N  N   . ILE C 1 252 ? 24.890 61.466 118.139 1.00 127.21 ? 316 ILE C N   1 
ATOM   7438  C  CA  . ILE C 1 252 ? 24.089 62.674 118.092 1.00 117.48 ? 316 ILE C CA  1 
ATOM   7439  C  C   . ILE C 1 252 ? 25.035 63.843 117.919 1.00 119.17 ? 316 ILE C C   1 
ATOM   7440  O  O   . ILE C 1 252 ? 26.188 63.778 118.332 1.00 144.91 ? 316 ILE C O   1 
ATOM   7441  C  CB  . ILE C 1 252 ? 23.319 62.855 119.422 1.00 110.58 ? 316 ILE C CB  1 
ATOM   7442  C  CG1 . ILE C 1 252 ? 22.025 63.629 119.192 1.00 122.66 ? 316 ILE C CG1 1 
ATOM   7443  C  CG2 . ILE C 1 252 ? 24.214 63.456 120.524 1.00 94.58  ? 316 ILE C CG2 1 
ATOM   7444  C  CD1 . ILE C 1 252 ? 20.915 62.800 118.576 1.00 131.73 ? 316 ILE C CD1 1 
ATOM   7445  N  N   . ASP C 1 253 ? 24.561 64.920 117.321 1.00 117.25 ? 317 ASP C N   1 
ATOM   7446  C  CA  . ASP C 1 253 ? 25.424 66.071 117.156 1.00 120.92 ? 317 ASP C CA  1 
ATOM   7447  C  C   . ASP C 1 253 ? 25.642 66.787 118.474 1.00 127.00 ? 317 ASP C C   1 
ATOM   7448  O  O   . ASP C 1 253 ? 24.767 66.804 119.332 1.00 157.19 ? 317 ASP C O   1 
ATOM   7449  C  CB  . ASP C 1 253 ? 24.881 66.988 116.076 1.00 123.09 ? 317 ASP C CB  1 
ATOM   7450  C  CG  . ASP C 1 253 ? 25.019 66.382 114.702 1.00 126.34 ? 317 ASP C CG  1 
ATOM   7451  O  OD1 . ASP C 1 253 ? 25.981 65.601 114.473 1.00 116.35 ? 317 ASP C OD1 1 
ATOM   7452  O  OD2 . ASP C 1 253 ? 24.158 66.691 113.856 1.00 128.97 ? 317 ASP C OD2 1 
ATOM   7453  N  N   . THR C 1 254 ? 26.827 67.355 118.640 1.00 125.94 ? 318 THR C N   1 
ATOM   7454  C  CA  . THR C 1 254 ? 27.231 67.904 119.928 1.00 135.45 ? 318 THR C CA  1 
ATOM   7455  C  C   . THR C 1 254 ? 27.501 69.396 119.807 1.00 129.50 ? 318 THR C C   1 
ATOM   7456  O  O   . THR C 1 254 ? 27.315 69.974 118.736 1.00 143.29 ? 318 THR C O   1 
ATOM   7457  C  CB  . THR C 1 254 ? 28.516 67.209 120.440 1.00 154.81 ? 318 THR C CB  1 
ATOM   7458  O  OG1 . THR C 1 254 ? 29.549 67.321 119.449 1.00 160.38 ? 318 THR C OG1 1 
ATOM   7459  C  CG2 . THR C 1 254 ? 28.266 65.732 120.744 1.00 139.91 ? 318 THR C CG2 1 
ATOM   7460  N  N   . THR C 1 255 ? 27.928 70.013 120.910 1.00 119.39 ? 319 THR C N   1 
ATOM   7461  C  CA  . THR C 1 255 ? 28.541 71.344 120.871 1.00 123.88 ? 319 THR C CA  1 
ATOM   7462  C  C   . THR C 1 255 ? 29.987 71.189 120.357 1.00 121.51 ? 319 THR C C   1 
ATOM   7463  O  O   . THR C 1 255 ? 30.516 70.075 120.326 1.00 125.97 ? 319 THR C O   1 
ATOM   7464  C  CB  . THR C 1 255 ? 28.559 72.009 122.264 1.00 125.30 ? 319 THR C CB  1 
ATOM   7465  O  OG1 . THR C 1 255 ? 29.287 71.174 123.167 1.00 151.93 ? 319 THR C OG1 1 
ATOM   7466  C  CG2 . THR C 1 255 ? 27.147 72.229 122.803 1.00 112.64 ? 319 THR C CG2 1 
ATOM   7467  N  N   . ASN C 1 256 ? 30.622 72.287 119.949 1.00 111.47 ? 320 ASN C N   1 
ATOM   7468  C  CA  . ASN C 1 256 ? 31.999 72.228 119.451 1.00 110.94 ? 320 ASN C CA  1 
ATOM   7469  C  C   . ASN C 1 256 ? 33.016 72.135 120.581 1.00 114.81 ? 320 ASN C C   1 
ATOM   7470  O  O   . ASN C 1 256 ? 32.964 72.907 121.525 1.00 126.48 ? 320 ASN C O   1 
ATOM   7471  C  CB  . ASN C 1 256 ? 32.338 73.450 118.588 1.00 111.67 ? 320 ASN C CB  1 
ATOM   7472  C  CG  . ASN C 1 256 ? 31.395 73.636 117.414 1.00 116.74 ? 320 ASN C CG  1 
ATOM   7473  O  OD1 . ASN C 1 256 ? 30.404 72.922 117.269 1.00 133.18 ? 320 ASN C OD1 1 
ATOM   7474  N  ND2 . ASN C 1 256 ? 31.703 74.608 116.567 1.00 104.36 ? 320 ASN C ND2 1 
ATOM   7475  N  N   . TYR C 1 257 ? 33.945 71.190 120.481 1.00 136.73 ? 321 TYR C N   1 
ATOM   7476  C  CA  . TYR C 1 257 ? 35.091 71.120 121.396 1.00 124.64 ? 321 TYR C CA  1 
ATOM   7477  C  C   . TYR C 1 257 ? 36.256 70.338 120.765 1.00 143.60 ? 321 TYR C C   1 
ATOM   7478  O  O   . TYR C 1 257 ? 36.045 69.463 119.912 1.00 139.02 ? 321 TYR C O   1 
ATOM   7479  C  CB  . TYR C 1 257 ? 34.692 70.534 122.753 1.00 110.33 ? 321 TYR C CB  1 
ATOM   7480  C  CG  . TYR C 1 257 ? 33.973 69.212 122.675 1.00 110.97 ? 321 TYR C CG  1 
ATOM   7481  C  CD1 . TYR C 1 257 ? 34.684 68.004 122.651 1.00 112.15 ? 321 TYR C CD1 1 
ATOM   7482  C  CD2 . TYR C 1 257 ? 32.583 69.162 122.635 1.00 108.51 ? 321 TYR C CD2 1 
ATOM   7483  C  CE1 . TYR C 1 257 ? 34.023 66.778 122.573 1.00 111.39 ? 321 TYR C CE1 1 
ATOM   7484  C  CE2 . TYR C 1 257 ? 31.912 67.941 122.559 1.00 122.67 ? 321 TYR C CE2 1 
ATOM   7485  C  CZ  . TYR C 1 257 ? 32.642 66.753 122.526 1.00 113.08 ? 321 TYR C CZ  1 
ATOM   7486  O  OH  . TYR C 1 257 ? 31.998 65.540 122.447 1.00 107.88 ? 321 TYR C OH  1 
ATOM   7487  N  N   . CYS C 1 258 ? 37.479 70.664 121.182 1.00 145.76 ? 322 CYS C N   1 
ATOM   7488  C  CA  . CYS C 1 258 ? 38.675 70.137 120.528 1.00 134.65 ? 322 CYS C CA  1 
ATOM   7489  C  C   . CYS C 1 258 ? 39.120 68.800 121.101 1.00 132.79 ? 322 CYS C C   1 
ATOM   7490  O  O   . CYS C 1 258 ? 40.171 68.268 120.734 1.00 124.64 ? 322 CYS C O   1 
ATOM   7491  C  CB  . CYS C 1 258 ? 39.799 71.175 120.525 1.00 155.12 ? 322 CYS C CB  1 
ATOM   7492  S  SG  . CYS C 1 258 ? 39.419 72.589 119.446 1.00 280.91 ? 322 CYS C SG  1 
ATOM   7493  N  N   . ASP C 1 259 ? 38.291 68.245 121.978 1.00 130.46 ? 323 ASP C N   1 
ATOM   7494  C  CA  . ASP C 1 259 ? 38.467 66.875 122.435 1.00 141.85 ? 323 ASP C CA  1 
ATOM   7495  C  C   . ASP C 1 259 ? 37.872 65.846 121.441 1.00 123.25 ? 323 ASP C C   1 
ATOM   7496  O  O   . ASP C 1 259 ? 37.381 66.199 120.361 1.00 119.55 ? 323 ASP C O   1 
ATOM   7497  C  CB  . ASP C 1 259 ? 37.863 66.722 123.830 1.00 150.50 ? 323 ASP C CB  1 
ATOM   7498  C  CG  . ASP C 1 259 ? 38.521 65.622 124.631 1.00 175.66 ? 323 ASP C CG  1 
ATOM   7499  O  OD1 . ASP C 1 259 ? 39.736 65.385 124.463 1.00 183.57 ? 323 ASP C OD1 1 
ATOM   7500  O  OD2 . ASP C 1 259 ? 37.815 64.989 125.436 1.00 229.87 ? 323 ASP C OD2 1 
ATOM   7501  N  N   . LYS C 1 260 ? 37.929 64.573 121.810 1.00 97.08  ? 324 LYS C N   1 
ATOM   7502  C  CA  . LYS C 1 260 ? 37.431 63.503 120.962 1.00 105.92 ? 324 LYS C CA  1 
ATOM   7503  C  C   . LYS C 1 260 ? 36.116 62.941 121.526 1.00 102.55 ? 324 LYS C C   1 
ATOM   7504  O  O   . LYS C 1 260 ? 36.021 62.684 122.722 1.00 117.15 ? 324 LYS C O   1 
ATOM   7505  C  CB  . LYS C 1 260 ? 38.527 62.437 120.835 1.00 109.89 ? 324 LYS C CB  1 
ATOM   7506  C  CG  . LYS C 1 260 ? 38.077 60.980 120.839 1.00 115.24 ? 324 LYS C CG  1 
ATOM   7507  C  CD  . LYS C 1 260 ? 39.153 60.064 121.403 1.00 108.47 ? 324 LYS C CD  1 
ATOM   7508  C  CE  . LYS C 1 260 ? 40.560 60.491 120.982 1.00 105.10 ? 324 LYS C CE  1 
ATOM   7509  N  NZ  . LYS C 1 260 ? 41.591 59.662 121.660 1.00 106.35 ? 324 LYS C NZ  1 
ATOM   7510  N  N   . THR C 1 261 ? 35.114 62.754 120.665 1.00 92.34  ? 325 THR C N   1 
ATOM   7511  C  CA  . THR C 1 261 ? 33.779 62.282 121.079 1.00 92.04  ? 325 THR C CA  1 
ATOM   7512  C  C   . THR C 1 261 ? 33.695 60.769 121.258 1.00 96.96  ? 325 THR C C   1 
ATOM   7513  O  O   . THR C 1 261 ? 33.566 60.025 120.284 1.00 116.35 ? 325 THR C O   1 
ATOM   7514  C  CB  . THR C 1 261 ? 32.709 62.703 120.061 1.00 101.23 ? 325 THR C CB  1 
ATOM   7515  O  OG1 . THR C 1 261 ? 32.693 64.131 119.957 1.00 109.93 ? 325 THR C OG1 1 
ATOM   7516  C  CG2 . THR C 1 261 ? 31.323 62.206 120.477 1.00 91.30  ? 325 THR C CG2 1 
ATOM   7517  N  N   . THR C 1 262 ? 33.730 60.316 122.506 1.00 101.52 ? 326 THR C N   1 
ATOM   7518  C  CA  . THR C 1 262 ? 33.869 58.890 122.797 1.00 99.24  ? 326 THR C CA  1 
ATOM   7519  C  C   . THR C 1 262 ? 32.554 58.114 122.750 1.00 97.36  ? 326 THR C C   1 
ATOM   7520  O  O   . THR C 1 262 ? 32.552 56.890 122.829 1.00 107.55 ? 326 THR C O   1 
ATOM   7521  C  CB  . THR C 1 262 ? 34.495 58.668 124.167 1.00 108.62 ? 326 THR C CB  1 
ATOM   7522  O  OG1 . THR C 1 262 ? 33.476 58.795 125.164 1.00 125.48 ? 326 THR C OG1 1 
ATOM   7523  C  CG2 . THR C 1 262 ? 35.603 59.694 124.434 1.00 119.72 ? 326 THR C CG2 1 
ATOM   7524  N  N   . THR C 1 263 ? 31.440 58.823 122.626 1.00 96.13  ? 327 THR C N   1 
ATOM   7525  C  CA  . THR C 1 263 ? 30.136 58.188 122.682 1.00 89.80  ? 327 THR C CA  1 
ATOM   7526  C  C   . THR C 1 263 ? 29.804 57.591 121.343 1.00 89.74  ? 327 THR C C   1 
ATOM   7527  O  O   . THR C 1 263 ? 29.808 58.293 120.338 1.00 94.44  ? 327 THR C O   1 
ATOM   7528  C  CB  . THR C 1 263 ? 29.063 59.186 123.078 1.00 87.83  ? 327 THR C CB  1 
ATOM   7529  O  OG1 . THR C 1 263 ? 29.591 60.059 124.087 1.00 87.18  ? 327 THR C OG1 1 
ATOM   7530  C  CG2 . THR C 1 263 ? 27.843 58.450 123.616 1.00 93.94  ? 327 THR C CG2 1 
ATOM   7531  N  N   . GLU C 1 264 ? 29.506 56.292 121.345 1.00 102.25 ? 328 GLU C N   1 
ATOM   7532  C  CA  . GLU C 1 264 ? 29.313 55.497 120.121 1.00 103.49 ? 328 GLU C CA  1 
ATOM   7533  C  C   . GLU C 1 264 ? 30.556 55.561 119.224 1.00 99.17  ? 328 GLU C C   1 
ATOM   7534  O  O   . GLU C 1 264 ? 30.473 55.442 117.996 1.00 109.56 ? 328 GLU C O   1 
ATOM   7535  C  CB  . GLU C 1 264 ? 28.035 55.909 119.362 1.00 111.51 ? 328 GLU C CB  1 
ATOM   7536  C  CG  . GLU C 1 264 ? 26.726 55.375 119.951 1.00 129.58 ? 328 GLU C CG  1 
ATOM   7537  C  CD  . GLU C 1 264 ? 25.774 54.861 118.873 1.00 157.22 ? 328 GLU C CD  1 
ATOM   7538  O  OE1 . GLU C 1 264 ? 26.109 53.854 118.209 1.00 200.62 ? 328 GLU C OE1 1 
ATOM   7539  O  OE2 . GLU C 1 264 ? 24.691 55.453 118.688 1.00 149.51 ? 328 GLU C OE2 1 
ATOM   7540  N  N   . GLY C 1 265 ? 31.712 55.742 119.856 1.00 99.68  ? 329 GLY C N   1 
ATOM   7541  C  CA  . GLY C 1 265 ? 32.970 55.903 119.139 1.00 109.01 ? 329 GLY C CA  1 
ATOM   7542  C  C   . GLY C 1 265 ? 33.426 54.641 118.437 1.00 109.32 ? 329 GLY C C   1 
ATOM   7543  O  O   . GLY C 1 265 ? 34.221 54.690 117.490 1.00 132.30 ? 329 GLY C O   1 
ATOM   7544  N  N   . GLU C 1 266 ? 32.907 53.508 118.885 1.00 87.23  ? 330 GLU C N   1 
ATOM   7545  C  CA  . GLU C 1 266 ? 33.331 52.236 118.352 1.00 90.43  ? 330 GLU C CA  1 
ATOM   7546  C  C   . GLU C 1 266 ? 32.572 51.809 117.109 1.00 91.46  ? 330 GLU C C   1 
ATOM   7547  O  O   . GLU C 1 266 ? 31.373 52.053 116.974 1.00 99.74  ? 330 GLU C O   1 
ATOM   7548  C  CB  . GLU C 1 266 ? 33.216 51.158 119.407 1.00 109.96 ? 330 GLU C CB  1 
ATOM   7549  C  CG  . GLU C 1 266 ? 33.849 49.859 118.977 1.00 133.72 ? 330 GLU C CG  1 
ATOM   7550  C  CD  . GLU C 1 266 ? 34.078 48.910 120.124 1.00 171.16 ? 330 GLU C CD  1 
ATOM   7551  O  OE1 . GLU C 1 266 ? 33.715 49.247 121.275 1.00 173.41 ? 330 GLU C OE1 1 
ATOM   7552  O  OE2 . GLU C 1 266 ? 34.630 47.820 119.868 1.00 197.17 ? 330 GLU C OE2 1 
ATOM   7553  N  N   . GLY C 1 267 ? 33.288 51.114 116.233 1.00 92.06  ? 331 GLY C N   1 
ATOM   7554  C  CA  . GLY C 1 267 ? 32.831 50.850 114.886 1.00 101.29 ? 331 GLY C CA  1 
ATOM   7555  C  C   . GLY C 1 267 ? 33.253 52.032 114.040 1.00 111.42 ? 331 GLY C C   1 
ATOM   7556  O  O   . GLY C 1 267 ? 33.767 53.042 114.554 1.00 115.21 ? 331 GLY C O   1 
ATOM   7557  N  N   . GLY C 1 268 ? 33.041 51.911 112.739 1.00 95.11  ? 332 GLY C N   1 
ATOM   7558  C  CA  . GLY C 1 268 ? 33.433 52.969 111.828 1.00 87.43  ? 332 GLY C CA  1 
ATOM   7559  C  C   . GLY C 1 268 ? 33.474 52.520 110.386 1.00 75.39  ? 332 GLY C C   1 
ATOM   7560  O  O   . GLY C 1 268 ? 33.438 51.334 110.083 1.00 73.58  ? 332 GLY C O   1 
ATOM   7561  N  N   . ILE C 1 269 ? 33.533 53.493 109.493 1.00 75.20  ? 333 ILE C N   1 
ATOM   7562  C  CA  . ILE C 1 269 ? 33.609 53.235 108.075 1.00 79.15  ? 333 ILE C CA  1 
ATOM   7563  C  C   . ILE C 1 269 ? 34.370 54.379 107.407 1.00 72.22  ? 333 ILE C C   1 
ATOM   7564  O  O   . ILE C 1 269 ? 34.252 55.532 107.799 1.00 81.15  ? 333 ILE C O   1 
ATOM   7565  C  CB  . ILE C 1 269 ? 32.195 53.056 107.452 1.00 81.55  ? 333 ILE C CB  1 
ATOM   7566  C  CG1 . ILE C 1 269 ? 32.310 52.333 106.101 1.00 80.78  ? 333 ILE C CG1 1 
ATOM   7567  C  CG2 . ILE C 1 269 ? 31.423 54.407 107.412 1.00 64.29  ? 333 ILE C CG2 1 
ATOM   7568  C  CD1 . ILE C 1 269 ? 31.000 51.760 105.580 1.00 101.35 ? 333 ILE C CD1 1 
ATOM   7569  N  N   . GLN C 1 270 ? 35.145 54.048 106.391 1.00 63.85  ? 334 GLN C N   1 
ATOM   7570  C  CA  . GLN C 1 270 ? 35.992 55.001 105.714 1.00 62.25  ? 334 GLN C CA  1 
ATOM   7571  C  C   . GLN C 1 270 ? 35.238 56.199 105.198 1.00 64.27  ? 334 GLN C C   1 
ATOM   7572  O  O   . GLN C 1 270 ? 34.202 56.056 104.542 1.00 78.47  ? 334 GLN C O   1 
ATOM   7573  C  CB  . GLN C 1 270 ? 36.661 54.302 104.547 1.00 62.87  ? 334 GLN C CB  1 
ATOM   7574  C  CG  . GLN C 1 270 ? 37.692 55.139 103.859 1.00 65.73  ? 334 GLN C CG  1 
ATOM   7575  C  CD  . GLN C 1 270 ? 38.354 54.361 102.776 1.00 68.66  ? 334 GLN C CD  1 
ATOM   7576  O  OE1 . GLN C 1 270 ? 37.813 53.344 102.315 1.00 64.11  ? 334 GLN C OE1 1 
ATOM   7577  N  NE2 . GLN C 1 270 ? 39.532 54.824 102.344 1.00 68.88  ? 334 GLN C NE2 1 
ATOM   7578  N  N   . GLY C 1 271 ? 35.780 57.379 105.476 1.00 73.14  ? 335 GLY C N   1 
ATOM   7579  C  CA  . GLY C 1 271 ? 35.169 58.645 105.037 1.00 73.01  ? 335 GLY C CA  1 
ATOM   7580  C  C   . GLY C 1 271 ? 36.145 59.802 105.101 1.00 61.10  ? 335 GLY C C   1 
ATOM   7581  O  O   . GLY C 1 271 ? 37.232 59.662 105.650 1.00 73.96  ? 335 GLY C O   1 
ATOM   7582  N  N   . PHE C 1 272 ? 35.755 60.949 104.560 1.00 62.01  ? 336 PHE C N   1 
ATOM   7583  C  CA  . PHE C 1 272 ? 36.672 62.084 104.461 1.00 63.91  ? 336 PHE C CA  1 
ATOM   7584  C  C   . PHE C 1 272 ? 36.219 63.388 105.147 1.00 71.77  ? 336 PHE C C   1 
ATOM   7585  O  O   . PHE C 1 272 ? 35.112 63.490 105.727 1.00 67.08  ? 336 PHE C O   1 
ATOM   7586  C  CB  . PHE C 1 272 ? 36.988 62.358 102.997 1.00 62.94  ? 336 PHE C CB  1 
ATOM   7587  C  CG  . PHE C 1 272 ? 35.789 62.686 102.199 1.00 70.33  ? 336 PHE C CG  1 
ATOM   7588  C  CD1 . PHE C 1 272 ? 35.489 64.018 101.905 1.00 72.26  ? 336 PHE C CD1 1 
ATOM   7589  C  CD2 . PHE C 1 272 ? 34.923 61.675 101.787 1.00 64.34  ? 336 PHE C CD2 1 
ATOM   7590  C  CE1 . PHE C 1 272 ? 34.367 64.338 101.186 1.00 69.37  ? 336 PHE C CE1 1 
ATOM   7591  C  CE2 . PHE C 1 272 ? 33.801 61.981 101.080 1.00 71.29  ? 336 PHE C CE2 1 
ATOM   7592  C  CZ  . PHE C 1 272 ? 33.517 63.319 100.766 1.00 71.22  ? 336 PHE C CZ  1 
ATOM   7593  N  N   . MET C 1 273 ? 37.145 64.348 105.106 1.00 76.52  ? 337 MET C N   1 
ATOM   7594  C  CA  . MET C 1 273 ? 36.947 65.748 105.463 1.00 69.03  ? 337 MET C CA  1 
ATOM   7595  C  C   . MET C 1 273 ? 37.937 66.505 104.607 1.00 69.23  ? 337 MET C C   1 
ATOM   7596  O  O   . MET C 1 273 ? 39.013 66.009 104.275 1.00 84.21  ? 337 MET C O   1 
ATOM   7597  C  CB  . MET C 1 273 ? 37.283 66.028 106.927 1.00 61.84  ? 337 MET C CB  1 
ATOM   7598  C  CG  . MET C 1 273 ? 36.355 65.403 107.931 1.00 71.47  ? 337 MET C CG  1 
ATOM   7599  S  SD  . MET C 1 273 ? 36.710 65.785 109.677 1.00 85.06  ? 337 MET C SD  1 
ATOM   7600  C  CE  . MET C 1 273 ? 38.430 65.291 109.806 1.00 89.31  ? 337 MET C CE  1 
ATOM   7601  N  N   . ILE C 1 274 ? 37.569 67.714 104.254 1.00 74.60  ? 338 ILE C N   1 
ATOM   7602  C  CA  . ILE C 1 274 ? 38.408 68.560 103.443 1.00 76.72  ? 338 ILE C CA  1 
ATOM   7603  C  C   . ILE C 1 274 ? 38.718 69.834 104.234 1.00 81.97  ? 338 ILE C C   1 
ATOM   7604  O  O   . ILE C 1 274 ? 37.813 70.494 104.746 1.00 79.83  ? 338 ILE C O   1 
ATOM   7605  C  CB  . ILE C 1 274 ? 37.686 68.920 102.136 1.00 72.22  ? 338 ILE C CB  1 
ATOM   7606  C  CG1 . ILE C 1 274 ? 37.101 67.666 101.500 1.00 66.83  ? 338 ILE C CG1 1 
ATOM   7607  C  CG2 . ILE C 1 274 ? 38.628 69.556 101.166 1.00 78.58  ? 338 ILE C CG2 1 
ATOM   7608  C  CD1 . ILE C 1 274 ? 36.680 67.881 100.090 1.00 62.46  ? 338 ILE C CD1 1 
ATOM   7609  N  N   . GLU C 1 275 ? 40.000 70.161 104.331 1.00 79.30  ? 339 GLU C N   1 
ATOM   7610  C  CA  . GLU C 1 275 ? 40.453 71.377 104.972 1.00 86.02  ? 339 GLU C CA  1 
ATOM   7611  C  C   . GLU C 1 275 ? 40.873 72.365 103.889 1.00 97.79  ? 339 GLU C C   1 
ATOM   7612  O  O   . GLU C 1 275 ? 41.624 72.017 102.985 1.00 105.53 ? 339 GLU C O   1 
ATOM   7613  C  CB  . GLU C 1 275 ? 41.605 71.051 105.931 1.00 95.98  ? 339 GLU C CB  1 
ATOM   7614  C  CG  . GLU C 1 275 ? 42.418 72.245 106.432 1.00 132.29 ? 339 GLU C CG  1 
ATOM   7615  C  CD  . GLU C 1 275 ? 41.694 73.135 107.456 1.00 163.72 ? 339 GLU C CD  1 
ATOM   7616  O  OE1 . GLU C 1 275 ? 40.647 72.729 108.008 1.00 174.67 ? 339 GLU C OE1 1 
ATOM   7617  O  OE2 . GLU C 1 275 ? 42.198 74.255 107.718 1.00 148.12 ? 339 GLU C OE2 1 
ATOM   7618  N  N   . GLY C 1 276 ? 40.362 73.590 103.961 1.00 113.13 ? 340 GLY C N   1 
ATOM   7619  C  CA  . GLY C 1 276 ? 40.740 74.631 102.999 1.00 117.33 ? 340 GLY C CA  1 
ATOM   7620  C  C   . GLY C 1 276 ? 40.259 76.005 103.416 1.00 109.23 ? 340 GLY C C   1 
ATOM   7621  O  O   . GLY C 1 276 ? 39.979 76.237 104.590 1.00 107.55 ? 340 GLY C O   1 
ATOM   7622  N  N   . SER C 1 277 ? 40.180 76.919 102.453 1.00 119.07 ? 341 SER C N   1 
ATOM   7623  C  CA  . SER C 1 277 ? 39.533 78.214 102.663 1.00 137.32 ? 341 SER C CA  1 
ATOM   7624  C  C   . SER C 1 277 ? 38.114 77.938 103.144 1.00 139.54 ? 341 SER C C   1 
ATOM   7625  O  O   . SER C 1 277 ? 37.735 78.310 104.265 1.00 125.45 ? 341 SER C O   1 
ATOM   7626  C  CB  . SER C 1 277 ? 39.498 79.017 101.359 1.00 162.19 ? 341 SER C CB  1 
ATOM   7627  O  OG  . SER C 1 277 ? 40.790 79.455 100.984 1.00 180.56 ? 341 SER C OG  1 
ATOM   7628  N  N   . ASN C 1 278 ? 37.344 77.292 102.267 1.00 126.22 ? 342 ASN C N   1 
ATOM   7629  C  CA  . ASN C 1 278 ? 36.144 76.569 102.649 1.00 107.22 ? 342 ASN C CA  1 
ATOM   7630  C  C   . ASN C 1 278 ? 36.577 75.191 103.152 1.00 94.71  ? 342 ASN C C   1 
ATOM   7631  O  O   . ASN C 1 278 ? 37.566 74.644 102.680 1.00 101.35 ? 342 ASN C O   1 
ATOM   7632  C  CB  . ASN C 1 278 ? 35.213 76.403 101.443 1.00 111.51 ? 342 ASN C CB  1 
ATOM   7633  C  CG  . ASN C 1 278 ? 34.538 77.702 101.023 1.00 102.44 ? 342 ASN C CG  1 
ATOM   7634  O  OD1 . ASN C 1 278 ? 33.947 78.409 101.837 1.00 110.80 ? 342 ASN C OD1 1 
ATOM   7635  N  ND2 . ASN C 1 278 ? 34.598 78.000 99.735  1.00 109.27 ? 342 ASN C ND2 1 
ATOM   7636  N  N   . SER C 1 279 ? 35.855 74.634 104.114 1.00 89.30  ? 343 SER C N   1 
ATOM   7637  C  CA  . SER C 1 279 ? 36.116 73.270 104.557 1.00 82.79  ? 343 SER C CA  1 
ATOM   7638  C  C   . SER C 1 279 ? 34.861 72.417 104.453 1.00 91.81  ? 343 SER C C   1 
ATOM   7639  O  O   . SER C 1 279 ? 33.741 72.938 104.544 1.00 88.93  ? 343 SER C O   1 
ATOM   7640  C  CB  . SER C 1 279 ? 36.665 73.264 105.971 1.00 93.11  ? 343 SER C CB  1 
ATOM   7641  O  OG  . SER C 1 279 ? 37.972 73.818 105.977 1.00 115.90 ? 343 SER C OG  1 
ATOM   7642  N  N   . TRP C 1 280 ? 35.050 71.110 104.234 1.00 87.07  ? 344 TRP C N   1 
ATOM   7643  C  CA  . TRP C 1 280 ? 33.920 70.188 104.039 1.00 65.24  ? 344 TRP C CA  1 
ATOM   7644  C  C   . TRP C 1 280 ? 33.949 68.988 104.918 1.00 69.02  ? 344 TRP C C   1 
ATOM   7645  O  O   . TRP C 1 280 ? 34.996 68.404 105.148 1.00 66.80  ? 344 TRP C O   1 
ATOM   7646  C  CB  . TRP C 1 280 ? 33.848 69.717 102.619 1.00 52.21  ? 344 TRP C CB  1 
ATOM   7647  C  CG  . TRP C 1 280 ? 33.696 70.834 101.643 1.00 56.34  ? 344 TRP C CG  1 
ATOM   7648  C  CD1 . TRP C 1 280 ? 34.709 71.618 101.086 1.00 58.17  ? 344 TRP C CD1 1 
ATOM   7649  C  CD2 . TRP C 1 280 ? 32.445 71.331 101.045 1.00 56.26  ? 344 TRP C CD2 1 
ATOM   7650  N  NE1 . TRP C 1 280 ? 34.191 72.543 100.213 1.00 59.59  ? 344 TRP C NE1 1 
ATOM   7651  C  CE2 . TRP C 1 280 ? 32.833 72.429 100.140 1.00 60.54  ? 344 TRP C CE2 1 
ATOM   7652  C  CE3 . TRP C 1 280 ? 31.104 71.013 101.180 1.00 53.74  ? 344 TRP C CE3 1 
ATOM   7653  C  CZ2 . TRP C 1 280 ? 31.887 73.165 99.421  1.00 56.31  ? 344 TRP C CZ2 1 
ATOM   7654  C  CZ3 . TRP C 1 280 ? 30.171 71.753 100.449 1.00 56.57  ? 344 TRP C CZ3 1 
ATOM   7655  C  CH2 . TRP C 1 280 ? 30.556 72.804 99.595  1.00 57.54  ? 344 TRP C CH2 1 
ATOM   7656  N  N   . ILE C 1 281 ? 32.782 68.603 105.422 1.00 78.16  ? 345 ILE C N   1 
ATOM   7657  C  CA  . ILE C 1 281 ? 32.625 67.283 106.020 1.00 73.59  ? 345 ILE C CA  1 
ATOM   7658  C  C   . ILE C 1 281 ? 31.492 66.562 105.329 1.00 75.37  ? 345 ILE C C   1 
ATOM   7659  O  O   . ILE C 1 281 ? 30.378 67.086 105.217 1.00 82.55  ? 345 ILE C O   1 
ATOM   7660  C  CB  . ILE C 1 281 ? 32.304 67.341 107.498 1.00 78.67  ? 345 ILE C CB  1 
ATOM   7661  C  CG1 . ILE C 1 281 ? 33.491 67.923 108.264 1.00 78.57  ? 345 ILE C CG1 1 
ATOM   7662  C  CG2 . ILE C 1 281 ? 31.954 65.933 107.997 1.00 71.32  ? 345 ILE C CG2 1 
ATOM   7663  C  CD1 . ILE C 1 281 ? 33.212 68.206 109.721 1.00 75.93  ? 345 ILE C CD1 1 
ATOM   7664  N  N   . GLY C 1 282 ? 31.797 65.365 104.845 1.00 66.92  ? 346 GLY C N   1 
ATOM   7665  C  CA  . GLY C 1 282 ? 30.796 64.501 104.254 1.00 64.18  ? 346 GLY C CA  1 
ATOM   7666  C  C   . GLY C 1 282 ? 30.472 63.416 105.253 1.00 59.27  ? 346 GLY C C   1 
ATOM   7667  O  O   . GLY C 1 282 ? 31.344 63.007 106.018 1.00 65.69  ? 346 GLY C O   1 
ATOM   7668  N  N   . ARG C 1 283 ? 29.229 62.947 105.246 1.00 57.66  ? 347 ARG C N   1 
ATOM   7669  C  CA  . ARG C 1 283 ? 28.821 61.857 106.119 1.00 64.36  ? 347 ARG C CA  1 
ATOM   7670  C  C   . ARG C 1 283 ? 27.530 61.149 105.710 1.00 77.89  ? 347 ARG C C   1 
ATOM   7671  O  O   . ARG C 1 283 ? 26.698 61.696 104.950 1.00 83.39  ? 347 ARG C O   1 
ATOM   7672  C  CB  . ARG C 1 283 ? 28.669 62.369 107.537 1.00 65.67  ? 347 ARG C CB  1 
ATOM   7673  C  CG  . ARG C 1 283 ? 27.349 62.998 107.816 1.00 78.01  ? 347 ARG C CG  1 
ATOM   7674  C  CD  . ARG C 1 283 ? 27.434 63.752 109.098 1.00 84.01  ? 347 ARG C CD  1 
ATOM   7675  N  NE  . ARG C 1 283 ? 26.126 64.121 109.603 1.00 84.17  ? 347 ARG C NE  1 
ATOM   7676  C  CZ  . ARG C 1 283 ? 25.926 64.600 110.817 1.00 92.49  ? 347 ARG C CZ  1 
ATOM   7677  N  NH1 . ARG C 1 283 ? 26.948 64.772 111.653 1.00 88.59  ? 347 ARG C NH1 1 
ATOM   7678  N  NH2 . ARG C 1 283 ? 24.698 64.895 111.193 1.00 115.44 ? 347 ARG C NH2 1 
ATOM   7679  N  N   . ILE C 1 284 ? 27.362 59.933 106.238 1.00 74.05  ? 348 ILE C N   1 
ATOM   7680  C  CA  . ILE C 1 284 ? 26.151 59.169 105.991 1.00 68.60  ? 348 ILE C CA  1 
ATOM   7681  C  C   . ILE C 1 284 ? 25.053 59.800 106.792 1.00 75.05  ? 348 ILE C C   1 
ATOM   7682  O  O   . ILE C 1 284 ? 25.242 60.064 107.963 1.00 82.64  ? 348 ILE C O   1 
ATOM   7683  C  CB  . ILE C 1 284 ? 26.316 57.724 106.382 1.00 64.37  ? 348 ILE C CB  1 
ATOM   7684  C  CG1 . ILE C 1 284 ? 27.543 57.187 105.639 1.00 76.92  ? 348 ILE C CG1 1 
ATOM   7685  C  CG2 . ILE C 1 284 ? 25.040 56.937 106.057 1.00 60.87  ? 348 ILE C CG2 1 
ATOM   7686  C  CD1 . ILE C 1 284 ? 27.654 55.680 105.512 1.00 71.56  ? 348 ILE C CD1 1 
ATOM   7687  N  N   . ILE C 1 285 ? 23.912 60.048 106.149 1.00 77.24  ? 349 ILE C N   1 
ATOM   7688  C  CA  . ILE C 1 285 ? 22.810 60.775 106.772 1.00 67.75  ? 349 ILE C CA  1 
ATOM   7689  C  C   . ILE C 1 285 ? 22.151 60.016 107.908 1.00 73.21  ? 349 ILE C C   1 
ATOM   7690  O  O   . ILE C 1 285 ? 22.056 60.540 109.006 1.00 90.21  ? 349 ILE C O   1 
ATOM   7691  C  CB  . ILE C 1 285 ? 21.747 61.208 105.746 1.00 67.51  ? 349 ILE C CB  1 
ATOM   7692  C  CG1 . ILE C 1 285 ? 22.380 62.129 104.696 1.00 70.82  ? 349 ILE C CG1 1 
ATOM   7693  C  CG2 . ILE C 1 285 ? 20.619 61.923 106.444 1.00 63.85  ? 349 ILE C CG2 1 
ATOM   7694  C  CD1 . ILE C 1 285 ? 21.419 62.719 103.683 1.00 58.81  ? 349 ILE C CD1 1 
ATOM   7695  N  N   . ASN C 1 286 ? 21.701 58.791 107.648 1.00 83.90  ? 350 ASN C N   1 
ATOM   7696  C  CA  . ASN C 1 286 ? 20.953 58.006 108.639 1.00 91.66  ? 350 ASN C CA  1 
ATOM   7697  C  C   . ASN C 1 286 ? 21.734 56.794 109.093 1.00 91.13  ? 350 ASN C C   1 
ATOM   7698  O  O   . ASN C 1 286 ? 21.571 55.713 108.535 1.00 100.92 ? 350 ASN C O   1 
ATOM   7699  C  CB  . ASN C 1 286 ? 19.598 57.565 108.077 1.00 99.70  ? 350 ASN C CB  1 
ATOM   7700  C  CG  . ASN C 1 286 ? 18.678 58.727 107.811 1.00 105.56 ? 350 ASN C CG  1 
ATOM   7701  O  OD1 . ASN C 1 286 ? 18.720 59.340 106.744 1.00 106.60 ? 350 ASN C OD1 1 
ATOM   7702  N  ND2 . ASN C 1 286 ? 17.834 59.040 108.786 1.00 126.73 ? 350 ASN C ND2 1 
ATOM   7703  N  N   . PRO C 1 287 ? 22.577 56.962 110.124 1.00 92.46  ? 351 PRO C N   1 
ATOM   7704  C  CA  . PRO C 1 287 ? 23.541 55.942 110.544 1.00 89.73  ? 351 PRO C CA  1 
ATOM   7705  C  C   . PRO C 1 287 ? 22.901 54.599 110.883 1.00 94.24  ? 351 PRO C C   1 
ATOM   7706  O  O   . PRO C 1 287 ? 23.593 53.589 110.845 1.00 92.06  ? 351 PRO C O   1 
ATOM   7707  C  CB  . PRO C 1 287 ? 24.165 56.549 111.804 1.00 81.16  ? 351 PRO C CB  1 
ATOM   7708  C  CG  . PRO C 1 287 ? 23.901 57.987 111.682 1.00 79.92  ? 351 PRO C CG  1 
ATOM   7709  C  CD  . PRO C 1 287 ? 22.547 58.076 111.078 1.00 82.67  ? 351 PRO C CD  1 
ATOM   7710  N  N   . GLY C 1 288 ? 21.608 54.594 111.220 1.00 116.67 ? 352 GLY C N   1 
ATOM   7711  C  CA  . GLY C 1 288 ? 20.860 53.349 111.419 1.00 121.72 ? 352 GLY C CA  1 
ATOM   7712  C  C   . GLY C 1 288 ? 20.714 52.550 110.127 1.00 126.04 ? 352 GLY C C   1 
ATOM   7713  O  O   . GLY C 1 288 ? 21.272 51.447 109.982 1.00 110.03 ? 352 GLY C O   1 
ATOM   7714  N  N   . SER C 1 289 ? 19.973 53.121 109.180 1.00 111.04 ? 353 SER C N   1 
ATOM   7715  C  CA  . SER C 1 289 ? 19.684 52.455 107.915 1.00 102.92 ? 353 SER C CA  1 
ATOM   7716  C  C   . SER C 1 289 ? 20.812 52.565 106.886 1.00 90.53  ? 353 SER C C   1 
ATOM   7717  O  O   . SER C 1 289 ? 20.762 51.914 105.843 1.00 85.56  ? 353 SER C O   1 
ATOM   7718  C  CB  . SER C 1 289 ? 18.350 52.958 107.331 1.00 111.49 ? 353 SER C CB  1 
ATOM   7719  O  OG  . SER C 1 289 ? 18.157 54.348 107.542 1.00 109.99 ? 353 SER C OG  1 
ATOM   7720  N  N   . LYS C 1 290 ? 21.814 53.395 107.188 1.00 88.37  ? 354 LYS C N   1 
ATOM   7721  C  CA  . LYS C 1 290 ? 22.925 53.692 106.275 1.00 83.43  ? 354 LYS C CA  1 
ATOM   7722  C  C   . LYS C 1 290 ? 22.467 54.417 104.987 1.00 85.28  ? 354 LYS C C   1 
ATOM   7723  O  O   . LYS C 1 290 ? 23.123 54.371 103.947 1.00 97.63  ? 354 LYS C O   1 
ATOM   7724  C  CB  . LYS C 1 290 ? 23.684 52.401 105.952 1.00 84.78  ? 354 LYS C CB  1 
ATOM   7725  C  CG  . LYS C 1 290 ? 24.259 51.689 107.155 1.00 87.82  ? 354 LYS C CG  1 
ATOM   7726  C  CD  . LYS C 1 290 ? 25.495 52.408 107.664 1.00 100.15 ? 354 LYS C CD  1 
ATOM   7727  C  CE  . LYS C 1 290 ? 25.990 51.785 108.952 1.00 106.40 ? 354 LYS C CE  1 
ATOM   7728  N  NZ  . LYS C 1 290 ? 26.552 50.444 108.683 1.00 95.87  ? 354 LYS C NZ  1 
ATOM   7729  N  N   . LYS C 1 291 ? 21.331 55.086 105.066 1.00 79.24  ? 355 LYS C N   1 
ATOM   7730  C  CA  . LYS C 1 291 ? 20.728 55.694 103.904 1.00 78.94  ? 355 LYS C CA  1 
ATOM   7731  C  C   . LYS C 1 291 ? 21.202 57.119 103.793 1.00 77.46  ? 355 LYS C C   1 
ATOM   7732  O  O   . LYS C 1 291 ? 21.266 57.851 104.786 1.00 80.19  ? 355 LYS C O   1 
ATOM   7733  C  CB  . LYS C 1 291 ? 19.203 55.669 104.025 1.00 90.54  ? 355 LYS C CB  1 
ATOM   7734  C  CG  . LYS C 1 291 ? 18.571 54.338 103.672 1.00 103.77 ? 355 LYS C CG  1 
ATOM   7735  C  CD  . LYS C 1 291 ? 17.839 54.398 102.333 1.00 115.90 ? 355 LYS C CD  1 
ATOM   7736  C  CE  . LYS C 1 291 ? 16.949 53.172 102.141 1.00 120.85 ? 355 LYS C CE  1 
ATOM   7737  N  NZ  . LYS C 1 291 ? 16.032 52.939 103.301 1.00 145.25 ? 355 LYS C NZ  1 
ATOM   7738  N  N   . GLY C 1 292 ? 21.542 57.507 102.575 1.00 72.84  ? 356 GLY C N   1 
ATOM   7739  C  CA  . GLY C 1 292 ? 21.807 58.900 102.273 1.00 78.70  ? 356 GLY C CA  1 
ATOM   7740  C  C   . GLY C 1 292 ? 23.212 59.371 102.569 1.00 74.05  ? 356 GLY C C   1 
ATOM   7741  O  O   . GLY C 1 292 ? 23.905 58.839 103.439 1.00 70.81  ? 356 GLY C O   1 
ATOM   7742  N  N   . PHE C 1 293 ? 23.625 60.388 101.828 1.00 70.85  ? 357 PHE C N   1 
ATOM   7743  C  CA  . PHE C 1 293 ? 24.915 60.994 102.041 1.00 71.43  ? 357 PHE C CA  1 
ATOM   7744  C  C   . PHE C 1 293 ? 24.805 62.500 101.924 1.00 72.87  ? 357 PHE C C   1 
ATOM   7745  O  O   . PHE C 1 293 ? 24.276 63.014 100.927 1.00 79.29  ? 357 PHE C O   1 
ATOM   7746  C  CB  . PHE C 1 293 ? 25.888 60.459 101.008 1.00 66.41  ? 357 PHE C CB  1 
ATOM   7747  C  CG  . PHE C 1 293 ? 27.266 60.947 101.184 1.00 58.53  ? 357 PHE C CG  1 
ATOM   7748  C  CD1 . PHE C 1 293 ? 27.663 62.159 100.635 1.00 57.05  ? 357 PHE C CD1 1 
ATOM   7749  C  CD2 . PHE C 1 293 ? 28.175 60.203 101.917 1.00 61.74  ? 357 PHE C CD2 1 
ATOM   7750  C  CE1 . PHE C 1 293 ? 28.960 62.615 100.800 1.00 63.67  ? 357 PHE C CE1 1 
ATOM   7751  C  CE2 . PHE C 1 293 ? 29.480 60.653 102.103 1.00 56.97  ? 357 PHE C CE2 1 
ATOM   7752  C  CZ  . PHE C 1 293 ? 29.876 61.851 101.538 1.00 60.38  ? 357 PHE C CZ  1 
ATOM   7753  N  N   . GLU C 1 294 ? 25.296 63.193 102.948 1.00 66.49  ? 358 GLU C N   1 
ATOM   7754  C  CA  . GLU C 1 294 ? 25.293 64.655 102.967 1.00 70.19  ? 358 GLU C CA  1 
ATOM   7755  C  C   . GLU C 1 294 ? 26.714 65.205 103.092 1.00 65.89  ? 358 GLU C C   1 
ATOM   7756  O  O   . GLU C 1 294 ? 27.575 64.590 103.692 1.00 64.81  ? 358 GLU C O   1 
ATOM   7757  C  CB  . GLU C 1 294 ? 24.387 65.194 104.077 1.00 73.04  ? 358 GLU C CB  1 
ATOM   7758  C  CG  . GLU C 1 294 ? 24.813 64.838 105.530 1.00 93.94  ? 358 GLU C CG  1 
ATOM   7759  C  CD  . GLU C 1 294 ? 23.807 65.323 106.617 1.00 132.20 ? 358 GLU C CD  1 
ATOM   7760  O  OE1 . GLU C 1 294 ? 23.042 66.279 106.351 1.00 151.05 ? 358 GLU C OE1 1 
ATOM   7761  O  OE2 . GLU C 1 294 ? 23.783 64.755 107.743 1.00 114.25 ? 358 GLU C OE2 1 
ATOM   7762  N  N   . ILE C 1 295 ? 26.963 66.355 102.491 1.00 62.45  ? 359 ILE C N   1 
ATOM   7763  C  CA  . ILE C 1 295 ? 28.247 67.025 102.647 1.00 64.90  ? 359 ILE C CA  1 
ATOM   7764  C  C   . ILE C 1 295 ? 27.965 68.468 103.045 1.00 64.55  ? 359 ILE C C   1 
ATOM   7765  O  O   . ILE C 1 295 ? 26.969 69.046 102.633 1.00 71.61  ? 359 ILE C O   1 
ATOM   7766  C  CB  . ILE C 1 295 ? 29.084 66.971 101.374 1.00 59.53  ? 359 ILE C CB  1 
ATOM   7767  C  CG1 . ILE C 1 295 ? 30.511 67.437 101.661 1.00 61.94  ? 359 ILE C CG1 1 
ATOM   7768  C  CG2 . ILE C 1 295 ? 28.465 67.857 100.307 1.00 58.34  ? 359 ILE C CG2 1 
ATOM   7769  C  CD1 . ILE C 1 295 ? 31.486 67.175 100.499 1.00 54.38  ? 359 ILE C CD1 1 
ATOM   7770  N  N   . TYR C 1 296 ? 28.850 69.053 103.828 1.00 62.75  ? 360 TYR C N   1 
ATOM   7771  C  CA  . TYR C 1 296 ? 28.462 70.199 104.627 1.00 65.54  ? 360 TYR C CA  1 
ATOM   7772  C  C   . TYR C 1 296 ? 29.614 71.179 104.719 1.00 64.20  ? 360 TYR C C   1 
ATOM   7773  O  O   . TYR C 1 296 ? 30.743 70.813 105.035 1.00 69.93  ? 360 TYR C O   1 
ATOM   7774  C  CB  . TYR C 1 296 ? 28.024 69.699 106.006 1.00 73.68  ? 360 TYR C CB  1 
ATOM   7775  C  CG  . TYR C 1 296 ? 27.471 70.745 106.925 1.00 78.84  ? 360 TYR C CG  1 
ATOM   7776  C  CD1 . TYR C 1 296 ? 26.215 71.279 106.733 1.00 87.82  ? 360 TYR C CD1 1 
ATOM   7777  C  CD2 . TYR C 1 296 ? 28.197 71.187 107.998 1.00 84.19  ? 360 TYR C CD2 1 
ATOM   7778  C  CE1 . TYR C 1 296 ? 25.705 72.243 107.580 1.00 83.87  ? 360 TYR C CE1 1 
ATOM   7779  C  CE2 . TYR C 1 296 ? 27.698 72.143 108.853 1.00 90.77  ? 360 TYR C CE2 1 
ATOM   7780  C  CZ  . TYR C 1 296 ? 26.451 72.668 108.642 1.00 88.58  ? 360 TYR C CZ  1 
ATOM   7781  O  OH  . TYR C 1 296 ? 25.964 73.617 109.508 1.00 89.60  ? 360 TYR C OH  1 
ATOM   7782  N  N   . LYS C 1 297 ? 29.318 72.431 104.423 1.00 64.59  ? 361 LYS C N   1 
ATOM   7783  C  CA  . LYS C 1 297 ? 30.346 73.435 104.199 1.00 70.67  ? 361 LYS C CA  1 
ATOM   7784  C  C   . LYS C 1 297 ? 30.586 74.286 105.434 1.00 78.66  ? 361 LYS C C   1 
ATOM   7785  O  O   . LYS C 1 297 ? 29.656 74.549 106.201 1.00 97.55  ? 361 LYS C O   1 
ATOM   7786  C  CB  . LYS C 1 297 ? 29.896 74.311 103.050 1.00 69.59  ? 361 LYS C CB  1 
ATOM   7787  C  CG  . LYS C 1 297 ? 30.883 75.309 102.525 1.00 69.76  ? 361 LYS C CG  1 
ATOM   7788  C  CD  . LYS C 1 297 ? 30.180 76.037 101.426 1.00 75.02  ? 361 LYS C CD  1 
ATOM   7789  C  CE  . LYS C 1 297 ? 30.797 77.370 101.072 1.00 71.80  ? 361 LYS C CE  1 
ATOM   7790  N  NZ  . LYS C 1 297 ? 30.080 77.914 99.853  1.00 79.08  ? 361 LYS C NZ  1 
ATOM   7791  N  N   . PHE C 1 298 ? 31.833 74.714 105.617 1.00 76.29  ? 362 PHE C N   1 
ATOM   7792  C  CA  . PHE C 1 298 ? 32.229 75.516 106.770 1.00 76.87  ? 362 PHE C CA  1 
ATOM   7793  C  C   . PHE C 1 298 ? 33.154 76.624 106.355 1.00 80.95  ? 362 PHE C C   1 
ATOM   7794  O  O   . PHE C 1 298 ? 34.091 76.390 105.591 1.00 81.76  ? 362 PHE C O   1 
ATOM   7795  C  CB  . PHE C 1 298 ? 33.007 74.671 107.757 1.00 76.61  ? 362 PHE C CB  1 
ATOM   7796  C  CG  . PHE C 1 298 ? 32.204 73.610 108.431 1.00 80.42  ? 362 PHE C CG  1 
ATOM   7797  C  CD1 . PHE C 1 298 ? 31.492 73.896 109.583 1.00 82.72  ? 362 PHE C CD1 1 
ATOM   7798  C  CD2 . PHE C 1 298 ? 32.202 72.307 107.949 1.00 73.64  ? 362 PHE C CD2 1 
ATOM   7799  C  CE1 . PHE C 1 298 ? 30.761 72.892 110.227 1.00 81.69  ? 362 PHE C CE1 1 
ATOM   7800  C  CE2 . PHE C 1 298 ? 31.484 71.315 108.599 1.00 71.48  ? 362 PHE C CE2 1 
ATOM   7801  C  CZ  . PHE C 1 298 ? 30.762 71.605 109.737 1.00 66.15  ? 362 PHE C CZ  1 
ATOM   7802  N  N   . LEU C 1 299 ? 32.943 77.819 106.894 1.00 86.62  ? 363 LEU C N   1 
ATOM   7803  C  CA  . LEU C 1 299 ? 33.916 78.873 106.678 1.00 95.10  ? 363 LEU C CA  1 
ATOM   7804  C  C   . LEU C 1 299 ? 35.130 78.656 107.569 1.00 114.18 ? 363 LEU C C   1 
ATOM   7805  O  O   . LEU C 1 299 ? 34.987 78.422 108.766 1.00 107.04 ? 363 LEU C O   1 
ATOM   7806  C  CB  . LEU C 1 299 ? 33.296 80.235 106.905 1.00 103.01 ? 363 LEU C CB  1 
ATOM   7807  C  CG  . LEU C 1 299 ? 32.484 80.739 105.709 1.00 111.77 ? 363 LEU C CG  1 
ATOM   7808  C  CD1 . LEU C 1 299 ? 33.247 80.440 104.389 1.00 94.53  ? 363 LEU C CD1 1 
ATOM   7809  C  CD2 . LEU C 1 299 ? 31.043 80.181 105.711 1.00 99.66  ? 363 LEU C CD2 1 
ATOM   7810  N  N   . GLY C 1 300 ? 36.318 78.691 106.963 1.00 131.39 ? 364 GLY C N   1 
ATOM   7811  C  CA  . GLY C 1 300 ? 37.577 78.512 107.687 1.00 117.11 ? 364 GLY C CA  1 
ATOM   7812  C  C   . GLY C 1 300 ? 37.794 77.096 108.180 1.00 109.75 ? 364 GLY C C   1 
ATOM   7813  O  O   . GLY C 1 300 ? 37.091 76.179 107.759 1.00 113.46 ? 364 GLY C O   1 
ATOM   7814  N  N   . THR C 1 301 ? 38.755 76.936 109.094 1.00 111.66 ? 365 THR C N   1 
ATOM   7815  C  CA  . THR C 1 301 ? 39.263 75.621 109.514 1.00 96.79  ? 365 THR C CA  1 
ATOM   7816  C  C   . THR C 1 301 ? 38.262 74.750 110.278 1.00 87.38  ? 365 THR C C   1 
ATOM   7817  O  O   . THR C 1 301 ? 37.299 75.239 110.856 1.00 90.36  ? 365 THR C O   1 
ATOM   7818  C  CB  . THR C 1 301 ? 40.597 75.745 110.312 1.00 99.58  ? 365 THR C CB  1 
ATOM   7819  O  OG1 . THR C 1 301 ? 41.116 74.443 110.596 1.00 124.81 ? 365 THR C OG1 1 
ATOM   7820  C  CG2 . THR C 1 301 ? 40.396 76.474 111.616 1.00 109.83 ? 365 THR C CG2 1 
ATOM   7821  N  N   . LEU C 1 302 ? 38.504 73.446 110.249 1.00 84.13  ? 366 LEU C N   1 
ATOM   7822  C  CA  . LEU C 1 302 ? 37.741 72.498 111.032 1.00 88.37  ? 366 LEU C CA  1 
ATOM   7823  C  C   . LEU C 1 302 ? 38.317 72.382 112.427 1.00 96.18  ? 366 LEU C C   1 
ATOM   7824  O  O   . LEU C 1 302 ? 37.790 71.655 113.274 1.00 109.82 ? 366 LEU C O   1 
ATOM   7825  C  CB  . LEU C 1 302 ? 37.799 71.128 110.383 1.00 80.76  ? 366 LEU C CB  1 
ATOM   7826  C  CG  . LEU C 1 302 ? 37.343 71.070 108.941 1.00 89.50  ? 366 LEU C CG  1 
ATOM   7827  C  CD1 . LEU C 1 302 ? 38.551 70.948 108.075 1.00 97.09  ? 366 LEU C CD1 1 
ATOM   7828  C  CD2 . LEU C 1 302 ? 36.475 69.857 108.771 1.00 92.80  ? 366 LEU C CD2 1 
ATOM   7829  N  N   . PHE C 1 303 ? 39.407 73.099 112.665 1.00 98.52  ? 367 PHE C N   1 
ATOM   7830  C  CA  . PHE C 1 303 ? 40.181 72.907 113.874 1.00 87.32  ? 367 PHE C CA  1 
ATOM   7831  C  C   . PHE C 1 303 ? 40.078 74.063 114.825 1.00 89.83  ? 367 PHE C C   1 
ATOM   7832  O  O   . PHE C 1 303 ? 40.731 74.075 115.855 1.00 99.99  ? 367 PHE C O   1 
ATOM   7833  C  CB  . PHE C 1 303 ? 41.627 72.595 113.509 1.00 86.25  ? 367 PHE C CB  1 
ATOM   7834  C  CG  . PHE C 1 303 ? 41.753 71.459 112.558 1.00 79.13  ? 367 PHE C CG  1 
ATOM   7835  C  CD1 . PHE C 1 303 ? 41.186 70.221 112.855 1.00 75.79  ? 367 PHE C CD1 1 
ATOM   7836  C  CD2 . PHE C 1 303 ? 42.402 71.627 111.347 1.00 102.33 ? 367 PHE C CD2 1 
ATOM   7837  C  CE1 . PHE C 1 303 ? 41.271 69.157 111.946 1.00 85.29  ? 367 PHE C CE1 1 
ATOM   7838  C  CE2 . PHE C 1 303 ? 42.500 70.565 110.427 1.00 118.96 ? 367 PHE C CE2 1 
ATOM   7839  C  CZ  . PHE C 1 303 ? 41.933 69.330 110.726 1.00 91.96  ? 367 PHE C CZ  1 
ATOM   7840  N  N   . SER C 1 304 ? 39.251 75.039 114.469 1.00 115.40 ? 368 SER C N   1 
ATOM   7841  C  CA  . SER C 1 304 ? 38.844 76.098 115.387 1.00 115.19 ? 368 SER C CA  1 
ATOM   7842  C  C   . SER C 1 304 ? 37.436 75.780 115.891 1.00 110.30 ? 368 SER C C   1 
ATOM   7843  O  O   . SER C 1 304 ? 36.563 75.382 115.127 1.00 99.48  ? 368 SER C O   1 
ATOM   7844  C  CB  . SER C 1 304 ? 38.872 77.462 114.690 1.00 115.92 ? 368 SER C CB  1 
ATOM   7845  O  OG  . SER C 1 304 ? 38.695 78.519 115.616 1.00 150.95 ? 368 SER C OG  1 
ATOM   7846  N  N   . VAL C 1 305 ? 37.220 75.947 117.186 1.00 118.84 ? 369 VAL C N   1 
ATOM   7847  C  CA  . VAL C 1 305 ? 35.891 75.788 117.766 1.00 122.93 ? 369 VAL C CA  1 
ATOM   7848  C  C   . VAL C 1 305 ? 34.964 76.954 117.339 1.00 120.87 ? 369 VAL C C   1 
ATOM   7849  O  O   . VAL C 1 305 ? 33.741 76.909 117.514 1.00 104.60 ? 369 VAL C O   1 
ATOM   7850  C  CB  . VAL C 1 305 ? 36.026 75.713 119.290 1.00 125.62 ? 369 VAL C CB  1 
ATOM   7851  C  CG1 . VAL C 1 305 ? 36.532 77.048 119.839 1.00 138.75 ? 369 VAL C CG1 1 
ATOM   7852  C  CG2 . VAL C 1 305 ? 34.720 75.309 119.931 1.00 127.88 ? 369 VAL C CG2 1 
ATOM   7853  N  N   . GLN C 1 306 ? 35.586 77.980 116.758 1.00 134.34 ? 370 GLN C N   1 
ATOM   7854  C  CA  . GLN C 1 306 ? 34.954 79.241 116.380 1.00 119.81 ? 370 GLN C CA  1 
ATOM   7855  C  C   . GLN C 1 306 ? 34.073 79.109 115.163 1.00 106.83 ? 370 GLN C C   1 
ATOM   7856  O  O   . GLN C 1 306 ? 33.159 79.908 114.951 1.00 109.92 ? 370 GLN C O   1 
ATOM   7857  C  CB  . GLN C 1 306 ? 36.043 80.278 116.063 1.00 125.60 ? 370 GLN C CB  1 
ATOM   7858  C  CG  . GLN C 1 306 ? 36.697 80.939 117.277 1.00 134.69 ? 370 GLN C CG  1 
ATOM   7859  C  CD  . GLN C 1 306 ? 35.813 82.004 117.917 1.00 149.10 ? 370 GLN C CD  1 
ATOM   7860  O  OE1 . GLN C 1 306 ? 34.896 81.686 118.672 1.00 153.07 ? 370 GLN C OE1 1 
ATOM   7861  N  NE2 . GLN C 1 306 ? 36.091 83.276 117.617 1.00 144.41 ? 370 GLN C NE2 1 
ATOM   7862  N  N   . THR C 1 307 ? 34.359 78.094 114.361 1.00 114.05 ? 371 THR C N   1 
ATOM   7863  C  CA  . THR C 1 307 ? 33.914 78.074 112.976 1.00 117.32 ? 371 THR C CA  1 
ATOM   7864  C  C   . THR C 1 307 ? 32.487 77.586 112.758 1.00 109.16 ? 371 THR C C   1 
ATOM   7865  O  O   . THR C 1 307 ? 31.984 76.733 113.491 1.00 109.87 ? 371 THR C O   1 
ATOM   7866  C  CB  . THR C 1 307 ? 34.925 77.350 112.077 1.00 122.46 ? 371 THR C CB  1 
ATOM   7867  O  OG1 . THR C 1 307 ? 35.201 76.059 112.619 1.00 140.17 ? 371 THR C OG1 1 
ATOM   7868  C  CG2 . THR C 1 307 ? 36.227 78.153 112.018 1.00 147.56 ? 371 THR C CG2 1 
ATOM   7869  N  N   . VAL C 1 308 ? 31.881 78.116 111.698 1.00 109.00 ? 372 VAL C N   1 
ATOM   7870  C  CA  . VAL C 1 308 ? 30.441 78.153 111.502 1.00 97.98  ? 372 VAL C CA  1 
ATOM   7871  C  C   . VAL C 1 308 ? 29.990 77.265 110.340 1.00 95.34  ? 372 VAL C C   1 
ATOM   7872  O  O   . VAL C 1 308 ? 30.545 77.344 109.230 1.00 83.33  ? 372 VAL C O   1 
ATOM   7873  C  CB  . VAL C 1 308 ? 30.027 79.618 111.208 1.00 88.16  ? 372 VAL C CB  1 
ATOM   7874  C  CG1 . VAL C 1 308 ? 28.546 79.761 111.143 1.00 80.95  ? 372 VAL C CG1 1 
ATOM   7875  C  CG2 . VAL C 1 308 ? 30.602 80.546 112.260 1.00 96.41  ? 372 VAL C CG2 1 
ATOM   7876  N  N   . GLY C 1 309 ? 28.987 76.424 110.593 1.00 97.65  ? 373 GLY C N   1 
ATOM   7877  C  CA  . GLY C 1 309 ? 28.278 75.746 109.507 1.00 97.57  ? 373 GLY C CA  1 
ATOM   7878  C  C   . GLY C 1 309 ? 27.670 76.778 108.562 1.00 121.59 ? 373 GLY C C   1 
ATOM   7879  O  O   . GLY C 1 309 ? 27.230 77.855 108.989 1.00 141.04 ? 373 GLY C O   1 
ATOM   7880  N  N   . ASN C 1 310 ? 27.652 76.470 107.275 1.00 101.83 ? 374 ASN C N   1 
ATOM   7881  C  CA  . ASN C 1 310 ? 27.146 77.420 106.321 1.00 100.27 ? 374 ASN C CA  1 
ATOM   7882  C  C   . ASN C 1 310 ? 26.108 76.770 105.438 1.00 107.47 ? 374 ASN C C   1 
ATOM   7883  O  O   . ASN C 1 310 ? 24.956 77.184 105.418 1.00 144.56 ? 374 ASN C O   1 
ATOM   7884  C  CB  . ASN C 1 310 ? 28.290 78.002 105.487 1.00 103.73 ? 374 ASN C CB  1 
ATOM   7885  C  CG  . ASN C 1 310 ? 27.798 78.918 104.351 1.00 98.59  ? 374 ASN C CG  1 
ATOM   7886  O  OD1 . ASN C 1 310 ? 27.703 78.497 103.202 1.00 82.39  ? 374 ASN C OD1 1 
ATOM   7887  N  ND2 . ASN C 1 310 ? 27.488 80.166 104.677 1.00 95.91  ? 374 ASN C ND2 1 
ATOM   7888  N  N   . ARG C 1 311 ? 26.518 75.739 104.718 1.00 106.80 ? 375 ARG C N   1 
ATOM   7889  C  CA  . ARG C 1 311 ? 25.674 75.153 103.686 1.00 100.05 ? 375 ARG C CA  1 
ATOM   7890  C  C   . ARG C 1 311 ? 25.672 73.632 103.751 1.00 88.48  ? 375 ARG C C   1 
ATOM   7891  O  O   . ARG C 1 311 ? 26.727 72.998 103.808 1.00 82.75  ? 375 ARG C O   1 
ATOM   7892  C  CB  . ARG C 1 311 ? 26.145 75.600 102.297 1.00 90.72  ? 375 ARG C CB  1 
ATOM   7893  C  CG  . ARG C 1 311 ? 25.306 75.048 101.152 1.00 96.37  ? 375 ARG C CG  1 
ATOM   7894  C  CD  . ARG C 1 311 ? 23.889 75.652 101.200 1.00 118.10 ? 375 ARG C CD  1 
ATOM   7895  N  NE  . ARG C 1 311 ? 23.029 75.206 100.109 1.00 84.70  ? 375 ARG C NE  1 
ATOM   7896  C  CZ  . ARG C 1 311 ? 23.074 75.704 98.877  1.00 89.87  ? 375 ARG C CZ  1 
ATOM   7897  N  NH1 . ARG C 1 311 ? 23.955 76.653 98.575  1.00 81.73  ? 375 ARG C NH1 1 
ATOM   7898  N  NH2 . ARG C 1 311 ? 22.247 75.244 97.939  1.00 95.76  ? 375 ARG C NH2 1 
ATOM   7899  N  N   . ASN C 1 312 ? 24.482 73.051 103.743 1.00 75.75  ? 376 ASN C N   1 
ATOM   7900  C  CA  . ASN C 1 312 ? 24.378 71.616 103.767 1.00 80.45  ? 376 ASN C CA  1 
ATOM   7901  C  C   . ASN C 1 312 ? 23.810 71.100 102.464 1.00 83.55  ? 376 ASN C C   1 
ATOM   7902  O  O   . ASN C 1 312 ? 22.668 71.429 102.124 1.00 105.69 ? 376 ASN C O   1 
ATOM   7903  C  CB  . ASN C 1 312 ? 23.497 71.156 104.928 1.00 86.23  ? 376 ASN C CB  1 
ATOM   7904  C  CG  . ASN C 1 312 ? 23.094 69.697 104.801 1.00 92.15  ? 376 ASN C CG  1 
ATOM   7905  O  OD1 . ASN C 1 312 ? 22.054 69.385 104.225 1.00 111.61 ? 376 ASN C OD1 1 
ATOM   7906  N  ND2 . ASN C 1 312 ? 23.930 68.798 105.309 1.00 84.68  ? 376 ASN C ND2 1 
ATOM   7907  N  N   . TYR C 1 313 ? 24.600 70.297 101.751 1.00 68.96  ? 377 TYR C N   1 
ATOM   7908  C  CA  . TYR C 1 313 ? 24.157 69.647 100.523 1.00 72.42  ? 377 TYR C CA  1 
ATOM   7909  C  C   . TYR C 1 313 ? 23.803 68.203 100.786 1.00 70.73  ? 377 TYR C C   1 
ATOM   7910  O  O   . TYR C 1 313 ? 24.659 67.424 101.200 1.00 72.55  ? 377 TYR C O   1 
ATOM   7911  C  CB  . TYR C 1 313 ? 25.253 69.669 99.471  1.00 71.00  ? 377 TYR C CB  1 
ATOM   7912  C  CG  . TYR C 1 313 ? 25.581 71.031 98.906  1.00 83.87  ? 377 TYR C CG  1 
ATOM   7913  C  CD1 . TYR C 1 313 ? 26.741 71.704 99.299  1.00 75.13  ? 377 TYR C CD1 1 
ATOM   7914  C  CD2 . TYR C 1 313 ? 24.750 71.639 97.940  1.00 81.29  ? 377 TYR C CD2 1 
ATOM   7915  C  CE1 . TYR C 1 313 ? 27.068 72.945 98.749  1.00 81.62  ? 377 TYR C CE1 1 
ATOM   7916  C  CE2 . TYR C 1 313 ? 25.068 72.879 97.396  1.00 73.72  ? 377 TYR C CE2 1 
ATOM   7917  C  CZ  . TYR C 1 313 ? 26.230 73.523 97.805  1.00 80.36  ? 377 TYR C CZ  1 
ATOM   7918  O  OH  . TYR C 1 313 ? 26.556 74.746 97.281  1.00 101.10 ? 377 TYR C OH  1 
ATOM   7919  N  N   . GLN C 1 314 ? 22.551 67.839 100.544 1.00 63.58  ? 378 GLN C N   1 
ATOM   7920  C  CA  . GLN C 1 314 ? 22.157 66.459 100.701 1.00 65.07  ? 378 GLN C CA  1 
ATOM   7921  C  C   . GLN C 1 314 ? 22.253 65.812 99.355  1.00 65.28  ? 378 GLN C C   1 
ATOM   7922  O  O   . GLN C 1 314 ? 21.314 65.866 98.568  1.00 85.67  ? 378 GLN C O   1 
ATOM   7923  C  CB  . GLN C 1 314 ? 20.746 66.334 101.256 1.00 70.69  ? 378 GLN C CB  1 
ATOM   7924  C  CG  . GLN C 1 314 ? 20.642 66.715 102.713 1.00 97.55  ? 378 GLN C CG  1 
ATOM   7925  C  CD  . GLN C 1 314 ? 19.475 66.050 103.400 1.00 112.55 ? 378 GLN C CD  1 
ATOM   7926  O  OE1 . GLN C 1 314 ? 18.787 65.167 102.682 1.00 131.52 ? 378 GLN C OE1 1 
ATOM   7927  N  NE2 . GLN C 1 314 ? 19.193 66.321 104.566 1.00 113.37 ? 378 GLN C NE2 1 
ATOM   7928  N  N   . LEU C 1 315 ? 23.398 65.206 99.071  1.00 65.89  ? 379 LEU C N   1 
ATOM   7929  C  CA  . LEU C 1 315 ? 23.653 64.657 97.728  1.00 70.92  ? 379 LEU C CA  1 
ATOM   7930  C  C   . LEU C 1 315 ? 22.849 63.403 97.391  1.00 81.14  ? 379 LEU C C   1 
ATOM   7931  O  O   . LEU C 1 315 ? 22.282 63.286 96.287  1.00 79.28  ? 379 LEU C O   1 
ATOM   7932  C  CB  . LEU C 1 315 ? 25.141 64.407 97.498  1.00 53.96  ? 379 LEU C CB  1 
ATOM   7933  C  CG  . LEU C 1 315 ? 25.996 65.666 97.500  1.00 54.40  ? 379 LEU C CG  1 
ATOM   7934  C  CD1 . LEU C 1 315 ? 27.492 65.333 97.298  1.00 51.09  ? 379 LEU C CD1 1 
ATOM   7935  C  CD2 . LEU C 1 315 ? 25.493 66.673 96.452  1.00 54.45  ? 379 LEU C CD2 1 
ATOM   7936  N  N   . LEU C 1 316 ? 22.810 62.467 98.336  1.00 71.95  ? 380 LEU C N   1 
ATOM   7937  C  CA  . LEU C 1 316 ? 22.097 61.228 98.122  1.00 69.21  ? 380 LEU C CA  1 
ATOM   7938  C  C   . LEU C 1 316 ? 21.098 60.993 99.232  1.00 68.94  ? 380 LEU C C   1 
ATOM   7939  O  O   . LEU C 1 316 ? 21.396 61.256 100.381 1.00 64.32  ? 380 LEU C O   1 
ATOM   7940  C  CB  . LEU C 1 316 ? 23.069 60.069 98.063  1.00 71.84  ? 380 LEU C CB  1 
ATOM   7941  C  CG  . LEU C 1 316 ? 24.218 60.142 97.065  1.00 77.37  ? 380 LEU C CG  1 
ATOM   7942  C  CD1 . LEU C 1 316 ? 24.797 58.768 96.917  1.00 76.54  ? 380 LEU C CD1 1 
ATOM   7943  C  CD2 . LEU C 1 316 ? 23.725 60.637 95.712  1.00 110.25 ? 380 LEU C CD2 1 
ATOM   7944  N  N   . SER C 1 317 ? 19.920 60.491 98.871  1.00 76.16  ? 381 SER C N   1 
ATOM   7945  C  CA  . SER C 1 317 ? 18.833 60.264 99.809  1.00 78.23  ? 381 SER C CA  1 
ATOM   7946  C  C   . SER C 1 317 ? 18.336 58.840 99.719  1.00 84.08  ? 381 SER C C   1 
ATOM   7947  O  O   . SER C 1 317 ? 18.211 58.160 100.726 1.00 96.17  ? 381 SER C O   1 
ATOM   7948  C  CB  . SER C 1 317 ? 17.667 61.209 99.524  1.00 103.13 ? 381 SER C CB  1 
ATOM   7949  O  OG  . SER C 1 317 ? 18.092 62.559 99.439  1.00 128.10 ? 381 SER C OG  1 
ATOM   7950  N  N   . ASN C 1 318 ? 18.061 58.381 98.506  1.00 93.44  ? 382 ASN C N   1 
ATOM   7951  C  CA  . ASN C 1 318 ? 17.467 57.068 98.322  1.00 111.59 ? 382 ASN C CA  1 
ATOM   7952  C  C   . ASN C 1 318 ? 18.433 55.885 98.343  1.00 100.94 ? 382 ASN C C   1 
ATOM   7953  O  O   . ASN C 1 318 ? 17.999 54.739 98.230  1.00 139.75 ? 382 ASN C O   1 
ATOM   7954  C  CB  . ASN C 1 318 ? 16.608 57.038 97.044  1.00 128.77 ? 382 ASN C CB  1 
ATOM   7955  C  CG  . ASN C 1 318 ? 15.115 56.994 97.339  1.00 137.31 ? 382 ASN C CG  1 
ATOM   7956  O  OD1 . ASN C 1 318 ? 14.691 56.711 98.463  1.00 155.33 ? 382 ASN C OD1 1 
ATOM   7957  N  ND2 . ASN C 1 318 ? 14.311 57.265 96.322  1.00 135.13 ? 382 ASN C ND2 1 
ATOM   7958  N  N   . SER C 1 319 ? 19.728 56.138 98.500  1.00 79.01  ? 383 SER C N   1 
ATOM   7959  C  CA  . SER C 1 319 ? 20.714 55.076 98.269  1.00 73.75  ? 383 SER C CA  1 
ATOM   7960  C  C   . SER C 1 319 ? 21.427 54.603 99.541  1.00 74.85  ? 383 SER C C   1 
ATOM   7961  O  O   . SER C 1 319 ? 21.780 55.406 100.392 1.00 96.96  ? 383 SER C O   1 
ATOM   7962  C  CB  . SER C 1 319 ? 21.727 55.524 97.215  1.00 69.42  ? 383 SER C CB  1 
ATOM   7963  O  OG  . SER C 1 319 ? 21.212 56.615 96.476  1.00 101.33 ? 383 SER C OG  1 
ATOM   7964  N  N   . THR C 1 320 ? 21.631 53.295 99.672  1.00 79.76  ? 384 THR C N   1 
ATOM   7965  C  CA  . THR C 1 320 ? 22.382 52.744 100.808 1.00 86.89  ? 384 THR C CA  1 
ATOM   7966  C  C   . THR C 1 320 ? 23.895 52.954 100.667 1.00 78.15  ? 384 THR C C   1 
ATOM   7967  O  O   . THR C 1 320 ? 24.535 52.414 99.763  1.00 85.41  ? 384 THR C O   1 
ATOM   7968  C  CB  . THR C 1 320 ? 22.078 51.249 101.031 1.00 89.56  ? 384 THR C CB  1 
ATOM   7969  O  OG1 . THR C 1 320 ? 20.671 51.081 101.247 1.00 113.14 ? 384 THR C OG1 1 
ATOM   7970  C  CG2 . THR C 1 320 ? 22.836 50.735 102.244 1.00 73.21  ? 384 THR C CG2 1 
ATOM   7971  N  N   . ILE C 1 321 ? 24.455 53.723 101.595 1.00 66.13  ? 385 ILE C N   1 
ATOM   7972  C  CA  . ILE C 1 321 ? 25.827 54.203 101.489 1.00 60.68  ? 385 ILE C CA  1 
ATOM   7973  C  C   . ILE C 1 321 ? 26.803 53.446 102.367 1.00 65.66  ? 385 ILE C C   1 
ATOM   7974  O  O   . ILE C 1 321 ? 26.418 52.768 103.322 1.00 66.92  ? 385 ILE C O   1 
ATOM   7975  C  CB  . ILE C 1 321 ? 25.936 55.684 101.861 1.00 61.97  ? 385 ILE C CB  1 
ATOM   7976  C  CG1 . ILE C 1 321 ? 24.837 56.505 101.186 1.00 74.25  ? 385 ILE C CG1 1 
ATOM   7977  C  CG2 . ILE C 1 321 ? 27.283 56.219 101.464 1.00 52.21  ? 385 ILE C CG2 1 
ATOM   7978  C  CD1 . ILE C 1 321 ? 25.034 56.645 99.690  1.00 94.38  ? 385 ILE C CD1 1 
ATOM   7979  N  N   . GLY C 1 322 ? 28.082 53.582 102.019 1.00 75.65  ? 386 GLY C N   1 
ATOM   7980  C  CA  . GLY C 1 322 ? 29.188 52.897 102.691 1.00 70.84  ? 386 GLY C CA  1 
ATOM   7981  C  C   . GLY C 1 322 ? 30.445 53.745 102.671 1.00 68.87  ? 386 GLY C C   1 
ATOM   7982  O  O   . GLY C 1 322 ? 30.434 54.892 103.135 1.00 85.05  ? 386 GLY C O   1 
ATOM   7983  N  N   . ARG C 1 323 ? 31.530 53.200 102.128 1.00 61.30  ? 387 ARG C N   1 
ATOM   7984  C  CA  . ARG C 1 323 ? 32.789 53.947 102.070 1.00 55.28  ? 387 ARG C CA  1 
ATOM   7985  C  C   . ARG C 1 323 ? 32.729 55.146 101.143 1.00 50.18  ? 387 ARG C C   1 
ATOM   7986  O  O   . ARG C 1 323 ? 31.937 55.198 100.184 1.00 56.90  ? 387 ARG C O   1 
ATOM   7987  C  CB  . ARG C 1 323 ? 33.921 53.036 101.647 1.00 59.47  ? 387 ARG C CB  1 
ATOM   7988  C  CG  . ARG C 1 323 ? 33.956 51.735 102.443 1.00 65.81  ? 387 ARG C CG  1 
ATOM   7989  C  CD  . ARG C 1 323 ? 34.806 50.707 101.750 1.00 67.36  ? 387 ARG C CD  1 
ATOM   7990  N  NE  . ARG C 1 323 ? 36.112 51.254 101.419 1.00 74.12  ? 387 ARG C NE  1 
ATOM   7991  C  CZ  . ARG C 1 323 ? 36.515 51.531 100.189 1.00 68.09  ? 387 ARG C CZ  1 
ATOM   7992  N  NH1 . ARG C 1 323 ? 35.717 51.296 99.160  1.00 56.79  ? 387 ARG C NH1 1 
ATOM   7993  N  NH2 . ARG C 1 323 ? 37.728 52.026 99.998  1.00 62.30  ? 387 ARG C NH2 1 
ATOM   7994  N  N   . SER C 1 324 ? 33.558 56.117 101.456 1.00 42.25  ? 388 SER C N   1 
ATOM   7995  C  CA  . SER C 1 324 ? 33.677 57.330 100.670 1.00 44.90  ? 388 SER C CA  1 
ATOM   7996  C  C   . SER C 1 324 ? 35.134 57.726 100.726 1.00 47.99  ? 388 SER C C   1 
ATOM   7997  O  O   . SER C 1 324 ? 35.803 57.475 101.735 1.00 61.70  ? 388 SER C O   1 
ATOM   7998  C  CB  . SER C 1 324 ? 32.797 58.458 101.248 1.00 50.04  ? 388 SER C CB  1 
ATOM   7999  O  OG  . SER C 1 324 ? 32.634 58.412 102.667 1.00 49.92  ? 388 SER C OG  1 
ATOM   8000  N  N   . GLY C 1 325 ? 35.652 58.344 99.679  1.00 43.19  ? 389 GLY C N   1 
ATOM   8001  C  CA  . GLY C 1 325 ? 37.051 58.735 99.704  1.00 40.64  ? 389 GLY C CA  1 
ATOM   8002  C  C   . GLY C 1 325 ? 37.356 59.796 98.692  1.00 42.65  ? 389 GLY C C   1 
ATOM   8003  O  O   . GLY C 1 325 ? 36.541 60.070 97.803  1.00 45.57  ? 389 GLY C O   1 
ATOM   8004  N  N   . LEU C 1 326 ? 38.532 60.391 98.832  1.00 41.61  ? 390 LEU C N   1 
ATOM   8005  C  CA  . LEU C 1 326 ? 38.955 61.478 97.969  1.00 45.57  ? 390 LEU C CA  1 
ATOM   8006  C  C   . LEU C 1 326 ? 39.888 60.978 96.888  1.00 59.28  ? 390 LEU C C   1 
ATOM   8007  O  O   . LEU C 1 326 ? 40.459 59.870 96.979  1.00 70.72  ? 390 LEU C O   1 
ATOM   8008  C  CB  . LEU C 1 326 ? 39.681 62.562 98.756  1.00 41.32  ? 390 LEU C CB  1 
ATOM   8009  C  CG  . LEU C 1 326 ? 38.933 63.305 99.858  1.00 43.31  ? 390 LEU C CG  1 
ATOM   8010  C  CD1 . LEU C 1 326 ? 39.919 63.788 100.854 1.00 49.52  ? 390 LEU C CD1 1 
ATOM   8011  C  CD2 . LEU C 1 326 ? 38.199 64.499 99.324  1.00 46.65  ? 390 LEU C CD2 1 
ATOM   8012  N  N   . TYR C 1 327 ? 40.013 61.808 95.849  1.00 71.31  ? 391 TYR C N   1 
ATOM   8013  C  CA  . TYR C 1 327 ? 40.997 61.634 94.780  1.00 64.78  ? 391 TYR C CA  1 
ATOM   8014  C  C   . TYR C 1 327 ? 41.209 62.920 94.003  1.00 68.93  ? 391 TYR C C   1 
ATOM   8015  O  O   . TYR C 1 327 ? 40.272 63.719 93.820  1.00 66.54  ? 391 TYR C O   1 
ATOM   8016  C  CB  . TYR C 1 327 ? 40.617 60.503 93.826  1.00 62.38  ? 391 TYR C CB  1 
ATOM   8017  C  CG  . TYR C 1 327 ? 39.438 60.724 92.905  1.00 59.57  ? 391 TYR C CG  1 
ATOM   8018  C  CD1 . TYR C 1 327 ? 39.612 61.248 91.622  1.00 60.89  ? 391 TYR C CD1 1 
ATOM   8019  C  CD2 . TYR C 1 327 ? 38.154 60.345 93.291  1.00 61.32  ? 391 TYR C CD2 1 
ATOM   8020  C  CE1 . TYR C 1 327 ? 38.519 61.420 90.760  1.00 59.45  ? 391 TYR C CE1 1 
ATOM   8021  C  CE2 . TYR C 1 327 ? 37.071 60.525 92.454  1.00 61.47  ? 391 TYR C CE2 1 
ATOM   8022  C  CZ  . TYR C 1 327 ? 37.262 61.047 91.193  1.00 60.92  ? 391 TYR C CZ  1 
ATOM   8023  O  OH  . TYR C 1 327 ? 36.183 61.187 90.377  1.00 70.06  ? 391 TYR C OH  1 
ATOM   8024  N  N   . GLN C 1 328 ? 42.451 63.121 93.568  1.00 70.06  ? 392 GLN C N   1 
ATOM   8025  C  CA  . GLN C 1 328 ? 42.772 64.284 92.754  1.00 69.12  ? 392 GLN C CA  1 
ATOM   8026  C  C   . GLN C 1 328 ? 43.164 63.858 91.361  1.00 71.48  ? 392 GLN C C   1 
ATOM   8027  O  O   . GLN C 1 328 ? 44.138 63.100 91.162  1.00 89.84  ? 392 GLN C O   1 
ATOM   8028  C  CB  . GLN C 1 328 ? 43.879 65.124 93.362  1.00 82.19  ? 392 GLN C CB  1 
ATOM   8029  C  CG  . GLN C 1 328 ? 43.641 65.549 94.770  1.00 80.00  ? 392 GLN C CG  1 
ATOM   8030  C  CD  . GLN C 1 328 ? 44.837 66.268 95.341  1.00 75.64  ? 392 GLN C CD  1 
ATOM   8031  O  OE1 . GLN C 1 328 ? 45.867 65.668 95.645  1.00 95.86  ? 392 GLN C OE1 1 
ATOM   8032  N  NE2 . GLN C 1 328 ? 44.701 67.559 95.501  1.00 69.94  ? 392 GLN C NE2 1 
ATOM   8033  N  N   . PRO C 1 329 ? 42.369 64.305 90.387  1.00 72.25  ? 393 PRO C N   1 
ATOM   8034  C  CA  . PRO C 1 329 ? 42.694 64.111 88.997  1.00 75.80  ? 393 PRO C CA  1 
ATOM   8035  C  C   . PRO C 1 329 ? 43.789 65.110 88.630  1.00 75.70  ? 393 PRO C C   1 
ATOM   8036  O  O   . PRO C 1 329 ? 43.823 66.194 89.201  1.00 80.26  ? 393 PRO C O   1 
ATOM   8037  C  CB  . PRO C 1 329 ? 41.366 64.406 88.292  1.00 61.59  ? 393 PRO C CB  1 
ATOM   8038  C  CG  . PRO C 1 329 ? 40.626 65.268 89.209  1.00 60.25  ? 393 PRO C CG  1 
ATOM   8039  C  CD  . PRO C 1 329 ? 41.020 64.873 90.572  1.00 70.62  ? 393 PRO C CD  1 
ATOM   8040  N  N   . ALA C 1 330 ? 44.689 64.728 87.722  1.00 78.97  ? 394 ALA C N   1 
ATOM   8041  C  CA  . ALA C 1 330 ? 45.792 65.595 87.307  1.00 78.69  ? 394 ALA C CA  1 
ATOM   8042  C  C   . ALA C 1 330 ? 45.724 65.964 85.831  1.00 103.88 ? 394 ALA C C   1 
ATOM   8043  O  O   . ALA C 1 330 ? 45.705 65.086 84.957  1.00 152.05 ? 394 ALA C O   1 
ATOM   8044  C  CB  . ALA C 1 330 ? 47.102 64.938 87.605  1.00 85.08  ? 394 ALA C CB  1 
ATOM   8045  N  N   . TYR C 1 331 ? 45.666 67.266 85.562  1.00 107.40 ? 395 TYR C N   1 
ATOM   8046  C  CA  . TYR C 1 331 ? 45.792 67.791 84.203  1.00 134.44 ? 395 TYR C CA  1 
ATOM   8047  C  C   . TYR C 1 331 ? 46.641 69.046 84.242  1.00 147.61 ? 395 TYR C C   1 
ATOM   8048  O  O   . TYR C 1 331 ? 47.051 69.491 85.318  1.00 163.20 ? 395 TYR C O   1 
ATOM   8049  C  CB  . TYR C 1 331 ? 44.430 68.141 83.602  1.00 137.02 ? 395 TYR C CB  1 
ATOM   8050  C  CG  . TYR C 1 331 ? 43.299 67.252 84.044  1.00 140.18 ? 395 TYR C CG  1 
ATOM   8051  C  CD1 . TYR C 1 331 ? 43.121 65.973 83.481  1.00 133.76 ? 395 TYR C CD1 1 
ATOM   8052  C  CD2 . TYR C 1 331 ? 42.400 67.686 85.024  1.00 121.04 ? 395 TYR C CD2 1 
ATOM   8053  C  CE1 . TYR C 1 331 ? 42.078 65.143 83.890  1.00 116.15 ? 395 TYR C CE1 1 
ATOM   8054  C  CE2 . TYR C 1 331 ? 41.348 66.874 85.437  1.00 123.71 ? 395 TYR C CE2 1 
ATOM   8055  C  CZ  . TYR C 1 331 ? 41.194 65.602 84.865  1.00 136.32 ? 395 TYR C CZ  1 
ATOM   8056  O  OH  . TYR C 1 331 ? 40.154 64.791 85.268  1.00 135.88 ? 395 TYR C OH  1 
ATOM   8057  N  N   . GLU C 1 332 ? 46.909 69.610 83.068  1.00 147.96 ? 396 GLU C N   1 
ATOM   8058  C  CA  . GLU C 1 332 ? 47.512 70.929 82.993  1.00 196.05 ? 396 GLU C CA  1 
ATOM   8059  C  C   . GLU C 1 332 ? 46.567 71.927 83.673  1.00 240.38 ? 396 GLU C C   1 
ATOM   8060  O  O   . GLU C 1 332 ? 46.997 72.700 84.536  1.00 287.39 ? 396 GLU C O   1 
ATOM   8061  C  CB  . GLU C 1 332 ? 47.789 71.316 81.535  1.00 184.57 ? 396 GLU C CB  1 
ATOM   8062  C  CG  . GLU C 1 332 ? 48.583 72.612 81.355  1.00 193.96 ? 396 GLU C CG  1 
ATOM   8063  C  CD  . GLU C 1 332 ? 47.726 73.859 81.497  1.00 209.30 ? 396 GLU C CD  1 
ATOM   8064  O  OE1 . GLU C 1 332 ? 46.658 73.930 80.848  1.00 175.86 ? 396 GLU C OE1 1 
ATOM   8065  O  OE2 . GLU C 1 332 ? 48.123 74.768 82.258  1.00 258.36 ? 396 GLU C OE2 1 
ATOM   8066  N  N   . SER C 1 333 ? 45.284 71.873 83.297  1.00 214.21 ? 397 SER C N   1 
ATOM   8067  C  CA  . SER C 1 333 ? 44.239 72.772 83.813  1.00 176.44 ? 397 SER C CA  1 
ATOM   8068  C  C   . SER C 1 333 ? 44.790 74.176 84.049  1.00 195.39 ? 397 SER C C   1 
ATOM   8069  O  O   . SER C 1 333 ? 45.081 74.893 83.093  1.00 222.43 ? 397 SER C O   1 
ATOM   8070  C  CB  . SER C 1 333 ? 43.607 72.204 85.086  1.00 159.73 ? 397 SER C CB  1 
ATOM   8071  O  OG  . SER C 1 333 ? 42.973 70.965 84.830  1.00 156.83 ? 397 SER C OG  1 
ATOM   8072  N  N   . ARG C 1 334 ? 44.942 74.555 85.318  1.00 181.18 ? 398 ARG C N   1 
ATOM   8073  C  CA  . ARG C 1 334 ? 45.622 75.799 85.687  1.00 167.39 ? 398 ARG C CA  1 
ATOM   8074  C  C   . ARG C 1 334 ? 46.194 75.726 87.091  1.00 150.52 ? 398 ARG C C   1 
ATOM   8075  O  O   . ARG C 1 334 ? 46.246 74.648 87.676  1.00 173.63 ? 398 ARG C O   1 
ATOM   8076  C  CB  . ARG C 1 334 ? 44.699 77.013 85.535  1.00 189.02 ? 398 ARG C CB  1 
ATOM   8077  C  CG  . ARG C 1 334 ? 43.316 76.874 86.150  1.00 176.61 ? 398 ARG C CG  1 
ATOM   8078  C  CD  . ARG C 1 334 ? 42.589 78.211 86.108  1.00 190.42 ? 398 ARG C CD  1 
ATOM   8079  N  NE  . ARG C 1 334 ? 42.735 78.881 84.814  1.00 194.25 ? 398 ARG C NE  1 
ATOM   8080  C  CZ  . ARG C 1 334 ? 42.185 80.051 84.501  1.00 207.10 ? 398 ARG C CZ  1 
ATOM   8081  N  NH1 . ARG C 1 334 ? 41.438 80.699 85.388  1.00 212.64 ? 398 ARG C NH1 1 
ATOM   8082  N  NH2 . ARG C 1 334 ? 42.377 80.573 83.295  1.00 212.16 ? 398 ARG C NH2 1 
ATOM   8083  N  N   . ASP C 1 335 ? 46.623 76.873 87.623  1.00 179.66 ? 399 ASP C N   1 
ATOM   8084  C  CA  . ASP C 1 335 ? 47.191 76.972 88.979  1.00 229.78 ? 399 ASP C CA  1 
ATOM   8085  C  C   . ASP C 1 335 ? 46.372 76.186 89.993  1.00 224.57 ? 399 ASP C C   1 
ATOM   8086  O  O   . ASP C 1 335 ? 46.867 75.782 91.053  1.00 229.19 ? 399 ASP C O   1 
ATOM   8087  C  CB  . ASP C 1 335 ? 47.270 78.438 89.419  1.00 244.87 ? 399 ASP C CB  1 
ATOM   8088  C  CG  . ASP C 1 335 ? 48.260 79.248 88.599  1.00 241.40 ? 399 ASP C CG  1 
ATOM   8089  O  OD1 . ASP C 1 335 ? 49.091 78.648 87.882  1.00 243.33 ? 399 ASP C OD1 1 
ATOM   8090  O  OD2 . ASP C 1 335 ? 48.211 80.493 88.677  1.00 224.22 ? 399 ASP C OD2 1 
ATOM   8091  N  N   . CYS C 1 336 ? 45.114 75.974 89.623  1.00 175.63 ? 400 CYS C N   1 
ATOM   8092  C  CA  . CYS C 1 336 ? 44.133 75.272 90.418  1.00 138.08 ? 400 CYS C CA  1 
ATOM   8093  C  C   . CYS C 1 336 ? 44.285 73.728 90.427  1.00 104.35 ? 400 CYS C C   1 
ATOM   8094  O  O   . CYS C 1 336 ? 44.299 73.081 89.388  1.00 82.40  ? 400 CYS C O   1 
ATOM   8095  C  CB  . CYS C 1 336 ? 42.762 75.661 89.888  1.00 152.04 ? 400 CYS C CB  1 
ATOM   8096  S  SG  . CYS C 1 336 ? 41.558 75.793 91.157  1.00 230.41 ? 400 CYS C SG  1 
ATOM   8097  N  N   . GLN C 1 337 ? 44.391 73.140 91.615  1.00 92.88  ? 401 GLN C N   1 
ATOM   8098  C  CA  . GLN C 1 337 ? 44.336 71.695 91.754  1.00 83.75  ? 401 GLN C CA  1 
ATOM   8099  C  C   . GLN C 1 337 ? 42.908 71.205 92.030  1.00 89.46  ? 401 GLN C C   1 
ATOM   8100  O  O   . GLN C 1 337 ? 42.345 71.457 93.105  1.00 92.89  ? 401 GLN C O   1 
ATOM   8101  C  CB  . GLN C 1 337 ? 45.295 71.203 92.850  1.00 75.13  ? 401 GLN C CB  1 
ATOM   8102  C  CG  . GLN C 1 337 ? 45.325 69.696 93.023  1.00 68.50  ? 401 GLN C CG  1 
ATOM   8103  C  CD  . GLN C 1 337 ? 45.290 68.950 91.693  1.00 95.22  ? 401 GLN C CD  1 
ATOM   8104  O  OE1 . GLN C 1 337 ? 46.124 69.189 90.811  1.00 105.79 ? 401 GLN C OE1 1 
ATOM   8105  N  NE2 . GLN C 1 337 ? 44.314 68.045 91.541  1.00 97.73  ? 401 GLN C NE2 1 
ATOM   8106  N  N   . GLU C 1 338 ? 42.345 70.491 91.057  1.00 81.83  ? 402 GLU C N   1 
ATOM   8107  C  CA  . GLU C 1 338 ? 41.008 69.920 91.181  1.00 81.98  ? 402 GLU C CA  1 
ATOM   8108  C  C   . GLU C 1 338 ? 40.934 68.832 92.265  1.00 78.14  ? 402 GLU C C   1 
ATOM   8109  O  O   . GLU C 1 338 ? 41.905 68.093 92.493  1.00 85.90  ? 402 GLU C O   1 
ATOM   8110  C  CB  . GLU C 1 338 ? 40.586 69.343 89.838  1.00 107.40 ? 402 GLU C CB  1 
ATOM   8111  C  CG  . GLU C 1 338 ? 39.126 68.931 89.760  1.00 152.45 ? 402 GLU C CG  1 
ATOM   8112  C  CD  . GLU C 1 338 ? 38.236 69.974 89.108  1.00 158.63 ? 402 GLU C CD  1 
ATOM   8113  O  OE1 . GLU C 1 338 ? 38.665 70.606 88.121  1.00 168.98 ? 402 GLU C OE1 1 
ATOM   8114  O  OE2 . GLU C 1 338 ? 37.090 70.146 89.568  1.00 174.48 ? 402 GLU C OE2 1 
ATOM   8115  N  N   . LEU C 1 339 ? 39.777 68.743 92.923  1.00 65.16  ? 403 LEU C N   1 
ATOM   8116  C  CA  . LEU C 1 339 ? 39.541 67.763 93.986  1.00 60.06  ? 403 LEU C CA  1 
ATOM   8117  C  C   . LEU C 1 339 ? 38.177 67.090 93.855  1.00 62.19  ? 403 LEU C C   1 
ATOM   8118  O  O   . LEU C 1 339 ? 37.150 67.758 93.791  1.00 66.61  ? 403 LEU C O   1 
ATOM   8119  C  CB  . LEU C 1 339 ? 39.689 68.412 95.360  1.00 58.66  ? 403 LEU C CB  1 
ATOM   8120  C  CG  . LEU C 1 339 ? 39.515 67.533 96.596  1.00 65.79  ? 403 LEU C CG  1 
ATOM   8121  C  CD1 . LEU C 1 339 ? 40.546 66.429 96.571  1.00 75.06  ? 403 LEU C CD1 1 
ATOM   8122  C  CD2 . LEU C 1 339 ? 39.655 68.358 97.875  1.00 60.20  ? 403 LEU C CD2 1 
ATOM   8123  N  N   . CYS C 1 340 ? 38.177 65.762 93.808  1.00 59.81  ? 404 CYS C N   1 
ATOM   8124  C  CA  . CYS C 1 340 ? 36.946 65.004 93.647  1.00 58.36  ? 404 CYS C CA  1 
ATOM   8125  C  C   . CYS C 1 340 ? 36.889 63.929 94.710  1.00 59.67  ? 404 CYS C C   1 
ATOM   8126  O  O   . CYS C 1 340 ? 37.908 63.630 95.353  1.00 51.94  ? 404 CYS C O   1 
ATOM   8127  C  CB  . CYS C 1 340 ? 36.917 64.330 92.288  1.00 67.97  ? 404 CYS C CB  1 
ATOM   8128  S  SG  . CYS C 1 340 ? 37.111 65.437 90.890  1.00 100.17 ? 404 CYS C SG  1 
ATOM   8129  N  N   . PHE C 1 341 ? 35.711 63.342 94.900  1.00 51.02  ? 405 PHE C N   1 
ATOM   8130  C  CA  . PHE C 1 341 ? 35.580 62.235 95.837  1.00 47.49  ? 405 PHE C CA  1 
ATOM   8131  C  C   . PHE C 1 341 ? 34.582 61.229 95.348  1.00 49.04  ? 405 PHE C C   1 
ATOM   8132  O  O   . PHE C 1 341 ? 33.690 61.551 94.558  1.00 61.44  ? 405 PHE C O   1 
ATOM   8133  C  CB  . PHE C 1 341 ? 35.193 62.718 97.238  1.00 51.89  ? 405 PHE C CB  1 
ATOM   8134  C  CG  . PHE C 1 341 ? 33.777 63.263 97.347  1.00 58.64  ? 405 PHE C CG  1 
ATOM   8135  C  CD1 . PHE C 1 341 ? 33.509 64.625 97.116  1.00 61.91  ? 405 PHE C CD1 1 
ATOM   8136  C  CD2 . PHE C 1 341 ? 32.717 62.419 97.704  1.00 56.09  ? 405 PHE C CD2 1 
ATOM   8137  C  CE1 . PHE C 1 341 ? 32.199 65.134 97.216  1.00 60.47  ? 405 PHE C CE1 1 
ATOM   8138  C  CE2 . PHE C 1 341 ? 31.429 62.912 97.798  1.00 60.14  ? 405 PHE C CE2 1 
ATOM   8139  C  CZ  . PHE C 1 341 ? 31.164 64.279 97.549  1.00 63.35  ? 405 PHE C CZ  1 
ATOM   8140  N  N   . TRP C 1 342 ? 34.716 60.009 95.835  1.00 42.47  ? 406 TRP C N   1 
ATOM   8141  C  CA  . TRP C 1 342 ? 33.841 58.948 95.395  1.00 45.19  ? 406 TRP C CA  1 
ATOM   8142  C  C   . TRP C 1 342 ? 33.112 58.425 96.568  1.00 52.81  ? 406 TRP C C   1 
ATOM   8143  O  O   . TRP C 1 342 ? 33.509 58.680 97.699  1.00 63.81  ? 406 TRP C O   1 
ATOM   8144  C  CB  . TRP C 1 342 ? 34.642 57.833 94.766  1.00 42.06  ? 406 TRP C CB  1 
ATOM   8145  C  CG  . TRP C 1 342 ? 35.744 57.349 95.667  1.00 45.84  ? 406 TRP C CG  1 
ATOM   8146  C  CD1 . TRP C 1 342 ? 37.098 57.708 95.635  1.00 47.56  ? 406 TRP C CD1 1 
ATOM   8147  C  CD2 . TRP C 1 342 ? 35.634 56.389 96.768  1.00 43.45  ? 406 TRP C CD2 1 
ATOM   8148  N  NE1 . TRP C 1 342 ? 37.803 57.045 96.604  1.00 41.44  ? 406 TRP C NE1 1 
ATOM   8149  C  CE2 . TRP C 1 342 ? 36.984 56.237 97.318  1.00 39.42  ? 406 TRP C CE2 1 
ATOM   8150  C  CE3 . TRP C 1 342 ? 34.596 55.646 97.317  1.00 47.77  ? 406 TRP C CE3 1 
ATOM   8151  C  CZ2 . TRP C 1 342 ? 37.251 55.392 98.374  1.00 38.75  ? 406 TRP C CZ2 1 
ATOM   8152  C  CZ3 . TRP C 1 342 ? 34.888 54.796 98.399  1.00 52.28  ? 406 TRP C CZ3 1 
ATOM   8153  C  CH2 . TRP C 1 342 ? 36.181 54.686 98.917  1.00 43.37  ? 406 TRP C CH2 1 
ATOM   8154  N  N   . ILE C 1 343 ? 32.051 57.665 96.308  1.00 51.73  ? 407 ILE C N   1 
ATOM   8155  C  CA  . ILE C 1 343 ? 31.193 57.148 97.343  1.00 45.96  ? 407 ILE C CA  1 
ATOM   8156  C  C   . ILE C 1 343 ? 30.771 55.841 96.807  1.00 46.12  ? 407 ILE C C   1 
ATOM   8157  O  O   . ILE C 1 343 ? 30.267 55.773 95.670  1.00 45.29  ? 407 ILE C O   1 
ATOM   8158  C  CB  . ILE C 1 343 ? 29.903 58.007 97.536  1.00 47.81  ? 407 ILE C CB  1 
ATOM   8159  C  CG1 . ILE C 1 343 ? 30.253 59.452 97.907  1.00 52.31  ? 407 ILE C CG1 1 
ATOM   8160  C  CG2 . ILE C 1 343 ? 28.976 57.404 98.593  1.00 45.53  ? 407 ILE C CG2 1 
ATOM   8161  C  CD1 . ILE C 1 343 ? 29.065 60.355 97.919  1.00 56.58  ? 407 ILE C CD1 1 
ATOM   8162  N  N   . GLU C 1 344 ? 30.947 54.819 97.646  1.00 46.57  ? 408 GLU C N   1 
ATOM   8163  C  CA  . GLU C 1 344 ? 30.521 53.444 97.355  1.00 46.92  ? 408 GLU C CA  1 
ATOM   8164  C  C   . GLU C 1 344 ? 29.098 53.139 97.791  1.00 47.51  ? 408 GLU C C   1 
ATOM   8165  O  O   . GLU C 1 344 ? 28.689 53.484 98.877  1.00 64.45  ? 408 GLU C O   1 
ATOM   8166  C  CB  . GLU C 1 344 ? 31.485 52.508 98.024  1.00 49.99  ? 408 GLU C CB  1 
ATOM   8167  C  CG  . GLU C 1 344 ? 31.441 51.061 97.613  1.00 61.60  ? 408 GLU C CG  1 
ATOM   8168  C  CD  . GLU C 1 344 ? 32.358 50.216 98.499  1.00 77.11  ? 408 GLU C CD  1 
ATOM   8169  O  OE1 . GLU C 1 344 ? 33.240 49.501 97.958  1.00 85.83  ? 408 GLU C OE1 1 
ATOM   8170  O  OE2 . GLU C 1 344 ? 32.216 50.302 99.749  1.00 74.37  ? 408 GLU C OE2 1 
ATOM   8171  N  N   . ILE C 1 345 ? 28.348 52.477 96.935  1.00 52.79  ? 409 ILE C N   1 
ATOM   8172  C  CA  . ILE C 1 345 ? 26.910 52.306 97.123  1.00 56.71  ? 409 ILE C CA  1 
ATOM   8173  C  C   . ILE C 1 345 ? 26.513 50.851 96.979  1.00 50.76  ? 409 ILE C C   1 
ATOM   8174  O  O   . ILE C 1 345 ? 26.869 50.226 95.999  1.00 64.26  ? 409 ILE C O   1 
ATOM   8175  C  CB  . ILE C 1 345 ? 26.172 53.088 96.037  1.00 57.21  ? 409 ILE C CB  1 
ATOM   8176  C  CG1 . ILE C 1 345 ? 26.357 54.591 96.261  1.00 59.94  ? 409 ILE C CG1 1 
ATOM   8177  C  CG2 . ILE C 1 345 ? 24.713 52.682 95.964  1.00 51.36  ? 409 ILE C CG2 1 
ATOM   8178  C  CD1 . ILE C 1 345 ? 25.444 55.475 95.344  1.00 65.37  ? 409 ILE C CD1 1 
ATOM   8179  N  N   . ALA C 1 346 ? 25.766 50.315 97.930  1.00 49.94  ? 410 ALA C N   1 
ATOM   8180  C  CA  . ALA C 1 346 ? 25.216 48.960 97.796  1.00 55.54  ? 410 ALA C CA  1 
ATOM   8181  C  C   . ALA C 1 346 ? 24.459 48.777 96.476  1.00 57.88  ? 410 ALA C C   1 
ATOM   8182  O  O   . ALA C 1 346 ? 23.644 49.614 96.116  1.00 64.45  ? 410 ALA C O   1 
ATOM   8183  C  CB  . ALA C 1 346 ? 24.292 48.666 98.948  1.00 58.77  ? 410 ALA C CB  1 
ATOM   8184  N  N   . ALA C 1 347 ? 24.747 47.698 95.750  1.00 66.62  ? 411 ALA C N   1 
ATOM   8185  C  CA  . ALA C 1 347 ? 23.945 47.314 94.573  1.00 65.97  ? 411 ALA C CA  1 
ATOM   8186  C  C   . ALA C 1 347 ? 23.326 45.948 94.808  1.00 69.52  ? 411 ALA C C   1 
ATOM   8187  O  O   . ALA C 1 347 ? 23.405 45.405 95.913  1.00 85.91  ? 411 ALA C O   1 
ATOM   8188  C  CB  . ALA C 1 347 ? 24.805 47.302 93.334  1.00 53.28  ? 411 ALA C CB  1 
ATOM   8189  N  N   . THR C 1 348 ? 22.680 45.411 93.783  1.00 79.19  ? 412 THR C N   1 
ATOM   8190  C  CA  . THR C 1 348 ? 22.342 43.972 93.731  1.00 89.96  ? 412 THR C CA  1 
ATOM   8191  C  C   . THR C 1 348 ? 22.436 43.458 92.287  1.00 77.87  ? 412 THR C C   1 
ATOM   8192  O  O   . THR C 1 348 ? 22.135 44.173 91.330  1.00 71.98  ? 412 THR C O   1 
ATOM   8193  C  CB  . THR C 1 348 ? 20.947 43.598 94.381  1.00 90.84  ? 412 THR C CB  1 
ATOM   8194  O  OG1 . THR C 1 348 ? 19.880 44.278 93.712  1.00 91.15  ? 412 THR C OG1 1 
ATOM   8195  C  CG2 . THR C 1 348 ? 20.894 43.935 95.885  1.00 106.72 ? 412 THR C CG2 1 
ATOM   8196  N  N   . THR C 1 349 ? 22.894 42.232 92.128  1.00 84.89  ? 413 THR C N   1 
ATOM   8197  C  CA  . THR C 1 349 ? 22.907 41.599 90.820  1.00 84.15  ? 413 THR C CA  1 
ATOM   8198  C  C   . THR C 1 349 ? 21.463 41.351 90.390  1.00 85.91  ? 413 THR C C   1 
ATOM   8199  O  O   . THR C 1 349 ? 20.537 41.459 91.200  1.00 86.77  ? 413 THR C O   1 
ATOM   8200  C  CB  . THR C 1 349 ? 23.731 40.311 90.902  1.00 90.63  ? 413 THR C CB  1 
ATOM   8201  O  OG1 . THR C 1 349 ? 25.087 40.678 91.179  1.00 97.89  ? 413 THR C OG1 1 
ATOM   8202  C  CG2 . THR C 1 349 ? 23.680 39.477 89.627  1.00 90.91  ? 413 THR C CG2 1 
ATOM   8203  N  N   . LYS C 1 350 ? 21.276 41.063 89.104  1.00 103.73 ? 414 LYS C N   1 
ATOM   8204  C  CA  . LYS C 1 350 ? 19.974 40.702 88.535  1.00 103.59 ? 414 LYS C CA  1 
ATOM   8205  C  C   . LYS C 1 350 ? 19.252 39.637 89.368  1.00 102.26 ? 414 LYS C C   1 
ATOM   8206  O  O   . LYS C 1 350 ? 18.029 39.559 89.334  1.00 127.08 ? 414 LYS C O   1 
ATOM   8207  C  CB  . LYS C 1 350 ? 20.150 40.232 87.086  1.00 121.55 ? 414 LYS C CB  1 
ATOM   8208  C  CG  . LYS C 1 350 ? 18.879 39.930 86.296  1.00 118.53 ? 414 LYS C CG  1 
ATOM   8209  C  CD  . LYS C 1 350 ? 19.219 39.177 85.003  1.00 134.54 ? 414 LYS C CD  1 
ATOM   8210  C  CE  . LYS C 1 350 ? 17.955 38.754 84.242  1.00 154.30 ? 414 LYS C CE  1 
ATOM   8211  N  NZ  . LYS C 1 350 ? 18.228 38.134 82.904  1.00 165.63 ? 414 LYS C NZ  1 
ATOM   8212  N  N   . ALA C 1 351 ? 20.001 38.835 90.123  1.00 92.72  ? 415 ALA C N   1 
ATOM   8213  C  CA  . ALA C 1 351 ? 19.400 37.880 91.040  1.00 87.34  ? 415 ALA C CA  1 
ATOM   8214  C  C   . ALA C 1 351 ? 20.153 37.800 92.360  1.00 91.82  ? 415 ALA C C   1 
ATOM   8215  O  O   . ALA C 1 351 ? 21.020 36.950 92.510  1.00 122.61 ? 415 ALA C O   1 
ATOM   8216  C  CB  . ALA C 1 351 ? 19.340 36.518 90.389  1.00 77.33  ? 415 ALA C CB  1 
ATOM   8217  N  N   . GLY C 1 352 ? 19.823 38.678 93.309  1.00 94.87  ? 416 GLY C N   1 
ATOM   8218  C  CA  . GLY C 1 352 ? 20.461 38.697 94.640  1.00 103.75 ? 416 GLY C CA  1 
ATOM   8219  C  C   . GLY C 1 352 ? 21.887 39.208 94.550  1.00 99.19  ? 416 GLY C C   1 
ATOM   8220  O  O   . GLY C 1 352 ? 22.276 39.735 93.518  1.00 91.24  ? 416 GLY C O   1 
ATOM   8221  N  N   . LEU C 1 353 ? 22.668 39.041 95.619  1.00 102.55 ? 417 LEU C N   1 
ATOM   8222  C  CA  . LEU C 1 353 ? 24.107 39.372 95.630  1.00 87.01  ? 417 LEU C CA  1 
ATOM   8223  C  C   . LEU C 1 353 ? 24.337 40.863 95.873  1.00 84.51  ? 417 LEU C C   1 
ATOM   8224  O  O   . LEU C 1 353 ? 23.553 41.674 95.412  1.00 88.08  ? 417 LEU C O   1 
ATOM   8225  C  CB  . LEU C 1 353 ? 24.799 38.885 94.347  1.00 78.86  ? 417 LEU C CB  1 
ATOM   8226  C  CG  . LEU C 1 353 ? 24.290 37.529 93.781  1.00 87.76  ? 417 LEU C CG  1 
ATOM   8227  C  CD1 . LEU C 1 353 ? 24.719 37.260 92.351  1.00 88.60  ? 417 LEU C CD1 1 
ATOM   8228  C  CD2 . LEU C 1 353 ? 24.639 36.322 94.637  1.00 82.50  ? 417 LEU C CD2 1 
ATOM   8229  N  N   . SER C 1 354 ? 25.397 41.210 96.604  1.00 78.64  ? 418 SER C N   1 
ATOM   8230  C  CA  . SER C 1 354 ? 25.582 42.566 97.076  1.00 90.84  ? 418 SER C CA  1 
ATOM   8231  C  C   . SER C 1 354 ? 26.856 43.189 96.523  1.00 111.71 ? 418 SER C C   1 
ATOM   8232  O  O   . SER C 1 354 ? 27.765 43.540 97.277  1.00 162.01 ? 418 SER C O   1 
ATOM   8233  C  CB  . SER C 1 354 ? 25.583 42.595 98.609  1.00 103.59 ? 418 SER C CB  1 
ATOM   8234  O  OG  . SER C 1 354 ? 26.593 41.747 99.132  1.00 141.95 ? 418 SER C OG  1 
ATOM   8235  N  N   . SER C 1 355 ? 26.934 43.331 95.208  1.00 97.55  ? 419 SER C N   1 
ATOM   8236  C  CA  . SER C 1 355 ? 28.024 44.102 94.644  1.00 101.90 ? 419 SER C CA  1 
ATOM   8237  C  C   . SER C 1 355 ? 27.811 45.569 95.019  1.00 94.48  ? 419 SER C C   1 
ATOM   8238  O  O   . SER C 1 355 ? 26.707 45.978 95.390  1.00 89.06  ? 419 SER C O   1 
ATOM   8239  C  CB  . SER C 1 355 ? 28.106 43.922 93.131  1.00 104.63 ? 419 SER C CB  1 
ATOM   8240  O  OG  . SER C 1 355 ? 29.306 44.478 92.612  1.00 97.58  ? 419 SER C OG  1 
ATOM   8241  N  N   . ASN C 1 356 ? 28.885 46.345 94.964  1.00 91.80  ? 420 ASN C N   1 
ATOM   8242  C  CA  . ASN C 1 356 ? 28.804 47.771 95.205  1.00 82.74  ? 420 ASN C CA  1 
ATOM   8243  C  C   . ASN C 1 356 ? 29.114 48.510 93.923  1.00 74.28  ? 420 ASN C C   1 
ATOM   8244  O  O   . ASN C 1 356 ? 29.869 48.011 93.098  1.00 96.29  ? 420 ASN C O   1 
ATOM   8245  C  CB  . ASN C 1 356 ? 29.809 48.205 96.286  1.00 89.28  ? 420 ASN C CB  1 
ATOM   8246  C  CG  . ASN C 1 356 ? 29.839 47.277 97.469  1.00 89.78  ? 420 ASN C CG  1 
ATOM   8247  O  OD1 . ASN C 1 356 ? 30.320 46.147 97.367  1.00 102.99 ? 420 ASN C OD1 1 
ATOM   8248  N  ND2 . ASN C 1 356 ? 29.335 47.748 98.606  1.00 79.00  ? 420 ASN C ND2 1 
ATOM   8249  N  N   . ASP C 1 357 ? 28.550 49.700 93.754  1.00 66.22  ? 421 ASP C N   1 
ATOM   8250  C  CA  . ASP C 1 357 ? 28.978 50.568 92.666  1.00 79.13  ? 421 ASP C CA  1 
ATOM   8251  C  C   . ASP C 1 357 ? 29.413 51.942 93.131  1.00 75.51  ? 421 ASP C C   1 
ATOM   8252  O  O   . ASP C 1 357 ? 29.263 52.281 94.293  1.00 76.36  ? 421 ASP C O   1 
ATOM   8253  C  CB  . ASP C 1 357 ? 27.916 50.691 91.576  1.00 89.06  ? 421 ASP C CB  1 
ATOM   8254  C  CG  . ASP C 1 357 ? 28.515 50.594 90.174  1.00 128.99 ? 421 ASP C CG  1 
ATOM   8255  O  OD1 . ASP C 1 357 ? 29.596 51.183 89.929  1.00 162.23 ? 421 ASP C OD1 1 
ATOM   8256  O  OD2 . ASP C 1 357 ? 27.910 49.916 89.312  1.00 142.49 ? 421 ASP C OD2 1 
ATOM   8257  N  N   . LEU C 1 358 ? 29.936 52.724 92.193  1.00 70.93  ? 422 LEU C N   1 
ATOM   8258  C  CA  . LEU C 1 358 ? 30.524 54.006 92.485  1.00 68.76  ? 422 LEU C CA  1 
ATOM   8259  C  C   . LEU C 1 358 ? 29.723 55.167 91.954  1.00 63.45  ? 422 LEU C C   1 
ATOM   8260  O  O   . LEU C 1 358 ? 29.121 55.074 90.903  1.00 58.88  ? 422 LEU C O   1 
ATOM   8261  C  CB  . LEU C 1 358 ? 31.895 54.076 91.854  1.00 58.58  ? 422 LEU C CB  1 
ATOM   8262  C  CG  . LEU C 1 358 ? 32.974 53.464 92.681  1.00 61.06  ? 422 LEU C CG  1 
ATOM   8263  C  CD1 . LEU C 1 358 ? 34.265 54.011 92.141  1.00 80.44  ? 422 LEU C CD1 1 
ATOM   8264  C  CD2 . LEU C 1 358 ? 32.775 53.906 94.098  1.00 75.46  ? 422 LEU C CD2 1 
ATOM   8265  N  N   . ILE C 1 359 ? 29.742 56.264 92.695  1.00 60.36  ? 423 ILE C N   1 
ATOM   8266  C  CA  . ILE C 1 359 ? 29.398 57.558 92.149  1.00 53.47  ? 423 ILE C CA  1 
ATOM   8267  C  C   . ILE C 1 359 ? 30.499 58.513 92.571  1.00 48.93  ? 423 ILE C C   1 
ATOM   8268  O  O   . ILE C 1 359 ? 31.031 58.391 93.651  1.00 58.66  ? 423 ILE C O   1 
ATOM   8269  C  CB  . ILE C 1 359 ? 27.981 58.039 92.555  1.00 49.34  ? 423 ILE C CB  1 
ATOM   8270  C  CG1 . ILE C 1 359 ? 27.798 59.527 92.238  1.00 50.75  ? 423 ILE C CG1 1 
ATOM   8271  C  CG2 . ILE C 1 359 ? 27.752 57.854 93.978  1.00 50.75  ? 423 ILE C CG2 1 
ATOM   8272  C  CD1 . ILE C 1 359 ? 26.419 59.862 91.787  1.00 53.35  ? 423 ILE C CD1 1 
ATOM   8273  N  N   . THR C 1 360 ? 30.873 59.422 91.688  1.00 45.96  ? 424 THR C N   1 
ATOM   8274  C  CA  . THR C 1 360 ? 31.926 60.357 91.970  1.00 48.27  ? 424 THR C CA  1 
ATOM   8275  C  C   . THR C 1 360 ? 31.418 61.768 91.740  1.00 51.03  ? 424 THR C C   1 
ATOM   8276  O  O   . THR C 1 360 ? 30.547 61.985 90.896  1.00 65.31  ? 424 THR C O   1 
ATOM   8277  C  CB  . THR C 1 360 ? 33.097 60.105 91.058  1.00 49.77  ? 424 THR C CB  1 
ATOM   8278  O  OG1 . THR C 1 360 ? 32.856 60.759 89.807  1.00 78.70  ? 424 THR C OG1 1 
ATOM   8279  C  CG2 . THR C 1 360 ? 33.232 58.646 90.815  1.00 43.94  ? 424 THR C CG2 1 
ATOM   8280  N  N   . PHE C 1 361 ? 31.967 62.716 92.491  1.00 48.18  ? 425 PHE C N   1 
ATOM   8281  C  CA  . PHE C 1 361 ? 31.587 64.131 92.418  1.00 51.63  ? 425 PHE C CA  1 
ATOM   8282  C  C   . PHE C 1 361 ? 32.820 64.977 92.297  1.00 61.31  ? 425 PHE C C   1 
ATOM   8283  O  O   . PHE C 1 361 ? 33.840 64.705 92.941  1.00 71.28  ? 425 PHE C O   1 
ATOM   8284  C  CB  . PHE C 1 361 ? 30.865 64.579 93.674  1.00 50.01  ? 425 PHE C CB  1 
ATOM   8285  C  CG  . PHE C 1 361 ? 29.528 63.962 93.846  1.00 54.37  ? 425 PHE C CG  1 
ATOM   8286  C  CD1 . PHE C 1 361 ? 29.372 62.776 94.561  1.00 53.78  ? 425 PHE C CD1 1 
ATOM   8287  C  CD2 . PHE C 1 361 ? 28.414 64.568 93.297  1.00 59.08  ? 425 PHE C CD2 1 
ATOM   8288  C  CE1 . PHE C 1 361 ? 28.126 62.195 94.717  1.00 55.90  ? 425 PHE C CE1 1 
ATOM   8289  C  CE2 . PHE C 1 361 ? 27.156 64.002 93.447  1.00 61.53  ? 425 PHE C CE2 1 
ATOM   8290  C  CZ  . PHE C 1 361 ? 27.012 62.811 94.163  1.00 62.59  ? 425 PHE C CZ  1 
ATOM   8291  N  N   . CYS C 1 362 ? 32.739 66.017 91.483  1.00 64.66  ? 426 CYS C N   1 
ATOM   8292  C  CA  . CYS C 1 362 ? 33.839 66.949 91.428  1.00 66.90  ? 426 CYS C CA  1 
ATOM   8293  C  C   . CYS C 1 362 ? 33.372 68.288 91.887  1.00 72.55  ? 426 CYS C C   1 
ATOM   8294  O  O   . CYS C 1 362 ? 32.197 68.608 91.760  1.00 81.01  ? 426 CYS C O   1 
ATOM   8295  C  CB  . CYS C 1 362 ? 34.507 66.969 90.063  1.00 67.34  ? 426 CYS C CB  1 
ATOM   8296  S  SG  . CYS C 1 362 ? 35.352 65.355 89.817  1.00 132.80 ? 426 CYS C SG  1 
ATOM   8297  N  N   . GLY C 1 363 ? 34.290 69.034 92.495  1.00 84.78  ? 427 GLY C N   1 
ATOM   8298  C  CA  . GLY C 1 363 ? 34.011 70.359 93.016  1.00 69.23  ? 427 GLY C CA  1 
ATOM   8299  C  C   . GLY C 1 363 ? 33.971 71.399 91.917  1.00 77.23  ? 427 GLY C C   1 
ATOM   8300  O  O   . GLY C 1 363 ? 34.837 71.431 91.057  1.00 96.67  ? 427 GLY C O   1 
ATOM   8301  N  N   . THR C 1 364 ? 32.943 72.240 91.936  1.00 88.76  ? 428 THR C N   1 
ATOM   8302  C  CA  . THR C 1 364 ? 32.940 73.464 91.146  1.00 91.50  ? 428 THR C CA  1 
ATOM   8303  C  C   . THR C 1 364 ? 33.053 74.726 92.033  1.00 93.37  ? 428 THR C C   1 
ATOM   8304  O  O   . THR C 1 364 ? 32.717 74.693 93.234  1.00 95.81  ? 428 THR C O   1 
ATOM   8305  C  CB  . THR C 1 364 ? 31.726 73.535 90.226  1.00 95.06  ? 428 THR C CB  1 
ATOM   8306  O  OG1 . THR C 1 364 ? 31.864 74.680 89.386  1.00 129.27 ? 428 THR C OG1 1 
ATOM   8307  C  CG2 . THR C 1 364 ? 30.441 73.656 91.023  1.00 99.64  ? 428 THR C CG2 1 
ATOM   8308  N  N   . GLY C 1 365 ? 33.552 75.815 91.436  1.00 92.64  ? 429 GLY C N   1 
ATOM   8309  C  CA  . GLY C 1 365 ? 33.779 77.079 92.144  1.00 97.66  ? 429 GLY C CA  1 
ATOM   8310  C  C   . GLY C 1 365 ? 32.452 77.742 92.451  1.00 111.36 ? 429 GLY C C   1 
ATOM   8311  O  O   . GLY C 1 365 ? 32.301 78.427 93.478  1.00 91.25  ? 429 GLY C O   1 
ATOM   8312  N  N   . GLY C 1 366 ? 31.492 77.514 91.550  1.00 98.66  ? 430 GLY C N   1 
ATOM   8313  C  CA  . GLY C 1 366 ? 30.142 78.050 91.670  1.00 92.27  ? 430 GLY C CA  1 
ATOM   8314  C  C   . GLY C 1 366 ? 29.301 77.386 92.746  1.00 100.15 ? 430 GLY C C   1 
ATOM   8315  O  O   . GLY C 1 366 ? 29.504 76.216 93.094  1.00 95.69  ? 430 GLY C O   1 
ATOM   8316  N  N   . SER C 1 367 ? 28.351 78.140 93.288  1.00 96.06  ? 431 SER C N   1 
ATOM   8317  C  CA  . SER C 1 367 ? 27.391 77.541 94.185  1.00 86.79  ? 431 SER C CA  1 
ATOM   8318  C  C   . SER C 1 367 ? 26.451 76.691 93.338  1.00 81.06  ? 431 SER C C   1 
ATOM   8319  O  O   . SER C 1 367 ? 26.302 76.910 92.144  1.00 79.35  ? 431 SER C O   1 
ATOM   8320  C  CB  . SER C 1 367 ? 26.630 78.601 94.975  1.00 86.72  ? 431 SER C CB  1 
ATOM   8321  O  OG  . SER C 1 367 ? 25.710 77.980 95.855  1.00 84.73  ? 431 SER C OG  1 
ATOM   8322  N  N   . MET C 1 368 ? 25.828 75.708 93.960  1.00 76.86  ? 432 MET C N   1 
ATOM   8323  C  CA  . MET C 1 368 ? 24.966 74.803 93.239  1.00 72.21  ? 432 MET C CA  1 
ATOM   8324  C  C   . MET C 1 368 ? 23.635 74.658 93.940  1.00 74.71  ? 432 MET C C   1 
ATOM   8325  O  O   . MET C 1 368 ? 23.535 74.860 95.157  1.00 82.21  ? 432 MET C O   1 
ATOM   8326  C  CB  . MET C 1 368 ? 25.633 73.440 93.150  1.00 80.71  ? 432 MET C CB  1 
ATOM   8327  C  CG  . MET C 1 368 ? 26.725 73.364 92.111  1.00 95.19  ? 432 MET C CG  1 
ATOM   8328  S  SD  . MET C 1 368 ? 26.084 72.858 90.501  1.00 105.47 ? 432 MET C SD  1 
ATOM   8329  C  CE  . MET C 1 368 ? 25.062 71.455 90.948  1.00 105.17 ? 432 MET C CE  1 
ATOM   8330  N  N   . PRO C 1 369 ? 22.601 74.286 93.180  1.00 73.29  ? 433 PRO C N   1 
ATOM   8331  C  CA  . PRO C 1 369 ? 21.266 74.131 93.722  1.00 83.73  ? 433 PRO C CA  1 
ATOM   8332  C  C   . PRO C 1 369 ? 21.155 72.814 94.486  1.00 84.89  ? 433 PRO C C   1 
ATOM   8333  O  O   . PRO C 1 369 ? 22.032 71.965 94.381  1.00 79.79  ? 433 PRO C O   1 
ATOM   8334  C  CB  . PRO C 1 369 ? 20.395 74.101 92.471  1.00 78.61  ? 433 PRO C CB  1 
ATOM   8335  C  CG  . PRO C 1 369 ? 21.257 73.447 91.482  1.00 71.99  ? 433 PRO C CG  1 
ATOM   8336  C  CD  . PRO C 1 369 ? 22.640 73.954 91.752  1.00 71.40  ? 433 PRO C CD  1 
ATOM   8337  N  N   . ASP C 1 370 ? 20.088 72.673 95.265  1.00 100.66 ? 434 ASP C N   1 
ATOM   8338  C  CA  . ASP C 1 370 ? 19.810 71.458 96.011  1.00 88.41  ? 434 ASP C CA  1 
ATOM   8339  C  C   . ASP C 1 370 ? 19.382 70.384 95.032  1.00 95.51  ? 434 ASP C C   1 
ATOM   8340  O  O   . ASP C 1 370 ? 18.439 70.566 94.247  1.00 105.38 ? 434 ASP C O   1 
ATOM   8341  C  CB  . ASP C 1 370 ? 18.696 71.700 97.028  1.00 123.51 ? 434 ASP C CB  1 
ATOM   8342  C  CG  . ASP C 1 370 ? 19.089 72.695 98.105  1.00 151.95 ? 434 ASP C CG  1 
ATOM   8343  O  OD1 . ASP C 1 370 ? 20.297 72.811 98.399  1.00 176.84 ? 434 ASP C OD1 1 
ATOM   8344  O  OD2 . ASP C 1 370 ? 18.188 73.356 98.662  1.00 133.93 ? 434 ASP C OD2 1 
ATOM   8345  N  N   . VAL C 1 371 ? 20.108 69.272 95.054  1.00 90.65  ? 435 VAL C N   1 
ATOM   8346  C  CA  . VAL C 1 371 ? 19.802 68.139 94.189  1.00 79.90  ? 435 VAL C CA  1 
ATOM   8347  C  C   . VAL C 1 371 ? 19.967 66.796 94.907  1.00 80.75  ? 435 VAL C C   1 
ATOM   8348  O  O   . VAL C 1 371 ? 20.926 66.567 95.644  1.00 66.16  ? 435 VAL C O   1 
ATOM   8349  C  CB  . VAL C 1 371 ? 20.644 68.133 92.894  1.00 67.92  ? 435 VAL C CB  1 
ATOM   8350  C  CG1 . VAL C 1 371 ? 20.115 67.105 91.961  1.00 72.44  ? 435 VAL C CG1 1 
ATOM   8351  C  CG2 . VAL C 1 371 ? 20.621 69.494 92.211  1.00 71.48  ? 435 VAL C CG2 1 
ATOM   8352  N  N   . ASN C 1 372 ? 18.991 65.926 94.692  1.00 78.47  ? 436 ASN C N   1 
ATOM   8353  C  CA  . ASN C 1 372 ? 19.074 64.571 95.130  1.00 78.31  ? 436 ASN C CA  1 
ATOM   8354  C  C   . ASN C 1 372 ? 19.435 63.720 93.907  1.00 71.66  ? 436 ASN C C   1 
ATOM   8355  O  O   . ASN C 1 372 ? 18.623 63.545 93.016  1.00 76.65  ? 436 ASN C O   1 
ATOM   8356  C  CB  . ASN C 1 372 ? 17.731 64.156 95.750  1.00 82.48  ? 436 ASN C CB  1 
ATOM   8357  C  CG  . ASN C 1 372 ? 17.664 62.669 96.072  1.00 109.79 ? 436 ASN C CG  1 
ATOM   8358  O  OD1 . ASN C 1 372 ? 18.559 61.888 95.722  1.00 118.90 ? 436 ASN C OD1 1 
ATOM   8359  N  ND2 . ASN C 1 372 ? 16.591 62.269 96.735  1.00 133.69 ? 436 ASN C ND2 1 
ATOM   8360  N  N   . TRP C 1 373 ? 20.649 63.180 93.864  1.00 70.73  ? 437 TRP C N   1 
ATOM   8361  C  CA  . TRP C 1 373 ? 21.094 62.318 92.721  1.00 70.43  ? 437 TRP C CA  1 
ATOM   8362  C  C   . TRP C 1 373 ? 20.685 60.871 92.767  1.00 60.05  ? 437 TRP C C   1 
ATOM   8363  O  O   . TRP C 1 373 ? 20.307 60.358 93.822  1.00 66.60  ? 437 TRP C O   1 
ATOM   8364  C  CB  . TRP C 1 373 ? 22.606 62.419 92.506  1.00 58.40  ? 437 TRP C CB  1 
ATOM   8365  C  CG  . TRP C 1 373 ? 23.033 63.849 92.290  1.00 59.65  ? 437 TRP C CG  1 
ATOM   8366  C  CD1 . TRP C 1 373 ? 23.406 64.784 93.246  1.00 67.29  ? 437 TRP C CD1 1 
ATOM   8367  C  CD2 . TRP C 1 373 ? 23.058 64.574 91.041  1.00 56.70  ? 437 TRP C CD2 1 
ATOM   8368  N  NE1 . TRP C 1 373 ? 23.677 66.000 92.676  1.00 60.19  ? 437 TRP C NE1 1 
ATOM   8369  C  CE2 . TRP C 1 373 ? 23.493 65.941 91.361  1.00 60.81  ? 437 TRP C CE2 1 
ATOM   8370  C  CE3 . TRP C 1 373 ? 22.763 64.255 89.740  1.00 56.14  ? 437 TRP C CE3 1 
ATOM   8371  C  CZ2 . TRP C 1 373 ? 23.639 66.908 90.393  1.00 67.64  ? 437 TRP C CZ2 1 
ATOM   8372  C  CZ3 . TRP C 1 373 ? 22.910 65.237 88.768  1.00 63.46  ? 437 TRP C CZ3 1 
ATOM   8373  C  CH2 . TRP C 1 373 ? 23.346 66.530 89.086  1.00 67.52  ? 437 TRP C CH2 1 
ATOM   8374  N  N   . ALA D 1 11  ? 53.256 55.410 54.999  1.00 109.34 ? 75  ALA D N   1 
ATOM   8375  C  CA  . ALA D 1 11  ? 52.611 54.327 54.181  1.00 109.02 ? 75  ALA D CA  1 
ATOM   8376  C  C   . ALA D 1 11  ? 53.087 54.346 52.736  1.00 111.73 ? 75  ALA D C   1 
ATOM   8377  O  O   . ALA D 1 11  ? 53.376 55.402 52.175  1.00 120.94 ? 75  ALA D O   1 
ATOM   8378  C  CB  . ALA D 1 11  ? 51.079 54.417 54.240  1.00 90.97  ? 75  ALA D CB  1 
ATOM   8379  N  N   . THR D 1 12  ? 53.149 53.164 52.138  1.00 103.97 ? 76  THR D N   1 
ATOM   8380  C  CA  . THR D 1 12  ? 53.702 53.003 50.808  1.00 115.39 ? 76  THR D CA  1 
ATOM   8381  C  C   . THR D 1 12  ? 52.740 52.172 49.968  1.00 112.85 ? 76  THR D C   1 
ATOM   8382  O  O   . THR D 1 12  ? 52.194 51.183 50.471  1.00 94.28  ? 76  THR D O   1 
ATOM   8383  C  CB  . THR D 1 12  ? 55.086 52.307 50.886  1.00 136.15 ? 76  THR D CB  1 
ATOM   8384  O  OG1 . THR D 1 12  ? 55.967 53.090 51.702  1.00 137.04 ? 76  THR D OG1 1 
ATOM   8385  C  CG2 . THR D 1 12  ? 55.714 52.115 49.493  1.00 150.25 ? 76  THR D CG2 1 
ATOM   8386  N  N   . PRO D 1 13  ? 52.531 52.569 48.687  1.00 115.91 ? 77  PRO D N   1 
ATOM   8387  C  CA  . PRO D 1 13  ? 51.668 51.801 47.781  1.00 110.07 ? 77  PRO D CA  1 
ATOM   8388  C  C   . PRO D 1 13  ? 52.014 50.318 47.825  1.00 123.43 ? 77  PRO D C   1 
ATOM   8389  O  O   . PRO D 1 13  ? 53.189 49.953 47.727  1.00 139.25 ? 77  PRO D O   1 
ATOM   8390  C  CB  . PRO D 1 13  ? 51.997 52.375 46.402  1.00 103.62 ? 77  PRO D CB  1 
ATOM   8391  C  CG  . PRO D 1 13  ? 52.448 53.764 46.672  1.00 115.79 ? 77  PRO D CG  1 
ATOM   8392  C  CD  . PRO D 1 13  ? 53.127 53.741 48.014  1.00 113.41 ? 77  PRO D CD  1 
ATOM   8393  N  N   . LEU D 1 14  ? 50.994 49.479 48.000  1.00 132.73 ? 78  LEU D N   1 
ATOM   8394  C  CA  . LEU D 1 14  ? 51.171 48.034 48.047  1.00 108.81 ? 78  LEU D CA  1 
ATOM   8395  C  C   . LEU D 1 14  ? 51.710 47.500 46.736  1.00 106.14 ? 78  LEU D C   1 
ATOM   8396  O  O   . LEU D 1 14  ? 51.106 47.695 45.676  1.00 119.82 ? 78  LEU D O   1 
ATOM   8397  C  CB  . LEU D 1 14  ? 49.854 47.343 48.353  1.00 115.16 ? 78  LEU D CB  1 
ATOM   8398  C  CG  . LEU D 1 14  ? 49.990 45.828 48.485  1.00 120.27 ? 78  LEU D CG  1 
ATOM   8399  C  CD1 . LEU D 1 14  ? 50.630 45.491 49.813  1.00 114.28 ? 78  LEU D CD1 1 
ATOM   8400  C  CD2 . LEU D 1 14  ? 48.635 45.145 48.343  1.00 123.62 ? 78  LEU D CD2 1 
ATOM   8401  N  N   . VAL D 1 15  ? 52.861 46.844 46.825  1.00 109.84 ? 79  VAL D N   1 
ATOM   8402  C  CA  . VAL D 1 15  ? 53.532 46.248 45.672  1.00 105.51 ? 79  VAL D CA  1 
ATOM   8403  C  C   . VAL D 1 15  ? 53.532 44.754 45.912  1.00 100.44 ? 79  VAL D C   1 
ATOM   8404  O  O   . VAL D 1 15  ? 53.924 44.287 46.986  1.00 118.97 ? 79  VAL D O   1 
ATOM   8405  C  CB  . VAL D 1 15  ? 55.000 46.809 45.470  1.00 100.38 ? 79  VAL D CB  1 
ATOM   8406  C  CG1 . VAL D 1 15  ? 55.967 45.739 44.999  1.00 99.58  ? 79  VAL D CG1 1 
ATOM   8407  C  CG2 . VAL D 1 15  ? 55.023 47.991 44.494  1.00 92.07  ? 79  VAL D CG2 1 
ATOM   8408  N  N   . LEU D 1 16  ? 53.067 44.001 44.926  1.00 93.19  ? 80  LEU D N   1 
ATOM   8409  C  CA  . LEU D 1 16  ? 53.107 42.544 45.030  1.00 92.30  ? 80  LEU D CA  1 
ATOM   8410  C  C   . LEU D 1 16  ? 54.324 41.952 44.327  1.00 83.03  ? 80  LEU D C   1 
ATOM   8411  O  O   . LEU D 1 16  ? 54.856 42.555 43.380  1.00 80.62  ? 80  LEU D O   1 
ATOM   8412  C  CB  . LEU D 1 16  ? 51.830 41.940 44.462  1.00 90.65  ? 80  LEU D CB  1 
ATOM   8413  C  CG  . LEU D 1 16  ? 50.564 42.213 45.261  1.00 80.62  ? 80  LEU D CG  1 
ATOM   8414  C  CD1 . LEU D 1 16  ? 49.334 41.895 44.437  1.00 82.72  ? 80  LEU D CD1 1 
ATOM   8415  C  CD2 . LEU D 1 16  ? 50.589 41.380 46.526  1.00 81.75  ? 80  LEU D CD2 1 
ATOM   8416  N  N   . GLY D 1 17  ? 54.751 40.777 44.793  1.00 69.23  ? 81  GLY D N   1 
ATOM   8417  C  CA  . GLY D 1 17  ? 55.895 40.077 44.207  1.00 77.04  ? 81  GLY D CA  1 
ATOM   8418  C  C   . GLY D 1 17  ? 55.625 39.597 42.792  1.00 79.42  ? 81  GLY D C   1 
ATOM   8419  O  O   . GLY D 1 17  ? 54.560 39.033 42.505  1.00 77.87  ? 81  GLY D O   1 
ATOM   8420  N  N   . GLU D 1 18  ? 56.586 39.820 41.904  1.00 80.09  ? 82  GLU D N   1 
ATOM   8421  C  CA  . GLU D 1 18  ? 56.393 39.484 40.507  1.00 90.55  ? 82  GLU D CA  1 
ATOM   8422  C  C   . GLU D 1 18  ? 56.433 37.972 40.326  1.00 90.76  ? 82  GLU D C   1 
ATOM   8423  O  O   . GLU D 1 18  ? 55.735 37.429 39.473  1.00 97.47  ? 82  GLU D O   1 
ATOM   8424  C  CB  . GLU D 1 18  ? 57.437 40.181 39.627  1.00 97.71  ? 82  GLU D CB  1 
ATOM   8425  C  CG  . GLU D 1 18  ? 56.891 40.696 38.286  1.00 108.85 ? 82  GLU D CG  1 
ATOM   8426  C  CD  . GLU D 1 18  ? 55.929 41.876 38.433  1.00 107.37 ? 82  GLU D CD  1 
ATOM   8427  O  OE1 . GLU D 1 18  ? 56.013 42.621 39.432  1.00 112.19 ? 82  GLU D OE1 1 
ATOM   8428  O  OE2 . GLU D 1 18  ? 55.084 42.063 37.537  1.00 105.10 ? 82  GLU D OE2 1 
ATOM   8429  N  N   . ASN D 1 19  ? 57.231 37.305 41.158  1.00 95.33  ? 83  ASN D N   1 
ATOM   8430  C  CA  . ASN D 1 19  ? 57.431 35.851 41.072  1.00 95.44  ? 83  ASN D CA  1 
ATOM   8431  C  C   . ASN D 1 19  ? 56.749 35.049 42.171  1.00 84.25  ? 83  ASN D C   1 
ATOM   8432  O  O   . ASN D 1 19  ? 56.891 35.352 43.359  1.00 85.91  ? 83  ASN D O   1 
ATOM   8433  C  CB  . ASN D 1 19  ? 58.918 35.531 41.047  1.00 95.65  ? 83  ASN D CB  1 
ATOM   8434  C  CG  . ASN D 1 19  ? 59.584 36.035 39.800  1.00 112.85 ? 83  ASN D CG  1 
ATOM   8435  O  OD1 . ASN D 1 19  ? 58.968 36.095 38.730  1.00 122.12 ? 83  ASN D OD1 1 
ATOM   8436  N  ND2 . ASN D 1 19  ? 60.851 36.408 39.921  1.00 132.52 ? 83  ASN D ND2 1 
ATOM   8437  N  N   . LEU D 1 20  ? 56.019 34.016 41.774  1.00 71.14  ? 84  LEU D N   1 
ATOM   8438  C  CA  . LEU D 1 20  ? 55.248 33.246 42.729  1.00 70.26  ? 84  LEU D CA  1 
ATOM   8439  C  C   . LEU D 1 20  ? 56.113 32.219 43.451  1.00 80.92  ? 84  LEU D C   1 
ATOM   8440  O  O   . LEU D 1 20  ? 57.034 31.636 42.871  1.00 86.96  ? 84  LEU D O   1 
ATOM   8441  C  CB  . LEU D 1 20  ? 54.090 32.557 42.016  1.00 64.94  ? 84  LEU D CB  1 
ATOM   8442  C  CG  . LEU D 1 20  ? 52.730 32.563 42.712  1.00 63.21  ? 84  LEU D CG  1 
ATOM   8443  C  CD1 . LEU D 1 20  ? 52.241 33.975 42.856  1.00 70.74  ? 84  LEU D CD1 1 
ATOM   8444  C  CD2 . LEU D 1 20  ? 51.719 31.762 41.912  1.00 64.85  ? 84  LEU D CD2 1 
ATOM   8445  N  N   . CYS D 1 21  ? 55.814 32.011 44.728  1.00 108.39 ? 85  CYS D N   1 
ATOM   8446  C  CA  . CYS D 1 21  ? 56.379 30.904 45.495  1.00 116.46 ? 85  CYS D CA  1 
ATOM   8447  C  C   . CYS D 1 21  ? 56.072 29.582 44.798  1.00 109.96 ? 85  CYS D C   1 
ATOM   8448  O  O   . CYS D 1 21  ? 54.988 29.420 44.217  1.00 94.65  ? 85  CYS D O   1 
ATOM   8449  C  CB  . CYS D 1 21  ? 55.823 30.909 46.930  1.00 116.58 ? 85  CYS D CB  1 
ATOM   8450  S  SG  . CYS D 1 21  ? 56.631 32.127 47.922  1.00 240.33 ? 85  CYS D SG  1 
ATOM   8451  N  N   . SER D 1 22  ? 57.033 28.657 44.817  1.00 108.32 ? 86  SER D N   1 
ATOM   8452  C  CA  . SER D 1 22  ? 56.760 27.283 44.400  1.00 100.93 ? 86  SER D CA  1 
ATOM   8453  C  C   . SER D 1 22  ? 55.855 26.706 45.452  1.00 87.83  ? 86  SER D C   1 
ATOM   8454  O  O   . SER D 1 22  ? 56.111 26.865 46.651  1.00 83.87  ? 86  SER D O   1 
ATOM   8455  C  CB  . SER D 1 22  ? 58.032 26.443 44.322  1.00 94.77  ? 86  SER D CB  1 
ATOM   8456  O  OG  . SER D 1 22  ? 58.906 26.974 43.352  1.00 126.30 ? 86  SER D OG  1 
ATOM   8457  N  N   . ILE D 1 23  ? 54.775 26.080 45.009  1.00 74.58  ? 87  ILE D N   1 
ATOM   8458  C  CA  . ILE D 1 23  ? 53.837 25.480 45.939  1.00 71.37  ? 87  ILE D CA  1 
ATOM   8459  C  C   . ILE D 1 23  ? 53.836 24.006 45.634  1.00 61.65  ? 87  ILE D C   1 
ATOM   8460  O  O   . ILE D 1 23  ? 53.617 23.622 44.476  1.00 61.63  ? 87  ILE D O   1 
ATOM   8461  C  CB  . ILE D 1 23  ? 52.418 26.117 45.828  1.00 69.40  ? 87  ILE D CB  1 
ATOM   8462  C  CG1 . ILE D 1 23  ? 52.453 27.546 46.361  1.00 70.83  ? 87  ILE D CG1 1 
ATOM   8463  C  CG2 . ILE D 1 23  ? 51.388 25.339 46.647  1.00 57.11  ? 87  ILE D CG2 1 
ATOM   8464  C  CD1 . ILE D 1 23  ? 51.732 28.546 45.499  1.00 70.18  ? 87  ILE D CD1 1 
ATOM   8465  N  N   . ASN D 1 24  ? 54.135 23.195 46.652  1.00 50.63  ? 88  ASN D N   1 
ATOM   8466  C  CA  . ASN D 1 24  ? 53.982 21.754 46.513  1.00 55.36  ? 88  ASN D CA  1 
ATOM   8467  C  C   . ASN D 1 24  ? 52.999 21.162 47.499  1.00 54.50  ? 88  ASN D C   1 
ATOM   8468  O  O   . ASN D 1 24  ? 52.601 20.026 47.378  1.00 54.99  ? 88  ASN D O   1 
ATOM   8469  C  CB  . ASN D 1 24  ? 55.322 21.046 46.562  1.00 57.21  ? 88  ASN D CB  1 
ATOM   8470  C  CG  . ASN D 1 24  ? 56.166 21.369 45.364  1.00 66.97  ? 88  ASN D CG  1 
ATOM   8471  O  OD1 . ASN D 1 24  ? 55.957 20.817 44.304  1.00 72.66  ? 88  ASN D OD1 1 
ATOM   8472  N  ND2 . ASN D 1 24  ? 57.119 22.287 45.519  1.00 98.00  ? 88  ASN D ND2 1 
ATOM   8473  N  N   . GLY D 1 25  ? 52.578 21.955 48.466  1.00 60.23  ? 89  GLY D N   1 
ATOM   8474  C  CA  . GLY D 1 25  ? 51.679 21.464 49.499  1.00 57.75  ? 89  GLY D CA  1 
ATOM   8475  C  C   . GLY D 1 25  ? 50.866 22.562 50.140  1.00 58.82  ? 89  GLY D C   1 
ATOM   8476  O  O   . GLY D 1 25  ? 50.980 23.733 49.789  1.00 62.64  ? 89  GLY D O   1 
ATOM   8477  N  N   . TRP D 1 26  ? 50.002 22.187 51.066  1.00 59.10  ? 90  TRP D N   1 
ATOM   8478  C  CA  . TRP D 1 26  ? 49.160 23.183 51.685  1.00 55.53  ? 90  TRP D CA  1 
ATOM   8479  C  C   . TRP D 1 26  ? 49.073 22.939 53.156  1.00 62.24  ? 90  TRP D C   1 
ATOM   8480  O  O   . TRP D 1 26  ? 48.914 21.783 53.600  1.00 57.19  ? 90  TRP D O   1 
ATOM   8481  C  CB  . TRP D 1 26  ? 47.782 23.196 51.034  1.00 58.13  ? 90  TRP D CB  1 
ATOM   8482  C  CG  . TRP D 1 26  ? 47.834 23.496 49.551  1.00 57.15  ? 90  TRP D CG  1 
ATOM   8483  C  CD1 . TRP D 1 26  ? 47.868 22.584 48.523  1.00 55.77  ? 90  TRP D CD1 1 
ATOM   8484  C  CD2 . TRP D 1 26  ? 47.888 24.813 48.890  1.00 57.30  ? 90  TRP D CD2 1 
ATOM   8485  N  NE1 . TRP D 1 26  ? 47.937 23.215 47.316  1.00 60.91  ? 90  TRP D NE1 1 
ATOM   8486  C  CE2 . TRP D 1 26  ? 47.951 24.548 47.467  1.00 58.83  ? 90  TRP D CE2 1 
ATOM   8487  C  CE3 . TRP D 1 26  ? 47.901 26.125 49.326  1.00 52.47  ? 90  TRP D CE3 1 
ATOM   8488  C  CZ2 . TRP D 1 26  ? 48.011 25.563 46.533  1.00 61.71  ? 90  TRP D CZ2 1 
ATOM   8489  C  CZ3 . TRP D 1 26  ? 47.955 27.138 48.371  1.00 53.59  ? 90  TRP D CZ3 1 
ATOM   8490  C  CH2 . TRP D 1 26  ? 48.018 26.864 47.011  1.00 50.28  ? 90  TRP D CH2 1 
ATOM   8491  N  N   . VAL D 1 27  ? 49.233 24.018 53.928  1.00 55.69  ? 91  VAL D N   1 
ATOM   8492  C  CA  . VAL D 1 27  ? 48.964 23.946 55.345  1.00 54.84  ? 91  VAL D CA  1 
ATOM   8493  C  C   . VAL D 1 27  ? 47.939 24.997 55.777  1.00 49.34  ? 91  VAL D C   1 
ATOM   8494  O  O   . VAL D 1 27  ? 47.947 26.108 55.259  1.00 39.89  ? 91  VAL D O   1 
ATOM   8495  C  CB  . VAL D 1 27  ? 50.232 23.972 56.171  1.00 53.15  ? 91  VAL D CB  1 
ATOM   8496  C  CG1 . VAL D 1 27  ? 51.378 23.408 55.355  1.00 60.21  ? 91  VAL D CG1 1 
ATOM   8497  C  CG2 . VAL D 1 27  ? 50.530 25.366 56.602  1.00 65.45  ? 91  VAL D CG2 1 
ATOM   8498  N  N   . PRO D 1 28  ? 47.014 24.604 56.681  1.00 49.52  ? 92  PRO D N   1 
ATOM   8499  C  CA  . PRO D 1 28  ? 46.018 25.518 57.190  1.00 45.47  ? 92  PRO D CA  1 
ATOM   8500  C  C   . PRO D 1 28  ? 46.646 26.556 58.075  1.00 43.99  ? 92  PRO D C   1 
ATOM   8501  O  O   . PRO D 1 28  ? 47.516 26.237 58.876  1.00 45.73  ? 92  PRO D O   1 
ATOM   8502  C  CB  . PRO D 1 28  ? 45.078 24.601 57.994  1.00 40.13  ? 92  PRO D CB  1 
ATOM   8503  C  CG  . PRO D 1 28  ? 45.834 23.392 58.262  1.00 39.27  ? 92  PRO D CG  1 
ATOM   8504  C  CD  . PRO D 1 28  ? 46.752 23.218 57.129  1.00 42.36  ? 92  PRO D CD  1 
ATOM   8505  N  N   . THR D 1 29  ? 46.209 27.797 57.940  1.00 46.51  ? 93  THR D N   1 
ATOM   8506  C  CA  . THR D 1 29  ? 46.815 28.864 58.731  1.00 50.92  ? 93  THR D CA  1 
ATOM   8507  C  C   . THR D 1 29  ? 45.789 29.375 59.681  1.00 42.85  ? 93  THR D C   1 
ATOM   8508  O  O   . THR D 1 29  ? 46.110 30.051 60.637  1.00 46.20  ? 93  THR D O   1 
ATOM   8509  C  CB  . THR D 1 29  ? 47.404 30.040 57.864  1.00 53.53  ? 93  THR D CB  1 
ATOM   8510  O  OG1 . THR D 1 29  ? 46.519 30.364 56.796  1.00 67.89  ? 93  THR D OG1 1 
ATOM   8511  C  CG2 . THR D 1 29  ? 48.724 29.653 57.233  1.00 50.97  ? 93  THR D CG2 1 
ATOM   8512  N  N   . TYR D 1 30  ? 44.542 29.045 59.409  1.00 43.69  ? 94  TYR D N   1 
ATOM   8513  C  CA  . TYR D 1 30  ? 43.424 29.524 60.231  1.00 44.97  ? 94  TYR D CA  1 
ATOM   8514  C  C   . TYR D 1 30  ? 42.212 28.615 60.093  1.00 47.15  ? 94  TYR D C   1 
ATOM   8515  O  O   . TYR D 1 30  ? 41.953 28.021 59.037  1.00 58.29  ? 94  TYR D O   1 
ATOM   8516  C  CB  . TYR D 1 30  ? 43.023 30.970 59.894  1.00 40.07  ? 94  TYR D CB  1 
ATOM   8517  C  CG  . TYR D 1 30  ? 41.730 31.396 60.583  1.00 47.29  ? 94  TYR D CG  1 
ATOM   8518  C  CD1 . TYR D 1 30  ? 41.725 31.806 61.898  1.00 49.62  ? 94  TYR D CD1 1 
ATOM   8519  C  CD2 . TYR D 1 30  ? 40.512 31.341 59.934  1.00 48.55  ? 94  TYR D CD2 1 
ATOM   8520  C  CE1 . TYR D 1 30  ? 40.559 32.166 62.528  1.00 48.86  ? 94  TYR D CE1 1 
ATOM   8521  C  CE2 . TYR D 1 30  ? 39.329 31.706 60.575  1.00 53.82  ? 94  TYR D CE2 1 
ATOM   8522  C  CZ  . TYR D 1 30  ? 39.364 32.122 61.874  1.00 51.36  ? 94  TYR D CZ  1 
ATOM   8523  O  OH  . TYR D 1 30  ? 38.212 32.520 62.535  1.00 61.91  ? 94  TYR D OH  1 
ATOM   8524  N  N   . ARG D 1 31  ? 41.468 28.513 61.177  1.00 43.75  ? 95  ARG D N   1 
ATOM   8525  C  CA  . ARG D 1 31  ? 40.293 27.689 61.194  1.00 46.81  ? 95  ARG D CA  1 
ATOM   8526  C  C   . ARG D 1 31  ? 39.310 28.317 62.175  1.00 45.30  ? 95  ARG D C   1 
ATOM   8527  O  O   . ARG D 1 31  ? 39.624 28.540 63.324  1.00 40.67  ? 95  ARG D O   1 
ATOM   8528  C  CB  . ARG D 1 31  ? 40.695 26.271 61.572  1.00 48.37  ? 95  ARG D CB  1 
ATOM   8529  C  CG  . ARG D 1 31  ? 39.571 25.355 61.865  1.00 65.17  ? 95  ARG D CG  1 
ATOM   8530  C  CD  . ARG D 1 31  ? 40.074 23.943 61.804  1.00 80.36  ? 95  ARG D CD  1 
ATOM   8531  N  NE  . ARG D 1 31  ? 40.989 23.694 62.902  1.00 67.78  ? 95  ARG D NE  1 
ATOM   8532  C  CZ  . ARG D 1 31  ? 41.367 22.490 63.283  1.00 60.19  ? 95  ARG D CZ  1 
ATOM   8533  N  NH1 . ARG D 1 31  ? 40.924 21.427 62.648  1.00 63.10  ? 95  ARG D NH1 1 
ATOM   8534  N  NH2 . ARG D 1 31  ? 42.178 22.355 64.311  1.00 93.22  ? 95  ARG D NH2 1 
ATOM   8535  N  N   . GLY D 1 32  ? 38.133 28.662 61.693  1.00 50.34  ? 96  GLY D N   1 
ATOM   8536  C  CA  . GLY D 1 32  ? 37.112 29.196 62.565  1.00 54.75  ? 96  GLY D CA  1 
ATOM   8537  C  C   . GLY D 1 32  ? 36.610 28.140 63.527  1.00 56.32  ? 96  GLY D C   1 
ATOM   8538  O  O   . GLY D 1 32  ? 36.743 26.941 63.299  1.00 62.66  ? 96  GLY D O   1 
ATOM   8539  N  N   . GLU D 1 33  ? 36.018 28.592 64.613  1.00 62.41  ? 97  GLU D N   1 
ATOM   8540  C  CA  . GLU D 1 33  ? 35.562 27.671 65.625  1.00 74.53  ? 97  GLU D CA  1 
ATOM   8541  C  C   . GLU D 1 33  ? 34.286 26.927 65.214  1.00 71.87  ? 97  GLU D C   1 
ATOM   8542  O  O   . GLU D 1 33  ? 33.967 25.876 65.774  1.00 82.15  ? 97  GLU D O   1 
ATOM   8543  C  CB  . GLU D 1 33  ? 35.400 28.390 66.966  1.00 84.63  ? 97  GLU D CB  1 
ATOM   8544  C  CG  . GLU D 1 33  ? 35.764 27.517 68.178  1.00 120.01 ? 97  GLU D CG  1 
ATOM   8545  C  CD  . GLU D 1 33  ? 37.251 27.131 68.247  1.00 130.22 ? 97  GLU D CD  1 
ATOM   8546  O  OE1 . GLU D 1 33  ? 38.110 27.954 67.875  1.00 176.47 ? 97  GLU D OE1 1 
ATOM   8547  O  OE2 . GLU D 1 33  ? 37.568 26.007 68.691  1.00 110.25 ? 97  GLU D OE2 1 
ATOM   8548  N  N   . GLY D 1 34  ? 33.570 27.454 64.229  1.00 56.60  ? 98  GLY D N   1 
ATOM   8549  C  CA  . GLY D 1 34  ? 32.409 26.745 63.708  1.00 62.12  ? 98  GLY D CA  1 
ATOM   8550  C  C   . GLY D 1 34  ? 32.738 25.645 62.716  1.00 58.87  ? 98  GLY D C   1 
ATOM   8551  O  O   . GLY D 1 34  ? 31.831 24.974 62.221  1.00 69.94  ? 98  GLY D O   1 
ATOM   8552  N  N   . THR D 1 35  ? 34.026 25.455 62.427  1.00 53.03  ? 99  THR D N   1 
ATOM   8553  C  CA  . THR D 1 35  ? 34.449 24.438 61.470  1.00 63.92  ? 99  THR D CA  1 
ATOM   8554  C  C   . THR D 1 35  ? 34.544 23.090 62.160  1.00 70.48  ? 99  THR D C   1 
ATOM   8555  O  O   . THR D 1 35  ? 34.734 22.064 61.518  1.00 97.24  ? 99  THR D O   1 
ATOM   8556  C  CB  . THR D 1 35  ? 35.822 24.751 60.882  1.00 65.40  ? 99  THR D CB  1 
ATOM   8557  O  OG1 . THR D 1 35  ? 36.778 24.757 61.943  1.00 84.01  ? 99  THR D OG1 1 
ATOM   8558  C  CG2 . THR D 1 35  ? 35.832 26.104 60.193  1.00 68.43  ? 99  THR D CG2 1 
ATOM   8559  N  N   . THR D 1 36  ? 34.425 23.109 63.480  1.00 71.93  ? 100 THR D N   1 
ATOM   8560  C  CA  . THR D 1 36  ? 34.610 21.915 64.291  1.00 86.40  ? 100 THR D CA  1 
ATOM   8561  C  C   . THR D 1 36  ? 33.411 21.769 65.221  1.00 83.30  ? 100 THR D C   1 
ATOM   8562  O  O   . THR D 1 36  ? 32.636 20.822 65.083  1.00 103.91 ? 100 THR D O   1 
ATOM   8563  C  CB  . THR D 1 36  ? 35.956 21.955 65.088  1.00 101.47 ? 100 THR D CB  1 
ATOM   8564  O  OG1 . THR D 1 36  ? 36.113 23.233 65.717  1.00 120.37 ? 100 THR D OG1 1 
ATOM   8565  C  CG2 . THR D 1 36  ? 37.155 21.716 64.167  1.00 71.45  ? 100 THR D CG2 1 
ATOM   8566  N  N   . GLY D 1 37  ? 33.250 22.721 66.140  1.00 70.65  ? 101 GLY D N   1 
ATOM   8567  C  CA  . GLY D 1 37  ? 32.085 22.767 67.021  1.00 80.96  ? 101 GLY D CA  1 
ATOM   8568  C  C   . GLY D 1 37  ? 30.938 23.619 66.491  1.00 87.22  ? 101 GLY D C   1 
ATOM   8569  O  O   . GLY D 1 37  ? 30.914 23.997 65.318  1.00 104.22 ? 101 GLY D O   1 
ATOM   8570  N  N   . LYS D 1 38  ? 29.984 23.913 67.371  1.00 76.58  ? 102 LYS D N   1 
ATOM   8571  C  CA  . LYS D 1 38  ? 28.861 24.780 67.057  1.00 77.29  ? 102 LYS D CA  1 
ATOM   8572  C  C   . LYS D 1 38  ? 29.194 26.249 67.372  1.00 77.49  ? 102 LYS D C   1 
ATOM   8573  O  O   . LYS D 1 38  ? 30.137 26.538 68.094  1.00 79.81  ? 102 LYS D O   1 
ATOM   8574  C  CB  . LYS D 1 38  ? 27.622 24.325 67.823  1.00 74.16  ? 102 LYS D CB  1 
ATOM   8575  C  CG  . LYS D 1 38  ? 27.035 23.028 67.308  1.00 104.27 ? 102 LYS D CG  1 
ATOM   8576  C  CD  . LYS D 1 38  ? 25.606 22.883 67.783  1.00 123.06 ? 102 LYS D CD  1 
ATOM   8577  C  CE  . LYS D 1 38  ? 24.804 21.975 66.872  1.00 136.21 ? 102 LYS D CE  1 
ATOM   8578  N  NZ  . LYS D 1 38  ? 23.347 22.154 67.135  1.00 134.80 ? 102 LYS D NZ  1 
ATOM   8579  N  N   . ILE D 1 39  ? 28.418 27.172 66.822  1.00 73.21  ? 103 ILE D N   1 
ATOM   8580  C  CA  . ILE D 1 39  ? 28.682 28.589 66.982  1.00 56.73  ? 103 ILE D CA  1 
ATOM   8581  C  C   . ILE D 1 39  ? 27.812 29.107 68.122  1.00 65.30  ? 103 ILE D C   1 
ATOM   8582  O  O   . ILE D 1 39  ? 26.614 28.820 68.173  1.00 66.51  ? 103 ILE D O   1 
ATOM   8583  C  CB  . ILE D 1 39  ? 28.304 29.380 65.696  1.00 61.02  ? 103 ILE D CB  1 
ATOM   8584  C  CG1 . ILE D 1 39  ? 28.817 28.680 64.431  1.00 51.41  ? 103 ILE D CG1 1 
ATOM   8585  C  CG2 . ILE D 1 39  ? 28.733 30.839 65.774  1.00 57.81  ? 103 ILE D CG2 1 
ATOM   8586  C  CD1 . ILE D 1 39  ? 30.020 29.224 63.876  1.00 40.01  ? 103 ILE D CD1 1 
ATOM   8587  N  N   . PRO D 1 40  ? 28.410 29.891 69.034  1.00 62.99  ? 104 PRO D N   1 
ATOM   8588  C  CA  . PRO D 1 40  ? 27.700 30.621 70.090  1.00 61.61  ? 104 PRO D CA  1 
ATOM   8589  C  C   . PRO D 1 40  ? 26.642 31.549 69.507  1.00 61.93  ? 104 PRO D C   1 
ATOM   8590  O  O   . PRO D 1 40  ? 26.852 32.188 68.464  1.00 67.27  ? 104 PRO D O   1 
ATOM   8591  C  CB  . PRO D 1 40  ? 28.808 31.440 70.750  1.00 55.74  ? 104 PRO D CB  1 
ATOM   8592  C  CG  . PRO D 1 40  ? 30.052 30.718 70.436  1.00 54.48  ? 104 PRO D CG  1 
ATOM   8593  C  CD  . PRO D 1 40  ? 29.860 30.124 69.088  1.00 55.75  ? 104 PRO D CD  1 
ATOM   8594  N  N   . ASP D 1 41  ? 25.514 31.626 70.184  1.00 63.57  ? 105 ASP D N   1 
ATOM   8595  C  CA  . ASP D 1 41  ? 24.360 32.321 69.632  1.00 80.28  ? 105 ASP D CA  1 
ATOM   8596  C  C   . ASP D 1 41  ? 24.571 33.814 69.483  1.00 84.49  ? 105 ASP D C   1 
ATOM   8597  O  O   . ASP D 1 41  ? 23.955 34.444 68.619  1.00 82.86  ? 105 ASP D O   1 
ATOM   8598  C  CB  . ASP D 1 41  ? 23.119 32.033 70.478  1.00 107.29 ? 105 ASP D CB  1 
ATOM   8599  C  CG  . ASP D 1 41  ? 22.828 30.552 70.582  1.00 133.48 ? 105 ASP D CG  1 
ATOM   8600  O  OD1 . ASP D 1 41  ? 23.782 29.772 70.421  1.00 207.66 ? 105 ASP D OD1 1 
ATOM   8601  O  OD2 . ASP D 1 41  ? 21.666 30.156 70.812  1.00 133.54 ? 105 ASP D OD2 1 
ATOM   8602  N  N   . GLU D 1 42  ? 25.449 34.371 70.317  1.00 91.71  ? 106 GLU D N   1 
ATOM   8603  C  CA  . GLU D 1 42  ? 25.698 35.809 70.312  1.00 92.08  ? 106 GLU D CA  1 
ATOM   8604  C  C   . GLU D 1 42  ? 26.490 36.281 69.097  1.00 81.03  ? 106 GLU D C   1 
ATOM   8605  O  O   . GLU D 1 42  ? 26.481 37.467 68.782  1.00 114.31 ? 106 GLU D O   1 
ATOM   8606  C  CB  . GLU D 1 42  ? 26.361 36.290 71.614  1.00 102.70 ? 106 GLU D CB  1 
ATOM   8607  C  CG  . GLU D 1 42  ? 27.778 35.812 71.852  1.00 114.07 ? 106 GLU D CG  1 
ATOM   8608  C  CD  . GLU D 1 42  ? 27.845 34.735 72.916  1.00 172.75 ? 106 GLU D CD  1 
ATOM   8609  O  OE1 . GLU D 1 42  ? 27.051 33.766 72.845  1.00 182.14 ? 106 GLU D OE1 1 
ATOM   8610  O  OE2 . GLU D 1 42  ? 28.697 34.862 73.825  1.00 241.74 ? 106 GLU D OE2 1 
ATOM   8611  N  N   . GLN D 1 43  ? 27.172 35.366 68.420  1.00 72.74  ? 107 GLN D N   1 
ATOM   8612  C  CA  . GLN D 1 43  ? 27.940 35.741 67.242  1.00 75.82  ? 107 GLN D CA  1 
ATOM   8613  C  C   . GLN D 1 43  ? 27.023 36.207 66.114  1.00 85.41  ? 107 GLN D C   1 
ATOM   8614  O  O   . GLN D 1 43  ? 25.852 35.813 66.035  1.00 91.61  ? 107 GLN D O   1 
ATOM   8615  C  CB  . GLN D 1 43  ? 28.832 34.604 66.772  1.00 63.60  ? 107 GLN D CB  1 
ATOM   8616  C  CG  . GLN D 1 43  ? 30.040 34.380 67.668  1.00 86.33  ? 107 GLN D CG  1 
ATOM   8617  C  CD  . GLN D 1 43  ? 31.177 33.598 66.975  1.00 102.20 ? 107 GLN D CD  1 
ATOM   8618  O  OE1 . GLN D 1 43  ? 31.287 33.589 65.745  1.00 92.83  ? 107 GLN D OE1 1 
ATOM   8619  N  NE2 . GLN D 1 43  ? 32.030 32.949 67.772  1.00 92.67  ? 107 GLN D NE2 1 
ATOM   8620  N  N   . MET D 1 44  ? 27.562 37.075 65.268  1.00 65.51  ? 108 MET D N   1 
ATOM   8621  C  CA  . MET D 1 44  ? 26.881 37.521 64.085  1.00 55.93  ? 108 MET D CA  1 
ATOM   8622  C  C   . MET D 1 44  ? 26.855 36.326 63.112  1.00 63.10  ? 108 MET D C   1 
ATOM   8623  O  O   . MET D 1 44  ? 27.860 35.635 62.973  1.00 71.56  ? 108 MET D O   1 
ATOM   8624  C  CB  . MET D 1 44  ? 27.669 38.698 63.515  1.00 51.09  ? 108 MET D CB  1 
ATOM   8625  C  CG  . MET D 1 44  ? 27.135 39.318 62.243  1.00 59.95  ? 108 MET D CG  1 
ATOM   8626  S  SD  . MET D 1 44  ? 25.591 40.145 62.567  1.00 85.32  ? 108 MET D SD  1 
ATOM   8627  C  CE  . MET D 1 44  ? 26.092 41.806 63.002  1.00 83.36  ? 108 MET D CE  1 
ATOM   8628  N  N   . LEU D 1 45  ? 25.709 36.054 62.483  1.00 64.89  ? 109 LEU D N   1 
ATOM   8629  C  CA  . LEU D 1 45  ? 25.641 35.049 61.409  1.00 66.76  ? 109 LEU D CA  1 
ATOM   8630  C  C   . LEU D 1 45  ? 26.297 35.617 60.146  1.00 72.40  ? 109 LEU D C   1 
ATOM   8631  O  O   . LEU D 1 45  ? 25.950 36.719 59.711  1.00 83.94  ? 109 LEU D O   1 
ATOM   8632  C  CB  . LEU D 1 45  ? 24.193 34.664 61.100  1.00 51.36  ? 109 LEU D CB  1 
ATOM   8633  C  CG  . LEU D 1 45  ? 23.353 34.111 62.239  1.00 58.44  ? 109 LEU D CG  1 
ATOM   8634  C  CD1 . LEU D 1 45  ? 21.875 34.133 61.878  1.00 60.66  ? 109 LEU D CD1 1 
ATOM   8635  C  CD2 . LEU D 1 45  ? 23.813 32.709 62.571  1.00 51.55  ? 109 LEU D CD2 1 
ATOM   8636  N  N   . THR D 1 46  ? 27.222 34.872 59.546  1.00 58.64  ? 110 THR D N   1 
ATOM   8637  C  CA  . THR D 1 46  ? 27.898 35.366 58.351  1.00 63.68  ? 110 THR D CA  1 
ATOM   8638  C  C   . THR D 1 46  ? 27.561 34.601 57.072  1.00 73.67  ? 110 THR D C   1 
ATOM   8639  O  O   . THR D 1 46  ? 27.170 33.432 57.103  1.00 75.38  ? 110 THR D O   1 
ATOM   8640  C  CB  . THR D 1 46  ? 29.397 35.330 58.506  1.00 59.90  ? 110 THR D CB  1 
ATOM   8641  O  OG1 . THR D 1 46  ? 29.814 33.964 58.552  1.00 65.45  ? 110 THR D OG1 1 
ATOM   8642  C  CG2 . THR D 1 46  ? 29.798 35.998 59.784  1.00 64.54  ? 110 THR D CG2 1 
ATOM   8643  N  N   . ARG D 1 47  ? 27.707 35.293 55.947  1.00 74.26  ? 111 ARG D N   1 
ATOM   8644  C  CA  . ARG D 1 47  ? 27.605 34.679 54.639  1.00 54.04  ? 111 ARG D CA  1 
ATOM   8645  C  C   . ARG D 1 47  ? 28.472 35.494 53.692  1.00 50.71  ? 111 ARG D C   1 
ATOM   8646  O  O   . ARG D 1 47  ? 28.784 36.652 53.968  1.00 56.48  ? 111 ARG D O   1 
ATOM   8647  C  CB  . ARG D 1 47  ? 26.156 34.598 54.173  1.00 46.55  ? 111 ARG D CB  1 
ATOM   8648  C  CG  . ARG D 1 47  ? 25.650 35.772 53.373  1.00 52.57  ? 111 ARG D CG  1 
ATOM   8649  C  CD  . ARG D 1 47  ? 24.476 35.377 52.452  1.00 54.01  ? 111 ARG D CD  1 
ATOM   8650  N  NE  . ARG D 1 47  ? 24.142 36.465 51.528  1.00 70.22  ? 111 ARG D NE  1 
ATOM   8651  C  CZ  . ARG D 1 47  ? 24.795 36.722 50.389  1.00 94.66  ? 111 ARG D CZ  1 
ATOM   8652  N  NH1 . ARG D 1 47  ? 25.820 35.970 50.009  1.00 110.82 ? 111 ARG D NH1 1 
ATOM   8653  N  NH2 . ARG D 1 47  ? 24.426 37.735 49.616  1.00 98.03  ? 111 ARG D NH2 1 
ATOM   8654  N  N   . GLN D 1 48  ? 28.871 34.877 52.591  1.00 43.16  ? 112 GLN D N   1 
ATOM   8655  C  CA  . GLN D 1 48  ? 29.737 35.518 51.618  1.00 41.49  ? 112 GLN D CA  1 
ATOM   8656  C  C   . GLN D 1 48  ? 31.080 35.961 52.226  1.00 42.22  ? 112 GLN D C   1 
ATOM   8657  O  O   . GLN D 1 48  ? 31.673 36.949 51.800  1.00 43.23  ? 112 GLN D O   1 
ATOM   8658  C  CB  . GLN D 1 48  ? 29.048 36.665 50.898  1.00 38.88  ? 112 GLN D CB  1 
ATOM   8659  C  CG  . GLN D 1 48  ? 30.019 37.780 50.624  1.00 45.81  ? 112 GLN D CG  1 
ATOM   8660  C  CD  . GLN D 1 48  ? 29.955 38.302 49.236  1.00 63.74  ? 112 GLN D CD  1 
ATOM   8661  O  OE1 . GLN D 1 48  ? 30.748 39.322 48.979  1.00 80.90  ? 112 GLN D OE1 1 
ATOM   8662  N  NE2 . GLN D 1 48  ? 29.200 37.813 48.390  1.00 71.32  ? 112 GLN D NE2 1 
ATOM   8663  N  N   . ASN D 1 49  ? 31.565 35.209 53.201  1.00 41.91  ? 113 ASN D N   1 
ATOM   8664  C  CA  . ASN D 1 49  ? 32.930 35.337 53.693  1.00 42.85  ? 113 ASN D CA  1 
ATOM   8665  C  C   . ASN D 1 49  ? 34.027 35.310 52.634  1.00 46.45  ? 113 ASN D C   1 
ATOM   8666  O  O   . ASN D 1 49  ? 34.014 34.501 51.712  1.00 57.93  ? 113 ASN D O   1 
ATOM   8667  C  CB  . ASN D 1 49  ? 33.228 34.177 54.638  1.00 46.41  ? 113 ASN D CB  1 
ATOM   8668  C  CG  . ASN D 1 49  ? 32.342 34.176 55.867  1.00 53.92  ? 113 ASN D CG  1 
ATOM   8669  O  OD1 . ASN D 1 49  ? 32.775 34.629 56.939  1.00 47.06  ? 113 ASN D OD1 1 
ATOM   8670  N  ND2 . ASN D 1 49  ? 31.090 33.664 55.728  1.00 50.45  ? 113 ASN D ND2 1 
ATOM   8671  N  N   . PHE D 1 50  ? 35.007 36.177 52.791  1.00 48.65  ? 114 PHE D N   1 
ATOM   8672  C  CA  . PHE D 1 50  ? 36.231 36.036 52.051  1.00 46.22  ? 114 PHE D CA  1 
ATOM   8673  C  C   . PHE D 1 50  ? 37.360 36.662 52.810  1.00 40.56  ? 114 PHE D C   1 
ATOM   8674  O  O   . PHE D 1 50  ? 37.181 37.175 53.892  1.00 45.63  ? 114 PHE D O   1 
ATOM   8675  C  CB  . PHE D 1 50  ? 36.086 36.630 50.636  1.00 68.15  ? 114 PHE D CB  1 
ATOM   8676  C  CG  . PHE D 1 50  ? 35.844 38.119 50.587  1.00 63.10  ? 114 PHE D CG  1 
ATOM   8677  C  CD1 . PHE D 1 50  ? 34.566 38.627 50.601  1.00 63.40  ? 114 PHE D CD1 1 
ATOM   8678  C  CD2 . PHE D 1 50  ? 36.908 39.006 50.462  1.00 73.70  ? 114 PHE D CD2 1 
ATOM   8679  C  CE1 . PHE D 1 50  ? 34.343 39.995 50.526  1.00 62.98  ? 114 PHE D CE1 1 
ATOM   8680  C  CE2 . PHE D 1 50  ? 36.694 40.374 50.385  1.00 76.55  ? 114 PHE D CE2 1 
ATOM   8681  C  CZ  . PHE D 1 50  ? 35.403 40.865 50.417  1.00 60.72  ? 114 PHE D CZ  1 
ATOM   8682  N  N   . VAL D 1 51  ? 38.545 36.636 52.244  1.00 37.65  ? 115 VAL D N   1 
ATOM   8683  C  CA  . VAL D 1 51  ? 39.694 37.182 52.950  1.00 36.02  ? 115 VAL D CA  1 
ATOM   8684  C  C   . VAL D 1 51  ? 40.458 38.059 52.004  1.00 41.00  ? 115 VAL D C   1 
ATOM   8685  O  O   . VAL D 1 51  ? 40.547 37.784 50.797  1.00 51.55  ? 115 VAL D O   1 
ATOM   8686  C  CB  . VAL D 1 51  ? 40.627 36.060 53.446  1.00 34.75  ? 115 VAL D CB  1 
ATOM   8687  C  CG1 . VAL D 1 51  ? 41.951 36.598 53.978  1.00 31.67  ? 115 VAL D CG1 1 
ATOM   8688  C  CG2 . VAL D 1 51  ? 39.928 35.210 54.472  1.00 33.25  ? 115 VAL D CG2 1 
ATOM   8689  N  N   . SER D 1 52  ? 41.022 39.118 52.554  1.00 46.04  ? 116 SER D N   1 
ATOM   8690  C  CA  . SER D 1 52  ? 41.733 40.127 51.769  1.00 56.35  ? 116 SER D CA  1 
ATOM   8691  C  C   . SER D 1 52  ? 42.759 40.686 52.688  1.00 49.81  ? 116 SER D C   1 
ATOM   8692  O  O   . SER D 1 52  ? 42.455 40.936 53.838  1.00 44.46  ? 116 SER D O   1 
ATOM   8693  C  CB  . SER D 1 52  ? 40.802 41.259 51.308  1.00 55.69  ? 116 SER D CB  1 
ATOM   8694  O  OG  . SER D 1 52  ? 41.537 42.220 50.586  1.00 69.76  ? 116 SER D OG  1 
ATOM   8695  N  N   . CYS D 1 53  ? 43.977 40.867 52.200  1.00 58.41  ? 117 CYS D N   1 
ATOM   8696  C  CA  . CYS D 1 53  ? 45.037 41.283 53.100  1.00 70.81  ? 117 CYS D CA  1 
ATOM   8697  C  C   . CYS D 1 53  ? 45.526 42.684 52.829  1.00 69.27  ? 117 CYS D C   1 
ATOM   8698  O  O   . CYS D 1 53  ? 45.575 43.121 51.680  1.00 84.29  ? 117 CYS D O   1 
ATOM   8699  C  CB  . CYS D 1 53  ? 46.191 40.273 53.100  1.00 77.01  ? 117 CYS D CB  1 
ATOM   8700  S  SG  . CYS D 1 53  ? 45.622 38.649 53.622  1.00 95.15  ? 117 CYS D SG  1 
ATOM   8701  N  N   . SER D 1 54  ? 45.850 43.389 53.912  1.00 69.00  ? 118 SER D N   1 
ATOM   8702  C  CA  . SER D 1 54  ? 46.645 44.616 53.847  1.00 72.63  ? 118 SER D CA  1 
ATOM   8703  C  C   . SER D 1 54  ? 48.115 44.240 54.067  1.00 74.53  ? 118 SER D C   1 
ATOM   8704  O  O   . SER D 1 54  ? 48.464 43.049 54.078  1.00 73.46  ? 118 SER D O   1 
ATOM   8705  C  CB  . SER D 1 54  ? 46.144 45.683 54.848  1.00 66.86  ? 118 SER D CB  1 
ATOM   8706  O  OG  . SER D 1 54  ? 46.670 45.510 56.151  1.00 68.71  ? 118 SER D OG  1 
ATOM   8707  N  N   . ASP D 1 55  ? 48.972 45.249 54.208  1.00 89.97  ? 119 ASP D N   1 
ATOM   8708  C  CA  . ASP D 1 55  ? 50.408 45.027 54.375  1.00 103.12 ? 119 ASP D CA  1 
ATOM   8709  C  C   . ASP D 1 55  ? 50.700 44.801 55.846  1.00 81.43  ? 119 ASP D C   1 
ATOM   8710  O  O   . ASP D 1 55  ? 51.817 44.451 56.245  1.00 94.49  ? 119 ASP D O   1 
ATOM   8711  C  CB  . ASP D 1 55  ? 51.221 46.206 53.796  1.00 122.98 ? 119 ASP D CB  1 
ATOM   8712  C  CG  . ASP D 1 55  ? 50.699 47.573 54.237  1.00 139.80 ? 119 ASP D CG  1 
ATOM   8713  O  OD1 . ASP D 1 55  ? 49.935 47.663 55.229  1.00 151.57 ? 119 ASP D OD1 1 
ATOM   8714  O  OD2 . ASP D 1 55  ? 51.068 48.570 53.580  1.00 162.14 ? 119 ASP D OD2 1 
ATOM   8715  N  N   . LYS D 1 56  ? 49.648 44.977 56.630  1.00 69.56  ? 120 LYS D N   1 
ATOM   8716  C  CA  . LYS D 1 56  ? 49.713 45.008 58.077  1.00 84.36  ? 120 LYS D CA  1 
ATOM   8717  C  C   . LYS D 1 56  ? 49.085 43.741 58.632  1.00 73.21  ? 120 LYS D C   1 
ATOM   8718  O  O   . LYS D 1 56  ? 49.511 43.240 59.672  1.00 84.67  ? 120 LYS D O   1 
ATOM   8719  C  CB  . LYS D 1 56  ? 48.952 46.241 58.585  1.00 111.63 ? 120 LYS D CB  1 
ATOM   8720  C  CG  . LYS D 1 56  ? 48.812 46.386 60.103  1.00 126.18 ? 120 LYS D CG  1 
ATOM   8721  C  CD  . LYS D 1 56  ? 47.864 47.533 60.495  1.00 130.94 ? 120 LYS D CD  1 
ATOM   8722  C  CE  . LYS D 1 56  ? 48.433 48.908 60.121  1.00 166.62 ? 120 LYS D CE  1 
ATOM   8723  N  NZ  . LYS D 1 56  ? 48.113 49.301 58.713  1.00 173.80 ? 120 LYS D NZ  1 
ATOM   8724  N  N   . GLU D 1 57  ? 48.083 43.222 57.929  1.00 59.48  ? 121 GLU D N   1 
ATOM   8725  C  CA  . GLU D 1 57  ? 47.203 42.180 58.470  1.00 60.20  ? 121 GLU D CA  1 
ATOM   8726  C  C   . GLU D 1 57  ? 46.199 41.669 57.434  1.00 59.49  ? 121 GLU D C   1 
ATOM   8727  O  O   . GLU D 1 57  ? 45.959 42.305 56.406  1.00 74.82  ? 121 GLU D O   1 
ATOM   8728  C  CB  . GLU D 1 57  ? 46.408 42.730 59.649  1.00 60.08  ? 121 GLU D CB  1 
ATOM   8729  C  CG  . GLU D 1 57  ? 45.117 43.431 59.204  1.00 76.22  ? 121 GLU D CG  1 
ATOM   8730  C  CD  . GLU D 1 57  ? 44.427 44.276 60.283  1.00 103.83 ? 121 GLU D CD  1 
ATOM   8731  O  OE1 . GLU D 1 57  ? 44.638 44.015 61.492  1.00 118.39 ? 121 GLU D OE1 1 
ATOM   8732  O  OE2 . GLU D 1 57  ? 43.651 45.197 59.909  1.00 90.78  ? 121 GLU D OE2 1 
ATOM   8733  N  N   . CYS D 1 58  ? 45.587 40.530 57.729  1.00 54.03  ? 122 CYS D N   1 
ATOM   8734  C  CA  . CYS D 1 58  ? 44.582 39.953 56.848  1.00 59.24  ? 122 CYS D CA  1 
ATOM   8735  C  C   . CYS D 1 58  ? 43.236 40.048 57.509  1.00 56.69  ? 122 CYS D C   1 
ATOM   8736  O  O   . CYS D 1 58  ? 43.104 39.754 58.695  1.00 66.86  ? 122 CYS D O   1 
ATOM   8737  C  CB  . CYS D 1 58  ? 44.887 38.497 56.527  1.00 54.50  ? 122 CYS D CB  1 
ATOM   8738  S  SG  . CYS D 1 58  ? 46.298 38.370 55.518  1.00 80.91  ? 122 CYS D SG  1 
ATOM   8739  N  N   . ARG D 1 59  ? 42.242 40.470 56.739  1.00 47.58  ? 123 ARG D N   1 
ATOM   8740  C  CA  . ARG D 1 59  ? 40.908 40.657 57.267  1.00 44.36  ? 123 ARG D CA  1 
ATOM   8741  C  C   . ARG D 1 59  ? 39.917 39.718 56.594  1.00 42.79  ? 123 ARG D C   1 
ATOM   8742  O  O   . ARG D 1 59  ? 40.088 39.290 55.445  1.00 45.15  ? 123 ARG D O   1 
ATOM   8743  C  CB  . ARG D 1 59  ? 40.458 42.107 57.126  1.00 39.71  ? 123 ARG D CB  1 
ATOM   8744  C  CG  . ARG D 1 59  ? 41.245 43.003 57.957  1.00 44.49  ? 123 ARG D CG  1 
ATOM   8745  C  CD  . ARG D 1 59  ? 40.664 44.357 57.938  1.00 54.34  ? 123 ARG D CD  1 
ATOM   8746  N  NE  . ARG D 1 59  ? 39.502 44.422 58.794  1.00 57.21  ? 123 ARG D NE  1 
ATOM   8747  C  CZ  . ARG D 1 59  ? 39.558 44.507 60.114  1.00 64.85  ? 123 ARG D CZ  1 
ATOM   8748  N  NH1 . ARG D 1 59  ? 40.748 44.527 60.736  1.00 57.26  ? 123 ARG D NH1 1 
ATOM   8749  N  NH2 . ARG D 1 59  ? 38.416 44.575 60.802  1.00 61.93  ? 123 ARG D NH2 1 
ATOM   8750  N  N   . ARG D 1 60  ? 38.881 39.384 57.339  1.00 37.65  ? 124 ARG D N   1 
ATOM   8751  C  CA  . ARG D 1 60  ? 37.853 38.521 56.859  1.00 36.35  ? 124 ARG D CA  1 
ATOM   8752  C  C   . ARG D 1 60  ? 36.665 39.406 56.670  1.00 41.43  ? 124 ARG D C   1 
ATOM   8753  O  O   . ARG D 1 60  ? 36.146 39.975 57.613  1.00 49.55  ? 124 ARG D O   1 
ATOM   8754  C  CB  . ARG D 1 60  ? 37.579 37.457 57.912  1.00 32.27  ? 124 ARG D CB  1 
ATOM   8755  C  CG  . ARG D 1 60  ? 36.169 36.928 57.982  1.00 33.63  ? 124 ARG D CG  1 
ATOM   8756  C  CD  . ARG D 1 60  ? 36.140 35.603 58.742  1.00 35.47  ? 124 ARG D CD  1 
ATOM   8757  N  NE  . ARG D 1 60  ? 34.804 35.035 58.860  1.00 34.95  ? 124 ARG D NE  1 
ATOM   8758  C  CZ  . ARG D 1 60  ? 34.409 34.297 59.892  1.00 42.89  ? 124 ARG D CZ  1 
ATOM   8759  N  NH1 . ARG D 1 60  ? 35.270 34.020 60.874  1.00 58.68  ? 124 ARG D NH1 1 
ATOM   8760  N  NH2 . ARG D 1 60  ? 33.163 33.821 59.945  1.00 41.73  ? 124 ARG D NH2 1 
ATOM   8761  N  N   . PHE D 1 61  ? 36.245 39.562 55.444  1.00 41.30  ? 125 PHE D N   1 
ATOM   8762  C  CA  . PHE D 1 61  ? 35.001 40.275 55.208  1.00 53.12  ? 125 PHE D CA  1 
ATOM   8763  C  C   . PHE D 1 61  ? 33.843 39.305 55.111  1.00 50.28  ? 125 PHE D C   1 
ATOM   8764  O  O   . PHE D 1 61  ? 34.028 38.128 54.768  1.00 48.29  ? 125 PHE D O   1 
ATOM   8765  C  CB  . PHE D 1 61  ? 35.095 41.113 53.929  1.00 55.57  ? 125 PHE D CB  1 
ATOM   8766  C  CG  . PHE D 1 61  ? 36.103 42.203 54.015  1.00 49.07  ? 125 PHE D CG  1 
ATOM   8767  C  CD1 . PHE D 1 61  ? 37.451 41.904 54.057  1.00 50.73  ? 125 PHE D CD1 1 
ATOM   8768  C  CD2 . PHE D 1 61  ? 35.699 43.525 54.083  1.00 51.96  ? 125 PHE D CD2 1 
ATOM   8769  C  CE1 . PHE D 1 61  ? 38.405 42.909 54.133  1.00 66.77  ? 125 PHE D CE1 1 
ATOM   8770  C  CE2 . PHE D 1 61  ? 36.618 44.544 54.170  1.00 58.48  ? 125 PHE D CE2 1 
ATOM   8771  C  CZ  . PHE D 1 61  ? 37.987 44.247 54.192  1.00 65.90  ? 125 PHE D CZ  1 
ATOM   8772  N  N   . PHE D 1 62  ? 32.647 39.798 55.410  1.00 43.80  ? 126 PHE D N   1 
ATOM   8773  C  CA  . PHE D 1 62  ? 31.460 38.979 55.223  1.00 51.35  ? 126 PHE D CA  1 
ATOM   8774  C  C   . PHE D 1 62  ? 30.191 39.835 55.184  1.00 52.50  ? 126 PHE D C   1 
ATOM   8775  O  O   . PHE D 1 62  ? 30.220 41.059 55.339  1.00 54.61  ? 126 PHE D O   1 
ATOM   8776  C  CB  . PHE D 1 62  ? 31.372 37.875 56.303  1.00 55.19  ? 126 PHE D CB  1 
ATOM   8777  C  CG  . PHE D 1 62  ? 31.311 38.421 57.669  1.00 58.78  ? 126 PHE D CG  1 
ATOM   8778  C  CD1 . PHE D 1 62  ? 30.087 38.795 58.220  1.00 64.00  ? 126 PHE D CD1 1 
ATOM   8779  C  CD2 . PHE D 1 62  ? 32.474 38.660 58.385  1.00 56.94  ? 126 PHE D CD2 1 
ATOM   8780  C  CE1 . PHE D 1 62  ? 30.018 39.388 59.487  1.00 56.45  ? 126 PHE D CE1 1 
ATOM   8781  C  CE2 . PHE D 1 62  ? 32.415 39.233 59.652  1.00 59.41  ? 126 PHE D CE2 1 
ATOM   8782  C  CZ  . PHE D 1 62  ? 31.177 39.606 60.196  1.00 59.23  ? 126 PHE D CZ  1 
ATOM   8783  N  N   . VAL D 1 63  ? 29.067 39.169 54.968  1.00 59.81  ? 127 VAL D N   1 
ATOM   8784  C  CA  . VAL D 1 63  ? 27.787 39.825 54.925  1.00 54.46  ? 127 VAL D CA  1 
ATOM   8785  C  C   . VAL D 1 63  ? 26.955 39.277 56.075  1.00 53.79  ? 127 VAL D C   1 
ATOM   8786  O  O   . VAL D 1 63  ? 26.794 38.060 56.196  1.00 53.24  ? 127 VAL D O   1 
ATOM   8787  C  CB  . VAL D 1 63  ? 27.120 39.550 53.585  1.00 52.57  ? 127 VAL D CB  1 
ATOM   8788  C  CG1 . VAL D 1 63  ? 25.668 39.900 53.638  1.00 62.82  ? 127 VAL D CG1 1 
ATOM   8789  C  CG2 . VAL D 1 63  ? 27.802 40.351 52.491  1.00 56.95  ? 127 VAL D CG2 1 
ATOM   8790  N  N   . SER D 1 64  ? 26.438 40.173 56.914  1.00 50.32  ? 128 SER D N   1 
ATOM   8791  C  CA  . SER D 1 64  ? 25.660 39.767 58.079  1.00 59.13  ? 128 SER D CA  1 
ATOM   8792  C  C   . SER D 1 64  ? 24.287 39.221 57.721  1.00 64.38  ? 128 SER D C   1 
ATOM   8793  O  O   . SER D 1 64  ? 23.655 39.698 56.787  1.00 76.15  ? 128 SER D O   1 
ATOM   8794  C  CB  . SER D 1 64  ? 25.468 40.949 59.017  1.00 69.79  ? 128 SER D CB  1 
ATOM   8795  O  OG  . SER D 1 64  ? 24.517 41.857 58.478  1.00 92.80  ? 128 SER D OG  1 
ATOM   8796  N  N   . MET D 1 65  ? 23.836 38.220 58.467  1.00 64.74  ? 129 MET D N   1 
ATOM   8797  C  CA  . MET D 1 65  ? 22.424 37.842 58.465  1.00 73.27  ? 129 MET D CA  1 
ATOM   8798  C  C   . MET D 1 65  ? 21.703 38.243 59.768  1.00 80.92  ? 129 MET D C   1 
ATOM   8799  O  O   . MET D 1 65  ? 20.534 37.908 59.973  1.00 97.71  ? 129 MET D O   1 
ATOM   8800  C  CB  . MET D 1 65  ? 22.245 36.344 58.207  1.00 79.87  ? 129 MET D CB  1 
ATOM   8801  C  CG  . MET D 1 65  ? 22.022 35.967 56.755  1.00 84.48  ? 129 MET D CG  1 
ATOM   8802  S  SD  . MET D 1 65  ? 23.311 34.947 56.044  1.00 91.86  ? 129 MET D SD  1 
ATOM   8803  C  CE  . MET D 1 65  ? 22.970 33.329 56.762  1.00 90.27  ? 129 MET D CE  1 
ATOM   8804  N  N   . GLY D 1 66  ? 22.384 38.979 60.640  1.00 88.36  ? 130 GLY D N   1 
ATOM   8805  C  CA  . GLY D 1 66  ? 21.851 39.247 61.991  1.00 84.86  ? 130 GLY D CA  1 
ATOM   8806  C  C   . GLY D 1 66  ? 22.509 38.383 63.078  1.00 79.21  ? 130 GLY D C   1 
ATOM   8807  O  O   . GLY D 1 66  ? 23.284 37.454 62.794  1.00 75.72  ? 130 GLY D O   1 
ATOM   8808  N  N   . TYR D 1 67  ? 22.218 38.687 64.335  1.00 68.25  ? 131 TYR D N   1 
ATOM   8809  C  CA  . TYR D 1 67  ? 22.815 37.948 65.420  1.00 64.49  ? 131 TYR D CA  1 
ATOM   8810  C  C   . TYR D 1 67  ? 22.024 36.686 65.556  1.00 65.17  ? 131 TYR D C   1 
ATOM   8811  O  O   . TYR D 1 67  ? 20.834 36.677 65.261  1.00 67.63  ? 131 TYR D O   1 
ATOM   8812  C  CB  . TYR D 1 67  ? 22.752 38.732 66.726  1.00 76.81  ? 131 TYR D CB  1 
ATOM   8813  C  CG  . TYR D 1 67  ? 23.460 40.059 66.685  1.00 81.71  ? 131 TYR D CG  1 
ATOM   8814  C  CD1 . TYR D 1 67  ? 24.849 40.133 66.621  1.00 92.35  ? 131 TYR D CD1 1 
ATOM   8815  C  CD2 . TYR D 1 67  ? 22.739 41.246 66.703  1.00 85.66  ? 131 TYR D CD2 1 
ATOM   8816  C  CE1 . TYR D 1 67  ? 25.505 41.367 66.577  1.00 99.07  ? 131 TYR D CE1 1 
ATOM   8817  C  CE2 . TYR D 1 67  ? 23.381 42.482 66.665  1.00 117.70 ? 131 TYR D CE2 1 
ATOM   8818  C  CZ  . TYR D 1 67  ? 24.760 42.539 66.602  1.00 109.36 ? 131 TYR D CZ  1 
ATOM   8819  O  OH  . TYR D 1 67  ? 25.364 43.776 66.571  1.00 111.67 ? 131 TYR D OH  1 
ATOM   8820  N  N   . GLY D 1 68  ? 22.685 35.632 66.022  1.00 68.26  ? 132 GLY D N   1 
ATOM   8821  C  CA  . GLY D 1 68  ? 22.095 34.300 66.083  1.00 73.95  ? 132 GLY D CA  1 
ATOM   8822  C  C   . GLY D 1 68  ? 21.053 34.169 67.163  1.00 73.76  ? 132 GLY D C   1 
ATOM   8823  O  O   . GLY D 1 68  ? 20.173 33.300 67.111  1.00 81.35  ? 132 GLY D O   1 
ATOM   8824  N  N   . THR D 1 69  ? 21.156 35.049 68.143  1.00 74.05  ? 133 THR D N   1 
ATOM   8825  C  CA  . THR D 1 69  ? 20.242 35.039 69.272  1.00 84.11  ? 133 THR D CA  1 
ATOM   8826  C  C   . THR D 1 69  ? 18.948 35.811 68.993  1.00 83.08  ? 133 THR D C   1 
ATOM   8827  O  O   . THR D 1 69  ? 17.897 35.456 69.508  1.00 73.44  ? 133 THR D O   1 
ATOM   8828  C  CB  . THR D 1 69  ? 20.929 35.544 70.569  1.00 80.85  ? 133 THR D CB  1 
ATOM   8829  O  OG1 . THR D 1 69  ? 19.947 35.659 71.602  1.00 95.81  ? 133 THR D OG1 1 
ATOM   8830  C  CG2 . THR D 1 69  ? 21.653 36.906 70.359  1.00 72.16  ? 133 THR D CG2 1 
ATOM   8831  N  N   . THR D 1 70  ? 19.040 36.856 68.172  1.00 110.24 ? 134 THR D N   1 
ATOM   8832  C  CA  . THR D 1 70  ? 17.899 37.730 67.863  1.00 104.83 ? 134 THR D CA  1 
ATOM   8833  C  C   . THR D 1 70  ? 17.224 37.271 66.581  1.00 101.15 ? 134 THR D C   1 
ATOM   8834  O  O   . THR D 1 70  ? 16.241 37.884 66.141  1.00 85.36  ? 134 THR D O   1 
ATOM   8835  C  CB  . THR D 1 70  ? 18.326 39.198 67.678  1.00 92.91  ? 134 THR D CB  1 
ATOM   8836  O  OG1 . THR D 1 70  ? 18.919 39.364 66.378  1.00 109.20 ? 134 THR D OG1 1 
ATOM   8837  C  CG2 . THR D 1 70  ? 19.333 39.570 68.729  1.00 113.02 ? 134 THR D CG2 1 
ATOM   8838  N  N   . THR D 1 71  ? 17.777 36.214 65.979  1.00 89.98  ? 135 THR D N   1 
ATOM   8839  C  CA  . THR D 1 71  ? 17.226 35.641 64.759  1.00 107.71 ? 135 THR D CA  1 
ATOM   8840  C  C   . THR D 1 71  ? 16.466 34.368 65.110  1.00 108.55 ? 135 THR D C   1 
ATOM   8841  O  O   . THR D 1 71  ? 17.000 33.493 65.796  1.00 109.49 ? 135 THR D O   1 
ATOM   8842  C  CB  . THR D 1 71  ? 18.328 35.349 63.683  1.00 98.68  ? 135 THR D CB  1 
ATOM   8843  O  OG1 . THR D 1 71  ? 18.949 36.577 63.254  1.00 84.70  ? 135 THR D OG1 1 
ATOM   8844  C  CG2 . THR D 1 71  ? 17.741 34.609 62.462  1.00 78.69  ? 135 THR D CG2 1 
ATOM   8845  N  N   . ASN D 1 72  ? 15.214 34.295 64.660  1.00 109.71 ? 136 ASN D N   1 
ATOM   8846  C  CA  . ASN D 1 72  ? 14.421 33.087 64.782  1.00 116.50 ? 136 ASN D CA  1 
ATOM   8847  C  C   . ASN D 1 72  ? 14.460 32.268 63.478  1.00 127.14 ? 136 ASN D C   1 
ATOM   8848  O  O   . ASN D 1 72  ? 14.474 32.845 62.386  1.00 155.70 ? 136 ASN D O   1 
ATOM   8849  C  CB  . ASN D 1 72  ? 12.984 33.424 65.197  1.00 120.17 ? 136 ASN D CB  1 
ATOM   8850  C  CG  . ASN D 1 72  ? 12.243 32.217 65.748  1.00 145.43 ? 136 ASN D CG  1 
ATOM   8851  O  OD1 . ASN D 1 72  ? 12.858 31.237 66.168  1.00 211.27 ? 136 ASN D OD1 1 
ATOM   8852  N  ND2 . ASN D 1 72  ? 10.923 32.276 65.739  1.00 145.84 ? 136 ASN D ND2 1 
ATOM   8853  N  N   . PHE D 1 73  ? 14.483 30.935 63.607  1.00 115.96 ? 137 PHE D N   1 
ATOM   8854  C  CA  . PHE D 1 73  ? 14.605 29.999 62.470  1.00 110.63 ? 137 PHE D CA  1 
ATOM   8855  C  C   . PHE D 1 73  ? 13.522 30.124 61.402  1.00 124.19 ? 137 PHE D C   1 
ATOM   8856  O  O   . PHE D 1 73  ? 13.829 30.053 60.212  1.00 134.53 ? 137 PHE D O   1 
ATOM   8857  C  CB  . PHE D 1 73  ? 14.665 28.539 62.947  1.00 118.67 ? 137 PHE D CB  1 
ATOM   8858  C  CG  . PHE D 1 73  ? 14.846 27.543 61.827  1.00 154.58 ? 137 PHE D CG  1 
ATOM   8859  C  CD1 . PHE D 1 73  ? 16.067 27.452 61.152  1.00 188.65 ? 137 PHE D CD1 1 
ATOM   8860  C  CD2 . PHE D 1 73  ? 13.797 26.703 61.436  1.00 156.58 ? 137 PHE D CD2 1 
ATOM   8861  C  CE1 . PHE D 1 73  ? 16.245 26.540 60.105  1.00 195.71 ? 137 PHE D CE1 1 
ATOM   8862  C  CE2 . PHE D 1 73  ? 13.961 25.782 60.387  1.00 147.63 ? 137 PHE D CE2 1 
ATOM   8863  C  CZ  . PHE D 1 73  ? 15.190 25.703 59.722  1.00 174.37 ? 137 PHE D CZ  1 
ATOM   8864  N  N   . ALA D 1 74  ? 12.269 30.289 61.836  1.00 154.26 ? 138 ALA D N   1 
ATOM   8865  C  CA  . ALA D 1 74  ? 11.102 30.377 60.942  1.00 165.43 ? 138 ALA D CA  1 
ATOM   8866  C  C   . ALA D 1 74  ? 11.193 31.503 59.906  1.00 168.16 ? 138 ALA D C   1 
ATOM   8867  O  O   . ALA D 1 74  ? 10.622 31.396 58.819  1.00 167.94 ? 138 ALA D O   1 
ATOM   8868  C  CB  . ALA D 1 74  ? 9.810  30.496 61.755  1.00 153.55 ? 138 ALA D CB  1 
ATOM   8869  N  N   . ASP D 1 75  ? 11.907 32.573 60.254  1.00 175.58 ? 139 ASP D N   1 
ATOM   8870  C  CA  . ASP D 1 75  ? 12.213 33.654 59.320  1.00 177.21 ? 139 ASP D CA  1 
ATOM   8871  C  C   . ASP D 1 75  ? 13.216 33.220 58.274  1.00 191.65 ? 139 ASP D C   1 
ATOM   8872  O  O   . ASP D 1 75  ? 14.192 32.530 58.576  1.00 248.37 ? 139 ASP D O   1 
ATOM   8873  C  CB  . ASP D 1 75  ? 12.816 34.852 60.053  1.00 173.74 ? 139 ASP D CB  1 
ATOM   8874  C  CG  . ASP D 1 75  ? 11.833 35.539 60.964  1.00 202.63 ? 139 ASP D CG  1 
ATOM   8875  O  OD1 . ASP D 1 75  ? 10.613 35.311 60.823  1.00 227.60 ? 139 ASP D OD1 1 
ATOM   8876  O  OD2 . ASP D 1 75  ? 12.288 36.318 61.826  1.00 214.79 ? 139 ASP D OD2 1 
ATOM   8877  N  N   . LEU D 1 76  ? 12.965 33.625 57.039  1.00 175.66 ? 140 LEU D N   1 
ATOM   8878  C  CA  . LEU D 1 76  ? 14.014 33.661 56.048  1.00 171.14 ? 140 LEU D CA  1 
ATOM   8879  C  C   . LEU D 1 76  ? 14.371 35.139 55.976  1.00 148.16 ? 140 LEU D C   1 
ATOM   8880  O  O   . LEU D 1 76  ? 13.477 35.987 55.936  1.00 128.59 ? 140 LEU D O   1 
ATOM   8881  C  CB  . LEU D 1 76  ? 13.537 33.089 54.699  1.00 182.34 ? 140 LEU D CB  1 
ATOM   8882  C  CG  . LEU D 1 76  ? 13.628 31.561 54.488  1.00 184.80 ? 140 LEU D CG  1 
ATOM   8883  C  CD1 . LEU D 1 76  ? 12.606 30.779 55.328  1.00 193.08 ? 140 LEU D CD1 1 
ATOM   8884  C  CD2 . LEU D 1 76  ? 13.498 31.183 53.011  1.00 155.03 ? 140 LEU D CD2 1 
ATOM   8885  N  N   . ILE D 1 77  ? 15.668 35.449 56.027  1.00 139.56 ? 141 ILE D N   1 
ATOM   8886  C  CA  . ILE D 1 77  ? 16.137 36.837 55.922  1.00 122.81 ? 141 ILE D CA  1 
ATOM   8887  C  C   . ILE D 1 77  ? 16.556 37.228 54.498  1.00 121.53 ? 141 ILE D C   1 
ATOM   8888  O  O   . ILE D 1 77  ? 16.913 36.384 53.673  1.00 145.88 ? 141 ILE D O   1 
ATOM   8889  C  CB  . ILE D 1 77  ? 17.250 37.182 56.942  1.00 121.47 ? 141 ILE D CB  1 
ATOM   8890  C  CG1 . ILE D 1 77  ? 17.423 38.706 57.047  1.00 119.06 ? 141 ILE D CG1 1 
ATOM   8891  C  CG2 . ILE D 1 77  ? 18.559 36.506 56.556  1.00 140.61 ? 141 ILE D CG2 1 
ATOM   8892  C  CD1 . ILE D 1 77  ? 17.850 39.238 58.420  1.00 94.76  ? 141 ILE D CD1 1 
ATOM   8893  N  N   . VAL D 1 78  ? 16.531 38.527 54.239  1.00 101.58 ? 142 VAL D N   1 
ATOM   8894  C  CA  . VAL D 1 78  ? 16.420 39.030 52.887  1.00 87.70  ? 142 VAL D CA  1 
ATOM   8895  C  C   . VAL D 1 78  ? 17.512 40.047 52.588  1.00 72.16  ? 142 VAL D C   1 
ATOM   8896  O  O   . VAL D 1 78  ? 17.905 40.788 53.472  1.00 73.65  ? 142 VAL D O   1 
ATOM   8897  C  CB  . VAL D 1 78  ? 15.027 39.623 52.695  1.00 86.34  ? 142 VAL D CB  1 
ATOM   8898  C  CG1 . VAL D 1 78  ? 14.714 40.665 53.791  1.00 86.41  ? 142 VAL D CG1 1 
ATOM   8899  C  CG2 . VAL D 1 78  ? 14.886 40.192 51.313  1.00 109.36 ? 142 VAL D CG2 1 
ATOM   8900  N  N   . SER D 1 79  ? 17.981 40.073 51.342  1.00 70.50  ? 143 SER D N   1 
ATOM   8901  C  CA  . SER D 1 79  ? 19.163 40.845 50.920  1.00 69.38  ? 143 SER D CA  1 
ATOM   8902  C  C   . SER D 1 79  ? 19.168 42.320 51.315  1.00 68.20  ? 143 SER D C   1 
ATOM   8903  O  O   . SER D 1 79  ? 20.227 42.904 51.552  1.00 74.98  ? 143 SER D O   1 
ATOM   8904  C  CB  . SER D 1 79  ? 19.352 40.738 49.406  1.00 64.13  ? 143 SER D CB  1 
ATOM   8905  O  OG  . SER D 1 79  ? 19.381 39.383 48.988  1.00 74.60  ? 143 SER D OG  1 
ATOM   8906  N  N   . GLU D 1 80  ? 17.989 42.923 51.382  1.00 77.69  ? 144 GLU D N   1 
ATOM   8907  C  CA  . GLU D 1 80  ? 17.889 44.351 51.699  1.00 82.86  ? 144 GLU D CA  1 
ATOM   8908  C  C   . GLU D 1 80  ? 18.287 44.667 53.128  1.00 74.62  ? 144 GLU D C   1 
ATOM   8909  O  O   . GLU D 1 80  ? 18.594 45.812 53.438  1.00 80.76  ? 144 GLU D O   1 
ATOM   8910  C  CB  . GLU D 1 80  ? 16.486 44.889 51.413  1.00 90.10  ? 144 GLU D CB  1 
ATOM   8911  C  CG  . GLU D 1 80  ? 16.151 44.954 49.920  1.00 117.78 ? 144 GLU D CG  1 
ATOM   8912  C  CD  . GLU D 1 80  ? 16.003 43.578 49.264  1.00 114.89 ? 144 GLU D CD  1 
ATOM   8913  O  OE1 . GLU D 1 80  ? 15.747 42.592 49.982  1.00 118.71 ? 144 GLU D OE1 1 
ATOM   8914  O  OE2 . GLU D 1 80  ? 16.139 43.484 48.027  1.00 120.00 ? 144 GLU D OE2 1 
ATOM   8915  N  N   . GLN D 1 81  ? 18.298 43.644 53.981  1.00 62.84  ? 145 GLN D N   1 
ATOM   8916  C  CA  . GLN D 1 81  ? 18.523 43.812 55.410  1.00 60.00  ? 145 GLN D CA  1 
ATOM   8917  C  C   . GLN D 1 81  ? 19.980 43.604 55.717  1.00 60.50  ? 145 GLN D C   1 
ATOM   8918  O  O   . GLN D 1 81  ? 20.429 43.768 56.838  1.00 82.38  ? 145 GLN D O   1 
ATOM   8919  C  CB  . GLN D 1 81  ? 17.669 42.835 56.220  1.00 61.46  ? 145 GLN D CB  1 
ATOM   8920  C  CG  . GLN D 1 81  ? 16.140 43.080 56.122  1.00 88.26  ? 145 GLN D CG  1 
ATOM   8921  C  CD  . GLN D 1 81  ? 15.332 42.348 57.196  1.00 105.46 ? 145 GLN D CD  1 
ATOM   8922  O  OE1 . GLN D 1 81  ? 15.208 41.126 57.179  1.00 115.69 ? 145 GLN D OE1 1 
ATOM   8923  N  NE2 . GLN D 1 81  ? 14.768 43.107 58.127  1.00 121.25 ? 145 GLN D NE2 1 
ATOM   8924  N  N   . MET D 1 82  ? 20.733 43.282 54.696  1.00 59.37  ? 146 MET D N   1 
ATOM   8925  C  CA  . MET D 1 82  ? 22.061 42.787 54.895  1.00 57.51  ? 146 MET D CA  1 
ATOM   8926  C  C   . MET D 1 82  ? 23.060 43.906 54.841  1.00 56.39  ? 146 MET D C   1 
ATOM   8927  O  O   . MET D 1 82  ? 22.879 44.863 54.080  1.00 67.03  ? 146 MET D O   1 
ATOM   8928  C  CB  . MET D 1 82  ? 22.374 41.778 53.802  1.00 62.29  ? 146 MET D CB  1 
ATOM   8929  C  CG  . MET D 1 82  ? 21.668 40.442 53.962  1.00 63.18  ? 146 MET D CG  1 
ATOM   8930  S  SD  . MET D 1 82  ? 21.945 39.268 52.588  1.00 72.14  ? 146 MET D SD  1 
ATOM   8931  C  CE  . MET D 1 82  ? 21.185 37.839 53.353  1.00 78.61  ? 146 MET D CE  1 
ATOM   8932  N  N   . ASN D 1 83  ? 24.128 43.739 55.619  1.00 53.90  ? 147 ASN D N   1 
ATOM   8933  C  CA  . ASN D 1 83  ? 25.218 44.713 55.742  1.00 56.35  ? 147 ASN D CA  1 
ATOM   8934  C  C   . ASN D 1 83  ? 26.563 44.029 55.570  1.00 55.24  ? 147 ASN D C   1 
ATOM   8935  O  O   . ASN D 1 83  ? 26.698 42.808 55.824  1.00 54.61  ? 147 ASN D O   1 
ATOM   8936  C  CB  . ASN D 1 83  ? 25.197 45.361 57.134  1.00 64.00  ? 147 ASN D CB  1 
ATOM   8937  C  CG  . ASN D 1 83  ? 24.051 46.321 57.323  1.00 58.15  ? 147 ASN D CG  1 
ATOM   8938  O  OD1 . ASN D 1 83  ? 23.746 47.098 56.446  1.00 67.53  ? 147 ASN D OD1 1 
ATOM   8939  N  ND2 . ASN D 1 83  ? 23.423 46.280 58.487  1.00 70.48  ? 147 ASN D ND2 1 
ATOM   8940  N  N   . VAL D 1 84  ? 27.559 44.824 55.171  1.00 50.38  ? 148 VAL D N   1 
ATOM   8941  C  CA  . VAL D 1 84  ? 28.933 44.330 55.024  1.00 49.52  ? 148 VAL D CA  1 
ATOM   8942  C  C   . VAL D 1 84  ? 29.830 44.663 56.231  1.00 49.91  ? 148 VAL D C   1 
ATOM   8943  O  O   . VAL D 1 84  ? 30.114 45.830 56.501  1.00 46.43  ? 148 VAL D O   1 
ATOM   8944  C  CB  . VAL D 1 84  ? 29.597 44.913 53.795  1.00 46.25  ? 148 VAL D CB  1 
ATOM   8945  C  CG1 . VAL D 1 84  ? 30.934 44.241 53.582  1.00 44.81  ? 148 VAL D CG1 1 
ATOM   8946  C  CG2 . VAL D 1 84  ? 28.699 44.765 52.577  1.00 47.34  ? 148 VAL D CG2 1 
ATOM   8947  N  N   . TYR D 1 85  ? 30.275 43.618 56.930  1.00 47.94  ? 149 TYR D N   1 
ATOM   8948  C  CA  . TYR D 1 85  ? 31.190 43.745 58.051  1.00 48.73  ? 149 TYR D CA  1 
ATOM   8949  C  C   . TYR D 1 85  ? 32.557 43.178 57.747  1.00 54.28  ? 149 TYR D C   1 
ATOM   8950  O  O   . TYR D 1 85  ? 32.726 42.323 56.854  1.00 61.50  ? 149 TYR D O   1 
ATOM   8951  C  CB  . TYR D 1 85  ? 30.653 42.994 59.248  1.00 46.17  ? 149 TYR D CB  1 
ATOM   8952  C  CG  . TYR D 1 85  ? 29.477 43.676 59.863  1.00 55.98  ? 149 TYR D CG  1 
ATOM   8953  C  CD1 . TYR D 1 85  ? 29.644 44.772 60.716  1.00 63.89  ? 149 TYR D CD1 1 
ATOM   8954  C  CD2 . TYR D 1 85  ? 28.178 43.228 59.602  1.00 53.37  ? 149 TYR D CD2 1 
ATOM   8955  C  CE1 . TYR D 1 85  ? 28.533 45.401 61.301  1.00 61.01  ? 149 TYR D CE1 1 
ATOM   8956  C  CE2 . TYR D 1 85  ? 27.080 43.834 60.171  1.00 52.75  ? 149 TYR D CE2 1 
ATOM   8957  C  CZ  . TYR D 1 85  ? 27.255 44.921 61.013  1.00 58.52  ? 149 TYR D CZ  1 
ATOM   8958  O  OH  . TYR D 1 85  ? 26.149 45.530 61.542  1.00 63.05  ? 149 TYR D OH  1 
ATOM   8959  N  N   . SER D 1 86  ? 33.522 43.649 58.535  1.00 54.23  ? 150 SER D N   1 
ATOM   8960  C  CA  . SER D 1 86  ? 34.902 43.187 58.501  1.00 54.31  ? 150 SER D CA  1 
ATOM   8961  C  C   . SER D 1 86  ? 35.298 42.693 59.886  1.00 47.25  ? 150 SER D C   1 
ATOM   8962  O  O   . SER D 1 86  ? 34.666 43.013 60.845  1.00 60.51  ? 150 SER D O   1 
ATOM   8963  C  CB  . SER D 1 86  ? 35.798 44.343 58.067  1.00 58.37  ? 150 SER D CB  1 
ATOM   8964  O  OG  . SER D 1 86  ? 37.149 43.976 58.086  1.00 88.51  ? 150 SER D OG  1 
ATOM   8965  N  N   . VAL D 1 87  ? 36.358 41.915 59.999  1.00 49.74  ? 151 VAL D N   1 
ATOM   8966  C  CA  . VAL D 1 87  ? 36.875 41.463 61.300  1.00 40.65  ? 151 VAL D CA  1 
ATOM   8967  C  C   . VAL D 1 87  ? 38.327 41.162 60.989  1.00 44.06  ? 151 VAL D C   1 
ATOM   8968  O  O   . VAL D 1 87  ? 38.703 41.104 59.806  1.00 53.73  ? 151 VAL D O   1 
ATOM   8969  C  CB  . VAL D 1 87  ? 36.110 40.220 61.800  1.00 36.38  ? 151 VAL D CB  1 
ATOM   8970  C  CG1 . VAL D 1 87  ? 36.494 39.003 61.017  1.00 42.47  ? 151 VAL D CG1 1 
ATOM   8971  C  CG2 . VAL D 1 87  ? 36.440 39.915 63.139  1.00 36.80  ? 151 VAL D CG2 1 
ATOM   8972  N  N   . LYS D 1 88  ? 39.172 41.005 61.996  1.00 48.10  ? 152 LYS D N   1 
ATOM   8973  C  CA  . LYS D 1 88  ? 40.554 40.635 61.698  1.00 51.07  ? 152 LYS D CA  1 
ATOM   8974  C  C   . LYS D 1 88  ? 40.575 39.130 61.528  1.00 47.22  ? 152 LYS D C   1 
ATOM   8975  O  O   . LYS D 1 88  ? 40.018 38.426 62.359  1.00 48.35  ? 152 LYS D O   1 
ATOM   8976  C  CB  . LYS D 1 88  ? 41.504 41.074 62.810  1.00 56.67  ? 152 LYS D CB  1 
ATOM   8977  C  CG  . LYS D 1 88  ? 42.995 41.068 62.384  1.00 69.19  ? 152 LYS D CG  1 
ATOM   8978  C  CD  . LYS D 1 88  ? 43.966 40.826 63.563  1.00 75.14  ? 152 LYS D CD  1 
ATOM   8979  C  CE  . LYS D 1 88  ? 44.126 39.334 63.864  1.00 86.52  ? 152 LYS D CE  1 
ATOM   8980  N  NZ  . LYS D 1 88  ? 44.906 39.083 65.110  1.00 83.63  ? 152 LYS D NZ  1 
ATOM   8981  N  N   . LEU D 1 89  ? 41.173 38.623 60.450  1.00 45.46  ? 153 LEU D N   1 
ATOM   8982  C  CA  . LEU D 1 89  ? 41.277 37.171 60.305  1.00 45.25  ? 153 LEU D CA  1 
ATOM   8983  C  C   . LEU D 1 89  ? 41.959 36.578 61.540  1.00 53.45  ? 153 LEU D C   1 
ATOM   8984  O  O   . LEU D 1 89  ? 43.078 36.973 61.910  1.00 48.49  ? 153 LEU D O   1 
ATOM   8985  C  CB  . LEU D 1 89  ? 42.049 36.763 59.055  1.00 47.28  ? 153 LEU D CB  1 
ATOM   8986  C  CG  . LEU D 1 89  ? 42.236 35.238 58.869  1.00 41.93  ? 153 LEU D CG  1 
ATOM   8987  C  CD1 . LEU D 1 89  ? 40.916 34.459 58.799  1.00 36.06  ? 153 LEU D CD1 1 
ATOM   8988  C  CD2 . LEU D 1 89  ? 43.050 34.980 57.626  1.00 37.45  ? 153 LEU D CD2 1 
ATOM   8989  N  N   . GLY D 1 90  ? 41.263 35.641 62.171  1.00 56.89  ? 154 GLY D N   1 
ATOM   8990  C  CA  . GLY D 1 90  ? 41.731 35.054 63.406  1.00 55.17  ? 154 GLY D CA  1 
ATOM   8991  C  C   . GLY D 1 90  ? 40.825 35.424 64.549  1.00 66.11  ? 154 GLY D C   1 
ATOM   8992  O  O   . GLY D 1 90  ? 40.856 34.795 65.605  1.00 75.97  ? 154 GLY D O   1 
ATOM   8993  N  N   . ASP D 1 91  ? 40.018 36.455 64.340  1.00 75.12  ? 155 ASP D N   1 
ATOM   8994  C  CA  . ASP D 1 91  ? 39.073 36.896 65.357  1.00 71.70  ? 155 ASP D CA  1 
ATOM   8995  C  C   . ASP D 1 91  ? 37.706 36.388 64.997  1.00 58.84  ? 155 ASP D C   1 
ATOM   8996  O  O   . ASP D 1 91  ? 37.437 36.166 63.832  1.00 83.45  ? 155 ASP D O   1 
ATOM   8997  C  CB  . ASP D 1 91  ? 39.067 38.416 65.487  1.00 90.94  ? 155 ASP D CB  1 
ATOM   8998  C  CG  . ASP D 1 91  ? 40.240 38.948 66.310  1.00 120.79 ? 155 ASP D CG  1 
ATOM   8999  O  OD1 . ASP D 1 91  ? 40.856 38.180 67.085  1.00 116.00 ? 155 ASP D OD1 1 
ATOM   9000  O  OD2 . ASP D 1 91  ? 40.541 40.152 66.189  1.00 154.09 ? 155 ASP D OD2 1 
ATOM   9001  N  N   . PRO D 1 92  ? 36.871 36.124 66.001  1.00 54.06  ? 156 PRO D N   1 
ATOM   9002  C  CA  . PRO D 1 92  ? 35.541 35.625 65.754  1.00 59.41  ? 156 PRO D CA  1 
ATOM   9003  C  C   . PRO D 1 92  ? 34.583 36.789 65.585  1.00 64.50  ? 156 PRO D C   1 
ATOM   9004  O  O   . PRO D 1 92  ? 34.798 37.836 66.185  1.00 78.15  ? 156 PRO D O   1 
ATOM   9005  C  CB  . PRO D 1 92  ? 35.227 34.836 67.027  1.00 61.09  ? 156 PRO D CB  1 
ATOM   9006  C  CG  . PRO D 1 92  ? 35.975 35.543 68.073  1.00 75.37  ? 156 PRO D CG  1 
ATOM   9007  C  CD  . PRO D 1 92  ? 37.248 35.979 67.415  1.00 72.70  ? 156 PRO D CD  1 
ATOM   9008  N  N   . PRO D 1 93  ? 33.540 36.624 64.761  1.00 59.41  ? 157 PRO D N   1 
ATOM   9009  C  CA  . PRO D 1 93  ? 32.546 37.684 64.580  1.00 61.04  ? 157 PRO D CA  1 
ATOM   9010  C  C   . PRO D 1 93  ? 31.636 37.918 65.795  1.00 67.30  ? 157 PRO D C   1 
ATOM   9011  O  O   . PRO D 1 93  ? 30.399 37.763 65.704  1.00 60.49  ? 157 PRO D O   1 
ATOM   9012  C  CB  . PRO D 1 93  ? 31.712 37.203 63.369  1.00 53.26  ? 157 PRO D CB  1 
ATOM   9013  C  CG  . PRO D 1 93  ? 31.913 35.752 63.306  1.00 57.71  ? 157 PRO D CG  1 
ATOM   9014  C  CD  . PRO D 1 93  ? 33.336 35.520 63.805  1.00 60.23  ? 157 PRO D CD  1 
ATOM   9015  N  N   . THR D 1 94  ? 32.245 38.288 66.921  1.00 78.08  ? 158 THR D N   1 
ATOM   9016  C  CA  . THR D 1 94  ? 31.486 38.801 68.063  1.00 75.03  ? 158 THR D CA  1 
ATOM   9017  C  C   . THR D 1 94  ? 31.125 40.243 67.769  1.00 60.94  ? 158 THR D C   1 
ATOM   9018  O  O   . THR D 1 94  ? 31.799 40.906 66.997  1.00 65.30  ? 158 THR D O   1 
ATOM   9019  C  CB  . THR D 1 94  ? 32.270 38.722 69.412  1.00 76.50  ? 158 THR D CB  1 
ATOM   9020  O  OG1 . THR D 1 94  ? 33.621 39.178 69.233  1.00 86.37  ? 158 THR D OG1 1 
ATOM   9021  C  CG2 . THR D 1 94  ? 32.250 37.288 69.970  1.00 81.22  ? 158 THR D CG2 1 
ATOM   9022  N  N   . PRO D 1 95  ? 30.060 40.736 68.386  1.00 65.26  ? 159 PRO D N   1 
ATOM   9023  C  CA  . PRO D 1 95  ? 29.627 42.122 68.243  1.00 73.43  ? 159 PRO D CA  1 
ATOM   9024  C  C   . PRO D 1 95  ? 30.735 43.151 68.490  1.00 73.60  ? 159 PRO D C   1 
ATOM   9025  O  O   . PRO D 1 95  ? 30.806 44.169 67.788  1.00 83.03  ? 159 PRO D O   1 
ATOM   9026  C  CB  . PRO D 1 95  ? 28.566 42.247 69.327  1.00 72.77  ? 159 PRO D CB  1 
ATOM   9027  C  CG  . PRO D 1 95  ? 28.037 40.875 69.469  1.00 60.77  ? 159 PRO D CG  1 
ATOM   9028  C  CD  . PRO D 1 95  ? 29.173 39.971 69.275  1.00 59.20  ? 159 PRO D CD  1 
ATOM   9029  N  N   . ASP D 1 96  ? 31.587 42.881 69.473  1.00 68.90  ? 160 ASP D N   1 
ATOM   9030  C  CA  . ASP D 1 96  ? 32.709 43.771 69.811  1.00 80.34  ? 160 ASP D CA  1 
ATOM   9031  C  C   . ASP D 1 96  ? 33.880 43.735 68.803  1.00 77.01  ? 160 ASP D C   1 
ATOM   9032  O  O   . ASP D 1 96  ? 34.639 44.695 68.688  1.00 74.82  ? 160 ASP D O   1 
ATOM   9033  C  CB  . ASP D 1 96  ? 33.207 43.448 71.217  1.00 90.96  ? 160 ASP D CB  1 
ATOM   9034  C  CG  . ASP D 1 96  ? 32.072 43.260 72.201  1.00 123.10 ? 160 ASP D CG  1 
ATOM   9035  O  OD1 . ASP D 1 96  ? 30.985 43.834 71.984  1.00 118.80 ? 160 ASP D OD1 1 
ATOM   9036  O  OD2 . ASP D 1 96  ? 32.265 42.537 73.200  1.00 196.21 ? 160 ASP D OD2 1 
ATOM   9037  N  N   . LYS D 1 97  ? 34.024 42.626 68.082  1.00 65.99  ? 161 LYS D N   1 
ATOM   9038  C  CA  . LYS D 1 97  ? 35.058 42.504 67.076  1.00 59.89  ? 161 LYS D CA  1 
ATOM   9039  C  C   . LYS D 1 97  ? 34.674 43.092 65.736  1.00 62.26  ? 161 LYS D C   1 
ATOM   9040  O  O   . LYS D 1 97  ? 35.557 43.477 64.952  1.00 77.36  ? 161 LYS D O   1 
ATOM   9041  C  CB  . LYS D 1 97  ? 35.459 41.053 66.896  1.00 53.50  ? 161 LYS D CB  1 
ATOM   9042  C  CG  . LYS D 1 97  ? 36.288 40.547 68.038  1.00 68.33  ? 161 LYS D CG  1 
ATOM   9043  C  CD  . LYS D 1 97  ? 37.470 41.476 68.321  1.00 76.10  ? 161 LYS D CD  1 
ATOM   9044  C  CE  . LYS D 1 97  ? 38.477 40.810 69.229  1.00 90.80  ? 161 LYS D CE  1 
ATOM   9045  N  NZ  . LYS D 1 97  ? 39.571 41.739 69.601  1.00 112.23 ? 161 LYS D NZ  1 
ATOM   9046  N  N   . LEU D 1 98  ? 33.369 43.167 65.475  1.00 58.37  ? 162 LEU D N   1 
ATOM   9047  C  CA  . LEU D 1 98  ? 32.850 43.654 64.188  1.00 54.87  ? 162 LEU D CA  1 
ATOM   9048  C  C   . LEU D 1 98  ? 33.232 45.067 63.848  1.00 52.63  ? 162 LEU D C   1 
ATOM   9049  O  O   . LEU D 1 98  ? 33.202 45.931 64.707  1.00 84.55  ? 162 LEU D O   1 
ATOM   9050  C  CB  . LEU D 1 98  ? 31.343 43.546 64.142  1.00 54.44  ? 162 LEU D CB  1 
ATOM   9051  C  CG  . LEU D 1 98  ? 30.819 42.107 64.153  1.00 62.58  ? 162 LEU D CG  1 
ATOM   9052  C  CD1 . LEU D 1 98  ? 29.505 42.045 63.421  1.00 65.15  ? 162 LEU D CD1 1 
ATOM   9053  C  CD2 . LEU D 1 98  ? 31.790 41.135 63.500  1.00 73.80  ? 162 LEU D CD2 1 
ATOM   9054  N  N   . LYS D 1 99  ? 33.627 45.289 62.603  1.00 45.74  ? 163 LYS D N   1 
ATOM   9055  C  CA  . LYS D 1 99  ? 33.783 46.626 62.056  1.00 49.67  ? 163 LYS D CA  1 
ATOM   9056  C  C   . LYS D 1 99  ? 32.824 46.772 60.894  1.00 53.45  ? 163 LYS D C   1 
ATOM   9057  O  O   . LYS D 1 99  ? 32.936 46.074 59.876  1.00 54.26  ? 163 LYS D O   1 
ATOM   9058  C  CB  . LYS D 1 99  ? 35.207 46.860 61.587  1.00 61.28  ? 163 LYS D CB  1 
ATOM   9059  C  CG  . LYS D 1 99  ? 35.390 48.109 60.761  1.00 74.61  ? 163 LYS D CG  1 
ATOM   9060  C  CD  . LYS D 1 99  ? 36.853 48.529 60.755  1.00 97.24  ? 163 LYS D CD  1 
ATOM   9061  C  CE  . LYS D 1 99  ? 37.232 49.206 59.446  1.00 107.28 ? 163 LYS D CE  1 
ATOM   9062  N  NZ  . LYS D 1 99  ? 36.978 50.679 59.490  1.00 175.42 ? 163 LYS D NZ  1 
ATOM   9063  N  N   . PHE D 1 100 ? 31.855 47.665 61.055  1.00 61.73  ? 164 PHE D N   1 
ATOM   9064  C  CA  . PHE D 1 100 ? 30.901 47.968 59.977  1.00 56.38  ? 164 PHE D CA  1 
ATOM   9065  C  C   . PHE D 1 100 ? 31.644 48.527 58.777  1.00 54.68  ? 164 PHE D C   1 
ATOM   9066  O  O   . PHE D 1 100 ? 32.458 49.443 58.908  1.00 52.25  ? 164 PHE D O   1 
ATOM   9067  C  CB  . PHE D 1 100 ? 29.889 48.992 60.445  1.00 54.48  ? 164 PHE D CB  1 
ATOM   9068  C  CG  . PHE D 1 100 ? 28.758 49.201 59.504  1.00 52.09  ? 164 PHE D CG  1 
ATOM   9069  C  CD1 . PHE D 1 100 ? 28.920 50.010 58.370  1.00 52.26  ? 164 PHE D CD1 1 
ATOM   9070  C  CD2 . PHE D 1 100 ? 27.497 48.608 59.766  1.00 49.82  ? 164 PHE D CD2 1 
ATOM   9071  C  CE1 . PHE D 1 100 ? 27.845 50.209 57.471  1.00 46.57  ? 164 PHE D CE1 1 
ATOM   9072  C  CE2 . PHE D 1 100 ? 26.413 48.811 58.909  1.00 45.18  ? 164 PHE D CE2 1 
ATOM   9073  C  CZ  . PHE D 1 100 ? 26.595 49.608 57.735  1.00 44.10  ? 164 PHE D CZ  1 
ATOM   9074  N  N   . GLU D 1 101 ? 31.374 47.955 57.611  1.00 61.45  ? 165 GLU D N   1 
ATOM   9075  C  CA  . GLU D 1 101 ? 32.110 48.333 56.418  1.00 60.07  ? 165 GLU D CA  1 
ATOM   9076  C  C   . GLU D 1 101 ? 31.260 49.142 55.440  1.00 54.40  ? 165 GLU D C   1 
ATOM   9077  O  O   . GLU D 1 101 ? 31.726 50.146 54.919  1.00 53.48  ? 165 GLU D O   1 
ATOM   9078  C  CB  . GLU D 1 101 ? 32.781 47.117 55.774  1.00 54.41  ? 165 GLU D CB  1 
ATOM   9079  C  CG  . GLU D 1 101 ? 34.088 46.692 56.484  1.00 77.50  ? 165 GLU D CG  1 
ATOM   9080  C  CD  . GLU D 1 101 ? 35.285 47.677 56.338  1.00 96.21  ? 165 GLU D CD  1 
ATOM   9081  O  OE1 . GLU D 1 101 ? 35.085 48.801 55.812  1.00 120.69 ? 165 GLU D OE1 1 
ATOM   9082  O  OE2 . GLU D 1 101 ? 36.430 47.320 56.757  1.00 86.47  ? 165 GLU D OE2 1 
ATOM   9083  N  N   . ALA D 1 102 ? 30.029 48.678 55.211  1.00 51.37  ? 166 ALA D N   1 
ATOM   9084  C  CA  . ALA D 1 102 ? 29.024 49.327 54.351  1.00 48.03  ? 166 ALA D CA  1 
ATOM   9085  C  C   . ALA D 1 102 ? 27.671 48.588 54.389  1.00 50.75  ? 166 ALA D C   1 
ATOM   9086  O  O   . ALA D 1 102 ? 27.544 47.522 55.023  1.00 49.77  ? 166 ALA D O   1 
ATOM   9087  C  CB  . ALA D 1 102 ? 29.508 49.432 52.913  1.00 45.84  ? 166 ALA D CB  1 
ATOM   9088  N  N   . VAL D 1 103 ? 26.666 49.156 53.708  1.00 50.38  ? 167 VAL D N   1 
ATOM   9089  C  CA  . VAL D 1 103 ? 25.345 48.513 53.602  1.00 51.82  ? 167 VAL D CA  1 
ATOM   9090  C  C   . VAL D 1 103 ? 25.264 47.845 52.273  1.00 53.79  ? 167 VAL D C   1 
ATOM   9091  O  O   . VAL D 1 103 ? 25.495 48.493 51.255  1.00 65.28  ? 167 VAL D O   1 
ATOM   9092  C  CB  . VAL D 1 103 ? 24.173 49.489 53.629  1.00 51.95  ? 167 VAL D CB  1 
ATOM   9093  C  CG1 . VAL D 1 103 ? 24.015 50.072 54.979  1.00 75.09  ? 167 VAL D CG1 1 
ATOM   9094  C  CG2 . VAL D 1 103 ? 24.414 50.589 52.666  1.00 61.85  ? 167 VAL D CG2 1 
ATOM   9095  N  N   . GLY D 1 104 ? 24.939 46.558 52.270  1.00 49.96  ? 168 GLY D N   1 
ATOM   9096  C  CA  . GLY D 1 104 ? 24.898 45.784 51.026  1.00 49.39  ? 168 GLY D CA  1 
ATOM   9097  C  C   . GLY D 1 104 ? 24.765 44.296 51.245  1.00 48.76  ? 168 GLY D C   1 
ATOM   9098  O  O   . GLY D 1 104 ? 24.879 43.835 52.369  1.00 62.79  ? 168 GLY D O   1 
ATOM   9099  N  N   . TRP D 1 105 ? 24.513 43.538 50.189  1.00 44.57  ? 169 TRP D N   1 
ATOM   9100  C  CA  . TRP D 1 105 ? 24.303 42.112 50.342  1.00 45.58  ? 169 TRP D CA  1 
ATOM   9101  C  C   . TRP D 1 105 ? 25.332 41.441 49.558  1.00 48.29  ? 169 TRP D C   1 
ATOM   9102  O  O   . TRP D 1 105 ? 25.309 40.220 49.458  1.00 62.56  ? 169 TRP D O   1 
ATOM   9103  C  CB  . TRP D 1 105 ? 22.942 41.669 49.832  1.00 48.77  ? 169 TRP D CB  1 
ATOM   9104  C  CG  . TRP D 1 105 ? 22.703 42.039 48.388  1.00 51.59  ? 169 TRP D CG  1 
ATOM   9105  C  CD1 . TRP D 1 105 ? 23.238 41.439 47.264  1.00 52.10  ? 169 TRP D CD1 1 
ATOM   9106  C  CD2 . TRP D 1 105 ? 21.868 43.136 47.868  1.00 58.13  ? 169 TRP D CD2 1 
ATOM   9107  N  NE1 . TRP D 1 105 ? 22.806 42.060 46.118  1.00 55.47  ? 169 TRP D NE1 1 
ATOM   9108  C  CE2 . TRP D 1 105 ? 21.985 43.086 46.409  1.00 59.43  ? 169 TRP D CE2 1 
ATOM   9109  C  CE3 . TRP D 1 105 ? 21.054 44.104 48.444  1.00 66.24  ? 169 TRP D CE3 1 
ATOM   9110  C  CZ2 . TRP D 1 105 ? 21.305 43.974 45.579  1.00 68.14  ? 169 TRP D CZ2 1 
ATOM   9111  C  CZ3 . TRP D 1 105 ? 20.374 44.995 47.595  1.00 71.95  ? 169 TRP D CZ3 1 
ATOM   9112  C  CH2 . TRP D 1 105 ? 20.505 44.933 46.198  1.00 70.76  ? 169 TRP D CH2 1 
ATOM   9113  N  N   . SER D 1 106 ? 26.218 42.224 48.948  1.00 45.58  ? 170 SER D N   1 
ATOM   9114  C  CA  . SER D 1 106 ? 27.362 41.647 48.280  1.00 53.56  ? 170 SER D CA  1 
ATOM   9115  C  C   . SER D 1 106 ? 28.519 42.618 48.244  1.00 55.11  ? 170 SER D C   1 
ATOM   9116  O  O   . SER D 1 106 ? 28.321 43.810 48.010  1.00 53.26  ? 170 SER D O   1 
ATOM   9117  C  CB  . SER D 1 106 ? 26.986 41.174 46.877  1.00 57.91  ? 170 SER D CB  1 
ATOM   9118  O  OG  . SER D 1 106 ? 28.129 40.891 46.079  1.00 78.04  ? 170 SER D OG  1 
ATOM   9119  N  N   . ALA D 1 107 ? 29.727 42.090 48.439  1.00 57.29  ? 171 ALA D N   1 
ATOM   9120  C  CA  . ALA D 1 107 ? 30.925 42.927 48.635  1.00 57.68  ? 171 ALA D CA  1 
ATOM   9121  C  C   . ALA D 1 107 ? 32.233 42.312 48.211  1.00 56.00  ? 171 ALA D C   1 
ATOM   9122  O  O   . ALA D 1 107 ? 32.406 41.115 48.214  1.00 61.49  ? 171 ALA D O   1 
ATOM   9123  C  CB  . ALA D 1 107 ? 31.050 43.330 50.048  1.00 50.70  ? 171 ALA D CB  1 
ATOM   9124  N  N   . SER D 1 108 ? 33.157 43.185 47.868  1.00 56.19  ? 172 SER D N   1 
ATOM   9125  C  CA  . SER D 1 108 ? 34.493 42.808 47.560  1.00 55.66  ? 172 SER D CA  1 
ATOM   9126  C  C   . SER D 1 108 ? 35.406 43.914 48.081  1.00 62.94  ? 172 SER D C   1 
ATOM   9127  O  O   . SER D 1 108 ? 34.987 45.070 48.188  1.00 73.52  ? 172 SER D O   1 
ATOM   9128  C  CB  . SER D 1 108 ? 34.624 42.660 46.072  1.00 53.20  ? 172 SER D CB  1 
ATOM   9129  O  OG  . SER D 1 108 ? 35.981 42.830 45.698  1.00 71.87  ? 172 SER D OG  1 
ATOM   9130  N  N   . SER D 1 109 ? 36.645 43.570 48.424  1.00 60.90  ? 173 SER D N   1 
ATOM   9131  C  CA  . SER D 1 109 ? 37.564 44.570 48.989  1.00 61.66  ? 173 SER D CA  1 
ATOM   9132  C  C   . SER D 1 109 ? 39.050 44.264 48.813  1.00 56.73  ? 173 SER D C   1 
ATOM   9133  O  O   . SER D 1 109 ? 39.467 43.120 48.621  1.00 52.25  ? 173 SER D O   1 
ATOM   9134  C  CB  . SER D 1 109 ? 37.285 44.775 50.466  1.00 62.35  ? 173 SER D CB  1 
ATOM   9135  O  OG  . SER D 1 109 ? 37.815 43.683 51.186  1.00 77.56  ? 173 SER D OG  1 
ATOM   9136  N  N   . CYS D 1 110 ? 39.843 45.314 48.885  1.00 53.33  ? 174 CYS D N   1 
ATOM   9137  C  CA  . CYS D 1 110 ? 41.261 45.192 48.673  1.00 62.90  ? 174 CYS D CA  1 
ATOM   9138  C  C   . CYS D 1 110 ? 41.939 46.419 49.248  1.00 69.86  ? 174 CYS D C   1 
ATOM   9139  O  O   . CYS D 1 110 ? 41.342 47.499 49.314  1.00 62.92  ? 174 CYS D O   1 
ATOM   9140  C  CB  . CYS D 1 110 ? 41.587 45.014 47.192  1.00 65.06  ? 174 CYS D CB  1 
ATOM   9141  S  SG  . CYS D 1 110 ? 40.586 45.964 46.039  1.00 99.35  ? 174 CYS D SG  1 
ATOM   9142  N  N   . HIS D 1 111 ? 43.176 46.245 49.696  1.00 66.81  ? 175 HIS D N   1 
ATOM   9143  C  CA  . HIS D 1 111 ? 43.868 47.323 50.358  1.00 68.03  ? 175 HIS D CA  1 
ATOM   9144  C  C   . HIS D 1 111 ? 44.958 47.800 49.469  1.00 75.70  ? 175 HIS D C   1 
ATOM   9145  O  O   . HIS D 1 111 ? 45.815 47.014 49.076  1.00 99.09  ? 175 HIS D O   1 
ATOM   9146  C  CB  . HIS D 1 111 ? 44.423 46.849 51.696  1.00 65.40  ? 175 HIS D CB  1 
ATOM   9147  C  CG  . HIS D 1 111 ? 44.926 47.966 52.568  1.00 68.25  ? 175 HIS D CG  1 
ATOM   9148  N  ND1 . HIS D 1 111 ? 46.156 48.496 52.428  1.00 73.28  ? 175 HIS D ND1 1 
ATOM   9149  C  CD2 . HIS D 1 111 ? 44.305 48.674 53.588  1.00 67.03  ? 175 HIS D CD2 1 
ATOM   9150  C  CE1 . HIS D 1 111 ? 46.319 49.486 53.323  1.00 74.27  ? 175 HIS D CE1 1 
ATOM   9151  N  NE2 . HIS D 1 111 ? 45.180 49.602 54.027  1.00 72.76  ? 175 HIS D NE2 1 
ATOM   9152  N  N   . ASP D 1 112 ? 44.948 49.087 49.136  1.00 76.13  ? 176 ASP D N   1 
ATOM   9153  C  CA  . ASP D 1 112 ? 45.974 49.612 48.228  1.00 83.76  ? 176 ASP D CA  1 
ATOM   9154  C  C   . ASP D 1 112 ? 47.350 49.926 48.847  1.00 84.29  ? 176 ASP D C   1 
ATOM   9155  O  O   . ASP D 1 112 ? 48.325 50.112 48.117  1.00 87.79  ? 176 ASP D O   1 
ATOM   9156  C  CB  . ASP D 1 112 ? 45.443 50.803 47.424  1.00 81.52  ? 176 ASP D CB  1 
ATOM   9157  C  CG  . ASP D 1 112 ? 45.077 52.000 48.288  1.00 87.39  ? 176 ASP D CG  1 
ATOM   9158  O  OD1 . ASP D 1 112 ? 45.255 51.952 49.533  1.00 75.78  ? 176 ASP D OD1 1 
ATOM   9159  O  OD2 . ASP D 1 112 ? 44.607 53.005 47.694  1.00 86.77  ? 176 ASP D OD2 1 
ATOM   9160  N  N   . GLY D 1 113 ? 47.423 49.970 50.176  1.00 75.81  ? 177 GLY D N   1 
ATOM   9161  C  CA  . GLY D 1 113 ? 48.637 50.412 50.875  1.00 76.12  ? 177 GLY D CA  1 
ATOM   9162  C  C   . GLY D 1 113 ? 48.379 51.669 51.689  1.00 78.56  ? 177 GLY D C   1 
ATOM   9163  O  O   . GLY D 1 113 ? 49.195 52.071 52.521  1.00 73.68  ? 177 GLY D O   1 
ATOM   9164  N  N   . PHE D 1 114 ? 47.223 52.283 51.446  1.00 90.89  ? 178 PHE D N   1 
ATOM   9165  C  CA  . PHE D 1 114 ? 46.815 53.491 52.148  1.00 76.15  ? 178 PHE D CA  1 
ATOM   9166  C  C   . PHE D 1 114 ? 45.539 53.273 52.914  1.00 70.45  ? 178 PHE D C   1 
ATOM   9167  O  O   . PHE D 1 114 ? 45.528 53.399 54.127  1.00 78.31  ? 178 PHE D O   1 
ATOM   9168  C  CB  . PHE D 1 114 ? 46.634 54.621 51.163  1.00 78.09  ? 178 PHE D CB  1 
ATOM   9169  C  CG  . PHE D 1 114 ? 47.876 54.954 50.405  1.00 78.57  ? 178 PHE D CG  1 
ATOM   9170  C  CD1 . PHE D 1 114 ? 48.916 55.624 51.030  1.00 80.44  ? 178 PHE D CD1 1 
ATOM   9171  C  CD2 . PHE D 1 114 ? 48.007 54.599 49.069  1.00 77.45  ? 178 PHE D CD2 1 
ATOM   9172  C  CE1 . PHE D 1 114 ? 50.063 55.937 50.334  1.00 91.53  ? 178 PHE D CE1 1 
ATOM   9173  C  CE2 . PHE D 1 114 ? 49.150 54.910 48.364  1.00 86.21  ? 178 PHE D CE2 1 
ATOM   9174  C  CZ  . PHE D 1 114 ? 50.184 55.583 48.992  1.00 91.28  ? 178 PHE D CZ  1 
ATOM   9175  N  N   . GLN D 1 115 ? 44.474 52.921 52.201  1.00 67.71  ? 179 GLN D N   1 
ATOM   9176  C  CA  . GLN D 1 115 ? 43.163 52.681 52.806  1.00 64.70  ? 179 GLN D CA  1 
ATOM   9177  C  C   . GLN D 1 115 ? 42.551 51.384 52.277  1.00 58.70  ? 179 GLN D C   1 
ATOM   9178  O  O   . GLN D 1 115 ? 43.039 50.819 51.299  1.00 71.30  ? 179 GLN D O   1 
ATOM   9179  C  CB  . GLN D 1 115 ? 42.234 53.871 52.509  1.00 70.23  ? 179 GLN D CB  1 
ATOM   9180  C  CG  . GLN D 1 115 ? 42.666 55.227 53.135  1.00 77.65  ? 179 GLN D CG  1 
ATOM   9181  C  CD  . GLN D 1 115 ? 42.573 55.234 54.653  1.00 75.69  ? 179 GLN D CD  1 
ATOM   9182  O  OE1 . GLN D 1 115 ? 41.885 54.409 55.257  1.00 97.08  ? 179 GLN D OE1 1 
ATOM   9183  N  NE2 . GLN D 1 115 ? 43.283 56.147 55.273  1.00 75.48  ? 179 GLN D NE2 1 
ATOM   9184  N  N   . TRP D 1 116 ? 41.497 50.900 52.918  1.00 51.53  ? 180 TRP D N   1 
ATOM   9185  C  CA  . TRP D 1 116 ? 40.696 49.822 52.327  1.00 51.89  ? 180 TRP D CA  1 
ATOM   9186  C  C   . TRP D 1 116 ? 39.706 50.358 51.336  1.00 64.98  ? 180 TRP D C   1 
ATOM   9187  O  O   . TRP D 1 116 ? 38.936 51.306 51.597  1.00 64.42  ? 180 TRP D O   1 
ATOM   9188  C  CB  . TRP D 1 116 ? 39.894 49.067 53.369  1.00 47.44  ? 180 TRP D CB  1 
ATOM   9189  C  CG  . TRP D 1 116 ? 40.688 48.130 54.192  1.00 46.69  ? 180 TRP D CG  1 
ATOM   9190  C  CD1 . TRP D 1 116 ? 41.229 48.346 55.449  1.00 49.61  ? 180 TRP D CD1 1 
ATOM   9191  C  CD2 . TRP D 1 116 ? 41.077 46.789 53.839  1.00 52.35  ? 180 TRP D CD2 1 
ATOM   9192  N  NE1 . TRP D 1 116 ? 41.924 47.250 55.882  1.00 45.88  ? 180 TRP D NE1 1 
ATOM   9193  C  CE2 . TRP D 1 116 ? 41.871 46.279 54.961  1.00 48.02  ? 180 TRP D CE2 1 
ATOM   9194  C  CE3 . TRP D 1 116 ? 40.871 45.978 52.736  1.00 65.28  ? 180 TRP D CE3 1 
ATOM   9195  C  CZ2 . TRP D 1 116 ? 42.404 45.004 54.960  1.00 46.81  ? 180 TRP D CZ2 1 
ATOM   9196  C  CZ3 . TRP D 1 116 ? 41.424 44.694 52.746  1.00 60.38  ? 180 TRP D CZ3 1 
ATOM   9197  C  CH2 . TRP D 1 116 ? 42.165 44.220 53.836  1.00 50.73  ? 180 TRP D CH2 1 
ATOM   9198  N  N   . THR D 1 117 ? 39.678 49.724 50.183  1.00 79.43  ? 181 THR D N   1 
ATOM   9199  C  CA  . THR D 1 117 ? 38.641 50.002 49.215  1.00 68.93  ? 181 THR D CA  1 
ATOM   9200  C  C   . THR D 1 117 ? 37.633 48.878 49.381  1.00 62.02  ? 181 THR D C   1 
ATOM   9201  O  O   . THR D 1 117 ? 38.005 47.689 49.491  1.00 55.11  ? 181 THR D O   1 
ATOM   9202  C  CB  . THR D 1 117 ? 39.231 50.051 47.802  1.00 74.94  ? 181 THR D CB  1 
ATOM   9203  O  OG1 . THR D 1 117 ? 40.192 51.118 47.728  1.00 80.35  ? 181 THR D OG1 1 
ATOM   9204  C  CG2 . THR D 1 117 ? 38.160 50.269 46.773  1.00 72.41  ? 181 THR D CG2 1 
ATOM   9205  N  N   . VAL D 1 118 ? 36.367 49.269 49.466  1.00 59.13  ? 182 VAL D N   1 
ATOM   9206  C  CA  . VAL D 1 118 ? 35.281 48.304 49.544  1.00 58.37  ? 182 VAL D CA  1 
ATOM   9207  C  C   . VAL D 1 118 ? 34.168 48.619 48.554  1.00 63.24  ? 182 VAL D C   1 
ATOM   9208  O  O   . VAL D 1 118 ? 33.638 49.750 48.523  1.00 72.46  ? 182 VAL D O   1 
ATOM   9209  C  CB  . VAL D 1 118 ? 34.720 48.179 50.953  1.00 50.02  ? 182 VAL D CB  1 
ATOM   9210  C  CG1 . VAL D 1 118 ? 33.501 47.270 50.954  1.00 56.47  ? 182 VAL D CG1 1 
ATOM   9211  C  CG2 . VAL D 1 118 ? 35.750 47.605 51.849  1.00 42.74  ? 182 VAL D CG2 1 
ATOM   9212  N  N   . LEU D 1 119 ? 33.844 47.604 47.747  1.00 61.59  ? 183 LEU D N   1 
ATOM   9213  C  CA  . LEU D 1 119 ? 32.717 47.641 46.809  1.00 70.56  ? 183 LEU D CA  1 
ATOM   9214  C  C   . LEU D 1 119 ? 31.521 46.894 47.378  1.00 60.48  ? 183 LEU D C   1 
ATOM   9215  O  O   . LEU D 1 119 ? 31.613 45.701 47.666  1.00 61.49  ? 183 LEU D O   1 
ATOM   9216  C  CB  . LEU D 1 119 ? 33.120 47.014 45.477  1.00 65.81  ? 183 LEU D CB  1 
ATOM   9217  C  CG  . LEU D 1 119 ? 34.329 47.693 44.856  1.00 65.21  ? 183 LEU D CG  1 
ATOM   9218  C  CD1 . LEU D 1 119 ? 35.351 46.671 44.605  1.00 74.82  ? 183 LEU D CD1 1 
ATOM   9219  C  CD2 . LEU D 1 119 ? 33.964 48.415 43.576  1.00 67.76  ? 183 LEU D CD2 1 
ATOM   9220  N  N   . SER D 1 120 ? 30.400 47.595 47.525  1.00 53.09  ? 184 SER D N   1 
ATOM   9221  C  CA  . SER D 1 120 ? 29.197 46.958 48.020  1.00 52.98  ? 184 SER D CA  1 
ATOM   9222  C  C   . SER D 1 120 ? 28.041 47.139 47.075  1.00 55.09  ? 184 SER D C   1 
ATOM   9223  O  O   . SER D 1 120 ? 27.958 48.148 46.381  1.00 67.20  ? 184 SER D O   1 
ATOM   9224  C  CB  . SER D 1 120 ? 28.834 47.527 49.358  1.00 60.05  ? 184 SER D CB  1 
ATOM   9225  O  OG  . SER D 1 120 ? 27.709 46.875 49.888  1.00 67.57  ? 184 SER D OG  1 
ATOM   9226  N  N   . VAL D 1 121 ? 27.171 46.136 47.036  1.00 51.10  ? 185 VAL D N   1 
ATOM   9227  C  CA  . VAL D 1 121 ? 25.944 46.188 46.254  1.00 51.44  ? 185 VAL D CA  1 
ATOM   9228  C  C   . VAL D 1 121 ? 24.711 46.310 47.159  1.00 57.97  ? 185 VAL D C   1 
ATOM   9229  O  O   . VAL D 1 121 ? 24.453 45.399 47.950  1.00 60.82  ? 185 VAL D O   1 
ATOM   9230  C  CB  . VAL D 1 121 ? 25.785 44.920 45.517  1.00 47.08  ? 185 VAL D CB  1 
ATOM   9231  C  CG1 . VAL D 1 121 ? 24.475 44.925 44.770  1.00 46.14  ? 185 VAL D CG1 1 
ATOM   9232  C  CG2 . VAL D 1 121 ? 26.938 44.743 44.599  1.00 50.94  ? 185 VAL D CG2 1 
ATOM   9233  N  N   . ALA D 1 122 ? 23.951 47.406 47.032  1.00 57.15  ? 186 ALA D N   1 
ATOM   9234  C  CA  . ALA D 1 122 ? 22.812 47.687 47.925  1.00 56.79  ? 186 ALA D CA  1 
ATOM   9235  C  C   . ALA D 1 122 ? 21.549 48.216 47.230  1.00 60.62  ? 186 ALA D C   1 
ATOM   9236  O  O   . ALA D 1 122 ? 21.547 48.431 46.018  1.00 56.61  ? 186 ALA D O   1 
ATOM   9237  C  CB  . ALA D 1 122 ? 23.235 48.631 48.977  1.00 58.51  ? 186 ALA D CB  1 
ATOM   9238  N  N   . GLY D 1 123 ? 20.485 48.400 48.020  1.00 63.46  ? 187 GLY D N   1 
ATOM   9239  C  CA  . GLY D 1 123 ? 19.150 48.857 47.545  1.00 77.26  ? 187 GLY D CA  1 
ATOM   9240  C  C   . GLY D 1 123 ? 18.654 48.408 46.159  1.00 81.75  ? 187 GLY D C   1 
ATOM   9241  O  O   . GLY D 1 123 ? 18.301 47.248 45.944  1.00 76.70  ? 187 GLY D O   1 
ATOM   9242  N  N   . ASP D 1 124 ? 18.606 49.362 45.229  1.00 81.06  ? 188 ASP D N   1 
ATOM   9243  C  CA  . ASP D 1 124 ? 18.296 49.129 43.827  1.00 78.44  ? 188 ASP D CA  1 
ATOM   9244  C  C   . ASP D 1 124 ? 19.060 47.907 43.257  1.00 78.92  ? 188 ASP D C   1 
ATOM   9245  O  O   . ASP D 1 124 ? 18.520 47.137 42.469  1.00 84.38  ? 188 ASP D O   1 
ATOM   9246  C  CB  . ASP D 1 124 ? 18.587 50.432 43.037  1.00 91.32  ? 188 ASP D CB  1 
ATOM   9247  C  CG  . ASP D 1 124 ? 18.506 50.266 41.506  1.00 121.78 ? 188 ASP D CG  1 
ATOM   9248  O  OD1 . ASP D 1 124 ? 17.519 49.685 40.997  1.00 142.32 ? 188 ASP D OD1 1 
ATOM   9249  O  OD2 . ASP D 1 124 ? 19.432 50.753 40.807  1.00 114.61 ? 188 ASP D OD2 1 
ATOM   9250  N  N   . GLY D 1 125 ? 20.300 47.713 43.692  1.00 69.36  ? 189 GLY D N   1 
ATOM   9251  C  CA  . GLY D 1 125 ? 21.190 46.768 43.052  1.00 70.70  ? 189 GLY D CA  1 
ATOM   9252  C  C   . GLY D 1 125 ? 22.368 47.475 42.390  1.00 79.20  ? 189 GLY D C   1 
ATOM   9253  O  O   . GLY D 1 125 ? 22.995 46.930 41.460  1.00 71.26  ? 189 GLY D O   1 
ATOM   9254  N  N   . PHE D 1 126 ? 22.670 48.689 42.867  1.00 73.01  ? 190 PHE D N   1 
ATOM   9255  C  CA  . PHE D 1 126 ? 23.870 49.430 42.451  1.00 63.45  ? 190 PHE D CA  1 
ATOM   9256  C  C   . PHE D 1 126 ? 25.072 49.191 43.354  1.00 61.69  ? 190 PHE D C   1 
ATOM   9257  O  O   . PHE D 1 126 ? 24.989 48.502 44.374  1.00 61.83  ? 190 PHE D O   1 
ATOM   9258  C  CB  . PHE D 1 126 ? 23.588 50.922 42.375  1.00 61.62  ? 190 PHE D CB  1 
ATOM   9259  C  CG  . PHE D 1 126 ? 23.441 51.583 43.702  1.00 71.49  ? 190 PHE D CG  1 
ATOM   9260  C  CD1 . PHE D 1 126 ? 24.461 52.376 44.211  1.00 78.01  ? 190 PHE D CD1 1 
ATOM   9261  C  CD2 . PHE D 1 126 ? 22.277 51.440 44.445  1.00 82.72  ? 190 PHE D CD2 1 
ATOM   9262  C  CE1 . PHE D 1 126 ? 24.332 53.007 45.444  1.00 67.23  ? 190 PHE D CE1 1 
ATOM   9263  C  CE2 . PHE D 1 126 ? 22.148 52.061 45.681  1.00 78.96  ? 190 PHE D CE2 1 
ATOM   9264  C  CZ  . PHE D 1 126 ? 23.177 52.845 46.171  1.00 71.95  ? 190 PHE D CZ  1 
ATOM   9265  N  N   . VAL D 1 127 ? 26.193 49.787 42.979  1.00 59.53  ? 191 VAL D N   1 
ATOM   9266  C  CA  . VAL D 1 127 ? 27.427 49.598 43.719  1.00 58.96  ? 191 VAL D CA  1 
ATOM   9267  C  C   . VAL D 1 127 ? 27.897 50.888 44.363  1.00 59.40  ? 191 VAL D C   1 
ATOM   9268  O  O   . VAL D 1 127 ? 28.078 51.888 43.685  1.00 72.62  ? 191 VAL D O   1 
ATOM   9269  C  CB  . VAL D 1 127 ? 28.504 49.039 42.794  1.00 63.67  ? 191 VAL D CB  1 
ATOM   9270  C  CG1 . VAL D 1 127 ? 29.894 49.389 43.271  1.00 69.65  ? 191 VAL D CG1 1 
ATOM   9271  C  CG2 . VAL D 1 127 ? 28.360 47.552 42.706  1.00 81.26  ? 191 VAL D CG2 1 
ATOM   9272  N  N   . SER D 1 128 ? 28.065 50.870 45.677  1.00 58.70  ? 192 SER D N   1 
ATOM   9273  C  CA  . SER D 1 128 ? 28.793 51.922 46.384  1.00 61.57  ? 192 SER D CA  1 
ATOM   9274  C  C   . SER D 1 128 ? 30.234 51.502 46.437  1.00 71.99  ? 192 SER D C   1 
ATOM   9275  O  O   . SER D 1 128 ? 30.551 50.309 46.603  1.00 84.22  ? 192 SER D O   1 
ATOM   9276  C  CB  . SER D 1 128 ? 28.323 52.033 47.827  1.00 59.74  ? 192 SER D CB  1 
ATOM   9277  O  OG  . SER D 1 128 ? 26.985 52.438 47.897  1.00 69.82  ? 192 SER D OG  1 
ATOM   9278  N  N   . ILE D 1 129 ? 31.115 52.476 46.309  1.00 75.90  ? 193 ILE D N   1 
ATOM   9279  C  CA  . ILE D 1 129 ? 32.541 52.214 46.436  1.00 81.54  ? 193 ILE D CA  1 
ATOM   9280  C  C   . ILE D 1 129 ? 32.988 53.045 47.597  1.00 88.71  ? 193 ILE D C   1 
ATOM   9281  O  O   . ILE D 1 129 ? 32.839 54.291 47.567  1.00 73.83  ? 193 ILE D O   1 
ATOM   9282  C  CB  . ILE D 1 129 ? 33.325 52.660 45.184  1.00 72.88  ? 193 ILE D CB  1 
ATOM   9283  C  CG1 . ILE D 1 129 ? 33.017 51.743 44.012  1.00 63.71  ? 193 ILE D CG1 1 
ATOM   9284  C  CG2 . ILE D 1 129 ? 34.804 52.636 45.448  1.00 67.46  ? 193 ILE D CG2 1 
ATOM   9285  C  CD1 . ILE D 1 129 ? 33.491 52.286 42.708  1.00 68.92  ? 193 ILE D CD1 1 
ATOM   9286  N  N   . LEU D 1 130 ? 33.523 52.387 48.625  1.00 78.60  ? 194 LEU D N   1 
ATOM   9287  C  CA  . LEU D 1 130 ? 34.060 53.180 49.714  1.00 70.85  ? 194 LEU D CA  1 
ATOM   9288  C  C   . LEU D 1 130 ? 35.520 52.998 50.112  1.00 63.65  ? 194 LEU D C   1 
ATOM   9289  O  O   . LEU D 1 130 ? 36.006 51.891 50.346  1.00 64.15  ? 194 LEU D O   1 
ATOM   9290  C  CB  . LEU D 1 130 ? 33.100 53.237 50.890  1.00 77.95  ? 194 LEU D CB  1 
ATOM   9291  C  CG  . LEU D 1 130 ? 32.492 51.962 51.425  1.00 79.85  ? 194 LEU D CG  1 
ATOM   9292  C  CD1 . LEU D 1 130 ? 33.203 51.627 52.742  1.00 114.50 ? 194 LEU D CD1 1 
ATOM   9293  C  CD2 . LEU D 1 130 ? 31.039 52.244 51.650  1.00 60.36  ? 194 LEU D CD2 1 
ATOM   9294  N  N   . TYR D 1 131 ? 36.200 54.136 50.162  1.00 64.23  ? 195 TYR D N   1 
ATOM   9295  C  CA  . TYR D 1 131 ? 37.622 54.193 50.394  1.00 65.01  ? 195 TYR D CA  1 
ATOM   9296  C  C   . TYR D 1 131 ? 37.810 54.685 51.802  1.00 68.16  ? 195 TYR D C   1 
ATOM   9297  O  O   . TYR D 1 131 ? 37.417 55.804 52.115  1.00 65.62  ? 195 TYR D O   1 
ATOM   9298  C  CB  . TYR D 1 131 ? 38.270 55.158 49.406  1.00 67.03  ? 195 TYR D CB  1 
ATOM   9299  C  CG  . TYR D 1 131 ? 39.775 55.098 49.343  1.00 75.18  ? 195 TYR D CG  1 
ATOM   9300  C  CD1 . TYR D 1 131 ? 40.431 53.997 48.782  1.00 85.51  ? 195 TYR D CD1 1 
ATOM   9301  C  CD2 . TYR D 1 131 ? 40.553 56.147 49.836  1.00 82.90  ? 195 TYR D CD2 1 
ATOM   9302  C  CE1 . TYR D 1 131 ? 41.828 53.933 48.732  1.00 91.89  ? 195 TYR D CE1 1 
ATOM   9303  C  CE2 . TYR D 1 131 ? 41.947 56.099 49.787  1.00 93.82  ? 195 TYR D CE2 1 
ATOM   9304  C  CZ  . TYR D 1 131 ? 42.576 54.994 49.233  1.00 103.95 ? 195 TYR D CZ  1 
ATOM   9305  O  OH  . TYR D 1 131 ? 43.948 54.968 49.180  1.00 116.65 ? 195 TYR D OH  1 
ATOM   9306  N  N   . GLY D 1 132 ? 38.373 53.824 52.653  1.00 70.91  ? 196 GLY D N   1 
ATOM   9307  C  CA  . GLY D 1 132 ? 38.671 54.161 54.044  1.00 70.69  ? 196 GLY D CA  1 
ATOM   9308  C  C   . GLY D 1 132 ? 37.430 54.479 54.851  1.00 74.92  ? 196 GLY D C   1 
ATOM   9309  O  O   . GLY D 1 132 ? 37.467 55.313 55.766  1.00 80.43  ? 196 GLY D O   1 
ATOM   9310  N  N   . GLY D 1 133 ? 36.324 53.831 54.493  1.00 71.50  ? 197 GLY D N   1 
ATOM   9311  C  CA  . GLY D 1 133 ? 35.070 53.994 55.222  1.00 65.20  ? 197 GLY D CA  1 
ATOM   9312  C  C   . GLY D 1 133 ? 34.127 55.070 54.714  1.00 58.82  ? 197 GLY D C   1 
ATOM   9313  O  O   . GLY D 1 133 ? 33.011 55.147 55.185  1.00 60.81  ? 197 GLY D O   1 
ATOM   9314  N  N   . ILE D 1 134 ? 34.568 55.895 53.765  1.00 57.82  ? 198 ILE D N   1 
ATOM   9315  C  CA  . ILE D 1 134 ? 33.746 56.995 53.267  1.00 66.20  ? 198 ILE D CA  1 
ATOM   9316  C  C   . ILE D 1 134 ? 33.424 56.754 51.815  1.00 73.69  ? 198 ILE D C   1 
ATOM   9317  O  O   . ILE D 1 134 ? 34.227 56.170 51.091  1.00 80.85  ? 198 ILE D O   1 
ATOM   9318  C  CB  . ILE D 1 134 ? 34.392 58.396 53.471  1.00 68.64  ? 198 ILE D CB  1 
ATOM   9319  C  CG1 . ILE D 1 134 ? 35.621 58.566 52.585  1.00 94.83  ? 198 ILE D CG1 1 
ATOM   9320  C  CG2 . ILE D 1 134 ? 34.773 58.594 54.935  1.00 73.18  ? 198 ILE D CG2 1 
ATOM   9321  C  CD1 . ILE D 1 134 ? 36.260 59.950 52.622  1.00 112.70 ? 198 ILE D CD1 1 
ATOM   9322  N  N   . ILE D 1 135 ? 32.249 57.203 51.391  1.00 81.92  ? 199 ILE D N   1 
ATOM   9323  C  CA  . ILE D 1 135 ? 31.759 56.900 50.049  1.00 76.29  ? 199 ILE D CA  1 
ATOM   9324  C  C   . ILE D 1 135 ? 32.352 57.818 48.998  1.00 83.28  ? 199 ILE D C   1 
ATOM   9325  O  O   . ILE D 1 135 ? 32.041 59.010 48.953  1.00 97.61  ? 199 ILE D O   1 
ATOM   9326  C  CB  . ILE D 1 135 ? 30.239 56.987 49.974  1.00 71.77  ? 199 ILE D CB  1 
ATOM   9327  C  CG1 . ILE D 1 135 ? 29.628 56.122 51.072  1.00 62.50  ? 199 ILE D CG1 1 
ATOM   9328  C  CG2 . ILE D 1 135 ? 29.757 56.614 48.575  1.00 73.55  ? 199 ILE D CG2 1 
ATOM   9329  C  CD1 . ILE D 1 135 ? 28.638 55.125 50.583  1.00 58.80  ? 199 ILE D CD1 1 
ATOM   9330  N  N   . THR D 1 136 ? 33.181 57.244 48.136  1.00 87.28  ? 200 THR D N   1 
ATOM   9331  C  CA  . THR D 1 136 ? 33.912 58.013 47.127  1.00 82.19  ? 200 THR D CA  1 
ATOM   9332  C  C   . THR D 1 136 ? 33.307 57.905 45.730  1.00 81.61  ? 200 THR D C   1 
ATOM   9333  O  O   . THR D 1 136 ? 33.565 58.768 44.882  1.00 92.10  ? 200 THR D O   1 
ATOM   9334  C  CB  . THR D 1 136 ? 35.401 57.591 47.056  1.00 79.00  ? 200 THR D CB  1 
ATOM   9335  O  OG1 . THR D 1 136 ? 35.478 56.176 46.892  1.00 87.06  ? 200 THR D OG1 1 
ATOM   9336  C  CG2 . THR D 1 136 ? 36.130 57.951 48.328  1.00 81.56  ? 200 THR D CG2 1 
ATOM   9337  N  N   . ASP D 1 137 ? 32.531 56.845 45.480  1.00 75.58  ? 201 ASP D N   1 
ATOM   9338  C  CA  . ASP D 1 137 ? 31.953 56.620 44.148  1.00 82.15  ? 201 ASP D CA  1 
ATOM   9339  C  C   . ASP D 1 137 ? 30.839 55.589 44.109  1.00 81.25  ? 201 ASP D C   1 
ATOM   9340  O  O   . ASP D 1 137 ? 30.793 54.682 44.933  1.00 94.04  ? 201 ASP D O   1 
ATOM   9341  C  CB  . ASP D 1 137 ? 33.039 56.228 43.140  1.00 93.35  ? 201 ASP D CB  1 
ATOM   9342  C  CG  . ASP D 1 137 ? 32.715 56.675 41.709  1.00 121.81 ? 201 ASP D CG  1 
ATOM   9343  O  OD1 . ASP D 1 137 ? 31.547 56.575 41.272  1.00 159.57 ? 201 ASP D OD1 1 
ATOM   9344  O  OD2 . ASP D 1 137 ? 33.639 57.131 41.004  1.00 115.56 ? 201 ASP D OD2 1 
ATOM   9345  N  N   . THR D 1 138 ? 29.943 55.746 43.138  1.00 90.24  ? 202 THR D N   1 
ATOM   9346  C  CA  . THR D 1 138 ? 28.850 54.806 42.898  1.00 93.74  ? 202 THR D CA  1 
ATOM   9347  C  C   . THR D 1 138 ? 28.839 54.380 41.439  1.00 90.34  ? 202 THR D C   1 
ATOM   9348  O  O   . THR D 1 138 ? 29.179 55.156 40.541  1.00 113.79 ? 202 THR D O   1 
ATOM   9349  C  CB  . THR D 1 138 ? 27.439 55.386 43.277  1.00 96.24  ? 202 THR D CB  1 
ATOM   9350  O  OG1 . THR D 1 138 ? 27.149 56.545 42.482  1.00 86.09  ? 202 THR D OG1 1 
ATOM   9351  C  CG2 . THR D 1 138 ? 27.360 55.753 44.772  1.00 86.47  ? 202 THR D CG2 1 
ATOM   9352  N  N   . ILE D 1 139 ? 28.432 53.142 41.212  1.00 75.89  ? 203 ILE D N   1 
ATOM   9353  C  CA  . ILE D 1 139 ? 28.296 52.611 39.866  1.00 72.58  ? 203 ILE D CA  1 
ATOM   9354  C  C   . ILE D 1 139 ? 26.884 52.087 39.686  1.00 79.40  ? 203 ILE D C   1 
ATOM   9355  O  O   . ILE D 1 139 ? 26.361 51.386 40.576  1.00 80.09  ? 203 ILE D O   1 
ATOM   9356  C  CB  . ILE D 1 139 ? 29.269 51.474 39.658  1.00 69.17  ? 203 ILE D CB  1 
ATOM   9357  C  CG1 . ILE D 1 139 ? 30.703 51.988 39.779  1.00 71.57  ? 203 ILE D CG1 1 
ATOM   9358  C  CG2 . ILE D 1 139 ? 29.030 50.788 38.319  1.00 63.58  ? 203 ILE D CG2 1 
ATOM   9359  C  CD1 . ILE D 1 139 ? 31.759 50.889 39.716  1.00 65.53  ? 203 ILE D CD1 1 
ATOM   9360  N  N   . HIS D 1 140 ? 26.270 52.434 38.549  1.00 80.76  ? 204 HIS D N   1 
ATOM   9361  C  CA  . HIS D 1 140 ? 24.884 52.016 38.253  1.00 86.63  ? 204 HIS D CA  1 
ATOM   9362  C  C   . HIS D 1 140 ? 24.709 51.041 37.096  1.00 92.20  ? 204 HIS D C   1 
ATOM   9363  O  O   . HIS D 1 140 ? 25.482 51.065 36.116  1.00 82.44  ? 204 HIS D O   1 
ATOM   9364  C  CB  . HIS D 1 140 ? 23.982 53.227 38.109  1.00 79.24  ? 204 HIS D CB  1 
ATOM   9365  C  CG  . HIS D 1 140 ? 24.074 54.161 39.271  1.00 87.67  ? 204 HIS D CG  1 
ATOM   9366  N  ND1 . HIS D 1 140 ? 23.281 54.051 40.347  1.00 102.38 ? 204 HIS D ND1 1 
ATOM   9367  C  CD2 . HIS D 1 140 ? 24.935 55.212 39.519  1.00 86.02  ? 204 HIS D CD2 1 
ATOM   9368  C  CE1 . HIS D 1 140 ? 23.606 54.999 41.234  1.00 103.86 ? 204 HIS D CE1 1 
ATOM   9369  N  NE2 . HIS D 1 140 ? 24.618 55.711 40.723  1.00 105.36 ? 204 HIS D NE2 1 
ATOM   9370  N  N   . PRO D 1 141 ? 23.686 50.162 37.198  1.00 80.88  ? 205 PRO D N   1 
ATOM   9371  C  CA  . PRO D 1 141 ? 23.476 49.134 36.200  1.00 80.60  ? 205 PRO D CA  1 
ATOM   9372  C  C   . PRO D 1 141 ? 22.894 49.716 34.927  1.00 95.00  ? 205 PRO D C   1 
ATOM   9373  O  O   . PRO D 1 141 ? 21.918 50.476 34.968  1.00 111.72 ? 205 PRO D O   1 
ATOM   9374  C  CB  . PRO D 1 141 ? 22.442 48.211 36.854  1.00 77.27  ? 205 PRO D CB  1 
ATOM   9375  C  CG  . PRO D 1 141 ? 22.262 48.704 38.254  1.00 73.95  ? 205 PRO D CG  1 
ATOM   9376  C  CD  . PRO D 1 141 ? 22.636 50.132 38.231  1.00 77.60  ? 205 PRO D CD  1 
ATOM   9377  N  N   . THR D 1 142 ? 23.508 49.360 33.808  1.00 105.22 ? 206 THR D N   1 
ATOM   9378  C  CA  . THR D 1 142 ? 22.984 49.695 32.491  1.00 132.11 ? 206 THR D CA  1 
ATOM   9379  C  C   . THR D 1 142 ? 22.135 48.514 32.011  1.00 126.85 ? 206 THR D C   1 
ATOM   9380  O  O   . THR D 1 142 ? 20.912 48.617 31.860  1.00 117.32 ? 206 THR D O   1 
ATOM   9381  C  CB  . THR D 1 142 ? 24.134 49.987 31.474  1.00 142.44 ? 206 THR D CB  1 
ATOM   9382  O  OG1 . THR D 1 142 ? 24.882 48.789 31.228  1.00 146.55 ? 206 THR D OG1 1 
ATOM   9383  C  CG2 . THR D 1 142 ? 25.089 51.074 31.998  1.00 130.62 ? 206 THR D CG2 1 
ATOM   9384  N  N   . ASN D 1 143 ? 22.811 47.384 31.830  1.00 130.35 ? 207 ASN D N   1 
ATOM   9385  C  CA  . ASN D 1 143 ? 22.234 46.138 31.346  1.00 135.61 ? 207 ASN D CA  1 
ATOM   9386  C  C   . ASN D 1 143 ? 21.022 45.621 32.145  1.00 144.03 ? 207 ASN D C   1 
ATOM   9387  O  O   . ASN D 1 143 ? 20.519 44.521 31.874  1.00 141.55 ? 207 ASN D O   1 
ATOM   9388  C  CB  . ASN D 1 143 ? 23.363 45.109 31.184  1.00 133.82 ? 207 ASN D CB  1 
ATOM   9389  C  CG  . ASN D 1 143 ? 23.314 44.387 29.862  1.00 125.95 ? 207 ASN D CG  1 
ATOM   9390  O  OD1 . ASN D 1 143 ? 23.041 44.989 28.828  1.00 141.48 ? 207 ASN D OD1 1 
ATOM   9391  N  ND2 . ASN D 1 143 ? 23.599 43.092 29.881  1.00 130.49 ? 207 ASN D ND2 1 
ATOM   9392  N  N   . GLY D 1 144 ? 20.575 46.408 33.131  1.00 124.91 ? 208 GLY D N   1 
ATOM   9393  C  CA  . GLY D 1 144 ? 19.423 46.065 33.968  1.00 117.87 ? 208 GLY D CA  1 
ATOM   9394  C  C   . GLY D 1 144 ? 19.708 45.053 35.060  1.00 121.49 ? 208 GLY D C   1 
ATOM   9395  O  O   . GLY D 1 144 ? 20.785 44.455 35.093  1.00 143.04 ? 208 GLY D O   1 
ATOM   9396  N  N   . GLY D 1 145 ? 18.742 44.863 35.961  1.00 132.52 ? 209 GLY D N   1 
ATOM   9397  C  CA  . GLY D 1 145 ? 18.880 43.901 37.061  1.00 130.60 ? 209 GLY D CA  1 
ATOM   9398  C  C   . GLY D 1 145 ? 20.097 44.208 37.913  1.00 108.58 ? 209 GLY D C   1 
ATOM   9399  O  O   . GLY D 1 145 ? 20.895 45.064 37.546  1.00 109.02 ? 209 GLY D O   1 
ATOM   9400  N  N   . PRO D 1 146 ? 20.271 43.489 39.037  1.00 100.33 ? 210 PRO D N   1 
ATOM   9401  C  CA  . PRO D 1 146 ? 21.242 43.916 40.060  1.00 81.33  ? 210 PRO D CA  1 
ATOM   9402  C  C   . PRO D 1 146 ? 22.676 43.706 39.616  1.00 68.14  ? 210 PRO D C   1 
ATOM   9403  O  O   . PRO D 1 146 ? 22.937 42.733 38.908  1.00 80.73  ? 210 PRO D O   1 
ATOM   9404  C  CB  . PRO D 1 146 ? 20.937 42.976 41.216  1.00 77.41  ? 210 PRO D CB  1 
ATOM   9405  C  CG  . PRO D 1 146 ? 20.471 41.708 40.553  1.00 74.77  ? 210 PRO D CG  1 
ATOM   9406  C  CD  . PRO D 1 146 ? 19.745 42.131 39.301  1.00 85.47  ? 210 PRO D CD  1 
ATOM   9407  N  N   . LEU D 1 147 ? 23.589 44.602 39.992  1.00 55.39  ? 211 LEU D N   1 
ATOM   9408  C  CA  . LEU D 1 147 ? 25.015 44.324 39.770  1.00 57.77  ? 211 LEU D CA  1 
ATOM   9409  C  C   . LEU D 1 147 ? 25.506 43.292 40.774  1.00 64.57  ? 211 LEU D C   1 
ATOM   9410  O  O   . LEU D 1 147 ? 24.784 42.925 41.738  1.00 61.19  ? 211 LEU D O   1 
ATOM   9411  C  CB  . LEU D 1 147 ? 25.896 45.559 39.847  1.00 53.48  ? 211 LEU D CB  1 
ATOM   9412  C  CG  . LEU D 1 147 ? 25.598 46.696 38.893  1.00 57.95  ? 211 LEU D CG  1 
ATOM   9413  C  CD1 . LEU D 1 147 ? 26.061 47.949 39.542  1.00 73.22  ? 211 LEU D CD1 1 
ATOM   9414  C  CD2 . LEU D 1 147 ? 26.317 46.531 37.628  1.00 59.53  ? 211 LEU D CD2 1 
ATOM   9415  N  N   . ARG D 1 148 ? 26.725 42.807 40.528  1.00 71.52  ? 212 ARG D N   1 
ATOM   9416  C  CA  . ARG D 1 148 ? 27.311 41.703 41.305  1.00 73.96  ? 212 ARG D CA  1 
ATOM   9417  C  C   . ARG D 1 148 ? 28.820 41.882 41.401  1.00 80.26  ? 212 ARG D C   1 
ATOM   9418  O  O   . ARG D 1 148 ? 29.473 42.146 40.389  1.00 93.85  ? 212 ARG D O   1 
ATOM   9419  C  CB  . ARG D 1 148 ? 26.966 40.357 40.661  1.00 61.89  ? 212 ARG D CB  1 
ATOM   9420  C  CG  . ARG D 1 148 ? 25.469 40.054 40.661  1.00 74.26  ? 212 ARG D CG  1 
ATOM   9421  C  CD  . ARG D 1 148 ? 25.120 38.715 40.030  1.00 86.74  ? 212 ARG D CD  1 
ATOM   9422  N  NE  . ARG D 1 148 ? 25.484 38.624 38.618  1.00 80.39  ? 212 ARG D NE  1 
ATOM   9423  C  CZ  . ARG D 1 148 ? 24.732 39.054 37.606  1.00 89.47  ? 212 ARG D CZ  1 
ATOM   9424  N  NH1 . ARG D 1 148 ? 23.553 39.629 37.821  1.00 85.68  ? 212 ARG D NH1 1 
ATOM   9425  N  NH2 . ARG D 1 148 ? 25.165 38.912 36.363  1.00 95.12  ? 212 ARG D NH2 1 
ATOM   9426  N  N   . THR D 1 149 ? 29.369 41.769 42.612  1.00 70.35  ? 213 THR D N   1 
ATOM   9427  C  CA  . THR D 1 149 ? 30.814 41.939 42.819  1.00 69.12  ? 213 THR D CA  1 
ATOM   9428  C  C   . THR D 1 149 ? 31.496 40.593 42.803  1.00 67.17  ? 213 THR D C   1 
ATOM   9429  O  O   . THR D 1 149 ? 30.821 39.567 42.871  1.00 77.46  ? 213 THR D O   1 
ATOM   9430  C  CB  . THR D 1 149 ? 31.125 42.566 44.173  1.00 78.00  ? 213 THR D CB  1 
ATOM   9431  O  OG1 . THR D 1 149 ? 30.531 41.778 45.216  1.00 90.42  ? 213 THR D OG1 1 
ATOM   9432  C  CG2 . THR D 1 149 ? 30.598 43.979 44.250  1.00 69.40  ? 213 THR D CG2 1 
ATOM   9433  N  N   . GLN D 1 150 ? 32.828 40.590 42.748  1.00 58.42  ? 214 GLN D N   1 
ATOM   9434  C  CA  . GLN D 1 150 ? 33.585 39.329 42.818  1.00 55.91  ? 214 GLN D CA  1 
ATOM   9435  C  C   . GLN D 1 150 ? 33.288 38.463 44.041  1.00 53.26  ? 214 GLN D C   1 
ATOM   9436  O  O   . GLN D 1 150 ? 33.451 37.246 43.977  1.00 56.88  ? 214 GLN D O   1 
ATOM   9437  C  CB  . GLN D 1 150 ? 35.067 39.600 42.809  1.00 56.41  ? 214 GLN D CB  1 
ATOM   9438  C  CG  . GLN D 1 150 ? 35.486 40.342 41.621  1.00 67.02  ? 214 GLN D CG  1 
ATOM   9439  C  CD  . GLN D 1 150 ? 36.942 40.685 41.643  1.00 74.90  ? 214 GLN D CD  1 
ATOM   9440  O  OE1 . GLN D 1 150 ? 37.508 40.968 42.689  1.00 77.10  ? 214 GLN D OE1 1 
ATOM   9441  N  NE2 . GLN D 1 150 ? 37.568 40.664 40.476  1.00 108.77 ? 214 GLN D NE2 1 
ATOM   9442  N  N   . ALA D 1 151 ? 32.879 39.070 45.156  1.00 47.48  ? 215 ALA D N   1 
ATOM   9443  C  CA  . ALA D 1 151 ? 32.657 38.304 46.377  1.00 46.42  ? 215 ALA D CA  1 
ATOM   9444  C  C   . ALA D 1 151 ? 33.956 37.597 46.695  1.00 54.18  ? 215 ALA D C   1 
ATOM   9445  O  O   . ALA D 1 151 ? 33.985 36.426 47.064  1.00 53.73  ? 215 ALA D O   1 
ATOM   9446  C  CB  . ALA D 1 151 ? 31.542 37.297 46.204  1.00 44.66  ? 215 ALA D CB  1 
ATOM   9447  N  N   . SER D 1 152 ? 35.031 38.348 46.516  1.00 60.95  ? 216 SER D N   1 
ATOM   9448  C  CA  . SER D 1 152 ? 36.382 37.883 46.662  1.00 61.20  ? 216 SER D CA  1 
ATOM   9449  C  C   . SER D 1 152 ? 37.203 39.156 46.709  1.00 54.69  ? 216 SER D C   1 
ATOM   9450  O  O   . SER D 1 152 ? 36.800 40.187 46.169  1.00 58.99  ? 216 SER D O   1 
ATOM   9451  C  CB  . SER D 1 152 ? 36.781 37.041 45.431  1.00 67.52  ? 216 SER D CB  1 
ATOM   9452  O  OG  . SER D 1 152 ? 38.186 36.831 45.347  1.00 94.13  ? 216 SER D OG  1 
ATOM   9453  N  N   . SER D 1 153 ? 38.357 39.079 47.342  1.00 46.82  ? 217 SER D N   1 
ATOM   9454  C  CA  . SER D 1 153 ? 39.327 40.153 47.291  1.00 51.95  ? 217 SER D CA  1 
ATOM   9455  C  C   . SER D 1 153 ? 39.606 40.606 45.860  1.00 51.11  ? 217 SER D C   1 
ATOM   9456  O  O   . SER D 1 153 ? 39.855 39.783 44.988  1.00 84.12  ? 217 SER D O   1 
ATOM   9457  C  CB  . SER D 1 153 ? 40.611 39.659 47.942  1.00 58.07  ? 217 SER D CB  1 
ATOM   9458  O  OG  . SER D 1 153 ? 41.683 40.525 47.685  1.00 66.27  ? 217 SER D OG  1 
ATOM   9459  N  N   . CYS D 1 154 ? 39.538 41.905 45.616  1.00 49.52  ? 218 CYS D N   1 
ATOM   9460  C  CA  . CYS D 1 154 ? 40.009 42.491 44.359  1.00 58.16  ? 218 CYS D CA  1 
ATOM   9461  C  C   . CYS D 1 154 ? 41.530 42.638 44.439  1.00 58.88  ? 218 CYS D C   1 
ATOM   9462  O  O   . CYS D 1 154 ? 42.143 42.254 45.422  1.00 57.58  ? 218 CYS D O   1 
ATOM   9463  C  CB  . CYS D 1 154 ? 39.352 43.854 44.117  1.00 82.74  ? 218 CYS D CB  1 
ATOM   9464  S  SG  . CYS D 1 154 ? 38.956 44.801 45.632  1.00 130.26 ? 218 CYS D SG  1 
ATOM   9465  N  N   . ILE D 1 155 ? 42.167 43.176 43.415  1.00 62.97  ? 219 ILE D N   1 
ATOM   9466  C  CA  . ILE D 1 155 ? 43.632 43.129 43.392  1.00 66.35  ? 219 ILE D CA  1 
ATOM   9467  C  C   . ILE D 1 155 ? 44.202 44.522 43.310  1.00 70.40  ? 219 ILE D C   1 
ATOM   9468  O  O   . ILE D 1 155 ? 43.853 45.282 42.408  1.00 84.23  ? 219 ILE D O   1 
ATOM   9469  C  CB  . ILE D 1 155 ? 44.167 42.254 42.227  1.00 66.22  ? 219 ILE D CB  1 
ATOM   9470  C  CG1 . ILE D 1 155 ? 43.986 40.777 42.555  1.00 70.03  ? 219 ILE D CG1 1 
ATOM   9471  C  CG2 . ILE D 1 155 ? 45.641 42.496 41.998  1.00 60.99  ? 219 ILE D CG2 1 
ATOM   9472  C  CD1 . ILE D 1 155 ? 42.560 40.301 42.504  1.00 99.45  ? 219 ILE D CD1 1 
ATOM   9473  N  N   . CYS D 1 156 ? 45.063 44.870 44.255  1.00 68.97  ? 220 CYS D N   1 
ATOM   9474  C  CA  . CYS D 1 156 ? 45.690 46.182 44.204  1.00 79.92  ? 220 CYS D CA  1 
ATOM   9475  C  C   . CYS D 1 156 ? 47.160 45.975 43.974  1.00 81.47  ? 220 CYS D C   1 
ATOM   9476  O  O   . CYS D 1 156 ? 47.760 45.054 44.539  1.00 78.76  ? 220 CYS D O   1 
ATOM   9477  C  CB  . CYS D 1 156 ? 45.444 47.006 45.473  1.00 79.35  ? 220 CYS D CB  1 
ATOM   9478  S  SG  . CYS D 1 156 ? 43.687 47.288 45.839  1.00 137.09 ? 220 CYS D SG  1 
ATOM   9479  N  N   . ASN D 1 157 ? 47.716 46.819 43.114  1.00 74.58  ? 221 ASN D N   1 
ATOM   9480  C  CA  . ASN D 1 157 ? 49.125 46.801 42.807  1.00 83.32  ? 221 ASN D CA  1 
ATOM   9481  C  C   . ASN D 1 157 ? 49.548 48.174 42.369  1.00 84.05  ? 221 ASN D C   1 
ATOM   9482  O  O   . ASN D 1 157 ? 49.079 48.668 41.341  1.00 96.43  ? 221 ASN D O   1 
ATOM   9483  C  CB  . ASN D 1 157 ? 49.438 45.779 41.701  1.00 94.57  ? 221 ASN D CB  1 
ATOM   9484  C  CG  . ASN D 1 157 ? 50.904 45.340 41.698  1.00 94.99  ? 221 ASN D CG  1 
ATOM   9485  O  OD1 . ASN D 1 157 ? 51.515 45.076 42.753  1.00 94.56  ? 221 ASN D OD1 1 
ATOM   9486  N  ND2 . ASN D 1 157 ? 51.469 45.245 40.505  1.00 84.36  ? 221 ASN D ND2 1 
ATOM   9487  N  N   . ASP D 1 158 ? 50.429 48.786 43.152  1.00 84.37  ? 222 ASP D N   1 
ATOM   9488  C  CA  . ASP D 1 158 ? 50.951 50.117 42.848  1.00 109.49 ? 222 ASP D CA  1 
ATOM   9489  C  C   . ASP D 1 158 ? 49.874 51.196 42.957  1.00 116.98 ? 222 ASP D C   1 
ATOM   9490  O  O   . ASP D 1 158 ? 49.837 52.135 42.148  1.00 121.40 ? 222 ASP D O   1 
ATOM   9491  C  CB  . ASP D 1 158 ? 51.586 50.168 41.445  1.00 125.65 ? 222 ASP D CB  1 
ATOM   9492  C  CG  . ASP D 1 158 ? 52.922 49.457 41.369  1.00 145.85 ? 222 ASP D CG  1 
ATOM   9493  O  OD1 . ASP D 1 158 ? 53.536 49.198 42.425  1.00 150.35 ? 222 ASP D OD1 1 
ATOM   9494  O  OD2 . ASP D 1 158 ? 53.366 49.166 40.235  1.00 156.69 ? 222 ASP D OD2 1 
ATOM   9495  N  N   . GLY D 1 159 ? 48.986 51.053 43.935  1.00 98.11  ? 223 GLY D N   1 
ATOM   9496  C  CA  . GLY D 1 159 ? 48.036 52.121 44.237  1.00 104.55 ? 223 GLY D CA  1 
ATOM   9497  C  C   . GLY D 1 159 ? 46.766 52.183 43.405  1.00 102.91 ? 223 GLY D C   1 
ATOM   9498  O  O   . GLY D 1 159 ? 45.838 52.936 43.742  1.00 119.36 ? 223 GLY D O   1 
ATOM   9499  N  N   . THR D 1 160 ? 46.728 51.416 42.315  1.00 92.96  ? 224 THR D N   1 
ATOM   9500  C  CA  . THR D 1 160 ? 45.499 51.235 41.528  1.00 96.18  ? 224 THR D CA  1 
ATOM   9501  C  C   . THR D 1 160 ? 44.929 49.829 41.755  1.00 81.64  ? 224 THR D C   1 
ATOM   9502  O  O   . THR D 1 160 ? 45.668 48.859 41.851  1.00 78.07  ? 224 THR D O   1 
ATOM   9503  C  CB  . THR D 1 160 ? 45.724 51.477 40.015  1.00 110.13 ? 224 THR D CB  1 
ATOM   9504  O  OG1 . THR D 1 160 ? 46.600 50.473 39.499  1.00 121.98 ? 224 THR D OG1 1 
ATOM   9505  C  CG2 . THR D 1 160 ? 46.323 52.886 39.735  1.00 111.38 ? 224 THR D CG2 1 
ATOM   9506  N  N   . CYS D 1 161 ? 43.616 49.723 41.866  1.00 75.48  ? 225 CYS D N   1 
ATOM   9507  C  CA  . CYS D 1 161 ? 42.993 48.436 42.129  1.00 70.39  ? 225 CYS D CA  1 
ATOM   9508  C  C   . CYS D 1 161 ? 42.086 48.024 40.985  1.00 74.03  ? 225 CYS D C   1 
ATOM   9509  O  O   . CYS D 1 161 ? 41.509 48.871 40.299  1.00 96.47  ? 225 CYS D O   1 
ATOM   9510  C  CB  . CYS D 1 161 ? 42.199 48.473 43.422  1.00 80.12  ? 225 CYS D CB  1 
ATOM   9511  S  SG  . CYS D 1 161 ? 43.183 48.990 44.813  1.00 116.56 ? 225 CYS D SG  1 
ATOM   9512  N  N   . TYR D 1 162 ? 41.965 46.715 40.792  1.00 69.50  ? 226 TYR D N   1 
ATOM   9513  C  CA  . TYR D 1 162 ? 41.227 46.122 39.667  1.00 63.77  ? 226 TYR D CA  1 
ATOM   9514  C  C   . TYR D 1 162 ? 40.172 45.198 40.218  1.00 60.11  ? 226 TYR D C   1 
ATOM   9515  O  O   . TYR D 1 162 ? 40.436 44.383 41.099  1.00 58.30  ? 226 TYR D O   1 
ATOM   9516  C  CB  . TYR D 1 162 ? 42.164 45.321 38.737  1.00 59.39  ? 226 TYR D CB  1 
ATOM   9517  C  CG  . TYR D 1 162 ? 43.389 46.099 38.283  1.00 61.33  ? 226 TYR D CG  1 
ATOM   9518  C  CD1 . TYR D 1 162 ? 43.358 46.862 37.117  1.00 69.19  ? 226 TYR D CD1 1 
ATOM   9519  C  CD2 . TYR D 1 162 ? 44.547 46.115 39.036  1.00 57.86  ? 226 TYR D CD2 1 
ATOM   9520  C  CE1 . TYR D 1 162 ? 44.451 47.605 36.704  1.00 73.47  ? 226 TYR D CE1 1 
ATOM   9521  C  CE2 . TYR D 1 162 ? 45.643 46.848 38.639  1.00 66.78  ? 226 TYR D CE2 1 
ATOM   9522  C  CZ  . TYR D 1 162 ? 45.596 47.589 37.462  1.00 80.96  ? 226 TYR D CZ  1 
ATOM   9523  O  OH  . TYR D 1 162 ? 46.687 48.323 37.028  1.00 98.08  ? 226 TYR D OH  1 
ATOM   9524  N  N   . THR D 1 163 ? 38.963 45.346 39.712  1.00 65.79  ? 227 THR D N   1 
ATOM   9525  C  CA  . THR D 1 163 ? 37.870 44.471 40.102  1.00 70.50  ? 227 THR D CA  1 
ATOM   9526  C  C   . THR D 1 163 ? 36.936 44.215 38.929  1.00 67.78  ? 227 THR D C   1 
ATOM   9527  O  O   . THR D 1 163 ? 36.883 44.996 37.986  1.00 83.03  ? 227 THR D O   1 
ATOM   9528  C  CB  . THR D 1 163 ? 37.073 45.040 41.279  1.00 73.92  ? 227 THR D CB  1 
ATOM   9529  O  OG1 . THR D 1 163 ? 36.094 44.074 41.702  1.00 90.92  ? 227 THR D OG1 1 
ATOM   9530  C  CG2 . THR D 1 163 ? 36.389 46.325 40.867  1.00 70.71  ? 227 THR D CG2 1 
ATOM   9531  N  N   . ILE D 1 164 ? 36.196 43.117 38.994  1.00 56.82  ? 228 ILE D N   1 
ATOM   9532  C  CA  . ILE D 1 164 ? 35.281 42.752 37.919  1.00 52.15  ? 228 ILE D CA  1 
ATOM   9533  C  C   . ILE D 1 164 ? 33.838 42.805 38.367  1.00 54.89  ? 228 ILE D C   1 
ATOM   9534  O  O   . ILE D 1 164 ? 33.462 42.204 39.376  1.00 63.29  ? 228 ILE D O   1 
ATOM   9535  C  CB  . ILE D 1 164 ? 35.591 41.370 37.381  1.00 48.48  ? 228 ILE D CB  1 
ATOM   9536  C  CG1 . ILE D 1 164 ? 36.954 41.381 36.695  1.00 49.13  ? 228 ILE D CG1 1 
ATOM   9537  C  CG2 . ILE D 1 164 ? 34.520 40.903 36.413  1.00 48.33  ? 228 ILE D CG2 1 
ATOM   9538  C  CD1 . ILE D 1 164 ? 37.587 40.023 36.592  1.00 46.50  ? 228 ILE D CD1 1 
ATOM   9539  N  N   . ILE D 1 165 ? 33.030 43.529 37.599  1.00 56.73  ? 229 ILE D N   1 
ATOM   9540  C  CA  . ILE D 1 165 ? 31.621 43.685 37.922  1.00 60.54  ? 229 ILE D CA  1 
ATOM   9541  C  C   . ILE D 1 165 ? 30.671 43.087 36.876  1.00 64.28  ? 229 ILE D C   1 
ATOM   9542  O  O   . ILE D 1 165 ? 30.824 43.341 35.685  1.00 63.37  ? 229 ILE D O   1 
ATOM   9543  C  CB  . ILE D 1 165 ? 31.293 45.155 38.178  1.00 61.68  ? 229 ILE D CB  1 
ATOM   9544  C  CG1 . ILE D 1 165 ? 32.356 45.739 39.101  1.00 57.57  ? 229 ILE D CG1 1 
ATOM   9545  C  CG2 . ILE D 1 165 ? 29.858 45.307 38.727  1.00 64.42  ? 229 ILE D CG2 1 
ATOM   9546  C  CD1 . ILE D 1 165 ? 31.792 46.377 40.330  1.00 63.94  ? 229 ILE D CD1 1 
ATOM   9547  N  N   . ALA D 1 166 ? 29.692 42.303 37.347  1.00 74.73  ? 230 ALA D N   1 
ATOM   9548  C  CA  . ALA D 1 166 ? 28.673 41.660 36.492  1.00 77.15  ? 230 ALA D CA  1 
ATOM   9549  C  C   . ALA D 1 166 ? 27.343 42.404 36.486  1.00 85.04  ? 230 ALA D C   1 
ATOM   9550  O  O   . ALA D 1 166 ? 26.910 42.937 37.508  1.00 87.25  ? 230 ALA D O   1 
ATOM   9551  C  CB  . ALA D 1 166 ? 28.444 40.218 36.901  1.00 62.27  ? 230 ALA D CB  1 
ATOM   9552  N  N   . ASP D 1 167 ? 26.711 42.393 35.315  1.00 102.97 ? 231 ASP D N   1 
ATOM   9553  C  CA  . ASP D 1 167 ? 25.419 43.004 35.059  1.00 110.09 ? 231 ASP D CA  1 
ATOM   9554  C  C   . ASP D 1 167 ? 24.510 41.997 34.350  1.00 116.50 ? 231 ASP D C   1 
ATOM   9555  O  O   . ASP D 1 167 ? 24.994 41.091 33.667  1.00 111.96 ? 231 ASP D O   1 
ATOM   9556  C  CB  . ASP D 1 167 ? 25.612 44.230 34.162  1.00 119.66 ? 231 ASP D CB  1 
ATOM   9557  C  CG  . ASP D 1 167 ? 24.558 45.299 34.395  1.00 154.68 ? 231 ASP D CG  1 
ATOM   9558  O  OD1 . ASP D 1 167 ? 23.557 45.024 35.097  1.00 159.24 ? 231 ASP D OD1 1 
ATOM   9559  O  OD2 . ASP D 1 167 ? 24.733 46.423 33.875  1.00 163.66 ? 231 ASP D OD2 1 
ATOM   9560  N  N   . GLY D 1 168 ? 23.197 42.144 34.506  1.00 115.03 ? 232 GLY D N   1 
ATOM   9561  C  CA  . GLY D 1 168 ? 22.266 41.364 33.697  1.00 107.95 ? 232 GLY D CA  1 
ATOM   9562  C  C   . GLY D 1 168 ? 21.231 40.564 34.451  1.00 111.97 ? 232 GLY D C   1 
ATOM   9563  O  O   . GLY D 1 168 ? 21.448 40.152 35.595  1.00 82.09  ? 232 GLY D O   1 
ATOM   9564  N  N   . THR D 1 169 ? 20.108 40.331 33.772  1.00 153.11 ? 233 THR D N   1 
ATOM   9565  C  CA  . THR D 1 169 ? 18.919 39.701 34.356  1.00 149.91 ? 233 THR D CA  1 
ATOM   9566  C  C   . THR D 1 169 ? 19.155 38.222 34.636  1.00 136.22 ? 233 THR D C   1 
ATOM   9567  O  O   . THR D 1 169 ? 18.711 37.695 35.661  1.00 110.10 ? 233 THR D O   1 
ATOM   9568  C  CB  . THR D 1 169 ? 17.690 39.862 33.422  1.00 132.43 ? 233 THR D CB  1 
ATOM   9569  O  OG1 . THR D 1 169 ? 17.538 41.239 33.070  1.00 153.12 ? 233 THR D OG1 1 
ATOM   9570  C  CG2 . THR D 1 169 ? 16.407 39.377 34.091  1.00 113.47 ? 233 THR D CG2 1 
ATOM   9571  N  N   . THR D 1 170 ? 19.852 37.564 33.715  1.00 127.49 ? 234 THR D N   1 
ATOM   9572  C  CA  . THR D 1 170 ? 20.144 36.144 33.837  1.00 124.62 ? 234 THR D CA  1 
ATOM   9573  C  C   . THR D 1 170 ? 21.501 35.818 33.213  1.00 119.69 ? 234 THR D C   1 
ATOM   9574  O  O   . THR D 1 170 ? 22.067 36.632 32.472  1.00 111.00 ? 234 THR D O   1 
ATOM   9575  C  CB  . THR D 1 170 ? 19.007 35.268 33.241  1.00 127.04 ? 234 THR D CB  1 
ATOM   9576  O  OG1 . THR D 1 170 ? 19.327 33.885 33.428  1.00 140.85 ? 234 THR D OG1 1 
ATOM   9577  C  CG2 . THR D 1 170 ? 18.795 35.555 31.753  1.00 106.72 ? 234 THR D CG2 1 
ATOM   9578  N  N   . TYR D 1 171 ? 21.999 34.620 33.518  1.00 119.36 ? 235 TYR D N   1 
ATOM   9579  C  CA  . TYR D 1 171 ? 23.373 34.214 33.194  1.00 113.87 ? 235 TYR D CA  1 
ATOM   9580  C  C   . TYR D 1 171 ? 23.551 33.914 31.731  1.00 104.70 ? 235 TYR D C   1 
ATOM   9581  O  O   . TYR D 1 171 ? 24.646 34.046 31.187  1.00 100.03 ? 235 TYR D O   1 
ATOM   9582  C  CB  . TYR D 1 171 ? 23.786 33.032 34.064  1.00 109.97 ? 235 TYR D CB  1 
ATOM   9583  C  CG  . TYR D 1 171 ? 23.482 33.303 35.530  1.00 166.38 ? 235 TYR D CG  1 
ATOM   9584  C  CD1 . TYR D 1 171 ? 24.136 34.332 36.233  1.00 161.62 ? 235 TYR D CD1 1 
ATOM   9585  C  CD2 . TYR D 1 171 ? 22.515 32.563 36.206  1.00 186.34 ? 235 TYR D CD2 1 
ATOM   9586  C  CE1 . TYR D 1 171 ? 23.845 34.595 37.575  1.00 132.01 ? 235 TYR D CE1 1 
ATOM   9587  C  CE2 . TYR D 1 171 ? 22.222 32.818 37.549  1.00 170.60 ? 235 TYR D CE2 1 
ATOM   9588  C  CZ  . TYR D 1 171 ? 22.891 33.832 38.220  1.00 151.84 ? 235 TYR D CZ  1 
ATOM   9589  O  OH  . TYR D 1 171 ? 22.599 34.078 39.537  1.00 170.49 ? 235 TYR D OH  1 
ATOM   9590  N  N   . THR D 1 172 ? 22.447 33.532 31.101  1.00 100.20 ? 236 THR D N   1 
ATOM   9591  C  CA  . THR D 1 172 ? 22.365 33.466 29.662  1.00 101.64 ? 236 THR D CA  1 
ATOM   9592  C  C   . THR D 1 172 ? 22.721 34.837 29.054  1.00 103.21 ? 236 THR D C   1 
ATOM   9593  O  O   . THR D 1 172 ? 23.345 34.905 27.992  1.00 101.75 ? 236 THR D O   1 
ATOM   9594  C  CB  . THR D 1 172 ? 20.959 33.006 29.231  1.00 112.11 ? 236 THR D CB  1 
ATOM   9595  O  OG1 . THR D 1 172 ? 20.031 34.096 29.321  1.00 117.39 ? 236 THR D OG1 1 
ATOM   9596  C  CG2 . THR D 1 172 ? 20.475 31.894 30.140  1.00 97.01  ? 236 THR D CG2 1 
ATOM   9597  N  N   . ALA D 1 173 ? 22.369 35.913 29.765  1.00 104.17 ? 237 ALA D N   1 
ATOM   9598  C  CA  . ALA D 1 173 ? 22.436 37.287 29.236  1.00 108.24 ? 237 ALA D CA  1 
ATOM   9599  C  C   . ALA D 1 173 ? 23.462 38.199 29.915  1.00 102.71 ? 237 ALA D C   1 
ATOM   9600  O  O   . ALA D 1 173 ? 23.412 39.416 29.747  1.00 102.42 ? 237 ALA D O   1 
ATOM   9601  C  CB  . ALA D 1 173 ? 21.040 37.936 29.302  1.00 116.46 ? 237 ALA D CB  1 
ATOM   9602  N  N   . SER D 1 174 ? 24.394 37.622 30.665  1.00 100.00 ? 238 SER D N   1 
ATOM   9603  C  CA  . SER D 1 174 ? 25.295 38.427 31.495  1.00 100.39 ? 238 SER D CA  1 
ATOM   9604  C  C   . SER D 1 174 ? 26.307 39.260 30.718  1.00 95.72  ? 238 SER D C   1 
ATOM   9605  O  O   . SER D 1 174 ? 26.694 38.916 29.602  1.00 100.56 ? 238 SER D O   1 
ATOM   9606  C  CB  . SER D 1 174 ? 26.023 37.552 32.515  1.00 104.80 ? 238 SER D CB  1 
ATOM   9607  O  OG  . SER D 1 174 ? 26.904 36.654 31.873  1.00 108.72 ? 238 SER D OG  1 
ATOM   9608  N  N   . SER D 1 175 ? 26.724 40.355 31.343  1.00 90.48  ? 239 SER D N   1 
ATOM   9609  C  CA  . SER D 1 175 ? 27.726 41.264 30.812  1.00 99.04  ? 239 SER D CA  1 
ATOM   9610  C  C   . SER D 1 175 ? 28.752 41.472 31.909  1.00 96.09  ? 239 SER D C   1 
ATOM   9611  O  O   . SER D 1 175 ? 28.387 41.554 33.078  1.00 130.13 ? 239 SER D O   1 
ATOM   9612  C  CB  . SER D 1 175 ? 27.067 42.605 30.470  1.00 120.47 ? 239 SER D CB  1 
ATOM   9613  O  OG  . SER D 1 175 ? 28.020 43.594 30.114  1.00 134.38 ? 239 SER D OG  1 
ATOM   9614  N  N   . HIS D 1 176 ? 30.030 41.557 31.556  1.00 84.30  ? 240 HIS D N   1 
ATOM   9615  C  CA  . HIS D 1 176 ? 31.062 41.809 32.573  1.00 78.31  ? 240 HIS D CA  1 
ATOM   9616  C  C   . HIS D 1 176 ? 32.035 42.889 32.220  1.00 74.69  ? 240 HIS D C   1 
ATOM   9617  O  O   . HIS D 1 176 ? 32.614 42.878 31.137  1.00 74.15  ? 240 HIS D O   1 
ATOM   9618  C  CB  . HIS D 1 176 ? 31.810 40.539 32.880  1.00 81.27  ? 240 HIS D CB  1 
ATOM   9619  C  CG  . HIS D 1 176 ? 30.914 39.409 33.231  1.00 81.17  ? 240 HIS D CG  1 
ATOM   9620  N  ND1 . HIS D 1 176 ? 30.475 38.951 34.458  1.00 82.76  ? 240 HIS D ND1 1 
ATOM   9621  C  CD2 . HIS D 1 176 ? 30.334 38.636 32.297  1.00 82.51  ? 240 HIS D CD2 1 
ATOM   9622  C  CE1 . HIS D 1 176 ? 29.661 37.910 34.225  1.00 85.52  ? 240 HIS D CE1 1 
ATOM   9623  N  NE2 . HIS D 1 176 ? 29.577 37.714 32.900  1.00 91.72  ? 240 HIS D NE2 1 
ATOM   9624  N  N   . ARG D 1 177 ? 32.208 43.836 33.141  1.00 75.40  ? 241 ARG D N   1 
ATOM   9625  C  CA  . ARG D 1 177 ? 33.160 44.937 32.987  1.00 73.43  ? 241 ARG D CA  1 
ATOM   9626  C  C   . ARG D 1 177 ? 34.300 44.777 33.979  1.00 71.10  ? 241 ARG D C   1 
ATOM   9627  O  O   . ARG D 1 177 ? 34.147 44.286 35.101  1.00 72.44  ? 241 ARG D O   1 
ATOM   9628  C  CB  . ARG D 1 177 ? 32.481 46.309 33.133  1.00 69.57  ? 241 ARG D CB  1 
ATOM   9629  C  CG  . ARG D 1 177 ? 31.378 46.513 32.119  1.00 77.63  ? 241 ARG D CG  1 
ATOM   9630  C  CD  . ARG D 1 177 ? 30.168 47.089 32.763  1.00 99.08  ? 241 ARG D CD  1 
ATOM   9631  N  NE  . ARG D 1 177 ? 30.224 48.550 32.810  1.00 119.21 ? 241 ARG D NE  1 
ATOM   9632  C  CZ  . ARG D 1 177 ? 29.743 49.357 31.865  1.00 102.73 ? 241 ARG D CZ  1 
ATOM   9633  N  NH1 . ARG D 1 177 ? 29.174 48.864 30.775  1.00 92.36  ? 241 ARG D NH1 1 
ATOM   9634  N  NH2 . ARG D 1 177 ? 29.837 50.667 32.014  1.00 101.16 ? 241 ARG D NH2 1 
ATOM   9635  N  N   . LEU D 1 178 ? 35.461 45.190 33.529  1.00 68.97  ? 242 LEU D N   1 
ATOM   9636  C  CA  . LEU D 1 178 ? 36.649 45.127 34.317  1.00 70.69  ? 242 LEU D CA  1 
ATOM   9637  C  C   . LEU D 1 178 ? 36.941 46.552 34.725  1.00 72.36  ? 242 LEU D C   1 
ATOM   9638  O  O   . LEU D 1 178 ? 37.247 47.368 33.888  1.00 85.87  ? 242 LEU D O   1 
ATOM   9639  C  CB  . LEU D 1 178 ? 37.747 44.576 33.431  1.00 74.00  ? 242 LEU D CB  1 
ATOM   9640  C  CG  . LEU D 1 178 ? 39.210 44.671 33.791  1.00 78.80  ? 242 LEU D CG  1 
ATOM   9641  C  CD1 . LEU D 1 178 ? 39.471 44.025 35.110  1.00 87.07  ? 242 LEU D CD1 1 
ATOM   9642  C  CD2 . LEU D 1 178 ? 39.958 43.949 32.706  1.00 86.44  ? 242 LEU D CD2 1 
ATOM   9643  N  N   . TYR D 1 179 ? 36.809 46.863 36.005  1.00 71.57  ? 243 TYR D N   1 
ATOM   9644  C  CA  . TYR D 1 179 ? 36.991 48.222 36.471  1.00 68.84  ? 243 TYR D CA  1 
ATOM   9645  C  C   . TYR D 1 179 ? 38.381 48.473 37.002  1.00 71.04  ? 243 TYR D C   1 
ATOM   9646  O  O   . TYR D 1 179 ? 39.027 47.581 37.514  1.00 74.49  ? 243 TYR D O   1 
ATOM   9647  C  CB  . TYR D 1 179 ? 35.975 48.537 37.554  1.00 67.16  ? 243 TYR D CB  1 
ATOM   9648  C  CG  . TYR D 1 179 ? 34.634 48.946 37.006  1.00 69.73  ? 243 TYR D CG  1 
ATOM   9649  C  CD1 . TYR D 1 179 ? 33.629 48.003 36.797  1.00 72.36  ? 243 TYR D CD1 1 
ATOM   9650  C  CD2 . TYR D 1 179 ? 34.373 50.272 36.693  1.00 70.84  ? 243 TYR D CD2 1 
ATOM   9651  C  CE1 . TYR D 1 179 ? 32.396 48.368 36.300  1.00 76.87  ? 243 TYR D CE1 1 
ATOM   9652  C  CE2 . TYR D 1 179 ? 33.149 50.658 36.198  1.00 79.39  ? 243 TYR D CE2 1 
ATOM   9653  C  CZ  . TYR D 1 179 ? 32.160 49.701 36.004  1.00 91.94  ? 243 TYR D CZ  1 
ATOM   9654  O  OH  . TYR D 1 179 ? 30.934 50.086 35.508  1.00 109.28 ? 243 TYR D OH  1 
ATOM   9655  N  N   . ARG D 1 180 ? 38.831 49.711 36.889  1.00 78.83  ? 244 ARG D N   1 
ATOM   9656  C  CA  . ARG D 1 180 ? 40.075 50.151 37.507  1.00 80.28  ? 244 ARG D CA  1 
ATOM   9657  C  C   . ARG D 1 180 ? 39.781 51.288 38.483  1.00 81.91  ? 244 ARG D C   1 
ATOM   9658  O  O   . ARG D 1 180 ? 39.068 52.235 38.150  1.00 100.20 ? 244 ARG D O   1 
ATOM   9659  C  CB  . ARG D 1 180 ? 41.033 50.578 36.409  1.00 98.96  ? 244 ARG D CB  1 
ATOM   9660  C  CG  . ARG D 1 180 ? 42.167 51.488 36.786  1.00 112.60 ? 244 ARG D CG  1 
ATOM   9661  C  CD  . ARG D 1 180 ? 42.945 51.853 35.514  1.00 114.50 ? 244 ARG D CD  1 
ATOM   9662  N  NE  . ARG D 1 180 ? 43.440 53.221 35.604  1.00 159.24 ? 244 ARG D NE  1 
ATOM   9663  C  CZ  . ARG D 1 180 ? 44.723 53.562 35.696  1.00 186.17 ? 244 ARG D CZ  1 
ATOM   9664  N  NH1 . ARG D 1 180 ? 45.667 52.633 35.680  1.00 218.06 ? 244 ARG D NH1 1 
ATOM   9665  N  NH2 . ARG D 1 180 ? 45.063 54.842 35.788  1.00 207.71 ? 244 ARG D NH2 1 
ATOM   9666  N  N   . LEU D 1 181 ? 40.313 51.180 39.693  1.00 72.97  ? 245 LEU D N   1 
ATOM   9667  C  CA  . LEU D 1 181 ? 39.999 52.127 40.754  1.00 75.06  ? 245 LEU D CA  1 
ATOM   9668  C  C   . LEU D 1 181 ? 41.263 52.731 41.299  1.00 80.15  ? 245 LEU D C   1 
ATOM   9669  O  O   . LEU D 1 181 ? 42.287 52.076 41.335  1.00 81.34  ? 245 LEU D O   1 
ATOM   9670  C  CB  . LEU D 1 181 ? 39.287 51.423 41.894  1.00 66.63  ? 245 LEU D CB  1 
ATOM   9671  C  CG  . LEU D 1 181 ? 38.083 50.592 41.488  1.00 70.09  ? 245 LEU D CG  1 
ATOM   9672  C  CD1 . LEU D 1 181 ? 37.787 49.598 42.565  1.00 76.21  ? 245 LEU D CD1 1 
ATOM   9673  C  CD2 . LEU D 1 181 ? 36.875 51.464 41.229  1.00 79.57  ? 245 LEU D CD2 1 
ATOM   9674  N  N   . VAL D 1 182 ? 41.189 53.982 41.730  1.00 84.22  ? 246 VAL D N   1 
ATOM   9675  C  CA  . VAL D 1 182 ? 42.313 54.648 42.367  1.00 82.06  ? 246 VAL D CA  1 
ATOM   9676  C  C   . VAL D 1 182 ? 41.779 55.506 43.501  1.00 78.01  ? 246 VAL D C   1 
ATOM   9677  O  O   . VAL D 1 182 ? 40.851 56.278 43.295  1.00 73.68  ? 246 VAL D O   1 
ATOM   9678  C  CB  . VAL D 1 182 ? 43.054 55.590 41.394  1.00 89.53  ? 246 VAL D CB  1 
ATOM   9679  C  CG1 . VAL D 1 182 ? 44.363 56.066 42.021  1.00 102.75 ? 246 VAL D CG1 1 
ATOM   9680  C  CG2 . VAL D 1 182 ? 43.299 54.923 40.048  1.00 83.06  ? 246 VAL D CG2 1 
ATOM   9681  N  N   . ASN D 1 183 ? 42.386 55.396 44.682  1.00 78.42  ? 247 ASN D N   1 
ATOM   9682  C  CA  . ASN D 1 183 ? 41.958 56.152 45.865  1.00 75.57  ? 247 ASN D CA  1 
ATOM   9683  C  C   . ASN D 1 183 ? 40.417 56.236 45.982  1.00 90.20  ? 247 ASN D C   1 
ATOM   9684  O  O   . ASN D 1 183 ? 39.837 57.236 46.485  1.00 92.98  ? 247 ASN D O   1 
ATOM   9685  C  CB  . ASN D 1 183 ? 42.609 57.538 45.899  1.00 78.24  ? 247 ASN D CB  1 
ATOM   9686  C  CG  . ASN D 1 183 ? 44.114 57.479 45.935  1.00 83.84  ? 247 ASN D CG  1 
ATOM   9687  O  OD1 . ASN D 1 183 ? 44.708 56.414 46.050  1.00 89.45  ? 247 ASN D OD1 1 
ATOM   9688  N  ND2 . ASN D 1 183 ? 44.741 58.643 45.836  1.00 98.75  ? 247 ASN D ND2 1 
ATOM   9689  N  N   . GLY D 1 184 ? 39.764 55.185 45.480  1.00 83.92  ? 248 GLY D N   1 
ATOM   9690  C  CA  . GLY D 1 184 ? 38.336 54.999 45.669  1.00 76.00  ? 248 GLY D CA  1 
ATOM   9691  C  C   . GLY D 1 184 ? 37.435 55.510 44.575  1.00 75.26  ? 248 GLY D C   1 
ATOM   9692  O  O   . GLY D 1 184 ? 36.225 55.331 44.637  1.00 81.89  ? 248 GLY D O   1 
ATOM   9693  N  N   . THR D 1 185 ? 38.010 56.150 43.569  1.00 80.33  ? 249 THR D N   1 
ATOM   9694  C  CA  . THR D 1 185 ? 37.221 56.594 42.428  1.00 89.53  ? 249 THR D CA  1 
ATOM   9695  C  C   . THR D 1 185 ? 37.524 55.702 41.198  1.00 97.22  ? 249 THR D C   1 
ATOM   9696  O  O   . THR D 1 185 ? 38.613 55.144 41.077  1.00 89.62  ? 249 THR D O   1 
ATOM   9697  C  CB  . THR D 1 185 ? 37.431 58.102 42.169  1.00 90.19  ? 249 THR D CB  1 
ATOM   9698  O  OG1 . THR D 1 185 ? 38.829 58.391 42.170  1.00 94.72  ? 249 THR D OG1 1 
ATOM   9699  C  CG2 . THR D 1 185 ? 36.747 58.948 43.269  1.00 87.09  ? 249 THR D CG2 1 
ATOM   9700  N  N   . SER D 1 186 ? 36.549 55.516 40.313  1.00 113.66 ? 250 SER D N   1 
ATOM   9701  C  CA  . SER D 1 186 ? 36.789 54.703 39.123  1.00 101.42 ? 250 SER D CA  1 
ATOM   9702  C  C   . SER D 1 186 ? 37.683 55.474 38.167  1.00 108.75 ? 250 SER D C   1 
ATOM   9703  O  O   . SER D 1 186 ? 37.449 56.646 37.879  1.00 127.93 ? 250 SER D O   1 
ATOM   9704  C  CB  . SER D 1 186 ? 35.485 54.271 38.441  1.00 98.65  ? 250 SER D CB  1 
ATOM   9705  O  OG  . SER D 1 186 ? 34.711 55.387 38.037  1.00 134.29 ? 250 SER D OG  1 
ATOM   9706  N  N   . ALA D 1 187 ? 38.741 54.813 37.720  1.00 106.56 ? 251 ALA D N   1 
ATOM   9707  C  CA  . ALA D 1 187 ? 39.652 55.387 36.746  1.00 98.83  ? 251 ALA D CA  1 
ATOM   9708  C  C   . ALA D 1 187 ? 39.457 54.669 35.418  1.00 96.24  ? 251 ALA D C   1 
ATOM   9709  O  O   . ALA D 1 187 ? 40.406 54.443 34.663  1.00 86.82  ? 251 ALA D O   1 
ATOM   9710  C  CB  . ALA D 1 187 ? 41.071 55.258 37.222  1.00 97.89  ? 251 ALA D CB  1 
ATOM   9711  N  N   . GLY D 1 188 ? 38.212 54.300 35.141  1.00 99.72  ? 252 GLY D N   1 
ATOM   9712  C  CA  . GLY D 1 188 ? 37.873 53.724 33.851  1.00 94.18  ? 252 GLY D CA  1 
ATOM   9713  C  C   . GLY D 1 188 ? 37.666 52.232 33.895  1.00 88.90  ? 252 GLY D C   1 
ATOM   9714  O  O   . GLY D 1 188 ? 37.893 51.586 34.920  1.00 88.73  ? 252 GLY D O   1 
ATOM   9715  N  N   . TRP D 1 189 ? 37.223 51.682 32.772  1.00 84.81  ? 253 TRP D N   1 
ATOM   9716  C  CA  . TRP D 1 189 ? 36.930 50.264 32.695  1.00 83.69  ? 253 TRP D CA  1 
ATOM   9717  C  C   . TRP D 1 189 ? 36.973 49.785 31.277  1.00 88.66  ? 253 TRP D C   1 
ATOM   9718  O  O   . TRP D 1 189 ? 37.155 50.557 30.354  1.00 105.13 ? 253 TRP D O   1 
ATOM   9719  C  CB  . TRP D 1 189 ? 35.569 49.982 33.320  1.00 87.03  ? 253 TRP D CB  1 
ATOM   9720  C  CG  . TRP D 1 189 ? 34.500 50.824 32.683  1.00 92.32  ? 253 TRP D CG  1 
ATOM   9721  C  CD1 . TRP D 1 189 ? 34.067 52.101 33.062  1.00 92.74  ? 253 TRP D CD1 1 
ATOM   9722  C  CD2 . TRP D 1 189 ? 33.719 50.491 31.504  1.00 85.66  ? 253 TRP D CD2 1 
ATOM   9723  N  NE1 . TRP D 1 189 ? 33.089 52.550 32.221  1.00 87.96  ? 253 TRP D NE1 1 
ATOM   9724  C  CE2 . TRP D 1 189 ? 32.830 51.639 31.259  1.00 86.44  ? 253 TRP D CE2 1 
ATOM   9725  C  CE3 . TRP D 1 189 ? 33.656 49.399 30.663  1.00 89.17  ? 253 TRP D CE3 1 
ATOM   9726  C  CZ2 . TRP D 1 189 ? 31.929 51.664 30.198  1.00 81.33  ? 253 TRP D CZ2 1 
ATOM   9727  C  CZ3 . TRP D 1 189 ? 32.745 49.432 29.600  1.00 98.32  ? 253 TRP D CZ3 1 
ATOM   9728  C  CH2 . TRP D 1 189 ? 31.899 50.542 29.377  1.00 86.82  ? 253 TRP D CH2 1 
ATOM   9729  N  N   . LYS D 1 190 ? 36.813 48.487 31.096  1.00 90.88  ? 254 LYS D N   1 
ATOM   9730  C  CA  . LYS D 1 190 ? 36.765 47.880 29.781  1.00 83.60  ? 254 LYS D CA  1 
ATOM   9731  C  C   . LYS D 1 190 ? 35.705 46.776 29.777  1.00 85.24  ? 254 LYS D C   1 
ATOM   9732  O  O   . LYS D 1 190 ? 35.557 46.039 30.754  1.00 89.18  ? 254 LYS D O   1 
ATOM   9733  C  CB  . LYS D 1 190 ? 38.135 47.320 29.427  1.00 79.98  ? 254 LYS D CB  1 
ATOM   9734  C  CG  . LYS D 1 190 ? 38.139 46.522 28.153  1.00 87.52  ? 254 LYS D CG  1 
ATOM   9735  C  CD  . LYS D 1 190 ? 39.455 46.629 27.400  1.00 94.36  ? 254 LYS D CD  1 
ATOM   9736  C  CE  . LYS D 1 190 ? 39.388 45.784 26.140  1.00 102.56 ? 254 LYS D CE  1 
ATOM   9737  N  NZ  . LYS D 1 190 ? 40.550 46.016 25.254  1.00 123.74 ? 254 LYS D NZ  1 
ATOM   9738  N  N   . ALA D 1 191 ? 34.939 46.677 28.696  1.00 88.44  ? 255 ALA D N   1 
ATOM   9739  C  CA  . ALA D 1 191 ? 34.005 45.563 28.557  1.00 88.69  ? 255 ALA D CA  1 
ATOM   9740  C  C   . ALA D 1 191 ? 34.799 44.301 28.285  1.00 93.29  ? 255 ALA D C   1 
ATOM   9741  O  O   . ALA D 1 191 ? 35.713 44.292 27.469  1.00 99.93  ? 255 ALA D O   1 
ATOM   9742  C  CB  . ALA D 1 191 ? 33.011 45.808 27.439  1.00 79.34  ? 255 ALA D CB  1 
ATOM   9743  N  N   . LEU D 1 192 ? 34.466 43.239 28.995  1.00 95.86  ? 256 LEU D N   1 
ATOM   9744  C  CA  . LEU D 1 192 ? 35.036 41.947 28.704  1.00 97.37  ? 256 LEU D CA  1 
ATOM   9745  C  C   . LEU D 1 192 ? 34.083 41.211 27.781  1.00 115.40 ? 256 LEU D C   1 
ATOM   9746  O  O   . LEU D 1 192 ? 32.873 41.181 28.033  1.00 126.07 ? 256 LEU D O   1 
ATOM   9747  C  CB  . LEU D 1 192 ? 35.240 41.159 29.991  1.00 88.33  ? 256 LEU D CB  1 
ATOM   9748  C  CG  . LEU D 1 192 ? 36.276 41.714 30.961  1.00 79.88  ? 256 LEU D CG  1 
ATOM   9749  C  CD1 . LEU D 1 192 ? 36.309 40.822 32.150  1.00 82.23  ? 256 LEU D CD1 1 
ATOM   9750  C  CD2 . LEU D 1 192 ? 37.652 41.771 30.337  1.00 88.25  ? 256 LEU D CD2 1 
ATOM   9751  N  N   . ASP D 1 193 ? 34.630 40.634 26.709  1.00 120.11 ? 257 ASP D N   1 
ATOM   9752  C  CA  . ASP D 1 193 ? 33.848 39.854 25.748  1.00 111.49 ? 257 ASP D CA  1 
ATOM   9753  C  C   . ASP D 1 193 ? 33.536 38.442 26.250  1.00 112.08 ? 257 ASP D C   1 
ATOM   9754  O  O   . ASP D 1 193 ? 34.364 37.538 26.179  1.00 112.44 ? 257 ASP D O   1 
ATOM   9755  C  CB  . ASP D 1 193 ? 34.556 39.786 24.402  1.00 105.73 ? 257 ASP D CB  1 
ATOM   9756  C  CG  . ASP D 1 193 ? 33.744 39.048 23.354  1.00 121.22 ? 257 ASP D CG  1 
ATOM   9757  O  OD1 . ASP D 1 193 ? 32.577 38.683 23.621  1.00 144.58 ? 257 ASP D OD1 1 
ATOM   9758  O  OD2 . ASP D 1 193 ? 34.277 38.834 22.249  1.00 116.54 ? 257 ASP D OD2 1 
ATOM   9759  N  N   . THR D 1 194 ? 32.306 38.275 26.718  1.00 123.31 ? 258 THR D N   1 
ATOM   9760  C  CA  . THR D 1 194 ? 31.867 37.080 27.410  1.00 121.35 ? 258 THR D CA  1 
ATOM   9761  C  C   . THR D 1 194 ? 31.041 36.181 26.494  1.00 126.13 ? 258 THR D C   1 
ATOM   9762  O  O   . THR D 1 194 ? 30.845 35.006 26.801  1.00 119.34 ? 258 THR D O   1 
ATOM   9763  C  CB  . THR D 1 194 ? 31.022 37.470 28.668  1.00 132.44 ? 258 THR D CB  1 
ATOM   9764  O  OG1 . THR D 1 194 ? 30.802 36.322 29.491  1.00 133.54 ? 258 THR D OG1 1 
ATOM   9765  C  CG2 . THR D 1 194 ? 29.660 38.092 28.277  1.00 125.63 ? 258 THR D CG2 1 
ATOM   9766  N  N   . THR D 1 195 ? 30.571 36.737 25.372  1.00 151.18 ? 259 THR D N   1 
ATOM   9767  C  CA  . THR D 1 195 ? 29.470 36.135 24.583  1.00 143.41 ? 259 THR D CA  1 
ATOM   9768  C  C   . THR D 1 195 ? 29.635 34.637 24.350  1.00 117.64 ? 259 THR D C   1 
ATOM   9769  O  O   . THR D 1 195 ? 30.718 34.155 24.000  1.00 94.10  ? 259 THR D O   1 
ATOM   9770  C  CB  . THR D 1 195 ? 29.195 36.841 23.210  1.00 127.80 ? 259 THR D CB  1 
ATOM   9771  O  OG1 . THR D 1 195 ? 30.379 36.815 22.405  1.00 116.17 ? 259 THR D OG1 1 
ATOM   9772  C  CG2 . THR D 1 195 ? 28.707 38.287 23.391  1.00 114.49 ? 259 THR D CG2 1 
ATOM   9773  N  N   . GLY D 1 196 ? 28.540 33.917 24.562  1.00 112.83 ? 260 GLY D N   1 
ATOM   9774  C  CA  . GLY D 1 196 ? 28.548 32.472 24.456  1.00 109.71 ? 260 GLY D CA  1 
ATOM   9775  C  C   . GLY D 1 196 ? 28.757 31.774 25.787  1.00 112.36 ? 260 GLY D C   1 
ATOM   9776  O  O   . GLY D 1 196 ? 28.421 30.604 25.929  1.00 111.91 ? 260 GLY D O   1 
ATOM   9777  N  N   . PHE D 1 197 ? 29.322 32.473 26.768  1.00 105.83 ? 261 PHE D N   1 
ATOM   9778  C  CA  . PHE D 1 197 ? 29.481 31.891 28.099  1.00 88.03  ? 261 PHE D CA  1 
ATOM   9779  C  C   . PHE D 1 197 ? 29.208 32.878 29.226  1.00 87.17  ? 261 PHE D C   1 
ATOM   9780  O  O   . PHE D 1 197 ? 28.699 33.974 28.977  1.00 95.12  ? 261 PHE D O   1 
ATOM   9781  C  CB  . PHE D 1 197 ? 30.847 31.234 28.248  1.00 78.84  ? 261 PHE D CB  1 
ATOM   9782  C  CG  . PHE D 1 197 ? 31.988 32.200 28.347  1.00 80.44  ? 261 PHE D CG  1 
ATOM   9783  C  CD1 . PHE D 1 197 ? 32.522 32.541 29.590  1.00 80.88  ? 261 PHE D CD1 1 
ATOM   9784  C  CD2 . PHE D 1 197 ? 32.565 32.746 27.204  1.00 81.78  ? 261 PHE D CD2 1 
ATOM   9785  C  CE1 . PHE D 1 197 ? 33.612 33.432 29.693  1.00 80.08  ? 261 PHE D CE1 1 
ATOM   9786  C  CE2 . PHE D 1 197 ? 33.657 33.639 27.299  1.00 82.57  ? 261 PHE D CE2 1 
ATOM   9787  C  CZ  . PHE D 1 197 ? 34.180 33.978 28.544  1.00 74.52  ? 261 PHE D CZ  1 
ATOM   9788  N  N   . ASN D 1 198 ? 29.541 32.484 30.458  1.00 79.63  ? 262 ASN D N   1 
ATOM   9789  C  CA  . ASN D 1 198 ? 29.262 33.288 31.663  1.00 76.71  ? 262 ASN D CA  1 
ATOM   9790  C  C   . ASN D 1 198 ? 30.388 33.200 32.738  1.00 90.66  ? 262 ASN D C   1 
ATOM   9791  O  O   . ASN D 1 198 ? 31.012 32.151 32.934  1.00 93.04  ? 262 ASN D O   1 
ATOM   9792  C  CB  . ASN D 1 198 ? 27.883 32.914 32.196  1.00 69.06  ? 262 ASN D CB  1 
ATOM   9793  C  CG  . ASN D 1 198 ? 27.736 33.144 33.669  1.00 84.80  ? 262 ASN D CG  1 
ATOM   9794  O  OD1 . ASN D 1 198 ? 27.750 32.192 34.447  1.00 102.67 ? 262 ASN D OD1 1 
ATOM   9795  N  ND2 . ASN D 1 198 ? 27.577 34.404 34.072  1.00 94.96  ? 262 ASN D ND2 1 
ATOM   9796  N  N   . PHE D 1 199 ? 30.649 34.309 33.425  1.00 81.05  ? 263 PHE D N   1 
ATOM   9797  C  CA  . PHE D 1 199 ? 31.884 34.477 34.170  1.00 71.02  ? 263 PHE D CA  1 
ATOM   9798  C  C   . PHE D 1 199 ? 31.591 35.194 35.462  1.00 78.70  ? 263 PHE D C   1 
ATOM   9799  O  O   . PHE D 1 199 ? 31.622 36.422 35.536  1.00 90.80  ? 263 PHE D O   1 
ATOM   9800  C  CB  . PHE D 1 199 ? 32.850 35.299 33.318  1.00 68.26  ? 263 PHE D CB  1 
ATOM   9801  C  CG  . PHE D 1 199 ? 34.208 35.451 33.903  1.00 65.30  ? 263 PHE D CG  1 
ATOM   9802  C  CD1 . PHE D 1 199 ? 35.079 34.368 33.979  1.00 63.81  ? 263 PHE D CD1 1 
ATOM   9803  C  CD2 . PHE D 1 199 ? 34.640 36.686 34.353  1.00 68.31  ? 263 PHE D CD2 1 
ATOM   9804  C  CE1 . PHE D 1 199 ? 36.362 34.509 34.521  1.00 62.73  ? 263 PHE D CE1 1 
ATOM   9805  C  CE2 . PHE D 1 199 ? 35.928 36.847 34.904  1.00 71.57  ? 263 PHE D CE2 1 
ATOM   9806  C  CZ  . PHE D 1 199 ? 36.790 35.745 34.996  1.00 65.80  ? 263 PHE D CZ  1 
ATOM   9807  N  N   . GLU D 1 200 ? 31.306 34.424 36.498  1.00 95.50  ? 264 GLU D N   1 
ATOM   9808  C  CA  . GLU D 1 200 ? 30.855 35.015 37.752  1.00 95.11  ? 264 GLU D CA  1 
ATOM   9809  C  C   . GLU D 1 200 ? 31.801 34.753 38.932  1.00 97.21  ? 264 GLU D C   1 
ATOM   9810  O  O   . GLU D 1 200 ? 32.531 33.750 38.955  1.00 100.71 ? 264 GLU D O   1 
ATOM   9811  C  CB  . GLU D 1 200 ? 29.470 34.484 38.071  1.00 96.11  ? 264 GLU D CB  1 
ATOM   9812  C  CG  . GLU D 1 200 ? 28.416 34.854 37.046  1.00 120.42 ? 264 GLU D CG  1 
ATOM   9813  C  CD  . GLU D 1 200 ? 27.624 36.094 37.432  1.00 152.34 ? 264 GLU D CD  1 
ATOM   9814  O  OE1 . GLU D 1 200 ? 27.751 36.568 38.594  1.00 155.74 ? 264 GLU D OE1 1 
ATOM   9815  O  OE2 . GLU D 1 200 ? 26.863 36.581 36.564  1.00 124.30 ? 264 GLU D OE2 1 
ATOM   9816  N  N   . PHE D 1 201 ? 31.789 35.661 39.907  1.00 76.33  ? 265 PHE D N   1 
ATOM   9817  C  CA  . PHE D 1 201 ? 32.545 35.460 41.121  1.00 58.11  ? 265 PHE D CA  1 
ATOM   9818  C  C   . PHE D 1 201 ? 34.012 35.134 40.802  1.00 59.44  ? 265 PHE D C   1 
ATOM   9819  O  O   . PHE D 1 201 ? 34.565 34.127 41.306  1.00 70.19  ? 265 PHE D O   1 
ATOM   9820  C  CB  . PHE D 1 201 ? 31.917 34.325 41.942  1.00 59.26  ? 265 PHE D CB  1 
ATOM   9821  C  CG  . PHE D 1 201 ? 30.441 34.455 42.148  1.00 66.91  ? 265 PHE D CG  1 
ATOM   9822  C  CD1 . PHE D 1 201 ? 29.913 35.511 42.901  1.00 72.44  ? 265 PHE D CD1 1 
ATOM   9823  C  CD2 . PHE D 1 201 ? 29.572 33.510 41.604  1.00 69.83  ? 265 PHE D CD2 1 
ATOM   9824  C  CE1 . PHE D 1 201 ? 28.534 35.650 43.078  1.00 76.73  ? 265 PHE D CE1 1 
ATOM   9825  C  CE2 . PHE D 1 201 ? 28.193 33.630 41.785  1.00 81.52  ? 265 PHE D CE2 1 
ATOM   9826  C  CZ  . PHE D 1 201 ? 27.672 34.713 42.524  1.00 80.22  ? 265 PHE D CZ  1 
ATOM   9827  N  N   . PRO D 1 202 ? 34.656 35.965 39.959  1.00 54.14  ? 266 PRO D N   1 
ATOM   9828  C  CA  . PRO D 1 202 ? 36.061 35.718 39.661  1.00 58.89  ? 266 PRO D CA  1 
ATOM   9829  C  C   . PRO D 1 202 ? 36.890 35.795 40.904  1.00 53.10  ? 266 PRO D C   1 
ATOM   9830  O  O   . PRO D 1 202 ? 36.619 36.609 41.776  1.00 59.16  ? 266 PRO D O   1 
ATOM   9831  C  CB  . PRO D 1 202 ? 36.442 36.879 38.736  1.00 60.26  ? 266 PRO D CB  1 
ATOM   9832  C  CG  . PRO D 1 202 ? 35.433 37.875 38.955  1.00 53.85  ? 266 PRO D CG  1 
ATOM   9833  C  CD  . PRO D 1 202 ? 34.175 37.148 39.241  1.00 56.04  ? 266 PRO D CD  1 
ATOM   9834  N  N   . THR D 1 203 ? 37.895 34.945 40.977  1.00 52.28  ? 267 THR D N   1 
ATOM   9835  C  CA  . THR D 1 203 ? 38.760 34.920 42.129  1.00 57.40  ? 267 THR D CA  1 
ATOM   9836  C  C   . THR D 1 203 ? 40.166 35.003 41.581  1.00 54.30  ? 267 THR D C   1 
ATOM   9837  O  O   . THR D 1 203 ? 40.526 34.255 40.674  1.00 59.08  ? 267 THR D O   1 
ATOM   9838  C  CB  . THR D 1 203 ? 38.471 33.694 43.041  1.00 57.76  ? 267 THR D CB  1 
ATOM   9839  O  OG1 . THR D 1 203 ? 39.259 33.798 44.233  1.00 61.38  ? 267 THR D OG1 1 
ATOM   9840  C  CG2 . THR D 1 203 ? 38.770 32.388 42.325  1.00 73.29  ? 267 THR D CG2 1 
ATOM   9841  N  N   . CYS D 1 204 ? 40.945 35.949 42.098  1.00 64.56  ? 268 CYS D N   1 
ATOM   9842  C  CA  . CYS D 1 204 ? 42.111 36.441 41.360  1.00 70.49  ? 268 CYS D CA  1 
ATOM   9843  C  C   . CYS D 1 204 ? 43.423 36.482 42.122  1.00 63.24  ? 268 CYS D C   1 
ATOM   9844  O  O   . CYS D 1 204 ? 43.446 36.550 43.340  1.00 72.95  ? 268 CYS D O   1 
ATOM   9845  C  CB  . CYS D 1 204 ? 41.798 37.838 40.844  1.00 79.56  ? 268 CYS D CB  1 
ATOM   9846  S  SG  . CYS D 1 204 ? 40.288 37.905 39.929  1.00 116.15 ? 268 CYS D SG  1 
ATOM   9847  N  N   . TYR D 1 205 ? 44.519 36.472 41.384  1.00 66.51  ? 269 TYR D N   1 
ATOM   9848  C  CA  . TYR D 1 205 ? 45.827 36.762 41.960  1.00 65.51  ? 269 TYR D CA  1 
ATOM   9849  C  C   . TYR D 1 205 ? 46.711 37.447 40.939  1.00 66.95  ? 269 TYR D C   1 
ATOM   9850  O  O   . TYR D 1 205 ? 46.321 37.637 39.789  1.00 68.28  ? 269 TYR D O   1 
ATOM   9851  C  CB  . TYR D 1 205 ? 46.502 35.491 42.477  1.00 60.66  ? 269 TYR D CB  1 
ATOM   9852  C  CG  . TYR D 1 205 ? 46.791 34.466 41.416  1.00 60.17  ? 269 TYR D CG  1 
ATOM   9853  C  CD1 . TYR D 1 205 ? 48.113 34.208 41.015  1.00 65.60  ? 269 TYR D CD1 1 
ATOM   9854  C  CD2 . TYR D 1 205 ? 45.749 33.746 40.809  1.00 58.38  ? 269 TYR D CD2 1 
ATOM   9855  C  CE1 . TYR D 1 205 ? 48.398 33.250 40.039  1.00 65.18  ? 269 TYR D CE1 1 
ATOM   9856  C  CE2 . TYR D 1 205 ? 46.009 32.792 39.835  1.00 63.87  ? 269 TYR D CE2 1 
ATOM   9857  C  CZ  . TYR D 1 205 ? 47.336 32.548 39.451  1.00 67.72  ? 269 TYR D CZ  1 
ATOM   9858  O  OH  . TYR D 1 205 ? 47.582 31.608 38.478  1.00 61.39  ? 269 TYR D OH  1 
ATOM   9859  N  N   . TYR D 1 206 ? 47.907 37.818 41.366  1.00 67.64  ? 270 TYR D N   1 
ATOM   9860  C  CA  . TYR D 1 206 ? 48.800 38.546 40.497  1.00 75.39  ? 270 TYR D CA  1 
ATOM   9861  C  C   . TYR D 1 206 ? 50.160 37.879 40.436  1.00 93.42  ? 270 TYR D C   1 
ATOM   9862  O  O   . TYR D 1 206 ? 50.747 37.527 41.465  1.00 113.54 ? 270 TYR D O   1 
ATOM   9863  C  CB  . TYR D 1 206 ? 48.924 40.009 40.952  1.00 72.86  ? 270 TYR D CB  1 
ATOM   9864  C  CG  . TYR D 1 206 ? 49.987 40.791 40.226  1.00 66.40  ? 270 TYR D CG  1 
ATOM   9865  C  CD1 . TYR D 1 206 ? 51.185 41.105 40.849  1.00 69.36  ? 270 TYR D CD1 1 
ATOM   9866  C  CD2 . TYR D 1 206 ? 49.803 41.188 38.915  1.00 70.11  ? 270 TYR D CD2 1 
ATOM   9867  C  CE1 . TYR D 1 206 ? 52.167 41.803 40.194  1.00 77.10  ? 270 TYR D CE1 1 
ATOM   9868  C  CE2 . TYR D 1 206 ? 50.782 41.888 38.245  1.00 79.33  ? 270 TYR D CE2 1 
ATOM   9869  C  CZ  . TYR D 1 206 ? 51.966 42.192 38.896  1.00 82.56  ? 270 TYR D CZ  1 
ATOM   9870  O  OH  . TYR D 1 206 ? 52.963 42.885 38.258  1.00 93.69  ? 270 TYR D OH  1 
ATOM   9871  N  N   . THR D 1 207 ? 50.655 37.714 39.215  1.00 95.98  ? 271 THR D N   1 
ATOM   9872  C  CA  . THR D 1 207 ? 52.012 37.256 38.998  1.00 89.41  ? 271 THR D CA  1 
ATOM   9873  C  C   . THR D 1 207 ? 52.503 37.673 37.625  1.00 81.63  ? 271 THR D C   1 
ATOM   9874  O  O   . THR D 1 207 ? 51.728 37.779 36.680  1.00 72.05  ? 271 THR D O   1 
ATOM   9875  C  CB  . THR D 1 207 ? 52.132 35.720 39.169  1.00 93.20  ? 271 THR D CB  1 
ATOM   9876  O  OG1 . THR D 1 207 ? 53.509 35.345 39.095  1.00 127.08 ? 271 THR D OG1 1 
ATOM   9877  C  CG2 . THR D 1 207 ? 51.327 34.962 38.086  1.00 82.75  ? 271 THR D CG2 1 
ATOM   9878  N  N   . SER D 1 208 ? 53.805 37.905 37.527  1.00 96.26  ? 272 SER D N   1 
ATOM   9879  C  CA  . SER D 1 208 ? 54.461 38.067 36.235  1.00 106.45 ? 272 SER D CA  1 
ATOM   9880  C  C   . SER D 1 208 ? 53.750 39.133 35.398  1.00 100.28 ? 272 SER D C   1 
ATOM   9881  O  O   . SER D 1 208 ? 53.475 38.937 34.206  1.00 90.08  ? 272 SER D O   1 
ATOM   9882  C  CB  . SER D 1 208 ? 54.520 36.717 35.500  1.00 112.28 ? 272 SER D CB  1 
ATOM   9883  O  OG  . SER D 1 208 ? 55.403 36.773 34.394  1.00 126.86 ? 272 SER D OG  1 
ATOM   9884  N  N   . GLY D 1 209 ? 53.433 40.250 36.054  1.00 95.31  ? 273 GLY D N   1 
ATOM   9885  C  CA  . GLY D 1 209 ? 52.815 41.395 35.397  1.00 85.07  ? 273 GLY D CA  1 
ATOM   9886  C  C   . GLY D 1 209 ? 51.388 41.214 34.912  1.00 82.92  ? 273 GLY D C   1 
ATOM   9887  O  O   . GLY D 1 209 ? 50.887 42.031 34.141  1.00 102.39 ? 273 GLY D O   1 
ATOM   9888  N  N   . LYS D 1 210 ? 50.720 40.156 35.350  1.00 74.67  ? 274 LYS D N   1 
ATOM   9889  C  CA  . LYS D 1 210 ? 49.359 39.896 34.891  1.00 76.57  ? 274 LYS D CA  1 
ATOM   9890  C  C   . LYS D 1 210 ? 48.493 39.419 36.007  1.00 75.41  ? 274 LYS D C   1 
ATOM   9891  O  O   . LYS D 1 210 ? 48.944 38.692 36.876  1.00 92.69  ? 274 LYS D O   1 
ATOM   9892  C  CB  . LYS D 1 210 ? 49.334 38.870 33.758  1.00 87.66  ? 274 LYS D CB  1 
ATOM   9893  C  CG  . LYS D 1 210 ? 49.764 39.469 32.411  1.00 103.20 ? 274 LYS D CG  1 
ATOM   9894  C  CD  . LYS D 1 210 ? 49.837 38.469 31.267  1.00 102.98 ? 274 LYS D CD  1 
ATOM   9895  C  CE  . LYS D 1 210 ? 51.116 37.632 31.335  1.00 110.37 ? 274 LYS D CE  1 
ATOM   9896  N  NZ  . LYS D 1 210 ? 51.623 37.300 29.980  1.00 119.58 ? 274 LYS D NZ  1 
ATOM   9897  N  N   . VAL D 1 211 ? 47.242 39.847 35.990  1.00 70.63  ? 275 VAL D N   1 
ATOM   9898  C  CA  . VAL D 1 211 ? 46.273 39.352 36.941  1.00 64.81  ? 275 VAL D CA  1 
ATOM   9899  C  C   . VAL D 1 211 ? 45.497 38.204 36.316  1.00 66.24  ? 275 VAL D C   1 
ATOM   9900  O  O   . VAL D 1 211 ? 45.076 38.283 35.174  1.00 71.79  ? 275 VAL D O   1 
ATOM   9901  C  CB  . VAL D 1 211 ? 45.329 40.439 37.389  1.00 64.88  ? 275 VAL D CB  1 
ATOM   9902  C  CG1 . VAL D 1 211 ? 44.223 39.839 38.242  1.00 69.24  ? 275 VAL D CG1 1 
ATOM   9903  C  CG2 . VAL D 1 211 ? 46.107 41.490 38.166  1.00 63.01  ? 275 VAL D CG2 1 
ATOM   9904  N  N   . LYS D 1 212 ? 45.322 37.138 37.085  1.00 64.80  ? 276 LYS D N   1 
ATOM   9905  C  CA  . LYS D 1 212 ? 44.785 35.884 36.594  1.00 62.97  ? 276 LYS D CA  1 
ATOM   9906  C  C   . LYS D 1 212 ? 43.618 35.472 37.446  1.00 64.07  ? 276 LYS D C   1 
ATOM   9907  O  O   . LYS D 1 212 ? 43.753 35.205 38.646  1.00 70.92  ? 276 LYS D O   1 
ATOM   9908  C  CB  . LYS D 1 212 ? 45.865 34.805 36.622  1.00 68.71  ? 276 LYS D CB  1 
ATOM   9909  C  CG  . LYS D 1 212 ? 47.104 35.209 35.859  1.00 81.06  ? 276 LYS D CG  1 
ATOM   9910  C  CD  . LYS D 1 212 ? 48.153 34.133 35.860  1.00 94.58  ? 276 LYS D CD  1 
ATOM   9911  C  CE  . LYS D 1 212 ? 49.352 34.574 35.031  1.00 105.30 ? 276 LYS D CE  1 
ATOM   9912  N  NZ  . LYS D 1 212 ? 50.346 33.485 34.878  1.00 100.17 ? 276 LYS D NZ  1 
ATOM   9913  N  N   . CYS D 1 213 ? 42.467 35.408 36.807  1.00 64.47  ? 277 CYS D N   1 
ATOM   9914  C  CA  . CYS D 1 213 ? 41.218 35.188 37.508  1.00 76.59  ? 277 CYS D CA  1 
ATOM   9915  C  C   . CYS D 1 213 ? 40.508 33.899 37.086  1.00 72.25  ? 277 CYS D C   1 
ATOM   9916  O  O   . CYS D 1 213 ? 40.377 33.593 35.897  1.00 67.89  ? 277 CYS D O   1 
ATOM   9917  C  CB  . CYS D 1 213 ? 40.286 36.391 37.305  1.00 83.52  ? 277 CYS D CB  1 
ATOM   9918  S  SG  . CYS D 1 213 ? 40.956 37.878 37.994  1.00 119.17 ? 277 CYS D SG  1 
ATOM   9919  N  N   . THR D 1 214 ? 40.040 33.161 38.080  1.00 63.17  ? 278 THR D N   1 
ATOM   9920  C  CA  . THR D 1 214 ? 39.182 32.016 37.863  1.00 63.15  ? 278 THR D CA  1 
ATOM   9921  C  C   . THR D 1 214 ? 37.679 32.361 38.076  1.00 65.46  ? 278 THR D C   1 
ATOM   9922  O  O   . THR D 1 214 ? 37.195 32.547 39.191  1.00 63.88  ? 278 THR D O   1 
ATOM   9923  C  CB  . THR D 1 214 ? 39.596 30.897 38.834  1.00 65.01  ? 278 THR D CB  1 
ATOM   9924  O  OG1 . THR D 1 214 ? 41.023 30.724 38.800  1.00 73.71  ? 278 THR D OG1 1 
ATOM   9925  C  CG2 . THR D 1 214 ? 38.882 29.609 38.482  1.00 60.35  ? 278 THR D CG2 1 
ATOM   9926  N  N   . GLY D 1 215 ? 36.915 32.425 37.009  1.00 72.94  ? 279 GLY D N   1 
ATOM   9927  C  CA  . GLY D 1 215 ? 35.489 32.618 37.180  1.00 78.92  ? 279 GLY D CA  1 
ATOM   9928  C  C   . GLY D 1 215 ? 34.686 31.348 37.403  1.00 88.99  ? 279 GLY D C   1 
ATOM   9929  O  O   . GLY D 1 215 ? 35.225 30.249 37.582  1.00 88.15  ? 279 GLY D O   1 
ATOM   9930  N  N   . THR D 1 216 ? 33.373 31.519 37.369  1.00 78.49  ? 280 THR D N   1 
ATOM   9931  C  CA  . THR D 1 216 ? 32.442 30.429 37.548  1.00 81.07  ? 280 THR D CA  1 
ATOM   9932  C  C   . THR D 1 216 ? 31.338 30.564 36.500  1.00 83.25  ? 280 THR D C   1 
ATOM   9933  O  O   . THR D 1 216 ? 30.688 31.602 36.423  1.00 65.08  ? 280 THR D O   1 
ATOM   9934  C  CB  . THR D 1 216 ? 31.913 30.441 38.994  1.00 76.57  ? 280 THR D CB  1 
ATOM   9935  O  OG1 . THR D 1 216 ? 32.857 29.759 39.842  1.00 90.66  ? 280 THR D OG1 1 
ATOM   9936  C  CG2 . THR D 1 216 ? 30.497 29.833 39.112  1.00 62.09  ? 280 THR D CG2 1 
ATOM   9937  N  N   . ASN D 1 217 ? 31.169 29.531 35.668  1.00 91.66  ? 281 ASN D N   1 
ATOM   9938  C  CA  . ASN D 1 217 ? 30.149 29.557 34.623  1.00 78.28  ? 281 ASN D CA  1 
ATOM   9939  C  C   . ASN D 1 217 ? 28.886 28.879 35.091  1.00 74.80  ? 281 ASN D C   1 
ATOM   9940  O  O   . ASN D 1 217 ? 28.832 27.646 35.235  1.00 69.52  ? 281 ASN D O   1 
ATOM   9941  C  CB  . ASN D 1 217 ? 30.661 28.890 33.358  1.00 90.88  ? 281 ASN D CB  1 
ATOM   9942  C  CG  . ASN D 1 217 ? 29.746 29.103 32.178  1.00 89.61  ? 281 ASN D CG  1 
ATOM   9943  O  OD1 . ASN D 1 217 ? 28.524 29.118 32.330  1.00 85.61  ? 281 ASN D OD1 1 
ATOM   9944  N  ND2 . ASN D 1 217 ? 30.334 29.261 30.982  1.00 85.69  ? 281 ASN D ND2 1 
ATOM   9945  N  N   . LEU D 1 218 ? 27.876 29.702 35.338  1.00 72.88  ? 282 LEU D N   1 
ATOM   9946  C  CA  . LEU D 1 218 ? 26.617 29.227 35.894  1.00 74.09  ? 282 LEU D CA  1 
ATOM   9947  C  C   . LEU D 1 218 ? 25.646 28.822 34.814  1.00 80.34  ? 282 LEU D C   1 
ATOM   9948  O  O   . LEU D 1 218 ? 24.532 28.407 35.112  1.00 82.81  ? 282 LEU D O   1 
ATOM   9949  C  CB  . LEU D 1 218 ? 25.955 30.294 36.760  1.00 72.10  ? 282 LEU D CB  1 
ATOM   9950  C  CG  . LEU D 1 218 ? 26.516 30.500 38.151  1.00 78.41  ? 282 LEU D CG  1 
ATOM   9951  C  CD1 . LEU D 1 218 ? 27.399 31.688 38.068  1.00 94.45  ? 282 LEU D CD1 1 
ATOM   9952  C  CD2 . LEU D 1 218 ? 25.380 30.764 39.110  1.00 75.40  ? 282 LEU D CD2 1 
ATOM   9953  N  N   . TRP D 1 219 ? 26.078 28.924 33.564  1.00 89.48  ? 283 TRP D N   1 
ATOM   9954  C  CA  . TRP D 1 219 ? 25.194 28.738 32.428  1.00 84.46  ? 283 TRP D CA  1 
ATOM   9955  C  C   . TRP D 1 219 ? 25.446 27.457 31.669  1.00 82.71  ? 283 TRP D C   1 
ATOM   9956  O  O   . TRP D 1 219 ? 24.692 26.496 31.807  1.00 79.90  ? 283 TRP D O   1 
ATOM   9957  C  CB  . TRP D 1 219 ? 25.293 29.964 31.529  1.00 84.13  ? 283 TRP D CB  1 
ATOM   9958  C  CG  . TRP D 1 219 ? 24.548 29.858 30.233  1.00 85.04  ? 283 TRP D CG  1 
ATOM   9959  C  CD1 . TRP D 1 219 ? 23.442 29.062 29.940  1.00 78.01  ? 283 TRP D CD1 1 
ATOM   9960  C  CD2 . TRP D 1 219 ? 24.819 30.609 29.016  1.00 87.80  ? 283 TRP D CD2 1 
ATOM   9961  N  NE1 . TRP D 1 219 ? 23.042 29.255 28.654  1.00 85.19  ? 283 TRP D NE1 1 
ATOM   9962  C  CE2 . TRP D 1 219 ? 23.822 30.175 28.043  1.00 94.74  ? 283 TRP D CE2 1 
ATOM   9963  C  CE3 . TRP D 1 219 ? 25.756 31.567 28.645  1.00 87.75  ? 283 TRP D CE3 1 
ATOM   9964  C  CZ2 . TRP D 1 219 ? 23.782 30.692 26.760  1.00 108.65 ? 283 TRP D CZ2 1 
ATOM   9965  C  CZ3 . TRP D 1 219 ? 25.715 32.074 27.342  1.00 92.91  ? 283 TRP D CZ3 1 
ATOM   9966  C  CH2 . TRP D 1 219 ? 24.751 31.647 26.425  1.00 102.81 ? 283 TRP D CH2 1 
ATOM   9967  N  N   . ASN D 1 220 ? 26.512 27.433 30.875  1.00 80.42  ? 284 ASN D N   1 
ATOM   9968  C  CA  . ASN D 1 220 ? 26.747 26.363 29.912  1.00 85.19  ? 284 ASN D CA  1 
ATOM   9969  C  C   . ASN D 1 220 ? 28.056 25.581 30.137  1.00 95.02  ? 284 ASN D C   1 
ATOM   9970  O  O   . ASN D 1 220 ? 28.556 24.944 29.211  1.00 127.49 ? 284 ASN D O   1 
ATOM   9971  C  CB  . ASN D 1 220 ? 26.744 26.970 28.508  1.00 82.36  ? 284 ASN D CB  1 
ATOM   9972  C  CG  . ASN D 1 220 ? 27.686 28.163 28.383  1.00 90.03  ? 284 ASN D CG  1 
ATOM   9973  O  OD1 . ASN D 1 220 ? 28.572 28.361 29.217  1.00 115.78 ? 284 ASN D OD1 1 
ATOM   9974  N  ND2 . ASN D 1 220 ? 27.498 28.964 27.345  1.00 80.13  ? 284 ASN D ND2 1 
ATOM   9975  N  N   . ASP D 1 221 ? 28.594 25.615 31.357  1.00 87.63  ? 285 ASP D N   1 
ATOM   9976  C  CA  . ASP D 1 221 ? 29.942 25.101 31.623  1.00 89.19  ? 285 ASP D CA  1 
ATOM   9977  C  C   . ASP D 1 221 ? 30.190 24.500 33.035  1.00 86.22  ? 285 ASP D C   1 
ATOM   9978  O  O   . ASP D 1 221 ? 29.858 25.099 34.072  1.00 78.92  ? 285 ASP D O   1 
ATOM   9979  C  CB  . ASP D 1 221 ? 30.971 26.196 31.306  1.00 90.67  ? 285 ASP D CB  1 
ATOM   9980  C  CG  . ASP D 1 221 ? 32.382 25.670 31.184  1.00 116.49 ? 285 ASP D CG  1 
ATOM   9981  O  OD1 . ASP D 1 221 ? 32.602 24.442 31.290  1.00 129.88 ? 285 ASP D OD1 1 
ATOM   9982  O  OD2 . ASP D 1 221 ? 33.284 26.503 30.964  1.00 141.58 ? 285 ASP D OD2 1 
ATOM   9983  N  N   . ALA D 1 222 ? 30.781 23.305 33.034  1.00 83.08  ? 286 ALA D N   1 
ATOM   9984  C  CA  . ALA D 1 222 ? 31.181 22.573 34.232  1.00 91.27  ? 286 ALA D CA  1 
ATOM   9985  C  C   . ALA D 1 222 ? 32.690 22.684 34.483  1.00 92.43  ? 286 ALA D C   1 
ATOM   9986  O  O   . ALA D 1 222 ? 33.214 22.132 35.457  1.00 96.36  ? 286 ALA D O   1 
ATOM   9987  C  CB  . ALA D 1 222 ? 30.773 21.104 34.115  1.00 116.11 ? 286 ALA D CB  1 
ATOM   9988  N  N   . LYS D 1 223 ? 33.385 23.374 33.588  1.00 87.82  ? 287 LYS D N   1 
ATOM   9989  C  CA  . LYS D 1 223 ? 34.750 23.791 33.843  1.00 93.36  ? 287 LYS D CA  1 
ATOM   9990  C  C   . LYS D 1 223 ? 34.715 25.248 34.305  1.00 95.59  ? 287 LYS D C   1 
ATOM   9991  O  O   . LYS D 1 223 ? 33.647 25.852 34.424  1.00 109.66 ? 287 LYS D O   1 
ATOM   9992  C  CB  . LYS D 1 223 ? 35.599 23.667 32.588  1.00 85.10  ? 287 LYS D CB  1 
ATOM   9993  C  CG  . LYS D 1 223 ? 35.702 22.279 31.984  1.00 82.13  ? 287 LYS D CG  1 
ATOM   9994  C  CD  . LYS D 1 223 ? 36.759 22.343 30.872  1.00 91.61  ? 287 LYS D CD  1 
ATOM   9995  C  CE  . LYS D 1 223 ? 36.756 21.168 29.922  1.00 87.95  ? 287 LYS D CE  1 
ATOM   9996  N  NZ  . LYS D 1 223 ? 37.976 21.211 29.083  1.00 102.13 ? 287 LYS D NZ  1 
ATOM   9997  N  N   . ARG D 1 224 ? 35.879 25.815 34.580  1.00 99.34  ? 288 ARG D N   1 
ATOM   9998  C  CA  . ARG D 1 224 ? 35.928 27.193 35.019  1.00 84.72  ? 288 ARG D CA  1 
ATOM   9999  C  C   . ARG D 1 224 ? 36.637 28.054 33.982  1.00 83.38  ? 288 ARG D C   1 
ATOM   10000 O  O   . ARG D 1 224 ? 37.786 27.804 33.641  1.00 84.94  ? 288 ARG D O   1 
ATOM   10001 C  CB  . ARG D 1 224 ? 36.622 27.311 36.373  1.00 77.05  ? 288 ARG D CB  1 
ATOM   10002 C  CG  . ARG D 1 224 ? 36.258 26.221 37.358  1.00 87.77  ? 288 ARG D CG  1 
ATOM   10003 C  CD  . ARG D 1 224 ? 36.516 26.653 38.788  1.00 80.16  ? 288 ARG D CD  1 
ATOM   10004 N  NE  . ARG D 1 224 ? 35.269 27.082 39.401  1.00 73.34  ? 288 ARG D NE  1 
ATOM   10005 C  CZ  . ARG D 1 224 ? 34.678 26.446 40.407  1.00 75.11  ? 288 ARG D CZ  1 
ATOM   10006 N  NH1 . ARG D 1 224 ? 35.238 25.360 40.947  1.00 91.43  ? 288 ARG D NH1 1 
ATOM   10007 N  NH2 . ARG D 1 224 ? 33.542 26.916 40.894  1.00 60.45  ? 288 ARG D NH2 1 
ATOM   10008 N  N   . PRO D 1 225 ? 35.955 29.093 33.487  1.00 77.98  ? 289 PRO D N   1 
ATOM   10009 C  CA  . PRO D 1 225 ? 36.611 30.036 32.588  1.00 65.61  ? 289 PRO D CA  1 
ATOM   10010 C  C   . PRO D 1 225 ? 37.764 30.670 33.304  1.00 63.80  ? 289 PRO D C   1 
ATOM   10011 O  O   . PRO D 1 225 ? 37.785 30.716 34.533  1.00 82.91  ? 289 PRO D O   1 
ATOM   10012 C  CB  . PRO D 1 225 ? 35.552 31.094 32.354  1.00 68.01  ? 289 PRO D CB  1 
ATOM   10013 C  CG  . PRO D 1 225 ? 34.268 30.434 32.747  1.00 77.64  ? 289 PRO D CG  1 
ATOM   10014 C  CD  . PRO D 1 225 ? 34.604 29.533 33.869  1.00 70.66  ? 289 PRO D CD  1 
ATOM   10015 N  N   . PHE D 1 226 ? 38.732 31.141 32.549  1.00 63.29  ? 290 PHE D N   1 
ATOM   10016 C  CA  . PHE D 1 226 ? 39.921 31.706 33.140  1.00 67.46  ? 290 PHE D CA  1 
ATOM   10017 C  C   . PHE D 1 226 ? 40.265 32.984 32.422  1.00 75.14  ? 290 PHE D C   1 
ATOM   10018 O  O   . PHE D 1 226 ? 40.067 33.094 31.221  1.00 95.13  ? 290 PHE D O   1 
ATOM   10019 C  CB  . PHE D 1 226 ? 41.073 30.722 33.061  1.00 61.88  ? 290 PHE D CB  1 
ATOM   10020 C  CG  . PHE D 1 226 ? 42.228 31.076 33.951  1.00 69.41  ? 290 PHE D CG  1 
ATOM   10021 C  CD1 . PHE D 1 226 ? 42.272 30.616 35.279  1.00 67.43  ? 290 PHE D CD1 1 
ATOM   10022 C  CD2 . PHE D 1 226 ? 43.287 31.859 33.463  1.00 69.97  ? 290 PHE D CD2 1 
ATOM   10023 C  CE1 . PHE D 1 226 ? 43.353 30.927 36.107  1.00 69.10  ? 290 PHE D CE1 1 
ATOM   10024 C  CE2 . PHE D 1 226 ? 44.373 32.179 34.276  1.00 70.32  ? 290 PHE D CE2 1 
ATOM   10025 C  CZ  . PHE D 1 226 ? 44.408 31.716 35.603  1.00 78.51  ? 290 PHE D CZ  1 
ATOM   10026 N  N   . LEU D 1 227 ? 40.775 33.958 33.160  1.00 75.15  ? 291 LEU D N   1 
ATOM   10027 C  CA  . LEU D 1 227 ? 41.015 35.269 32.595  1.00 73.47  ? 291 LEU D CA  1 
ATOM   10028 C  C   . LEU D 1 227 ? 42.382 35.786 32.936  1.00 77.85  ? 291 LEU D C   1 
ATOM   10029 O  O   . LEU D 1 227 ? 42.828 35.682 34.081  1.00 112.90 ? 291 LEU D O   1 
ATOM   10030 C  CB  . LEU D 1 227 ? 39.987 36.250 33.132  1.00 77.00  ? 291 LEU D CB  1 
ATOM   10031 C  CG  . LEU D 1 227 ? 40.171 37.711 32.727  1.00 68.05  ? 291 LEU D CG  1 
ATOM   10032 C  CD1 . LEU D 1 227 ? 39.975 37.841 31.219  1.00 68.89  ? 291 LEU D CD1 1 
ATOM   10033 C  CD2 . LEU D 1 227 ? 39.197 38.577 33.506  1.00 64.74  ? 291 LEU D CD2 1 
ATOM   10034 N  N   . GLU D 1 228 ? 43.025 36.371 31.940  1.00 78.28  ? 292 GLU D N   1 
ATOM   10035 C  CA  . GLU D 1 228 ? 44.317 37.006 32.099  1.00 91.09  ? 292 GLU D CA  1 
ATOM   10036 C  C   . GLU D 1 228 ? 44.143 38.443 31.628  1.00 89.33  ? 292 GLU D C   1 
ATOM   10037 O  O   . GLU D 1 228 ? 43.534 38.669 30.591  1.00 84.01  ? 292 GLU D O   1 
ATOM   10038 C  CB  . GLU D 1 228 ? 45.349 36.287 31.229  1.00 103.93 ? 292 GLU D CB  1 
ATOM   10039 C  CG  . GLU D 1 228 ? 46.724 36.093 31.858  1.00 135.42 ? 292 GLU D CG  1 
ATOM   10040 C  CD  . GLU D 1 228 ? 47.747 35.544 30.865  1.00 156.41 ? 292 GLU D CD  1 
ATOM   10041 O  OE1 . GLU D 1 228 ? 48.315 34.464 31.126  1.00 163.23 ? 292 GLU D OE1 1 
ATOM   10042 O  OE2 . GLU D 1 228 ? 47.977 36.187 29.817  1.00 152.91 ? 292 GLU D OE2 1 
ATOM   10043 N  N   . PHE D 1 229 ? 44.638 39.407 32.402  1.00 87.42  ? 293 PHE D N   1 
ATOM   10044 C  CA  . PHE D 1 229 ? 44.722 40.788 31.951  1.00 82.19  ? 293 PHE D CA  1 
ATOM   10045 C  C   . PHE D 1 229 ? 45.838 41.500 32.648  1.00 84.78  ? 293 PHE D C   1 
ATOM   10046 O  O   . PHE D 1 229 ? 46.262 41.076 33.728  1.00 85.71  ? 293 PHE D O   1 
ATOM   10047 C  CB  . PHE D 1 229 ? 43.408 41.529 32.187  1.00 85.36  ? 293 PHE D CB  1 
ATOM   10048 C  CG  . PHE D 1 229 ? 43.034 41.701 33.629  1.00 78.18  ? 293 PHE D CG  1 
ATOM   10049 C  CD1 . PHE D 1 229 ? 43.543 42.763 34.379  1.00 78.44  ? 293 PHE D CD1 1 
ATOM   10050 C  CD2 . PHE D 1 229 ? 42.113 40.841 34.224  1.00 78.98  ? 293 PHE D CD2 1 
ATOM   10051 C  CE1 . PHE D 1 229 ? 43.177 42.935 35.729  1.00 73.65  ? 293 PHE D CE1 1 
ATOM   10052 C  CE2 . PHE D 1 229 ? 41.737 41.011 35.568  1.00 71.96  ? 293 PHE D CE2 1 
ATOM   10053 C  CZ  . PHE D 1 229 ? 42.281 42.055 36.318  1.00 65.71  ? 293 PHE D CZ  1 
ATOM   10054 N  N   . ASP D 1 230 ? 46.302 42.593 32.050  1.00 86.77  ? 294 ASP D N   1 
ATOM   10055 C  CA  . ASP D 1 230 ? 47.386 43.360 32.659  1.00 107.88 ? 294 ASP D CA  1 
ATOM   10056 C  C   . ASP D 1 230 ? 46.947 44.788 32.969  1.00 110.69 ? 294 ASP D C   1 
ATOM   10057 O  O   . ASP D 1 230 ? 45.754 45.093 32.898  1.00 93.75  ? 294 ASP D O   1 
ATOM   10058 C  CB  . ASP D 1 230 ? 48.595 43.361 31.743  1.00 112.82 ? 294 ASP D CB  1 
ATOM   10059 C  CG  . ASP D 1 230 ? 48.289 43.967 30.410  1.00 126.38 ? 294 ASP D CG  1 
ATOM   10060 O  OD1 . ASP D 1 230 ? 47.200 44.569 30.270  1.00 127.05 ? 294 ASP D OD1 1 
ATOM   10061 O  OD2 . ASP D 1 230 ? 49.133 43.840 29.504  1.00 144.42 ? 294 ASP D OD2 1 
ATOM   10062 N  N   . GLN D 1 231 ? 47.906 45.658 33.301  1.00 119.07 ? 295 GLN D N   1 
ATOM   10063 C  CA  . GLN D 1 231 ? 47.570 47.028 33.686  1.00 109.96 ? 295 GLN D CA  1 
ATOM   10064 C  C   . GLN D 1 231 ? 46.915 47.838 32.560  1.00 109.43 ? 295 GLN D C   1 
ATOM   10065 O  O   . GLN D 1 231 ? 46.061 48.669 32.825  1.00 106.87 ? 295 GLN D O   1 
ATOM   10066 C  CB  . GLN D 1 231 ? 48.743 47.771 34.357  1.00 117.19 ? 295 GLN D CB  1 
ATOM   10067 C  CG  . GLN D 1 231 ? 50.039 47.930 33.562  1.00 134.67 ? 295 GLN D CG  1 
ATOM   10068 C  CD  . GLN D 1 231 ? 51.120 48.639 34.374  1.00 152.36 ? 295 GLN D CD  1 
ATOM   10069 O  OE1 . GLN D 1 231 ? 51.079 48.655 35.607  1.00 156.63 ? 295 GLN D OE1 1 
ATOM   10070 N  NE2 . GLN D 1 231 ? 52.090 49.227 33.685  1.00 171.87 ? 295 GLN D NE2 1 
ATOM   10071 N  N   . SER D 1 232 ? 47.269 47.564 31.309  1.00 108.31 ? 296 SER D N   1 
ATOM   10072 C  CA  . SER D 1 232 ? 46.682 48.290 30.183  1.00 103.27 ? 296 SER D CA  1 
ATOM   10073 C  C   . SER D 1 232 ? 45.317 47.745 29.719  1.00 108.36 ? 296 SER D C   1 
ATOM   10074 O  O   . SER D 1 232 ? 44.791 48.174 28.687  1.00 110.51 ? 296 SER D O   1 
ATOM   10075 C  CB  . SER D 1 232 ? 47.653 48.291 29.015  1.00 104.17 ? 296 SER D CB  1 
ATOM   10076 O  OG  . SER D 1 232 ? 47.821 46.974 28.527  1.00 118.79 ? 296 SER D OG  1 
ATOM   10077 N  N   . PHE D 1 233 ? 44.751 46.808 30.480  1.00 103.05 ? 297 PHE D N   1 
ATOM   10078 C  CA  . PHE D 1 233 ? 43.488 46.135 30.129  1.00 96.06  ? 297 PHE D CA  1 
ATOM   10079 C  C   . PHE D 1 233 ? 43.468 45.281 28.857  1.00 98.63  ? 297 PHE D C   1 
ATOM   10080 O  O   . PHE D 1 233 ? 42.386 44.978 28.350  1.00 91.56  ? 297 PHE D O   1 
ATOM   10081 C  CB  . PHE D 1 233 ? 42.328 47.122 30.057  1.00 103.07 ? 297 PHE D CB  1 
ATOM   10082 C  CG  . PHE D 1 233 ? 41.867 47.610 31.386  1.00 115.35 ? 297 PHE D CG  1 
ATOM   10083 C  CD1 . PHE D 1 233 ? 41.905 46.781 32.504  1.00 107.99 ? 297 PHE D CD1 1 
ATOM   10084 C  CD2 . PHE D 1 233 ? 41.367 48.898 31.518  1.00 123.75 ? 297 PHE D CD2 1 
ATOM   10085 C  CE1 . PHE D 1 233 ? 41.472 47.236 33.744  1.00 114.49 ? 297 PHE D CE1 1 
ATOM   10086 C  CE2 . PHE D 1 233 ? 40.934 49.360 32.751  1.00 138.70 ? 297 PHE D CE2 1 
ATOM   10087 C  CZ  . PHE D 1 233 ? 40.985 48.523 33.868  1.00 133.58 ? 297 PHE D CZ  1 
ATOM   10088 N  N   . THR D 1 234 ? 44.633 44.902 28.325  1.00 100.50 ? 298 THR D N   1 
ATOM   10089 C  CA  . THR D 1 234 ? 44.660 43.864 27.289  1.00 92.42  ? 298 THR D CA  1 
ATOM   10090 C  C   . THR D 1 234 ? 44.466 42.528 27.998  1.00 98.66  ? 298 THR D C   1 
ATOM   10091 O  O   . THR D 1 234 ? 45.126 42.227 29.007  1.00 124.36 ? 298 THR D O   1 
ATOM   10092 C  CB  . THR D 1 234 ? 45.920 43.899 26.396  1.00 96.00  ? 298 THR D CB  1 
ATOM   10093 O  OG1 . THR D 1 234 ? 47.106 43.863 27.200  1.00 93.28  ? 298 THR D OG1 1 
ATOM   10094 C  CG2 . THR D 1 234 ? 45.931 45.166 25.529  1.00 104.81 ? 298 THR D CG2 1 
ATOM   10095 N  N   . TYR D 1 235 ? 43.509 41.754 27.503  1.00 90.16  ? 299 TYR D N   1 
ATOM   10096 C  CA  . TYR D 1 235 ? 43.041 40.583 28.222  1.00 85.25  ? 299 TYR D CA  1 
ATOM   10097 C  C   . TYR D 1 235 ? 42.727 39.445 27.268  1.00 84.35  ? 299 TYR D C   1 
ATOM   10098 O  O   . TYR D 1 235 ? 42.332 39.681 26.144  1.00 94.72  ? 299 TYR D O   1 
ATOM   10099 C  CB  . TYR D 1 235 ? 41.776 40.942 29.001  1.00 81.39  ? 299 TYR D CB  1 
ATOM   10100 C  CG  . TYR D 1 235 ? 40.540 41.014 28.137  1.00 81.81  ? 299 TYR D CG  1 
ATOM   10101 C  CD1 . TYR D 1 235 ? 40.198 42.184 27.482  1.00 78.56  ? 299 TYR D CD1 1 
ATOM   10102 C  CD2 . TYR D 1 235 ? 39.718 39.893 27.967  1.00 85.85  ? 299 TYR D CD2 1 
ATOM   10103 C  CE1 . TYR D 1 235 ? 39.068 42.246 26.685  1.00 89.08  ? 299 TYR D CE1 1 
ATOM   10104 C  CE2 . TYR D 1 235 ? 38.585 39.942 27.172  1.00 89.21  ? 299 TYR D CE2 1 
ATOM   10105 C  CZ  . TYR D 1 235 ? 38.263 41.125 26.530  1.00 95.44  ? 299 TYR D CZ  1 
ATOM   10106 O  OH  . TYR D 1 235 ? 37.137 41.198 25.731  1.00 101.46 ? 299 TYR D OH  1 
ATOM   10107 N  N   . THR D 1 236 ? 42.882 38.211 27.726  1.00 89.90  ? 300 THR D N   1 
ATOM   10108 C  CA  . THR D 1 236 ? 42.397 37.046 26.974  1.00 94.39  ? 300 THR D CA  1 
ATOM   10109 C  C   . THR D 1 236 ? 41.701 36.049 27.906  1.00 92.67  ? 300 THR D C   1 
ATOM   10110 O  O   . THR D 1 236 ? 42.136 35.851 29.045  1.00 99.49  ? 300 THR D O   1 
ATOM   10111 C  CB  . THR D 1 236 ? 43.531 36.282 26.236  1.00 98.01  ? 300 THR D CB  1 
ATOM   10112 O  OG1 . THR D 1 236 ? 44.301 35.531 27.185  1.00 101.39 ? 300 THR D OG1 1 
ATOM   10113 C  CG2 . THR D 1 236 ? 44.447 37.228 25.444  1.00 101.62 ? 300 THR D CG2 1 
ATOM   10114 N  N   . PHE D 1 237 ? 40.618 35.436 27.427  1.00 84.25  ? 301 PHE D N   1 
ATOM   10115 C  CA  . PHE D 1 237 ? 39.997 34.326 28.136  1.00 75.14  ? 301 PHE D CA  1 
ATOM   10116 C  C   . PHE D 1 237 ? 40.614 33.031 27.650  1.00 74.48  ? 301 PHE D C   1 
ATOM   10117 O  O   . PHE D 1 237 ? 40.823 32.845 26.462  1.00 68.33  ? 301 PHE D O   1 
ATOM   10118 C  CB  . PHE D 1 237 ? 38.505 34.282 27.894  1.00 76.19  ? 301 PHE D CB  1 
ATOM   10119 C  CG  . PHE D 1 237 ? 37.728 35.293 28.677  1.00 82.54  ? 301 PHE D CG  1 
ATOM   10120 C  CD1 . PHE D 1 237 ? 37.406 36.536 28.125  1.00 83.81  ? 301 PHE D CD1 1 
ATOM   10121 C  CD2 . PHE D 1 237 ? 37.288 34.997 29.954  1.00 85.22  ? 301 PHE D CD2 1 
ATOM   10122 C  CE1 . PHE D 1 237 ? 36.664 37.474 28.850  1.00 83.68  ? 301 PHE D CE1 1 
ATOM   10123 C  CE2 . PHE D 1 237 ? 36.548 35.927 30.686  1.00 88.43  ? 301 PHE D CE2 1 
ATOM   10124 C  CZ  . PHE D 1 237 ? 36.239 37.165 30.131  1.00 88.74  ? 301 PHE D CZ  1 
ATOM   10125 N  N   . LYS D 1 238 ? 40.937 32.154 28.592  1.00 85.09  ? 302 LYS D N   1 
ATOM   10126 C  CA  . LYS D 1 238 ? 41.453 30.823 28.307  1.00 85.43  ? 302 LYS D CA  1 
ATOM   10127 C  C   . LYS D 1 238 ? 40.507 29.826 28.954  1.00 88.66  ? 302 LYS D C   1 
ATOM   10128 O  O   . LYS D 1 238 ? 39.942 30.081 30.010  1.00 91.96  ? 302 LYS D O   1 
ATOM   10129 C  CB  . LYS D 1 238 ? 42.858 30.626 28.884  1.00 81.06  ? 302 LYS D CB  1 
ATOM   10130 C  CG  . LYS D 1 238 ? 43.869 31.710 28.528  1.00 95.76  ? 302 LYS D CG  1 
ATOM   10131 C  CD  . LYS D 1 238 ? 45.241 31.427 29.148  1.00 107.84 ? 302 LYS D CD  1 
ATOM   10132 C  CE  . LYS D 1 238 ? 46.374 31.843 28.215  1.00 111.29 ? 302 LYS D CE  1 
ATOM   10133 N  NZ  . LYS D 1 238 ? 47.574 30.973 28.383  1.00 112.55 ? 302 LYS D NZ  1 
ATOM   10134 N  N   . GLU D 1 239 ? 40.334 28.685 28.317  1.00 98.33  ? 303 GLU D N   1 
ATOM   10135 C  CA  . GLU D 1 239 ? 39.546 27.624 28.906  1.00 102.83 ? 303 GLU D CA  1 
ATOM   10136 C  C   . GLU D 1 239 ? 40.499 26.472 29.205  1.00 106.24 ? 303 GLU D C   1 
ATOM   10137 O  O   . GLU D 1 239 ? 41.272 26.081 28.325  1.00 120.47 ? 303 GLU D O   1 
ATOM   10138 C  CB  . GLU D 1 239 ? 38.461 27.193 27.917  1.00 117.79 ? 303 GLU D CB  1 
ATOM   10139 C  CG  . GLU D 1 239 ? 37.674 25.939 28.303  1.00 133.01 ? 303 GLU D CG  1 
ATOM   10140 C  CD  . GLU D 1 239 ? 36.489 26.205 29.228  1.00 145.73 ? 303 GLU D CD  1 
ATOM   10141 O  OE1 . GLU D 1 239 ? 36.124 27.375 29.458  1.00 178.30 ? 303 GLU D OE1 1 
ATOM   10142 O  OE2 . GLU D 1 239 ? 35.903 25.223 29.719  1.00 160.39 ? 303 GLU D OE2 1 
ATOM   10143 N  N   . PRO D 1 240 ? 40.442 25.916 30.433  1.00 80.41  ? 304 PRO D N   1 
ATOM   10144 C  CA  . PRO D 1 240 ? 41.341 24.844 30.833  1.00 85.35  ? 304 PRO D CA  1 
ATOM   10145 C  C   . PRO D 1 240 ? 41.054 23.563 30.075  1.00 106.64 ? 304 PRO D C   1 
ATOM   10146 O  O   . PRO D 1 240 ? 39.883 23.183 29.936  1.00 97.60  ? 304 PRO D O   1 
ATOM   10147 C  CB  . PRO D 1 240 ? 41.022 24.648 32.317  1.00 79.23  ? 304 PRO D CB  1 
ATOM   10148 C  CG  . PRO D 1 240 ? 39.660 25.072 32.475  1.00 69.91  ? 304 PRO D CG  1 
ATOM   10149 C  CD  . PRO D 1 240 ? 39.401 26.151 31.442  1.00 77.03  ? 304 PRO D CD  1 
ATOM   10150 N  N   . CYS D 1 241 ? 42.119 22.914 29.595  1.00 119.77 ? 305 CYS D N   1 
ATOM   10151 C  CA  . CYS D 1 241 ? 42.006 21.720 28.767  1.00 109.22 ? 305 CYS D CA  1 
ATOM   10152 C  C   . CYS D 1 241 ? 42.298 20.486 29.593  1.00 113.38 ? 305 CYS D C   1 
ATOM   10153 O  O   . CYS D 1 241 ? 43.227 19.741 29.277  1.00 154.25 ? 305 CYS D O   1 
ATOM   10154 C  CB  . CYS D 1 241 ? 43.002 21.780 27.611  1.00 127.73 ? 305 CYS D CB  1 
ATOM   10155 S  SG  . CYS D 1 241 ? 42.994 23.306 26.651  1.00 193.96 ? 305 CYS D SG  1 
ATOM   10156 N  N   . LEU D 1 242 ? 41.522 20.267 30.652  1.00 103.49 ? 306 LEU D N   1 
ATOM   10157 C  CA  . LEU D 1 242 ? 41.741 19.116 31.526  1.00 101.37 ? 306 LEU D CA  1 
ATOM   10158 C  C   . LEU D 1 242 ? 40.434 18.469 31.968  1.00 109.39 ? 306 LEU D C   1 
ATOM   10159 O  O   . LEU D 1 242 ? 39.472 19.163 32.270  1.00 113.06 ? 306 LEU D O   1 
ATOM   10160 C  CB  . LEU D 1 242 ? 42.606 19.494 32.735  1.00 83.83  ? 306 LEU D CB  1 
ATOM   10161 C  CG  . LEU D 1 242 ? 44.075 19.864 32.460  1.00 102.83 ? 306 LEU D CG  1 
ATOM   10162 C  CD1 . LEU D 1 242 ? 44.748 20.438 33.708  1.00 103.54 ? 306 LEU D CD1 1 
ATOM   10163 C  CD2 . LEU D 1 242 ? 44.910 18.692 31.887  1.00 98.73  ? 306 LEU D CD2 1 
ATOM   10164 N  N   . GLY D 1 243 ? 40.419 17.136 31.999  1.00 141.26 ? 307 GLY D N   1 
ATOM   10165 C  CA  . GLY D 1 243 ? 39.238 16.350 32.367  1.00 128.20 ? 307 GLY D CA  1 
ATOM   10166 C  C   . GLY D 1 243 ? 38.812 16.473 33.819  1.00 122.46 ? 307 GLY D C   1 
ATOM   10167 O  O   . GLY D 1 243 ? 37.794 15.892 34.217  1.00 115.76 ? 307 GLY D O   1 
ATOM   10168 N  N   . PHE D 1 244 ? 39.596 17.222 34.601  1.00 110.38 ? 308 PHE D N   1 
ATOM   10169 C  CA  . PHE D 1 244 ? 39.272 17.572 35.992  1.00 105.60 ? 308 PHE D CA  1 
ATOM   10170 C  C   . PHE D 1 244 ? 38.320 18.781 36.049  1.00 104.20 ? 308 PHE D C   1 
ATOM   10171 O  O   . PHE D 1 244 ? 38.693 19.937 35.772  1.00 94.47  ? 308 PHE D O   1 
ATOM   10172 C  CB  . PHE D 1 244 ? 40.550 17.875 36.756  1.00 95.58  ? 308 PHE D CB  1 
ATOM   10173 C  CG  . PHE D 1 244 ? 40.483 17.561 38.214  1.00 97.64  ? 308 PHE D CG  1 
ATOM   10174 C  CD1 . PHE D 1 244 ? 40.499 16.240 38.661  1.00 93.29  ? 308 PHE D CD1 1 
ATOM   10175 C  CD2 . PHE D 1 244 ? 40.460 18.585 39.157  1.00 95.47  ? 308 PHE D CD2 1 
ATOM   10176 C  CE1 . PHE D 1 244 ? 40.469 15.940 40.038  1.00 81.14  ? 308 PHE D CE1 1 
ATOM   10177 C  CE2 . PHE D 1 244 ? 40.432 18.295 40.530  1.00 79.09  ? 308 PHE D CE2 1 
ATOM   10178 C  CZ  . PHE D 1 244 ? 40.436 16.960 40.968  1.00 68.69  ? 308 PHE D CZ  1 
ATOM   10179 N  N   . LEU D 1 245 ? 37.077 18.490 36.394  1.00 84.51  ? 309 LEU D N   1 
ATOM   10180 C  CA  . LEU D 1 245 ? 36.034 19.470 36.338  1.00 78.74  ? 309 LEU D CA  1 
ATOM   10181 C  C   . LEU D 1 245 ? 35.984 20.221 37.637  1.00 76.15  ? 309 LEU D C   1 
ATOM   10182 O  O   . LEU D 1 245 ? 35.726 19.616 38.677  1.00 91.35  ? 309 LEU D O   1 
ATOM   10183 C  CB  . LEU D 1 245 ? 34.710 18.769 36.106  1.00 87.98  ? 309 LEU D CB  1 
ATOM   10184 C  CG  . LEU D 1 245 ? 34.563 18.009 34.795  1.00 77.39  ? 309 LEU D CG  1 
ATOM   10185 C  CD1 . LEU D 1 245 ? 33.065 17.887 34.461  1.00 82.17  ? 309 LEU D CD1 1 
ATOM   10186 C  CD2 . LEU D 1 245 ? 35.297 18.753 33.702  1.00 75.62  ? 309 LEU D CD2 1 
ATOM   10187 N  N   . GLY D 1 246 ? 36.237 21.529 37.580  1.00 69.30  ? 310 GLY D N   1 
ATOM   10188 C  CA  . GLY D 1 246 ? 36.300 22.359 38.791  1.00 71.47  ? 310 GLY D CA  1 
ATOM   10189 C  C   . GLY D 1 246 ? 34.962 22.666 39.455  1.00 66.93  ? 310 GLY D C   1 
ATOM   10190 O  O   . GLY D 1 246 ? 34.856 22.685 40.693  1.00 84.30  ? 310 GLY D O   1 
ATOM   10191 N  N   . ASP D 1 247 ? 33.947 22.889 38.624  1.00 63.52  ? 311 ASP D N   1 
ATOM   10192 C  CA  . ASP D 1 247 ? 32.684 23.486 39.045  1.00 72.33  ? 311 ASP D CA  1 
ATOM   10193 C  C   . ASP D 1 247 ? 31.836 22.508 39.835  1.00 74.41  ? 311 ASP D C   1 
ATOM   10194 O  O   . ASP D 1 247 ? 32.222 21.350 39.995  1.00 81.79  ? 311 ASP D O   1 
ATOM   10195 C  CB  . ASP D 1 247 ? 31.908 24.003 37.829  1.00 76.63  ? 311 ASP D CB  1 
ATOM   10196 C  CG  . ASP D 1 247 ? 31.123 25.278 38.128  1.00 84.90  ? 311 ASP D CG  1 
ATOM   10197 O  OD1 . ASP D 1 247 ? 30.752 25.492 39.319  1.00 67.25  ? 311 ASP D OD1 1 
ATOM   10198 O  OD2 . ASP D 1 247 ? 30.883 26.056 37.159  1.00 92.69  ? 311 ASP D OD2 1 
ATOM   10199 N  N   . THR D 1 248 ? 30.703 22.993 40.351  1.00 67.86  ? 312 THR D N   1 
ATOM   10200 C  CA  . THR D 1 248 ? 29.743 22.154 41.053  1.00 73.83  ? 312 THR D CA  1 
ATOM   10201 C  C   . THR D 1 248 ? 28.328 22.728 40.941  1.00 79.49  ? 312 THR D C   1 
ATOM   10202 O  O   . THR D 1 248 ? 28.134 23.884 41.263  1.00 91.38  ? 312 THR D O   1 
ATOM   10203 C  CB  . THR D 1 248 ? 30.131 22.009 42.520  1.00 87.26  ? 312 THR D CB  1 
ATOM   10204 O  OG1 . THR D 1 248 ? 31.406 21.349 42.613  1.00 103.66 ? 312 THR D OG1 1 
ATOM   10205 C  CG2 . THR D 1 248 ? 29.069 21.214 43.296  1.00 90.13  ? 312 THR D CG2 1 
ATOM   10206 N  N   . PRO D 1 249 ? 27.338 21.911 40.511  1.00 83.17  ? 313 PRO D N   1 
ATOM   10207 C  CA  . PRO D 1 249 ? 27.520 20.492 40.250  1.00 87.78  ? 313 PRO D CA  1 
ATOM   10208 C  C   . PRO D 1 249 ? 28.162 20.277 38.897  1.00 88.35  ? 313 PRO D C   1 
ATOM   10209 O  O   . PRO D 1 249 ? 28.369 21.241 38.141  1.00 86.35  ? 313 PRO D O   1 
ATOM   10210 C  CB  . PRO D 1 249 ? 26.095 19.945 40.263  1.00 86.78  ? 313 PRO D CB  1 
ATOM   10211 C  CG  . PRO D 1 249 ? 25.295 21.061 39.725  1.00 90.14  ? 313 PRO D CG  1 
ATOM   10212 C  CD  . PRO D 1 249 ? 25.977 22.346 40.156  1.00 82.06  ? 313 PRO D CD  1 
ATOM   10213 N  N   . ARG D 1 250 ? 28.466 19.011 38.623  1.00 89.00  ? 314 ARG D N   1 
ATOM   10214 C  CA  . ARG D 1 250 ? 29.177 18.581 37.434  1.00 83.65  ? 314 ARG D CA  1 
ATOM   10215 C  C   . ARG D 1 250 ? 28.868 17.092 37.214  1.00 94.63  ? 314 ARG D C   1 
ATOM   10216 O  O   . ARG D 1 250 ? 28.382 16.407 38.119  1.00 96.46  ? 314 ARG D O   1 
ATOM   10217 C  CB  . ARG D 1 250 ? 30.678 18.831 37.606  1.00 68.64  ? 314 ARG D CB  1 
ATOM   10218 C  CG  . ARG D 1 250 ? 31.241 18.260 38.889  1.00 61.76  ? 314 ARG D CG  1 
ATOM   10219 C  CD  . ARG D 1 250 ? 32.753 18.270 38.899  1.00 61.27  ? 314 ARG D CD  1 
ATOM   10220 N  NE  . ARG D 1 250 ? 33.288 18.314 40.263  1.00 62.11  ? 314 ARG D NE  1 
ATOM   10221 C  CZ  . ARG D 1 250 ? 33.512 17.242 41.010  1.00 70.29  ? 314 ARG D CZ  1 
ATOM   10222 N  NH1 . ARG D 1 250 ? 33.274 16.022 40.529  1.00 107.84 ? 314 ARG D NH1 1 
ATOM   10223 N  NH2 . ARG D 1 250 ? 33.988 17.384 42.230  1.00 62.49  ? 314 ARG D NH2 1 
ATOM   10224 N  N   . GLY D 1 251 ? 29.141 16.595 36.017  1.00 98.30  ? 315 GLY D N   1 
ATOM   10225 C  CA  . GLY D 1 251 ? 28.696 15.261 35.673  1.00 122.57 ? 315 GLY D CA  1 
ATOM   10226 C  C   . GLY D 1 251 ? 29.665 14.200 36.120  1.00 130.78 ? 315 GLY D C   1 
ATOM   10227 O  O   . GLY D 1 251 ? 29.370 13.396 37.006  1.00 148.91 ? 315 GLY D O   1 
ATOM   10228 N  N   . ILE D 1 252 ? 30.838 14.227 35.501  1.00 131.19 ? 316 ILE D N   1 
ATOM   10229 C  CA  . ILE D 1 252 ? 31.767 13.109 35.504  1.00 126.42 ? 316 ILE D CA  1 
ATOM   10230 C  C   . ILE D 1 252 ? 33.051 13.591 34.863  1.00 128.51 ? 316 ILE D C   1 
ATOM   10231 O  O   . ILE D 1 252 ? 33.027 14.522 34.050  1.00 164.57 ? 316 ILE D O   1 
ATOM   10232 C  CB  . ILE D 1 252 ? 31.213 11.925 34.662  1.00 140.23 ? 316 ILE D CB  1 
ATOM   10233 C  CG1 . ILE D 1 252 ? 31.776 10.587 35.153  1.00 130.08 ? 316 ILE D CG1 1 
ATOM   10234 C  CG2 . ILE D 1 252 ? 31.442 12.139 33.148  1.00 132.04 ? 316 ILE D CG2 1 
ATOM   10235 C  CD1 . ILE D 1 252 ? 31.103 10.050 36.405  1.00 123.83 ? 316 ILE D CD1 1 
ATOM   10236 N  N   . ASP D 1 253 ? 34.169 12.961 35.206  1.00 95.24  ? 317 ASP D N   1 
ATOM   10237 C  CA  . ASP D 1 253 ? 35.436 13.401 34.664  1.00 89.17  ? 317 ASP D CA  1 
ATOM   10238 C  C   . ASP D 1 253 ? 35.572 12.917 33.247  1.00 95.64  ? 317 ASP D C   1 
ATOM   10239 O  O   . ASP D 1 253 ? 35.075 11.853 32.901  1.00 109.66 ? 317 ASP D O   1 
ATOM   10240 C  CB  . ASP D 1 253 ? 36.595 12.964 35.546  1.00 115.10 ? 317 ASP D CB  1 
ATOM   10241 C  CG  . ASP D 1 253 ? 36.661 13.753 36.858  1.00 119.70 ? 317 ASP D CG  1 
ATOM   10242 O  OD1 . ASP D 1 253 ? 36.263 14.945 36.870  1.00 98.39  ? 317 ASP D OD1 1 
ATOM   10243 O  OD2 . ASP D 1 253 ? 37.112 13.175 37.876  1.00 126.13 ? 317 ASP D OD2 1 
ATOM   10244 N  N   . THR D 1 254 ? 36.214 13.726 32.417  1.00 112.00 ? 318 THR D N   1 
ATOM   10245 C  CA  . THR D 1 254 ? 36.248 13.483 30.976  1.00 131.07 ? 318 THR D CA  1 
ATOM   10246 C  C   . THR D 1 254 ? 37.678 13.244 30.502  1.00 126.19 ? 318 THR D C   1 
ATOM   10247 O  O   . THR D 1 254 ? 38.606 13.196 31.306  1.00 135.04 ? 318 THR D O   1 
ATOM   10248 C  CB  . THR D 1 254 ? 35.655 14.690 30.179  1.00 133.06 ? 318 THR D CB  1 
ATOM   10249 O  OG1 . THR D 1 254 ? 36.390 15.880 30.496  1.00 165.43 ? 318 THR D OG1 1 
ATOM   10250 C  CG2 . THR D 1 254 ? 34.175 14.904 30.496  1.00 113.82 ? 318 THR D CG2 1 
ATOM   10251 N  N   . THR D 1 255 ? 37.843 13.080 29.193  1.00 131.71 ? 319 THR D N   1 
ATOM   10252 C  CA  . THR D 1 255 ? 39.155 13.166 28.560  1.00 126.30 ? 319 THR D CA  1 
ATOM   10253 C  C   . THR D 1 255 ? 39.504 14.654 28.449  1.00 114.80 ? 319 THR D C   1 
ATOM   10254 O  O   . THR D 1 255 ? 38.635 15.516 28.638  1.00 107.90 ? 319 THR D O   1 
ATOM   10255 C  CB  . THR D 1 255 ? 39.146 12.517 27.164  1.00 124.64 ? 319 THR D CB  1 
ATOM   10256 O  OG1 . THR D 1 255 ? 38.143 13.147 26.354  1.00 126.52 ? 319 THR D OG1 1 
ATOM   10257 C  CG2 . THR D 1 255 ? 38.845 11.020 27.266  1.00 124.55 ? 319 THR D CG2 1 
ATOM   10258 N  N   . ASN D 1 256 ? 40.762 14.965 28.152  1.00 112.69 ? 320 ASN D N   1 
ATOM   10259 C  CA  . ASN D 1 256 ? 41.182 16.366 28.024  1.00 109.92 ? 320 ASN D CA  1 
ATOM   10260 C  C   . ASN D 1 256 ? 40.821 16.944 26.661  1.00 112.10 ? 320 ASN D C   1 
ATOM   10261 O  O   . ASN D 1 256 ? 41.035 16.306 25.647  1.00 125.75 ? 320 ASN D O   1 
ATOM   10262 C  CB  . ASN D 1 256 ? 42.695 16.533 28.245  1.00 100.18 ? 320 ASN D CB  1 
ATOM   10263 C  CG  . ASN D 1 256 ? 43.171 15.990 29.580  1.00 93.43  ? 320 ASN D CG  1 
ATOM   10264 O  OD1 . ASN D 1 256 ? 42.419 15.365 30.322  1.00 94.80  ? 320 ASN D OD1 1 
ATOM   10265 N  ND2 . ASN D 1 256 ? 44.437 16.220 29.884  1.00 94.21  ? 320 ASN D ND2 1 
ATOM   10266 N  N   . TYR D 1 257 ? 40.280 18.154 26.642  1.00 117.05 ? 321 TYR D N   1 
ATOM   10267 C  CA  . TYR D 1 257 ? 40.055 18.871 25.395  1.00 105.82 ? 321 TYR D CA  1 
ATOM   10268 C  C   . TYR D 1 257 ? 39.829 20.346 25.661  1.00 117.67 ? 321 TYR D C   1 
ATOM   10269 O  O   . TYR D 1 257 ? 39.330 20.725 26.725  1.00 123.68 ? 321 TYR D O   1 
ATOM   10270 C  CB  . TYR D 1 257 ? 38.867 18.296 24.646  1.00 116.41 ? 321 TYR D CB  1 
ATOM   10271 C  CG  . TYR D 1 257 ? 37.596 18.154 25.458  1.00 126.52 ? 321 TYR D CG  1 
ATOM   10272 C  CD1 . TYR D 1 257 ? 36.663 19.197 25.532  1.00 123.34 ? 321 TYR D CD1 1 
ATOM   10273 C  CD2 . TYR D 1 257 ? 37.305 16.958 26.117  1.00 120.44 ? 321 TYR D CD2 1 
ATOM   10274 C  CE1 . TYR D 1 257 ? 35.479 19.052 26.260  1.00 131.66 ? 321 TYR D CE1 1 
ATOM   10275 C  CE2 . TYR D 1 257 ? 36.130 16.804 26.848  1.00 123.56 ? 321 TYR D CE2 1 
ATOM   10276 C  CZ  . TYR D 1 257 ? 35.221 17.852 26.914  1.00 127.57 ? 321 TYR D CZ  1 
ATOM   10277 O  OH  . TYR D 1 257 ? 34.059 17.692 27.636  1.00 109.04 ? 321 TYR D OH  1 
ATOM   10278 N  N   . CYS D 1 258 ? 40.182 21.171 24.682  1.00 120.50 ? 322 CYS D N   1 
ATOM   10279 C  CA  . CYS D 1 258 ? 40.220 22.616 24.885  1.00 128.10 ? 322 CYS D CA  1 
ATOM   10280 C  C   . CYS D 1 258 ? 38.888 23.302 24.645  1.00 124.90 ? 322 CYS D C   1 
ATOM   10281 O  O   . CYS D 1 258 ? 38.795 24.528 24.669  1.00 119.52 ? 322 CYS D O   1 
ATOM   10282 C  CB  . CYS D 1 258 ? 41.353 23.242 24.076  1.00 140.02 ? 322 CYS D CB  1 
ATOM   10283 S  SG  . CYS D 1 258 ? 42.968 22.697 24.699  1.00 220.88 ? 322 CYS D SG  1 
ATOM   10284 N  N   . ASP D 1 259 ? 37.856 22.492 24.447  1.00 136.91 ? 323 ASP D N   1 
ATOM   10285 C  CA  . ASP D 1 259 ? 36.489 22.984 24.406  1.00 150.33 ? 323 ASP D CA  1 
ATOM   10286 C  C   . ASP D 1 259 ? 35.893 23.115 25.835  1.00 138.05 ? 323 ASP D C   1 
ATOM   10287 O  O   . ASP D 1 259 ? 36.575 22.878 26.846  1.00 125.58 ? 323 ASP D O   1 
ATOM   10288 C  CB  . ASP D 1 259 ? 35.645 22.070 23.508  1.00 155.42 ? 323 ASP D CB  1 
ATOM   10289 C  CG  . ASP D 1 259 ? 34.466 22.788 22.874  1.00 197.70 ? 323 ASP D CG  1 
ATOM   10290 O  OD1 . ASP D 1 259 ? 34.581 23.991 22.548  1.00 207.28 ? 323 ASP D OD1 1 
ATOM   10291 O  OD2 . ASP D 1 259 ? 33.418 22.137 22.695  1.00 250.60 ? 323 ASP D OD2 1 
ATOM   10292 N  N   . LYS D 1 260 ? 34.623 23.502 25.900  1.00 109.84 ? 324 LYS D N   1 
ATOM   10293 C  CA  . LYS D 1 260 ? 33.910 23.702 27.147  1.00 105.28 ? 324 LYS D CA  1 
ATOM   10294 C  C   . LYS D 1 260 ? 32.901 22.567 27.401  1.00 98.37  ? 324 LYS D C   1 
ATOM   10295 O  O   . LYS D 1 260 ? 32.176 22.172 26.511  1.00 95.05  ? 324 LYS D O   1 
ATOM   10296 C  CB  . LYS D 1 260 ? 33.246 25.078 27.105  1.00 98.84  ? 324 LYS D CB  1 
ATOM   10297 C  CG  . LYS D 1 260 ? 31.882 25.185 27.747  1.00 112.73 ? 324 LYS D CG  1 
ATOM   10298 C  CD  . LYS D 1 260 ? 31.046 26.291 27.091  1.00 114.94 ? 324 LYS D CD  1 
ATOM   10299 C  CE  . LYS D 1 260 ? 31.886 27.509 26.718  1.00 104.26 ? 324 LYS D CE  1 
ATOM   10300 N  NZ  . LYS D 1 260 ? 31.092 28.471 25.924  1.00 94.27  ? 324 LYS D NZ  1 
ATOM   10301 N  N   . THR D 1 261 ? 32.871 22.052 28.626  1.00 104.72 ? 325 THR D N   1 
ATOM   10302 C  CA  . THR D 1 261 ? 32.049 20.896 28.991  1.00 88.85  ? 325 THR D CA  1 
ATOM   10303 C  C   . THR D 1 261 ? 30.627 21.281 29.335  1.00 85.14  ? 325 THR D C   1 
ATOM   10304 O  O   . THR D 1 261 ? 30.340 21.699 30.439  1.00 95.60  ? 325 THR D O   1 
ATOM   10305 C  CB  . THR D 1 261 ? 32.649 20.173 30.200  1.00 83.81  ? 325 THR D CB  1 
ATOM   10306 O  OG1 . THR D 1 261 ? 33.967 19.722 29.865  1.00 84.74  ? 325 THR D OG1 1 
ATOM   10307 C  CG2 . THR D 1 261 ? 31.779 18.980 30.603  1.00 89.72  ? 325 THR D CG2 1 
ATOM   10308 N  N   . THR D 1 262 ? 29.718 21.099 28.401  1.00 97.89  ? 326 THR D N   1 
ATOM   10309 C  CA  . THR D 1 262 ? 28.372 21.640 28.566  1.00 98.82  ? 326 THR D CA  1 
ATOM   10310 C  C   . THR D 1 262 ? 27.439 20.757 29.390  1.00 100.27 ? 326 THR D C   1 
ATOM   10311 O  O   . THR D 1 262 ? 26.314 21.153 29.680  1.00 102.80 ? 326 THR D O   1 
ATOM   10312 C  CB  . THR D 1 262 ? 27.713 21.863 27.216  1.00 101.25 ? 326 THR D CB  1 
ATOM   10313 O  OG1 . THR D 1 262 ? 27.225 20.604 26.731  1.00 133.44 ? 326 THR D OG1 1 
ATOM   10314 C  CG2 . THR D 1 262 ? 28.719 22.437 26.219  1.00 101.65 ? 326 THR D CG2 1 
ATOM   10315 N  N   . THR D 1 263 ? 27.896 19.561 29.745  1.00 113.20 ? 327 THR D N   1 
ATOM   10316 C  CA  . THR D 1 263 ? 27.046 18.594 30.431  1.00 113.92 ? 327 THR D CA  1 
ATOM   10317 C  C   . THR D 1 263 ? 27.050 18.925 31.907  1.00 98.15  ? 327 THR D C   1 
ATOM   10318 O  O   . THR D 1 263 ? 28.121 19.013 32.522  1.00 90.82  ? 327 THR D O   1 
ATOM   10319 C  CB  . THR D 1 263 ? 27.523 17.133 30.213  1.00 124.42 ? 327 THR D CB  1 
ATOM   10320 O  OG1 . THR D 1 263 ? 27.974 16.960 28.860  1.00 103.70 ? 327 THR D OG1 1 
ATOM   10321 C  CG2 . THR D 1 263 ? 26.393 16.147 30.503  1.00 111.93 ? 327 THR D CG2 1 
ATOM   10322 N  N   . GLU D 1 264 ? 25.845 19.090 32.458  1.00 98.52  ? 328 GLU D N   1 
ATOM   10323 C  CA  . GLU D 1 264 ? 25.628 19.602 33.822  1.00 107.10 ? 328 GLU D CA  1 
ATOM   10324 C  C   . GLU D 1 264 ? 26.305 20.968 34.041  1.00 106.01 ? 328 GLU D C   1 
ATOM   10325 O  O   . GLU D 1 264 ? 26.660 21.340 35.165  1.00 127.84 ? 328 GLU D O   1 
ATOM   10326 C  CB  . GLU D 1 264 ? 26.057 18.577 34.890  1.00 108.01 ? 328 GLU D CB  1 
ATOM   10327 C  CG  . GLU D 1 264 ? 25.066 17.444 35.140  1.00 124.11 ? 328 GLU D CG  1 
ATOM   10328 C  CD  . GLU D 1 264 ? 24.902 17.138 36.627  1.00 127.48 ? 328 GLU D CD  1 
ATOM   10329 O  OE1 . GLU D 1 264 ? 24.375 17.998 37.364  1.00 120.55 ? 328 GLU D OE1 1 
ATOM   10330 O  OE2 . GLU D 1 264 ? 25.294 16.037 37.064  1.00 145.31 ? 328 GLU D OE2 1 
ATOM   10331 N  N   . GLY D 1 265 ? 26.466 21.715 32.952  1.00 96.45  ? 329 GLY D N   1 
ATOM   10332 C  CA  . GLY D 1 265 ? 27.155 22.991 32.983  1.00 85.74  ? 329 GLY D CA  1 
ATOM   10333 C  C   . GLY D 1 265 ? 26.407 24.051 33.761  1.00 85.90  ? 329 GLY D C   1 
ATOM   10334 O  O   . GLY D 1 265 ? 27.006 25.036 34.202  1.00 99.26  ? 329 GLY D O   1 
ATOM   10335 N  N   . GLU D 1 266 ? 25.103 23.847 33.943  1.00 77.16  ? 330 GLU D N   1 
ATOM   10336 C  CA  . GLU D 1 266 ? 24.276 24.828 34.613  1.00 78.87  ? 330 GLU D CA  1 
ATOM   10337 C  C   . GLU D 1 266 ? 24.268 24.678 36.123  1.00 95.91  ? 330 GLU D C   1 
ATOM   10338 O  O   . GLU D 1 266 ? 24.302 23.567 36.654  1.00 119.11 ? 330 GLU D O   1 
ATOM   10339 C  CB  . GLU D 1 266 ? 22.865 24.786 34.085  1.00 81.43  ? 330 GLU D CB  1 
ATOM   10340 C  CG  . GLU D 1 266 ? 22.028 25.922 34.595  1.00 90.87  ? 330 GLU D CG  1 
ATOM   10341 C  CD  . GLU D 1 266 ? 20.736 26.096 33.841  1.00 133.84 ? 330 GLU D CD  1 
ATOM   10342 O  OE1 . GLU D 1 266 ? 20.482 25.308 32.906  1.00 164.11 ? 330 GLU D OE1 1 
ATOM   10343 O  OE2 . GLU D 1 266 ? 19.977 27.026 34.189  1.00 163.30 ? 330 GLU D OE2 1 
ATOM   10344 N  N   . GLY D 1 267 ? 24.181 25.820 36.802  1.00 111.82 ? 331 GLY D N   1 
ATOM   10345 C  CA  . GLY D 1 267 ? 24.450 25.914 38.227  1.00 106.59 ? 331 GLY D CA  1 
ATOM   10346 C  C   . GLY D 1 267 ? 25.947 26.127 38.410  1.00 111.07 ? 331 GLY D C   1 
ATOM   10347 O  O   . GLY D 1 267 ? 26.744 26.021 37.459  1.00 99.84  ? 331 GLY D O   1 
ATOM   10348 N  N   . GLY D 1 268 ? 26.341 26.432 39.635  1.00 96.41  ? 332 GLY D N   1 
ATOM   10349 C  CA  . GLY D 1 268 ? 27.742 26.653 39.915  1.00 93.65  ? 332 GLY D CA  1 
ATOM   10350 C  C   . GLY D 1 268 ? 27.954 27.273 41.273  1.00 79.71  ? 332 GLY D C   1 
ATOM   10351 O  O   . GLY D 1 268 ? 27.019 27.802 41.884  1.00 81.85  ? 332 GLY D O   1 
ATOM   10352 N  N   . ILE D 1 269 ? 29.192 27.188 41.743  1.00 58.10  ? 333 ILE D N   1 
ATOM   10353 C  CA  . ILE D 1 269 ? 29.590 27.855 42.958  1.00 61.52  ? 333 ILE D CA  1 
ATOM   10354 C  C   . ILE D 1 269 ? 31.035 28.378 42.819  1.00 61.35  ? 333 ILE D C   1 
ATOM   10355 O  O   . ILE D 1 269 ? 31.836 27.791 42.096  1.00 59.09  ? 333 ILE D O   1 
ATOM   10356 C  CB  . ILE D 1 269 ? 29.418 26.928 44.157  1.00 63.50  ? 333 ILE D CB  1 
ATOM   10357 C  CG1 . ILE D 1 269 ? 29.393 27.737 45.454  1.00 84.55  ? 333 ILE D CG1 1 
ATOM   10358 C  CG2 . ILE D 1 269 ? 30.499 25.868 44.174  1.00 61.66  ? 333 ILE D CG2 1 
ATOM   10359 C  CD1 . ILE D 1 269 ? 28.915 26.947 46.665  1.00 90.73  ? 333 ILE D CD1 1 
ATOM   10360 N  N   . GLN D 1 270 ? 31.339 29.494 43.487  1.00 59.13  ? 334 GLN D N   1 
ATOM   10361 C  CA  . GLN D 1 270 ? 32.627 30.160 43.372  1.00 53.80  ? 334 GLN D CA  1 
ATOM   10362 C  C   . GLN D 1 270 ? 33.765 29.215 43.711  1.00 57.01  ? 334 GLN D C   1 
ATOM   10363 O  O   . GLN D 1 270 ? 33.738 28.516 44.741  1.00 64.48  ? 334 GLN D O   1 
ATOM   10364 C  CB  . GLN D 1 270 ? 32.663 31.356 44.314  1.00 54.29  ? 334 GLN D CB  1 
ATOM   10365 C  CG  . GLN D 1 270 ? 33.935 32.226 44.223  1.00 56.69  ? 334 GLN D CG  1 
ATOM   10366 C  CD  . GLN D 1 270 ? 33.828 33.466 45.121  1.00 59.88  ? 334 GLN D CD  1 
ATOM   10367 O  OE1 . GLN D 1 270 ? 32.990 33.512 46.020  1.00 76.43  ? 334 GLN D OE1 1 
ATOM   10368 N  NE2 . GLN D 1 270 ? 34.653 34.475 44.866  1.00 55.97  ? 334 GLN D NE2 1 
ATOM   10369 N  N   . GLY D 1 271 ? 34.773 29.190 42.846  1.00 54.23  ? 335 GLY D N   1 
ATOM   10370 C  CA  . GLY D 1 271 ? 35.963 28.376 43.108  1.00 55.26  ? 335 GLY D CA  1 
ATOM   10371 C  C   . GLY D 1 271 ? 37.174 28.878 42.362  1.00 55.04  ? 335 GLY D C   1 
ATOM   10372 O  O   . GLY D 1 271 ? 37.058 29.797 41.546  1.00 68.22  ? 335 GLY D O   1 
ATOM   10373 N  N   . PHE D 1 272 ? 38.331 28.270 42.620  1.00 51.81  ? 336 PHE D N   1 
ATOM   10374 C  CA  . PHE D 1 272 ? 39.561 28.713 41.955  1.00 62.42  ? 336 PHE D CA  1 
ATOM   10375 C  C   . PHE D 1 272 ? 40.354 27.630 41.171  1.00 69.14  ? 336 PHE D C   1 
ATOM   10376 O  O   . PHE D 1 272 ? 40.041 26.413 41.195  1.00 66.14  ? 336 PHE D O   1 
ATOM   10377 C  CB  . PHE D 1 272 ? 40.474 29.374 42.978  1.00 56.04  ? 336 PHE D CB  1 
ATOM   10378 C  CG  . PHE D 1 272 ? 40.855 28.457 44.065  1.00 67.53  ? 336 PHE D CG  1 
ATOM   10379 C  CD1 . PHE D 1 272 ? 42.088 27.801 44.028  1.00 68.53  ? 336 PHE D CD1 1 
ATOM   10380 C  CD2 . PHE D 1 272 ? 39.951 28.166 45.097  1.00 69.44  ? 336 PHE D CD2 1 
ATOM   10381 C  CE1 . PHE D 1 272 ? 42.452 26.906 45.019  1.00 54.19  ? 336 PHE D CE1 1 
ATOM   10382 C  CE2 . PHE D 1 272 ? 40.292 27.267 46.091  1.00 60.08  ? 336 PHE D CE2 1 
ATOM   10383 C  CZ  . PHE D 1 272 ? 41.560 26.639 46.052  1.00 54.30  ? 336 PHE D CZ  1 
ATOM   10384 N  N   . MET D 1 273 ? 41.356 28.139 40.447  1.00 65.43  ? 337 MET D N   1 
ATOM   10385 C  CA  . MET D 1 273 ? 42.408 27.374 39.791  1.00 70.73  ? 337 MET D CA  1 
ATOM   10386 C  C   . MET D 1 273 ? 43.647 28.242 39.839  1.00 68.79  ? 337 MET D C   1 
ATOM   10387 O  O   . MET D 1 273 ? 43.572 29.473 39.821  1.00 82.66  ? 337 MET D O   1 
ATOM   10388 C  CB  . MET D 1 273 ? 42.098 27.065 38.319  1.00 75.41  ? 337 MET D CB  1 
ATOM   10389 C  CG  . MET D 1 273 ? 40.918 26.129 38.072  1.00 82.74  ? 337 MET D CG  1 
ATOM   10390 S  SD  . MET D 1 273 ? 40.555 25.772 36.327  1.00 87.27  ? 337 MET D SD  1 
ATOM   10391 C  CE  . MET D 1 273 ? 40.484 27.426 35.601  1.00 97.18  ? 337 MET D CE  1 
ATOM   10392 N  N   . ILE D 1 274 ? 44.794 27.595 39.881  1.00 65.08  ? 338 ILE D N   1 
ATOM   10393 C  CA  . ILE D 1 274 ? 46.034 28.306 39.987  1.00 64.91  ? 338 ILE D CA  1 
ATOM   10394 C  C   . ILE D 1 274 ? 46.888 27.889 38.817  1.00 64.87  ? 338 ILE D C   1 
ATOM   10395 O  O   . ILE D 1 274 ? 47.064 26.706 38.580  1.00 60.85  ? 338 ILE D O   1 
ATOM   10396 C  CB  . ILE D 1 274 ? 46.751 27.988 41.313  1.00 59.83  ? 338 ILE D CB  1 
ATOM   10397 C  CG1 . ILE D 1 274 ? 45.776 28.118 42.488  1.00 48.59  ? 338 ILE D CG1 1 
ATOM   10398 C  CG2 . ILE D 1 274 ? 47.913 28.927 41.503  1.00 57.77  ? 338 ILE D CG2 1 
ATOM   10399 C  CD1 . ILE D 1 274 ? 46.415 28.030 43.815  1.00 47.04  ? 338 ILE D CD1 1 
ATOM   10400 N  N   . GLU D 1 275 ? 47.384 28.876 38.079  1.00 74.08  ? 339 GLU D N   1 
ATOM   10401 C  CA  . GLU D 1 275 ? 48.284 28.650 36.963  1.00 79.19  ? 339 GLU D CA  1 
ATOM   10402 C  C   . GLU D 1 275 ? 49.710 29.028 37.371  1.00 88.46  ? 339 GLU D C   1 
ATOM   10403 O  O   . GLU D 1 275 ? 49.949 30.123 37.897  1.00 87.08  ? 339 GLU D O   1 
ATOM   10404 C  CB  . GLU D 1 275 ? 47.806 29.451 35.752  1.00 79.44  ? 339 GLU D CB  1 
ATOM   10405 C  CG  . GLU D 1 275 ? 48.822 29.608 34.619  1.00 114.15 ? 339 GLU D CG  1 
ATOM   10406 C  CD  . GLU D 1 275 ? 49.035 28.349 33.772  1.00 143.42 ? 339 GLU D CD  1 
ATOM   10407 O  OE1 . GLU D 1 275 ? 48.243 27.392 33.874  1.00 166.93 ? 339 GLU D OE1 1 
ATOM   10408 O  OE2 . GLU D 1 275 ? 50.003 28.324 32.982  1.00 150.87 ? 339 GLU D OE2 1 
ATOM   10409 N  N   . GLY D 1 276 ? 50.651 28.112 37.149  1.00 86.09  ? 340 GLY D N   1 
ATOM   10410 C  CA  . GLY D 1 276 ? 52.045 28.369 37.491  1.00 89.87  ? 340 GLY D CA  1 
ATOM   10411 C  C   . GLY D 1 276 ? 52.979 27.355 36.876  1.00 101.90 ? 340 GLY D C   1 
ATOM   10412 O  O   . GLY D 1 276 ? 52.625 26.693 35.890  1.00 97.44  ? 340 GLY D O   1 
ATOM   10413 N  N   . SER D 1 277 ? 54.182 27.260 37.447  1.00 113.83 ? 341 SER D N   1 
ATOM   10414 C  CA  . SER D 1 277 ? 55.110 26.149 37.182  1.00 117.11 ? 341 SER D CA  1 
ATOM   10415 C  C   . SER D 1 277 ? 54.381 24.839 37.470  1.00 114.46 ? 341 SER D C   1 
ATOM   10416 O  O   . SER D 1 277 ? 54.159 24.018 36.577  1.00 120.36 ? 341 SER D O   1 
ATOM   10417 C  CB  . SER D 1 277 ? 56.356 26.251 38.072  1.00 108.78 ? 341 SER D CB  1 
ATOM   10418 O  OG  . SER D 1 277 ? 57.182 27.330 37.682  1.00 148.90 ? 341 SER D OG  1 
ATOM   10419 N  N   . ASN D 1 278 ? 54.033 24.656 38.740  1.00 110.05 ? 342 ASN D N   1 
ATOM   10420 C  CA  . ASN D 1 278 ? 52.986 23.737 39.139  1.00 92.71  ? 342 ASN D CA  1 
ATOM   10421 C  C   . ASN D 1 278 ? 51.662 24.463 38.957  1.00 84.64  ? 342 ASN D C   1 
ATOM   10422 O  O   . ASN D 1 278 ? 51.576 25.682 39.154  1.00 75.45  ? 342 ASN D O   1 
ATOM   10423 C  CB  . ASN D 1 278 ? 53.143 23.343 40.613  1.00 95.28  ? 342 ASN D CB  1 
ATOM   10424 C  CG  . ASN D 1 278 ? 54.327 22.429 40.858  1.00 98.71  ? 342 ASN D CG  1 
ATOM   10425 O  OD1 . ASN D 1 278 ? 54.519 21.425 40.170  1.00 98.95  ? 342 ASN D OD1 1 
ATOM   10426 N  ND2 . ASN D 1 278 ? 55.128 22.774 41.852  1.00 113.68 ? 342 ASN D ND2 1 
ATOM   10427 N  N   . SER D 1 279 ? 50.630 23.718 38.582  1.00 81.87  ? 343 SER D N   1 
ATOM   10428 C  CA  . SER D 1 279 ? 49.271 24.259 38.548  1.00 77.01  ? 343 SER D CA  1 
ATOM   10429 C  C   . SER D 1 279 ? 48.289 23.467 39.424  1.00 79.06  ? 343 SER D C   1 
ATOM   10430 O  O   . SER D 1 279 ? 48.459 22.259 39.635  1.00 79.66  ? 343 SER D O   1 
ATOM   10431 C  CB  . SER D 1 279 ? 48.782 24.366 37.115  1.00 75.94  ? 343 SER D CB  1 
ATOM   10432 O  OG  . SER D 1 279 ? 49.560 25.326 36.408  1.00 90.45  ? 343 SER D OG  1 
ATOM   10433 N  N   . TRP D 1 280 ? 47.276 24.163 39.952  1.00 84.08  ? 344 TRP D N   1 
ATOM   10434 C  CA  . TRP D 1 280 ? 46.329 23.561 40.912  1.00 61.55  ? 344 TRP D CA  1 
ATOM   10435 C  C   . TRP D 1 280 ? 44.918 23.731 40.534  1.00 53.03  ? 344 TRP D C   1 
ATOM   10436 O  O   . TRP D 1 280 ? 44.526 24.775 40.033  1.00 54.14  ? 344 TRP D O   1 
ATOM   10437 C  CB  . TRP D 1 280 ? 46.517 24.151 42.290  1.00 58.01  ? 344 TRP D CB  1 
ATOM   10438 C  CG  . TRP D 1 280 ? 47.904 23.904 42.816  1.00 67.36  ? 344 TRP D CG  1 
ATOM   10439 C  CD1 . TRP D 1 280 ? 49.049 24.667 42.581  1.00 60.58  ? 344 TRP D CD1 1 
ATOM   10440 C  CD2 . TRP D 1 280 ? 48.356 22.781 43.666  1.00 61.78  ? 344 TRP D CD2 1 
ATOM   10441 N  NE1 . TRP D 1 280 ? 50.140 24.117 43.217  1.00 63.49  ? 344 TRP D NE1 1 
ATOM   10442 C  CE2 . TRP D 1 280 ? 49.796 22.986 43.882  1.00 58.02  ? 344 TRP D CE2 1 
ATOM   10443 C  CE3 . TRP D 1 280 ? 47.731 21.693 44.264  1.00 56.37  ? 344 TRP D CE3 1 
ATOM   10444 C  CZ2 . TRP D 1 280 ? 50.555 22.114 44.643  1.00 51.97  ? 344 TRP D CZ2 1 
ATOM   10445 C  CZ3 . TRP D 1 280 ? 48.510 20.823 45.035  1.00 51.14  ? 344 TRP D CZ3 1 
ATOM   10446 C  CH2 . TRP D 1 280 ? 49.889 21.024 45.203  1.00 53.40  ? 344 TRP D CH2 1 
ATOM   10447 N  N   . ILE D 1 281 ? 44.139 22.685 40.749  1.00 52.87  ? 345 ILE D N   1 
ATOM   10448 C  CA  . ILE D 1 281 ? 42.701 22.812 40.707  1.00 58.47  ? 345 ILE D CA  1 
ATOM   10449 C  C   . ILE D 1 281 ? 42.127 22.308 42.008  1.00 64.79  ? 345 ILE D C   1 
ATOM   10450 O  O   . ILE D 1 281 ? 42.390 21.177 42.425  1.00 72.92  ? 345 ILE D O   1 
ATOM   10451 C  CB  . ILE D 1 281 ? 42.077 22.027 39.574  1.00 59.34  ? 345 ILE D CB  1 
ATOM   10452 C  CG1 . ILE D 1 281 ? 42.487 22.633 38.245  1.00 65.00  ? 345 ILE D CG1 1 
ATOM   10453 C  CG2 . ILE D 1 281 ? 40.571 22.063 39.704  1.00 61.38  ? 345 ILE D CG2 1 
ATOM   10454 C  CD1 . ILE D 1 281 ? 42.005 21.853 37.030  1.00 75.14  ? 345 ILE D CD1 1 
ATOM   10455 N  N   . GLY D 1 282 ? 41.354 23.163 42.658  1.00 59.80  ? 346 GLY D N   1 
ATOM   10456 C  CA  . GLY D 1 282 ? 40.631 22.748 43.840  1.00 61.66  ? 346 GLY D CA  1 
ATOM   10457 C  C   . GLY D 1 282 ? 39.194 22.497 43.439  1.00 58.09  ? 346 GLY D C   1 
ATOM   10458 O  O   . GLY D 1 282 ? 38.699 23.118 42.488  1.00 59.70  ? 346 GLY D O   1 
ATOM   10459 N  N   . ARG D 1 283 ? 38.522 21.595 44.162  1.00 54.67  ? 347 ARG D N   1 
ATOM   10460 C  CA  . ARG D 1 283 ? 37.105 21.319 43.917  1.00 51.78  ? 347 ARG D CA  1 
ATOM   10461 C  C   . ARG D 1 283 ? 36.394 20.578 45.022  1.00 50.10  ? 347 ARG D C   1 
ATOM   10462 O  O   . ARG D 1 283 ? 37.027 19.964 45.864  1.00 55.96  ? 347 ARG D O   1 
ATOM   10463 C  CB  . ARG D 1 283 ? 36.942 20.547 42.633  1.00 57.82  ? 347 ARG D CB  1 
ATOM   10464 C  CG  . ARG D 1 283 ? 37.070 19.073 42.766  1.00 54.25  ? 347 ARG D CG  1 
ATOM   10465 C  CD  . ARG D 1 283 ? 37.215 18.517 41.387  1.00 57.93  ? 347 ARG D CD  1 
ATOM   10466 N  NE  . ARG D 1 283 ? 37.083 17.074 41.388  1.00 66.62  ? 347 ARG D NE  1 
ATOM   10467 C  CZ  . ARG D 1 283 ? 36.978 16.349 40.287  1.00 76.55  ? 347 ARG D CZ  1 
ATOM   10468 N  NH1 . ARG D 1 283 ? 36.997 16.931 39.095  1.00 76.18  ? 347 ARG D NH1 1 
ATOM   10469 N  NH2 . ARG D 1 283 ? 36.854 15.037 40.382  1.00 105.23 ? 347 ARG D NH2 1 
ATOM   10470 N  N   . ILE D 1 284 ? 35.065 20.682 45.026  1.00 58.72  ? 348 ILE D N   1 
ATOM   10471 C  CA  . ILE D 1 284 ? 34.244 19.954 45.987  1.00 63.19  ? 348 ILE D CA  1 
ATOM   10472 C  C   . ILE D 1 284 ? 34.251 18.493 45.578  1.00 66.69  ? 348 ILE D C   1 
ATOM   10473 O  O   . ILE D 1 284 ? 34.062 18.177 44.413  1.00 79.24  ? 348 ILE D O   1 
ATOM   10474 C  CB  . ILE D 1 284 ? 32.814 20.502 46.057  1.00 58.86  ? 348 ILE D CB  1 
ATOM   10475 C  CG1 . ILE D 1 284 ? 32.866 22.012 46.269  1.00 73.47  ? 348 ILE D CG1 1 
ATOM   10476 C  CG2 . ILE D 1 284 ? 31.997 19.796 47.166  1.00 55.74  ? 348 ILE D CG2 1 
ATOM   10477 C  CD1 . ILE D 1 284 ? 31.642 22.617 46.973  1.00 86.77  ? 348 ILE D CD1 1 
ATOM   10478 N  N   . ILE D 1 285 ? 34.492 17.607 46.537  1.00 66.94  ? 349 ILE D N   1 
ATOM   10479 C  CA  . ILE D 1 285 ? 34.672 16.201 46.220  1.00 68.04  ? 349 ILE D CA  1 
ATOM   10480 C  C   . ILE D 1 285 ? 33.389 15.502 45.789  1.00 70.49  ? 349 ILE D C   1 
ATOM   10481 O  O   . ILE D 1 285 ? 33.380 14.883 44.735  1.00 75.07  ? 349 ILE D O   1 
ATOM   10482 C  CB  . ILE D 1 285 ? 35.321 15.433 47.361  1.00 65.39  ? 349 ILE D CB  1 
ATOM   10483 C  CG1 . ILE D 1 285 ? 36.711 16.005 47.639  1.00 49.18  ? 349 ILE D CG1 1 
ATOM   10484 C  CG2 . ILE D 1 285 ? 35.385 13.940 46.990  1.00 55.48  ? 349 ILE D CG2 1 
ATOM   10485 C  CD1 . ILE D 1 285 ? 37.397 15.336 48.777  1.00 45.13  ? 349 ILE D CD1 1 
ATOM   10486 N  N   . ASN D 1 286 ? 32.331 15.600 46.600  1.00 72.23  ? 350 ASN D N   1 
ATOM   10487 C  CA  . ASN D 1 286 ? 31.050 14.916 46.340  1.00 78.63  ? 350 ASN D CA  1 
ATOM   10488 C  C   . ASN D 1 286 ? 29.936 15.879 45.989  1.00 77.49  ? 350 ASN D C   1 
ATOM   10489 O  O   . ASN D 1 286 ? 29.159 16.258 46.857  1.00 104.23 ? 350 ASN D O   1 
ATOM   10490 C  CB  . ASN D 1 286 ? 30.622 14.066 47.542  1.00 78.66  ? 350 ASN D CB  1 
ATOM   10491 C  CG  . ASN D 1 286 ? 31.554 12.919 47.786  1.00 99.97  ? 350 ASN D CG  1 
ATOM   10492 O  OD1 . ASN D 1 286 ? 32.558 13.055 48.486  1.00 125.02 ? 350 ASN D OD1 1 
ATOM   10493 N  ND2 . ASN D 1 286 ? 31.240 11.776 47.196  1.00 112.23 ? 350 ASN D ND2 1 
ATOM   10494 N  N   . PRO D 1 287 ? 29.839 16.266 44.711  1.00 72.83  ? 351 PRO D N   1 
ATOM   10495 C  CA  . PRO D 1 287 ? 28.926 17.320 44.266  1.00 83.91  ? 351 PRO D CA  1 
ATOM   10496 C  C   . PRO D 1 287 ? 27.465 17.114 44.686  1.00 96.60  ? 351 PRO D C   1 
ATOM   10497 O  O   . PRO D 1 287 ? 26.706 18.084 44.750  1.00 108.76 ? 351 PRO D O   1 
ATOM   10498 C  CB  . PRO D 1 287 ? 29.058 17.270 42.739  1.00 79.77  ? 351 PRO D CB  1 
ATOM   10499 C  CG  . PRO D 1 287 ? 30.391 16.641 42.513  1.00 68.84  ? 351 PRO D CG  1 
ATOM   10500 C  CD  . PRO D 1 287 ? 30.468 15.595 43.567  1.00 73.61  ? 351 PRO D CD  1 
ATOM   10501 N  N   . GLY D 1 288 ? 27.078 15.872 44.968  1.00 101.56 ? 352 GLY D N   1 
ATOM   10502 C  CA  . GLY D 1 288 ? 25.752 15.605 45.508  1.00 107.31 ? 352 GLY D CA  1 
ATOM   10503 C  C   . GLY D 1 288 ? 25.595 16.204 46.899  1.00 105.48 ? 352 GLY D C   1 
ATOM   10504 O  O   . GLY D 1 288 ? 24.832 17.158 47.110  1.00 95.53  ? 352 GLY D O   1 
ATOM   10505 N  N   . SER D 1 289 ? 26.343 15.647 47.847  1.00 101.27 ? 353 SER D N   1 
ATOM   10506 C  CA  . SER D 1 289 ? 26.224 16.007 49.262  1.00 90.53  ? 353 SER D CA  1 
ATOM   10507 C  C   . SER D 1 289 ? 27.016 17.249 49.637  1.00 104.94 ? 353 SER D C   1 
ATOM   10508 O  O   . SER D 1 289 ? 26.916 17.730 50.773  1.00 108.15 ? 353 SER D O   1 
ATOM   10509 C  CB  . SER D 1 289 ? 26.646 14.836 50.157  1.00 96.71  ? 353 SER D CB  1 
ATOM   10510 O  OG  . SER D 1 289 ? 27.774 14.147 49.633  1.00 143.34 ? 353 SER D OG  1 
ATOM   10511 N  N   . LYS D 1 290 ? 27.801 17.756 48.683  1.00 105.92 ? 354 LYS D N   1 
ATOM   10512 C  CA  . LYS D 1 290 ? 28.661 18.933 48.868  1.00 87.53  ? 354 LYS D CA  1 
ATOM   10513 C  C   . LYS D 1 290 ? 29.722 18.692 49.935  1.00 76.41  ? 354 LYS D C   1 
ATOM   10514 O  O   . LYS D 1 290 ? 30.256 19.630 50.501  1.00 96.08  ? 354 LYS D O   1 
ATOM   10515 C  CB  . LYS D 1 290 ? 27.822 20.178 49.205  1.00 93.97  ? 354 LYS D CB  1 
ATOM   10516 C  CG  . LYS D 1 290 ? 26.776 20.550 48.172  1.00 80.12  ? 354 LYS D CG  1 
ATOM   10517 C  CD  . LYS D 1 290 ? 27.439 21.221 46.997  1.00 114.39 ? 354 LYS D CD  1 
ATOM   10518 C  CE  . LYS D 1 290 ? 26.444 21.461 45.877  1.00 168.27 ? 354 LYS D CE  1 
ATOM   10519 N  NZ  . LYS D 1 290 ? 25.453 22.498 46.257  1.00 192.17 ? 354 LYS D NZ  1 
ATOM   10520 N  N   . LYS D 1 291 ? 30.013 17.424 50.204  1.00 70.29  ? 355 LYS D N   1 
ATOM   10521 C  CA  . LYS D 1 291 ? 30.989 17.013 51.217  1.00 70.51  ? 355 LYS D CA  1 
ATOM   10522 C  C   . LYS D 1 291 ? 32.413 16.928 50.657  1.00 83.89  ? 355 LYS D C   1 
ATOM   10523 O  O   . LYS D 1 291 ? 32.659 16.348 49.586  1.00 88.06  ? 355 LYS D O   1 
ATOM   10524 C  CB  . LYS D 1 291 ? 30.621 15.636 51.770  1.00 77.88  ? 355 LYS D CB  1 
ATOM   10525 C  CG  . LYS D 1 291 ? 29.461 15.624 52.722  1.00 108.15 ? 355 LYS D CG  1 
ATOM   10526 C  CD  . LYS D 1 291 ? 29.935 15.284 54.129  1.00 135.91 ? 355 LYS D CD  1 
ATOM   10527 C  CE  . LYS D 1 291 ? 28.759 15.040 55.074  1.00 131.10 ? 355 LYS D CE  1 
ATOM   10528 N  NZ  . LYS D 1 291 ? 27.857 13.972 54.567  1.00 136.24 ? 355 LYS D NZ  1 
ATOM   10529 N  N   . GLY D 1 292 ? 33.364 17.490 51.391  1.00 79.16  ? 356 GLY D N   1 
ATOM   10530 C  CA  . GLY D 1 292 ? 34.776 17.299 51.070  1.00 64.30  ? 356 GLY D CA  1 
ATOM   10531 C  C   . GLY D 1 292 ? 35.361 18.287 50.091  1.00 63.57  ? 356 GLY D C   1 
ATOM   10532 O  O   . GLY D 1 292 ? 34.682 18.803 49.204  1.00 64.89  ? 356 GLY D O   1 
ATOM   10533 N  N   . PHE D 1 293 ? 36.641 18.564 50.257  1.00 56.97  ? 357 PHE D N   1 
ATOM   10534 C  CA  . PHE D 1 293 ? 37.309 19.461 49.335  1.00 57.01  ? 357 PHE D CA  1 
ATOM   10535 C  C   . PHE D 1 293 ? 38.662 18.870 48.991  1.00 56.31  ? 357 PHE D C   1 
ATOM   10536 O  O   . PHE D 1 293 ? 39.405 18.466 49.888  1.00 70.13  ? 357 PHE D O   1 
ATOM   10537 C  CB  . PHE D 1 293 ? 37.460 20.852 49.963  1.00 62.05  ? 357 PHE D CB  1 
ATOM   10538 C  CG  . PHE D 1 293 ? 38.091 21.862 49.050  1.00 59.53  ? 357 PHE D CG  1 
ATOM   10539 C  CD1 . PHE D 1 293 ? 39.465 21.995 48.981  1.00 57.09  ? 357 PHE D CD1 1 
ATOM   10540 C  CD2 . PHE D 1 293 ? 37.309 22.675 48.251  1.00 58.11  ? 357 PHE D CD2 1 
ATOM   10541 C  CE1 . PHE D 1 293 ? 40.035 22.918 48.129  1.00 61.03  ? 357 PHE D CE1 1 
ATOM   10542 C  CE2 . PHE D 1 293 ? 37.883 23.594 47.387  1.00 52.12  ? 357 PHE D CE2 1 
ATOM   10543 C  CZ  . PHE D 1 293 ? 39.241 23.714 47.323  1.00 51.31  ? 357 PHE D CZ  1 
ATOM   10544 N  N   . GLU D 1 294 ? 38.964 18.808 47.698  1.00 49.15  ? 358 GLU D N   1 
ATOM   10545 C  CA  . GLU D 1 294 ? 40.218 18.252 47.207  1.00 52.13  ? 358 GLU D CA  1 
ATOM   10546 C  C   . GLU D 1 294 ? 40.911 19.258 46.310  1.00 53.55  ? 358 GLU D C   1 
ATOM   10547 O  O   . GLU D 1 294 ? 40.278 20.088 45.690  1.00 63.32  ? 358 GLU D O   1 
ATOM   10548 C  CB  . GLU D 1 294 ? 40.011 16.908 46.483  1.00 58.98  ? 358 GLU D CB  1 
ATOM   10549 C  CG  . GLU D 1 294 ? 39.157 16.930 45.215  1.00 71.64  ? 358 GLU D CG  1 
ATOM   10550 C  CD  . GLU D 1 294 ? 38.945 15.542 44.562  1.00 96.51  ? 358 GLU D CD  1 
ATOM   10551 O  OE1 . GLU D 1 294 ? 39.775 14.636 44.774  1.00 116.09 ? 358 GLU D OE1 1 
ATOM   10552 O  OE2 . GLU D 1 294 ? 37.951 15.359 43.817  1.00 92.47  ? 358 GLU D OE2 1 
ATOM   10553 N  N   . ILE D 1 295 ? 42.226 19.213 46.288  1.00 54.45  ? 359 ILE D N   1 
ATOM   10554 C  CA  . ILE D 1 295 ? 43.016 20.085 45.433  1.00 57.98  ? 359 ILE D CA  1 
ATOM   10555 C  C   . ILE D 1 295 ? 44.086 19.218 44.813  1.00 67.82  ? 359 ILE D C   1 
ATOM   10556 O  O   . ILE D 1 295 ? 44.649 18.322 45.445  1.00 63.46  ? 359 ILE D O   1 
ATOM   10557 C  CB  . ILE D 1 295 ? 43.694 21.222 46.194  1.00 56.00  ? 359 ILE D CB  1 
ATOM   10558 C  CG1 . ILE D 1 295 ? 44.287 22.229 45.217  1.00 55.25  ? 359 ILE D CG1 1 
ATOM   10559 C  CG2 . ILE D 1 295 ? 44.795 20.689 47.082  1.00 56.23  ? 359 ILE D CG2 1 
ATOM   10560 C  CD1 . ILE D 1 295 ? 44.697 23.536 45.892  1.00 55.88  ? 359 ILE D CD1 1 
ATOM   10561 N  N   . TYR D 1 296 ? 44.385 19.515 43.568  1.00 74.23  ? 360 TYR D N   1 
ATOM   10562 C  CA  . TYR D 1 296 ? 44.990 18.544 42.712  1.00 59.82  ? 360 TYR D CA  1 
ATOM   10563 C  C   . TYR D 1 296 ? 46.077 19.230 41.871  1.00 64.30  ? 360 TYR D C   1 
ATOM   10564 O  O   . TYR D 1 296 ? 45.879 20.303 41.283  1.00 73.16  ? 360 TYR D O   1 
ATOM   10565 C  CB  . TYR D 1 296 ? 43.868 17.927 41.878  1.00 61.37  ? 360 TYR D CB  1 
ATOM   10566 C  CG  . TYR D 1 296 ? 44.288 16.785 41.022  1.00 79.31  ? 360 TYR D CG  1 
ATOM   10567 C  CD1 . TYR D 1 296 ? 44.599 15.550 41.562  1.00 93.79  ? 360 TYR D CD1 1 
ATOM   10568 C  CD2 . TYR D 1 296 ? 44.380 16.935 39.666  1.00 97.79  ? 360 TYR D CD2 1 
ATOM   10569 C  CE1 . TYR D 1 296 ? 45.003 14.489 40.756  1.00 89.35  ? 360 TYR D CE1 1 
ATOM   10570 C  CE2 . TYR D 1 296 ? 44.772 15.895 38.855  1.00 112.96 ? 360 TYR D CE2 1 
ATOM   10571 C  CZ  . TYR D 1 296 ? 45.082 14.678 39.398  1.00 98.52  ? 360 TYR D CZ  1 
ATOM   10572 O  OH  . TYR D 1 296 ? 45.460 13.669 38.549  1.00 89.49  ? 360 TYR D OH  1 
ATOM   10573 N  N   . LYS D 1 297 ? 47.240 18.608 41.837  1.00 59.74  ? 361 LYS D N   1 
ATOM   10574 C  CA  . LYS D 1 297 ? 48.425 19.222 41.276  1.00 73.09  ? 361 LYS D CA  1 
ATOM   10575 C  C   . LYS D 1 297 ? 48.653 18.785 39.821  1.00 83.00  ? 361 LYS D C   1 
ATOM   10576 O  O   . LYS D 1 297 ? 48.297 17.667 39.441  1.00 91.07  ? 361 LYS D O   1 
ATOM   10577 C  CB  . LYS D 1 297 ? 49.605 18.827 42.162  1.00 63.08  ? 361 LYS D CB  1 
ATOM   10578 C  CG  . LYS D 1 297 ? 50.889 19.546 41.946  1.00 58.77  ? 361 LYS D CG  1 
ATOM   10579 C  CD  . LYS D 1 297 ? 51.824 19.029 42.967  1.00 52.75  ? 361 LYS D CD  1 
ATOM   10580 C  CE  . LYS D 1 297 ? 53.254 19.236 42.582  1.00 59.30  ? 361 LYS D CE  1 
ATOM   10581 N  NZ  . LYS D 1 297 ? 54.103 18.691 43.667  1.00 71.22  ? 361 LYS D NZ  1 
ATOM   10582 N  N   . PHE D 1 298 ? 49.240 19.673 39.019  1.00 70.70  ? 362 PHE D N   1 
ATOM   10583 C  CA  . PHE D 1 298 ? 49.523 19.391 37.624  1.00 67.30  ? 362 PHE D CA  1 
ATOM   10584 C  C   . PHE D 1 298 ? 50.850 19.967 37.206  1.00 74.93  ? 362 PHE D C   1 
ATOM   10585 O  O   . PHE D 1 298 ? 51.173 21.107 37.549  1.00 80.03  ? 362 PHE D O   1 
ATOM   10586 C  CB  . PHE D 1 298 ? 48.500 20.066 36.766  1.00 68.85  ? 362 PHE D CB  1 
ATOM   10587 C  CG  . PHE D 1 298 ? 47.142 19.492 36.877  1.00 77.89  ? 362 PHE D CG  1 
ATOM   10588 C  CD1 . PHE D 1 298 ? 46.762 18.413 36.084  1.00 90.42  ? 362 PHE D CD1 1 
ATOM   10589 C  CD2 . PHE D 1 298 ? 46.218 20.055 37.734  1.00 80.04  ? 362 PHE D CD2 1 
ATOM   10590 C  CE1 . PHE D 1 298 ? 45.479 17.888 36.161  1.00 85.31  ? 362 PHE D CE1 1 
ATOM   10591 C  CE2 . PHE D 1 298 ? 44.926 19.549 37.812  1.00 82.78  ? 362 PHE D CE2 1 
ATOM   10592 C  CZ  . PHE D 1 298 ? 44.554 18.465 37.025  1.00 79.35  ? 362 PHE D CZ  1 
ATOM   10593 N  N   . LEU D 1 299 ? 51.617 19.197 36.446  1.00 77.18  ? 363 LEU D N   1 
ATOM   10594 C  CA  . LEU D 1 299 ? 52.858 19.721 35.936  1.00 83.67  ? 363 LEU D CA  1 
ATOM   10595 C  C   . LEU D 1 299 ? 52.542 20.568 34.734  1.00 97.48  ? 363 LEU D C   1 
ATOM   10596 O  O   . LEU D 1 299 ? 51.786 20.143 33.863  1.00 121.12 ? 363 LEU D O   1 
ATOM   10597 C  CB  . LEU D 1 299 ? 53.826 18.598 35.605  1.00 93.62  ? 363 LEU D CB  1 
ATOM   10598 C  CG  . LEU D 1 299 ? 54.611 18.065 36.816  1.00 103.90 ? 363 LEU D CG  1 
ATOM   10599 C  CD1 . LEU D 1 299 ? 55.140 19.215 37.704  1.00 122.41 ? 363 LEU D CD1 1 
ATOM   10600 C  CD2 . LEU D 1 299 ? 53.791 17.074 37.641  1.00 78.38  ? 363 LEU D CD2 1 
ATOM   10601 N  N   . GLY D 1 300 ? 53.079 21.786 34.717  1.00 106.55 ? 364 GLY D N   1 
ATOM   10602 C  CA  . GLY D 1 300 ? 52.833 22.730 33.620  1.00 106.18 ? 364 GLY D CA  1 
ATOM   10603 C  C   . GLY D 1 300 ? 51.409 23.262 33.546  1.00 92.37  ? 364 GLY D C   1 
ATOM   10604 O  O   . GLY D 1 300 ? 50.615 23.050 34.465  1.00 80.33  ? 364 GLY D O   1 
ATOM   10605 N  N   . THR D 1 301 ? 51.090 23.920 32.430  1.00 90.98  ? 365 THR D N   1 
ATOM   10606 C  CA  . THR D 1 301 ? 49.845 24.682 32.271  1.00 86.22  ? 365 THR D CA  1 
ATOM   10607 C  C   . THR D 1 301 ? 48.556 23.848 32.312  1.00 82.31  ? 365 THR D C   1 
ATOM   10608 O  O   . THR D 1 301 ? 48.565 22.650 32.098  1.00 92.46  ? 365 THR D O   1 
ATOM   10609 C  CB  . THR D 1 301 ? 49.860 25.568 30.997  1.00 87.80  ? 365 THR D CB  1 
ATOM   10610 O  OG1 . THR D 1 301 ? 48.682 26.389 30.955  1.00 117.87 ? 365 THR D OG1 1 
ATOM   10611 C  CG2 . THR D 1 301 ? 49.873 24.724 29.768  1.00 92.45  ? 365 THR D CG2 1 
ATOM   10612 N  N   . LEU D 1 302 ? 47.453 24.519 32.609  1.00 78.56  ? 366 LEU D N   1 
ATOM   10613 C  CA  . LEU D 1 302 ? 46.148 23.918 32.604  1.00 76.81  ? 366 LEU D CA  1 
ATOM   10614 C  C   . LEU D 1 302 ? 45.573 24.061 31.215  1.00 83.87  ? 366 LEU D C   1 
ATOM   10615 O  O   . LEU D 1 302 ? 44.475 23.567 30.913  1.00 87.10  ? 366 LEU D O   1 
ATOM   10616 C  CB  . LEU D 1 302 ? 45.239 24.661 33.570  1.00 78.50  ? 366 LEU D CB  1 
ATOM   10617 C  CG  . LEU D 1 302 ? 45.672 24.773 35.022  1.00 88.91  ? 366 LEU D CG  1 
ATOM   10618 C  CD1 . LEU D 1 302 ? 46.176 26.153 35.307  1.00 105.51 ? 366 LEU D CD1 1 
ATOM   10619 C  CD2 . LEU D 1 302 ? 44.480 24.519 35.879  1.00 91.07  ? 366 LEU D CD2 1 
ATOM   10620 N  N   . PHE D 1 303 ? 46.316 24.749 30.365  1.00 83.69  ? 367 PHE D N   1 
ATOM   10621 C  CA  . PHE D 1 303 ? 45.811 25.096 29.065  1.00 84.99  ? 367 PHE D CA  1 
ATOM   10622 C  C   . PHE D 1 303 ? 46.419 24.272 27.937  1.00 100.00 ? 367 PHE D C   1 
ATOM   10623 O  O   . PHE D 1 303 ? 46.143 24.514 26.767  1.00 115.03 ? 367 PHE D O   1 
ATOM   10624 C  CB  . PHE D 1 303 ? 46.020 26.571 28.871  1.00 77.93  ? 367 PHE D CB  1 
ATOM   10625 C  CG  . PHE D 1 303 ? 45.456 27.372 29.971  1.00 82.55  ? 367 PHE D CG  1 
ATOM   10626 C  CD1 . PHE D 1 303 ? 44.106 27.242 30.321  1.00 82.53  ? 367 PHE D CD1 1 
ATOM   10627 C  CD2 . PHE D 1 303 ? 46.256 28.255 30.678  1.00 90.57  ? 367 PHE D CD2 1 
ATOM   10628 C  CE1 . PHE D 1 303 ? 43.562 27.990 31.365  1.00 79.13  ? 367 PHE D CE1 1 
ATOM   10629 C  CE2 . PHE D 1 303 ? 45.719 29.025 31.726  1.00 100.13 ? 367 PHE D CE2 1 
ATOM   10630 C  CZ  . PHE D 1 303 ? 44.374 28.884 32.077  1.00 85.58  ? 367 PHE D CZ  1 
ATOM   10631 N  N   . SER D 1 304 ? 47.244 23.298 28.300  1.00 105.99 ? 368 SER D N   1 
ATOM   10632 C  CA  . SER D 1 304 ? 47.701 22.277 27.361  1.00 130.21 ? 368 SER D CA  1 
ATOM   10633 C  C   . SER D 1 304 ? 46.928 20.982 27.621  1.00 121.00 ? 368 SER D C   1 
ATOM   10634 O  O   . SER D 1 304 ? 46.741 20.579 28.769  1.00 114.82 ? 368 SER D O   1 
ATOM   10635 C  CB  . SER D 1 304 ? 49.214 22.040 27.499  1.00 136.62 ? 368 SER D CB  1 
ATOM   10636 O  OG  . SER D 1 304 ? 49.723 21.220 26.460  1.00 111.44 ? 368 SER D OG  1 
ATOM   10637 N  N   . VAL D 1 305 ? 46.475 20.341 26.550  1.00 107.84 ? 369 VAL D N   1 
ATOM   10638 C  CA  . VAL D 1 305 ? 45.809 19.058 26.646  1.00 98.68  ? 369 VAL D CA  1 
ATOM   10639 C  C   . VAL D 1 305 ? 46.846 17.978 27.018  1.00 107.83 ? 369 VAL D C   1 
ATOM   10640 O  O   . VAL D 1 305 ? 46.494 16.854 27.379  1.00 99.62  ? 369 VAL D O   1 
ATOM   10641 C  CB  . VAL D 1 305 ? 45.110 18.751 25.311  1.00 104.95 ? 369 VAL D CB  1 
ATOM   10642 C  CG1 . VAL D 1 305 ? 46.134 18.548 24.199  1.00 129.72 ? 369 VAL D CG1 1 
ATOM   10643 C  CG2 . VAL D 1 305 ? 44.222 17.555 25.432  1.00 112.52 ? 369 VAL D CG2 1 
ATOM   10644 N  N   . GLN D 1 306 ? 48.122 18.361 26.941  1.00 124.37 ? 370 GLN D N   1 
ATOM   10645 C  CA  . GLN D 1 306 ? 49.276 17.482 27.151  1.00 137.16 ? 370 GLN D CA  1 
ATOM   10646 C  C   . GLN D 1 306 ? 49.525 17.138 28.607  1.00 128.20 ? 370 GLN D C   1 
ATOM   10647 O  O   . GLN D 1 306 ? 50.160 16.129 28.918  1.00 146.86 ? 370 GLN D O   1 
ATOM   10648 C  CB  . GLN D 1 306 ? 50.544 18.169 26.628  1.00 148.16 ? 370 GLN D CB  1 
ATOM   10649 C  CG  . GLN D 1 306 ? 50.732 18.136 25.123  1.00 154.18 ? 370 GLN D CG  1 
ATOM   10650 C  CD  . GLN D 1 306 ? 51.227 16.795 24.645  1.00 171.42 ? 370 GLN D CD  1 
ATOM   10651 O  OE1 . GLN D 1 306 ? 50.449 15.855 24.500  1.00 182.97 ? 370 GLN D OE1 1 
ATOM   10652 N  NE2 . GLN D 1 306 ? 52.532 16.696 24.398  1.00 202.24 ? 370 GLN D NE2 1 
ATOM   10653 N  N   . THR D 1 307 ? 49.025 17.985 29.494  1.00 122.52 ? 371 THR D N   1 
ATOM   10654 C  CA  . THR D 1 307 ? 49.522 18.033 30.863  1.00 114.60 ? 371 THR D CA  1 
ATOM   10655 C  C   . THR D 1 307 ? 48.879 17.023 31.815  1.00 101.14 ? 371 THR D C   1 
ATOM   10656 O  O   . THR D 1 307 ? 47.728 16.618 31.651  1.00 111.03 ? 371 THR D O   1 
ATOM   10657 C  CB  . THR D 1 307 ? 49.452 19.470 31.399  1.00 97.23  ? 371 THR D CB  1 
ATOM   10658 O  OG1 . THR D 1 307 ? 48.139 19.978 31.163  1.00 105.85 ? 371 THR D OG1 1 
ATOM   10659 C  CG2 . THR D 1 307 ? 50.445 20.367 30.638  1.00 87.09  ? 371 THR D CG2 1 
ATOM   10660 N  N   . VAL D 1 308 ? 49.652 16.654 32.827  1.00 99.49  ? 372 VAL D N   1 
ATOM   10661 C  CA  . VAL D 1 308 ? 49.480 15.413 33.569  1.00 108.78 ? 372 VAL D CA  1 
ATOM   10662 C  C   . VAL D 1 308 ? 49.112 15.649 35.042  1.00 109.47 ? 372 VAL D C   1 
ATOM   10663 O  O   . VAL D 1 308 ? 49.771 16.427 35.762  1.00 89.89  ? 372 VAL D O   1 
ATOM   10664 C  CB  . VAL D 1 308 ? 50.809 14.607 33.524  1.00 103.67 ? 372 VAL D CB  1 
ATOM   10665 C  CG1 . VAL D 1 308 ? 50.666 13.266 34.216  1.00 95.36  ? 372 VAL D CG1 1 
ATOM   10666 C  CG2 . VAL D 1 308 ? 51.287 14.436 32.078  1.00 106.92 ? 372 VAL D CG2 1 
ATOM   10667 N  N   . GLY D 1 309 ? 48.067 14.958 35.493  1.00 99.51  ? 373 GLY D N   1 
ATOM   10668 C  CA  . GLY D 1 309 ? 47.783 14.883 36.920  1.00 91.12  ? 373 GLY D CA  1 
ATOM   10669 C  C   . GLY D 1 309 ? 48.979 14.297 37.646  1.00 100.29 ? 373 GLY D C   1 
ATOM   10670 O  O   . GLY D 1 309 ? 49.657 13.406 37.129  1.00 135.25 ? 373 GLY D O   1 
ATOM   10671 N  N   . ASN D 1 310 ? 49.257 14.799 38.838  1.00 91.27  ? 374 ASN D N   1 
ATOM   10672 C  CA  . ASN D 1 310 ? 50.415 14.350 39.573  1.00 90.14  ? 374 ASN D CA  1 
ATOM   10673 C  C   . ASN D 1 310 ? 50.019 13.936 40.972  1.00 91.00  ? 374 ASN D C   1 
ATOM   10674 O  O   . ASN D 1 310 ? 50.166 12.779 41.344  1.00 132.34 ? 374 ASN D O   1 
ATOM   10675 C  CB  . ASN D 1 310 ? 51.476 15.455 39.599  1.00 98.73  ? 374 ASN D CB  1 
ATOM   10676 C  CG  . ASN D 1 310 ? 52.672 15.100 40.439  1.00 92.23  ? 374 ASN D CG  1 
ATOM   10677 O  OD1 . ASN D 1 310 ? 52.782 15.534 41.579  1.00 96.59  ? 374 ASN D OD1 1 
ATOM   10678 N  ND2 . ASN D 1 310 ? 53.569 14.298 39.887  1.00 106.54 ? 374 ASN D ND2 1 
ATOM   10679 N  N   . ARG D 1 311 ? 49.502 14.883 41.738  1.00 76.64  ? 375 ARG D N   1 
ATOM   10680 C  CA  . ARG D 1 311 ? 49.260 14.672 43.153  1.00 73.97  ? 375 ARG D CA  1 
ATOM   10681 C  C   . ARG D 1 311 ? 47.892 15.200 43.575  1.00 70.27  ? 375 ARG D C   1 
ATOM   10682 O  O   . ARG D 1 311 ? 47.534 16.340 43.281  1.00 67.10  ? 375 ARG D O   1 
ATOM   10683 C  CB  . ARG D 1 311 ? 50.359 15.354 43.985  1.00 65.28  ? 375 ARG D CB  1 
ATOM   10684 C  CG  . ARG D 1 311 ? 50.191 15.218 45.495  1.00 64.66  ? 375 ARG D CG  1 
ATOM   10685 C  CD  . ARG D 1 311 ? 50.415 13.770 45.886  1.00 75.80  ? 375 ARG D CD  1 
ATOM   10686 N  NE  . ARG D 1 311 ? 50.302 13.503 47.319  1.00 65.14  ? 375 ARG D NE  1 
ATOM   10687 C  CZ  . ARG D 1 311 ? 51.290 13.665 48.193  1.00 67.03  ? 375 ARG D CZ  1 
ATOM   10688 N  NH1 . ARG D 1 311 ? 52.476 14.146 47.802  1.00 75.81  ? 375 ARG D NH1 1 
ATOM   10689 N  NH2 . ARG D 1 311 ? 51.084 13.364 49.469  1.00 67.11  ? 375 ARG D NH2 1 
ATOM   10690 N  N   . ASN D 1 312 ? 47.141 14.364 44.279  1.00 70.89  ? 376 ASN D N   1 
ATOM   10691 C  CA  . ASN D 1 312 ? 45.835 14.757 44.780  1.00 77.52  ? 376 ASN D CA  1 
ATOM   10692 C  C   . ASN D 1 312 ? 45.808 14.820 46.292  1.00 68.07  ? 376 ASN D C   1 
ATOM   10693 O  O   . ASN D 1 312 ? 46.018 13.809 46.953  1.00 69.32  ? 376 ASN D O   1 
ATOM   10694 C  CB  . ASN D 1 312 ? 44.743 13.801 44.281  1.00 95.34  ? 376 ASN D CB  1 
ATOM   10695 C  CG  . ASN D 1 312 ? 43.432 13.973 45.030  1.00 96.63  ? 376 ASN D CG  1 
ATOM   10696 O  OD1 . ASN D 1 312 ? 43.212 13.341 46.072  1.00 101.39 ? 376 ASN D OD1 1 
ATOM   10697 N  ND2 . ASN D 1 312 ? 42.556 14.835 44.507  1.00 85.81  ? 376 ASN D ND2 1 
ATOM   10698 N  N   . TYR D 1 313 ? 45.523 16.008 46.822  1.00 60.67  ? 377 TYR D N   1 
ATOM   10699 C  CA  . TYR D 1 313 ? 45.429 16.232 48.255  1.00 57.21  ? 377 TYR D CA  1 
ATOM   10700 C  C   . TYR D 1 313 ? 43.982 16.356 48.628  1.00 63.29  ? 377 TYR D C   1 
ATOM   10701 O  O   . TYR D 1 313 ? 43.321 17.314 48.226  1.00 70.05  ? 377 TYR D O   1 
ATOM   10702 C  CB  . TYR D 1 313 ? 46.106 17.543 48.657  1.00 54.69  ? 377 TYR D CB  1 
ATOM   10703 C  CG  . TYR D 1 313 ? 47.603 17.554 48.581  1.00 57.03  ? 377 TYR D CG  1 
ATOM   10704 C  CD1 . TYR D 1 313 ? 48.254 18.223 47.544  1.00 58.79  ? 377 TYR D CD1 1 
ATOM   10705 C  CD2 . TYR D 1 313 ? 48.373 16.910 49.545  1.00 51.29  ? 377 TYR D CD2 1 
ATOM   10706 C  CE1 . TYR D 1 313 ? 49.636 18.233 47.457  1.00 63.05  ? 377 TYR D CE1 1 
ATOM   10707 C  CE2 . TYR D 1 313 ? 49.751 16.927 49.474  1.00 61.68  ? 377 TYR D CE2 1 
ATOM   10708 C  CZ  . TYR D 1 313 ? 50.380 17.590 48.423  1.00 61.23  ? 377 TYR D CZ  1 
ATOM   10709 O  OH  . TYR D 1 313 ? 51.750 17.624 48.342  1.00 67.69  ? 377 TYR D OH  1 
ATOM   10710 N  N   . GLN D 1 314 ? 43.477 15.415 49.413  1.00 65.78  ? 378 GLN D N   1 
ATOM   10711 C  CA  . GLN D 1 314 ? 42.112 15.537 49.883  1.00 63.91  ? 378 GLN D CA  1 
ATOM   10712 C  C   . GLN D 1 314 ? 42.153 16.238 51.194  1.00 58.50  ? 378 GLN D C   1 
ATOM   10713 O  O   . GLN D 1 314 ? 42.326 15.595 52.213  1.00 63.41  ? 378 GLN D O   1 
ATOM   10714 C  CB  . GLN D 1 314 ? 41.476 14.179 50.048  1.00 75.88  ? 378 GLN D CB  1 
ATOM   10715 C  CG  . GLN D 1 314 ? 41.130 13.544 48.731  1.00 87.45  ? 378 GLN D CG  1 
ATOM   10716 C  CD  . GLN D 1 314 ? 40.062 12.490 48.876  1.00 109.40 ? 378 GLN D CD  1 
ATOM   10717 O  OE1 . GLN D 1 314 ? 39.502 12.369 50.080  1.00 141.52 ? 378 GLN D OE1 1 
ATOM   10718 N  NE2 . GLN D 1 314 ? 39.738 11.789 47.919  1.00 100.78 ? 378 GLN D NE2 1 
ATOM   10719 N  N   . LEU D 1 315 ? 42.008 17.559 51.163  1.00 57.80  ? 379 LEU D N   1 
ATOM   10720 C  CA  . LEU D 1 315 ? 42.169 18.387 52.360  1.00 61.36  ? 379 LEU D CA  1 
ATOM   10721 C  C   . LEU D 1 315 ? 41.050 18.254 53.373  1.00 67.76  ? 379 LEU D C   1 
ATOM   10722 O  O   . LEU D 1 315 ? 41.315 18.187 54.578  1.00 84.02  ? 379 LEU D O   1 
ATOM   10723 C  CB  . LEU D 1 315 ? 42.346 19.861 51.994  1.00 62.63  ? 379 LEU D CB  1 
ATOM   10724 C  CG  . LEU D 1 315 ? 43.607 20.226 51.195  1.00 64.31  ? 379 LEU D CG  1 
ATOM   10725 C  CD1 . LEU D 1 315 ? 43.676 21.728 50.944  1.00 59.44  ? 379 LEU D CD1 1 
ATOM   10726 C  CD2 . LEU D 1 315 ? 44.880 19.740 51.867  1.00 53.26  ? 379 LEU D CD2 1 
ATOM   10727 N  N   . LEU D 1 316 ? 39.809 18.219 52.898  1.00 63.12  ? 380 LEU D N   1 
ATOM   10728 C  CA  . LEU D 1 316 ? 38.670 18.110 53.793  1.00 59.72  ? 380 LEU D CA  1 
ATOM   10729 C  C   . LEU D 1 316 ? 37.812 16.939 53.373  1.00 63.63  ? 380 LEU D C   1 
ATOM   10730 O  O   . LEU D 1 316 ? 37.576 16.763 52.170  1.00 58.09  ? 380 LEU D O   1 
ATOM   10731 C  CB  . LEU D 1 316 ? 37.855 19.398 53.752  1.00 50.04  ? 380 LEU D CB  1 
ATOM   10732 C  CG  . LEU D 1 316 ? 38.550 20.710 54.118  1.00 48.53  ? 380 LEU D CG  1 
ATOM   10733 C  CD1 . LEU D 1 316 ? 37.515 21.782 54.448  1.00 61.25  ? 380 LEU D CD1 1 
ATOM   10734 C  CD2 . LEU D 1 316 ? 39.475 20.537 55.270  1.00 38.00  ? 380 LEU D CD2 1 
ATOM   10735 N  N   . SER D 1 317 ? 37.337 16.163 54.355  1.00 63.05  ? 381 SER D N   1 
ATOM   10736 C  CA  . SER D 1 317 ? 36.452 15.026 54.078  1.00 65.27  ? 381 SER D CA  1 
ATOM   10737 C  C   . SER D 1 317 ? 35.123 15.100 54.781  1.00 72.62  ? 381 SER D C   1 
ATOM   10738 O  O   . SER D 1 317 ? 34.075 14.917 54.165  1.00 113.12 ? 381 SER D O   1 
ATOM   10739 C  CB  . SER D 1 317 ? 37.119 13.739 54.477  1.00 70.91  ? 381 SER D CB  1 
ATOM   10740 O  OG  . SER D 1 317 ? 38.388 13.656 53.884  1.00 91.81  ? 381 SER D OG  1 
ATOM   10741 N  N   . ASN D 1 318 ? 35.164 15.353 56.077  1.00 72.23  ? 382 ASN D N   1 
ATOM   10742 C  CA  . ASN D 1 318 ? 33.944 15.386 56.872  1.00 91.31  ? 382 ASN D CA  1 
ATOM   10743 C  C   . ASN D 1 318 ? 33.076 16.671 56.827  1.00 85.45  ? 382 ASN D C   1 
ATOM   10744 O  O   . ASN D 1 318 ? 32.045 16.745 57.501  1.00 108.57 ? 382 ASN D O   1 
ATOM   10745 C  CB  . ASN D 1 318 ? 34.279 15.010 58.315  1.00 109.46 ? 382 ASN D CB  1 
ATOM   10746 C  CG  . ASN D 1 318 ? 33.852 13.599 58.664  1.00 133.24 ? 382 ASN D CG  1 
ATOM   10747 O  OD1 . ASN D 1 318 ? 33.051 12.985 57.959  1.00 150.78 ? 382 ASN D OD1 1 
ATOM   10748 N  ND2 . ASN D 1 318 ? 34.365 13.085 59.774  1.00 153.08 ? 382 ASN D ND2 1 
ATOM   10749 N  N   . SER D 1 319 ? 33.463 17.665 56.033  1.00 67.71  ? 383 SER D N   1 
ATOM   10750 C  CA  . SER D 1 319 ? 32.819 18.980 56.134  1.00 77.87  ? 383 SER D CA  1 
ATOM   10751 C  C   . SER D 1 319 ? 31.974 19.367 54.900  1.00 66.96  ? 383 SER D C   1 
ATOM   10752 O  O   . SER D 1 319 ? 32.373 19.161 53.761  1.00 68.16  ? 383 SER D O   1 
ATOM   10753 C  CB  . SER D 1 319 ? 33.867 20.066 56.471  1.00 70.22  ? 383 SER D CB  1 
ATOM   10754 O  OG  . SER D 1 319 ? 34.988 19.491 57.116  1.00 85.56  ? 383 SER D OG  1 
ATOM   10755 N  N   . THR D 1 320 ? 30.802 19.935 55.139  1.00 62.54  ? 384 THR D N   1 
ATOM   10756 C  CA  . THR D 1 320 ? 30.010 20.499 54.056  1.00 67.12  ? 384 THR D CA  1 
ATOM   10757 C  C   . THR D 1 320 ? 30.611 21.818 53.526  1.00 63.14  ? 384 THR D C   1 
ATOM   10758 O  O   . THR D 1 320 ? 30.629 22.844 54.232  1.00 57.15  ? 384 THR D O   1 
ATOM   10759 C  CB  . THR D 1 320 ? 28.541 20.714 54.478  1.00 59.28  ? 384 THR D CB  1 
ATOM   10760 O  OG1 . THR D 1 320 ? 27.980 19.479 54.924  1.00 80.57  ? 384 THR D OG1 1 
ATOM   10761 C  CG2 . THR D 1 320 ? 27.744 21.207 53.310  1.00 55.40  ? 384 THR D CG2 1 
ATOM   10762 N  N   . ILE D 1 321 ? 31.057 21.771 52.272  1.00 53.22  ? 385 ILE D N   1 
ATOM   10763 C  CA  . ILE D 1 321 ? 31.764 22.861 51.600  1.00 49.44  ? 385 ILE D CA  1 
ATOM   10764 C  C   . ILE D 1 321 ? 30.871 23.724 50.694  1.00 64.87  ? 385 ILE D C   1 
ATOM   10765 O  O   . ILE D 1 321 ? 29.750 23.336 50.310  1.00 90.75  ? 385 ILE D O   1 
ATOM   10766 C  CB  . ILE D 1 321 ? 32.900 22.290 50.738  1.00 44.04  ? 385 ILE D CB  1 
ATOM   10767 C  CG1 . ILE D 1 321 ? 33.696 21.273 51.534  1.00 45.70  ? 385 ILE D CG1 1 
ATOM   10768 C  CG2 . ILE D 1 321 ? 33.794 23.360 50.197  1.00 36.56  ? 385 ILE D CG2 1 
ATOM   10769 C  CD1 . ILE D 1 321 ? 34.465 21.870 52.640  1.00 49.16  ? 385 ILE D CD1 1 
ATOM   10770 N  N   . GLY D 1 322 ? 31.401 24.899 50.361  1.00 55.99  ? 386 GLY D N   1 
ATOM   10771 C  CA  . GLY D 1 322 ? 30.738 25.858 49.495  1.00 62.01  ? 386 GLY D CA  1 
ATOM   10772 C  C   . GLY D 1 322 ? 31.746 26.664 48.709  1.00 57.40  ? 386 GLY D C   1 
ATOM   10773 O  O   . GLY D 1 322 ? 32.571 26.103 47.962  1.00 56.17  ? 386 GLY D O   1 
ATOM   10774 N  N   . ARG D 1 323 ? 31.696 27.982 48.872  1.00 57.08  ? 387 ARG D N   1 
ATOM   10775 C  CA  . ARG D 1 323 ? 32.627 28.851 48.134  1.00 59.65  ? 387 ARG D CA  1 
ATOM   10776 C  C   . ARG D 1 323 ? 34.072 28.676 48.590  1.00 49.26  ? 387 ARG D C   1 
ATOM   10777 O  O   . ARG D 1 323 ? 34.346 28.280 49.712  1.00 54.63  ? 387 ARG D O   1 
ATOM   10778 C  CB  . ARG D 1 323 ? 32.221 30.327 48.197  1.00 53.44  ? 387 ARG D CB  1 
ATOM   10779 C  CG  . ARG D 1 323 ? 30.753 30.562 47.976  1.00 54.35  ? 387 ARG D CG  1 
ATOM   10780 C  CD  . ARG D 1 323 ? 30.321 31.845 48.621  1.00 60.10  ? 387 ARG D CD  1 
ATOM   10781 N  NE  . ARG D 1 323 ? 31.158 32.937 48.155  1.00 75.16  ? 387 ARG D NE  1 
ATOM   10782 C  CZ  . ARG D 1 323 ? 31.967 33.640 48.937  1.00 64.85  ? 387 ARG D CZ  1 
ATOM   10783 N  NH1 . ARG D 1 323 ? 32.028 33.358 50.231  1.00 55.89  ? 387 ARG D NH1 1 
ATOM   10784 N  NH2 . ARG D 1 323 ? 32.702 34.621 48.419  1.00 59.31  ? 387 ARG D NH2 1 
ATOM   10785 N  N   . SER D 1 324 ? 34.982 28.965 47.688  1.00 40.72  ? 388 SER D N   1 
ATOM   10786 C  CA  . SER D 1 324 ? 36.397 28.890 47.947  1.00 43.33  ? 388 SER D CA  1 
ATOM   10787 C  C   . SER D 1 324 ? 36.970 30.061 47.172  1.00 40.11  ? 388 SER D C   1 
ATOM   10788 O  O   . SER D 1 324 ? 36.400 30.461 46.155  1.00 42.47  ? 388 SER D O   1 
ATOM   10789 C  CB  . SER D 1 324 ? 37.000 27.538 47.443  1.00 49.52  ? 388 SER D CB  1 
ATOM   10790 O  OG  . SER D 1 324 ? 36.254 26.914 46.377  1.00 59.57  ? 388 SER D OG  1 
ATOM   10791 N  N   . GLY D 1 325 ? 38.076 30.626 47.618  1.00 33.94  ? 389 GLY D N   1 
ATOM   10792 C  CA  . GLY D 1 325 ? 38.698 31.632 46.811  1.00 35.86  ? 389 GLY D CA  1 
ATOM   10793 C  C   . GLY D 1 325 ? 40.107 31.925 47.206  1.00 38.82  ? 389 GLY D C   1 
ATOM   10794 O  O   . GLY D 1 325 ? 40.530 31.515 48.281  1.00 44.82  ? 389 GLY D O   1 
ATOM   10795 N  N   . LEU D 1 326 ? 40.837 32.661 46.366  1.00 39.12  ? 390 LEU D N   1 
ATOM   10796 C  CA  . LEU D 1 326 ? 42.231 32.928 46.665  1.00 44.26  ? 390 LEU D CA  1 
ATOM   10797 C  C   . LEU D 1 326 ? 42.423 34.252 47.360  1.00 54.14  ? 390 LEU D C   1 
ATOM   10798 O  O   . LEU D 1 326 ? 41.530 35.111 47.364  1.00 71.60  ? 390 LEU D O   1 
ATOM   10799 C  CB  . LEU D 1 326 ? 43.052 32.931 45.403  1.00 46.04  ? 390 LEU D CB  1 
ATOM   10800 C  CG  . LEU D 1 326 ? 43.032 31.671 44.561  1.00 49.01  ? 390 LEU D CG  1 
ATOM   10801 C  CD1 . LEU D 1 326 ? 43.226 32.056 43.121  1.00 64.84  ? 390 LEU D CD1 1 
ATOM   10802 C  CD2 . LEU D 1 326 ? 44.142 30.840 44.983  1.00 46.75  ? 390 LEU D CD2 1 
ATOM   10803 N  N   . TYR D 1 327 ? 43.605 34.398 47.960  1.00 63.47  ? 391 TYR D N   1 
ATOM   10804 C  CA  . TYR D 1 327 ? 44.099 35.680 48.454  1.00 58.04  ? 391 TYR D CA  1 
ATOM   10805 C  C   . TYR D 1 327 ? 45.614 35.693 48.602  1.00 56.35  ? 391 TYR D C   1 
ATOM   10806 O  O   . TYR D 1 327 ? 46.218 34.685 48.925  1.00 69.11  ? 391 TYR D O   1 
ATOM   10807 C  CB  . TYR D 1 327 ? 43.429 36.059 49.768  1.00 53.56  ? 391 TYR D CB  1 
ATOM   10808 C  CG  . TYR D 1 327 ? 43.799 35.234 50.981  1.00 58.00  ? 391 TYR D CG  1 
ATOM   10809 C  CD1 . TYR D 1 327 ? 44.835 35.620 51.841  1.00 64.09  ? 391 TYR D CD1 1 
ATOM   10810 C  CD2 . TYR D 1 327 ? 43.085 34.102 51.293  1.00 63.27  ? 391 TYR D CD2 1 
ATOM   10811 C  CE1 . TYR D 1 327 ? 45.153 34.881 52.966  1.00 54.13  ? 391 TYR D CE1 1 
ATOM   10812 C  CE2 . TYR D 1 327 ? 43.381 33.361 52.413  1.00 68.45  ? 391 TYR D CE2 1 
ATOM   10813 C  CZ  . TYR D 1 327 ? 44.407 33.748 53.245  1.00 59.67  ? 391 TYR D CZ  1 
ATOM   10814 O  OH  . TYR D 1 327 ? 44.654 32.961 54.347  1.00 49.54  ? 391 TYR D OH  1 
ATOM   10815 N  N   . GLN D 1 328 ? 46.219 36.840 48.353  1.00 59.82  ? 392 GLN D N   1 
ATOM   10816 C  CA  . GLN D 1 328 ? 47.638 36.985 48.561  1.00 62.70  ? 392 GLN D CA  1 
ATOM   10817 C  C   . GLN D 1 328 ? 47.921 37.919 49.729  1.00 73.83  ? 392 GLN D C   1 
ATOM   10818 O  O   . GLN D 1 328 ? 47.523 39.100 49.733  1.00 102.20 ? 392 GLN D O   1 
ATOM   10819 C  CB  . GLN D 1 328 ? 48.330 37.490 47.308  1.00 64.84  ? 392 GLN D CB  1 
ATOM   10820 C  CG  . GLN D 1 328 ? 48.052 36.688 46.080  1.00 69.64  ? 392 GLN D CG  1 
ATOM   10821 C  CD  . GLN D 1 328 ? 48.729 37.271 44.852  1.00 80.45  ? 392 GLN D CD  1 
ATOM   10822 O  OE1 . GLN D 1 328 ? 48.319 38.301 44.284  1.00 95.06  ? 392 GLN D OE1 1 
ATOM   10823 N  NE2 . GLN D 1 328 ? 49.769 36.601 44.429  1.00 85.72  ? 392 GLN D NE2 1 
ATOM   10824 N  N   . PRO D 1 329 ? 48.592 37.378 50.743  1.00 65.11  ? 393 PRO D N   1 
ATOM   10825 C  CA  . PRO D 1 329 ? 49.075 38.189 51.843  1.00 64.42  ? 393 PRO D CA  1 
ATOM   10826 C  C   . PRO D 1 329 ? 50.317 38.931 51.376  1.00 73.62  ? 393 PRO D C   1 
ATOM   10827 O  O   . PRO D 1 329 ? 51.013 38.445 50.481  1.00 75.61  ? 393 PRO D O   1 
ATOM   10828 C  CB  . PRO D 1 329 ? 49.406 37.158 52.909  1.00 59.92  ? 393 PRO D CB  1 
ATOM   10829 C  CG  . PRO D 1 329 ? 49.606 35.876 52.157  1.00 57.24  ? 393 PRO D CG  1 
ATOM   10830 C  CD  . PRO D 1 329 ? 48.785 35.933 50.950  1.00 55.74  ? 393 PRO D CD  1 
ATOM   10831 N  N   . ALA D 1 330 ? 50.576 40.101 51.957  1.00 92.52  ? 394 ALA D N   1 
ATOM   10832 C  CA  . ALA D 1 330 ? 51.723 40.916 51.561  1.00 99.30  ? 394 ALA D CA  1 
ATOM   10833 C  C   . ALA D 1 330 ? 52.669 41.208 52.727  1.00 123.58 ? 394 ALA D C   1 
ATOM   10834 O  O   . ALA D 1 330 ? 52.268 41.762 53.765  1.00 102.77 ? 394 ALA D O   1 
ATOM   10835 C  CB  . ALA D 1 330 ? 51.257 42.205 50.923  1.00 109.13 ? 394 ALA D CB  1 
ATOM   10836 N  N   . TYR D 1 331 ? 53.926 40.802 52.546  1.00 150.67 ? 395 TYR D N   1 
ATOM   10837 C  CA  . TYR D 1 331 ? 55.017 41.132 53.462  1.00 139.35 ? 395 TYR D CA  1 
ATOM   10838 C  C   . TYR D 1 331 ? 56.276 41.401 52.655  1.00 147.75 ? 395 TYR D C   1 
ATOM   10839 O  O   . TYR D 1 331 ? 56.297 41.221 51.434  1.00 134.95 ? 395 TYR D O   1 
ATOM   10840 C  CB  . TYR D 1 331 ? 55.309 39.990 54.438  1.00 122.10 ? 395 TYR D CB  1 
ATOM   10841 C  CG  . TYR D 1 331 ? 54.115 39.156 54.825  1.00 142.05 ? 395 TYR D CG  1 
ATOM   10842 C  CD1 . TYR D 1 331 ? 53.184 39.623 55.765  1.00 130.76 ? 395 TYR D CD1 1 
ATOM   10843 C  CD2 . TYR D 1 331 ? 53.917 37.893 54.254  1.00 131.07 ? 395 TYR D CD2 1 
ATOM   10844 C  CE1 . TYR D 1 331 ? 52.083 38.854 56.125  1.00 143.17 ? 395 TYR D CE1 1 
ATOM   10845 C  CE2 . TYR D 1 331 ? 52.821 37.115 54.604  1.00 137.17 ? 395 TYR D CE2 1 
ATOM   10846 C  CZ  . TYR D 1 331 ? 51.908 37.601 55.541  1.00 159.87 ? 395 TYR D CZ  1 
ATOM   10847 O  OH  . TYR D 1 331 ? 50.819 36.836 55.896  1.00 155.36 ? 395 TYR D OH  1 
ATOM   10848 N  N   . GLU D 1 332 ? 57.328 41.832 53.343  1.00 179.28 ? 396 GLU D N   1 
ATOM   10849 C  CA  . GLU D 1 332 ? 58.641 41.930 52.730  1.00 190.64 ? 396 GLU D CA  1 
ATOM   10850 C  C   . GLU D 1 332 ? 59.048 40.534 52.252  1.00 213.04 ? 396 GLU D C   1 
ATOM   10851 O  O   . GLU D 1 332 ? 59.452 40.369 51.099  1.00 245.30 ? 396 GLU D O   1 
ATOM   10852 C  CB  . GLU D 1 332 ? 59.660 42.505 53.722  1.00 187.69 ? 396 GLU D CB  1 
ATOM   10853 C  CG  . GLU D 1 332 ? 61.038 42.805 53.127  1.00 183.30 ? 396 GLU D CG  1 
ATOM   10854 C  CD  . GLU D 1 332 ? 61.916 41.569 52.992  1.00 181.99 ? 396 GLU D CD  1 
ATOM   10855 O  OE1 . GLU D 1 332 ? 62.040 40.803 53.972  1.00 186.50 ? 396 GLU D OE1 1 
ATOM   10856 O  OE2 . GLU D 1 332 ? 62.486 41.365 51.903  1.00 178.52 ? 396 GLU D OE2 1 
ATOM   10857 N  N   . SER D 1 333 ? 58.901 39.540 53.137  1.00 188.31 ? 397 SER D N   1 
ATOM   10858 C  CA  . SER D 1 333 ? 59.265 38.143 52.865  1.00 157.05 ? 397 SER D CA  1 
ATOM   10859 C  C   . SER D 1 333 ? 60.512 38.064 51.993  1.00 170.18 ? 397 SER D C   1 
ATOM   10860 O  O   . SER D 1 333 ? 61.611 38.378 52.451  1.00 189.06 ? 397 SER D O   1 
ATOM   10861 C  CB  . SER D 1 333 ? 58.097 37.386 52.226  1.00 144.20 ? 397 SER D CB  1 
ATOM   10862 O  OG  . SER D 1 333 ? 56.986 37.326 53.104  1.00 159.73 ? 397 SER D OG  1 
ATOM   10863 N  N   . ARG D 1 334 ? 60.333 37.661 50.738  1.00 162.69 ? 398 ARG D N   1 
ATOM   10864 C  CA  . ARG D 1 334 ? 61.407 37.708 49.746  1.00 174.30 ? 398 ARG D CA  1 
ATOM   10865 C  C   . ARG D 1 334 ? 60.856 37.797 48.331  1.00 169.39 ? 398 ARG D C   1 
ATOM   10866 O  O   . ARG D 1 334 ? 59.664 38.043 48.150  1.00 174.48 ? 398 ARG D O   1 
ATOM   10867 C  CB  . ARG D 1 334 ? 62.367 36.523 49.893  1.00 189.54 ? 398 ARG D CB  1 
ATOM   10868 C  CG  . ARG D 1 334 ? 61.712 35.153 50.001  1.00 191.57 ? 398 ARG D CG  1 
ATOM   10869 C  CD  . ARG D 1 334 ? 62.766 34.056 49.934  1.00 224.05 ? 398 ARG D CD  1 
ATOM   10870 N  NE  . ARG D 1 334 ? 63.946 34.370 50.745  1.00 249.13 ? 398 ARG D NE  1 
ATOM   10871 C  CZ  . ARG D 1 334 ? 65.004 33.575 50.889  1.00 251.04 ? 398 ARG D CZ  1 
ATOM   10872 N  NH1 . ARG D 1 334 ? 65.049 32.398 50.287  1.00 267.17 ? 398 ARG D NH1 1 
ATOM   10873 N  NH2 . ARG D 1 334 ? 66.018 33.957 51.647  1.00 264.57 ? 398 ARG D NH2 1 
ATOM   10874 N  N   . ASP D 1 335 ? 61.726 37.597 47.338  1.00 182.21 ? 399 ASP D N   1 
ATOM   10875 C  CA  . ASP D 1 335 ? 61.357 37.649 45.915  1.00 209.00 ? 399 ASP D CA  1 
ATOM   10876 C  C   . ASP D 1 335 ? 60.074 36.877 45.648  1.00 196.77 ? 399 ASP D C   1 
ATOM   10877 O  O   . ASP D 1 335 ? 59.354 37.135 44.678  1.00 223.33 ? 399 ASP D O   1 
ATOM   10878 C  CB  . ASP D 1 335 ? 62.484 37.073 45.049  1.00 228.52 ? 399 ASP D CB  1 
ATOM   10879 C  CG  . ASP D 1 335 ? 63.740 37.934 45.062  1.00 253.15 ? 399 ASP D CG  1 
ATOM   10880 O  OD1 . ASP D 1 335 ? 63.679 39.104 45.496  1.00 274.55 ? 399 ASP D OD1 1 
ATOM   10881 O  OD2 . ASP D 1 335 ? 64.799 37.436 44.629  1.00 274.25 ? 399 ASP D OD2 1 
ATOM   10882 N  N   . CYS D 1 336 ? 59.807 35.938 46.545  1.00 159.19 ? 400 CYS D N   1 
ATOM   10883 C  CA  . CYS D 1 336 ? 58.661 35.061 46.490  1.00 138.78 ? 400 CYS D CA  1 
ATOM   10884 C  C   . CYS D 1 336 ? 57.339 35.732 46.911  1.00 120.62 ? 400 CYS D C   1 
ATOM   10885 O  O   . CYS D 1 336 ? 57.246 36.303 48.003  1.00 138.68 ? 400 CYS D O   1 
ATOM   10886 C  CB  . CYS D 1 336 ? 58.954 33.893 47.414  1.00 146.50 ? 400 CYS D CB  1 
ATOM   10887 S  SG  . CYS D 1 336 ? 58.309 32.388 46.822  1.00 202.00 ? 400 CYS D SG  1 
ATOM   10888 N  N   . GLN D 1 337 ? 56.320 35.652 46.050  1.00 86.52  ? 401 GLN D N   1 
ATOM   10889 C  CA  . GLN D 1 337 ? 54.962 36.070 46.420  1.00 78.22  ? 401 GLN D CA  1 
ATOM   10890 C  C   . GLN D 1 337 ? 54.108 34.921 46.948  1.00 75.62  ? 401 GLN D C   1 
ATOM   10891 O  O   . GLN D 1 337 ? 53.752 34.006 46.204  1.00 77.56  ? 401 GLN D O   1 
ATOM   10892 C  CB  . GLN D 1 337 ? 54.237 36.763 45.256  1.00 82.96  ? 401 GLN D CB  1 
ATOM   10893 C  CG  . GLN D 1 337 ? 52.839 37.286 45.607  1.00 82.00  ? 401 GLN D CG  1 
ATOM   10894 C  CD  . GLN D 1 337 ? 52.753 37.914 46.999  1.00 76.11  ? 401 GLN D CD  1 
ATOM   10895 O  OE1 . GLN D 1 337 ? 53.473 38.860 47.311  1.00 90.70  ? 401 GLN D OE1 1 
ATOM   10896 N  NE2 . GLN D 1 337 ? 51.876 37.381 47.837  1.00 66.74  ? 401 GLN D NE2 1 
ATOM   10897 N  N   . GLU D 1 338 ? 53.753 34.998 48.227  1.00 76.55  ? 402 GLU D N   1 
ATOM   10898 C  CA  . GLU D 1 338 ? 52.937 33.975 48.867  1.00 74.86  ? 402 GLU D CA  1 
ATOM   10899 C  C   . GLU D 1 338 ? 51.501 33.937 48.298  1.00 73.68  ? 402 GLU D C   1 
ATOM   10900 O  O   . GLU D 1 338 ? 50.939 34.959 47.911  1.00 85.23  ? 402 GLU D O   1 
ATOM   10901 C  CB  . GLU D 1 338 ? 52.929 34.197 50.381  1.00 96.23  ? 402 GLU D CB  1 
ATOM   10902 C  CG  . GLU D 1 338 ? 52.278 33.077 51.204  1.00 123.92 ? 402 GLU D CG  1 
ATOM   10903 C  CD  . GLU D 1 338 ? 53.268 32.138 51.864  1.00 154.75 ? 402 GLU D CD  1 
ATOM   10904 O  OE1 . GLU D 1 338 ? 54.329 32.611 52.331  1.00 199.96 ? 402 GLU D OE1 1 
ATOM   10905 O  OE2 . GLU D 1 338 ? 52.965 30.926 51.935  1.00 145.69 ? 402 GLU D OE2 1 
ATOM   10906 N  N   . LEU D 1 339 ? 50.930 32.739 48.246  1.00 66.60  ? 403 LEU D N   1 
ATOM   10907 C  CA  . LEU D 1 339 ? 49.574 32.517 47.768  1.00 58.63  ? 403 LEU D CA  1 
ATOM   10908 C  C   . LEU D 1 339 ? 48.773 31.581 48.693  1.00 61.63  ? 403 LEU D C   1 
ATOM   10909 O  O   . LEU D 1 339 ? 49.211 30.473 49.011  1.00 60.40  ? 403 LEU D O   1 
ATOM   10910 C  CB  . LEU D 1 339 ? 49.600 31.943 46.366  1.00 59.31  ? 403 LEU D CB  1 
ATOM   10911 C  CG  . LEU D 1 339 ? 48.220 31.739 45.742  1.00 66.87  ? 403 LEU D CG  1 
ATOM   10912 C  CD1 . LEU D 1 339 ? 47.457 33.061 45.678  1.00 58.64  ? 403 LEU D CD1 1 
ATOM   10913 C  CD2 . LEU D 1 339 ? 48.386 31.163 44.368  1.00 80.70  ? 403 LEU D CD2 1 
ATOM   10914 N  N   . CYS D 1 340 ? 47.600 32.051 49.122  1.00 61.93  ? 404 CYS D N   1 
ATOM   10915 C  CA  . CYS D 1 340 ? 46.748 31.337 50.064  1.00 56.06  ? 404 CYS D CA  1 
ATOM   10916 C  C   . CYS D 1 340 ? 45.341 31.309 49.557  1.00 52.57  ? 404 CYS D C   1 
ATOM   10917 O  O   . CYS D 1 340 ? 44.965 32.104 48.686  1.00 60.02  ? 404 CYS D O   1 
ATOM   10918 C  CB  . CYS D 1 340 ? 46.716 32.036 51.416  1.00 62.11  ? 404 CYS D CB  1 
ATOM   10919 S  SG  . CYS D 1 340 ? 48.290 32.180 52.211  1.00 84.02  ? 404 CYS D SG  1 
ATOM   10920 N  N   . PHE D 1 341 ? 44.543 30.404 50.100  1.00 42.40  ? 405 PHE D N   1 
ATOM   10921 C  CA  . PHE D 1 341 ? 43.137 30.389 49.705  1.00 46.46  ? 405 PHE D CA  1 
ATOM   10922 C  C   . PHE D 1 341 ? 42.267 30.027 50.881  1.00 45.79  ? 405 PHE D C   1 
ATOM   10923 O  O   . PHE D 1 341 ? 42.716 29.398 51.833  1.00 55.55  ? 405 PHE D O   1 
ATOM   10924 C  CB  . PHE D 1 341 ? 42.875 29.449 48.501  1.00 43.34  ? 405 PHE D CB  1 
ATOM   10925 C  CG  . PHE D 1 341 ? 43.038 27.969 48.817  1.00 48.17  ? 405 PHE D CG  1 
ATOM   10926 C  CD1 . PHE D 1 341 ? 44.271 27.326 48.652  1.00 44.46  ? 405 PHE D CD1 1 
ATOM   10927 C  CD2 . PHE D 1 341 ? 41.950 27.220 49.293  1.00 52.69  ? 405 PHE D CD2 1 
ATOM   10928 C  CE1 . PHE D 1 341 ? 44.412 25.971 48.946  1.00 47.09  ? 405 PHE D CE1 1 
ATOM   10929 C  CE2 . PHE D 1 341 ? 42.086 25.855 49.583  1.00 46.05  ? 405 PHE D CE2 1 
ATOM   10930 C  CZ  . PHE D 1 341 ? 43.310 25.240 49.419  1.00 48.69  ? 405 PHE D CZ  1 
ATOM   10931 N  N   . TRP D 1 342 ? 41.015 30.419 50.791  1.00 41.76  ? 406 TRP D N   1 
ATOM   10932 C  CA  . TRP D 1 342 ? 40.051 30.171 51.832  1.00 41.13  ? 406 TRP D CA  1 
ATOM   10933 C  C   . TRP D 1 342 ? 38.933 29.339 51.300  1.00 43.13  ? 406 TRP D C   1 
ATOM   10934 O  O   . TRP D 1 342 ? 38.711 29.284 50.102  1.00 49.14  ? 406 TRP D O   1 
ATOM   10935 C  CB  . TRP D 1 342 ? 39.496 31.485 52.361  1.00 38.99  ? 406 TRP D CB  1 
ATOM   10936 C  CG  . TRP D 1 342 ? 38.900 32.359 51.291  1.00 38.13  ? 406 TRP D CG  1 
ATOM   10937 C  CD1 . TRP D 1 342 ? 39.472 33.468 50.670  1.00 38.94  ? 406 TRP D CD1 1 
ATOM   10938 C  CD2 . TRP D 1 342 ? 37.593 32.223 50.681  1.00 44.24  ? 406 TRP D CD2 1 
ATOM   10939 N  NE1 . TRP D 1 342 ? 38.624 34.027 49.744  1.00 37.99  ? 406 TRP D NE1 1 
ATOM   10940 C  CE2 . TRP D 1 342 ? 37.475 33.318 49.703  1.00 43.28  ? 406 TRP D CE2 1 
ATOM   10941 C  CE3 . TRP D 1 342 ? 36.524 31.345 50.845  1.00 54.52  ? 406 TRP D CE3 1 
ATOM   10942 C  CZ2 . TRP D 1 342 ? 36.335 33.491 48.942  1.00 43.21  ? 406 TRP D CZ2 1 
ATOM   10943 C  CZ3 . TRP D 1 342 ? 35.375 31.539 50.060  1.00 57.33  ? 406 TRP D CZ3 1 
ATOM   10944 C  CH2 . TRP D 1 342 ? 35.287 32.589 49.138  1.00 45.90  ? 406 TRP D CH2 1 
ATOM   10945 N  N   . ILE D 1 343 ? 38.205 28.701 52.211  1.00 45.66  ? 407 ILE D N   1 
ATOM   10946 C  CA  . ILE D 1 343 ? 37.120 27.800 51.887  1.00 44.28  ? 407 ILE D CA  1 
ATOM   10947 C  C   . ILE D 1 343 ? 36.087 28.022 52.932  1.00 48.24  ? 407 ILE D C   1 
ATOM   10948 O  O   . ILE D 1 343 ? 36.365 27.962 54.113  1.00 67.20  ? 407 ILE D O   1 
ATOM   10949 C  CB  . ILE D 1 343 ? 37.529 26.328 51.971  1.00 42.73  ? 407 ILE D CB  1 
ATOM   10950 C  CG1 . ILE D 1 343 ? 38.751 26.058 51.080  1.00 47.54  ? 407 ILE D CG1 1 
ATOM   10951 C  CG2 . ILE D 1 343 ? 36.356 25.473 51.570  1.00 37.43  ? 407 ILE D CG2 1 
ATOM   10952 C  CD1 . ILE D 1 343 ? 39.304 24.690 51.203  1.00 61.11  ? 407 ILE D CD1 1 
ATOM   10953 N  N   . GLU D 1 344 ? 34.874 28.278 52.489  1.00 58.59  ? 408 GLU D N   1 
ATOM   10954 C  CA  . GLU D 1 344 ? 33.766 28.557 53.378  1.00 46.25  ? 408 GLU D CA  1 
ATOM   10955 C  C   . GLU D 1 344 ? 33.089 27.237 53.704  1.00 47.17  ? 408 GLU D C   1 
ATOM   10956 O  O   . GLU D 1 344 ? 32.925 26.361 52.854  1.00 74.64  ? 408 GLU D O   1 
ATOM   10957 C  CB  . GLU D 1 344 ? 32.858 29.542 52.671  1.00 41.86  ? 408 GLU D CB  1 
ATOM   10958 C  CG  . GLU D 1 344 ? 31.766 30.156 53.471  1.00 51.07  ? 408 GLU D CG  1 
ATOM   10959 C  CD  . GLU D 1 344 ? 30.805 30.960 52.567  1.00 87.39  ? 408 GLU D CD  1 
ATOM   10960 O  OE1 . GLU D 1 344 ? 30.539 32.151 52.891  1.00 66.36  ? 408 GLU D OE1 1 
ATOM   10961 O  OE2 . GLU D 1 344 ? 30.344 30.398 51.522  1.00 99.58  ? 408 GLU D OE2 1 
ATOM   10962 N  N   . ILE D 1 345 ? 32.692 27.091 54.944  1.00 43.00  ? 409 ILE D N   1 
ATOM   10963 C  CA  . ILE D 1 345 ? 32.142 25.836 55.411  1.00 47.83  ? 409 ILE D CA  1 
ATOM   10964 C  C   . ILE D 1 345 ? 30.796 26.042 56.113  1.00 47.86  ? 409 ILE D C   1 
ATOM   10965 O  O   . ILE D 1 345 ? 30.646 26.983 56.896  1.00 45.24  ? 409 ILE D O   1 
ATOM   10966 C  CB  . ILE D 1 345 ? 33.120 25.244 56.405  1.00 46.92  ? 409 ILE D CB  1 
ATOM   10967 C  CG1 . ILE D 1 345 ? 34.374 24.811 55.673  1.00 51.18  ? 409 ILE D CG1 1 
ATOM   10968 C  CG2 . ILE D 1 345 ? 32.479 24.125 57.232  1.00 46.40  ? 409 ILE D CG2 1 
ATOM   10969 C  CD1 . ILE D 1 345 ? 35.361 24.109 56.605  1.00 67.33  ? 409 ILE D CD1 1 
ATOM   10970 N  N   . ALA D 1 346 ? 29.846 25.142 55.872  1.00 45.17  ? 410 ALA D N   1 
ATOM   10971 C  CA  . ALA D 1 346 ? 28.600 25.156 56.629  1.00 49.38  ? 410 ALA D CA  1 
ATOM   10972 C  C   . ALA D 1 346 ? 28.851 25.028 58.124  1.00 57.39  ? 410 ALA D C   1 
ATOM   10973 O  O   . ALA D 1 346 ? 29.627 24.157 58.558  1.00 53.69  ? 410 ALA D O   1 
ATOM   10974 C  CB  . ALA D 1 346 ? 27.701 24.041 56.184  1.00 46.50  ? 410 ALA D CB  1 
ATOM   10975 N  N   . ALA D 1 347 ? 28.204 25.897 58.910  1.00 60.43  ? 411 ALA D N   1 
ATOM   10976 C  CA  . ALA D 1 347 ? 28.170 25.730 60.365  1.00 56.57  ? 411 ALA D CA  1 
ATOM   10977 C  C   . ALA D 1 347 ? 26.737 25.588 60.858  1.00 59.36  ? 411 ALA D C   1 
ATOM   10978 O  O   . ALA D 1 347 ? 25.809 25.434 60.066  1.00 79.90  ? 411 ALA D O   1 
ATOM   10979 C  CB  . ALA D 1 347 ? 28.856 26.883 61.050  1.00 61.15  ? 411 ALA D CB  1 
ATOM   10980 N  N   . THR D 1 348 ? 26.573 25.589 62.172  1.00 58.08  ? 412 THR D N   1 
ATOM   10981 C  CA  . THR D 1 348 ? 25.268 25.783 62.777  1.00 63.49  ? 412 THR D CA  1 
ATOM   10982 C  C   . THR D 1 348 ? 25.470 26.523 64.106  1.00 60.74  ? 412 THR D C   1 
ATOM   10983 O  O   . THR D 1 348 ? 26.493 26.369 64.762  1.00 55.19  ? 412 THR D O   1 
ATOM   10984 C  CB  . THR D 1 348 ? 24.430 24.444 62.928  1.00 70.03  ? 412 THR D CB  1 
ATOM   10985 O  OG1 . THR D 1 348 ? 25.106 23.516 63.779  1.00 74.19  ? 412 THR D OG1 1 
ATOM   10986 C  CG2 . THR D 1 348 ? 24.154 23.753 61.554  1.00 69.76  ? 412 THR D CG2 1 
ATOM   10987 N  N   . THR D 1 349 ? 24.510 27.356 64.473  1.00 61.54  ? 413 THR D N   1 
ATOM   10988 C  CA  . THR D 1 349 ? 24.514 28.007 65.762  1.00 69.50  ? 413 THR D CA  1 
ATOM   10989 C  C   . THR D 1 349 ? 24.159 26.949 66.810  1.00 84.74  ? 413 THR D C   1 
ATOM   10990 O  O   . THR D 1 349 ? 23.600 25.904 66.474  1.00 86.10  ? 413 THR D O   1 
ATOM   10991 C  CB  . THR D 1 349 ? 23.480 29.144 65.734  1.00 71.62  ? 413 THR D CB  1 
ATOM   10992 O  OG1 . THR D 1 349 ? 23.933 30.126 64.804  1.00 82.79  ? 413 THR D OG1 1 
ATOM   10993 C  CG2 . THR D 1 349 ? 23.268 29.811 67.090  1.00 74.76  ? 413 THR D CG2 1 
ATOM   10994 N  N   . LYS D 1 350 ? 24.491 27.226 68.072  1.00 101.75 ? 414 LYS D N   1 
ATOM   10995 C  CA  . LYS D 1 350 ? 24.147 26.375 69.220  1.00 88.76  ? 414 LYS D CA  1 
ATOM   10996 C  C   . LYS D 1 350 ? 22.714 25.848 69.146  1.00 97.58  ? 414 LYS D C   1 
ATOM   10997 O  O   . LYS D 1 350 ? 22.424 24.809 69.726  1.00 108.10 ? 414 LYS D O   1 
ATOM   10998 C  CB  . LYS D 1 350 ? 24.380 27.139 70.532  1.00 106.78 ? 414 LYS D CB  1 
ATOM   10999 C  CG  . LYS D 1 350 ? 24.175 26.371 71.841  1.00 101.71 ? 414 LYS D CG  1 
ATOM   11000 C  CD  . LYS D 1 350 ? 24.095 27.341 73.035  1.00 125.26 ? 414 LYS D CD  1 
ATOM   11001 C  CE  . LYS D 1 350 ? 23.812 26.621 74.356  1.00 103.39 ? 414 LYS D CE  1 
ATOM   11002 N  NZ  . LYS D 1 350 ? 23.882 27.555 75.528  1.00 119.93 ? 414 LYS D NZ  1 
ATOM   11003 N  N   . ALA D 1 351 ? 21.833 26.546 68.425  1.00 96.01  ? 415 ALA D N   1 
ATOM   11004 C  CA  . ALA D 1 351 ? 20.466 26.071 68.216  1.00 100.54 ? 415 ALA D CA  1 
ATOM   11005 C  C   . ALA D 1 351 ? 19.962 26.358 66.804  1.00 108.11 ? 415 ALA D C   1 
ATOM   11006 O  O   . ALA D 1 351 ? 19.315 27.380 66.588  1.00 129.22 ? 415 ALA D O   1 
ATOM   11007 C  CB  . ALA D 1 351 ? 19.532 26.693 69.246  1.00 93.30  ? 415 ALA D CB  1 
ATOM   11008 N  N   . GLY D 1 352 ? 20.254 25.458 65.857  1.00 94.40  ? 416 GLY D N   1 
ATOM   11009 C  CA  . GLY D 1 352 ? 19.830 25.599 64.446  1.00 86.82  ? 416 GLY D CA  1 
ATOM   11010 C  C   . GLY D 1 352 ? 20.627 26.678 63.741  1.00 100.29 ? 416 GLY D C   1 
ATOM   11011 O  O   . GLY D 1 352 ? 21.653 27.114 64.268  1.00 121.19 ? 416 GLY D O   1 
ATOM   11012 N  N   . LEU D 1 353 ? 20.166 27.116 62.564  1.00 92.12  ? 417 LEU D N   1 
ATOM   11013 C  CA  . LEU D 1 353 ? 20.735 28.290 61.840  1.00 81.37  ? 417 LEU D CA  1 
ATOM   11014 C  C   . LEU D 1 353 ? 21.997 27.917 61.077  1.00 89.23  ? 417 LEU D C   1 
ATOM   11015 O  O   . LEU D 1 353 ? 22.777 27.114 61.538  1.00 103.18 ? 417 LEU D O   1 
ATOM   11016 C  CB  . LEU D 1 353 ? 20.994 29.497 62.768  1.00 64.43  ? 417 LEU D CB  1 
ATOM   11017 C  CG  . LEU D 1 353 ? 19.988 29.726 63.929  1.00 80.28  ? 417 LEU D CG  1 
ATOM   11018 C  CD1 . LEU D 1 353 ? 20.463 30.662 65.055  1.00 83.84  ? 417 LEU D CD1 1 
ATOM   11019 C  CD2 . LEU D 1 353 ? 18.626 30.172 63.470  1.00 66.72  ? 417 LEU D CD2 1 
ATOM   11020 N  N   . SER D 1 354 ? 22.199 28.508 59.910  1.00 107.34 ? 418 SER D N   1 
ATOM   11021 C  CA  . SER D 1 354 ? 23.249 28.051 59.019  1.00 112.82 ? 418 SER D CA  1 
ATOM   11022 C  C   . SER D 1 354 ? 24.283 29.130 58.762  1.00 115.53 ? 418 SER D C   1 
ATOM   11023 O  O   . SER D 1 354 ? 24.447 29.588 57.632  1.00 196.44 ? 418 SER D O   1 
ATOM   11024 C  CB  . SER D 1 354 ? 22.645 27.558 57.696  1.00 145.83 ? 418 SER D CB  1 
ATOM   11025 O  OG  . SER D 1 354 ? 21.889 28.582 57.066  1.00 187.38 ? 418 SER D OG  1 
ATOM   11026 N  N   . SER D 1 355 ? 24.988 29.545 59.798  1.00 92.03  ? 419 SER D N   1 
ATOM   11027 C  CA  . SER D 1 355 ? 26.116 30.424 59.568  1.00 101.68 ? 419 SER D CA  1 
ATOM   11028 C  C   . SER D 1 355 ? 27.161 29.594 58.811  1.00 78.91  ? 419 SER D C   1 
ATOM   11029 O  O   . SER D 1 355 ? 27.074 28.363 58.764  1.00 66.17  ? 419 SER D O   1 
ATOM   11030 C  CB  . SER D 1 355 ? 26.650 31.002 60.897  1.00 119.98 ? 419 SER D CB  1 
ATOM   11031 O  OG  . SER D 1 355 ? 27.619 32.033 60.712  1.00 99.14  ? 419 SER D OG  1 
ATOM   11032 N  N   . ASN D 1 356 ? 28.104 30.281 58.176  1.00 86.54  ? 420 ASN D N   1 
ATOM   11033 C  CA  . ASN D 1 356 ? 29.267 29.646 57.589  1.00 69.91  ? 420 ASN D CA  1 
ATOM   11034 C  C   . ASN D 1 356 ? 30.511 30.053 58.342  1.00 65.85  ? 420 ASN D C   1 
ATOM   11035 O  O   . ASN D 1 356 ? 30.535 31.132 58.943  1.00 81.68  ? 420 ASN D O   1 
ATOM   11036 C  CB  . ASN D 1 356 ? 29.398 30.047 56.132  1.00 69.60  ? 420 ASN D CB  1 
ATOM   11037 C  CG  . ASN D 1 356 ? 28.096 30.030 55.432  1.00 78.38  ? 420 ASN D CG  1 
ATOM   11038 O  OD1 . ASN D 1 356 ? 27.271 30.892 55.678  1.00 84.50  ? 420 ASN D OD1 1 
ATOM   11039 N  ND2 . ASN D 1 356 ? 27.882 29.044 54.561  1.00 86.30  ? 420 ASN D ND2 1 
ATOM   11040 N  N   . ASP D 1 357 ? 31.537 29.193 58.327  1.00 70.26  ? 421 ASP D N   1 
ATOM   11041 C  CA  . ASP D 1 357 ? 32.877 29.605 58.788  1.00 68.50  ? 421 ASP D CA  1 
ATOM   11042 C  C   . ASP D 1 357 ? 33.974 29.371 57.785  1.00 59.14  ? 421 ASP D C   1 
ATOM   11043 O  O   . ASP D 1 357 ? 33.761 28.754 56.755  1.00 94.75  ? 421 ASP D O   1 
ATOM   11044 C  CB  . ASP D 1 357 ? 33.258 28.981 60.125  1.00 71.85  ? 421 ASP D CB  1 
ATOM   11045 C  CG  . ASP D 1 357 ? 33.838 30.012 61.102  1.00 95.84  ? 421 ASP D CG  1 
ATOM   11046 O  OD1 . ASP D 1 357 ? 34.668 30.854 60.689  1.00 137.28 ? 421 ASP D OD1 1 
ATOM   11047 O  OD2 . ASP D 1 357 ? 33.464 29.985 62.292  1.00 98.18  ? 421 ASP D OD2 1 
ATOM   11048 N  N   . LEU D 1 358 ? 35.153 29.876 58.108  1.00 56.71  ? 422 LEU D N   1 
ATOM   11049 C  CA  . LEU D 1 358 ? 36.295 29.884 57.214  1.00 48.14  ? 422 LEU D CA  1 
ATOM   11050 C  C   . LEU D 1 358 ? 37.394 28.970 57.668  1.00 45.60  ? 422 LEU D C   1 
ATOM   11051 O  O   . LEU D 1 358 ? 37.641 28.827 58.851  1.00 48.92  ? 422 LEU D O   1 
ATOM   11052 C  CB  . LEU D 1 358 ? 36.886 31.271 57.182  1.00 46.03  ? 422 LEU D CB  1 
ATOM   11053 C  CG  . LEU D 1 358 ? 36.250 32.147 56.147  1.00 48.03  ? 422 LEU D CG  1 
ATOM   11054 C  CD1 . LEU D 1 358 ? 37.236 33.248 55.817  1.00 49.59  ? 422 LEU D CD1 1 
ATOM   11055 C  CD2 . LEU D 1 358 ? 35.970 31.289 54.948  1.00 48.25  ? 422 LEU D CD2 1 
ATOM   11056 N  N   . ILE D 1 359 ? 38.059 28.357 56.709  1.00 44.29  ? 423 ILE D N   1 
ATOM   11057 C  CA  . ILE D 1 359 ? 39.333 27.733 56.948  1.00 42.29  ? 423 ILE D CA  1 
ATOM   11058 C  C   . ILE D 1 359 ? 40.211 28.241 55.831  1.00 45.63  ? 423 ILE D C   1 
ATOM   11059 O  O   . ILE D 1 359 ? 39.732 28.411 54.719  1.00 59.63  ? 423 ILE D O   1 
ATOM   11060 C  CB  . ILE D 1 359 ? 39.257 26.188 57.045  1.00 33.78  ? 423 ILE D CB  1 
ATOM   11061 C  CG1 . ILE D 1 359 ? 40.642 25.608 56.980  1.00 35.82  ? 423 ILE D CG1 1 
ATOM   11062 C  CG2 . ILE D 1 359 ? 38.527 25.620 55.954  1.00 36.61  ? 423 ILE D CG2 1 
ATOM   11063 C  CD1 . ILE D 1 359 ? 40.709 24.376 57.752  1.00 50.20  ? 423 ILE D CD1 1 
ATOM   11064 N  N   . THR D 1 360 ? 41.471 28.533 56.137  1.00 46.55  ? 424 THR D N   1 
ATOM   11065 C  CA  . THR D 1 360 ? 42.409 29.053 55.147  1.00 46.18  ? 424 THR D CA  1 
ATOM   11066 C  C   . THR D 1 360 ? 43.642 28.175 55.078  1.00 42.03  ? 424 THR D C   1 
ATOM   11067 O  O   . THR D 1 360 ? 44.086 27.638 56.090  1.00 57.41  ? 424 THR D O   1 
ATOM   11068 C  CB  . THR D 1 360 ? 42.841 30.499 55.488  1.00 50.36  ? 424 THR D CB  1 
ATOM   11069 O  OG1 . THR D 1 360 ? 43.907 30.467 56.431  1.00 56.93  ? 424 THR D OG1 1 
ATOM   11070 C  CG2 . THR D 1 360 ? 41.704 31.284 56.093  1.00 56.60  ? 424 THR D CG2 1 
ATOM   11071 N  N   . PHE D 1 361 ? 44.203 28.053 53.894  1.00 38.76  ? 425 PHE D N   1 
ATOM   11072 C  CA  . PHE D 1 361 ? 45.432 27.280 53.693  1.00 45.95  ? 425 PHE D CA  1 
ATOM   11073 C  C   . PHE D 1 361 ? 46.470 28.148 53.048  1.00 43.80  ? 425 PHE D C   1 
ATOM   11074 O  O   . PHE D 1 361 ? 46.136 29.005 52.232  1.00 50.67  ? 425 PHE D O   1 
ATOM   11075 C  CB  . PHE D 1 361 ? 45.156 26.065 52.779  1.00 43.60  ? 425 PHE D CB  1 
ATOM   11076 C  CG  . PHE D 1 361 ? 44.289 25.042 53.406  1.00 36.98  ? 425 PHE D CG  1 
ATOM   11077 C  CD1 . PHE D 1 361 ? 42.931 25.115 53.285  1.00 35.71  ? 425 PHE D CD1 1 
ATOM   11078 C  CD2 . PHE D 1 361 ? 44.844 24.040 54.191  1.00 36.61  ? 425 PHE D CD2 1 
ATOM   11079 C  CE1 . PHE D 1 361 ? 42.113 24.161 53.890  1.00 37.10  ? 425 PHE D CE1 1 
ATOM   11080 C  CE2 . PHE D 1 361 ? 44.041 23.079 54.803  1.00 35.81  ? 425 PHE D CE2 1 
ATOM   11081 C  CZ  . PHE D 1 361 ? 42.664 23.140 54.635  1.00 35.15  ? 425 PHE D CZ  1 
ATOM   11082 N  N   . CYS D 1 362 ? 47.727 27.916 53.375  1.00 47.03  ? 426 CYS D N   1 
ATOM   11083 C  CA  . CYS D 1 362 ? 48.791 28.593 52.647  1.00 62.42  ? 426 CYS D CA  1 
ATOM   11084 C  C   . CYS D 1 362 ? 49.715 27.597 52.042  1.00 58.39  ? 426 CYS D C   1 
ATOM   11085 O  O   . CYS D 1 362 ? 49.891 26.508 52.571  1.00 61.50  ? 426 CYS D O   1 
ATOM   11086 C  CB  . CYS D 1 362 ? 49.513 29.621 53.510  1.00 69.70  ? 426 CYS D CB  1 
ATOM   11087 S  SG  . CYS D 1 362 ? 48.305 30.968 53.879  1.00 124.80 ? 426 CYS D SG  1 
ATOM   11088 N  N   . GLY D 1 363 ? 50.265 27.959 50.900  1.00 55.66  ? 427 GLY D N   1 
ATOM   11089 C  CA  . GLY D 1 363 ? 51.169 27.072 50.202  1.00 62.95  ? 427 GLY D CA  1 
ATOM   11090 C  C   . GLY D 1 363 ? 52.557 27.020 50.803  1.00 63.08  ? 427 GLY D C   1 
ATOM   11091 O  O   . GLY D 1 363 ? 53.100 28.033 51.232  1.00 75.97  ? 427 GLY D O   1 
ATOM   11092 N  N   . THR D 1 364 ? 53.114 25.817 50.852  1.00 71.76  ? 428 THR D N   1 
ATOM   11093 C  CA  . THR D 1 364 ? 54.517 25.616 51.166  1.00 76.41  ? 428 THR D CA  1 
ATOM   11094 C  C   . THR D 1 364 ? 55.249 24.988 49.976  1.00 77.32  ? 428 THR D C   1 
ATOM   11095 O  O   . THR D 1 364 ? 54.635 24.325 49.102  1.00 60.19  ? 428 THR D O   1 
ATOM   11096 C  CB  . THR D 1 364 ? 54.731 24.789 52.461  1.00 83.43  ? 428 THR D CB  1 
ATOM   11097 O  OG1 . THR D 1 364 ? 56.124 24.781 52.779  1.00 108.65 ? 428 THR D OG1 1 
ATOM   11098 C  CG2 . THR D 1 364 ? 54.257 23.365 52.307  1.00 74.77  ? 428 THR D CG2 1 
ATOM   11099 N  N   . GLY D 1 365 ? 56.560 25.231 49.942  1.00 84.10  ? 429 GLY D N   1 
ATOM   11100 C  CA  . GLY D 1 365 ? 57.425 24.750 48.867  1.00 92.28  ? 429 GLY D CA  1 
ATOM   11101 C  C   . GLY D 1 365 ? 57.625 23.257 48.981  1.00 85.29  ? 429 GLY D C   1 
ATOM   11102 O  O   . GLY D 1 365 ? 57.849 22.570 47.979  1.00 80.65  ? 429 GLY D O   1 
ATOM   11103 N  N   . GLY D 1 366 ? 57.527 22.765 50.219  1.00 78.67  ? 430 GLY D N   1 
ATOM   11104 C  CA  . GLY D 1 366 ? 57.741 21.360 50.533  1.00 69.84  ? 430 GLY D CA  1 
ATOM   11105 C  C   . GLY D 1 366 ? 56.561 20.511 50.134  1.00 84.61  ? 430 GLY D C   1 
ATOM   11106 O  O   . GLY D 1 366 ? 55.432 20.991 50.033  1.00 89.35  ? 430 GLY D O   1 
ATOM   11107 N  N   . SER D 1 367 ? 56.819 19.239 49.872  1.00 91.27  ? 431 SER D N   1 
ATOM   11108 C  CA  . SER D 1 367 ? 55.724 18.315 49.720  1.00 77.84  ? 431 SER D CA  1 
ATOM   11109 C  C   . SER D 1 367 ? 55.124 18.095 51.106  1.00 70.35  ? 431 SER D C   1 
ATOM   11110 O  O   . SER D 1 367 ? 55.760 18.346 52.119  1.00 68.95  ? 431 SER D O   1 
ATOM   11111 C  CB  . SER D 1 367 ? 56.199 17.006 49.108  1.00 75.21  ? 431 SER D CB  1 
ATOM   11112 O  OG  . SER D 1 367 ? 55.099 16.117 48.952  1.00 98.34  ? 431 SER D OG  1 
ATOM   11113 N  N   . MET D 1 368 ? 53.878 17.666 51.152  1.00 71.50  ? 432 MET D N   1 
ATOM   11114 C  CA  . MET D 1 368 ? 53.218 17.452 52.421  1.00 61.21  ? 432 MET D CA  1 
ATOM   11115 C  C   . MET D 1 368 ? 52.516 16.106 52.440  1.00 72.15  ? 432 MET D C   1 
ATOM   11116 O  O   . MET D 1 368 ? 52.109 15.601 51.393  1.00 74.03  ? 432 MET D O   1 
ATOM   11117 C  CB  . MET D 1 368 ? 52.203 18.542 52.646  1.00 58.77  ? 432 MET D CB  1 
ATOM   11118 C  CG  . MET D 1 368 ? 52.829 19.846 53.068  1.00 68.51  ? 432 MET D CG  1 
ATOM   11119 S  SD  . MET D 1 368 ? 52.880 20.082 54.844  1.00 67.43  ? 432 MET D SD  1 
ATOM   11120 C  CE  . MET D 1 368 ? 51.262 19.466 55.344  1.00 62.85  ? 432 MET D CE  1 
ATOM   11121 N  N   . PRO D 1 369 ? 52.362 15.521 53.637  1.00 60.77  ? 433 PRO D N   1 
ATOM   11122 C  CA  . PRO D 1 369 ? 51.726 14.237 53.797  1.00 57.84  ? 433 PRO D CA  1 
ATOM   11123 C  C   . PRO D 1 369 ? 50.220 14.363 53.624  1.00 67.22  ? 433 PRO D C   1 
ATOM   11124 O  O   . PRO D 1 369 ? 49.700 15.470 53.623  1.00 70.46  ? 433 PRO D O   1 
ATOM   11125 C  CB  . PRO D 1 369 ? 52.030 13.900 55.235  1.00 56.06  ? 433 PRO D CB  1 
ATOM   11126 C  CG  . PRO D 1 369 ? 52.034 15.221 55.902  1.00 62.02  ? 433 PRO D CG  1 
ATOM   11127 C  CD  . PRO D 1 369 ? 52.737 16.099 54.935  1.00 64.85  ? 433 PRO D CD  1 
ATOM   11128 N  N   . ASP D 1 370 ? 49.541 13.228 53.472  1.00 74.78  ? 434 ASP D N   1 
ATOM   11129 C  CA  . ASP D 1 370 ? 48.100 13.189 53.310  1.00 70.95  ? 434 ASP D CA  1 
ATOM   11130 C  C   . ASP D 1 370 ? 47.479 13.464 54.640  1.00 68.68  ? 434 ASP D C   1 
ATOM   11131 O  O   . ASP D 1 370 ? 47.803 12.777 55.611  1.00 75.05  ? 434 ASP D O   1 
ATOM   11132 C  CB  . ASP D 1 370 ? 47.645 11.809 52.846  1.00 116.98 ? 434 ASP D CB  1 
ATOM   11133 C  CG  . ASP D 1 370 ? 48.111 11.476 51.442  1.00 151.24 ? 434 ASP D CG  1 
ATOM   11134 O  OD1 . ASP D 1 370 ? 48.344 12.409 50.647  1.00 161.21 ? 434 ASP D OD1 1 
ATOM   11135 O  OD2 . ASP D 1 370 ? 48.237 10.272 51.126  1.00 162.02 ? 434 ASP D OD2 1 
ATOM   11136 N  N   . VAL D 1 371 ? 46.598 14.472 54.683  1.00 65.07  ? 435 VAL D N   1 
ATOM   11137 C  CA  . VAL D 1 371 ? 45.925 14.877 55.926  1.00 57.01  ? 435 VAL D CA  1 
ATOM   11138 C  C   . VAL D 1 371 ? 44.506 15.258 55.647  1.00 57.71  ? 435 VAL D C   1 
ATOM   11139 O  O   . VAL D 1 371 ? 44.239 16.008 54.714  1.00 62.84  ? 435 VAL D O   1 
ATOM   11140 C  CB  . VAL D 1 371 ? 46.591 16.091 56.611  1.00 53.53  ? 435 VAL D CB  1 
ATOM   11141 C  CG1 . VAL D 1 371 ? 45.905 16.373 57.912  1.00 71.06  ? 435 VAL D CG1 1 
ATOM   11142 C  CG2 . VAL D 1 371 ? 48.091 15.837 56.863  1.00 60.57  ? 435 VAL D CG2 1 
ATOM   11143 N  N   . ASN D 1 372 ? 43.606 14.716 56.458  1.00 61.53  ? 436 ASN D N   1 
ATOM   11144 C  CA  . ASN D 1 372 ? 42.231 15.180 56.534  1.00 72.09  ? 436 ASN D CA  1 
ATOM   11145 C  C   . ASN D 1 372 ? 42.058 16.192 57.699  1.00 65.36  ? 436 ASN D C   1 
ATOM   11146 O  O   . ASN D 1 372 ? 42.074 15.804 58.866  1.00 80.07  ? 436 ASN D O   1 
ATOM   11147 C  CB  . ASN D 1 372 ? 41.295 13.968 56.695  1.00 73.66  ? 436 ASN D CB  1 
ATOM   11148 C  CG  . ASN D 1 372 ? 39.829 14.366 56.927  1.00 113.25 ? 436 ASN D CG  1 
ATOM   11149 O  OD1 . ASN D 1 372 ? 39.475 15.553 57.049  1.00 121.98 ? 436 ASN D OD1 1 
ATOM   11150 N  ND2 . ASN D 1 372 ? 38.968 13.361 56.985  1.00 127.99 ? 436 ASN D ND2 1 
ATOM   11151 N  N   . TRP D 1 373 ? 41.887 17.475 57.392  1.00 48.64  ? 437 TRP D N   1 
ATOM   11152 C  CA  . TRP D 1 373 ? 41.682 18.511 58.457  1.00 55.89  ? 437 TRP D CA  1 
ATOM   11153 C  C   . TRP D 1 373 ? 40.284 18.625 59.048  1.00 48.52  ? 437 TRP D C   1 
ATOM   11154 O  O   . TRP D 1 373 ? 39.303 18.121 58.478  1.00 51.47  ? 437 TRP D O   1 
ATOM   11155 C  CB  . TRP D 1 373 ? 42.156 19.892 57.979  1.00 48.58  ? 437 TRP D CB  1 
ATOM   11156 C  CG  . TRP D 1 373 ? 43.592 19.870 57.519  1.00 49.46  ? 437 TRP D CG  1 
ATOM   11157 C  CD1 . TRP D 1 373 ? 44.084 19.648 56.241  1.00 51.87  ? 437 TRP D CD1 1 
ATOM   11158 C  CD2 . TRP D 1 373 ? 44.766 20.019 58.343  1.00 44.81  ? 437 TRP D CD2 1 
ATOM   11159 N  NE1 . TRP D 1 373 ? 45.453 19.667 56.232  1.00 46.58  ? 437 TRP D NE1 1 
ATOM   11160 C  CE2 . TRP D 1 373 ? 45.922 19.883 57.446  1.00 46.35  ? 437 TRP D CE2 1 
ATOM   11161 C  CE3 . TRP D 1 373 ? 44.977 20.249 59.678  1.00 41.11  ? 437 TRP D CE3 1 
ATOM   11162 C  CZ2 . TRP D 1 373 ? 47.216 19.984 57.899  1.00 53.22  ? 437 TRP D CZ2 1 
ATOM   11163 C  CZ3 . TRP D 1 373 ? 46.292 20.321 60.138  1.00 47.53  ? 437 TRP D CZ3 1 
ATOM   11164 C  CH2 . TRP D 1 373 ? 47.387 20.195 59.267  1.00 52.40  ? 437 TRP D CH2 1 
HETATM 11165 C  C1  . NAG E 2 .   ? 66.532 38.090 61.635  1.00 61.88  ? 501 NAG A C1  1 
HETATM 11166 C  C2  . NAG E 2 .   ? 67.504 38.414 60.500  1.00 62.48  ? 501 NAG A C2  1 
HETATM 11167 C  C3  . NAG E 2 .   ? 68.184 39.794 60.617  1.00 78.88  ? 501 NAG A C3  1 
HETATM 11168 C  C4  . NAG E 2 .   ? 67.231 40.961 60.975  1.00 91.42  ? 501 NAG A C4  1 
HETATM 11169 C  C5  . NAG E 2 .   ? 66.322 40.497 62.118  1.00 67.44  ? 501 NAG A C5  1 
HETATM 11170 C  C6  . NAG E 2 .   ? 65.170 41.479 62.168  1.00 72.23  ? 501 NAG A C6  1 
HETATM 11171 C  C7  . NAG E 2 .   ? 68.071 36.219 59.566  1.00 76.04  ? 501 NAG A C7  1 
HETATM 11172 C  C8  . NAG E 2 .   ? 69.058 35.098 59.426  1.00 56.88  ? 501 NAG A C8  1 
HETATM 11173 N  N2  . NAG E 2 .   ? 68.433 37.295 60.312  1.00 63.93  ? 501 NAG A N2  1 
HETATM 11174 O  O3  . NAG E 2 .   ? 68.634 40.102 59.315  1.00 83.91  ? 501 NAG A O3  1 
HETATM 11175 O  O4  . NAG E 2 .   ? 67.835 42.287 61.151  1.00 80.99  ? 501 NAG A O4  1 
HETATM 11176 O  O5  . NAG E 2 .   ? 65.719 39.230 61.847  1.00 67.83  ? 501 NAG A O5  1 
HETATM 11177 O  O6  . NAG E 2 .   ? 64.317 40.967 63.165  1.00 113.73 ? 501 NAG A O6  1 
HETATM 11178 O  O7  . NAG E 2 .   ? 66.972 36.094 58.988  1.00 74.19  ? 501 NAG A O7  1 
HETATM 11179 CA CA  . CA  F 3 .   ? 57.440 8.783  86.179  1.00 64.09  ? 502 CA  A CA  1 
HETATM 11180 CA CA  . CA  G 3 .   ? 33.440 41.927 74.776  1.00 65.68  ? 503 CA  A CA  1 
HETATM 11181 C  C1  . NAG H 2 .   ? 42.195 76.261 74.132  1.00 88.97  ? 501 NAG B C1  1 
HETATM 11182 C  C2  . NAG H 2 .   ? 42.904 77.556 74.521  1.00 96.66  ? 501 NAG B C2  1 
HETATM 11183 C  C3  . NAG H 2 .   ? 44.084 77.823 73.605  1.00 102.46 ? 501 NAG B C3  1 
HETATM 11184 C  C4  . NAG H 2 .   ? 45.066 76.685 73.792  1.00 107.79 ? 501 NAG B C4  1 
HETATM 11185 C  C5  . NAG H 2 .   ? 44.372 75.414 73.295  1.00 104.05 ? 501 NAG B C5  1 
HETATM 11186 C  C6  . NAG H 2 .   ? 45.379 74.291 73.531  1.00 102.58 ? 501 NAG B C6  1 
HETATM 11187 C  C7  . NAG H 2 .   ? 41.527 79.230 75.646  1.00 106.70 ? 501 NAG B C7  1 
HETATM 11188 C  C8  . NAG H 2 .   ? 40.578 80.399 75.531  1.00 96.54  ? 501 NAG B C8  1 
HETATM 11189 N  N2  . NAG H 2 .   ? 41.996 78.687 74.515  1.00 103.33 ? 501 NAG B N2  1 
HETATM 11190 O  O3  . NAG H 2 .   ? 44.711 78.995 74.036  1.00 118.31 ? 501 NAG B O3  1 
HETATM 11191 O  O4  . NAG H 2 .   ? 46.331 76.942 73.178  1.00 102.93 ? 501 NAG B O4  1 
HETATM 11192 O  O5  . NAG H 2 .   ? 43.099 75.169 73.937  1.00 94.10  ? 501 NAG B O5  1 
HETATM 11193 O  O6  . NAG H 2 .   ? 44.803 73.078 73.134  1.00 125.97 ? 501 NAG B O6  1 
HETATM 11194 O  O7  . NAG H 2 .   ? 41.835 78.793 76.754  1.00 102.14 ? 501 NAG B O7  1 
HETATM 11195 CA CA  . CA  I 3 .   ? 4.284  71.389 65.625  1.00 42.96  ? 502 CA  B CA  1 
HETATM 11196 C  C1  . NAG J 2 .   ? 63.220 56.052 88.724  1.00 82.93  ? 501 NAG C C1  1 
HETATM 11197 C  C2  . NAG J 2 .   ? 64.740 56.374 88.761  1.00 81.61  ? 501 NAG C C2  1 
HETATM 11198 C  C3  . NAG J 2 .   ? 65.128 57.687 87.993  1.00 90.96  ? 501 NAG C C3  1 
HETATM 11199 C  C4  . NAG J 2 .   ? 64.496 57.783 86.589  1.00 103.51 ? 501 NAG C C4  1 
HETATM 11200 C  C5  . NAG J 2 .   ? 63.022 57.454 86.767  1.00 86.68  ? 501 NAG C C5  1 
HETATM 11201 C  C6  . NAG J 2 .   ? 62.360 57.446 85.410  1.00 92.61  ? 501 NAG C C6  1 
HETATM 11202 C  C7  . NAG J 2 .   ? 65.339 55.130 90.841  1.00 96.81  ? 501 NAG C C7  1 
HETATM 11203 C  C8  . NAG J 2 .   ? 65.900 55.207 92.231  1.00 75.44  ? 501 NAG C C8  1 
HETATM 11204 N  N2  . NAG J 2 .   ? 65.256 56.295 90.140  1.00 83.50  ? 501 NAG C N2  1 
HETATM 11205 O  O3  . NAG J 2 .   ? 66.517 57.878 87.792  1.00 79.32  ? 501 NAG C O3  1 
HETATM 11206 O  O4  . NAG J 2 .   ? 64.684 59.036 85.901  1.00 97.24  ? 501 NAG C O4  1 
HETATM 11207 O  O5  . NAG J 2 .   ? 62.865 56.164 87.352  1.00 78.46  ? 501 NAG C O5  1 
HETATM 11208 O  O6  . NAG J 2 .   ? 61.067 56.961 85.680  1.00 108.49 ? 501 NAG C O6  1 
HETATM 11209 O  O7  . NAG J 2 .   ? 64.982 54.007 90.429  1.00 101.78 ? 501 NAG C O7  1 
HETATM 11210 CA CA  . CA  K 3 .   ? 34.103 55.286 115.317 1.00 63.02  ? 502 CA  C CA  1 
HETATM 11211 C  C1  . NAG L 2 .   ? 46.173 58.771 45.845  1.00 114.97 ? 501 NAG D C1  1 
HETATM 11212 C  C2  . NAG L 2 .   ? 46.747 59.905 44.999  1.00 112.39 ? 501 NAG D C2  1 
HETATM 11213 C  C3  . NAG L 2 .   ? 48.294 59.968 45.104  1.00 126.09 ? 501 NAG D C3  1 
HETATM 11214 C  C4  . NAG L 2 .   ? 48.823 59.847 46.554  1.00 132.26 ? 501 NAG D C4  1 
HETATM 11215 C  C5  . NAG L 2 .   ? 48.053 58.726 47.281  1.00 126.58 ? 501 NAG D C5  1 
HETATM 11216 C  C6  . NAG L 2 .   ? 48.243 58.695 48.781  1.00 113.99 ? 501 NAG D C6  1 
HETATM 11217 C  C7  . NAG L 2 .   ? 45.245 60.331 43.080  1.00 105.66 ? 501 NAG D C7  1 
HETATM 11218 C  C8  . NAG L 2 .   ? 44.893 59.898 41.683  1.00 103.27 ? 501 NAG D C8  1 
HETATM 11219 N  N2  . NAG L 2 .   ? 46.252 59.661 43.656  1.00 104.02 ? 501 NAG D N2  1 
HETATM 11220 O  O3  . NAG L 2 .   ? 48.806 61.158 44.525  1.00 114.89 ? 501 NAG D O3  1 
HETATM 11221 O  O4  . NAG L 2 .   ? 50.244 59.653 46.575  1.00 116.99 ? 501 NAG D O4  1 
HETATM 11222 O  O5  . NAG L 2 .   ? 46.654 58.920 47.155  1.00 134.76 ? 501 NAG D O5  1 
HETATM 11223 O  O6  . NAG L 2 .   ? 47.055 58.098 49.267  1.00 112.88 ? 501 NAG D O6  1 
HETATM 11224 O  O7  . NAG L 2 .   ? 44.619 61.256 43.606  1.00 98.03  ? 501 NAG D O7  1 
HETATM 11225 CA CA  . CA  M 3 .   ? 28.478 25.160 36.105  1.00 68.23  ? 502 CA  D CA  1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1     N N   . ALA A 11  ? 1.0843 0.6573 0.8588 -0.0469 0.0634  0.0451  75  ALA A N   
2     C CA  . ALA A 11  ? 1.3072 0.9220 1.1131 -0.0478 0.0553  0.0388  75  ALA A CA  
3     C C   . ALA A 11  ? 1.4700 1.1065 1.3069 -0.0633 0.0642  0.0390  75  ALA A C   
4     O O   . ALA A 11  ? 1.1819 0.8096 1.0161 -0.0699 0.0782  0.0450  75  ALA A O   
5     C CB  . ALA A 11  ? 0.8598 0.4889 0.6561 -0.0318 0.0499  0.0381  75  ALA A CB  
6     N N   . THR A 12  ? 1.7586 1.4241 1.6243 -0.0681 0.0558  0.0320  76  THR A N   
7     C CA  . THR A 12  ? 1.4879 1.1761 1.3849 -0.0818 0.0614  0.0298  76  THR A CA  
8     C C   . THR A 12  ? 1.1543 0.8760 1.0692 -0.0763 0.0540  0.0253  76  THR A C   
9     O O   . THR A 12  ? 1.3783 1.1078 1.2917 -0.0681 0.0416  0.0207  76  THR A O   
10    C CB  . THR A 12  ? 1.7079 1.3946 1.6228 -0.0945 0.0576  0.0242  76  THR A CB  
11    O OG1 . THR A 12  ? 1.8122 1.4642 1.7083 -0.1004 0.0650  0.0286  76  THR A OG1 
12    C CG2 . THR A 12  ? 1.6373 1.3512 1.5874 -0.1081 0.0621  0.0200  76  THR A CG2 
13    N N   . PRO A 13  ? 1.0822 0.8230 1.0133 -0.0808 0.0618  0.0264  77  PRO A N   
14    C CA  . PRO A 13  ? 0.9877 0.7584 0.9348 -0.0760 0.0552  0.0220  77  PRO A CA  
15    C C   . PRO A 13  ? 1.0476 0.8327 1.0109 -0.0769 0.0421  0.0138  77  PRO A C   
16    O O   . PRO A 13  ? 1.2307 1.0172 1.2100 -0.0868 0.0410  0.0098  77  PRO A O   
17    C CB  . PRO A 13  ? 0.8264 0.6136 0.7937 -0.0848 0.0660  0.0228  77  PRO A CB  
18    C CG  . PRO A 13  ? 0.9326 0.6968 0.8856 -0.0900 0.0806  0.0304  77  PRO A CG  
19    C CD  . PRO A 13  ? 1.0706 0.8059 1.0063 -0.0913 0.0777  0.0314  77  PRO A CD  
20    N N   . LEU A 14  ? 1.0099 0.8046 0.9682 -0.0666 0.0324  0.0112  78  LEU A N   
21    C CA  . LEU A 14  ? 1.0008 0.8080 0.9708 -0.0657 0.0206  0.0040  78  LEU A CA  
22    C C   . LEU A 14  ? 1.0741 0.9032 1.0706 -0.0728 0.0202  -0.0010 78  LEU A C   
23    O O   . LEU A 14  ? 1.0598 0.9046 1.0641 -0.0714 0.0238  -0.0006 78  LEU A O   
24    C CB  . LEU A 14  ? 1.0719 0.8862 1.0317 -0.0544 0.0130  0.0026  78  LEU A CB  
25    C CG  . LEU A 14  ? 1.2416 1.0652 1.2090 -0.0526 0.0017  -0.0041 78  LEU A CG  
26    C CD1 . LEU A 14  ? 1.7198 1.5269 1.6760 -0.0509 -0.0037 -0.0053 78  LEU A CD1 
27    C CD2 . LEU A 14  ? 1.4833 1.3187 1.4464 -0.0447 -0.0029 -0.0057 78  LEU A CD2 
28    N N   . VAL A 15  ? 1.2507 1.0803 1.2604 -0.0795 0.0153  -0.0064 79  VAL A N   
29    C CA  . VAL A 15  ? 1.1045 0.9557 1.1400 -0.0849 0.0122  -0.0134 79  VAL A CA  
30    C C   . VAL A 15  ? 1.1618 1.0181 1.1984 -0.0791 -0.0014 -0.0201 79  VAL A C   
31    O O   . VAL A 15  ? 1.3206 1.1624 1.3479 -0.0781 -0.0072 -0.0213 79  VAL A O   
32    C CB  . VAL A 15  ? 0.9177 0.7668 0.9703 -0.0988 0.0181  -0.0157 79  VAL A CB  
33    C CG1 . VAL A 15  ? 0.9772 0.8404 1.0516 -0.1027 0.0080  -0.0260 79  VAL A CG1 
34    C CG2 . VAL A 15  ? 0.6555 0.5147 0.7192 -0.1052 0.0314  -0.0123 79  VAL A CG2 
35    N N   . LEU A 16  ? 1.1160 0.9914 1.1620 -0.0743 -0.0062 -0.0242 80  LEU A N   
36    C CA  . LEU A 16  ? 1.0714 0.9511 1.1173 -0.0683 -0.0182 -0.0305 80  LEU A CA  
37    C C   . LEU A 16  ? 1.0447 0.9366 1.1128 -0.0736 -0.0236 -0.0392 80  LEU A C   
38    O O   . LEU A 16  ? 0.9625 0.8678 1.0495 -0.0804 -0.0181 -0.0412 80  LEU A O   
39    C CB  . LEU A 16  ? 1.0077 0.8969 1.0463 -0.0588 -0.0207 -0.0301 80  LEU A CB  
40    C CG  . LEU A 16  ? 1.0515 0.9302 1.0688 -0.0529 -0.0182 -0.0238 80  LEU A CG  
41    C CD1 . LEU A 16  ? 1.4090 1.2974 1.4222 -0.0466 -0.0183 -0.0234 80  LEU A CD1 
42    C CD2 . LEU A 16  ? 1.1514 1.0179 1.1553 -0.0489 -0.0248 -0.0248 80  LEU A CD2 
43    N N   . GLY A 17  ? 0.8323 0.7206 0.8985 -0.0700 -0.0344 -0.0449 81  GLY A N   
44    C CA  . GLY A 17  ? 0.9901 0.8906 1.0758 -0.0722 -0.0425 -0.0549 81  GLY A CA  
45    C C   . GLY A 17  ? 0.9583 0.8807 1.0557 -0.0668 -0.0454 -0.0600 81  GLY A C   
46    O O   . GLY A 17  ? 0.7757 0.6996 0.8599 -0.0572 -0.0471 -0.0577 81  GLY A O   
47    N N   . GLU A 18  ? 0.9904 0.9295 1.1124 -0.0729 -0.0460 -0.0674 82  GLU A N   
48    C CA  . GLU A 18  ? 0.9905 0.9516 1.1245 -0.0669 -0.0490 -0.0733 82  GLU A CA  
49    C C   . GLU A 18  ? 1.0677 1.0301 1.1952 -0.0553 -0.0629 -0.0807 82  GLU A C   
50    O O   . GLU A 18  ? 1.1451 1.1153 1.2665 -0.0450 -0.0661 -0.0822 82  GLU A O   
51    C CB  . GLU A 18  ? 0.8234 0.8050 0.9877 -0.0768 -0.0455 -0.0802 82  GLU A CB  
52    C CG  . GLU A 18  ? 1.2062 1.2084 1.3799 -0.0736 -0.0396 -0.0802 82  GLU A CG  
53    C CD  . GLU A 18  ? 1.4439 1.4378 1.6053 -0.0762 -0.0259 -0.0682 82  GLU A CD  
54    O OE1 . GLU A 18  ? 1.4035 1.3792 1.5560 -0.0839 -0.0185 -0.0608 82  GLU A OE1 
55    O OE2 . GLU A 18  ? 1.6254 1.6300 1.7845 -0.0693 -0.0229 -0.0666 82  GLU A OE2 
56    N N   . ASN A 19  ? 0.9888 0.9408 1.1144 -0.0562 -0.0709 -0.0850 83  ASN A N   
57    C CA  . ASN A 19  ? 0.9748 0.9258 1.0931 -0.0450 -0.0841 -0.0925 83  ASN A CA  
58    C C   . ASN A 19  ? 0.9463 0.8763 1.0365 -0.0377 -0.0864 -0.0865 83  ASN A C   
59    O O   . ASN A 19  ? 0.9007 0.8158 0.9830 -0.0428 -0.0832 -0.0815 83  ASN A O   
60    C CB  . ASN A 19  ? 1.1227 1.0803 1.2609 -0.0497 -0.0931 -0.1040 83  ASN A CB  
61    C CG  . ASN A 19  ? 1.4287 1.4129 1.5969 -0.0547 -0.0928 -0.1128 83  ASN A CG  
62    O OD1 . ASN A 19  ? 1.4067 1.4058 1.5776 -0.0483 -0.0910 -0.1133 83  ASN A OD1 
63    N ND2 . ASN A 19  ? 1.4103 1.4007 1.6013 -0.0661 -0.0943 -0.1202 83  ASN A ND2 
64    N N   . LEU A 20  ? 0.8977 0.8264 0.9724 -0.0254 -0.0913 -0.0873 84  LEU A N   
65    C CA  . LEU A 20  ? 0.6828 0.5941 0.7319 -0.0185 -0.0925 -0.0823 84  LEU A CA  
66    C C   . LEU A 20  ? 0.7954 0.6973 0.8388 -0.0139 -0.1031 -0.0886 84  LEU A C   
67    O O   . LEU A 20  ? 0.8237 0.7334 0.8777 -0.0102 -0.1126 -0.0984 84  LEU A O   
68    C CB  . LEU A 20  ? 0.6307 0.5423 0.6644 -0.0083 -0.0924 -0.0807 84  LEU A CB  
69    C CG  . LEU A 20  ? 0.7363 0.6352 0.7482 -0.0068 -0.0851 -0.0713 84  LEU A CG  
70    C CD1 . LEU A 20  ? 0.7789 0.6802 0.7964 -0.0158 -0.0744 -0.0637 84  LEU A CD1 
71    C CD2 . LEU A 20  ? 0.6518 0.5481 0.6475 0.0030  -0.0859 -0.0710 84  LEU A CD2 
72    N N   . CYS A 21  ? 1.0136 0.8998 1.0405 -0.0133 -0.1017 -0.0836 85  CYS A N   
73    C CA  . CYS A 21  ? 1.0456 0.9208 1.0618 -0.0067 -0.1110 -0.0883 85  CYS A CA  
74    C C   . CYS A 21  ? 1.2882 1.1631 1.2912 0.0062  -0.1174 -0.0924 85  CYS A C   
75    O O   . CYS A 21  ? 1.8388 1.7143 1.8310 0.0102  -0.1121 -0.0877 85  CYS A O   
76    C CB  . CYS A 21  ? 1.3939 1.2544 1.3922 -0.0065 -0.1066 -0.0813 85  CYS A CB  
77    S SG  . CYS A 21  ? 2.9023 2.7558 2.9100 -0.0181 -0.1032 -0.0790 85  CYS A SG  
78    N N   . SER A 22  ? 1.0331 0.9055 1.0354 0.0131  -0.1289 -0.1012 86  SER A N   
79    C CA  . SER A 22  ? 1.0202 0.8866 1.0035 0.0273  -0.1352 -0.1045 86  SER A CA  
80    C C   . SER A 22  ? 1.1005 0.9513 1.0584 0.0314  -0.1299 -0.0970 86  SER A C   
81    O O   . SER A 22  ? 1.0990 0.9421 1.0538 0.0285  -0.1295 -0.0951 86  SER A O   
82    C CB  . SER A 22  ? 1.1205 0.9869 1.1077 0.0347  -0.1494 -0.1163 86  SER A CB  
83    O OG  . SER A 22  ? 1.9864 1.8706 1.9998 0.0306  -0.1546 -0.1249 86  SER A OG  
84    N N   . ILE A 23  ? 1.0942 0.9404 1.0343 0.0380  -0.1252 -0.0928 87  ILE A N   
85    C CA  . ILE A 23  ? 0.8640 0.6977 0.7815 0.0409  -0.1186 -0.0860 87  ILE A CA  
86    C C   . ILE A 23  ? 0.9007 0.7229 0.7958 0.0547  -0.1241 -0.0896 87  ILE A C   
87    O O   . ILE A 23  ? 0.8376 0.6595 0.7268 0.0614  -0.1262 -0.0919 87  ILE A O   
88    C CB  . ILE A 23  ? 0.9012 0.7375 0.8161 0.0344  -0.1063 -0.0773 87  ILE A CB  
89    C CG1 . ILE A 23  ? 1.1365 0.9810 1.0693 0.0225  -0.1012 -0.0736 87  ILE A CG1 
90    C CG2 . ILE A 23  ? 0.9457 0.7709 0.8376 0.0375  -0.0991 -0.0716 87  ILE A CG2 
91    C CD1 . ILE A 23  ? 1.3207 1.1744 1.2633 0.0161  -0.0940 -0.0694 87  ILE A CD1 
92    N N   . ASN A 24  ? 0.7933 0.6049 0.6745 0.0602  -0.1267 -0.0904 88  ASN A N   
93    C CA  . ASN A 24  ? 0.8974 0.6947 0.7524 0.0737  -0.1296 -0.0923 88  ASN A CA  
94    C C   . ASN A 24  ? 0.8327 0.6193 0.6663 0.0746  -0.1197 -0.0852 88  ASN A C   
95    O O   . ASN A 24  ? 0.7696 0.5426 0.5788 0.0848  -0.1191 -0.0851 88  ASN A O   
96    C CB  . ASN A 24  ? 1.0019 0.7956 0.8567 0.0834  -0.1440 -0.1023 88  ASN A CB  
97    C CG  . ASN A 24  ? 1.2425 1.0475 1.1155 0.0851  -0.1541 -0.1111 88  ASN A CG  
98    O OD1 . ASN A 24  ? 1.0630 0.8657 0.9259 0.0944  -0.1570 -0.1139 88  ASN A OD1 
99    N ND2 . ASN A 24  ? 1.3372 1.1546 1.2370 0.0760  -0.1591 -0.1158 88  ASN A ND2 
100   N N   . GLY A 25  ? 0.7105 0.5036 0.5531 0.0642  -0.1116 -0.0796 89  GLY A N   
101   C CA  . GLY A 25  ? 0.7025 0.4904 0.5296 0.0637  -0.1019 -0.0739 89  GLY A CA  
102   C C   . GLY A 25  ? 0.7498 0.5483 0.5895 0.0518  -0.0927 -0.0681 89  GLY A C   
103   O O   . GLY A 25  ? 0.6442 0.4521 0.5028 0.0440  -0.0930 -0.0675 89  GLY A O   
104   N N   . TRP A 26  ? 0.6900 0.4877 0.5192 0.0509  -0.0840 -0.0642 90  TRP A N   
105   C CA  . TRP A 26  ? 0.5804 0.3887 0.4201 0.0413  -0.0761 -0.0599 90  TRP A CA  
106   C C   . TRP A 26  ? 0.7027 0.5129 0.5366 0.0434  -0.0734 -0.0599 90  TRP A C   
107   O O   . TRP A 26  ? 0.7014 0.5060 0.5186 0.0494  -0.0699 -0.0601 90  TRP A O   
108   C CB  . TRP A 26  ? 0.6114 0.4208 0.4462 0.0360  -0.0658 -0.0554 90  TRP A CB  
109   C CG  . TRP A 26  ? 0.6737 0.4808 0.5120 0.0356  -0.0684 -0.0555 90  TRP A CG  
110   C CD1 . TRP A 26  ? 0.7310 0.5264 0.5540 0.0427  -0.0702 -0.0568 90  TRP A CD1 
111   C CD2 . TRP A 26  ? 0.6418 0.4583 0.4988 0.0289  -0.0696 -0.0548 90  TRP A CD2 
112   N NE1 . TRP A 26  ? 0.7525 0.5508 0.5842 0.0414  -0.0731 -0.0575 90  TRP A NE1 
113   C CE2 . TRP A 26  ? 0.7453 0.5569 0.5983 0.0328  -0.0725 -0.0563 90  TRP A CE2 
114   C CE3 . TRP A 26  ? 0.6533 0.4802 0.5273 0.0214  -0.0685 -0.0532 90  TRP A CE3 
115   C CZ2 . TRP A 26  ? 0.6015 0.4214 0.4697 0.0287  -0.0738 -0.0563 90  TRP A CZ2 
116   C CZ3 . TRP A 26  ? 0.6296 0.4628 0.5176 0.0169  -0.0692 -0.0527 90  TRP A CZ3 
117   C CH2 . TRP A 26  ? 0.5197 0.3507 0.4058 0.0203  -0.0717 -0.0544 90  TRP A CH2 
118   N N   . VAL A 27  ? 0.6362 0.4539 0.4827 0.0392  -0.0747 -0.0597 91  VAL A N   
119   C CA  . VAL A 27  ? 0.6787 0.5005 0.5203 0.0416  -0.0719 -0.0600 91  VAL A CA  
120   C C   . VAL A 27  ? 0.6517 0.4855 0.5030 0.0342  -0.0650 -0.0571 91  VAL A C   
121   O O   . VAL A 27  ? 0.6806 0.5170 0.5443 0.0283  -0.0662 -0.0555 91  VAL A O   
122   C CB  . VAL A 27  ? 0.7110 0.5269 0.5521 0.0479  -0.0817 -0.0640 91  VAL A CB  
123   C CG1 . VAL A 27  ? 0.8742 0.6795 0.7133 0.0527  -0.0914 -0.0680 91  VAL A CG1 
124   C CG2 . VAL A 27  ? 0.7030 0.5222 0.5571 0.0426  -0.0839 -0.0634 91  VAL A CG2 
125   N N   . PRO A 28  ? 0.6274 0.4691 0.4730 0.0347  -0.0574 -0.0567 92  PRO A N   
126   C CA  . PRO A 28  ? 0.7162 0.5709 0.5706 0.0288  -0.0515 -0.0555 92  PRO A CA  
127   C C   . PRO A 28  ? 0.7460 0.6023 0.6064 0.0314  -0.0576 -0.0569 92  PRO A C   
128   O O   . PRO A 28  ? 0.7922 0.6434 0.6463 0.0387  -0.0633 -0.0597 92  PRO A O   
129   C CB  . PRO A 28  ? 0.6301 0.4935 0.4769 0.0301  -0.0431 -0.0567 92  PRO A CB  
130   C CG  . PRO A 28  ? 0.7191 0.5735 0.5527 0.0393  -0.0467 -0.0589 92  PRO A CG  
131   C CD  . PRO A 28  ? 0.5980 0.4375 0.4289 0.0413  -0.0542 -0.0584 92  PRO A CD  
132   N N   . THR A 29  ? 0.7450 0.6060 0.6153 0.0259  -0.0566 -0.0549 93  THR A N   
133   C CA  . THR A 29  ? 0.7018 0.5610 0.5746 0.0283  -0.0612 -0.0556 93  THR A CA  
134   C C   . THR A 29  ? 0.7945 0.6678 0.6685 0.0291  -0.0565 -0.0568 93  THR A C   
135   O O   . THR A 29  ? 0.9022 0.7749 0.7740 0.0342  -0.0600 -0.0583 93  THR A O   
136   C CB  . THR A 29  ? 0.6704 0.5217 0.5519 0.0225  -0.0640 -0.0526 93  THR A CB  
137   O OG1 . THR A 29  ? 0.6882 0.5455 0.5768 0.0154  -0.0583 -0.0496 93  THR A OG1 
138   C CG2 . THR A 29  ? 0.7891 0.6283 0.6713 0.0230  -0.0708 -0.0537 93  THR A CG2 
139   N N   . TYR A 30  ? 0.6534 0.5387 0.5306 0.0243  -0.0489 -0.0566 94  TYR A N   
140   C CA  . TYR A 30  ? 0.6100 0.5116 0.4906 0.0248  -0.0448 -0.0594 94  TYR A CA  
141   C C   . TYR A 30  ? 0.7686 0.6826 0.6511 0.0194  -0.0359 -0.0606 94  TYR A C   
142   O O   . TYR A 30  ? 0.6555 0.5640 0.5375 0.0128  -0.0316 -0.0577 94  TYR A O   
143   C CB  . TYR A 30  ? 0.6693 0.5723 0.5566 0.0213  -0.0450 -0.0575 94  TYR A CB  
144   C CG  . TYR A 30  ? 0.9393 0.8607 0.8313 0.0214  -0.0412 -0.0614 94  TYR A CG  
145   C CD1 . TYR A 30  ? 0.7899 0.7194 0.6792 0.0302  -0.0446 -0.0661 94  TYR A CD1 
146   C CD2 . TYR A 30  ? 1.0189 0.9495 0.9178 0.0131  -0.0348 -0.0611 94  TYR A CD2 
147   C CE1 . TYR A 30  ? 0.8608 0.8092 0.7558 0.0311  -0.0421 -0.0711 94  TYR A CE1 
148   C CE2 . TYR A 30  ? 0.8803 0.8290 0.7853 0.0128  -0.0321 -0.0660 94  TYR A CE2 
149   C CZ  . TYR A 30  ? 0.9472 0.9058 0.8510 0.0219  -0.0360 -0.0713 94  TYR A CZ  
150   O OH  . TYR A 30  ? 1.1707 1.1496 1.0817 0.0225  -0.0343 -0.0776 94  TYR A OH  
151   N N   . ARG A 31  ? 0.7468 0.6775 0.6313 0.0221  -0.0330 -0.0655 95  ARG A N   
152   C CA  . ARG A 31  ? 0.8525 0.7972 0.7402 0.0162  -0.0235 -0.0679 95  ARG A CA  
153   C C   . ARG A 31  ? 1.1221 1.0895 1.0190 0.0173  -0.0219 -0.0742 95  ARG A C   
154   O O   . ARG A 31  ? 0.8082 0.7838 0.7037 0.0269  -0.0263 -0.0787 95  ARG A O   
155   C CB  . ARG A 31  ? 0.7577 0.6991 0.6357 0.0197  -0.0205 -0.0686 95  ARG A CB  
156   C CG  . ARG A 31  ? 0.9151 0.8711 0.7949 0.0142  -0.0095 -0.0716 95  ARG A CG  
157   C CD  . ARG A 31  ? 1.0893 1.0365 0.9557 0.0181  -0.0058 -0.0706 95  ARG A CD  
158   N NE  . ARG A 31  ? 0.9918 0.9406 0.8525 0.0304  -0.0120 -0.0737 95  ARG A NE  
159   C CZ  . ARG A 31  ? 0.9103 0.8569 0.7599 0.0360  -0.0087 -0.0747 95  ARG A CZ  
160   N NH1 . ARG A 31  ? 0.9462 0.8878 0.7883 0.0302  0.0016  -0.0724 95  ARG A NH1 
161   N NH2 . ARG A 31  ? 1.0875 1.0349 0.9314 0.0481  -0.0154 -0.0778 95  ARG A NH2 
162   N N   . GLY A 32  ? 1.2317 1.2087 1.1374 0.0082  -0.0163 -0.0751 96  GLY A N   
163   C CA  . GLY A 32  ? 1.1280 1.1283 1.0445 0.0082  -0.0150 -0.0822 96  GLY A CA  
164   C C   . GLY A 32  ? 0.8503 0.8705 0.7700 0.0094  -0.0091 -0.0889 96  GLY A C   
165   O O   . GLY A 32  ? 0.7611 0.7761 0.6748 0.0065  -0.0029 -0.0869 96  GLY A O   
166   N N   . GLU A 33  ? 0.9164 0.9598 0.8451 0.0145  -0.0110 -0.0972 97  GLU A N   
167   C CA  . GLU A 33  ? 1.0980 1.1638 1.0316 0.0166  -0.0054 -0.1045 97  GLU A CA  
168   C C   . GLU A 33  ? 1.0695 1.1487 1.0131 0.0019  0.0073  -0.1071 97  GLU A C   
169   O O   . GLU A 33  ? 0.9375 1.0302 0.8832 0.0001  0.0155  -0.1109 97  GLU A O   
170   C CB  . GLU A 33  ? 1.1188 1.2066 1.0586 0.0286  -0.0122 -0.1138 97  GLU A CB  
171   C CG  . GLU A 33  ? 1.6613 1.7631 1.5983 0.0384  -0.0111 -0.1193 97  GLU A CG  
172   C CD  . GLU A 33  ? 1.5557 1.6324 1.4744 0.0479  -0.0166 -0.1128 97  GLU A CD  
173   O OE1 . GLU A 33  ? 1.6302 1.6845 1.5396 0.0530  -0.0257 -0.1075 97  GLU A OE1 
174   O OE2 . GLU A 33  ? 1.3344 1.4139 1.2480 0.0502  -0.0116 -0.1135 97  GLU A OE2 
175   N N   . GLY A 34  ? 1.0811 1.1544 1.0294 -0.0087 0.0093  -0.1047 98  GLY A N   
176   C CA  . GLY A 34  ? 1.1132 1.1926 1.0682 -0.0243 0.0214  -0.1061 98  GLY A CA  
177   C C   . GLY A 34  ? 0.9334 0.9881 0.8739 -0.0312 0.0293  -0.0975 98  GLY A C   
178   O O   . GLY A 34  ? 0.7693 0.8230 0.7109 -0.0443 0.0405  -0.0974 98  GLY A O   
179   N N   . THR A 35  ? 0.7308 0.7642 0.6566 -0.0222 0.0235  -0.0907 99  THR A N   
180   C CA  . THR A 35  ? 0.7592 0.7677 0.6693 -0.0260 0.0288  -0.0830 99  THR A CA  
181   C C   . THR A 35  ? 0.8373 0.8509 0.7408 -0.0242 0.0373  -0.0848 99  THR A C   
182   O O   . THR A 35  ? 0.9230 0.9176 0.8113 -0.0269 0.0440  -0.0796 99  THR A O   
183   C CB  . THR A 35  ? 0.7616 0.7463 0.6602 -0.0171 0.0182  -0.0762 99  THR A CB  
184   O OG1 . THR A 35  ? 0.8623 0.8511 0.7582 -0.0045 0.0112  -0.0783 99  THR A OG1 
185   C CG2 . THR A 35  ? 0.9346 0.9159 0.8399 -0.0176 0.0102  -0.0746 99  THR A CG2 
186   N N   . THR A 36  ? 0.8572 0.8963 0.7707 -0.0184 0.0368  -0.0924 100 THR A N   
187   C CA  . THR A 36  ? 1.0913 1.1390 0.9994 -0.0145 0.0443  -0.0949 100 THR A CA  
188   C C   . THR A 36  ? 1.1257 1.2076 1.0521 -0.0213 0.0537  -0.1048 100 THR A C   
189   O O   . THR A 36  ? 1.4093 1.4947 1.3354 -0.0323 0.0681  -0.1053 100 THR A O   
190   C CB  . THR A 36  ? 1.0601 1.1042 0.9595 0.0031  0.0333  -0.0951 100 THR A CB  
191   O OG1 . THR A 36  ? 1.4489 1.5046 1.3584 0.0106  0.0216  -0.0994 100 THR A OG1 
192   C CG2 . THR A 36  ? 0.8807 0.8918 0.7615 0.0082  0.0270  -0.0864 100 THR A CG2 
193   N N   . GLY A 37  ? 1.1364 1.2432 1.0781 -0.0147 0.0458  -0.1129 101 GLY A N   
194   C CA  . GLY A 37  ? 1.0427 1.1863 1.0054 -0.0204 0.0525  -0.1243 101 GLY A CA  
195   C C   . GLY A 37  ? 1.0481 1.2002 1.0263 -0.0328 0.0529  -0.1279 101 GLY A C   
196   O O   . GLY A 37  ? 1.1733 1.3013 1.1445 -0.0393 0.0513  -0.1205 101 GLY A O   
197   N N   . LYS A 38  ? 0.8922 1.0799 0.8918 -0.0352 0.0547  -0.1400 102 LYS A N   
198   C CA  . LYS A 38  ? 0.7963 0.9962 0.8122 -0.0449 0.0531  -0.1458 102 LYS A CA  
199   C C   . LYS A 38  ? 0.8558 1.0599 0.8745 -0.0310 0.0364  -0.1491 102 LYS A C   
200   O O   . LYS A 38  ? 1.0350 1.2403 1.0468 -0.0142 0.0270  -0.1497 102 LYS A O   
201   C CB  . LYS A 38  ? 0.8760 1.1140 0.9151 -0.0553 0.0636  -0.1589 102 LYS A CB  
202   C CG  . LYS A 38  ? 1.0112 1.2428 1.0480 -0.0728 0.0821  -0.1557 102 LYS A CG  
203   C CD  . LYS A 38  ? 1.4013 1.6683 1.4645 -0.0878 0.0919  -0.1690 102 LYS A CD  
204   C CE  . LYS A 38  ? 1.2930 1.5441 1.3525 -0.1099 0.1094  -0.1645 102 LYS A CE  
205   N NZ  . LYS A 38  ? 1.5768 1.8590 1.6637 -0.1261 0.1158  -0.1779 102 LYS A NZ  
206   N N   . ILE A 39  ? 0.7700 0.9748 0.7970 -0.0378 0.0329  -0.1513 103 ILE A N   
207   C CA  . ILE A 39  ? 0.7021 0.9060 0.7281 -0.0248 0.0180  -0.1530 103 ILE A CA  
208   C C   . ILE A 39  ? 0.8846 1.1274 0.9301 -0.0187 0.0133  -0.1688 103 ILE A C   
209   O O   . ILE A 39  ? 0.9816 1.2496 1.0465 -0.0312 0.0207  -0.1784 103 ILE A O   
210   C CB  . ILE A 39  ? 0.6478 0.8302 0.6699 -0.0325 0.0155  -0.1469 103 ILE A CB  
211   C CG1 . ILE A 39  ? 0.6944 0.8432 0.7008 -0.0418 0.0226  -0.1336 103 ILE A CG1 
212   C CG2 . ILE A 39  ? 0.4875 0.6619 0.5030 -0.0177 0.0008  -0.1460 103 ILE A CG2 
213   C CD1 . ILE A 39  ? 0.6670 0.7854 0.6552 -0.0321 0.0141  -0.1224 103 ILE A CD1 
214   N N   . PRO A 40  ? 0.9869 1.2343 1.0269 0.0007  0.0007  -0.1721 104 PRO A N   
215   C CA  . PRO A 40  ? 1.0700 1.3520 1.1254 0.0106  -0.0069 -0.1876 104 PRO A CA  
216   C C   . PRO A 40  ? 0.9529 1.2410 1.0191 0.0039  -0.0107 -0.1930 104 PRO A C   
217   O O   . PRO A 40  ? 1.1421 1.4018 1.1960 0.0027  -0.0148 -0.1836 104 PRO A O   
218   C CB  . PRO A 40  ? 1.1798 1.4494 1.2174 0.0332  -0.0204 -0.1854 104 PRO A CB  
219   C CG  . PRO A 40  ? 1.0453 1.2850 1.0641 0.0340  -0.0170 -0.1721 104 PRO A CG  
220   C CD  . PRO A 40  ? 0.7758 0.9957 0.7938 0.0148  -0.0066 -0.1621 104 PRO A CD  
221   N N   . ASP A 41  ? 0.9811 1.3071 1.0704 0.0004  -0.0098 -0.2087 105 ASP A N   
222   C CA  . ASP A 41  ? 1.0455 1.3797 1.1474 -0.0085 -0.0121 -0.2154 105 ASP A CA  
223   C C   . ASP A 41  ? 1.0200 1.3401 1.1094 0.0071  -0.0271 -0.2145 105 ASP A C   
224   O O   . ASP A 41  ? 1.3498 1.6605 1.4403 0.0001  -0.0290 -0.2138 105 ASP A O   
225   C CB  . ASP A 41  ? 1.2369 1.6187 1.3688 -0.0150 -0.0087 -0.2347 105 ASP A CB  
226   C CG  . ASP A 41  ? 1.4210 1.8163 1.5652 -0.0323 0.0085  -0.2354 105 ASP A CG  
227   O OD1 . ASP A 41  ? 1.9851 2.3585 2.1130 -0.0316 0.0148  -0.2232 105 ASP A OD1 
228   O OD2 . ASP A 41  ? 1.3509 1.7778 1.5202 -0.0465 0.0161  -0.2482 105 ASP A OD2 
229   N N   . GLU A 42  ? 0.8622 1.1787 0.9378 0.0284  -0.0373 -0.2144 106 GLU A N   
230   C CA  . GLU A 42  ? 1.1170 1.4186 1.1777 0.0446  -0.0509 -0.2137 106 GLU A CA  
231   C C   . GLU A 42  ? 1.1872 1.4439 1.2260 0.0419  -0.0508 -0.1957 106 GLU A C   
232   O O   . GLU A 42  ? 1.3596 1.6012 1.3869 0.0506  -0.0591 -0.1937 106 GLU A O   
233   C CB  . GLU A 42  ? 1.2320 1.5418 1.2824 0.0692  -0.0620 -0.2200 106 GLU A CB  
234   C CG  . GLU A 42  ? 1.7309 2.0168 1.7617 0.0768  -0.0609 -0.2085 106 GLU A CG  
235   C CD  . GLU A 42  ? 2.0348 2.3491 2.0766 0.0796  -0.0566 -0.2168 106 GLU A CD  
236   O OE1 . GLU A 42  ? 1.6195 1.9596 1.6835 0.0637  -0.0460 -0.2230 106 GLU A OE1 
237   O OE2 . GLU A 42  ? 2.3233 2.6331 2.3505 0.0980  -0.0635 -0.2173 106 GLU A OE2 
238   N N   . GLN A 43  ? 0.7827 1.0188 0.8153 0.0306  -0.0413 -0.1833 107 GLN A N   
239   C CA  . GLN A 43  ? 0.5845 0.7819 0.5995 0.0270  -0.0406 -0.1676 107 GLN A CA  
240   C C   . GLN A 43  ? 0.7158 0.9071 0.7361 0.0143  -0.0383 -0.1663 107 GLN A C   
241   O O   . GLN A 43  ? 0.6744 0.8869 0.7126 0.0018  -0.0330 -0.1750 107 GLN A O   
242   C CB  . GLN A 43  ? 0.5526 0.7317 0.5603 0.0192  -0.0321 -0.1564 107 GLN A CB  
243   C CG  . GLN A 43  ? 0.8456 1.0174 0.8402 0.0339  -0.0367 -0.1536 107 GLN A CG  
244   C CD  . GLN A 43  ? 0.9986 1.1438 0.9813 0.0282  -0.0311 -0.1406 107 GLN A CD  
245   O OE1 . GLN A 43  ? 0.9412 1.0648 0.9195 0.0176  -0.0270 -0.1311 107 GLN A OE1 
246   N NE2 . GLN A 43  ? 0.8273 0.9741 0.8042 0.0364  -0.0314 -0.1409 107 GLN A NE2 
247   N N   . MET A 44  ? 0.9087 1.0708 0.9130 0.0178  -0.0422 -0.1560 108 MET A N   
248   C CA  . MET A 44  ? 0.7643 0.9140 0.7690 0.0072  -0.0400 -0.1521 108 MET A CA  
249   C C   . MET A 44  ? 0.6726 0.8118 0.6800 -0.0106 -0.0285 -0.1448 108 MET A C   
250   O O   . MET A 44  ? 0.7473 0.8718 0.7460 -0.0107 -0.0249 -0.1360 108 MET A O   
251   C CB  . MET A 44  ? 0.8578 0.9776 0.8429 0.0165  -0.0455 -0.1413 108 MET A CB  
252   C CG  . MET A 44  ? 1.0428 1.1486 1.0257 0.0086  -0.0442 -0.1369 108 MET A CG  
253   S SD  . MET A 44  ? 1.1934 1.3227 1.1877 0.0110  -0.0506 -0.1519 108 MET A SD  
254   C CE  . MET A 44  ? 1.0478 1.1641 1.0229 0.0333  -0.0621 -0.1506 108 MET A CE  
255   N N   . LEU A 45  ? 0.5754 0.7213 0.5936 -0.0251 -0.0230 -0.1489 109 LEU A N   
256   C CA  . LEU A 45  ? 0.6165 0.7464 0.6325 -0.0414 -0.0121 -0.1411 109 LEU A CA  
257   C C   . LEU A 45  ? 0.6607 0.7580 0.6599 -0.0401 -0.0138 -0.1281 109 LEU A C   
258   O O   . LEU A 45  ? 0.6930 0.7854 0.6893 -0.0356 -0.0200 -0.1286 109 LEU A O   
259   C CB  . LEU A 45  ? 0.5885 0.7319 0.6188 -0.0574 -0.0059 -0.1496 109 LEU A CB  
260   C CG  . LEU A 45  ? 0.7331 0.9135 0.7848 -0.0614 -0.0035 -0.1649 109 LEU A CG  
261   C CD1 . LEU A 45  ? 0.7611 0.9528 0.8272 -0.0770 0.0006  -0.1741 109 LEU A CD1 
262   C CD2 . LEU A 45  ? 0.8476 1.0335 0.9011 -0.0662 0.0061  -0.1631 109 LEU A CD2 
263   N N   . THR A 46  ? 0.5488 0.6250 0.5372 -0.0432 -0.0088 -0.1171 110 THR A N   
264   C CA  . THR A 46  ? 0.6117 0.6597 0.5860 -0.0414 -0.0107 -0.1056 110 THR A CA  
265   C C   . THR A 46  ? 0.6404 0.6702 0.6091 -0.0540 -0.0031 -0.0995 110 THR A C   
266   O O   . THR A 46  ? 0.7815 0.8139 0.7529 -0.0641 0.0050  -0.1011 110 THR A O   
267   C CB  . THR A 46  ? 0.5185 0.5526 0.4824 -0.0321 -0.0136 -0.0975 110 THR A CB  
268   O OG1 . THR A 46  ? 0.7223 0.7539 0.6849 -0.0375 -0.0070 -0.0951 110 THR A OG1 
269   C CG2 . THR A 46  ? 0.5596 0.6061 0.5245 -0.0186 -0.0210 -0.1025 110 THR A CG2 
270   N N   . ARG A 47  ? 0.5961 0.6068 0.5558 -0.0526 -0.0056 -0.0926 111 ARG A N   
271   C CA  . ARG A 47  ? 0.5916 0.5821 0.5428 -0.0615 0.0001  -0.0862 111 ARG A CA  
272   C C   . ARG A 47  ? 0.5167 0.4882 0.4576 -0.0547 -0.0041 -0.0773 111 ARG A C   
273   O O   . ARG A 47  ? 0.5929 0.5667 0.5339 -0.0456 -0.0104 -0.0770 111 ARG A O   
274   C CB  . ARG A 47  ? 0.6165 0.6100 0.5720 -0.0726 0.0038  -0.0922 111 ARG A CB  
275   C CG  . ARG A 47  ? 0.5435 0.5283 0.4949 -0.0701 -0.0010 -0.0911 111 ARG A CG  
276   C CD  . ARG A 47  ? 0.6057 0.5820 0.5550 -0.0825 0.0042  -0.0935 111 ARG A CD  
277   N NE  . ARG A 47  ? 0.8795 0.8448 0.8222 -0.0785 -0.0008 -0.0915 111 ARG A NE  
278   C CZ  . ARG A 47  ? 0.9749 0.9190 0.9045 -0.0744 -0.0014 -0.0822 111 ARG A CZ  
279   N NH1 . ARG A 47  ? 1.1050 1.0366 1.0269 -0.0736 0.0019  -0.0745 111 ARG A NH1 
280   N NH2 . ARG A 47  ? 1.4304 1.3667 1.3546 -0.0703 -0.0054 -0.0813 111 ARG A NH2 
281   N N   . GLN A 48  ? 0.4317 0.3841 0.3629 -0.0587 -0.0004 -0.0704 112 GLN A N   
282   C CA  . GLN A 48  ? 0.5142 0.4504 0.4373 -0.0525 -0.0038 -0.0624 112 GLN A CA  
283   C C   . GLN A 48  ? 0.4959 0.4327 0.4194 -0.0429 -0.0084 -0.0586 112 GLN A C   
284   O O   . GLN A 48  ? 0.5891 0.5188 0.5101 -0.0370 -0.0120 -0.0540 112 GLN A O   
285   C CB  . GLN A 48  ? 0.4422 0.3746 0.3636 -0.0515 -0.0063 -0.0624 112 GLN A CB  
286   C CG  . GLN A 48  ? 0.6213 0.5490 0.5404 -0.0419 -0.0111 -0.0572 112 GLN A CG  
287   C CD  . GLN A 48  ? 0.7641 0.6778 0.6760 -0.0412 -0.0109 -0.0520 112 GLN A CD  
288   O OE1 . GLN A 48  ? 1.2108 1.1212 1.1213 -0.0337 -0.0137 -0.0475 112 GLN A OE1 
289   N NE2 . GLN A 48  ? 0.7565 0.6616 0.6632 -0.0471 -0.0079 -0.0521 112 GLN A NE2 
290   N N   . ASN A 49  ? 0.5218 0.4657 0.4479 -0.0418 -0.0078 -0.0606 113 ASN A N   
291   C CA  . ASN A 49  ? 0.5135 0.4553 0.4384 -0.0335 -0.0121 -0.0574 113 ASN A CA  
292   C C   . ASN A 49  ? 0.4699 0.3949 0.3888 -0.0318 -0.0133 -0.0500 113 ASN A C   
293   O O   . ASN A 49  ? 0.5207 0.4359 0.4347 -0.0361 -0.0102 -0.0474 113 ASN A O   
294   C CB  . ASN A 49  ? 0.4992 0.4484 0.4253 -0.0331 -0.0106 -0.0604 113 ASN A CB  
295   C CG  . ASN A 49  ? 0.7696 0.7401 0.7043 -0.0335 -0.0099 -0.0692 113 ASN A CG  
296   O OD1 . ASN A 49  ? 0.5952 0.5752 0.5321 -0.0251 -0.0146 -0.0723 113 ASN A OD1 
297   N ND2 . ASN A 49  ? 0.4687 0.4469 0.4080 -0.0430 -0.0043 -0.0740 113 ASN A ND2 
298   N N   . PHE A 50  ? 0.4362 0.3576 0.3552 -0.0254 -0.0176 -0.0469 114 PHE A N   
299   C CA  . PHE A 50  ? 0.4601 0.3693 0.3766 -0.0240 -0.0189 -0.0415 114 PHE A CA  
300   C C   . PHE A 50  ? 0.4915 0.3991 0.4087 -0.0179 -0.0231 -0.0402 114 PHE A C   
301   O O   . PHE A 50  ? 0.7128 0.6274 0.6301 -0.0136 -0.0251 -0.0434 114 PHE A O   
302   C CB  . PHE A 50  ? 0.7170 0.6184 0.6322 -0.0258 -0.0179 -0.0376 114 PHE A CB  
303   C CG  . PHE A 50  ? 0.7808 0.6835 0.6972 -0.0227 -0.0189 -0.0364 114 PHE A CG  
304   C CD1 . PHE A 50  ? 0.8090 0.7174 0.7250 -0.0238 -0.0178 -0.0395 114 PHE A CD1 
305   C CD2 . PHE A 50  ? 0.6193 0.5165 0.5365 -0.0189 -0.0205 -0.0323 114 PHE A CD2 
306   C CE1 . PHE A 50  ? 0.8739 0.7821 0.7885 -0.0195 -0.0190 -0.0385 114 PHE A CE1 
307   C CE2 . PHE A 50  ? 0.7635 0.6595 0.6790 -0.0157 -0.0202 -0.0306 114 PHE A CE2 
308   C CZ  . PHE A 50  ? 0.7255 0.6268 0.6388 -0.0151 -0.0197 -0.0336 114 PHE A CZ  
309   N N   . VAL A 51  ? 0.4245 0.3223 0.3416 -0.0172 -0.0248 -0.0363 115 VAL A N   
310   C CA  . VAL A 51  ? 0.4149 0.3081 0.3320 -0.0128 -0.0283 -0.0350 115 VAL A CA  
311   C C   . VAL A 51  ? 0.4608 0.3462 0.3805 -0.0139 -0.0279 -0.0304 115 VAL A C   
312   O O   . VAL A 51  ? 0.6304 0.5141 0.5528 -0.0171 -0.0264 -0.0287 115 VAL A O   
313   C CB  . VAL A 51  ? 0.4255 0.3157 0.3413 -0.0113 -0.0312 -0.0364 115 VAL A CB  
314   C CG1 . VAL A 51  ? 0.5268 0.4089 0.4417 -0.0075 -0.0352 -0.0352 115 VAL A CG1 
315   C CG2 . VAL A 51  ? 0.4242 0.3237 0.3375 -0.0096 -0.0305 -0.0411 115 VAL A CG2 
316   N N   . SER A 52  ? 0.5401 0.4205 0.4580 -0.0109 -0.0288 -0.0286 116 SER A N   
317   C CA  . SER A 52  ? 0.5344 0.4071 0.4550 -0.0126 -0.0271 -0.0242 116 SER A CA  
318   C C   . SER A 52  ? 0.7276 0.5907 0.6440 -0.0098 -0.0291 -0.0233 116 SER A C   
319   O O   . SER A 52  ? 0.6229 0.4855 0.5314 -0.0042 -0.0311 -0.0254 116 SER A O   
320   C CB  . SER A 52  ? 0.5372 0.4112 0.4556 -0.0121 -0.0233 -0.0220 116 SER A CB  
321   O OG  . SER A 52  ? 0.9291 0.7960 0.8497 -0.0137 -0.0203 -0.0175 116 SER A OG  
322   N N   . CYS A 53  ? 0.5966 0.4521 0.5182 -0.0135 -0.0286 -0.0208 117 CYS A N   
323   C CA  . CYS A 53  ? 0.6638 0.5070 0.5805 -0.0120 -0.0305 -0.0201 117 CYS A CA  
324   C C   . CYS A 53  ? 0.6255 0.4576 0.5401 -0.0142 -0.0255 -0.0153 117 CYS A C   
325   O O   . CYS A 53  ? 0.9850 0.8202 0.9077 -0.0192 -0.0210 -0.0127 117 CYS A O   
326   C CB  . CYS A 53  ? 0.7590 0.6001 0.6815 -0.0144 -0.0350 -0.0227 117 CYS A CB  
327   S SG  . CYS A 53  ? 1.5226 1.3726 1.4429 -0.0103 -0.0399 -0.0279 117 CYS A SG  
328   N N   . SER A 54  ? 0.7649 0.5834 0.6669 -0.0099 -0.0258 -0.0141 118 SER A N   
329   C CA  . SER A 54  ? 0.7700 0.5718 0.6663 -0.0124 -0.0205 -0.0092 118 SER A CA  
330   C C   . SER A 54  ? 0.8326 0.6232 0.7328 -0.0176 -0.0227 -0.0099 118 SER A C   
331   O O   . SER A 54  ? 1.1077 0.9045 1.0150 -0.0183 -0.0286 -0.0142 118 SER A O   
332   C CB  . SER A 54  ? 0.8559 0.6452 0.7322 -0.0034 -0.0196 -0.0074 118 SER A CB  
333   O OG  . SER A 54  ? 0.8893 0.6672 0.7534 0.0028  -0.0251 -0.0099 118 SER A OG  
334   N N   . ASP A 55  ? 0.8900 0.6630 0.7850 -0.0216 -0.0176 -0.0059 119 ASP A N   
335   C CA  . ASP A 55  ? 1.1862 0.9465 1.0848 -0.0278 -0.0193 -0.0070 119 ASP A CA  
336   C C   . ASP A 55  ? 1.2173 0.9611 1.0976 -0.0198 -0.0255 -0.0090 119 ASP A C   
337   O O   . ASP A 55  ? 1.3427 1.0742 1.2227 -0.0230 -0.0291 -0.0110 119 ASP A O   
338   C CB  . ASP A 55  ? 1.3129 1.0602 1.2139 -0.0372 -0.0100 -0.0022 119 ASP A CB  
339   C CG  . ASP A 55  ? 1.8289 1.5594 1.7090 -0.0320 -0.0028 0.0040  119 ASP A CG  
340   O OD1 . ASP A 55  ? 2.1316 1.8564 1.9934 -0.0204 -0.0069 0.0035  119 ASP A OD1 
341   O OD2 . ASP A 55  ? 1.7748 1.4979 1.6564 -0.0390 0.0070  0.0089  119 ASP A OD2 
342   N N   . LYS A 56  ? 1.0240 0.7689 0.8895 -0.0089 -0.0273 -0.0091 120 LYS A N   
343   C CA  . LYS A 56  ? 1.0055 0.7363 0.8512 0.0015  -0.0326 -0.0111 120 LYS A CA  
344   C C   . LYS A 56  ? 1.0163 0.7653 0.8656 0.0083  -0.0404 -0.0173 120 LYS A C   
345   O O   . LYS A 56  ? 1.6061 1.3474 1.4462 0.0144  -0.0466 -0.0207 120 LYS A O   
346   C CB  . LYS A 56  ? 1.0608 0.7819 0.8873 0.0102  -0.0291 -0.0079 120 LYS A CB  
347   C CG  . LYS A 56  ? 1.6633 1.3710 1.4668 0.0240  -0.0351 -0.0106 120 LYS A CG  
348   C CD  . LYS A 56  ? 2.1683 1.8703 1.9534 0.0347  -0.0328 -0.0087 120 LYS A CD  
349   C CE  . LYS A 56  ? 2.5762 2.2524 2.3482 0.0307  -0.0235 -0.0009 120 LYS A CE  
350   N NZ  . LYS A 56  ? 3.2079 2.8964 2.9962 0.0207  -0.0152 0.0032  120 LYS A NZ  
351   N N   . GLU A 57  ? 1.0047 0.7768 0.8667 0.0072  -0.0396 -0.0188 121 GLU A N   
352   C CA  . GLU A 57  ? 0.9924 0.7827 0.8563 0.0135  -0.0446 -0.0243 121 GLU A CA  
353   C C   . GLU A 57  ? 0.8454 0.6568 0.7237 0.0088  -0.0419 -0.0249 121 GLU A C   
354   O O   . GLU A 57  ? 0.8399 0.6529 0.7238 0.0036  -0.0367 -0.0213 121 GLU A O   
355   C CB  . GLU A 57  ? 0.8209 0.6106 0.6691 0.0254  -0.0467 -0.0265 121 GLU A CB  
356   C CG  . GLU A 57  ? 0.7753 0.5745 0.6239 0.0268  -0.0427 -0.0253 121 GLU A CG  
357   C CD  . GLU A 57  ? 1.2397 1.0351 1.0709 0.0396  -0.0452 -0.0276 121 GLU A CD  
358   O OE1 . GLU A 57  ? 1.5252 1.3183 1.3466 0.0487  -0.0509 -0.0321 121 GLU A OE1 
359   O OE2 . GLU A 57  ? 1.5677 1.3626 1.3944 0.0416  -0.0417 -0.0255 121 GLU A OE2 
360   N N   . CYS A 58  ? 0.8304 0.6567 0.7129 0.0111  -0.0451 -0.0295 122 CYS A N   
361   C CA  . CYS A 58  ? 0.7033 0.5468 0.5960 0.0071  -0.0424 -0.0304 122 CYS A CA  
362   C C   . CYS A 58  ? 0.6613 0.5170 0.5497 0.0131  -0.0424 -0.0339 122 CYS A C   
363   O O   . CYS A 58  ? 0.6888 0.5466 0.5698 0.0208  -0.0462 -0.0381 122 CYS A O   
364   C CB  . CYS A 58  ? 0.8612 0.7113 0.7607 0.0044  -0.0448 -0.0332 122 CYS A CB  
365   S SG  . CYS A 58  ? 1.3647 1.2048 1.2727 -0.0026 -0.0459 -0.0311 122 CYS A SG  
366   N N   . ARG A 59  ? 0.5999 0.4642 0.4929 0.0100  -0.0387 -0.0331 123 ARG A N   
367   C CA  . ARG A 59  ? 0.4836 0.3612 0.3748 0.0146  -0.0389 -0.0376 123 ARG A CA  
368   C C   . ARG A 59  ? 0.4681 0.3603 0.3688 0.0086  -0.0366 -0.0401 123 ARG A C   
369   O O   . ARG A 59  ? 0.5756 0.4656 0.4820 0.0017  -0.0340 -0.0370 123 ARG A O   
370   C CB  . ARG A 59  ? 0.4464 0.3190 0.3312 0.0180  -0.0373 -0.0354 123 ARG A CB  
371   C CG  . ARG A 59  ? 0.5196 0.3742 0.3906 0.0250  -0.0389 -0.0328 123 ARG A CG  
372   C CD  . ARG A 59  ? 0.5928 0.4412 0.4529 0.0311  -0.0374 -0.0312 123 ARG A CD  
373   N NE  . ARG A 59  ? 0.7233 0.5863 0.5807 0.0394  -0.0414 -0.0385 123 ARG A NE  
374   C CZ  . ARG A 59  ? 0.7176 0.5812 0.5657 0.0498  -0.0467 -0.0435 123 ARG A CZ  
375   N NH1 . ARG A 59  ? 0.8275 0.6746 0.6658 0.0532  -0.0485 -0.0413 123 ARG A NH1 
376   N NH2 . ARG A 59  ? 0.8042 0.6848 0.6528 0.0569  -0.0504 -0.0515 123 ARG A NH2 
377   N N   . ARG A 60  ? 0.4400 0.3470 0.3418 0.0113  -0.0375 -0.0463 124 ARG A N   
378   C CA  . ARG A 60  ? 0.4533 0.3734 0.3629 0.0048  -0.0341 -0.0493 124 ARG A CA  
379   C C   . ARG A 60  ? 0.5066 0.4339 0.4176 0.0046  -0.0330 -0.0514 124 ARG A C   
380   O O   . ARG A 60  ? 0.8489 0.7840 0.7575 0.0114  -0.0359 -0.0564 124 ARG A O   
381   C CB  . ARG A 60  ? 0.4486 0.3819 0.3602 0.0069  -0.0349 -0.0556 124 ARG A CB  
382   C CG  . ARG A 60  ? 0.4941 0.4447 0.4131 0.0016  -0.0313 -0.0614 124 ARG A CG  
383   C CD  . ARG A 60  ? 0.4858 0.4471 0.4073 0.0011  -0.0296 -0.0659 124 ARG A CD  
384   N NE  . ARG A 60  ? 0.5798 0.5586 0.5094 -0.0051 -0.0249 -0.0721 124 ARG A NE  
385   C CZ  . ARG A 60  ? 0.8492 0.8455 0.7837 -0.0039 -0.0234 -0.0792 124 ARG A CZ  
386   N NH1 . ARG A 60  ? 0.8779 0.8756 0.8083 0.0049  -0.0270 -0.0806 124 ARG A NH1 
387   N NH2 . ARG A 60  ? 0.7789 0.7917 0.7226 -0.0116 -0.0181 -0.0852 124 ARG A NH2 
388   N N   . PHE A 61  ? 0.5121 0.4359 0.4255 -0.0017 -0.0297 -0.0482 125 PHE A N   
389   C CA  . PHE A 61  ? 0.5726 0.5031 0.4869 -0.0020 -0.0290 -0.0510 125 PHE A CA  
390   C C   . PHE A 61  ? 0.5200 0.4634 0.4411 -0.0089 -0.0265 -0.0567 125 PHE A C   
391   O O   . PHE A 61  ? 0.5545 0.4970 0.4778 -0.0151 -0.0234 -0.0559 125 PHE A O   
392   C CB  . PHE A 61  ? 0.4114 0.3304 0.3228 -0.0037 -0.0269 -0.0448 125 PHE A CB  
393   C CG  . PHE A 61  ? 0.4473 0.3540 0.3518 0.0023  -0.0278 -0.0397 125 PHE A CG  
394   C CD1 . PHE A 61  ? 0.4786 0.3757 0.3827 0.0017  -0.0279 -0.0355 125 PHE A CD1 
395   C CD2 . PHE A 61  ? 0.4438 0.3473 0.3409 0.0088  -0.0286 -0.0395 125 PHE A CD2 
396   C CE1 . PHE A 61  ? 0.5232 0.4070 0.4207 0.0056  -0.0277 -0.0308 125 PHE A CE1 
397   C CE2 . PHE A 61  ? 0.5817 0.4707 0.4699 0.0139  -0.0279 -0.0340 125 PHE A CE2 
398   C CZ  . PHE A 61  ? 0.5098 0.3886 0.3986 0.0114  -0.0270 -0.0295 125 PHE A CZ  
399   N N   . PHE A 62  ? 0.4475 0.4022 0.3712 -0.0078 -0.0277 -0.0629 126 PHE A N   
400   C CA  . PHE A 62  ? 0.6413 0.6069 0.5721 -0.0167 -0.0243 -0.0684 126 PHE A CA  
401   C C   . PHE A 62  ? 0.5593 0.5334 0.4926 -0.0163 -0.0262 -0.0743 126 PHE A C   
402   O O   . PHE A 62  ? 0.7806 0.7514 0.7085 -0.0079 -0.0302 -0.0738 126 PHE A O   
403   C CB  . PHE A 62  ? 0.9169 0.8969 0.8539 -0.0179 -0.0232 -0.0743 126 PHE A CB  
404   C CG  . PHE A 62  ? 0.6900 0.6844 0.6290 -0.0082 -0.0286 -0.0813 126 PHE A CG  
405   C CD1 . PHE A 62  ? 0.5700 0.5838 0.5172 -0.0082 -0.0301 -0.0913 126 PHE A CD1 
406   C CD2 . PHE A 62  ? 0.6285 0.6165 0.5607 0.0014  -0.0324 -0.0784 126 PHE A CD2 
407   C CE1 . PHE A 62  ? 0.8195 0.8476 0.7679 0.0027  -0.0361 -0.0988 126 PHE A CE1 
408   C CE2 . PHE A 62  ? 0.6706 0.6697 0.6017 0.0122  -0.0380 -0.0851 126 PHE A CE2 
409   C CZ  . PHE A 62  ? 0.9076 0.9275 0.8467 0.0136  -0.0400 -0.0954 126 PHE A CZ  
410   N N   . VAL A 63  ? 0.5257 0.5093 0.4661 -0.0254 -0.0230 -0.0803 127 VAL A N   
411   C CA  . VAL A 63  ? 0.5577 0.5501 0.5016 -0.0260 -0.0254 -0.0874 127 VAL A CA  
412   C C   . VAL A 63  ? 0.6039 0.6204 0.5605 -0.0288 -0.0257 -0.0991 127 VAL A C   
413   O O   . VAL A 63  ? 0.8754 0.8970 0.8378 -0.0381 -0.0199 -0.1006 127 VAL A O   
414   C CB  . VAL A 63  ? 0.5458 0.5261 0.4868 -0.0355 -0.0214 -0.0847 127 VAL A CB  
415   C CG1 . VAL A 63  ? 0.6225 0.6147 0.5702 -0.0402 -0.0227 -0.0947 127 VAL A CG1 
416   C CG2 . VAL A 63  ? 0.4718 0.4331 0.4017 -0.0302 -0.0225 -0.0756 127 VAL A CG2 
417   N N   . SER A 64  ? 0.6566 0.6880 0.6167 -0.0200 -0.0324 -0.1076 128 SER A N   
418   C CA  . SER A 64  ? 0.6461 0.7052 0.6205 -0.0207 -0.0339 -0.1207 128 SER A CA  
419   C C   . SER A 64  ? 0.6239 0.6948 0.6105 -0.0344 -0.0302 -0.1292 128 SER A C   
420   O O   . SER A 64  ? 0.8218 0.8837 0.8049 -0.0373 -0.0314 -0.1290 128 SER A O   
421   C CB  . SER A 64  ? 0.7984 0.8687 0.7709 -0.0051 -0.0435 -0.1279 128 SER A CB  
422   O OG  . SER A 64  ? 1.2269 1.2952 1.1973 -0.0034 -0.0476 -0.1315 128 SER A OG  
423   N N   . MET A 65  ? 0.5724 0.6629 0.5728 -0.0429 -0.0253 -0.1367 129 MET A N   
424   C CA  . MET A 65  ? 0.7424 0.8502 0.7580 -0.0559 -0.0221 -0.1481 129 MET A CA  
425   C C   . MET A 65  ? 0.8217 0.9634 0.8537 -0.0495 -0.0288 -0.1644 129 MET A C   
426   O O   . MET A 65  ? 0.9005 1.0619 0.9490 -0.0605 -0.0266 -0.1763 129 MET A O   
427   C CB  . MET A 65  ? 0.7145 0.8208 0.7347 -0.0725 -0.0099 -0.1463 129 MET A CB  
428   C CG  . MET A 65  ? 0.8302 0.9084 0.8389 -0.0841 -0.0034 -0.1374 129 MET A CG  
429   S SD  . MET A 65  ? 1.3740 1.4243 1.3656 -0.0854 0.0040  -0.1216 129 MET A SD  
430   C CE  . MET A 65  ? 0.8187 0.8831 0.8200 -0.0985 0.0160  -0.1265 129 MET A CE  
431   N N   . GLY A 66  ? 0.7413 0.8888 0.7682 -0.0317 -0.0373 -0.1654 130 GLY A N   
432   C CA  . GLY A 66  ? 0.7162 0.8961 0.7566 -0.0224 -0.0445 -0.1809 130 GLY A CA  
433   C C   . GLY A 66  ? 0.7888 0.9843 0.8353 -0.0198 -0.0412 -0.1827 130 GLY A C   
434   O O   . GLY A 66  ? 0.8318 1.0131 0.8728 -0.0268 -0.0328 -0.1724 130 GLY A O   
435   N N   . TYR A 67  ? 0.9282 1.1525 0.9847 -0.0082 -0.0484 -0.1960 131 TYR A N   
436   C CA  . TYR A 67  ? 0.8710 1.1128 0.9331 -0.0033 -0.0462 -0.1993 131 TYR A CA  
437   C C   . TYR A 67  ? 0.8237 1.0879 0.9072 -0.0223 -0.0348 -0.2063 131 TYR A C   
438   O O   . TYR A 67  ? 0.8450 1.1231 0.9440 -0.0349 -0.0325 -0.2154 131 TYR A O   
439   C CB  . TYR A 67  ? 0.9480 1.2137 1.0127 0.0169  -0.0583 -0.2123 131 TYR A CB  
440   C CG  . TYR A 67  ? 0.9637 1.2050 1.0043 0.0365  -0.0690 -0.2057 131 TYR A CG  
441   C CD1 . TYR A 67  ? 0.9809 1.1941 1.0003 0.0449  -0.0687 -0.1916 131 TYR A CD1 
442   C CD2 . TYR A 67  ? 0.9247 1.1702 0.9629 0.0465  -0.0790 -0.2137 131 TYR A CD2 
443   C CE1 . TYR A 67  ? 0.9440 1.1329 0.9404 0.0615  -0.0769 -0.1852 131 TYR A CE1 
444   C CE2 . TYR A 67  ? 1.0222 1.2431 1.0357 0.0646  -0.0875 -0.2072 131 TYR A CE2 
445   C CZ  . TYR A 67  ? 1.0060 1.1983 0.9988 0.0714  -0.0857 -0.1927 131 TYR A CZ  
446   O OH  . TYR A 67  ? 0.9823 1.1486 0.9499 0.0881  -0.0926 -0.1860 131 TYR A OH  
447   N N   . GLY A 68  ? 1.0348 1.3014 1.1183 -0.0244 -0.0273 -0.2023 132 GLY A N   
448   C CA  . GLY A 68  ? 1.0469 1.3323 1.1479 -0.0423 -0.0143 -0.2075 132 GLY A CA  
449   C C   . GLY A 68  ? 0.9056 1.2371 1.0335 -0.0433 -0.0154 -0.2276 132 GLY A C   
450   O O   . GLY A 68  ? 1.1212 1.4702 1.2673 -0.0616 -0.0045 -0.2344 132 GLY A O   
451   N N   . THR A 69  ? 0.8339 1.1847 0.9637 -0.0235 -0.0283 -0.2375 133 THR A N   
452   C CA  . THR A 69  ? 0.9169 1.3150 1.0728 -0.0210 -0.0314 -0.2582 133 THR A CA  
453   C C   . THR A 69  ? 1.1035 1.5168 1.2744 -0.0261 -0.0378 -0.2712 133 THR A C   
454   O O   . THR A 69  ? 1.0525 1.5042 1.2512 -0.0351 -0.0356 -0.2886 133 THR A O   
455   C CB  . THR A 69  ? 0.9260 1.3387 1.0755 0.0049  -0.0430 -0.2642 133 THR A CB  
456   O OG1 . THR A 69  ? 1.4498 1.9103 1.6251 0.0095  -0.0482 -0.2861 133 THR A OG1 
457   C CG2 . THR A 69  ? 0.8291 1.2116 0.9522 0.0245  -0.0566 -0.2562 133 THR A CG2 
458   N N   . THR A 70  ? 1.2030 1.5862 1.3558 -0.0209 -0.0454 -0.2631 134 THR A N   
459   C CA  . THR A 70  ? 1.1332 1.5260 1.2954 -0.0225 -0.0534 -0.2744 134 THR A CA  
460   C C   . THR A 70  ? 1.2089 1.5851 1.3754 -0.0472 -0.0429 -0.2693 134 THR A C   
461   O O   . THR A 70  ? 1.3274 1.7110 1.5039 -0.0533 -0.0473 -0.2791 134 THR A O   
462   C CB  . THR A 70  ? 1.5436 1.9125 1.6815 -0.0011 -0.0677 -0.2690 134 THR A CB  
463   O OG1 . THR A 70  ? 2.2355 2.5603 2.3511 -0.0070 -0.0628 -0.2494 134 THR A OG1 
464   C CG2 . THR A 70  ? 1.7955 2.1666 1.9198 0.0232  -0.0762 -0.2686 134 THR A CG2 
465   N N   . THR A 71  ? 1.0387 1.3906 1.1957 -0.0604 -0.0295 -0.2542 135 THR A N   
466   C CA  . THR A 71  ? 1.1600 1.4914 1.3165 -0.0831 -0.0185 -0.2478 135 THR A CA  
467   C C   . THR A 71  ? 1.3844 1.7410 1.5644 -0.1042 -0.0044 -0.2571 135 THR A C   
468   O O   . THR A 71  ? 1.8307 2.1984 2.0142 -0.1042 0.0033  -0.2555 135 THR A O   
469   C CB  . THR A 71  ? 1.1195 1.4055 1.2484 -0.0842 -0.0124 -0.2255 135 THR A CB  
470   O OG1 . THR A 71  ? 1.0073 1.2695 1.1158 -0.0675 -0.0238 -0.2171 135 THR A OG1 
471   C CG2 . THR A 71  ? 0.9062 1.1700 1.0322 -0.1065 -0.0005 -0.2191 135 THR A CG2 
472   N N   . ASN A 72  ? 1.4768 1.8420 1.6726 -0.1221 -0.0008 -0.2669 136 ASN A N   
473   C CA  . ASN A 72  ? 1.4053 1.7885 1.6215 -0.1458 0.0151  -0.2741 136 ASN A CA  
474   C C   . ASN A 72  ? 1.4875 1.8298 1.6859 -0.1648 0.0293  -0.2587 136 ASN A C   
475   O O   . ASN A 72  ? 1.8796 2.1886 2.0593 -0.1640 0.0248  -0.2494 136 ASN A O   
476   C CB  . ASN A 72  ? 1.4344 1.8544 1.6810 -0.1559 0.0116  -0.2963 136 ASN A CB  
477   C CG  . ASN A 72  ? 1.8805 2.3304 2.1538 -0.1780 0.0278  -0.3072 136 ASN A CG  
478   O OD1 . ASN A 72  ? 1.7455 2.1987 2.0171 -0.1799 0.0392  -0.3011 136 ASN A OD1 
479   N ND2 . ASN A 72  ? 1.9782 2.4499 2.2760 -0.1951 0.0293  -0.3238 136 ASN A ND2 
480   N N   . PHE A 73  ? 1.5518 1.8961 1.7545 -0.1805 0.0463  -0.2561 137 PHE A N   
481   C CA  . PHE A 73  ? 1.6459 1.9490 1.8276 -0.1962 0.0607  -0.2405 137 PHE A CA  
482   C C   . PHE A 73  ? 1.7757 2.0584 1.9554 -0.2144 0.0640  -0.2421 137 PHE A C   
483   O O   . PHE A 73  ? 1.6599 1.8999 1.8135 -0.2164 0.0660  -0.2275 137 PHE A O   
484   C CB  . PHE A 73  ? 1.6948 2.0064 1.8816 -0.2093 0.0791  -0.2393 137 PHE A CB  
485   C CG  . PHE A 73  ? 2.0384 2.3055 2.2000 -0.2234 0.0939  -0.2233 137 PHE A CG  
486   C CD1 . PHE A 73  ? 2.0825 2.3124 2.2135 -0.2106 0.0916  -0.2049 137 PHE A CD1 
487   C CD2 . PHE A 73  ? 1.8863 2.1478 2.0536 -0.2491 0.1099  -0.2272 137 PHE A CD2 
488   C CE1 . PHE A 73  ? 1.8199 2.0086 1.9259 -0.2213 0.1040  -0.1911 137 PHE A CE1 
489   C CE2 . PHE A 73  ? 2.0832 2.3003 2.2232 -0.2604 0.1233  -0.2124 137 PHE A CE2 
490   C CZ  . PHE A 73  ? 1.9623 2.1433 2.0712 -0.2454 0.1197  -0.1945 137 PHE A CZ  
491   N N   . ALA A 74  ? 1.9919 2.3056 2.1992 -0.2272 0.0640  -0.2606 138 ALA A N   
492   C CA  . ALA A 74  ? 1.8444 2.1424 2.0532 -0.2464 0.0672  -0.2651 138 ALA A CA  
493   C C   . ALA A 74  ? 1.8683 2.1345 2.0558 -0.2352 0.0533  -0.2578 138 ALA A C   
494   O O   . ALA A 74  ? 1.6038 1.8395 1.7789 -0.2487 0.0578  -0.2537 138 ALA A O   
495   C CB  . ALA A 74  ? 1.5340 1.8773 1.7800 -0.2593 0.0667  -0.2889 138 ALA A CB  
496   N N   . ASP A 75  ? 2.4605 2.7335 2.6430 -0.2103 0.0372  -0.2562 139 ASP A N   
497   C CA  . ASP A 75  ? 2.1872 2.4301 2.3473 -0.1967 0.0248  -0.2473 139 ASP A CA  
498   C C   . ASP A 75  ? 2.0739 2.2723 2.2027 -0.1943 0.0310  -0.2256 139 ASP A C   
499   O O   . ASP A 75  ? 2.2672 2.4622 2.3887 -0.1897 0.0372  -0.2162 139 ASP A O   
500   C CB  . ASP A 75  ? 1.8737 2.1342 2.0345 -0.1703 0.0076  -0.2505 139 ASP A CB  
501   C CG  . ASP A 75  ? 1.9735 2.2749 2.1612 -0.1674 -0.0030 -0.2726 139 ASP A CG  
502   O OD1 . ASP A 75  ? 2.4225 2.7353 2.6275 -0.1855 0.0004  -0.2853 139 ASP A OD1 
503   O OD2 . ASP A 75  ? 1.5882 1.9099 1.7789 -0.1463 -0.0153 -0.2776 139 ASP A OD2 
504   N N   . LEU A 76  ? 2.1436 2.3085 2.2538 -0.1965 0.0287  -0.2184 140 LEU A N   
505   C CA  . LEU A 76  ? 2.3153 2.4417 2.3959 -0.1870 0.0288  -0.1993 140 LEU A CA  
506   C C   . LEU A 76  ? 1.7433 1.8702 1.8181 -0.1661 0.0124  -0.1987 140 LEU A C   
507   O O   . LEU A 76  ? 1.0370 1.1741 1.1204 -0.1654 0.0038  -0.2098 140 LEU A O   
508   C CB  . LEU A 76  ? 2.6972 2.7851 2.7588 -0.2021 0.0376  -0.1915 140 LEU A CB  
509   C CG  . LEU A 76  ? 2.5676 2.6394 2.6215 -0.2187 0.0553  -0.1850 140 LEU A CG  
510   C CD1 . LEU A 76  ? 2.2116 2.3112 2.2907 -0.2389 0.0661  -0.1994 140 LEU A CD1 
511   C CD2 . LEU A 76  ? 2.1557 2.1811 2.1815 -0.2261 0.0610  -0.1738 140 LEU A CD2 
512   N N   . ILE A 77  ? 1.8577 1.9746 1.9185 -0.1491 0.0083  -0.1867 141 ILE A N   
513   C CA  . ILE A 77  ? 1.7945 1.9084 1.8469 -0.1292 -0.0055 -0.1845 141 ILE A CA  
514   C C   . ILE A 77  ? 1.6175 1.6935 1.6453 -0.1257 -0.0063 -0.1706 141 ILE A C   
515   O O   . ILE A 77  ? 1.7581 1.8091 1.7725 -0.1340 0.0028  -0.1600 141 ILE A O   
516   C CB  . ILE A 77  ? 2.0623 2.1914 2.1158 -0.1111 -0.0113 -0.1823 141 ILE A CB  
517   C CG1 . ILE A 77  ? 1.8925 2.0225 1.9396 -0.0919 -0.0253 -0.1839 141 ILE A CG1 
518   C CG2 . ILE A 77  ? 1.8476 1.9545 1.8850 -0.1085 -0.0047 -0.1661 141 ILE A CG2 
519   C CD1 . ILE A 77  ? 1.8863 2.0425 1.9416 -0.0756 -0.0336 -0.1912 141 ILE A CD1 
520   N N   . VAL A 78  ? 1.1926 1.2652 1.2138 -0.1119 -0.0173 -0.1710 142 VAL A N   
521   C CA  . VAL A 78  ? 0.9346 0.9773 0.9369 -0.1102 -0.0190 -0.1628 142 VAL A CA  
522   C C   . VAL A 78  ? 0.9792 1.0100 0.9664 -0.0909 -0.0257 -0.1521 142 VAL A C   
523   O O   . VAL A 78  ? 0.8258 0.8734 0.8177 -0.0772 -0.0331 -0.1557 142 VAL A O   
524   C CB  . VAL A 78  ? 0.9217 0.9699 0.9303 -0.1149 -0.0249 -0.1755 142 VAL A CB  
525   C CG1 . VAL A 78  ? 0.8817 0.9594 0.9039 -0.1022 -0.0366 -0.1885 142 VAL A CG1 
526   C CG2 . VAL A 78  ? 1.2001 1.2173 1.1878 -0.1117 -0.0273 -0.1676 142 VAL A CG2 
527   N N   . SER A 79  ? 0.8550 0.8567 0.8237 -0.0899 -0.0229 -0.1396 143 SER A N   
528   C CA  . SER A 79  ? 0.7262 0.7142 0.6806 -0.0746 -0.0264 -0.1279 143 SER A CA  
529   C C   . SER A 79  ? 0.7761 0.7723 0.7287 -0.0584 -0.0366 -0.1316 143 SER A C   
530   O O   . SER A 79  ? 1.1049 1.0984 1.0507 -0.0455 -0.0389 -0.1243 143 SER A O   
531   C CB  . SER A 79  ? 0.9181 0.8766 0.8550 -0.0769 -0.0228 -0.1176 143 SER A CB  
532   O OG  . SER A 79  ? 1.2841 1.2316 1.2188 -0.0904 -0.0137 -0.1143 143 SER A OG  
533   N N   . GLU A 80  ? 0.7035 0.7082 0.6608 -0.0589 -0.0425 -0.1430 144 GLU A N   
534   C CA  . GLU A 80  ? 0.8959 0.9055 0.8480 -0.0423 -0.0524 -0.1467 144 GLU A CA  
535   C C   . GLU A 80  ? 0.8220 0.8550 0.7833 -0.0317 -0.0577 -0.1533 144 GLU A C   
536   O O   . GLU A 80  ? 0.9501 0.9830 0.9025 -0.0153 -0.0649 -0.1534 144 GLU A O   
537   C CB  . GLU A 80  ? 0.9967 1.0081 0.9502 -0.0445 -0.0586 -0.1582 144 GLU A CB  
538   C CG  . GLU A 80  ? 1.1268 1.1110 1.0649 -0.0489 -0.0560 -0.1514 144 GLU A CG  
539   C CD  . GLU A 80  ? 1.2196 1.1919 1.1592 -0.0675 -0.0462 -0.1479 144 GLU A CD  
540   O OE1 . GLU A 80  ? 1.2208 1.2077 1.1757 -0.0803 -0.0414 -0.1541 144 GLU A OE1 
541   O OE2 . GLU A 80  ? 1.5776 1.5249 1.5015 -0.0688 -0.0429 -0.1389 144 GLU A OE2 
542   N N   . GLN A 81  ? 0.6664 0.7180 0.6436 -0.0404 -0.0540 -0.1588 145 GLN A N   
543   C CA  . GLN A 81  ? 0.7052 0.7806 0.6915 -0.0301 -0.0594 -0.1665 145 GLN A CA  
544   C C   . GLN A 81  ? 0.7269 0.7938 0.7049 -0.0228 -0.0559 -0.1543 145 GLN A C   
545   O O   . GLN A 81  ? 0.8036 0.8856 0.7852 -0.0128 -0.0599 -0.1585 145 GLN A O   
546   C CB  . GLN A 81  ? 0.8784 0.9821 0.8881 -0.0429 -0.0571 -0.1805 145 GLN A CB  
547   C CG  . GLN A 81  ? 0.9061 1.0220 0.9274 -0.0508 -0.0614 -0.1953 145 GLN A CG  
548   C CD  . GLN A 81  ? 1.1658 1.3161 1.2135 -0.0612 -0.0603 -0.2117 145 GLN A CD  
549   O OE1 . GLN A 81  ? 1.4504 1.6041 1.5082 -0.0784 -0.0496 -0.2110 145 GLN A OE1 
550   N NE2 . GLN A 81  ? 1.4128 1.5890 1.4711 -0.0503 -0.0713 -0.2270 145 GLN A NE2 
551   N N   . MET A 82  ? 0.6313 0.6738 0.5976 -0.0271 -0.0492 -0.1400 146 MET A N   
552   C CA  . MET A 82  ? 0.5401 0.5749 0.5019 -0.0252 -0.0445 -0.1293 146 MET A CA  
553   C C   . MET A 82  ? 0.5417 0.5618 0.4878 -0.0096 -0.0481 -0.1201 146 MET A C   
554   O O   . MET A 82  ? 0.7052 0.7115 0.6398 -0.0036 -0.0504 -0.1164 146 MET A O   
555   C CB  . MET A 82  ? 0.4954 0.5131 0.4542 -0.0386 -0.0352 -0.1200 146 MET A CB  
556   C CG  . MET A 82  ? 0.5101 0.5390 0.4817 -0.0541 -0.0287 -0.1262 146 MET A CG  
557   S SD  . MET A 82  ? 0.8922 0.8956 0.8543 -0.0679 -0.0187 -0.1158 146 MET A SD  
558   C CE  . MET A 82  ? 0.5530 0.5737 0.5304 -0.0841 -0.0104 -0.1245 146 MET A CE  
559   N N   . ASN A 83  ? 0.5377 0.5596 0.4825 -0.0037 -0.0477 -0.1164 147 ASN A N   
560   C CA  . ASN A 83  ? 0.5582 0.5667 0.4886 0.0104  -0.0505 -0.1086 147 ASN A CA  
561   C C   . ASN A 83  ? 0.6102 0.6071 0.5376 0.0077  -0.0451 -0.0978 147 ASN A C   
562   O O   . ASN A 83  ? 0.7039 0.7094 0.6405 0.0003  -0.0417 -0.0993 147 ASN A O   
563   C CB  . ASN A 83  ? 0.5751 0.5985 0.5051 0.0242  -0.0582 -0.1176 147 ASN A CB  
564   C CG  . ASN A 83  ? 0.5900 0.6218 0.5183 0.0323  -0.0658 -0.1276 147 ASN A CG  
565   O OD1 . ASN A 83  ? 0.8018 0.8193 0.7198 0.0349  -0.0664 -0.1238 147 ASN A OD1 
566   N ND2 . ASN A 83  ? 0.6715 0.7275 0.6100 0.0372  -0.0720 -0.1414 147 ASN A ND2 
567   N N   . VAL A 84  ? 0.5018 0.4795 0.4162 0.0143  -0.0443 -0.0877 148 VAL A N   
568   C CA  . VAL A 84  ? 0.4689 0.4352 0.3812 0.0114  -0.0399 -0.0782 148 VAL A CA  
569   C C   . VAL A 84  ? 0.4556 0.4212 0.3619 0.0220  -0.0433 -0.0780 148 VAL A C   
570   O O   . VAL A 84  ? 0.6364 0.5914 0.5299 0.0329  -0.0459 -0.0753 148 VAL A O   
571   C CB  . VAL A 84  ? 0.4764 0.4223 0.3798 0.0105  -0.0359 -0.0671 148 VAL A CB  
572   C CG1 . VAL A 84  ? 0.4316 0.3678 0.3351 0.0073  -0.0322 -0.0589 148 VAL A CG1 
573   C CG2 . VAL A 84  ? 0.3567 0.3003 0.2624 0.0024  -0.0333 -0.0671 148 VAL A CG2 
574   N N   . TYR A 85  ? 0.4475 0.4220 0.3609 0.0193  -0.0428 -0.0804 149 TYR A N   
575   C CA  . TYR A 85  ? 0.5057 0.4769 0.4121 0.0289  -0.0459 -0.0796 149 TYR A CA  
576   C C   . TYR A 85  ? 0.4635 0.4204 0.3673 0.0252  -0.0423 -0.0706 149 TYR A C   
577   O O   . TYR A 85  ? 0.7359 0.6898 0.6457 0.0150  -0.0377 -0.0665 149 TYR A O   
578   C CB  . TYR A 85  ? 0.5100 0.5032 0.4249 0.0318  -0.0493 -0.0904 149 TYR A CB  
579   C CG  . TYR A 85  ? 0.6168 0.6269 0.5345 0.0388  -0.0551 -0.1015 149 TYR A CG  
580   C CD1 . TYR A 85  ? 0.6946 0.7033 0.6004 0.0550  -0.0621 -0.1053 149 TYR A CD1 
581   C CD2 . TYR A 85  ? 0.6561 0.6829 0.5875 0.0293  -0.0538 -0.1092 149 TYR A CD2 
582   C CE1 . TYR A 85  ? 0.9791 1.0046 0.8872 0.0632  -0.0687 -0.1170 149 TYR A CE1 
583   C CE2 . TYR A 85  ? 0.8066 0.8512 0.7425 0.0357  -0.0601 -0.1213 149 TYR A CE2 
584   C CZ  . TYR A 85  ? 0.9966 1.0414 0.9211 0.0534  -0.0681 -0.1254 149 TYR A CZ  
585   O OH  . TYR A 85  ? 1.2055 1.2679 1.1331 0.0620  -0.0757 -0.1382 149 TYR A OH  
586   N N   . SER A 86  ? 0.5815 0.5286 0.4750 0.0345  -0.0452 -0.0684 150 SER A N   
587   C CA  . SER A 86  ? 0.7214 0.6543 0.6116 0.0325  -0.0433 -0.0613 150 SER A CA  
588   C C   . SER A 86  ? 0.5879 0.5271 0.4755 0.0405  -0.0477 -0.0666 150 SER A C   
589   O O   . SER A 86  ? 0.8331 0.7838 0.7182 0.0498  -0.0525 -0.0745 150 SER A O   
590   C CB  . SER A 86  ? 0.5829 0.4932 0.4605 0.0361  -0.0417 -0.0526 150 SER A CB  
591   O OG  . SER A 86  ? 0.9799 0.8770 0.8548 0.0344  -0.0407 -0.0472 150 SER A OG  
592   N N   . VAL A 87  ? 0.5713 0.5033 0.4590 0.0378  -0.0468 -0.0630 151 VAL A N   
593   C CA  . VAL A 87  ? 0.6236 0.5589 0.5071 0.0458  -0.0511 -0.0674 151 VAL A CA  
594   C C   . VAL A 87  ? 0.6970 0.6133 0.5762 0.0424  -0.0499 -0.0600 151 VAL A C   
595   O O   . VAL A 87  ? 0.9249 0.8329 0.8089 0.0328  -0.0457 -0.0537 151 VAL A O   
596   C CB  . VAL A 87  ? 0.6260 0.5860 0.5223 0.0426  -0.0505 -0.0757 151 VAL A CB  
597   C CG1 . VAL A 87  ? 0.7018 0.6598 0.6058 0.0311  -0.0454 -0.0715 151 VAL A CG1 
598   C CG2 . VAL A 87  ? 0.6243 0.5920 0.5159 0.0537  -0.0555 -0.0821 151 VAL A CG2 
599   N N   . LYS A 88  ? 0.6283 0.5373 0.4984 0.0504  -0.0540 -0.0612 152 LYS A N   
600   C CA  . LYS A 88  ? 0.7373 0.6274 0.6036 0.0469  -0.0537 -0.0551 152 LYS A CA  
601   C C   . LYS A 88  ? 0.8629 0.7645 0.7399 0.0406  -0.0523 -0.0571 152 LYS A C   
602   O O   . LYS A 88  ? 0.9024 0.8215 0.7828 0.0444  -0.0535 -0.0639 152 LYS A O   
603   C CB  . LYS A 88  ? 0.7396 0.6132 0.5895 0.0579  -0.0588 -0.0553 152 LYS A CB  
604   C CG  . LYS A 88  ? 1.0761 0.9262 0.9217 0.0527  -0.0582 -0.0485 152 LYS A CG  
605   C CD  . LYS A 88  ? 1.0175 0.8545 0.8502 0.0613  -0.0638 -0.0505 152 LYS A CD  
606   C CE  . LYS A 88  ? 1.1698 1.0202 1.0109 0.0601  -0.0656 -0.0548 152 LYS A CE  
607   N NZ  . LYS A 88  ? 1.9359 1.7773 1.7633 0.0712  -0.0719 -0.0585 152 LYS A NZ  
608   N N   . LEU A 89  ? 0.5848 0.4775 0.4669 0.0316  -0.0497 -0.0518 153 LEU A N   
609   C CA  . LEU A 89  ? 0.5203 0.4219 0.4096 0.0268  -0.0482 -0.0536 153 LEU A CA  
610   C C   . LEU A 89  ? 0.6496 0.5507 0.5323 0.0348  -0.0526 -0.0574 153 LEU A C   
611   O O   . LEU A 89  ? 0.7979 0.6818 0.6717 0.0392  -0.0567 -0.0553 153 LEU A O   
612   C CB  . LEU A 89  ? 0.5949 0.4862 0.4889 0.0182  -0.0461 -0.0482 153 LEU A CB  
613   C CG  . LEU A 89  ? 0.6280 0.5234 0.5251 0.0150  -0.0452 -0.0496 153 LEU A CG  
614   C CD1 . LEU A 89  ? 0.6046 0.5162 0.5072 0.0105  -0.0399 -0.0525 153 LEU A CD1 
615   C CD2 . LEU A 89  ? 0.5481 0.4313 0.4477 0.0096  -0.0456 -0.0453 153 LEU A CD2 
616   N N   . GLY A 90  ? 0.8420 0.7616 0.7287 0.0365  -0.0513 -0.0633 154 GLY A N   
617   C CA  . GLY A 90  ? 0.7446 0.6679 0.6253 0.0454  -0.0550 -0.0681 154 GLY A CA  
618   C C   . GLY A 90  ? 0.6660 0.6063 0.5459 0.0545  -0.0570 -0.0754 154 GLY A C   
619   O O   . GLY A 90  ? 0.8789 0.8291 0.7560 0.0626  -0.0593 -0.0812 154 GLY A O   
620   N N   . ASP A 91  ? 0.7675 0.7117 0.6495 0.0543  -0.0566 -0.0759 155 ASP A N   
621   C CA  . ASP A 91  ? 0.9777 0.9408 0.8605 0.0633  -0.0593 -0.0843 155 ASP A CA  
622   C C   . ASP A 91  ? 0.8409 0.8289 0.7399 0.0545  -0.0535 -0.0892 155 ASP A C   
623   O O   . ASP A 91  ? 1.0316 1.0162 0.9371 0.0427  -0.0483 -0.0846 155 ASP A O   
624   C CB  . ASP A 91  ? 1.0413 0.9926 0.9135 0.0709  -0.0635 -0.0832 155 ASP A CB  
625   C CG  . ASP A 91  ? 1.4605 1.3889 1.3137 0.0825  -0.0695 -0.0810 155 ASP A CG  
626   O OD1 . ASP A 91  ? 1.7594 1.6867 1.6082 0.0876  -0.0722 -0.0832 155 ASP A OD1 
627   O OD2 . ASP A 91  ? 1.5577 1.4676 1.3987 0.0867  -0.0713 -0.0770 155 ASP A OD2 
628   N N   . PRO A 92  ? 0.8196 0.8328 0.7251 0.0599  -0.0543 -0.0991 156 PRO A N   
629   C CA  . PRO A 92  ? 0.6793 0.7168 0.6011 0.0505  -0.0484 -0.1050 156 PRO A CA  
630   C C   . PRO A 92  ? 0.6522 0.6958 0.5771 0.0518  -0.0511 -0.1084 156 PRO A C   
631   O O   . PRO A 92  ? 0.9141 0.9509 0.8284 0.0643  -0.0582 -0.1097 156 PRO A O   
632   C CB  . PRO A 92  ? 0.6675 0.7304 0.5953 0.0572  -0.0487 -0.1151 156 PRO A CB  
633   C CG  . PRO A 92  ? 0.9889 1.0444 0.9024 0.0748  -0.0580 -0.1174 156 PRO A CG  
634   C CD  . PRO A 92  ? 1.0890 1.1097 0.9875 0.0745  -0.0600 -0.1059 156 PRO A CD  
635   N N   . PRO A 93  ? 0.5984 0.6525 0.5358 0.0397  -0.0457 -0.1098 157 PRO A N   
636   C CA  . PRO A 93  ? 0.6337 0.6959 0.5750 0.0410  -0.0487 -0.1146 157 PRO A CA  
637   C C   . PRO A 93  ? 0.6084 0.6998 0.5580 0.0502  -0.0536 -0.1288 157 PRO A C   
638   O O   . PRO A 93  ? 0.6590 0.7713 0.6233 0.0432  -0.0515 -0.1367 157 PRO A O   
639   C CB  . PRO A 93  ? 0.5280 0.5906 0.4792 0.0244  -0.0411 -0.1120 157 PRO A CB  
640   C CG  . PRO A 93  ? 0.6068 0.6727 0.5631 0.0152  -0.0336 -0.1104 157 PRO A CG  
641   C CD  . PRO A 93  ? 0.5764 0.6274 0.5204 0.0243  -0.0369 -0.1051 157 PRO A CD  
642   N N   . THR A 94  ? 0.9355 1.0278 0.8753 0.0662  -0.0606 -0.1325 158 THR A N   
643   C CA  . THR A 94  ? 0.8985 1.0149 0.8419 0.0795  -0.0679 -0.1459 158 THR A CA  
644   C C   . THR A 94  ? 0.8597 0.9645 0.7929 0.0872  -0.0742 -0.1456 158 THR A C   
645   O O   . THR A 94  ? 0.8608 0.9352 0.7783 0.0877  -0.0742 -0.1342 158 THR A O   
646   C CB  . THR A 94  ? 0.8684 0.9872 0.8009 0.0969  -0.0743 -0.1503 158 THR A CB  
647   O OG1 . THR A 94  ? 1.1100 1.1930 1.0206 0.1024  -0.0765 -0.1384 158 THR A OG1 
648   C CG2 . THR A 94  ? 1.2528 1.3937 1.1985 0.0920  -0.0689 -0.1553 158 THR A CG2 
649   N N   . PRO A 95  ? 0.8164 0.9463 0.7585 0.0937  -0.0795 -0.1587 159 PRO A N   
650   C CA  . PRO A 95  ? 0.8350 0.9562 0.7665 0.1033  -0.0864 -0.1603 159 PRO A CA  
651   C C   . PRO A 95  ? 1.0588 1.1475 0.9614 0.1195  -0.0919 -0.1522 159 PRO A C   
652   O O   . PRO A 95  ? 1.2241 1.2905 1.1129 0.1219  -0.0930 -0.1455 159 PRO A O   
653   C CB  . PRO A 95  ? 0.7025 0.8598 0.6469 0.1130  -0.0935 -0.1786 159 PRO A CB  
654   C CG  . PRO A 95  ? 0.5887 0.7761 0.5587 0.0987  -0.0861 -0.1853 159 PRO A CG  
655   C CD  . PRO A 95  ? 0.6292 0.7989 0.5928 0.0925  -0.0793 -0.1737 159 PRO A CD  
656   N N   . ASP A 96  ? 1.0009 1.0856 0.8938 0.1298  -0.0948 -0.1524 160 ASP A N   
657   C CA  . ASP A 96  ? 1.0043 1.0568 0.8684 0.1450  -0.0998 -0.1456 160 ASP A CA  
658   C C   . ASP A 96  ? 0.9566 0.9742 0.8103 0.1342  -0.0930 -0.1289 160 ASP A C   
659   O O   . ASP A 96  ? 0.9274 0.9140 0.7584 0.1417  -0.0946 -0.1210 160 ASP A O   
660   C CB  . ASP A 96  ? 1.1517 1.2122 1.0089 0.1598  -0.1056 -0.1527 160 ASP A CB  
661   C CG  . ASP A 96  ? 1.1995 1.2991 1.0700 0.1705  -0.1122 -0.1706 160 ASP A CG  
662   O OD1 . ASP A 96  ? 1.2737 1.3876 1.1517 0.1715  -0.1152 -0.1778 160 ASP A OD1 
663   O OD2 . ASP A 96  ? 1.4430 1.5602 1.3172 0.1783  -0.1148 -0.1782 160 ASP A OD2 
664   N N   . LYS A 97  ? 0.8265 0.8492 0.6966 0.1166  -0.0851 -0.1240 161 LYS A N   
665   C CA  . LYS A 97  ? 0.8018 0.7953 0.6650 0.1063  -0.0793 -0.1098 161 LYS A CA  
666   C C   . LYS A 97  ? 0.8397 0.8235 0.7062 0.0953  -0.0744 -0.1027 161 LYS A C   
667   O O   . LYS A 97  ? 1.0256 0.9838 0.8837 0.0898  -0.0706 -0.0915 161 LYS A O   
668   C CB  . LYS A 97  ? 0.7382 0.7384 0.6138 0.0949  -0.0740 -0.1076 161 LYS A CB  
669   C CG  . LYS A 97  ? 0.8644 0.8630 0.7314 0.1053  -0.0780 -0.1103 161 LYS A CG  
670   C CD  . LYS A 97  ? 1.0074 0.9725 0.8501 0.1154  -0.0822 -0.1033 161 LYS A CD  
671   C CE  . LYS A 97  ? 1.0678 1.0280 0.9017 0.1237  -0.0857 -0.1050 161 LYS A CE  
672   N NZ  . LYS A 97  ? 1.4099 1.3352 1.2179 0.1339  -0.0900 -0.0990 161 LYS A NZ  
673   N N   . LEU A 98  ? 0.8987 0.9032 0.7776 0.0921  -0.0745 -0.1099 162 LEU A N   
674   C CA  . LEU A 98  ? 0.7599 0.7570 0.6432 0.0808  -0.0695 -0.1038 162 LEU A CA  
675   C C   . LEU A 98  ? 0.6867 0.6576 0.5500 0.0890  -0.0710 -0.0966 162 LEU A C   
676   O O   . LEU A 98  ? 0.9835 0.9488 0.8311 0.1049  -0.0773 -0.1004 162 LEU A O   
677   C CB  . LEU A 98  ? 0.8474 0.8712 0.7473 0.0761  -0.0701 -0.1141 162 LEU A CB  
678   C CG  . LEU A 98  ? 1.0104 1.0593 0.9315 0.0641  -0.0657 -0.1204 162 LEU A CG  
679   C CD1 . LEU A 98  ? 1.2664 1.3312 1.2020 0.0540  -0.0637 -0.1264 162 LEU A CD1 
680   C CD2 . LEU A 98  ? 0.9098 0.9444 0.8318 0.0525  -0.0585 -0.1099 162 LEU A CD2 
681   N N   . LYS A 99  ? 0.6245 0.5783 0.4871 0.0787  -0.0648 -0.0862 163 LYS A N   
682   C CA  . LYS A 99  ? 0.6933 0.6259 0.5399 0.0840  -0.0641 -0.0798 163 LYS A CA  
683   C C   . LYS A 99  ? 0.6036 0.5427 0.4589 0.0760  -0.0611 -0.0797 163 LYS A C   
684   O O   . LYS A 99  ? 0.6839 0.6227 0.5502 0.0624  -0.0553 -0.0745 163 LYS A O   
685   C CB  . LYS A 99  ? 0.6267 0.5313 0.4624 0.0805  -0.0591 -0.0674 163 LYS A CB  
686   C CG  . LYS A 99  ? 0.6076 0.4922 0.4302 0.0823  -0.0555 -0.0599 163 LYS A CG  
687   C CD  . LYS A 99  ? 0.9243 0.7808 0.7315 0.0837  -0.0522 -0.0504 163 LYS A CD  
688   C CE  . LYS A 99  ? 0.9437 0.7841 0.7489 0.0757  -0.0441 -0.0403 163 LYS A CE  
689   N NZ  . LYS A 99  ? 1.4241 1.2473 1.2075 0.0872  -0.0434 -0.0378 163 LYS A NZ  
690   N N   . PHE A 100 ? 0.6267 0.5717 0.4765 0.0852  -0.0658 -0.0862 164 PHE A N   
691   C CA  . PHE A 100 ? 0.6548 0.6050 0.5119 0.0782  -0.0637 -0.0867 164 PHE A CA  
692   C C   . PHE A 100 ? 0.6215 0.5475 0.4702 0.0726  -0.0565 -0.0734 164 PHE A C   
693   O O   . PHE A 100 ? 0.6738 0.5781 0.5046 0.0804  -0.0552 -0.0663 164 PHE A O   
694   C CB  . PHE A 100 ? 0.6229 0.5803 0.4721 0.0915  -0.0710 -0.0959 164 PHE A CB  
695   C CG  . PHE A 100 ? 0.5987 0.5628 0.4557 0.0848  -0.0701 -0.0984 164 PHE A CG  
696   C CD1 . PHE A 100 ? 0.6149 0.5589 0.4616 0.0829  -0.0651 -0.0885 164 PHE A CD1 
697   C CD2 . PHE A 100 ? 0.5721 0.5630 0.4471 0.0798  -0.0739 -0.1110 164 PHE A CD2 
698   C CE1 . PHE A 100 ? 0.5898 0.5391 0.4425 0.0774  -0.0648 -0.0911 164 PHE A CE1 
699   C CE2 . PHE A 100 ? 0.5003 0.4958 0.3819 0.0730  -0.0734 -0.1139 164 PHE A CE2 
700   C CZ  . PHE A 100 ? 0.5682 0.5423 0.4378 0.0723  -0.0693 -0.1039 164 PHE A CZ  
701   N N   . GLU A 101 ? 0.5610 0.4905 0.4220 0.0593  -0.0514 -0.0702 165 GLU A N   
702   C CA  . GLU A 101 ? 0.6102 0.5207 0.4663 0.0536  -0.0445 -0.0586 165 GLU A CA  
703   C C   . GLU A 101 ? 0.6737 0.5816 0.5266 0.0536  -0.0432 -0.0578 165 GLU A C   
704   O O   . GLU A 101 ? 0.7585 0.6493 0.5979 0.0587  -0.0399 -0.0506 165 GLU A O   
705   C CB  . GLU A 101 ? 0.6467 0.5580 0.5157 0.0402  -0.0396 -0.0538 165 GLU A CB  
706   C CG  . GLU A 101 ? 0.9902 0.8934 0.8566 0.0411  -0.0393 -0.0502 165 GLU A CG  
707   C CD  . GLU A 101 ? 0.9430 0.8228 0.7959 0.0445  -0.0357 -0.0406 165 GLU A CD  
708   O OE1 . GLU A 101 ? 1.1394 1.0090 0.9819 0.0489  -0.0334 -0.0370 165 GLU A OE1 
709   O OE2 . GLU A 101 ? 1.2219 1.0928 1.0740 0.0425  -0.0347 -0.0369 165 GLU A OE2 
710   N N   . ALA A 102 ? 0.5942 0.5183 0.4586 0.0482  -0.0454 -0.0654 166 ALA A N   
711   C CA  . ALA A 102 ? 0.5546 0.4772 0.4152 0.0496  -0.0459 -0.0668 166 ALA A CA  
712   C C   . ALA A 102 ? 0.6007 0.5433 0.4748 0.0437  -0.0499 -0.0783 166 ALA A C   
713   O O   . ALA A 102 ? 0.5741 0.5318 0.4611 0.0377  -0.0509 -0.0842 166 ALA A O   
714   C CB  . ALA A 102 ? 0.4908 0.4005 0.3507 0.0422  -0.0388 -0.0568 166 ALA A CB  
715   N N   . VAL A 103 ? 0.5605 0.5029 0.4316 0.0451  -0.0519 -0.0817 167 VAL A N   
716   C CA  . VAL A 103 ? 0.5789 0.5374 0.4636 0.0362  -0.0544 -0.0920 167 VAL A CA  
717   C C   . VAL A 103 ? 0.6490 0.5993 0.5377 0.0233  -0.0481 -0.0859 167 VAL A C   
718   O O   . VAL A 103 ? 0.9218 0.8565 0.8004 0.0255  -0.0450 -0.0779 167 VAL A O   
719   C CB  . VAL A 103 ? 0.6509 0.6137 0.5303 0.0445  -0.0613 -0.1009 167 VAL A CB  
720   C CG1 . VAL A 103 ? 0.8335 0.8078 0.7095 0.0586  -0.0694 -0.1101 167 VAL A CG1 
721   C CG2 . VAL A 103 ? 1.0765 1.0189 0.9387 0.0516  -0.0591 -0.0921 167 VAL A CG2 
722   N N   . GLY A 104 ? 0.6322 0.5923 0.5344 0.0105  -0.0457 -0.0899 168 GLY A N   
723   C CA  . GLY A 104 ? 0.5632 0.5134 0.4666 -0.0011 -0.0400 -0.0847 168 GLY A CA  
724   C C   . GLY A 104 ? 0.6111 0.5699 0.5267 -0.0138 -0.0363 -0.0878 168 GLY A C   
725   O O   . GLY A 104 ? 0.4929 0.4658 0.4168 -0.0137 -0.0373 -0.0924 168 GLY A O   
726   N N   . TRP A 105 ? 0.7173 0.6665 0.6321 -0.0242 -0.0316 -0.0850 169 TRP A N   
727   C CA  . TRP A 105 ? 0.6686 0.6213 0.5912 -0.0368 -0.0265 -0.0868 169 TRP A CA  
728   C C   . TRP A 105 ? 0.6132 0.5511 0.5300 -0.0391 -0.0214 -0.0763 169 TRP A C   
729   O O   . TRP A 105 ? 0.6683 0.6037 0.5870 -0.0483 -0.0165 -0.0759 169 TRP A O   
730   C CB  . TRP A 105 ? 0.5599 0.5114 0.4842 -0.0474 -0.0251 -0.0935 169 TRP A CB  
731   C CG  . TRP A 105 ? 0.5742 0.5054 0.4857 -0.0471 -0.0243 -0.0878 169 TRP A CG  
732   C CD1 . TRP A 105 ? 0.6722 0.5851 0.5744 -0.0500 -0.0196 -0.0788 169 TRP A CD1 
733   C CD2 . TRP A 105 ? 0.5546 0.4815 0.4599 -0.0424 -0.0291 -0.0914 169 TRP A CD2 
734   N NE1 . TRP A 105 ? 0.7909 0.6895 0.6820 -0.0471 -0.0209 -0.0767 169 TRP A NE1 
735   C CE2 . TRP A 105 ? 0.6873 0.5929 0.5794 -0.0429 -0.0262 -0.0837 169 TRP A CE2 
736   C CE3 . TRP A 105 ? 0.6401 0.5782 0.5485 -0.0370 -0.0356 -0.1004 169 TRP A CE3 
737   C CZ2 . TRP A 105 ? 0.8202 0.7161 0.7026 -0.0382 -0.0295 -0.0847 169 TRP A CZ2 
738   C CZ3 . TRP A 105 ? 0.8275 0.7551 0.7256 -0.0323 -0.0393 -0.1015 169 TRP A CZ3 
739   C CH2 . TRP A 105 ? 0.9069 0.8136 0.7922 -0.0330 -0.0360 -0.0936 169 TRP A CH2 
740   N N   . SER A 106 ? 0.5815 0.5094 0.4910 -0.0308 -0.0222 -0.0681 170 SER A N   
741   C CA  . SER A 106 ? 0.7131 0.6292 0.6189 -0.0321 -0.0184 -0.0593 170 SER A CA  
742   C C   . SER A 106 ? 0.7485 0.6599 0.6506 -0.0226 -0.0196 -0.0523 170 SER A C   
743   O O   . SER A 106 ? 0.7282 0.6373 0.6251 -0.0155 -0.0215 -0.0515 170 SER A O   
744   C CB  . SER A 106 ? 0.7567 0.6585 0.6551 -0.0379 -0.0152 -0.0567 170 SER A CB  
745   O OG  . SER A 106 ? 0.9954 0.8863 0.8889 -0.0345 -0.0136 -0.0484 170 SER A OG  
746   N N   . ALA A 107 ? 0.5749 0.4841 0.4792 -0.0227 -0.0180 -0.0475 171 ALA A N   
747   C CA  . ALA A 107 ? 0.5538 0.4604 0.4568 -0.0155 -0.0188 -0.0424 171 ALA A CA  
748   C C   . ALA A 107 ? 0.6004 0.5007 0.5053 -0.0173 -0.0166 -0.0365 171 ALA A C   
749   O O   . ALA A 107 ? 0.7159 0.6166 0.6235 -0.0224 -0.0158 -0.0373 171 ALA A O   
750   C CB  . ALA A 107 ? 0.4729 0.3888 0.3779 -0.0104 -0.0221 -0.0467 171 ALA A CB  
751   N N   . SER A 108 ? 0.6133 0.5078 0.5166 -0.0130 -0.0157 -0.0309 172 SER A N   
752   C CA  . SER A 108 ? 0.5782 0.4686 0.4853 -0.0141 -0.0145 -0.0263 172 SER A CA  
753   C C   . SER A 108 ? 0.6381 0.5249 0.5437 -0.0092 -0.0139 -0.0227 172 SER A C   
754   O O   . SER A 108 ? 0.6737 0.5586 0.5730 -0.0041 -0.0134 -0.0221 172 SER A O   
755   C CB  . SER A 108 ? 0.7187 0.6042 0.6258 -0.0158 -0.0122 -0.0231 172 SER A CB  
756   O OG  . SER A 108 ? 0.8812 0.7642 0.7925 -0.0146 -0.0106 -0.0185 172 SER A OG  
757   N N   . SER A 109 ? 0.5567 0.4407 0.4665 -0.0104 -0.0139 -0.0203 173 SER A N   
758   C CA  . SER A 109 ? 0.5513 0.4287 0.4579 -0.0069 -0.0128 -0.0169 173 SER A CA  
759   C C   . SER A 109 ? 0.5828 0.4559 0.4959 -0.0104 -0.0120 -0.0140 173 SER A C   
760   O O   . SER A 109 ? 0.6576 0.5339 0.5773 -0.0142 -0.0139 -0.0156 173 SER A O   
761   C CB  . SER A 109 ? 0.7472 0.6254 0.6475 -0.0017 -0.0164 -0.0205 173 SER A CB  
762   O OG  . SER A 109 ? 0.6633 0.5455 0.5677 -0.0035 -0.0196 -0.0237 173 SER A OG  
763   N N   . CYS A 110 ? 0.5508 0.4154 0.4611 -0.0091 -0.0091 -0.0100 174 CYS A N   
764   C CA  . CYS A 110 ? 0.6031 0.4633 0.5209 -0.0137 -0.0075 -0.0075 174 CYS A CA  
765   C C   . CYS A 110 ? 0.7114 0.5591 0.6213 -0.0119 -0.0034 -0.0033 174 CYS A C   
766   O O   . CYS A 110 ? 0.7413 0.5849 0.6422 -0.0077 0.0004  -0.0006 174 CYS A O   
767   C CB  . CYS A 110 ? 0.6937 0.5598 0.6222 -0.0180 -0.0047 -0.0063 174 CYS A CB  
768   S SG  . CYS A 110 ? 0.9792 0.8482 0.9036 -0.0152 0.0002  -0.0038 174 CYS A SG  
769   N N   . HIS A 111 ? 0.6441 0.4839 0.5559 -0.0147 -0.0041 -0.0027 175 HIS A N   
770   C CA  . HIS A 111 ? 0.6003 0.4241 0.5023 -0.0138 0.0002  0.0015  175 HIS A CA  
771   C C   . HIS A 111 ? 0.6478 0.4685 0.5600 -0.0219 0.0068  0.0050  175 HIS A C   
772   O O   . HIS A 111 ? 0.9266 0.7524 0.8525 -0.0281 0.0045  0.0027  175 HIS A O   
773   C CB  . HIS A 111 ? 0.7835 0.5984 0.6788 -0.0113 -0.0051 -0.0008 175 HIS A CB  
774   C CG  . HIS A 111 ? 0.8266 0.6208 0.7053 -0.0077 -0.0019 0.0030  175 HIS A CG  
775   N ND1 . HIS A 111 ? 0.8431 0.6236 0.7228 -0.0143 0.0035  0.0068  175 HIS A ND1 
776   C CD2 . HIS A 111 ? 0.8909 0.6750 0.7500 0.0026  -0.0034 0.0030  175 HIS A CD2 
777   C CE1 . HIS A 111 ? 1.0761 0.8355 0.9353 -0.0087 0.0061  0.0101  175 HIS A CE1 
778   N NE2 . HIS A 111 ? 0.8002 0.5620 0.6462 0.0026  0.0013  0.0076  175 HIS A NE2 
779   N N   . ASP A 112 ? 0.7406 0.5534 0.6465 -0.0219 0.0151  0.0102  176 ASP A N   
780   C CA  . ASP A 112 ? 0.7336 0.5460 0.6514 -0.0308 0.0233  0.0134  176 ASP A CA  
781   C C   . ASP A 112 ? 0.7893 0.5849 0.7052 -0.0371 0.0269  0.0155  176 ASP A C   
782   O O   . ASP A 112 ? 0.8678 0.6655 0.7972 -0.0463 0.0333  0.0167  176 ASP A O   
783   C CB  . ASP A 112 ? 0.7449 0.5575 0.6582 -0.0292 0.0325  0.0182  176 ASP A CB  
784   C CG  . ASP A 112 ? 0.8810 0.6735 0.7701 -0.0220 0.0371  0.0230  176 ASP A CG  
785   O OD1 . ASP A 112 ? 1.0090 0.7864 0.8844 -0.0183 0.0334  0.0228  176 ASP A OD1 
786   O OD2 . ASP A 112 ? 1.0947 0.8864 0.9773 -0.0189 0.0443  0.0269  176 ASP A OD2 
787   N N   . GLY A 113 ? 0.9038 0.6832 0.8034 -0.0320 0.0227  0.0154  177 GLY A N   
788   C CA  . GLY A 113 ? 0.8631 0.6209 0.7555 -0.0368 0.0259  0.0177  177 GLY A CA  
789   C C   . GLY A 113 ? 0.9376 0.6712 0.8029 -0.0296 0.0316  0.0233  177 GLY A C   
790   O O   . GLY A 113 ? 1.3276 1.0377 1.1793 -0.0307 0.0335  0.0255  177 GLY A O   
791   N N   . PHE A 114 ? 1.0027 0.7404 0.8581 -0.0213 0.0336  0.0253  178 PHE A N   
792   C CA  . PHE A 114 ? 0.9174 0.6335 0.7450 -0.0115 0.0378  0.0298  178 PHE A CA  
793   C C   . PHE A 114 ? 0.9932 0.7152 0.8083 0.0026  0.0283  0.0255  178 PHE A C   
794   O O   . PHE A 114 ? 1.1390 0.8466 0.9359 0.0113  0.0230  0.0240  178 PHE A O   
795   C CB  . PHE A 114 ? 0.9826 0.6969 0.8078 -0.0133 0.0497  0.0358  178 PHE A CB  
796   C CG  . PHE A 114 ? 1.1139 0.8238 0.9519 -0.0275 0.0607  0.0397  178 PHE A CG  
797   C CD1 . PHE A 114 ? 1.0974 0.7792 0.9214 -0.0322 0.0676  0.0441  178 PHE A CD1 
798   C CD2 . PHE A 114 ? 1.0687 0.8023 0.9328 -0.0362 0.0643  0.0384  178 PHE A CD2 
799   C CE1 . PHE A 114 ? 1.0799 0.7587 0.9181 -0.0473 0.0786  0.0469  178 PHE A CE1 
800   C CE2 . PHE A 114 ? 1.1662 0.8995 1.0453 -0.0498 0.0745  0.0406  178 PHE A CE2 
801   C CZ  . PHE A 114 ? 1.0529 0.7594 0.9202 -0.0563 0.0821  0.0448  178 PHE A CZ  
802   N N   . GLN A 115 ? 0.7980 0.5411 0.6229 0.0049  0.0262  0.0231  179 GLN A N   
803   C CA  . GLN A 115 ? 0.7704 0.5228 0.5874 0.0164  0.0174  0.0177  179 GLN A CA  
804   C C   . GLN A 115 ? 0.6469 0.4254 0.4847 0.0126  0.0108  0.0117  179 GLN A C   
805   O O   . GLN A 115 ? 0.7271 0.5161 0.5834 0.0030  0.0128  0.0120  179 GLN A O   
806   C CB  . GLN A 115 ? 0.9192 0.6656 0.7197 0.0254  0.0216  0.0205  179 GLN A CB  
807   C CG  . GLN A 115 ? 0.9103 0.6272 0.6842 0.0317  0.0281  0.0265  179 GLN A CG  
808   C CD  . GLN A 115 ? 1.0223 0.7271 0.7769 0.0435  0.0198  0.0226  179 GLN A CD  
809   O OE1 . GLN A 115 ? 1.3335 1.0548 1.0956 0.0474  0.0094  0.0150  179 GLN A OE1 
810   N NE2 . GLN A 115 ? 1.2392 0.9147 0.9680 0.0494  0.0248  0.0276  179 GLN A NE2 
811   N N   . TRP A 116 ? 0.6478 0.4365 0.4825 0.0202  0.0028  0.0057  180 TRP A N   
812   C CA  . TRP A 116 ? 0.5739 0.3846 0.4261 0.0158  -0.0017 0.0006  180 TRP A CA  
813   C C   . TRP A 116 ? 0.6292 0.4474 0.4825 0.0169  0.0011  0.0013  180 TRP A C   
814   O O   . TRP A 116 ? 0.6625 0.4755 0.5014 0.0256  0.0015  0.0015  180 TRP A O   
815   C CB  . TRP A 116 ? 0.6374 0.4578 0.4879 0.0218  -0.0104 -0.0068 180 TRP A CB  
816   C CG  . TRP A 116 ? 0.6405 0.4598 0.4947 0.0198  -0.0146 -0.0092 180 TRP A CG  
817   C CD1 . TRP A 116 ? 0.7068 0.5133 0.5476 0.0266  -0.0177 -0.0100 180 TRP A CD1 
818   C CD2 . TRP A 116 ? 0.6788 0.5089 0.5491 0.0117  -0.0167 -0.0114 180 TRP A CD2 
819   N NE1 . TRP A 116 ? 0.8074 0.6171 0.6558 0.0231  -0.0217 -0.0126 180 TRP A NE1 
820   C CE2 . TRP A 116 ? 0.7133 0.5371 0.5795 0.0142  -0.0212 -0.0135 180 TRP A CE2 
821   C CE3 . TRP A 116 ? 0.6831 0.5256 0.5682 0.0043  -0.0158 -0.0120 180 TRP A CE3 
822   C CZ2 . TRP A 116 ? 0.7368 0.5672 0.6139 0.0091  -0.0243 -0.0161 180 TRP A CZ2 
823   C CZ3 . TRP A 116 ? 0.7346 0.5828 0.6295 -0.0005 -0.0189 -0.0145 180 TRP A CZ3 
824   C CH2 . TRP A 116 ? 0.6999 0.5425 0.5912 0.0018  -0.0230 -0.0165 180 TRP A CH2 
825   N N   . THR A 117 ? 0.6273 0.4576 0.4964 0.0093  0.0023  0.0010  181 THR A N   
826   C CA  . THR A 117 ? 0.5828 0.4205 0.4523 0.0108  0.0038  0.0007  181 THR A CA  
827   C C   . THR A 117 ? 0.5959 0.4472 0.4713 0.0106  -0.0032 -0.0062 181 THR A C   
828   O O   . THR A 117 ? 0.7559 0.6136 0.6418 0.0049  -0.0060 -0.0086 181 THR A O   
829   C CB  . THR A 117 ? 0.5668 0.4079 0.4477 0.0040  0.0098  0.0046  181 THR A CB  
830   O OG1 . THR A 117 ? 0.6988 0.5278 0.5757 0.0025  0.0177  0.0108  181 THR A OG1 
831   C CG2 . THR A 117 ? 0.4372 0.2852 0.3172 0.0066  0.0106  0.0039  181 THR A CG2 
832   N N   . VAL A 118 ? 0.5812 0.4360 0.4492 0.0166  -0.0059 -0.0098 182 VAL A N   
833   C CA  . VAL A 118 ? 0.5978 0.4655 0.4719 0.0148  -0.0112 -0.0168 182 VAL A CA  
834   C C   . VAL A 118 ? 0.7037 0.5751 0.5765 0.0153  -0.0108 -0.0183 182 VAL A C   
835   O O   . VAL A 118 ? 1.0318 0.8988 0.8939 0.0226  -0.0105 -0.0180 182 VAL A O   
836   C CB  . VAL A 118 ? 0.4958 0.3682 0.3648 0.0209  -0.0173 -0.0235 182 VAL A CB  
837   C CG1 . VAL A 118 ? 0.5458 0.4330 0.4228 0.0173  -0.0214 -0.0314 182 VAL A CG1 
838   C CG2 . VAL A 118 ? 0.4527 0.3224 0.3231 0.0204  -0.0187 -0.0231 182 VAL A CG2 
839   N N   . LEU A 119 ? 0.5400 0.4177 0.4217 0.0083  -0.0112 -0.0200 183 LEU A N   
840   C CA  . LEU A 119 ? 0.5992 0.4786 0.4787 0.0082  -0.0114 -0.0221 183 LEU A CA  
841   C C   . LEU A 119 ? 0.6272 0.5146 0.5092 0.0054  -0.0161 -0.0301 183 LEU A C   
842   O O   . LEU A 119 ? 0.8579 0.7498 0.7472 -0.0013 -0.0168 -0.0323 183 LEU A O   
843   C CB  . LEU A 119 ? 0.5466 0.4245 0.4313 0.0031  -0.0082 -0.0187 183 LEU A CB  
844   C CG  . LEU A 119 ? 0.6027 0.4767 0.4900 0.0035  -0.0029 -0.0119 183 LEU A CG  
845   C CD1 . LEU A 119 ? 0.7327 0.6092 0.6311 -0.0029 -0.0028 -0.0109 183 LEU A CD1 
846   C CD2 . LEU A 119 ? 0.6181 0.4899 0.5010 0.0068  0.0004  -0.0094 183 LEU A CD2 
847   N N   . SER A 120 ? 0.7018 0.5910 0.5775 0.0104  -0.0191 -0.0347 184 SER A N   
848   C CA  . SER A 120 ? 0.7171 0.6157 0.5968 0.0070  -0.0233 -0.0436 184 SER A CA  
849   C C   . SER A 120 ? 0.7107 0.6065 0.5862 0.0058  -0.0241 -0.0464 184 SER A C   
850   O O   . SER A 120 ? 0.9666 0.8549 0.8333 0.0120  -0.0230 -0.0429 184 SER A O   
851   C CB  . SER A 120 ? 0.9143 0.8200 0.7916 0.0145  -0.0282 -0.0496 184 SER A CB  
852   O OG  . SER A 120 ? 1.4391 1.3575 1.3230 0.0108  -0.0324 -0.0597 184 SER A OG  
853   N N   . VAL A 121 ? 0.5531 0.4541 0.4342 -0.0023 -0.0254 -0.0527 185 VAL A N   
854   C CA  . VAL A 121 ? 0.5580 0.4549 0.4346 -0.0046 -0.0266 -0.0566 185 VAL A CA  
855   C C   . VAL A 121 ? 0.6469 0.5556 0.5277 -0.0049 -0.0319 -0.0676 185 VAL A C   
856   O O   . VAL A 121 ? 0.6934 0.6135 0.5843 -0.0109 -0.0324 -0.0729 185 VAL A O   
857   C CB  . VAL A 121 ? 0.5598 0.4512 0.4386 -0.0153 -0.0234 -0.0560 185 VAL A CB  
858   C CG1 . VAL A 121 ? 0.5830 0.4678 0.4557 -0.0186 -0.0248 -0.0609 185 VAL A CG1 
859   C CG2 . VAL A 121 ? 0.6244 0.5068 0.5006 -0.0144 -0.0193 -0.0469 185 VAL A CG2 
860   N N   . ALA A 122 ? 0.6300 0.5369 0.5034 0.0019  -0.0361 -0.0717 186 ALA A N   
861   C CA  . ALA A 122 ? 0.5765 0.4963 0.4544 0.0033  -0.0426 -0.0838 186 ALA A CA  
862   C C   . ALA A 122 ? 0.6735 0.5881 0.5445 0.0048  -0.0466 -0.0896 186 ALA A C   
863   O O   . ALA A 122 ? 0.6202 0.5198 0.4807 0.0063  -0.0443 -0.0837 186 ALA A O   
864   C CB  . ALA A 122 ? 0.7018 0.6282 0.5766 0.0161  -0.0467 -0.0851 186 ALA A CB  
865   N N   . GLY A 123 ? 0.7526 0.6804 0.6297 0.0052  -0.0533 -0.1021 187 GLY A N   
866   C CA  . GLY A 123 ? 0.7217 0.6466 0.5938 0.0065  -0.0588 -0.1104 187 GLY A CA  
867   C C   . GLY A 123 ? 0.7513 0.6597 0.6169 -0.0019 -0.0556 -0.1077 187 GLY A C   
868   O O   . GLY A 123 ? 0.6724 0.5802 0.5454 -0.0164 -0.0521 -0.1102 187 GLY A O   
869   N N   . ASP A 124 ? 1.0474 0.9411 0.8971 0.0080  -0.0565 -0.1025 188 ASP A N   
870   C CA  . ASP A 124 ? 1.1419 1.0176 0.9813 0.0039  -0.0540 -0.0990 188 ASP A CA  
871   C C   . ASP A 124 ? 0.9904 0.8584 0.8322 -0.0063 -0.0460 -0.0906 188 ASP A C   
872   O O   . ASP A 124 ? 0.9768 0.8326 0.8142 -0.0148 -0.0442 -0.0913 188 ASP A O   
873   C CB  . ASP A 124 ? 1.3304 1.1942 1.1526 0.0192  -0.0548 -0.0926 188 ASP A CB  
874   C CG  . ASP A 124 ? 1.8826 1.7282 1.6931 0.0179  -0.0510 -0.0862 188 ASP A CG  
875   O OD1 . ASP A 124 ? 2.4944 2.3315 2.3023 0.0097  -0.0529 -0.0920 188 ASP A OD1 
876   O OD2 . ASP A 124 ? 2.2385 2.0778 2.0418 0.0255  -0.0462 -0.0758 188 ASP A OD2 
877   N N   . GLY A 125 ? 0.8188 0.6928 0.6666 -0.0051 -0.0417 -0.0832 189 GLY A N   
878   C CA  . GLY A 125 ? 0.6778 0.5443 0.5262 -0.0114 -0.0351 -0.0748 189 GLY A CA  
879   C C   . GLY A 125 ? 0.7613 0.6224 0.6031 -0.0011 -0.0319 -0.0640 189 GLY A C   
880   O O   . GLY A 125 ? 0.8146 0.6679 0.6543 -0.0034 -0.0275 -0.0572 189 GLY A O   
881   N N   . PHE A 126 ? 0.5836 0.4486 0.4217 0.0102  -0.0339 -0.0629 190 PHE A N   
882   C CA  . PHE A 126 ? 0.6218 0.4836 0.4560 0.0182  -0.0293 -0.0528 190 PHE A CA  
883   C C   . PHE A 126 ? 0.8225 0.6924 0.6661 0.0170  -0.0265 -0.0488 190 PHE A C   
884   O O   . PHE A 126 ? 0.6269 0.5064 0.4798 0.0117  -0.0287 -0.0538 190 PHE A O   
885   C CB  . PHE A 126 ? 0.7071 0.5655 0.5293 0.0313  -0.0310 -0.0522 190 PHE A CB  
886   C CG  . PHE A 126 ? 0.8009 0.6673 0.6234 0.0376  -0.0353 -0.0571 190 PHE A CG  
887   C CD1 . PHE A 126 ? 1.0605 0.9256 0.8783 0.0461  -0.0322 -0.0507 190 PHE A CD1 
888   C CD2 . PHE A 126 ? 1.0292 0.9040 0.8558 0.0356  -0.0426 -0.0686 190 PHE A CD2 
889   C CE1 . PHE A 126 ? 1.0278 0.8977 0.8423 0.0539  -0.0367 -0.0554 190 PHE A CE1 
890   C CE2 . PHE A 126 ? 0.9590 0.8425 0.7852 0.0436  -0.0478 -0.0743 190 PHE A CE2 
891   C CZ  . PHE A 126 ? 0.8720 0.7519 0.6907 0.0535  -0.0451 -0.0674 190 PHE A CZ  
892   N N   . VAL A 127 ? 0.7289 0.5949 0.5699 0.0222  -0.0216 -0.0400 191 VAL A N   
893   C CA  . VAL A 127 ? 0.6463 0.5164 0.4946 0.0209  -0.0185 -0.0352 191 VAL A CA  
894   C C   . VAL A 127 ? 0.7484 0.6161 0.5890 0.0309  -0.0173 -0.0320 191 VAL A C   
895   O O   . VAL A 127 ? 0.7930 0.6537 0.6243 0.0380  -0.0137 -0.0270 191 VAL A O   
896   C CB  . VAL A 127 ? 0.7325 0.5997 0.5859 0.0165  -0.0131 -0.0283 191 VAL A CB  
897   C CG1 . VAL A 127 ? 0.7733 0.6416 0.6310 0.0177  -0.0091 -0.0222 191 VAL A CG1 
898   C CG2 . VAL A 127 ? 0.6846 0.5538 0.5454 0.0068  -0.0143 -0.0312 191 VAL A CG2 
899   N N   . SER A 128 ? 0.7637 0.6365 0.6067 0.0322  -0.0202 -0.0350 192 SER A N   
900   C CA  . SER A 128 ? 0.7131 0.5804 0.5471 0.0412  -0.0184 -0.0310 192 SER A CA  
901   C C   . SER A 128 ? 0.7340 0.5993 0.5753 0.0356  -0.0129 -0.0239 192 SER A C   
902   O O   . SER A 128 ? 1.0662 0.9379 0.9195 0.0270  -0.0136 -0.0253 192 SER A O   
903   C CB  . SER A 128 ? 0.8363 0.7095 0.6683 0.0464  -0.0251 -0.0385 192 SER A CB  
904   O OG  . SER A 128 ? 0.9550 0.8304 0.7798 0.0531  -0.0310 -0.0460 192 SER A OG  
905   N N   . ILE A 129 ? 0.6594 0.5152 0.4928 0.0405  -0.0071 -0.0166 193 ILE A N   
906   C CA  . ILE A 129 ? 0.6405 0.4935 0.4805 0.0352  -0.0020 -0.0106 193 ILE A CA  
907   C C   . ILE A 129 ? 0.6816 0.5254 0.5097 0.0427  -0.0019 -0.0092 193 ILE A C   
908   O O   . ILE A 129 ? 0.7819 0.6153 0.5941 0.0519  0.0008  -0.0064 193 ILE A O   
909   C CB  . ILE A 129 ? 0.6459 0.4947 0.4875 0.0332  0.0065  -0.0030 193 ILE A CB  
910   C CG1 . ILE A 129 ? 0.7014 0.5584 0.5540 0.0268  0.0057  -0.0047 193 ILE A CG1 
911   C CG2 . ILE A 129 ? 0.6529 0.4969 0.4993 0.0288  0.0124  0.0029  193 ILE A CG2 
912   C CD1 . ILE A 129 ? 0.8621 0.7184 0.7164 0.0268  0.0129  0.0008  193 ILE A CD1 
913   N N   . LEU A 130 ? 0.6082 0.4537 0.4410 0.0401  -0.0048 -0.0110 194 LEU A N   
914   C CA  . LEU A 130 ? 0.6863 0.5195 0.5046 0.0482  -0.0045 -0.0091 194 LEU A CA  
915   C C   . LEU A 130 ? 0.7439 0.5684 0.5645 0.0433  -0.0002 -0.0037 194 LEU A C   
916   O O   . LEU A 130 ? 1.0607 0.8927 0.8952 0.0352  -0.0023 -0.0054 194 LEU A O   
917   C CB  . LEU A 130 ? 0.7494 0.5872 0.5596 0.0578  -0.0134 -0.0177 194 LEU A CB  
918   C CG  . LEU A 130 ? 0.9691 0.8246 0.7938 0.0529  -0.0207 -0.0266 194 LEU A CG  
919   C CD1 . LEU A 130 ? 1.1543 1.0082 0.9763 0.0564  -0.0241 -0.0286 194 LEU A CD1 
920   C CD2 . LEU A 130 ? 0.8234 0.6882 0.6454 0.0589  -0.0271 -0.0352 194 LEU A CD2 
921   N N   . TYR A 131 ? 0.6956 0.5023 0.5006 0.0484  0.0061  0.0028  195 TYR A N   
922   C CA  . TYR A 131 ? 0.8211 0.6158 0.6268 0.0425  0.0123  0.0091  195 TYR A CA  
923   C C   . TYR A 131 ? 0.8271 0.6058 0.6137 0.0517  0.0096  0.0086  195 TYR A C   
924   O O   . TYR A 131 ? 0.7922 0.5562 0.5570 0.0626  0.0114  0.0106  195 TYR A O   
925   C CB  . TYR A 131 ? 0.6912 0.4765 0.4944 0.0391  0.0241  0.0175  195 TYR A CB  
926   C CG  . TYR A 131 ? 0.6621 0.4387 0.4722 0.0293  0.0313  0.0230  195 TYR A CG  
927   C CD1 . TYR A 131 ? 0.6452 0.4354 0.4787 0.0175  0.0304  0.0215  195 TYR A CD1 
928   C CD2 . TYR A 131 ? 0.6799 0.4335 0.4722 0.0317  0.0389  0.0292  195 TYR A CD2 
929   C CE1 . TYR A 131 ? 0.6641 0.4474 0.5055 0.0080  0.0362  0.0252  195 TYR A CE1 
930   C CE2 . TYR A 131 ? 0.7617 0.5065 0.5612 0.0210  0.0459  0.0337  195 TYR A CE2 
931   C CZ  . TYR A 131 ? 0.7492 0.5101 0.5744 0.0091  0.0441  0.0312  195 TYR A CZ  
932   O OH  . TYR A 131 ? 1.1033 0.8559 0.9361 -0.0014 0.0502  0.0344  195 TYR A OH  
933   N N   . GLY A 132 ? 0.9257 0.7066 0.7187 0.0485  0.0047  0.0056  196 GLY A N   
934   C CA  . GLY A 132 ? 0.9616 0.7284 0.7361 0.0585  0.0004  0.0039  196 GLY A CA  
935   C C   . GLY A 132 ? 0.8784 0.6511 0.6409 0.0727  -0.0080 -0.0037 196 GLY A C   
936   O O   . GLY A 132 ? 1.1357 0.8916 0.8747 0.0855  -0.0094 -0.0036 196 GLY A O   
937   N N   . GLY A 133 ? 0.8579 0.6537 0.6358 0.0705  -0.0136 -0.0108 197 GLY A N   
938   C CA  . GLY A 133 ? 1.0628 0.8690 0.8343 0.0822  -0.0226 -0.0202 197 GLY A CA  
939   C C   . GLY A 133 ? 0.9936 0.7959 0.7520 0.0913  -0.0222 -0.0206 197 GLY A C   
940   O O   . GLY A 133 ? 1.2367 1.0510 0.9934 0.0997  -0.0304 -0.0299 197 GLY A O   
941   N N   . ILE A 134 ? 0.8494 0.6359 0.5988 0.0899  -0.0128 -0.0113 198 ILE A N   
942   C CA  . ILE A 134 ? 0.9963 0.7773 0.7311 0.0994  -0.0117 -0.0109 198 ILE A CA  
943   C C   . ILE A 134 ? 0.9313 0.7230 0.6814 0.0895  -0.0072 -0.0086 198 ILE A C   
944   O O   . ILE A 134 ? 1.1406 0.9361 0.9068 0.0766  -0.0014 -0.0038 198 ILE A O   
945   C CB  . ILE A 134 ? 0.9803 0.7319 0.6860 0.1095  -0.0041 -0.0024 198 ILE A CB  
946   C CG1 . ILE A 134 ? 1.2547 0.9945 0.9648 0.0975  0.0092  0.0090  198 ILE A CG1 
947   C CG2 . ILE A 134 ? 1.0751 0.8131 0.7626 0.1204  -0.0093 -0.0049 198 ILE A CG2 
948   C CD1 . ILE A 134 ? 1.2894 0.9994 0.9711 0.1053  0.0190  0.0180  198 ILE A CD1 
949   N N   . ILE A 135 ? 1.1084 0.9048 0.8530 0.0965  -0.0106 -0.0128 199 ILE A N   
950   C CA  . ILE A 135 ? 0.9949 0.8014 0.7525 0.0886  -0.0078 -0.0120 199 ILE A CA  
951   C C   . ILE A 135 ? 0.8759 0.6688 0.6251 0.0882  0.0039  -0.0016 199 ILE A C   
952   O O   . ILE A 135 ? 0.8975 0.6766 0.6255 0.0998  0.0065  0.0010  199 ILE A O   
953   C CB  . ILE A 135 ? 0.8637 0.6803 0.6192 0.0955  -0.0164 -0.0214 199 ILE A CB  
954   C CG1 . ILE A 135 ? 0.9472 0.7805 0.7136 0.0950  -0.0272 -0.0330 199 ILE A CG1 
955   C CG2 . ILE A 135 ? 0.7903 0.6141 0.5571 0.0874  -0.0134 -0.0201 199 ILE A CG2 
956   C CD1 . ILE A 135 ? 0.7622 0.6143 0.5488 0.0843  -0.0315 -0.0401 199 ILE A CD1 
957   N N   . THR A 136 ? 0.8754 0.6733 0.6416 0.0752  0.0107  0.0037  200 THR A N   
958   C CA  . THR A 136 ? 0.9558 0.7447 0.7185 0.0730  0.0228  0.0131  200 THR A CA  
959   C C   . THR A 136 ? 0.9567 0.7558 0.7270 0.0710  0.0243  0.0127  200 THR A C   
960   O O   . THR A 136 ? 0.9496 0.7423 0.7127 0.0736  0.0334  0.0189  200 THR A O   
961   C CB  . THR A 136 ? 0.8395 0.6271 0.6156 0.0608  0.0300  0.0189  200 THR A CB  
962   O OG1 . THR A 136 ? 0.9306 0.7349 0.7288 0.0509  0.0237  0.0138  200 THR A OG1 
963   C CG2 . THR A 136 ? 0.9853 0.7558 0.7473 0.0645  0.0312  0.0214  200 THR A CG2 
964   N N   . ASP A 137 ? 0.9506 0.7645 0.7341 0.0668  0.0159  0.0053  201 ASP A N   
965   C CA  . ASP A 137 ? 1.0694 0.8912 0.8597 0.0644  0.0166  0.0046  201 ASP A CA  
966   C C   . ASP A 137 ? 0.8735 0.7065 0.6722 0.0614  0.0064  -0.0045 201 ASP A C   
967   O O   . ASP A 137 ? 0.9018 0.7412 0.7087 0.0569  0.0003  -0.0097 201 ASP A O   
968   C CB  . ASP A 137 ? 1.3856 1.2127 1.1916 0.0543  0.0247  0.0104  201 ASP A CB  
969   C CG  . ASP A 137 ? 1.3463 1.1758 1.1509 0.0570  0.0297  0.0128  201 ASP A CG  
970   O OD1 . ASP A 137 ? 1.4149 1.2462 1.2138 0.0619  0.0240  0.0081  201 ASP A OD1 
971   O OD2 . ASP A 137 ? 1.2738 1.1040 1.0834 0.0540  0.0395  0.0191  201 ASP A OD2 
972   N N   . THR A 138 ? 0.9521 0.7866 0.7477 0.0640  0.0051  -0.0066 202 THR A N   
973   C CA  . THR A 138 ? 0.9279 0.7703 0.7311 0.0591  -0.0027 -0.0144 202 THR A CA  
974   C C   . THR A 138 ? 0.8288 0.6728 0.6370 0.0551  0.0004  -0.0122 202 THR A C   
975   O O   . THR A 138 ? 1.1242 0.9645 0.9269 0.0597  0.0071  -0.0065 202 THR A O   
976   C CB  . THR A 138 ? 0.8981 0.7389 0.6896 0.0674  -0.0105 -0.0222 202 THR A CB  
977   O OG1 . THR A 138 ? 1.1580 0.9900 0.9339 0.0778  -0.0073 -0.0190 202 THR A OG1 
978   C CG2 . THR A 138 ? 0.9928 0.8336 0.7789 0.0733  -0.0151 -0.0260 202 THR A CG2 
979   N N   . ILE A 139 ? 0.8866 0.7357 0.7039 0.0471  -0.0043 -0.0171 203 ILE A N   
980   C CA  . ILE A 139 ? 0.8618 0.7109 0.6822 0.0439  -0.0028 -0.0161 203 ILE A CA  
981   C C   . ILE A 139 ? 0.9632 0.8099 0.7794 0.0420  -0.0100 -0.0240 203 ILE A C   
982   O O   . ILE A 139 ? 0.8582 0.7087 0.6805 0.0354  -0.0147 -0.0297 203 ILE A O   
983   C CB  . ILE A 139 ? 0.7451 0.5997 0.5802 0.0344  -0.0006 -0.0138 203 ILE A CB  
984   C CG1 . ILE A 139 ? 0.7402 0.5973 0.5815 0.0344  0.0066  -0.0068 203 ILE A CG1 
985   C CG2 . ILE A 139 ? 0.7055 0.5586 0.5407 0.0328  -0.0009 -0.0144 203 ILE A CG2 
986   C CD1 . ILE A 139 ? 0.7174 0.5807 0.5742 0.0254  0.0076  -0.0056 203 ILE A CD1 
987   N N   . HIS A 140 ? 0.9596 0.7998 0.7656 0.0473  -0.0105 -0.0246 204 HIS A N   
988   C CA  . HIS A 140 ? 0.7359 0.5706 0.5356 0.0455  -0.0172 -0.0322 204 HIS A CA  
989   C C   . HIS A 140 ? 0.9479 0.7763 0.7460 0.0414  -0.0170 -0.0322 204 HIS A C   
990   O O   . HIS A 140 ? 0.9896 0.8179 0.7879 0.0446  -0.0123 -0.0265 204 HIS A O   
991   C CB  . HIS A 140 ? 0.7609 0.5898 0.5459 0.0564  -0.0201 -0.0349 204 HIS A CB  
992   C CG  . HIS A 140 ? 1.0782 0.9104 0.8602 0.0632  -0.0210 -0.0353 204 HIS A CG  
993   N ND1 . HIS A 140 ? 1.0972 0.9331 0.8801 0.0625  -0.0282 -0.0437 204 HIS A ND1 
994   C CD2 . HIS A 140 ? 1.3541 1.1852 1.1303 0.0717  -0.0150 -0.0284 204 HIS A CD2 
995   C CE1 . HIS A 140 ? 1.0907 0.9273 0.8674 0.0717  -0.0279 -0.0424 204 HIS A CE1 
996   N NE2 . HIS A 140 ? 1.1289 0.9608 0.9003 0.0770  -0.0194 -0.0326 204 HIS A NE2 
997   N N   . PRO A 141 ? 0.9123 0.7350 0.7084 0.0345  -0.0221 -0.0391 205 PRO A N   
998   C CA  . PRO A 141 ? 1.0465 0.8593 0.8384 0.0297  -0.0220 -0.0394 205 PRO A CA  
999   C C   . PRO A 141 ? 1.1676 0.9685 0.9433 0.0385  -0.0233 -0.0396 205 PRO A C   
1000  O O   . PRO A 141 ? 0.9107 0.7062 0.6768 0.0428  -0.0275 -0.0444 205 PRO A O   
1001  C CB  . PRO A 141 ? 0.8589 0.6685 0.6531 0.0184  -0.0259 -0.0469 205 PRO A CB  
1002  C CG  . PRO A 141 ? 0.8202 0.6417 0.6224 0.0180  -0.0286 -0.0513 205 PRO A CG  
1003  C CD  . PRO A 141 ? 0.7388 0.5640 0.5364 0.0305  -0.0278 -0.0475 205 PRO A CD  
1004  N N   . THR A 142 ? 1.4248 1.2224 1.1975 0.0420  -0.0202 -0.0350 206 THR A N   
1005  C CA  . THR A 142 ? 1.4029 1.1891 1.1596 0.0512  -0.0214 -0.0351 206 THR A CA  
1006  C C   . THR A 142 ? 1.6613 1.4301 1.4076 0.0447  -0.0251 -0.0397 206 THR A C   
1007  O O   . THR A 142 ? 1.2494 1.0049 0.9830 0.0443  -0.0297 -0.0452 206 THR A O   
1008  C CB  . THR A 142 ? 1.8568 1.6505 1.6164 0.0595  -0.0161 -0.0287 206 THR A CB  
1009  O OG1 . THR A 142 ? 2.1757 1.9705 1.9425 0.0537  -0.0151 -0.0274 206 THR A OG1 
1010  C CG2 . THR A 142 ? 1.3641 1.1737 1.1349 0.0634  -0.0103 -0.0235 206 THR A CG2 
1011  N N   . ASN A 143 ? 2.0196 1.7870 1.7700 0.0394  -0.0232 -0.0376 207 ASN A N   
1012  C CA  . ASN A 143 ? 1.7120 1.4595 1.4491 0.0340  -0.0253 -0.0407 207 ASN A CA  
1013  C C   . ASN A 143 ? 1.6963 1.4337 1.4306 0.0218  -0.0279 -0.0471 207 ASN A C   
1014  O O   . ASN A 143 ? 1.4028 1.1215 1.1254 0.0153  -0.0283 -0.0495 207 ASN A O   
1015  C CB  . ASN A 143 ? 1.8592 1.6080 1.6016 0.0308  -0.0227 -0.0373 207 ASN A CB  
1016  C CG  . ASN A 143 ? 1.7996 1.5313 1.5238 0.0383  -0.0241 -0.0369 207 ASN A CG  
1017  O OD1 . ASN A 143 ? 1.7851 1.5114 1.4974 0.0494  -0.0258 -0.0372 207 ASN A OD1 
1018  N ND2 . ASN A 143 ? 1.5197 1.2420 1.2401 0.0336  -0.0235 -0.0366 207 ASN A ND2 
1019  N N   . GLY A 144 ? 1.9297 1.6793 1.6743 0.0190  -0.0293 -0.0503 208 GLY A N   
1020  C CA  . GLY A 144 ? 1.4546 1.2000 1.2007 0.0074  -0.0320 -0.0581 208 GLY A CA  
1021  C C   . GLY A 144 ? 1.5477 1.3027 1.3092 -0.0056 -0.0290 -0.0591 208 GLY A C   
1022  O O   . GLY A 144 ? 1.6743 1.4352 1.4427 -0.0062 -0.0253 -0.0535 208 GLY A O   
1023  N N   . GLY A 145 ? 1.3662 1.1239 1.1336 -0.0159 -0.0310 -0.0670 209 GLY A N   
1024  C CA  . GLY A 145 ? 1.3501 1.1185 1.1325 -0.0285 -0.0279 -0.0692 209 GLY A CA  
1025  C C   . GLY A 145 ? 1.0907 0.8804 0.8890 -0.0241 -0.0263 -0.0645 209 GLY A C   
1026  O O   . GLY A 145 ? 0.9604 0.7543 0.7575 -0.0127 -0.0263 -0.0585 209 GLY A O   
1027  N N   . PRO A 146 ? 1.0906 0.8930 0.9032 -0.0334 -0.0243 -0.0670 210 PRO A N   
1028  C CA  . PRO A 146 ? 0.8814 0.7035 0.7085 -0.0292 -0.0240 -0.0642 210 PRO A CA  
1029  C C   . PRO A 146 ? 0.8161 0.6371 0.6431 -0.0242 -0.0204 -0.0548 210 PRO A C   
1030  O O   . PRO A 146 ? 0.9401 0.7490 0.7604 -0.0275 -0.0176 -0.0518 210 PRO A O   
1031  C CB  . PRO A 146 ? 0.8288 0.6614 0.6684 -0.0413 -0.0224 -0.0699 210 PRO A CB  
1032  C CG  . PRO A 146 ? 1.0352 0.8500 0.8657 -0.0516 -0.0181 -0.0699 210 PRO A CG  
1033  C CD  . PRO A 146 ? 1.2259 1.0209 1.0389 -0.0476 -0.0204 -0.0701 210 PRO A CD  
1034  N N   . LEU A 147 ? 0.6064 0.4389 0.4400 -0.0159 -0.0206 -0.0506 211 LEU A N   
1035  C CA  . LEU A 147 ? 0.7014 0.5365 0.5395 -0.0135 -0.0173 -0.0434 211 LEU A CA  
1036  C C   . LEU A 147 ? 0.8923 0.7354 0.7413 -0.0214 -0.0157 -0.0442 211 LEU A C   
1037  O O   . LEU A 147 ? 0.7460 0.5959 0.6009 -0.0279 -0.0167 -0.0502 211 LEU A O   
1038  C CB  . LEU A 147 ? 0.7546 0.5977 0.5959 -0.0038 -0.0168 -0.0386 211 LEU A CB  
1039  C CG  . LEU A 147 ? 0.7866 0.6248 0.6181 0.0061  -0.0170 -0.0365 211 LEU A CG  
1040  C CD1 . LEU A 147 ? 0.7213 0.5680 0.5557 0.0132  -0.0164 -0.0344 211 LEU A CD1 
1041  C CD2 . LEU A 147 ? 0.8617 0.6954 0.6903 0.0099  -0.0141 -0.0310 211 LEU A CD2 
1042  N N   . ARG A 148 ? 0.8452 0.6886 0.6975 -0.0202 -0.0134 -0.0387 212 ARG A N   
1043  C CA  . ARG A 148 ? 0.8193 0.6670 0.6789 -0.0266 -0.0119 -0.0389 212 ARG A CA  
1044  C C   . ARG A 148 ? 0.7875 0.6413 0.6544 -0.0220 -0.0112 -0.0334 212 ARG A C   
1045  O O   . ARG A 148 ? 0.7460 0.5961 0.6103 -0.0165 -0.0106 -0.0293 212 ARG A O   
1046  C CB  . ARG A 148 ? 0.8955 0.7290 0.7457 -0.0326 -0.0099 -0.0395 212 ARG A CB  
1047  C CG  . ARG A 148 ? 1.0079 0.8329 0.8507 -0.0400 -0.0096 -0.0454 212 ARG A CG  
1048  C CD  . ARG A 148 ? 1.1503 0.9575 0.9810 -0.0467 -0.0061 -0.0453 212 ARG A CD  
1049  N NE  . ARG A 148 ? 1.2800 1.0715 1.0966 -0.0396 -0.0066 -0.0409 212 ARG A NE  
1050  C CZ  . ARG A 148 ? 1.2126 0.9907 1.0160 -0.0360 -0.0082 -0.0416 212 ARG A CZ  
1051  N NH1 . ARG A 148 ? 1.1604 0.9381 0.9629 -0.0395 -0.0096 -0.0465 212 ARG A NH1 
1052  N NH2 . ARG A 148 ? 0.9389 0.7045 0.7299 -0.0281 -0.0091 -0.0381 212 ARG A NH2 
1053  N N   . THR A 149 ? 0.8610 0.7248 0.7374 -0.0240 -0.0113 -0.0340 213 THR A N   
1054  C CA  . THR A 149 ? 1.0590 0.9279 0.9428 -0.0206 -0.0109 -0.0294 213 THR A CA  
1055  C C   . THR A 149 ? 0.7965 0.6625 0.6818 -0.0243 -0.0104 -0.0288 213 THR A C   
1056  O O   . THR A 149 ? 0.8252 0.6862 0.7057 -0.0296 -0.0096 -0.0317 213 THR A O   
1057  C CB  . THR A 149 ? 0.9329 0.8114 0.8234 -0.0190 -0.0120 -0.0304 213 THR A CB  
1058  O OG1 . THR A 149 ? 1.0477 0.9315 0.9408 -0.0241 -0.0130 -0.0358 213 THR A OG1 
1059  C CG2 . THR A 149 ? 0.6443 0.5242 0.5313 -0.0128 -0.0127 -0.0303 213 THR A CG2 
1060  N N   . GLN A 150 ? 0.5715 0.4400 0.4630 -0.0217 -0.0106 -0.0254 214 GLN A N   
1061  C CA  . GLN A 150 ? 0.6199 0.4864 0.5128 -0.0239 -0.0112 -0.0254 214 GLN A CA  
1062  C C   . GLN A 150 ? 0.7192 0.5887 0.6132 -0.0287 -0.0110 -0.0286 214 GLN A C   
1063  O O   . GLN A 150 ? 0.9789 0.8433 0.8690 -0.0311 -0.0105 -0.0293 214 GLN A O   
1064  C CB  . GLN A 150 ? 0.7656 0.6368 0.6676 -0.0211 -0.0122 -0.0226 214 GLN A CB  
1065  C CG  . GLN A 150 ? 1.1645 1.0363 1.0684 -0.0170 -0.0114 -0.0201 214 GLN A CG  
1066  C CD  . GLN A 150 ? 0.9233 0.8007 0.8381 -0.0161 -0.0117 -0.0182 214 GLN A CD  
1067  O OE1 . GLN A 150 ? 0.9561 0.8361 0.8758 -0.0178 -0.0121 -0.0178 214 GLN A OE1 
1068  N NE2 . GLN A 150 ? 1.2935 1.1729 1.2122 -0.0133 -0.0118 -0.0175 214 GLN A NE2 
1069  N N   . ALA A 151 ? 0.5709 0.4489 0.4692 -0.0292 -0.0114 -0.0308 215 ALA A N   
1070  C CA  . ALA A 151 ? 0.5553 0.4394 0.4565 -0.0328 -0.0112 -0.0346 215 ALA A CA  
1071  C C   . ALA A 151 ? 0.5436 0.4269 0.4477 -0.0314 -0.0123 -0.0325 215 ALA A C   
1072  O O   . ALA A 151 ? 0.6449 0.5267 0.5468 -0.0342 -0.0113 -0.0340 215 ALA A O   
1073  C CB  . ALA A 151 ? 0.4094 0.2895 0.3050 -0.0395 -0.0083 -0.0381 215 ALA A CB  
1074  N N   . SER A 152 ? 0.4991 0.3824 0.4074 -0.0272 -0.0140 -0.0291 216 SER A N   
1075  C CA  . SER A 152 ? 0.5836 0.4657 0.4956 -0.0257 -0.0159 -0.0276 216 SER A CA  
1076  C C   . SER A 152 ? 0.6847 0.5684 0.6022 -0.0226 -0.0166 -0.0246 216 SER A C   
1077  O O   . SER A 152 ? 0.8659 0.7495 0.7829 -0.0212 -0.0149 -0.0227 216 SER A O   
1078  C CB  . SER A 152 ? 0.6826 0.5575 0.5914 -0.0254 -0.0163 -0.0264 216 SER A CB  
1079  O OG  . SER A 152 ? 0.9830 0.8579 0.8976 -0.0232 -0.0192 -0.0255 216 SER A OG  
1080  N N   . SER A 153 ? 0.5615 0.4453 0.4833 -0.0216 -0.0185 -0.0241 217 SER A N   
1081  C CA  . SER A 153 ? 0.6934 0.5756 0.6198 -0.0203 -0.0181 -0.0209 217 SER A CA  
1082  C C   . SER A 153 ? 0.7230 0.6049 0.6534 -0.0206 -0.0159 -0.0183 217 SER A C   
1083  O O   . SER A 153 ? 0.7270 0.6088 0.6591 -0.0210 -0.0172 -0.0194 217 SER A O   
1084  C CB  . SER A 153 ? 0.6410 0.5209 0.5713 -0.0204 -0.0211 -0.0214 217 SER A CB  
1085  O OG  . SER A 153 ? 0.6892 0.5664 0.6255 -0.0212 -0.0199 -0.0186 217 SER A OG  
1086  N N   . CYS A 154 ? 0.5826 0.4641 0.5132 -0.0194 -0.0126 -0.0153 218 CYS A N   
1087  C CA  . CYS A 154 ? 0.5611 0.4444 0.4973 -0.0195 -0.0097 -0.0129 218 CYS A CA  
1088  C C   . CYS A 154 ? 0.6813 0.5646 0.6275 -0.0222 -0.0094 -0.0119 218 CYS A C   
1089  O O   . CYS A 154 ? 0.5948 0.4745 0.5409 -0.0232 -0.0117 -0.0127 218 CYS A O   
1090  C CB  . CYS A 154 ? 0.6971 0.5792 0.6280 -0.0169 -0.0053 -0.0100 218 CYS A CB  
1091  S SG  . CYS A 154 ? 1.1748 1.0517 1.0963 -0.0139 -0.0049 -0.0092 218 CYS A SG  
1092  N N   . ILE A 155 ? 0.7014 0.5893 0.6566 -0.0234 -0.0067 -0.0109 219 ILE A N   
1093  C CA  . ILE A 155 ? 0.5869 0.4766 0.5542 -0.0274 -0.0068 -0.0115 219 ILE A CA  
1094  C C   . ILE A 155 ? 0.6221 0.5106 0.5934 -0.0301 0.0004  -0.0075 219 ILE A C   
1095  O O   . ILE A 155 ? 0.8391 0.7326 0.8120 -0.0290 0.0054  -0.0056 219 ILE A O   
1096  C CB  . ILE A 155 ? 0.6839 0.5825 0.6613 -0.0272 -0.0100 -0.0154 219 ILE A CB  
1097  C CG1 . ILE A 155 ? 0.8355 0.7314 0.8074 -0.0248 -0.0170 -0.0192 219 ILE A CG1 
1098  C CG2 . ILE A 155 ? 0.7831 0.6872 0.7769 -0.0320 -0.0093 -0.0170 219 ILE A CG2 
1099  C CD1 . ILE A 155 ? 1.1482 1.0400 1.1060 -0.0215 -0.0172 -0.0189 219 ILE A CD1 
1100  N N   . CYS A 156 ? 0.7334 0.6139 0.7049 -0.0335 0.0016  -0.0060 220 CYS A N   
1101  C CA  . CYS A 156 ? 0.8184 0.6947 0.7928 -0.0375 0.0099  -0.0018 220 CYS A CA  
1102  C C   . CYS A 156 ? 0.8674 0.7473 0.8584 -0.0450 0.0100  -0.0043 220 CYS A C   
1103  O O   . CYS A 156 ? 0.9503 0.8275 0.9442 -0.0465 0.0035  -0.0079 220 CYS A O   
1104  C CB  . CYS A 156 ? 0.7450 0.6053 0.7031 -0.0353 0.0126  0.0023  220 CYS A CB  
1105  S SG  . CYS A 156 ? 1.1841 1.0418 1.1239 -0.0261 0.0113  0.0034  220 CYS A SG  
1106  N N   . ASN A 157 ? 0.7615 0.6484 0.7641 -0.0496 0.0175  -0.0030 221 ASN A N   
1107  C CA  . ASN A 157 ? 0.8469 0.7385 0.8676 -0.0584 0.0192  -0.0059 221 ASN A CA  
1108  C C   . ASN A 157 ? 0.9189 0.8097 0.9441 -0.0643 0.0319  -0.0012 221 ASN A C   
1109  O O   . ASN A 157 ? 0.8170 0.7180 0.8445 -0.0617 0.0375  0.0004  221 ASN A O   
1110  C CB  . ASN A 157 ? 0.9975 0.9081 1.0360 -0.0580 0.0127  -0.0133 221 ASN A CB  
1111  C CG  . ASN A 157 ? 1.2360 1.1506 1.2925 -0.0660 0.0094  -0.0190 221 ASN A CG  
1112  O OD1 . ASN A 157 ? 1.0912 0.9924 1.1428 -0.0689 0.0060  -0.0192 221 ASN A OD1 
1113  N ND2 . ASN A 157 ? 1.3640 1.2978 1.4415 -0.0690 0.0098  -0.0245 221 ASN A ND2 
1114  N N   . ASP A 158 ? 0.9824 0.8593 1.0071 -0.0721 0.0370  0.0010  222 ASP A N   
1115  C CA  . ASP A 158 ? 1.1189 0.9910 1.1459 -0.0794 0.0509  0.0061  222 ASP A CA  
1116  C C   . ASP A 158 ? 1.1316 0.9933 1.1373 -0.0721 0.0586  0.0138  222 ASP A C   
1117  O O   . ASP A 158 ? 1.0977 0.9645 1.1071 -0.0743 0.0697  0.0172  222 ASP A O   
1118  C CB  . ASP A 158 ? 1.2866 1.1825 1.3406 -0.0864 0.0559  0.0018  222 ASP A CB  
1119  C CG  . ASP A 158 ? 1.7303 1.6350 1.8068 -0.0956 0.0504  -0.0062 222 ASP A CG  
1120  O OD1 . ASP A 158 ? 2.1110 1.9990 2.1815 -0.0993 0.0463  -0.0066 222 ASP A OD1 
1121  O OD2 . ASP A 158 ? 2.1472 2.0761 2.2474 -0.0984 0.0496  -0.0128 222 ASP A OD2 
1122  N N   . GLY A 159 ? 1.1576 1.0060 1.1417 -0.0629 0.0526  0.0158  223 GLY A N   
1123  C CA  . GLY A 159 ? 1.3054 1.1402 1.2668 -0.0554 0.0588  0.0224  223 GLY A CA  
1124  C C   . GLY A 159 ? 1.0627 0.9099 1.0209 -0.0469 0.0583  0.0225  223 GLY A C   
1125  O O   . GLY A 159 ? 1.0645 0.9008 1.0026 -0.0389 0.0610  0.0268  223 GLY A O   
1126  N N   . THR A 160 ? 0.9599 0.8284 0.9364 -0.0479 0.0543  0.0175  224 THR A N   
1127  C CA  . THR A 160 ? 0.7970 0.6763 0.7698 -0.0394 0.0509  0.0162  224 THR A CA  
1128  C C   . THR A 160 ? 0.6842 0.5677 0.6564 -0.0355 0.0382  0.0108  224 THR A C   
1129  O O   . THR A 160 ? 0.6225 0.5097 0.6056 -0.0399 0.0322  0.0065  224 THR A O   
1130  C CB  . THR A 160 ? 0.7558 0.6541 0.7450 -0.0410 0.0565  0.0148  224 THR A CB  
1131  O OG1 . THR A 160 ? 0.8046 0.7177 0.8154 -0.0466 0.0513  0.0084  224 THR A OG1 
1132  C CG2 . THR A 160 ? 0.9191 0.8142 0.9099 -0.0460 0.0712  0.0203  224 THR A CG2 
1133  N N   . CYS A 161 ? 0.7315 0.6131 0.6900 -0.0275 0.0343  0.0108  225 CYS A N   
1134  C CA  . CYS A 161 ? 0.7760 0.6597 0.7322 -0.0248 0.0239  0.0061  225 CYS A CA  
1135  C C   . CYS A 161 ? 0.7201 0.6134 0.6772 -0.0205 0.0215  0.0036  225 CYS A C   
1136  O O   . CYS A 161 ? 1.2145 1.1091 1.1665 -0.0166 0.0264  0.0060  225 CYS A O   
1137  C CB  . CYS A 161 ? 0.6981 0.5701 0.6373 -0.0203 0.0204  0.0067  225 CYS A CB  
1138  S SG  . CYS A 161 ? 1.2270 1.0839 1.1604 -0.0230 0.0223  0.0094  225 CYS A SG  
1139  N N   . TYR A 162 ? 0.6263 0.5246 0.5878 -0.0205 0.0140  -0.0011 226 TYR A N   
1140  C CA  . TYR A 162 ? 0.5855 0.4895 0.5451 -0.0160 0.0110  -0.0038 226 TYR A CA  
1141  C C   . TYR A 162 ? 0.6051 0.5023 0.5525 -0.0138 0.0049  -0.0061 226 TYR A C   
1142  O O   . TYR A 162 ? 0.5193 0.4134 0.4668 -0.0163 0.0005  -0.0080 226 TYR A O   
1143  C CB  . TYR A 162 ? 0.4725 0.3874 0.4465 -0.0173 0.0082  -0.0080 226 TYR A CB  
1144  C CG  . TYR A 162 ? 0.6123 0.5365 0.6024 -0.0217 0.0141  -0.0073 226 TYR A CG  
1145  C CD1 . TYR A 162 ? 0.8341 0.7691 0.8306 -0.0192 0.0193  -0.0072 226 TYR A CD1 
1146  C CD2 . TYR A 162 ? 0.7199 0.6422 0.7192 -0.0287 0.0150  -0.0071 226 TYR A CD2 
1147  C CE1 . TYR A 162 ? 1.0013 0.9472 1.0150 -0.0246 0.0261  -0.0071 226 TYR A CE1 
1148  C CE2 . TYR A 162 ? 0.7326 0.6632 0.7480 -0.0347 0.0215  -0.0070 226 TYR A CE2 
1149  C CZ  . TYR A 162 ? 0.8881 0.8316 0.9117 -0.0331 0.0275  -0.0070 226 TYR A CZ  
1150  O OH  . TYR A 162 ? 0.8897 0.8436 0.9312 -0.0402 0.0352  -0.0074 226 TYR A OH  
1151  N N   . THR A 163 ? 0.5746 0.4694 0.5115 -0.0094 0.0048  -0.0062 227 THR A N   
1152  C CA  . THR A 163 ? 0.6881 0.5769 0.6148 -0.0090 -0.0001 -0.0090 227 THR A CA  
1153  C C   . THR A 163 ? 0.6455 0.5325 0.5646 -0.0051 -0.0013 -0.0106 227 THR A C   
1154  O O   . THR A 163 ? 0.7151 0.6056 0.6348 -0.0012 0.0018  -0.0092 227 THR A O   
1155  C CB  . THR A 163 ? 0.5549 0.4387 0.4732 -0.0088 -0.0001 -0.0085 227 THR A CB  
1156  O OG1 . THR A 163 ? 1.0199 0.9007 0.9317 -0.0101 -0.0042 -0.0123 227 THR A OG1 
1157  C CG2 . THR A 163 ? 0.4139 0.2958 0.3247 -0.0042 0.0036  -0.0062 227 THR A CG2 
1158  N N   . ILE A 164 ? 0.5279 0.4086 0.4390 -0.0061 -0.0052 -0.0136 228 ILE A N   
1159  C CA  . ILE A 164 ? 0.5026 0.3770 0.4029 -0.0026 -0.0065 -0.0153 228 ILE A CA  
1160  C C   . ILE A 164 ? 0.5607 0.4273 0.4493 -0.0039 -0.0070 -0.0168 228 ILE A C   
1161  O O   . ILE A 164 ? 0.9794 0.8446 0.8674 -0.0086 -0.0082 -0.0185 228 ILE A O   
1162  C CB  . ILE A 164 ? 0.4647 0.3352 0.3628 -0.0021 -0.0101 -0.0178 228 ILE A CB  
1163  C CG1 . ILE A 164 ? 0.4391 0.3196 0.3498 0.0006  -0.0106 -0.0180 228 ILE A CG1 
1164  C CG2 . ILE A 164 ? 0.6390 0.4983 0.5214 0.0020  -0.0114 -0.0195 228 ILE A CG2 
1165  C CD1 . ILE A 164 ? 0.4505 0.3284 0.3610 0.0011  -0.0152 -0.0211 228 ILE A CD1 
1166  N N   . ILE A 165 ? 0.7555 0.6180 0.6353 0.0005  -0.0064 -0.0168 229 ILE A N   
1167  C CA  . ILE A 165 ? 0.7159 0.5711 0.5850 -0.0006 -0.0074 -0.0192 229 ILE A CA  
1168  C C   . ILE A 165 ? 0.7616 0.6043 0.6166 0.0011  -0.0091 -0.0215 229 ILE A C   
1169  O O   . ILE A 165 ? 0.7246 0.5653 0.5748 0.0078  -0.0088 -0.0204 229 ILE A O   
1170  C CB  . ILE A 165 ? 0.6241 0.4828 0.4922 0.0036  -0.0057 -0.0178 229 ILE A CB  
1171  C CG1 . ILE A 165 ? 0.7245 0.5917 0.6032 0.0030  -0.0033 -0.0148 229 ILE A CG1 
1172  C CG2 . ILE A 165 ? 0.5899 0.4435 0.4498 0.0019  -0.0081 -0.0219 229 ILE A CG2 
1173  C CD1 . ILE A 165 ? 0.8008 0.6691 0.6776 0.0032  -0.0040 -0.0159 229 ILE A CD1 
1174  N N   . ALA A 166 ? 0.7418 0.5760 0.5898 -0.0051 -0.0103 -0.0250 230 ALA A N   
1175  C CA  . ALA A 166 ? 0.7389 0.5566 0.5709 -0.0056 -0.0114 -0.0274 230 ALA A CA  
1176  C C   . ALA A 166 ? 0.8322 0.6443 0.6559 -0.0056 -0.0124 -0.0304 230 ALA A C   
1177  O O   . ALA A 166 ? 0.9826 0.8019 0.8124 -0.0095 -0.0128 -0.0329 230 ALA A O   
1178  C CB  . ALA A 166 ? 0.6316 0.4408 0.4594 -0.0135 -0.0109 -0.0294 230 ALA A CB  
1179  N N   . ASP A 167 ? 0.9117 0.7106 0.7208 -0.0006 -0.0135 -0.0308 231 ASP A N   
1180  C CA  . ASP A 167 ? 0.9014 0.6912 0.6996 0.0001  -0.0153 -0.0343 231 ASP A CA  
1181  C C   . ASP A 167 ? 0.9690 0.7363 0.7490 -0.0035 -0.0160 -0.0370 231 ASP A C   
1182  O O   . ASP A 167 ? 1.0567 0.8144 0.8289 -0.0014 -0.0155 -0.0350 231 ASP A O   
1183  C CB  . ASP A 167 ? 1.1305 0.9233 0.9250 0.0117  -0.0158 -0.0320 231 ASP A CB  
1184  C CG  . ASP A 167 ? 1.6868 1.4785 1.4763 0.0139  -0.0179 -0.0352 231 ASP A CG  
1185  O OD1 . ASP A 167 ? 1.7084 1.4962 1.4969 0.0059  -0.0198 -0.0404 231 ASP A OD1 
1186  O OD2 . ASP A 167 ? 1.3706 1.1660 1.1573 0.0238  -0.0176 -0.0330 231 ASP A OD2 
1187  N N   . GLY A 168 ? 0.8485 0.6061 0.6207 -0.0088 -0.0174 -0.0419 232 GLY A N   
1188  C CA  . GLY A 168 ? 1.0389 0.7711 0.7906 -0.0118 -0.0177 -0.0443 232 GLY A CA  
1189  C C   . GLY A 168 ? 1.2023 0.9255 0.9521 -0.0263 -0.0160 -0.0498 232 GLY A C   
1190  O O   . GLY A 168 ? 1.0624 0.7993 0.8274 -0.0350 -0.0137 -0.0513 232 GLY A O   
1191  N N   . THR A 169 ? 1.4064 1.1059 1.1371 -0.0289 -0.0168 -0.0531 233 THR A N   
1192  C CA  . THR A 169 ? 1.2819 0.9717 1.0106 -0.0439 -0.0148 -0.0595 233 THR A CA  
1193  C C   . THR A 169 ? 1.3134 0.9926 1.0381 -0.0541 -0.0086 -0.0579 233 THR A C   
1194  O O   . THR A 169 ? 1.3200 1.0052 1.0549 -0.0678 -0.0049 -0.0622 233 THR A O   
1195  C CB  . THR A 169 ? 1.2654 0.9293 0.9724 -0.0438 -0.0174 -0.0634 233 THR A CB  
1196  O OG1 . THR A 169 ? 1.3178 0.9901 1.0259 -0.0324 -0.0232 -0.0646 233 THR A OG1 
1197  C CG2 . THR A 169 ? 1.6065 1.2630 1.3149 -0.0609 -0.0152 -0.0712 233 THR A CG2 
1198  N N   . THR A 170 ? 1.3621 1.0258 1.0713 -0.0466 -0.0075 -0.0523 234 THR A N   
1199  C CA  . THR A 170 ? 1.5602 1.2096 1.2604 -0.0535 -0.0017 -0.0500 234 THR A CA  
1200  C C   . THR A 170 ? 1.3744 1.0249 1.0705 -0.0406 -0.0031 -0.0439 234 THR A C   
1201  O O   . THR A 170 ? 1.7486 1.4067 1.4460 -0.0273 -0.0079 -0.0419 234 THR A O   
1202  C CB  . THR A 170 ? 1.4663 1.0793 1.1393 -0.0616 0.0019  -0.0522 234 THR A CB  
1203  O OG1 . THR A 170 ? 1.5877 1.1855 1.2499 -0.0676 0.0086  -0.0494 234 THR A OG1 
1204  C CG2 . THR A 170 ? 1.0477 0.6374 0.6959 -0.0485 -0.0028 -0.0508 234 THR A CG2 
1205  N N   . TYR A 171 ? 1.1353 0.7789 0.8271 -0.0446 0.0013  -0.0416 235 TYR A N   
1206  C CA  . TYR A 171 ? 1.1833 0.8338 0.8771 -0.0339 -0.0005 -0.0373 235 TYR A CA  
1207  C C   . TYR A 171 ? 1.3253 0.9529 0.9941 -0.0206 -0.0038 -0.0354 235 TYR A C   
1208  O O   . TYR A 171 ? 1.2856 0.9239 0.9587 -0.0079 -0.0080 -0.0333 235 TYR A O   
1209  C CB  . TYR A 171 ? 1.0948 0.7453 0.7913 -0.0420 0.0050  -0.0362 235 TYR A CB  
1210  C CG  . TYR A 171 ? 1.2986 0.9720 1.0191 -0.0548 0.0082  -0.0392 235 TYR A CG  
1211  C CD1 . TYR A 171 ? 1.4606 1.1652 1.2069 -0.0514 0.0044  -0.0393 235 TYR A CD1 
1212  C CD2 . TYR A 171 ? 1.5662 1.2302 1.2831 -0.0699 0.0151  -0.0423 235 TYR A CD2 
1213  C CE1 . TYR A 171 ? 1.5827 1.3079 1.3491 -0.0609 0.0063  -0.0428 235 TYR A CE1 
1214  C CE2 . TYR A 171 ? 1.7224 1.4106 1.4627 -0.0803 0.0173  -0.0463 235 TYR A CE2 
1215  C CZ  . TYR A 171 ? 1.8470 1.5654 1.6111 -0.0747 0.0122  -0.0467 235 TYR A CZ  
1216  O OH  . TYR A 171 ? 2.0823 1.8239 1.8674 -0.0828 0.0135  -0.0512 235 TYR A OH  
1217  N N   . THR A 172 ? 1.3896 0.9858 1.0322 -0.0236 -0.0021 -0.0369 236 THR A N   
1218  C CA  . THR A 172 ? 1.2512 0.8224 0.8662 -0.0100 -0.0060 -0.0361 236 THR A CA  
1219  C C   . THR A 172 ? 1.0592 0.6508 0.6862 0.0027  -0.0125 -0.0366 236 THR A C   
1220  O O   . THR A 172 ? 1.1727 0.7620 0.7904 0.0182  -0.0171 -0.0356 236 THR A O   
1221  C CB  . THR A 172 ? 1.2250 0.7577 0.8101 -0.0173 -0.0028 -0.0382 236 THR A CB  
1222  O OG1 . THR A 172 ? 1.4620 1.0004 1.0544 -0.0214 -0.0050 -0.0418 236 THR A OG1 
1223  C CG2 . THR A 172 ? 1.1033 0.6218 0.6836 -0.0348 0.0061  -0.0384 236 THR A CG2 
1224  N N   . ALA A 173 ? 1.1352 0.7485 0.7836 -0.0034 -0.0128 -0.0383 237 ALA A N   
1225  C CA  . ALA A 173 ? 1.4877 1.1164 1.1441 0.0072  -0.0175 -0.0388 237 ALA A CA  
1226  C C   . ALA A 173 ? 1.3002 0.9659 0.9878 0.0094  -0.0181 -0.0370 237 ALA A C   
1227  O O   . ALA A 173 ? 1.2137 0.8932 0.9099 0.0148  -0.0202 -0.0374 237 ALA A O   
1228  C CB  . ALA A 173 ? 2.2259 1.8436 1.8751 0.0012  -0.0182 -0.0428 237 ALA A CB  
1229  N N   . SER A 174 ? 1.1435 0.8230 0.8458 0.0056  -0.0160 -0.0350 238 SER A N   
1230  C CA  . SER A 174 ? 1.0613 0.7722 0.7917 0.0051  -0.0159 -0.0336 238 SER A CA  
1231  C C   . SER A 174 ? 0.9335 0.6612 0.6730 0.0183  -0.0184 -0.0314 238 SER A C   
1232  O O   . SER A 174 ? 1.0815 0.8022 0.8103 0.0284  -0.0206 -0.0312 238 SER A O   
1233  C CB  . SER A 174 ? 1.3135 1.0327 1.0558 -0.0027 -0.0132 -0.0325 238 SER A CB  
1234  O OG  . SER A 174 ? 1.7242 1.4356 1.4579 0.0040  -0.0143 -0.0310 238 SER A OG  
1235  N N   . SER A 175 ? 0.9399 0.6899 0.6988 0.0182  -0.0176 -0.0304 239 SER A N   
1236  C CA  . SER A 175 ? 0.9227 0.6910 0.6935 0.0280  -0.0179 -0.0282 239 SER A CA  
1237  C C   . SER A 175 ? 1.1658 0.9557 0.9601 0.0226  -0.0157 -0.0261 239 SER A C   
1238  O O   . SER A 175 ? 1.1502 0.9438 0.9516 0.0140  -0.0143 -0.0265 239 SER A O   
1239  C CB  . SER A 175 ? 0.9656 0.7363 0.7333 0.0335  -0.0180 -0.0284 239 SER A CB  
1240  O OG  . SER A 175 ? 1.5079 1.2975 1.2882 0.0418  -0.0164 -0.0259 239 SER A OG  
1241  N N   . HIS A 176 ? 0.8708 0.6750 0.6774 0.0279  -0.0156 -0.0246 240 HIS A N   
1242  C CA  . HIS A 176 ? 0.7906 0.6127 0.6182 0.0225  -0.0135 -0.0227 240 HIS A CA  
1243  C C   . HIS A 176 ? 0.7587 0.5994 0.6015 0.0276  -0.0111 -0.0206 240 HIS A C   
1244  O O   . HIS A 176 ? 0.9796 0.8262 0.8244 0.0352  -0.0118 -0.0214 240 HIS A O   
1245  C CB  . HIS A 176 ? 0.7064 0.5268 0.5369 0.0193  -0.0152 -0.0236 240 HIS A CB  
1246  C CG  . HIS A 176 ? 0.7647 0.5662 0.5799 0.0133  -0.0158 -0.0251 240 HIS A CG  
1247  N ND1 . HIS A 176 ? 0.9509 0.7506 0.7686 0.0032  -0.0141 -0.0256 240 HIS A ND1 
1248  C CD2 . HIS A 176 ? 0.9280 0.7096 0.7224 0.0172  -0.0175 -0.0267 240 HIS A CD2 
1249  C CE1 . HIS A 176 ? 0.9705 0.7499 0.7701 0.0001  -0.0138 -0.0272 240 HIS A CE1 
1250  N NE2 . HIS A 176 ? 1.2259 0.9923 1.0098 0.0088  -0.0160 -0.0276 240 HIS A NE2 
1251  N N   . ARG A 177 ? 0.6044 0.4543 0.4574 0.0236  -0.0078 -0.0182 241 ARG A N   
1252  C CA  . ARG A 177 ? 0.6039 0.4702 0.4719 0.0259  -0.0035 -0.0154 241 ARG A CA  
1253  C C   . ARG A 177 ? 0.6770 0.5531 0.5616 0.0189  -0.0021 -0.0140 241 ARG A C   
1254  O O   . ARG A 177 ? 0.6948 0.5670 0.5798 0.0125  -0.0032 -0.0141 241 ARG A O   
1255  C CB  . ARG A 177 ? 0.6897 0.5563 0.5533 0.0287  0.0000  -0.0131 241 ARG A CB  
1256  C CG  . ARG A 177 ? 1.4167 1.2731 1.2633 0.0363  -0.0018 -0.0148 241 ARG A CG  
1257  C CD  . ARG A 177 ? 1.5296 1.3767 1.3654 0.0352  -0.0027 -0.0155 241 ARG A CD  
1258  N NE  . ARG A 177 ? 1.1907 1.0442 1.0273 0.0405  0.0018  -0.0124 241 ARG A NE  
1259  C CZ  . ARG A 177 ? 1.0065 0.8572 0.8326 0.0496  0.0028  -0.0122 241 ARG A CZ  
1260  N NH1 . ARG A 177 ? 0.7976 0.6394 0.6118 0.0547  -0.0009 -0.0151 241 ARG A NH1 
1261  N NH2 . ARG A 177 ? 1.1856 1.0410 1.0112 0.0544  0.0077  -0.0090 241 ARG A NH2 
1262  N N   . LEU A 178 ? 0.6102 0.4997 0.5091 0.0203  0.0005  -0.0132 242 LEU A N   
1263  C CA  . LEU A 178 ? 0.6104 0.5083 0.5249 0.0141  0.0019  -0.0123 242 LEU A CA  
1264  C C   . LEU A 178 ? 0.6075 0.5109 0.5270 0.0134  0.0088  -0.0081 242 LEU A C   
1265  O O   . LEU A 178 ? 0.6851 0.5966 0.6086 0.0176  0.0134  -0.0070 242 LEU A O   
1266  C CB  . LEU A 178 ? 0.7863 0.6956 0.7134 0.0161  0.0001  -0.0153 242 LEU A CB  
1267  C CG  . LEU A 178 ? 0.8474 0.7700 0.7950 0.0109  0.0021  -0.0156 242 LEU A CG  
1268  C CD1 . LEU A 178 ? 0.8361 0.7521 0.7846 0.0039  -0.0006 -0.0153 242 LEU A CD1 
1269  C CD2 . LEU A 178 ? 0.8903 0.8236 0.8468 0.0155  -0.0020 -0.0209 242 LEU A CD2 
1270  N N   . TYR A 179 ? 0.5698 0.4678 0.4872 0.0090  0.0100  -0.0059 243 TYR A N   
1271  C CA  . TYR A 179 ? 0.4853 0.3843 0.4034 0.0092  0.0167  -0.0015 243 TYR A CA  
1272  C C   . TYR A 179 ? 0.5118 0.4165 0.4441 0.0031  0.0207  0.0005  243 TYR A C   
1273  O O   . TYR A 179 ? 0.8065 0.7117 0.7460 -0.0019 0.0166  -0.0016 243 TYR A O   
1274  C CB  . TYR A 179 ? 0.4996 0.3883 0.4050 0.0096  0.0150  -0.0009 243 TYR A CB  
1275  C CG  . TYR A 179 ? 0.5202 0.4031 0.4113 0.0159  0.0136  -0.0020 243 TYR A CG  
1276  C CD1 . TYR A 179 ? 0.4932 0.3702 0.3766 0.0159  0.0075  -0.0063 243 TYR A CD1 
1277  C CD2 . TYR A 179 ? 0.5321 0.4138 0.4161 0.0220  0.0189  0.0011  243 TYR A CD2 
1278  C CE1 . TYR A 179 ? 0.6518 0.5218 0.5214 0.0213  0.0059  -0.0079 243 TYR A CE1 
1279  C CE2 . TYR A 179 ? 0.6955 0.5710 0.5653 0.0287  0.0169  -0.0004 243 TYR A CE2 
1280  C CZ  . TYR A 179 ? 0.7870 0.6568 0.6501 0.0281  0.0100  -0.0052 243 TYR A CZ  
1281  O OH  . TYR A 179 ? 0.8935 0.7558 0.7422 0.0343  0.0079  -0.0072 243 TYR A OH  
1282  N N   . ARG A 180 ? 0.4365 0.3438 0.3713 0.0036  0.0290  0.0046  244 ARG A N   
1283  C CA  . ARG A 180 ? 0.4997 0.4080 0.4446 -0.0030 0.0347  0.0075  244 ARG A CA  
1284  C C   . ARG A 180 ? 0.5376 0.4330 0.4688 -0.0016 0.0396  0.0124  244 ARG A C   
1285  O O   . ARG A 180 ? 0.8030 0.6948 0.7230 0.0045  0.0439  0.0151  244 ARG A O   
1286  C CB  . ARG A 180 ? 0.6117 0.5339 0.5721 -0.0049 0.0418  0.0078  244 ARG A CB  
1287  C CG  . ARG A 180 ? 0.7511 0.6729 0.7194 -0.0116 0.0514  0.0119  244 ARG A CG  
1288  C CD  . ARG A 180 ? 0.7146 0.6547 0.7016 -0.0140 0.0580  0.0103  244 ARG A CD  
1289  N NE  . ARG A 180 ? 0.7496 0.6870 0.7367 -0.0176 0.0713  0.0160  244 ARG A NE  
1290  C CZ  . ARG A 180 ? 0.8775 0.8201 0.8810 -0.0277 0.0786  0.0164  244 ARG A CZ  
1291  N NH1 . ARG A 180 ? 0.9071 0.8599 0.9298 -0.0345 0.0724  0.0105  244 ARG A NH1 
1292  N NH2 . ARG A 180 ? 1.0615 0.9982 1.0615 -0.0311 0.0922  0.0226  244 ARG A NH2 
1293  N N   . LEU A 181 ? 0.6465 0.5337 0.5766 -0.0058 0.0384  0.0134  245 LEU A N   
1294  C CA  . LEU A 181 ? 0.5755 0.4484 0.4895 -0.0025 0.0418  0.0174  245 LEU A CA  
1295  C C   . LEU A 181 ? 0.6536 0.5202 0.5718 -0.0087 0.0491  0.0214  245 LEU A C   
1296  O O   . LEU A 181 ? 0.8071 0.6787 0.7403 -0.0164 0.0475  0.0194  245 LEU A O   
1297  C CB  . LEU A 181 ? 0.5741 0.4406 0.4792 -0.0004 0.0328  0.0141  245 LEU A CB  
1298  C CG  . LEU A 181 ? 0.6323 0.5048 0.5363 0.0022  0.0249  0.0090  245 LEU A CG  
1299  C CD1 . LEU A 181 ? 0.6757 0.5465 0.5789 0.0003  0.0170  0.0048  245 LEU A CD1 
1300  C CD2 . LEU A 181 ? 0.5872 0.4563 0.4773 0.0101  0.0255  0.0092  245 LEU A CD2 
1301  N N   . VAL A 182 ? 0.6786 0.5325 0.5822 -0.0051 0.0571  0.0269  246 VAL A N   
1302  C CA  . VAL A 182 ? 0.6691 0.5102 0.5705 -0.0107 0.0651  0.0316  246 VAL A CA  
1303  C C   . VAL A 182 ? 0.6905 0.5105 0.5663 -0.0029 0.0659  0.0351  246 VAL A C   
1304  O O   . VAL A 182 ? 0.5958 0.4103 0.4554 0.0062  0.0686  0.0373  246 VAL A O   
1305  C CB  . VAL A 182 ? 0.5786 0.4235 0.4875 -0.0154 0.0785  0.0360  246 VAL A CB  
1306  C CG1 . VAL A 182 ? 0.6639 0.4956 0.5734 -0.0240 0.0865  0.0399  246 VAL A CG1 
1307  C CG2 . VAL A 182 ? 0.5090 0.3775 0.4420 -0.0200 0.0773  0.0315  246 VAL A CG2 
1308  N N   . ASN A 183 ? 0.7264 0.5339 0.5971 -0.0052 0.0630  0.0351  247 ASN A N   
1309  C CA  . ASN A 183 ? 0.6990 0.4859 0.5441 0.0039  0.0624  0.0374  247 ASN A CA  
1310  C C   . ASN A 183 ? 0.7335 0.5244 0.5662 0.0160  0.0551  0.0340  247 ASN A C   
1311  O O   . ASN A 183 ? 0.7735 0.5506 0.5838 0.0263  0.0569  0.0363  247 ASN A O   
1312  C CB  . ASN A 183 ? 0.7044 0.4716 0.5347 0.0036  0.0762  0.0454  247 ASN A CB  
1313  C CG  . ASN A 183 ? 0.8920 0.6527 0.7336 -0.0095 0.0830  0.0480  247 ASN A CG  
1314  O OD1 . ASN A 183 ? 1.0436 0.8151 0.9040 -0.0173 0.0764  0.0433  247 ASN A OD1 
1315  N ND2 . ASN A 183 ? 0.9931 0.7349 0.8222 -0.0121 0.0968  0.0552  247 ASN A ND2 
1316  N N   . GLY A 184 ? 0.5804 0.3896 0.4275 0.0144  0.0468  0.0281  248 GLY A N   
1317  C CA  . GLY A 184 ? 0.6517 0.4654 0.4906 0.0230  0.0382  0.0230  248 GLY A CA  
1318  C C   . GLY A 184 ? 0.7363 0.5547 0.5706 0.0285  0.0406  0.0235  248 GLY A C   
1319  O O   . GLY A 184 ? 0.9521 0.7741 0.7800 0.0351  0.0336  0.0187  248 GLY A O   
1320  N N   . THR A 185 ? 0.7225 0.5414 0.5604 0.0260  0.0507  0.0287  249 THR A N   
1321  C CA  . THR A 185 ? 0.7790 0.6037 0.6137 0.0315  0.0527  0.0287  249 THR A CA  
1322  C C   . THR A 185 ? 0.8013 0.6430 0.6571 0.0241  0.0527  0.0267  249 THR A C   
1323  O O   . THR A 185 ? 1.1927 1.0402 1.0646 0.0149  0.0555  0.0275  249 THR A O   
1324  C CB  . THR A 185 ? 0.9873 0.8004 0.8073 0.0367  0.0644  0.0356  249 THR A CB  
1325  O OG1 . THR A 185 ? 1.2790 1.0893 1.1082 0.0273  0.0744  0.0407  249 THR A OG1 
1326  C CG2 . THR A 185 ? 1.5002 1.2949 1.2938 0.0482  0.0621  0.0363  249 THR A CG2 
1327  N N   . SER A 186 ? 0.8379 0.6871 0.6930 0.0286  0.0486  0.0234  250 SER A N   
1328  C CA  . SER A 186 ? 0.9142 0.7779 0.7861 0.0239  0.0481  0.0212  250 SER A CA  
1329  C C   . SER A 186 ? 0.7509 0.6204 0.6303 0.0221  0.0600  0.0260  250 SER A C   
1330  O O   . SER A 186 ? 0.7802 0.6431 0.6475 0.0278  0.0679  0.0305  250 SER A O   
1331  C CB  . SER A 186 ? 0.7717 0.6387 0.6381 0.0296  0.0408  0.0164  250 SER A CB  
1332  O OG  . SER A 186 ? 0.8912 0.7518 0.7411 0.0392  0.0436  0.0182  250 SER A OG  
1333  N N   . ALA A 187 ? 0.9080 0.7899 0.8078 0.0140  0.0614  0.0247  251 ALA A N   
1334  C CA  . ALA A 187 ? 0.8040 0.6967 0.7164 0.0108  0.0720  0.0272  251 ALA A CA  
1335  C C   . ALA A 187 ? 0.7405 0.6502 0.6645 0.0133  0.0678  0.0222  251 ALA A C   
1336  O O   . ALA A 187 ? 0.7329 0.6581 0.6764 0.0082  0.0708  0.0201  251 ALA A O   
1337  C CB  . ALA A 187 ? 1.0157 0.9106 0.9442 -0.0006 0.0762  0.0281  251 ALA A CB  
1338  N N   . GLY A 188 ? 0.6204 0.5267 0.5320 0.0213  0.0601  0.0194  252 GLY A N   
1339  C CA  . GLY A 188 ? 0.6263 0.5444 0.5439 0.0252  0.0561  0.0149  252 GLY A CA  
1340  C C   . GLY A 188 ? 0.6962 0.6149 0.6179 0.0229  0.0447  0.0092  252 GLY A C   
1341  O O   . GLY A 188 ? 0.9221 0.8356 0.8464 0.0167  0.0403  0.0085  252 GLY A O   
1342  N N   . TRP A 189 ? 0.5571 0.4811 0.4774 0.0288  0.0402  0.0053  253 TRP A N   
1343  C CA  . TRP A 189 ? 0.5203 0.4419 0.4405 0.0279  0.0302  0.0003  253 TRP A CA  
1344  C C   . TRP A 189 ? 0.5188 0.4495 0.4419 0.0344  0.0274  -0.0040 253 TRP A C   
1345  O O   . TRP A 189 ? 0.5653 0.5057 0.4908 0.0402  0.0328  -0.0035 253 TRP A O   
1346  C CB  . TRP A 189 ? 0.5271 0.4322 0.4288 0.0295  0.0243  -0.0003 253 TRP A CB  
1347  C CG  . TRP A 189 ? 0.5925 0.4914 0.4781 0.0384  0.0252  0.0003  253 TRP A CG  
1348  C CD1 . TRP A 189 ? 0.6373 0.5303 0.5124 0.0422  0.0298  0.0038  253 TRP A CD1 
1349  C CD2 . TRP A 189 ? 0.7234 0.6193 0.5987 0.0461  0.0211  -0.0030 253 TRP A CD2 
1350  N NE1 . TRP A 189 ? 0.6077 0.4952 0.4680 0.0512  0.0284  0.0026  253 TRP A NE1 
1351  C CE2 . TRP A 189 ? 0.6234 0.5122 0.4833 0.0538  0.0234  -0.0013 253 TRP A CE2 
1352  C CE3 . TRP A 189 ? 0.7579 0.6540 0.6328 0.0484  0.0154  -0.0072 253 TRP A CE3 
1353  C CZ2 . TRP A 189 ? 0.5533 0.4358 0.3991 0.0625  0.0200  -0.0040 253 TRP A CZ2 
1354  C CZ3 . TRP A 189 ? 0.6301 0.5188 0.4895 0.0576  0.0124  -0.0095 253 TRP A CZ3 
1355  C CH2 . TRP A 189 ? 0.5644 0.4467 0.4101 0.0641  0.0146  -0.0080 253 TRP A CH2 
1356  N N   . LYS A 190 ? 0.5106 0.4376 0.4319 0.0344  0.0190  -0.0084 254 LYS A N   
1357  C CA  . LYS A 190 ? 0.4993 0.4311 0.4188 0.0424  0.0146  -0.0131 254 LYS A CA  
1358  C C   . LYS A 190 ? 0.5158 0.4289 0.4162 0.0448  0.0064  -0.0155 254 LYS A C   
1359  O O   . LYS A 190 ? 0.6648 0.5683 0.5624 0.0380  0.0034  -0.0153 254 LYS A O   
1360  C CB  . LYS A 190 ? 0.5101 0.4586 0.4503 0.0400  0.0133  -0.0170 254 LYS A CB  
1361  C CG  . LYS A 190 ? 0.6011 0.5538 0.5380 0.0498  0.0070  -0.0230 254 LYS A CG  
1362  C CD  . LYS A 190 ? 0.6298 0.6079 0.5902 0.0513  0.0088  -0.0275 254 LYS A CD  
1363  C CE  . LYS A 190 ? 0.7537 0.7352 0.7078 0.0639  0.0011  -0.0345 254 LYS A CE  
1364  N NZ  . LYS A 190 ? 1.2587 1.2689 1.2376 0.0666  0.0024  -0.0405 254 LYS A NZ  
1365  N N   . ALA A 191 ? 0.6781 0.5849 0.5640 0.0544  0.0033  -0.0180 255 ALA A N   
1366  C CA  . ALA A 191 ? 0.7749 0.6613 0.6411 0.0559  -0.0037 -0.0204 255 ALA A CA  
1367  C C   . ALA A 191 ? 0.8622 0.7510 0.7333 0.0565  -0.0089 -0.0243 255 ALA A C   
1368  O O   . ALA A 191 ? 0.8871 0.7921 0.7704 0.0620  -0.0093 -0.0272 255 ALA A O   
1369  C CB  . ALA A 191 ? 0.6803 0.5558 0.5267 0.0662  -0.0056 -0.0218 255 ALA A CB  
1370  N N   . LEU A 192 ? 0.8112 0.6848 0.6735 0.0509  -0.0127 -0.0247 256 LEU A N   
1371  C CA  . LEU A 192 ? 0.8076 0.6782 0.6684 0.0531  -0.0181 -0.0284 256 LEU A CA  
1372  C C   . LEU A 192 ? 0.8609 0.7101 0.6953 0.0615  -0.0227 -0.0308 256 LEU A C   
1373  O O   . LEU A 192 ? 0.6469 0.4768 0.4639 0.0582  -0.0221 -0.0292 256 LEU A O   
1374  C CB  . LEU A 192 ? 0.7373 0.6023 0.6016 0.0427  -0.0187 -0.0272 256 LEU A CB  
1375  C CG  . LEU A 192 ? 0.6832 0.5657 0.5710 0.0347  -0.0154 -0.0254 256 LEU A CG  
1376  C CD1 . LEU A 192 ? 0.5792 0.4531 0.4659 0.0256  -0.0163 -0.0243 256 LEU A CD1 
1377  C CD2 . LEU A 192 ? 0.5798 0.4818 0.4865 0.0385  -0.0169 -0.0289 256 LEU A CD2 
1378  N N   . ASP A 193 ? 0.8479 0.7002 0.6792 0.0725  -0.0274 -0.0352 257 ASP A N   
1379  C CA  . ASP A 193 ? 1.0297 0.8590 0.8330 0.0826  -0.0324 -0.0379 257 ASP A CA  
1380  C C   . ASP A 193 ? 0.8206 0.6267 0.6072 0.0781  -0.0351 -0.0379 257 ASP A C   
1381  O O   . ASP A 193 ? 0.8243 0.6333 0.6141 0.0811  -0.0390 -0.0407 257 ASP A O   
1382  C CB  . ASP A 193 ? 1.1583 0.9999 0.9634 0.0977  -0.0371 -0.0434 257 ASP A CB  
1383  C CG  . ASP A 193 ? 1.2485 1.0636 1.0208 0.1104  -0.0427 -0.0463 257 ASP A CG  
1384  O OD1 . ASP A 193 ? 1.5496 1.3360 1.2978 0.1064  -0.0420 -0.0436 257 ASP A OD1 
1385  O OD2 . ASP A 193 ? 1.5944 1.4174 1.3649 0.1246  -0.0479 -0.0517 257 ASP A OD2 
1386  N N   . THR A 194 ? 0.8771 0.6602 0.6453 0.0716  -0.0329 -0.0353 258 THR A N   
1387  C CA  . THR A 194 ? 1.3257 1.0865 1.0787 0.0642  -0.0328 -0.0345 258 THR A CA  
1388  C C   . THR A 194 ? 1.3032 1.0316 1.0215 0.0721  -0.0356 -0.0361 258 THR A C   
1389  O O   . THR A 194 ? 1.1805 0.8874 0.8821 0.0684  -0.0353 -0.0358 258 THR A O   
1390  C CB  . THR A 194 ? 1.3327 1.0910 1.0905 0.0494  -0.0275 -0.0313 258 THR A CB  
1391  O OG1 . THR A 194 ? 1.3891 1.1322 1.1383 0.0407  -0.0260 -0.0307 258 THR A OG1 
1392  C CG2 . THR A 194 ? 1.5058 1.2493 1.2475 0.0499  -0.0264 -0.0311 258 THR A CG2 
1393  N N   . THR A 195 ? 1.2507 0.9745 0.9570 0.0835  -0.0380 -0.0378 259 THR A N   
1394  C CA  . THR A 195 ? 1.5344 1.2229 1.2049 0.0890  -0.0397 -0.0386 259 THR A CA  
1395  C C   . THR A 195 ? 1.3011 0.9650 0.9486 0.0930  -0.0421 -0.0398 259 THR A C   
1396  O O   . THR A 195 ? 1.0141 0.6892 0.6679 0.1016  -0.0464 -0.0423 259 THR A O   
1397  C CB  . THR A 195 ? 1.3526 1.0393 1.0109 0.1048  -0.0434 -0.0412 259 THR A CB  
1398  O OG1 . THR A 195 ? 1.4708 1.1782 1.1398 0.1188  -0.0483 -0.0450 259 THR A OG1 
1399  C CG2 . THR A 195 ? 1.3404 1.0424 1.0126 0.1010  -0.0401 -0.0396 259 THR A CG2 
1400  N N   . GLY A 196 ? 1.2955 0.9255 0.9160 0.0862  -0.0391 -0.0381 260 GLY A N   
1401  C CA  . GLY A 196 ? 1.2393 0.8405 0.8330 0.0894  -0.0398 -0.0383 260 GLY A CA  
1402  C C   . GLY A 196 ? 1.1625 0.7660 0.7670 0.0742  -0.0344 -0.0357 260 GLY A C   
1403  O O   . GLY A 196 ? 1.3456 0.9202 0.9255 0.0716  -0.0317 -0.0345 260 GLY A O   
1404  N N   . PHE A 197 ? 1.0963 0.7326 0.7357 0.0648  -0.0325 -0.0347 261 PHE A N   
1405  C CA  . PHE A 197 ? 1.0475 0.6885 0.6988 0.0506  -0.0274 -0.0325 261 PHE A CA  
1406  C C   . PHE A 197 ? 0.9452 0.6100 0.6246 0.0367  -0.0233 -0.0311 261 PHE A C   
1407  O O   . PHE A 197 ? 0.9714 0.6432 0.6564 0.0366  -0.0234 -0.0313 261 PHE A O   
1408  C CB  . PHE A 197 ? 1.0485 0.7012 0.7085 0.0568  -0.0311 -0.0337 261 PHE A CB  
1409  C CG  . PHE A 197 ? 1.1879 0.8781 0.8817 0.0601  -0.0348 -0.0353 261 PHE A CG  
1410  C CD1 . PHE A 197 ? 1.0573 0.7698 0.7781 0.0490  -0.0321 -0.0337 261 PHE A CD1 
1411  C CD2 . PHE A 197 ? 1.3193 1.0218 1.0172 0.0743  -0.0408 -0.0386 261 PHE A CD2 
1412  C CE1 . PHE A 197 ? 1.2578 1.0015 1.0079 0.0510  -0.0347 -0.0349 261 PHE A CE1 
1413  C CE2 . PHE A 197 ? 1.2205 0.9574 0.9503 0.0757  -0.0429 -0.0402 261 PHE A CE2 
1414  C CZ  . PHE A 197 ? 1.3052 1.0613 1.0605 0.0635  -0.0396 -0.0381 261 PHE A CZ  
1415  N N   . ASN A 198 ? 0.8833 0.5594 0.5782 0.0265  -0.0201 -0.0299 262 ASN A N   
1416  C CA  . ASN A 198 ? 0.8808 0.5758 0.5983 0.0136  -0.0162 -0.0291 262 ASN A CA  
1417  C C   . ASN A 198 ? 0.9574 0.6744 0.6978 0.0099  -0.0161 -0.0284 262 ASN A C   
1418  O O   . ASN A 198 ? 0.9478 0.6579 0.6817 0.0116  -0.0165 -0.0284 262 ASN A O   
1419  C CB  . ASN A 198 ? 0.9715 0.6467 0.6752 0.0011  -0.0104 -0.0292 262 ASN A CB  
1420  C CG  . ASN A 198 ? 1.0637 0.7566 0.7884 -0.0122 -0.0063 -0.0295 262 ASN A CG  
1421  O OD1 . ASN A 198 ? 1.2988 0.9863 1.0211 -0.0200 -0.0020 -0.0293 262 ASN A OD1 
1422  N ND2 . ASN A 198 ? 0.9001 0.6140 0.6443 -0.0139 -0.0075 -0.0301 262 ASN A ND2 
1423  N N   . PHE A 199 ? 1.0020 0.7434 0.7670 0.0054  -0.0157 -0.0280 263 PHE A N   
1424  C CA  . PHE A 199 ? 0.8237 0.5874 0.6113 0.0048  -0.0170 -0.0275 263 PHE A CA  
1425  C C   . PHE A 199 ? 0.8424 0.6214 0.6474 -0.0048 -0.0140 -0.0268 263 PHE A C   
1426  O O   . PHE A 199 ? 1.0716 0.8654 0.8901 -0.0039 -0.0143 -0.0262 263 PHE A O   
1427  C CB  . PHE A 199 ? 0.7684 0.5480 0.5683 0.0144  -0.0211 -0.0279 263 PHE A CB  
1428  C CG  . PHE A 199 ? 0.5786 0.3786 0.4003 0.0141  -0.0228 -0.0279 263 PHE A CG  
1429  C CD1 . PHE A 199 ? 0.7491 0.5467 0.5693 0.0171  -0.0258 -0.0295 263 PHE A CD1 
1430  C CD2 . PHE A 199 ? 0.7498 0.5694 0.5918 0.0118  -0.0215 -0.0267 263 PHE A CD2 
1431  C CE1 . PHE A 199 ? 0.8293 0.6449 0.6698 0.0168  -0.0281 -0.0303 263 PHE A CE1 
1432  C CE2 . PHE A 199 ? 0.7662 0.6024 0.6276 0.0109  -0.0228 -0.0268 263 PHE A CE2 
1433  C CZ  . PHE A 199 ? 0.6902 0.5248 0.5516 0.0131  -0.0264 -0.0289 263 PHE A CZ  
1434  N N   . GLU A 200 ? 0.9121 0.6875 0.7159 -0.0133 -0.0109 -0.0273 264 GLU A N   
1435  C CA  . GLU A 200 ? 0.9273 0.7155 0.7445 -0.0217 -0.0084 -0.0279 264 GLU A CA  
1436  C C   . GLU A 200 ? 0.8406 0.6427 0.6723 -0.0240 -0.0086 -0.0277 264 GLU A C   
1437  O O   . GLU A 200 ? 0.9153 0.7122 0.7426 -0.0222 -0.0092 -0.0275 264 GLU A O   
1438  C CB  . GLU A 200 ? 0.8717 0.6466 0.6772 -0.0309 -0.0040 -0.0300 264 GLU A CB  
1439  C CG  . GLU A 200 ? 1.1097 0.8699 0.9008 -0.0294 -0.0041 -0.0308 264 GLU A CG  
1440  C CD  . GLU A 200 ? 1.3305 1.1023 1.1317 -0.0321 -0.0047 -0.0328 264 GLU A CD  
1441  O OE1 . GLU A 200 ? 1.2555 1.0446 1.0728 -0.0366 -0.0043 -0.0341 264 GLU A OE1 
1442  O OE2 . GLU A 200 ? 1.0699 0.8325 0.8613 -0.0286 -0.0061 -0.0334 264 GLU A OE2 
1443  N N   . PHE A 201 ? 0.7002 0.5183 0.5471 -0.0270 -0.0084 -0.0280 265 PHE A N   
1444  C CA  . PHE A 201 ? 0.6239 0.4533 0.4824 -0.0295 -0.0085 -0.0283 265 PHE A CA  
1445  C C   . PHE A 201 ? 0.4866 0.3193 0.3505 -0.0237 -0.0119 -0.0268 265 PHE A C   
1446  O O   . PHE A 201 ? 0.5221 0.3551 0.3869 -0.0246 -0.0123 -0.0273 265 PHE A O   
1447  C CB  . PHE A 201 ? 0.5638 0.3872 0.4155 -0.0366 -0.0048 -0.0305 265 PHE A CB  
1448  C CG  . PHE A 201 ? 0.8655 0.6864 0.7135 -0.0440 -0.0012 -0.0334 265 PHE A CG  
1449  C CD1 . PHE A 201 ? 0.9617 0.7968 0.8211 -0.0458 -0.0022 -0.0357 265 PHE A CD1 
1450  C CD2 . PHE A 201 ? 1.0051 0.8082 0.8370 -0.0491 0.0029  -0.0343 265 PHE A CD2 
1451  C CE1 . PHE A 201 ? 1.0743 0.9086 0.9318 -0.0525 0.0001  -0.0399 265 PHE A CE1 
1452  C CE2 . PHE A 201 ? 0.9711 0.7718 0.8009 -0.0574 0.0063  -0.0379 265 PHE A CE2 
1453  C CZ  . PHE A 201 ? 1.1222 0.9399 0.9661 -0.0592 0.0044  -0.0412 265 PHE A CZ  
1454  N N   . PRO A 202 ? 0.4765 0.3129 0.3449 -0.0177 -0.0144 -0.0254 266 PRO A N   
1455  C CA  . PRO A 202 ? 0.5639 0.4060 0.4406 -0.0130 -0.0180 -0.0254 266 PRO A CA  
1456  C C   . PRO A 202 ? 0.5069 0.3591 0.3963 -0.0160 -0.0186 -0.0253 266 PRO A C   
1457  O O   . PRO A 202 ? 0.6134 0.4726 0.5095 -0.0191 -0.0168 -0.0244 266 PRO A O   
1458  C CB  . PRO A 202 ? 0.4652 0.3155 0.3502 -0.0086 -0.0186 -0.0243 266 PRO A CB  
1459  C CG  . PRO A 202 ? 0.5332 0.3848 0.4172 -0.0113 -0.0154 -0.0230 266 PRO A CG  
1460  C CD  . PRO A 202 ? 0.5189 0.3584 0.3888 -0.0155 -0.0137 -0.0244 266 PRO A CD  
1461  N N   . THR A 203 ? 0.5775 0.4286 0.4679 -0.0140 -0.0217 -0.0266 267 THR A N   
1462  C CA  . THR A 203 ? 0.6571 0.5155 0.5579 -0.0158 -0.0232 -0.0269 267 THR A CA  
1463  C C   . THR A 203 ? 0.7687 0.6324 0.6797 -0.0118 -0.0277 -0.0281 267 THR A C   
1464  O O   . THR A 203 ? 0.7109 0.5700 0.6167 -0.0068 -0.0312 -0.0303 267 THR A O   
1465  C CB  . THR A 203 ? 0.7432 0.5957 0.6356 -0.0176 -0.0227 -0.0282 267 THR A CB  
1466  O OG1 . THR A 203 ? 0.8846 0.7441 0.7863 -0.0184 -0.0246 -0.0287 267 THR A OG1 
1467  C CG2 . THR A 203 ? 1.0722 0.9136 0.9526 -0.0131 -0.0249 -0.0297 267 THR A CG2 
1468  N N   . CYS A 204 ? 0.7575 0.6304 0.6825 -0.0140 -0.0276 -0.0271 268 CYS A N   
1469  C CA  . CYS A 204 ? 0.5735 0.4541 0.5117 -0.0124 -0.0300 -0.0283 268 CYS A CA  
1470  C C   . CYS A 204 ? 0.6392 0.5238 0.5889 -0.0146 -0.0329 -0.0297 268 CYS A C   
1471  O O   . CYS A 204 ? 0.9824 0.8643 0.9307 -0.0173 -0.0321 -0.0285 268 CYS A O   
1472  C CB  . CYS A 204 ? 0.6614 0.5480 0.6054 -0.0136 -0.0254 -0.0255 268 CYS A CB  
1473  S SG  . CYS A 204 ? 1.4791 1.3596 1.4088 -0.0107 -0.0228 -0.0244 268 CYS A SG  
1474  N N   . TYR A 205 ? 0.5974 0.4883 0.5583 -0.0131 -0.0367 -0.0331 269 TYR A N   
1475  C CA  . TYR A 205 ? 0.6091 0.5042 0.5838 -0.0169 -0.0386 -0.0346 269 TYR A CA  
1476  C C   . TYR A 205 ? 0.6828 0.5898 0.6748 -0.0182 -0.0387 -0.0372 269 TYR A C   
1477  O O   . TYR A 205 ? 0.7746 0.6876 0.7675 -0.0148 -0.0375 -0.0378 269 TYR A O   
1478  C CB  . TYR A 205 ? 0.6538 0.5439 0.6254 -0.0145 -0.0454 -0.0386 269 TYR A CB  
1479  C CG  . TYR A 205 ? 0.8849 0.7759 0.8540 -0.0077 -0.0514 -0.0437 269 TYR A CG  
1480  C CD1 . TYR A 205 ? 0.7744 0.6728 0.7571 -0.0065 -0.0578 -0.0498 269 TYR A CD1 
1481  C CD2 . TYR A 205 ? 0.6790 0.5626 0.6313 -0.0022 -0.0509 -0.0431 269 TYR A CD2 
1482  C CE1 . TYR A 205 ? 0.7445 0.6441 0.7239 0.0019  -0.0647 -0.0557 269 TYR A CE1 
1483  C CE2 . TYR A 205 ? 0.7058 0.5873 0.6522 0.0058  -0.0568 -0.0479 269 TYR A CE2 
1484  C CZ  . TYR A 205 ? 0.8055 0.6957 0.7654 0.0087  -0.0642 -0.0544 269 TYR A CZ  
1485  O OH  . TYR A 205 ? 0.6740 0.5626 0.6272 0.0187  -0.0713 -0.0602 269 TYR A OH  
1486  N N   . TYR A 206 ? 0.7250 0.6355 0.7307 -0.0232 -0.0397 -0.0390 270 TYR A N   
1487  C CA  . TYR A 206 ? 0.7680 0.6915 0.7930 -0.0270 -0.0377 -0.0413 270 TYR A CA  
1488  C C   . TYR A 206 ? 0.7843 0.7132 0.8230 -0.0281 -0.0449 -0.0486 270 TYR A C   
1489  O O   . TYR A 206 ? 0.9655 0.8863 1.0033 -0.0312 -0.0477 -0.0492 270 TYR A O   
1490  C CB  . TYR A 206 ? 0.7462 0.6685 0.7767 -0.0348 -0.0289 -0.0358 270 TYR A CB  
1491  C CG  . TYR A 206 ? 0.7671 0.7026 0.8193 -0.0409 -0.0253 -0.0385 270 TYR A CG  
1492  C CD1 . TYR A 206 ? 0.7806 0.7140 0.8442 -0.0491 -0.0248 -0.0400 270 TYR A CD1 
1493  C CD2 . TYR A 206 ? 1.0598 1.0101 1.1212 -0.0386 -0.0225 -0.0402 270 TYR A CD2 
1494  C CE1 . TYR A 206 ? 0.9693 0.9156 1.0546 -0.0565 -0.0206 -0.0432 270 TYR A CE1 
1495  C CE2 . TYR A 206 ? 1.1311 1.0965 1.2147 -0.0449 -0.0184 -0.0435 270 TYR A CE2 
1496  C CZ  . TYR A 206 ? 0.8266 0.7902 0.9229 -0.0547 -0.0171 -0.0450 270 TYR A CZ  
1497  O OH  . TYR A 206 ? 0.7846 0.7631 0.9042 -0.0629 -0.0120 -0.0487 270 TYR A OH  
1498  N N   . THR A 207 ? 0.7392 0.6825 0.7906 -0.0250 -0.0484 -0.0549 271 THR A N   
1499  C CA  . THR A 207 ? 0.8722 0.8249 0.9412 -0.0265 -0.0556 -0.0637 271 THR A CA  
1500  C C   . THR A 207 ? 0.9299 0.9043 1.0198 -0.0263 -0.0554 -0.0699 271 THR A C   
1501  O O   . THR A 207 ? 0.8650 0.8457 0.9509 -0.0208 -0.0526 -0.0686 271 THR A O   
1502  C CB  . THR A 207 ? 0.8889 0.8345 0.9464 -0.0176 -0.0666 -0.0691 271 THR A CB  
1503  O OG1 . THR A 207 ? 1.1749 1.1287 1.2498 -0.0195 -0.0744 -0.0782 271 THR A OG1 
1504  C CG2 . THR A 207 ? 0.8170 0.7640 0.8618 -0.0058 -0.0699 -0.0710 271 THR A CG2 
1505  N N   . SER A 208 ? 0.8576 0.8439 0.9702 -0.0326 -0.0584 -0.0773 272 SER A N   
1506  C CA  . SER A 208 ? 0.9121 0.9228 1.0477 -0.0318 -0.0602 -0.0860 272 SER A CA  
1507  C C   . SER A 208 ? 1.0902 1.1109 1.2284 -0.0321 -0.0496 -0.0808 272 SER A C   
1508  O O   . SER A 208 ? 1.1160 1.1504 1.2564 -0.0230 -0.0522 -0.0853 272 SER A O   
1509  C CB  . SER A 208 ? 0.7909 0.8063 0.9213 -0.0178 -0.0734 -0.0953 272 SER A CB  
1510  O OG  . SER A 208 ? 1.3121 1.3532 1.4677 -0.0164 -0.0778 -0.1066 272 SER A OG  
1511  N N   . GLY A 209 ? 0.9254 0.9376 1.0608 -0.0413 -0.0381 -0.0715 273 GLY A N   
1512  C CA  . GLY A 209 ? 0.8579 0.8786 0.9963 -0.0427 -0.0270 -0.0664 273 GLY A CA  
1513  C C   . GLY A 209 ? 0.7247 0.7394 0.8416 -0.0315 -0.0270 -0.0618 273 GLY A C   
1514  O O   . GLY A 209 ? 0.9967 1.0205 1.1157 -0.0296 -0.0200 -0.0595 273 GLY A O   
1515  N N   . LYS A 210 ? 0.5944 0.5930 0.6900 -0.0241 -0.0344 -0.0608 274 LYS A N   
1516  C CA  . LYS A 210 ? 0.6521 0.6418 0.7257 -0.0146 -0.0343 -0.0567 274 LYS A CA  
1517  C C   . LYS A 210 ? 0.6829 0.6497 0.7330 -0.0145 -0.0342 -0.0499 274 LYS A C   
1518  O O   . LYS A 210 ? 0.6836 0.6411 0.7301 -0.0168 -0.0386 -0.0506 274 LYS A O   
1519  C CB  . LYS A 210 ? 0.6345 0.6313 0.7051 -0.0023 -0.0435 -0.0647 274 LYS A CB  
1520  C CG  . LYS A 210 ? 0.9381 0.9595 1.0288 0.0003  -0.0419 -0.0706 274 LYS A CG  
1521  C CD  . LYS A 210 ? 1.2285 1.2577 1.3158 0.0144  -0.0521 -0.0797 274 LYS A CD  
1522  C CE  . LYS A 210 ? 1.5722 1.6106 1.6741 0.0154  -0.0626 -0.0901 274 LYS A CE  
1523  N NZ  . LYS A 210 ? 1.7174 1.7782 1.8325 0.0261  -0.0700 -0.1018 274 LYS A NZ  
1524  N N   . VAL A 211 ? 0.7620 0.7209 0.7966 -0.0119 -0.0291 -0.0438 275 VAL A N   
1525  C CA  . VAL A 211 ? 0.7069 0.6475 0.7206 -0.0111 -0.0297 -0.0392 275 VAL A CA  
1526  C C   . VAL A 211 ? 0.6733 0.6065 0.6703 -0.0017 -0.0356 -0.0419 275 VAL A C   
1527  O O   . VAL A 211 ? 0.9725 0.9109 0.9675 0.0049  -0.0362 -0.0439 275 VAL A O   
1528  C CB  . VAL A 211 ? 0.5546 0.4892 0.5601 -0.0140 -0.0215 -0.0319 275 VAL A CB  
1529  C CG1 . VAL A 211 ? 0.5508 0.4697 0.5365 -0.0129 -0.0227 -0.0289 275 VAL A CG1 
1530  C CG2 . VAL A 211 ? 0.5182 0.4547 0.5349 -0.0224 -0.0160 -0.0289 275 VAL A CG2 
1531  N N   . LYS A 212 ? 0.7160 0.6360 0.6998 -0.0010 -0.0395 -0.0417 276 LYS A N   
1532  C CA  . LYS A 212 ? 0.6933 0.6026 0.6593 0.0072  -0.0447 -0.0442 276 LYS A CA  
1533  C C   . LYS A 212 ? 0.6508 0.5441 0.5982 0.0048  -0.0413 -0.0393 276 LYS A C   
1534  O O   . LYS A 212 ? 0.6561 0.5457 0.6038 -0.0003 -0.0406 -0.0376 276 LYS A O   
1535  C CB  . LYS A 212 ? 0.8000 0.7101 0.7694 0.0110  -0.0531 -0.0505 276 LYS A CB  
1536  C CG  . LYS A 212 ? 1.2092 1.1386 1.2015 0.0121  -0.0569 -0.0572 276 LYS A CG  
1537  C CD  . LYS A 212 ? 1.1386 1.0694 1.1343 0.0171  -0.0668 -0.0650 276 LYS A CD  
1538  C CE  . LYS A 212 ? 1.0427 0.9956 1.0644 0.0170  -0.0705 -0.0728 276 LYS A CE  
1539  N NZ  . LYS A 212 ? 1.2343 1.1891 1.2580 0.0242  -0.0818 -0.0820 276 LYS A NZ  
1540  N N   . CYS A 213 ? 0.8166 0.7011 0.7483 0.0083  -0.0392 -0.0375 277 CYS A N   
1541  C CA  . CYS A 213 ? 0.7970 0.6683 0.7129 0.0048  -0.0350 -0.0335 277 CYS A CA  
1542  C C   . CYS A 213 ? 0.7714 0.6256 0.6649 0.0100  -0.0367 -0.0347 277 CYS A C   
1543  O O   . CYS A 213 ? 0.7720 0.6220 0.6569 0.0173  -0.0389 -0.0365 277 CYS A O   
1544  C CB  . CYS A 213 ? 0.8067 0.6802 0.7224 0.0027  -0.0295 -0.0301 277 CYS A CB  
1545  S SG  . CYS A 213 ? 1.3238 1.2112 1.2587 -0.0034 -0.0253 -0.0272 277 CYS A SG  
1546  N N   . THR A 214 ? 0.7730 0.6168 0.6562 0.0063  -0.0351 -0.0335 278 THR A N   
1547  C CA  . THR A 214 ? 0.7919 0.6163 0.6515 0.0089  -0.0341 -0.0335 278 THR A CA  
1548  C C   . THR A 214 ? 0.7868 0.6025 0.6360 0.0026  -0.0276 -0.0305 278 THR A C   
1549  O O   . THR A 214 ? 0.8490 0.6678 0.7022 -0.0050 -0.0237 -0.0291 278 THR A O   
1550  C CB  . THR A 214 ? 0.8889 0.7071 0.7428 0.0082  -0.0351 -0.0343 278 THR A CB  
1551  O OG1 . THR A 214 ? 1.0015 0.8283 0.8664 0.0134  -0.0420 -0.0379 278 THR A OG1 
1552  C CG2 . THR A 214 ? 0.7247 0.5209 0.5523 0.0113  -0.0331 -0.0341 278 THR A CG2 
1553  N N   . GLY A 215 ? 0.8113 0.6163 0.6469 0.0062  -0.0268 -0.0303 279 GLY A N   
1554  C CA  . GLY A 215 ? 0.8987 0.6944 0.7244 -0.0003 -0.0212 -0.0284 279 GLY A CA  
1555  C C   . GLY A 215 ? 0.7973 0.5720 0.6014 -0.0034 -0.0174 -0.0282 279 GLY A C   
1556  O O   . GLY A 215 ? 0.8056 0.5730 0.6018 -0.0004 -0.0186 -0.0289 279 GLY A O   
1557  N N   . THR A 216 ? 0.6667 0.4308 0.4604 -0.0095 -0.0125 -0.0275 280 THR A N   
1558  C CA  . THR A 216 ? 0.6864 0.4294 0.4597 -0.0150 -0.0068 -0.0273 280 THR A CA  
1559  C C   . THR A 216 ? 0.8485 0.5729 0.6038 -0.0146 -0.0052 -0.0271 280 THR A C   
1560  O O   . THR A 216 ? 0.8336 0.5650 0.5964 -0.0178 -0.0049 -0.0276 280 THR A O   
1561  C CB  . THR A 216 ? 0.7611 0.5146 0.5458 -0.0268 -0.0014 -0.0278 280 THR A CB  
1562  O OG1 . THR A 216 ? 0.9341 0.6947 0.7248 -0.0259 -0.0020 -0.0278 280 THR A OG1 
1563  C CG2 . THR A 216 ? 0.7258 0.4616 0.4944 -0.0360 0.0061  -0.0283 280 THR A CG2 
1564  N N   . ASN A 217 ? 0.8740 0.5727 0.6032 -0.0093 -0.0047 -0.0267 281 ASN A N   
1565  C CA  . ASN A 217 ? 0.8118 0.4895 0.5207 -0.0073 -0.0040 -0.0268 281 ASN A CA  
1566  C C   . ASN A 217 ? 0.9714 0.6292 0.6650 -0.0199 0.0047  -0.0264 281 ASN A C   
1567  O O   . ASN A 217 ? 0.8997 0.5374 0.5742 -0.0216 0.0094  -0.0253 281 ASN A O   
1568  C CB  . ASN A 217 ? 0.9535 0.6123 0.6400 0.0073  -0.0089 -0.0270 281 ASN A CB  
1569  C CG  . ASN A 217 ? 1.1606 0.7970 0.8245 0.0120  -0.0094 -0.0273 281 ASN A CG  
1570  O OD1 . ASN A 217 ? 0.9618 0.5819 0.6141 0.0023  -0.0037 -0.0268 281 ASN A OD1 
1571  N ND2 . ASN A 217 ? 1.3388 0.9740 0.9958 0.0274  -0.0167 -0.0288 281 ASN A ND2 
1572  N N   . LEU A 218 ? 0.8794 0.5431 0.5816 -0.0289 0.0070  -0.0278 282 LEU A N   
1573  C CA  . LEU A 218 ? 0.9543 0.6043 0.6480 -0.0433 0.0153  -0.0290 282 LEU A CA  
1574  C C   . LEU A 218 ? 1.1193 0.7349 0.7826 -0.0432 0.0176  -0.0288 282 LEU A C   
1575  O O   . LEU A 218 ? 1.2163 0.8166 0.8702 -0.0562 0.0251  -0.0301 282 LEU A O   
1576  C CB  . LEU A 218 ? 0.8501 0.5236 0.5681 -0.0534 0.0160  -0.0321 282 LEU A CB  
1577  C CG  . LEU A 218 ? 0.8972 0.5998 0.6414 -0.0578 0.0165  -0.0331 282 LEU A CG  
1578  C CD1 . LEU A 218 ? 1.0158 0.7406 0.7782 -0.0482 0.0089  -0.0323 282 LEU A CD1 
1579  C CD2 . LEU A 218 ? 0.9976 0.7112 0.7543 -0.0716 0.0211  -0.0374 282 LEU A CD2 
1580  N N   . TRP A 219 ? 1.0498 0.6531 0.6976 -0.0284 0.0113  -0.0276 283 TRP A N   
1581  C CA  . TRP A 219 ? 1.0285 0.5983 0.6456 -0.0250 0.0117  -0.0276 283 TRP A CA  
1582  C C   . TRP A 219 ? 1.0653 0.6025 0.6492 -0.0165 0.0129  -0.0255 283 TRP A C   
1583  O O   . TRP A 219 ? 1.0910 0.6002 0.6526 -0.0255 0.0213  -0.0244 283 TRP A O   
1584  C CB  . TRP A 219 ? 1.1832 0.7630 0.8057 -0.0135 0.0035  -0.0288 283 TRP A CB  
1585  C CG  . TRP A 219 ? 1.4623 1.0092 1.0530 -0.0063 0.0019  -0.0292 283 TRP A CG  
1586  C CD1 . TRP A 219 ? 1.6400 1.1487 1.1998 -0.0135 0.0079  -0.0290 283 TRP A CD1 
1587  C CD2 . TRP A 219 ? 1.3466 0.8946 0.9316 0.0099  -0.0061 -0.0301 283 TRP A CD2 
1588  N NE1 . TRP A 219 ? 1.6540 1.1388 1.1884 -0.0022 0.0034  -0.0296 283 TRP A NE1 
1589  C CE2 . TRP A 219 ? 1.3361 0.8441 0.8845 0.0127  -0.0053 -0.0305 283 TRP A CE2 
1590  C CE3 . TRP A 219 ? 1.2993 0.8764 0.9052 0.0216  -0.0131 -0.0307 283 TRP A CE3 
1591  C CZ2 . TRP A 219 ? 1.3723 0.8713 0.9057 0.0282  -0.0120 -0.0318 283 TRP A CZ2 
1592  C CZ3 . TRP A 219 ? 1.2820 0.8518 0.8744 0.0364  -0.0189 -0.0321 283 TRP A CZ3 
1593  C CH2 . TRP A 219 ? 1.3000 0.8320 0.8567 0.0403  -0.0189 -0.0327 283 TRP A CH2 
1594  N N   . ASN A 220 ? 1.1331 0.6742 0.7135 0.0010  0.0049  -0.0253 284 ASN A N   
1595  C CA  . ASN A 220 ? 1.1348 0.6425 0.6791 0.0139  0.0034  -0.0243 284 ASN A CA  
1596  C C   . ASN A 220 ? 1.1418 0.6572 0.6880 0.0235  0.0000  -0.0240 284 ASN A C   
1597  O O   . ASN A 220 ? 1.6193 1.1167 1.1418 0.0399  -0.0055 -0.0247 284 ASN A O   
1598  C CB  . ASN A 220 ? 1.1907 0.6894 0.7208 0.0298  -0.0048 -0.0261 284 ASN A CB  
1599  C CG  . ASN A 220 ? 1.1670 0.7046 0.7289 0.0384  -0.0132 -0.0282 284 ASN A CG  
1600  O OD1 . ASN A 220 ? 1.1968 0.7644 0.7877 0.0350  -0.0140 -0.0283 284 ASN A OD1 
1601  N ND2 . ASN A 220 ? 1.2131 0.7504 0.7700 0.0493  -0.0190 -0.0301 284 ASN A ND2 
1602  N N   . ASP A 221 ? 1.0303 0.5706 0.6025 0.0142  0.0029  -0.0235 285 ASP A N   
1603  C CA  . ASP A 221 ? 1.0993 0.6523 0.6787 0.0237  -0.0020 -0.0241 285 ASP A CA  
1604  C C   . ASP A 221 ? 0.9626 0.5260 0.5545 0.0124  0.0046  -0.0227 285 ASP A C   
1605  O O   . ASP A 221 ? 0.8554 0.4405 0.4725 -0.0016 0.0091  -0.0226 285 ASP A O   
1606  C CB  . ASP A 221 ? 1.2775 0.8644 0.8856 0.0337  -0.0124 -0.0270 285 ASP A CB  
1607  C CG  . ASP A 221 ? 1.4373 1.0338 1.0490 0.0471  -0.0201 -0.0294 285 ASP A CG  
1608  O OD1 . ASP A 221 ? 1.0343 0.6102 0.6240 0.0511  -0.0185 -0.0287 285 ASP A OD1 
1609  O OD2 . ASP A 221 ? 1.6994 1.3245 1.3364 0.0536  -0.0277 -0.0323 285 ASP A OD2 
1610  N N   . ALA A 222 ? 0.9555 0.5028 0.5280 0.0204  0.0045  -0.0221 286 ALA A N   
1611  C CA  . ALA A 222 ? 1.1488 0.7038 0.7288 0.0139  0.0096  -0.0210 286 ALA A CA  
1612  C C   . ALA A 222 ? 1.0628 0.6450 0.6651 0.0239  -0.0001 -0.0236 286 ALA A C   
1613  O O   . ALA A 222 ? 1.0589 0.6512 0.6703 0.0204  0.0021  -0.0233 286 ALA A O   
1614  C CB  . ALA A 222 ? 1.2449 0.7611 0.7859 0.0152  0.0177  -0.0183 286 ALA A CB  
1615  N N   . LYS A 223 ? 1.0642 0.6576 0.6743 0.0366  -0.0108 -0.0266 287 LYS A N   
1616  C CA  . LYS A 223 ? 0.9106 0.5336 0.5476 0.0430  -0.0197 -0.0298 287 LYS A CA  
1617  C C   . LYS A 223 ? 0.9678 0.6228 0.6404 0.0336  -0.0203 -0.0300 287 LYS A C   
1618  O O   . LYS A 223 ? 1.3356 0.9892 1.0102 0.0232  -0.0143 -0.0280 287 LYS A O   
1619  C CB  . LYS A 223 ? 1.1426 0.7622 0.7702 0.0617  -0.0307 -0.0340 287 LYS A CB  
1620  C CG  . LYS A 223 ? 1.2828 0.8685 0.8712 0.0752  -0.0321 -0.0345 287 LYS A CG  
1621  C CD  . LYS A 223 ? 1.6607 1.2539 1.2492 0.0949  -0.0456 -0.0409 287 LYS A CD  
1622  C CE  . LYS A 223 ? 1.3946 0.9526 0.9408 0.1126  -0.0493 -0.0426 287 LYS A CE  
1623  N NZ  . LYS A 223 ? 1.4432 1.0170 0.9969 0.1316  -0.0638 -0.0508 287 LYS A NZ  
1624  N N   . ARG A 224 ? 0.9359 0.6186 0.6356 0.0370  -0.0273 -0.0327 288 ARG A N   
1625  C CA  . ARG A 224 ? 0.9246 0.6353 0.6555 0.0288  -0.0273 -0.0324 288 ARG A CA  
1626  C C   . ARG A 224 ? 0.8126 0.5397 0.5577 0.0381  -0.0351 -0.0355 288 ARG A C   
1627  O O   . ARG A 224 ? 0.7512 0.4877 0.5035 0.0474  -0.0426 -0.0393 288 ARG A O   
1628  C CB  . ARG A 224 ? 0.9474 0.6781 0.7011 0.0211  -0.0263 -0.0322 288 ARG A CB  
1629  C CG  . ARG A 224 ? 1.0425 0.7603 0.7833 0.0150  -0.0198 -0.0304 288 ARG A CG  
1630  C CD  . ARG A 224 ? 0.9997 0.7391 0.7640 0.0066  -0.0183 -0.0303 288 ARG A CD  
1631  N NE  . ARG A 224 ? 1.0182 0.7610 0.7874 -0.0056 -0.0106 -0.0285 288 ARG A NE  
1632  C CZ  . ARG A 224 ? 1.0075 0.7464 0.7720 -0.0140 -0.0032 -0.0277 288 ARG A CZ  
1633  N NH1 . ARG A 224 ? 1.1787 0.9093 0.9324 -0.0111 -0.0019 -0.0277 288 ARG A NH1 
1634  N NH2 . ARG A 224 ? 0.8022 0.5469 0.5736 -0.0249 0.0028  -0.0276 288 ARG A NH2 
1635  N N   . PRO A 225 ? 0.7935 0.5253 0.5436 0.0355  -0.0332 -0.0344 289 PRO A N   
1636  C CA  . PRO A 225 ? 0.7581 0.5080 0.5235 0.0435  -0.0391 -0.0372 289 PRO A CA  
1637  C C   . PRO A 225 ? 0.7234 0.5009 0.5195 0.0401  -0.0417 -0.0386 289 PRO A C   
1638  O O   . PRO A 225 ? 0.8140 0.5964 0.6194 0.0307  -0.0383 -0.0366 289 PRO A O   
1639  C CB  . PRO A 225 ? 0.8321 0.5838 0.6000 0.0379  -0.0345 -0.0347 289 PRO A CB  
1640  C CG  . PRO A 225 ? 0.9455 0.6714 0.6900 0.0305  -0.0281 -0.0319 289 PRO A CG  
1641  C CD  . PRO A 225 ? 0.7350 0.4590 0.4802 0.0246  -0.0257 -0.0312 289 PRO A CD  
1642  N N   . PHE A 226 ? 0.6775 0.4727 0.4891 0.0476  -0.0474 -0.0425 290 PHE A N   
1643  C CA  . PHE A 226 ? 0.6573 0.4770 0.4977 0.0437  -0.0495 -0.0442 290 PHE A CA  
1644  C C   . PHE A 226 ? 0.8057 0.6467 0.6661 0.0457  -0.0501 -0.0459 290 PHE A C   
1645  O O   . PHE A 226 ? 0.9129 0.7535 0.7664 0.0557  -0.0533 -0.0489 290 PHE A O   
1646  C CB  . PHE A 226 ? 0.7077 0.5276 0.5477 0.0508  -0.0568 -0.0492 290 PHE A CB  
1647  C CG  . PHE A 226 ? 0.8972 0.7367 0.7633 0.0448  -0.0587 -0.0508 290 PHE A CG  
1648  C CD1 . PHE A 226 ? 0.7870 0.6210 0.6519 0.0379  -0.0567 -0.0485 290 PHE A CD1 
1649  C CD2 . PHE A 226 ? 0.9566 0.8195 0.8477 0.0463  -0.0625 -0.0553 290 PHE A CD2 
1650  C CE1 . PHE A 226 ? 0.6987 0.5474 0.5846 0.0333  -0.0591 -0.0503 290 PHE A CE1 
1651  C CE2 . PHE A 226 ? 0.9265 0.8042 0.8400 0.0401  -0.0641 -0.0571 290 PHE A CE2 
1652  C CZ  . PHE A 226 ? 0.7566 0.6259 0.6663 0.0339  -0.0628 -0.0544 290 PHE A CZ  
1653  N N   . LEU A 227 ? 0.8236 0.6824 0.7076 0.0365  -0.0468 -0.0440 291 LEU A N   
1654  C CA  . LEU A 227 ? 0.6648 0.5420 0.5668 0.0356  -0.0442 -0.0438 291 LEU A CA  
1655  C C   . LEU A 227 ? 0.6963 0.5947 0.6256 0.0311  -0.0451 -0.0462 291 LEU A C   
1656  O O   . LEU A 227 ? 0.7096 0.6081 0.6460 0.0235  -0.0442 -0.0445 291 LEU A O   
1657  C CB  . LEU A 227 ? 0.6949 0.5683 0.5944 0.0278  -0.0367 -0.0377 291 LEU A CB  
1658  C CG  . LEU A 227 ? 0.8748 0.7651 0.7900 0.0273  -0.0327 -0.0366 291 LEU A CG  
1659  C CD1 . LEU A 227 ? 1.0706 0.9637 0.9800 0.0384  -0.0351 -0.0400 291 LEU A CD1 
1660  C CD2 . LEU A 227 ? 0.8547 0.7404 0.7664 0.0204  -0.0261 -0.0309 291 LEU A CD2 
1661  N N   . GLU A 228 ? 0.7889 0.7053 0.7335 0.0358  -0.0467 -0.0504 292 GLU A N   
1662  C CA  . GLU A 228 ? 0.7172 0.6550 0.6897 0.0305  -0.0465 -0.0534 292 GLU A CA  
1663  C C   . GLU A 228 ? 0.8233 0.7748 0.8077 0.0279  -0.0390 -0.0508 292 GLU A C   
1664  O O   . GLU A 228 ? 1.0133 0.9647 0.9886 0.0359  -0.0385 -0.0513 292 GLU A O   
1665  C CB  . GLU A 228 ? 0.9946 0.9440 0.9755 0.0394  -0.0554 -0.0629 292 GLU A CB  
1666  C CG  . GLU A 228 ? 1.2879 1.2488 1.2896 0.0336  -0.0593 -0.0675 292 GLU A CG  
1667  C CD  . GLU A 228 ? 1.6586 1.6364 1.6732 0.0428  -0.0685 -0.0787 292 GLU A CD  
1668  O OE1 . GLU A 228 ? 1.7169 1.6896 1.7279 0.0470  -0.0770 -0.0839 292 GLU A OE1 
1669  O OE2 . GLU A 228 ? 2.0710 2.0680 2.0993 0.0467  -0.0676 -0.0829 292 GLU A OE2 
1670  N N   . PHE A 229 ? 0.7454 0.7061 0.7473 0.0174  -0.0328 -0.0477 293 PHE A N   
1671  C CA  . PHE A 229 ? 0.7794 0.7541 0.7942 0.0146  -0.0245 -0.0453 293 PHE A CA  
1672  C C   . PHE A 229 ? 0.7949 0.7798 0.8310 0.0035  -0.0196 -0.0443 293 PHE A C   
1673  O O   . PHE A 229 ? 0.8023 0.7784 0.8380 -0.0025 -0.0217 -0.0433 293 PHE A O   
1674  C CB  . PHE A 229 ? 0.6761 0.6381 0.6739 0.0144  -0.0181 -0.0378 293 PHE A CB  
1675  C CG  . PHE A 229 ? 0.6150 0.5631 0.6055 0.0062  -0.0150 -0.0318 293 PHE A CG  
1676  C CD1 . PHE A 229 ? 0.6826 0.6351 0.6848 -0.0022 -0.0082 -0.0279 293 PHE A CD1 
1677  C CD2 . PHE A 229 ? 0.6064 0.5366 0.5773 0.0073  -0.0183 -0.0301 293 PHE A CD2 
1678  C CE1 . PHE A 229 ? 0.6572 0.5965 0.6507 -0.0077 -0.0061 -0.0230 293 PHE A CE1 
1679  C CE2 . PHE A 229 ? 0.6900 0.6102 0.6553 0.0006  -0.0157 -0.0257 293 PHE A CE2 
1680  C CZ  . PHE A 229 ? 0.5306 0.4557 0.5070 -0.0060 -0.0103 -0.0224 293 PHE A CZ  
1681  N N   . ASP A 230 ? 0.7169 0.7187 0.7700 0.0006  -0.0124 -0.0444 294 ASP A N   
1682  C CA  . ASP A 230 ? 0.7109 0.7220 0.7849 -0.0110 -0.0063 -0.0439 294 ASP A CA  
1683  C C   . ASP A 230 ? 0.8002 0.8084 0.8717 -0.0159 0.0059  -0.0358 294 ASP A C   
1684  O O   . ASP A 230 ? 0.6524 0.6511 0.7058 -0.0101 0.0082  -0.0310 294 ASP A O   
1685  C CB  . ASP A 230 ? 0.8778 0.9144 0.9784 -0.0114 -0.0080 -0.0530 294 ASP A CB  
1686  C CG  . ASP A 230 ? 1.2630 1.3168 1.3687 -0.0040 -0.0041 -0.0552 294 ASP A CG  
1687  O OD1 . ASP A 230 ? 1.4988 1.5439 1.5882 -0.0001 0.0016  -0.0485 294 ASP A OD1 
1688  O OD2 . ASP A 230 ? 1.5862 1.6633 1.7128 -0.0016 -0.0072 -0.0643 294 ASP A OD2 
1689  N N   . GLN A 231 ? 0.8858 0.9009 0.9744 -0.0265 0.0138  -0.0345 295 GLN A N   
1690  C CA  . GLN A 231 ? 0.8207 0.8287 0.9033 -0.0309 0.0260  -0.0261 295 GLN A CA  
1691  C C   . GLN A 231 ? 0.7490 0.7675 0.8297 -0.0240 0.0323  -0.0248 295 GLN A C   
1692  O O   . GLN A 231 ? 0.7907 0.7976 0.8556 -0.0221 0.0390  -0.0175 295 GLN A O   
1693  C CB  . GLN A 231 ? 0.9822 0.9907 1.0797 -0.0440 0.0343  -0.0242 295 GLN A CB  
1694  C CG  . GLN A 231 ? 1.2688 1.3015 1.3963 -0.0509 0.0375  -0.0314 295 GLN A CG  
1695  C CD  . GLN A 231 ? 1.4117 1.4387 1.5500 -0.0655 0.0462  -0.0288 295 GLN A CD  
1696  O OE1 . GLN A 231 ? 2.0103 2.0148 2.1340 -0.0691 0.0459  -0.0235 295 GLN A OE1 
1697  N NE2 . GLN A 231 ? 1.9004 1.9476 2.0641 -0.0738 0.0543  -0.0329 295 GLN A NE2 
1698  N N   . SER A 232 ? 0.8740 0.9139 0.9692 -0.0186 0.0293  -0.0323 296 SER A N   
1699  C CA  . SER A 232 ? 0.9898 1.0414 1.0837 -0.0108 0.0353  -0.0317 296 SER A CA  
1700  C C   . SER A 232 ? 0.8360 0.8769 0.9063 0.0026  0.0280  -0.0315 296 SER A C   
1701  O O   . SER A 232 ? 1.0208 1.0715 1.0888 0.0114  0.0302  -0.0328 296 SER A O   
1702  C CB  . SER A 232 ? 1.0742 1.1561 1.1956 -0.0107 0.0365  -0.0406 296 SER A CB  
1703  O OG  . SER A 232 ? 1.6018 1.6904 1.7253 -0.0024 0.0228  -0.0496 296 SER A OG  
1704  N N   . PHE A 233 ? 0.7547 0.7751 0.8071 0.0037  0.0199  -0.0299 297 PHE A N   
1705  C CA  . PHE A 233 ? 0.8736 0.8793 0.9018 0.0142  0.0128  -0.0297 297 PHE A CA  
1706  C C   . PHE A 233 ? 0.9237 0.9388 0.9517 0.0255  0.0045  -0.0376 297 PHE A C   
1707  O O   . PHE A 233 ? 1.1798 1.1832 1.1871 0.0349  0.0008  -0.0373 297 PHE A O   
1708  C CB  . PHE A 233 ? 0.8813 0.8763 0.8913 0.0183  0.0190  -0.0233 297 PHE A CB  
1709  C CG  . PHE A 233 ? 0.9711 0.9489 0.9701 0.0117  0.0228  -0.0162 297 PHE A CG  
1710  C CD1 . PHE A 233 ? 1.0136 0.9791 1.0084 0.0064  0.0174  -0.0159 297 PHE A CD1 
1711  C CD2 . PHE A 233 ? 1.2859 1.2596 1.2773 0.0123  0.0316  -0.0103 297 PHE A CD2 
1712  C CE1 . PHE A 233 ? 1.2896 1.2408 1.2742 0.0017  0.0202  -0.0104 297 PHE A CE1 
1713  C CE2 . PHE A 233 ? 1.3210 1.2787 1.3008 0.0081  0.0342  -0.0046 297 PHE A CE2 
1714  C CZ  . PHE A 233 ? 1.2901 1.2374 1.2671 0.0029  0.0282  -0.0051 297 PHE A CZ  
1715  N N   . THR A 234 ? 0.8242 0.8595 0.8740 0.0252  0.0013  -0.0452 298 THR A N   
1716  C CA  . THR A 234 ? 0.8408 0.8819 0.8874 0.0374  -0.0089 -0.0537 298 THR A CA  
1717  C C   . THR A 234 ? 0.7475 0.7674 0.7777 0.0379  -0.0183 -0.0541 298 THR A C   
1718  O O   . THR A 234 ? 0.7640 0.7804 0.8020 0.0284  -0.0191 -0.0532 298 THR A O   
1719  C CB  . THR A 234 ? 0.7223 0.7954 0.7983 0.0392  -0.0103 -0.0637 298 THR A CB  
1720  O OG1 . THR A 234 ? 1.0032 1.0849 1.1016 0.0263  -0.0089 -0.0654 298 THR A OG1 
1721  C CG2 . THR A 234 ? 0.8908 0.9841 0.9792 0.0405  -0.0001 -0.0631 298 THR A CG2 
1722  N N   . TYR A 235 ? 0.6086 0.6121 0.6141 0.0487  -0.0245 -0.0547 299 TYR A N   
1723  C CA  . TYR A 235 ? 0.7010 0.6811 0.6872 0.0484  -0.0308 -0.0534 299 TYR A CA  
1724  C C   . TYR A 235 ? 0.8478 0.8194 0.8162 0.0625  -0.0400 -0.0593 299 TYR A C   
1725  O O   . TYR A 235 ? 1.3393 1.3163 1.3023 0.0731  -0.0409 -0.0622 299 TYR A O   
1726  C CB  . TYR A 235 ? 0.6763 0.6345 0.6423 0.0438  -0.0259 -0.0450 299 TYR A CB  
1727  C CG  . TYR A 235 ? 0.8290 0.7751 0.7727 0.0535  -0.0261 -0.0439 299 TYR A CG  
1728  C CD1 . TYR A 235 ? 0.9013 0.8567 0.8478 0.0565  -0.0201 -0.0420 299 TYR A CD1 
1729  C CD2 . TYR A 235 ? 0.7898 0.7133 0.7078 0.0598  -0.0320 -0.0449 299 TYR A CD2 
1730  C CE1 . TYR A 235 ? 0.9971 0.9394 0.9212 0.0662  -0.0211 -0.0415 299 TYR A CE1 
1731  C CE2 . TYR A 235 ? 0.8134 0.7226 0.7090 0.0683  -0.0324 -0.0441 299 TYR A CE2 
1732  C CZ  . TYR A 235 ? 0.8482 0.7669 0.7471 0.0717  -0.0276 -0.0427 299 TYR A CZ  
1733  O OH  . TYR A 235 ? 0.9765 0.8789 0.8515 0.0805  -0.0288 -0.0424 299 TYR A OH  
1734  N N   . THR A 236 ? 0.8097 0.7667 0.7669 0.0634  -0.0468 -0.0611 300 THR A N   
1735  C CA  . THR A 236 ? 0.8903 0.8300 0.8221 0.0768  -0.0549 -0.0651 300 THR A CA  
1736  C C   . THR A 236 ? 0.7848 0.6956 0.6931 0.0727  -0.0556 -0.0604 300 THR A C   
1737  O O   . THR A 236 ? 0.7505 0.6608 0.6671 0.0630  -0.0546 -0.0583 300 THR A O   
1738  C CB  . THR A 236 ? 0.9681 0.9226 0.9099 0.0874  -0.0647 -0.0757 300 THR A CB  
1739  O OG1 . THR A 236 ? 1.4324 1.3841 1.3801 0.0816  -0.0685 -0.0770 300 THR A OG1 
1740  C CG2 . THR A 236 ? 0.9354 0.9254 0.9091 0.0885  -0.0636 -0.0820 300 THR A CG2 
1741  N N   . PHE A 237 ? 0.8361 0.7225 0.7145 0.0801  -0.0570 -0.0589 301 PHE A N   
1742  C CA  . PHE A 237 ? 0.7145 0.5743 0.5704 0.0767  -0.0571 -0.0555 301 PHE A CA  
1743  C C   . PHE A 237 ? 0.7840 0.6367 0.6285 0.0883  -0.0660 -0.0619 301 PHE A C   
1744  O O   . PHE A 237 ? 1.0298 0.8860 0.8685 0.1025  -0.0720 -0.0680 301 PHE A O   
1745  C CB  . PHE A 237 ? 0.9104 0.7445 0.7377 0.0781  -0.0536 -0.0512 301 PHE A CB  
1746  C CG  . PHE A 237 ? 0.9135 0.7480 0.7462 0.0659  -0.0455 -0.0448 301 PHE A CG  
1747  C CD1 . PHE A 237 ? 0.8933 0.7386 0.7331 0.0673  -0.0423 -0.0437 301 PHE A CD1 
1748  C CD2 . PHE A 237 ? 1.1052 0.9288 0.9345 0.0541  -0.0414 -0.0405 301 PHE A CD2 
1749  C CE1 . PHE A 237 ? 1.1607 1.0051 1.0032 0.0577  -0.0357 -0.0385 301 PHE A CE1 
1750  C CE2 . PHE A 237 ? 1.0086 0.8332 0.8424 0.0443  -0.0351 -0.0359 301 PHE A CE2 
1751  C CZ  . PHE A 237 ? 1.3046 1.1388 1.1442 0.0464  -0.0326 -0.0349 301 PHE A CZ  
1752  N N   . LYS A 238 ? 0.9061 0.7487 0.7461 0.0837  -0.0671 -0.0610 302 LYS A N   
1753  C CA  . LYS A 238 ? 0.9760 0.8053 0.7985 0.0952  -0.0751 -0.0663 302 LYS A CA  
1754  C C   . LYS A 238 ? 1.0942 0.8901 0.8853 0.0923  -0.0712 -0.0607 302 LYS A C   
1755  O O   . LYS A 238 ? 1.0475 0.8390 0.8411 0.0786  -0.0635 -0.0544 302 LYS A O   
1756  C CB  . LYS A 238 ? 0.8319 0.6806 0.6783 0.0933  -0.0805 -0.0714 302 LYS A CB  
1757  C CG  . LYS A 238 ? 0.8574 0.7413 0.7397 0.0918  -0.0823 -0.0767 302 LYS A CG  
1758  C CD  . LYS A 238 ? 0.9485 0.8488 0.8534 0.0884  -0.0875 -0.0821 302 LYS A CD  
1759  C CE  . LYS A 238 ? 0.9004 0.8301 0.8310 0.0950  -0.0941 -0.0922 302 LYS A CE  
1760  N NZ  . LYS A 238 ? 1.1439 1.0794 1.0822 0.0997  -0.1041 -0.1007 302 LYS A NZ  
1761  N N   . GLU A 239 ? 1.1867 0.9588 0.9477 0.1054  -0.0761 -0.0634 303 GLU A N   
1762  C CA  . GLU A 239 ? 1.2655 1.0048 0.9957 0.1027  -0.0717 -0.0586 303 GLU A CA  
1763  C C   . GLU A 239 ? 1.1616 0.8953 0.8846 0.1103  -0.0780 -0.0627 303 GLU A C   
1764  O O   . GLU A 239 ? 1.2261 0.9625 0.9445 0.1260  -0.0877 -0.0700 303 GLU A O   
1765  C CB  . GLU A 239 ? 1.3378 1.0459 1.0315 0.1114  -0.0704 -0.0572 303 GLU A CB  
1766  C CG  . GLU A 239 ? 1.4358 1.1062 1.0937 0.1095  -0.0651 -0.0527 303 GLU A CG  
1767  C CD  . GLU A 239 ? 1.7002 1.3598 1.3555 0.0912  -0.0531 -0.0452 303 GLU A CD  
1768  O OE1 . GLU A 239 ? 1.6518 1.3290 1.3282 0.0816  -0.0496 -0.0432 303 GLU A OE1 
1769  O OE2 . GLU A 239 ? 1.8384 1.4712 1.4695 0.0866  -0.0470 -0.0416 303 GLU A OE2 
1770  N N   . PRO A 240 ? 1.0185 0.7446 0.7398 0.1001  -0.0729 -0.0585 304 PRO A N   
1771  C CA  . PRO A 240 ? 1.0269 0.7485 0.7421 0.1070  -0.0787 -0.0622 304 PRO A CA  
1772  C C   . PRO A 240 ? 1.2327 0.9205 0.9062 0.1225  -0.0817 -0.0636 304 PRO A C   
1773  O O   . PRO A 240 ? 1.1295 0.7891 0.7745 0.1207  -0.0742 -0.0582 304 PRO A O   
1774  C CB  . PRO A 240 ? 0.9624 0.6813 0.6822 0.0918  -0.0702 -0.0562 304 PRO A CB  
1775  C CG  . PRO A 240 ? 1.0631 0.7708 0.7746 0.0804  -0.0596 -0.0494 304 PRO A CG  
1776  C CD  . PRO A 240 ? 1.0171 0.7352 0.7371 0.0836  -0.0616 -0.0507 304 PRO A CD  
1777  N N   . CYS A 241 ? 1.6239 1.3143 1.2939 0.1380  -0.0928 -0.0713 305 CYS A N   
1778  C CA  . CYS A 241 ? 1.5110 1.1704 1.1406 0.1568  -0.0981 -0.0743 305 CYS A CA  
1779  C C   . CYS A 241 ? 1.5935 1.2332 1.2033 0.1587  -0.0970 -0.0728 305 CYS A C   
1780  O O   . CYS A 241 ? 2.1093 1.7474 1.7109 0.1744  -0.1077 -0.0801 305 CYS A O   
1781  C CB  . CYS A 241 ? 1.4660 1.1430 1.1040 0.1759  -0.1129 -0.0858 305 CYS A CB  
1782  S SG  . CYS A 241 ? 2.4450 2.1559 2.1153 0.1751  -0.1156 -0.0898 305 CYS A SG  
1783  N N   . LEU A 242 ? 1.3927 1.0187 0.9953 0.1432  -0.0844 -0.0642 306 LEU A N   
1784  C CA  . LEU A 242 ? 1.3421 0.9512 0.9272 0.1437  -0.0815 -0.0622 306 LEU A CA  
1785  C C   . LEU A 242 ? 1.5084 1.0839 1.0621 0.1344  -0.0667 -0.0531 306 LEU A C   
1786  O O   . LEU A 242 ? 1.3293 0.9089 0.8937 0.1177  -0.0565 -0.0474 306 LEU A O   
1787  C CB  . LEU A 242 ? 1.0668 0.7061 0.6884 0.1327  -0.0827 -0.0633 306 LEU A CB  
1788  C CG  . LEU A 242 ? 0.9994 0.6684 0.6500 0.1411  -0.0971 -0.0730 306 LEU A CG  
1789  C CD1 . LEU A 242 ? 1.0304 0.7238 0.7137 0.1270  -0.0953 -0.0721 306 LEU A CD1 
1790  C CD2 . LEU A 242 ? 1.0598 0.7148 0.6872 0.1624  -0.1089 -0.0808 306 LEU A CD2 
1791  N N   . GLY A 243 ? 1.4337 0.9761 0.9485 0.1453  -0.0653 -0.0522 307 GLY A N   
1792  C CA  . GLY A 243 ? 1.4477 0.9548 0.9291 0.1369  -0.0501 -0.0438 307 GLY A CA  
1793  C C   . GLY A 243 ? 1.6420 1.1613 1.1426 0.1156  -0.0376 -0.0381 307 GLY A C   
1794  O O   . GLY A 243 ? 1.9287 1.4235 1.4069 0.1058  -0.0237 -0.0318 307 GLY A O   
1795  N N   . PHE A 244 ? 1.8612 1.4184 1.4031 0.1085  -0.0425 -0.0409 308 PHE A N   
1796  C CA  . PHE A 244 ? 1.3292 0.9036 0.8938 0.0901  -0.0329 -0.0369 308 PHE A CA  
1797  C C   . PHE A 244 ? 1.2455 0.8348 0.8319 0.0738  -0.0265 -0.0339 308 PHE A C   
1798  O O   . PHE A 244 ? 1.2170 0.8319 0.8319 0.0727  -0.0335 -0.0367 308 PHE A O   
1799  C CB  . PHE A 244 ? 1.2142 0.8187 0.8094 0.0917  -0.0420 -0.0415 308 PHE A CB  
1800  C CG  . PHE A 244 ? 1.1532 0.7645 0.7564 0.0806  -0.0337 -0.0384 308 PHE A CG  
1801  C CD1 . PHE A 244 ? 1.1516 0.7398 0.7260 0.0859  -0.0284 -0.0366 308 PHE A CD1 
1802  C CD2 . PHE A 244 ? 0.9651 0.6058 0.6034 0.0664  -0.0315 -0.0376 308 PHE A CD2 
1803  C CE1 . PHE A 244 ? 1.0927 0.6889 0.6747 0.0768  -0.0207 -0.0343 308 PHE A CE1 
1804  C CE2 . PHE A 244 ? 0.8814 0.5293 0.5265 0.0579  -0.0246 -0.0356 308 PHE A CE2 
1805  C CZ  . PHE A 244 ? 1.0300 0.6568 0.6477 0.0631  -0.0192 -0.0341 308 PHE A CZ  
1806  N N   . LEU A 245 ? 1.0458 0.6184 0.6181 0.0611  -0.0128 -0.0285 309 LEU A N   
1807  C CA  . LEU A 245 ? 1.1256 0.7050 0.7104 0.0481  -0.0073 -0.0263 309 LEU A CA  
1808  C C   . LEU A 245 ? 1.0473 0.6579 0.6672 0.0333  -0.0037 -0.0259 309 LEU A C   
1809  O O   . LEU A 245 ? 1.3657 0.9753 0.9839 0.0256  0.0045  -0.0241 309 LEU A O   
1810  C CB  . LEU A 245 ? 1.2593 0.8035 0.8107 0.0416  0.0052  -0.0218 309 LEU A CB  
1811  C CG  . LEU A 245 ? 1.2633 0.7701 0.7739 0.0564  0.0027  -0.0216 309 LEU A CG  
1812  C CD1 . LEU A 245 ? 1.6420 1.1202 1.1296 0.0450  0.0149  -0.0174 309 LEU A CD1 
1813  C CD2 . LEU A 245 ? 1.0384 0.5575 0.5581 0.0715  -0.0121 -0.0266 309 LEU A CD2 
1814  N N   . GLY A 246 ? 0.9469 0.5848 0.5971 0.0304  -0.0098 -0.0279 310 GLY A N   
1815  C CA  . GLY A 246 ? 0.9857 0.6529 0.6683 0.0184  -0.0077 -0.0278 310 GLY A CA  
1816  C C   . GLY A 246 ? 0.9421 0.6090 0.6272 0.0024  0.0038  -0.0252 310 GLY A C   
1817  O O   . GLY A 246 ? 0.9498 0.6299 0.6475 -0.0067 0.0093  -0.0251 310 GLY A O   
1818  N N   . ASP A 247 ? 0.9838 0.6357 0.6564 -0.0005 0.0070  -0.0241 311 ASP A N   
1819  C CA  . ASP A 247 ? 1.1619 0.8177 0.8422 -0.0155 0.0153  -0.0232 311 ASP A CA  
1820  C C   . ASP A 247 ? 1.1614 0.8031 0.8276 -0.0265 0.0279  -0.0217 311 ASP A C   
1821  O O   . ASP A 247 ? 0.9818 0.6074 0.6288 -0.0216 0.0308  -0.0204 311 ASP A O   
1822  C CB  . ASP A 247 ? 1.3164 0.9567 0.9841 -0.0141 0.0143  -0.0229 311 ASP A CB  
1823  C CG  . ASP A 247 ? 1.3180 0.9774 1.0081 -0.0242 0.0151  -0.0239 311 ASP A CG  
1824  O OD1 . ASP A 247 ? 1.0154 0.6920 0.7233 -0.0357 0.0201  -0.0249 311 ASP A OD1 
1825  O OD2 . ASP A 247 ? 1.1529 0.8102 0.8419 -0.0193 0.0103  -0.0244 311 ASP A OD2 
1826  N N   . THR A 248 ? 1.1986 0.8468 0.8747 -0.0411 0.0353  -0.0224 312 THR A N   
1827  C CA  . THR A 248 ? 1.0779 0.7169 0.7455 -0.0546 0.0486  -0.0221 312 THR A CA  
1828  C C   . THR A 248 ? 1.2138 0.8513 0.8855 -0.0686 0.0545  -0.0238 312 THR A C   
1829  O O   . THR A 248 ? 1.6779 1.3402 1.3750 -0.0722 0.0498  -0.0266 312 THR A O   
1830  C CB  . THR A 248 ? 1.1565 0.8226 0.8463 -0.0595 0.0511  -0.0240 312 THR A CB  
1831  O OG1 . THR A 248 ? 1.3782 1.0439 1.0627 -0.0467 0.0456  -0.0228 312 THR A OG1 
1832  C CG2 . THR A 248 ? 1.0792 0.7396 0.7631 -0.0744 0.0660  -0.0245 312 THR A CG2 
1833  N N   . PRO A 249 ? 1.3068 0.9139 0.9525 -0.0767 0.0650  -0.0224 313 PRO A N   
1834  C CA  . PRO A 249 ? 1.2595 0.8351 0.8724 -0.0726 0.0721  -0.0187 313 PRO A CA  
1835  C C   . PRO A 249 ? 1.2423 0.7927 0.8293 -0.0548 0.0633  -0.0161 313 PRO A C   
1836  O O   . PRO A 249 ? 1.2220 0.7814 0.8185 -0.0470 0.0525  -0.0174 313 PRO A O   
1837  C CB  . PRO A 249 ? 1.6818 1.2339 1.2780 -0.0894 0.0866  -0.0184 313 PRO A CB  
1838  C CG  . PRO A 249 ? 1.7085 1.2666 1.3168 -0.0954 0.0824  -0.0214 313 PRO A CG  
1839  C CD  . PRO A 249 ? 1.3047 0.9034 0.9491 -0.0899 0.0704  -0.0244 313 PRO A CD  
1840  N N   . ARG A 250 ? 1.1852 0.7049 0.7392 -0.0479 0.0681  -0.0129 314 ARG A N   
1841  C CA  . ARG A 250 ? 1.1593 0.6534 0.6846 -0.0285 0.0597  -0.0114 314 ARG A CA  
1842  C C   . ARG A 250 ? 1.3008 0.7527 0.7834 -0.0271 0.0706  -0.0075 314 ARG A C   
1843  O O   . ARG A 250 ? 1.6206 1.0692 1.1007 -0.0399 0.0840  -0.0060 314 ARG A O   
1844  C CB  . ARG A 250 ? 1.1015 0.6197 0.6438 -0.0134 0.0469  -0.0133 314 ARG A CB  
1845  C CG  . ARG A 250 ? 1.1648 0.6999 0.7197 -0.0172 0.0514  -0.0133 314 ARG A CG  
1846  C CD  . ARG A 250 ? 1.2090 0.7605 0.7742 -0.0013 0.0385  -0.0154 314 ARG A CD  
1847  N NE  . ARG A 250 ? 1.2952 0.8751 0.8860 -0.0066 0.0396  -0.0167 314 ARG A NE  
1848  C CZ  . ARG A 250 ? 1.2070 0.7795 0.7854 -0.0054 0.0459  -0.0156 314 ARG A CZ  
1849  N NH1 . ARG A 250 ? 1.5597 1.0960 1.0995 0.0005  0.0523  -0.0126 314 ARG A NH1 
1850  N NH2 . ARG A 250 ? 1.1388 0.7388 0.7414 -0.0091 0.0457  -0.0173 314 ARG A NH2 
1851  N N   . GLY A 251 ? 1.3637 0.7831 0.8118 -0.0108 0.0653  -0.0061 315 GLY A N   
1852  C CA  . GLY A 251 ? 1.9763 1.3489 1.3778 -0.0090 0.0764  -0.0019 315 GLY A CA  
1853  C C   . GLY A 251 ? 2.1568 1.5238 1.5441 0.0024  0.0767  -0.0006 315 GLY A C   
1854  O O   . GLY A 251 ? 2.4503 1.8099 1.8299 -0.0077 0.0905  0.0021  315 GLY A O   
1855  N N   . ILE A 252 ? 1.8987 1.2708 1.2838 0.0238  0.0612  -0.0032 316 ILE A N   
1856  C CA  . ILE A 252 ? 1.6262 0.9807 0.9850 0.0404  0.0589  -0.0026 316 ILE A CA  
1857  C C   . ILE A 252 ? 1.5703 0.9445 0.9422 0.0609  0.0389  -0.0081 316 ILE A C   
1858  O O   . ILE A 252 ? 1.8337 1.2195 1.2192 0.0646  0.0293  -0.0109 316 ILE A O   
1859  C CB  . ILE A 252 ? 1.7487 1.0453 1.0492 0.0481  0.0673  0.0017  316 ILE A CB  
1860  C CG1 . ILE A 252 ? 1.6613 0.9375 0.9336 0.0568  0.0734  0.0042  316 ILE A CG1 
1861  C CG2 . ILE A 252 ? 1.8563 1.1323 1.1334 0.0681  0.0537  -0.0008 316 ILE A CG2 
1862  C CD1 . ILE A 252 ? 1.4446 0.7210 0.7204 0.0356  0.0933  0.0085  316 ILE A CD1 
1863  N N   . ASP A 253 ? 1.5871 0.9651 0.9549 0.0745  0.0326  -0.0100 317 ASP A N   
1864  C CA  . ASP A 253 ? 1.6483 1.0478 1.0319 0.0929  0.0133  -0.0165 317 ASP A CA  
1865  C C   . ASP A 253 ? 1.5163 0.8821 0.8607 0.1141  0.0051  -0.0184 317 ASP A C   
1866  O O   . ASP A 253 ? 1.5466 0.8681 0.8446 0.1195  0.0135  -0.0144 317 ASP A O   
1867  C CB  . ASP A 253 ? 1.7070 1.1258 1.1042 0.0995  0.0077  -0.0193 317 ASP A CB  
1868  C CG  . ASP A 253 ? 1.8086 1.2691 1.2522 0.0820  0.0105  -0.0195 317 ASP A CG  
1869  O OD1 . ASP A 253 ? 1.5293 1.0149 1.0044 0.0703  0.0094  -0.0202 317 ASP A OD1 
1870  O OD2 . ASP A 253 ? 1.9498 1.4169 1.3964 0.0811  0.0137  -0.0192 317 ASP A OD2 
1871  N N   . THR A 254 ? 1.4973 0.8840 0.8602 0.1258  -0.0106 -0.0246 318 THR A N   
1872  C CA  . THR A 254 ? 1.7020 1.0627 1.0331 0.1455  -0.0196 -0.0276 318 THR A CA  
1873  C C   . THR A 254 ? 1.4846 0.8585 0.8189 0.1686  -0.0374 -0.0360 318 THR A C   
1874  O O   . THR A 254 ? 1.1503 0.5492 0.5084 0.1681  -0.0417 -0.0388 318 THR A O   
1875  C CB  . THR A 254 ? 1.7785 1.1525 1.1275 0.1408  -0.0231 -0.0290 318 THR A CB  
1876  O OG1 . THR A 254 ? 1.8060 1.2309 1.2073 0.1364  -0.0324 -0.0338 318 THR A OG1 
1877  C CG2 . THR A 254 ? 1.6086 0.9656 0.9508 0.1194  -0.0068 -0.0219 318 THR A CG2 
1878  N N   . THR A 255 ? 1.8642 1.2203 1.1733 0.1893  -0.0480 -0.0407 319 THR A N   
1879  C CA  . THR A 255 ? 1.7607 1.1374 1.0806 0.2111  -0.0672 -0.0512 319 THR A CA  
1880  C C   . THR A 255 ? 1.5069 0.9342 0.8818 0.2024  -0.0748 -0.0559 319 THR A C   
1881  O O   . THR A 255 ? 1.3914 0.8288 0.7850 0.1841  -0.0660 -0.0509 319 THR A O   
1882  C CB  . THR A 255 ? 1.7801 1.1199 1.0522 0.2375  -0.0758 -0.0553 319 THR A CB  
1883  O OG1 . THR A 255 ? 1.7618 1.0909 1.0263 0.2337  -0.0724 -0.0529 319 THR A OG1 
1884  C CG2 . THR A 255 ? 1.5633 0.8492 0.7772 0.2465  -0.0672 -0.0499 319 THR A CG2 
1885  N N   . ASN A 256 ? 1.3738 0.8324 0.7744 0.2151  -0.0906 -0.0657 320 ASN A N   
1886  C CA  . ASN A 256 ? 1.6955 1.1999 1.1457 0.2076  -0.0969 -0.0703 320 ASN A CA  
1887  C C   . ASN A 256 ? 1.6744 1.1772 1.1180 0.2178  -0.1023 -0.0737 320 ASN A C   
1888  O O   . ASN A 256 ? 1.7935 1.2757 1.2058 0.2402  -0.1114 -0.0793 320 ASN A O   
1889  C CB  . ASN A 256 ? 1.6808 1.2208 1.1636 0.2153  -0.1110 -0.0802 320 ASN A CB  
1890  C CG  . ASN A 256 ? 1.5055 1.0480 0.9950 0.2071  -0.1073 -0.0777 320 ASN A CG  
1891  O OD1 . ASN A 256 ? 1.5099 1.0275 0.9780 0.1971  -0.0939 -0.0689 320 ASN A OD1 
1892  N ND2 . ASN A 256 ? 1.5524 1.1253 1.0720 0.2111  -0.1188 -0.0860 320 ASN A ND2 
1893  N N   . TYR A 257 ? 1.7101 1.2344 1.1821 0.2026  -0.0972 -0.0708 321 TYR A N   
1894  C CA  . TYR A 257 ? 1.8693 1.4008 1.3432 0.2121  -0.1033 -0.0751 321 TYR A CA  
1895  C C   . TYR A 257 ? 1.9580 1.5256 1.4757 0.1943  -0.0991 -0.0731 321 TYR A C   
1896  O O   . TYR A 257 ? 1.6788 1.2515 1.2119 0.1733  -0.0879 -0.0657 321 TYR A O   
1897  C CB  . TYR A 257 ? 1.7344 1.2181 1.1573 0.2201  -0.0981 -0.0706 321 TYR A CB  
1898  C CG  . TYR A 257 ? 1.6742 1.1312 1.0816 0.1993  -0.0809 -0.0593 321 TYR A CG  
1899  C CD1 . TYR A 257 ? 1.6049 1.0717 1.0302 0.1823  -0.0729 -0.0546 321 TYR A CD1 
1900  C CD2 . TYR A 257 ? 1.6405 1.0628 1.0151 0.1970  -0.0724 -0.0538 321 TYR A CD2 
1901  C CE1 . TYR A 257 ? 1.6504 1.0946 1.0632 0.1631  -0.0578 -0.0457 321 TYR A CE1 
1902  C CE2 . TYR A 257 ? 1.6912 1.0908 1.0532 0.1770  -0.0559 -0.0444 321 TYR A CE2 
1903  C CZ  . TYR A 257 ? 1.6417 1.0531 1.0238 0.1600  -0.0491 -0.0409 321 TYR A CZ  
1904  O OH  . TYR A 257 ? 1.5546 0.9451 0.9257 0.1401  -0.0334 -0.0330 321 TYR A OH  
1905  N N   . CYS A 258 ? 1.8373 1.4293 1.3732 0.2039  -0.1078 -0.0801 322 CYS A N   
1906  C CA  . CYS A 258 ? 1.6194 1.2498 1.1993 0.1897  -0.1052 -0.0796 322 CYS A CA  
1907  C C   . CYS A 258 ? 1.7233 1.3405 1.2941 0.1800  -0.0956 -0.0725 322 CYS A C   
1908  O O   . CYS A 258 ? 1.6380 1.2828 1.2397 0.1702  -0.0931 -0.0718 322 CYS A O   
1909  C CB  . CYS A 258 ? 1.6645 1.3325 1.2740 0.2022  -0.1177 -0.0907 322 CYS A CB  
1910  S SG  . CYS A 258 ? 2.5967 2.2895 2.2308 0.2064  -0.1281 -0.0993 322 CYS A SG  
1911  N N   . ASP A 259 ? 1.9753 1.5483 1.5021 0.1824  -0.0898 -0.0673 323 ASP A N   
1912  C CA  . ASP A 259 ? 1.9637 1.5183 1.4779 0.1713  -0.0800 -0.0605 323 ASP A CA  
1913  C C   . ASP A 259 ? 1.3872 0.9429 0.9152 0.1466  -0.0674 -0.0525 323 ASP A C   
1914  O O   . ASP A 259 ? 1.2582 0.8268 0.8023 0.1398  -0.0663 -0.0520 323 ASP A O   
1915  C CB  . ASP A 259 ? 2.0435 1.5479 1.5028 0.1848  -0.0795 -0.0592 323 ASP A CB  
1916  C CG  . ASP A 259 ? 1.9472 1.4372 1.3939 0.1820  -0.0754 -0.0564 323 ASP A CG  
1917  O OD1 . ASP A 259 ? 1.7921 1.3134 1.2681 0.1811  -0.0785 -0.0590 323 ASP A OD1 
1918  O OD2 . ASP A 259 ? 2.3285 1.7740 1.7344 0.1807  -0.0686 -0.0516 323 ASP A OD2 
1919  N N   . LYS A 260 ? 1.1430 0.6857 0.6644 0.1342  -0.0585 -0.0471 324 LYS A N   
1920  C CA  . LYS A 260 ? 1.2108 0.7529 0.7424 0.1117  -0.0466 -0.0406 324 LYS A CA  
1921  C C   . LYS A 260 ? 1.4003 0.8970 0.8912 0.1060  -0.0366 -0.0354 324 LYS A C   
1922  O O   . LYS A 260 ? 1.3403 0.8015 0.7945 0.1132  -0.0354 -0.0345 324 LYS A O   
1923  C CB  . LYS A 260 ? 1.0843 0.6446 0.6380 0.1015  -0.0438 -0.0393 324 LYS A CB  
1924  C CG  . LYS A 260 ? 1.1808 0.7270 0.7299 0.0825  -0.0324 -0.0339 324 LYS A CG  
1925  C CD  . LYS A 260 ? 1.4808 1.0274 1.0309 0.0814  -0.0324 -0.0340 324 LYS A CD  
1926  C CE  . LYS A 260 ? 1.4195 1.0028 0.9999 0.0899  -0.0405 -0.0379 324 LYS A CE  
1927  N NZ  . LYS A 260 ? 1.4094 0.9894 0.9856 0.0911  -0.0404 -0.0379 324 LYS A NZ  
1928  N N   . THR A 261 ? 1.3024 0.7998 0.7993 0.0928  -0.0287 -0.0320 325 THR A N   
1929  C CA  . THR A 261 ? 1.2637 0.7211 0.7251 0.0857  -0.0175 -0.0271 325 THR A CA  
1930  C C   . THR A 261 ? 1.2202 0.6649 0.6784 0.0667  -0.0059 -0.0230 325 THR A C   
1931  O O   . THR A 261 ? 1.3412 0.8067 0.8261 0.0490  0.0009  -0.0214 325 THR A O   
1932  C CB  . THR A 261 ? 1.1760 0.6412 0.6459 0.0790  -0.0128 -0.0255 325 THR A CB  
1933  O OG1 . THR A 261 ? 1.3507 0.8250 0.8213 0.0969  -0.0240 -0.0300 325 THR A OG1 
1934  C CG2 . THR A 261 ? 1.2239 0.6480 0.6567 0.0713  0.0005  -0.0204 325 THR A CG2 
1935  N N   . THR A 262 ? 1.3699 0.7788 0.7940 0.0705  -0.0039 -0.0220 326 THR A N   
1936  C CA  . THR A 262 ? 1.4486 0.8488 0.8734 0.0532  0.0047  -0.0198 326 THR A CA  
1937  C C   . THR A 262 ? 1.4011 0.7763 0.8097 0.0349  0.0199  -0.0156 326 THR A C   
1938  O O   . THR A 262 ? 1.4877 0.8599 0.9019 0.0179  0.0276  -0.0147 326 THR A O   
1939  C CB  . THR A 262 ? 1.4759 0.8472 0.8711 0.0634  0.0010  -0.0207 326 THR A CB  
1940  O OG1 . THR A 262 ? 2.3520 1.6709 1.6967 0.0677  0.0071  -0.0179 326 THR A OG1 
1941  C CG2 . THR A 262 ? 1.3853 0.7750 0.7875 0.0857  -0.0137 -0.0255 326 THR A CG2 
1942  N N   . THR A 263 ? 1.4234 0.7812 0.8121 0.0385  0.0242  -0.0134 327 THR A N   
1943  C CA  . THR A 263 ? 1.4110 0.7415 0.7798 0.0222  0.0401  -0.0093 327 THR A CA  
1944  C C   . THR A 263 ? 1.3333 0.7008 0.7422 0.0034  0.0467  -0.0094 327 THR A C   
1945  O O   . THR A 263 ? 1.3443 0.7418 0.7771 0.0084  0.0413  -0.0106 327 THR A O   
1946  C CB  . THR A 263 ? 1.4728 0.7686 0.8019 0.0341  0.0433  -0.0066 327 THR A CB  
1947  O OG1 . THR A 263 ? 1.5959 0.8700 0.8956 0.0585  0.0317  -0.0085 327 THR A OG1 
1948  C CG2 . THR A 263 ? 1.4646 0.7173 0.7595 0.0189  0.0611  -0.0017 327 THR A CG2 
1949  N N   . GLU A 264 ? 1.3071 0.6709 0.7217 -0.0177 0.0580  -0.0087 328 GLU A N   
1950  C CA  . GLU A 264 ? 1.2971 0.6986 0.7521 -0.0361 0.0635  -0.0102 328 GLU A CA  
1951  C C   . GLU A 264 ? 1.4353 0.8840 0.9333 -0.0316 0.0510  -0.0138 328 GLU A C   
1952  O O   . GLU A 264 ? 1.7657 1.2498 1.2973 -0.0390 0.0514  -0.0152 328 GLU A O   
1953  C CB  . GLU A 264 ? 1.1462 0.5499 0.6005 -0.0412 0.0726  -0.0082 328 GLU A CB  
1954  C CG  . GLU A 264 ? 1.3375 0.7051 0.7625 -0.0558 0.0901  -0.0051 328 GLU A CG  
1955  C CD  . GLU A 264 ? 1.7610 1.1530 1.2101 -0.0728 0.1016  -0.0057 328 GLU A CD  
1956  O OE1 . GLU A 264 ? 1.8065 1.2313 1.2914 -0.0875 0.1027  -0.0096 328 GLU A OE1 
1957  O OE2 . GLU A 264 ? 1.7378 1.1166 1.1695 -0.0706 0.1093  -0.0027 328 GLU A OE2 
1958  N N   . GLY A 265 ? 1.3529 0.8012 0.8484 -0.0190 0.0404  -0.0152 329 GLY A N   
1959  C CA  . GLY A 265 ? 1.2259 0.7154 0.7583 -0.0136 0.0295  -0.0180 329 GLY A CA  
1960  C C   . GLY A 265 ? 1.1783 0.6930 0.7408 -0.0295 0.0323  -0.0200 329 GLY A C   
1961  O O   . GLY A 265 ? 1.5062 1.0562 1.1009 -0.0278 0.0257  -0.0218 329 GLY A O   
1962  N N   . GLU A 266 ? 1.1835 0.6795 0.7349 -0.0449 0.0422  -0.0201 330 GLU A N   
1963  C CA  . GLU A 266 ? 1.3393 0.8567 0.9166 -0.0593 0.0440  -0.0233 330 GLU A CA  
1964  C C   . GLU A 266 ? 1.3529 0.8984 0.9579 -0.0732 0.0503  -0.0250 330 GLU A C   
1965  O O   . GLU A 266 ? 1.2896 0.8245 0.8844 -0.0790 0.0592  -0.0233 330 GLU A O   
1966  C CB  . GLU A 266 ? 1.3696 0.8560 0.9248 -0.0696 0.0502  -0.0243 330 GLU A CB  
1967  C CG  . GLU A 266 ? 2.1172 1.6274 1.6996 -0.0815 0.0491  -0.0290 330 GLU A CG  
1968  C CD  . GLU A 266 ? 2.7561 2.2374 2.3179 -0.0877 0.0512  -0.0309 330 GLU A CD  
1969  O OE1 . GLU A 266 ? 2.8066 2.2469 2.3310 -0.0830 0.0539  -0.0282 330 GLU A OE1 
1970  O OE2 . GLU A 266 ? 3.6432 3.1415 3.2248 -0.0966 0.0496  -0.0355 330 GLU A OE2 
1971  N N   . GLY A 267 ? 1.1703 0.7504 0.8085 -0.0776 0.0460  -0.0284 331 GLY A N   
1972  C CA  . GLY A 267 ? 1.1605 0.7732 0.8282 -0.0858 0.0485  -0.0305 331 GLY A CA  
1973  C C   . GLY A 267 ? 1.3256 0.9586 1.0065 -0.0722 0.0405  -0.0286 331 GLY A C   
1974  O O   . GLY A 267 ? 1.1916 0.8140 0.8596 -0.0577 0.0338  -0.0261 331 GLY A O   
1975  N N   . GLY A 268 ? 1.1346 0.7970 0.8412 -0.0764 0.0408  -0.0304 332 GLY A N   
1976  C CA  . GLY A 268 ? 0.9976 0.6790 0.7179 -0.0651 0.0332  -0.0291 332 GLY A CA  
1977  C C   . GLY A 268 ? 1.0988 0.8136 0.8491 -0.0703 0.0325  -0.0319 332 GLY A C   
1978  O O   . GLY A 268 ? 1.1863 0.9136 0.9497 -0.0808 0.0357  -0.0356 332 GLY A O   
1979  N N   . ILE A 269 ? 0.7843 0.5129 0.5444 -0.0624 0.0277  -0.0308 333 ILE A N   
1980  C CA  . ILE A 269 ? 0.8497 0.6076 0.6358 -0.0643 0.0253  -0.0332 333 ILE A CA  
1981  C C   . ILE A 269 ? 0.8537 0.6225 0.6494 -0.0524 0.0161  -0.0315 333 ILE A C   
1982  O O   . ILE A 269 ? 0.6796 0.4349 0.4623 -0.0440 0.0132  -0.0293 333 ILE A O   
1983  C CB  . ILE A 269 ? 0.8414 0.6051 0.6297 -0.0712 0.0325  -0.0348 333 ILE A CB  
1984  C CG1 . ILE A 269 ? 1.0755 0.8699 0.8900 -0.0748 0.0307  -0.0388 333 ILE A CG1 
1985  C CG2 . ILE A 269 ? 0.6349 0.3872 0.4100 -0.0627 0.0316  -0.0318 333 ILE A CG2 
1986  C CD1 . ILE A 269 ? 1.0516 0.8564 0.8717 -0.0844 0.0393  -0.0425 333 ILE A CD1 
1987  N N   . GLN A 270 ? 0.7242 0.5164 0.5419 -0.0519 0.0118  -0.0329 334 GLN A N   
1988  C CA  . GLN A 270 ? 0.6556 0.4588 0.4847 -0.0429 0.0040  -0.0316 334 GLN A CA  
1989  C C   . GLN A 270 ? 0.7612 0.5635 0.5883 -0.0376 0.0020  -0.0310 334 GLN A C   
1990  O O   . GLN A 270 ? 0.9371 0.7433 0.7649 -0.0413 0.0058  -0.0322 334 GLN A O   
1991  C CB  . GLN A 270 ? 0.8063 0.6312 0.6556 -0.0447 0.0018  -0.0332 334 GLN A CB  
1992  C CG  . GLN A 270 ? 0.8602 0.6947 0.7210 -0.0372 -0.0048 -0.0315 334 GLN A CG  
1993  C CD  . GLN A 270 ? 0.8957 0.7466 0.7713 -0.0383 -0.0062 -0.0325 334 GLN A CD  
1994  O OE1 . GLN A 270 ? 0.7497 0.6083 0.6291 -0.0434 -0.0035 -0.0355 334 GLN A OE1 
1995  N NE2 . GLN A 270 ? 0.9336 0.7900 0.8175 -0.0331 -0.0103 -0.0305 334 GLN A NE2 
1996  N N   . GLY A 271 ? 0.6963 0.4947 0.5217 -0.0287 -0.0042 -0.0298 335 GLY A N   
1997  C CA  . GLY A 271 ? 0.7241 0.5211 0.5475 -0.0224 -0.0079 -0.0301 335 GLY A CA  
1998  C C   . GLY A 271 ? 0.7994 0.5993 0.6288 -0.0137 -0.0160 -0.0304 335 GLY A C   
1999  O O   . GLY A 271 ? 0.9547 0.7571 0.7883 -0.0122 -0.0178 -0.0299 335 GLY A O   
2000  N N   . PHE A 272 ? 0.8511 0.6515 0.6811 -0.0077 -0.0208 -0.0317 336 PHE A N   
2001  C CA  . PHE A 272 ? 0.8039 0.6116 0.6449 -0.0008 -0.0289 -0.0335 336 PHE A CA  
2002  C C   . PHE A 272 ? 0.8435 0.6398 0.6716 0.0093  -0.0346 -0.0360 336 PHE A C   
2003  O O   . PHE A 272 ? 1.2174 0.9970 1.0247 0.0121  -0.0322 -0.0357 336 PHE A O   
2004  C CB  . PHE A 272 ? 0.8938 0.7172 0.7540 -0.0028 -0.0320 -0.0343 336 PHE A CB  
2005  C CG  . PHE A 272 ? 0.8177 0.6385 0.6731 -0.0021 -0.0322 -0.0354 336 PHE A CG  
2006  C CD1 . PHE A 272 ? 0.6526 0.4716 0.5078 0.0049  -0.0391 -0.0383 336 PHE A CD1 
2007  C CD2 . PHE A 272 ? 0.9253 0.7463 0.7765 -0.0080 -0.0255 -0.0343 336 PHE A CD2 
2008  C CE1 . PHE A 272 ? 0.6913 0.5071 0.5405 0.0065  -0.0394 -0.0393 336 PHE A CE1 
2009  C CE2 . PHE A 272 ? 0.7571 0.5767 0.6033 -0.0065 -0.0251 -0.0355 336 PHE A CE2 
2010  C CZ  . PHE A 272 ? 0.5617 0.3778 0.4059 0.0010  -0.0319 -0.0376 336 PHE A CZ  
2011  N N   . MET A 273 ? 0.6720 0.4778 0.5126 0.0148  -0.0419 -0.0387 337 MET A N   
2012  C CA  . MET A 273 ? 0.7395 0.5414 0.5752 0.0254  -0.0501 -0.0433 337 MET A CA  
2013  C C   . MET A 273 ? 0.8061 0.6277 0.6678 0.0248  -0.0563 -0.0465 337 MET A C   
2014  O O   . MET A 273 ? 1.2230 1.0577 1.1016 0.0186  -0.0538 -0.0448 337 MET A O   
2015  C CB  . MET A 273 ? 0.7587 0.5499 0.5796 0.0342  -0.0525 -0.0448 337 MET A CB  
2016  C CG  . MET A 273 ? 1.0199 0.7864 0.8110 0.0353  -0.0464 -0.0418 337 MET A CG  
2017  S SD  . MET A 273 ? 1.0612 0.8104 0.8298 0.0468  -0.0492 -0.0433 337 MET A SD  
2018  C CE  . MET A 273 ? 0.8659 0.6372 0.6590 0.0443  -0.0507 -0.0439 337 MET A CE  
2019  N N   . ILE A 274 ? 0.6692 0.4919 0.5331 0.0312  -0.0640 -0.0514 338 ILE A N   
2020  C CA  . ILE A 274 ? 0.6553 0.4952 0.5438 0.0296  -0.0698 -0.0553 338 ILE A CA  
2021  C C   . ILE A 274 ? 0.6739 0.5174 0.5643 0.0399  -0.0789 -0.0625 338 ILE A C   
2022  O O   . ILE A 274 ? 0.8101 0.6411 0.6823 0.0500  -0.0838 -0.0656 338 ILE A O   
2023  C CB  . ILE A 274 ? 0.5666 0.4064 0.4588 0.0272  -0.0720 -0.0562 338 ILE A CB  
2024  C CG1 . ILE A 274 ? 0.6274 0.4625 0.5130 0.0197  -0.0634 -0.0502 338 ILE A CG1 
2025  C CG2 . ILE A 274 ? 0.4690 0.3242 0.3864 0.0224  -0.0760 -0.0592 338 ILE A CG2 
2026  C CD1 . ILE A 274 ? 0.7220 0.5610 0.6160 0.0163  -0.0651 -0.0507 338 ILE A CD1 
2027  N N   . GLU A 275 ? 0.7164 0.5772 0.6281 0.0381  -0.0809 -0.0653 339 GLU A N   
2028  C CA  . GLU A 275 ? 0.8573 0.7270 0.7761 0.0477  -0.0903 -0.0739 339 GLU A CA  
2029  C C   . GLU A 275 ? 0.8227 0.7090 0.7679 0.0432  -0.0961 -0.0798 339 GLU A C   
2030  O O   . GLU A 275 ? 0.9246 0.8216 0.8890 0.0319  -0.0910 -0.0769 339 GLU A O   
2031  C CB  . GLU A 275 ? 0.8642 0.7421 0.7866 0.0503  -0.0881 -0.0740 339 GLU A CB  
2032  C CG  . GLU A 275 ? 1.2154 1.1121 1.1555 0.0575  -0.0964 -0.0835 339 GLU A CG  
2033  C CD  . GLU A 275 ? 1.3902 1.2775 1.3117 0.0741  -0.1065 -0.0909 339 GLU A CD  
2034  O OE1 . GLU A 275 ? 1.0268 0.8896 0.9175 0.0804  -0.1052 -0.0872 339 GLU A OE1 
2035  O OE2 . GLU A 275 ? 1.4935 1.3979 1.4308 0.0811  -0.1156 -0.1010 339 GLU A OE2 
2036  N N   . GLY A 276 ? 0.8222 0.7087 0.7667 0.0522  -0.1067 -0.0883 340 GLY A N   
2037  C CA  . GLY A 276 ? 1.0757 0.9766 1.0447 0.0480  -0.1135 -0.0954 340 GLY A CA  
2038  C C   . GLY A 276 ? 1.3015 1.2037 1.2679 0.0612  -0.1269 -0.1067 340 GLY A C   
2039  O O   . GLY A 276 ? 1.2410 1.1380 1.1913 0.0743  -0.1312 -0.1099 340 GLY A O   
2040  N N   . SER A 277 ? 1.0861 0.9940 1.0671 0.0585  -0.1340 -0.1130 341 SER A N   
2041  C CA  . SER A 277 ? 1.1821 1.0886 1.1585 0.0714  -0.1479 -0.1242 341 SER A CA  
2042  C C   . SER A 277 ? 1.1096 0.9898 1.0482 0.0837  -0.1486 -0.1203 341 SER A C   
2043  O O   . SER A 277 ? 1.2307 1.1033 1.1505 0.0986  -0.1542 -0.1244 341 SER A O   
2044  C CB  . SER A 277 ? 1.3016 1.2140 1.2969 0.0645  -0.1542 -0.1301 341 SER A CB  
2045  O OG  . SER A 277 ? 1.2879 1.2244 1.3180 0.0544  -0.1551 -0.1362 341 SER A OG  
2046  N N   . ASN A 278 ? 0.8812 0.7471 0.8083 0.0778  -0.1426 -0.1127 342 ASN A N   
2047  C CA  . ASN A 278 ? 0.8513 0.6937 0.7449 0.0836  -0.1366 -0.1052 342 ASN A CA  
2048  C C   . ASN A 278 ? 0.8472 0.6878 0.7367 0.0755  -0.1237 -0.0952 342 ASN A C   
2049  O O   . ASN A 278 ? 0.9564 0.8105 0.8671 0.0629  -0.1177 -0.0916 342 ASN A O   
2050  C CB  . ASN A 278 ? 0.8678 0.7000 0.7546 0.0793  -0.1344 -0.1015 342 ASN A CB  
2051  C CG  . ASN A 278 ? 0.9803 0.8087 0.8638 0.0891  -0.1468 -0.1105 342 ASN A CG  
2052  O OD1 . ASN A 278 ? 1.1404 0.9601 1.0064 0.1040  -0.1548 -0.1164 342 ASN A OD1 
2053  N ND2 . ASN A 278 ? 1.2193 1.0524 1.1175 0.0817  -0.1492 -0.1120 342 ASN A ND2 
2054  N N   . SER A 279 ? 0.8190 0.6412 0.6799 0.0827  -0.1193 -0.0909 343 SER A N   
2055  C CA  . SER A 279 ? 0.9413 0.7584 0.7947 0.0752  -0.1072 -0.0818 343 SER A CA  
2056  C C   . SER A 279 ? 0.6856 0.4825 0.5143 0.0730  -0.0983 -0.0742 343 SER A C   
2057  O O   . SER A 279 ? 0.8100 0.5920 0.6187 0.0814  -0.1011 -0.0758 343 SER A O   
2058  C CB  . SER A 279 ? 0.9014 0.7161 0.7455 0.0837  -0.1084 -0.0835 343 SER A CB  
2059  O OG  . SER A 279 ? 0.8149 0.6535 0.6870 0.0829  -0.1140 -0.0898 343 SER A OG  
2060  N N   . TRP A 280 ? 0.7997 0.5972 0.6304 0.0616  -0.0873 -0.0666 344 TRP A N   
2061  C CA  . TRP A 280 ? 0.7936 0.5764 0.6054 0.0574  -0.0779 -0.0603 344 TRP A CA  
2062  C C   . TRP A 280 ? 0.8450 0.6185 0.6440 0.0527  -0.0681 -0.0544 344 TRP A C   
2063  O O   . TRP A 280 ? 0.9954 0.7794 0.8082 0.0471  -0.0660 -0.0530 344 TRP A O   
2064  C CB  . TRP A 280 ? 0.6444 0.4385 0.4728 0.0472  -0.0746 -0.0580 344 TRP A CB  
2065  C CG  . TRP A 280 ? 0.5794 0.3792 0.4177 0.0513  -0.0840 -0.0636 344 TRP A CG  
2066  C CD1 . TRP A 280 ? 0.6459 0.4611 0.5084 0.0501  -0.0921 -0.0689 344 TRP A CD1 
2067  C CD2 . TRP A 280 ? 0.5874 0.3772 0.4120 0.0569  -0.0862 -0.0650 344 TRP A CD2 
2068  N NE1 . TRP A 280 ? 0.5965 0.4111 0.4612 0.0540  -0.0997 -0.0738 344 TRP A NE1 
2069  C CE2 . TRP A 280 ? 0.6872 0.4868 0.5292 0.0591  -0.0971 -0.0717 344 TRP A CE2 
2070  C CE3 . TRP A 280 ? 0.6267 0.4008 0.4269 0.0599  -0.0799 -0.0617 344 TRP A CE3 
2071  C CZ2 . TRP A 280 ? 0.6950 0.4878 0.5287 0.0654  -0.1025 -0.0750 344 TRP A CZ2 
2072  C CZ3 . TRP A 280 ? 0.7160 0.4843 0.5078 0.0667  -0.0846 -0.0648 344 TRP A CZ3 
2073  C CH2 . TRP A 280 ? 0.7884 0.5655 0.5962 0.0700  -0.0963 -0.0714 344 TRP A CH2 
2074  N N   . ILE A 281 ? 0.7599 0.5125 0.5317 0.0547  -0.0615 -0.0512 345 ILE A N   
2075  C CA  . ILE A 281 ? 0.7642 0.5075 0.5251 0.0461  -0.0500 -0.0452 345 ILE A CA  
2076  C C   . ILE A 281 ? 0.8620 0.6014 0.6166 0.0385  -0.0408 -0.0416 345 ILE A C   
2077  O O   . ILE A 281 ? 1.0431 0.7694 0.7799 0.0442  -0.0402 -0.0420 345 ILE A O   
2078  C CB  . ILE A 281 ? 0.7911 0.5105 0.5231 0.0536  -0.0482 -0.0443 345 ILE A CB  
2079  C CG1 . ILE A 281 ? 0.8686 0.5947 0.6080 0.0612  -0.0566 -0.0482 345 ILE A CG1 
2080  C CG2 . ILE A 281 ? 0.6572 0.3662 0.3787 0.0428  -0.0358 -0.0386 345 ILE A CG2 
2081  C CD1 . ILE A 281 ? 1.0869 0.7885 0.7959 0.0728  -0.0578 -0.0489 345 ILE A CD1 
2082  N N   . GLY A 282 ? 0.8526 0.6042 0.6219 0.0262  -0.0340 -0.0387 346 GLY A N   
2083  C CA  . GLY A 282 ? 0.8594 0.6111 0.6255 0.0182  -0.0247 -0.0363 346 GLY A CA  
2084  C C   . GLY A 282 ? 0.7981 0.5354 0.5478 0.0116  -0.0142 -0.0329 346 GLY A C   
2085  O O   . GLY A 282 ? 0.7455 0.4799 0.4952 0.0104  -0.0146 -0.0321 346 GLY A O   
2086  N N   . ARG A 283 ? 0.6807 0.4085 0.4162 0.0072  -0.0047 -0.0312 347 ARG A N   
2087  C CA  . ARG A 283 ? 0.7540 0.4692 0.4767 -0.0020 0.0064  -0.0285 347 ARG A CA  
2088  C C   . ARG A 283 ? 0.7644 0.4801 0.4827 -0.0108 0.0181  -0.0276 347 ARG A C   
2089  O O   . ARG A 283 ? 0.6943 0.4138 0.4115 -0.0066 0.0178  -0.0286 347 ARG A O   
2090  C CB  . ARG A 283 ? 0.7823 0.4684 0.4757 0.0055  0.0067  -0.0270 347 ARG A CB  
2091  C CG  . ARG A 283 ? 0.8916 0.5549 0.5567 0.0116  0.0114  -0.0258 347 ARG A CG  
2092  C CD  . ARG A 283 ? 1.0687 0.7034 0.7047 0.0227  0.0083  -0.0251 347 ARG A CD  
2093  N NE  . ARG A 283 ? 1.0448 0.6505 0.6464 0.0282  0.0154  -0.0229 347 ARG A NE  
2094  C CZ  . ARG A 283 ? 1.0846 0.6589 0.6529 0.0388  0.0147  -0.0219 347 ARG A CZ  
2095  N NH1 . ARG A 283 ? 1.3107 0.8799 0.8764 0.0452  0.0070  -0.0232 347 ARG A NH1 
2096  N NH2 . ARG A 283 ? 1.1407 0.6880 0.6767 0.0436  0.0221  -0.0194 347 ARG A NH2 
2097  N N   . ILE A 284 ? 0.7747 0.4873 0.4912 -0.0230 0.0283  -0.0265 348 ILE A N   
2098  C CA  . ILE A 284 ? 0.7671 0.4792 0.4786 -0.0330 0.0414  -0.0263 348 ILE A CA  
2099  C C   . ILE A 284 ? 0.8885 0.5692 0.5656 -0.0282 0.0484  -0.0233 348 ILE A C   
2100  O O   . ILE A 284 ? 1.1698 0.8246 0.8242 -0.0231 0.0476  -0.0211 348 ILE A O   
2101  C CB  . ILE A 284 ? 0.7557 0.4733 0.4759 -0.0480 0.0496  -0.0270 348 ILE A CB  
2102  C CG1 . ILE A 284 ? 0.9378 0.6823 0.6876 -0.0497 0.0410  -0.0297 348 ILE A CG1 
2103  C CG2 . ILE A 284 ? 0.7452 0.4677 0.4655 -0.0599 0.0636  -0.0283 348 ILE A CG2 
2104  C CD1 . ILE A 284 ? 0.7914 0.5546 0.5596 -0.0634 0.0472  -0.0330 348 ILE A CD1 
2105  N N   . ILE A 285 ? 0.9034 0.5856 0.5751 -0.0285 0.0554  -0.0233 349 ILE A N   
2106  C CA  . ILE A 285 ? 1.0538 0.7060 0.6913 -0.0211 0.0612  -0.0204 349 ILE A CA  
2107  C C   . ILE A 285 ? 0.9818 0.6067 0.5944 -0.0312 0.0763  -0.0171 349 ILE A C   
2108  O O   . ILE A 285 ? 0.9216 0.5142 0.5038 -0.0239 0.0764  -0.0141 349 ILE A O   
2109  C CB  . ILE A 285 ? 0.9719 0.6330 0.6092 -0.0166 0.0638  -0.0213 349 ILE A CB  
2110  C CG1 . ILE A 285 ? 0.9060 0.5855 0.5611 -0.0041 0.0473  -0.0245 349 ILE A CG1 
2111  C CG2 . ILE A 285 ? 0.8856 0.5130 0.4844 -0.0097 0.0721  -0.0178 349 ILE A CG2 
2112  C CD1 . ILE A 285 ? 0.8466 0.5321 0.4990 0.0035  0.0469  -0.0259 349 ILE A CD1 
2113  N N   . ASN A 286 ? 1.0611 0.6993 0.6869 -0.0479 0.0886  -0.0181 350 ASN A N   
2114  C CA  . ASN A 286 ? 1.1736 0.7879 0.7785 -0.0607 0.1050  -0.0156 350 ASN A CA  
2115  C C   . ASN A 286 ? 1.1764 0.7982 0.7973 -0.0748 0.1065  -0.0176 350 ASN A C   
2116  O O   . ASN A 286 ? 1.3486 0.9959 0.9944 -0.0888 0.1128  -0.0214 350 ASN A O   
2117  C CB  . ASN A 286 ? 1.2681 0.8910 0.8742 -0.0702 0.1204  -0.0162 350 ASN A CB  
2118  C CG  . ASN A 286 ? 1.4276 1.0355 1.0101 -0.0565 0.1214  -0.0136 350 ASN A CG  
2119  O OD1 . ASN A 286 ? 1.5070 1.1356 1.1036 -0.0462 0.1119  -0.0159 350 ASN A OD1 
2120  N ND2 . ASN A 286 ? 1.8237 1.3931 1.3676 -0.0555 0.1329  -0.0088 350 ASN A ND2 
2121  N N   . PRO A 287 ? 1.1485 0.7475 0.7538 -0.0704 0.1008  -0.0156 351 PRO A N   
2122  C CA  . PRO A 287 ? 1.2385 0.8441 0.8584 -0.0803 0.0989  -0.0177 351 PRO A CA  
2123  C C   . PRO A 287 ? 1.2585 0.8616 0.8802 -0.1013 0.1147  -0.0193 351 PRO A C   
2124  O O   . PRO A 287 ? 1.1364 0.7575 0.7806 -0.1115 0.1131  -0.0233 351 PRO A O   
2125  C CB  . PRO A 287 ? 1.1152 0.6875 0.7067 -0.0692 0.0924  -0.0145 351 PRO A CB  
2126  C CG  . PRO A 287 ? 1.1544 0.7158 0.7287 -0.0510 0.0854  -0.0124 351 PRO A CG  
2127  C CD  . PRO A 287 ? 1.0905 0.6527 0.6592 -0.0553 0.0969  -0.0115 351 PRO A CD  
2128  N N   . GLY A 288 ? 1.1513 0.7322 0.7494 -0.1076 0.1301  -0.0167 352 GLY A N   
2129  C CA  . GLY A 288 ? 1.2117 0.7944 0.8151 -0.1291 0.1467  -0.0191 352 GLY A CA  
2130  C C   . GLY A 288 ? 1.2248 0.8553 0.8698 -0.1381 0.1471  -0.0259 352 GLY A C   
2131  O O   . GLY A 288 ? 1.4810 1.1324 1.1509 -0.1494 0.1456  -0.0313 352 GLY A O   
2132  N N   . SER A 289 ? 1.2141 0.8614 0.8653 -0.1316 0.1482  -0.0260 353 SER A N   
2133  C CA  . SER A 289 ? 1.3536 1.0446 1.0403 -0.1388 0.1500  -0.0327 353 SER A CA  
2134  C C   . SER A 289 ? 1.1350 0.8591 0.8514 -0.1284 0.1320  -0.0363 353 SER A C   
2135  O O   . SER A 289 ? 1.1616 0.9218 0.9074 -0.1327 0.1311  -0.0425 353 SER A O   
2136  C CB  . SER A 289 ? 1.7162 1.4098 1.3946 -0.1366 0.1606  -0.0315 353 SER A CB  
2137  O OG  . SER A 289 ? 1.7552 1.4239 1.4059 -0.1185 0.1548  -0.0253 353 SER A OG  
2138  N N   . LYS A 290 ? 1.1835 0.8944 0.8911 -0.1145 0.1180  -0.0328 354 LYS A N   
2139  C CA  . LYS A 290 ? 1.1034 0.8398 0.8346 -0.1037 0.1014  -0.0349 354 LYS A CA  
2140  C C   . LYS A 290 ? 1.0176 0.7739 0.7586 -0.0937 0.0972  -0.0360 354 LYS A C   
2141  O O   . LYS A 290 ? 0.9973 0.7799 0.7617 -0.0884 0.0866  -0.0392 354 LYS A O   
2142  C CB  . LYS A 290 ? 1.2912 1.0542 1.0512 -0.1136 0.0984  -0.0408 354 LYS A CB  
2143  C CG  . LYS A 290 ? 1.2887 1.0329 1.0401 -0.1220 0.1003  -0.0404 354 LYS A CG  
2144  C CD  . LYS A 290 ? 1.3305 1.0601 1.0727 -0.1089 0.0872  -0.0364 354 LYS A CD  
2145  C CE  . LYS A 290 ? 1.6301 1.3368 1.3589 -0.1156 0.0893  -0.0356 354 LYS A CE  
2146  N NZ  . LYS A 290 ? 1.6140 1.3427 1.3669 -0.1269 0.0887  -0.0418 354 LYS A NZ  
2147  N N   . LYS A 291 ? 1.0236 0.7645 0.7438 -0.0905 0.1056  -0.0332 355 LYS A N   
2148  C CA  . LYS A 291 ? 1.0429 0.7994 0.7684 -0.0813 0.1033  -0.0343 355 LYS A CA  
2149  C C   . LYS A 291 ? 0.9730 0.7163 0.6860 -0.0631 0.0898  -0.0311 355 LYS A C   
2150  O O   . LYS A 291 ? 1.0228 0.7358 0.7101 -0.0567 0.0885  -0.0268 355 LYS A O   
2151  C CB  . LYS A 291 ? 1.3033 1.0502 1.0119 -0.0871 0.1204  -0.0332 355 LYS A CB  
2152  C CG  . LYS A 291 ? 1.5892 1.3619 1.3188 -0.1042 0.1335  -0.0389 355 LYS A CG  
2153  C CD  . LYS A 291 ? 1.7033 1.5045 1.4473 -0.0996 0.1351  -0.0430 355 LYS A CD  
2154  C CE  . LYS A 291 ? 1.5442 1.3685 1.3045 -0.1163 0.1512  -0.0489 355 LYS A CE  
2155  N NZ  . LYS A 291 ? 1.7240 1.5200 1.4604 -0.1295 0.1701  -0.0452 355 LYS A NZ  
2156  N N   . GLY A 292 ? 1.0073 0.7733 0.7382 -0.0543 0.0794  -0.0338 356 GLY A N   
2157  C CA  . GLY A 292 ? 0.9300 0.6862 0.6513 -0.0378 0.0669  -0.0321 356 GLY A CA  
2158  C C   . GLY A 292 ? 0.9279 0.6811 0.6554 -0.0315 0.0529  -0.0315 356 GLY A C   
2159  O O   . GLY A 292 ? 0.9335 0.6777 0.6591 -0.0371 0.0536  -0.0301 356 GLY A O   
2160  N N   . PHE A 293 ? 0.8311 0.5922 0.5666 -0.0201 0.0402  -0.0328 357 PHE A N   
2161  C CA  . PHE A 293 ? 0.8508 0.6108 0.5934 -0.0139 0.0273  -0.0327 357 PHE A CA  
2162  C C   . PHE A 293 ? 1.0178 0.7656 0.7479 0.0009  0.0175  -0.0330 357 PHE A C   
2163  O O   . PHE A 293 ? 0.9219 0.6771 0.6544 0.0070  0.0142  -0.0350 357 PHE A O   
2164  C CB  . PHE A 293 ? 0.7129 0.4996 0.4848 -0.0172 0.0206  -0.0354 357 PHE A CB  
2165  C CG  . PHE A 293 ? 0.7239 0.5111 0.5050 -0.0129 0.0095  -0.0351 357 PHE A CG  
2166  C CD1 . PHE A 293 ? 0.7792 0.5679 0.5647 -0.0028 -0.0019 -0.0364 357 PHE A CD1 
2167  C CD2 . PHE A 293 ? 0.8832 0.6694 0.6686 -0.0190 0.0107  -0.0339 357 PHE A CD2 
2168  C CE1 . PHE A 293 ? 0.7929 0.5841 0.5889 0.0001  -0.0111 -0.0367 357 PHE A CE1 
2169  C CE2 . PHE A 293 ? 0.9597 0.7477 0.7540 -0.0148 0.0013  -0.0337 357 PHE A CE2 
2170  C CZ  . PHE A 293 ? 0.7117 0.5032 0.5122 -0.0056 -0.0091 -0.0351 357 PHE A CZ  
2171  N N   . GLU A 294 ? 0.8932 0.6225 0.6094 0.0073  0.0123  -0.0318 358 GLU A N   
2172  C CA  . GLU A 294 ? 0.8284 0.5469 0.5338 0.0220  0.0014  -0.0335 358 GLU A CA  
2173  C C   . GLU A 294 ? 0.7865 0.5124 0.5074 0.0260  -0.0112 -0.0356 358 GLU A C   
2174  O O   . GLU A 294 ? 0.8317 0.5586 0.5583 0.0203  -0.0099 -0.0342 358 GLU A O   
2175  C CB  . GLU A 294 ? 1.1043 0.7918 0.7742 0.0293  0.0064  -0.0313 358 GLU A CB  
2176  C CG  . GLU A 294 ? 1.2423 0.9103 0.8965 0.0279  0.0093  -0.0288 358 GLU A CG  
2177  C CD  . GLU A 294 ? 1.5917 1.2246 1.2057 0.0356  0.0158  -0.0261 358 GLU A CD  
2178  O OE1 . GLU A 294 ? 1.6755 1.2988 1.2735 0.0468  0.0133  -0.0272 358 GLU A OE1 
2179  O OE2 . GLU A 294 ? 1.5530 1.1661 1.1492 0.0309  0.0235  -0.0231 358 GLU A OE2 
2180  N N   . ILE A 295 ? 0.6471 0.3788 0.3754 0.0355  -0.0230 -0.0393 359 ILE A N   
2181  C CA  . ILE A 295 ? 0.6588 0.3976 0.4015 0.0401  -0.0348 -0.0423 359 ILE A CA  
2182  C C   . ILE A 295 ? 0.7268 0.4526 0.4546 0.0550  -0.0449 -0.0463 359 ILE A C   
2183  O O   . ILE A 295 ? 0.8181 0.5371 0.5342 0.0620  -0.0466 -0.0479 359 ILE A O   
2184  C CB  . ILE A 295 ? 0.6322 0.3940 0.4039 0.0357  -0.0408 -0.0443 359 ILE A CB  
2185  C CG1 . ILE A 295 ? 0.7001 0.4703 0.4882 0.0371  -0.0497 -0.0468 359 ILE A CG1 
2186  C CG2 . ILE A 295 ? 0.6045 0.3675 0.3759 0.0429  -0.0475 -0.0478 359 ILE A CG2 
2187  C CD1 . ILE A 295 ? 0.8293 0.6198 0.6449 0.0299  -0.0524 -0.0473 359 ILE A CD1 
2188  N N   . TYR A 296 ? 0.8028 0.5265 0.5317 0.0607  -0.0523 -0.0488 360 TYR A N   
2189  C CA  . TYR A 296 ? 0.8904 0.5962 0.5969 0.0759  -0.0597 -0.0524 360 TYR A CA  
2190  C C   . TYR A 296 ? 0.8885 0.6082 0.6142 0.0820  -0.0734 -0.0589 360 TYR A C   
2191  O O   . TYR A 296 ? 0.9688 0.7006 0.7115 0.0763  -0.0736 -0.0586 360 TYR A O   
2192  C CB  . TYR A 296 ? 0.9219 0.6030 0.5986 0.0778  -0.0512 -0.0482 360 TYR A CB  
2193  C CG  . TYR A 296 ? 1.0316 0.6886 0.6776 0.0949  -0.0571 -0.0512 360 TYR A CG  
2194  C CD1 . TYR A 296 ? 1.2599 0.8992 0.8810 0.1030  -0.0552 -0.0509 360 TYR A CD1 
2195  C CD2 . TYR A 296 ? 1.3010 0.9527 0.9412 0.1042  -0.0647 -0.0545 360 TYR A CD2 
2196  C CE1 . TYR A 296 ? 1.5068 1.1218 1.0966 0.1207  -0.0612 -0.0539 360 TYR A CE1 
2197  C CE2 . TYR A 296 ? 1.7890 1.4178 1.3989 0.1220  -0.0713 -0.0580 360 TYR A CE2 
2198  C CZ  . TYR A 296 ? 1.6415 1.2511 1.2255 0.1304  -0.0696 -0.0576 360 TYR A CZ  
2199  O OH  . TYR A 296 ? 1.6297 1.2145 1.1805 0.1498  -0.0764 -0.0613 360 TYR A OH  
2200  N N   . LYS A 297 ? 0.8378 0.5568 0.5617 0.0935  -0.0846 -0.0654 361 LYS A N   
2201  C CA  . LYS A 297 ? 0.7885 0.5241 0.5347 0.0983  -0.0981 -0.0734 361 LYS A CA  
2202  C C   . LYS A 297 ? 0.8307 0.5567 0.5620 0.1127  -0.1061 -0.0786 361 LYS A C   
2203  O O   . LYS A 297 ? 0.9810 0.6826 0.6791 0.1232  -0.1042 -0.0774 361 LYS A O   
2204  C CB  . LYS A 297 ? 0.8714 0.6112 0.6237 0.1029  -0.1067 -0.0787 361 LYS A CB  
2205  C CG  . LYS A 297 ? 0.9179 0.6779 0.6992 0.1034  -0.1196 -0.0873 361 LYS A CG  
2206  C CD  . LYS A 297 ? 0.9028 0.6610 0.6837 0.1070  -0.1258 -0.0911 361 LYS A CD  
2207  C CE  . LYS A 297 ? 0.9569 0.7271 0.7566 0.1125  -0.1410 -0.1019 361 LYS A CE  
2208  N NZ  . LYS A 297 ? 1.0212 0.7880 0.8196 0.1145  -0.1460 -0.1047 361 LYS A NZ  
2209  N N   . PHE A 298 ? 0.7781 0.5234 0.5334 0.1135  -0.1148 -0.0848 362 PHE A N   
2210  C CA  . PHE A 298 ? 0.8097 0.5515 0.5558 0.1279  -0.1240 -0.0916 362 PHE A CA  
2211  C C   . PHE A 298 ? 0.9604 0.7279 0.7379 0.1303  -0.1374 -0.1023 362 PHE A C   
2212  O O   . PHE A 298 ? 1.1011 0.8912 0.9113 0.1169  -0.1359 -0.1021 362 PHE A O   
2213  C CB  . PHE A 298 ? 0.8592 0.6010 0.6043 0.1236  -0.1171 -0.0871 362 PHE A CB  
2214  C CG  . PHE A 298 ? 0.9185 0.6338 0.6319 0.1217  -0.1046 -0.0780 362 PHE A CG  
2215  C CD1 . PHE A 298 ? 1.0300 0.7179 0.7065 0.1363  -0.1057 -0.0785 362 PHE A CD1 
2216  C CD2 . PHE A 298 ? 0.8256 0.5427 0.5455 0.1053  -0.0918 -0.0696 362 PHE A CD2 
2217  C CE1 . PHE A 298 ? 0.9632 0.6243 0.6098 0.1328  -0.0929 -0.0700 362 PHE A CE1 
2218  C CE2 . PHE A 298 ? 0.9702 0.6642 0.6631 0.1017  -0.0798 -0.0621 362 PHE A CE2 
2219  C CZ  . PHE A 298 ? 0.9213 0.5866 0.5777 0.1146  -0.0798 -0.0620 362 PHE A CZ  
2220  N N   . LEU A 299 ? 0.9624 0.7266 0.7302 0.1475  -0.1503 -0.1121 363 LEU A N   
2221  C CA  . LEU A 299 ? 1.0844 0.8752 0.8839 0.1496  -0.1632 -0.1239 363 LEU A CA  
2222  C C   . LEU A 299 ? 1.2465 1.0533 1.0605 0.1492  -0.1630 -0.1260 363 LEU A C   
2223  O O   . LEU A 299 ? 1.3110 1.1026 1.0996 0.1603  -0.1621 -0.1248 363 LEU A O   
2224  C CB  . LEU A 299 ? 1.2884 1.0726 1.0743 0.1687  -0.1785 -0.1354 363 LEU A CB  
2225  C CG  . LEU A 299 ? 1.3259 1.1058 1.1122 0.1675  -0.1825 -0.1371 363 LEU A CG  
2226  C CD1 . LEU A 299 ? 1.2551 1.0581 1.0800 0.1476  -0.1793 -0.1359 363 LEU A CD1 
2227  C CD2 . LEU A 299 ? 0.9801 0.7284 0.7275 0.1711  -0.1729 -0.1273 363 LEU A CD2 
2228  N N   . GLY A 300 ? 1.0986 0.9342 0.9516 0.1364  -0.1630 -0.1286 364 GLY A N   
2229  C CA  . GLY A 300 ? 1.0818 0.9360 0.9522 0.1348  -0.1617 -0.1306 364 GLY A CA  
2230  C C   . GLY A 300 ? 1.1455 0.9891 1.0037 0.1267  -0.1475 -0.1182 364 GLY A C   
2231  O O   . GLY A 300 ? 1.4480 1.2751 1.2920 0.1182  -0.1374 -0.1081 364 GLY A O   
2232  N N   . THR A 301 ? 0.9869 0.8410 0.8508 0.1301  -0.1471 -0.1200 365 THR A N   
2233  C CA  . THR A 301 ? 0.9390 0.7891 0.7991 0.1210  -0.1345 -0.1099 365 THR A CA  
2234  C C   . THR A 301 ? 0.9424 0.7587 0.7621 0.1254  -0.1275 -0.1014 365 THR A C   
2235  O O   . THR A 301 ? 1.0651 0.8599 0.8558 0.1391  -0.1327 -0.1039 365 THR A O   
2236  C CB  . THR A 301 ? 1.0532 0.9240 0.9297 0.1249  -0.1365 -0.1149 365 THR A CB  
2237  O OG1 . THR A 301 ? 1.3024 1.1685 1.1749 0.1158  -0.1245 -0.1050 365 THR A OG1 
2238  C CG2 . THR A 301 ? 0.8485 0.7108 0.7028 0.1465  -0.1468 -0.1232 365 THR A CG2 
2239  N N   . LEU A 302 ? 0.9203 0.7315 0.7378 0.1136  -0.1154 -0.0916 366 LEU A N   
2240  C CA  . LEU A 302 ? 0.8967 0.6774 0.6787 0.1153  -0.1074 -0.0838 366 LEU A CA  
2241  C C   . LEU A 302 ? 1.0484 0.8225 0.8157 0.1259  -0.1090 -0.0855 366 LEU A C   
2242  O O   . LEU A 302 ? 1.1836 0.9301 0.9191 0.1289  -0.1033 -0.0802 366 LEU A O   
2243  C CB  . LEU A 302 ? 0.8879 0.6682 0.6766 0.0974  -0.0946 -0.0740 366 LEU A CB  
2244  C CG  . LEU A 302 ? 0.9866 0.7759 0.7920 0.0861  -0.0922 -0.0719 366 LEU A CG  
2245  C CD1 . LEU A 302 ? 1.1475 0.9645 0.9889 0.0747  -0.0911 -0.0721 366 LEU A CD1 
2246  C CD2 . LEU A 302 ? 1.0889 0.8603 0.8769 0.0772  -0.0811 -0.0634 366 LEU A CD2 
2247  N N   . PHE A 303 ? 1.2026 1.0020 0.9930 0.1315  -0.1165 -0.0934 367 PHE A N   
2248  C CA  . PHE A 303 ? 1.2004 0.9993 0.9823 0.1410  -0.1178 -0.0954 367 PHE A CA  
2249  C C   . PHE A 303 ? 1.4285 1.2238 1.1951 0.1633  -0.1310 -0.1061 367 PHE A C   
2250  O O   . PHE A 303 ? 1.5277 1.3233 1.2860 0.1744  -0.1340 -0.1095 367 PHE A O   
2251  C CB  . PHE A 303 ? 1.3457 1.1763 1.1637 0.1309  -0.1146 -0.0957 367 PHE A CB  
2252  C CG  . PHE A 303 ? 1.2737 1.1072 1.1050 0.1110  -0.1028 -0.0860 367 PHE A CG  
2253  C CD1 . PHE A 303 ? 1.1466 0.9548 0.9534 0.1050  -0.0933 -0.0766 367 PHE A CD1 
2254  C CD2 . PHE A 303 ? 1.1046 0.9648 0.9718 0.0986  -0.1014 -0.0868 367 PHE A CD2 
2255  C CE1 . PHE A 303 ? 1.0478 0.8597 0.8666 0.0882  -0.0836 -0.0690 367 PHE A CE1 
2256  C CE2 . PHE A 303 ? 1.3386 1.1995 1.2148 0.0823  -0.0912 -0.0781 367 PHE A CE2 
2257  C CZ  . PHE A 303 ? 1.0988 0.9367 0.9513 0.0778  -0.0828 -0.0696 367 PHE A CZ  
2258  N N   . SER A 304 ? 1.3681 1.1597 1.1300 0.1709  -0.1393 -0.1119 368 SER A N   
2259  C CA  . SER A 304 ? 1.4117 1.1927 1.1507 0.1940  -0.1520 -0.1216 368 SER A CA  
2260  C C   . SER A 304 ? 1.5302 1.2665 1.2203 0.2015  -0.1481 -0.1150 368 SER A C   
2261  O O   . SER A 304 ? 1.7524 1.4753 1.4362 0.1900  -0.1402 -0.1074 368 SER A O   
2262  C CB  . SER A 304 ? 1.4658 1.2708 1.2295 0.1995  -0.1650 -0.1337 368 SER A CB  
2263  O OG  . SER A 304 ? 1.6434 1.4426 1.3878 0.2239  -0.1789 -0.1451 368 SER A OG  
2264  N N   . VAL A 305 ? 1.4989 1.2117 1.1536 0.2210  -0.1533 -0.1182 369 VAL A N   
2265  C CA  . VAL A 305 ? 1.2846 0.9514 0.8886 0.2299  -0.1495 -0.1125 369 VAL A CA  
2266  C C   . VAL A 305 ? 1.3742 1.0354 0.9687 0.2420  -0.1593 -0.1192 369 VAL A C   
2267  O O   . VAL A 305 ? 1.3714 0.9971 0.9280 0.2469  -0.1551 -0.1141 369 VAL A O   
2268  C CB  . VAL A 305 ? 1.2695 0.9112 0.8369 0.2482  -0.1523 -0.1141 369 VAL A CB  
2269  C CG1 . VAL A 305 ? 1.4436 1.1030 1.0158 0.2720  -0.1704 -0.1294 369 VAL A CG1 
2270  C CG2 . VAL A 305 ? 1.2917 0.8809 0.8039 0.2540  -0.1448 -0.1060 369 VAL A CG2 
2271  N N   . GLN A 306 ? 1.4667 1.1637 1.0967 0.2460  -0.1719 -0.1310 370 GLN A N   
2272  C CA  . GLN A 306 ? 1.4535 1.1522 1.0813 0.2586  -0.1844 -0.1404 370 GLN A CA  
2273  C C   . GLN A 306 ? 1.2295 0.9233 0.8620 0.2448  -0.1781 -0.1342 370 GLN A C   
2274  O O   . GLN A 306 ? 1.3632 1.0436 0.9779 0.2567  -0.1855 -0.1387 370 GLN A O   
2275  C CB  . GLN A 306 ? 1.9014 1.6450 1.5735 0.2626  -0.1987 -0.1554 370 GLN A CB  
2276  C CG  . GLN A 306 ? 1.9639 1.7151 1.6292 0.2846  -0.2109 -0.1670 370 GLN A CG  
2277  C CD  . GLN A 306 ? 1.8624 1.5916 1.4918 0.3121  -0.2253 -0.1769 370 GLN A CD  
2278  O OE1 . GLN A 306 ? 1.8751 1.5608 1.4536 0.3242  -0.2217 -0.1706 370 GLN A OE1 
2279  N NE2 . GLN A 306 ? 1.8540 1.6125 1.5092 0.3221  -0.2416 -0.1929 370 GLN A NE2 
2280  N N   . THR A 307 ? 1.2482 0.9530 0.9040 0.2210  -0.1651 -0.1244 371 THR A N   
2281  C CA  . THR A 307 ? 1.2360 0.9503 0.9114 0.2066  -0.1618 -0.1216 371 THR A CA  
2282  C C   . THR A 307 ? 1.1729 0.8535 0.8140 0.2041  -0.1516 -0.1118 371 THR A C   
2283  O O   . THR A 307 ? 1.1989 0.8511 0.8085 0.2034  -0.1409 -0.1031 371 THR A O   
2284  C CB  . THR A 307 ? 1.1881 0.9327 0.9064 0.1840  -0.1543 -0.1174 371 THR A CB  
2285  O OG1 . THR A 307 ? 1.4517 1.1854 1.1602 0.1744  -0.1412 -0.1071 371 THR A OG1 
2286  C CG2 . THR A 307 ? 1.2407 1.0225 0.9976 0.1858  -0.1651 -0.1289 371 THR A CG2 
2287  N N   . VAL A 308 ? 1.2549 0.9400 0.9041 0.2019  -0.1548 -0.1138 372 VAL A N   
2288  C CA  . VAL A 308 ? 1.1468 0.8014 0.7607 0.2080  -0.1507 -0.1094 372 VAL A CA  
2289  C C   . VAL A 308 ? 1.2336 0.8913 0.8593 0.1884  -0.1381 -0.1002 372 VAL A C   
2290  O O   . VAL A 308 ? 1.0924 0.7776 0.7548 0.1766  -0.1405 -0.1024 372 VAL A O   
2291  C CB  . VAL A 308 ? 1.2253 0.8827 0.8369 0.2255  -0.1673 -0.1214 372 VAL A CB  
2292  C CG1 . VAL A 308 ? 1.4249 1.0486 0.9957 0.2349  -0.1636 -0.1174 372 VAL A CG1 
2293  C CG2 . VAL A 308 ? 1.3305 0.9922 0.9371 0.2458  -0.1824 -0.1334 372 VAL A CG2 
2294  N N   . GLY A 309 ? 1.3598 0.9888 0.9536 0.1851  -0.1245 -0.0903 373 GLY A N   
2295  C CA  . GLY A 309 ? 1.3223 0.9527 0.9226 0.1699  -0.1133 -0.0830 373 GLY A CA  
2296  C C   . GLY A 309 ? 1.1768 0.8127 0.7816 0.1774  -0.1229 -0.0892 373 GLY A C   
2297  O O   . GLY A 309 ? 1.3701 0.9946 0.9560 0.1963  -0.1345 -0.0968 373 GLY A O   
2298  N N   . ASN A 310 ? 1.0928 0.7454 0.7214 0.1637  -0.1189 -0.0868 374 ASN A N   
2299  C CA  . ASN A 310 ? 1.0950 0.7539 0.7302 0.1702  -0.1290 -0.0933 374 ASN A CA  
2300  C C   . ASN A 310 ? 1.0966 0.7488 0.7244 0.1616  -0.1176 -0.0860 374 ASN A C   
2301  O O   . ASN A 310 ? 1.7230 1.3551 1.3225 0.1725  -0.1171 -0.0859 374 ASN A O   
2302  C CB  . ASN A 310 ? 1.1522 0.8438 0.8309 0.1640  -0.1405 -0.1013 374 ASN A CB  
2303  C CG  . ASN A 310 ? 1.1431 0.8401 0.8294 0.1686  -0.1504 -0.1079 374 ASN A CG  
2304  O OD1 . ASN A 310 ? 1.2584 0.9640 0.9595 0.1570  -0.1457 -0.1044 374 ASN A OD1 
2305  N ND2 . ASN A 310 ? 1.3446 1.0350 1.0187 0.1866  -0.1646 -0.1178 374 ASN A ND2 
2306  N N   . ARG A 311 ? 1.1150 0.7845 0.7677 0.1431  -0.1084 -0.0804 375 ARG A N   
2307  C CA  . ARG A 311 ? 1.0678 0.7367 0.7189 0.1351  -0.0989 -0.0750 375 ARG A CA  
2308  C C   . ARG A 311 ? 1.0828 0.7552 0.7390 0.1180  -0.0824 -0.0658 375 ARG A C   
2309  O O   . ARG A 311 ? 1.0462 0.7371 0.7288 0.1061  -0.0810 -0.0646 375 ARG A O   
2310  C CB  . ARG A 311 ? 0.9061 0.5965 0.5864 0.1313  -0.1079 -0.0802 375 ARG A CB  
2311  C CG  . ARG A 311 ? 0.8555 0.5474 0.5353 0.1242  -0.0990 -0.0755 375 ARG A CG  
2312  C CD  . ARG A 311 ? 1.0043 0.6763 0.6538 0.1382  -0.1002 -0.0769 375 ARG A CD  
2313  N NE  . ARG A 311 ? 1.1964 0.8711 0.8449 0.1338  -0.0928 -0.0736 375 ARG A NE  
2314  C CZ  . ARG A 311 ? 1.2559 0.9408 0.9180 0.1357  -0.1016 -0.0784 375 ARG A CZ  
2315  N NH1 . ARG A 311 ? 1.4460 1.1396 1.1256 0.1400  -0.1174 -0.0867 375 ARG A NH1 
2316  N NH2 . ARG A 311 ? 1.1359 0.8226 0.7944 0.1332  -0.0944 -0.0755 375 ARG A NH2 
2317  N N   . ASN A 312 ? 0.9659 0.6211 0.5972 0.1169  -0.0697 -0.0599 376 ASN A N   
2318  C CA  . ASN A 312 ? 0.9841 0.6434 0.6204 0.1006  -0.0540 -0.0525 376 ASN A CA  
2319  C C   . ASN A 312 ? 1.0401 0.7136 0.6893 0.0925  -0.0482 -0.0510 376 ASN A C   
2320  O O   . ASN A 312 ? 1.1561 0.8188 0.7864 0.0992  -0.0450 -0.0507 376 ASN A O   
2321  C CB  . ASN A 312 ? 1.0653 0.6959 0.6658 0.1024  -0.0416 -0.0470 376 ASN A CB  
2322  C CG  . ASN A 312 ? 1.2067 0.8402 0.8098 0.0857  -0.0245 -0.0405 376 ASN A CG  
2323  O OD1 . ASN A 312 ? 1.5622 1.1925 1.1558 0.0830  -0.0148 -0.0380 376 ASN A OD1 
2324  N ND2 . ASN A 312 ? 1.0639 0.7048 0.6808 0.0745  -0.0207 -0.0382 376 ASN A ND2 
2325  N N   . TYR A 313 ? 0.8120 0.5091 0.4917 0.0796  -0.0471 -0.0502 377 TYR A N   
2326  C CA  . TYR A 313 ? 0.8200 0.5319 0.5123 0.0715  -0.0407 -0.0488 377 TYR A CA  
2327  C C   . TYR A 313 ? 0.8623 0.5759 0.5528 0.0583  -0.0244 -0.0433 377 TYR A C   
2328  O O   . TYR A 313 ? 1.0658 0.7880 0.7705 0.0483  -0.0215 -0.0414 377 TYR A O   
2329  C CB  . TYR A 313 ? 0.6809 0.4162 0.4057 0.0661  -0.0493 -0.0518 377 TYR A CB  
2330  C CG  . TYR A 313 ? 0.8084 0.5453 0.5395 0.0764  -0.0647 -0.0581 377 TYR A CG  
2331  C CD1 . TYR A 313 ? 0.7352 0.4766 0.4796 0.0783  -0.0751 -0.0620 377 TYR A CD1 
2332  C CD2 . TYR A 313 ? 0.9016 0.6360 0.6258 0.0841  -0.0688 -0.0611 377 TYR A CD2 
2333  C CE1 . TYR A 313 ? 0.8002 0.5446 0.5530 0.0862  -0.0892 -0.0690 377 TYR A CE1 
2334  C CE2 . TYR A 313 ? 0.9848 0.7197 0.7149 0.0930  -0.0836 -0.0678 377 TYR A CE2 
2335  C CZ  . TYR A 313 ? 0.9200 0.6603 0.6653 0.0934  -0.0938 -0.0720 377 TYR A CZ  
2336  O OH  . TYR A 313 ? 0.8673 0.6094 0.6205 0.1009  -0.1083 -0.0798 377 TYR A OH  
2337  N N   . GLN A 314 ? 0.8688 0.5752 0.5428 0.0578  -0.0137 -0.0411 378 GLN A N   
2338  C CA  . GLN A 314 ? 0.9107 0.6234 0.5880 0.0439  0.0016  -0.0374 378 GLN A CA  
2339  C C   . GLN A 314 ? 0.8641 0.6035 0.5666 0.0377  0.0015  -0.0395 378 GLN A C   
2340  O O   . GLN A 314 ? 1.0679 0.8112 0.7657 0.0411  0.0050  -0.0405 378 GLN A O   
2341  C CB  . GLN A 314 ? 1.0636 0.7562 0.7111 0.0449  0.0154  -0.0342 378 GLN A CB  
2342  C CG  . GLN A 314 ? 1.1564 0.8184 0.7742 0.0507  0.0173  -0.0315 378 GLN A CG  
2343  C CD  . GLN A 314 ? 1.3726 1.0158 0.9652 0.0444  0.0356  -0.0269 378 GLN A CD  
2344  O OE1 . GLN A 314 ? 1.7772 1.4365 1.3800 0.0345  0.0471  -0.0265 378 GLN A OE1 
2345  N NE2 . GLN A 314 ? 1.5289 1.1431 1.0927 0.0484  0.0397  -0.0239 378 GLN A NE2 
2346  N N   . LEU A 315 ? 0.8121 0.5693 0.5399 0.0298  -0.0022 -0.0402 379 LEU A N   
2347  C CA  . LEU A 315 ? 0.7432 0.5239 0.4933 0.0265  -0.0046 -0.0426 379 LEU A CA  
2348  C C   . LEU A 315 ? 0.8140 0.6076 0.5682 0.0174  0.0083  -0.0424 379 LEU A C   
2349  O O   . LEU A 315 ? 0.9377 0.7456 0.6994 0.0195  0.0080  -0.0450 379 LEU A O   
2350  C CB  . LEU A 315 ? 0.7801 0.5736 0.5534 0.0220  -0.0126 -0.0434 379 LEU A CB  
2351  C CG  . LEU A 315 ? 0.7787 0.5659 0.5551 0.0298  -0.0260 -0.0451 379 LEU A CG  
2352  C CD1 . LEU A 315 ? 0.8360 0.6368 0.6354 0.0234  -0.0306 -0.0451 379 LEU A CD1 
2353  C CD2 . LEU A 315 ? 0.6605 0.4468 0.4345 0.0398  -0.0347 -0.0486 379 LEU A CD2 
2354  N N   . LEU A 316 ? 0.8434 0.6328 0.5933 0.0073  0.0193  -0.0399 380 LEU A N   
2355  C CA  . LEU A 316 ? 0.9154 0.7200 0.6729 -0.0035 0.0319  -0.0409 380 LEU A CA  
2356  C C   . LEU A 316 ? 0.9783 0.7645 0.7136 -0.0086 0.0460  -0.0380 380 LEU A C   
2357  O O   . LEU A 316 ? 1.0714 0.8359 0.7917 -0.0089 0.0465  -0.0347 380 LEU A O   
2358  C CB  . LEU A 316 ? 0.9116 0.7338 0.6918 -0.0141 0.0317  -0.0422 380 LEU A CB  
2359  C CG  . LEU A 316 ? 0.7638 0.6036 0.5659 -0.0109 0.0196  -0.0447 380 LEU A CG  
2360  C CD1 . LEU A 316 ? 0.9126 0.7709 0.7328 -0.0208 0.0230  -0.0467 380 LEU A CD1 
2361  C CD2 . LEU A 316 ? 0.8894 0.7396 0.6951 -0.0022 0.0143  -0.0477 380 LEU A CD2 
2362  N N   . SER A 317 ? 0.9124 0.7068 0.6450 -0.0125 0.0579  -0.0392 381 SER A N   
2363  C CA  . SER A 317 ? 0.9101 0.6860 0.6204 -0.0188 0.0740  -0.0361 381 SER A CA  
2364  C C   . SER A 317 ? 1.0413 0.8363 0.7659 -0.0347 0.0883  -0.0387 381 SER A C   
2365  O O   . SER A 317 ? 1.4260 1.2093 1.1435 -0.0466 0.0991  -0.0368 381 SER A O   
2366  C CB  . SER A 317 ? 0.9631 0.7254 0.6503 -0.0076 0.0771  -0.0349 381 SER A CB  
2367  O OG  . SER A 317 ? 1.5385 1.2869 1.2158 0.0079  0.0619  -0.0344 381 SER A OG  
2368  N N   . ASN A 318 ? 1.1327 0.9574 0.8776 -0.0346 0.0879  -0.0438 382 ASN A N   
2369  C CA  . ASN A 318 ? 1.4643 1.3120 1.2252 -0.0486 0.1012  -0.0481 382 ASN A CA  
2370  C C   . ASN A 318 ? 1.2007 1.0679 0.9873 -0.0602 0.0986  -0.0519 382 ASN A C   
2371  O O   . ASN A 318 ? 1.6068 1.4949 1.4088 -0.0723 0.1087  -0.0569 382 ASN A O   
2372  C CB  . ASN A 318 ? 1.6185 1.4906 1.3883 -0.0427 0.1033  -0.0528 382 ASN A CB  
2373  C CG  . ASN A 318 ? 2.3145 2.1796 2.0670 -0.0467 0.1216  -0.0516 382 ASN A CG  
2374  O OD1 . ASN A 318 ? 2.9616 2.8076 2.6996 -0.0578 0.1350  -0.0481 382 ASN A OD1 
2375  N ND2 . ASN A 318 ? 2.3283 2.2081 2.0813 -0.0378 0.1228  -0.0546 382 ASN A ND2 
2376  N N   . SER A 319 ? 0.8931 0.7538 0.6841 -0.0565 0.0856  -0.0502 383 SER A N   
2377  C CA  . SER A 319 ? 0.9606 0.8427 0.7765 -0.0632 0.0803  -0.0544 383 SER A CA  
2378  C C   . SER A 319 ? 0.9822 0.8484 0.7942 -0.0726 0.0820  -0.0518 383 SER A C   
2379  O O   . SER A 319 ? 1.2342 1.0740 1.0282 -0.0677 0.0781  -0.0464 383 SER A O   
2380  C CB  . SER A 319 ? 0.7733 0.6666 0.6017 -0.0511 0.0637  -0.0556 383 SER A CB  
2381  O OG  . SER A 319 ? 0.9854 0.8757 0.8045 -0.0386 0.0596  -0.0549 383 SER A OG  
2382  N N   . THR A 320 ? 0.9066 0.7894 0.7355 -0.0853 0.0872  -0.0566 384 THR A N   
2383  C CA  . THR A 320 ? 0.9389 0.8083 0.7656 -0.0939 0.0876  -0.0551 384 THR A CA  
2384  C C   . THR A 320 ? 0.8908 0.7608 0.7253 -0.0859 0.0723  -0.0538 384 THR A C   
2385  O O   . THR A 320 ? 0.9415 0.8357 0.7967 -0.0830 0.0644  -0.0582 384 THR A O   
2386  C CB  . THR A 320 ? 0.9535 0.8404 0.7961 -0.1105 0.0975  -0.0617 384 THR A CB  
2387  O OG1 . THR A 320 ? 1.0538 0.9370 0.8872 -0.1195 0.1138  -0.0622 384 THR A OG1 
2388  C CG2 . THR A 320 ? 0.8940 0.7639 0.7319 -0.1187 0.0972  -0.0602 384 THR A CG2 
2389  N N   . ILE A 321 ? 0.7250 0.5679 0.5419 -0.0819 0.0686  -0.0479 385 ILE A N   
2390  C CA  . ILE A 321 ? 0.6884 0.5297 0.5102 -0.0729 0.0549  -0.0459 385 ILE A CA  
2391  C C   . ILE A 321 ? 0.7174 0.5526 0.5412 -0.0791 0.0537  -0.0456 385 ILE A C   
2392  O O   . ILE A 321 ? 0.8833 0.7059 0.6976 -0.0892 0.0627  -0.0456 385 ILE A O   
2393  C CB  . ILE A 321 ? 0.7168 0.5358 0.5199 -0.0608 0.0488  -0.0406 385 ILE A CB  
2394  C CG1 . ILE A 321 ? 0.8426 0.6625 0.6386 -0.0540 0.0506  -0.0407 385 ILE A CG1 
2395  C CG2 . ILE A 321 ? 0.5598 0.3841 0.3733 -0.0519 0.0352  -0.0398 385 ILE A CG2 
2396  C CD1 . ILE A 321 ? 0.6975 0.5411 0.5120 -0.0473 0.0423  -0.0440 385 ILE A CD1 
2397  N N   . GLY A 322 ? 0.8383 0.6817 0.6737 -0.0730 0.0428  -0.0455 386 GLY A N   
2398  C CA  . GLY A 322 ? 0.6787 0.5189 0.5174 -0.0763 0.0397  -0.0454 386 GLY A CA  
2399  C C   . GLY A 322 ? 0.8539 0.6897 0.6932 -0.0655 0.0288  -0.0419 386 GLY A C   
2400  O O   . GLY A 322 ? 0.9088 0.7272 0.7338 -0.0584 0.0262  -0.0381 386 GLY A O   
2401  N N   . ARG A 323 ? 0.8884 0.7398 0.7437 -0.0639 0.0225  -0.0436 387 ARG A N   
2402  C CA  . ARG A 323 ? 0.7426 0.5901 0.5994 -0.0553 0.0137  -0.0403 387 ARG A CA  
2403  C C   . ARG A 323 ? 0.5556 0.4067 0.4154 -0.0467 0.0079  -0.0390 387 ARG A C   
2404  O O   . ARG A 323 ? 0.5872 0.4484 0.4515 -0.0461 0.0089  -0.0412 387 ARG A O   
2405  C CB  . ARG A 323 ? 0.6330 0.4932 0.5032 -0.0558 0.0097  -0.0418 387 ARG A CB  
2406  C CG  . ARG A 323 ? 0.6142 0.4756 0.4849 -0.0647 0.0146  -0.0451 387 ARG A CG  
2407  C CD  . ARG A 323 ? 0.6757 0.5548 0.5611 -0.0643 0.0106  -0.0486 387 ARG A CD  
2408  N NE  . ARG A 323 ? 0.8630 0.7418 0.7512 -0.0558 0.0038  -0.0450 387 ARG A NE  
2409  C CZ  . ARG A 323 ? 0.7561 0.6463 0.6536 -0.0497 -0.0009 -0.0449 387 ARG A CZ  
2410  N NH1 . ARG A 323 ? 0.5825 0.4859 0.4867 -0.0497 -0.0006 -0.0486 387 ARG A NH1 
2411  N NH2 . ARG A 323 ? 0.7292 0.6168 0.6283 -0.0436 -0.0054 -0.0412 387 ARG A NH2 
2412  N N   . SER A 324 ? 0.4712 0.3144 0.3288 -0.0400 0.0018  -0.0361 388 SER A N   
2413  C CA  . SER A 324 ? 0.6065 0.4511 0.4672 -0.0321 -0.0047 -0.0354 388 SER A CA  
2414  C C   . SER A 324 ? 0.6091 0.4559 0.4783 -0.0284 -0.0108 -0.0338 388 SER A C   
2415  O O   . SER A 324 ? 0.7873 0.6279 0.6527 -0.0291 -0.0102 -0.0325 388 SER A O   
2416  C CB  . SER A 324 ? 0.5947 0.4231 0.4391 -0.0273 -0.0046 -0.0345 388 SER A CB  
2417  O OG  . SER A 324 ? 0.6681 0.4788 0.4964 -0.0280 -0.0014 -0.0328 388 SER A OG  
2418  N N   . GLY A 325 ? 0.5329 0.3879 0.4130 -0.0248 -0.0161 -0.0339 389 GLY A N   
2419  C CA  . GLY A 325 ? 0.5629 0.4201 0.4514 -0.0226 -0.0202 -0.0323 389 GLY A CA  
2420  C C   . GLY A 325 ? 0.6160 0.4762 0.5125 -0.0185 -0.0260 -0.0328 389 GLY A C   
2421  O O   . GLY A 325 ? 0.5823 0.4437 0.4778 -0.0170 -0.0273 -0.0343 389 GLY A O   
2422  N N   . LEU A 326 ? 0.4730 0.3346 0.3774 -0.0169 -0.0292 -0.0318 390 LEU A N   
2423  C CA  . LEU A 326 ? 0.5242 0.3883 0.4379 -0.0147 -0.0344 -0.0327 390 LEU A CA  
2424  C C   . LEU A 326 ? 0.5783 0.4485 0.5014 -0.0171 -0.0336 -0.0310 390 LEU A C   
2425  O O   . LEU A 326 ? 0.7791 0.6525 0.7022 -0.0193 -0.0297 -0.0293 390 LEU A O   
2426  C CB  . LEU A 326 ? 0.4807 0.3442 0.3993 -0.0122 -0.0380 -0.0335 390 LEU A CB  
2427  C CG  . LEU A 326 ? 0.4611 0.3164 0.3681 -0.0073 -0.0402 -0.0356 390 LEU A CG  
2428  C CD1 . LEU A 326 ? 0.5654 0.4232 0.4771 -0.0050 -0.0418 -0.0362 390 LEU A CD1 
2429  C CD2 . LEU A 326 ? 0.6223 0.4753 0.5296 -0.0033 -0.0462 -0.0389 390 LEU A CD2 
2430  N N   . TYR A 327 ? 0.6434 0.5133 0.5727 -0.0163 -0.0374 -0.0319 391 TYR A N   
2431  C CA  . TYR A 327 ? 0.6517 0.5229 0.5880 -0.0182 -0.0367 -0.0300 391 TYR A CA  
2432  C C   . TYR A 327 ? 0.6353 0.5033 0.5787 -0.0184 -0.0413 -0.0316 391 TYR A C   
2433  O O   . TYR A 327 ? 0.8726 0.7374 0.8132 -0.0157 -0.0460 -0.0347 391 TYR A O   
2434  C CB  . TYR A 327 ? 0.4807 0.3527 0.4112 -0.0173 -0.0349 -0.0296 391 TYR A CB  
2435  C CG  . TYR A 327 ? 0.5497 0.4200 0.4751 -0.0142 -0.0381 -0.0324 391 TYR A CG  
2436  C CD1 . TYR A 327 ? 0.6033 0.4684 0.5294 -0.0125 -0.0415 -0.0327 391 TYR A CD1 
2437  C CD2 . TYR A 327 ? 0.7471 0.6200 0.6658 -0.0128 -0.0372 -0.0346 391 TYR A CD2 
2438  C CE1 . TYR A 327 ? 0.6134 0.4767 0.5335 -0.0083 -0.0449 -0.0355 391 TYR A CE1 
2439  C CE2 . TYR A 327 ? 0.8342 0.7067 0.7480 -0.0092 -0.0396 -0.0372 391 TYR A CE2 
2440  C CZ  . TYR A 327 ? 0.7225 0.5907 0.6370 -0.0063 -0.0439 -0.0378 391 TYR A CZ  
2441  O OH  . TYR A 327 ? 0.7168 0.5843 0.6252 -0.0014 -0.0467 -0.0408 391 TYR A OH  
2442  N N   . GLN A 328 ? 0.6871 0.5552 0.6391 -0.0218 -0.0396 -0.0297 392 GLN A N   
2443  C CA  . GLN A 328 ? 0.6572 0.5213 0.6170 -0.0238 -0.0433 -0.0316 392 GLN A CA  
2444  C C   . GLN A 328 ? 0.7174 0.5735 0.6731 -0.0249 -0.0415 -0.0291 392 GLN A C   
2445  O O   . GLN A 328 ? 1.3877 1.2427 1.3427 -0.0268 -0.0360 -0.0252 392 GLN A O   
2446  C CB  . GLN A 328 ? 0.5616 0.4315 0.5358 -0.0280 -0.0422 -0.0321 392 GLN A CB  
2447  C CG  . GLN A 328 ? 0.6170 0.4944 0.5930 -0.0253 -0.0435 -0.0343 392 GLN A CG  
2448  C CD  . GLN A 328 ? 0.7518 0.6380 0.7430 -0.0283 -0.0427 -0.0359 392 GLN A CD  
2449  O OE1 . GLN A 328 ? 0.9656 0.8563 0.9601 -0.0304 -0.0365 -0.0325 392 GLN A OE1 
2450  N NE2 . GLN A 328 ? 0.9214 0.8113 0.9224 -0.0279 -0.0491 -0.0417 392 GLN A NE2 
2451  N N   . PRO A 329 ? 0.5592 0.4083 0.5096 -0.0223 -0.0464 -0.0315 393 PRO A N   
2452  C CA  . PRO A 329 ? 0.6229 0.4609 0.5675 -0.0224 -0.0459 -0.0298 393 PRO A CA  
2453  C C   . PRO A 329 ? 0.7335 0.5653 0.6884 -0.0294 -0.0448 -0.0294 393 PRO A C   
2454  O O   . PRO A 329 ? 0.8275 0.6650 0.7949 -0.0328 -0.0476 -0.0327 393 PRO A O   
2455  C CB  . PRO A 329 ? 0.6256 0.4589 0.5616 -0.0168 -0.0522 -0.0335 393 PRO A CB  
2456  C CG  . PRO A 329 ? 0.6168 0.4562 0.5583 -0.0161 -0.0566 -0.0374 393 PRO A CG  
2457  C CD  . PRO A 329 ? 0.6273 0.4767 0.5740 -0.0181 -0.0524 -0.0358 393 PRO A CD  
2458  N N   . ALA A 330 ? 0.9795 0.7999 0.9290 -0.0316 -0.0405 -0.0256 394 ALA A N   
2459  C CA  . ALA A 330 ? 1.1400 0.9534 1.0992 -0.0401 -0.0374 -0.0248 394 ALA A CA  
2460  C C   . ALA A 330 ? 1.4814 1.2750 1.4311 -0.0406 -0.0397 -0.0251 394 ALA A C   
2461  O O   . ALA A 330 ? 1.8404 1.6220 1.7731 -0.0352 -0.0384 -0.0221 394 ALA A O   
2462  C CB  . ALA A 330 ? 1.1199 0.9345 1.0807 -0.0438 -0.0280 -0.0194 394 ALA A CB  
2463  N N   . TYR A 331 ? 1.5509 1.3409 1.5109 -0.0463 -0.0440 -0.0295 395 TYR A N   
2464  C CA  . TYR A 331 ? 1.8923 1.6608 1.8445 -0.0490 -0.0458 -0.0300 395 TYR A CA  
2465  C C   . TYR A 331 ? 2.1218 1.8898 2.0927 -0.0613 -0.0442 -0.0329 395 TYR A C   
2466  O O   . TYR A 331 ? 2.2267 2.0135 2.2167 -0.0661 -0.0426 -0.0350 395 TYR A O   
2467  C CB  . TYR A 331 ? 1.9110 1.6733 1.8532 -0.0410 -0.0561 -0.0349 395 TYR A CB  
2468  C CG  . TYR A 331 ? 1.9453 1.7190 1.8784 -0.0301 -0.0591 -0.0353 395 TYR A CG  
2469  C CD1 . TYR A 331 ? 2.0799 1.8485 1.9959 -0.0224 -0.0568 -0.0319 395 TYR A CD1 
2470  C CD2 . TYR A 331 ? 1.5931 1.3824 1.5344 -0.0274 -0.0641 -0.0396 395 TYR A CD2 
2471  C CE1 . TYR A 331 ? 2.1310 1.9123 2.0413 -0.0139 -0.0589 -0.0331 395 TYR A CE1 
2472  C CE2 . TYR A 331 ? 1.3096 1.1082 1.2424 -0.0189 -0.0653 -0.0398 395 TYR A CE2 
2473  C CZ  . TYR A 331 ? 1.8227 1.6185 1.7416 -0.0131 -0.0624 -0.0368 395 TYR A CZ  
2474  O OH  . TYR A 331 ? 1.4979 1.3050 1.4110 -0.0063 -0.0628 -0.0379 395 TYR A OH  
2475  N N   . GLU A 332 ? 2.1946 1.9415 2.1600 -0.0664 -0.0448 -0.0335 396 GLU A N   
2476  C CA  . GLU A 332 ? 2.5514 2.2976 2.5358 -0.0790 -0.0449 -0.0384 396 GLU A CA  
2477  C C   . GLU A 332 ? 2.9948 2.7573 2.9937 -0.0763 -0.0564 -0.0475 396 GLU A C   
2478  O O   . GLU A 332 ? 3.6769 3.4575 3.6987 -0.0828 -0.0566 -0.0523 396 GLU A O   
2479  C CB  . GLU A 332 ? 2.4930 2.2093 2.4649 -0.0843 -0.0443 -0.0377 396 GLU A CB  
2480  C CG  . GLU A 332 ? 2.3565 2.0700 2.3489 -0.1003 -0.0422 -0.0426 396 GLU A CG  
2481  C CD  . GLU A 332 ? 2.4388 2.1605 2.4452 -0.1005 -0.0553 -0.0533 396 GLU A CD  
2482  O OE1 . GLU A 332 ? 2.6512 2.3602 2.6415 -0.0912 -0.0650 -0.0559 396 GLU A OE1 
2483  O OE2 . GLU A 332 ? 2.3638 2.1053 2.3971 -0.1089 -0.0562 -0.0598 396 GLU A OE2 
2484  N N   . SER A 333 ? 2.7498 2.5061 2.7341 -0.0656 -0.0658 -0.0501 397 SER A N   
2485  C CA  . SER A 333 ? 2.5904 2.3577 2.5823 -0.0604 -0.0772 -0.0584 397 SER A CA  
2486  C C   . SER A 333 ? 2.7717 2.5461 2.7875 -0.0709 -0.0806 -0.0662 397 SER A C   
2487  O O   . SER A 333 ? 3.5963 3.3549 3.6140 -0.0786 -0.0823 -0.0692 397 SER A O   
2488  C CB  . SER A 333 ? 2.5602 2.3477 2.5525 -0.0517 -0.0779 -0.0577 397 SER A CB  
2489  O OG  . SER A 333 ? 2.6013 2.3839 2.5733 -0.0423 -0.0761 -0.0525 397 SER A OG  
2490  N N   . ARG A 334 ? 2.2038 2.0018 2.2378 -0.0712 -0.0817 -0.0700 398 ARG A N   
2491  C CA  . ARG A 334 ? 2.2957 2.1063 2.3563 -0.0812 -0.0840 -0.0783 398 ARG A CA  
2492  C C   . ARG A 334 ? 2.0296 1.8662 2.1073 -0.0816 -0.0800 -0.0790 398 ARG A C   
2493  O O   . ARG A 334 ? 2.1462 1.9875 2.2143 -0.0762 -0.0737 -0.0717 398 ARG A O   
2494  C CB  . ARG A 334 ? 2.2294 2.0391 2.2940 -0.0772 -0.0985 -0.0893 398 ARG A CB  
2495  C CG  . ARG A 334 ? 1.6281 1.4422 1.6786 -0.0611 -0.1075 -0.0912 398 ARG A CG  
2496  C CD  . ARG A 334 ? 1.9239 1.7388 1.9806 -0.0572 -0.1218 -0.1030 398 ARG A CD  
2497  N NE  . ARG A 334 ? 2.1676 1.9639 2.2250 -0.0649 -0.1256 -0.1070 398 ARG A NE  
2498  C CZ  . ARG A 334 ? 2.2124 2.0047 2.2740 -0.0629 -0.1384 -0.1176 398 ARG A CZ  
2499  N NH1 . ARG A 334 ? 2.2807 2.0866 2.3454 -0.0522 -0.1488 -0.1255 398 ARG A NH1 
2500  N NH2 . ARG A 334 ? 2.2000 1.9728 2.2609 -0.0709 -0.1410 -0.1207 398 ARG A NH2 
2501  N N   . ASP A 335 ? 2.2367 2.0903 2.3396 -0.0875 -0.0841 -0.0884 399 ASP A N   
2502  C CA  . ASP A 335 ? 2.3749 2.2549 2.4957 -0.0869 -0.0817 -0.0910 399 ASP A CA  
2503  C C   . ASP A 335 ? 1.9512 1.8368 2.0559 -0.0723 -0.0839 -0.0873 399 ASP A C   
2504  O O   . ASP A 335 ? 1.8660 1.7673 1.9766 -0.0704 -0.0789 -0.0853 399 ASP A O   
2505  C CB  . ASP A 335 ? 2.5739 2.4719 2.7204 -0.0896 -0.0914 -0.1049 399 ASP A CB  
2506  C CG  . ASP A 335 ? 2.6223 2.5188 2.7902 -0.1069 -0.0877 -0.1097 399 ASP A CG  
2507  O OD1 . ASP A 335 ? 2.6785 2.5622 2.8426 -0.1174 -0.0750 -0.1012 399 ASP A OD1 
2508  O OD2 . ASP A 335 ? 2.5665 2.4740 2.7543 -0.1100 -0.0973 -0.1223 399 ASP A OD2 
2509  N N   . CYS A 336 ? 1.3694 1.2412 1.4532 -0.0625 -0.0910 -0.0866 400 CYS A N   
2510  C CA  . CYS A 336 ? 1.0737 0.9468 1.1397 -0.0494 -0.0933 -0.0836 400 CYS A CA  
2511  C C   . CYS A 336 ? 1.0759 0.9430 1.1259 -0.0482 -0.0827 -0.0723 400 CYS A C   
2512  O O   . CYS A 336 ? 1.1361 0.9879 1.1742 -0.0505 -0.0787 -0.0667 400 CYS A O   
2513  C CB  . CYS A 336 ? 1.4257 1.2857 1.4759 -0.0407 -0.1034 -0.0872 400 CYS A CB  
2514  S SG  . CYS A 336 ? 2.3883 2.2546 2.4265 -0.0255 -0.1110 -0.0907 400 CYS A SG  
2515  N N   . GLN A 337 ? 1.1073 0.9857 1.1557 -0.0436 -0.0792 -0.0697 401 GLN A N   
2516  C CA  . GLN A 337 ? 0.9506 0.8247 0.9831 -0.0408 -0.0711 -0.0605 401 GLN A CA  
2517  C C   . GLN A 337 ? 0.8143 0.6822 0.8267 -0.0305 -0.0748 -0.0594 401 GLN A C   
2518  O O   . GLN A 337 ? 1.2304 1.1042 1.2395 -0.0238 -0.0784 -0.0621 401 GLN A O   
2519  C CB  . GLN A 337 ? 0.7874 0.6751 0.8277 -0.0422 -0.0640 -0.0577 401 GLN A CB  
2520  C CG  . GLN A 337 ? 0.8368 0.7198 0.8621 -0.0402 -0.0559 -0.0491 401 GLN A CG  
2521  C CD  . GLN A 337 ? 1.0182 0.8861 1.0320 -0.0428 -0.0520 -0.0437 401 GLN A CD  
2522  O OE1 . GLN A 337 ? 1.3758 1.2377 1.3959 -0.0503 -0.0482 -0.0424 401 GLN A OE1 
2523  N NE2 . GLN A 337 ? 0.9791 0.8406 0.9756 -0.0365 -0.0525 -0.0409 401 GLN A NE2 
2524  N N   . GLU A 338 ? 0.9061 0.7618 0.9042 -0.0292 -0.0733 -0.0554 402 GLU A N   
2525  C CA  . GLU A 338 ? 0.9244 0.7755 0.9046 -0.0206 -0.0753 -0.0545 402 GLU A CA  
2526  C C   . GLU A 338 ? 0.8925 0.7503 0.8664 -0.0181 -0.0694 -0.0504 402 GLU A C   
2527  O O   . GLU A 338 ? 0.8513 0.7137 0.8299 -0.0225 -0.0625 -0.0461 402 GLU A O   
2528  C CB  . GLU A 338 ? 1.1830 1.0223 1.1511 -0.0197 -0.0743 -0.0516 402 GLU A CB  
2529  C CG  . GLU A 338 ? 1.7959 1.6318 1.7474 -0.0110 -0.0768 -0.0521 402 GLU A CG  
2530  C CD  . GLU A 338 ? 2.1232 1.9509 2.0696 -0.0060 -0.0857 -0.0576 402 GLU A CD  
2531  O OE1 . GLU A 338 ? 2.4262 2.2456 2.3769 -0.0093 -0.0892 -0.0596 402 GLU A OE1 
2532  O OE2 . GLU A 338 ? 1.9118 1.7396 1.8484 0.0014  -0.0888 -0.0599 402 GLU A OE2 
2533  N N   . LEU A 339 ? 0.7480 0.6049 0.7102 -0.0111 -0.0719 -0.0518 403 LEU A N   
2534  C CA  . LEU A 339 ? 0.6393 0.4991 0.5926 -0.0091 -0.0663 -0.0482 403 LEU A CA  
2535  C C   . LEU A 339 ? 0.6183 0.4726 0.5550 -0.0046 -0.0650 -0.0471 403 LEU A C   
2536  O O   . LEU A 339 ? 0.8010 0.6500 0.7297 0.0008  -0.0698 -0.0503 403 LEU A O   
2537  C CB  . LEU A 339 ? 0.5892 0.4531 0.5441 -0.0055 -0.0689 -0.0512 403 LEU A CB  
2538  C CG  . LEU A 339 ? 0.5857 0.4495 0.5300 -0.0036 -0.0636 -0.0480 403 LEU A CG  
2539  C CD1 . LEU A 339 ? 0.6828 0.5518 0.6322 -0.0094 -0.0561 -0.0430 403 LEU A CD1 
2540  C CD2 . LEU A 339 ? 0.7587 0.6250 0.7043 0.0013  -0.0678 -0.0519 403 LEU A CD2 
2541  N N   . CYS A 340 ? 0.6814 0.5380 0.6133 -0.0067 -0.0581 -0.0429 404 CYS A N   
2542  C CA  . CYS A 340 ? 0.7052 0.5601 0.6246 -0.0041 -0.0554 -0.0424 404 CYS A CA  
2543  C C   . CYS A 340 ? 0.6455 0.5031 0.5591 -0.0058 -0.0489 -0.0400 404 CYS A C   
2544  O O   . CYS A 340 ? 0.7991 0.6597 0.7180 -0.0088 -0.0463 -0.0380 404 CYS A O   
2545  C CB  . CYS A 340 ? 0.7313 0.5869 0.6509 -0.0049 -0.0543 -0.0412 404 CYS A CB  
2546  S SG  . CYS A 340 ? 1.0500 0.8980 0.9724 -0.0028 -0.0618 -0.0441 404 CYS A SG  
2547  N N   . PHE A 341 ? 0.4564 0.3127 0.3589 -0.0042 -0.0457 -0.0403 405 PHE A N   
2548  C CA  . PHE A 341 ? 0.4815 0.3399 0.3794 -0.0077 -0.0388 -0.0384 405 PHE A CA  
2549  C C   . PHE A 341 ? 0.5046 0.3679 0.3976 -0.0088 -0.0342 -0.0392 405 PHE A C   
2550  O O   . PHE A 341 ? 0.5748 0.4379 0.4640 -0.0051 -0.0361 -0.0413 405 PHE A O   
2551  C CB  . PHE A 341 ? 0.5501 0.4001 0.4382 -0.0060 -0.0380 -0.0384 405 PHE A CB  
2552  C CG  . PHE A 341 ? 0.6111 0.4527 0.4850 -0.0015 -0.0380 -0.0400 405 PHE A CG  
2553  C CD1 . PHE A 341 ? 0.8022 0.6380 0.6734 0.0051  -0.0452 -0.0427 405 PHE A CD1 
2554  C CD2 . PHE A 341 ? 0.7003 0.5396 0.5633 -0.0039 -0.0306 -0.0394 405 PHE A CD2 
2555  C CE1 . PHE A 341 ? 0.6217 0.4484 0.4776 0.0107  -0.0452 -0.0441 405 PHE A CE1 
2556  C CE2 . PHE A 341 ? 0.6891 0.5196 0.5376 0.0004  -0.0293 -0.0404 405 PHE A CE2 
2557  C CZ  . PHE A 341 ? 0.6624 0.4861 0.5065 0.0084  -0.0368 -0.0425 405 PHE A CZ  
2558  N N   . TRP A 342 ? 0.5178 0.3863 0.4114 -0.0136 -0.0285 -0.0383 406 TRP A N   
2559  C CA  . TRP A 342 ? 0.5473 0.4240 0.4392 -0.0158 -0.0235 -0.0404 406 TRP A CA  
2560  C C   . TRP A 342 ? 0.6649 0.5375 0.5484 -0.0202 -0.0168 -0.0402 406 TRP A C   
2561  O O   . TRP A 342 ? 0.8267 0.6900 0.7054 -0.0215 -0.0161 -0.0381 406 TRP A O   
2562  C CB  . TRP A 342 ? 0.5616 0.4490 0.4623 -0.0178 -0.0229 -0.0408 406 TRP A CB  
2563  C CG  . TRP A 342 ? 0.5718 0.4575 0.4753 -0.0215 -0.0214 -0.0384 406 TRP A CG  
2564  C CD1 . TRP A 342 ? 0.5826 0.4658 0.4916 -0.0204 -0.0244 -0.0357 406 TRP A CD1 
2565  C CD2 . TRP A 342 ? 0.5561 0.4418 0.4565 -0.0268 -0.0161 -0.0386 406 TRP A CD2 
2566  N NE1 . TRP A 342 ? 0.4744 0.3569 0.3835 -0.0234 -0.0216 -0.0342 406 TRP A NE1 
2567  C CE2 . TRP A 342 ? 0.5590 0.4421 0.4625 -0.0273 -0.0171 -0.0360 406 TRP A CE2 
2568  C CE3 . TRP A 342 ? 0.6971 0.5840 0.5924 -0.0317 -0.0101 -0.0408 406 TRP A CE3 
2569  C CZ2 . TRP A 342 ? 0.5524 0.4333 0.4528 -0.0314 -0.0135 -0.0358 406 TRP A CZ2 
2570  C CZ3 . TRP A 342 ? 0.5826 0.4664 0.4753 -0.0373 -0.0061 -0.0407 406 TRP A CZ3 
2571  C CH2 . TRP A 342 ? 0.5437 0.4242 0.4383 -0.0366 -0.0083 -0.0383 406 TRP A CH2 
2572  N N   . ILE A 343 ? 0.7719 0.6513 0.6530 -0.0227 -0.0113 -0.0428 407 ILE A N   
2573  C CA  . ILE A 343 ? 0.6574 0.5327 0.5302 -0.0289 -0.0029 -0.0430 407 ILE A CA  
2574  C C   . ILE A 343 ? 0.7607 0.6528 0.6416 -0.0344 0.0023  -0.0472 407 ILE A C   
2575  O O   . ILE A 343 ? 0.8694 0.7739 0.7553 -0.0312 0.0015  -0.0504 407 ILE A O   
2576  C CB  . ILE A 343 ? 0.6385 0.5029 0.4972 -0.0261 0.0000  -0.0426 407 ILE A CB  
2577  C CG1 . ILE A 343 ? 0.7354 0.5858 0.5872 -0.0184 -0.0074 -0.0404 407 ILE A CG1 
2578  C CG2 . ILE A 343 ? 0.6346 0.4900 0.4820 -0.0334 0.0097  -0.0419 407 ILE A CG2 
2579  C CD1 . ILE A 343 ? 0.9174 0.7559 0.7531 -0.0131 -0.0059 -0.0404 407 ILE A CD1 
2580  N N   . GLU A 344 ? 0.6755 0.5685 0.5576 -0.0422 0.0074  -0.0479 408 GLU A N   
2581  C CA  . GLU A 344 ? 0.6542 0.5645 0.5460 -0.0483 0.0119  -0.0531 408 GLU A CA  
2582  C C   . GLU A 344 ? 0.7623 0.6726 0.6481 -0.0556 0.0223  -0.0553 408 GLU A C   
2583  O O   . GLU A 344 ? 0.7037 0.5958 0.5756 -0.0597 0.0280  -0.0521 408 GLU A O   
2584  C CB  . GLU A 344 ? 0.6411 0.5522 0.5379 -0.0527 0.0110  -0.0534 408 GLU A CB  
2585  C CG  . GLU A 344 ? 1.0129 0.9437 0.9222 -0.0579 0.0130  -0.0601 408 GLU A CG  
2586  C CD  . GLU A 344 ? 1.1823 1.1094 1.0928 -0.0628 0.0127  -0.0604 408 GLU A CD  
2587  O OE1 . GLU A 344 ? 1.0212 0.9591 0.9403 -0.0593 0.0074  -0.0629 408 GLU A OE1 
2588  O OE2 . GLU A 344 ? 1.2842 1.1954 1.1847 -0.0690 0.0176  -0.0579 408 GLU A OE2 
2589  N N   . ILE A 345 ? 0.7559 0.6865 0.6515 -0.0569 0.0252  -0.0610 409 ILE A N   
2590  C CA  . ILE A 345 ? 0.6366 0.5702 0.5280 -0.0627 0.0356  -0.0634 409 ILE A CA  
2591  C C   . ILE A 345 ? 0.6810 0.6375 0.5877 -0.0718 0.0413  -0.0712 409 ILE A C   
2592  O O   . ILE A 345 ? 0.8631 0.8404 0.7843 -0.0675 0.0352  -0.0764 409 ILE A O   
2593  C CB  . ILE A 345 ? 0.6304 0.5708 0.5207 -0.0531 0.0330  -0.0642 409 ILE A CB  
2594  C CG1 . ILE A 345 ? 0.6400 0.5572 0.5146 -0.0448 0.0278  -0.0576 409 ILE A CG1 
2595  C CG2 . ILE A 345 ? 0.6610 0.6137 0.5523 -0.0583 0.0438  -0.0685 409 ILE A CG2 
2596  C CD1 . ILE A 345 ? 0.8312 0.7500 0.6999 -0.0361 0.0268  -0.0582 409 ILE A CD1 
2597  N N   . ALA A 346 ? 0.7308 0.6834 0.6338 -0.0840 0.0529  -0.0724 410 ALA A N   
2598  C CA  . ALA A 346 ? 0.6393 0.6159 0.5588 -0.0948 0.0599  -0.0813 410 ALA A CA  
2599  C C   . ALA A 346 ? 0.7817 0.7868 0.7144 -0.0894 0.0600  -0.0882 410 ALA A C   
2600  O O   . ALA A 346 ? 0.6923 0.6939 0.6162 -0.0837 0.0628  -0.0857 410 ALA A O   
2601  C CB  . ALA A 346 ? 0.5712 0.5348 0.4814 -0.1092 0.0743  -0.0807 410 ALA A CB  
2602  N N   . ALA A 347 ? 0.8810 0.9142 0.8337 -0.0901 0.0564  -0.0974 411 ALA A N   
2603  C CA  . ALA A 347 ? 0.8838 0.9469 0.8501 -0.0852 0.0568  -0.1057 411 ALA A CA  
2604  C C   . ALA A 347 ? 0.9004 0.9893 0.8855 -0.0984 0.0649  -0.1164 411 ALA A C   
2605  O O   . ALA A 347 ? 1.0778 1.1573 1.0629 -0.1120 0.0710  -0.1164 411 ALA A O   
2606  C CB  . ALA A 347 ? 1.0829 1.1574 1.0551 -0.0697 0.0424  -0.1080 411 ALA A CB  
2607  N N   . THR A 348 ? 0.8729 0.9946 0.8744 -0.0943 0.0647  -0.1263 412 THR A N   
2608  C CA  . THR A 348 ? 0.8714 1.0251 0.8963 -0.1041 0.0684  -0.1394 412 THR A CA  
2609  C C   . THR A 348 ? 0.8593 1.0455 0.8993 -0.0894 0.0577  -0.1495 412 THR A C   
2610  O O   . THR A 348 ? 0.7862 0.9737 0.8192 -0.0752 0.0531  -0.1474 412 THR A O   
2611  C CB  . THR A 348 ? 0.8717 1.0348 0.9026 -0.1216 0.0871  -0.1434 412 THR A CB  
2612  O OG1 . THR A 348 ? 0.9849 1.1548 1.0109 -0.1150 0.0928  -0.1423 412 THR A OG1 
2613  C CG2 . THR A 348 ? 0.7530 0.8806 0.7660 -0.1361 0.0976  -0.1339 412 THR A CG2 
2614  N N   . THR A 349 ? 0.8449 1.0560 0.9041 -0.0918 0.0530  -0.1610 413 THR A N   
2615  C CA  . THR A 349 ? 0.8386 1.0836 0.9127 -0.0784 0.0440  -0.1729 413 THR A CA  
2616  C C   . THR A 349 ? 0.8914 1.1673 0.9796 -0.0820 0.0545  -0.1819 413 THR A C   
2617  O O   . THR A 349 ? 0.7581 1.0302 0.8466 -0.0976 0.0698  -0.1797 413 THR A O   
2618  C CB  . THR A 349 ? 0.9960 1.2581 1.0857 -0.0801 0.0362  -0.1833 413 THR A CB  
2619  O OG1 . THR A 349 ? 1.4177 1.6498 1.4914 -0.0740 0.0267  -0.1737 413 THR A OG1 
2620  C CG2 . THR A 349 ? 1.2385 1.5385 1.3447 -0.0659 0.0265  -0.1981 413 THR A CG2 
2621  N N   . LYS A 350 ? 1.0694 1.3742 1.1672 -0.0667 0.0465  -0.1916 414 LYS A N   
2622  C CA  . LYS A 350 ? 1.0566 1.3975 1.1710 -0.0677 0.0549  -0.2026 414 LYS A CA  
2623  C C   . LYS A 350 ? 1.0341 1.3997 1.1724 -0.0900 0.0685  -0.2130 414 LYS A C   
2624  O O   . LYS A 350 ? 1.1340 1.5211 1.2832 -0.0980 0.0818  -0.2184 414 LYS A O   
2625  C CB  . LYS A 350 ? 1.5851 1.9565 1.7089 -0.0469 0.0412  -0.2145 414 LYS A CB  
2626  C CG  . LYS A 350 ? 1.8660 2.2782 2.0067 -0.0432 0.0475  -0.2270 414 LYS A CG  
2627  C CD  . LYS A 350 ? 2.0922 2.5363 2.2438 -0.0229 0.0321  -0.2414 414 LYS A CD  
2628  C CE  . LYS A 350 ? 2.4954 2.9847 2.6663 -0.0186 0.0380  -0.2557 414 LYS A CE  
2629  N NZ  . LYS A 350 ? 2.9684 3.4860 3.1455 0.0050  0.0217  -0.2695 414 LYS A NZ  
2630  N N   . ALA A 351 ? 0.9944 1.3565 1.1404 -0.1005 0.0657  -0.2160 415 ALA A N   
2631  C CA  . ALA A 351 ? 0.9647 1.3439 1.1310 -0.1239 0.0789  -0.2248 415 ALA A CA  
2632  C C   . ALA A 351 ? 1.1242 1.4702 1.2806 -0.1380 0.0802  -0.2171 415 ALA A C   
2633  O O   . ALA A 351 ? 1.4064 1.7580 1.5712 -0.1366 0.0695  -0.2236 415 ALA A O   
2634  C CB  . ALA A 351 ? 1.0743 1.5036 1.2723 -0.1220 0.0730  -0.2458 415 ALA A CB  
2635  N N   . GLY A 352 ? 1.1796 1.4903 1.3165 -0.1501 0.0929  -0.2036 416 GLY A N   
2636  C CA  . GLY A 352 ? 0.9009 1.1753 1.0239 -0.1626 0.0949  -0.1949 416 GLY A CA  
2637  C C   . GLY A 352 ? 1.0262 1.2728 1.1304 -0.1469 0.0790  -0.1850 416 GLY A C   
2638  O O   . GLY A 352 ? 1.4215 1.6699 1.5191 -0.1276 0.0684  -0.1820 416 GLY A O   
2639  N N   . LEU A 353 ? 1.1010 1.3215 1.1962 -0.1552 0.0777  -0.1799 417 LEU A N   
2640  C CA  . LEU A 353 ? 0.9887 1.1857 1.0688 -0.1416 0.0630  -0.1719 417 LEU A CA  
2641  C C   . LEU A 353 ? 0.9066 1.0663 0.9593 -0.1336 0.0630  -0.1549 417 LEU A C   
2642  O O   . LEU A 353 ? 1.0202 1.1796 1.0664 -0.1282 0.0673  -0.1507 417 LEU A O   
2643  C CB  . LEU A 353 ? 0.8378 1.0606 0.9292 -0.1232 0.0473  -0.1804 417 LEU A CB  
2644  C CG  . LEU A 353 ? 0.8096 1.0786 0.9306 -0.1261 0.0463  -0.1997 417 LEU A CG  
2645  C CD1 . LEU A 353 ? 0.8908 1.1849 1.0185 -0.1042 0.0318  -0.2076 417 LEU A CD1 
2646  C CD2 . LEU A 353 ? 0.6812 0.9564 0.8154 -0.1400 0.0461  -0.2089 417 LEU A CD2 
2647  N N   . SER A 354 ? 0.8317 0.9614 0.8687 -0.1320 0.0576  -0.1459 418 SER A N   
2648  C CA  . SER A 354 ? 1.0126 1.1072 1.0252 -0.1275 0.0591  -0.1312 418 SER A CA  
2649  C C   . SER A 354 ? 1.1159 1.1986 1.1191 -0.1105 0.0451  -0.1244 418 SER A C   
2650  O O   . SER A 354 ? 1.8612 1.9186 1.8514 -0.1099 0.0419  -0.1167 418 SER A O   
2651  C CB  . SER A 354 ? 1.3910 1.4565 1.3902 -0.1420 0.0677  -0.1255 418 SER A CB  
2652  O OG  . SER A 354 ? 1.7819 1.8450 1.7853 -0.1448 0.0610  -0.1289 418 SER A OG  
2653  N N   . SER A 355 ? 1.2003 1.3005 1.2093 -0.0965 0.0372  -0.1275 419 SER A N   
2654  C CA  . SER A 355 ? 1.2085 1.2934 1.2059 -0.0813 0.0261  -0.1197 419 SER A CA  
2655  C C   . SER A 355 ? 1.0756 1.1320 1.0542 -0.0803 0.0300  -0.1075 419 SER A C   
2656  O O   . SER A 355 ? 1.0351 1.0865 1.0090 -0.0883 0.0404  -0.1058 419 SER A O   
2657  C CB  . SER A 355 ? 1.3156 1.4226 1.3206 -0.0663 0.0173  -0.1258 419 SER A CB  
2658  O OG  . SER A 355 ? 1.2092 1.3015 1.2038 -0.0528 0.0066  -0.1196 419 SER A OG  
2659  N N   . ASN A 356 ? 0.9608 0.9983 0.9283 -0.0707 0.0220  -0.0993 420 ASN A N   
2660  C CA  . ASN A 356 ? 0.8840 0.8980 0.8358 -0.0671 0.0229  -0.0894 420 ASN A CA  
2661  C C   . ASN A 356 ? 0.9053 0.9212 0.8550 -0.0528 0.0144  -0.0877 420 ASN A C   
2662  O O   . ASN A 356 ? 1.3127 1.3393 1.2685 -0.0450 0.0065  -0.0912 420 ASN A O   
2663  C CB  . ASN A 356 ? 1.0674 1.0560 1.0080 -0.0691 0.0212  -0.0815 420 ASN A CB  
2664  C CG  . ASN A 356 ? 0.9579 0.9435 0.9000 -0.0815 0.0270  -0.0841 420 ASN A CG  
2665  O OD1 . ASN A 356 ? 1.0788 1.0781 1.0318 -0.0834 0.0240  -0.0905 420 ASN A OD1 
2666  N ND2 . ASN A 356 ? 1.0796 1.0452 1.0091 -0.0893 0.0349  -0.0794 420 ASN A ND2 
2667  N N   . ASP A 357 ? 0.9657 0.9695 0.9050 -0.0489 0.0157  -0.0824 421 ASP A N   
2668  C CA  . ASP A 357 ? 0.9882 0.9870 0.9228 -0.0361 0.0070  -0.0795 421 ASP A CA  
2669  C C   . ASP A 357 ? 0.8497 0.8229 0.7713 -0.0337 0.0047  -0.0706 421 ASP A C   
2670  O O   . ASP A 357 ? 0.7846 0.7433 0.6989 -0.0403 0.0097  -0.0665 421 ASP A O   
2671  C CB  . ASP A 357 ? 0.9601 0.9740 0.8967 -0.0294 0.0073  -0.0844 421 ASP A CB  
2672  C CG  . ASP A 357 ? 1.4842 1.5067 1.4236 -0.0167 -0.0029 -0.0875 421 ASP A CG  
2673  O OD1 . ASP A 357 ? 1.1799 1.1866 1.1132 -0.0109 -0.0102 -0.0822 421 ASP A OD1 
2674  O OD2 . ASP A 357 ? 1.6047 1.6495 1.5518 -0.0123 -0.0032 -0.0957 421 ASP A OD2 
2675  N N   . LEU A 358 ? 0.9084 0.8761 0.8270 -0.0237 -0.0033 -0.0683 422 LEU A N   
2676  C CA  . LEU A 358 ? 0.7479 0.6948 0.6580 -0.0209 -0.0075 -0.0614 422 LEU A CA  
2677  C C   . LEU A 358 ? 0.8971 0.8376 0.7995 -0.0145 -0.0093 -0.0605 422 LEU A C   
2678  O O   . LEU A 358 ? 0.9691 0.9208 0.8727 -0.0088 -0.0105 -0.0648 422 LEU A O   
2679  C CB  . LEU A 358 ? 0.6922 0.6359 0.6052 -0.0155 -0.0152 -0.0595 422 LEU A CB  
2680  C CG  . LEU A 358 ? 0.6595 0.5989 0.5752 -0.0203 -0.0147 -0.0570 422 LEU A CG  
2681  C CD1 . LEU A 358 ? 0.7592 0.6891 0.6741 -0.0150 -0.0211 -0.0530 422 LEU A CD1 
2682  C CD2 . LEU A 358 ? 0.6834 0.6103 0.5931 -0.0266 -0.0101 -0.0533 422 LEU A CD2 
2683  N N   . ILE A 359 ? 0.8299 0.7524 0.7236 -0.0145 -0.0102 -0.0556 423 ILE A N   
2684  C CA  . ILE A 359 ? 0.7417 0.6544 0.6279 -0.0068 -0.0152 -0.0545 423 ILE A CA  
2685  C C   . ILE A 359 ? 0.6713 0.5691 0.5565 -0.0060 -0.0210 -0.0502 423 ILE A C   
2686  O O   . ILE A 359 ? 0.6602 0.5527 0.5456 -0.0113 -0.0186 -0.0476 423 ILE A O   
2687  C CB  . ILE A 359 ? 0.6783 0.5863 0.5536 -0.0066 -0.0093 -0.0548 423 ILE A CB  
2688  C CG1 . ILE A 359 ? 0.7972 0.6926 0.6637 0.0023  -0.0162 -0.0538 423 ILE A CG1 
2689  C CG2 . ILE A 359 ? 0.5280 0.4257 0.3963 -0.0142 -0.0021 -0.0519 423 ILE A CG2 
2690  C CD1 . ILE A 359 ? 0.9902 0.8869 0.8470 0.0068  -0.0124 -0.0560 423 ILE A CD1 
2691  N N   . THR A 360 ? 0.6723 0.5638 0.5568 0.0005  -0.0286 -0.0499 424 THR A N   
2692  C CA  . THR A 360 ? 0.6492 0.5296 0.5360 0.0005  -0.0341 -0.0470 424 THR A CA  
2693  C C   . THR A 360 ? 0.6766 0.5462 0.5568 0.0065  -0.0400 -0.0477 424 THR A C   
2694  O O   . THR A 360 ? 0.6389 0.5092 0.5145 0.0122  -0.0424 -0.0503 424 THR A O   
2695  C CB  . THR A 360 ? 0.7236 0.6061 0.6182 0.0012  -0.0383 -0.0464 424 THR A CB  
2696  O OG1 . THR A 360 ? 0.9781 0.8567 0.8700 0.0076  -0.0442 -0.0482 424 THR A OG1 
2697  C CG2 . THR A 360 ? 0.7704 0.6656 0.6690 -0.0006 -0.0344 -0.0478 424 THR A CG2 
2698  N N   . PHE A 361 ? 0.5741 0.4344 0.4541 0.0059  -0.0429 -0.0462 425 PHE A N   
2699  C CA  . PHE A 361 ? 0.5565 0.4066 0.4312 0.0118  -0.0496 -0.0480 425 PHE A CA  
2700  C C   . PHE A 361 ? 0.6419 0.4890 0.5270 0.0106  -0.0562 -0.0480 425 PHE A C   
2701  O O   . PHE A 361 ? 0.6686 0.5184 0.5614 0.0057  -0.0542 -0.0457 425 PHE A O   
2702  C CB  . PHE A 361 ? 0.4722 0.3142 0.3355 0.0132  -0.0470 -0.0475 425 PHE A CB  
2703  C CG  . PHE A 361 ? 0.5280 0.3702 0.3789 0.0141  -0.0396 -0.0477 425 PHE A CG  
2704  C CD1 . PHE A 361 ? 0.4469 0.2941 0.2969 0.0072  -0.0302 -0.0459 425 PHE A CD1 
2705  C CD2 . PHE A 361 ? 0.5207 0.3591 0.3616 0.0213  -0.0415 -0.0500 425 PHE A CD2 
2706  C CE1 . PHE A 361 ? 0.4575 0.3063 0.2980 0.0062  -0.0218 -0.0464 425 PHE A CE1 
2707  C CE2 . PHE A 361 ? 0.5639 0.4040 0.3941 0.0214  -0.0330 -0.0501 425 PHE A CE2 
2708  C CZ  . PHE A 361 ? 0.5091 0.3549 0.3399 0.0131  -0.0226 -0.0483 425 PHE A CZ  
2709  N N   . CYS A 362 ? 0.7724 0.6137 0.6580 0.0150  -0.0639 -0.0508 426 CYS A N   
2710  C CA  . CYS A 362 ? 0.7538 0.5921 0.6503 0.0129  -0.0699 -0.0519 426 CYS A CA  
2711  C C   . CYS A 362 ? 0.7207 0.5524 0.6133 0.0184  -0.0770 -0.0560 426 CYS A C   
2712  O O   . CYS A 362 ? 0.9164 0.7427 0.7962 0.0253  -0.0788 -0.0581 426 CYS A O   
2713  C CB  . CYS A 362 ? 0.7753 0.6118 0.6783 0.0112  -0.0729 -0.0521 426 CYS A CB  
2714  S SG  . CYS A 362 ? 1.6578 1.5021 1.5649 0.0056  -0.0647 -0.0473 426 CYS A SG  
2715  N N   . GLY A 363 ? 0.7497 0.5825 0.6531 0.0162  -0.0809 -0.0576 427 GLY A N   
2716  C CA  . GLY A 363 ? 0.7394 0.5677 0.6407 0.0224  -0.0890 -0.0630 427 GLY A CA  
2717  C C   . GLY A 363 ? 0.8215 0.6450 0.7271 0.0246  -0.0982 -0.0681 427 GLY A C   
2718  O O   . GLY A 363 ? 1.1009 0.9255 1.0178 0.0184  -0.0987 -0.0678 427 GLY A O   
2719  N N   . THR A 364 ? 0.9558 0.7720 0.8501 0.0337  -0.1051 -0.0729 428 THR A N   
2720  C CA  . THR A 364 ? 1.2531 1.0641 1.1517 0.0368  -0.1159 -0.0796 428 THR A CA  
2721  C C   . THR A 364 ? 1.2447 1.0568 1.1475 0.0417  -0.1245 -0.0865 428 THR A C   
2722  O O   . THR A 364 ? 0.8002 0.6130 0.6947 0.0464  -0.1223 -0.0857 428 THR A O   
2723  C CB  . THR A 364 ? 1.3327 1.1338 1.2144 0.0449  -0.1187 -0.0809 428 THR A CB  
2724  O OG1 . THR A 364 ? 1.5597 1.3545 1.4467 0.0466  -0.1296 -0.0876 428 THR A OG1 
2725  C CG2 . THR A 364 ? 0.9307 0.7260 0.7923 0.0555  -0.1183 -0.0815 428 THR A CG2 
2726  N N   . GLY A 365 ? 1.3443 1.1565 1.2601 0.0405  -0.1344 -0.0936 429 GLY A N   
2727  C CA  . GLY A 365 ? 1.0448 0.8606 0.9685 0.0453  -0.1449 -0.1027 429 GLY A CA  
2728  C C   . GLY A 365 ? 1.0714 0.8763 0.9733 0.0602  -0.1521 -0.1071 429 GLY A C   
2729  O O   . GLY A 365 ? 1.1845 0.9904 1.0828 0.0687  -0.1586 -0.1127 429 GLY A O   
2730  N N   . GLY A 366 ? 0.9660 0.7602 0.8517 0.0644  -0.1509 -0.1046 430 GLY A N   
2731  C CA  . GLY A 366 ? 1.2491 1.0313 1.1118 0.0789  -0.1568 -0.1083 430 GLY A CA  
2732  C C   . GLY A 366 ? 1.0712 0.8488 0.9127 0.0856  -0.1483 -0.1027 430 GLY A C   
2733  O O   . GLY A 366 ? 0.7692 0.5516 0.6113 0.0784  -0.1366 -0.0949 430 GLY A O   
2734  N N   . SER A 367 ? 1.1731 0.9397 0.9942 0.0995  -0.1540 -0.1068 431 SER A N   
2735  C CA  . SER A 367 ? 0.8756 0.6327 0.6715 0.1057  -0.1444 -0.1007 431 SER A CA  
2736  C C   . SER A 367 ? 0.8924 0.6451 0.6756 0.1051  -0.1355 -0.0950 431 SER A C   
2737  O O   . SER A 367 ? 1.4019 1.1543 1.1886 0.1057  -0.1404 -0.0976 431 SER A O   
2738  C CB  . SER A 367 ? 0.9941 0.7380 0.7684 0.1222  -0.1529 -0.1068 431 SER A CB  
2739  O OG  . SER A 367 ? 0.9443 0.6757 0.6917 0.1276  -0.1422 -0.1003 431 SER A OG  
2740  N N   . MET A 368 ? 0.9141 0.6633 0.6822 0.1040  -0.1225 -0.0878 432 MET A N   
2741  C CA  . MET A 368 ? 0.9699 0.7191 0.7289 0.1024  -0.1128 -0.0829 432 MET A CA  
2742  C C   . MET A 368 ? 1.0409 0.7767 0.7708 0.1109  -0.1046 -0.0799 432 MET A C   
2743  O O   . MET A 368 ? 0.9824 0.7096 0.7003 0.1135  -0.1017 -0.0784 432 MET A O   
2744  C CB  . MET A 368 ? 0.8762 0.6390 0.6511 0.0882  -0.1020 -0.0767 432 MET A CB  
2745  C CG  . MET A 368 ? 0.9637 0.7374 0.7631 0.0800  -0.1076 -0.0783 432 MET A CG  
2746  S SD  . MET A 368 ? 0.9926 0.7694 0.7908 0.0804  -0.1057 -0.0778 432 MET A SD  
2747  C CE  . MET A 368 ? 0.9132 0.6929 0.6955 0.0801  -0.0898 -0.0718 432 MET A CE  
2748  N N   . PRO A 369 ? 1.2027 0.9359 0.9201 0.1154  -0.1002 -0.0789 433 PRO A N   
2749  C CA  . PRO A 369 ? 1.0837 0.8041 0.7726 0.1229  -0.0903 -0.0758 433 PRO A CA  
2750  C C   . PRO A 369 ? 1.0298 0.7543 0.7171 0.1118  -0.0732 -0.0683 433 PRO A C   
2751  O O   . PRO A 369 ? 0.9007 0.6400 0.6095 0.0990  -0.0694 -0.0658 433 PRO A O   
2752  C CB  . PRO A 369 ? 1.2179 0.9409 0.9016 0.1283  -0.0901 -0.0772 433 PRO A CB  
2753  C CG  . PRO A 369 ? 1.2702 1.0109 0.9807 0.1175  -0.0917 -0.0773 433 PRO A CG  
2754  C CD  . PRO A 369 ? 1.3214 1.0641 1.0505 0.1131  -0.1027 -0.0804 433 PRO A CD  
2755  N N   . ASP A 370 ? 1.2158 0.9258 0.8766 0.1166  -0.0629 -0.0649 434 ASP A N   
2756  C CA  . ASP A 370 ? 1.0978 0.8090 0.7546 0.1056  -0.0459 -0.0584 434 ASP A CA  
2757  C C   . ASP A 370 ? 1.1840 0.9136 0.8528 0.0974  -0.0362 -0.0568 434 ASP A C   
2758  O O   . ASP A 370 ? 1.2001 0.9302 0.8597 0.1050  -0.0354 -0.0586 434 ASP A O   
2759  C CB  . ASP A 370 ? 1.0264 0.7134 0.6487 0.1131  -0.0368 -0.0553 434 ASP A CB  
2760  C CG  . ASP A 370 ? 1.3308 0.9993 0.9394 0.1224  -0.0464 -0.0572 434 ASP A CG  
2761  O OD1 . ASP A 370 ? 1.4289 1.1058 1.0573 0.1174  -0.0542 -0.0589 434 ASP A OD1 
2762  O OD2 . ASP A 370 ? 1.6143 1.2599 1.1915 0.1357  -0.0461 -0.0574 434 ASP A OD2 
2763  N N   . VAL A 371 ? 0.9990 0.7443 0.6880 0.0832  -0.0297 -0.0543 435 VAL A N   
2764  C CA  . VAL A 371 ? 0.8860 0.6510 0.5875 0.0756  -0.0207 -0.0538 435 VAL A CA  
2765  C C   . VAL A 371 ? 0.9848 0.7577 0.6946 0.0608  -0.0077 -0.0500 435 VAL A C   
2766  O O   . VAL A 371 ? 0.8616 0.6341 0.5813 0.0541  -0.0103 -0.0486 435 VAL A O   
2767  C CB  . VAL A 371 ? 0.9460 0.7280 0.6711 0.0750  -0.0315 -0.0575 435 VAL A CB  
2768  C CG1 . VAL A 371 ? 1.1629 0.9639 0.8964 0.0713  -0.0236 -0.0583 435 VAL A CG1 
2769  C CG2 . VAL A 371 ? 0.8615 0.6343 0.5817 0.0877  -0.0467 -0.0620 435 VAL A CG2 
2770  N N   . ASN A 372 ? 1.0314 0.8126 0.7377 0.0557  0.0063  -0.0490 436 ASN A N   
2771  C CA  . ASN A 372 ? 0.8889 0.6832 0.6075 0.0408  0.0184  -0.0473 436 ASN A CA  
2772  C C   . ASN A 372 ? 0.9097 0.7322 0.6534 0.0370  0.0162  -0.0511 436 ASN A C   
2773  O O   . ASN A 372 ? 1.1150 0.9488 0.8580 0.0411  0.0199  -0.0538 436 ASN A O   
2774  C CB  . ASN A 372 ? 0.8820 0.6687 0.5817 0.0369  0.0360  -0.0449 436 ASN A CB  
2775  C CG  . ASN A 372 ? 1.1642 0.9669 0.8781 0.0204  0.0496  -0.0446 436 ASN A CG  
2776  O OD1 . ASN A 372 ? 1.2164 1.0377 0.9543 0.0127  0.0457  -0.0465 436 ASN A OD1 
2777  N ND2 . ASN A 372 ? 1.5790 1.3739 1.2773 0.0147  0.0661  -0.0424 436 ASN A ND2 
2778  N N   . TRP A 373 ? 0.7462 0.5791 0.5101 0.0305  0.0102  -0.0515 437 TRP A N   
2779  C CA  . TRP A 373 ? 0.8389 0.6965 0.6246 0.0273  0.0080  -0.0551 437 TRP A CA  
2780  C C   . TRP A 373 ? 0.8940 0.7718 0.6908 0.0164  0.0207  -0.0568 437 TRP A C   
2781  O O   . TRP A 373 ? 0.9246 0.7976 0.7162 0.0068  0.0322  -0.0546 437 TRP A O   
2782  C CB  . TRP A 373 ? 0.7850 0.6439 0.5857 0.0259  -0.0034 -0.0548 437 TRP A CB  
2783  C CG  . TRP A 373 ? 0.8103 0.6537 0.6047 0.0355  -0.0163 -0.0548 437 TRP A CG  
2784  C CD1 . TRP A 373 ? 0.9574 0.7832 0.7442 0.0373  -0.0212 -0.0527 437 TRP A CD1 
2785  C CD2 . TRP A 373 ? 0.8373 0.6812 0.6322 0.0455  -0.0265 -0.0580 437 TRP A CD2 
2786  N NE1 . TRP A 373 ? 0.7716 0.5895 0.5565 0.0467  -0.0337 -0.0550 437 TRP A NE1 
2787  C CE2 . TRP A 373 ? 0.8762 0.7027 0.6650 0.0514  -0.0372 -0.0580 437 TRP A CE2 
2788  C CE3 . TRP A 373 ? 0.8481 0.7042 0.6470 0.0504  -0.0283 -0.0615 437 TRP A CE3 
2789  C CZ2 . TRP A 373 ? 0.9696 0.7910 0.7577 0.0602  -0.0488 -0.0613 437 TRP A CZ2 
2790  C CZ3 . TRP A 373 ? 0.7388 0.5874 0.5343 0.0603  -0.0400 -0.0641 437 TRP A CZ3 
2791  C CH2 . TRP A 373 ? 0.7911 0.6225 0.5818 0.0643  -0.0500 -0.0640 437 TRP A CH2 
2792  N N   . ALA B 11  ? 0.9238 1.2809 1.9619 0.0584  -0.3703 -0.1815 75  ALA B N   
2793  C CA  . ALA B 11  ? 0.9782 1.3154 1.9577 0.0563  -0.3569 -0.1850 75  ALA B CA  
2794  C C   . ALA B 11  ? 1.1731 1.5086 2.1899 0.0442  -0.3575 -0.1820 75  ALA B C   
2795  O O   . ALA B 11  ? 1.2862 1.6252 2.3586 0.0383  -0.3817 -0.1873 75  ALA B O   
2796  C CB  . ALA B 11  ? 0.7158 1.0275 1.6244 0.0648  -0.3762 -0.2063 75  ALA B CB  
2797  N N   . THR B 12  ? 1.2188 1.5482 2.2042 0.0408  -0.3316 -0.1737 76  THR B N   
2798  C CA  . THR B 12  ? 1.0958 1.4249 2.1126 0.0299  -0.3247 -0.1672 76  THR B CA  
2799  C C   . THR B 12  ? 1.1278 1.4334 2.0807 0.0294  -0.3213 -0.1768 76  THR B C   
2800  O O   . THR B 12  ? 1.0739 1.3711 1.9655 0.0358  -0.3050 -0.1763 76  THR B O   
2801  C CB  . THR B 12  ? 1.2191 1.5685 2.2718 0.0267  -0.2900 -0.1418 76  THR B CB  
2802  O OG1 . THR B 12  ? 2.0383 2.4107 3.1540 0.0277  -0.2923 -0.1314 76  THR B OG1 
2803  C CG2 . THR B 12  ? 1.1460 1.4951 2.2305 0.0160  -0.2804 -0.1334 76  THR B CG2 
2804  N N   . PRO B 13  ? 1.2055 1.5000 2.1739 0.0219  -0.3369 -0.1850 77  PRO B N   
2805  C CA  . PRO B 13  ? 1.0437 1.3165 1.9555 0.0214  -0.3332 -0.1930 77  PRO B CA  
2806  C C   . PRO B 13  ? 1.0898 1.3655 1.9690 0.0214  -0.2967 -0.1776 77  PRO B C   
2807  O O   . PRO B 13  ? 1.1712 1.4632 2.0895 0.0167  -0.2747 -0.1595 77  PRO B O   
2808  C CB  . PRO B 13  ? 0.8959 1.1650 1.8527 0.0109  -0.3462 -0.1955 77  PRO B CB  
2809  C CG  . PRO B 13  ? 0.9244 1.2044 1.9466 0.0088  -0.3721 -0.1991 77  PRO B CG  
2810  C CD  . PRO B 13  ? 1.0866 1.3882 2.1285 0.0136  -0.3588 -0.1866 77  PRO B CD  
2811  N N   . LEU B 14  ? 1.2982 1.5577 2.1070 0.0276  -0.2908 -0.1845 78  LEU B N   
2812  C CA  . LEU B 14  ? 1.1517 1.4098 1.9232 0.0283  -0.2599 -0.1724 78  LEU B CA  
2813  C C   . LEU B 14  ? 1.0306 1.2869 1.8177 0.0193  -0.2462 -0.1644 78  LEU B C   
2814  O O   . LEU B 14  ? 1.1501 1.3920 1.9275 0.0151  -0.2591 -0.1746 78  LEU B O   
2815  C CB  . LEU B 14  ? 1.2199 1.4596 1.9174 0.0360  -0.2602 -0.1824 78  LEU B CB  
2816  C CG  . LEU B 14  ? 1.0063 1.2431 1.6644 0.0373  -0.2312 -0.1711 78  LEU B CG  
2817  C CD1 . LEU B 14  ? 0.8296 1.0793 1.4882 0.0438  -0.2164 -0.1606 78  LEU B CD1 
2818  C CD2 . LEU B 14  ? 0.7760 0.9921 1.3698 0.0414  -0.2338 -0.1810 78  LEU B CD2 
2819  N N   . VAL B 15  ? 0.7491 1.0194 1.5593 0.0175  -0.2197 -0.1457 79  VAL B N   
2820  C CA  . VAL B 15  ? 0.8032 1.0734 1.6281 0.0105  -0.2022 -0.1350 79  VAL B CA  
2821  C C   . VAL B 15  ? 0.8530 1.1171 1.6261 0.0154  -0.1753 -0.1266 79  VAL B C   
2822  O O   . VAL B 15  ? 0.8465 1.1181 1.6085 0.0227  -0.1605 -0.1178 79  VAL B O   
2823  C CB  . VAL B 15  ? 0.7054 0.9966 1.6058 0.0056  -0.1932 -0.1185 79  VAL B CB  
2824  C CG1 . VAL B 15  ? 0.9569 1.2520 1.8597 0.0045  -0.1612 -0.0999 79  VAL B CG1 
2825  C CG2 . VAL B 15  ? 0.7426 1.0342 1.6953 -0.0033 -0.2185 -0.1265 79  VAL B CG2 
2826  N N   . LEU B 16  ? 0.8105 1.0598 1.5512 0.0121  -0.1703 -0.1296 80  LEU B N   
2827  C CA  . LEU B 16  ? 0.8365 1.0792 1.5322 0.0162  -0.1465 -0.1216 80  LEU B CA  
2828  C C   . LEU B 16  ? 1.0306 1.2804 1.7537 0.0132  -0.1231 -0.1046 80  LEU B C   
2829  O O   . LEU B 16  ? 1.0178 1.2731 1.7875 0.0056  -0.1268 -0.1015 80  LEU B O   
2830  C CB  . LEU B 16  ? 0.9235 1.1459 1.5640 0.0159  -0.1532 -0.1338 80  LEU B CB  
2831  C CG  . LEU B 16  ? 1.1509 1.3641 1.7533 0.0218  -0.1710 -0.1480 80  LEU B CG  
2832  C CD1 . LEU B 16  ? 1.1056 1.2997 1.6659 0.0207  -0.1795 -0.1592 80  LEU B CD1 
2833  C CD2 . LEU B 16  ? 1.4445 1.6597 2.0161 0.0303  -0.1585 -0.1427 80  LEU B CD2 
2834  N N   . GLY B 17  ? 0.7967 1.0454 1.4908 0.0200  -0.0996 -0.0936 81  GLY B N   
2835  C CA  . GLY B 17  ? 0.6657 0.9182 1.3747 0.0204  -0.0749 -0.0769 81  GLY B CA  
2836  C C   . GLY B 17  ? 0.7476 0.9879 1.4462 0.0131  -0.0745 -0.0801 81  GLY B C   
2837  O O   . GLY B 17  ? 0.8108 1.0352 1.4636 0.0117  -0.0830 -0.0921 81  GLY B O   
2838  N N   . GLU B 18  ? 0.8841 1.1321 1.6263 0.0086  -0.0640 -0.0685 82  GLU B N   
2839  C CA  . GLU B 18  ? 1.0966 1.3336 1.8320 0.0017  -0.0627 -0.0705 82  GLU B CA  
2840  C C   . GLU B 18  ? 1.0768 1.3016 1.7604 0.0077  -0.0427 -0.0651 82  GLU B C   
2841  O O   . GLU B 18  ? 0.9658 1.1763 1.6175 0.0040  -0.0467 -0.0730 82  GLU B O   
2842  C CB  . GLU B 18  ? 1.1117 1.3602 1.9112 -0.0048 -0.0572 -0.0589 82  GLU B CB  
2843  C CG  . GLU B 18  ? 1.3285 1.5679 2.1409 -0.0157 -0.0744 -0.0696 82  GLU B CG  
2844  C CD  . GLU B 18  ? 1.2571 1.4941 2.0797 -0.0204 -0.1065 -0.0879 82  GLU B CD  
2845  O OE1 . GLU B 18  ? 1.1121 1.3601 1.9571 -0.0177 -0.1157 -0.0889 82  GLU B OE1 
2846  O OE2 . GLU B 18  ? 1.3622 1.5852 2.1689 -0.0256 -0.1228 -0.1013 82  GLU B OE2 
2847  N N   . ASN B 19  ? 1.1639 1.3936 1.8386 0.0179  -0.0226 -0.0522 83  ASN B N   
2848  C CA  . ASN B 19  ? 1.0427 1.2605 1.6721 0.0255  -0.0036 -0.0458 83  ASN B CA  
2849  C C   . ASN B 19  ? 0.9691 1.1773 1.5457 0.0332  -0.0066 -0.0530 83  ASN B C   
2850  O O   . ASN B 19  ? 1.2791 1.4949 1.8598 0.0388  -0.0086 -0.0522 83  ASN B O   
2851  C CB  . ASN B 19  ? 1.0882 1.3148 1.7421 0.0338  0.0228  -0.0249 83  ASN B CB  
2852  C CG  . ASN B 19  ? 1.3784 1.6114 2.0796 0.0264  0.0291  -0.0160 83  ASN B CG  
2853  O OD1 . ASN B 19  ? 1.3706 1.5950 2.0679 0.0169  0.0191  -0.0248 83  ASN B OD1 
2854  N ND2 . ASN B 19  ? 1.5162 1.7642 2.2633 0.0312  0.0464  0.0022  83  ASN B ND2 
2855  N N   . LEU B 20  ? 0.9528 1.1441 1.4815 0.0333  -0.0071 -0.0595 84  LEU B N   
2856  C CA  . LEU B 20  ? 0.8845 1.0646 1.3628 0.0398  -0.0106 -0.0661 84  LEU B CA  
2857  C C   . LEU B 20  ? 0.8717 1.0479 1.3277 0.0529  0.0088  -0.0545 84  LEU B C   
2858  O O   . LEU B 20  ? 1.2669 1.4412 1.7263 0.0572  0.0262  -0.0432 84  LEU B O   
2859  C CB  . LEU B 20  ? 0.8100 0.9737 1.2500 0.0348  -0.0184 -0.0761 84  LEU B CB  
2860  C CG  . LEU B 20  ? 0.7547 0.9105 1.1625 0.0339  -0.0355 -0.0894 84  LEU B CG  
2861  C CD1 . LEU B 20  ? 0.8265 0.9916 1.2610 0.0288  -0.0534 -0.0982 84  LEU B CD1 
2862  C CD2 . LEU B 20  ? 0.7144 0.8552 1.0895 0.0296  -0.0398 -0.0959 84  LEU B CD2 
2863  N N   . CYS B 21  ? 0.9392 1.1128 1.3706 0.0603  0.0055  -0.0576 85  CYS B N   
2864  C CA  . CYS B 21  ? 0.9274 1.0925 1.3277 0.0742  0.0203  -0.0496 85  CYS B CA  
2865  C C   . CYS B 21  ? 0.8074 0.9537 1.1672 0.0757  0.0242  -0.0512 85  CYS B C   
2866  O O   . CYS B 21  ? 0.8130 0.9518 1.1582 0.0666  0.0115  -0.0616 85  CYS B O   
2867  C CB  . CYS B 21  ? 1.1177 1.2804 1.4951 0.0796  0.0110  -0.0561 85  CYS B CB  
2868  S SG  . CYS B 21  ? 2.7955 2.9792 3.2158 0.0840  0.0134  -0.0491 85  CYS B SG  
2869  N N   . SER B 22  ? 0.7286 0.8668 1.0704 0.0880  0.0416  -0.0407 86  SER B N   
2870  C CA  . SER B 22  ? 0.9677 1.0858 1.2669 0.0913  0.0436  -0.0430 86  SER B CA  
2871  C C   . SER B 22  ? 1.0126 1.1186 1.2737 0.0945  0.0312  -0.0524 86  SER B C   
2872  O O   . SER B 22  ? 1.0739 1.1820 1.3303 0.1033  0.0327  -0.0503 86  SER B O   
2873  C CB  . SER B 22  ? 1.1181 1.2287 1.4050 0.1061  0.0644  -0.0297 86  SER B CB  
2874  O OG  . SER B 22  ? 1.5991 1.7204 1.9223 0.1034  0.0774  -0.0194 86  SER B OG  
2875  N N   . ILE B 23  ? 0.7910 0.8850 1.0276 0.0872  0.0192  -0.0620 87  ILE B N   
2876  C CA  . ILE B 23  ? 0.6924 0.7745 0.8959 0.0890  0.0069  -0.0703 87  ILE B CA  
2877  C C   . ILE B 23  ? 0.8016 0.8625 0.9668 0.0949  0.0087  -0.0702 87  ILE B C   
2878  O O   . ILE B 23  ? 0.8060 0.8617 0.9680 0.0884  0.0080  -0.0716 87  ILE B O   
2879  C CB  . ILE B 23  ? 0.7627 0.8493 0.9727 0.0763  -0.0098 -0.0808 87  ILE B CB  
2880  C CG1 . ILE B 23  ? 0.8118 0.9162 1.0535 0.0737  -0.0142 -0.0821 87  ILE B CG1 
2881  C CG2 . ILE B 23  ? 1.3264 1.3989 1.5022 0.0775  -0.0213 -0.0878 87  ILE B CG2 
2882  C CD1 . ILE B 23  ? 1.2548 1.3682 1.5206 0.0614  -0.0248 -0.0887 87  ILE B CD1 
2883  N N   . ASN B 24  ? 0.5573 0.6056 0.6943 0.1079  0.0106  -0.0685 88  ASN B N   
2884  C CA  . ASN B 24  ? 0.5963 0.6224 0.6962 0.1140  0.0083  -0.0702 88  ASN B CA  
2885  C C   . ASN B 24  ? 0.6419 0.6547 0.7149 0.1155  -0.0064 -0.0778 88  ASN B C   
2886  O O   . ASN B 24  ? 0.7383 0.7313 0.7814 0.1204  -0.0116 -0.0800 88  ASN B O   
2887  C CB  . ASN B 24  ? 0.6634 0.6797 0.7479 0.1305  0.0238  -0.0610 88  ASN B CB  
2888  C CG  . ASN B 24  ? 0.7534 0.7785 0.8607 0.1289  0.0387  -0.0526 88  ASN B CG  
2889  O OD1 . ASN B 24  ? 0.7164 0.7332 0.8149 0.1254  0.0389  -0.0533 88  ASN B OD1 
2890  N ND2 . ASN B 24  ? 0.9982 1.0405 1.1367 0.1315  0.0512  -0.0440 88  ASN B ND2 
2891  N N   . GLY B 25  ? 0.5824 0.6057 0.6673 0.1113  -0.0139 -0.0816 89  GLY B N   
2892  C CA  . GLY B 25  ? 0.6600 0.6720 0.7229 0.1125  -0.0273 -0.0879 89  GLY B CA  
2893  C C   . GLY B 25  ? 0.6737 0.7003 0.7550 0.1050  -0.0353 -0.0922 89  GLY B C   
2894  O O   . GLY B 25  ? 0.7431 0.7880 0.8537 0.0996  -0.0316 -0.0911 89  GLY B O   
2895  N N   . TRP B 26  ? 0.5922 0.6103 0.6574 0.1048  -0.0472 -0.0972 90  TRP B N   
2896  C CA  . TRP B 26  ? 0.5366 0.5672 0.6161 0.0995  -0.0546 -0.1012 90  TRP B CA  
2897  C C   . TRP B 26  ? 0.5996 0.6231 0.6633 0.1075  -0.0599 -0.1025 90  TRP B C   
2898  O O   . TRP B 26  ? 0.6168 0.6221 0.6558 0.1114  -0.0660 -0.1038 90  TRP B O   
2899  C CB  . TRP B 26  ? 0.5546 0.5851 0.6360 0.0882  -0.0643 -0.1059 90  TRP B CB  
2900  C CG  . TRP B 26  ? 0.5030 0.5398 0.5992 0.0801  -0.0600 -0.1052 90  TRP B CG  
2901  C CD1 . TRP B 26  ? 0.5208 0.5471 0.6070 0.0776  -0.0579 -0.1038 90  TRP B CD1 
2902  C CD2 . TRP B 26  ? 0.5116 0.5656 0.6361 0.0735  -0.0583 -0.1063 90  TRP B CD2 
2903  N NE1 . TRP B 26  ? 0.5204 0.5567 0.6258 0.0699  -0.0540 -0.1036 90  TRP B NE1 
2904  C CE2 . TRP B 26  ? 0.5994 0.6518 0.7285 0.0670  -0.0546 -0.1053 90  TRP B CE2 
2905  C CE3 . TRP B 26  ? 0.4791 0.5483 0.6252 0.0724  -0.0608 -0.1083 90  TRP B CE3 
2906  C CZ2 . TRP B 26  ? 0.4973 0.5622 0.6518 0.0598  -0.0536 -0.1064 90  TRP B CZ2 
2907  C CZ3 . TRP B 26  ? 0.4736 0.5552 0.6462 0.0651  -0.0608 -0.1097 90  TRP B CZ3 
2908  C CH2 . TRP B 26  ? 0.4191 0.4983 0.5957 0.0590  -0.0574 -0.1089 90  TRP B CH2 
2909  N N   . VAL B 27  ? 0.5550 0.5921 0.6335 0.1103  -0.0586 -0.1022 91  VAL B N   
2910  C CA  . VAL B 27  ? 0.6455 0.6762 0.7091 0.1174  -0.0646 -0.1039 91  VAL B CA  
2911  C C   . VAL B 27  ? 0.5986 0.6412 0.6755 0.1113  -0.0733 -0.1084 91  VAL B C   
2912  O O   . VAL B 27  ? 0.6690 0.7289 0.7711 0.1066  -0.0717 -0.1090 91  VAL B O   
2913  C CB  . VAL B 27  ? 0.7917 0.8229 0.8522 0.1309  -0.0550 -0.0989 91  VAL B CB  
2914  C CG1 . VAL B 27  ? 1.0392 1.0645 1.0947 0.1372  -0.0428 -0.0929 91  VAL B CG1 
2915  C CG2 . VAL B 27  ? 0.8002 0.8537 0.8904 0.1301  -0.0512 -0.0973 91  VAL B CG2 
2916  N N   . PRO B 28  ? 0.6084 0.6408 0.6686 0.1120  -0.0831 -0.1114 92  PRO B N   
2917  C CA  . PRO B 28  ? 0.5480 0.5897 0.6165 0.1084  -0.0910 -0.1151 92  PRO B CA  
2918  C C   . PRO B 28  ? 0.5781 0.6328 0.6593 0.1146  -0.0884 -0.1148 92  PRO B C   
2919  O O   . PRO B 28  ? 0.7740 0.8234 0.8456 0.1242  -0.0838 -0.1118 92  PRO B O   
2920  C CB  . PRO B 28  ? 0.5163 0.5414 0.5628 0.1103  -0.0993 -0.1160 92  PRO B CB  
2921  C CG  . PRO B 28  ? 0.6069 0.6158 0.6346 0.1183  -0.0965 -0.1136 92  PRO B CG  
2922  C CD  . PRO B 28  ? 0.5989 0.6096 0.6321 0.1168  -0.0878 -0.1113 92  PRO B CD  
2923  N N   . THR B 29  ? 0.5237 0.5944 0.6259 0.1102  -0.0919 -0.1178 93  THR B N   
2924  C CA  . THR B 29  ? 0.6344 0.7188 0.7524 0.1155  -0.0910 -0.1175 93  THR B CA  
2925  C C   . THR B 29  ? 0.7017 0.7861 0.8121 0.1174  -0.1011 -0.1219 93  THR B C   
2926  O O   . THR B 29  ? 0.6449 0.7359 0.7601 0.1239  -0.1018 -0.1218 93  THR B O   
2927  C CB  . THR B 29  ? 0.7348 0.8376 0.8859 0.1106  -0.0885 -0.1176 93  THR B CB  
2928  O OG1 . THR B 29  ? 0.7880 0.8915 0.9436 0.1013  -0.0951 -0.1223 93  THR B OG1 
2929  C CG2 . THR B 29  ? 0.7048 0.8097 0.8660 0.1129  -0.0752 -0.1105 93  THR B CG2 
2930  N N   . TYR B 30  ? 0.7987 0.8753 0.8973 0.1125  -0.1082 -0.1248 94  TYR B N   
2931  C CA  . TYR B 30  ? 0.7077 0.7830 0.7977 0.1151  -0.1167 -0.1277 94  TYR B CA  
2932  C C   . TYR B 30  ? 0.7089 0.7699 0.7804 0.1121  -0.1205 -0.1269 94  TYR B C   
2933  O O   . TYR B 30  ? 0.5859 0.6426 0.6568 0.1056  -0.1191 -0.1261 94  TYR B O   
2934  C CB  . TYR B 30  ? 0.6723 0.7618 0.7797 0.1133  -0.1230 -0.1328 94  TYR B CB  
2935  C CG  . TYR B 30  ? 0.7761 0.8621 0.8708 0.1168  -0.1315 -0.1356 94  TYR B CG  
2936  C CD1 . TYR B 30  ? 0.7374 0.8245 0.8269 0.1245  -0.1342 -0.1358 94  TYR B CD1 
2937  C CD2 . TYR B 30  ? 0.9260 1.0072 1.0131 0.1135  -0.1359 -0.1373 94  TYR B CD2 
2938  C CE1 . TYR B 30  ? 0.8634 0.9470 0.9407 0.1288  -0.1409 -0.1376 94  TYR B CE1 
2939  C CE2 . TYR B 30  ? 0.8774 0.9548 0.9515 0.1188  -0.1420 -0.1385 94  TYR B CE2 
2940  C CZ  . TYR B 30  ? 1.0125 1.0911 1.0819 0.1264  -0.1445 -0.1386 94  TYR B CZ  
2941  O OH  . TYR B 30  ? 1.4291 1.5037 1.4852 0.1329  -0.1496 -0.1391 94  TYR B OH  
2942  N N   . ARG B 31  ? 0.6297 0.6842 0.6881 0.1169  -0.1252 -0.1265 95  ARG B N   
2943  C CA  . ARG B 31  ? 0.6846 0.7261 0.7292 0.1147  -0.1284 -0.1239 95  ARG B CA  
2944  C C   . ARG B 31  ? 0.6236 0.6655 0.6620 0.1203  -0.1335 -0.1243 95  ARG B C   
2945  O O   . ARG B 31  ? 0.5330 0.5759 0.5686 0.1268  -0.1345 -0.1248 95  ARG B O   
2946  C CB  . ARG B 31  ? 0.6852 0.7108 0.7172 0.1156  -0.1270 -0.1202 95  ARG B CB  
2947  C CG  . ARG B 31  ? 0.9631 0.9746 0.9842 0.1146  -0.1315 -0.1165 95  ARG B CG  
2948  C CD  . ARG B 31  ? 1.1193 1.1139 1.1303 0.1146  -0.1325 -0.1141 95  ARG B CD  
2949  N NE  . ARG B 31  ? 0.9171 0.9052 0.9185 0.1229  -0.1328 -0.1152 95  ARG B NE  
2950  C CZ  . ARG B 31  ? 0.7933 0.7632 0.7815 0.1260  -0.1361 -0.1141 95  ARG B CZ  
2951  N NH1 . ARG B 31  ? 1.0166 0.9740 1.0025 0.1206  -0.1403 -0.1120 95  ARG B NH1 
2952  N NH2 . ARG B 31  ? 0.8316 0.7947 0.8087 0.1352  -0.1362 -0.1153 95  ARG B NH2 
2953  N N   . GLY B 32  ? 0.8014 0.8428 0.8373 0.1189  -0.1361 -0.1236 96  GLY B N   
2954  C CA  . GLY B 32  ? 0.8322 0.8733 0.8605 0.1257  -0.1402 -0.1232 96  GLY B CA  
2955  C C   . GLY B 32  ? 0.7320 0.7593 0.7489 0.1283  -0.1405 -0.1171 96  GLY B C   
2956  O O   . GLY B 32  ? 0.6939 0.7105 0.7085 0.1239  -0.1392 -0.1134 96  GLY B O   
2957  N N   . GLU B 33  ? 0.7707 0.7972 0.7808 0.1357  -0.1432 -0.1161 97  GLU B N   
2958  C CA  . GLU B 33  ? 0.8540 0.8672 0.8555 0.1383  -0.1441 -0.1102 97  GLU B CA  
2959  C C   . GLU B 33  ? 0.8672 0.8705 0.8671 0.1353  -0.1430 -0.1022 97  GLU B C   
2960  O O   . GLU B 33  ? 0.7052 0.6953 0.7035 0.1340  -0.1444 -0.0964 97  GLU B O   
2961  C CB  . GLU B 33  ? 0.9401 0.9554 0.9356 0.1476  -0.1467 -0.1112 97  GLU B CB  
2962  C CG  . GLU B 33  ? 1.3876 1.3910 1.3764 0.1506  -0.1483 -0.1086 97  GLU B CG  
2963  C CD  . GLU B 33  ? 1.4426 1.4454 1.4326 0.1495  -0.1473 -0.1126 97  GLU B CD  
2964  O OE1 . GLU B 33  ? 1.3214 1.3377 1.3191 0.1499  -0.1451 -0.1176 97  GLU B OE1 
2965  O OE2 . GLU B 33  ? 1.4826 1.4705 1.4661 0.1491  -0.1489 -0.1102 97  GLU B OE2 
2966  N N   . GLY B 34  ? 0.8379 0.8470 0.8395 0.1345  -0.1410 -0.1016 98  GLY B N   
2967  C CA  . GLY B 34  ? 0.7173 0.7192 0.7195 0.1322  -0.1381 -0.0927 98  GLY B CA  
2968  C C   . GLY B 34  ? 0.8227 0.8193 0.8322 0.1225  -0.1369 -0.0907 98  GLY B C   
2969  O O   . GLY B 34  ? 0.9820 0.9720 0.9952 0.1196  -0.1348 -0.0823 98  GLY B O   
2970  N N   . THR B 35  ? 0.6645 0.6637 0.6767 0.1180  -0.1379 -0.0975 99  THR B N   
2971  C CA  . THR B 35  ? 0.7929 0.7866 0.8101 0.1099  -0.1371 -0.0964 99  THR B CA  
2972  C C   . THR B 35  ? 0.8416 0.8194 0.8573 0.1087  -0.1412 -0.0920 99  THR B C   
2973  O O   . THR B 35  ? 0.7807 0.7504 0.7995 0.1029  -0.1426 -0.0903 99  THR B O   
2974  C CB  . THR B 35  ? 0.7922 0.7936 0.8121 0.1074  -0.1356 -0.1042 99  THR B CB  
2975  O OG1 . THR B 35  ? 0.9413 0.9412 0.9569 0.1122  -0.1374 -0.1074 99  THR B OG1 
2976  C CG2 . THR B 35  ? 0.6797 0.6957 0.7040 0.1086  -0.1341 -0.1094 99  THR B CG2 
2977  N N   . THR B 36  ? 0.9352 0.9078 0.9459 0.1146  -0.1444 -0.0907 100 THR B N   
2978  C CA  . THR B 36  ? 1.0592 1.0153 1.0673 0.1149  -0.1505 -0.0882 100 THR B CA  
2979  C C   . THR B 36  ? 1.0247 0.9743 1.0351 0.1184  -0.1524 -0.0801 100 THR B C   
2980  O O   . THR B 36  ? 1.4913 1.4301 1.5103 0.1146  -0.1553 -0.0722 100 THR B O   
2981  C CB  . THR B 36  ? 1.0084 0.9619 1.0065 0.1202  -0.1527 -0.0954 100 THR B CB  
2982  O OG1 . THR B 36  ? 1.0061 0.9728 1.0016 0.1264  -0.1497 -0.0989 100 THR B OG1 
2983  C CG2 . THR B 36  ? 0.9028 0.8573 0.8991 0.1173  -0.1507 -0.1007 100 THR B CG2 
2984  N N   . GLY B 37  ? 0.8740 0.8304 0.8786 0.1258  -0.1508 -0.0816 101 GLY B N   
2985  C CA  . GLY B 37  ? 1.0796 1.0314 1.0854 0.1307  -0.1509 -0.0733 101 GLY B CA  
2986  C C   . GLY B 37  ? 0.9225 0.8841 0.9302 0.1335  -0.1440 -0.0678 101 GLY B C   
2987  O O   . GLY B 37  ? 1.0167 0.9867 1.0261 0.1303  -0.1403 -0.0699 101 GLY B O   
2988  N N   . LYS B 38  ? 0.7289 0.6881 0.7351 0.1406  -0.1423 -0.0605 102 LYS B N   
2989  C CA  . LYS B 38  ? 0.7179 0.6843 0.7210 0.1472  -0.1354 -0.0548 102 LYS B CA  
2990  C C   . LYS B 38  ? 0.7733 0.7506 0.7630 0.1558  -0.1356 -0.0641 102 LYS B C   
2991  O O   . LYS B 38  ? 0.9577 0.9365 0.9430 0.1574  -0.1400 -0.0717 102 LYS B O   
2992  C CB  . LYS B 38  ? 0.8614 0.8190 0.8700 0.1521  -0.1323 -0.0406 102 LYS B CB  
2993  C CG  . LYS B 38  ? 1.1475 1.0961 1.1743 0.1441  -0.1317 -0.0294 102 LYS B CG  
2994  C CD  . LYS B 38  ? 1.3598 1.3045 1.3945 0.1505  -0.1246 -0.0128 102 LYS B CD  
2995  C CE  . LYS B 38  ? 1.2815 1.2232 1.3358 0.1441  -0.1205 -0.0003 102 LYS B CE  
2996  N NZ  . LYS B 38  ? 1.7608 1.7020 1.8213 0.1531  -0.1099 0.0171  102 LYS B NZ  
2997  N N   . ILE B 39  ? 0.8603 0.8447 0.8435 0.1620  -0.1313 -0.0633 103 ILE B N   
2998  C CA  . ILE B 39  ? 0.7389 0.7331 0.7103 0.1704  -0.1336 -0.0730 103 ILE B CA  
2999  C C   . ILE B 39  ? 0.9169 0.9079 0.8777 0.1831  -0.1322 -0.0677 103 ILE B C   
3000  O O   . ILE B 39  ? 0.9031 0.8879 0.8622 0.1887  -0.1259 -0.0556 103 ILE B O   
3001  C CB  . ILE B 39  ? 0.6730 0.6735 0.6395 0.1727  -0.1316 -0.0761 103 ILE B CB  
3002  C CG1 . ILE B 39  ? 0.6532 0.6548 0.6307 0.1604  -0.1307 -0.0774 103 ILE B CG1 
3003  C CG2 . ILE B 39  ? 0.6575 0.6674 0.6150 0.1801  -0.1375 -0.0882 103 ILE B CG2 
3004  C CD1 . ILE B 39  ? 0.5720 0.5822 0.5540 0.1543  -0.1356 -0.0899 103 ILE B CD1 
3005  N N   . PRO B 40  ? 0.9648 0.9604 0.9193 0.1885  -0.1374 -0.0760 104 PRO B N   
3006  C CA  . PRO B 40  ? 0.7935 0.7871 0.7360 0.2018  -0.1368 -0.0726 104 PRO B CA  
3007  C C   . PRO B 40  ? 1.0468 1.0423 0.9757 0.2132  -0.1338 -0.0711 104 PRO B C   
3008  O O   . PRO B 40  ? 0.9369 0.9388 0.8639 0.2120  -0.1365 -0.0791 104 PRO B O   
3009  C CB  . PRO B 40  ? 0.8258 0.8267 0.7663 0.2037  -0.1440 -0.0843 104 PRO B CB  
3010  C CG  . PRO B 40  ? 0.7804 0.7833 0.7335 0.1909  -0.1464 -0.0897 104 PRO B CG  
3011  C CD  . PRO B 40  ? 0.8567 0.8596 0.8166 0.1826  -0.1433 -0.0877 104 PRO B CD  
3012  N N   . ASP B 41  ? 1.3338 1.3225 1.2527 0.2251  -0.1283 -0.0606 105 ASP B N   
3013  C CA  . ASP B 41  ? 1.2184 1.2053 1.1217 0.2384  -0.1232 -0.0558 105 ASP B CA  
3014  C C   . ASP B 41  ? 1.3127 1.3057 1.1994 0.2490  -0.1315 -0.0696 105 ASP B C   
3015  O O   . ASP B 41  ? 1.5456 1.5375 1.4187 0.2579  -0.1310 -0.0710 105 ASP B O   
3016  C CB  . ASP B 41  ? 1.4922 1.4697 1.3896 0.2499  -0.1136 -0.0391 105 ASP B CB  
3017  C CG  . ASP B 41  ? 1.8872 1.8580 1.8055 0.2393  -0.1069 -0.0246 105 ASP B CG  
3018  O OD1 . ASP B 41  ? 2.7580 2.7299 2.6922 0.2240  -0.1121 -0.0296 105 ASP B OD1 
3019  O OD2 . ASP B 41  ? 1.9776 1.9416 1.8972 0.2467  -0.0966 -0.0079 105 ASP B OD2 
3020  N N   . GLU B 42  ? 1.1577 1.1565 1.0457 0.2488  -0.1401 -0.0799 106 GLU B N   
3021  C CA  . GLU B 42  ? 1.2046 1.2093 1.0803 0.2590  -0.1500 -0.0930 106 GLU B CA  
3022  C C   . GLU B 42  ? 1.1763 1.1894 1.0608 0.2506  -0.1578 -0.1056 106 GLU B C   
3023  O O   . GLU B 42  ? 1.4557 1.4721 1.3314 0.2591  -0.1673 -0.1164 106 GLU B O   
3024  C CB  . GLU B 42  ? 1.4380 1.4468 1.3138 0.2629  -0.1564 -0.0988 106 GLU B CB  
3025  C CG  . GLU B 42  ? 1.7869 1.8035 1.6831 0.2482  -0.1602 -0.1049 106 GLU B CG  
3026  C CD  . GLU B 42  ? 2.3037 2.3136 2.2052 0.2440  -0.1545 -0.0955 106 GLU B CD  
3027  O OE1 . GLU B 42  ? 2.3987 2.3991 2.3008 0.2420  -0.1462 -0.0831 106 GLU B OE1 
3028  O OE2 . GLU B 42  ? 2.3729 2.3867 2.2790 0.2430  -0.1587 -0.1004 106 GLU B OE2 
3029  N N   . GLN B 43  ? 0.8617 0.8773 0.7639 0.2345  -0.1546 -0.1045 107 GLN B N   
3030  C CA  . GLN B 43  ? 0.7426 0.7656 0.6547 0.2261  -0.1604 -0.1148 107 GLN B CA  
3031  C C   . GLN B 43  ? 0.7871 0.8052 0.6861 0.2329  -0.1596 -0.1146 107 GLN B C   
3032  O O   . GLN B 43  ? 0.7931 0.8023 0.6802 0.2397  -0.1506 -0.1030 107 GLN B O   
3033  C CB  . GLN B 43  ? 0.6487 0.6747 0.5806 0.2088  -0.1568 -0.1133 107 GLN B CB  
3034  C CG  . GLN B 43  ? 0.7633 0.7947 0.7071 0.2030  -0.1595 -0.1168 107 GLN B CG  
3035  C CD  . GLN B 43  ? 1.1277 1.1631 1.0890 0.1881  -0.1579 -0.1189 107 GLN B CD  
3036  O OE1 . GLN B 43  ? 1.1917 1.2295 1.1586 0.1820  -0.1577 -0.1214 107 GLN B OE1 
3037  N NE2 . GLN B 43  ? 0.8581 0.8930 0.8265 0.1834  -0.1568 -0.1177 107 GLN B NE2 
3038  N N   . MET B 44  ? 0.8683 0.8921 0.7703 0.2319  -0.1694 -0.1271 108 MET B N   
3039  C CA  . MET B 44  ? 0.9595 0.9781 0.8496 0.2375  -0.1707 -0.1293 108 MET B CA  
3040  C C   . MET B 44  ? 0.9501 0.9670 0.8502 0.2250  -0.1606 -0.1210 108 MET B C   
3041  O O   . MET B 44  ? 0.8702 0.8935 0.7909 0.2094  -0.1593 -0.1220 108 MET B O   
3042  C CB  . MET B 44  ? 0.9682 0.9937 0.8655 0.2366  -0.1857 -0.1456 108 MET B CB  
3043  C CG  . MET B 44  ? 0.9882 1.0072 0.8729 0.2430  -0.1904 -0.1507 108 MET B CG  
3044  S SD  . MET B 44  ? 1.3363 1.3404 1.1823 0.2693  -0.1913 -0.1481 108 MET B SD  
3045  C CE  . MET B 44  ? 1.5292 1.5364 1.3732 0.2790  -0.2138 -0.1669 108 MET B CE  
3046  N N   . LEU B 45  ? 0.8566 0.8646 0.7418 0.2328  -0.1529 -0.1124 109 LEU B N   
3047  C CA  . LEU B 45  ? 0.8795 0.8863 0.7750 0.2214  -0.1442 -0.1050 109 LEU B CA  
3048  C C   . LEU B 45  ? 0.8262 0.8369 0.7270 0.2155  -0.1522 -0.1171 109 LEU B C   
3049  O O   . LEU B 45  ? 1.0266 1.0338 0.9117 0.2272  -0.1601 -0.1253 109 LEU B O   
3050  C CB  . LEU B 45  ? 0.7662 0.7629 0.6462 0.2325  -0.1324 -0.0903 109 LEU B CB  
3051  C CG  . LEU B 45  ? 0.6916 0.6829 0.5661 0.2411  -0.1233 -0.0760 109 LEU B CG  
3052  C CD1 . LEU B 45  ? 0.8145 0.7964 0.6707 0.2565  -0.1124 -0.0631 109 LEU B CD1 
3053  C CD2 . LEU B 45  ? 0.6090 0.6024 0.5065 0.2258  -0.1177 -0.0673 109 LEU B CD2 
3054  N N   . THR B 46  ? 0.6461 0.6629 0.5680 0.1984  -0.1508 -0.1184 110 THR B N   
3055  C CA  . THR B 46  ? 0.6050 0.6261 0.5352 0.1917  -0.1580 -0.1295 110 THR B CA  
3056  C C   . THR B 46  ? 0.6291 0.6464 0.5608 0.1854  -0.1505 -0.1238 110 THR B C   
3057  O O   . THR B 46  ? 0.7825 0.7969 0.7178 0.1806  -0.1398 -0.1115 110 THR B O   
3058  C CB  . THR B 46  ? 0.6157 0.6480 0.5700 0.1782  -0.1635 -0.1375 110 THR B CB  
3059  O OG1 . THR B 46  ? 0.8967 0.9302 0.8645 0.1651  -0.1545 -0.1297 110 THR B OG1 
3060  C CG2 . THR B 46  ? 0.6523 0.6893 0.6078 0.1833  -0.1692 -0.1412 110 THR B CG2 
3061  N N   . ARG B 47  ? 0.5961 0.6129 0.5259 0.1860  -0.1571 -0.1328 111 ARG B N   
3062  C CA  . ARG B 47  ? 0.5362 0.5509 0.4703 0.1783  -0.1511 -0.1292 111 ARG B CA  
3063  C C   . ARG B 47  ? 0.5587 0.5778 0.5039 0.1719  -0.1615 -0.1427 111 ARG B C   
3064  O O   . ARG B 47  ? 0.7051 0.7268 0.6510 0.1768  -0.1738 -0.1539 111 ARG B O   
3065  C CB  . ARG B 47  ? 0.4816 0.4853 0.3932 0.1914  -0.1436 -0.1201 111 ARG B CB  
3066  C CG  . ARG B 47  ? 0.5825 0.5793 0.4756 0.2037  -0.1520 -0.1293 111 ARG B CG  
3067  C CD  . ARG B 47  ? 0.8259 0.8128 0.7017 0.2124  -0.1416 -0.1191 111 ARG B CD  
3068  N NE  . ARG B 47  ? 0.9246 0.9025 0.7805 0.2246  -0.1511 -0.1296 111 ARG B NE  
3069  C CZ  . ARG B 47  ? 0.9961 0.9747 0.8606 0.2162  -0.1579 -0.1391 111 ARG B CZ  
3070  N NH1 . ARG B 47  ? 0.9162 0.9045 0.8080 0.1961  -0.1547 -0.1385 111 ARG B NH1 
3071  N NH2 . ARG B 47  ? 1.3043 1.2724 1.1490 0.2288  -0.1681 -0.1490 111 ARG B NH2 
3072  N N   . GLN B 48  ? 0.5606 0.5810 0.5170 0.1606  -0.1570 -0.1412 112 GLN B N   
3073  C CA  . GLN B 48  ? 0.6168 0.6413 0.5871 0.1532  -0.1655 -0.1525 112 GLN B CA  
3074  C C   . GLN B 48  ? 0.5932 0.6293 0.5868 0.1449  -0.1728 -0.1603 112 GLN B C   
3075  O O   . GLN B 48  ? 0.6925 0.7321 0.6966 0.1448  -0.1845 -0.1715 112 GLN B O   
3076  C CB  . GLN B 48  ? 0.5800 0.5956 0.5323 0.1659  -0.1756 -0.1612 112 GLN B CB  
3077  C CG  . GLN B 48  ? 0.6915 0.7120 0.6591 0.1636  -0.1919 -0.1764 112 GLN B CG  
3078  C CD  . GLN B 48  ? 0.8625 0.8770 0.8296 0.1633  -0.1990 -0.1841 112 GLN B CD  
3079  O OE1 . GLN B 48  ? 0.9912 1.0090 0.9744 0.1614  -0.2146 -0.1969 112 GLN B OE1 
3080  N NE2 . GLN B 48  ? 0.6805 0.6871 0.6341 0.1650  -0.1911 -0.1783 112 GLN B NE2 
3081  N N   . ASN B 49  ? 0.5156 0.5570 0.5184 0.1386  -0.1659 -0.1539 113 ASN B N   
3082  C CA  . ASN B 49  ? 0.5703 0.6227 0.5954 0.1312  -0.1697 -0.1589 113 ASN B CA  
3083  C C   . ASN B 49  ? 0.5659 0.6248 0.6136 0.1197  -0.1709 -0.1637 113 ASN B C   
3084  O O   . ASN B 49  ? 0.5915 0.6472 0.6400 0.1130  -0.1643 -0.1599 113 ASN B O   
3085  C CB  . ASN B 49  ? 0.4980 0.5520 0.5257 0.1270  -0.1608 -0.1504 113 ASN B CB  
3086  C CG  . ASN B 49  ? 0.6807 0.7297 0.6910 0.1379  -0.1605 -0.1460 113 ASN B CG  
3087  O OD1 . ASN B 49  ? 0.5586 0.6124 0.5718 0.1418  -0.1648 -0.1489 113 ASN B OD1 
3088  N ND2 . ASN B 49  ? 0.8011 0.8407 0.7938 0.1438  -0.1548 -0.1381 113 ASN B ND2 
3089  N N   . PHE B 50  ? 0.5171 0.5852 0.5847 0.1178  -0.1793 -0.1715 114 PHE B N   
3090  C CA  . PHE B 50  ? 0.5505 0.6268 0.6445 0.1062  -0.1771 -0.1727 114 PHE B CA  
3091  C C   . PHE B 50  ? 0.4915 0.5802 0.6097 0.1045  -0.1811 -0.1757 114 PHE B C   
3092  O O   . PHE B 50  ? 0.5593 0.6504 0.6735 0.1117  -0.1859 -0.1773 114 PHE B O   
3093  C CB  . PHE B 50  ? 0.6997 0.7730 0.7993 0.1036  -0.1833 -0.1789 114 PHE B CB  
3094  C CG  . PHE B 50  ? 0.6054 0.6781 0.7079 0.1111  -0.2000 -0.1900 114 PHE B CG  
3095  C CD1 . PHE B 50  ? 0.6460 0.7073 0.7209 0.1237  -0.2070 -0.1937 114 PHE B CD1 
3096  C CD2 . PHE B 50  ? 0.6078 0.6907 0.7415 0.1063  -0.2089 -0.1964 114 PHE B CD2 
3097  C CE1 . PHE B 50  ? 0.7138 0.7724 0.7889 0.1321  -0.2243 -0.2050 114 PHE B CE1 
3098  C CE2 . PHE B 50  ? 0.5727 0.6539 0.7114 0.1130  -0.2269 -0.2075 114 PHE B CE2 
3099  C CZ  . PHE B 50  ? 0.6088 0.6771 0.7166 0.1262  -0.2354 -0.2125 114 PHE B CZ  
3100  N N   . VAL B 51  ? 0.4237 0.5206 0.5681 0.0953  -0.1779 -0.1753 115 VAL B N   
3101  C CA  . VAL B 51  ? 0.4517 0.5614 0.6221 0.0937  -0.1790 -0.1757 115 VAL B CA  
3102  C C   . VAL B 51  ? 0.4277 0.5447 0.6287 0.0882  -0.1864 -0.1811 115 VAL B C   
3103  O O   . VAL B 51  ? 0.6006 0.7145 0.8057 0.0821  -0.1837 -0.1809 115 VAL B O   
3104  C CB  . VAL B 51  ? 0.4855 0.5987 0.6604 0.0892  -0.1644 -0.1665 115 VAL B CB  
3105  C CG1 . VAL B 51  ? 0.4904 0.6176 0.6940 0.0892  -0.1642 -0.1657 115 VAL B CG1 
3106  C CG2 . VAL B 51  ? 0.4952 0.5994 0.6416 0.0942  -0.1587 -0.1612 115 VAL B CG2 
3107  N N   . SER B 52  ? 0.4902 0.6171 0.7144 0.0905  -0.1963 -0.1858 116 SER B N   
3108  C CA  . SER B 52  ? 0.5000 0.6356 0.7608 0.0849  -0.2043 -0.1900 116 SER B CA  
3109  C C   . SER B 52  ? 0.5668 0.7174 0.8574 0.0858  -0.2050 -0.1877 116 SER B C   
3110  O O   . SER B 52  ? 0.5465 0.6985 0.8260 0.0936  -0.2088 -0.1889 116 SER B O   
3111  C CB  . SER B 52  ? 0.5009 0.6288 0.7574 0.0895  -0.2237 -0.2019 116 SER B CB  
3112  O OG  . SER B 52  ? 0.6189 0.7557 0.9165 0.0838  -0.2337 -0.2061 116 SER B OG  
3113  N N   . CYS B 53  ? 0.5882 0.7506 0.9174 0.0783  -0.2006 -0.1834 117 CYS B N   
3114  C CA  . CYS B 53  ? 0.6969 0.8748 1.0572 0.0795  -0.1982 -0.1785 117 CYS B CA  
3115  C C   . CYS B 53  ? 0.7059 0.8948 1.1105 0.0774  -0.2143 -0.1841 117 CYS B C   
3116  O O   . CYS B 53  ? 0.8480 1.0356 1.2726 0.0713  -0.2220 -0.1882 117 CYS B O   
3117  C CB  . CYS B 53  ? 0.8995 1.0838 1.2705 0.0754  -0.1768 -0.1655 117 CYS B CB  
3118  S SG  . CYS B 53  ? 1.5009 1.6715 1.8225 0.0789  -0.1610 -0.1595 117 CYS B SG  
3119  N N   . SER B 54  ? 0.7799 0.9792 1.2008 0.0828  -0.2204 -0.1845 118 SER B N   
3120  C CA  . SER B 54  ? 0.7720 0.9858 1.2449 0.0803  -0.2328 -0.1862 118 SER B CA  
3121  C C   . SER B 54  ? 0.6571 0.8877 1.1670 0.0764  -0.2142 -0.1714 118 SER B C   
3122  O O   . SER B 54  ? 0.6987 0.9271 1.1897 0.0762  -0.1933 -0.1616 118 SER B O   
3123  C CB  . SER B 54  ? 0.8548 1.0706 1.3272 0.0892  -0.2516 -0.1951 118 SER B CB  
3124  O OG  . SER B 54  ? 0.6721 0.8987 1.1478 0.0946  -0.2422 -0.1876 118 SER B OG  
3125  N N   . ASP B 55  ? 0.9154 1.1619 1.4783 0.0740  -0.2218 -0.1694 119 ASP B N   
3126  C CA  . ASP B 55  ? 0.9219 1.1857 1.5244 0.0721  -0.2032 -0.1535 119 ASP B CA  
3127  C C   . ASP B 55  ? 0.8630 1.1339 1.4549 0.0813  -0.1944 -0.1474 119 ASP B C   
3128  O O   . ASP B 55  ? 1.0453 1.3281 1.6578 0.0832  -0.1758 -0.1332 119 ASP B O   
3129  C CB  . ASP B 55  ? 0.9866 1.2655 1.6554 0.0656  -0.2142 -0.1519 119 ASP B CB  
3130  C CG  . ASP B 55  ? 1.4664 1.7478 2.1528 0.0686  -0.2426 -0.1649 119 ASP B CG  
3131  O OD1 . ASP B 55  ? 1.5414 1.8172 2.1939 0.0772  -0.2499 -0.1720 119 ASP B OD1 
3132  O OD2 . ASP B 55  ? 1.8657 2.1540 2.6014 0.0626  -0.2583 -0.1679 119 ASP B OD2 
3133  N N   . LYS B 56  ? 0.7673 1.0295 1.3248 0.0881  -0.2073 -0.1579 120 LYS B N   
3134  C CA  . LYS B 56  ? 0.7344 1.0011 1.2787 0.0975  -0.2037 -0.1551 120 LYS B CA  
3135  C C   . LYS B 56  ? 0.7203 0.9724 1.2079 0.1026  -0.1895 -0.1528 120 LYS B C   
3136  O O   . LYS B 56  ? 1.2930 1.5485 1.7711 0.1090  -0.1763 -0.1447 120 LYS B O   
3137  C CB  . LYS B 56  ? 0.8471 1.1130 1.3921 0.1025  -0.2290 -0.1684 120 LYS B CB  
3138  C CG  . LYS B 56  ? 1.0024 1.2745 1.5396 0.1126  -0.2296 -0.1671 120 LYS B CG  
3139  C CD  . LYS B 56  ? 1.1561 1.4244 1.6881 0.1186  -0.2562 -0.1818 120 LYS B CD  
3140  C CE  . LYS B 56  ? 1.9105 2.1918 2.5002 0.1146  -0.2760 -0.1862 120 LYS B CE  
3141  N NZ  . LYS B 56  ? 2.0009 2.2736 2.6008 0.1071  -0.2901 -0.1951 120 LYS B NZ  
3142  N N   . GLU B 57  ? 0.5939 0.8293 1.0453 0.1000  -0.1926 -0.1597 121 GLU B N   
3143  C CA  . GLU B 57  ? 0.6014 0.8213 0.9998 0.1051  -0.1859 -0.1605 121 GLU B CA  
3144  C C   . GLU B 57  ? 0.6547 0.8589 1.0254 0.1005  -0.1894 -0.1666 121 GLU B C   
3145  O O   . GLU B 57  ? 0.6977 0.9012 1.0842 0.0956  -0.2015 -0.1735 121 GLU B O   
3146  C CB  . GLU B 57  ? 0.6398 0.8571 1.0185 0.1144  -0.1983 -0.1675 121 GLU B CB  
3147  C CG  . GLU B 57  ? 0.7875 0.9943 1.1499 0.1159  -0.2186 -0.1810 121 GLU B CG  
3148  C CD  . GLU B 57  ? 1.1051 1.3111 1.4561 0.1260  -0.2335 -0.1886 121 GLU B CD  
3149  O OE1 . GLU B 57  ? 1.5595 1.7690 1.9013 0.1323  -0.2266 -0.1837 121 GLU B OE1 
3150  O OE2 . GLU B 57  ? 1.3245 1.5252 1.6741 0.1287  -0.2527 -0.1998 121 GLU B OE2 
3151  N N   . CYS B 58  ? 0.6967 0.8875 1.0263 0.1027  -0.1799 -0.1642 122 CYS B N   
3152  C CA  . CYS B 58  ? 0.5615 0.7373 0.8621 0.0999  -0.1824 -0.1689 122 CYS B CA  
3153  C C   . CYS B 58  ? 0.5778 0.7428 0.8437 0.1080  -0.1917 -0.1752 122 CYS B C   
3154  O O   . CYS B 58  ? 0.6658 0.8305 0.9172 0.1147  -0.1887 -0.1726 122 CYS B O   
3155  C CB  . CYS B 58  ? 0.6326 0.8007 0.9149 0.0963  -0.1650 -0.1605 122 CYS B CB  
3156  S SG  . CYS B 58  ? 1.1457 1.3242 1.4646 0.0884  -0.1527 -0.1523 122 CYS B SG  
3157  N N   . ARG B 59  ? 0.5186 0.6741 0.7706 0.1084  -0.2026 -0.1831 123 ARG B N   
3158  C CA  . ARG B 59  ? 0.5168 0.6614 0.7354 0.1178  -0.2106 -0.1881 123 ARG B CA  
3159  C C   . ARG B 59  ? 0.5647 0.6945 0.7509 0.1171  -0.2038 -0.1858 123 ARG B C   
3160  O O   . ARG B 59  ? 0.5199 0.6473 0.7113 0.1093  -0.1990 -0.1843 123 ARG B O   
3161  C CB  . ARG B 59  ? 0.5609 0.7057 0.7880 0.1231  -0.2311 -0.1996 123 ARG B CB  
3162  C CG  . ARG B 59  ? 0.4988 0.6582 0.7585 0.1251  -0.2399 -0.2019 123 ARG B CG  
3163  C CD  . ARG B 59  ? 0.5402 0.6966 0.8007 0.1333  -0.2627 -0.2143 123 ARG B CD  
3164  N NE  . ARG B 59  ? 0.5536 0.6988 0.7744 0.1459  -0.2667 -0.2173 123 ARG B NE  
3165  C CZ  . ARG B 59  ? 0.5061 0.6555 0.7198 0.1524  -0.2634 -0.2139 123 ARG B CZ  
3166  N NH1 . ARG B 59  ? 0.6039 0.7683 0.8466 0.1479  -0.2565 -0.2079 123 ARG B NH1 
3167  N NH2 . ARG B 59  ? 0.5313 0.6696 0.7092 0.1641  -0.2666 -0.2160 123 ARG B NH2 
3168  N N   . ARG B 60  ? 0.5286 0.6490 0.6832 0.1252  -0.2028 -0.1844 124 ARG B N   
3169  C CA  . ARG B 60  ? 0.5593 0.6658 0.6848 0.1257  -0.1965 -0.1808 124 ARG B CA  
3170  C C   . ARG B 60  ? 0.5575 0.6546 0.6627 0.1355  -0.2083 -0.1879 124 ARG B C   
3171  O O   . ARG B 60  ? 0.8093 0.9044 0.9014 0.1460  -0.2149 -0.1905 124 ARG B O   
3172  C CB  . ARG B 60  ? 0.4894 0.5907 0.5957 0.1278  -0.1854 -0.1721 124 ARG B CB  
3173  C CG  . ARG B 60  ? 0.5532 0.6409 0.6292 0.1334  -0.1827 -0.1685 124 ARG B CG  
3174  C CD  . ARG B 60  ? 0.6025 0.6852 0.6676 0.1323  -0.1717 -0.1591 124 ARG B CD  
3175  N NE  . ARG B 60  ? 0.7166 0.7873 0.7572 0.1377  -0.1683 -0.1534 124 ARG B NE  
3176  C CZ  . ARG B 60  ? 0.8419 0.9068 0.8709 0.1409  -0.1630 -0.1462 124 ARG B CZ  
3177  N NH1 . ARG B 60  ? 0.7849 0.8539 0.8213 0.1398  -0.1613 -0.1451 124 ARG B NH1 
3178  N NH2 . ARG B 60  ? 0.8249 0.8796 0.8359 0.1458  -0.1592 -0.1395 124 ARG B NH2 
3179  N N   . PHE B 61  ? 0.4540 0.5448 0.5557 0.1334  -0.2114 -0.1913 125 PHE B N   
3180  C CA  . PHE B 61  ? 0.5037 0.5830 0.5817 0.1452  -0.2223 -0.1978 125 PHE B CA  
3181  C C   . PHE B 61  ? 0.5583 0.6255 0.6049 0.1500  -0.2113 -0.1896 125 PHE B C   
3182  O O   . PHE B 61  ? 0.6356 0.7024 0.6834 0.1412  -0.1981 -0.1810 125 PHE B O   
3183  C CB  . PHE B 61  ? 0.4294 0.5067 0.5194 0.1427  -0.2338 -0.2070 125 PHE B CB  
3184  C CG  . PHE B 61  ? 0.4175 0.5056 0.5402 0.1400  -0.2479 -0.2155 125 PHE B CG  
3185  C CD1 . PHE B 61  ? 0.4174 0.5200 0.5746 0.1280  -0.2412 -0.2112 125 PHE B CD1 
3186  C CD2 . PHE B 61  ? 0.4482 0.5315 0.5676 0.1507  -0.2679 -0.2271 125 PHE B CD2 
3187  C CE1 . PHE B 61  ? 0.5072 0.6214 0.6997 0.1254  -0.2530 -0.2171 125 PHE B CE1 
3188  C CE2 . PHE B 61  ? 0.5008 0.5946 0.6549 0.1478  -0.2823 -0.2347 125 PHE B CE2 
3189  C CZ  . PHE B 61  ? 0.5352 0.6455 0.7283 0.1346  -0.2745 -0.2290 125 PHE B CZ  
3190  N N   . PHE B 62  ? 0.5312 0.5883 0.5504 0.1647  -0.2166 -0.1913 126 PHE B N   
3191  C CA  . PHE B 62  ? 0.6698 0.7154 0.6616 0.1705  -0.2056 -0.1820 126 PHE B CA  
3192  C C   . PHE B 62  ? 0.6419 0.6747 0.6037 0.1888  -0.2133 -0.1859 126 PHE B C   
3193  O O   . PHE B 62  ? 0.7467 0.7784 0.7074 0.1970  -0.2290 -0.1971 126 PHE B O   
3194  C CB  . PHE B 62  ? 0.5763 0.6236 0.5649 0.1684  -0.1926 -0.1704 126 PHE B CB  
3195  C CG  . PHE B 62  ? 0.5665 0.6159 0.5499 0.1773  -0.1976 -0.1720 126 PHE B CG  
3196  C CD1 . PHE B 62  ? 0.6964 0.7361 0.6526 0.1929  -0.1977 -0.1690 126 PHE B CD1 
3197  C CD2 . PHE B 62  ? 0.6474 0.7087 0.6532 0.1715  -0.2019 -0.1761 126 PHE B CD2 
3198  C CE1 . PHE B 62  ? 0.8787 0.9201 0.8293 0.2019  -0.2024 -0.1705 126 PHE B CE1 
3199  C CE2 . PHE B 62  ? 0.6686 0.7323 0.6700 0.1803  -0.2069 -0.1778 126 PHE B CE2 
3200  C CZ  . PHE B 62  ? 0.7952 0.8488 0.7686 0.1953  -0.2076 -0.1754 126 PHE B CZ  
3201  N N   . VAL B 63  ? 0.6055 0.6280 0.5432 0.1960  -0.2025 -0.1762 127 VAL B N   
3202  C CA  . VAL B 63  ? 0.6318 0.6404 0.5370 0.2158  -0.2065 -0.1773 127 VAL B CA  
3203  C C   . VAL B 63  ? 0.6381 0.6433 0.5264 0.2249  -0.1951 -0.1649 127 VAL B C   
3204  O O   . VAL B 63  ? 0.7777 0.7847 0.6717 0.2171  -0.1804 -0.1520 127 VAL B O   
3205  C CB  . VAL B 63  ? 0.6616 0.6605 0.5538 0.2179  -0.2021 -0.1750 127 VAL B CB  
3206  C CG1 . VAL B 63  ? 0.7847 0.7682 0.6396 0.2399  -0.1993 -0.1703 127 VAL B CG1 
3207  C CG2 . VAL B 63  ? 0.6420 0.6412 0.5469 0.2128  -0.2168 -0.1892 127 VAL B CG2 
3208  N N   . SER B 64  ? 0.6676 0.6673 0.5365 0.2418  -0.2027 -0.1686 128 SER B N   
3209  C CA  . SER B 64  ? 0.7529 0.7495 0.6068 0.2516  -0.1928 -0.1572 128 SER B CA  
3210  C C   . SER B 64  ? 0.8766 0.8609 0.7053 0.2642  -0.1792 -0.1437 128 SER B C   
3211  O O   . SER B 64  ? 1.0451 1.0191 0.8539 0.2755  -0.1820 -0.1467 128 SER B O   
3212  C CB  . SER B 64  ? 0.8565 0.8505 0.6962 0.2671  -0.2057 -0.1659 128 SER B CB  
3213  O OG  . SER B 64  ? 1.2242 1.2038 1.0333 0.2872  -0.2140 -0.1719 128 SER B OG  
3214  N N   . MET B 65  ? 0.9224 0.9074 0.7531 0.2627  -0.1643 -0.1281 129 MET B N   
3215  C CA  . MET B 65  ? 1.0445 1.0185 0.8528 0.2778  -0.1503 -0.1127 129 MET B CA  
3216  C C   . MET B 65  ? 0.9301 0.8990 0.7196 0.2952  -0.1487 -0.1076 129 MET B C   
3217  O O   . MET B 65  ? 1.2524 1.2132 1.0258 0.3085  -0.1353 -0.0924 129 MET B O   
3218  C CB  . MET B 65  ? 1.0196 0.9965 0.8458 0.2646  -0.1338 -0.0962 129 MET B CB  
3219  C CG  . MET B 65  ? 0.9105 0.8846 0.7376 0.2602  -0.1291 -0.0941 129 MET B CG  
3220  S SD  . MET B 65  ? 1.4315 1.4172 1.2942 0.2319  -0.1292 -0.0969 129 MET B SD  
3221  C CE  . MET B 65  ? 1.1855 1.1730 1.0662 0.2228  -0.1135 -0.0767 129 MET B CE  
3222  N N   . GLY B 66  ? 0.8575 0.8312 0.6496 0.2959  -0.1618 -0.1196 130 GLY B N   
3223  C CA  . GLY B 66  ? 0.9369 0.9076 0.7156 0.3095  -0.1602 -0.1148 130 GLY B CA  
3224  C C   . GLY B 66  ? 1.0237 1.0043 0.8273 0.2944  -0.1547 -0.1084 130 GLY B C   
3225  O O   . GLY B 66  ? 0.9982 0.9867 0.8278 0.2743  -0.1513 -0.1067 130 GLY B O   
3226  N N   . TYR B 67  ? 0.9860 0.9648 0.7801 0.3049  -0.1546 -0.1054 131 TYR B N   
3227  C CA  . TYR B 67  ? 1.0434 1.0290 0.8575 0.2933  -0.1500 -0.0993 131 TYR B CA  
3228  C C   . TYR B 67  ? 1.2006 1.1815 1.0207 0.2904  -0.1326 -0.0792 131 TYR B C   
3229  O O   . TYR B 67  ? 1.1405 1.1123 0.9435 0.3045  -0.1223 -0.0672 131 TYR B O   
3230  C CB  . TYR B 67  ? 1.1196 1.1046 0.9218 0.3060  -0.1562 -0.1031 131 TYR B CB  
3231  C CG  . TYR B 67  ? 1.0719 1.0617 0.8713 0.3096  -0.1749 -0.1224 131 TYR B CG  
3232  C CD1 . TYR B 67  ? 0.9245 0.9272 0.7507 0.2927  -0.1842 -0.1333 131 TYR B CD1 
3233  C CD2 . TYR B 67  ? 1.1489 1.1297 0.9196 0.3311  -0.1835 -0.1290 131 TYR B CD2 
3234  C CE1 . TYR B 67  ? 1.0176 1.0256 0.8463 0.2959  -0.2017 -0.1498 131 TYR B CE1 
3235  C CE2 . TYR B 67  ? 1.1824 1.1668 0.9530 0.3348  -0.2030 -0.1470 131 TYR B CE2 
3236  C CZ  . TYR B 67  ? 1.1951 1.1938 0.9969 0.3165  -0.2121 -0.1570 131 TYR B CZ  
3237  O OH  . TYR B 67  ? 1.2924 1.2953 1.0985 0.3203  -0.2318 -0.1736 131 TYR B OH  
3238  N N   . GLY B 68  ? 1.1654 1.1520 1.0106 0.2728  -0.1296 -0.0752 132 GLY B N   
3239  C CA  . GLY B 68  ? 1.2996 1.2819 1.1570 0.2669  -0.1159 -0.0572 132 GLY B CA  
3240  C C   . GLY B 68  ? 1.3401 1.3147 1.1868 0.2815  -0.1066 -0.0426 132 GLY B C   
3241  O O   . GLY B 68  ? 1.6278 1.5971 1.4808 0.2828  -0.0937 -0.0250 132 GLY B O   
3242  N N   . THR B 69  ? 1.3184 1.2929 1.1508 0.2928  -0.1132 -0.0494 133 THR B N   
3243  C CA  . THR B 69  ? 1.5113 1.4788 1.3338 0.3068  -0.1051 -0.0364 133 THR B CA  
3244  C C   . THR B 69  ? 1.3421 1.3006 1.1351 0.3307  -0.0983 -0.0295 133 THR B C   
3245  O O   . THR B 69  ? 1.5243 1.4754 1.3117 0.3425  -0.0851 -0.0118 133 THR B O   
3246  C CB  . THR B 69  ? 1.3384 1.3093 1.1596 0.3081  -0.1145 -0.0455 133 THR B CB  
3247  O OG1 . THR B 69  ? 1.6302 1.5932 1.4383 0.3242  -0.1063 -0.0329 133 THR B OG1 
3248  C CG2 . THR B 69  ? 1.1819 1.1582 0.9896 0.3138  -0.1298 -0.0656 133 THR B CG2 
3249  N N   . THR B 70  ? 1.4676 1.4259 1.2422 0.3384  -0.1073 -0.0432 134 THR B N   
3250  C CA  . THR B 70  ? 1.7303 1.6777 1.4707 0.3639  -0.1037 -0.0400 134 THR B CA  
3251  C C   . THR B 70  ? 1.5982 1.5410 1.3359 0.3656  -0.0928 -0.0301 134 THR B C   
3252  O O   . THR B 70  ? 1.5832 1.5155 1.2914 0.3876  -0.0877 -0.0257 134 THR B O   
3253  C CB  . THR B 70  ? 1.7173 1.6640 1.4360 0.3743  -0.1224 -0.0616 134 THR B CB  
3254  O OG1 . THR B 70  ? 2.3396 2.2897 2.0644 0.3642  -0.1309 -0.0736 134 THR B OG1 
3255  C CG2 . THR B 70  ? 1.4637 1.4191 1.1941 0.3665  -0.1354 -0.0739 134 THR B CG2 
3256  N N   . THR B 71  ? 1.4827 1.4326 1.2498 0.3436  -0.0895 -0.0269 135 THR B N   
3257  C CA  . THR B 71  ? 1.5176 1.4647 1.2874 0.3423  -0.0792 -0.0171 135 THR B CA  
3258  C C   . THR B 71  ? 1.6056 1.5514 1.3955 0.3387  -0.0611 0.0074  135 THR B C   
3259  O O   . THR B 71  ? 1.5111 1.4622 1.3289 0.3217  -0.0614 0.0111  135 THR B O   
3260  C CB  . THR B 71  ? 1.5787 1.5343 1.3683 0.3203  -0.0887 -0.0304 135 THR B CB  
3261  O OG1 . THR B 71  ? 1.3274 1.2836 1.1008 0.3247  -0.1051 -0.0515 135 THR B OG1 
3262  C CG2 . THR B 71  ? 1.6081 1.5616 1.4038 0.3172  -0.0772 -0.0189 135 THR B CG2 
3263  N N   . ASN B 72  ? 1.6729 1.6108 1.4490 0.3558  -0.0457 0.0244  136 ASN B N   
3264  C CA  . ASN B 72  ? 2.0326 1.9699 1.8325 0.3523  -0.0280 0.0493  136 ASN B CA  
3265  C C   . ASN B 72  ? 2.2581 2.1990 2.0771 0.3388  -0.0233 0.0540  136 ASN B C   
3266  O O   . ASN B 72  ? 1.9713 1.9107 1.7724 0.3434  -0.0272 0.0440  136 ASN B O   
3267  C CB  . ASN B 72  ? 1.8805 1.8078 1.6587 0.3797  -0.0110 0.0693  136 ASN B CB  
3268  C CG  . ASN B 72  ? 2.2514 2.1791 2.0605 0.3757  0.0062  0.0960  136 ASN B CG  
3269  O OD1 . ASN B 72  ? 2.6547 2.5884 2.4988 0.3535  0.0020  0.0974  136 ASN B OD1 
3270  N ND2 . ASN B 72  ? 2.3947 2.3149 2.1914 0.3979  0.0253  0.1180  136 ASN B ND2 
3271  N N   . PHE B 73  ? 2.4396 2.3844 2.2948 0.3226  -0.0161 0.0687  137 PHE B N   
3272  C CA  . PHE B 73  ? 2.1649 2.1140 2.0436 0.3068  -0.0132 0.0730  137 PHE B CA  
3273  C C   . PHE B 73  ? 2.1894 2.1341 2.0545 0.3223  0.0013  0.0862  137 PHE B C   
3274  O O   . PHE B 73  ? 1.6110 1.5581 1.4763 0.3152  -0.0017 0.0791  137 PHE B O   
3275  C CB  . PHE B 73  ? 2.0381 1.9902 1.9589 0.2885  -0.0097 0.0873  137 PHE B CB  
3276  C CG  . PHE B 73  ? 2.0675 2.0238 2.0135 0.2723  -0.0082 0.0913  137 PHE B CG  
3277  C CD1 . PHE B 73  ? 2.3210 2.2824 2.2713 0.2544  -0.0223 0.0716  137 PHE B CD1 
3278  C CD2 . PHE B 73  ? 1.6939 1.6491 1.6601 0.2754  0.0078  0.1156  137 PHE B CD2 
3279  C CE1 . PHE B 73  ? 2.0452 2.0098 2.0172 0.2402  -0.0212 0.0750  137 PHE B CE1 
3280  C CE2 . PHE B 73  ? 1.7783 1.7374 1.7683 0.2607  0.0085  0.1193  137 PHE B CE2 
3281  C CZ  . PHE B 73  ? 1.8357 1.7991 1.8272 0.2432  -0.0064 0.0984  137 PHE B CZ  
3282  N N   . ALA B 74  ? 2.5710 2.5090 2.4243 0.3443  0.0176  0.1063  138 ALA B N   
3283  C CA  . ALA B 74  ? 2.3195 2.2521 2.1589 0.3631  0.0350  0.1232  138 ALA B CA  
3284  C C   . ALA B 74  ? 2.4967 2.4237 2.2962 0.3764  0.0280  0.1059  138 ALA B C   
3285  O O   . ALA B 74  ? 2.6802 2.6043 2.4725 0.3843  0.0379  0.1142  138 ALA B O   
3286  C CB  . ALA B 74  ? 1.4919 1.4174 1.3224 0.3873  0.0541  0.1476  138 ALA B CB  
3287  N N   . ASP B 75  ? 2.6392 2.5642 2.4142 0.3790  0.0104  0.0822  139 ASP B N   
3288  C CA  . ASP B 75  ? 2.1665 2.0861 1.9083 0.3879  -0.0016 0.0618  139 ASP B CA  
3289  C C   . ASP B 75  ? 1.9566 1.8843 1.7190 0.3638  -0.0121 0.0482  139 ASP B C   
3290  O O   . ASP B 75  ? 2.0013 1.9391 1.7951 0.3392  -0.0201 0.0421  139 ASP B O   
3291  C CB  . ASP B 75  ? 2.0261 1.9428 1.7439 0.3947  -0.0197 0.0402  139 ASP B CB  
3292  C CG  . ASP B 75  ? 2.2157 2.1217 1.9030 0.4231  -0.0117 0.0498  139 ASP B CG  
3293  O OD1 . ASP B 75  ? 2.4945 2.3932 2.1711 0.4421  0.0082  0.0720  139 ASP B OD1 
3294  O OD2 . ASP B 75  ? 2.3648 2.2698 2.0389 0.4272  -0.0249 0.0356  139 ASP B OD2 
3295  N N   . LEU B 76  ? 2.1028 2.0249 1.8459 0.3721  -0.0118 0.0439  140 LEU B N   
3296  C CA  . LEU B 76  ? 2.3450 2.2724 2.0974 0.3536  -0.0258 0.0252  140 LEU B CA  
3297  C C   . LEU B 76  ? 2.0337 1.9536 1.7519 0.3665  -0.0434 0.0023  140 LEU B C   
3298  O O   . LEU B 76  ? 1.6956 1.6024 1.3768 0.3936  -0.0403 0.0045  140 LEU B O   
3299  C CB  . LEU B 76  ? 2.5399 2.4660 2.2961 0.3532  -0.0147 0.0354  140 LEU B CB  
3300  C CG  . LEU B 76  ? 2.4322 2.3685 2.2312 0.3318  -0.0042 0.0515  140 LEU B CG  
3301  C CD1 . LEU B 76  ? 2.1536 2.0901 1.9687 0.3390  0.0144  0.0787  140 LEU B CD1 
3302  C CD2 . LEU B 76  ? 2.0483 1.9843 1.8498 0.3285  0.0010  0.0542  140 LEU B CD2 
3303  N N   . ILE B 77  ? 2.2817 2.2091 2.0128 0.3483  -0.0622 -0.0189 141 ILE B N   
3304  C CA  . ILE B 77  ? 2.0656 1.9870 1.7713 0.3580  -0.0816 -0.0416 141 ILE B CA  
3305  C C   . ILE B 77  ? 1.6207 1.5389 1.3205 0.3541  -0.0915 -0.0556 141 ILE B C   
3306  O O   . ILE B 77  ? 1.5203 1.4452 1.2428 0.3367  -0.0867 -0.0522 141 ILE B O   
3307  C CB  . ILE B 77  ? 2.2104 2.1410 1.9314 0.3453  -0.0970 -0.0563 141 ILE B CB  
3308  C CG1 . ILE B 77  ? 1.7994 1.7217 1.4916 0.3613  -0.1160 -0.0761 141 ILE B CG1 
3309  C CG2 . ILE B 77  ? 2.3086 2.2532 2.0669 0.3153  -0.1034 -0.0643 141 ILE B CG2 
3310  C CD1 . ILE B 77  ? 1.5940 1.5198 1.2863 0.3639  -0.1247 -0.0823 141 ILE B CD1 
3311  N N   . VAL B 78  ? 1.2506 1.1578 0.9200 0.3707  -0.1067 -0.0720 142 VAL B N   
3312  C CA  . VAL B 78  ? 1.2506 1.1481 0.9025 0.3771  -0.1138 -0.0819 142 VAL B CA  
3313  C C   . VAL B 78  ? 1.2149 1.1133 0.8703 0.3691  -0.1396 -0.1080 142 VAL B C   
3314  O O   . VAL B 78  ? 1.2143 1.1129 0.8652 0.3737  -0.1531 -0.1190 142 VAL B O   
3315  C CB  . VAL B 78  ? 1.2648 1.1425 0.8701 0.4112  -0.1064 -0.0741 142 VAL B CB  
3316  C CG1 . VAL B 78  ? 1.1316 1.0001 0.7088 0.4319  -0.1171 -0.0821 142 VAL B CG1 
3317  C CG2 . VAL B 78  ? 1.5116 1.3766 1.0951 0.4201  -0.1133 -0.0836 142 VAL B CG2 
3318  N N   . SER B 79  ? 1.2657 1.1646 0.9310 0.3575  -0.1460 -0.1169 143 SER B N   
3319  C CA  . SER B 79  ? 1.2041 1.1054 0.8813 0.3465  -0.1694 -0.1399 143 SER B CA  
3320  C C   . SER B 79  ? 1.1846 1.0740 0.8362 0.3653  -0.1911 -0.1575 143 SER B C   
3321  O O   . SER B 79  ? 1.1521 1.0494 0.8240 0.3540  -0.2092 -0.1732 143 SER B O   
3322  C CB  . SER B 79  ? 1.1843 1.0811 0.8632 0.3405  -0.1713 -0.1447 143 SER B CB  
3323  O OG  . SER B 79  ? 1.3891 1.2956 1.0896 0.3251  -0.1519 -0.1284 143 SER B OG  
3324  N N   . GLU B 80  ? 1.0842 0.9544 0.6918 0.3949  -0.1895 -0.1546 144 GLU B N   
3325  C CA  . GLU B 80  ? 1.2918 1.1477 0.8714 0.4151  -0.2120 -0.1722 144 GLU B CA  
3326  C C   . GLU B 80  ? 1.2784 1.1436 0.8685 0.4132  -0.2180 -0.1749 144 GLU B C   
3327  O O   . GLU B 80  ? 1.3295 1.1885 0.9104 0.4220  -0.2404 -0.1923 144 GLU B O   
3328  C CB  . GLU B 80  ? 1.3530 1.1839 0.8779 0.4507  -0.2083 -0.1679 144 GLU B CB  
3329  C CG  . GLU B 80  ? 1.6931 1.5100 1.2001 0.4576  -0.2089 -0.1707 144 GLU B CG  
3330  C CD  . GLU B 80  ? 2.0656 1.8937 1.5943 0.4416  -0.1840 -0.1514 144 GLU B CD  
3331  O OE1 . GLU B 80  ? 2.2745 2.1149 1.8189 0.4348  -0.1627 -0.1317 144 GLU B OE1 
3332  O OE2 . GLU B 80  ? 2.1597 1.9837 1.6906 0.4358  -0.1867 -0.1562 144 GLU B OE2 
3333  N N   . GLN B 81  ? 1.1774 1.0568 0.7875 0.4020  -0.1990 -0.1580 145 GLN B N   
3334  C CA  . GLN B 81  ? 1.1206 1.0078 0.7378 0.4019  -0.2016 -0.1579 145 GLN B CA  
3335  C C   . GLN B 81  ? 1.0273 0.9347 0.6902 0.3729  -0.2114 -0.1675 145 GLN B C   
3336  O O   . GLN B 81  ? 1.0165 0.9321 0.6905 0.3699  -0.2175 -0.1711 145 GLN B O   
3337  C CB  . GLN B 81  ? 1.2448 1.1344 0.8580 0.4073  -0.1763 -0.1340 145 GLN B CB  
3338  C CG  . GLN B 81  ? 1.4089 1.2788 0.9760 0.4398  -0.1644 -0.1218 145 GLN B CG  
3339  C CD  . GLN B 81  ? 1.6834 1.5560 1.2493 0.4470  -0.1422 -0.0991 145 GLN B CD  
3340  O OE1 . GLN B 81  ? 1.9745 1.8573 1.5658 0.4323  -0.1232 -0.0813 145 GLN B OE1 
3341  N NE2 . GLN B 81  ? 1.6349 1.4976 1.1718 0.4699  -0.1456 -0.0997 145 GLN B NE2 
3342  N N   . MET B 82  ? 0.9419 0.8567 0.6302 0.3530  -0.2130 -0.1717 146 MET B N   
3343  C CA  . MET B 82  ? 0.8615 0.7958 0.5938 0.3254  -0.2164 -0.1761 146 MET B CA  
3344  C C   . MET B 82  ? 0.9297 0.8678 0.6775 0.3204  -0.2412 -0.1968 146 MET B C   
3345  O O   . MET B 82  ? 1.0490 0.9748 0.7819 0.3308  -0.2578 -0.2103 146 MET B O   
3346  C CB  . MET B 82  ? 0.8228 0.7636 0.5763 0.3066  -0.2048 -0.1692 146 MET B CB  
3347  C CG  . MET B 82  ? 0.9392 0.8816 0.6917 0.3050  -0.1807 -0.1476 146 MET B CG  
3348  S SD  . MET B 82  ? 1.1117 1.0590 0.8843 0.2864  -0.1681 -0.1395 146 MET B SD  
3349  C CE  . MET B 82  ? 0.9591 0.9103 0.7378 0.2842  -0.1437 -0.1146 146 MET B CE  
3350  N N   . ASN B 83  ? 0.8316 0.7863 0.6110 0.3043  -0.2435 -0.1986 147 ASN B N   
3351  C CA  . ASN B 83  ? 0.8912 0.8540 0.6947 0.2970  -0.2649 -0.2154 147 ASN B CA  
3352  C C   . ASN B 83  ? 0.8889 0.8707 0.7370 0.2703  -0.2615 -0.2149 147 ASN B C   
3353  O O   . ASN B 83  ? 1.0820 1.0726 0.9418 0.2584  -0.2435 -0.2018 147 ASN B O   
3354  C CB  . ASN B 83  ? 0.8642 0.8290 0.6615 0.3075  -0.2721 -0.2182 147 ASN B CB  
3355  C CG  . ASN B 83  ? 0.9528 0.8982 0.7075 0.3356  -0.2820 -0.2235 147 ASN B CG  
3356  O OD1 . ASN B 83  ? 1.1934 1.1252 0.9317 0.3463  -0.2965 -0.2347 147 ASN B OD1 
3357  N ND2 . ASN B 83  ? 1.0900 1.0325 0.8246 0.3491  -0.2744 -0.2154 147 ASN B ND2 
3358  N N   . VAL B 84  ? 0.7820 0.7696 0.6556 0.2618  -0.2790 -0.2288 148 VAL B N   
3359  C CA  . VAL B 84  ? 0.7294 0.7351 0.6460 0.2380  -0.2751 -0.2277 148 VAL B CA  
3360  C C   . VAL B 84  ? 0.6979 0.7183 0.6397 0.2325  -0.2807 -0.2304 148 VAL B C   
3361  O O   . VAL B 84  ? 0.6369 0.6581 0.5875 0.2382  -0.3005 -0.2428 148 VAL B O   
3362  C CB  . VAL B 84  ? 0.6393 0.6452 0.5769 0.2285  -0.2867 -0.2378 148 VAL B CB  
3363  C CG1 . VAL B 84  ? 0.5661 0.5902 0.5457 0.2057  -0.2788 -0.2337 148 VAL B CG1 
3364  C CG2 . VAL B 84  ? 0.6375 0.6292 0.5507 0.2336  -0.2803 -0.2347 148 VAL B CG2 
3365  N N   . TYR B 85  ? 0.6222 0.6535 0.5763 0.2217  -0.2641 -0.2187 149 TYR B N   
3366  C CA  . TYR B 85  ? 0.5998 0.6455 0.5780 0.2156  -0.2657 -0.2190 149 TYR B CA  
3367  C C   . TYR B 85  ? 0.5615 0.6226 0.5782 0.1956  -0.2597 -0.2165 149 TYR B C   
3368  O O   . TYR B 85  ? 0.7039 0.7652 0.7269 0.1849  -0.2495 -0.2114 149 TYR B O   
3369  C CB  . TYR B 85  ? 0.6161 0.6607 0.5764 0.2211  -0.2522 -0.2078 149 TYR B CB  
3370  C CG  . TYR B 85  ? 0.6712 0.7032 0.5971 0.2425  -0.2584 -0.2097 149 TYR B CG  
3371  C CD1 . TYR B 85  ? 0.6424 0.6770 0.5693 0.2520  -0.2728 -0.2182 149 TYR B CD1 
3372  C CD2 . TYR B 85  ? 0.6420 0.6593 0.5345 0.2543  -0.2491 -0.2021 149 TYR B CD2 
3373  C CE1 . TYR B 85  ? 0.6908 0.7127 0.5837 0.2731  -0.2783 -0.2198 149 TYR B CE1 
3374  C CE2 . TYR B 85  ? 0.7087 0.7136 0.5678 0.2757  -0.2528 -0.2023 149 TYR B CE2 
3375  C CZ  . TYR B 85  ? 0.7689 0.7757 0.6271 0.2853  -0.2678 -0.2117 149 TYR B CZ  
3376  O OH  . TYR B 85  ? 0.9057 0.8992 0.7288 0.3082  -0.2720 -0.2123 149 TYR B OH  
3377  N N   . SER B 86  ? 0.5927 0.6668 0.6346 0.1920  -0.2652 -0.2194 150 SER B N   
3378  C CA  . SER B 86  ? 0.6761 0.7654 0.7539 0.1760  -0.2581 -0.2155 150 SER B CA  
3379  C C   . SER B 86  ? 0.6125 0.7097 0.6928 0.1764  -0.2492 -0.2083 150 SER B C   
3380  O O   . SER B 86  ? 0.7404 0.8335 0.8016 0.1883  -0.2530 -0.2090 150 SER B O   
3381  C CB  . SER B 86  ? 0.8007 0.8987 0.9125 0.1719  -0.2749 -0.2259 150 SER B CB  
3382  O OG  . SER B 86  ? 1.2661 1.3800 1.4152 0.1585  -0.2676 -0.2212 150 SER B OG  
3383  N N   . VAL B 87  ? 0.5630 0.6704 0.6651 0.1644  -0.2374 -0.2013 151 VAL B N   
3384  C CA  . VAL B 87  ? 0.6208 0.7353 0.7272 0.1644  -0.2289 -0.1947 151 VAL B CA  
3385  C C   . VAL B 87  ? 0.6534 0.7809 0.7934 0.1519  -0.2213 -0.1908 151 VAL B C   
3386  O O   . VAL B 87  ? 0.7085 0.8367 0.8616 0.1431  -0.2193 -0.1912 151 VAL B O   
3387  C CB  . VAL B 87  ? 0.5935 0.6971 0.6699 0.1671  -0.2154 -0.1852 151 VAL B CB  
3388  C CG1 . VAL B 87  ? 0.6894 0.7906 0.7686 0.1557  -0.2021 -0.1778 151 VAL B CG1 
3389  C CG2 . VAL B 87  ? 0.5678 0.6755 0.6437 0.1706  -0.2110 -0.1807 151 VAL B CG2 
3390  N N   . LYS B 88  ? 0.5745 0.7115 0.7277 0.1519  -0.2161 -0.1865 152 LYS B N   
3391  C CA  . LYS B 88  ? 0.5990 0.7477 0.7829 0.1425  -0.2075 -0.1816 152 LYS B CA  
3392  C C   . LYS B 88  ? 0.6040 0.7450 0.7718 0.1376  -0.1912 -0.1727 152 LYS B C   
3393  O O   . LYS B 88  ? 0.8475 0.9804 0.9914 0.1425  -0.1861 -0.1686 152 LYS B O   
3394  C CB  . LYS B 88  ? 0.7974 0.9593 1.0023 0.1460  -0.2075 -0.1796 152 LYS B CB  
3395  C CG  . LYS B 88  ? 0.9989 1.1745 1.2403 0.1384  -0.1994 -0.1741 152 LYS B CG  
3396  C CD  . LYS B 88  ? 1.2363 1.4205 1.4863 0.1427  -0.1901 -0.1668 152 LYS B CD  
3397  C CE  . LYS B 88  ? 1.3582 1.5325 1.5842 0.1421  -0.1735 -0.1583 152 LYS B CE  
3398  N NZ  . LYS B 88  ? 1.8110 1.9896 2.0372 0.1489  -0.1653 -0.1519 152 LYS B NZ  
3399  N N   . LEU B 89  ? 0.6214 0.7638 0.8022 0.1284  -0.1840 -0.1697 153 LEU B N   
3400  C CA  . LEU B 89  ? 0.6350 0.7679 0.7987 0.1242  -0.1703 -0.1621 153 LEU B CA  
3401  C C   . LEU B 89  ? 0.7745 0.9074 0.9321 0.1282  -0.1614 -0.1556 153 LEU B C   
3402  O O   . LEU B 89  ? 0.8730 1.0169 1.0520 0.1289  -0.1577 -0.1530 153 LEU B O   
3403  C CB  . LEU B 89  ? 0.5086 0.6443 0.6895 0.1147  -0.1636 -0.1597 153 LEU B CB  
3404  C CG  . LEU B 89  ? 0.4922 0.6180 0.6571 0.1109  -0.1503 -0.1522 153 LEU B CG  
3405  C CD1 . LEU B 89  ? 0.4828 0.5935 0.6176 0.1114  -0.1506 -0.1514 153 LEU B CD1 
3406  C CD2 . LEU B 89  ? 0.3862 0.5159 0.5697 0.1028  -0.1436 -0.1497 153 LEU B CD2 
3407  N N   . GLY B 90  ? 0.6742 0.7941 0.8036 0.1315  -0.1580 -0.1523 154 GLY B N   
3408  C CA  . GLY B 90  ? 0.6899 0.8069 0.8102 0.1369  -0.1523 -0.1474 154 GLY B CA  
3409  C C   . GLY B 90  ? 0.8340 0.9480 0.9393 0.1456  -0.1590 -0.1495 154 GLY B C   
3410  O O   . GLY B 90  ? 1.2944 1.4022 1.3864 0.1506  -0.1554 -0.1456 154 GLY B O   
3411  N N   . ASP B 91  ? 0.8247 0.9420 0.9310 0.1485  -0.1693 -0.1557 155 ASP B N   
3412  C CA  . ASP B 91  ? 0.7863 0.8990 0.8749 0.1581  -0.1756 -0.1574 155 ASP B CA  
3413  C C   . ASP B 91  ? 0.8412 0.9397 0.9053 0.1589  -0.1749 -0.1553 155 ASP B C   
3414  O O   . ASP B 91  ? 0.8549 0.9504 0.9197 0.1529  -0.1738 -0.1556 155 ASP B O   
3415  C CB  . ASP B 91  ? 0.9242 1.0475 1.0262 0.1637  -0.1882 -0.1654 155 ASP B CB  
3416  C CG  . ASP B 91  ? 1.1471 1.2844 1.2722 0.1659  -0.1885 -0.1653 155 ASP B CG  
3417  O OD1 . ASP B 91  ? 1.2205 1.3572 1.3440 0.1660  -0.1786 -0.1589 155 ASP B OD1 
3418  O OD2 . ASP B 91  ? 1.0067 1.1551 1.1520 0.1682  -0.1992 -0.1715 155 ASP B OD2 
3419  N N   . PRO B 92  ? 0.8272 0.9169 0.8709 0.1665  -0.1744 -0.1518 156 PRO B N   
3420  C CA  . PRO B 92  ? 0.7577 0.8349 0.7805 0.1692  -0.1728 -0.1478 156 PRO B CA  
3421  C C   . PRO B 92  ? 0.7237 0.8010 0.7374 0.1784  -0.1818 -0.1534 156 PRO B C   
3422  O O   . PRO B 92  ? 0.7878 0.8719 0.8054 0.1854  -0.1899 -0.1594 156 PRO B O   
3423  C CB  . PRO B 92  ? 0.7104 0.7790 0.7197 0.1739  -0.1684 -0.1409 156 PRO B CB  
3424  C CG  . PRO B 92  ? 0.8247 0.9021 0.8412 0.1793  -0.1724 -0.1448 156 PRO B CG  
3425  C CD  . PRO B 92  ? 0.8984 0.9883 0.9386 0.1722  -0.1728 -0.1492 156 PRO B CD  
3426  N N   . PRO B 93  ? 0.7968 0.8658 0.7975 0.1796  -0.1806 -0.1516 157 PRO B N   
3427  C CA  . PRO B 93  ? 0.7461 0.8116 0.7320 0.1913  -0.1887 -0.1564 157 PRO B CA  
3428  C C   . PRO B 93  ? 0.8334 0.8921 0.7985 0.2051  -0.1888 -0.1526 157 PRO B C   
3429  O O   . PRO B 93  ? 0.8282 0.8764 0.7727 0.2135  -0.1850 -0.1468 157 PRO B O   
3430  C CB  . PRO B 93  ? 0.6569 0.7143 0.6338 0.1889  -0.1842 -0.1530 157 PRO B CB  
3431  C CG  . PRO B 93  ? 0.6979 0.7521 0.6797 0.1784  -0.1727 -0.1435 157 PRO B CG  
3432  C CD  . PRO B 93  ? 0.7942 0.8570 0.7946 0.1705  -0.1724 -0.1455 157 PRO B CD  
3433  N N   . THR B 94  ? 0.9269 0.9919 0.8980 0.2080  -0.1923 -0.1549 158 THR B N   
3434  C CA  . THR B 94  ? 0.9813 1.0419 0.9347 0.2223  -0.1950 -0.1537 158 THR B CA  
3435  C C   . THR B 94  ? 1.0426 1.1048 0.9898 0.2333  -0.2086 -0.1643 158 THR B C   
3436  O O   . THR B 94  ? 1.1339 1.2041 1.0983 0.2281  -0.2175 -0.1734 158 THR B O   
3437  C CB  . THR B 94  ? 0.9684 1.0347 0.9297 0.2225  -0.1945 -0.1528 158 THR B CB  
3438  O OG1 . THR B 94  ? 0.7871 0.8670 0.7734 0.2150  -0.1994 -0.1597 158 THR B OG1 
3439  C CG2 . THR B 94  ? 1.1210 1.1798 1.0795 0.2167  -0.1829 -0.1419 158 THR B CG2 
3440  N N   . PRO B 95  ? 1.0531 1.1068 0.9758 0.2492  -0.2109 -0.1630 159 PRO B N   
3441  C CA  . PRO B 95  ? 1.1506 1.2020 1.0609 0.2632  -0.2252 -0.1733 159 PRO B CA  
3442  C C   . PRO B 95  ? 1.0957 1.1601 1.0288 0.2611  -0.2398 -0.1852 159 PRO B C   
3443  O O   . PRO B 95  ? 1.5578 1.6229 1.4940 0.2652  -0.2543 -0.1963 159 PRO B O   
3444  C CB  . PRO B 95  ? 1.0714 1.1127 0.9539 0.2803  -0.2220 -0.1673 159 PRO B CB  
3445  C CG  . PRO B 95  ? 1.0051 1.0394 0.8820 0.2752  -0.2046 -0.1521 159 PRO B CG  
3446  C CD  . PRO B 95  ? 0.9189 0.9624 0.8230 0.2558  -0.1994 -0.1506 159 PRO B CD  
3447  N N   . ASP B 96  ? 1.1007 1.1748 1.0505 0.2550  -0.2361 -0.1826 160 ASP B N   
3448  C CA  . ASP B 96  ? 1.2581 1.3466 1.2339 0.2529  -0.2475 -0.1912 160 ASP B CA  
3449  C C   . ASP B 96  ? 1.0882 1.1888 1.0978 0.2374  -0.2492 -0.1949 160 ASP B C   
3450  O O   . ASP B 96  ? 1.1113 1.2234 1.1456 0.2363  -0.2613 -0.2029 160 ASP B O   
3451  C CB  . ASP B 96  ? 1.3993 1.4928 1.3784 0.2541  -0.2415 -0.1857 160 ASP B CB  
3452  C CG  . ASP B 96  ? 1.7159 1.7971 1.6635 0.2680  -0.2374 -0.1799 160 ASP B CG  
3453  O OD1 . ASP B 96  ? 1.8342 1.9051 1.7582 0.2807  -0.2427 -0.1823 160 ASP B OD1 
3454  O OD2 . ASP B 96  ? 2.0948 2.1755 2.0405 0.2673  -0.2284 -0.1724 160 ASP B OD2 
3455  N N   . LYS B 97  ? 0.8706 0.9685 0.8826 0.2259  -0.2372 -0.1885 161 LYS B N   
3456  C CA  . LYS B 97  ? 0.7240 0.8314 0.7650 0.2121  -0.2371 -0.1908 161 LYS B CA  
3457  C C   . LYS B 97  ? 0.7358 0.8390 0.7767 0.2117  -0.2465 -0.1983 161 LYS B C   
3458  O O   . LYS B 97  ? 0.8580 0.9702 0.9266 0.2027  -0.2518 -0.2031 161 LYS B O   
3459  C CB  . LYS B 97  ? 0.6737 0.7797 0.7174 0.2005  -0.2206 -0.1810 161 LYS B CB  
3460  C CG  . LYS B 97  ? 0.8443 0.9562 0.8965 0.1983  -0.2125 -0.1751 161 LYS B CG  
3461  C CD  . LYS B 97  ? 0.9587 1.0869 1.0406 0.1977  -0.2196 -0.1801 161 LYS B CD  
3462  C CE  . LYS B 97  ? 1.1410 1.2743 1.2306 0.1959  -0.2094 -0.1732 161 LYS B CE  
3463  N NZ  . LYS B 97  ? 1.4124 1.5623 1.5320 0.1969  -0.2151 -0.1763 161 LYS B NZ  
3464  N N   . LEU B 98  ? 0.7377 0.8266 0.7477 0.2220  -0.2482 -0.1987 162 LEU B N   
3465  C CA  . LEU B 98  ? 0.7041 0.7859 0.7087 0.2225  -0.2551 -0.2046 162 LEU B CA  
3466  C C   . LEU B 98  ? 0.7038 0.7907 0.7255 0.2260  -0.2757 -0.2182 162 LEU B C   
3467  O O   . LEU B 98  ? 0.8332 0.9228 0.8552 0.2356  -0.2871 -0.2238 162 LEU B O   
3468  C CB  . LEU B 98  ? 0.7387 0.8034 0.7041 0.2364  -0.2522 -0.2013 162 LEU B CB  
3469  C CG  . LEU B 98  ? 0.7798 0.8378 0.7309 0.2327  -0.2330 -0.1873 162 LEU B CG  
3470  C CD1 . LEU B 98  ? 1.1153 1.1582 1.0367 0.2439  -0.2315 -0.1854 162 LEU B CD1 
3471  C CD2 . LEU B 98  ? 0.6509 0.7162 0.6255 0.2141  -0.2234 -0.1829 162 LEU B CD2 
3472  N N   . LYS B 99  ? 0.6519 0.7396 0.6895 0.2180  -0.2813 -0.2234 163 LYS B N   
3473  C CA  . LYS B 99  ? 0.7388 0.8258 0.7880 0.2231  -0.3038 -0.2374 163 LYS B CA  
3474  C C   . LYS B 99  ? 0.7301 0.8001 0.7533 0.2304  -0.3099 -0.2427 163 LYS B C   
3475  O O   . LYS B 99  ? 0.6866 0.7541 0.7111 0.2212  -0.3007 -0.2387 163 LYS B O   
3476  C CB  . LYS B 99  ? 0.6785 0.7820 0.7761 0.2079  -0.3087 -0.2403 163 LYS B CB  
3477  C CG  . LYS B 99  ? 0.6766 0.7784 0.7917 0.2102  -0.3322 -0.2541 163 LYS B CG  
3478  C CD  . LYS B 99  ? 0.7733 0.8948 0.9413 0.1980  -0.3371 -0.2548 163 LYS B CD  
3479  C CE  . LYS B 99  ? 0.8811 1.0025 1.0766 0.1910  -0.3517 -0.2632 163 LYS B CE  
3480  N NZ  . LYS B 99  ? 1.3502 1.4662 1.5514 0.2020  -0.3805 -0.2781 163 LYS B NZ  
3481  N N   . PHE B 100 ? 0.8926 0.9497 0.8893 0.2486  -0.3253 -0.2515 164 PHE B N   
3482  C CA  . PHE B 100 ? 0.8678 0.9068 0.8363 0.2584  -0.3316 -0.2567 164 PHE B CA  
3483  C C   . PHE B 100 ? 0.8650 0.9068 0.8629 0.2480  -0.3453 -0.2665 164 PHE B C   
3484  O O   . PHE B 100 ? 0.9208 0.9712 0.9499 0.2447  -0.3630 -0.2760 164 PHE B O   
3485  C CB  . PHE B 100 ? 0.7411 0.7642 0.6738 0.2825  -0.3472 -0.2653 164 PHE B CB  
3486  C CG  . PHE B 100 ? 0.8233 0.8256 0.7193 0.2961  -0.3501 -0.2683 164 PHE B CG  
3487  C CD1 . PHE B 100 ? 0.8765 0.8708 0.7791 0.2967  -0.3694 -0.2817 164 PHE B CD1 
3488  C CD2 . PHE B 100 ? 0.8650 0.8548 0.7204 0.3089  -0.3333 -0.2571 164 PHE B CD2 
3489  C CE1 . PHE B 100 ? 0.7729 0.7458 0.6379 0.3114  -0.3723 -0.2848 164 PHE B CE1 
3490  C CE2 . PHE B 100 ? 0.8315 0.8013 0.6513 0.3235  -0.3345 -0.2588 164 PHE B CE2 
3491  C CZ  . PHE B 100 ? 0.7766 0.7376 0.5997 0.3251  -0.3541 -0.2730 164 PHE B CZ  
3492  N N   . GLU B 101 ? 0.8140 0.8484 0.8039 0.2427  -0.3373 -0.2636 165 GLU B N   
3493  C CA  . GLU B 101 ? 0.7828 0.8201 0.8025 0.2311  -0.3479 -0.2713 165 GLU B CA  
3494  C C   . GLU B 101 ? 0.8283 0.8451 0.8225 0.2441  -0.3643 -0.2826 165 GLU B C   
3495  O O   . GLU B 101 ? 0.8387 0.8541 0.8546 0.2431  -0.3864 -0.2955 165 GLU B O   
3496  C CB  . GLU B 101 ? 0.7769 0.8246 0.8173 0.2116  -0.3274 -0.2601 165 GLU B CB  
3497  C CG  . GLU B 101 ? 0.7848 0.8538 0.8645 0.1962  -0.3179 -0.2532 165 GLU B CG  
3498  C CD  . GLU B 101 ? 0.9188 1.0008 1.0458 0.1876  -0.3340 -0.2613 165 GLU B CD  
3499  O OE1 . GLU B 101 ? 1.2981 1.3722 1.4284 0.1949  -0.3574 -0.2747 165 GLU B OE1 
3500  O OE2 . GLU B 101 ? 0.9377 1.0371 1.0990 0.1741  -0.3232 -0.2538 165 GLU B OE2 
3501  N N   . ALA B 102 ? 0.8324 0.8331 0.7822 0.2568  -0.3536 -0.2771 166 ALA B N   
3502  C CA  . ALA B 102 ? 0.8063 0.7837 0.7205 0.2749  -0.3676 -0.2868 166 ALA B CA  
3503  C C   . ALA B 102 ? 0.8081 0.7713 0.6742 0.2897  -0.3491 -0.2754 166 ALA B C   
3504  O O   . ALA B 102 ? 0.8447 0.8169 0.7109 0.2825  -0.3259 -0.2601 166 ALA B O   
3505  C CB  . ALA B 102 ? 1.0196 0.9949 0.9537 0.2637  -0.3745 -0.2928 166 ALA B CB  
3506  N N   . VAL B 103 ? 0.7865 0.7269 0.6127 0.3109  -0.3593 -0.2824 167 VAL B N   
3507  C CA  . VAL B 103 ? 0.8167 0.7429 0.5981 0.3265  -0.3402 -0.2699 167 VAL B CA  
3508  C C   . VAL B 103 ? 0.8718 0.7946 0.6548 0.3174  -0.3298 -0.2653 167 VAL B C   
3509  O O   . VAL B 103 ? 1.0737 0.9889 0.8633 0.3158  -0.3464 -0.2777 167 VAL B O   
3510  C CB  . VAL B 103 ? 0.8125 0.7137 0.5442 0.3573  -0.3535 -0.2777 167 VAL B CB  
3511  C CG1 . VAL B 103 ? 0.8726 0.7745 0.5946 0.3704  -0.3622 -0.2810 167 VAL B CG1 
3512  C CG2 . VAL B 103 ? 0.8709 0.7591 0.6040 0.3614  -0.3802 -0.2966 167 VAL B CG2 
3513  N N   . GLY B 104 ? 0.8115 0.7394 0.5899 0.3114  -0.3034 -0.2474 168 GLY B N   
3514  C CA  . GLY B 104 ? 0.8004 0.7267 0.5822 0.3019  -0.2919 -0.2415 168 GLY B CA  
3515  C C   . GLY B 104 ? 0.9013 0.8396 0.6933 0.2889  -0.2648 -0.2221 168 GLY B C   
3516  O O   . GLY B 104 ? 0.7988 0.7486 0.6016 0.2839  -0.2563 -0.2144 168 GLY B O   
3517  N N   . TRP B 105 ? 0.9135 0.8485 0.7025 0.2838  -0.2523 -0.2145 169 TRP B N   
3518  C CA  . TRP B 105 ? 0.8204 0.7638 0.6170 0.2733  -0.2277 -0.1959 169 TRP B CA  
3519  C C   . TRP B 105 ? 0.8274 0.7835 0.6593 0.2490  -0.2239 -0.1957 169 TRP B C   
3520  O O   . TRP B 105 ? 0.8927 0.8561 0.7354 0.2377  -0.2061 -0.1820 169 TRP B O   
3521  C CB  . TRP B 105 ? 0.8839 0.8128 0.6462 0.2901  -0.2134 -0.1838 169 TRP B CB  
3522  C CG  . TRP B 105 ? 0.8914 0.8077 0.6408 0.2949  -0.2197 -0.1909 169 TRP B CG  
3523  C CD1 . TRP B 105 ? 0.8907 0.8122 0.6612 0.2776  -0.2156 -0.1904 169 TRP B CD1 
3524  C CD2 . TRP B 105 ? 0.8945 0.7889 0.6044 0.3201  -0.2317 -0.1998 169 TRP B CD2 
3525  N NE1 . TRP B 105 ? 0.9748 0.8801 0.7233 0.2894  -0.2240 -0.1982 169 TRP B NE1 
3526  C CE2 . TRP B 105 ? 0.9983 0.8862 0.7095 0.3152  -0.2343 -0.2045 169 TRP B CE2 
3527  C CE3 . TRP B 105 ? 1.1322 1.0110 0.8055 0.3462  -0.2409 -0.2047 169 TRP B CE3 
3528  C CZ2 . TRP B 105 ? 1.0948 0.9605 0.7712 0.3361  -0.2464 -0.2141 169 TRP B CZ2 
3529  C CZ3 . TRP B 105 ? 1.3515 1.2073 0.9881 0.3683  -0.2533 -0.2146 169 TRP B CZ3 
3530  C CH2 . TRP B 105 ? 1.2732 1.1223 0.9112 0.3633  -0.2562 -0.2194 169 TRP B CH2 
3531  N N   . SER B 106 ? 0.8211 0.7790 0.6717 0.2412  -0.2410 -0.2106 170 SER B N   
3532  C CA  . SER B 106 ? 0.7655 0.7363 0.6527 0.2179  -0.2378 -0.2108 170 SER B CA  
3533  C C   . SER B 106 ? 0.6833 0.6613 0.5999 0.2094  -0.2572 -0.2256 170 SER B C   
3534  O O   . SER B 106 ? 0.7224 0.6904 0.6289 0.2215  -0.2769 -0.2390 170 SER B O   
3535  C CB  . SER B 106 ? 0.8786 0.8409 0.7573 0.2164  -0.2315 -0.2080 170 SER B CB  
3536  O OG  . SER B 106 ? 0.8220 0.7927 0.7330 0.1979  -0.2356 -0.2136 170 SER B OG  
3537  N N   . ALA B 107 ? 0.5895 0.5844 0.5431 0.1895  -0.2520 -0.2229 171 ALA B N   
3538  C CA  . ALA B 107 ? 0.6164 0.6215 0.6027 0.1817  -0.2676 -0.2337 171 ALA B CA  
3539  C C   . ALA B 107 ? 0.5765 0.5965 0.6017 0.1607  -0.2603 -0.2302 171 ALA B C   
3540  O O   . ALA B 107 ? 0.7145 0.7405 0.7427 0.1516  -0.2423 -0.2186 171 ALA B O   
3541  C CB  . ALA B 107 ? 0.6018 0.6138 0.5893 0.1875  -0.2715 -0.2341 171 ALA B CB  
3542  N N   . SER B 108 ? 0.6141 0.6393 0.6697 0.1541  -0.2752 -0.2402 172 SER B N   
3543  C CA  . SER B 108 ? 0.6452 0.6862 0.7426 0.1358  -0.2697 -0.2371 172 SER B CA  
3544  C C   . SER B 108 ? 0.6666 0.7183 0.7982 0.1335  -0.2858 -0.2453 172 SER B C   
3545  O O   . SER B 108 ? 0.8494 0.8933 0.9746 0.1447  -0.3059 -0.2568 172 SER B O   
3546  C CB  . SER B 108 ? 0.6704 0.7060 0.7756 0.1281  -0.2693 -0.2388 172 SER B CB  
3547  O OG  . SER B 108 ? 0.7522 0.7998 0.9018 0.1146  -0.2740 -0.2413 172 SER B OG  
3548  N N   . SER B 109 ? 0.6090 0.6781 0.7767 0.1204  -0.2775 -0.2392 173 SER B N   
3549  C CA  . SER B 109 ? 0.6856 0.7664 0.8890 0.1185  -0.2912 -0.2449 173 SER B CA  
3550  C C   . SER B 109 ? 0.6950 0.7931 0.9439 0.1029  -0.2816 -0.2377 173 SER B C   
3551  O O   . SER B 109 ? 0.6496 0.7512 0.8973 0.0947  -0.2620 -0.2273 173 SER B O   
3552  C CB  . SER B 109 ? 0.6954 0.7799 0.8858 0.1279  -0.2921 -0.2440 173 SER B CB  
3553  O OG  . SER B 109 ? 0.7474 0.8413 0.9371 0.1219  -0.2709 -0.2311 173 SER B OG  
3554  N N   . CYS B 110 ? 0.6462 0.7544 0.9355 0.0998  -0.2958 -0.2430 174 CYS B N   
3555  C CA  . CYS B 110 ? 0.6744 0.7996 1.0121 0.0866  -0.2876 -0.2356 174 CYS B CA  
3556  C C   . CYS B 110 ? 0.6970 0.8330 1.0735 0.0876  -0.3049 -0.2411 174 CYS B C   
3557  O O   . CYS B 110 ? 0.8410 0.9681 1.2123 0.0959  -0.3279 -0.2539 174 CYS B O   
3558  C CB  . CYS B 110 ? 0.7091 0.8305 1.0633 0.0770  -0.2863 -0.2356 174 CYS B CB  
3559  S SG  . CYS B 110 ? 0.9885 1.0887 1.3254 0.0837  -0.3113 -0.2520 174 CYS B SG  
3560  N N   . HIS B 111 ? 0.7828 0.9375 1.1981 0.0801  -0.2940 -0.2312 175 HIS B N   
3561  C CA  . HIS B 111 ? 0.6566 0.8252 1.1157 0.0804  -0.3079 -0.2336 175 HIS B CA  
3562  C C   . HIS B 111 ? 0.6345 0.8136 1.1502 0.0691  -0.3112 -0.2308 175 HIS B C   
3563  O O   . HIS B 111 ? 0.7974 0.9860 1.3319 0.0604  -0.2905 -0.2181 175 HIS B O   
3564  C CB  . HIS B 111 ? 0.5463 0.7292 1.0090 0.0823  -0.2922 -0.2230 175 HIS B CB  
3565  C CG  . HIS B 111 ? 0.6146 0.8100 1.1122 0.0858  -0.3071 -0.2261 175 HIS B CG  
3566  N ND1 . HIS B 111 ? 0.6482 0.8612 1.2042 0.0782  -0.3071 -0.2198 175 HIS B ND1 
3567  C CD2 . HIS B 111 ? 0.6880 0.8804 1.1700 0.0970  -0.3233 -0.2348 175 HIS B CD2 
3568  C CE1 . HIS B 111 ? 0.7023 0.9240 1.2812 0.0837  -0.3230 -0.2242 175 HIS B CE1 
3569  N NE2 . HIS B 111 ? 0.7065 0.9153 1.2388 0.0953  -0.3332 -0.2340 175 HIS B NE2 
3570  N N   . ASP B 112 ? 0.6265 0.8033 1.1708 0.0696  -0.3373 -0.2422 176 ASP B N   
3571  C CA  . ASP B 112 ? 0.7446 0.9305 1.3473 0.0581  -0.3421 -0.2393 176 ASP B CA  
3572  C C   . ASP B 112 ? 0.7520 0.9623 1.4150 0.0526  -0.3362 -0.2278 176 ASP B C   
3573  O O   . ASP B 112 ? 1.0867 1.3069 1.8016 0.0427  -0.3346 -0.2213 176 ASP B O   
3574  C CB  . ASP B 112 ? 0.7432 0.9148 1.3556 0.0601  -0.3740 -0.2562 176 ASP B CB  
3575  C CG  . ASP B 112 ? 0.8301 1.0010 1.4506 0.0695  -0.4008 -0.2681 176 ASP B CG  
3576  O OD1 . ASP B 112 ? 1.1124 1.2955 1.7335 0.0740  -0.3942 -0.2628 176 ASP B OD1 
3577  O OD2 . ASP B 112 ? 0.8630 1.0199 1.4879 0.0734  -0.4296 -0.2834 176 ASP B OD2 
3578  N N   . GLY B 113 ? 0.5983 0.8181 1.2558 0.0593  -0.3320 -0.2243 177 GLY B N   
3579  C CA  . GLY B 113 ? 0.7160 0.9587 1.4312 0.0561  -0.3288 -0.2140 177 GLY B CA  
3580  C C   . GLY B 113 ? 0.6843 0.9300 1.4155 0.0635  -0.3550 -0.2247 177 GLY B C   
3581  O O   . GLY B 113 ? 0.8820 1.1463 1.6520 0.0639  -0.3526 -0.2167 177 GLY B O   
3582  N N   . PHE B 114 ? 0.6665 0.8929 1.3650 0.0707  -0.3798 -0.2425 178 PHE B N   
3583  C CA  . PHE B 114 ? 0.7497 0.9748 1.4559 0.0796  -0.4076 -0.2549 178 PHE B CA  
3584  C C   . PHE B 114 ? 0.8072 1.0164 1.4445 0.0938  -0.4102 -0.2637 178 PHE B C   
3585  O O   . PHE B 114 ? 0.9525 1.1695 1.5833 0.1011  -0.4085 -0.2616 178 PHE B O   
3586  C CB  . PHE B 114 ? 0.8016 1.0160 1.5364 0.0777  -0.4402 -0.2696 178 PHE B CB  
3587  C CG  . PHE B 114 ? 0.8605 1.0901 1.6677 0.0635  -0.4392 -0.2606 178 PHE B CG  
3588  C CD1 . PHE B 114 ? 0.9219 1.1745 1.7935 0.0594  -0.4415 -0.2518 178 PHE B CD1 
3589  C CD2 . PHE B 114 ? 1.0809 1.3023 1.8935 0.0545  -0.4346 -0.2596 178 PHE B CD2 
3590  C CE1 . PHE B 114 ? 1.1006 1.3683 2.0434 0.0467  -0.4389 -0.2412 178 PHE B CE1 
3591  C CE2 . PHE B 114 ? 1.2608 1.4966 2.1432 0.0415  -0.4327 -0.2499 178 PHE B CE2 
3592  C CZ  . PHE B 114 ? 1.0317 1.2909 1.9804 0.0377  -0.4346 -0.2402 178 PHE B CZ  
3593  N N   . GLN B 115 ? 0.7027 0.8900 1.2899 0.0983  -0.4133 -0.2724 179 GLN B N   
3594  C CA  . GLN B 115 ? 0.7028 0.8735 1.2245 0.1127  -0.4149 -0.2796 179 GLN B CA  
3595  C C   . GLN B 115 ? 0.7358 0.8954 1.2106 0.1112  -0.3921 -0.2736 179 GLN B C   
3596  O O   . GLN B 115 ? 0.6387 0.8011 1.1305 0.0998  -0.3798 -0.2669 179 GLN B O   
3597  C CB  . GLN B 115 ? 0.8442 0.9954 1.3494 0.1245  -0.4489 -0.2992 179 GLN B CB  
3598  C CG  . GLN B 115 ? 1.0025 1.1624 1.5510 0.1278  -0.4755 -0.3071 179 GLN B CG  
3599  C CD  . GLN B 115 ? 0.9843 1.1531 1.5185 0.1370  -0.4704 -0.3037 179 GLN B CD  
3600  O OE1 . GLN B 115 ? 1.2250 1.3878 1.7080 0.1441  -0.4527 -0.2991 179 GLN B OE1 
3601  N NE2 . GLN B 115 ? 1.1350 1.3181 1.7161 0.1368  -0.4862 -0.3053 179 GLN B NE2 
3602  N N   . TRP B 116 ? 0.9098 1.0576 1.3281 0.1227  -0.3858 -0.2749 180 TRP B N   
3603  C CA  . TRP B 116 ? 0.7336 0.8674 1.1047 0.1236  -0.3693 -0.2713 180 TRP B CA  
3604  C C   . TRP B 116 ? 0.7479 0.8599 1.0926 0.1310  -0.3876 -0.2845 180 TRP B C   
3605  O O   . TRP B 116 ? 0.7932 0.8928 1.1182 0.1448  -0.4094 -0.2970 180 TRP B O   
3606  C CB  . TRP B 116 ? 0.7148 0.8436 1.0385 0.1339  -0.3567 -0.2670 180 TRP B CB  
3607  C CG  . TRP B 116 ? 0.7622 0.9071 1.0969 0.1270  -0.3329 -0.2524 180 TRP B CG  
3608  C CD1 . TRP B 116 ? 0.7309 0.8892 1.0801 0.1298  -0.3309 -0.2483 180 TRP B CD1 
3609  C CD2 . TRP B 116 ? 0.8568 1.0050 1.1866 0.1174  -0.3073 -0.2397 180 TRP B CD2 
3610  N NE1 . TRP B 116 ? 0.7974 0.9656 1.1489 0.1234  -0.3063 -0.2344 180 TRP B NE1 
3611  C CE2 . TRP B 116 ? 0.8496 1.0121 1.1900 0.1158  -0.2917 -0.2289 180 TRP B CE2 
3612  C CE3 . TRP B 116 ? 0.8125 0.9525 1.1296 0.1108  -0.2967 -0.2365 180 TRP B CE3 
3613  C CZ2 . TRP B 116 ? 0.8444 1.0115 1.1818 0.1086  -0.2676 -0.2161 180 TRP B CZ2 
3614  C CZ3 . TRP B 116 ? 0.7352 0.8810 1.0508 0.1029  -0.2724 -0.2235 180 TRP B CZ3 
3615  C CH2 . TRP B 116 ? 0.8249 0.9832 1.1499 0.1021  -0.2588 -0.2138 180 TRP B CH2 
3616  N N   . THR B 117 ? 0.7059 0.8117 1.0469 0.1234  -0.3786 -0.2818 181 THR B N   
3617  C CA  . THR B 117 ? 0.6557 0.7388 0.9625 0.1315  -0.3909 -0.2923 181 THR B CA  
3618  C C   . THR B 117 ? 0.6554 0.7279 0.9062 0.1387  -0.3707 -0.2852 181 THR B C   
3619  O O   . THR B 117 ? 0.6778 0.7592 0.9283 0.1293  -0.3458 -0.2719 181 THR B O   
3620  C CB  . THR B 117 ? 0.6590 0.7415 0.9973 0.1190  -0.3937 -0.2933 181 THR B CB  
3621  O OG1 . THR B 117 ? 0.6116 0.7062 1.0083 0.1115  -0.4108 -0.2974 181 THR B OG1 
3622  C CG2 . THR B 117 ? 0.6966 0.7542 0.9996 0.1285  -0.4081 -0.3050 181 THR B CG2 
3623  N N   . VAL B 118 ? 0.6589 0.7122 0.8635 0.1562  -0.3816 -0.2936 182 VAL B N   
3624  C CA  . VAL B 118 ? 0.6671 0.7093 0.8202 0.1647  -0.3636 -0.2862 182 VAL B CA  
3625  C C   . VAL B 118 ? 0.7102 0.7286 0.8246 0.1778  -0.3737 -0.2947 182 VAL B C   
3626  O O   . VAL B 118 ? 0.8352 0.8393 0.9346 0.1925  -0.3971 -0.3081 182 VAL B O   
3627  C CB  . VAL B 118 ? 0.6237 0.6668 0.7504 0.1768  -0.3591 -0.2828 182 VAL B CB  
3628  C CG1 . VAL B 118 ? 0.6617 0.6918 0.7384 0.1868  -0.3428 -0.2752 182 VAL B CG1 
3629  C CG2 . VAL B 118 ? 0.5743 0.6389 0.7311 0.1649  -0.3444 -0.2723 182 VAL B CG2 
3630  N N   . LEU B 119 ? 0.7408 0.7542 0.8378 0.1734  -0.3560 -0.2866 183 LEU B N   
3631  C CA  . LEU B 119 ? 0.7517 0.7427 0.8100 0.1858  -0.3608 -0.2918 183 LEU B CA  
3632  C C   . LEU B 119 ? 0.7413 0.7244 0.7527 0.1986  -0.3434 -0.2820 183 LEU B C   
3633  O O   . LEU B 119 ? 0.8372 0.8306 0.8501 0.1894  -0.3202 -0.2679 183 LEU B O   
3634  C CB  . LEU B 119 ? 0.7534 0.7448 0.8269 0.1720  -0.3519 -0.2882 183 LEU B CB  
3635  C CG  . LEU B 119 ? 0.7619 0.7621 0.8867 0.1569  -0.3648 -0.2946 183 LEU B CG  
3636  C CD1 . LEU B 119 ? 0.7636 0.7807 0.9180 0.1372  -0.3429 -0.2817 183 LEU B CD1 
3637  C CD2 . LEU B 119 ? 0.9575 0.9386 1.0740 0.1627  -0.3835 -0.3070 183 LEU B CD2 
3638  N N   . SER B 120 ? 0.7983 0.7621 0.7685 0.2206  -0.3549 -0.2890 184 SER B N   
3639  C CA  . SER B 120 ? 0.8875 0.8430 0.8136 0.2355  -0.3387 -0.2788 184 SER B CA  
3640  C C   . SER B 120 ? 0.8534 0.7854 0.7371 0.2527  -0.3410 -0.2816 184 SER B C   
3641  O O   . SER B 120 ? 1.0839 1.0012 0.9617 0.2609  -0.3626 -0.2960 184 SER B O   
3642  C CB  . SER B 120 ? 0.9554 0.9105 0.8677 0.2496  -0.3469 -0.2818 184 SER B CB  
3643  O OG  . SER B 120 ? 0.9684 0.9139 0.8377 0.2660  -0.3321 -0.2716 184 SER B OG  
3644  N N   . VAL B 121 ? 0.7867 0.7147 0.6419 0.2588  -0.3189 -0.2673 185 VAL B N   
3645  C CA  . VAL B 121 ? 0.8456 0.7518 0.6570 0.2778  -0.3166 -0.2665 185 VAL B CA  
3646  C C   . VAL B 121 ? 0.9176 0.8125 0.6859 0.3021  -0.3109 -0.2605 185 VAL B C   
3647  O O   . VAL B 121 ? 1.1845 1.0898 0.9525 0.2994  -0.2910 -0.2454 185 VAL B O   
3648  C CB  . VAL B 121 ? 0.8018 0.7127 0.6160 0.2664  -0.2926 -0.2517 185 VAL B CB  
3649  C CG1 . VAL B 121 ? 0.8291 0.7187 0.5984 0.2870  -0.2869 -0.2480 185 VAL B CG1 
3650  C CG2 . VAL B 121 ? 0.7477 0.6692 0.6022 0.2435  -0.2960 -0.2561 185 VAL B CG2 
3651  N N   . ALA B 122 ? 0.9479 0.8204 0.6788 0.3269  -0.3279 -0.2716 186 ALA B N   
3652  C CA  . ALA B 122 ? 1.0225 0.8825 0.7102 0.3530  -0.3238 -0.2665 186 ALA B CA  
3653  C C   . ALA B 122 ? 1.0620 0.8926 0.6951 0.3832  -0.3293 -0.2704 186 ALA B C   
3654  O O   . ALA B 122 ? 0.9069 0.7242 0.5339 0.3855  -0.3416 -0.2807 186 ALA B O   
3655  C CB  . ALA B 122 ? 0.9510 0.8153 0.6471 0.3569  -0.3420 -0.2771 186 ALA B CB  
3656  N N   . GLY B 123 ? 1.1527 0.9730 0.7461 0.4071  -0.3196 -0.2616 187 GLY B N   
3657  C CA  . GLY B 123 ? 1.2501 1.0416 0.7857 0.4408  -0.3219 -0.2627 187 GLY B CA  
3658  C C   . GLY B 123 ? 1.3323 1.1117 0.8503 0.4453  -0.3117 -0.2574 187 GLY B C   
3659  O O   . GLY B 123 ? 1.3669 1.1544 0.8867 0.4400  -0.2840 -0.2374 187 GLY B O   
3660  N N   . ASP B 124 ? 1.4378 1.1968 0.9389 0.4559  -0.3356 -0.2757 188 ASP B N   
3661  C CA  . ASP B 124 ? 1.5422 1.2872 1.0265 0.4605  -0.3314 -0.2749 188 ASP B CA  
3662  C C   . ASP B 124 ? 1.3849 1.1539 0.9156 0.4278  -0.3125 -0.2633 188 ASP B C   
3663  O O   . ASP B 124 ? 1.5530 1.3188 1.0716 0.4300  -0.2931 -0.2504 188 ASP B O   
3664  C CB  . ASP B 124 ? 1.9122 1.6343 1.3845 0.4705  -0.3669 -0.3008 188 ASP B CB  
3665  C CG  . ASP B 124 ? 2.0595 1.7701 1.5271 0.4679  -0.3670 -0.3035 188 ASP B CG  
3666  O OD1 . ASP B 124 ? 2.2740 1.9751 1.7091 0.4824  -0.3450 -0.2887 188 ASP B OD1 
3667  O OD2 . ASP B 124 ? 1.7428 1.4535 1.2402 0.4521  -0.3894 -0.3201 188 ASP B OD2 
3668  N N   . GLY B 125 ? 1.1304 0.9233 0.7131 0.3988  -0.3175 -0.2671 189 GLY B N   
3669  C CA  . GLY B 125 ? 0.9577 0.7701 0.5841 0.3686  -0.3061 -0.2611 189 GLY B CA  
3670  C C   . GLY B 125 ? 0.9287 0.7451 0.5920 0.3507  -0.3310 -0.2800 189 GLY B C   
3671  O O   . GLY B 125 ? 0.9036 0.7301 0.5970 0.3299  -0.3256 -0.2781 189 GLY B O   
3672  N N   . PHE B 126 ? 1.0330 0.8417 0.6964 0.3587  -0.3584 -0.2976 190 PHE B N   
3673  C CA  . PHE B 126 ? 1.0495 0.8628 0.7539 0.3417  -0.3835 -0.3148 190 PHE B CA  
3674  C C   . PHE B 126 ? 1.0826 0.9249 0.8399 0.3166  -0.3812 -0.3120 190 PHE B C   
3675  O O   . PHE B 126 ? 1.0059 0.8630 0.7656 0.3130  -0.3624 -0.2986 190 PHE B O   
3676  C CB  . PHE B 126 ? 1.1944 0.9828 0.8748 0.3636  -0.4176 -0.3364 190 PHE B CB  
3677  C CG  . PHE B 126 ? 1.3457 1.1350 1.0175 0.3759  -0.4287 -0.3411 190 PHE B CG  
3678  C CD1 . PHE B 126 ? 1.3954 1.1940 1.1064 0.3649  -0.4533 -0.3550 190 PHE B CD1 
3679  C CD2 . PHE B 126 ? 1.4016 1.1826 1.0278 0.3988  -0.4142 -0.3307 190 PHE B CD2 
3680  C CE1 . PHE B 126 ? 1.3379 1.1377 1.0414 0.3763  -0.4636 -0.3592 190 PHE B CE1 
3681  C CE2 . PHE B 126 ? 1.3828 1.1643 1.0005 0.4104  -0.4240 -0.3348 190 PHE B CE2 
3682  C CZ  . PHE B 126 ? 1.2995 1.0903 0.9551 0.3992  -0.4490 -0.3495 190 PHE B CZ  
3683  N N   . VAL B 127 ? 1.0803 0.9295 0.8802 0.3002  -0.4008 -0.3246 191 VAL B N   
3684  C CA  . VAL B 127 ? 0.9570 0.8328 0.8095 0.2770  -0.3994 -0.3223 191 VAL B CA  
3685  C C   . VAL B 127 ? 1.0572 0.9320 0.9280 0.2812  -0.4291 -0.3385 191 VAL B C   
3686  O O   . VAL B 127 ? 1.1928 1.0541 1.0717 0.2844  -0.4556 -0.3547 191 VAL B O   
3687  C CB  . VAL B 127 ? 0.9386 0.8280 0.8349 0.2517  -0.3933 -0.3195 191 VAL B CB  
3688  C CG1 . VAL B 127 ? 1.0685 0.9791 1.0224 0.2316  -0.4031 -0.3235 191 VAL B CG1 
3689  C CG2 . VAL B 127 ? 0.8773 0.7784 0.7708 0.2416  -0.3619 -0.3008 191 VAL B CG2 
3690  N N   . SER B 128 ? 1.0289 0.9171 0.9067 0.2814  -0.4253 -0.3342 192 SER B N   
3691  C CA  . SER B 128 ? 0.9990 0.8939 0.9073 0.2795  -0.4497 -0.3465 192 SER B CA  
3692  C C   . SER B 128 ? 0.9708 0.8931 0.9420 0.2509  -0.4432 -0.3411 192 SER B C   
3693  O O   . SER B 128 ? 1.1888 1.1281 1.1719 0.2362  -0.4160 -0.3253 192 SER B O   
3694  C CB  . SER B 128 ? 1.0419 0.9397 0.9288 0.2929  -0.4463 -0.3429 192 SER B CB  
3695  O OG  . SER B 128 ? 1.1834 1.0557 1.0102 0.3214  -0.4500 -0.3460 192 SER B OG  
3696  N N   . ILE B 129 ? 0.8449 0.7712 0.8572 0.2436  -0.4680 -0.3536 193 ILE B N   
3697  C CA  . ILE B 129 ? 0.8315 0.7845 0.9054 0.2187  -0.4617 -0.3473 193 ILE B CA  
3698  C C   . ILE B 129 ? 0.8890 0.8518 0.9849 0.2217  -0.4775 -0.3530 193 ILE B C   
3699  O O   . ILE B 129 ? 0.9404 0.8899 1.0370 0.2331  -0.5082 -0.3692 193 ILE B O   
3700  C CB  . ILE B 129 ? 0.8923 0.8438 1.0058 0.2056  -0.4765 -0.3551 193 ILE B CB  
3701  C CG1 . ILE B 129 ? 1.0125 0.9578 1.1093 0.1999  -0.4576 -0.3475 193 ILE B CG1 
3702  C CG2 . ILE B 129 ? 0.8225 0.8008 1.0032 0.1833  -0.4741 -0.3496 193 ILE B CG2 
3703  C CD1 . ILE B 129 ? 1.0127 0.9489 1.1351 0.1924  -0.4745 -0.3571 193 ILE B CD1 
3704  N N   . LEU B 130 ? 0.8805 0.8652 0.9931 0.2126  -0.4583 -0.3404 194 LEU B N   
3705  C CA  . LEU B 130 ? 0.9434 0.9396 1.0835 0.2138  -0.4735 -0.3454 194 LEU B CA  
3706  C C   . LEU B 130 ? 0.9085 0.9329 1.1107 0.1926  -0.4655 -0.3370 194 LEU B C   
3707  O O   . LEU B 130 ? 1.2170 1.2571 1.4280 0.1802  -0.4380 -0.3218 194 LEU B O   
3708  C CB  . LEU B 130 ? 0.9589 0.9486 1.0554 0.2328  -0.4714 -0.3447 194 LEU B CB  
3709  C CG  . LEU B 130 ? 1.0486 1.0412 1.1103 0.2348  -0.4404 -0.3289 194 LEU B CG  
3710  C CD1 . LEU B 130 ? 1.3805 1.3951 1.4664 0.2276  -0.4300 -0.3203 194 LEU B CD1 
3711  C CD2 . LEU B 130 ? 1.0006 0.9687 1.0004 0.2605  -0.4451 -0.3334 194 LEU B CD2 
3712  N N   . TYR B 131 ? 0.8352 0.8646 1.0802 0.1901  -0.4911 -0.3473 195 TYR B N   
3713  C CA  . TYR B 131 ? 0.7561 0.8113 1.0666 0.1717  -0.4878 -0.3403 195 TYR B CA  
3714  C C   . TYR B 131 ? 0.7566 0.8238 1.0785 0.1776  -0.4943 -0.3405 195 TYR B C   
3715  O O   . TYR B 131 ? 0.7551 0.8119 1.0721 0.1909  -0.5221 -0.3545 195 TYR B O   
3716  C CB  . TYR B 131 ? 0.7692 0.8222 1.1271 0.1635  -0.5124 -0.3504 195 TYR B CB  
3717  C CG  . TYR B 131 ? 0.7874 0.8668 1.2165 0.1430  -0.5044 -0.3399 195 TYR B CG  
3718  C CD1 . TYR B 131 ? 0.7971 0.8883 1.2417 0.1273  -0.4766 -0.3253 195 TYR B CD1 
3719  C CD2 . TYR B 131 ? 0.8800 0.9724 1.3618 0.1402  -0.5245 -0.3441 195 TYR B CD2 
3720  C CE1 . TYR B 131 ? 0.8080 0.9224 1.3163 0.1106  -0.4678 -0.3145 195 TYR B CE1 
3721  C CE2 . TYR B 131 ? 0.9107 1.0276 1.4598 0.1226  -0.5157 -0.3327 195 TYR B CE2 
3722  C CZ  . TYR B 131 ? 0.9378 1.0653 1.4988 0.1085  -0.4867 -0.3176 195 TYR B CZ  
3723  O OH  . TYR B 131 ? 1.2348 1.3860 1.8614 0.0932  -0.4767 -0.3051 195 TYR B OH  
3724  N N   . GLY B 132 ? 0.8040 0.8915 1.1379 0.1690  -0.4687 -0.3252 196 GLY B N   
3725  C CA  . GLY B 132 ? 0.7709 0.8714 1.1156 0.1741  -0.4712 -0.3234 196 GLY B CA  
3726  C C   . GLY B 132 ? 0.7403 0.8229 1.0286 0.1955  -0.4807 -0.3316 196 GLY B C   
3727  O O   . GLY B 132 ? 0.7522 0.8373 1.0479 0.2044  -0.4976 -0.3382 196 GLY B O   
3728  N N   . GLY B 133 ? 0.8112 0.8757 1.0443 0.2044  -0.4694 -0.3304 197 GLY B N   
3729  C CA  . GLY B 133 ? 1.0056 1.0541 1.1816 0.2254  -0.4709 -0.3337 197 GLY B CA  
3730  C C   . GLY B 133 ? 0.9500 0.9735 1.0963 0.2451  -0.5010 -0.3516 197 GLY B C   
3731  O O   . GLY B 133 ? 1.0061 1.0144 1.1033 0.2652  -0.5038 -0.3548 197 GLY B O   
3732  N N   . ILE B 134 ? 0.9640 0.9819 1.1390 0.2405  -0.5239 -0.3632 198 ILE B N   
3733  C CA  . ILE B 134 ? 1.0478 1.0386 1.1935 0.2601  -0.5555 -0.3819 198 ILE B CA  
3734  C C   . ILE B 134 ? 1.0389 1.0129 1.1707 0.2586  -0.5569 -0.3859 198 ILE B C   
3735  O O   . ILE B 134 ? 1.1066 1.0939 1.2738 0.2384  -0.5432 -0.3777 198 ILE B O   
3736  C CB  . ILE B 134 ? 1.1572 1.1516 1.3488 0.2597  -0.5899 -0.3960 198 ILE B CB  
3737  C CG1 . ILE B 134 ? 1.0132 1.0232 1.2728 0.2361  -0.5939 -0.3943 198 ILE B CG1 
3738  C CG2 . ILE B 134 ? 1.4402 1.4515 1.6445 0.2625  -0.5884 -0.3918 198 ILE B CG2 
3739  C CD1 . ILE B 134 ? 1.2043 1.2160 1.5143 0.2348  -0.6301 -0.4082 198 ILE B CD1 
3740  N N   . ILE B 135 ? 1.1121 1.0563 1.1913 0.2810  -0.5732 -0.3980 199 ILE B N   
3741  C CA  . ILE B 135 ? 1.2467 1.1726 1.3006 0.2827  -0.5696 -0.3997 199 ILE B CA  
3742  C C   . ILE B 135 ? 1.1069 1.0255 1.1980 0.2755  -0.5980 -0.4138 199 ILE B C   
3743  O O   . ILE B 135 ? 1.1044 1.0039 1.1871 0.2907  -0.6313 -0.4315 199 ILE B O   
3744  C CB  . ILE B 135 ? 1.2874 1.1830 1.2652 0.3112  -0.5711 -0.4045 199 ILE B CB  
3745  C CG1 . ILE B 135 ? 1.5899 1.4929 1.5332 0.3183  -0.5417 -0.3887 199 ILE B CG1 
3746  C CG2 . ILE B 135 ? 1.1316 1.0101 1.0878 0.3117  -0.5662 -0.4052 199 ILE B CG2 
3747  C CD1 . ILE B 135 ? 1.7779 1.6721 1.6774 0.3233  -0.5132 -0.3756 199 ILE B CD1 
3748  N N   . THR B 136 ? 1.0898 1.0221 1.2207 0.2530  -0.5847 -0.4059 200 THR B N   
3749  C CA  . THR B 136 ? 1.1410 1.0703 1.3185 0.2422  -0.6093 -0.4168 200 THR B CA  
3750  C C   . THR B 136 ? 1.1575 1.0615 1.3043 0.2482  -0.6142 -0.4236 200 THR B C   
3751  O O   . THR B 136 ? 1.3029 1.1934 1.4718 0.2478  -0.6433 -0.4380 200 THR B O   
3752  C CB  . THR B 136 ? 1.0615 1.0230 1.3120 0.2134  -0.5942 -0.4039 200 THR B CB  
3753  O OG1 . THR B 136 ? 1.0377 1.0121 1.2764 0.2023  -0.5555 -0.3853 200 THR B OG1 
3754  C CG2 . THR B 136 ? 0.9140 0.8976 1.2040 0.2090  -0.5990 -0.4012 200 THR B CG2 
3755  N N   . ASP B 137 ? 1.0524 0.9498 1.1503 0.2538  -0.5868 -0.4131 201 ASP B N   
3756  C CA  . ASP B 137 ? 1.1156 0.9913 1.1843 0.2588  -0.5870 -0.4170 201 ASP B CA  
3757  C C   . ASP B 137 ? 1.0833 0.9508 1.0913 0.2703  -0.5571 -0.4047 201 ASP B C   
3758  O O   . ASP B 137 ? 1.0856 0.9710 1.0889 0.2649  -0.5290 -0.3888 201 ASP B O   
3759  C CB  . ASP B 137 ? 1.3491 1.2392 1.4730 0.2329  -0.5805 -0.4117 201 ASP B CB  
3760  C CG  . ASP B 137 ? 1.6272 1.4915 1.7391 0.2381  -0.5992 -0.4242 201 ASP B CG  
3761  O OD1 . ASP B 137 ? 1.9676 1.8066 2.0183 0.2582  -0.5985 -0.4283 201 ASP B OD1 
3762  O OD2 . ASP B 137 ? 1.8392 1.7082 2.0042 0.2224  -0.6141 -0.4293 201 ASP B OD2 
3763  N N   . THR B 138 ? 1.0657 0.9053 1.0287 0.2866  -0.5640 -0.4119 202 THR B N   
3764  C CA  . THR B 138 ? 1.1385 0.9692 1.0478 0.2975  -0.5362 -0.3996 202 THR B CA  
3765  C C   . THR B 138 ? 1.1310 0.9521 1.0380 0.2910  -0.5303 -0.3986 202 THR B C   
3766  O O   . THR B 138 ? 1.2613 1.0689 1.1849 0.2897  -0.5554 -0.4130 202 THR B O   
3767  C CB  . THR B 138 ? 1.2956 1.0983 1.1358 0.3315  -0.5448 -0.4062 202 THR B CB  
3768  O OG1 . THR B 138 ? 1.8395 1.6124 1.6622 0.3482  -0.5797 -0.4271 202 THR B OG1 
3769  C CG2 . THR B 138 ? 1.2350 1.0466 1.0716 0.3396  -0.5473 -0.4054 202 THR B CG2 
3770  N N   . ILE B 139 ? 1.1296 0.9571 1.0165 0.2873  -0.4974 -0.3815 203 ILE B N   
3771  C CA  . ILE B 139 ? 1.1320 0.9513 1.0123 0.2821  -0.4878 -0.3783 203 ILE B CA  
3772  C C   . ILE B 139 ? 1.2330 1.0338 1.0485 0.3046  -0.4704 -0.3704 203 ILE B C   
3773  O O   . ILE B 139 ? 1.1987 1.0094 0.9951 0.3088  -0.4469 -0.3558 203 ILE B O   
3774  C CB  . ILE B 139 ? 1.0026 0.8503 0.9296 0.2527  -0.4626 -0.3630 203 ILE B CB  
3775  C CG1 . ILE B 139 ? 0.9627 0.8291 0.9560 0.2314  -0.4775 -0.3687 203 ILE B CG1 
3776  C CG2 . ILE B 139 ? 1.0517 0.8904 0.9695 0.2483  -0.4519 -0.3593 203 ILE B CG2 
3777  C CD1 . ILE B 139 ? 0.9746 0.8682 1.0135 0.2039  -0.4524 -0.3533 203 ILE B CD1 
3778  N N   . HIS B 140 ? 1.2312 1.0054 1.0145 0.3194  -0.4816 -0.3792 204 HIS B N   
3779  C CA  . HIS B 140 ? 1.2920 1.0470 1.0131 0.3431  -0.4651 -0.3711 204 HIS B CA  
3780  C C   . HIS B 140 ? 1.4180 1.1731 1.1350 0.3350  -0.4435 -0.3601 204 HIS B C   
3781  O O   . HIS B 140 ? 1.4105 1.1692 1.1619 0.3170  -0.4500 -0.3649 204 HIS B O   
3782  C CB  . HIS B 140 ? 1.2787 0.9988 0.9502 0.3752  -0.4928 -0.3885 204 HIS B CB  
3783  C CG  . HIS B 140 ? 1.3640 1.0832 1.0369 0.3846  -0.5141 -0.3992 204 HIS B CG  
3784  N ND1 . HIS B 140 ? 1.4079 1.1273 1.0473 0.4017  -0.5021 -0.3909 204 HIS B ND1 
3785  C CD2 . HIS B 140 ? 1.5527 1.2726 1.2623 0.3778  -0.5471 -0.4170 204 HIS B CD2 
3786  C CE1 . HIS B 140 ? 1.5967 1.3158 1.2470 0.4066  -0.5268 -0.4038 204 HIS B CE1 
3787  N NE2 . HIS B 140 ? 1.5856 1.3052 1.2798 0.3918  -0.5546 -0.4197 204 HIS B NE2 
3788  N N   . PRO B 141 ? 1.4604 1.2118 1.1368 0.3484  -0.4169 -0.3440 205 PRO B N   
3789  C CA  . PRO B 141 ? 1.5117 1.2651 1.1848 0.3410  -0.3942 -0.3314 205 PRO B CA  
3790  C C   . PRO B 141 ? 1.8210 1.5439 1.4600 0.3588  -0.4092 -0.3430 205 PRO B C   
3791  O O   . PRO B 141 ? 1.9993 1.6950 1.5877 0.3890  -0.4222 -0.3512 205 PRO B O   
3792  C CB  . PRO B 141 ? 1.6651 1.4225 1.3048 0.3536  -0.3641 -0.3110 205 PRO B CB  
3793  C CG  . PRO B 141 ? 1.5038 1.2617 1.1303 0.3669  -0.3711 -0.3132 205 PRO B CG  
3794  C CD  . PRO B 141 ? 1.4925 1.2362 1.1236 0.3731  -0.4075 -0.3367 205 PRO B CD  
3795  N N   . THR B 142 ? 1.9820 1.7084 1.6473 0.3410  -0.4075 -0.3436 206 THR B N   
3796  C CA  . THR B 142 ? 2.0868 1.7857 1.7213 0.3556  -0.4174 -0.3519 206 THR B CA  
3797  C C   . THR B 142 ? 2.0784 1.7784 1.6854 0.3611  -0.3845 -0.3319 206 THR B C   
3798  O O   . THR B 142 ? 2.1508 1.8282 1.7027 0.3899  -0.3795 -0.3289 206 THR B O   
3799  C CB  . THR B 142 ? 1.9977 1.6991 1.6786 0.3329  -0.4345 -0.3636 206 THR B CB  
3800  O OG1 . THR B 142 ? 1.7708 1.5007 1.4936 0.3043  -0.4090 -0.3478 206 THR B OG1 
3801  C CG2 . THR B 142 ? 1.6903 1.3949 1.4092 0.3242  -0.4658 -0.3810 206 THR B CG2 
3802  N N   . ASN B 143 ? 1.9176 1.6445 1.5646 0.3340  -0.3617 -0.3174 207 ASN B N   
3803  C CA  . ASN B 143 ? 1.6765 1.4094 1.3107 0.3330  -0.3307 -0.2976 207 ASN B CA  
3804  C C   . ASN B 143 ? 1.5588 1.2915 1.1557 0.3527  -0.3085 -0.2806 207 ASN B C   
3805  O O   . ASN B 143 ? 1.3536 1.0953 0.9471 0.3500  -0.2812 -0.2617 207 ASN B O   
3806  C CB  . ASN B 143 ? 1.4647 1.2268 1.1535 0.2990  -0.3151 -0.2878 207 ASN B CB  
3807  C CG  . ASN B 143 ? 1.7846 1.5438 1.4724 0.2931  -0.3016 -0.2807 207 ASN B CG  
3808  O OD1 . ASN B 143 ? 2.1082 1.8442 1.7730 0.3057  -0.3146 -0.2910 207 ASN B OD1 
3809  N ND2 . ASN B 143 ? 1.9975 1.7794 1.7103 0.2742  -0.2765 -0.2635 207 ASN B ND2 
3810  N N   . GLY B 144 ? 1.7867 1.5096 1.3588 0.3720  -0.3204 -0.2870 208 GLY B N   
3811  C CA  . GLY B 144 ? 1.8726 1.5929 1.4077 0.3938  -0.3014 -0.2716 208 GLY B CA  
3812  C C   . GLY B 144 ? 2.1725 1.9227 1.7393 0.3752  -0.2790 -0.2541 208 GLY B C   
3813  O O   . GLY B 144 ? 2.3997 2.1732 2.0154 0.3453  -0.2752 -0.2522 208 GLY B O   
3814  N N   . GLY B 145 ? 2.1150 1.8635 1.6534 0.3938  -0.2639 -0.2408 209 GLY B N   
3815  C CA  . GLY B 145 ? 1.7123 1.4866 1.2774 0.3788  -0.2424 -0.2231 209 GLY B CA  
3816  C C   . GLY B 145 ? 1.5282 1.3199 1.1342 0.3573  -0.2577 -0.2343 209 GLY B C   
3817  O O   . GLY B 145 ? 1.4833 1.2699 1.1035 0.3508  -0.2823 -0.2534 209 GLY B O   
3818  N N   . PRO B 146 ? 1.5000 1.3122 1.1272 0.3461  -0.2435 -0.2219 210 PRO B N   
3819  C CA  . PRO B 146 ? 1.1151 0.9416 0.7733 0.3319  -0.2577 -0.2318 210 PRO B CA  
3820  C C   . PRO B 146 ? 1.0754 0.9185 0.7832 0.3017  -0.2642 -0.2387 210 PRO B C   
3821  O O   . PRO B 146 ? 1.2869 1.1381 1.0108 0.2872  -0.2493 -0.2294 210 PRO B O   
3822  C CB  . PRO B 146 ? 1.0301 0.8728 0.6955 0.3281  -0.2361 -0.2135 210 PRO B CB  
3823  C CG  . PRO B 146 ? 1.2898 1.1380 0.9580 0.3217  -0.2105 -0.1945 210 PRO B CG  
3824  C CD  . PRO B 146 ? 1.3870 1.2131 1.0214 0.3397  -0.2135 -0.1982 210 PRO B CD  
3825  N N   . LEU B 147 ? 0.9372 0.7847 0.6691 0.2935  -0.2862 -0.2544 211 LEU B N   
3826  C CA  . LEU B 147 ? 0.8913 0.7584 0.6751 0.2647  -0.2891 -0.2577 211 LEU B CA  
3827  C C   . LEU B 147 ? 1.0680 0.9592 0.8787 0.2480  -0.2704 -0.2436 211 LEU B C   
3828  O O   . LEU B 147 ? 1.0432 0.9363 0.8362 0.2579  -0.2596 -0.2339 211 LEU B O   
3829  C CB  . LEU B 147 ? 0.8415 0.7068 0.6469 0.2616  -0.3178 -0.2772 211 LEU B CB  
3830  C CG  . LEU B 147 ? 1.0192 0.8595 0.8034 0.2772  -0.3430 -0.2948 211 LEU B CG  
3831  C CD1 . LEU B 147 ? 1.3105 1.1477 1.1055 0.2821  -0.3708 -0.3114 211 LEU B CD1 
3832  C CD2 . LEU B 147 ? 1.2495 1.0911 1.0612 0.2603  -0.3463 -0.2990 211 LEU B CD2 
3833  N N   . ARG B 148 ? 1.0348 0.9434 0.8879 0.2233  -0.2668 -0.2425 212 ARG B N   
3834  C CA  . ARG B 148 ? 0.9402 0.8696 0.8187 0.2069  -0.2500 -0.2301 212 ARG B CA  
3835  C C   . ARG B 148 ? 0.9549 0.9005 0.8800 0.1861  -0.2583 -0.2369 212 ARG B C   
3836  O O   . ARG B 148 ? 1.0960 1.0403 1.0401 0.1772  -0.2669 -0.2444 212 ARG B O   
3837  C CB  . ARG B 148 ? 1.0091 0.9418 0.8841 0.2003  -0.2268 -0.2141 212 ARG B CB  
3838  C CG  . ARG B 148 ? 1.1148 1.0335 0.9480 0.2210  -0.2152 -0.2039 212 ARG B CG  
3839  C CD  . ARG B 148 ? 1.4392 1.3620 1.2741 0.2135  -0.1932 -0.1875 212 ARG B CD  
3840  N NE  . ARG B 148 ? 1.4805 1.3996 1.3238 0.2052  -0.1951 -0.1919 212 ARG B NE  
3841  C CZ  . ARG B 148 ? 1.4807 1.3823 1.2968 0.2196  -0.1988 -0.1955 212 ARG B CZ  
3842  N NH1 . ARG B 148 ? 1.3494 1.2346 1.1260 0.2446  -0.2006 -0.1951 212 ARG B NH1 
3843  N NH2 . ARG B 148 ? 1.5967 1.4962 1.4240 0.2100  -0.2004 -0.1993 212 ARG B NH2 
3844  N N   . THR B 149 ? 1.0693 1.0297 1.0126 0.1793  -0.2554 -0.2335 213 THR B N   
3845  C CA  . THR B 149 ? 0.9333 0.9105 0.9211 0.1611  -0.2602 -0.2371 213 THR B CA  
3846  C C   . THR B 149 ? 0.8378 0.8296 0.8457 0.1438  -0.2394 -0.2238 213 THR B C   
3847  O O   . THR B 149 ? 0.7699 0.7600 0.7591 0.1457  -0.2226 -0.2118 213 THR B O   
3848  C CB  . THR B 149 ? 0.9017 0.8869 0.8992 0.1645  -0.2697 -0.2415 213 THR B CB  
3849  O OG1 . THR B 149 ? 0.7193 0.7076 0.6977 0.1701  -0.2550 -0.2301 213 THR B OG1 
3850  C CG2 . THR B 149 ? 0.9191 0.8902 0.9010 0.1810  -0.2937 -0.2565 213 THR B CG2 
3851  N N   . GLN B 150 ? 0.7615 0.7673 0.8082 0.1281  -0.2407 -0.2253 214 GLN B N   
3852  C CA  . GLN B 150 ? 0.6604 0.6789 0.7260 0.1128  -0.2224 -0.2137 214 GLN B CA  
3853  C C   . GLN B 150 ? 0.6300 0.6540 0.6845 0.1143  -0.2092 -0.2031 214 GLN B C   
3854  O O   . GLN B 150 ? 0.7005 0.7291 0.7585 0.1058  -0.1939 -0.1928 214 GLN B O   
3855  C CB  . GLN B 150 ? 0.7606 0.7931 0.8683 0.0992  -0.2260 -0.2165 214 GLN B CB  
3856  C CG  . GLN B 150 ? 0.8612 0.8897 0.9877 0.0955  -0.2393 -0.2261 214 GLN B CG  
3857  C CD  . GLN B 150 ? 0.7981 0.8417 0.9697 0.0821  -0.2400 -0.2258 214 GLN B CD  
3858  O OE1 . GLN B 150 ? 0.6987 0.7538 0.8867 0.0805  -0.2395 -0.2239 214 GLN B OE1 
3859  N NE2 . GLN B 150 ? 1.4290 1.4725 1.6218 0.0730  -0.2402 -0.2268 214 GLN B NE2 
3860  N N   . ALA B 151 ? 0.6235 0.6465 0.6660 0.1252  -0.2161 -0.2059 215 ALA B N   
3861  C CA  . ALA B 151 ? 0.5564 0.5846 0.5911 0.1266  -0.2050 -0.1963 215 ALA B CA  
3862  C C   . ALA B 151 ? 0.5602 0.6031 0.6248 0.1116  -0.1967 -0.1913 215 ALA B C   
3863  O O   . ALA B 151 ? 0.5352 0.5808 0.5968 0.1071  -0.1830 -0.1810 215 ALA B O   
3864  C CB  . ALA B 151 ? 0.4976 0.5174 0.5059 0.1316  -0.1913 -0.1853 215 ALA B CB  
3865  N N   . SER B 152 ? 0.5509 0.6021 0.6446 0.1051  -0.2058 -0.1986 216 SER B N   
3866  C CA  . SER B 152 ? 0.6369 0.7014 0.7608 0.0924  -0.1982 -0.1942 216 SER B CA  
3867  C C   . SER B 152 ? 0.6550 0.7270 0.8082 0.0909  -0.2127 -0.2035 216 SER B C   
3868  O O   . SER B 152 ? 0.7218 0.7868 0.8734 0.0962  -0.2278 -0.2133 216 SER B O   
3869  C CB  . SER B 152 ? 0.6920 0.7554 0.8233 0.0821  -0.1881 -0.1894 216 SER B CB  
3870  O OG  . SER B 152 ? 0.9655 1.0407 1.1287 0.0712  -0.1826 -0.1866 216 SER B OG  
3871  N N   . SER B 153 ? 0.6271 0.7128 0.8078 0.0843  -0.2084 -0.1999 217 SER B N   
3872  C CA  . SER B 153 ? 0.5564 0.6523 0.7744 0.0803  -0.2193 -0.2057 217 SER B CA  
3873  C C   . SER B 153 ? 0.6035 0.6960 0.8395 0.0743  -0.2266 -0.2110 217 SER B C   
3874  O O   . SER B 153 ? 0.6546 0.7450 0.8901 0.0671  -0.2150 -0.2054 217 SER B O   
3875  C CB  . SER B 153 ? 0.4565 0.5671 0.7003 0.0730  -0.2064 -0.1966 217 SER B CB  
3876  O OG  . SER B 153 ? 0.5375 0.6598 0.8240 0.0674  -0.2129 -0.1987 217 SER B OG  
3877  N N   . CYS B 154 ? 0.5351 0.6259 0.7863 0.0778  -0.2468 -0.2221 218 CYS B N   
3878  C CA  . CYS B 154 ? 0.5940 0.6830 0.8712 0.0711  -0.2560 -0.2276 218 CYS B CA  
3879  C C   . CYS B 154 ? 0.6661 0.7729 0.9933 0.0602  -0.2510 -0.2216 218 CYS B C   
3880  O O   . CYS B 154 ? 0.6332 0.7521 0.9698 0.0596  -0.2413 -0.2143 218 CYS B O   
3881  C CB  . CYS B 154 ? 0.7492 0.8270 1.0226 0.0802  -0.2819 -0.2425 218 CYS B CB  
3882  S SG  . CYS B 154 ? 1.1598 1.2394 1.4252 0.0929  -0.2967 -0.2493 218 CYS B SG  
3883  N N   . ILE B 155 ? 0.7149 0.8230 1.0745 0.0522  -0.2568 -0.2238 219 ILE B N   
3884  C CA  . ILE B 155 ? 0.6177 0.7427 1.0262 0.0420  -0.2485 -0.2153 219 ILE B CA  
3885  C C   . ILE B 155 ? 0.6407 0.7721 1.0945 0.0402  -0.2690 -0.2225 219 ILE B C   
3886  O O   . ILE B 155 ? 0.8842 1.0051 1.3446 0.0399  -0.2869 -0.2328 219 ILE B O   
3887  C CB  . ILE B 155 ? 0.5838 0.7077 0.9999 0.0328  -0.2338 -0.2079 219 ILE B CB  
3888  C CG1 . ILE B 155 ? 0.7449 0.8673 1.1271 0.0334  -0.2114 -0.1978 219 ILE B CG1 
3889  C CG2 . ILE B 155 ? 0.5012 0.6410 0.9725 0.0235  -0.2278 -0.1997 219 ILE B CG2 
3890  C CD1 . ILE B 155 ? 1.1033 1.2106 1.4349 0.0413  -0.2132 -0.2024 219 ILE B CD1 
3891  N N   . CYS B 156 ? 0.6928 0.8405 1.1784 0.0394  -0.2675 -0.2174 220 CYS B N   
3892  C CA  . CYS B 156 ? 0.6849 0.8412 1.2227 0.0363  -0.2864 -0.2222 220 CYS B CA  
3893  C C   . CYS B 156 ? 0.6701 0.8442 1.2591 0.0260  -0.2704 -0.2079 220 CYS B C   
3894  O O   . CYS B 156 ? 0.8763 1.0601 1.4611 0.0254  -0.2472 -0.1948 220 CYS B O   
3895  C CB  . CYS B 156 ? 0.7201 0.8811 1.2600 0.0448  -0.3016 -0.2286 220 CYS B CB  
3896  S SG  . CYS B 156 ? 1.4362 1.5756 1.9131 0.0600  -0.3190 -0.2440 220 CYS B SG  
3897  N N   . ASN B 157 ? 0.8683 1.0451 1.5046 0.0188  -0.2829 -0.2102 221 ASN B N   
3898  C CA  . ASN B 157 ? 0.9059 1.1003 1.5991 0.0096  -0.2696 -0.1959 221 ASN B CA  
3899  C C   . ASN B 157 ? 0.9438 1.1421 1.6948 0.0048  -0.2944 -0.2025 221 ASN B C   
3900  O O   . ASN B 157 ? 1.1530 1.3366 1.9032 0.0029  -0.3134 -0.2144 221 ASN B O   
3901  C CB  . ASN B 157 ? 0.8873 1.0777 1.5733 0.0030  -0.2491 -0.1868 221 ASN B CB  
3902  C CG  . ASN B 157 ? 0.9172 1.1261 1.6463 -0.0026 -0.2254 -0.1676 221 ASN B CG  
3903  O OD1 . ASN B 157 ? 0.8426 1.0649 1.5791 0.0015  -0.2131 -0.1581 221 ASN B OD1 
3904  N ND2 . ASN B 157 ? 0.9316 1.1407 1.6886 -0.0107 -0.2186 -0.1614 221 ASN B ND2 
3905  N N   . ASP B 158 ? 0.8629 1.0804 1.6642 0.0034  -0.2948 -0.1947 222 ASP B N   
3906  C CA  . ASP B 158 ? 0.9590 1.1830 1.8247 -0.0018 -0.3188 -0.1992 222 ASP B CA  
3907  C C   . ASP B 158 ? 0.9754 1.1832 1.8236 0.0049  -0.3545 -0.2210 222 ASP B C   
3908  O O   . ASP B 158 ? 1.0716 1.2719 1.9522 0.0009  -0.3793 -0.2308 222 ASP B O   
3909  C CB  . ASP B 158 ? 1.0956 1.3188 2.0027 -0.0129 -0.3169 -0.1939 222 ASP B CB  
3910  C CG  . ASP B 158 ? 1.3910 1.6330 2.3331 -0.0188 -0.2848 -0.1708 222 ASP B CG  
3911  O OD1 . ASP B 158 ? 1.4108 1.6694 2.3629 -0.0150 -0.2688 -0.1587 222 ASP B OD1 
3912  O OD2 . ASP B 158 ? 1.7093 1.9487 2.6678 -0.0263 -0.2752 -0.1644 222 ASP B OD2 
3913  N N   . GLY B 159 ? 0.9032 1.1040 1.6985 0.0160  -0.3574 -0.2287 223 GLY B N   
3914  C CA  . GLY B 159 ? 1.0339 1.2216 1.8144 0.0252  -0.3902 -0.2478 223 GLY B CA  
3915  C C   . GLY B 159 ? 0.9122 1.0725 1.6429 0.0314  -0.4073 -0.2646 223 GLY B C   
3916  O O   . GLY B 159 ? 0.9310 1.0771 1.6370 0.0424  -0.4329 -0.2807 223 GLY B O   
3917  N N   . THR B 160 ? 0.8300 0.9824 1.5460 0.0255  -0.3931 -0.2605 224 THR B N   
3918  C CA  . THR B 160 ? 0.8561 0.9829 1.5167 0.0323  -0.4018 -0.2731 224 THR B CA  
3919  C C   . THR B 160 ? 0.7957 0.9195 1.3970 0.0362  -0.3735 -0.2649 224 THR B C   
3920  O O   . THR B 160 ? 0.7901 0.9284 1.4010 0.0291  -0.3462 -0.2491 224 THR B O   
3921  C CB  . THR B 160 ? 0.8769 0.9938 1.5633 0.0236  -0.4107 -0.2766 224 THR B CB  
3922  O OG1 . THR B 160 ? 0.7558 0.8858 1.4635 0.0117  -0.3816 -0.2592 224 THR B OG1 
3923  C CG2 . THR B 160 ? 0.7548 0.8734 1.5039 0.0193  -0.4413 -0.2850 224 THR B CG2 
3924  N N   . CYS B 161 ? 0.8114 0.9161 1.3524 0.0484  -0.3801 -0.2751 225 CYS B N   
3925  C CA  . CYS B 161 ? 0.7150 0.8168 1.2037 0.0523  -0.3552 -0.2670 225 CYS B CA  
3926  C C   . CYS B 161 ? 0.6894 0.7710 1.1393 0.0551  -0.3552 -0.2723 225 CYS B C   
3927  O O   . CYS B 161 ? 0.9558 1.0205 1.3991 0.0609  -0.3786 -0.2861 225 CYS B O   
3928  C CB  . CYS B 161 ? 0.9113 1.0107 1.3620 0.0654  -0.3582 -0.2707 225 CYS B CB  
3929  S SG  . CYS B 161 ? 1.3271 1.4495 1.8208 0.0640  -0.3598 -0.2654 225 CYS B SG  
3930  N N   . TYR B 162 ? 0.6404 0.7229 1.0646 0.0518  -0.3297 -0.2614 226 TYR B N   
3931  C CA  . TYR B 162 ? 0.6034 0.6688 0.9926 0.0535  -0.3256 -0.2636 226 TYR B CA  
3932  C C   . TYR B 162 ? 0.6184 0.6767 0.9516 0.0631  -0.3116 -0.2598 226 TYR B C   
3933  O O   . TYR B 162 ? 0.8176 0.8879 1.1463 0.0608  -0.2928 -0.2488 226 TYR B O   
3934  C CB  . TYR B 162 ? 0.5800 0.6531 0.9943 0.0396  -0.3068 -0.2524 226 TYR B CB  
3935  C CG  . TYR B 162 ? 0.6520 0.7358 1.1286 0.0288  -0.3154 -0.2517 226 TYR B CG  
3936  C CD1 . TYR B 162 ? 0.6735 0.7457 1.1681 0.0257  -0.3323 -0.2604 226 TYR B CD1 
3937  C CD2 . TYR B 162 ? 0.7267 0.8319 1.2461 0.0226  -0.3072 -0.2419 226 TYR B CD2 
3938  C CE1 . TYR B 162 ? 0.8504 0.9326 1.4075 0.0154  -0.3412 -0.2590 226 TYR B CE1 
3939  C CE2 . TYR B 162 ? 0.9188 1.0351 1.5004 0.0131  -0.3143 -0.2394 226 TYR B CE2 
3940  C CZ  . TYR B 162 ? 1.0548 1.1596 1.6565 0.0091  -0.3316 -0.2479 226 TYR B CZ  
3941  O OH  . TYR B 162 ? 1.0251 1.1406 1.6924 -0.0007 -0.3393 -0.2446 226 TYR B OH  
3942  N N   . THR B 163 ? 0.5651 0.6033 0.8562 0.0746  -0.3210 -0.2684 227 THR B N   
3943  C CA  . THR B 163 ? 0.6708 0.7019 0.9114 0.0838  -0.3065 -0.2630 227 THR B CA  
3944  C C   . THR B 163 ? 0.7201 0.7325 0.9269 0.0894  -0.3059 -0.2658 227 THR B C   
3945  O O   . THR B 163 ? 0.8075 0.8085 1.0219 0.0904  -0.3224 -0.2758 227 THR B O   
3946  C CB  . THR B 163 ? 0.7218 0.7491 0.9357 0.0985  -0.3157 -0.2679 227 THR B CB  
3947  O OG1 . THR B 163 ? 0.8770 0.8993 1.0474 0.1059  -0.2984 -0.2596 227 THR B OG1 
3948  C CG2 . THR B 163 ? 0.7603 0.7691 0.9597 0.1121  -0.3433 -0.2843 227 THR B CG2 
3949  N N   . ILE B 164 ? 0.7396 0.7487 0.9106 0.0933  -0.2872 -0.2565 228 ILE B N   
3950  C CA  . ILE B 164 ? 0.7267 0.7198 0.8654 0.0990  -0.2831 -0.2565 228 ILE B CA  
3951  C C   . ILE B 164 ? 0.8432 0.8220 0.9320 0.1179  -0.2840 -0.2576 228 ILE B C   
3952  O O   . ILE B 164 ? 0.9951 0.9799 1.0687 0.1214  -0.2718 -0.2491 228 ILE B O   
3953  C CB  . ILE B 164 ? 0.6488 0.6496 0.7922 0.0868  -0.2595 -0.2431 228 ILE B CB  
3954  C CG1 . ILE B 164 ? 0.6157 0.6267 0.8046 0.0709  -0.2593 -0.2425 228 ILE B CG1 
3955  C CG2 . ILE B 164 ? 0.8611 0.8461 0.9704 0.0935  -0.2539 -0.2418 228 ILE B CG2 
3956  C CD1 . ILE B 164 ? 0.6099 0.6317 0.8076 0.0592  -0.2360 -0.2289 228 ILE B CD1 
3957  N N   . ILE B 165 ? 0.9294 0.8879 0.9926 0.1308  -0.2982 -0.2675 229 ILE B N   
3958  C CA  . ILE B 165 ? 0.8552 0.7972 0.8693 0.1520  -0.3003 -0.2691 229 ILE B CA  
3959  C C   . ILE B 165 ? 0.8965 0.8235 0.8773 0.1598  -0.2907 -0.2648 229 ILE B C   
3960  O O   . ILE B 165 ? 0.8847 0.8019 0.8697 0.1576  -0.2983 -0.2712 229 ILE B O   
3961  C CB  . ILE B 165 ? 0.9862 0.9142 0.9906 0.1670  -0.3280 -0.2856 229 ILE B CB  
3962  C CG1 . ILE B 165 ? 1.1693 1.1138 1.2145 0.1573  -0.3386 -0.2898 229 ILE B CG1 
3963  C CG2 . ILE B 165 ? 0.9942 0.9072 0.9472 0.1904  -0.3273 -0.2849 229 ILE B CG2 
3964  C CD1 . ILE B 165 ? 1.2805 1.2224 1.3065 0.1723  -0.3482 -0.2941 229 ILE B CD1 
3965  N N   . ALA B 166 ? 0.9028 0.8281 0.8517 0.1694  -0.2738 -0.2533 230 ALA B N   
3966  C CA  . ALA B 166 ? 1.0401 0.9536 0.9572 0.1781  -0.2606 -0.2454 230 ALA B CA  
3967  C C   . ALA B 166 ? 1.1228 1.0138 0.9924 0.2047  -0.2694 -0.2506 230 ALA B C   
3968  O O   . ALA B 166 ? 1.2195 1.1080 1.0726 0.2177  -0.2748 -0.2525 230 ALA B O   
3969  C CB  . ALA B 166 ? 0.9661 0.8928 0.8831 0.1711  -0.2349 -0.2270 230 ALA B CB  
3970  N N   . ASP B 167 ? 1.0296 0.9041 0.8761 0.2137  -0.2696 -0.2522 231 ASP B N   
3971  C CA  . ASP B 167 ? 1.0337 0.8840 0.8304 0.2413  -0.2754 -0.2558 231 ASP B CA  
3972  C C   . ASP B 167 ? 1.1121 0.9570 0.8834 0.2481  -0.2528 -0.2405 231 ASP B C   
3973  O O   . ASP B 167 ? 1.0775 0.9325 0.8703 0.2312  -0.2397 -0.2327 231 ASP B O   
3974  C CB  . ASP B 167 ? 1.2386 1.0698 1.0313 0.2483  -0.3030 -0.2758 231 ASP B CB  
3975  C CG  . ASP B 167 ? 1.5706 1.3759 1.3146 0.2787  -0.3185 -0.2854 231 ASP B CG  
3976  O OD1 . ASP B 167 ? 2.0556 1.8573 1.7659 0.2958  -0.3047 -0.2747 231 ASP B OD1 
3977  O OD2 . ASP B 167 ? 1.6818 1.4693 1.4212 0.2864  -0.3450 -0.3036 231 ASP B OD2 
3978  N N   . GLY B 168 ? 1.0708 0.8997 0.7970 0.2736  -0.2477 -0.2355 232 GLY B N   
3979  C CA  . GLY B 168 ? 1.1990 1.0204 0.9008 0.2829  -0.2284 -0.2218 232 GLY B CA  
3980  C C   . GLY B 168 ? 1.4171 1.2429 1.0997 0.2943  -0.2051 -0.2017 232 GLY B C   
3981  O O   . GLY B 168 ? 1.2877 1.1295 0.9876 0.2861  -0.1979 -0.1943 232 GLY B O   
3982  N N   . THR B 169 ? 1.5555 1.3667 1.2034 0.3137  -0.1930 -0.1921 233 THR B N   
3983  C CA  . THR B 169 ? 1.4442 1.2555 1.0695 0.3300  -0.1709 -0.1719 233 THR B CA  
3984  C C   . THR B 169 ? 1.2223 1.0574 0.8830 0.3083  -0.1488 -0.1530 233 THR B C   
3985  O O   . THR B 169 ? 1.1212 0.9658 0.7857 0.3099  -0.1364 -0.1398 233 THR B O   
3986  C CB  . THR B 169 ? 1.6876 1.4766 1.2684 0.3568  -0.1628 -0.1656 233 THR B CB  
3987  O OG1 . THR B 169 ? 1.7789 1.5429 1.3262 0.3766  -0.1867 -0.1856 233 THR B OG1 
3988  C CG2 . THR B 169 ? 1.7188 1.5058 1.2741 0.3781  -0.1404 -0.1440 233 THR B CG2 
3989  N N   . THR B 170 ? 1.5428 1.3862 1.2291 0.2887  -0.1448 -0.1521 234 THR B N   
3990  C CA  . THR B 170 ? 1.4642 1.3278 1.1829 0.2686  -0.1258 -0.1355 234 THR B CA  
3991  C C   . THR B 170 ? 1.2497 1.1248 1.0048 0.2418  -0.1321 -0.1439 234 THR B C   
3992  O O   . THR B 170 ? 1.6852 1.5517 1.4398 0.2399  -0.1488 -0.1605 234 THR B O   
3993  C CB  . THR B 170 ? 1.6010 1.4609 1.3045 0.2802  -0.1038 -0.1152 234 THR B CB  
3994  O OG1 . THR B 170 ? 2.0251 1.9043 1.7638 0.2593  -0.0886 -0.1005 234 THR B OG1 
3995  C CG2 . THR B 170 ? 1.1881 1.0322 0.8710 0.2893  -0.1068 -0.1208 234 THR B CG2 
3996  N N   . TYR B 171 ? 1.0703 0.9636 0.8566 0.2223  -0.1190 -0.1320 235 TYR B N   
3997  C CA  . TYR B 171 ? 1.1289 1.0353 0.9516 0.1967  -0.1237 -0.1386 235 TYR B CA  
3998  C C   . TYR B 171 ? 1.0846 0.9865 0.9103 0.1908  -0.1218 -0.1400 235 TYR B C   
3999  O O   . TYR B 171 ? 1.3148 1.2206 1.1620 0.1755  -0.1308 -0.1506 235 TYR B O   
4000  C CB  . TYR B 171 ? 1.1649 1.0892 1.0150 0.1808  -0.1119 -0.1263 235 TYR B CB  
4001  C CG  . TYR B 171 ? 1.9685 1.8959 1.8136 0.1881  -0.1135 -0.1245 235 TYR B CG  
4002  C CD1 . TYR B 171 ? 2.0410 1.9687 1.8891 0.1876  -0.1303 -0.1398 235 TYR B CD1 
4003  C CD2 . TYR B 171 ? 2.1390 2.0686 1.9774 0.1962  -0.0987 -0.1071 235 TYR B CD2 
4004  C CE1 . TYR B 171 ? 1.9178 1.8480 1.7602 0.1950  -0.1318 -0.1381 235 TYR B CE1 
4005  C CE2 . TYR B 171 ? 2.4901 2.4219 2.3237 0.2034  -0.0997 -0.1050 235 TYR B CE2 
4006  C CZ  . TYR B 171 ? 2.1558 2.0878 1.9900 0.2029  -0.1162 -0.1208 235 TYR B CZ  
4007  O OH  . TYR B 171 ? 2.1040 2.0380 1.9328 0.2103  -0.1171 -0.1186 235 TYR B OH  
4008  N N   . THR B 172 ? 1.0606 0.9539 0.8643 0.2044  -0.1094 -0.1285 236 THR B N   
4009  C CA  . THR B 172 ? 1.0552 0.9393 0.8513 0.2056  -0.1086 -0.1306 236 THR B CA  
4010  C C   . THR B 172 ? 1.0549 0.9231 0.8367 0.2126  -0.1300 -0.1515 236 THR B C   
4011  O O   . THR B 172 ? 1.4274 1.2922 1.2189 0.2036  -0.1358 -0.1593 236 THR B O   
4012  C CB  . THR B 172 ? 1.1792 1.0547 0.9484 0.2249  -0.0919 -0.1141 236 THR B CB  
4013  O OG1 . THR B 172 ? 1.3514 1.2076 1.0807 0.2513  -0.0987 -0.1197 236 THR B OG1 
4014  C CG2 . THR B 172 ? 0.9576 0.8466 0.7395 0.2225  -0.0744 -0.0942 236 THR B CG2 
4015  N N   . ALA B 173 ? 1.0139 0.8722 0.7749 0.2282  -0.1425 -0.1605 237 ALA B N   
4016  C CA  . ALA B 173 ? 1.2743 1.1132 1.0155 0.2403  -0.1645 -0.1799 237 ALA B CA  
4017  C C   . ALA B 173 ? 1.2328 1.0760 0.9941 0.2314  -0.1855 -0.1964 237 ALA B C   
4018  O O   . ALA B 173 ? 1.5447 1.3712 1.2887 0.2440  -0.2059 -0.2123 237 ALA B O   
4019  C CB  . ALA B 173 ? 1.3870 1.2045 1.0786 0.2722  -0.1642 -0.1779 237 ALA B CB  
4020  N N   . SER B 174 ? 1.0850 0.9494 0.8826 0.2106  -0.1813 -0.1929 238 SER B N   
4021  C CA  . SER B 174 ? 1.1080 0.9785 0.9263 0.2030  -0.1988 -0.2061 238 SER B CA  
4022  C C   . SER B 174 ? 1.0577 0.9237 0.8973 0.1931  -0.2188 -0.2232 238 SER B C   
4023  O O   . SER B 174 ? 1.1910 1.0553 1.0409 0.1841  -0.2161 -0.2233 238 SER B O   
4024  C CB  . SER B 174 ? 1.0028 0.8966 0.8532 0.1846  -0.1877 -0.1968 238 SER B CB  
4025  O OG  . SER B 174 ? 1.3685 1.2746 1.2485 0.1638  -0.1781 -0.1914 238 SER B OG  
4026  N N   . SER B 175 ? 0.9208 0.7850 0.7688 0.1948  -0.2388 -0.2369 239 SER B N   
4027  C CA  . SER B 175 ? 0.9639 0.8254 0.8387 0.1851  -0.2598 -0.2527 239 SER B CA  
4028  C C   . SER B 175 ? 1.0016 0.8810 0.9121 0.1718  -0.2661 -0.2557 239 SER B C   
4029  O O   . SER B 175 ? 1.2077 1.0908 1.1070 0.1799  -0.2654 -0.2534 239 SER B O   
4030  C CB  . SER B 175 ? 1.1742 1.0098 1.0183 0.2066  -0.2835 -0.2688 239 SER B CB  
4031  O OG  . SER B 175 ? 1.7116 1.5446 1.5860 0.1973  -0.3070 -0.2848 239 SER B OG  
4032  N N   . HIS B 176 ? 0.9871 0.8777 0.9407 0.1525  -0.2718 -0.2601 240 HIS B N   
4033  C CA  . HIS B 176 ? 0.7818 0.6910 0.7724 0.1396  -0.2756 -0.2610 240 HIS B CA  
4034  C C   . HIS B 176 ? 0.7755 0.6838 0.8002 0.1320  -0.2973 -0.2745 240 HIS B C   
4035  O O   . HIS B 176 ? 0.9128 0.8193 0.9580 0.1219  -0.2993 -0.2768 240 HIS B O   
4036  C CB  . HIS B 176 ? 0.7982 0.7286 0.8143 0.1211  -0.2530 -0.2463 240 HIS B CB  
4037  C CG  . HIS B 176 ? 0.8322 0.7648 0.8208 0.1265  -0.2317 -0.2317 240 HIS B CG  
4038  N ND1 . HIS B 176 ? 0.8786 0.8195 0.8578 0.1301  -0.2218 -0.2231 240 HIS B ND1 
4039  C CD2 . HIS B 176 ? 0.8847 0.8098 0.8537 0.1294  -0.2195 -0.2244 240 HIS B CD2 
4040  C CE1 . HIS B 176 ? 0.9911 0.9299 0.9487 0.1341  -0.2041 -0.2104 240 HIS B CE1 
4041  N NE2 . HIS B 176 ? 1.0487 0.9783 1.0003 0.1338  -0.2025 -0.2110 240 HIS B NE2 
4042  N N   . ARG B 177 ? 0.8031 0.7125 0.8362 0.1369  -0.3143 -0.2834 241 ARG B N   
4043  C CA  . ARG B 177 ? 0.7709 0.6826 0.8454 0.1281  -0.3356 -0.2951 241 ARG B CA  
4044  C C   . ARG B 177 ? 0.7971 0.7335 0.9138 0.1133  -0.3299 -0.2891 241 ARG B C   
4045  O O   . ARG B 177 ? 0.7048 0.6513 0.8118 0.1162  -0.3199 -0.2823 241 ARG B O   
4046  C CB  . ARG B 177 ? 0.8184 0.7089 0.8744 0.1458  -0.3655 -0.3129 241 ARG B CB  
4047  C CG  . ARG B 177 ? 1.0024 0.8658 1.0121 0.1637  -0.3721 -0.3194 241 ARG B CG  
4048  C CD  . ARG B 177 ? 1.1678 1.0139 1.1287 0.1892  -0.3822 -0.3258 241 ARG B CD  
4049  N NE  . ARG B 177 ? 1.2467 1.0769 1.2118 0.1990  -0.4162 -0.3452 241 ARG B NE  
4050  C CZ  . ARG B 177 ? 1.1222 0.9251 1.0646 0.2130  -0.4376 -0.3593 241 ARG B CZ  
4051  N NH1 . ARG B 177 ? 0.9877 0.7767 0.9006 0.2190  -0.4270 -0.3556 241 ARG B NH1 
4052  N NH2 . ARG B 177 ? 1.0053 0.7941 0.9543 0.2215  -0.4705 -0.3774 241 ARG B NH2 
4053  N N   . LEU B 178 ? 0.7848 0.7303 0.9496 0.0981  -0.3362 -0.2912 242 LEU B N   
4054  C CA  . LEU B 178 ? 0.7756 0.7436 0.9850 0.0847  -0.3318 -0.2856 242 LEU B CA  
4055  C C   . LEU B 178 ? 0.8680 0.8321 1.1008 0.0890  -0.3610 -0.2999 242 LEU B C   
4056  O O   . LEU B 178 ? 0.8705 0.8244 1.1238 0.0871  -0.3802 -0.3100 242 LEU B O   
4057  C CB  . LEU B 178 ? 0.8538 0.8327 1.1010 0.0668  -0.3190 -0.2773 242 LEU B CB  
4058  C CG  . LEU B 178 ? 1.1256 1.1253 1.4307 0.0513  -0.3163 -0.2718 242 LEU B CG  
4059  C CD1 . LEU B 178 ? 1.5731 1.5908 1.8794 0.0496  -0.3002 -0.2613 242 LEU B CD1 
4060  C CD2 . LEU B 178 ? 0.9970 1.0011 1.3238 0.0380  -0.3012 -0.2632 242 LEU B CD2 
4061  N N   . TYR B 179 ? 0.8017 0.7726 1.0304 0.0957  -0.3655 -0.3011 243 TYR B N   
4062  C CA  . TYR B 179 ? 0.7377 0.7056 0.9876 0.1010  -0.3941 -0.3146 243 TYR B CA  
4063  C C   . TYR B 179 ? 0.7334 0.7244 1.0436 0.0860  -0.3943 -0.3098 243 TYR B C   
4064  O O   . TYR B 179 ? 0.9631 0.9738 1.2872 0.0765  -0.3711 -0.2956 243 TYR B O   
4065  C CB  . TYR B 179 ? 0.7843 0.7450 0.9936 0.1190  -0.4004 -0.3192 243 TYR B CB  
4066  C CG  . TYR B 179 ? 0.8533 0.7863 1.0098 0.1388  -0.4129 -0.3296 243 TYR B CG  
4067  C CD1 . TYR B 179 ? 0.9106 0.8353 1.0199 0.1467  -0.3924 -0.3211 243 TYR B CD1 
4068  C CD2 . TYR B 179 ? 0.7875 0.7011 0.9416 0.1505  -0.4456 -0.3478 243 TYR B CD2 
4069  C CE1 . TYR B 179 ? 0.9857 0.8839 1.0446 0.1671  -0.4024 -0.3295 243 TYR B CE1 
4070  C CE2 . TYR B 179 ? 0.8964 0.7816 0.9978 0.1712  -0.4574 -0.3578 243 TYR B CE2 
4071  C CZ  . TYR B 179 ? 0.8962 0.7740 0.9494 0.1800  -0.4347 -0.3480 243 TYR B CZ  
4072  O OH  . TYR B 179 ? 0.9165 0.7660 0.9161 0.2026  -0.4444 -0.3563 243 TYR B OH  
4073  N N   . ARG B 180 ? 0.7429 0.7307 1.0888 0.0851  -0.4214 -0.3214 244 ARG B N   
4074  C CA  . ARG B 180 ? 0.7414 0.7513 1.1482 0.0730  -0.4245 -0.3171 244 ARG B CA  
4075  C C   . ARG B 180 ? 0.6665 0.6728 1.0713 0.0848  -0.4489 -0.3288 244 ARG B C   
4076  O O   . ARG B 180 ? 0.7658 0.7501 1.1507 0.0975  -0.4760 -0.3450 244 ARG B O   
4077  C CB  . ARG B 180 ? 0.8833 0.8944 1.3442 0.0597  -0.4353 -0.3190 244 ARG B CB  
4078  C CG  . ARG B 180 ? 0.8533 0.8832 1.3848 0.0486  -0.4456 -0.3167 244 ARG B CG  
4079  C CD  . ARG B 180 ? 0.9970 1.0243 1.5763 0.0362  -0.4543 -0.3175 244 ARG B CD  
4080  N NE  . ARG B 180 ? 2.1752 2.2027 2.8065 0.0346  -0.4860 -0.3278 244 ARG B NE  
4081  C CZ  . ARG B 180 ? 2.6219 2.6705 3.3254 0.0208  -0.4853 -0.3186 244 ARG B CZ  
4082  N NH1 . ARG B 180 ? 2.7535 2.8237 3.4833 0.0084  -0.4535 -0.2988 244 ARG B NH1 
4083  N NH2 . ARG B 180 ? 2.4397 2.4868 3.1899 0.0203  -0.5169 -0.3289 244 ARG B NH2 
4084  N N   . LEU B 181 ? 0.6657 0.6921 1.0888 0.0821  -0.4398 -0.3209 245 LEU B N   
4085  C CA  . LEU B 181 ? 0.8096 0.8344 1.2323 0.0934  -0.4623 -0.3312 245 LEU B CA  
4086  C C   . LEU B 181 ? 0.9302 0.9772 1.4211 0.0818  -0.4687 -0.3271 245 LEU B C   
4087  O O   . LEU B 181 ? 1.0434 1.1119 1.5688 0.0677  -0.4453 -0.3114 245 LEU B O   
4088  C CB  . LEU B 181 ? 0.7072 0.7338 1.0818 0.1046  -0.4469 -0.3260 245 LEU B CB  
4089  C CG  . LEU B 181 ? 0.6846 0.6951 0.9968 0.1138  -0.4312 -0.3235 245 LEU B CG  
4090  C CD1 . LEU B 181 ? 0.7586 0.7810 1.0454 0.1154  -0.4050 -0.3102 245 LEU B CD1 
4091  C CD2 . LEU B 181 ? 0.6801 0.6636 0.9479 0.1338  -0.4549 -0.3395 245 LEU B CD2 
4092  N N   . VAL B 182 ? 0.9680 1.0098 1.4778 0.0889  -0.5002 -0.3408 246 VAL B N   
4093  C CA  . VAL B 182 ? 0.9105 0.9739 1.4860 0.0801  -0.5088 -0.3372 246 VAL B CA  
4094  C C   . VAL B 182 ? 0.8632 0.9231 1.4246 0.0945  -0.5300 -0.3479 246 VAL B C   
4095  O O   . VAL B 182 ? 0.8199 0.8561 1.3508 0.1091  -0.5579 -0.3655 246 VAL B O   
4096  C CB  . VAL B 182 ? 0.9474 1.0099 1.5864 0.0696  -0.5324 -0.3432 246 VAL B CB  
4097  C CG1 . VAL B 182 ? 0.9392 1.0290 1.6531 0.0582  -0.5334 -0.3338 246 VAL B CG1 
4098  C CG2 . VAL B 182 ? 0.7613 0.8198 1.4068 0.0583  -0.5176 -0.3368 246 VAL B CG2 
4099  N N   . ASN B 183 ? 0.9507 1.0334 1.5342 0.0913  -0.5172 -0.3373 247 ASN B N   
4100  C CA  . ASN B 183 ? 0.7763 0.8586 1.3486 0.1045  -0.5346 -0.3456 247 ASN B CA  
4101  C C   . ASN B 183 ? 0.7971 0.8523 1.2920 0.1251  -0.5440 -0.3584 247 ASN B C   
4102  O O   . ASN B 183 ? 0.8398 0.8831 1.3202 0.1396  -0.5703 -0.3723 247 ASN B O   
4103  C CB  . ASN B 183 ? 0.7686 0.8551 1.4029 0.1017  -0.5680 -0.3553 247 ASN B CB  
4104  C CG  . ASN B 183 ? 0.8360 0.9530 1.5484 0.0833  -0.5547 -0.3389 247 ASN B CG  
4105  O OD1 . ASN B 183 ? 0.8798 1.0131 1.5954 0.0738  -0.5204 -0.3211 247 ASN B OD1 
4106  N ND2 . ASN B 183 ? 0.8059 0.9303 1.5819 0.0792  -0.5817 -0.3444 247 ASN B ND2 
4107  N N   . GLY B 184 ? 0.7942 0.8394 1.2406 0.1269  -0.5219 -0.3529 248 GLY B N   
4108  C CA  . GLY B 184 ? 0.8452 0.8683 1.2178 0.1464  -0.5221 -0.3596 248 GLY B CA  
4109  C C   . GLY B 184 ? 0.9177 0.9106 1.2554 0.1582  -0.5428 -0.3747 248 GLY B C   
4110  O O   . GLY B 184 ? 0.9463 0.9195 1.2210 0.1758  -0.5409 -0.3788 248 GLY B O   
4111  N N   . THR B 185 ? 1.0197 1.0080 1.3983 0.1498  -0.5628 -0.3826 249 THR B N   
4112  C CA  . THR B 185 ? 1.2122 1.1703 1.5596 0.1608  -0.5836 -0.3975 249 THR B CA  
4113  C C   . THR B 185 ? 1.1691 1.1281 1.5250 0.1467  -0.5645 -0.3888 249 THR B C   
4114  O O   . THR B 185 ? 1.2319 1.2141 1.6384 0.1265  -0.5471 -0.3756 249 THR B O   
4115  C CB  . THR B 185 ? 1.3293 1.2747 1.7101 0.1653  -0.6270 -0.4165 249 THR B CB  
4116  O OG1 . THR B 185 ? 1.4550 1.4251 1.9170 0.1442  -0.6294 -0.4099 249 THR B OG1 
4117  C CG2 . THR B 185 ? 1.3291 1.2647 1.6819 0.1856  -0.6490 -0.4285 249 THR B CG2 
4118  N N   . SER B 186 ? 1.0688 1.0029 1.3737 0.1584  -0.5658 -0.3950 250 SER B N   
4119  C CA  . SER B 186 ? 1.0400 0.9742 1.3491 0.1461  -0.5471 -0.3867 250 SER B CA  
4120  C C   . SER B 186 ? 0.9823 0.9149 1.3483 0.1336  -0.5690 -0.3942 250 SER B C   
4121  O O   . SER B 186 ? 0.9348 0.8485 1.3048 0.1432  -0.6038 -0.4118 250 SER B O   
4122  C CB  . SER B 186 ? 1.0971 1.0052 1.3369 0.1628  -0.5420 -0.3905 250 SER B CB  
4123  O OG  . SER B 186 ? 1.2675 1.1454 1.4814 0.1814  -0.5764 -0.4107 250 SER B OG  
4124  N N   . ALA B 187 ? 1.0267 0.9789 1.4379 0.1126  -0.5487 -0.3804 251 ALA B N   
4125  C CA  . ALA B 187 ? 0.9903 0.9434 1.4611 0.0987  -0.5649 -0.3841 251 ALA B CA  
4126  C C   . ALA B 187 ? 0.9646 0.9067 1.4169 0.0942  -0.5511 -0.3806 251 ALA B C   
4127  O O   . ALA B 187 ? 1.0311 0.9854 1.5298 0.0767  -0.5408 -0.3715 251 ALA B O   
4128  C CB  . ALA B 187 ? 1.1722 1.1579 1.7148 0.0789  -0.5516 -0.3692 251 ALA B CB  
4129  N N   . GLY B 188 ? 0.9974 0.9165 1.3809 0.1109  -0.5496 -0.3867 252 GLY B N   
4130  C CA  . GLY B 188 ? 0.9806 0.8865 1.3420 0.1089  -0.5384 -0.3846 252 GLY B CA  
4131  C C   . GLY B 188 ? 0.9950 0.9129 1.3255 0.1048  -0.4987 -0.3667 252 GLY B C   
4132  O O   . GLY B 188 ? 1.0634 1.0022 1.3960 0.1006  -0.4774 -0.3543 252 GLY B O   
4133  N N   . TRP B 189 ? 0.8851 0.7885 1.1868 0.1066  -0.4898 -0.3658 253 TRP B N   
4134  C CA  . TRP B 189 ? 0.9548 0.8672 1.2279 0.1030  -0.4545 -0.3496 253 TRP B CA  
4135  C C   . TRP B 189 ? 0.9675 0.8712 1.2386 0.0963  -0.4457 -0.3467 253 TRP B C   
4136  O O   . TRP B 189 ? 1.1524 1.0406 1.4398 0.0958  -0.4674 -0.3580 253 TRP B O   
4137  C CB  . TRP B 189 ? 1.0594 0.9601 1.2667 0.1231  -0.4481 -0.3501 253 TRP B CB  
4138  C CG  . TRP B 189 ? 1.1189 0.9873 1.2836 0.1435  -0.4725 -0.3666 253 TRP B CG  
4139  C CD1 . TRP B 189 ? 1.2962 1.1471 1.4494 0.1597  -0.5045 -0.3839 253 TRP B CD1 
4140  C CD2 . TRP B 189 ? 1.2805 1.1276 1.4069 0.1519  -0.4690 -0.3685 253 TRP B CD2 
4141  N NE1 . TRP B 189 ? 1.3431 1.1624 1.4514 0.1782  -0.5207 -0.3963 253 TRP B NE1 
4142  C CE2 . TRP B 189 ? 1.2505 1.0664 1.3412 0.1745  -0.5001 -0.3876 253 TRP B CE2 
4143  C CE3 . TRP B 189 ? 1.5484 1.3983 1.6657 0.1442  -0.4443 -0.3568 253 TRP B CE3 
4144  C CZ2 . TRP B 189 ? 1.1372 0.9259 1.1838 0.1892  -0.5046 -0.3938 253 TRP B CZ2 
4145  C CZ3 . TRP B 189 ? 1.5773 1.4012 1.6528 0.1579  -0.4490 -0.3628 253 TRP B CZ3 
4146  C CH2 . TRP B 189 ? 1.1504 0.9444 1.1909 0.1802  -0.4780 -0.3807 253 TRP B CH2 
4147  N N   . LYS B 190 ? 0.9141 0.8275 1.1666 0.0911  -0.4144 -0.3316 254 LYS B N   
4148  C CA  . LYS B 190 ? 0.7936 0.6994 1.0383 0.0859  -0.4027 -0.3273 254 LYS B CA  
4149  C C   . LYS B 190 ? 0.7927 0.6933 0.9809 0.0961  -0.3802 -0.3186 254 LYS B C   
4150  O O   . LYS B 190 ? 0.7372 0.6518 0.9135 0.0963  -0.3619 -0.3081 254 LYS B O   
4151  C CB  . LYS B 190 ? 0.8143 0.7420 1.1126 0.0637  -0.3854 -0.3145 254 LYS B CB  
4152  C CG  . LYS B 190 ? 0.8790 0.7998 1.1709 0.0576  -0.3721 -0.3093 254 LYS B CG  
4153  C CD  . LYS B 190 ? 0.9080 0.8377 1.2587 0.0400  -0.3733 -0.3061 254 LYS B CD  
4154  C CE  . LYS B 190 ? 1.1890 1.1138 1.5289 0.0345  -0.3559 -0.2988 254 LYS B CE  
4155  N NZ  . LYS B 190 ? 1.4377 1.3679 1.8320 0.0190  -0.3577 -0.2960 254 LYS B NZ  
4156  N N   . ALA B 191 ? 0.9335 0.8130 1.0875 0.1055  -0.3824 -0.3230 255 ALA B N   
4157  C CA  . ALA B 191 ? 0.8758 0.7518 0.9835 0.1131  -0.3589 -0.3124 255 ALA B CA  
4158  C C   . ALA B 191 ? 0.8398 0.7352 0.9717 0.0946  -0.3321 -0.2965 255 ALA B C   
4159  O O   . ALA B 191 ? 0.8918 0.7909 1.0592 0.0810  -0.3330 -0.2962 255 ALA B O   
4160  C CB  . ALA B 191 ? 0.8653 0.7141 0.9333 0.1281  -0.3679 -0.3204 255 ALA B CB  
4161  N N   . LEU B 192 ? 0.8530 0.7606 0.9668 0.0945  -0.3089 -0.2831 256 LEU B N   
4162  C CA  . LEU B 192 ? 0.7890 0.7122 0.9180 0.0797  -0.2837 -0.2682 256 LEU B CA  
4163  C C   . LEU B 192 ? 0.8008 0.7105 0.8916 0.0875  -0.2726 -0.2638 256 LEU B C   
4164  O O   . LEU B 192 ? 0.7809 0.6782 0.8294 0.1044  -0.2733 -0.2649 256 LEU B O   
4165  C CB  . LEU B 192 ? 0.8039 0.7463 0.9358 0.0754  -0.2665 -0.2565 256 LEU B CB  
4166  C CG  . LEU B 192 ? 0.8966 0.8552 1.0688 0.0669  -0.2735 -0.2581 256 LEU B CG  
4167  C CD1 . LEU B 192 ? 1.1423 1.1157 1.3069 0.0657  -0.2559 -0.2467 256 LEU B CD1 
4168  C CD2 . LEU B 192 ? 0.7921 0.7619 1.0149 0.0497  -0.2722 -0.2558 256 LEU B CD2 
4169  N N   . ASP B 193 ? 0.9022 0.8141 1.0085 0.0760  -0.2621 -0.2584 257 ASP B N   
4170  C CA  . ASP B 193 ? 1.0072 0.9084 1.0823 0.0815  -0.2498 -0.2527 257 ASP B CA  
4171  C C   . ASP B 193 ? 1.0174 0.9316 1.0792 0.0789  -0.2247 -0.2366 257 ASP B C   
4172  O O   . ASP B 193 ? 0.7663 0.6963 0.8528 0.0642  -0.2096 -0.2268 257 ASP B O   
4173  C CB  . ASP B 193 ? 1.3711 1.2691 1.4692 0.0703  -0.2495 -0.2536 257 ASP B CB  
4174  C CG  . ASP B 193 ? 1.5278 1.4140 1.5939 0.0765  -0.2378 -0.2484 257 ASP B CG  
4175  O OD1 . ASP B 193 ? 1.9257 1.8050 1.9522 0.0906  -0.2311 -0.2443 257 ASP B OD1 
4176  O OD2 . ASP B 193 ? 1.3437 1.2276 1.4253 0.0677  -0.2348 -0.2475 257 ASP B OD2 
4177  N N   . THR B 194 ? 1.0652 0.9715 1.0877 0.0945  -0.2209 -0.2337 258 THR B N   
4178  C CA  . THR B 194 ? 1.2327 1.1502 1.2436 0.0939  -0.2005 -0.2190 258 THR B CA  
4179  C C   . THR B 194 ? 1.3317 1.2419 1.3176 0.0991  -0.1860 -0.2097 258 THR B C   
4180  O O   . THR B 194 ? 1.4992 1.4190 1.4820 0.0956  -0.1683 -0.1963 258 THR B O   
4181  C CB  . THR B 194 ? 1.3346 1.2502 1.3224 0.1081  -0.2045 -0.2197 258 THR B CB  
4182  O OG1 . THR B 194 ? 2.0665 1.9951 2.0520 0.1046  -0.1859 -0.2053 258 THR B OG1 
4183  C CG2 . THR B 194 ? 1.3110 1.2049 1.2555 0.1302  -0.2114 -0.2243 258 THR B CG2 
4184  N N   . THR B 195 ? 1.7287 1.6211 1.6976 0.1078  -0.1945 -0.2170 259 THR B N   
4185  C CA  . THR B 195 ? 1.4213 1.3029 1.3581 0.1190  -0.1831 -0.2092 259 THR B CA  
4186  C C   . THR B 195 ? 1.0075 0.9029 0.9545 0.1076  -0.1612 -0.1935 259 THR B C   
4187  O O   . THR B 195 ? 0.8809 0.7875 0.8581 0.0903  -0.1565 -0.1915 259 THR B O   
4188  C CB  . THR B 195 ? 1.5194 1.3804 1.4420 0.1266  -0.1941 -0.2190 259 THR B CB  
4189  O OG1 . THR B 195 ? 1.3387 1.2051 1.2957 0.1089  -0.1965 -0.2225 259 THR B OG1 
4190  C CG2 . THR B 195 ? 1.8658 1.7075 1.7675 0.1437  -0.2175 -0.2350 259 THR B CG2 
4191  N N   . GLY B 196 ? 0.9445 0.8386 0.8665 0.1183  -0.1480 -0.1817 260 GLY B N   
4192  C CA  . GLY B 196 ? 1.0171 0.9225 0.9469 0.1096  -0.1286 -0.1662 260 GLY B CA  
4193  C C   . GLY B 196 ? 0.7204 0.6420 0.6648 0.1019  -0.1209 -0.1577 260 GLY B C   
4194  O O   . GLY B 196 ? 0.6827 0.6120 0.6297 0.0981  -0.1064 -0.1444 260 GLY B O   
4195  N N   . PHE B 197 ? 0.7667 0.6933 0.7223 0.0995  -0.1313 -0.1656 261 PHE B N   
4196  C CA  . PHE B 197 ? 0.7373 0.6773 0.7027 0.0948  -0.1249 -0.1581 261 PHE B CA  
4197  C C   . PHE B 197 ? 0.8007 0.7388 0.7567 0.1049  -0.1357 -0.1648 261 PHE B C   
4198  O O   . PHE B 197 ? 0.9001 0.8248 0.8366 0.1184  -0.1476 -0.1743 261 PHE B O   
4199  C CB  . PHE B 197 ? 0.8380 0.7924 0.8360 0.0757  -0.1207 -0.1564 261 PHE B CB  
4200  C CG  . PHE B 197 ? 0.8676 0.8253 0.8887 0.0680  -0.1334 -0.1686 261 PHE B CG  
4201  C CD1 . PHE B 197 ? 0.8932 0.8602 0.9275 0.0653  -0.1382 -0.1712 261 PHE B CD1 
4202  C CD2 . PHE B 197 ? 0.7608 0.7133 0.7937 0.0628  -0.1396 -0.1760 261 PHE B CD2 
4203  C CE1 . PHE B 197 ? 1.0330 1.0047 1.0929 0.0581  -0.1491 -0.1807 261 PHE B CE1 
4204  C CE2 . PHE B 197 ? 0.8516 0.8083 0.9112 0.0551  -0.1506 -0.1853 261 PHE B CE2 
4205  C CZ  . PHE B 197 ? 0.9843 0.9512 1.0584 0.0528  -0.1552 -0.1873 261 PHE B CZ  
4206  N N   . ASN B 198 ? 0.8333 0.7835 0.8014 0.0993  -0.1321 -0.1602 262 ASN B N   
4207  C CA  . ASN B 198 ? 0.6876 0.6375 0.6480 0.1083  -0.1412 -0.1654 262 ASN B CA  
4208  C C   . ASN B 198 ? 0.7171 0.6814 0.7047 0.0958  -0.1434 -0.1672 262 ASN B C   
4209  O O   . ASN B 198 ? 1.1230 1.0977 1.1278 0.0835  -0.1331 -0.1593 262 ASN B O   
4210  C CB  . ASN B 198 ? 0.7114 0.6569 0.6456 0.1227  -0.1317 -0.1542 262 ASN B CB  
4211  C CG  . ASN B 198 ? 0.7637 0.7145 0.6963 0.1274  -0.1342 -0.1535 262 ASN B CG  
4212  O OD1 . ASN B 198 ? 0.7972 0.7572 0.7377 0.1223  -0.1236 -0.1424 262 ASN B OD1 
4213  N ND2 . ASN B 198 ? 0.6709 0.6149 0.5935 0.1373  -0.1493 -0.1656 262 ASN B ND2 
4214  N N   . PHE B 199 ? 0.7566 0.7210 0.7474 0.0999  -0.1571 -0.1774 263 PHE B N   
4215  C CA  . PHE B 199 ? 0.6447 0.6226 0.6653 0.0880  -0.1611 -0.1810 263 PHE B CA  
4216  C C   . PHE B 199 ? 0.6953 0.6746 0.7095 0.0967  -0.1695 -0.1851 263 PHE B C   
4217  O O   . PHE B 199 ? 0.9189 0.8933 0.9332 0.1029  -0.1856 -0.1969 263 PHE B O   
4218  C CB  . PHE B 199 ? 0.6694 0.6468 0.7132 0.0802  -0.1724 -0.1917 263 PHE B CB  
4219  C CG  . PHE B 199 ? 0.5398 0.5313 0.6179 0.0679  -0.1744 -0.1936 263 PHE B CG  
4220  C CD1 . PHE B 199 ? 0.5754 0.5780 0.6710 0.0558  -0.1607 -0.1845 263 PHE B CD1 
4221  C CD2 . PHE B 199 ? 0.6830 0.6760 0.7758 0.0698  -0.1904 -0.2041 263 PHE B CD2 
4222  C CE1 . PHE B 199 ? 0.7100 0.7251 0.8361 0.0465  -0.1611 -0.1850 263 PHE B CE1 
4223  C CE2 . PHE B 199 ? 0.6654 0.6722 0.7923 0.0593  -0.1912 -0.2044 263 PHE B CE2 
4224  C CZ  . PHE B 199 ? 0.6254 0.6433 0.7683 0.0482  -0.1757 -0.1944 263 PHE B CZ  
4225  N N   . GLU B 200 ? 0.7897 0.7754 0.7991 0.0973  -0.1596 -0.1754 264 GLU B N   
4226  C CA  . GLU B 200 ? 0.7441 0.7293 0.7418 0.1079  -0.1658 -0.1777 264 GLU B CA  
4227  C C   . GLU B 200 ? 0.6903 0.6893 0.7094 0.0988  -0.1639 -0.1757 264 GLU B C   
4228  O O   . GLU B 200 ? 0.7349 0.7422 0.7691 0.0871  -0.1530 -0.1679 264 GLU B O   
4229  C CB  . GLU B 200 ? 0.6585 0.6368 0.6275 0.1206  -0.1560 -0.1671 264 GLU B CB  
4230  C CG  . GLU B 200 ? 0.9750 0.9383 0.9178 0.1339  -0.1573 -0.1684 264 GLU B CG  
4231  C CD  . GLU B 200 ? 1.6295 1.5806 1.5464 0.1531  -0.1702 -0.1771 264 GLU B CD  
4232  O OE1 . GLU B 200 ? 1.8259 1.7813 1.7451 0.1561  -0.1769 -0.1807 264 GLU B OE1 
4233  O OE2 . GLU B 200 ? 1.5299 1.4660 1.4222 0.1665  -0.1738 -0.1803 264 GLU B OE2 
4234  N N   . PHE B 201 ? 0.5802 0.5804 0.5986 0.1056  -0.1748 -0.1826 265 PHE B N   
4235  C CA  . PHE B 201 ? 0.5483 0.5608 0.5840 0.0995  -0.1732 -0.1806 265 PHE B CA  
4236  C C   . PHE B 201 ? 0.4917 0.5156 0.5600 0.0837  -0.1701 -0.1806 265 PHE B C   
4237  O O   . PHE B 201 ? 0.5286 0.5600 0.6050 0.0765  -0.1593 -0.1724 265 PHE B O   
4238  C CB  . PHE B 201 ? 0.5166 0.5304 0.5393 0.1015  -0.1600 -0.1681 265 PHE B CB  
4239  C CG  . PHE B 201 ? 0.5868 0.5897 0.5786 0.1172  -0.1585 -0.1641 265 PHE B CG  
4240  C CD1 . PHE B 201 ? 0.7777 0.7757 0.7544 0.1310  -0.1691 -0.1707 265 PHE B CD1 
4241  C CD2 . PHE B 201 ? 0.6412 0.6390 0.6199 0.1191  -0.1459 -0.1526 265 PHE B CD2 
4242  C CE1 . PHE B 201 ? 1.0377 1.0248 0.9839 0.1477  -0.1663 -0.1658 265 PHE B CE1 
4243  C CE2 . PHE B 201 ? 0.7071 0.6953 0.6586 0.1350  -0.1422 -0.1465 265 PHE B CE2 
4244  C CZ  . PHE B 201 ? 1.0495 1.0318 0.9833 0.1500  -0.1519 -0.1530 265 PHE B CZ  
4245  N N   . PRO B 202 ? 0.4931 0.5170 0.5796 0.0790  -0.1793 -0.1892 266 PRO B N   
4246  C CA  . PRO B 202 ? 0.5171 0.5523 0.6366 0.0652  -0.1751 -0.1877 266 PRO B CA  
4247  C C   . PRO B 202 ? 0.4615 0.5088 0.5982 0.0628  -0.1746 -0.1863 266 PRO B C   
4248  O O   . PRO B 202 ? 0.5912 0.6388 0.7235 0.0704  -0.1842 -0.1914 266 PRO B O   
4249  C CB  . PRO B 202 ? 0.4685 0.5008 0.6057 0.0636  -0.1889 -0.1983 266 PRO B CB  
4250  C CG  . PRO B 202 ? 0.5251 0.5456 0.6393 0.0774  -0.2035 -0.2073 266 PRO B CG  
4251  C CD  . PRO B 202 ? 0.5393 0.5520 0.6179 0.0863  -0.1934 -0.1997 266 PRO B CD  
4252  N N   . THR B 203 ? 0.5253 0.5815 0.6794 0.0534  -0.1631 -0.1791 267 THR B N   
4253  C CA  . THR B 203 ? 0.5675 0.6348 0.7379 0.0515  -0.1604 -0.1764 267 THR B CA  
4254  C C   . THR B 203 ? 0.6062 0.6828 0.8103 0.0417  -0.1559 -0.1745 267 THR B C   
4255  O O   . THR B 203 ? 0.6771 0.7521 0.8843 0.0354  -0.1462 -0.1695 267 THR B O   
4256  C CB  . THR B 203 ? 0.7334 0.7998 0.8850 0.0531  -0.1490 -0.1674 267 THR B CB  
4257  O OG1 . THR B 203 ? 0.8143 0.8902 0.9790 0.0533  -0.1478 -0.1658 267 THR B OG1 
4258  C CG2 . THR B 203 ? 0.5966 0.6600 0.7442 0.0464  -0.1357 -0.1592 267 THR B CG2 
4259  N N   . CYS B 204 ? 0.7118 0.7981 0.9424 0.0412  -0.1631 -0.1781 268 CYS B N   
4260  C CA  . CYS B 204 ? 0.7119 0.8056 0.9789 0.0335  -0.1634 -0.1781 268 CYS B CA  
4261  C C   . CYS B 204 ? 0.7155 0.8235 1.0114 0.0309  -0.1566 -0.1720 268 CYS B C   
4262  O O   . CYS B 204 ? 0.7894 0.9023 1.0817 0.0361  -0.1580 -0.1716 268 CYS B O   
4263  C CB  . CYS B 204 ? 0.6372 0.7275 0.9172 0.0351  -0.1826 -0.1895 268 CYS B CB  
4264  S SG  . CYS B 204 ? 1.1654 1.2373 1.4088 0.0416  -0.1913 -0.1971 268 CYS B SG  
4265  N N   . TYR B 205 ? 0.5666 0.6811 0.8915 0.0238  -0.1486 -0.1666 269 TYR B N   
4266  C CA  . TYR B 205 ? 0.5316 0.6605 0.8914 0.0221  -0.1429 -0.1603 269 TYR B CA  
4267  C C   . TYR B 205 ? 0.5826 0.7173 0.9834 0.0148  -0.1446 -0.1594 269 TYR B C   
4268  O O   . TYR B 205 ? 0.4626 0.5888 0.8614 0.0111  -0.1511 -0.1647 269 TYR B O   
4269  C CB  . TYR B 205 ? 0.5718 0.7029 0.9202 0.0236  -0.1236 -0.1490 269 TYR B CB  
4270  C CG  . TYR B 205 ? 0.6214 0.7463 0.9620 0.0193  -0.1106 -0.1428 269 TYR B CG  
4271  C CD1 . TYR B 205 ? 0.6098 0.7420 0.9768 0.0163  -0.0972 -0.1334 269 TYR B CD1 
4272  C CD2 . TYR B 205 ? 0.5608 0.6726 0.8685 0.0189  -0.1113 -0.1457 269 TYR B CD2 
4273  C CE1 . TYR B 205 ? 0.5505 0.6763 0.9094 0.0133  -0.0854 -0.1278 269 TYR B CE1 
4274  C CE2 . TYR B 205 ? 0.5237 0.6298 0.8249 0.0151  -0.1003 -0.1404 269 TYR B CE2 
4275  C CZ  . TYR B 205 ? 0.5918 0.7045 0.9176 0.0123  -0.0876 -0.1319 269 TYR B CZ  
4276  O OH  . TYR B 205 ? 0.4730 0.5794 0.7911 0.0095  -0.0764 -0.1264 269 TYR B OH  
4277  N N   . TYR B 206 ? 0.6535 0.8025 1.0923 0.0134  -0.1388 -0.1521 270 TYR B N   
4278  C CA  . TYR B 206 ? 0.6019 0.7587 1.0883 0.0065  -0.1406 -0.1495 270 TYR B CA  
4279  C C   . TYR B 206 ? 0.5653 0.7317 1.0731 0.0051  -0.1187 -0.1342 270 TYR B C   
4280  O O   . TYR B 206 ? 0.6209 0.7948 1.1276 0.0105  -0.1077 -0.1264 270 TYR B O   
4281  C CB  . TYR B 206 ? 0.5711 0.7371 1.0941 0.0065  -0.1586 -0.1557 270 TYR B CB  
4282  C CG  . TYR B 206 ? 0.7913 0.9674 1.3713 -0.0008 -0.1599 -0.1508 270 TYR B CG  
4283  C CD1 . TYR B 206 ? 1.1275 1.3211 1.7504 -0.0008 -0.1518 -0.1399 270 TYR B CD1 
4284  C CD2 . TYR B 206 ? 0.8191 0.9873 1.4120 -0.0072 -0.1692 -0.1563 270 TYR B CD2 
4285  C CE1 . TYR B 206 ? 1.1914 1.3953 1.8721 -0.0076 -0.1524 -0.1336 270 TYR B CE1 
4286  C CE2 . TYR B 206 ? 0.8880 1.0653 1.5373 -0.0144 -0.1710 -0.1511 270 TYR B CE2 
4287  C CZ  . TYR B 206 ? 1.0333 1.2289 1.7279 -0.0148 -0.1623 -0.1393 270 TYR B CZ  
4288  O OH  . TYR B 206 ? 0.9609 1.1668 1.7162 -0.0218 -0.1631 -0.1321 270 TYR B OH  
4289  N N   . THR B 207 ? 0.5161 0.6810 1.0418 -0.0011 -0.1122 -0.1298 271 THR B N   
4290  C CA  . THR B 207 ? 0.6917 0.8654 1.2427 -0.0017 -0.0912 -0.1143 271 THR B CA  
4291  C C   . THR B 207 ? 0.6630 0.8375 1.2495 -0.0098 -0.0909 -0.1115 271 THR B C   
4292  O O   . THR B 207 ? 0.5925 0.7558 1.1669 -0.0143 -0.1020 -0.1209 271 THR B O   
4293  C CB  . THR B 207 ? 0.7619 0.9280 1.2717 0.0037  -0.0717 -0.1066 271 THR B CB  
4294  O OG1 . THR B 207 ? 1.2297 1.4042 1.7631 0.0062  -0.0510 -0.0909 271 THR B OG1 
4295  C CG2 . THR B 207 ? 0.6068 0.7576 1.0837 0.0004  -0.0728 -0.1120 271 THR B CG2 
4296  N N   . SER B 208 ? 0.8962 1.0840 1.5276 -0.0108 -0.0778 -0.0979 272 SER B N   
4297  C CA  . SER B 208 ? 1.0286 1.2176 1.6949 -0.0177 -0.0721 -0.0912 272 SER B CA  
4298  C C   . SER B 208 ? 0.9293 1.1123 1.6140 -0.0258 -0.0969 -0.1052 272 SER B C   
4299  O O   . SER B 208 ? 1.0034 1.1758 1.6807 -0.0307 -0.0989 -0.1088 272 SER B O   
4300  C CB  . SER B 208 ? 1.1246 1.3027 1.7554 -0.0160 -0.0538 -0.0852 272 SER B CB  
4301  O OG  . SER B 208 ? 1.4809 1.6617 2.1463 -0.0209 -0.0431 -0.0752 272 SER B OG  
4302  N N   . GLY B 209 ? 0.6870 0.8756 1.3930 -0.0261 -0.1169 -0.1138 273 GLY B N   
4303  C CA  . GLY B 209 ? 0.7473 0.9289 1.4718 -0.0318 -0.1433 -0.1281 273 GLY B CA  
4304  C C   . GLY B 209 ? 0.7354 0.8974 1.4096 -0.0306 -0.1575 -0.1439 273 GLY B C   
4305  O O   . GLY B 209 ? 0.8541 1.0069 1.5398 -0.0344 -0.1780 -0.1553 273 GLY B O   
4306  N N   . LYS B 210 ? 0.5723 0.7270 1.1917 -0.0247 -0.1473 -0.1443 274 LYS B N   
4307  C CA  . LYS B 210 ? 0.5668 0.7038 1.1381 -0.0221 -0.1588 -0.1574 274 LYS B CA  
4308  C C   . LYS B 210 ? 0.5592 0.6931 1.0866 -0.0138 -0.1604 -0.1620 274 LYS B C   
4309  O O   . LYS B 210 ? 0.7348 0.8766 1.2542 -0.0104 -0.1455 -0.1530 274 LYS B O   
4310  C CB  . LYS B 210 ? 0.5663 0.6939 1.1158 -0.0250 -0.1446 -0.1527 274 LYS B CB  
4311  C CG  . LYS B 210 ? 0.8285 0.9534 1.4148 -0.0329 -0.1505 -0.1534 274 LYS B CG  
4312  C CD  . LYS B 210 ? 0.9890 1.1056 1.5587 -0.0360 -0.1358 -0.1477 274 LYS B CD  
4313  C CE  . LYS B 210 ? 1.2084 1.3359 1.7939 -0.0368 -0.1096 -0.1300 274 LYS B CE  
4314  N NZ  . LYS B 210 ? 1.4765 1.6002 2.0790 -0.0426 -0.1004 -0.1238 274 LYS B NZ  
4315  N N   . VAL B 211 ? 0.5221 0.6436 1.0209 -0.0095 -0.1786 -0.1757 275 VAL B N   
4316  C CA  . VAL B 211 ? 0.5669 0.6827 1.0184 -0.0012 -0.1778 -0.1789 275 VAL B CA  
4317  C C   . VAL B 211 ? 0.5515 0.6550 0.9594 0.0000  -0.1670 -0.1771 275 VAL B C   
4318  O O   . VAL B 211 ? 0.7137 0.8069 1.1155 -0.0025 -0.1709 -0.1811 275 VAL B O   
4319  C CB  . VAL B 211 ? 0.6339 0.7432 1.0746 0.0055  -0.2011 -0.1927 275 VAL B CB  
4320  C CG1 . VAL B 211 ? 0.5054 0.6078 0.8965 0.0145  -0.1988 -0.1947 275 VAL B CG1 
4321  C CG2 . VAL B 211 ? 0.6194 0.7425 1.1033 0.0047  -0.2111 -0.1933 275 VAL B CG2 
4322  N N   . LYS B 212 ? 0.5563 0.6606 0.9354 0.0039  -0.1540 -0.1709 276 LYS B N   
4323  C CA  . LYS B 212 ? 0.5712 0.6663 0.9160 0.0043  -0.1419 -0.1666 276 LYS B CA  
4324  C C   . LYS B 212 ? 0.5082 0.5963 0.8135 0.0120  -0.1453 -0.1699 276 LYS B C   
4325  O O   . LYS B 212 ? 0.7313 0.8253 1.0323 0.0158  -0.1429 -0.1675 276 LYS B O   
4326  C CB  . LYS B 212 ? 0.6256 0.7275 0.9781 0.0012  -0.1215 -0.1538 276 LYS B CB  
4327  C CG  . LYS B 212 ? 0.7020 0.8116 1.0969 -0.0054 -0.1163 -0.1485 276 LYS B CG  
4328  C CD  . LYS B 212 ? 0.8293 0.9429 1.2268 -0.0061 -0.0951 -0.1354 276 LYS B CD  
4329  C CE  . LYS B 212 ? 0.8412 0.9624 1.2820 -0.0119 -0.0888 -0.1288 276 LYS B CE  
4330  N NZ  . LYS B 212 ? 1.1913 1.3139 1.6289 -0.0103 -0.0669 -0.1157 276 LYS B NZ  
4331  N N   . CYS B 213 ? 0.5672 0.6428 0.8448 0.0149  -0.1506 -0.1750 277 CYS B N   
4332  C CA  . CYS B 213 ? 0.6785 0.7465 0.9200 0.0234  -0.1542 -0.1775 277 CYS B CA  
4333  C C   . CYS B 213 ? 0.6977 0.7572 0.9090 0.0240  -0.1430 -0.1715 277 CYS B C   
4334  O O   . CYS B 213 ? 0.6235 0.6767 0.8319 0.0207  -0.1400 -0.1709 277 CYS B O   
4335  C CB  . CYS B 213 ? 0.7582 0.8177 0.9912 0.0302  -0.1727 -0.1892 277 CYS B CB  
4336  S SG  . CYS B 213 ? 1.5350 1.6031 1.8011 0.0310  -0.1893 -0.1972 277 CYS B SG  
4337  N N   . THR B 214 ? 0.5473 0.6063 0.7376 0.0285  -0.1377 -0.1669 278 THR B N   
4338  C CA  . THR B 214 ? 0.5135 0.5649 0.6781 0.0296  -0.1287 -0.1606 278 THR B CA  
4339  C C   . THR B 214 ? 0.5245 0.5671 0.6619 0.0389  -0.1349 -0.1631 278 THR B C   
4340  O O   . THR B 214 ? 0.5495 0.5930 0.6761 0.0448  -0.1369 -0.1624 278 THR B O   
4341  C CB  . THR B 214 ? 0.5536 0.6088 0.7141 0.0286  -0.1186 -0.1525 278 THR B CB  
4342  O OG1 . THR B 214 ? 0.8083 0.8712 0.9919 0.0227  -0.1116 -0.1492 278 THR B OG1 
4343  C CG2 . THR B 214 ? 0.4501 0.4974 0.5890 0.0288  -0.1107 -0.1455 278 THR B CG2 
4344  N N   . GLY B 215 ? 0.5507 0.5842 0.6757 0.0411  -0.1370 -0.1652 279 GLY B N   
4345  C CA  . GLY B 215 ? 0.5947 0.6191 0.6920 0.0522  -0.1409 -0.1660 279 GLY B CA  
4346  C C   . GLY B 215 ? 0.6002 0.6212 0.6788 0.0539  -0.1293 -0.1551 279 GLY B C   
4347  O O   . GLY B 215 ? 0.6676 0.6927 0.7534 0.0466  -0.1200 -0.1480 279 GLY B O   
4348  N N   . THR B 216 ? 0.6304 0.6430 0.6853 0.0646  -0.1305 -0.1536 280 THR B N   
4349  C CA  . THR B 216 ? 0.5443 0.5536 0.5840 0.0678  -0.1204 -0.1423 280 THR B CA  
4350  C C   . THR B 216 ? 0.7137 0.7125 0.7339 0.0765  -0.1194 -0.1411 280 THR B C   
4351  O O   . THR B 216 ? 0.6906 0.6821 0.6954 0.0880  -0.1276 -0.1476 280 THR B O   
4352  C CB  . THR B 216 ? 0.6794 0.6903 0.7107 0.0749  -0.1212 -0.1392 280 THR B CB  
4353  O OG1 . THR B 216 ? 0.7387 0.7580 0.7858 0.0662  -0.1180 -0.1365 280 THR B OG1 
4354  C CG2 . THR B 216 ? 0.7048 0.7095 0.7171 0.0835  -0.1135 -0.1283 280 THR B CG2 
4355  N N   . ASN B 217 ? 0.8557 0.8528 0.8757 0.0719  -0.1099 -0.1330 281 ASN B N   
4356  C CA  . ASN B 217 ? 0.7137 0.7011 0.7161 0.0802  -0.1074 -0.1307 281 ASN B CA  
4357  C C   . ASN B 217 ? 0.7527 0.7372 0.7398 0.0894  -0.0986 -0.1180 281 ASN B C   
4358  O O   . ASN B 217 ? 0.7929 0.7813 0.7882 0.0832  -0.0891 -0.1067 281 ASN B O   
4359  C CB  . ASN B 217 ? 0.5614 0.5486 0.5736 0.0705  -0.1021 -0.1291 281 ASN B CB  
4360  C CG  . ASN B 217 ? 0.6894 0.6664 0.6841 0.0790  -0.1000 -0.1277 281 ASN B CG  
4361  O OD1 . ASN B 217 ? 0.6960 0.6672 0.6713 0.0913  -0.0959 -0.1209 281 ASN B OD1 
4362  N ND2 . ASN B 217 ? 0.8060 0.7803 0.8075 0.0731  -0.1020 -0.1333 281 ASN B ND2 
4363  N N   . LEU B 218 ? 0.5598 0.5369 0.5255 0.1050  -0.1021 -0.1196 282 LEU B N   
4364  C CA  . LEU B 218 ? 0.6823 0.6567 0.6339 0.1160  -0.0926 -0.1059 282 LEU B CA  
4365  C C   . LEU B 218 ? 0.6940 0.6609 0.6320 0.1240  -0.0833 -0.0967 282 LEU B C   
4366  O O   . LEU B 218 ? 0.6548 0.6195 0.5829 0.1343  -0.0740 -0.0837 282 LEU B O   
4367  C CB  . LEU B 218 ? 0.7810 0.7504 0.7139 0.1313  -0.0982 -0.1092 282 LEU B CB  
4368  C CG  . LEU B 218 ? 0.7609 0.7377 0.7039 0.1275  -0.1043 -0.1134 282 LEU B CG  
4369  C CD1 . LEU B 218 ? 0.8323 0.8089 0.7788 0.1258  -0.1193 -0.1305 282 LEU B CD1 
4370  C CD2 . LEU B 218 ? 0.8563 0.8284 0.7797 0.1438  -0.1015 -0.1068 282 LEU B CD2 
4371  N N   . TRP B 219 ? 0.8574 0.8211 0.7972 0.1192  -0.0851 -0.1024 283 TRP B N   
4372  C CA  . TRP B 219 ? 0.6817 0.6374 0.6071 0.1275  -0.0773 -0.0955 283 TRP B CA  
4373  C C   . TRP B 219 ? 0.7107 0.6721 0.6537 0.1149  -0.0679 -0.0863 283 TRP B C   
4374  O O   . TRP B 219 ? 0.7071 0.6710 0.6532 0.1169  -0.0568 -0.0710 283 TRP B O   
4375  C CB  . TRP B 219 ? 0.8499 0.7948 0.7608 0.1337  -0.0881 -0.1099 283 TRP B CB  
4376  C CG  . TRP B 219 ? 0.9318 0.8662 0.8249 0.1435  -0.0819 -0.1053 283 TRP B CG  
4377  C CD1 . TRP B 219 ? 0.8962 0.8286 0.7794 0.1527  -0.0670 -0.0886 283 TRP B CD1 
4378  C CD2 . TRP B 219 ? 0.9076 0.8307 0.7901 0.1467  -0.0906 -0.1174 283 TRP B CD2 
4379  N NE1 . TRP B 219 ? 0.9936 0.9151 0.8598 0.1614  -0.0651 -0.0894 283 TRP B NE1 
4380  C CE2 . TRP B 219 ? 0.9930 0.9077 0.8569 0.1583  -0.0794 -0.1069 283 TRP B CE2 
4381  C CE3 . TRP B 219 ? 0.9233 0.8425 0.8119 0.1412  -0.1062 -0.1346 283 TRP B CE3 
4382  C CZ2 . TRP B 219 ? 1.0674 0.9691 0.9163 0.1644  -0.0843 -0.1146 283 TRP B CZ2 
4383  C CZ3 . TRP B 219 ? 0.7671 0.6733 0.6433 0.1465  -0.1119 -0.1423 283 TRP B CZ3 
4384  C CH2 . TRP B 219 ? 0.9882 0.8852 0.8432 0.1581  -0.1014 -0.1330 283 TRP B CH2 
4385  N N   . ASN B 220 ? 0.8059 0.7693 0.7622 0.1021  -0.0726 -0.0951 284 ASN B N   
4386  C CA  . ASN B 220 ? 0.7367 0.7025 0.7043 0.0928  -0.0646 -0.0882 284 ASN B CA  
4387  C C   . ASN B 220 ? 0.8059 0.7809 0.7982 0.0752  -0.0656 -0.0900 284 ASN B C   
4388  O O   . ASN B 220 ? 1.0958 1.0716 1.0971 0.0667  -0.0620 -0.0885 284 ASN B O   
4389  C CB  . ASN B 220 ? 0.7853 0.7417 0.7414 0.0968  -0.0672 -0.0953 284 ASN B CB  
4390  C CG  . ASN B 220 ? 0.8093 0.7629 0.7678 0.0935  -0.0806 -0.1123 284 ASN B CG  
4391  O OD1 . ASN B 220 ? 1.0599 1.0209 1.0334 0.0854  -0.0868 -0.1184 284 ASN B OD1 
4392  N ND2 . ASN B 220 ? 1.1112 1.0539 1.0563 0.1002  -0.0858 -0.1198 284 ASN B ND2 
4393  N N   . ASP B 221 ? 0.7891 0.7702 0.7905 0.0708  -0.0700 -0.0929 285 ASP B N   
4394  C CA  . ASP B 221 ? 0.6631 0.6512 0.6843 0.0566  -0.0716 -0.0960 285 ASP B CA  
4395  C C   . ASP B 221 ? 0.5562 0.5502 0.5864 0.0530  -0.0716 -0.0917 285 ASP B C   
4396  O O   . ASP B 221 ? 0.6537 0.6486 0.6784 0.0592  -0.0756 -0.0937 285 ASP B O   
4397  C CB  . ASP B 221 ? 0.6841 0.6725 0.7109 0.0527  -0.0801 -0.1101 285 ASP B CB  
4398  C CG  . ASP B 221 ? 1.0384 1.0327 1.0846 0.0395  -0.0790 -0.1122 285 ASP B CG  
4399  O OD1 . ASP B 221 ? 0.8331 0.8297 0.8857 0.0336  -0.0728 -0.1042 285 ASP B OD1 
4400  O OD2 . ASP B 221 ? 1.3426 1.3384 1.3982 0.0358  -0.0848 -0.1219 285 ASP B OD2 
4401  N N   . ALA B 222 ? 0.5439 0.5407 0.5868 0.0436  -0.0680 -0.0864 286 ALA B N   
4402  C CA  . ALA B 222 ? 0.6395 0.6398 0.6914 0.0391  -0.0694 -0.0834 286 ALA B CA  
4403  C C   . ALA B 222 ? 0.7212 0.7252 0.7826 0.0316  -0.0734 -0.0922 286 ALA B C   
4404  O O   . ALA B 222 ? 1.0542 1.0598 1.1207 0.0291  -0.0750 -0.0911 286 ALA B O   
4405  C CB  . ALA B 222 ? 0.5855 0.5842 0.6445 0.0354  -0.0648 -0.0718 286 ALA B CB  
4406  N N   . LYS B 223 ? 0.6862 0.6909 0.7507 0.0286  -0.0744 -0.0999 287 LYS B N   
4407  C CA  . LYS B 223 ? 0.4769 0.4861 0.5521 0.0236  -0.0770 -0.1074 287 LYS B CA  
4408  C C   . LYS B 223 ? 0.6702 0.6821 0.7449 0.0285  -0.0842 -0.1161 287 LYS B C   
4409  O O   . LYS B 223 ? 0.7634 0.7722 0.8261 0.0366  -0.0874 -0.1166 287 LYS B O   
4410  C CB  . LYS B 223 ? 0.4699 0.4783 0.5523 0.0177  -0.0739 -0.1097 287 LYS B CB  
4411  C CG  . LYS B 223 ? 0.5801 0.5848 0.6620 0.0136  -0.0677 -0.1023 287 LYS B CG  
4412  C CD  . LYS B 223 ? 0.6177 0.6226 0.7084 0.0079  -0.0645 -0.1058 287 LYS B CD  
4413  C CE  . LYS B 223 ? 0.6121 0.6127 0.7012 0.0045  -0.0589 -0.0996 287 LYS B CE  
4414  N NZ  . LYS B 223 ? 0.7049 0.7057 0.8024 -0.0001 -0.0549 -0.1021 287 LYS B NZ  
4415  N N   . ARG B 224 ? 0.6350 0.6520 0.7228 0.0247  -0.0871 -0.1225 288 ARG B N   
4416  C CA  . ARG B 224 ? 0.4949 0.5145 0.5849 0.0291  -0.0956 -0.1307 288 ARG B CA  
4417  C C   . ARG B 224 ? 0.5016 0.5222 0.6050 0.0254  -0.0991 -0.1379 288 ARG B C   
4418  O O   . ARG B 224 ? 1.0125 1.0373 1.1319 0.0184  -0.0949 -0.1373 288 ARG B O   
4419  C CB  . ARG B 224 ? 0.5621 0.5883 0.6598 0.0290  -0.0976 -0.1318 288 ARG B CB  
4420  C CG  . ARG B 224 ? 0.5842 0.6092 0.6730 0.0307  -0.0939 -0.1243 288 ARG B CG  
4421  C CD  . ARG B 224 ? 0.6574 0.6874 0.7494 0.0336  -0.0980 -0.1268 288 ARG B CD  
4422  N NE  . ARG B 224 ? 0.6392 0.6668 0.7178 0.0419  -0.1024 -0.1267 288 ARG B NE  
4423  C CZ  . ARG B 224 ? 0.7178 0.7433 0.7881 0.0452  -0.1007 -0.1203 288 ARG B CZ  
4424  N NH1 . ARG B 224 ? 0.9237 0.9484 0.9975 0.0407  -0.0966 -0.1148 288 ARG B NH1 
4425  N NH2 . ARG B 224 ? 0.5080 0.5312 0.5661 0.0539  -0.1036 -0.1195 288 ARG B NH2 
4426  N N   . PRO B 225 ? 0.4829 0.4987 0.5800 0.0309  -0.1072 -0.1447 289 PRO B N   
4427  C CA  . PRO B 225 ? 0.5401 0.5556 0.6526 0.0275  -0.1134 -0.1527 289 PRO B CA  
4428  C C   . PRO B 225 ? 0.5872 0.6122 0.7240 0.0231  -0.1172 -0.1565 289 PRO B C   
4429  O O   . PRO B 225 ? 0.6988 0.7289 0.8350 0.0259  -0.1189 -0.1561 289 PRO B O   
4430  C CB  . PRO B 225 ? 0.5687 0.5755 0.6654 0.0376  -0.1246 -0.1603 289 PRO B CB  
4431  C CG  . PRO B 225 ? 0.7058 0.7073 0.7766 0.0456  -0.1188 -0.1529 289 PRO B CG  
4432  C CD  . PRO B 225 ? 0.5218 0.5311 0.5971 0.0420  -0.1118 -0.1454 289 PRO B CD  
4433  N N   . PHE B 226 ? 0.5902 0.6180 0.7497 0.0164  -0.1180 -0.1592 290 PHE B N   
4434  C CA  . PHE B 226 ? 0.5947 0.6326 0.7818 0.0124  -0.1202 -0.1610 290 PHE B CA  
4435  C C   . PHE B 226 ? 0.6600 0.6967 0.8683 0.0104  -0.1318 -0.1696 290 PHE B C   
4436  O O   . PHE B 226 ? 0.7716 0.8007 0.9780 0.0088  -0.1331 -0.1717 290 PHE B O   
4437  C CB  . PHE B 226 ? 0.5042 0.5481 0.7037 0.0058  -0.1064 -0.1523 290 PHE B CB  
4438  C CG  . PHE B 226 ? 0.5988 0.6538 0.8223 0.0039  -0.1046 -0.1507 290 PHE B CG  
4439  C CD1 . PHE B 226 ? 0.5073 0.5664 0.7224 0.0073  -0.1008 -0.1468 290 PHE B CD1 
4440  C CD2 . PHE B 226 ? 0.7030 0.7643 0.9594 -0.0010 -0.1061 -0.1519 290 PHE B CD2 
4441  C CE1 . PHE B 226 ? 0.5854 0.6544 0.8216 0.0068  -0.0979 -0.1443 290 PHE B CE1 
4442  C CE2 . PHE B 226 ? 0.6973 0.7699 0.9784 -0.0019 -0.1028 -0.1485 290 PHE B CE2 
4443  C CZ  . PHE B 226 ? 0.5554 0.6319 0.8252 0.0024  -0.0982 -0.1446 290 PHE B CZ  
4444  N N   . LEU B 227 ? 0.8322 0.8761 1.0615 0.0108  -0.1410 -0.1744 291 LEU B N   
4445  C CA  . LEU B 227 ? 0.6332 0.6752 0.8846 0.0100  -0.1566 -0.1840 291 LEU B CA  
4446  C C   . LEU B 227 ? 0.5813 0.6369 0.8754 0.0034  -0.1565 -0.1820 291 LEU B C   
4447  O O   . LEU B 227 ? 0.5118 0.5775 0.8129 0.0041  -0.1518 -0.1776 291 LEU B O   
4448  C CB  . LEU B 227 ? 0.5722 0.6069 0.8047 0.0202  -0.1730 -0.1939 291 LEU B CB  
4449  C CG  . LEU B 227 ? 0.7424 0.7724 0.9955 0.0209  -0.1926 -0.2056 291 LEU B CG  
4450  C CD1 . LEU B 227 ? 0.6779 0.6965 0.9293 0.0183  -0.1945 -0.2084 291 LEU B CD1 
4451  C CD2 . LEU B 227 ? 0.6132 0.6357 0.8466 0.0329  -0.2099 -0.2157 291 LEU B CD2 
4452  N N   . GLU B 228 ? 0.6207 0.6762 0.9443 -0.0028 -0.1610 -0.1841 292 GLU B N   
4453  C CA  . GLU B 228 ? 0.5504 0.6184 0.9199 -0.0092 -0.1608 -0.1808 292 GLU B CA  
4454  C C   . GLU B 228 ? 0.5557 0.6180 0.9454 -0.0091 -0.1830 -0.1927 292 GLU B C   
4455  O O   . GLU B 228 ? 0.6929 0.7417 1.0702 -0.0084 -0.1907 -0.1992 292 GLU B O   
4456  C CB  . GLU B 228 ? 0.6712 0.7427 1.0601 -0.0170 -0.1447 -0.1708 292 GLU B CB  
4457  C CG  . GLU B 228 ? 1.4661 1.5533 1.8855 -0.0202 -0.1305 -0.1592 292 GLU B CG  
4458  C CD  . GLU B 228 ? 1.9873 2.0772 2.4282 -0.0264 -0.1147 -0.1489 292 GLU B CD  
4459  O OE1 . GLU B 228 ? 1.8849 1.9789 2.3170 -0.0251 -0.0959 -0.1379 292 GLU B OE1 
4460  O OE2 . GLU B 228 ? 2.4197 2.5063 2.8853 -0.0316 -0.1216 -0.1518 292 GLU B OE2 
4461  N N   . PHE B 229 ? 0.5325 0.6037 0.9520 -0.0090 -0.1944 -0.1961 293 PHE B N   
4462  C CA  . PHE B 229 ? 0.5843 0.6516 1.0352 -0.0106 -0.2169 -0.2066 293 PHE B CA  
4463  C C   . PHE B 229 ? 0.6195 0.7031 1.1204 -0.0150 -0.2203 -0.2029 293 PHE B C   
4464  O O   . PHE B 229 ? 0.6142 0.7108 1.1172 -0.0136 -0.2089 -0.1950 293 PHE B O   
4465  C CB  . PHE B 229 ? 0.6633 0.7154 1.0825 0.0000  -0.2390 -0.2217 293 PHE B CB  
4466  C CG  . PHE B 229 ? 0.5955 0.6529 0.9979 0.0080  -0.2423 -0.2235 293 PHE B CG  
4467  C CD1 . PHE B 229 ? 0.6727 0.7386 1.1078 0.0083  -0.2572 -0.2281 293 PHE B CD1 
4468  C CD2 . PHE B 229 ? 0.5302 0.5833 0.8857 0.0155  -0.2320 -0.2208 293 PHE B CD2 
4469  C CE1 . PHE B 229 ? 0.7250 0.7953 1.1442 0.0163  -0.2610 -0.2302 293 PHE B CE1 
4470  C CE2 . PHE B 229 ? 0.7719 0.8291 1.1126 0.0233  -0.2356 -0.2224 293 PHE B CE2 
4471  C CZ  . PHE B 229 ? 0.6896 0.7553 1.0610 0.0238  -0.2498 -0.2273 293 PHE B CZ  
4472  N N   . ASP B 230 ? 0.7127 0.7955 1.2552 -0.0198 -0.2371 -0.2086 294 ASP B N   
4473  C CA  . ASP B 230 ? 0.9041 1.0037 1.5025 -0.0247 -0.2405 -0.2035 294 ASP B CA  
4474  C C   . ASP B 230 ? 0.7882 0.8820 1.4025 -0.0210 -0.2715 -0.2186 294 ASP B C   
4475  O O   . ASP B 230 ? 0.5510 0.6272 1.1265 -0.0129 -0.2881 -0.2325 294 ASP B O   
4476  C CB  . ASP B 230 ? 1.1087 1.2161 1.7563 -0.0354 -0.2301 -0.1926 294 ASP B CB  
4477  C CG  . ASP B 230 ? 1.0700 1.1620 1.7282 -0.0391 -0.2473 -0.2024 294 ASP B CG  
4478  O OD1 . ASP B 230 ? 1.1319 1.2075 1.7649 -0.0328 -0.2706 -0.2187 294 ASP B OD1 
4479  O OD2 . ASP B 230 ? 1.1238 1.2191 1.8147 -0.0474 -0.2373 -0.1935 294 ASP B OD2 
4480  N N   . GLN B 231 ? 0.8965 1.0046 1.5680 -0.0259 -0.2794 -0.2156 295 GLN B N   
4481  C CA  . GLN B 231 ? 0.7403 0.8438 1.4303 -0.0221 -0.3105 -0.2299 295 GLN B CA  
4482  C C   . GLN B 231 ? 0.7787 0.8604 1.4646 -0.0208 -0.3366 -0.2459 295 GLN B C   
4483  O O   . GLN B 231 ? 0.8507 0.9189 1.5177 -0.0118 -0.3624 -0.2618 295 GLN B O   
4484  C CB  . GLN B 231 ? 0.9422 1.0665 1.6988 -0.0279 -0.3136 -0.2222 295 GLN B CB  
4485  C CG  . GLN B 231 ? 0.9839 1.1201 1.8052 -0.0401 -0.3046 -0.2093 295 GLN B CG  
4486  C CD  . GLN B 231 ? 1.2082 1.3666 2.0934 -0.0438 -0.3061 -0.2000 295 GLN B CD  
4487  O OE1 . GLN B 231 ? 1.2141 1.3826 2.0901 -0.0378 -0.3036 -0.1985 295 GLN B OE1 
4488  N NE2 . GLN B 231 ? 1.3322 1.4983 2.2842 -0.0534 -0.3099 -0.1930 295 GLN B NE2 
4489  N N   . SER B 232 ? 0.8411 0.9174 1.5398 -0.0284 -0.3299 -0.2419 296 SER B N   
4490  C CA  . SER B 232 ? 0.8781 0.9323 1.5745 -0.0273 -0.3546 -0.2568 296 SER B CA  
4491  C C   . SER B 232 ? 0.7288 0.7608 1.3532 -0.0167 -0.3554 -0.2664 296 SER B C   
4492  O O   . SER B 232 ? 0.8786 0.8903 1.4920 -0.0143 -0.3717 -0.2775 296 SER B O   
4493  C CB  . SER B 232 ? 1.2740 1.3317 2.0207 -0.0402 -0.3485 -0.2482 296 SER B CB  
4494  O OG  . SER B 232 ? 1.4040 1.4657 2.1294 -0.0439 -0.3174 -0.2345 296 SER B OG  
4495  N N   . PHE B 233 ? 0.6328 0.6684 1.2096 -0.0098 -0.3376 -0.2616 297 PHE B N   
4496  C CA  . PHE B 233 ? 0.6419 0.6601 1.1523 0.0000  -0.3318 -0.2660 297 PHE B CA  
4497  C C   . PHE B 233 ? 0.6792 0.6908 1.1768 -0.0052 -0.3154 -0.2597 297 PHE B C   
4498  O O   . PHE B 233 ? 0.7253 0.7198 1.1736 0.0034  -0.3157 -0.2652 297 PHE B O   
4499  C CB  . PHE B 233 ? 0.7314 0.7263 1.2077 0.0141  -0.3605 -0.2850 297 PHE B CB  
4500  C CG  . PHE B 233 ? 0.9787 0.9762 1.4403 0.0243  -0.3714 -0.2909 297 PHE B CG  
4501  C CD1 . PHE B 233 ? 0.9129 0.9259 1.3588 0.0252  -0.3504 -0.2800 297 PHE B CD1 
4502  C CD2 . PHE B 233 ? 1.1603 1.1431 1.6227 0.0338  -0.4040 -0.3080 297 PHE B CD2 
4503  C CE1 . PHE B 233 ? 1.0454 1.0608 1.4778 0.0348  -0.3600 -0.2850 297 PHE B CE1 
4504  C CE2 . PHE B 233 ? 1.3131 1.2979 1.7607 0.0441  -0.4143 -0.3135 297 PHE B CE2 
4505  C CZ  . PHE B 233 ? 1.3099 1.3116 1.7426 0.0443  -0.3913 -0.3015 297 PHE B CZ  
4506  N N   . THR B 234 ? 0.7065 0.7308 1.2472 -0.0181 -0.3008 -0.2477 298 THR B N   
4507  C CA  . THR B 234 ? 0.8001 0.8201 1.3250 -0.0225 -0.2814 -0.2397 298 THR B CA  
4508  C C   . THR B 234 ? 0.8427 0.8718 1.3303 -0.0196 -0.2554 -0.2284 298 THR B C   
4509  O O   . THR B 234 ? 0.7358 0.7819 1.2367 -0.0212 -0.2441 -0.2198 298 THR B O   
4510  C CB  . THR B 234 ? 0.8522 0.8800 1.4329 -0.0357 -0.2747 -0.2307 298 THR B CB  
4511  O OG1 . THR B 234 ? 1.1916 1.2419 1.8178 -0.0423 -0.2636 -0.2185 298 THR B OG1 
4512  C CG2 . THR B 234 ? 1.0103 1.0242 1.6221 -0.0377 -0.3035 -0.2437 298 THR B CG2 
4513  N N   . TYR B 235 ? 0.9264 0.9429 1.3659 -0.0141 -0.2477 -0.2293 299 TYR B N   
4514  C CA  . TYR B 235 ? 0.7718 0.7930 1.1717 -0.0095 -0.2287 -0.2214 299 TYR B CA  
4515  C C   . TYR B 235 ? 0.7351 0.7494 1.1085 -0.0108 -0.2123 -0.2151 299 TYR B C   
4516  O O   . TYR B 235 ? 1.0170 1.0168 1.3824 -0.0099 -0.2202 -0.2213 299 TYR B O   
4517  C CB  . TYR B 235 ? 0.6903 0.7017 1.0494 0.0038  -0.2417 -0.2313 299 TYR B CB  
4518  C CG  . TYR B 235 ? 0.7425 0.7323 1.0610 0.0131  -0.2506 -0.2401 299 TYR B CG  
4519  C CD1 . TYR B 235 ? 0.7721 0.7457 1.0947 0.0178  -0.2750 -0.2543 299 TYR B CD1 
4520  C CD2 . TYR B 235 ? 0.7712 0.7560 1.0480 0.0178  -0.2345 -0.2338 299 TYR B CD2 
4521  C CE1 . TYR B 235 ? 0.8848 0.8370 1.1664 0.0284  -0.2820 -0.2618 299 TYR B CE1 
4522  C CE2 . TYR B 235 ? 0.6797 0.6454 0.9197 0.0274  -0.2404 -0.2400 299 TYR B CE2 
4523  C CZ  . TYR B 235 ? 0.7483 0.6976 0.9886 0.0334  -0.2632 -0.2538 299 TYR B CZ  
4524  O OH  . TYR B 235 ? 0.7635 0.6931 0.9635 0.0447  -0.2670 -0.2588 299 TYR B OH  
4525  N N   . THR B 236 ? 0.6797 0.7032 1.0387 -0.0123 -0.1905 -0.2032 300 THR B N   
4526  C CA  . THR B 236 ? 0.9529 0.9695 1.2802 -0.0117 -0.1755 -0.1973 300 THR B CA  
4527  C C   . THR B 236 ? 0.7359 0.7547 1.0264 -0.0055 -0.1646 -0.1921 300 THR B C   
4528  O O   . THR B 236 ? 0.7416 0.7715 1.0375 -0.0052 -0.1600 -0.1879 300 THR B O   
4529  C CB  . THR B 236 ? 1.0447 1.0678 1.3948 -0.0215 -0.1576 -0.1860 300 THR B CB  
4530  O OG1 . THR B 236 ? 1.2148 1.2521 1.5717 -0.0238 -0.1408 -0.1748 300 THR B OG1 
4531  C CG2 . THR B 236 ? 1.1518 1.1758 1.5482 -0.0292 -0.1660 -0.1882 300 THR B CG2 
4532  N N   . PHE B 237 ? 0.6946 0.7023 0.9488 -0.0002 -0.1609 -0.1919 301 PHE B N   
4533  C CA  . PHE B 237 ? 0.6578 0.6675 0.8819 0.0042  -0.1489 -0.1847 301 PHE B CA  
4534  C C   . PHE B 237 ? 0.7675 0.7818 0.9938 -0.0027 -0.1299 -0.1733 301 PHE B C   
4535  O O   . PHE B 237 ? 1.0882 1.0976 1.3191 -0.0069 -0.1259 -0.1719 301 PHE B O   
4536  C CB  . PHE B 237 ? 0.6327 0.6285 0.8177 0.0149  -0.1537 -0.1886 301 PHE B CB  
4537  C CG  . PHE B 237 ? 0.7004 0.6910 0.8715 0.0255  -0.1692 -0.1976 301 PHE B CG  
4538  C CD1 . PHE B 237 ? 0.7208 0.6992 0.8911 0.0313  -0.1877 -0.2099 301 PHE B CD1 
4539  C CD2 . PHE B 237 ? 0.7856 0.7816 0.9420 0.0308  -0.1659 -0.1941 301 PHE B CD2 
4540  C CE1 . PHE B 237 ? 0.7713 0.7429 0.9248 0.0432  -0.2029 -0.2188 301 PHE B CE1 
4541  C CE2 . PHE B 237 ? 0.6863 0.6768 0.8277 0.0419  -0.1797 -0.2021 301 PHE B CE2 
4542  C CZ  . PHE B 237 ? 0.7456 0.7238 0.8845 0.0485  -0.1981 -0.2145 301 PHE B CZ  
4543  N N   . LYS B 238 ? 0.7105 0.7333 0.9324 -0.0032 -0.1190 -0.1654 302 LYS B N   
4544  C CA  . LYS B 238 ? 0.6014 0.6267 0.8204 -0.0076 -0.1026 -0.1552 302 LYS B CA  
4545  C C   . LYS B 238 ? 0.6506 0.6726 0.8384 -0.0022 -0.0982 -0.1511 302 LYS B C   
4546  O O   . LYS B 238 ? 0.7896 0.8118 0.9657 0.0038  -0.1049 -0.1542 302 LYS B O   
4547  C CB  . LYS B 238 ? 0.4578 0.4949 0.7018 -0.0119 -0.0943 -0.1491 302 LYS B CB  
4548  C CG  . LYS B 238 ? 0.6186 0.6612 0.9008 -0.0172 -0.0983 -0.1513 302 LYS B CG  
4549  C CD  . LYS B 238 ? 0.7778 0.8322 1.0839 -0.0199 -0.0866 -0.1425 302 LYS B CD  
4550  C CE  . LYS B 238 ? 0.9609 1.0188 1.3015 -0.0261 -0.0812 -0.1384 302 LYS B CE  
4551  N NZ  . LYS B 238 ? 0.9196 0.9837 1.2674 -0.0262 -0.0625 -0.1261 302 LYS B NZ  
4552  N N   . GLU B 239 ? 0.7265 0.7451 0.9020 -0.0039 -0.0875 -0.1440 303 GLU B N   
4553  C CA  . GLU B 239 ? 0.6425 0.6589 0.7947 -0.0002 -0.0824 -0.1381 303 GLU B CA  
4554  C C   . GLU B 239 ? 0.6390 0.6593 0.7957 -0.0040 -0.0714 -0.1303 303 GLU B C   
4555  O O   . GLU B 239 ? 0.8412 0.8605 1.0058 -0.0083 -0.0643 -0.1271 303 GLU B O   
4556  C CB  . GLU B 239 ? 0.8169 0.8241 0.9498 0.0025  -0.0812 -0.1366 303 GLU B CB  
4557  C CG  . GLU B 239 ? 0.8927 0.8978 1.0071 0.0051  -0.0748 -0.1283 303 GLU B CG  
4558  C CD  . GLU B 239 ? 1.1054 1.1087 1.2032 0.0133  -0.0799 -0.1284 303 GLU B CD  
4559  O OE1 . GLU B 239 ? 1.2624 1.2641 1.3576 0.0186  -0.0888 -0.1356 303 GLU B OE1 
4560  O OE2 . GLU B 239 ? 1.3648 1.3675 1.4526 0.0150  -0.0753 -0.1207 303 GLU B OE2 
4561  N N   . PRO B 240 ? 0.6763 0.6994 0.8261 -0.0014 -0.0703 -0.1272 304 PRO B N   
4562  C CA  . PRO B 240 ? 0.6647 0.6890 0.8149 -0.0027 -0.0616 -0.1206 304 PRO B CA  
4563  C C   . PRO B 240 ? 0.6018 0.6189 0.7384 -0.0037 -0.0557 -0.1149 304 PRO B C   
4564  O O   . PRO B 240 ? 0.5569 0.5694 0.6797 -0.0019 -0.0584 -0.1137 304 PRO B O   
4565  C CB  . PRO B 240 ? 0.5569 0.5834 0.6993 0.0015  -0.0649 -0.1201 304 PRO B CB  
4566  C CG  . PRO B 240 ? 0.5253 0.5494 0.6560 0.0051  -0.0726 -0.1232 304 PRO B CG  
4567  C CD  . PRO B 240 ? 0.5897 0.6127 0.7267 0.0042  -0.0771 -0.1291 304 PRO B CD  
4568  N N   . CYS B 241 ? 0.7274 0.7434 0.8686 -0.0057 -0.0476 -0.1108 305 CYS B N   
4569  C CA  . CYS B 241 ? 0.8133 0.8222 0.9444 -0.0068 -0.0424 -0.1059 305 CYS B CA  
4570  C C   . CYS B 241 ? 0.7796 0.7841 0.8988 -0.0037 -0.0408 -0.1013 305 CYS B C   
4571  O O   . CYS B 241 ? 1.1614 1.1619 1.2785 -0.0029 -0.0345 -0.0978 305 CYS B O   
4572  C CB  . CYS B 241 ? 0.8923 0.9012 1.0355 -0.0097 -0.0346 -0.1046 305 CYS B CB  
4573  S SG  . CYS B 241 ? 1.2829 1.2956 1.4454 -0.0139 -0.0380 -0.1106 305 CYS B SG  
4574  N N   . LEU B 242 ? 0.6263 0.6303 0.7371 -0.0011 -0.0468 -0.1012 306 LEU B N   
4575  C CA  . LEU B 242 ? 0.6711 0.6694 0.7717 0.0022  -0.0475 -0.0978 306 LEU B CA  
4576  C C   . LEU B 242 ? 0.7758 0.7703 0.8676 0.0029  -0.0539 -0.0952 306 LEU B C   
4577  O O   . LEU B 242 ? 0.7607 0.7593 0.8535 0.0034  -0.0578 -0.0967 306 LEU B O   
4578  C CB  . LEU B 242 ? 0.6287 0.6310 0.7328 0.0057  -0.0475 -0.0995 306 LEU B CB  
4579  C CG  . LEU B 242 ? 0.7332 0.7388 0.8474 0.0069  -0.0393 -0.0991 306 LEU B CG  
4580  C CD1 . LEU B 242 ? 0.8662 0.8773 0.9855 0.0109  -0.0397 -0.1003 306 LEU B CD1 
4581  C CD2 . LEU B 242 ? 0.9843 0.9807 1.0885 0.0099  -0.0329 -0.0946 306 LEU B CD2 
4582  N N   . GLY B 243 ? 0.6841 0.6700 0.7677 0.0038  -0.0552 -0.0910 307 GLY B N   
4583  C CA  . GLY B 243 ? 0.8130 0.7946 0.8927 0.0040  -0.0613 -0.0866 307 GLY B CA  
4584  C C   . GLY B 243 ? 0.8582 0.8408 0.9369 0.0067  -0.0672 -0.0867 307 GLY B C   
4585  O O   . GLY B 243 ? 1.3938 1.3735 1.4726 0.0069  -0.0718 -0.0819 307 GLY B O   
4586  N N   . PHE B 244 ? 1.0391 1.0260 1.1187 0.0089  -0.0665 -0.0913 308 PHE B N   
4587  C CA  . PHE B 244 ? 0.9565 0.9451 1.0349 0.0121  -0.0716 -0.0923 308 PHE B CA  
4588  C C   . PHE B 244 ? 0.8580 0.8549 0.9406 0.0121  -0.0722 -0.0939 308 PHE B C   
4589  O O   . PHE B 244 ? 1.1182 1.1219 1.2062 0.0117  -0.0700 -0.0989 308 PHE B O   
4590  C CB  . PHE B 244 ? 1.0150 1.0043 1.0922 0.0155  -0.0698 -0.0958 308 PHE B CB  
4591  C CG  . PHE B 244 ? 1.9770 1.9624 2.0484 0.0198  -0.0757 -0.0958 308 PHE B CG  
4592  C CD1 . PHE B 244 ? 2.2659 2.2390 2.3284 0.0221  -0.0813 -0.0932 308 PHE B CD1 
4593  C CD2 . PHE B 244 ? 2.2351 2.2281 2.3100 0.0220  -0.0768 -0.0988 308 PHE B CD2 
4594  C CE1 . PHE B 244 ? 2.1205 2.0883 2.1774 0.0264  -0.0877 -0.0935 308 PHE B CE1 
4595  C CE2 . PHE B 244 ? 2.0910 2.0799 2.1600 0.0264  -0.0820 -0.0988 308 PHE B CE2 
4596  C CZ  . PHE B 244 ? 1.4991 1.4750 1.5588 0.0286  -0.0874 -0.0961 308 PHE B CZ  
4597  N N   . LEU B 245 ? 0.5711 0.5662 0.6517 0.0134  -0.0756 -0.0893 309 LEU B N   
4598  C CA  . LEU B 245 ? 0.5987 0.5989 0.6791 0.0156  -0.0755 -0.0895 309 LEU B CA  
4599  C C   . LEU B 245 ? 0.6487 0.6527 0.7280 0.0196  -0.0792 -0.0926 309 LEU B C   
4600  O O   . LEU B 245 ? 0.9468 0.9474 1.0245 0.0213  -0.0825 -0.0893 309 LEU B O   
4601  C CB  . LEU B 245 ? 0.7753 0.7722 0.8549 0.0166  -0.0751 -0.0808 309 LEU B CB  
4602  C CG  . LEU B 245 ? 0.6942 0.6878 0.7757 0.0132  -0.0716 -0.0763 309 LEU B CG  
4603  C CD1 . LEU B 245 ? 0.4934 0.4867 0.5755 0.0162  -0.0693 -0.0673 309 LEU B CD1 
4604  C CD2 . LEU B 245 ? 0.7103 0.7065 0.7913 0.0111  -0.0678 -0.0827 309 LEU B CD2 
4605  N N   . GLY B 246 ? 0.6033 0.6134 0.6842 0.0213  -0.0798 -0.0992 310 GLY B N   
4606  C CA  . GLY B 246 ? 0.7086 0.7232 0.7893 0.0254  -0.0839 -0.1033 310 GLY B CA  
4607  C C   . GLY B 246 ? 0.6298 0.6435 0.7030 0.0314  -0.0865 -0.1000 310 GLY B C   
4608  O O   . GLY B 246 ? 0.6283 0.6421 0.6996 0.0346  -0.0893 -0.0988 310 GLY B O   
4609  N N   . ASP B 247 ? 0.8101 0.8223 0.8784 0.0340  -0.0847 -0.0977 311 ASP B N   
4610  C CA  . ASP B 247 ? 0.7520 0.7632 0.8109 0.0424  -0.0857 -0.0948 311 ASP B CA  
4611  C C   . ASP B 247 ? 0.6878 0.6956 0.7467 0.0439  -0.0837 -0.0840 311 ASP B C   
4612  O O   . ASP B 247 ? 0.5468 0.5521 0.6128 0.0381  -0.0835 -0.0800 311 ASP B O   
4613  C CB  . ASP B 247 ? 0.7908 0.7994 0.8424 0.0461  -0.0831 -0.0943 311 ASP B CB  
4614  C CG  . ASP B 247 ? 0.7615 0.7691 0.8008 0.0565  -0.0868 -0.0985 311 ASP B CG  
4615  O OD1 . ASP B 247 ? 0.6193 0.6275 0.6541 0.0623  -0.0885 -0.0964 311 ASP B OD1 
4616  O OD2 . ASP B 247 ? 0.7801 0.7850 0.8132 0.0597  -0.0885 -0.1041 311 ASP B OD2 
4617  N N   . THR B 248 ? 0.7645 0.7714 0.8157 0.0525  -0.0828 -0.0791 312 THR B N   
4618  C CA  . THR B 248 ? 0.6388 0.6429 0.6924 0.0555  -0.0805 -0.0672 312 THR B CA  
4619  C C   . THR B 248 ? 0.7495 0.7522 0.7926 0.0668  -0.0757 -0.0605 312 THR B C   
4620  O O   . THR B 248 ? 1.2899 1.2931 1.3207 0.0750  -0.0782 -0.0667 312 THR B O   
4621  C CB  . THR B 248 ? 0.6470 0.6518 0.7028 0.0559  -0.0855 -0.0690 312 THR B CB  
4622  O OG1 . THR B 248 ? 0.7905 0.7948 0.8534 0.0477  -0.0892 -0.0741 312 THR B OG1 
4623  C CG2 . THR B 248 ? 0.6757 0.6771 0.7363 0.0590  -0.0835 -0.0563 312 THR B CG2 
4624  N N   . PRO B 249 ? 0.7042 0.7044 0.7515 0.0686  -0.0689 -0.0473 313 PRO B N   
4625  C CA  . PRO B 249 ? 0.9662 0.9654 1.0299 0.0594  -0.0682 -0.0400 313 PRO B CA  
4626  C C   . PRO B 249 ? 1.0088 1.0079 1.0736 0.0527  -0.0675 -0.0450 313 PRO B C   
4627  O O   . PRO B 249 ? 0.7546 0.7545 0.8087 0.0552  -0.0672 -0.0536 313 PRO B O   
4628  C CB  . PRO B 249 ? 1.2548 1.2525 1.3245 0.0656  -0.0606 -0.0229 313 PRO B CB  
4629  C CG  . PRO B 249 ? 1.1765 1.1738 1.2280 0.0779  -0.0546 -0.0230 313 PRO B CG  
4630  C CD  . PRO B 249 ? 0.6989 0.6969 0.7353 0.0806  -0.0615 -0.0389 313 PRO B CD  
4631  N N   . ARG B 250 ? 1.0626 1.0597 1.1409 0.0447  -0.0682 -0.0398 314 ARG B N   
4632  C CA  . ARG B 250 ? 0.8523 0.8486 0.9333 0.0376  -0.0678 -0.0435 314 ARG B CA  
4633  C C   . ARG B 250 ? 0.9048 0.8979 1.0011 0.0325  -0.0682 -0.0329 314 ARG B C   
4634  O O   . ARG B 250 ? 0.9287 0.9199 1.0355 0.0329  -0.0708 -0.0247 314 ARG B O   
4635  C CB  . ARG B 250 ? 0.7480 0.7447 0.8269 0.0318  -0.0732 -0.0562 314 ARG B CB  
4636  C CG  . ARG B 250 ? 0.8871 0.8813 0.9709 0.0296  -0.0795 -0.0567 314 ARG B CG  
4637  C CD  . ARG B 250 ? 0.7601 0.7539 0.8416 0.0253  -0.0828 -0.0670 314 ARG B CD  
4638  N NE  . ARG B 250 ? 0.6855 0.6784 0.7655 0.0269  -0.0878 -0.0705 314 ARG B NE  
4639  C CZ  . ARG B 250 ? 0.6849 0.6709 0.7683 0.0254  -0.0931 -0.0678 314 ARG B CZ  
4640  N NH1 . ARG B 250 ? 1.0717 1.0514 1.1619 0.0219  -0.0951 -0.0617 314 ARG B NH1 
4641  N NH2 . ARG B 250 ? 0.5978 0.5827 0.6779 0.0279  -0.0973 -0.0716 314 ARG B NH2 
4642  N N   . GLY B 251 ? 0.6821 0.6740 0.7810 0.0278  -0.0664 -0.0331 315 GLY B N   
4643  C CA  . GLY B 251 ? 1.2611 1.2503 1.3755 0.0242  -0.0666 -0.0220 315 GLY B CA  
4644  C C   . GLY B 251 ? 1.1783 1.1617 1.2999 0.0173  -0.0761 -0.0256 315 GLY B C   
4645  O O   . GLY B 251 ? 1.8343 1.8139 1.9680 0.0163  -0.0820 -0.0194 315 GLY B O   
4646  N N   . ILE B 252 ? 0.9912 0.9728 1.1046 0.0135  -0.0776 -0.0358 316 ILE B N   
4647  C CA  . ILE B 252 ? 1.0258 0.9998 1.1424 0.0087  -0.0849 -0.0386 316 ILE B CA  
4648  C C   . ILE B 252 ? 0.8477 0.8218 0.9521 0.0072  -0.0825 -0.0495 316 ILE B C   
4649  O O   . ILE B 252 ? 1.2298 1.2095 1.3287 0.0080  -0.0755 -0.0525 316 ILE B O   
4650  C CB  . ILE B 252 ? 1.3017 1.2725 1.4318 0.0056  -0.0860 -0.0291 316 ILE B CB  
4651  C CG1 . ILE B 252 ? 0.7802 0.7402 0.9165 0.0025  -0.0981 -0.0298 316 ILE B CG1 
4652  C CG2 . ILE B 252 ? 1.3151 1.2887 1.4398 0.0043  -0.0785 -0.0308 316 ILE B CG2 
4653  C CD1 . ILE B 252 ? 0.7400 0.6970 0.8907 0.0030  -0.1054 -0.0224 316 ILE B CD1 
4654  N N   . ASP B 253 ? 0.9813 0.9482 1.0814 0.0059  -0.0884 -0.0550 317 ASP B N   
4655  C CA  . ASP B 253 ? 1.1885 1.1557 1.2784 0.0056  -0.0846 -0.0638 317 ASP B CA  
4656  C C   . ASP B 253 ? 0.9456 0.9113 1.0363 0.0029  -0.0808 -0.0622 317 ASP B C   
4657  O O   . ASP B 253 ? 1.0566 1.0174 1.1541 0.0013  -0.0846 -0.0558 317 ASP B O   
4658  C CB  . ASP B 253 ? 1.2929 1.2523 1.3750 0.0078  -0.0903 -0.0695 317 ASP B CB  
4659  C CG  . ASP B 253 ? 1.3271 1.2904 1.4063 0.0109  -0.0914 -0.0731 317 ASP B CG  
4660  O OD1 . ASP B 253 ? 0.8997 0.8729 0.9802 0.0114  -0.0862 -0.0749 317 ASP B OD1 
4661  O OD2 . ASP B 253 ? 1.5252 1.4806 1.6001 0.0136  -0.0983 -0.0747 317 ASP B OD2 
4662  N N   . THR B 254 ? 0.7946 0.7648 0.8803 0.0023  -0.0737 -0.0675 318 THR B N   
4663  C CA  . THR B 254 ? 1.2134 1.1831 1.2996 -0.0001 -0.0687 -0.0660 318 THR B CA  
4664  C C   . THR B 254 ? 1.0015 0.9666 1.0810 -0.0003 -0.0663 -0.0712 318 THR B C   
4665  O O   . THR B 254 ? 0.6851 0.6469 0.7592 0.0023  -0.0683 -0.0752 318 THR B O   
4666  C CB  . THR B 254 ? 1.0041 0.9816 1.0907 -0.0002 -0.0617 -0.0669 318 THR B CB  
4667  O OG1 . THR B 254 ? 1.3118 1.2939 1.3957 0.0008  -0.0602 -0.0747 318 THR B OG1 
4668  C CG2 . THR B 254 ? 0.9127 0.8936 1.0033 0.0023  -0.0619 -0.0599 318 THR B CG2 
4669  N N   . THR B 255 ? 0.9831 0.9477 1.0625 -0.0022 -0.0611 -0.0702 319 THR B N   
4670  C CA  . THR B 255 ? 1.0489 1.0107 1.1229 -0.0017 -0.0560 -0.0744 319 THR B CA  
4671  C C   . THR B 255 ? 0.8115 0.7821 0.8891 -0.0024 -0.0500 -0.0795 319 THR B C   
4672  O O   . THR B 255 ? 0.8463 0.8232 0.9279 -0.0029 -0.0510 -0.0802 319 THR B O   
4673  C CB  . THR B 255 ? 0.9394 0.8975 1.0127 -0.0034 -0.0525 -0.0715 319 THR B CB  
4674  O OG1 . THR B 255 ? 1.2558 1.2204 1.3347 -0.0061 -0.0483 -0.0696 319 THR B OG1 
4675  C CG2 . THR B 255 ? 1.3999 1.3487 1.4719 -0.0025 -0.0605 -0.0668 319 THR B CG2 
4676  N N   . ASN B 256 ? 0.7100 0.6805 0.7871 -0.0017 -0.0443 -0.0825 320 ASN B N   
4677  C CA  . ASN B 256 ? 0.7386 0.7176 0.8244 -0.0030 -0.0398 -0.0869 320 ASN B CA  
4678  C C   . ASN B 256 ? 0.5811 0.5626 0.6724 -0.0065 -0.0356 -0.0876 320 ASN B C   
4679  O O   . ASN B 256 ? 0.8388 0.8158 0.9279 -0.0074 -0.0312 -0.0852 320 ASN B O   
4680  C CB  . ASN B 256 ? 0.8556 0.8346 0.9432 -0.0004 -0.0341 -0.0883 320 ASN B CB  
4681  C CG  . ASN B 256 ? 0.8009 0.7758 0.8805 0.0048  -0.0377 -0.0881 320 ASN B CG  
4682  O OD1 . ASN B 256 ? 1.1063 1.0775 1.1798 0.0057  -0.0455 -0.0872 320 ASN B OD1 
4683  N ND2 . ASN B 256 ? 0.7541 0.7291 0.8342 0.0089  -0.0317 -0.0882 320 ASN B ND2 
4684  N N   . TYR B 257 ? 0.6886 0.6760 0.7855 -0.0077 -0.0376 -0.0911 321 TYR B N   
4685  C CA  . TYR B 257 ? 0.7304 0.7186 0.8320 -0.0101 -0.0349 -0.0933 321 TYR B CA  
4686  C C   . TYR B 257 ? 0.7658 0.7594 0.8749 -0.0099 -0.0389 -0.0996 321 TYR B C   
4687  O O   . TYR B 257 ? 0.8342 0.8309 0.9417 -0.0074 -0.0441 -0.1013 321 TYR B O   
4688  C CB  . TYR B 257 ? 0.4799 0.4642 0.5738 -0.0098 -0.0352 -0.0894 321 TYR B CB  
4689  C CG  . TYR B 257 ? 0.7115 0.6965 0.7995 -0.0066 -0.0401 -0.0863 321 TYR B CG  
4690  C CD1 . TYR B 257 ? 0.5145 0.5016 0.6000 -0.0034 -0.0429 -0.0890 321 TYR B CD1 
4691  C CD2 . TYR B 257 ? 0.9480 0.9304 1.0330 -0.0058 -0.0422 -0.0804 321 TYR B CD2 
4692  C CE1 . TYR B 257 ? 0.6252 0.6128 0.7052 0.0009  -0.0457 -0.0847 321 TYR B CE1 
4693  C CE2 . TYR B 257 ? 1.1044 1.0878 1.1877 -0.0030 -0.0459 -0.0761 321 TYR B CE2 
4694  C CZ  . TYR B 257 ? 0.7601 0.7467 0.8408 0.0005  -0.0465 -0.0776 321 TYR B CZ  
4695  O OH  . TYR B 257 ? 0.8317 0.8191 0.9104 0.0046  -0.0484 -0.0718 321 TYR B OH  
4696  N N   . CYS B 258 ? 0.7962 0.7900 0.9137 -0.0122 -0.0376 -0.1033 322 CYS B N   
4697  C CA  . CYS B 258 ? 0.7984 0.7960 0.9260 -0.0121 -0.0435 -0.1105 322 CYS B CA  
4698  C C   . CYS B 258 ? 0.8443 0.8386 0.9619 -0.0083 -0.0504 -0.1142 322 CYS B C   
4699  O O   . CYS B 258 ? 0.8718 0.8667 0.9948 -0.0068 -0.0575 -0.1213 322 CYS B O   
4700  C CB  . CYS B 258 ? 0.9816 0.9809 1.1280 -0.0163 -0.0403 -0.1128 322 CYS B CB  
4701  S SG  . CYS B 258 ? 2.5258 2.5301 2.6842 -0.0173 -0.0314 -0.1077 322 CYS B SG  
4702  N N   . ASP B 259 ? 1.1748 1.1649 1.2774 -0.0054 -0.0486 -0.1090 323 ASP B N   
4703  C CA  . ASP B 259 ? 1.0835 1.0701 1.1732 0.0010  -0.0532 -0.1102 323 ASP B CA  
4704  C C   . ASP B 259 ? 0.8351 0.8252 0.9195 0.0056  -0.0573 -0.1094 323 ASP B C   
4705  O O   . ASP B 259 ? 0.9495 0.9445 1.0407 0.0032  -0.0574 -0.1088 323 ASP B O   
4706  C CB  . ASP B 259 ? 1.5788 1.5605 1.6576 0.0029  -0.0477 -0.1029 323 ASP B CB  
4707  C CG  . ASP B 259 ? 1.3761 1.3517 1.4416 0.0104  -0.0501 -0.1045 323 ASP B CG  
4708  O OD1 . ASP B 259 ? 0.9793 0.9515 1.0449 0.0125  -0.0563 -0.1133 323 ASP B OD1 
4709  O OD2 . ASP B 259 ? 2.0941 2.0677 2.1494 0.0151  -0.0459 -0.0964 323 ASP B OD2 
4710  N N   . LYS B 260 ? 0.6616 0.6483 0.7326 0.0132  -0.0601 -0.1088 324 LYS B N   
4711  C CA  . LYS B 260 ? 0.6224 0.6114 0.6870 0.0189  -0.0633 -0.1073 324 LYS B CA  
4712  C C   . LYS B 260 ? 0.6738 0.6619 0.7309 0.0221  -0.0578 -0.0957 324 LYS B C   
4713  O O   . LYS B 260 ? 1.3210 1.3050 1.3711 0.0253  -0.0533 -0.0902 324 LYS B O   
4714  C CB  . LYS B 260 ? 0.6628 0.6475 0.7172 0.0274  -0.0706 -0.1147 324 LYS B CB  
4715  C CG  . LYS B 260 ? 0.8017 0.7833 0.8388 0.0386  -0.0703 -0.1095 324 LYS B CG  
4716  C CD  . LYS B 260 ? 0.7012 0.6732 0.7207 0.0496  -0.0745 -0.1146 324 LYS B CD  
4717  C CE  . LYS B 260 ? 0.8164 0.7857 0.8422 0.0477  -0.0851 -0.1283 324 LYS B CE  
4718  N NZ  . LYS B 260 ? 0.8114 0.7685 0.8164 0.0605  -0.0912 -0.1338 324 LYS B NZ  
4719  N N   . THR B 261 ? 0.5607 0.5526 0.6210 0.0216  -0.0585 -0.0917 325 THR B N   
4720  C CA  . THR B 261 ? 0.7555 0.7470 0.8151 0.0231  -0.0546 -0.0800 325 THR B CA  
4721  C C   . THR B 261 ? 0.7163 0.7062 0.7657 0.0332  -0.0529 -0.0735 325 THR B C   
4722  O O   . THR B 261 ? 0.5166 0.5083 0.5637 0.0375  -0.0558 -0.0734 325 THR B O   
4723  C CB  . THR B 261 ? 0.6629 0.6572 0.7306 0.0189  -0.0571 -0.0781 325 THR B CB  
4724  O OG1 . THR B 261 ? 0.7822 0.7765 0.8569 0.0116  -0.0569 -0.0819 325 THR B OG1 
4725  C CG2 . THR B 261 ? 0.5516 0.5446 0.6225 0.0199  -0.0550 -0.0661 325 THR B CG2 
4726  N N   . THR B 262 ? 0.8607 0.8471 0.9040 0.0379  -0.0472 -0.0667 326 THR B N   
4727  C CA  . THR B 262 ? 1.1443 1.1277 1.1742 0.0505  -0.0442 -0.0611 326 THR B CA  
4728  C C   . THR B 262 ? 0.9251 0.9112 0.9609 0.0537  -0.0398 -0.0472 326 THR B C   
4729  O O   . THR B 262 ? 0.8551 0.8394 0.8806 0.0653  -0.0365 -0.0413 326 THR B O   
4730  C CB  . THR B 262 ? 0.9936 0.9712 1.0125 0.0567  -0.0388 -0.0584 326 THR B CB  
4731  O OG1 . THR B 262 ? 0.9338 0.9133 0.9623 0.0544  -0.0312 -0.0450 326 THR B OG1 
4732  C CG2 . THR B 262 ? 0.8842 0.8588 0.9027 0.0509  -0.0427 -0.0703 326 THR B CG2 
4733  N N   . THR B 263 ? 0.7099 0.6993 0.7624 0.0444  -0.0404 -0.0421 327 THR B N   
4734  C CA  . THR B 263 ? 0.7428 0.7341 0.8063 0.0460  -0.0373 -0.0279 327 THR B CA  
4735  C C   . THR B 263 ? 0.8469 0.8399 0.9107 0.0481  -0.0417 -0.0292 327 THR B C   
4736  O O   . THR B 263 ? 0.7999 0.7941 0.8670 0.0415  -0.0487 -0.0384 327 THR B O   
4737  C CB  . THR B 263 ? 0.8424 0.8345 0.9239 0.0358  -0.0389 -0.0227 327 THR B CB  
4738  O OG1 . THR B 263 ? 1.3687 1.3590 1.4483 0.0322  -0.0364 -0.0255 327 THR B OG1 
4739  C CG2 . THR B 263 ? 0.7822 0.7757 0.8787 0.0382  -0.0349 -0.0056 327 THR B CG2 
4740  N N   . GLU B 264 ? 0.8833 0.8763 0.9438 0.0583  -0.0366 -0.0189 328 GLU B N   
4741  C CA  . GLU B 264 ? 0.8428 0.8368 0.8999 0.0631  -0.0397 -0.0199 328 GLU B CA  
4742  C C   . GLU B 264 ? 0.7581 0.7512 0.7994 0.0653  -0.0463 -0.0364 328 GLU B C   
4743  O O   . GLU B 264 ? 0.7639 0.7587 0.8058 0.0642  -0.0521 -0.0420 328 GLU B O   
4744  C CB  . GLU B 264 ? 0.8036 0.7994 0.8793 0.0545  -0.0447 -0.0161 328 GLU B CB  
4745  C CG  . GLU B 264 ? 1.0138 1.0103 1.1077 0.0555  -0.0396 0.0024  328 GLU B CG  
4746  C CD  . GLU B 264 ? 1.3016 1.2983 1.4062 0.0556  -0.0434 0.0078  328 GLU B CD  
4747  O OE1 . GLU B 264 ? 1.6966 1.6937 1.7901 0.0650  -0.0409 0.0085  328 GLU B OE1 
4748  O OE2 . GLU B 264 ? 1.2869 1.2824 1.4101 0.0469  -0.0495 0.0111  328 GLU B OE2 
4749  N N   . GLY B 265 ? 0.9070 0.8969 0.9352 0.0691  -0.0458 -0.0437 329 GLY B N   
4750  C CA  . GLY B 265 ? 0.6107 0.5992 0.6278 0.0704  -0.0536 -0.0596 329 GLY B CA  
4751  C C   . GLY B 265 ? 0.6194 0.6050 0.6203 0.0837  -0.0558 -0.0615 329 GLY B C   
4752  O O   . GLY B 265 ? 1.0044 0.9902 1.0006 0.0843  -0.0644 -0.0739 329 GLY B O   
4753  N N   . GLU B 266 ? 0.5805 0.5637 0.5741 0.0948  -0.0479 -0.0484 330 GLU B N   
4754  C CA  . GLU B 266 ? 0.6769 0.6560 0.6519 0.1101  -0.0484 -0.0484 330 GLU B CA  
4755  C C   . GLU B 266 ? 0.6563 0.6399 0.6390 0.1091  -0.0506 -0.0456 330 GLU B C   
4756  O O   . GLU B 266 ? 0.6140 0.6024 0.6156 0.1009  -0.0473 -0.0360 330 GLU B O   
4757  C CB  . GLU B 266 ? 0.7931 0.7667 0.7546 0.1255  -0.0370 -0.0341 330 GLU B CB  
4758  C CG  . GLU B 266 ? 1.3167 1.2828 1.2519 0.1448  -0.0375 -0.0356 330 GLU B CG  
4759  C CD  . GLU B 266 ? 1.9965 1.9542 1.9113 0.1630  -0.0265 -0.0244 330 GLU B CD  
4760  O OE1 . GLU B 266 ? 2.4956 2.4547 2.4192 0.1597  -0.0180 -0.0148 330 GLU B OE1 
4761  O OE2 . GLU B 266 ? 2.3121 2.2613 2.2008 0.1818  -0.0264 -0.0252 330 GLU B OE2 
4762  N N   . GLY B 267 ? 0.6319 0.6126 0.5987 0.1189  -0.0566 -0.0539 331 GLY B N   
4763  C CA  . GLY B 267 ? 0.8546 0.8391 0.8262 0.1180  -0.0610 -0.0554 331 GLY B CA  
4764  C C   . GLY B 267 ? 0.8095 0.7990 0.7928 0.1045  -0.0713 -0.0700 331 GLY B C   
4765  O O   . GLY B 267 ? 0.8728 0.8628 0.8619 0.0961  -0.0735 -0.0768 331 GLY B O   
4766  N N   . GLY B 268 ? 0.7091 0.7023 0.6963 0.1033  -0.0766 -0.0739 332 GLY B N   
4767  C CA  . GLY B 268 ? 0.6792 0.6779 0.6790 0.0918  -0.0848 -0.0857 332 GLY B CA  
4768  C C   . GLY B 268 ? 0.6903 0.6916 0.6882 0.0956  -0.0910 -0.0906 332 GLY B C   
4769  O O   . GLY B 268 ? 0.8649 0.8629 0.8493 0.1079  -0.0902 -0.0869 332 GLY B O   
4770  N N   . ILE B 269 ? 0.5062 0.5133 0.5174 0.0859  -0.0964 -0.0984 333 ILE B N   
4771  C CA  . ILE B 269 ? 0.6469 0.6574 0.6581 0.0888  -0.1027 -0.1041 333 ILE B CA  
4772  C C   . ILE B 269 ? 0.6685 0.6851 0.6934 0.0800  -0.1092 -0.1156 333 ILE B C   
4773  O O   . ILE B 269 ? 0.4489 0.4675 0.4855 0.0701  -0.1065 -0.1158 333 ILE B O   
4774  C CB  . ILE B 269 ? 0.6307 0.6420 0.6469 0.0872  -0.0992 -0.0951 333 ILE B CB  
4775  C CG1 . ILE B 269 ? 0.8918 0.9050 0.9024 0.0945  -0.1049 -0.0995 333 ILE B CG1 
4776  C CG2 . ILE B 269 ? 0.4031 0.4172 0.4352 0.0744  -0.0983 -0.0948 333 ILE B CG2 
4777  C CD1 . ILE B 269 ? 1.1421 1.1537 1.1530 0.0971  -0.1013 -0.0893 333 ILE B CD1 
4778  N N   . GLN B 270 ? 0.6432 0.6629 0.6674 0.0847  -0.1174 -0.1243 334 GLN B N   
4779  C CA  . GLN B 270 ? 0.5943 0.6206 0.6343 0.0782  -0.1238 -0.1344 334 GLN B CA  
4780  C C   . GLN B 270 ? 0.6521 0.6840 0.7078 0.0678  -0.1189 -0.1312 334 GLN B C   
4781  O O   . GLN B 270 ? 0.6879 0.7197 0.7419 0.0680  -0.1161 -0.1254 334 GLN B O   
4782  C CB  . GLN B 270 ? 0.7306 0.7596 0.7684 0.0860  -0.1336 -0.1422 334 GLN B CB  
4783  C CG  . GLN B 270 ? 0.7661 0.8027 0.8240 0.0805  -0.1415 -0.1524 334 GLN B CG  
4784  C CD  . GLN B 270 ? 0.7227 0.7612 0.7789 0.0889  -0.1527 -0.1604 334 GLN B CD  
4785  O OE1 . GLN B 270 ? 0.8373 0.8719 0.8762 0.0986  -0.1534 -0.1579 334 GLN B OE1 
4786  N NE2 . GLN B 270 ? 0.7342 0.7785 0.8096 0.0856  -0.1618 -0.1695 334 GLN B NE2 
4787  N N   . GLY B 271 ? 0.6397 0.6750 0.7096 0.0596  -0.1182 -0.1348 335 GLY B N   
4788  C CA  . GLY B 271 ? 0.6198 0.6595 0.7030 0.0518  -0.1134 -0.1326 335 GLY B CA  
4789  C C   . GLY B 271 ? 0.6351 0.6802 0.7364 0.0455  -0.1136 -0.1377 335 GLY B C   
4790  O O   . GLY B 271 ? 0.8209 0.8658 0.9259 0.0458  -0.1186 -0.1436 335 GLY B O   
4791  N N   . PHE B 272 ? 0.5074 0.5562 0.6196 0.0406  -0.1081 -0.1351 336 PHE B N   
4792  C CA  . PHE B 272 ? 0.4413 0.4965 0.5740 0.0355  -0.1064 -0.1380 336 PHE B CA  
4793  C C   . PHE B 272 ? 0.4005 0.4535 0.5367 0.0299  -0.0971 -0.1327 336 PHE B C   
4794  O O   . PHE B 272 ? 0.5344 0.5803 0.6571 0.0297  -0.0928 -0.1272 336 PHE B O   
4795  C CB  . PHE B 272 ? 0.4343 0.4985 0.5814 0.0372  -0.1082 -0.1399 336 PHE B CB  
4796  C CG  . PHE B 272 ? 0.4706 0.5333 0.6100 0.0394  -0.1029 -0.1345 336 PHE B CG  
4797  C CD1 . PHE B 272 ? 0.4116 0.4757 0.5589 0.0374  -0.0944 -0.1303 336 PHE B CD1 
4798  C CD2 . PHE B 272 ? 0.5223 0.5805 0.6450 0.0445  -0.1061 -0.1333 336 PHE B CD2 
4799  C CE1 . PHE B 272 ? 0.4647 0.5246 0.6012 0.0411  -0.0906 -0.1259 336 PHE B CE1 
4800  C CE2 . PHE B 272 ? 0.5708 0.6256 0.6860 0.0467  -0.1025 -0.1287 336 PHE B CE2 
4801  C CZ  . PHE B 272 ? 0.4447 0.4997 0.5656 0.0453  -0.0955 -0.1257 336 PHE B CZ  
4802  N N   . MET B 273 ? 0.3538 0.4123 0.5095 0.0257  -0.0948 -0.1344 337 MET B N   
4803  C CA  . MET B 273 ? 0.4216 0.4797 0.5846 0.0219  -0.0850 -0.1294 337 MET B CA  
4804  C C   . MET B 273 ? 0.4456 0.5142 0.6350 0.0209  -0.0831 -0.1301 337 MET B C   
4805  O O   . MET B 273 ? 0.7722 0.8471 0.9778 0.0203  -0.0908 -0.1356 337 MET B O   
4806  C CB  . MET B 273 ? 0.4194 0.4723 0.5810 0.0172  -0.0825 -0.1289 337 MET B CB  
4807  C CG  . MET B 273 ? 0.5352 0.5787 0.6746 0.0179  -0.0823 -0.1260 337 MET B CG  
4808  S SD  . MET B 273 ? 0.8422 0.8798 0.9792 0.0134  -0.0797 -0.1254 337 MET B SD  
4809  C CE  . MET B 273 ? 0.6549 0.6965 0.8064 0.0126  -0.0877 -0.1338 337 MET B CE  
4810  N N   . ILE B 274 ? 0.4497 0.5197 0.6444 0.0215  -0.0730 -0.1240 338 ILE B N   
4811  C CA  . ILE B 274 ? 0.5236 0.6039 0.7463 0.0210  -0.0683 -0.1219 338 ILE B CA  
4812  C C   . ILE B 274 ? 0.5714 0.6506 0.8046 0.0173  -0.0581 -0.1169 338 ILE B C   
4813  O O   . ILE B 274 ? 0.6278 0.6983 0.8433 0.0185  -0.0506 -0.1123 338 ILE B O   
4814  C CB  . ILE B 274 ? 0.5459 0.6294 0.7664 0.0277  -0.0627 -0.1173 338 ILE B CB  
4815  C CG1 . ILE B 274 ? 0.4645 0.5464 0.6693 0.0316  -0.0721 -0.1217 338 ILE B CG1 
4816  C CG2 . ILE B 274 ? 0.3963 0.4926 0.6490 0.0284  -0.0580 -0.1141 338 ILE B CG2 
4817  C CD1 . ILE B 274 ? 0.3842 0.4700 0.5898 0.0381  -0.0683 -0.1184 338 ILE B CD1 
4818  N N   . GLU B 275 ? 0.5866 0.6737 0.8494 0.0130  -0.0586 -0.1176 339 GLU B N   
4819  C CA  . GLU B 275 ? 0.7588 0.8458 1.0351 0.0099  -0.0479 -0.1116 339 GLU B CA  
4820  C C   . GLU B 275 ? 0.6641 0.7617 0.9682 0.0128  -0.0376 -0.1037 339 GLU B C   
4821  O O   . GLU B 275 ? 0.7883 0.8966 1.1186 0.0120  -0.0434 -0.1056 339 GLU B O   
4822  C CB  . GLU B 275 ? 0.8487 0.9351 1.1393 0.0028  -0.0556 -0.1173 339 GLU B CB  
4823  C CG  . GLU B 275 ? 1.2169 1.3066 1.5343 -0.0015 -0.0465 -0.1115 339 GLU B CG  
4824  C CD  . GLU B 275 ? 1.3320 1.4126 1.6307 -0.0009 -0.0343 -0.1054 339 GLU B CD  
4825  O OE1 . GLU B 275 ? 1.6902 1.7610 1.9566 0.0009  -0.0359 -0.1072 339 GLU B OE1 
4826  O OE2 . GLU B 275 ? 1.0347 1.1179 1.3526 -0.0020 -0.0231 -0.0981 339 GLU B OE2 
4827  N N   . GLY B 276 ? 0.5953 0.6896 0.8937 0.0172  -0.0225 -0.0944 340 GLY B N   
4828  C CA  . GLY B 276 ? 0.7914 0.8952 1.1149 0.0222  -0.0094 -0.0844 340 GLY B CA  
4829  C C   . GLY B 276 ? 0.8531 0.9502 1.1667 0.0278  0.0078  -0.0742 340 GLY B C   
4830  O O   . GLY B 276 ? 0.8890 0.9761 1.1858 0.0251  0.0088  -0.0753 340 GLY B O   
4831  N N   . SER B 277 ? 0.8193 0.9213 1.1422 0.0369  0.0217  -0.0639 341 SER B N   
4832  C CA  . SER B 277 ? 0.8921 0.9852 1.1983 0.0463  0.0386  -0.0538 341 SER B CA  
4833  C C   . SER B 277 ? 0.9332 1.0088 1.1919 0.0506  0.0331  -0.0594 341 SER B C   
4834  O O   . SER B 277 ? 1.2244 1.2891 1.4649 0.0490  0.0341  -0.0603 341 SER B O   
4835  C CB  . SER B 277 ? 1.1092 1.2089 1.4265 0.0583  0.0532  -0.0423 341 SER B CB  
4836  O OG  . SER B 277 ? 1.6753 1.7912 2.0411 0.0549  0.0608  -0.0342 341 SER B OG  
4837  N N   . ASN B 278 ? 0.7973 0.8706 1.0383 0.0558  0.0267  -0.0631 342 ASN B N   
4838  C CA  . ASN B 278 ? 0.6104 0.6699 0.8150 0.0563  0.0155  -0.0708 342 ASN B CA  
4839  C C   . ASN B 278 ? 0.5082 0.5724 0.7197 0.0446  -0.0003 -0.0808 342 ASN B C   
4840  O O   . ASN B 278 ? 0.5320 0.6086 0.7678 0.0404  -0.0055 -0.0835 342 ASN B O   
4841  C CB  . ASN B 278 ? 0.5741 0.6291 0.7596 0.0667  0.0146  -0.0704 342 ASN B CB  
4842  C CG  . ASN B 278 ? 0.6185 0.6625 0.7839 0.0816  0.0283  -0.0618 342 ASN B CG  
4843  O OD1 . ASN B 278 ? 0.9947 1.0257 1.1404 0.0849  0.0323  -0.0601 342 ASN B OD1 
4844  N ND2 . ASN B 278 ? 0.7377 0.7855 0.9056 0.0920  0.0351  -0.0567 342 ASN B ND2 
4845  N N   . SER B 279 ? 0.5600 0.6136 0.7499 0.0403  -0.0080 -0.0860 343 SER B N   
4846  C CA  . SER B 279 ? 0.6714 0.7273 0.8619 0.0322  -0.0221 -0.0945 343 SER B CA  
4847  C C   . SER B 279 ? 0.5641 0.6101 0.7264 0.0349  -0.0311 -0.0983 343 SER B C   
4848  O O   . SER B 279 ? 0.6951 0.7291 0.8350 0.0406  -0.0285 -0.0956 343 SER B O   
4849  C CB  . SER B 279 ? 0.7525 0.8066 0.9480 0.0240  -0.0236 -0.0966 343 SER B CB  
4850  O OG  . SER B 279 ? 0.7061 0.7700 0.9324 0.0203  -0.0179 -0.0940 343 SER B OG  
4851  N N   . TRP B 280 ? 0.5001 0.5504 0.6641 0.0316  -0.0420 -0.1042 344 TRP B N   
4852  C CA  . TRP B 280 ? 0.4696 0.5119 0.6113 0.0341  -0.0502 -0.1067 344 TRP B CA  
4853  C C   . TRP B 280 ? 0.4806 0.5213 0.6172 0.0287  -0.0595 -0.1110 344 TRP B C   
4854  O O   . TRP B 280 ? 0.4820 0.5303 0.6325 0.0248  -0.0634 -0.1150 344 TRP B O   
4855  C CB  . TRP B 280 ? 0.3795 0.4273 0.5238 0.0392  -0.0529 -0.1077 344 TRP B CB  
4856  C CG  . TRP B 280 ? 0.3862 0.4347 0.5327 0.0469  -0.0432 -0.1024 344 TRP B CG  
4857  C CD1 . TRP B 280 ? 0.3704 0.4304 0.5413 0.0482  -0.0346 -0.0986 344 TRP B CD1 
4858  C CD2 . TRP B 280 ? 0.4001 0.4366 0.5235 0.0560  -0.0409 -0.0995 344 TRP B CD2 
4859  N NE1 . TRP B 280 ? 0.3870 0.4437 0.5507 0.0582  -0.0253 -0.0926 344 TRP B NE1 
4860  C CE2 . TRP B 280 ? 0.4135 0.4554 0.5468 0.0638  -0.0293 -0.0936 344 TRP B CE2 
4861  C CE3 . TRP B 280 ? 0.3902 0.4118 0.4877 0.0590  -0.0476 -0.1007 344 TRP B CE3 
4862  C CZ2 . TRP B 280 ? 0.4315 0.4627 0.5445 0.0756  -0.0246 -0.0900 344 TRP B CZ2 
4863  C CZ3 . TRP B 280 ? 0.4016 0.4120 0.4805 0.0697  -0.0448 -0.0980 344 TRP B CZ3 
4864  C CH2 . TRP B 280 ? 0.4673 0.4816 0.5514 0.0785  -0.0334 -0.0931 344 TRP B CH2 
4865  N N   . ILE B 281 ? 0.4413 0.4713 0.5584 0.0294  -0.0632 -0.1099 345 ILE B N   
4866  C CA  . ILE B 281 ? 0.4385 0.4670 0.5492 0.0271  -0.0711 -0.1120 345 ILE B CA  
4867  C C   . ILE B 281 ? 0.5141 0.5373 0.6120 0.0314  -0.0766 -0.1111 345 ILE B C   
4868  O O   . ILE B 281 ? 0.8568 0.8703 0.9432 0.0342  -0.0764 -0.1082 345 ILE B O   
4869  C CB  . ILE B 281 ? 0.4366 0.4583 0.5408 0.0232  -0.0706 -0.1098 345 ILE B CB  
4870  C CG1 . ILE B 281 ? 0.5201 0.5470 0.6372 0.0187  -0.0664 -0.1115 345 ILE B CG1 
4871  C CG2 . ILE B 281 ? 0.3556 0.3753 0.4526 0.0229  -0.0770 -0.1097 345 ILE B CG2 
4872  C CD1 . ILE B 281 ? 0.7282 0.7481 0.8391 0.0152  -0.0640 -0.1087 345 ILE B CD1 
4873  N N   . GLY B 282 ? 0.5194 0.5479 0.6192 0.0329  -0.0821 -0.1139 346 GLY B N   
4874  C CA  . GLY B 282 ? 0.4773 0.5009 0.5662 0.0367  -0.0874 -0.1124 346 GLY B CA  
4875  C C   . GLY B 282 ? 0.4834 0.5030 0.5663 0.0352  -0.0908 -0.1099 346 GLY B C   
4876  O O   . GLY B 282 ? 0.8252 0.8481 0.9115 0.0329  -0.0903 -0.1112 346 GLY B O   
4877  N N   . ARG B 283 ? 0.4188 0.4305 0.4933 0.0370  -0.0942 -0.1056 347 ARG B N   
4878  C CA  . ARG B 283 ? 0.5642 0.5728 0.6360 0.0364  -0.0958 -0.1009 347 ARG B CA  
4879  C C   . ARG B 283 ? 0.5025 0.5041 0.5699 0.0391  -0.1001 -0.0958 347 ARG B C   
4880  O O   . ARG B 283 ? 0.5688 0.5644 0.6330 0.0405  -0.1029 -0.0960 347 ARG B O   
4881  C CB  . ARG B 283 ? 0.5419 0.5463 0.6149 0.0316  -0.0927 -0.0975 347 ARG B CB  
4882  C CG  . ARG B 283 ? 0.4376 0.4316 0.5081 0.0301  -0.0949 -0.0926 347 ARG B CG  
4883  C CD  . ARG B 283 ? 0.5740 0.5658 0.6464 0.0257  -0.0914 -0.0910 347 ARG B CD  
4884  N NE  . ARG B 283 ? 0.6937 0.6746 0.7647 0.0244  -0.0953 -0.0863 347 ARG B NE  
4885  C CZ  . ARG B 283 ? 0.7149 0.6921 0.7878 0.0209  -0.0939 -0.0833 347 ARG B CZ  
4886  N NH1 . ARG B 283 ? 0.6935 0.6769 0.7690 0.0183  -0.0877 -0.0843 347 ARG B NH1 
4887  N NH2 . ARG B 283 ? 1.1572 1.1236 1.2298 0.0202  -0.0996 -0.0795 347 ARG B NH2 
4888  N N   . ILE B 284 ? 0.6347 0.6364 0.7017 0.0408  -0.1005 -0.0906 348 ILE B N   
4889  C CA  . ILE B 284 ? 0.6318 0.6270 0.6988 0.0429  -0.1038 -0.0835 348 ILE B CA  
4890  C C   . ILE B 284 ? 0.5548 0.5410 0.6262 0.0383  -0.1056 -0.0779 348 ILE B C   
4891  O O   . ILE B 284 ? 0.7046 0.6912 0.7791 0.0347  -0.1023 -0.0757 348 ILE B O   
4892  C CB  . ILE B 284 ? 0.6259 0.6241 0.6922 0.0475  -0.1017 -0.0776 348 ILE B CB  
4893  C CG1 . ILE B 284 ? 0.7458 0.7520 0.8059 0.0528  -0.1012 -0.0847 348 ILE B CG1 
4894  C CG2 . ILE B 284 ? 0.6474 0.6395 0.7165 0.0501  -0.1048 -0.0697 348 ILE B CG2 
4895  C CD1 . ILE B 284 ? 0.5840 0.5910 0.6383 0.0611  -0.1008 -0.0802 348 ILE B CD1 
4896  N N   . ILE B 285 ? 0.4769 0.4540 0.5483 0.0388  -0.1118 -0.0762 349 ILE B N   
4897  C CA  . ILE B 285 ? 0.4338 0.3999 0.5085 0.0353  -0.1167 -0.0731 349 ILE B CA  
4898  C C   . ILE B 285 ? 0.4909 0.4550 0.5777 0.0325  -0.1170 -0.0627 349 ILE B C   
4899  O O   . ILE B 285 ? 0.4319 0.3936 0.5230 0.0286  -0.1165 -0.0605 349 ILE B O   
4900  C CB  . ILE B 285 ? 0.4285 0.3835 0.4985 0.0380  -0.1251 -0.0752 349 ILE B CB  
4901  C CG1 . ILE B 285 ? 0.4859 0.4431 0.5443 0.0416  -0.1228 -0.0842 349 ILE B CG1 
4902  C CG2 . ILE B 285 ? 0.3040 0.2455 0.3770 0.0354  -0.1329 -0.0726 349 ILE B CG2 
4903  C CD1 . ILE B 285 ? 0.4544 0.3989 0.5039 0.0462  -0.1305 -0.0870 349 ILE B CD1 
4904  N N   . ASN B 286 ? 0.6665 0.6317 0.7596 0.0352  -0.1172 -0.0555 350 ASN B N   
4905  C CA  . ASN B 286 ? 0.6324 0.5958 0.7409 0.0336  -0.1167 -0.0429 350 ASN B CA  
4906  C C   . ASN B 286 ? 0.6220 0.5952 0.7306 0.0381  -0.1070 -0.0368 350 ASN B C   
4907  O O   . ASN B 286 ? 0.7448 0.7196 0.8537 0.0433  -0.1056 -0.0323 350 ASN B O   
4908  C CB  . ASN B 286 ? 0.6837 0.6376 0.8027 0.0339  -0.1255 -0.0369 350 ASN B CB  
4909  C CG  . ASN B 286 ? 0.6211 0.5618 0.7395 0.0308  -0.1369 -0.0420 350 ASN B CG  
4910  O OD1 . ASN B 286 ? 0.8614 0.7970 0.9669 0.0335  -0.1416 -0.0508 350 ASN B OD1 
4911  N ND2 . ASN B 286 ? 0.9331 0.8674 1.0649 0.0262  -0.1418 -0.0363 350 ASN B ND2 
4912  N N   . PRO B 287 ? 0.6987 0.6772 0.8056 0.0371  -0.1002 -0.0363 351 PRO B N   
4913  C CA  . PRO B 287 ? 0.6263 0.6123 0.7271 0.0434  -0.0912 -0.0330 351 PRO B CA  
4914  C C   . PRO B 287 ? 0.7394 0.7253 0.8500 0.0489  -0.0866 -0.0179 351 PRO B C   
4915  O O   . PRO B 287 ? 0.9046 0.8945 1.0057 0.0576  -0.0804 -0.0156 351 PRO B O   
4916  C CB  . PRO B 287 ? 0.5457 0.5338 0.6463 0.0401  -0.0867 -0.0335 351 PRO B CB  
4917  C CG  . PRO B 287 ? 0.6261 0.6096 0.7274 0.0327  -0.0931 -0.0417 351 PRO B CG  
4918  C CD  . PRO B 287 ? 0.5477 0.5235 0.6582 0.0309  -0.1011 -0.0378 351 PRO B CD  
4919  N N   . GLY B 288 ? 0.7235 0.7041 0.8535 0.0446  -0.0901 -0.0075 352 GLY B N   
4920  C CA  . GLY B 288 ? 0.7312 0.7118 0.8761 0.0493  -0.0856 0.0088  352 GLY B CA  
4921  C C   . GLY B 288 ? 0.8665 0.8465 1.0052 0.0553  -0.0869 0.0081  352 GLY B C   
4922  O O   . GLY B 288 ? 1.0190 1.0034 1.1472 0.0649  -0.0788 0.0115  352 GLY B O   
4923  N N   . SER B 289 ? 0.9206 0.8940 1.0635 0.0507  -0.0976 0.0028  353 SER B N   
4924  C CA  . SER B 289 ? 0.6940 0.6655 0.8323 0.0556  -0.1002 0.0017  353 SER B CA  
4925  C C   . SER B 289 ? 0.6123 0.5884 0.7268 0.0602  -0.0999 -0.0126 353 SER B C   
4926  O O   . SER B 289 ? 0.9662 0.9422 1.0748 0.0659  -0.1006 -0.0132 353 SER B O   
4927  C CB  . SER B 289 ? 0.8741 0.8348 1.0256 0.0498  -0.1128 0.0018  353 SER B CB  
4928  O OG  . SER B 289 ? 1.0563 1.0112 1.2054 0.0427  -0.1212 -0.0079 353 SER B OG  
4929  N N   . LYS B 290 ? 0.5736 0.5538 0.6766 0.0578  -0.0991 -0.0236 354 LYS B N   
4930  C CA  . LYS B 290 ? 0.6202 0.6051 0.7057 0.0607  -0.1001 -0.0374 354 LYS B CA  
4931  C C   . LYS B 290 ? 0.7027 0.6832 0.7858 0.0587  -0.1085 -0.0453 354 LYS B C   
4932  O O   . LYS B 290 ? 0.8083 0.7929 0.8808 0.0628  -0.1094 -0.0535 354 LYS B O   
4933  C CB  . LYS B 290 ? 0.7583 0.7486 0.8330 0.0711  -0.0945 -0.0358 354 LYS B CB  
4934  C CG  . LYS B 290 ? 0.8665 0.8596 0.9382 0.0763  -0.0857 -0.0285 354 LYS B CG  
4935  C CD  . LYS B 290 ? 1.1768 1.1740 1.2388 0.0745  -0.0853 -0.0395 354 LYS B CD  
4936  C CE  . LYS B 290 ? 1.6141 1.6119 1.6720 0.0799  -0.0771 -0.0323 354 LYS B CE  
4937  N NZ  . LYS B 290 ? 1.8096 1.8077 1.8527 0.0937  -0.0727 -0.0294 354 LYS B NZ  
4938  N N   . LYS B 291 ? 0.6951 0.6663 0.7879 0.0532  -0.1153 -0.0428 355 LYS B N   
4939  C CA  . LYS B 291 ? 0.6205 0.5841 0.7093 0.0527  -0.1239 -0.0494 355 LYS B CA  
4940  C C   . LYS B 291 ? 0.7783 0.7409 0.8579 0.0496  -0.1260 -0.0606 355 LYS B C   
4941  O O   . LYS B 291 ? 0.6833 0.6447 0.7659 0.0449  -0.1251 -0.0607 355 LYS B O   
4942  C CB  . LYS B 291 ? 0.6712 0.6224 0.7741 0.0498  -0.1321 -0.0414 355 LYS B CB  
4943  C CG  . LYS B 291 ? 0.9436 0.8938 1.0564 0.0538  -0.1313 -0.0307 355 LYS B CG  
4944  C CD  . LYS B 291 ? 1.0449 0.9859 1.1539 0.0562  -0.1402 -0.0345 355 LYS B CD  
4945  C CE  . LYS B 291 ? 1.1006 1.0377 1.2250 0.0586  -0.1410 -0.0217 355 LYS B CE  
4946  N NZ  . LYS B 291 ? 1.7773 1.7096 1.9264 0.0533  -0.1428 -0.0086 355 LYS B NZ  
4947  N N   . GLY B 292 ? 0.6209 0.5840 0.6899 0.0531  -0.1280 -0.0691 356 GLY B N   
4948  C CA  . GLY B 292 ? 0.5700 0.5310 0.6310 0.0520  -0.1289 -0.0778 356 GLY B CA  
4949  C C   . GLY B 292 ? 0.5568 0.5293 0.6153 0.0507  -0.1215 -0.0836 356 GLY B C   
4950  O O   . GLY B 292 ? 0.6911 0.6709 0.7538 0.0487  -0.1165 -0.0813 356 GLY B O   
4951  N N   . PHE B 293 ? 0.5182 0.4918 0.5701 0.0527  -0.1206 -0.0907 357 PHE B N   
4952  C CA  . PHE B 293 ? 0.5253 0.5094 0.5785 0.0513  -0.1142 -0.0958 357 PHE B CA  
4953  C C   . PHE B 293 ? 0.7310 0.7092 0.7792 0.0516  -0.1132 -0.0989 357 PHE B C   
4954  O O   . PHE B 293 ? 0.7040 0.6749 0.7442 0.0567  -0.1161 -0.1008 357 PHE B O   
4955  C CB  . PHE B 293 ? 0.4468 0.4417 0.5004 0.0553  -0.1126 -0.1004 357 PHE B CB  
4956  C CG  . PHE B 293 ? 0.3834 0.3897 0.4431 0.0535  -0.1075 -0.1053 357 PHE B CG  
4957  C CD1 . PHE B 293 ? 0.3870 0.3962 0.4488 0.0543  -0.1042 -0.1090 357 PHE B CD1 
4958  C CD2 . PHE B 293 ? 0.4202 0.4335 0.4840 0.0519  -0.1062 -0.1058 357 PHE B CD2 
4959  C CE1 . PHE B 293 ? 0.4571 0.4773 0.5292 0.0523  -0.1001 -0.1127 357 PHE B CE1 
4960  C CE2 . PHE B 293 ? 0.4544 0.4767 0.5255 0.0501  -0.1037 -0.1110 357 PHE B CE2 
4961  C CZ  . PHE B 293 ? 0.4259 0.4523 0.5033 0.0497  -0.1008 -0.1143 357 PHE B CZ  
4962  N N   . GLU B 294 ? 0.5697 0.5499 0.6211 0.0474  -0.1087 -0.0991 358 GLU B N   
4963  C CA  . GLU B 294 ? 0.4704 0.4455 0.5166 0.0486  -0.1057 -0.1013 358 GLU B CA  
4964  C C   . GLU B 294 ? 0.4776 0.4653 0.5318 0.0466  -0.0973 -0.1041 358 GLU B C   
4965  O O   . GLU B 294 ? 0.6209 0.6174 0.6835 0.0423  -0.0955 -0.1043 358 GLU B O   
4966  C CB  . GLU B 294 ? 0.5780 0.5410 0.6210 0.0458  -0.1092 -0.0981 358 GLU B CB  
4967  C CG  . GLU B 294 ? 1.0441 1.0124 1.0962 0.0390  -0.1065 -0.0949 358 GLU B CG  
4968  C CD  . GLU B 294 ? 1.2274 1.1837 1.2782 0.0363  -0.1108 -0.0913 358 GLU B CD  
4969  O OE1 . GLU B 294 ? 1.5022 1.4457 1.5431 0.0400  -0.1153 -0.0929 358 GLU B OE1 
4970  O OE2 . GLU B 294 ? 1.0247 0.9837 1.0837 0.0314  -0.1100 -0.0869 358 GLU B OE2 
4971  N N   . ILE B 295 ? 0.4056 0.3933 0.4575 0.0506  -0.0921 -0.1058 359 ILE B N   
4972  C CA  . ILE B 295 ? 0.4183 0.4171 0.4815 0.0485  -0.0838 -0.1071 359 ILE B CA  
4973  C C   . ILE B 295 ? 0.4532 0.4438 0.5097 0.0507  -0.0785 -0.1052 359 ILE B C   
4974  O O   . ILE B 295 ? 0.5427 0.5210 0.5848 0.0574  -0.0801 -0.1044 359 ILE B O   
4975  C CB  . ILE B 295 ? 0.4768 0.4863 0.5484 0.0525  -0.0805 -0.1091 359 ILE B CB  
4976  C CG1 . ILE B 295 ? 0.4943 0.5169 0.5845 0.0485  -0.0739 -0.1101 359 ILE B CG1 
4977  C CG2 . ILE B 295 ? 0.3675 0.3692 0.4279 0.0614  -0.0778 -0.1076 359 ILE B CG2 
4978  C CD1 . ILE B 295 ? 0.7390 0.7746 0.8437 0.0510  -0.0733 -0.1123 359 ILE B CD1 
4979  N N   . TYR B 296 ? 0.5576 0.5541 0.6236 0.0464  -0.0721 -0.1047 360 TYR B N   
4980  C CA  . TYR B 296 ? 0.5853 0.5723 0.6433 0.0474  -0.0682 -0.1024 360 TYR B CA  
4981  C C   . TYR B 296 ? 0.5494 0.5450 0.6196 0.0475  -0.0568 -0.1010 360 TYR B C   
4982  O O   . TYR B 296 ? 0.8724 0.8807 0.9604 0.0417  -0.0546 -0.1023 360 TYR B O   
4983  C CB  . TYR B 296 ? 0.7530 0.7353 0.8096 0.0407  -0.0735 -0.1016 360 TYR B CB  
4984  C CG  . TYR B 296 ? 1.2661 1.2371 1.3134 0.0417  -0.0720 -0.0995 360 TYR B CG  
4985  C CD1 . TYR B 296 ? 2.3048 2.2595 2.3349 0.0483  -0.0774 -0.0990 360 TYR B CD1 
4986  C CD2 . TYR B 296 ? 2.1253 2.1005 2.1799 0.0369  -0.0658 -0.0985 360 TYR B CD2 
4987  C CE1 . TYR B 296 ? 2.9785 2.9214 2.9983 0.0505  -0.0769 -0.0977 360 TYR B CE1 
4988  C CE2 . TYR B 296 ? 2.9062 2.8708 2.9515 0.0384  -0.0641 -0.0966 360 TYR B CE2 
4989  C CZ  . TYR B 296 ? 3.0339 2.9825 3.0616 0.0454  -0.0698 -0.0962 360 TYR B CZ  
4990  O OH  . TYR B 296 ? 2.8431 2.7803 2.8604 0.0479  -0.0691 -0.0948 360 TYR B OH  
4991  N N   . LYS B 297 ? 0.5084 0.4965 0.5693 0.0550  -0.0497 -0.0980 361 LYS B N   
4992  C CA  . LYS B 297 ? 0.4899 0.4865 0.5639 0.0577  -0.0370 -0.0945 361 LYS B CA  
4993  C C   . LYS B 297 ? 0.4952 0.4884 0.5701 0.0550  -0.0307 -0.0919 361 LYS B C   
4994  O O   . LYS B 297 ? 0.6598 0.6393 0.7169 0.0565  -0.0343 -0.0918 361 LYS B O   
4995  C CB  . LYS B 297 ? 0.4857 0.4755 0.5469 0.0707  -0.0311 -0.0912 361 LYS B CB  
4996  C CG  . LYS B 297 ? 0.5543 0.5538 0.6313 0.0758  -0.0163 -0.0853 361 LYS B CG  
4997  C CD  . LYS B 297 ? 0.5411 0.5316 0.6001 0.0909  -0.0112 -0.0818 361 LYS B CD  
4998  C CE  . LYS B 297 ? 0.5902 0.5848 0.6576 0.1002  0.0065  -0.0729 361 LYS B CE  
4999  N NZ  . LYS B 297 ? 0.7090 0.6925 0.7539 0.1171  0.0111  -0.0695 361 LYS B NZ  
5000  N N   . PHE B 298 ? 0.6351 0.6407 0.7324 0.0511  -0.0220 -0.0897 362 PHE B N   
5001  C CA  . PHE B 298 ? 0.6566 0.6602 0.7574 0.0482  -0.0150 -0.0868 362 PHE B CA  
5002  C C   . PHE B 298 ? 0.6673 0.6783 0.7851 0.0523  -0.0006 -0.0804 362 PHE B C   
5003  O O   . PHE B 298 ? 0.8527 0.8775 0.9939 0.0506  0.0019  -0.0797 362 PHE B O   
5004  C CB  . PHE B 298 ? 0.4482 0.4593 0.5636 0.0365  -0.0205 -0.0907 362 PHE B CB  
5005  C CG  . PHE B 298 ? 0.4375 0.4416 0.5387 0.0325  -0.0320 -0.0946 362 PHE B CG  
5006  C CD1 . PHE B 298 ? 0.5696 0.5627 0.6569 0.0315  -0.0335 -0.0935 362 PHE B CD1 
5007  C CD2 . PHE B 298 ? 0.4225 0.4316 0.5260 0.0301  -0.0409 -0.0986 362 PHE B CD2 
5008  C CE1 . PHE B 298 ? 0.9755 0.9635 1.0543 0.0277  -0.0435 -0.0955 362 PHE B CE1 
5009  C CE2 . PHE B 298 ? 0.6534 0.6569 0.7466 0.0270  -0.0500 -0.1003 362 PHE B CE2 
5010  C CZ  . PHE B 298 ? 0.7802 0.7737 0.8627 0.0255  -0.0511 -0.0983 362 PHE B CZ  
5011  N N   . LEU B 299 ? 0.8205 0.8227 0.9283 0.0582  0.0090  -0.0751 363 LEU B N   
5012  C CA  . LEU B 299 ? 0.9121 0.9220 1.0395 0.0618  0.0247  -0.0671 363 LEU B CA  
5013  C C   . LEU B 299 ? 1.0570 1.0774 1.2113 0.0493  0.0249  -0.0682 363 LEU B C   
5014  O O   . LEU B 299 ? 1.3609 1.3754 1.5069 0.0430  0.0195  -0.0717 363 LEU B O   
5015  C CB  . LEU B 299 ? 1.2618 1.2571 1.3665 0.0743  0.0355  -0.0605 363 LEU B CB  
5016  C CG  . LEU B 299 ? 1.6324 1.6184 1.7153 0.0904  0.0396  -0.0572 363 LEU B CG  
5017  C CD1 . LEU B 299 ? 1.2699 1.2717 1.3771 0.0917  0.0448  -0.0539 363 LEU B CD1 
5018  C CD2 . LEU B 299 ? 1.9550 1.9248 2.0057 0.0935  0.0241  -0.0648 363 LEU B CD2 
5019  N N   . GLY B 300 ? 0.7905 0.8262 0.9779 0.0459  0.0298  -0.0654 364 GLY B N   
5020  C CA  . GLY B 300 ? 1.0721 1.1171 1.2883 0.0348  0.0290  -0.0666 364 GLY B CA  
5021  C C   . GLY B 300 ? 0.7665 0.8141 0.9843 0.0243  0.0125  -0.0771 364 GLY B C   
5022  O O   . GLY B 300 ? 0.9317 0.9773 1.1343 0.0253  0.0027  -0.0825 364 GLY B O   
5023  N N   . THR B 301 ? 0.6368 0.6877 0.8719 0.0155  0.0099  -0.0796 365 THR B N   
5024  C CA  . THR B 301 ? 0.6093 0.6631 0.8490 0.0074  -0.0047 -0.0890 365 THR B CA  
5025  C C   . THR B 301 ? 0.5777 0.6211 0.7866 0.0066  -0.0135 -0.0942 365 THR B C   
5026  O O   . THR B 301 ? 0.6493 0.6827 0.8370 0.0095  -0.0093 -0.0913 365 THR B O   
5027  C CB  . THR B 301 ? 0.6456 0.7035 0.9113 -0.0007 -0.0059 -0.0905 365 THR B CB  
5028  O OG1 . THR B 301 ? 0.7457 0.8040 1.0113 -0.0060 -0.0210 -0.1003 365 THR B OG1 
5029  C CG2 . THR B 301 ? 0.7593 0.8084 1.0145 -0.0017 0.0017  -0.0869 365 THR B CG2 
5030  N N   . LEU B 302 ? 0.6330 0.6789 0.8412 0.0034  -0.0258 -0.1016 366 LEU B N   
5031  C CA  . LEU B 302 ? 0.6375 0.6756 0.8225 0.0024  -0.0338 -0.1054 366 LEU B CA  
5032  C C   . LEU B 302 ? 0.5997 0.6343 0.7862 -0.0029 -0.0351 -0.1073 366 LEU B C   
5033  O O   . LEU B 302 ? 1.0956 1.1237 1.2645 -0.0035 -0.0398 -0.1089 366 LEU B O   
5034  C CB  . LEU B 302 ? 0.6217 0.6640 0.8058 0.0029  -0.0450 -0.1115 366 LEU B CB  
5035  C CG  . LEU B 302 ? 0.7368 0.7829 0.9198 0.0082  -0.0450 -0.1103 366 LEU B CG  
5036  C CD1 . LEU B 302 ? 1.1044 1.1618 1.3134 0.0069  -0.0483 -0.1133 366 LEU B CD1 
5037  C CD2 . LEU B 302 ? 0.7834 0.8252 0.9467 0.0106  -0.0532 -0.1129 366 LEU B CD2 
5038  N N   . PHE B 303 ? 0.5783 0.6171 0.7870 -0.0064 -0.0306 -0.1064 367 PHE B N   
5039  C CA  . PHE B 303 ? 0.6631 0.6987 0.8764 -0.0115 -0.0335 -0.1096 367 PHE B CA  
5040  C C   . PHE B 303 ? 0.7120 0.7421 0.9236 -0.0128 -0.0230 -0.1038 367 PHE B C   
5041  O O   . PHE B 303 ? 1.0323 1.0592 1.2479 -0.0168 -0.0241 -0.1057 367 PHE B O   
5042  C CB  . PHE B 303 ? 0.5601 0.6025 0.8002 -0.0151 -0.0407 -0.1150 367 PHE B CB  
5043  C CG  . PHE B 303 ? 0.6868 0.7337 0.9268 -0.0127 -0.0518 -0.1210 367 PHE B CG  
5044  C CD1 . PHE B 303 ? 0.6801 0.7215 0.8955 -0.0099 -0.0601 -0.1255 367 PHE B CD1 
5045  C CD2 . PHE B 303 ? 0.7687 0.8254 1.0335 -0.0125 -0.0533 -0.1212 367 PHE B CD2 
5046  C CE1 . PHE B 303 ? 0.6084 0.6534 0.8221 -0.0065 -0.0697 -0.1306 367 PHE B CE1 
5047  C CE2 . PHE B 303 ? 0.7250 0.7857 0.9890 -0.0098 -0.0639 -0.1269 367 PHE B CE2 
5048  C CZ  . PHE B 303 ? 0.5601 0.6145 0.7973 -0.0065 -0.0721 -0.1319 367 PHE B CZ  
5049  N N   . SER B 304 ? 0.6215 0.6493 0.8246 -0.0082 -0.0133 -0.0971 368 SER B N   
5050  C CA  . SER B 304 ? 0.7688 0.7891 0.9622 -0.0071 -0.0042 -0.0917 368 SER B CA  
5051  C C   . SER B 304 ? 1.0109 1.0216 1.1748 -0.0040 -0.0075 -0.0915 368 SER B C   
5052  O O   . SER B 304 ? 0.8906 0.9002 1.0425 0.0000  -0.0116 -0.0921 368 SER B O   
5053  C CB  . SER B 304 ? 0.8272 0.8491 1.0298 -0.0020 0.0092  -0.0837 368 SER B CB  
5054  O OG  . SER B 304 ? 0.9923 1.0064 1.1863 -0.0003 0.0184  -0.0785 368 SER B OG  
5055  N N   . VAL B 305 ? 1.1122 1.1159 1.2663 -0.0059 -0.0061 -0.0904 369 VAL B N   
5056  C CA  . VAL B 305 ? 1.0392 1.0336 1.1696 -0.0034 -0.0094 -0.0891 369 VAL B CA  
5057  C C   . VAL B 305 ? 0.8057 0.7928 0.9232 0.0042  -0.0029 -0.0841 369 VAL B C   
5058  O O   . VAL B 305 ? 0.7806 0.7586 0.8790 0.0078  -0.0073 -0.0832 369 VAL B O   
5059  C CB  . VAL B 305 ? 0.8072 0.7971 0.9335 -0.0074 -0.0097 -0.0890 369 VAL B CB  
5060  C CG1 . VAL B 305 ? 1.0816 1.0688 1.2137 -0.0073 0.0008  -0.0850 369 VAL B CG1 
5061  C CG2 . VAL B 305 ? 1.2316 1.2138 1.3388 -0.0058 -0.0152 -0.0874 369 VAL B CG2 
5062  N N   . GLN B 306 ? 0.7461 0.7366 0.8751 0.0075  0.0071  -0.0804 370 GLN B N   
5063  C CA  . GLN B 306 ? 1.0046 0.9871 1.1206 0.0170  0.0159  -0.0747 370 GLN B CA  
5064  C C   . GLN B 306 ? 1.0419 1.0217 1.1454 0.0247  0.0126  -0.0751 370 GLN B C   
5065  O O   . GLN B 306 ? 1.0157 0.9845 1.0997 0.0345  0.0158  -0.0720 370 GLN B O   
5066  C CB  . GLN B 306 ? 1.3474 1.3358 1.4835 0.0187  0.0299  -0.0688 370 GLN B CB  
5067  C CG  . GLN B 306 ? 1.2302 1.2167 1.3735 0.0149  0.0366  -0.0661 370 GLN B CG  
5068  C CD  . GLN B 306 ? 1.2630 1.2362 1.3826 0.0233  0.0428  -0.0615 370 GLN B CD  
5069  O OE1 . GLN B 306 ? 1.3341 1.2981 1.4331 0.0233  0.0346  -0.0645 370 GLN B OE1 
5070  N NE2 . GLN B 306 ? 1.0193 0.9907 1.1418 0.0316  0.0573  -0.0535 370 GLN B NE2 
5071  N N   . THR B 307 ? 0.9709 0.9595 1.0845 0.0211  0.0057  -0.0792 371 THR B N   
5072  C CA  . THR B 307 ? 0.8932 0.8826 1.0026 0.0282  0.0056  -0.0786 371 THR B CA  
5073  C C   . THR B 307 ? 0.9819 0.9609 1.0677 0.0320  -0.0052 -0.0816 371 THR B C   
5074  O O   . THR B 307 ? 0.7454 0.7214 0.8255 0.0265  -0.0147 -0.0847 371 THR B O   
5075  C CB  . THR B 307 ? 0.9457 0.9499 1.0796 0.0237  0.0041  -0.0810 371 THR B CB  
5076  O OG1 . THR B 307 ? 1.1913 1.1995 1.3294 0.0151  -0.0070 -0.0872 371 THR B OG1 
5077  C CG2 . THR B 307 ? 0.8091 0.8223 0.9697 0.0215  0.0152  -0.0765 371 THR B CG2 
5078  N N   . VAL B 308 ? 1.1170 1.0904 1.1906 0.0420  -0.0033 -0.0798 372 VAL B N   
5079  C CA  . VAL B 308 ? 0.9956 0.9535 1.0430 0.0493  -0.0116 -0.0812 372 VAL B CA  
5080  C C   . VAL B 308 ? 1.1823 1.1425 1.2280 0.0509  -0.0194 -0.0844 372 VAL B C   
5081  O O   . VAL B 308 ? 1.8085 1.7768 1.8633 0.0548  -0.0132 -0.0829 372 VAL B O   
5082  C CB  . VAL B 308 ? 1.4901 1.4357 1.5193 0.0633  -0.0022 -0.0764 372 VAL B CB  
5083  C CG1 . VAL B 308 ? 1.6307 1.5564 1.6303 0.0723  -0.0128 -0.0788 372 VAL B CG1 
5084  C CG2 . VAL B 308 ? 1.7013 1.6463 1.7347 0.0628  0.0086  -0.0720 372 VAL B CG2 
5085  N N   . GLY B 309 ? 0.7039 0.6573 0.7398 0.0483  -0.0327 -0.0879 373 GLY B N   
5086  C CA  . GLY B 309 ? 0.6451 0.5960 0.6742 0.0522  -0.0406 -0.0903 373 GLY B CA  
5087  C C   . GLY B 309 ? 0.6743 0.6126 0.6837 0.0663  -0.0377 -0.0889 373 GLY B C   
5088  O O   . GLY B 309 ? 0.9395 0.8641 0.9319 0.0740  -0.0355 -0.0871 373 GLY B O   
5089  N N   . ASN B 310 ? 0.5854 0.5275 0.5953 0.0713  -0.0372 -0.0894 374 ASN B N   
5090  C CA  . ASN B 310 ? 0.6505 0.5813 0.6415 0.0863  -0.0319 -0.0871 374 ASN B CA  
5091  C C   . ASN B 310 ? 0.6407 0.5619 0.6176 0.0911  -0.0440 -0.0909 374 ASN B C   
5092  O O   . ASN B 310 ? 0.9431 0.8443 0.8948 0.1013  -0.0509 -0.0923 374 ASN B O   
5093  C CB  . ASN B 310 ? 0.6950 0.6398 0.7018 0.0905  -0.0155 -0.0817 374 ASN B CB  
5094  C CG  . ASN B 310 ? 1.0335 0.9673 1.0201 0.1084  -0.0087 -0.0782 374 ASN B CG  
5095  O OD1 . ASN B 310 ? 0.8919 0.8283 0.8779 0.1128  -0.0106 -0.0790 374 ASN B OD1 
5096  N ND2 . ASN B 310 ? 1.5877 1.5079 1.5553 0.1200  -0.0009 -0.0741 374 ASN B ND2 
5097  N N   . ARG B 311 ? 0.6315 0.5657 0.6238 0.0845  -0.0475 -0.0929 375 ARG B N   
5098  C CA  . ARG B 311 ? 0.8271 0.7535 0.8073 0.0905  -0.0564 -0.0955 375 ARG B CA  
5099  C C   . ARG B 311 ? 0.8312 0.7676 0.8265 0.0790  -0.0655 -0.0984 375 ARG B C   
5100  O O   . ARG B 311 ? 1.1573 1.1114 1.1737 0.0709  -0.0608 -0.0981 375 ARG B O   
5101  C CB  . ARG B 311 ? 0.7126 0.6435 0.6913 0.1014  -0.0463 -0.0929 375 ARG B CB  
5102  C CG  . ARG B 311 ? 0.6061 0.5289 0.5716 0.1084  -0.0550 -0.0957 375 ARG B CG  
5103  C CD  . ARG B 311 ? 0.6933 0.5896 0.6269 0.1207  -0.0633 -0.0976 375 ARG B CD  
5104  N NE  . ARG B 311 ? 0.8491 0.7345 0.7685 0.1279  -0.0734 -0.1008 375 ARG B NE  
5105  C CZ  . ARG B 311 ? 1.2780 1.1601 1.1854 0.1415  -0.0667 -0.0991 375 ARG B CZ  
5106  N NH1 . ARG B 311 ? 1.6714 1.5611 1.5813 0.1494  -0.0493 -0.0932 375 ARG B NH1 
5107  N NH2 . ARG B 311 ? 1.7187 1.5899 1.6127 0.1477  -0.0769 -0.1025 375 ARG B NH2 
5108  N N   . ASN B 312 ? 0.7749 0.6988 0.7595 0.0793  -0.0791 -0.1008 376 ASN B N   
5109  C CA  . ASN B 312 ? 0.6345 0.5662 0.6315 0.0708  -0.0870 -0.1021 376 ASN B CA  
5110  C C   . ASN B 312 ? 0.5780 0.5044 0.5668 0.0773  -0.0933 -0.1038 376 ASN B C   
5111  O O   . ASN B 312 ? 0.6669 0.5744 0.6377 0.0846  -0.1024 -0.1052 376 ASN B O   
5112  C CB  . ASN B 312 ? 0.7353 0.6583 0.7326 0.0642  -0.0974 -0.1016 376 ASN B CB  
5113  C CG  . ASN B 312 ? 0.7612 0.6871 0.7673 0.0589  -0.1065 -0.1012 376 ASN B CG  
5114  O OD1 . ASN B 312 ? 1.0766 0.9899 1.0743 0.0629  -0.1167 -0.1020 376 ASN B OD1 
5115  N ND2 . ASN B 312 ? 0.8703 0.8114 0.8926 0.0507  -0.1028 -0.0999 376 ASN B ND2 
5116  N N   . TYR B 313 ? 0.5659 0.5078 0.5676 0.0749  -0.0896 -0.1042 377 TYR B N   
5117  C CA  . TYR B 313 ? 0.5576 0.4970 0.5540 0.0800  -0.0951 -0.1057 377 TYR B CA  
5118  C C   . TYR B 313 ? 0.5714 0.5136 0.5767 0.0722  -0.1042 -0.1057 377 TYR B C   
5119  O O   . TYR B 313 ? 0.7361 0.6933 0.7571 0.0647  -0.1011 -0.1052 377 TYR B O   
5120  C CB  . TYR B 313 ? 0.4996 0.4549 0.5062 0.0829  -0.0855 -0.1056 377 TYR B CB  
5121  C CG  . TYR B 313 ? 0.6308 0.5844 0.6306 0.0928  -0.0747 -0.1034 377 TYR B CG  
5122  C CD1 . TYR B 313 ? 0.7097 0.6761 0.7248 0.0900  -0.0629 -0.1007 377 TYR B CD1 
5123  C CD2 . TYR B 313 ? 0.7826 0.7218 0.7616 0.1059  -0.0756 -0.1033 377 TYR B CD2 
5124  C CE1 . TYR B 313 ? 0.9131 0.8793 0.9249 0.1000  -0.0507 -0.0965 377 TYR B CE1 
5125  C CE2 . TYR B 313 ? 0.9965 0.9342 0.9685 0.1172  -0.0635 -0.0997 377 TYR B CE2 
5126  C CZ  . TYR B 313 ? 1.0017 0.9536 0.9912 0.1141  -0.0503 -0.0956 377 TYR B CZ  
5127  O OH  . TYR B 313 ? 1.3634 1.3146 1.3485 0.1261  -0.0364 -0.0900 377 TYR B OH  
5128  N N   . GLN B 314 ? 0.6132 0.5404 0.6087 0.0750  -0.1155 -0.1060 378 GLN B N   
5129  C CA  . GLN B 314 ? 0.6960 0.6256 0.7009 0.0695  -0.1229 -0.1043 378 GLN B CA  
5130  C C   . GLN B 314 ? 0.6352 0.5698 0.6392 0.0741  -0.1231 -0.1057 378 GLN B C   
5131  O O   . GLN B 314 ? 1.0124 0.9335 1.0046 0.0807  -0.1302 -0.1068 378 GLN B O   
5132  C CB  . GLN B 314 ? 0.7486 0.6597 0.7488 0.0690  -0.1356 -0.1027 378 GLN B CB  
5133  C CG  . GLN B 314 ? 1.6882 1.5977 1.6946 0.0624  -0.1358 -0.1003 378 GLN B CG  
5134  C CD  . GLN B 314 ? 2.3704 2.2695 2.3849 0.0578  -0.1476 -0.0962 378 GLN B CD  
5135  O OE1 . GLN B 314 ? 2.6641 2.5578 2.6810 0.0592  -0.1556 -0.0948 378 GLN B OE1 
5136  N NE2 . GLN B 314 ? 2.4203 2.3165 2.4407 0.0530  -0.1496 -0.0937 378 GLN B NE2 
5137  N N   . LEU B 315 ? 0.5363 0.4891 0.5522 0.0713  -0.1165 -0.1061 379 LEU B N   
5138  C CA  . LEU B 315 ? 0.5504 0.5095 0.5658 0.0766  -0.1158 -0.1078 379 LEU B CA  
5139  C C   . LEU B 315 ? 0.6776 0.6318 0.6927 0.0764  -0.1243 -0.1061 379 LEU B C   
5140  O O   . LEU B 315 ? 0.6091 0.5570 0.6160 0.0830  -0.1281 -0.1072 379 LEU B O   
5141  C CB  . LEU B 315 ? 0.4603 0.4397 0.4899 0.0740  -0.1079 -0.1093 379 LEU B CB  
5142  C CG  . LEU B 315 ? 0.5089 0.4947 0.5432 0.0748  -0.0985 -0.1099 379 LEU B CG  
5143  C CD1 . LEU B 315 ? 0.5789 0.5845 0.6317 0.0718  -0.0934 -0.1117 379 LEU B CD1 
5144  C CD2 . LEU B 315 ? 0.5031 0.4798 0.5243 0.0849  -0.0956 -0.1096 379 LEU B CD2 
5145  N N   . LEU B 316 ? 0.7389 0.6960 0.7633 0.0697  -0.1265 -0.1026 380 LEU B N   
5146  C CA  . LEU B 316 ? 0.6491 0.6028 0.6762 0.0699  -0.1326 -0.0990 380 LEU B CA  
5147  C C   . LEU B 316 ? 0.6411 0.5845 0.6737 0.0648  -0.1384 -0.0934 380 LEU B C   
5148  O O   . LEU B 316 ? 0.7321 0.6786 0.7704 0.0595  -0.1352 -0.0916 380 LEU B O   
5149  C CB  . LEU B 316 ? 0.8501 0.8195 0.8852 0.0689  -0.1281 -0.0984 380 LEU B CB  
5150  C CG  . LEU B 316 ? 0.9635 0.9458 0.9986 0.0730  -0.1237 -0.1037 380 LEU B CG  
5151  C CD1 . LEU B 316 ? 1.2619 1.2536 1.3013 0.0741  -0.1236 -0.1027 380 LEU B CD1 
5152  C CD2 . LEU B 316 ? 0.8260 0.8019 0.8519 0.0800  -0.1259 -0.1062 380 LEU B CD2 
5153  N N   . SER B 317 ? 0.7260 0.6571 0.7585 0.0665  -0.1471 -0.0901 381 SER B N   
5154  C CA  . SER B 317 ? 0.6712 0.5910 0.7132 0.0619  -0.1546 -0.0838 381 SER B CA  
5155  C C   . SER B 317 ? 0.7312 0.6524 0.7855 0.0609  -0.1564 -0.0758 381 SER B C   
5156  O O   . SER B 317 ? 0.7640 0.6889 0.8321 0.0563  -0.1543 -0.0681 381 SER B O   
5157  C CB  . SER B 317 ? 0.7821 0.6812 0.8149 0.0652  -0.1663 -0.0868 381 SER B CB  
5158  O OG  . SER B 317 ? 1.7053 1.6019 1.7233 0.0688  -0.1632 -0.0936 381 SER B OG  
5159  N N   . ASN B 318 ? 0.8766 0.7950 0.9260 0.0662  -0.1594 -0.0768 382 ASN B N   
5160  C CA  . ASN B 318 ? 0.9484 0.8659 1.0090 0.0667  -0.1614 -0.0685 382 ASN B CA  
5161  C C   . ASN B 318 ? 0.8815 0.8153 0.9449 0.0686  -0.1512 -0.0647 382 ASN B C   
5162  O O   . ASN B 318 ? 1.1278 1.0610 1.1996 0.0703  -0.1510 -0.0566 382 ASN B O   
5163  C CB  . ASN B 318 ? 1.4200 1.3248 1.4732 0.0721  -0.1701 -0.0710 382 ASN B CB  
5164  C CG  . ASN B 318 ? 1.4994 1.3863 1.5642 0.0697  -0.1826 -0.0654 382 ASN B CG  
5165  O OD1 . ASN B 318 ? 1.6911 1.5779 1.7738 0.0638  -0.1834 -0.0571 382 ASN B OD1 
5166  N ND2 . ASN B 318 ? 1.9291 1.8003 1.9851 0.0746  -0.1931 -0.0695 382 ASN B ND2 
5167  N N   . SER B 319 ? 0.8959 0.8431 0.9526 0.0690  -0.1432 -0.0704 383 SER B N   
5168  C CA  . SER B 319 ? 0.8679 0.8286 0.9227 0.0731  -0.1358 -0.0698 383 SER B CA  
5169  C C   . SER B 319 ? 0.7609 0.7301 0.8211 0.0707  -0.1287 -0.0654 383 SER B C   
5170  O O   . SER B 319 ? 0.8722 0.8429 0.9340 0.0658  -0.1270 -0.0678 383 SER B O   
5171  C CB  . SER B 319 ? 0.7314 0.7006 0.7755 0.0771  -0.1341 -0.0801 383 SER B CB  
5172  O OG  . SER B 319 ? 1.2008 1.1611 1.2386 0.0781  -0.1392 -0.0852 383 SER B OG  
5173  N N   . THR B 320 ? 0.6361 0.6098 0.6976 0.0755  -0.1241 -0.0587 384 THR B N   
5174  C CA  . THR B 320 ? 0.6715 0.6522 0.7341 0.0762  -0.1168 -0.0545 384 THR B CA  
5175  C C   . THR B 320 ? 0.6916 0.6826 0.7435 0.0789  -0.1142 -0.0650 384 THR B C   
5176  O O   . THR B 320 ? 0.9023 0.8982 0.9459 0.0856  -0.1147 -0.0696 384 THR B O   
5177  C CB  . THR B 320 ? 0.8406 0.8208 0.9067 0.0827  -0.1119 -0.0422 384 THR B CB  
5178  O OG1 . THR B 320 ? 1.0227 0.9937 1.1044 0.0789  -0.1151 -0.0318 384 THR B OG1 
5179  C CG2 . THR B 320 ? 0.7740 0.7597 0.8386 0.0855  -0.1036 -0.0372 384 THR B CG2 
5180  N N   . ILE B 321 ? 0.5208 0.5145 0.5743 0.0736  -0.1123 -0.0685 385 ILE B N   
5181  C CA  . ILE B 321 ? 0.4998 0.5019 0.5478 0.0739  -0.1115 -0.0788 385 ILE B CA  
5182  C C   . ILE B 321 ? 0.6638 0.6704 0.7069 0.0781  -0.1073 -0.0781 385 ILE B C   
5183  O O   . ILE B 321 ? 0.6730 0.6765 0.7173 0.0796  -0.1027 -0.0686 385 ILE B O   
5184  C CB  . ILE B 321 ? 0.4824 0.4841 0.5349 0.0662  -0.1121 -0.0839 385 ILE B CB  
5185  C CG1 . ILE B 321 ? 0.5840 0.5781 0.6375 0.0642  -0.1166 -0.0844 385 ILE B CG1 
5186  C CG2 . ILE B 321 ? 0.4138 0.4244 0.4651 0.0662  -0.1118 -0.0939 385 ILE B CG2 
5187  C CD1 . ILE B 321 ? 0.4296 0.4271 0.4784 0.0686  -0.1190 -0.0909 385 ILE B CD1 
5188  N N   . GLY B 322 ? 0.6476 0.6610 0.6858 0.0807  -0.1093 -0.0882 386 GLY B N   
5189  C CA  . GLY B 322 ? 0.5802 0.5961 0.6106 0.0864  -0.1082 -0.0907 386 GLY B CA  
5190  C C   . GLY B 322 ? 0.6863 0.7080 0.7203 0.0825  -0.1115 -0.1019 386 GLY B C   
5191  O O   . GLY B 322 ? 0.7667 0.7888 0.8086 0.0742  -0.1095 -0.1030 386 GLY B O   
5192  N N   . ARG B 323 ? 0.5637 0.5896 0.5933 0.0887  -0.1169 -0.1102 387 ARG B N   
5193  C CA  . ARG B 323 ? 0.6167 0.6479 0.6535 0.0850  -0.1209 -0.1202 387 ARG B CA  
5194  C C   . ARG B 323 ? 0.5244 0.5616 0.5757 0.0777  -0.1216 -0.1239 387 ARG B C   
5195  O O   . ARG B 323 ? 0.3809 0.4180 0.4323 0.0785  -0.1214 -0.1214 387 ARG B O   
5196  C CB  . ARG B 323 ? 0.7311 0.7636 0.7601 0.0945  -0.1288 -0.1284 387 ARG B CB  
5197  C CG  . ARG B 323 ? 0.5455 0.5701 0.5552 0.1054  -0.1276 -0.1246 387 ARG B CG  
5198  C CD  . ARG B 323 ? 0.4898 0.5132 0.4873 0.1178  -0.1360 -0.1315 387 ARG B CD  
5199  N NE  . ARG B 323 ? 0.7621 0.7905 0.7700 0.1155  -0.1465 -0.1445 387 ARG B NE  
5200  C CZ  . ARG B 323 ? 0.6987 0.7346 0.7185 0.1142  -0.1536 -0.1512 387 ARG B CZ  
5201  N NH1 . ARG B 323 ? 0.4972 0.5360 0.5170 0.1155  -0.1511 -0.1469 387 ARG B NH1 
5202  N NH2 . ARG B 323 ? 0.5809 0.6214 0.6144 0.1118  -0.1634 -0.1620 387 ARG B NH2 
5203  N N   . SER B 324 ? 0.4720 0.5135 0.5351 0.0714  -0.1219 -0.1291 388 SER B N   
5204  C CA  . SER B 324 ? 0.5079 0.5560 0.5861 0.0659  -0.1210 -0.1319 388 SER B CA  
5205  C C   . SER B 324 ? 0.4857 0.5405 0.5779 0.0637  -0.1251 -0.1397 388 SER B C   
5206  O O   . SER B 324 ? 0.4905 0.5422 0.5797 0.0634  -0.1267 -0.1418 388 SER B O   
5207  C CB  . SER B 324 ? 0.4615 0.5053 0.5417 0.0591  -0.1139 -0.1263 388 SER B CB  
5208  O OG  . SER B 324 ? 0.7189 0.7566 0.7927 0.0570  -0.1111 -0.1223 388 SER B OG  
5209  N N   . GLY B 325 ? 0.4263 0.4898 0.5349 0.0626  -0.1271 -0.1436 389 GLY B N   
5210  C CA  . GLY B 325 ? 0.3745 0.4450 0.5017 0.0604  -0.1328 -0.1507 389 GLY B CA  
5211  C C   . GLY B 325 ? 0.4021 0.4827 0.5522 0.0572  -0.1298 -0.1503 389 GLY B C   
5212  O O   . GLY B 325 ? 0.4406 0.5226 0.5885 0.0591  -0.1253 -0.1463 389 GLY B O   
5213  N N   . LEU B 326 ? 0.4197 0.5069 0.5928 0.0528  -0.1320 -0.1538 390 LEU B N   
5214  C CA  . LEU B 326 ? 0.4041 0.5022 0.6032 0.0505  -0.1281 -0.1518 390 LEU B CA  
5215  C C   . LEU B 326 ? 0.4307 0.5380 0.6472 0.0543  -0.1386 -0.1575 390 LEU B C   
5216  O O   . LEU B 326 ? 0.5047 0.6090 0.7128 0.0587  -0.1505 -0.1646 390 LEU B O   
5217  C CB  . LEU B 326 ? 0.4136 0.5148 0.6339 0.0434  -0.1242 -0.1510 390 LEU B CB  
5218  C CG  . LEU B 326 ? 0.4846 0.5774 0.6911 0.0394  -0.1141 -0.1456 390 LEU B CG  
5219  C CD1 . LEU B 326 ? 0.7950 0.8885 1.0181 0.0334  -0.1156 -0.1481 390 LEU B CD1 
5220  C CD2 . LEU B 326 ? 0.5395 0.6340 0.7485 0.0396  -0.1017 -0.1376 390 LEU B CD2 
5221  N N   . TYR B 327 ? 0.4675 0.5857 0.7078 0.0537  -0.1337 -0.1539 391 TYR B N   
5222  C CA  . TYR B 327 ? 0.5771 0.7067 0.8443 0.0555  -0.1433 -0.1583 391 TYR B CA  
5223  C C   . TYR B 327 ? 0.5989 0.7406 0.8967 0.0534  -0.1332 -0.1507 391 TYR B C   
5224  O O   . TYR B 327 ? 0.6596 0.7996 0.9478 0.0546  -0.1194 -0.1426 391 TYR B O   
5225  C CB  . TYR B 327 ? 0.4393 0.5687 0.6917 0.0637  -0.1513 -0.1620 391 TYR B CB  
5226  C CG  . TYR B 327 ? 0.5515 0.6815 0.7914 0.0682  -0.1414 -0.1550 391 TYR B CG  
5227  C CD1 . TYR B 327 ? 0.5362 0.6779 0.7973 0.0710  -0.1385 -0.1516 391 TYR B CD1 
5228  C CD2 . TYR B 327 ? 0.6385 0.7566 0.8458 0.0703  -0.1357 -0.1517 391 TYR B CD2 
5229  C CE1 . TYR B 327 ? 0.5383 0.6783 0.7845 0.0766  -0.1301 -0.1459 391 TYR B CE1 
5230  C CE2 . TYR B 327 ? 0.6242 0.7403 0.8191 0.0749  -0.1287 -0.1463 391 TYR B CE2 
5231  C CZ  . TYR B 327 ? 0.5982 0.7246 0.8105 0.0785  -0.1261 -0.1439 391 TYR B CZ  
5232  O OH  . TYR B 327 ? 0.6390 0.7613 0.8357 0.0841  -0.1196 -0.1390 391 TYR B OH  
5233  N N   . GLN B 328 ? 0.5935 0.7468 0.9284 0.0511  -0.1404 -0.1530 392 GLN B N   
5234  C CA  . GLN B 328 ? 0.5392 0.7057 0.9083 0.0500  -0.1297 -0.1439 392 GLN B CA  
5235  C C   . GLN B 328 ? 0.5548 0.7327 0.9425 0.0551  -0.1366 -0.1450 392 GLN B C   
5236  O O   . GLN B 328 ? 0.9376 1.1194 1.3428 0.0546  -0.1535 -0.1535 392 GLN B O   
5237  C CB  . GLN B 328 ? 0.6998 0.8723 1.1056 0.0422  -0.1298 -0.1425 392 GLN B CB  
5238  C CG  . GLN B 328 ? 0.8368 0.9980 1.2249 0.0371  -0.1241 -0.1421 392 GLN B CG  
5239  C CD  . GLN B 328 ? 0.8164 0.9826 1.2408 0.0296  -0.1249 -0.1409 392 GLN B CD  
5240  O OE1 . GLN B 328 ? 0.8133 0.9782 1.2514 0.0263  -0.1412 -0.1501 392 GLN B OE1 
5241  N NE2 . GLN B 328 ? 0.8172 0.9876 1.2562 0.0277  -0.1075 -0.1296 392 GLN B NE2 
5242  N N   . PRO B 329 ? 0.4611 0.6429 0.8431 0.0609  -0.1245 -0.1370 393 PRO B N   
5243  C CA  . PRO B 329 ? 0.4784 0.6731 0.8828 0.0661  -0.1277 -0.1354 393 PRO B CA  
5244  C C   . PRO B 329 ? 0.5810 0.7919 1.0384 0.0623  -0.1239 -0.1285 393 PRO B C   
5245  O O   . PRO B 329 ? 0.5595 0.7713 1.0293 0.0584  -0.1110 -0.1205 393 PRO B O   
5246  C CB  . PRO B 329 ? 0.3999 0.5908 0.7782 0.0738  -0.1134 -0.1277 393 PRO B CB  
5247  C CG  . PRO B 329 ? 0.3605 0.5402 0.7166 0.0719  -0.1006 -0.1227 393 PRO B CG  
5248  C CD  . PRO B 329 ? 0.3717 0.5434 0.7207 0.0643  -0.1095 -0.1302 393 PRO B CD  
5249  N N   . ALA B 330 ? 0.7227 0.9464 1.2127 0.0636  -0.1353 -0.1309 394 ALA B N   
5250  C CA  . ALA B 330 ? 0.8481 1.0885 1.3953 0.0596  -0.1336 -0.1238 394 ALA B CA  
5251  C C   . ALA B 330 ? 0.9003 1.1559 1.4713 0.0666  -0.1248 -0.1138 394 ALA B C   
5252  O O   . ALA B 330 ? 0.9432 1.2014 1.5080 0.0720  -0.1352 -0.1192 394 ALA B O   
5253  C CB  . ALA B 330 ? 0.8850 1.1277 1.4605 0.0537  -0.1574 -0.1354 394 ALA B CB  
5254  N N   . TYR B 331 ? 1.4858 1.7506 2.0820 0.0677  -0.1045 -0.0984 395 TYR B N   
5255  C CA  . TYR B 331 ? 1.9185 2.2000 2.5465 0.0749  -0.0936 -0.0859 395 TYR B CA  
5256  C C   . TYR B 331 ? 2.2514 2.5469 2.9330 0.0712  -0.0804 -0.0714 395 TYR B C   
5257  O O   . TYR B 331 ? 2.3286 2.6196 3.0189 0.0632  -0.0799 -0.0718 395 TYR B O   
5258  C CB  . TYR B 331 ? 1.8702 2.1451 2.4577 0.0866  -0.0753 -0.0782 395 TYR B CB  
5259  C CG  . TYR B 331 ? 1.9911 2.2463 2.5174 0.0889  -0.0815 -0.0893 395 TYR B CG  
5260  C CD1 . TYR B 331 ? 1.7079 1.9608 2.2163 0.0919  -0.0973 -0.0998 395 TYR B CD1 
5261  C CD2 . TYR B 331 ? 1.9615 2.2004 2.4497 0.0884  -0.0716 -0.0885 395 TYR B CD2 
5262  C CE1 . TYR B 331 ? 1.8559 2.0912 2.3118 0.0941  -0.1020 -0.1083 395 TYR B CE1 
5263  C CE2 . TYR B 331 ? 1.9335 2.1550 2.3707 0.0900  -0.0775 -0.0974 395 TYR B CE2 
5264  C CZ  . TYR B 331 ? 2.2151 2.4352 2.6375 0.0928  -0.0921 -0.1066 395 TYR B CZ  
5265  O OH  . TYR B 331 ? 2.2308 2.4342 2.6063 0.0946  -0.0969 -0.1137 395 TYR B OH  
5266  N N   . GLU B 332 ? 2.3324 2.6450 3.0508 0.0776  -0.0691 -0.0578 396 GLU B N   
5267  C CA  . GLU B 332 ? 2.5484 2.8746 3.3157 0.0772  -0.0508 -0.0398 396 GLU B CA  
5268  C C   . GLU B 332 ? 2.7781 3.0914 3.5081 0.0823  -0.0273 -0.0308 396 GLU B C   
5269  O O   . GLU B 332 ? 3.0522 3.3648 3.7998 0.0765  -0.0197 -0.0251 396 GLU B O   
5270  C CB  . GLU B 332 ? 2.3177 2.6639 3.1256 0.0858  -0.0406 -0.0253 396 GLU B CB  
5271  C CG  . GLU B 332 ? 2.3213 2.6848 3.1906 0.0857  -0.0219 -0.0045 396 GLU B CG  
5272  C CD  . GLU B 332 ? 2.2450 2.6022 3.0889 0.0965  0.0095  0.0121  396 GLU B CD  
5273  O OE1 . GLU B 332 ? 2.3869 2.7374 3.1891 0.1099  0.0217  0.0156  396 GLU B OE1 
5274  O OE2 . GLU B 332 ? 1.9358 2.2935 2.8004 0.0925  0.0213  0.0214  396 GLU B OE2 
5275  N N   . SER B 333 ? 2.4927 2.7946 3.1706 0.0934  -0.0175 -0.0304 397 SER B N   
5276  C CA  . SER B 333 ? 2.3309 2.6178 2.9671 0.1008  0.0027  -0.0232 397 SER B CA  
5277  C C   . SER B 333 ? 2.3083 2.6041 2.9822 0.1020  0.0236  -0.0053 397 SER B C   
5278  O O   . SER B 333 ? 2.3756 2.6863 3.0839 0.1106  0.0393  0.0110  397 SER B O   
5279  C CB  . SER B 333 ? 2.3440 2.6102 2.9320 0.0937  -0.0085 -0.0382 397 SER B CB  
5280  O OG  . SER B 333 ? 2.4908 2.7477 3.0409 0.0950  -0.0238 -0.0518 397 SER B OG  
5281  N N   . ARG B 334 ? 2.0149 2.3019 2.6836 0.0939  0.0243  -0.0076 398 ARG B N   
5282  C CA  . ARG B 334 ? 2.1462 2.4416 2.8549 0.0931  0.0420  0.0085  398 ARG B CA  
5283  C C   . ARG B 334 ? 1.7930 2.0821 2.5090 0.0786  0.0310  -0.0002 398 ARG B C   
5284  O O   . ARG B 334 ? 1.3950 1.6764 2.0938 0.0691  0.0082  -0.0184 398 ARG B O   
5285  C CB  . ARG B 334 ? 2.4889 2.7759 3.1683 0.1091  0.0705  0.0243  398 ARG B CB  
5286  C CG  . ARG B 334 ? 2.3718 2.6337 2.9777 0.1148  0.0707  0.0148  398 ARG B CG  
5287  C CD  . ARG B 334 ? 2.4444 2.6968 3.0258 0.1312  0.0978  0.0306  398 ARG B CD  
5288  N NE  . ARG B 334 ? 2.4875 2.7532 3.0941 0.1460  0.1169  0.0488  398 ARG B NE  
5289  C CZ  . ARG B 334 ? 2.1925 2.4519 2.7813 0.1643  0.1424  0.0651  398 ARG B CZ  
5290  N NH1 . ARG B 334 ? 2.0285 2.2674 2.5730 0.1701  0.1507  0.0647  398 ARG B NH1 
5291  N NH2 . ARG B 334 ? 2.3288 2.6015 2.9431 0.1781  0.1594  0.0820  398 ARG B NH2 
5292  N N   . ASP B 335 ? 1.9572 2.2493 2.6985 0.0780  0.0479  0.0134  399 ASP B N   
5293  C CA  . ASP B 335 ? 2.1467 2.4323 2.8957 0.0653  0.0407  0.0073  399 ASP B CA  
5294  C C   . ASP B 335 ? 1.7960 2.0603 2.4841 0.0610  0.0267  -0.0112 399 ASP B C   
5295  O O   . ASP B 335 ? 1.6294 1.8879 2.3198 0.0492  0.0121  -0.0221 399 ASP B O   
5296  C CB  . ASP B 335 ? 2.2870 2.5730 3.0499 0.0704  0.0668  0.0260  399 ASP B CB  
5297  C CG  . ASP B 335 ? 2.2495 2.5576 3.0818 0.0730  0.0810  0.0461  399 ASP B CG  
5298  O OD1 . ASP B 335 ? 2.1111 2.4349 2.9891 0.0670  0.0665  0.0438  399 ASP B OD1 
5299  O OD2 . ASP B 335 ? 2.8664 3.1760 3.7086 0.0816  0.1069  0.0650  399 ASP B OD2 
5300  N N   . CYS B 336 ? 1.3720 1.6248 2.0073 0.0713  0.0313  -0.0138 400 CYS B N   
5301  C CA  . CYS B 336 ? 0.9020 1.1347 1.4787 0.0699  0.0218  -0.0279 400 CYS B CA  
5302  C C   . CYS B 336 ? 0.8403 1.0712 1.4068 0.0623  -0.0042 -0.0461 400 CYS B C   
5303  O O   . CYS B 336 ? 0.8893 1.1273 1.4596 0.0664  -0.0110 -0.0485 400 CYS B O   
5304  C CB  . CYS B 336 ? 1.2981 1.5196 1.8283 0.0850  0.0360  -0.0225 400 CYS B CB  
5305  S SG  . CYS B 336 ? 2.2798 2.4761 2.7481 0.0866  0.0379  -0.0290 400 CYS B SG  
5306  N N   . GLN B 337 ? 0.8592 1.0799 1.4104 0.0526  -0.0180 -0.0583 401 GLN B N   
5307  C CA  . GLN B 337 ? 0.9018 1.1165 1.4316 0.0481  -0.0407 -0.0752 401 GLN B CA  
5308  C C   . GLN B 337 ? 0.8977 1.0952 1.3678 0.0533  -0.0410 -0.0814 401 GLN B C   
5309  O O   . GLN B 337 ? 0.7472 0.9314 1.1889 0.0514  -0.0372 -0.0829 401 GLN B O   
5310  C CB  . GLN B 337 ? 0.8724 1.0844 1.4168 0.0365  -0.0569 -0.0855 401 GLN B CB  
5311  C CG  . GLN B 337 ? 0.9471 1.1520 1.4691 0.0341  -0.0799 -0.1022 401 GLN B CG  
5312  C CD  . GLN B 337 ? 0.9091 1.1223 1.4359 0.0399  -0.0880 -0.1049 401 GLN B CD  
5313  O OE1 . GLN B 337 ? 1.4503 1.6790 2.0209 0.0402  -0.0889 -0.0997 401 GLN B OE1 
5314  N NE2 . GLN B 337 ? 0.9110 1.1141 1.3946 0.0447  -0.0938 -0.1123 401 GLN B NE2 
5315  N N   . GLU B 338 ? 0.8787 1.0767 1.3325 0.0597  -0.0465 -0.0849 402 GLU B N   
5316  C CA  . GLU B 338 ? 0.8373 1.0195 1.2392 0.0647  -0.0479 -0.0901 402 GLU B CA  
5317  C C   . GLU B 338 ? 0.6391 0.8100 1.0171 0.0574  -0.0633 -0.1027 402 GLU B C   
5318  O O   . GLU B 338 ? 0.6721 0.8478 1.0695 0.0510  -0.0774 -0.1105 402 GLU B O   
5319  C CB  . GLU B 338 ? 1.0192 1.2054 1.4134 0.0731  -0.0507 -0.0906 402 GLU B CB  
5320  C CG  . GLU B 338 ? 1.4143 1.5840 1.7581 0.0797  -0.0503 -0.0935 402 GLU B CG  
5321  C CD  . GLU B 338 ? 1.8037 1.9688 2.1320 0.0915  -0.0332 -0.0829 402 GLU B CD  
5322  O OE1 . GLU B 338 ? 2.2032 2.3810 2.5580 0.0977  -0.0237 -0.0739 402 GLU B OE1 
5323  O OE2 . GLU B 338 ? 1.4628 1.6108 1.7522 0.0955  -0.0300 -0.0834 402 GLU B OE2 
5324  N N   . LEU B 339 ? 0.5683 0.7235 0.9050 0.0593  -0.0605 -0.1043 403 LEU B N   
5325  C CA  . LEU B 339 ? 0.5048 0.6486 0.8166 0.0540  -0.0722 -0.1139 403 LEU B CA  
5326  C C   . LEU B 339 ? 0.5298 0.6607 0.8006 0.0593  -0.0744 -0.1163 403 LEU B C   
5327  O O   . LEU B 339 ? 0.8321 0.9545 1.0826 0.0644  -0.0645 -0.1106 403 LEU B O   
5328  C CB  . LEU B 339 ? 0.4535 0.5909 0.7641 0.0478  -0.0668 -0.1122 403 LEU B CB  
5329  C CG  . LEU B 339 ? 0.4525 0.5792 0.7411 0.0426  -0.0775 -0.1207 403 LEU B CG  
5330  C CD1 . LEU B 339 ? 0.5120 0.6442 0.8154 0.0395  -0.0937 -0.1300 403 LEU B CD1 
5331  C CD2 . LEU B 339 ? 0.3906 0.5122 0.6805 0.0371  -0.0710 -0.1182 403 LEU B CD2 
5332  N N   . CYS B 340 ? 0.5138 0.6423 0.7728 0.0589  -0.0878 -0.1245 404 CYS B N   
5333  C CA  . CYS B 340 ? 0.4720 0.5898 0.6977 0.0640  -0.0907 -0.1260 404 CYS B CA  
5334  C C   . CYS B 340 ? 0.4911 0.6002 0.6990 0.0601  -0.1001 -0.1323 404 CYS B C   
5335  O O   . CYS B 340 ? 0.5945 0.7066 0.8148 0.0553  -0.1067 -0.1371 404 CYS B O   
5336  C CB  . CYS B 340 ? 0.4336 0.5582 0.6628 0.0702  -0.0961 -0.1278 404 CYS B CB  
5337  S SG  . CYS B 340 ? 0.9122 1.0486 1.1649 0.0762  -0.0846 -0.1194 404 CYS B SG  
5338  N N   . PHE B 341 ? 0.3890 0.4866 0.5684 0.0629  -0.1008 -0.1317 405 PHE B N   
5339  C CA  . PHE B 341 ? 0.5090 0.5995 0.6728 0.0612  -0.1088 -0.1360 405 PHE B CA  
5340  C C   . PHE B 341 ? 0.5210 0.6045 0.6628 0.0669  -0.1126 -0.1357 405 PHE B C   
5341  O O   . PHE B 341 ? 0.7521 0.8324 0.8862 0.0709  -0.1085 -0.1320 405 PHE B O   
5342  C CB  . PHE B 341 ? 0.5446 0.6263 0.6993 0.0558  -0.1043 -0.1337 405 PHE B CB  
5343  C CG  . PHE B 341 ? 0.6429 0.7135 0.7787 0.0572  -0.0978 -0.1279 405 PHE B CG  
5344  C CD1 . PHE B 341 ? 0.7775 0.8470 0.9166 0.0579  -0.0886 -0.1232 405 PHE B CD1 
5345  C CD2 . PHE B 341 ? 0.6299 0.6903 0.7451 0.0588  -0.1014 -0.1267 405 PHE B CD2 
5346  C CE1 . PHE B 341 ? 0.6717 0.7287 0.7914 0.0608  -0.0851 -0.1192 405 PHE B CE1 
5347  C CE2 . PHE B 341 ? 0.6411 0.6900 0.7413 0.0601  -0.0980 -0.1220 405 PHE B CE2 
5348  C CZ  . PHE B 341 ? 0.6295 0.6759 0.7306 0.0614  -0.0910 -0.1191 405 PHE B CZ  
5349  N N   . TRP B 342 ? 0.4793 0.5594 0.6107 0.0682  -0.1201 -0.1392 406 TRP B N   
5350  C CA  . TRP B 342 ? 0.5127 0.5864 0.6251 0.0740  -0.1237 -0.1382 406 TRP B CA  
5351  C C   . TRP B 342 ? 0.6332 0.6959 0.7288 0.0724  -0.1225 -0.1346 406 TRP B C   
5352  O O   . TRP B 342 ? 0.7002 0.7613 0.7975 0.0680  -0.1214 -0.1350 406 TRP B O   
5353  C CB  . TRP B 342 ? 0.3989 0.4780 0.5128 0.0797  -0.1331 -0.1441 406 TRP B CB  
5354  C CG  . TRP B 342 ? 0.4672 0.5472 0.5850 0.0786  -0.1395 -0.1498 406 TRP B CG  
5355  C CD1 . TRP B 342 ? 0.5625 0.6509 0.7020 0.0761  -0.1452 -0.1561 406 TRP B CD1 
5356  C CD2 . TRP B 342 ? 0.5432 0.6141 0.6433 0.0807  -0.1415 -0.1497 406 TRP B CD2 
5357  N NE1 . TRP B 342 ? 0.5208 0.6045 0.6546 0.0769  -0.1518 -0.1610 406 TRP B NE1 
5358  C CE2 . TRP B 342 ? 0.5172 0.5905 0.6261 0.0803  -0.1491 -0.1572 406 TRP B CE2 
5359  C CE3 . TRP B 342 ? 0.7010 0.7622 0.7809 0.0835  -0.1379 -0.1437 406 TRP B CE3 
5360  C CZ2 . TRP B 342 ? 0.4821 0.5471 0.5753 0.0840  -0.1523 -0.1588 406 TRP B CZ2 
5361  C CZ3 . TRP B 342 ? 0.5387 0.5935 0.6061 0.0868  -0.1397 -0.1439 406 TRP B CZ3 
5362  C CH2 . TRP B 342 ? 0.4433 0.4995 0.5153 0.0876  -0.1465 -0.1516 406 TRP B CH2 
5363  N N   . ILE B 343 ? 0.5122 0.5675 0.5931 0.0764  -0.1228 -0.1305 407 ILE B N   
5364  C CA  . ILE B 343 ? 0.5210 0.5666 0.5894 0.0757  -0.1215 -0.1252 407 ILE B CA  
5365  C C   . ILE B 343 ? 0.5373 0.5798 0.5944 0.0831  -0.1249 -0.1231 407 ILE B C   
5366  O O   . ILE B 343 ? 0.6087 0.6509 0.6636 0.0869  -0.1263 -0.1227 407 ILE B O   
5367  C CB  . ILE B 343 ? 0.5722 0.6091 0.6371 0.0720  -0.1172 -0.1195 407 ILE B CB  
5368  C CG1 . ILE B 343 ? 0.5569 0.5962 0.6311 0.0667  -0.1127 -0.1210 407 ILE B CG1 
5369  C CG2 . ILE B 343 ? 0.5443 0.5719 0.6013 0.0705  -0.1164 -0.1129 407 ILE B CG2 
5370  C CD1 . ILE B 343 ? 0.6289 0.6575 0.6966 0.0648  -0.1098 -0.1164 407 ILE B CD1 
5371  N N   . GLU B 344 ? 0.5878 0.6271 0.6369 0.0861  -0.1256 -0.1211 408 GLU B N   
5372  C CA  . GLU B 344 ? 0.5640 0.5998 0.6014 0.0947  -0.1274 -0.1178 408 GLU B CA  
5373  C C   . GLU B 344 ? 0.6965 0.7229 0.7294 0.0935  -0.1230 -0.1072 408 GLU B C   
5374  O O   . GLU B 344 ? 0.7498 0.7719 0.7855 0.0879  -0.1192 -0.1023 408 GLU B O   
5375  C CB  . GLU B 344 ? 0.6168 0.6531 0.6466 0.1007  -0.1298 -0.1208 408 GLU B CB  
5376  C CG  . GLU B 344 ? 0.8686 0.9014 0.8837 0.1125  -0.1315 -0.1183 408 GLU B CG  
5377  C CD  . GLU B 344 ? 1.2460 1.2758 1.2495 0.1200  -0.1331 -0.1204 408 GLU B CD  
5378  O OE1 . GLU B 344 ? 1.2342 1.2650 1.2294 0.1294  -0.1404 -0.1276 408 GLU B OE1 
5379  O OE2 . GLU B 344 ? 1.0718 1.0975 1.0738 0.1170  -0.1277 -0.1152 408 GLU B OE2 
5380  N N   . ILE B 345 ? 0.6634 0.6864 0.6912 0.0989  -0.1240 -0.1033 409 ILE B N   
5381  C CA  . ILE B 345 ? 0.6394 0.6532 0.6679 0.0970  -0.1218 -0.0936 409 ILE B CA  
5382  C C   . ILE B 345 ? 0.6093 0.6195 0.6306 0.1056  -0.1204 -0.0862 409 ILE B C   
5383  O O   . ILE B 345 ? 0.6575 0.6708 0.6720 0.1132  -0.1230 -0.0897 409 ILE B O   
5384  C CB  . ILE B 345 ? 0.7600 0.7711 0.7909 0.0950  -0.1249 -0.0959 409 ILE B CB  
5385  C CG1 . ILE B 345 ? 0.6788 0.6906 0.7158 0.0876  -0.1244 -0.1005 409 ILE B CG1 
5386  C CG2 . ILE B 345 ? 0.8102 0.8105 0.8409 0.0958  -0.1259 -0.0871 409 ILE B CG2 
5387  C CD1 . ILE B 345 ? 0.8908 0.8971 0.9266 0.0876  -0.1267 -0.1018 409 ILE B CD1 
5388  N N   . ALA B 346 ? 0.6031 0.6072 0.6269 0.1052  -0.1160 -0.0750 410 ALA B N   
5389  C CA  . ALA B 346 ? 0.6081 0.6080 0.6276 0.1140  -0.1128 -0.0648 410 ALA B CA  
5390  C C   . ALA B 346 ? 0.5392 0.5358 0.5584 0.1166  -0.1167 -0.0646 410 ALA B C   
5391  O O   . ALA B 346 ? 0.5432 0.5355 0.5692 0.1101  -0.1207 -0.0660 410 ALA B O   
5392  C CB  . ALA B 346 ? 0.5968 0.5906 0.6261 0.1111  -0.1073 -0.0511 410 ALA B CB  
5393  N N   . ALA B 347 ? 0.5833 0.5808 0.5928 0.1273  -0.1159 -0.0630 411 ALA B N   
5394  C CA  . ALA B 347 ? 0.6895 0.6830 0.6984 0.1310  -0.1186 -0.0608 411 ALA B CA  
5395  C C   . ALA B 347 ? 0.8165 0.8048 0.8239 0.1396  -0.1124 -0.0468 411 ALA B C   
5396  O O   . ALA B 347 ? 0.9265 0.9140 0.9354 0.1418  -0.1056 -0.0379 411 ALA B O   
5397  C CB  . ALA B 347 ? 0.7228 0.7231 0.7215 0.1370  -0.1235 -0.0724 411 ALA B CB  
5398  N N   . THR B 348 ? 0.9472 0.9319 0.9527 0.1450  -0.1139 -0.0438 412 THR B N   
5399  C CA  . THR B 348 ? 1.0203 1.0010 1.0219 0.1562  -0.1072 -0.0310 412 THR B CA  
5400  C C   . THR B 348 ? 0.8869 0.8677 0.8780 0.1643  -0.1110 -0.0357 412 THR B C   
5401  O O   . THR B 348 ? 0.8612 0.8416 0.8549 0.1591  -0.1180 -0.0435 412 THR B O   
5402  C CB  . THR B 348 ? 1.0011 0.9733 1.0223 0.1520  -0.1026 -0.0135 412 THR B CB  
5403  O OG1 . THR B 348 ? 1.1153 1.0806 1.1479 0.1438  -0.1104 -0.0150 412 THR B OG1 
5404  C CG2 . THR B 348 ? 0.9078 0.8803 0.9410 0.1449  -0.0981 -0.0070 412 THR B CG2 
5405  N N   . THR B 349 ? 0.9100 0.8910 0.8876 0.1784  -0.1061 -0.0308 413 THR B N   
5406  C CA  . THR B 349 ? 0.8002 0.7802 0.7676 0.1877  -0.1086 -0.0328 413 THR B CA  
5407  C C   . THR B 349 ? 0.8353 0.8065 0.8161 0.1853  -0.1071 -0.0209 413 THR B C   
5408  O O   . THR B 349 ? 0.9041 0.8699 0.9014 0.1792  -0.1030 -0.0088 413 THR B O   
5409  C CB  . THR B 349 ? 0.8644 0.8451 0.8117 0.2052  -0.1035 -0.0301 413 THR B CB  
5410  O OG1 . THR B 349 ? 0.9216 0.9091 0.8573 0.2066  -0.1089 -0.0443 413 THR B OG1 
5411  C CG2 . THR B 349 ? 1.3700 1.3486 1.3056 0.2169  -0.1049 -0.0299 413 THR B CG2 
5412  N N   . LYS B 350 ? 1.3046 1.2741 1.2798 0.1899  -0.1114 -0.0244 414 LYS B N   
5413  C CA  . LYS B 350 ? 1.4320 1.3918 1.4180 0.1895  -0.1111 -0.0137 414 LYS B CA  
5414  C C   . LYS B 350 ? 1.4090 1.3630 1.4053 0.1945  -0.1005 0.0064  414 LYS B C   
5415  O O   . LYS B 350 ? 1.4005 1.3459 1.4155 0.1894  -0.1007 0.0173  414 LYS B O   
5416  C CB  . LYS B 350 ? 1.4912 1.4511 1.4637 0.1990  -0.1146 -0.0191 414 LYS B CB  
5417  C CG  . LYS B 350 ? 1.3604 1.3096 1.3420 0.1993  -0.1157 -0.0101 414 LYS B CG  
5418  C CD  . LYS B 350 ? 1.7798 1.7301 1.7448 0.2122  -0.1164 -0.0134 414 LYS B CD  
5419  C CE  . LYS B 350 ? 1.7497 1.6884 1.7236 0.2134  -0.1170 -0.0036 414 LYS B CE  
5420  N NZ  . LYS B 350 ? 1.7886 1.7282 1.7461 0.2250  -0.1189 -0.0084 414 LYS B NZ  
5421  N N   . ALA B 351 ? 1.2748 1.2328 1.2597 0.2051  -0.0915 0.0117  415 ALA B N   
5422  C CA  . ALA B 351 ? 1.2186 1.1722 1.2141 0.2108  -0.0791 0.0324  415 ALA B CA  
5423  C C   . ALA B 351 ? 1.3103 1.2684 1.3001 0.2137  -0.0719 0.0347  415 ALA B C   
5424  O O   . ALA B 351 ? 1.6644 1.6241 1.6321 0.2293  -0.0657 0.0355  415 ALA B O   
5425  C CB  . ALA B 351 ? 1.0920 1.0421 1.0752 0.2280  -0.0715 0.0424  415 ALA B CB  
5426  N N   . GLY B 352 ? 1.1033 1.0625 1.1112 0.1998  -0.0734 0.0354  416 GLY B N   
5427  C CA  . GLY B 352 ? 1.0191 0.9822 1.0235 0.2013  -0.0666 0.0380  416 GLY B CA  
5428  C C   . GLY B 352 ? 1.0218 0.9912 1.0036 0.2028  -0.0732 0.0185  416 GLY B C   
5429  O O   . GLY B 352 ? 1.2034 1.1755 1.1786 0.1991  -0.0835 0.0032  416 GLY B O   
5430  N N   . LEU B 353 ? 1.2346 1.2062 1.2057 0.2086  -0.0675 0.0192  417 LEU B N   
5431  C CA  . LEU B 353 ? 1.1583 1.1345 1.1077 0.2122  -0.0742 0.0012  417 LEU B CA  
5432  C C   . LEU B 353 ? 1.2669 1.2485 1.2277 0.1946  -0.0834 -0.0126 417 LEU B C   
5433  O O   . LEU B 353 ? 1.4552 1.4370 1.4325 0.1818  -0.0890 -0.0151 417 LEU B O   
5434  C CB  . LEU B 353 ? 0.9088 0.8858 0.8374 0.2236  -0.0810 -0.0100 417 LEU B CB  
5435  C CG  . LEU B 353 ? 0.9524 0.9235 0.8725 0.2391  -0.0735 0.0032  417 LEU B CG  
5436  C CD1 . LEU B 353 ? 1.1593 1.1314 1.0640 0.2468  -0.0821 -0.0084 417 LEU B CD1 
5437  C CD2 . LEU B 353 ? 0.9339 0.8997 0.8366 0.2579  -0.0610 0.0161  417 LEU B CD2 
5438  N N   . SER B 354 ? 1.1439 1.1286 1.0949 0.1951  -0.0851 -0.0215 418 SER B N   
5439  C CA  . SER B 354 ? 1.1978 1.1870 1.1616 0.1790  -0.0907 -0.0308 418 SER B CA  
5440  C C   . SER B 354 ? 1.1540 1.1490 1.1077 0.1781  -0.1011 -0.0501 418 SER B C   
5441  O O   . SER B 354 ? 1.9425 1.9396 1.8915 0.1771  -0.1028 -0.0571 418 SER B O   
5442  C CB  . SER B 354 ? 1.3371 1.3250 1.3056 0.1770  -0.0830 -0.0223 418 SER B CB  
5443  O OG  . SER B 354 ? 2.0934 2.0795 2.0397 0.1919  -0.0793 -0.0233 418 SER B OG  
5444  N N   . SER B 355 ? 1.1507 1.1484 1.1032 0.1783  -0.1083 -0.0583 419 SER B N   
5445  C CA  . SER B 355 ? 1.2270 1.2318 1.1787 0.1743  -0.1183 -0.0753 419 SER B CA  
5446  C C   . SER B 355 ? 0.9471 0.9555 0.9165 0.1575  -0.1197 -0.0792 419 SER B C   
5447  O O   . SER B 355 ? 1.1846 1.1891 1.1657 0.1494  -0.1154 -0.0703 419 SER B O   
5448  C CB  . SER B 355 ? 1.3606 1.3682 1.3098 0.1782  -0.1247 -0.0816 419 SER B CB  
5449  O OG  . SER B 355 ? 1.4054 1.4207 1.3548 0.1771  -0.1343 -0.0968 419 SER B OG  
5450  N N   . ASN B 356 ? 0.8071 0.8220 0.7788 0.1531  -0.1260 -0.0919 420 ASN B N   
5451  C CA  . ASN B 356 ? 0.7230 0.7417 0.7103 0.1390  -0.1272 -0.0964 420 ASN B CA  
5452  C C   . ASN B 356 ? 0.7130 0.7385 0.7072 0.1359  -0.1337 -0.1060 420 ASN B C   
5453  O O   . ASN B 356 ? 0.9036 0.9332 0.8922 0.1436  -0.1392 -0.1126 420 ASN B O   
5454  C CB  . ASN B 356 ? 0.7377 0.7591 0.7259 0.1356  -0.1279 -0.1019 420 ASN B CB  
5455  C CG  . ASN B 356 ? 0.7979 0.8134 0.7744 0.1433  -0.1225 -0.0946 420 ASN B CG  
5456  O OD1 . ASN B 356 ? 0.7517 0.7646 0.7124 0.1563  -0.1238 -0.0954 420 ASN B OD1 
5457  N ND2 . ASN B 356 ? 0.8806 0.8932 0.8637 0.1364  -0.1162 -0.0872 420 ASN B ND2 
5458  N N   . ASP B 357 ? 0.7151 0.7411 0.7209 0.1259  -0.1329 -0.1061 421 ASP B N   
5459  C CA  . ASP B 357 ? 0.7600 0.7933 0.7739 0.1231  -0.1370 -0.1145 421 ASP B CA  
5460  C C   . ASP B 357 ? 0.7563 0.7944 0.7827 0.1134  -0.1361 -0.1192 421 ASP B C   
5461  O O   . ASP B 357 ? 0.8380 0.8732 0.8663 0.1078  -0.1327 -0.1165 421 ASP B O   
5462  C CB  . ASP B 357 ? 0.6781 0.7073 0.6913 0.1242  -0.1372 -0.1114 421 ASP B CB  
5463  C CG  . ASP B 357 ? 1.1999 1.2369 1.2134 0.1304  -0.1420 -0.1184 421 ASP B CG  
5464  O OD1 . ASP B 357 ? 1.3805 1.4275 1.4032 0.1290  -0.1449 -0.1262 421 ASP B OD1 
5465  O OD2 . ASP B 357 ? 1.3837 1.4169 1.3902 0.1367  -0.1429 -0.1155 421 ASP B OD2 
5466  N N   . LEU B 358 ? 0.6042 0.6499 0.6398 0.1122  -0.1382 -0.1252 422 LEU B N   
5467  C CA  . LEU B 358 ? 0.5432 0.5949 0.5922 0.1048  -0.1365 -0.1290 422 LEU B CA  
5468  C C   . LEU B 358 ? 0.6128 0.6619 0.6651 0.1018  -0.1327 -0.1267 422 LEU B C   
5469  O O   . LEU B 358 ? 0.5631 0.6097 0.6105 0.1065  -0.1335 -0.1253 422 LEU B O   
5470  C CB  . LEU B 358 ? 0.6055 0.6692 0.6667 0.1068  -0.1417 -0.1372 422 LEU B CB  
5471  C CG  . LEU B 358 ? 0.5745 0.6404 0.6361 0.1079  -0.1467 -0.1422 422 LEU B CG  
5472  C CD1 . LEU B 358 ? 0.7128 0.7903 0.7936 0.1070  -0.1525 -0.1499 422 LEU B CD1 
5473  C CD2 . LEU B 358 ? 0.7456 0.8065 0.8071 0.1006  -0.1415 -0.1389 422 LEU B CD2 
5474  N N   . ILE B 359 ? 0.5698 0.6185 0.6288 0.0950  -0.1285 -0.1262 423 ILE B N   
5475  C CA  . ILE B 359 ? 0.5488 0.5965 0.6116 0.0937  -0.1243 -0.1253 423 ILE B CA  
5476  C C   . ILE B 359 ? 0.5633 0.6201 0.6417 0.0888  -0.1208 -0.1281 423 ILE B C   
5477  O O   . ILE B 359 ? 0.6348 0.6925 0.7167 0.0839  -0.1210 -0.1290 423 ILE B O   
5478  C CB  . ILE B 359 ? 0.4867 0.5199 0.5383 0.0919  -0.1226 -0.1201 423 ILE B CB  
5479  C CG1 . ILE B 359 ? 0.6080 0.6385 0.6604 0.0923  -0.1181 -0.1198 423 ILE B CG1 
5480  C CG2 . ILE B 359 ? 0.5249 0.5539 0.5761 0.0859  -0.1218 -0.1176 423 ILE B CG2 
5481  C CD1 . ILE B 359 ? 0.7020 0.7166 0.7398 0.0958  -0.1200 -0.1166 423 ILE B CD1 
5482  N N   . THR B 360 ? 0.6466 0.7106 0.7357 0.0907  -0.1174 -0.1288 424 THR B N   
5483  C CA  . THR B 360 ? 0.5964 0.6706 0.7051 0.0866  -0.1136 -0.1302 424 THR B CA  
5484  C C   . THR B 360 ? 0.6675 0.7380 0.7758 0.0878  -0.1047 -0.1256 424 THR B C   
5485  O O   . THR B 360 ? 0.7451 0.8108 0.8439 0.0944  -0.1028 -0.1233 424 THR B O   
5486  C CB  . THR B 360 ? 0.6374 0.7264 0.7657 0.0892  -0.1172 -0.1341 424 THR B CB  
5487  O OG1 . THR B 360 ? 0.7768 0.8693 0.9090 0.0949  -0.1123 -0.1310 424 THR B OG1 
5488  C CG2 . THR B 360 ? 0.7999 0.8894 0.9211 0.0930  -0.1268 -0.1385 424 THR B CG2 
5489  N N   . PHE B 361 ? 0.5059 0.5777 0.6231 0.0825  -0.0994 -0.1243 425 PHE B N   
5490  C CA  . PHE B 361 ? 0.4721 0.5409 0.5897 0.0846  -0.0897 -0.1196 425 PHE B CA  
5491  C C   . PHE B 361 ? 0.5521 0.6353 0.6970 0.0827  -0.0833 -0.1183 425 PHE B C   
5492  O O   . PHE B 361 ? 0.6189 0.7100 0.7805 0.0759  -0.0868 -0.1215 425 PHE B O   
5493  C CB  . PHE B 361 ? 0.4564 0.5126 0.5605 0.0804  -0.0880 -0.1179 425 PHE B CB  
5494  C CG  . PHE B 361 ? 0.4915 0.5324 0.5728 0.0823  -0.0934 -0.1174 425 PHE B CG  
5495  C CD1 . PHE B 361 ? 0.4922 0.5305 0.5691 0.0779  -0.1005 -0.1190 425 PHE B CD1 
5496  C CD2 . PHE B 361 ? 0.4907 0.5187 0.5552 0.0894  -0.0918 -0.1149 425 PHE B CD2 
5497  C CE1 . PHE B 361 ? 0.5029 0.5273 0.5631 0.0792  -0.1055 -0.1170 425 PHE B CE1 
5498  C CE2 . PHE B 361 ? 0.5102 0.5225 0.5562 0.0907  -0.0991 -0.1145 425 PHE B CE2 
5499  C CZ  . PHE B 361 ? 0.4770 0.4882 0.5232 0.0848  -0.1056 -0.1150 425 PHE B CZ  
5500  N N   . CYS B 362 ? 0.5253 0.6110 0.6752 0.0892  -0.0739 -0.1129 426 CYS B N   
5501  C CA  . CYS B 362 ? 0.6588 0.7575 0.8371 0.0880  -0.0653 -0.1089 426 CYS B CA  
5502  C C   . CYS B 362 ? 0.5848 0.6750 0.7547 0.0909  -0.0533 -0.1024 426 CYS B C   
5503  O O   . CYS B 362 ? 0.7312 0.8062 0.8734 0.0979  -0.0509 -0.1005 426 CYS B O   
5504  C CB  . CYS B 362 ? 0.6656 0.7789 0.8660 0.0936  -0.0631 -0.1064 426 CYS B CB  
5505  S SG  . CYS B 362 ? 1.6770 1.8018 1.8937 0.0884  -0.0795 -0.1156 426 CYS B SG  
5506  N N   . GLY B 363 ? 0.4566 0.5552 0.6495 0.0861  -0.0468 -0.0993 427 GLY B N   
5507  C CA  . GLY B 363 ? 0.5728 0.6643 0.7595 0.0897  -0.0342 -0.0924 427 GLY B CA  
5508  C C   . GLY B 363 ? 0.7126 0.8069 0.9034 0.1019  -0.0205 -0.0832 427 GLY B C   
5509  O O   . GLY B 363 ? 0.9088 1.0186 1.1266 0.1039  -0.0175 -0.0799 427 GLY B O   
5510  N N   . THR B 364 ? 1.0091 1.0874 1.1724 0.1111  -0.0125 -0.0789 428 THR B N   
5511  C CA  . THR B 364 ? 1.1767 1.2550 1.3404 0.1249  0.0037  -0.0684 428 THR B CA  
5512  C C   . THR B 364 ? 1.1103 1.1830 1.2726 0.1268  0.0161  -0.0618 428 THR B C   
5513  O O   . THR B 364 ? 0.9664 1.0290 1.1152 0.1198  0.0106  -0.0664 428 THR B O   
5514  C CB  . THR B 364 ? 1.1206 1.1831 1.2495 0.1394  0.0034  -0.0683 428 THR B CB  
5515  O OG1 . THR B 364 ? 1.3983 1.4626 1.5295 0.1546  0.0205  -0.0571 428 THR B OG1 
5516  C CG2 . THR B 364 ? 0.7874 0.8257 0.8772 0.1413  -0.0039 -0.0734 428 THR B CG2 
5517  N N   . GLY B 365 ? 1.1297 1.2096 1.3077 0.1368  0.0333  -0.0501 429 GLY B N   
5518  C CA  . GLY B 365 ? 0.9632 1.0395 1.1431 0.1411  0.0483  -0.0413 429 GLY B CA  
5519  C C   . GLY B 365 ? 0.9005 0.9514 1.0331 0.1542  0.0505  -0.0413 429 GLY B C   
5520  O O   . GLY B 365 ? 1.0374 1.0788 1.1593 0.1546  0.0553  -0.0394 429 GLY B O   
5521  N N   . GLY B 366 ? 0.9781 1.0172 1.0822 0.1652  0.0458  -0.0441 430 GLY B N   
5522  C CA  . GLY B 366 ? 1.0353 1.0469 1.0916 0.1791  0.0441  -0.0459 430 GLY B CA  
5523  C C   . GLY B 366 ? 1.0050 1.0014 1.0393 0.1689  0.0263  -0.0573 430 GLY B C   
5524  O O   . GLY B 366 ? 0.7995 0.8042 0.8474 0.1535  0.0130  -0.0651 430 GLY B O   
5525  N N   . SER B 367 ? 1.0565 1.0301 1.0569 0.1782  0.0260  -0.0578 431 SER B N   
5526  C CA  . SER B 367 ? 1.0509 1.0079 1.0293 0.1708  0.0079  -0.0679 431 SER B CA  
5527  C C   . SER B 367 ? 1.0955 1.0420 1.0549 0.1749  -0.0057 -0.0744 431 SER B C   
5528  O O   . SER B 367 ? 1.0166 0.9613 0.9675 0.1885  0.0001  -0.0709 431 SER B O   
5529  C CB  . SER B 367 ? 0.9912 0.9254 0.9386 0.1811  0.0095  -0.0670 431 SER B CB  
5530  O OG  . SER B 367 ? 1.1879 1.1079 1.1201 0.1726  -0.0088 -0.0762 431 SER B OG  
5531  N N   . MET B 368 ? 1.1086 1.0489 1.0632 0.1634  -0.0231 -0.0829 432 MET B N   
5532  C CA  . MET B 368 ? 1.0135 0.9447 0.9544 0.1653  -0.0367 -0.0887 432 MET B CA  
5533  C C   . MET B 368 ? 1.0287 0.9346 0.9419 0.1664  -0.0526 -0.0949 432 MET B C   
5534  O O   . MET B 368 ? 1.0906 0.9917 1.0036 0.1593  -0.0560 -0.0961 432 MET B O   
5535  C CB  . MET B 368 ? 0.8893 0.8405 0.8579 0.1498  -0.0430 -0.0920 432 MET B CB  
5536  C CG  . MET B 368 ? 1.2357 1.2090 1.2294 0.1511  -0.0320 -0.0874 432 MET B CG  
5537  S SD  . MET B 368 ? 1.2253 1.1939 1.2054 0.1633  -0.0353 -0.0881 432 MET B SD  
5538  C CE  . MET B 368 ? 1.3228 1.2792 1.2906 0.1537  -0.0567 -0.0974 432 MET B CE  
5539  N N   . PRO B 369 ? 1.0847 0.9736 0.9758 0.1753  -0.0631 -0.0986 433 PRO B N   
5540  C CA  . PRO B 369 ? 1.1485 1.0126 1.0176 0.1755  -0.0812 -0.1048 433 PRO B CA  
5541  C C   . PRO B 369 ? 1.0906 0.9631 0.9804 0.1564  -0.0937 -0.1084 433 PRO B C   
5542  O O   . PRO B 369 ? 0.9624 0.8575 0.8780 0.1454  -0.0899 -0.1073 433 PRO B O   
5543  C CB  . PRO B 369 ? 1.0384 0.8849 0.8828 0.1904  -0.0878 -0.1072 433 PRO B CB  
5544  C CG  . PRO B 369 ? 0.9801 0.8498 0.8454 0.1882  -0.0783 -0.1040 433 PRO B CG  
5545  C CD  . PRO B 369 ? 0.9843 0.8763 0.8721 0.1851  -0.0597 -0.0973 433 PRO B CD  
5546  N N   . ASP B 370 ? 0.9269 0.7805 0.8054 0.1537  -0.1087 -0.1121 434 ASP B N   
5547  C CA  . ASP B 370 ? 0.7754 0.6340 0.6716 0.1384  -0.1202 -0.1138 434 ASP B CA  
5548  C C   . ASP B 370 ? 0.7193 0.5780 0.6177 0.1384  -0.1280 -0.1155 434 ASP B C   
5549  O O   . ASP B 370 ? 0.9846 0.8235 0.8620 0.1496  -0.1367 -0.1182 434 ASP B O   
5550  C CB  . ASP B 370 ? 1.1356 0.9729 1.0211 0.1370  -0.1345 -0.1163 434 ASP B CB  
5551  C CG  . ASP B 370 ? 1.4154 1.2523 1.2983 0.1368  -0.1273 -0.1147 434 ASP B CG  
5552  O OD1 . ASP B 370 ? 1.3686 1.2262 1.2676 0.1315  -0.1123 -0.1112 434 ASP B OD1 
5553  O OD2 . ASP B 370 ? 1.9091 1.7242 1.7747 0.1420  -0.1376 -0.1172 434 ASP B OD2 
5554  N N   . VAL B 371 ? 0.5861 0.4658 0.5086 0.1267  -0.1254 -0.1140 435 VAL B N   
5555  C CA  . VAL B 371 ? 0.6554 0.5365 0.5818 0.1258  -0.1324 -0.1149 435 VAL B CA  
5556  C C   . VAL B 371 ? 0.8055 0.6987 0.7540 0.1115  -0.1367 -0.1132 435 VAL B C   
5557  O O   . VAL B 371 ? 1.0913 1.0021 1.0564 0.1029  -0.1290 -0.1115 435 VAL B O   
5558  C CB  . VAL B 371 ? 0.5995 0.4948 0.5282 0.1325  -0.1217 -0.1141 435 VAL B CB  
5559  C CG1 . VAL B 371 ? 0.7614 0.6547 0.6893 0.1341  -0.1295 -0.1154 435 VAL B CG1 
5560  C CG2 . VAL B 371 ? 0.5301 0.4155 0.4387 0.1477  -0.1140 -0.1136 435 VAL B CG2 
5561  N N   . ASN B 372 ? 0.9104 0.7928 0.8584 0.1102  -0.1489 -0.1132 436 ASN B N   
5562  C CA  . ASN B 372 ? 0.8583 0.7515 0.8254 0.1000  -0.1515 -0.1100 436 ASN B CA  
5563  C C   . ASN B 372 ? 0.7988 0.7015 0.7681 0.1034  -0.1494 -0.1102 436 ASN B C   
5564  O O   . ASN B 372 ? 1.0777 0.9673 1.0376 0.1093  -0.1574 -0.1111 436 ASN B O   
5565  C CB  . ASN B 372 ? 0.7825 0.6582 0.7519 0.0963  -0.1658 -0.1079 436 ASN B CB  
5566  C CG  . ASN B 372 ? 1.1818 1.0672 1.1705 0.0880  -0.1672 -0.1025 436 ASN B CG  
5567  O OD1 . ASN B 372 ? 1.7503 1.6535 1.7468 0.0864  -0.1590 -0.1014 436 ASN B OD1 
5568  N ND2 . ASN B 372 ? 1.3386 1.2116 1.3358 0.0836  -0.1780 -0.0986 436 ASN B ND2 
5569  N N   . TRP B 373 ? 0.6730 0.5972 0.6547 0.1000  -0.1399 -0.1098 437 TRP B N   
5570  C CA  . TRP B 373 ? 0.7644 0.6991 0.7493 0.1033  -0.1381 -0.1103 437 TRP B CA  
5571  C C   . TRP B 373 ? 0.6951 0.6304 0.6876 0.0995  -0.1440 -0.1072 437 TRP B C   
5572  O O   . TRP B 373 ? 0.8249 0.7576 0.8255 0.0927  -0.1473 -0.1033 437 TRP B O   
5573  C CB  . TRP B 373 ? 0.7048 0.6612 0.7012 0.1018  -0.1275 -0.1116 437 TRP B CB  
5574  C CG  . TRP B 373 ? 0.6343 0.5912 0.6258 0.1070  -0.1197 -0.1128 437 TRP B CG  
5575  C CD1 . TRP B 373 ? 0.7124 0.6711 0.7072 0.1035  -0.1140 -0.1122 437 TRP B CD1 
5576  C CD2 . TRP B 373 ? 0.5863 0.5412 0.5682 0.1180  -0.1154 -0.1135 437 TRP B CD2 
5577  N NE1 . TRP B 373 ? 0.5996 0.5575 0.5879 0.1117  -0.1061 -0.1119 437 TRP B NE1 
5578  C CE2 . TRP B 373 ? 0.6274 0.5834 0.6081 0.1209  -0.1061 -0.1124 437 TRP B CE2 
5579  C CE3 . TRP B 373 ? 0.6078 0.5602 0.5823 0.1262  -0.1174 -0.1142 437 TRP B CE3 
5580  C CZ2 . TRP B 373 ? 0.7022 0.6571 0.6749 0.1324  -0.0983 -0.1110 437 TRP B CZ2 
5581  C CZ3 . TRP B 373 ? 0.7385 0.6900 0.7046 0.1374  -0.1101 -0.1136 437 TRP B CZ3 
5582  C CH2 . TRP B 373 ? 0.7719 0.7246 0.7372 0.1408  -0.1004 -0.1116 437 TRP B CH2 
5583  N N   . ALA C 11  ? 1.2826 1.5834 1.3137 0.0668  -0.1637 0.1502  75  ALA C N   
5584  C CA  . ALA C 11  ? 1.5287 1.7840 1.5584 0.0591  -0.1773 0.1295  75  ALA C CA  
5585  C C   . ALA C 11  ? 1.5985 1.8395 1.6533 0.0388  -0.1905 0.1435  75  ALA C C   
5586  O O   . ALA C 11  ? 1.1542 1.4218 1.2311 0.0318  -0.1879 0.1621  75  ALA C O   
5587  C CB  . ALA C 11  ? 1.3116 1.5614 1.3301 0.0717  -0.1723 0.1015  75  ALA C CB  
5588  N N   . THR C 12  ? 1.9670 2.1657 2.0180 0.0303  -0.2055 0.1334  76  THR C N   
5589  C CA  . THR C 12  ? 1.7491 1.9265 1.8203 0.0120  -0.2219 0.1445  76  THR C CA  
5590  C C   . THR C 12  ? 1.3509 1.4898 1.4144 0.0116  -0.2320 0.1191  76  THR C C   
5591  O O   . THR C 12  ? 1.3268 1.4437 1.3690 0.0207  -0.2316 0.0974  76  THR C O   
5592  C CB  . THR C 12  ? 1.6053 1.7669 1.6796 0.0013  -0.2336 0.1622  76  THR C CB  
5593  O OG1 . THR C 12  ? 1.5453 1.7446 1.6261 0.0017  -0.2231 0.1878  76  THR C OG1 
5594  C CG2 . THR C 12  ? 1.3805 1.5165 1.4759 -0.0175 -0.2539 0.1733  76  THR C CG2 
5595  N N   . PRO C 13  ? 1.1151 1.2467 1.1961 0.0013  -0.2412 0.1225  77  PRO C N   
5596  C CA  . PRO C 13  ? 1.1818 1.2772 1.2547 0.0009  -0.2515 0.1008  77  PRO C CA  
5597  C C   . PRO C 13  ? 1.4206 1.4782 1.4773 0.0010  -0.2624 0.0890  77  PRO C C   
5598  O O   . PRO C 13  ? 1.6801 1.7271 1.7437 -0.0081 -0.2737 0.1038  77  PRO C O   
5599  C CB  . PRO C 13  ? 1.1720 1.2632 1.2698 -0.0141 -0.2653 0.1150  77  PRO C CB  
5600  C CG  . PRO C 13  ? 1.0678 1.2038 1.1870 -0.0172 -0.2553 0.1384  77  PRO C CG  
5601  C CD  . PRO C 13  ? 1.2086 1.3659 1.3188 -0.0109 -0.2434 0.1482  77  PRO C CD  
5602  N N   . LEU C 14  ? 1.6268 1.6654 1.6630 0.0115  -0.2591 0.0633  78  LEU C N   
5603  C CA  . LEU C 14  ? 1.3538 1.3584 1.3745 0.0137  -0.2685 0.0495  78  LEU C CA  
5604  C C   . LEU C 14  ? 1.4640 1.4370 1.4925 0.0026  -0.2892 0.0526  78  LEU C C   
5605  O O   . LEU C 14  ? 1.5117 1.4744 1.5447 -0.0005 -0.2950 0.0470  78  LEU C O   
5606  C CB  . LEU C 14  ? 1.4130 1.4064 1.4140 0.0261  -0.2605 0.0226  78  LEU C CB  
5607  C CG  . LEU C 14  ? 1.3735 1.3368 1.3588 0.0305  -0.2678 0.0072  78  LEU C CG  
5608  C CD1 . LEU C 14  ? 1.3045 1.2791 1.2827 0.0366  -0.2617 0.0098  78  LEU C CD1 
5609  C CD2 . LEU C 14  ? 1.6329 1.5817 1.6042 0.0389  -0.2632 -0.0171 78  LEU C CD2 
5610  N N   . VAL C 15  ? 1.5921 1.5490 1.6215 -0.0027 -0.3013 0.0616  79  VAL C N   
5611  C CA  . VAL C 15  ? 1.5900 1.5127 1.6246 -0.0116 -0.3238 0.0632  79  VAL C CA  
5612  C C   . VAL C 15  ? 1.4854 1.3773 1.4989 -0.0030 -0.3304 0.0442  79  VAL C C   
5613  O O   . VAL C 15  ? 1.4694 1.3659 1.4740 0.0026  -0.3249 0.0441  79  VAL C O   
5614  C CB  . VAL C 15  ? 1.6164 1.5447 1.6734 -0.0265 -0.3357 0.0924  79  VAL C CB  
5615  C CG1 . VAL C 15  ? 1.5480 1.4370 1.6021 -0.0314 -0.3588 0.0924  79  VAL C CG1 
5616  C CG2 . VAL C 15  ? 1.3247 1.2683 1.4064 -0.0379 -0.3393 0.1077  79  VAL C CG2 
5617  N N   . LEU C 16  ? 1.2376 1.0993 1.2426 -0.0006 -0.3420 0.0277  80  LEU C N   
5618  C CA  . LEU C 16  ? 1.4001 1.2339 1.3861 0.0085  -0.3487 0.0095  80  LEU C CA  
5619  C C   . LEU C 16  ? 1.5598 1.3627 1.5505 0.0015  -0.3735 0.0170  80  LEU C C   
5620  O O   . LEU C 16  ? 1.4468 1.2426 1.4539 -0.0102 -0.3879 0.0307  80  LEU C O   
5621  C CB  . LEU C 16  ? 1.2726 1.0932 1.2428 0.0183  -0.3447 -0.0147 80  LEU C CB  
5622  C CG  . LEU C 16  ? 1.2517 1.0975 1.2147 0.0268  -0.3215 -0.0252 80  LEU C CG  
5623  C CD1 . LEU C 16  ? 1.2471 1.0818 1.1992 0.0328  -0.3186 -0.0430 80  LEU C CD1 
5624  C CD2 . LEU C 16  ? 1.3016 1.1528 1.2534 0.0360  -0.3123 -0.0337 80  LEU C CD2 
5625  N N   . GLY C 17  ? 1.5006 1.2850 1.4779 0.0086  -0.3796 0.0080  81  GLY C N   
5626  C CA  . GLY C 17  ? 1.6671 1.4176 1.6456 0.0046  -0.4050 0.0119  81  GLY C CA  
5627  C C   . GLY C 17  ? 1.4962 1.2144 1.4692 0.0065  -0.4230 -0.0018 81  GLY C C   
5628  O O   . GLY C 17  ? 1.3407 1.0533 1.2972 0.0180  -0.4160 -0.0236 81  GLY C O   
5629  N N   . GLU C 18  ? 1.4537 1.1503 1.4402 -0.0046 -0.4469 0.0115  82  GLU C N   
5630  C CA  . GLU C 18  ? 1.5999 1.2651 1.5816 -0.0027 -0.4665 -0.0006 82  GLU C CA  
5631  C C   . GLU C 18  ? 1.5238 1.1561 1.4815 0.0127  -0.4781 -0.0239 82  GLU C C   
5632  O O   . GLU C 18  ? 1.6673 1.2819 1.6095 0.0229  -0.4829 -0.0435 82  GLU C O   
5633  C CB  . GLU C 18  ? 1.6267 1.2779 1.6323 -0.0195 -0.4907 0.0204  82  GLU C CB  
5634  C CG  . GLU C 18  ? 1.9341 1.5757 1.9452 -0.0225 -0.5008 0.0159  82  GLU C CG  
5635  C CD  . GLU C 18  ? 1.9249 1.6044 1.9458 -0.0263 -0.4779 0.0218  82  GLU C CD  
5636  O OE1 . GLU C 18  ? 1.7038 1.4187 1.7363 -0.0317 -0.4587 0.0372  82  GLU C OE1 
5637  O OE2 . GLU C 18  ? 2.1592 1.8324 2.1751 -0.0227 -0.4800 0.0105  82  GLU C OE2 
5638  N N   . ASN C 19  ? 1.5683 1.1943 1.5221 0.0155  -0.4817 -0.0217 83  ASN C N   
5639  C CA  . ASN C 19  ? 1.3061 0.9015 1.2392 0.0304  -0.4946 -0.0422 83  ASN C CA  
5640  C C   . ASN C 19  ? 1.1540 0.7672 1.0714 0.0444  -0.4727 -0.0575 83  ASN C C   
5641  O O   . ASN C 19  ? 1.1084 0.7467 1.0321 0.0409  -0.4576 -0.0468 83  ASN C O   
5642  C CB  . ASN C 19  ? 1.3745 0.9428 1.3151 0.0241  -0.5205 -0.0297 83  ASN C CB  
5643  C CG  . ASN C 19  ? 1.5699 1.1122 1.5255 0.0117  -0.5481 -0.0181 83  ASN C CG  
5644  O OD1 . ASN C 19  ? 1.5051 1.0346 1.4557 0.0151  -0.5554 -0.0298 83  ASN C OD1 
5645  N ND2 . ASN C 19  ? 1.6274 1.1617 1.6021 -0.0030 -0.5643 0.0057  83  ASN C ND2 
5646  N N   . LEU C 20  ? 1.2111 0.8120 1.1082 0.0607  -0.4712 -0.0824 84  LEU C N   
5647  C CA  . LEU C 20  ? 1.1233 0.7421 1.0073 0.0742  -0.4504 -0.0985 84  LEU C CA  
5648  C C   . LEU C 20  ? 1.1518 0.7573 1.0291 0.0824  -0.4596 -0.1035 84  LEU C C   
5649  O O   . LEU C 20  ? 1.2194 0.7923 1.0922 0.0855  -0.4843 -0.1063 84  LEU C O   
5650  C CB  . LEU C 20  ? 1.2073 0.8202 1.0736 0.0883  -0.4448 -0.1214 84  LEU C CB  
5651  C CG  . LEU C 20  ? 1.3282 0.9718 1.1898 0.0942  -0.4162 -0.1309 84  LEU C CG  
5652  C CD1 . LEU C 20  ? 1.5761 1.2440 1.4518 0.0810  -0.4025 -0.1159 84  LEU C CD1 
5653  C CD2 . LEU C 20  ? 1.7012 1.3348 1.5444 0.1083  -0.4142 -0.1517 84  LEU C CD2 
5654  N N   . CYS C 21  ? 1.3227 0.9527 1.1991 0.0868  -0.4408 -0.1055 85  CYS C N   
5655  C CA  . CYS C 21  ? 1.3825 1.0039 1.2511 0.0972  -0.4463 -0.1137 85  CYS C CA  
5656  C C   . CYS C 21  ? 1.4193 1.0182 1.2708 0.1143  -0.4560 -0.1378 85  CYS C C   
5657  O O   . CYS C 21  ? 1.5587 1.1632 1.4025 0.1208  -0.4461 -0.1509 85  CYS C O   
5658  C CB  . CYS C 21  ? 1.6347 1.2890 1.5043 0.1010  -0.4221 -0.1162 85  CYS C CB  
5659  S SG  . CYS C 21  ? 3.2394 2.9139 3.1242 0.0857  -0.4170 -0.0883 85  CYS C SG  
5660  N N   . SER C 22  ? 1.4371 1.0104 1.2820 0.1222  -0.4759 -0.1432 86  SER C N   
5661  C CA  . SER C 22  ? 1.4402 0.9969 1.2676 0.1422  -0.4828 -0.1681 86  SER C CA  
5662  C C   . SER C 22  ? 1.4255 1.0121 1.2498 0.1528  -0.4586 -0.1809 86  SER C C   
5663  O O   . SER C 22  ? 1.4060 1.0087 1.2376 0.1497  -0.4505 -0.1738 86  SER C O   
5664  C CB  . SER C 22  ? 1.5211 1.0432 1.3426 0.1492  -0.5109 -0.1712 86  SER C CB  
5665  O OG  . SER C 22  ? 1.8360 1.3278 1.6622 0.1389  -0.5363 -0.1592 86  SER C OG  
5666  N N   . ILE C 23  ? 1.3460 0.9402 1.1599 0.1651  -0.4473 -0.1991 87  ILE C N   
5667  C CA  . ILE C 23  ? 1.2259 0.8494 1.0397 0.1743  -0.4244 -0.2109 87  ILE C CA  
5668  C C   . ILE C 23  ? 1.1815 0.7932 0.9811 0.1952  -0.4318 -0.2327 87  ILE C C   
5669  O O   . ILE C 23  ? 1.0447 0.6391 0.8310 0.2044  -0.4406 -0.2433 87  ILE C O   
5670  C CB  . ILE C 23  ? 1.2294 0.8788 1.0462 0.1692  -0.4006 -0.2107 87  ILE C CB  
5671  C CG1 . ILE C 23  ? 1.3028 0.9680 1.1345 0.1506  -0.3923 -0.1900 87  ILE C CG1 
5672  C CG2 . ILE C 23  ? 1.2360 0.9124 1.0528 0.1800  -0.3794 -0.2248 87  ILE C CG2 
5673  C CD1 . ILE C 23  ? 1.2027 0.8725 1.0360 0.1416  -0.3853 -0.1837 87  ILE C CD1 
5674  N N   . ASN C 24  ? 1.1658 0.7863 0.9677 0.2038  -0.4296 -0.2394 88  ASN C N   
5675  C CA  . ASN C 24  ? 1.2012 0.8175 0.9919 0.2250  -0.4332 -0.2606 88  ASN C CA  
5676  C C   . ASN C 24  ? 1.3593 1.0109 1.1569 0.2327  -0.4096 -0.2707 88  ASN C C   
5677  O O   . ASN C 24  ? 1.4405 1.0965 1.2314 0.2506  -0.4082 -0.2883 88  ASN C O   
5678  C CB  . ASN C 24  ? 1.1862 0.7725 0.9716 0.2324  -0.4599 -0.2630 88  ASN C CB  
5679  C CG  . ASN C 24  ? 1.3466 0.8940 1.1233 0.2293  -0.4864 -0.2583 88  ASN C CG  
5680  O OD1 . ASN C 24  ? 1.1479 0.6777 0.9095 0.2430  -0.4967 -0.2730 88  ASN C OD1 
5681  N ND2 . ASN C 24  ? 1.6199 1.1540 1.4065 0.2116  -0.4985 -0.2375 88  ASN C ND2 
5682  N N   . GLY C 25  ? 1.2595 0.9370 1.0712 0.2197  -0.3916 -0.2598 89  GLY C N   
5683  C CA  . GLY C 25  ? 1.0616 0.7721 0.8827 0.2250  -0.3704 -0.2683 89  GLY C CA  
5684  C C   . GLY C 25  ? 0.9731 0.7077 0.8069 0.2097  -0.3516 -0.2563 89  GLY C C   
5685  O O   . GLY C 25  ? 1.2602 0.9876 1.0947 0.1960  -0.3539 -0.2417 89  GLY C O   
5686  N N   . TRP C 26  ? 0.8681 0.6315 0.7126 0.2123  -0.3338 -0.2625 90  TRP C N   
5687  C CA  . TRP C 26  ? 0.8693 0.6549 0.7254 0.1995  -0.3167 -0.2530 90  TRP C CA  
5688  C C   . TRP C 26  ? 0.9227 0.7293 0.7919 0.2005  -0.3095 -0.2552 90  TRP C C   
5689  O O   . TRP C 26  ? 0.8810 0.6978 0.7548 0.2123  -0.3077 -0.2683 90  TRP C O   
5690  C CB  . TRP C 26  ? 0.8476 0.6470 0.7037 0.1985  -0.2999 -0.2569 90  TRP C CB  
5691  C CG  . TRP C 26  ? 0.8842 0.6620 0.7257 0.1980  -0.3079 -0.2550 90  TRP C CG  
5692  C CD1 . TRP C 26  ? 0.8839 0.6470 0.7112 0.2114  -0.3160 -0.2665 90  TRP C CD1 
5693  C CD2 . TRP C 26  ? 0.8790 0.6463 0.7179 0.1846  -0.3107 -0.2412 90  TRP C CD2 
5694  N NE1 . TRP C 26  ? 0.8810 0.6243 0.6968 0.2073  -0.3240 -0.2615 90  TRP C NE1 
5695  C CE2 . TRP C 26  ? 0.9480 0.6933 0.7713 0.1907  -0.3213 -0.2461 90  TRP C CE2 
5696  C CE3 . TRP C 26  ? 0.8653 0.6402 0.7130 0.1699  -0.3059 -0.2264 90  TRP C CE3 
5697  C CZ2 . TRP C 26  ? 1.0507 0.7820 0.8695 0.1811  -0.3271 -0.2362 90  TRP C CZ2 
5698  C CZ3 . TRP C 26  ? 0.9514 0.7141 0.7951 0.1604  -0.3108 -0.2160 90  TRP C CZ3 
5699  C CH2 . TRP C 26  ? 1.0192 0.7603 0.8497 0.1653  -0.3216 -0.2207 90  TRP C CH2 
5700  N N   . VAL C 27  ? 0.8938 0.7077 0.7691 0.1892  -0.3061 -0.2426 91  VAL C N   
5701  C CA  . VAL C 27  ? 0.9003 0.7349 0.7873 0.1904  -0.2989 -0.2452 91  VAL C CA  
5702  C C   . VAL C 27  ? 0.8038 0.6574 0.6991 0.1802  -0.2835 -0.2387 91  VAL C C   
5703  O O   . VAL C 27  ? 0.7477 0.5958 0.6388 0.1702  -0.2827 -0.2264 91  VAL C O   
5704  C CB  . VAL C 27  ? 0.9538 0.7786 0.8382 0.1916  -0.3130 -0.2391 91  VAL C CB  
5705  C CG1 . VAL C 27  ? 0.9861 0.7826 0.8589 0.1972  -0.3323 -0.2392 91  VAL C CG1 
5706  C CG2 . VAL C 27  ? 0.9515 0.7786 0.8356 0.1798  -0.3115 -0.2221 91  VAL C CG2 
5707  N N   . PRO C 28  ? 0.8204 0.6962 0.7285 0.1829  -0.2720 -0.2472 92  PRO C N   
5708  C CA  . PRO C 28  ? 0.7690 0.6620 0.6858 0.1746  -0.2588 -0.2430 92  PRO C CA  
5709  C C   . PRO C 28  ? 0.7329 0.6272 0.6480 0.1699  -0.2627 -0.2325 92  PRO C C   
5710  O O   . PRO C 28  ? 0.8946 0.7869 0.8086 0.1751  -0.2715 -0.2332 92  PRO C O   
5711  C CB  . PRO C 28  ? 0.6633 0.5769 0.5958 0.1803  -0.2500 -0.2557 92  PRO C CB  
5712  C CG  . PRO C 28  ? 0.7082 0.6178 0.6407 0.1916  -0.2600 -0.2649 92  PRO C CG  
5713  C CD  . PRO C 28  ? 0.7610 0.6469 0.6775 0.1944  -0.2718 -0.2618 92  PRO C CD  
5714  N N   . THR C 29  ? 0.7637 0.6615 0.6775 0.1609  -0.2566 -0.2223 93  THR C N   
5715  C CA  . THR C 29  ? 0.8501 0.7528 0.7616 0.1574  -0.2583 -0.2116 93  THR C CA  
5716  C C   . THR C 29  ? 0.7942 0.7166 0.7149 0.1567  -0.2477 -0.2157 93  THR C C   
5717  O O   . THR C 29  ? 0.8576 0.7877 0.7767 0.1578  -0.2487 -0.2112 93  THR C O   
5718  C CB  . THR C 29  ? 0.9473 0.8401 0.8505 0.1484  -0.2614 -0.1949 93  THR C CB  
5719  O OG1 . THR C 29  ? 0.9387 0.8300 0.8427 0.1427  -0.2542 -0.1948 93  THR C OG1 
5720  C CG2 . THR C 29  ? 0.9876 0.8597 0.8826 0.1488  -0.2762 -0.1886 93  THR C CG2 
5721  N N   . TYR C 30  ? 0.7477 0.6775 0.6774 0.1555  -0.2382 -0.2240 94  TYR C N   
5722  C CA  . TYR C 30  ? 0.7043 0.6498 0.6442 0.1543  -0.2299 -0.2283 94  TYR C CA  
5723  C C   . TYR C 30  ? 0.7520 0.7049 0.7048 0.1544  -0.2219 -0.2387 94  TYR C C   
5724  O O   . TYR C 30  ? 1.0115 0.9582 0.9621 0.1534  -0.2190 -0.2395 94  TYR C O   
5725  C CB  . TYR C 30  ? 0.7790 0.7263 0.7145 0.1471  -0.2245 -0.2182 94  TYR C CB  
5726  C CG  . TYR C 30  ? 0.8309 0.7913 0.7770 0.1461  -0.2167 -0.2241 94  TYR C CG  
5727  C CD1 . TYR C 30  ? 0.9678 0.9381 0.9170 0.1509  -0.2190 -0.2278 94  TYR C CD1 
5728  C CD2 . TYR C 30  ? 0.8120 0.7734 0.7646 0.1410  -0.2082 -0.2265 94  TYR C CD2 
5729  C CE1 . TYR C 30  ? 0.9356 0.9152 0.8953 0.1505  -0.2145 -0.2344 94  TYR C CE1 
5730  C CE2 . TYR C 30  ? 0.8250 0.7961 0.7887 0.1395  -0.2029 -0.2316 94  TYR C CE2 
5731  C CZ  . TYR C 30  ? 0.9094 0.8888 0.8770 0.1442  -0.2067 -0.2358 94  TYR C CZ  
5732  O OH  . TYR C 30  ? 1.1351 1.1213 1.1137 0.1430  -0.2038 -0.2413 94  TYR C OH  
5733  N N   . ARG C 31  ? 0.6376 0.6042 0.6041 0.1557  -0.2185 -0.2460 95  ARG C N   
5734  C CA  . ARG C 31  ? 0.6804 0.6570 0.6634 0.1551  -0.2112 -0.2547 95  ARG C CA  
5735  C C   . ARG C 31  ? 0.7278 0.7148 0.7226 0.1524  -0.2084 -0.2573 95  ARG C C   
5736  O O   . ARG C 31  ? 0.8454 0.8362 0.8415 0.1567  -0.2149 -0.2603 95  ARG C O   
5737  C CB  . ARG C 31  ? 0.7581 0.7399 0.7499 0.1632  -0.2158 -0.2645 95  ARG C CB  
5738  C CG  . ARG C 31  ? 1.0043 1.0014 1.0174 0.1630  -0.2083 -0.2728 95  ARG C CG  
5739  C CD  . ARG C 31  ? 1.1411 1.1429 1.1601 0.1717  -0.2116 -0.2811 95  ARG C CD  
5740  N NE  . ARG C 31  ? 1.1317 1.1335 1.1517 0.1789  -0.2231 -0.2862 95  ARG C NE  
5741  C CZ  . ARG C 31  ? 0.8227 0.8319 0.8528 0.1873  -0.2278 -0.2955 95  ARG C CZ  
5742  N NH1 . ARG C 31  ? 0.8951 0.9145 0.9360 0.1899  -0.2208 -0.3005 95  ARG C NH1 
5743  N NH2 . ARG C 31  ? 0.7735 0.7813 0.8029 0.1940  -0.2392 -0.2997 95  ARG C NH2 
5744  N N   . GLY C 32  ? 0.8305 0.8206 0.8325 0.1457  -0.1996 -0.2560 96  GLY C N   
5745  C CA  . GLY C 32  ? 0.9401 0.9378 0.9549 0.1428  -0.1983 -0.2590 96  GLY C CA  
5746  C C   . GLY C 32  ? 0.8361 0.8461 0.8731 0.1454  -0.2005 -0.2694 96  GLY C C   
5747  O O   . GLY C 32  ? 0.9637 0.9791 1.0086 0.1481  -0.1991 -0.2735 96  GLY C O   
5748  N N   . GLU C 33  ? 0.7648 0.7795 0.8126 0.1453  -0.2047 -0.2741 97  GLU C N   
5749  C CA  . GLU C 33  ? 1.0251 1.0513 1.0962 0.1475  -0.2090 -0.2840 97  GLU C CA  
5750  C C   . GLU C 33  ? 1.0906 1.1262 1.1841 0.1396  -0.1999 -0.2839 97  GLU C C   
5751  O O   . GLU C 33  ? 1.4418 1.4900 1.5580 0.1403  -0.2011 -0.2903 97  GLU C O   
5752  C CB  . GLU C 33  ? 1.2603 1.2871 1.3354 0.1513  -0.2191 -0.2904 97  GLU C CB  
5753  C CG  . GLU C 33  ? 1.5520 1.5871 1.6415 0.1587  -0.2293 -0.3014 97  GLU C CG  
5754  C CD  . GLU C 33  ? 1.8481 1.8800 1.9209 0.1679  -0.2348 -0.3018 97  GLU C CD  
5755  O OE1 . GLU C 33  ? 2.0809 2.1034 2.1291 0.1705  -0.2353 -0.2945 97  GLU C OE1 
5756  O OE2 . GLU C 33  ? 1.3882 1.4273 1.4734 0.1726  -0.2390 -0.3089 97  GLU C OE2 
5757  N N   . GLY C 34  ? 0.9480 0.9784 1.0356 0.1322  -0.1907 -0.2756 98  GLY C N   
5758  C CA  . GLY C 34  ? 0.9635 1.0029 1.0696 0.1245  -0.1806 -0.2729 98  GLY C CA  
5759  C C   . GLY C 34  ? 0.9399 0.9856 1.0437 0.1271  -0.1724 -0.2713 98  GLY C C   
5760  O O   . GLY C 34  ? 0.9082 0.9645 1.0261 0.1223  -0.1625 -0.2682 98  GLY C O   
5761  N N   . THR C 35  ? 0.9329 0.9721 1.0186 0.1352  -0.1769 -0.2732 99  THR C N   
5762  C CA  . THR C 35  ? 0.9990 1.0406 1.0778 0.1399  -0.1712 -0.2728 99  THR C CA  
5763  C C   . THR C 35  ? 0.9539 1.0126 1.0536 0.1457  -0.1727 -0.2813 99  THR C C   
5764  O O   . THR C 35  ? 1.1744 1.2399 1.2733 0.1513  -0.1677 -0.2830 99  THR C O   
5765  C CB  . THR C 35  ? 0.8946 0.9197 0.9463 0.1463  -0.1777 -0.2713 99  THR C CB  
5766  O OG1 . THR C 35  ? 0.9935 1.0173 1.0450 0.1525  -0.1894 -0.2769 99  THR C OG1 
5767  C CG2 . THR C 35  ? 1.0013 1.0111 1.0339 0.1406  -0.1769 -0.2622 99  THR C CG2 
5768  N N   . THR C 36  ? 0.8265 0.8922 0.9444 0.1455  -0.1805 -0.2873 100 THR C N   
5769  C CA  . THR C 36  ? 1.1142 1.1967 1.2544 0.1514  -0.1846 -0.2965 100 THR C CA  
5770  C C   . THR C 36  ? 1.1726 1.2703 1.3458 0.1440  -0.1845 -0.2986 100 THR C C   
5771  O O   . THR C 36  ? 1.1843 1.3012 1.3815 0.1411  -0.1763 -0.2980 100 THR C O   
5772  C CB  . THR C 36  ? 1.1410 1.2155 1.2703 0.1614  -0.1990 -0.3037 100 THR C CB  
5773  O OG1 . THR C 36  ? 1.3588 1.4203 1.4760 0.1593  -0.2065 -0.3019 100 THR C OG1 
5774  C CG2 . THR C 36  ? 1.2382 1.3008 1.3422 0.1692  -0.2004 -0.3024 100 THR C CG2 
5775  N N   . GLY C 37  ? 1.1867 1.2763 1.3614 0.1413  -0.1940 -0.3007 101 GLY C N   
5776  C CA  . GLY C 37  ? 1.0869 1.1856 1.2911 0.1333  -0.1963 -0.3022 101 GLY C CA  
5777  C C   . GLY C 37  ? 1.2096 1.3004 1.4121 0.1222  -0.1894 -0.2929 101 GLY C C   
5778  O O   . GLY C 37  ? 0.9958 1.0783 1.1777 0.1199  -0.1796 -0.2845 101 GLY C O   
5779  N N   . LYS C 38  ? 1.1104 1.2028 1.3354 0.1157  -0.1959 -0.2950 102 LYS C N   
5780  C CA  . LYS C 38  ? 0.9491 1.0327 1.1754 0.1054  -0.1923 -0.2872 102 LYS C CA  
5781  C C   . LYS C 38  ? 0.8880 0.9515 1.0901 0.1093  -0.2017 -0.2896 102 LYS C C   
5782  O O   . LYS C 38  ? 0.9458 1.0051 1.1372 0.1188  -0.2126 -0.2979 102 LYS C O   
5783  C CB  . LYS C 38  ? 0.9717 1.0665 1.2368 0.0958  -0.1956 -0.2875 102 LYS C CB  
5784  C CG  . LYS C 38  ? 1.2369 1.3540 1.5267 0.0894  -0.1822 -0.2805 102 LYS C CG  
5785  C CD  . LYS C 38  ? 1.4899 1.6143 1.8157 0.0759  -0.1834 -0.2750 102 LYS C CD  
5786  C CE  . LYS C 38  ? 1.3952 1.5386 1.7368 0.0674  -0.1651 -0.2619 102 LYS C CE  
5787  N NZ  . LYS C 38  ? 1.4560 1.6000 1.8259 0.0522  -0.1658 -0.2527 102 LYS C NZ  
5788  N N   . ILE C 39  ? 0.8502 0.9025 1.0428 0.1027  -0.1971 -0.2820 103 ILE C N   
5789  C CA  . ILE C 39  ? 0.8173 0.8531 0.9873 0.1070  -0.2045 -0.2835 103 ILE C CA  
5790  C C   . ILE C 39  ? 0.9698 1.0007 1.1572 0.1053  -0.2178 -0.2904 103 ILE C C   
5791  O O   . ILE C 39  ? 0.9593 0.9929 1.1721 0.0952  -0.2172 -0.2874 103 ILE C O   
5792  C CB  . ILE C 39  ? 0.8282 0.8536 0.9797 0.1015  -0.1943 -0.2727 103 ILE C CB  
5793  C CG1 . ILE C 39  ? 0.6708 0.7007 0.8106 0.1008  -0.1809 -0.2653 103 ILE C CG1 
5794  C CG2 . ILE C 39  ? 0.8206 0.8320 0.9471 0.1076  -0.2009 -0.2738 103 ILE C CG2 
5795  C CD1 . ILE C 39  ? 0.5652 0.5868 0.6746 0.1083  -0.1807 -0.2637 103 ILE C CD1 
5796  N N   . PRO C 40  ? 1.0866 1.1099 1.2599 0.1157  -0.2304 -0.2991 104 PRO C N   
5797  C CA  . PRO C 40  ? 0.9804 0.9950 1.1623 0.1178  -0.2454 -0.3074 104 PRO C CA  
5798  C C   . PRO C 40  ? 1.0204 1.0225 1.1992 0.1108  -0.2432 -0.3010 104 PRO C C   
5799  O O   . PRO C 40  ? 1.0144 1.0109 1.1696 0.1109  -0.2337 -0.2931 104 PRO C O   
5800  C CB  . PRO C 40  ? 0.9747 0.9846 1.1299 0.1330  -0.2543 -0.3149 104 PRO C CB  
5801  C CG  . PRO C 40  ? 0.8532 0.8719 0.9972 0.1376  -0.2476 -0.3128 104 PRO C CG  
5802  C CD  . PRO C 40  ? 0.9745 0.9974 1.1213 0.1273  -0.2315 -0.3014 104 PRO C CD  
5803  N N   . ASP C 41  ? 1.0708 1.0677 1.2739 0.1048  -0.2532 -0.3046 105 ASP C N   
5804  C CA  . ASP C 41  ? 1.2901 1.2747 1.4955 0.0960  -0.2515 -0.2975 105 ASP C CA  
5805  C C   . ASP C 41  ? 1.3055 1.2762 1.4812 0.1054  -0.2556 -0.2997 105 ASP C C   
5806  O O   . ASP C 41  ? 1.7101 1.6715 1.8783 0.0999  -0.2499 -0.2917 105 ASP C O   
5807  C CB  . ASP C 41  ? 1.3384 1.3189 1.5784 0.0871  -0.2638 -0.3005 105 ASP C CB  
5808  C CG  . ASP C 41  ? 1.7102 1.7082 1.9836 0.0768  -0.2585 -0.2964 105 ASP C CG  
5809  O OD1 . ASP C 41  ? 1.7477 1.7605 2.0171 0.0812  -0.2508 -0.2971 105 ASP C OD1 
5810  O OD2 . ASP C 41  ? 2.1669 2.1647 2.4716 0.0644  -0.2624 -0.2920 105 ASP C OD2 
5811  N N   . GLU C 42  ? 1.1290 1.0995 1.2874 0.1202  -0.2650 -0.3102 106 GLU C N   
5812  C CA  . GLU C 42  ? 1.0243 0.9857 1.1549 0.1313  -0.2688 -0.3127 106 GLU C CA  
5813  C C   . GLU C 42  ? 1.0784 1.0434 1.1829 0.1322  -0.2535 -0.3018 106 GLU C C   
5814  O O   . GLU C 42  ? 1.3089 1.2679 1.3941 0.1378  -0.2533 -0.3002 106 GLU C O   
5815  C CB  . GLU C 42  ? 1.0413 1.0027 1.1606 0.1483  -0.2837 -0.3267 106 GLU C CB  
5816  C CG  . GLU C 42  ? 1.3869 1.3607 1.4935 0.1565  -0.2804 -0.3280 106 GLU C CG  
5817  C CD  . GLU C 42  ? 2.1744 2.1534 2.3032 0.1578  -0.2916 -0.3382 106 GLU C CD  
5818  O OE1 . GLU C 42  ? 2.6920 2.6732 2.8509 0.1451  -0.2911 -0.3365 106 GLU C OE1 
5819  O OE2 . GLU C 42  ? 2.3767 2.3585 2.4931 0.1717  -0.3009 -0.3474 106 GLU C OE2 
5820  N N   . GLN C 43  ? 0.9098 0.8847 1.0146 0.1271  -0.2417 -0.2947 107 GLN C N   
5821  C CA  . GLN C 43  ? 0.8128 0.7892 0.8950 0.1268  -0.2288 -0.2842 107 GLN C CA  
5822  C C   . GLN C 43  ? 0.8226 0.7908 0.9034 0.1172  -0.2205 -0.2744 107 GLN C C   
5823  O O   . GLN C 43  ? 1.0364 0.9999 1.1364 0.1077  -0.2207 -0.2727 107 GLN C O   
5824  C CB  . GLN C 43  ? 0.8774 0.8636 0.9602 0.1246  -0.2204 -0.2802 107 GLN C CB  
5825  C CG  . GLN C 43  ? 0.9812 0.9741 1.0568 0.1357  -0.2275 -0.2875 107 GLN C CG  
5826  C CD  . GLN C 43  ? 1.0542 1.0533 1.1219 0.1354  -0.2195 -0.2820 107 GLN C CD  
5827  O OE1 . GLN C 43  ? 1.2372 1.2342 1.2960 0.1298  -0.2091 -0.2723 107 GLN C OE1 
5828  N NE2 . GLN C 43  ? 1.1867 1.1921 1.2568 0.1423  -0.2257 -0.2886 107 GLN C NE2 
5829  N N   . MET C 44  ? 0.8649 0.8312 0.9232 0.1199  -0.2141 -0.2675 108 MET C N   
5830  C CA  . MET C 44  ? 0.8117 0.7705 0.8647 0.1121  -0.2059 -0.2577 108 MET C CA  
5831  C C   . MET C 44  ? 0.7804 0.7430 0.8399 0.1023  -0.1941 -0.2497 108 MET C C   
5832  O O   . MET C 44  ? 0.6762 0.6469 0.7326 0.1045  -0.1906 -0.2497 108 MET C O   
5833  C CB  . MET C 44  ? 0.7382 0.6967 0.7668 0.1189  -0.2035 -0.2532 108 MET C CB  
5834  C CG  . MET C 44  ? 1.0648 1.0153 1.0857 0.1124  -0.1965 -0.2437 108 MET C CG  
5835  S SD  . MET C 44  ? 1.2849 1.2224 1.3137 0.1112  -0.2043 -0.2472 108 MET C SD  
5836  C CE  . MET C 44  ? 0.9312 0.8711 0.9407 0.1261  -0.2111 -0.2516 108 MET C CE  
5837  N N   . LEU C 45  ? 0.8045 0.7614 0.8730 0.0925  -0.1887 -0.2433 109 LEU C N   
5838  C CA  . LEU C 45  ? 0.8101 0.7712 0.8810 0.0850  -0.1765 -0.2350 109 LEU C CA  
5839  C C   . LEU C 45  ? 0.7950 0.7513 0.8414 0.0866  -0.1698 -0.2277 109 LEU C C   
5840  O O   . LEU C 45  ? 0.9697 0.9169 1.0048 0.0870  -0.1713 -0.2246 109 LEU C O   
5841  C CB  . LEU C 45  ? 0.8073 0.7642 0.8948 0.0741  -0.1727 -0.2289 109 LEU C CB  
5842  C CG  . LEU C 45  ? 0.7815 0.7413 0.8980 0.0694  -0.1805 -0.2339 109 LEU C CG  
5843  C CD1 . LEU C 45  ? 0.8031 0.7551 0.9317 0.0581  -0.1773 -0.2247 109 LEU C CD1 
5844  C CD2 . LEU C 45  ? 0.6474 0.6237 0.7814 0.0690  -0.1777 -0.2371 109 LEU C CD2 
5845  N N   . THR C 46  ? 0.8021 0.7639 0.8407 0.0879  -0.1635 -0.2253 110 THR C N   
5846  C CA  . THR C 46  ? 0.7252 0.6813 0.7415 0.0898  -0.1599 -0.2190 110 THR C CA  
5847  C C   . THR C 46  ? 0.8013 0.7552 0.8125 0.0852  -0.1502 -0.2121 110 THR C C   
5848  O O   . THR C 46  ? 0.8463 0.8076 0.8692 0.0826  -0.1446 -0.2124 110 THR C O   
5849  C CB  . THR C 46  ? 0.7292 0.6898 0.7349 0.0970  -0.1634 -0.2214 110 THR C CB  
5850  O OG1 . THR C 46  ? 0.8439 0.8114 0.8560 0.0976  -0.1603 -0.2239 110 THR C OG1 
5851  C CG2 . THR C 46  ? 0.9710 0.9360 0.9789 0.1036  -0.1724 -0.2281 110 THR C CG2 
5852  N N   . ARG C 47  ? 0.8527 0.7975 0.8459 0.0850  -0.1485 -0.2060 111 ARG C N   
5853  C CA  . ARG C 47  ? 0.7061 0.6469 0.6888 0.0832  -0.1409 -0.2002 111 ARG C CA  
5854  C C   . ARG C 47  ? 0.6344 0.5668 0.5971 0.0862  -0.1439 -0.1966 111 ARG C C   
5855  O O   . ARG C 47  ? 0.8011 0.7309 0.7597 0.0874  -0.1497 -0.1959 111 ARG C O   
5856  C CB  . ARG C 47  ? 0.7153 0.6514 0.7021 0.0765  -0.1347 -0.1942 111 ARG C CB  
5857  C CG  . ARG C 47  ? 0.6446 0.5677 0.6174 0.0747  -0.1358 -0.1883 111 ARG C CG  
5858  C CD  . ARG C 47  ? 0.6942 0.6122 0.6639 0.0695  -0.1272 -0.1805 111 ARG C CD  
5859  N NE  . ARG C 47  ? 0.8773 0.7814 0.8308 0.0688  -0.1288 -0.1748 111 ARG C NE  
5860  C CZ  . ARG C 47  ? 0.9647 0.8619 0.8987 0.0723  -0.1294 -0.1725 111 ARG C CZ  
5861  N NH1 . ARG C 47  ? 0.8034 0.7044 0.7303 0.0769  -0.1289 -0.1752 111 ARG C NH1 
5862  N NH2 . ARG C 47  ? 1.1695 1.0547 1.0912 0.0716  -0.1319 -0.1677 111 ARG C NH2 
5863  N N   . GLN C 48  ? 0.6282 0.5569 0.5791 0.0878  -0.1407 -0.1943 112 GLN C N   
5864  C CA  . GLN C 48  ? 0.6742 0.5929 0.6071 0.0897  -0.1450 -0.1903 112 GLN C CA  
5865  C C   . GLN C 48  ? 0.6541 0.5758 0.5864 0.0931  -0.1530 -0.1920 112 GLN C C   
5866  O O   . GLN C 48  ? 0.7220 0.6385 0.6455 0.0931  -0.1582 -0.1873 112 GLN C O   
5867  C CB  . GLN C 48  ? 0.6244 0.5334 0.5489 0.0864  -0.1453 -0.1841 112 GLN C CB  
5868  C CG  . GLN C 48  ? 0.9368 0.8424 0.8536 0.0878  -0.1533 -0.1811 112 GLN C CG  
5869  C CD  . GLN C 48  ? 0.9920 0.8856 0.8942 0.0868  -0.1552 -0.1753 112 GLN C CD  
5870  O OE1 . GLN C 48  ? 1.0074 0.9005 0.9069 0.0869  -0.1620 -0.1714 112 GLN C OE1 
5871  N NE2 . GLN C 48  ? 0.8278 0.7137 0.7215 0.0862  -0.1509 -0.1738 112 GLN C NE2 
5872  N N   . ASN C 49  ? 0.6725 0.6033 0.6148 0.0960  -0.1541 -0.1979 113 ASN C N   
5873  C CA  . ASN C 49  ? 0.6481 0.5817 0.5886 0.0999  -0.1614 -0.1990 113 ASN C CA  
5874  C C   . ASN C 49  ? 0.6565 0.5806 0.5830 0.1011  -0.1665 -0.1944 113 ASN C C   
5875  O O   . ASN C 49  ? 0.5961 0.5125 0.5146 0.1022  -0.1650 -0.1949 113 ASN C O   
5876  C CB  . ASN C 49  ? 0.6426 0.5852 0.5939 0.1036  -0.1617 -0.2065 113 ASN C CB  
5877  C CG  . ASN C 49  ? 0.7884 0.7403 0.7560 0.1025  -0.1601 -0.2115 113 ASN C CG  
5878  O OD1 . ASN C 49  ? 0.7015 0.6587 0.6734 0.1055  -0.1656 -0.2145 113 ASN C OD1 
5879  N ND2 . ASN C 49  ? 0.6919 0.6453 0.6685 0.0983  -0.1532 -0.2119 113 ASN C ND2 
5880  N N   . PHE C 50  ? 0.6358 0.5604 0.5594 0.1012  -0.1729 -0.1895 114 PHE C N   
5881  C CA  . PHE C 50  ? 0.7008 0.6172 0.6155 0.1020  -0.1803 -0.1852 114 PHE C CA  
5882  C C   . PHE C 50  ? 0.6430 0.5657 0.5597 0.1031  -0.1864 -0.1808 114 PHE C C   
5883  O O   . PHE C 50  ? 0.8510 0.7852 0.7742 0.1048  -0.1847 -0.1823 114 PHE C O   
5884  C CB  . PHE C 50  ? 0.7531 0.6579 0.6580 0.0986  -0.1823 -0.1789 114 PHE C CB  
5885  C CG  . PHE C 50  ? 0.6959 0.6050 0.6025 0.0951  -0.1824 -0.1720 114 PHE C CG  
5886  C CD1 . PHE C 50  ? 0.7498 0.6608 0.6586 0.0935  -0.1761 -0.1732 114 PHE C CD1 
5887  C CD2 . PHE C 50  ? 0.6669 0.5781 0.5734 0.0934  -0.1892 -0.1635 114 PHE C CD2 
5888  C CE1 . PHE C 50  ? 0.8159 0.7308 0.7258 0.0918  -0.1769 -0.1677 114 PHE C CE1 
5889  C CE2 . PHE C 50  ? 0.7641 0.6820 0.6731 0.0911  -0.1888 -0.1568 114 PHE C CE2 
5890  C CZ  . PHE C 50  ? 0.7895 0.7092 0.6997 0.0910  -0.1828 -0.1598 114 PHE C CZ  
5891  N N   . VAL C 51  ? 0.5783 0.4932 0.4891 0.1025  -0.1943 -0.1751 115 VAL C N   
5892  C CA  . VAL C 51  ? 0.5713 0.4928 0.4838 0.1031  -0.1999 -0.1687 115 VAL C CA  
5893  C C   . VAL C 51  ? 0.5994 0.5151 0.5086 0.0980  -0.2061 -0.1567 115 VAL C C   
5894  O O   . VAL C 51  ? 0.7670 0.6678 0.6705 0.0957  -0.2111 -0.1556 115 VAL C O   
5895  C CB  . VAL C 51  ? 0.5481 0.4658 0.4598 0.1075  -0.2057 -0.1728 115 VAL C CB  
5896  C CG1 . VAL C 51  ? 0.5085 0.4310 0.4201 0.1075  -0.2121 -0.1637 115 VAL C CG1 
5897  C CG2 . VAL C 51  ? 0.5932 0.5193 0.5114 0.1124  -0.2002 -0.1842 115 VAL C CG2 
5898  N N   . SER C 52  ? 0.5876 0.5159 0.5004 0.0968  -0.2063 -0.1478 116 SER C N   
5899  C CA  . SER C 52  ? 0.7443 0.6725 0.6581 0.0912  -0.2120 -0.1338 116 SER C CA  
5900  C C   . SER C 52  ? 0.7226 0.6644 0.6395 0.0923  -0.2140 -0.1244 116 SER C C   
5901  O O   . SER C 52  ? 0.6738 0.6302 0.5915 0.0979  -0.2083 -0.1280 116 SER C O   
5902  C CB  . SER C 52  ? 0.7639 0.6989 0.6803 0.0885  -0.2071 -0.1302 116 SER C CB  
5903  O OG  . SER C 52  ? 0.9874 0.9247 0.9079 0.0825  -0.2129 -0.1160 116 SER C OG  
5904  N N   . CYS C 53  ? 0.7718 0.7085 0.6900 0.0871  -0.2228 -0.1118 117 CYS C N   
5905  C CA  . CYS C 53  ? 0.8418 0.7918 0.7622 0.0879  -0.2242 -0.1007 117 CYS C CA  
5906  C C   . CYS C 53  ? 0.8271 0.7931 0.7548 0.0825  -0.2234 -0.0832 117 CYS C C   
5907  O O   . CYS C 53  ? 1.1385 1.0983 1.0713 0.0753  -0.2277 -0.0763 117 CYS C O   
5908  C CB  . CYS C 53  ? 0.9122 0.8468 0.8296 0.0871  -0.2349 -0.0987 117 CYS C CB  
5909  S SG  . CYS C 53  ? 1.3314 1.2543 1.2423 0.0956  -0.2342 -0.1194 117 CYS C SG  
5910  N N   . SER C 54  ? 0.8176 0.8055 0.7457 0.0871  -0.2177 -0.0764 118 SER C N   
5911  C CA  . SER C 54  ? 0.8063 0.8134 0.7419 0.0828  -0.2170 -0.0565 118 SER C CA  
5912  C C   . SER C 54  ? 0.9777 0.9814 0.9136 0.0791  -0.2250 -0.0429 118 SER C C   
5913  O O   . SER C 54  ? 1.2078 1.1916 1.1382 0.0798  -0.2324 -0.0501 118 SER C O   
5914  C CB  . SER C 54  ? 0.8190 0.8543 0.7532 0.0918  -0.2056 -0.0563 118 SER C CB  
5915  O OG  . SER C 54  ? 0.9332 0.9791 0.8594 0.1007  -0.2030 -0.0574 118 SER C OG  
5916  N N   . ASP C 55  ? 1.0305 1.0541 0.9735 0.0754  -0.2236 -0.0225 119 ASP C N   
5917  C CA  . ASP C 55  ? 1.2068 1.2281 1.1512 0.0707  -0.2313 -0.0061 119 ASP C CA  
5918  C C   . ASP C 55  ? 1.1875 1.2209 1.1203 0.0818  -0.2259 -0.0087 119 ASP C C   
5919  O O   . ASP C 55  ? 1.6283 1.6581 1.5583 0.0804  -0.2319 0.0021  119 ASP C O   
5920  C CB  . ASP C 55  ? 1.7375 1.7766 1.6969 0.0606  -0.2321 0.0196  119 ASP C CB  
5921  C CG  . ASP C 55  ? 1.9185 1.9924 1.8813 0.0664  -0.2180 0.0249  119 ASP C CG  
5922  O OD1 . ASP C 55  ? 1.9766 2.0624 1.9280 0.0795  -0.2082 0.0114  119 ASP C OD1 
5923  O OD2 . ASP C 55  ? 2.1021 2.1918 2.0801 0.0582  -0.2176 0.0426  119 ASP C OD2 
5924  N N   . LYS C 56  ? 1.2280 1.2742 1.1536 0.0930  -0.2158 -0.0236 120 LYS C N   
5925  C CA  . LYS C 56  ? 1.1055 1.1663 1.0194 0.1058  -0.2101 -0.0283 120 LYS C CA  
5926  C C   . LYS C 56  ? 1.0480 1.0902 0.9536 0.1129  -0.2130 -0.0513 120 LYS C C   
5927  O O   . LYS C 56  ? 1.2516 1.2942 1.1482 0.1206  -0.2149 -0.0545 120 LYS C O   
5928  C CB  . LYS C 56  ? 1.2923 1.3809 1.2051 0.1145  -0.1983 -0.0294 120 LYS C CB  
5929  C CG  . LYS C 56  ? 1.7497 1.8543 1.6485 0.1307  -0.1926 -0.0377 120 LYS C CG  
5930  C CD  . LYS C 56  ? 1.5016 1.6292 1.3984 0.1412  -0.1829 -0.0435 120 LYS C CD  
5931  C CE  . LYS C 56  ? 2.0923 2.2472 1.9966 0.1383  -0.1764 -0.0216 120 LYS C CE  
5932  N NZ  . LYS C 56  ? 2.4666 2.6157 2.3870 0.1251  -0.1778 -0.0160 120 LYS C NZ  
5933  N N   . GLU C 57  ? 1.0361 1.0629 0.9453 0.1104  -0.2135 -0.0665 121 GLU C N   
5934  C CA  . GLU C 57  ? 1.0240 1.0391 0.9286 0.1173  -0.2136 -0.0884 121 GLU C CA  
5935  C C   . GLU C 57  ? 0.9861 0.9848 0.8959 0.1119  -0.2140 -0.0994 121 GLU C C   
5936  O O   . GLU C 57  ? 0.8699 0.8691 0.7851 0.1051  -0.2127 -0.0925 121 GLU C O   
5937  C CB  . GLU C 57  ? 1.0692 1.1022 0.9693 0.1288  -0.2058 -0.0983 121 GLU C CB  
5938  C CG  . GLU C 57  ? 1.1403 1.1782 1.0453 0.1281  -0.1993 -0.1045 121 GLU C CG  
5939  C CD  . GLU C 57  ? 1.2658 1.3225 1.1661 0.1400  -0.1932 -0.1115 121 GLU C CD  
5940  O OE1 . GLU C 57  ? 1.4353 1.4979 1.3279 0.1501  -0.1942 -0.1175 121 GLU C OE1 
5941  O OE2 . GLU C 57  ? 1.1388 1.2031 1.0427 0.1399  -0.1884 -0.1117 121 GLU C OE2 
5942  N N   . CYS C 58  ? 0.9046 0.8909 0.8127 0.1157  -0.2153 -0.1162 122 CYS C N   
5943  C CA  . CYS C 58  ? 0.8389 0.8116 0.7504 0.1122  -0.2140 -0.1273 122 CYS C CA  
5944  C C   . CYS C 58  ? 0.6752 0.6562 0.5884 0.1178  -0.2063 -0.1406 122 CYS C C   
5945  O O   . CYS C 58  ? 0.6626 0.6515 0.5744 0.1257  -0.2054 -0.1484 122 CYS C O   
5946  C CB  . CYS C 58  ? 0.8363 0.7900 0.7464 0.1121  -0.2207 -0.1354 122 CYS C CB  
5947  S SG  . CYS C 58  ? 1.3828 1.3210 1.2914 0.1047  -0.2326 -0.1207 122 CYS C SG  
5948  N N   . ARG C 59  ? 0.5923 0.5705 0.5086 0.1139  -0.2020 -0.1431 123 ARG C N   
5949  C CA  . ARG C 59  ? 0.5776 0.5617 0.4965 0.1182  -0.1959 -0.1544 123 ARG C CA  
5950  C C   . ARG C 59  ? 0.5745 0.5454 0.4965 0.1151  -0.1942 -0.1644 123 ARG C C   
5951  O O   . ARG C 59  ? 0.6611 0.6193 0.5814 0.1095  -0.1963 -0.1612 123 ARG C O   
5952  C CB  . ARG C 59  ? 0.5875 0.5829 0.5070 0.1181  -0.1917 -0.1482 123 ARG C CB  
5953  C CG  . ARG C 59  ? 0.6777 0.6917 0.5940 0.1234  -0.1914 -0.1383 123 ARG C CG  
5954  C CD  . ARG C 59  ? 0.7260 0.7552 0.6427 0.1275  -0.1866 -0.1360 123 ARG C CD  
5955  N NE  . ARG C 59  ? 0.7466 0.7766 0.6632 0.1350  -0.1846 -0.1511 123 ARG C NE  
5956  C CZ  . ARG C 59  ? 0.6118 0.6506 0.5244 0.1455  -0.1855 -0.1588 123 ARG C CZ  
5957  N NH1 . ARG C 59  ? 0.6704 0.7194 0.5771 0.1506  -0.1870 -0.1526 123 ARG C NH1 
5958  N NH2 . ARG C 59  ? 0.6210 0.6574 0.5355 0.1509  -0.1858 -0.1724 123 ARG C NH2 
5959  N N   . ARG C 60  ? 0.5247 0.4985 0.4515 0.1190  -0.1910 -0.1763 124 ARG C N   
5960  C CA  . ARG C 60  ? 0.5629 0.5271 0.4942 0.1157  -0.1876 -0.1843 124 ARG C CA  
5961  C C   . ARG C 60  ? 0.6608 0.6258 0.5943 0.1136  -0.1830 -0.1851 124 ARG C C   
5962  O O   . ARG C 60  ? 0.9948 0.9678 0.9316 0.1180  -0.1825 -0.1896 124 ARG C O   
5963  C CB  . ARG C 60  ? 0.4852 0.4515 0.4236 0.1197  -0.1879 -0.1956 124 ARG C CB  
5964  C CG  . ARG C 60  ? 0.5515 0.5153 0.4989 0.1172  -0.1828 -0.2036 124 ARG C CG  
5965  C CD  . ARG C 60  ? 0.6252 0.5921 0.5821 0.1202  -0.1839 -0.2132 124 ARG C CD  
5966  N NE  . ARG C 60  ? 0.6588 0.6269 0.6283 0.1174  -0.1792 -0.2196 124 ARG C NE  
5967  C CZ  . ARG C 60  ? 0.8944 0.8693 0.8774 0.1199  -0.1808 -0.2285 124 ARG C CZ  
5968  N NH1 . ARG C 60  ? 0.8933 0.8734 0.8768 0.1264  -0.1873 -0.2329 124 ARG C NH1 
5969  N NH2 . ARG C 60  ? 0.8285 0.8050 0.8254 0.1155  -0.1765 -0.2321 124 ARG C NH2 
5970  N N   . PHE C 61  ? 0.6191 0.5749 0.5497 0.1080  -0.1809 -0.1809 125 PHE C N   
5971  C CA  . PHE C 61  ? 0.6681 0.6228 0.6002 0.1061  -0.1772 -0.1814 125 PHE C CA  
5972  C C   . PHE C 61  ? 0.7348 0.6827 0.6720 0.1037  -0.1730 -0.1886 125 PHE C C   
5973  O O   . PHE C 61  ? 1.0415 0.9841 0.9784 0.1023  -0.1718 -0.1907 125 PHE C O   
5974  C CB  . PHE C 61  ? 0.5664 0.5155 0.4923 0.1017  -0.1778 -0.1721 125 PHE C CB  
5975  C CG  . PHE C 61  ? 0.6061 0.5656 0.5305 0.1031  -0.1810 -0.1629 125 PHE C CG  
5976  C CD1 . PHE C 61  ? 0.5392 0.5010 0.4620 0.1031  -0.1853 -0.1572 125 PHE C CD1 
5977  C CD2 . PHE C 61  ? 0.6055 0.5737 0.5307 0.1049  -0.1798 -0.1594 125 PHE C CD2 
5978  C CE1 . PHE C 61  ? 0.5521 0.5257 0.4750 0.1035  -0.1874 -0.1462 125 PHE C CE1 
5979  C CE2 . PHE C 61  ? 0.5794 0.5611 0.5046 0.1065  -0.1814 -0.1496 125 PHE C CE2 
5980  C CZ  . PHE C 61  ? 0.5484 0.5337 0.4730 0.1054  -0.1848 -0.1421 125 PHE C CZ  
5981  N N   . PHE C 62  ? 0.5775 0.5259 0.5198 0.1035  -0.1709 -0.1921 126 PHE C N   
5982  C CA  . PHE C 62  ? 0.6757 0.6178 0.6240 0.0994  -0.1664 -0.1958 126 PHE C CA  
5983  C C   . PHE C 62  ? 0.6854 0.6233 0.6361 0.0975  -0.1654 -0.1956 126 PHE C C   
5984  O O   . PHE C 62  ? 0.7475 0.6880 0.6949 0.1006  -0.1685 -0.1941 126 PHE C O   
5985  C CB  . PHE C 62  ? 0.7617 0.7099 0.7217 0.1013  -0.1665 -0.2039 126 PHE C CB  
5986  C CG  . PHE C 62  ? 0.8537 0.8093 0.8207 0.1063  -0.1714 -0.2101 126 PHE C CG  
5987  C CD1 . PHE C 62  ? 0.8874 0.8411 0.8638 0.1052  -0.1724 -0.2144 126 PHE C CD1 
5988  C CD2 . PHE C 62  ? 0.9507 0.9141 0.9138 0.1127  -0.1761 -0.2111 126 PHE C CD2 
5989  C CE1 . PHE C 62  ? 0.7841 0.7429 0.7656 0.1116  -0.1790 -0.2216 126 PHE C CE1 
5990  C CE2 . PHE C 62  ? 0.9694 0.9396 0.9361 0.1194  -0.1813 -0.2175 126 PHE C CE2 
5991  C CZ  . PHE C 62  ? 0.9294 0.8969 0.9050 0.1194  -0.1832 -0.2236 126 PHE C CZ  
5992  N N   . VAL C 63  ? 0.6074 0.5393 0.5637 0.0927  -0.1610 -0.1966 127 VAL C N   
5993  C CA  . VAL C 63  ? 0.6360 0.5615 0.5953 0.0901  -0.1610 -0.1959 127 VAL C CA  
5994  C C   . VAL C 63  ? 0.6868 0.6152 0.6631 0.0891  -0.1623 -0.2027 127 VAL C C   
5995  O O   . VAL C 63  ? 0.6754 0.6076 0.6607 0.0862  -0.1586 -0.2043 127 VAL C O   
5996  C CB  . VAL C 63  ? 0.7025 0.6176 0.6541 0.0846  -0.1553 -0.1891 127 VAL C CB  
5997  C CG1 . VAL C 63  ? 0.7349 0.6416 0.6914 0.0806  -0.1548 -0.1877 127 VAL C CG1 
5998  C CG2 . VAL C 63  ? 0.7739 0.6847 0.7104 0.0859  -0.1568 -0.1833 127 VAL C CG2 
5999  N N   . SER C 64  ? 0.7387 0.6655 0.7200 0.0919  -0.1686 -0.2069 128 SER C N   
6000  C CA  . SER C 64  ? 0.8438 0.7712 0.8422 0.0912  -0.1733 -0.2142 128 SER C CA  
6001  C C   . SER C 64  ? 0.9375 0.8564 0.9466 0.0821  -0.1699 -0.2101 128 SER C C   
6002  O O   . SER C 64  ? 1.1833 1.0923 1.1845 0.0785  -0.1673 -0.2034 128 SER C O   
6003  C CB  . SER C 64  ? 0.9917 0.9185 0.9899 0.0992  -0.1831 -0.2211 128 SER C CB  
6004  O OG  . SER C 64  ? 1.2832 1.1995 1.2760 0.0984  -0.1847 -0.2178 128 SER C OG  
6005  N N   . MET C 65  ? 0.8532 0.7765 0.8811 0.0781  -0.1703 -0.2134 129 MET C N   
6006  C CA  . MET C 65  ? 1.1279 1.0446 1.1712 0.0689  -0.1692 -0.2092 129 MET C CA  
6007  C C   . MET C 65  ? 1.2650 1.1767 1.3250 0.0698  -0.1819 -0.2172 129 MET C C   
6008  O O   . MET C 65  ? 1.4684 1.3738 1.5455 0.0614  -0.1838 -0.2140 129 MET C O   
6009  C CB  . MET C 65  ? 1.1516 1.0782 1.2073 0.0621  -0.1594 -0.2046 129 MET C CB  
6010  C CG  . MET C 65  ? 1.1174 1.0419 1.1598 0.0580  -0.1473 -0.1939 129 MET C CG  
6011  S SD  . MET C 65  ? 1.3160 1.2529 1.3476 0.0629  -0.1386 -0.1943 129 MET C SD  
6012  C CE  . MET C 65  ? 0.9657 0.9190 1.0243 0.0577  -0.1326 -0.1944 129 MET C CE  
6013  N N   . GLY C 66  ? 1.0174 0.9313 1.0720 0.0803  -0.1913 -0.2271 130 GLY C N   
6014  C CA  . GLY C 66  ? 0.9447 0.8537 1.0135 0.0837  -0.2053 -0.2371 130 GLY C CA  
6015  C C   . GLY C 66  ? 1.0018 0.9228 1.0831 0.0870  -0.2092 -0.2455 130 GLY C C   
6016  O O   . GLY C 66  ? 1.0366 0.9693 1.1175 0.0855  -0.2005 -0.2428 130 GLY C O   
6017  N N   . TYR C 67  ? 0.9761 0.8936 1.0677 0.0927  -0.2236 -0.2567 131 TYR C N   
6018  C CA  . TYR C 67  ? 0.9571 0.8847 1.0610 0.0966  -0.2294 -0.2656 131 TYR C CA  
6019  C C   . TYR C 67  ? 0.9980 0.9292 1.1310 0.0837  -0.2275 -0.2620 131 TYR C C   
6020  O O   . TYR C 67  ? 1.0826 1.0047 1.2296 0.0734  -0.2279 -0.2557 131 TYR C O   
6021  C CB  . TYR C 67  ? 1.0210 0.9426 1.1249 0.1083  -0.2470 -0.2796 131 TYR C CB  
6022  C CG  . TYR C 67  ? 1.2192 1.1405 1.2955 0.1225  -0.2487 -0.2830 131 TYR C CG  
6023  C CD1 . TYR C 67  ? 1.2812 1.2158 1.3399 0.1312  -0.2431 -0.2830 131 TYR C CD1 
6024  C CD2 . TYR C 67  ? 1.3465 1.2552 1.4151 0.1276  -0.2564 -0.2858 131 TYR C CD2 
6025  C CE1 . TYR C 67  ? 1.0893 1.0271 1.1247 0.1439  -0.2438 -0.2843 131 TYR C CE1 
6026  C CE2 . TYR C 67  ? 1.2774 1.1896 1.3222 0.1418  -0.2574 -0.2887 131 TYR C CE2 
6027  C CZ  . TYR C 67  ? 1.0737 1.0018 1.1027 0.1495  -0.2504 -0.2873 131 TYR C CZ  
6028  O OH  . TYR C 67  ? 1.1906 1.1252 1.1981 0.1630  -0.2504 -0.2883 131 TYR C OH  
6029  N N   . GLY C 68  ? 0.9478 0.8932 1.0909 0.0844  -0.2253 -0.2652 132 GLY C N   
6030  C CA  . GLY C 68  ? 1.1796 1.1338 1.3521 0.0729  -0.2218 -0.2611 132 GLY C CA  
6031  C C   . GLY C 68  ? 1.2244 1.1722 1.4260 0.0680  -0.2370 -0.2669 132 GLY C C   
6032  O O   . GLY C 68  ? 1.4827 1.4353 1.7117 0.0552  -0.2342 -0.2598 132 GLY C O   
6033  N N   . THR C 69  ? 0.9779 0.9154 1.1736 0.0785  -0.2538 -0.2796 133 THR C N   
6034  C CA  . THR C 69  ? 1.2170 1.1449 1.4382 0.0760  -0.2722 -0.2875 133 THR C CA  
6035  C C   . THR C 69  ? 1.3715 1.2797 1.5967 0.0689  -0.2782 -0.2823 133 THR C C   
6036  O O   . THR C 69  ? 1.4940 1.3944 1.7483 0.0590  -0.2891 -0.2816 133 THR C O   
6037  C CB  . THR C 69  ? 1.2634 1.1885 1.4760 0.0928  -0.2900 -0.3055 133 THR C CB  
6038  O OG1 . THR C 69  ? 1.8735 1.7853 2.1095 0.0911  -0.3106 -0.3142 133 THR C OG1 
6039  C CG2 . THR C 69  ? 0.8710 0.7898 1.0467 0.1082  -0.2903 -0.3100 133 THR C CG2 
6040  N N   . THR C 70  ? 1.3148 1.2147 1.5119 0.0737  -0.2718 -0.2782 134 THR C N   
6041  C CA  . THR C 70  ? 1.3309 1.2106 1.5269 0.0697  -0.2782 -0.2743 134 THR C CA  
6042  C C   . THR C 70  ? 1.4164 1.2965 1.6183 0.0538  -0.2622 -0.2558 134 THR C C   
6043  O O   . THR C 70  ? 1.5285 1.3917 1.7321 0.0476  -0.2661 -0.2496 134 THR C O   
6044  C CB  . THR C 70  ? 1.4018 1.2730 1.5645 0.0850  -0.2810 -0.2804 134 THR C CB  
6045  O OG1 . THR C 70  ? 1.3328 1.2118 1.4738 0.0837  -0.2621 -0.2692 134 THR C OG1 
6046  C CG2 . THR C 70  ? 1.5993 1.4770 1.7495 0.1028  -0.2910 -0.2962 134 THR C CG2 
6047  N N   . THR C 71  ? 1.1008 0.9997 1.3043 0.0484  -0.2449 -0.2476 135 THR C N   
6048  C CA  . THR C 71  ? 1.2365 1.1391 1.4419 0.0357  -0.2278 -0.2303 135 THR C CA  
6049  C C   . THR C 71  ? 1.3803 1.2936 1.6219 0.0214  -0.2254 -0.2225 135 THR C C   
6050  O O   . THR C 71  ? 1.5747 1.5048 1.8318 0.0225  -0.2252 -0.2278 135 THR C O   
6051  C CB  . THR C 71  ? 1.1643 1.0808 1.3454 0.0404  -0.2098 -0.2258 135 THR C CB  
6052  O OG1 . THR C 71  ? 0.9436 0.8511 1.0937 0.0515  -0.2111 -0.2298 135 THR C OG1 
6053  C CG2 . THR C 71  ? 1.1156 1.0375 1.2984 0.0289  -0.1924 -0.2090 135 THR C CG2 
6054  N N   . ASN C 72  ? 1.6659 1.5703 1.9215 0.0080  -0.2237 -0.2093 136 ASN C N   
6055  C CA  . ASN C 72  ? 1.8826 1.7999 2.1738 -0.0074 -0.2187 -0.1977 136 ASN C CA  
6056  C C   . ASN C 72  ? 2.0309 1.9649 2.3140 -0.0131 -0.1944 -0.1819 136 ASN C C   
6057  O O   . ASN C 72  ? 1.8208 1.7465 2.0748 -0.0102 -0.1851 -0.1758 136 ASN C O   
6058  C CB  . ASN C 72  ? 1.6481 1.5463 1.9632 -0.0197 -0.2324 -0.1911 136 ASN C CB  
6059  C CG  . ASN C 72  ? 1.6171 1.5299 1.9767 -0.0352 -0.2327 -0.1818 136 ASN C CG  
6060  O OD1 . ASN C 72  ? 1.9055 1.8414 2.2814 -0.0343 -0.2283 -0.1858 136 ASN C OD1 
6061  N ND2 . ASN C 72  ? 1.4051 1.3050 1.7858 -0.0499 -0.2381 -0.1685 136 ASN C ND2 
6062  N N   . PHE C 73  ? 2.2480 2.2062 2.5568 -0.0201 -0.1849 -0.1758 137 PHE C N   
6063  C CA  . PHE C 73  ? 2.0619 2.0400 2.3631 -0.0225 -0.1619 -0.1629 137 PHE C CA  
6064  C C   . PHE C 73  ? 2.4416 2.4123 2.7366 -0.0327 -0.1507 -0.1437 137 PHE C C   
6065  O O   . PHE C 73  ? 2.4366 2.4105 2.7040 -0.0283 -0.1353 -0.1372 137 PHE C O   
6066  C CB  . PHE C 73  ? 1.7928 1.8005 2.1268 -0.0273 -0.1550 -0.1606 137 PHE C CB  
6067  C CG  . PHE C 73  ? 2.0364 2.0666 2.3617 -0.0271 -0.1316 -0.1488 137 PHE C CG  
6068  C CD1 . PHE C 73  ? 1.9736 2.0093 2.2674 -0.0132 -0.1229 -0.1565 137 PHE C CD1 
6069  C CD2 . PHE C 73  ? 2.0769 2.1225 2.4249 -0.0402 -0.1187 -0.1298 137 PHE C CD2 
6070  C CE1 . PHE C 73  ? 2.0084 2.0630 2.2920 -0.0109 -0.1029 -0.1473 137 PHE C CE1 
6071  C CE2 . PHE C 73  ? 2.0497 2.1174 2.3871 -0.0376 -0.0966 -0.1196 137 PHE C CE2 
6072  C CZ  . PHE C 73  ? 2.0643 2.1357 2.3687 -0.0222 -0.0894 -0.1294 137 PHE C CZ  
6073  N N   . ALA C 74  ? 2.5898 2.5493 2.9103 -0.0459 -0.1599 -0.1347 138 ALA C N   
6074  C CA  . ALA C 74  ? 2.1986 2.1501 2.5176 -0.0574 -0.1510 -0.1144 138 ALA C CA  
6075  C C   . ALA C 74  ? 2.2132 2.1423 2.4901 -0.0498 -0.1490 -0.1140 138 ALA C C   
6076  O O   . ALA C 74  ? 1.9484 1.8764 2.2123 -0.0546 -0.1355 -0.0980 138 ALA C O   
6077  C CB  . ALA C 74  ? 1.6533 1.5922 2.0084 -0.0728 -0.1661 -0.1066 138 ALA C CB  
6078  N N   . ASP C 75  ? 2.5049 2.4178 2.7614 -0.0375 -0.1623 -0.1313 139 ASP C N   
6079  C CA  . ASP C 75  ? 2.3047 2.2002 2.5223 -0.0283 -0.1608 -0.1332 139 ASP C CA  
6080  C C   . ASP C 75  ? 2.1436 2.0541 2.3343 -0.0197 -0.1434 -0.1327 139 ASP C C   
6081  O O   . ASP C 75  ? 2.1983 2.1274 2.3920 -0.0136 -0.1392 -0.1409 139 ASP C O   
6082  C CB  . ASP C 75  ? 1.9518 1.8311 2.1571 -0.0163 -0.1789 -0.1518 139 ASP C CB  
6083  C CG  . ASP C 75  ? 2.0001 1.8580 2.2239 -0.0213 -0.1992 -0.1547 139 ASP C CG  
6084  O OD1 . ASP C 75  ? 2.0268 1.8769 2.2687 -0.0350 -0.1998 -0.1404 139 ASP C OD1 
6085  O OD2 . ASP C 75  ? 2.1041 1.9525 2.3236 -0.0109 -0.2152 -0.1713 139 ASP C OD2 
6086  N N   . LEU C 76  ? 2.1835 2.0845 2.3480 -0.0188 -0.1346 -0.1233 140 LEU C N   
6087  C CA  . LEU C 76  ? 2.3062 2.2124 2.4391 -0.0078 -0.1245 -0.1267 140 LEU C CA  
6088  C C   . LEU C 76  ? 2.0758 1.9611 2.1866 0.0007  -0.1370 -0.1364 140 LEU C C   
6089  O O   . LEU C 76  ? 1.7337 1.5995 1.8444 -0.0030 -0.1460 -0.1330 140 LEU C O   
6090  C CB  . LEU C 76  ? 2.3074 2.2180 2.4248 -0.0110 -0.1071 -0.1106 140 LEU C CB  
6091  C CG  . LEU C 76  ? 2.1298 2.0678 2.2593 -0.0133 -0.0906 -0.1032 140 LEU C CG  
6092  C CD1 . LEU C 76  ? 2.2169 2.1670 2.3861 -0.0272 -0.0899 -0.0932 140 LEU C CD1 
6093  C CD2 . LEU C 76  ? 1.6791 1.6201 1.7816 -0.0101 -0.0744 -0.0917 140 LEU C CD2 
6094  N N   . ILE C 77  ? 1.9880 1.8782 2.0825 0.0122  -0.1385 -0.1485 141 ILE C N   
6095  C CA  . ILE C 77  ? 1.7637 1.6391 1.8378 0.0211  -0.1485 -0.1567 141 ILE C CA  
6096  C C   . ILE C 77  ? 1.6425 1.5132 1.6861 0.0261  -0.1404 -0.1517 141 ILE C C   
6097  O O   . ILE C 77  ? 1.3739 1.2545 1.4082 0.0264  -0.1279 -0.1463 141 ILE C O   
6098  C CB  . ILE C 77  ? 1.7725 1.6545 1.8489 0.0308  -0.1582 -0.1725 141 ILE C CB  
6099  C CG1 . ILE C 77  ? 1.8103 1.6777 1.8719 0.0390  -0.1700 -0.1797 141 ILE C CG1 
6100  C CG2 . ILE C 77  ? 1.3669 1.2650 1.4321 0.0370  -0.1490 -0.1756 141 ILE C CG2 
6101  C CD1 . ILE C 77  ? 1.5395 1.4080 1.6105 0.0466  -0.1841 -0.1940 141 ILE C CD1 
6102  N N   . VAL C 78  ? 1.3478 1.2034 1.3763 0.0311  -0.1487 -0.1546 142 VAL C N   
6103  C CA  . VAL C 78  ? 1.0820 0.9277 1.0860 0.0331  -0.1441 -0.1475 142 VAL C CA  
6104  C C   . VAL C 78  ? 1.0491 0.8944 1.0346 0.0437  -0.1491 -0.1558 142 VAL C C   
6105  O O   . VAL C 78  ? 1.0499 0.8965 1.0406 0.0494  -0.1589 -0.1656 142 VAL C O   
6106  C CB  . VAL C 78  ? 1.0425 0.8690 1.0479 0.0269  -0.1492 -0.1394 142 VAL C CB  
6107  C CG1 . VAL C 78  ? 1.0283 0.8442 1.0452 0.0297  -0.1656 -0.1488 142 VAL C CG1 
6108  C CG2 . VAL C 78  ? 1.2694 1.0840 1.2486 0.0297  -0.1460 -0.1325 142 VAL C CG2 
6109  N N   . SER C 79  ? 0.9468 0.7909 0.9113 0.0465  -0.1428 -0.1512 143 SER C N   
6110  C CA  . SER C 79  ? 1.1059 0.9514 1.0546 0.0550  -0.1466 -0.1565 143 SER C CA  
6111  C C   . SER C 79  ? 1.0742 0.9132 1.0216 0.0606  -0.1581 -0.1620 143 SER C C   
6112  O O   . SER C 79  ? 1.2103 1.0577 1.1545 0.0676  -0.1622 -0.1684 143 SER C O   
6113  C CB  . SER C 79  ? 1.2157 1.0553 1.1427 0.0560  -0.1407 -0.1493 143 SER C CB  
6114  O OG  . SER C 79  ? 1.4938 1.3398 1.4192 0.0532  -0.1300 -0.1447 143 SER C OG  
6115  N N   . GLU C 80  ? 1.0258 0.8507 0.9758 0.0579  -0.1633 -0.1592 144 GLU C N   
6116  C CA  . GLU C 80  ? 1.1600 0.9783 1.1075 0.0648  -0.1743 -0.1648 144 GLU C CA  
6117  C C   . GLU C 80  ? 0.9789 0.8052 0.9399 0.0703  -0.1823 -0.1760 144 GLU C C   
6118  O O   . GLU C 80  ? 0.9838 0.8106 0.9412 0.0793  -0.1905 -0.1826 144 GLU C O   
6119  C CB  . GLU C 80  ? 1.4220 1.2206 1.3684 0.0612  -0.1794 -0.1593 144 GLU C CB  
6120  C CG  . GLU C 80  ? 2.0369 1.8253 1.9646 0.0591  -0.1742 -0.1492 144 GLU C CG  
6121  C CD  . GLU C 80  ? 2.0274 1.8184 1.9520 0.0514  -0.1616 -0.1397 144 GLU C CD  
6122  O OE1 . GLU C 80  ? 1.5800 1.3773 1.5206 0.0452  -0.1572 -0.1385 144 GLU C OE1 
6123  O OE2 . GLU C 80  ? 2.1497 1.9372 2.0560 0.0524  -0.1565 -0.1338 144 GLU C OE2 
6124  N N   . GLN C 81  ? 0.9014 0.7349 0.8777 0.0660  -0.1801 -0.1785 145 GLN C N   
6125  C CA  . GLN C 81  ? 0.9075 0.7474 0.8969 0.0714  -0.1889 -0.1897 145 GLN C CA  
6126  C C   . GLN C 81  ? 0.9245 0.7824 0.9103 0.0778  -0.1856 -0.1951 145 GLN C C   
6127  O O   . GLN C 81  ? 1.2116 1.0768 1.2043 0.0843  -0.1923 -0.2046 145 GLN C O   
6128  C CB  . GLN C 81  ? 0.9680 0.8049 0.9790 0.0630  -0.1908 -0.1897 145 GLN C CB  
6129  C CG  . GLN C 81  ? 1.2281 1.0453 1.2461 0.0559  -0.1966 -0.1838 145 GLN C CG  
6130  C CD  . GLN C 81  ? 1.2443 1.0584 1.2881 0.0482  -0.2028 -0.1852 145 GLN C CD  
6131  O OE1 . GLN C 81  ? 1.2006 1.0230 1.2575 0.0386  -0.1940 -0.1782 145 GLN C OE1 
6132  N NE2 . GLN C 81  ? 1.4824 1.2850 1.5344 0.0530  -0.2188 -0.1944 145 GLN C NE2 
6133  N N   . MET C 82  ? 0.9379 0.8017 0.9116 0.0766  -0.1766 -0.1890 146 MET C N   
6134  C CA  . MET C 82  ? 0.7615 0.6406 0.7332 0.0804  -0.1732 -0.1921 146 MET C CA  
6135  C C   . MET C 82  ? 0.7362 0.6230 0.6967 0.0896  -0.1767 -0.1944 146 MET C C   
6136  O O   . MET C 82  ? 0.9655 0.8475 0.9160 0.0917  -0.1781 -0.1907 146 MET C O   
6137  C CB  . MET C 82  ? 0.8270 0.7076 0.7926 0.0747  -0.1630 -0.1848 146 MET C CB  
6138  C CG  . MET C 82  ? 0.9146 0.7964 0.8935 0.0672  -0.1573 -0.1828 146 MET C CG  
6139  S SD  . MET C 82  ? 1.1748 1.0587 1.1419 0.0638  -0.1451 -0.1747 146 MET C SD  
6140  C CE  . MET C 82  ? 0.9532 0.8452 0.9418 0.0566  -0.1386 -0.1733 146 MET C CE  
6141  N N   . ASN C 83  ? 0.6360 0.5361 0.5991 0.0949  -0.1779 -0.1997 147 ASN C N   
6142  C CA  . ASN C 83  ? 0.6673 0.5787 0.6222 0.1037  -0.1806 -0.2008 147 ASN C CA  
6143  C C   . ASN C 83  ? 0.6611 0.5834 0.6130 0.1035  -0.1763 -0.1985 147 ASN C C   
6144  O O   . ASN C 83  ? 0.7459 0.6690 0.7043 0.0998  -0.1736 -0.2003 147 ASN C O   
6145  C CB  . ASN C 83  ? 0.7634 0.6803 0.7236 0.1130  -0.1885 -0.2107 147 ASN C CB  
6146  C CG  . ASN C 83  ? 0.7367 0.6438 0.6970 0.1168  -0.1954 -0.2141 147 ASN C CG  
6147  O OD1 . ASN C 83  ? 0.9396 0.8425 0.8922 0.1169  -0.1946 -0.2088 147 ASN C OD1 
6148  N ND2 . ASN C 83  ? 0.9429 0.8455 0.9122 0.1208  -0.2037 -0.2235 147 ASN C ND2 
6149  N N   . VAL C 84  ? 0.5872 0.5184 0.5308 0.1077  -0.1765 -0.1941 148 VAL C N   
6150  C CA  . VAL C 84  ? 0.6413 0.5804 0.5816 0.1070  -0.1741 -0.1903 148 VAL C CA  
6151  C C   . VAL C 84  ? 0.6031 0.5567 0.5447 0.1152  -0.1772 -0.1942 148 VAL C C   
6152  O O   . VAL C 84  ? 0.6946 0.6578 0.6325 0.1223  -0.1795 -0.1931 148 VAL C O   
6153  C CB  . VAL C 84  ? 0.6143 0.5537 0.5461 0.1047  -0.1731 -0.1806 148 VAL C CB  
6154  C CG1 . VAL C 84  ? 0.5501 0.4948 0.4797 0.1033  -0.1726 -0.1765 148 VAL C CG1 
6155  C CG2 . VAL C 84  ? 0.5472 0.4714 0.4746 0.0982  -0.1709 -0.1769 148 VAL C CG2 
6156  N N   . TYR C 85  ? 0.6261 0.5823 0.5720 0.1152  -0.1771 -0.1984 149 TYR C N   
6157  C CA  . TYR C 85  ? 0.6288 0.5980 0.5740 0.1232  -0.1803 -0.2017 149 TYR C CA  
6158  C C   . TYR C 85  ? 0.6900 0.6646 0.6309 0.1218  -0.1789 -0.1952 149 TYR C C   
6159  O O   . TYR C 85  ? 0.9126 0.8793 0.8528 0.1147  -0.1764 -0.1913 149 TYR C O   
6160  C CB  . TYR C 85  ? 0.5373 0.5053 0.4917 0.1260  -0.1840 -0.2128 149 TYR C CB  
6161  C CG  . TYR C 85  ? 0.6197 0.5833 0.5784 0.1301  -0.1889 -0.2201 149 TYR C CG  
6162  C CD1 . TYR C 85  ? 0.6090 0.5812 0.5620 0.1421  -0.1941 -0.2247 149 TYR C CD1 
6163  C CD2 . TYR C 85  ? 0.6832 0.6337 0.6508 0.1228  -0.1887 -0.2220 149 TYR C CD2 
6164  C CE1 . TYR C 85  ? 0.7011 0.6670 0.6571 0.1472  -0.2006 -0.2327 149 TYR C CE1 
6165  C CE2 . TYR C 85  ? 0.8042 0.7478 0.7765 0.1261  -0.1952 -0.2284 149 TYR C CE2 
6166  C CZ  . TYR C 85  ? 0.8420 0.7923 0.8082 0.1387  -0.2019 -0.2346 149 TYR C CZ  
6167  O OH  . TYR C 85  ? 0.9848 0.9259 0.9547 0.1432  -0.2102 -0.2421 149 TYR C OH  
6168  N N   . SER C 86  ? 0.7198 0.7074 0.6567 0.1294  -0.1812 -0.1943 150 SER C N   
6169  C CA  . SER C 86  ? 0.7925 0.7852 0.7257 0.1289  -0.1816 -0.1879 150 SER C CA  
6170  C C   . SER C 86  ? 0.6489 0.6485 0.5826 0.1369  -0.1852 -0.1956 150 SER C C   
6171  O O   . SER C 86  ? 0.9065 0.9101 0.8417 0.1443  -0.1879 -0.2043 150 SER C O   
6172  C CB  . SER C 86  ? 0.8069 0.8106 0.7343 0.1300  -0.1807 -0.1757 150 SER C CB  
6173  O OG  . SER C 86  ? 1.0543 1.0644 0.9784 0.1307  -0.1822 -0.1688 150 SER C OG  
6174  N N   . VAL C 87  ? 0.6027 0.6026 0.5349 0.1360  -0.1866 -0.1930 151 VAL C N   
6175  C CA  . VAL C 87  ? 0.5773 0.5832 0.5088 0.1439  -0.1908 -0.1996 151 VAL C CA  
6176  C C   . VAL C 87  ? 0.6148 0.6223 0.5403 0.1423  -0.1920 -0.1897 151 VAL C C   
6177  O O   . VAL C 87  ? 0.8116 0.8124 0.7364 0.1343  -0.1905 -0.1806 151 VAL C O   
6178  C CB  . VAL C 87  ? 0.5575 0.5557 0.4998 0.1426  -0.1929 -0.2120 151 VAL C CB  
6179  C CG1 . VAL C 87  ? 0.5131 0.5033 0.4583 0.1358  -0.1917 -0.2099 151 VAL C CG1 
6180  C CG2 . VAL C 87  ? 0.6734 0.6782 0.6160 0.1523  -0.1988 -0.2209 151 VAL C CG2 
6181  N N   . LYS C 88  ? 0.5914 0.6064 0.5120 0.1501  -0.1958 -0.1906 152 LYS C N   
6182  C CA  . LYS C 88  ? 0.6638 0.6782 0.5789 0.1480  -0.1982 -0.1800 152 LYS C CA  
6183  C C   . LYS C 88  ? 0.6222 0.6239 0.5429 0.1445  -0.2013 -0.1870 152 LYS C C   
6184  O O   . LYS C 88  ? 0.6309 0.6318 0.5578 0.1484  -0.2030 -0.1998 152 LYS C O   
6185  C CB  . LYS C 88  ? 0.6123 0.6398 0.5181 0.1578  -0.2008 -0.1760 152 LYS C CB  
6186  C CG  . LYS C 88  ? 0.6860 0.7134 0.5863 0.1540  -0.2029 -0.1608 152 LYS C CG  
6187  C CD  . LYS C 88  ? 0.9279 0.9621 0.8192 0.1633  -0.2073 -0.1596 152 LYS C CD  
6188  C CE  . LYS C 88  ? 1.4635 1.4841 1.3581 0.1634  -0.2138 -0.1695 152 LYS C CE  
6189  N NZ  . LYS C 88  ? 1.4388 1.4648 1.3247 0.1743  -0.2194 -0.1723 152 LYS C NZ  
6190  N N   . LEU C 89  ? 0.5793 0.5710 0.4987 0.1376  -0.2028 -0.1793 153 LEU C N   
6191  C CA  . LEU C 89  ? 0.5965 0.5768 0.5205 0.1359  -0.2055 -0.1870 153 LEU C CA  
6192  C C   . LEU C 89  ? 0.7910 0.7747 0.7144 0.1438  -0.2110 -0.1933 153 LEU C C   
6193  O O   . LEU C 89  ? 0.8422 0.8286 0.7573 0.1470  -0.2155 -0.1851 153 LEU C O   
6194  C CB  . LEU C 89  ? 0.5244 0.4920 0.4448 0.1296  -0.2086 -0.1785 153 LEU C CB  
6195  C CG  . LEU C 89  ? 0.5333 0.4902 0.4561 0.1308  -0.2124 -0.1870 153 LEU C CG  
6196  C CD1 . LEU C 89  ? 0.6553 0.6115 0.5869 0.1301  -0.2064 -0.1989 153 LEU C CD1 
6197  C CD2 . LEU C 89  ? 0.5300 0.4727 0.4473 0.1262  -0.2175 -0.1796 153 LEU C CD2 
6198  N N   . GLY C 90  ? 0.7366 0.7208 0.6694 0.1468  -0.2111 -0.2071 154 GLY C N   
6199  C CA  . GLY C 90  ? 0.8171 0.8056 0.7509 0.1552  -0.2172 -0.2149 154 GLY C CA  
6200  C C   . GLY C 90  ? 0.8332 0.8312 0.7717 0.1614  -0.2177 -0.2245 154 GLY C C   
6201  O O   . GLY C 90  ? 1.0830 1.0841 1.0255 0.1684  -0.2235 -0.2341 154 GLY C O   
6202  N N   . ASP C 91  ? 0.8355 0.8372 0.7732 0.1597  -0.2131 -0.2224 155 ASP C N   
6203  C CA  . ASP C 91  ? 0.8268 0.8342 0.7696 0.1654  -0.2149 -0.2326 155 ASP C CA  
6204  C C   . ASP C 91  ? 0.9432 0.9456 0.9022 0.1584  -0.2117 -0.2402 155 ASP C C   
6205  O O   . ASP C 91  ? 1.1435 1.1399 1.1049 0.1496  -0.2056 -0.2346 155 ASP C O   
6206  C CB  . ASP C 91  ? 0.9700 0.9848 0.9016 0.1698  -0.2129 -0.2264 155 ASP C CB  
6207  C CG  . ASP C 91  ? 1.3705 1.3945 1.2872 0.1797  -0.2164 -0.2210 155 ASP C CG  
6208  O OD1 . ASP C 91  ? 1.6938 1.7170 1.6092 0.1846  -0.2223 -0.2251 155 ASP C OD1 
6209  O OD2 . ASP C 91  ? 1.7402 1.7734 1.6465 0.1832  -0.2131 -0.2121 155 ASP C OD2 
6210  N N   . PRO C 92  ? 0.8472 0.8518 0.8180 0.1622  -0.2166 -0.2525 156 PRO C N   
6211  C CA  . PRO C 92  ? 0.7020 0.7029 0.6908 0.1546  -0.2139 -0.2582 156 PRO C CA  
6212  C C   . PRO C 92  ? 0.7070 0.7056 0.6942 0.1533  -0.2123 -0.2571 156 PRO C C   
6213  O O   . PRO C 92  ? 0.9068 0.9091 0.8824 0.1617  -0.2159 -0.2573 156 PRO C O   
6214  C CB  . PRO C 92  ? 0.7227 0.7271 0.7259 0.1596  -0.2224 -0.2710 156 PRO C CB  
6215  C CG  . PRO C 92  ? 0.7461 0.7546 0.7347 0.1722  -0.2303 -0.2740 156 PRO C CG  
6216  C CD  . PRO C 92  ? 0.7177 0.7275 0.6868 0.1735  -0.2259 -0.2616 156 PRO C CD  
6217  N N   . PRO C 93  ? 0.6465 0.6395 0.6440 0.1438  -0.2067 -0.2553 157 PRO C N   
6218  C CA  . PRO C 93  ? 0.6921 0.6809 0.6875 0.1426  -0.2060 -0.2540 157 PRO C CA  
6219  C C   . PRO C 93  ? 0.6938 0.6814 0.6996 0.1474  -0.2151 -0.2654 157 PRO C C   
6220  O O   . PRO C 93  ? 0.8329 0.8142 0.8528 0.1407  -0.2154 -0.2676 157 PRO C O   
6221  C CB  . PRO C 93  ? 0.6560 0.6381 0.6582 0.1307  -0.1975 -0.2478 157 PRO C CB  
6222  C CG  . PRO C 93  ? 0.6802 0.6648 0.6941 0.1269  -0.1953 -0.2500 157 PRO C CG  
6223  C CD  . PRO C 93  ? 0.6560 0.6461 0.6617 0.1346  -0.1996 -0.2516 157 PRO C CD  
6224  N N   . THR C 94  ? 0.7727 0.7655 0.7713 0.1594  -0.2234 -0.2723 158 THR C N   
6225  C CA  . THR C 94  ? 0.8078 0.7979 0.8114 0.1672  -0.2346 -0.2841 158 THR C CA  
6226  C C   . THR C 94  ? 0.8105 0.7990 0.8005 0.1722  -0.2338 -0.2813 158 THR C C   
6227  O O   . THR C 94  ? 0.7196 0.7132 0.6949 0.1722  -0.2258 -0.2707 158 THR C O   
6228  C CB  . THR C 94  ? 0.9321 0.9284 0.9292 0.1809  -0.2446 -0.2934 158 THR C CB  
6229  O OG1 . THR C 94  ? 0.8843 0.8893 0.8601 0.1877  -0.2400 -0.2853 158 THR C OG1 
6230  C CG2 . THR C 94  ? 1.0659 1.0629 1.0820 0.1771  -0.2492 -0.3002 158 THR C CG2 
6231  N N   . PRO C 95  ? 0.9091 0.8902 0.9050 0.1764  -0.2431 -0.2908 159 PRO C N   
6232  C CA  . PRO C 95  ? 0.9207 0.8994 0.9051 0.1829  -0.2443 -0.2906 159 PRO C CA  
6233  C C   . PRO C 95  ? 0.9260 0.9179 0.8873 0.1976  -0.2431 -0.2883 159 PRO C C   
6234  O O   . PRO C 95  ? 0.9942 0.9904 0.9443 0.1996  -0.2372 -0.2810 159 PRO C O   
6235  C CB  . PRO C 95  ? 0.8494 0.8173 0.8448 0.1881  -0.2591 -0.3049 159 PRO C CB  
6236  C CG  . PRO C 95  ? 1.0194 0.9816 1.0395 0.1754  -0.2610 -0.3069 159 PRO C CG  
6237  C CD  . PRO C 95  ? 0.9974 0.9709 1.0151 0.1734  -0.2536 -0.3019 159 PRO C CD  
6238  N N   . ASP C 96  ? 0.8596 0.8592 0.8143 0.2076  -0.2482 -0.2937 160 ASP C N   
6239  C CA  . ASP C 96  ? 0.9582 0.9727 0.8906 0.2219  -0.2463 -0.2900 160 ASP C CA  
6240  C C   . ASP C 96  ? 0.9189 0.9435 0.8430 0.2151  -0.2334 -0.2727 160 ASP C C   
6241  O O   . ASP C 96  ? 1.0309 1.0689 0.9390 0.2234  -0.2289 -0.2650 160 ASP C O   
6242  C CB  . ASP C 96  ? 1.2477 1.2656 1.1745 0.2353  -0.2568 -0.3012 160 ASP C CB  
6243  C CG  . ASP C 96  ? 1.5403 1.5456 1.4793 0.2401  -0.2720 -0.3187 160 ASP C CG  
6244  O OD1 . ASP C 96  ? 1.5660 1.5619 1.5115 0.2378  -0.2749 -0.3222 160 ASP C OD1 
6245  O OD2 . ASP C 96  ? 1.9969 2.0006 1.9398 0.2459  -0.2821 -0.3289 160 ASP C OD2 
6246  N N   . LYS C 97  ? 0.8353 0.8540 0.7707 0.2005  -0.2282 -0.2666 161 LYS C N   
6247  C CA  . LYS C 97  ? 0.7749 0.7994 0.7040 0.1933  -0.2186 -0.2512 161 LYS C CA  
6248  C C   . LYS C 97  ? 0.8506 0.8724 0.7808 0.1836  -0.2104 -0.2409 161 LYS C C   
6249  O O   . LYS C 97  ? 0.7833 0.8116 0.7062 0.1801  -0.2039 -0.2275 161 LYS C O   
6250  C CB  . LYS C 97  ? 0.7665 0.7851 0.7053 0.1843  -0.2181 -0.2507 161 LYS C CB  
6251  C CG  . LYS C 97  ? 0.8240 0.8475 0.7581 0.1934  -0.2246 -0.2560 161 LYS C CG  
6252  C CD  . LYS C 97  ? 0.8810 0.9175 0.7951 0.2039  -0.2233 -0.2474 161 LYS C CD  
6253  C CE  . LYS C 97  ? 1.0943 1.1338 1.0023 0.2118  -0.2295 -0.2507 161 LYS C CE  
6254  N NZ  . LYS C 97  ? 1.2565 1.3100 1.1440 0.2232  -0.2281 -0.2416 161 LYS C NZ  
6255  N N   . LEU C 98  ? 0.8720 0.8835 0.8119 0.1790  -0.2117 -0.2467 162 LEU C N   
6256  C CA  . LEU C 98  ? 0.7485 0.7545 0.6905 0.1689  -0.2048 -0.2379 162 LEU C CA  
6257  C C   . LEU C 98  ? 0.6616 0.6785 0.5917 0.1752  -0.2017 -0.2302 162 LEU C C   
6258  O O   . LEU C 98  ? 0.8062 0.8325 0.7281 0.1887  -0.2056 -0.2352 162 LEU C O   
6259  C CB  . LEU C 98  ? 0.7372 0.7295 0.6913 0.1635  -0.2077 -0.2451 162 LEU C CB  
6260  C CG  . LEU C 98  ? 0.8984 0.8812 0.8686 0.1538  -0.2084 -0.2495 162 LEU C CG  
6261  C CD1 . LEU C 98  ? 1.0868 1.0574 1.0663 0.1447  -0.2068 -0.2485 162 LEU C CD1 
6262  C CD2 . LEU C 98  ? 0.8939 0.8788 0.8643 0.1464  -0.2018 -0.2421 162 LEU C CD2 
6263  N N   . LYS C 99  ? 0.6430 0.6597 0.5720 0.1662  -0.1948 -0.2180 163 LYS C N   
6264  C CA  . LYS C 99  ? 0.7237 0.7515 0.6454 0.1700  -0.1914 -0.2093 163 LYS C CA  
6265  C C   . LYS C 99  ? 0.7719 0.7879 0.6989 0.1605  -0.1889 -0.2064 163 LYS C C   
6266  O O   . LYS C 99  ? 0.6852 0.6924 0.6156 0.1486  -0.1853 -0.1994 163 LYS C O   
6267  C CB  . LYS C 99  ? 0.7027 0.7439 0.6186 0.1682  -0.1867 -0.1946 163 LYS C CB  
6268  C CG  . LYS C 99  ? 0.8052 0.8586 0.7183 0.1691  -0.1825 -0.1836 163 LYS C CG  
6269  C CD  . LYS C 99  ? 0.9411 1.0142 0.8489 0.1718  -0.1791 -0.1697 163 LYS C CD  
6270  C CE  . LYS C 99  ? 1.1327 1.2108 1.0449 0.1628  -0.1752 -0.1544 163 LYS C CE  
6271  N NZ  . LYS C 99  ? 1.7358 1.8330 1.6465 0.1719  -0.1724 -0.1511 163 LYS C NZ  
6272  N N   . PHE C 100 ? 0.7191 0.7337 0.6456 0.1669  -0.1919 -0.2123 164 PHE C N   
6273  C CA  . PHE C 100 ? 0.6538 0.6566 0.5837 0.1593  -0.1904 -0.2095 164 PHE C CA  
6274  C C   . PHE C 100 ? 0.6803 0.6912 0.6070 0.1541  -0.1848 -0.1954 164 PHE C C   
6275  O O   . PHE C 100 ? 0.7043 0.7341 0.6262 0.1615  -0.1831 -0.1891 164 PHE C O   
6276  C CB  . PHE C 100 ? 0.6816 0.6829 0.6101 0.1692  -0.1960 -0.2179 164 PHE C CB  
6277  C CG  . PHE C 100 ? 0.6240 0.6093 0.5564 0.1615  -0.1962 -0.2166 164 PHE C CG  
6278  C CD1 . PHE C 100 ? 0.5967 0.5865 0.5256 0.1595  -0.1925 -0.2071 164 PHE C CD1 
6279  C CD2 . PHE C 100 ? 0.6036 0.5698 0.5437 0.1561  -0.2007 -0.2240 164 PHE C CD2 
6280  C CE1 . PHE C 100 ? 0.6130 0.5873 0.5437 0.1531  -0.1933 -0.2057 164 PHE C CE1 
6281  C CE2 . PHE C 100 ? 0.6272 0.5783 0.5696 0.1489  -0.2007 -0.2213 164 PHE C CE2 
6282  C CZ  . PHE C 100 ? 0.6570 0.6114 0.5934 0.1479  -0.1971 -0.2125 164 PHE C CZ  
6283  N N   . GLU C 101 ? 0.6066 0.6040 0.5363 0.1420  -0.1823 -0.1900 165 GLU C N   
6284  C CA  . GLU C 101 ? 0.6077 0.6098 0.5356 0.1362  -0.1791 -0.1771 165 GLU C CA  
6285  C C   . GLU C 101 ? 0.6679 0.6630 0.5959 0.1335  -0.1793 -0.1746 165 GLU C C   
6286  O O   . GLU C 101 ? 0.7774 0.7844 0.7050 0.1352  -0.1787 -0.1664 165 GLU C O   
6287  C CB  . GLU C 101 ? 0.6982 0.6916 0.6268 0.1260  -0.1775 -0.1720 165 GLU C CB  
6288  C CG  . GLU C 101 ? 1.0163 1.0204 0.9439 0.1287  -0.1777 -0.1697 165 GLU C CG  
6289  C CD  . GLU C 101 ? 1.1422 1.1647 1.0679 0.1311  -0.1769 -0.1572 165 GLU C CD  
6290  O OE1 . GLU C 101 ? 1.2566 1.2867 1.1833 0.1318  -0.1760 -0.1512 165 GLU C OE1 
6291  O OE2 . GLU C 101 ? 1.0763 1.1064 1.0003 0.1322  -0.1773 -0.1528 165 GLU C OE2 
6292  N N   . ALA C 102 ? 0.6775 0.6542 0.6069 0.1292  -0.1804 -0.1807 166 ALA C N   
6293  C CA  . ALA C 102 ? 0.6712 0.6373 0.5993 0.1271  -0.1817 -0.1793 166 ALA C CA  
6294  C C   . ALA C 102 ? 0.6763 0.6221 0.6066 0.1224  -0.1828 -0.1858 166 ALA C C   
6295  O O   . ALA C 102 ? 0.7124 0.6537 0.6469 0.1197  -0.1821 -0.1908 166 ALA C O   
6296  C CB  . ALA C 102 ? 0.5730 0.5367 0.4987 0.1195  -0.1799 -0.1685 166 ALA C CB  
6297  N N   . VAL C 103 ? 0.6279 0.5622 0.5561 0.1211  -0.1848 -0.1849 167 VAL C N   
6298  C CA  . VAL C 103 ? 0.6748 0.5897 0.6054 0.1155  -0.1857 -0.1883 167 VAL C CA  
6299  C C   . VAL C 103 ? 0.7772 0.6814 0.7025 0.1060  -0.1811 -0.1803 167 VAL C C   
6300  O O   . VAL C 103 ? 1.1786 1.0836 1.0978 0.1058  -0.1814 -0.1741 167 VAL C O   
6301  C CB  . VAL C 103 ? 0.6856 0.5908 0.6155 0.1202  -0.1918 -0.1918 167 VAL C CB  
6302  C CG1 . VAL C 103 ? 0.7944 0.7063 0.7281 0.1313  -0.1984 -0.2020 167 VAL C CG1 
6303  C CG2 . VAL C 103 ? 0.8533 0.7626 0.7767 0.1229  -0.1925 -0.1856 167 VAL C CG2 
6304  N N   . GLY C 104 ? 0.7704 0.6653 0.6982 0.0988  -0.1772 -0.1805 168 GLY C N   
6305  C CA  . GLY C 104 ? 0.6976 0.5831 0.6181 0.0915  -0.1722 -0.1737 168 GLY C CA  
6306  C C   . GLY C 104 ? 0.7669 0.6512 0.6918 0.0864  -0.1667 -0.1749 168 GLY C C   
6307  O O   . GLY C 104 ? 0.8274 0.7197 0.7619 0.0880  -0.1671 -0.1806 168 GLY C O   
6308  N N   . TRP C 105 ? 0.8442 0.7194 0.7617 0.0812  -0.1616 -0.1697 169 TRP C N   
6309  C CA  . TRP C 105 ? 0.7141 0.5899 0.6359 0.0771  -0.1552 -0.1701 169 TRP C CA  
6310  C C   . TRP C 105 ? 0.7566 0.6353 0.6698 0.0780  -0.1528 -0.1686 169 TRP C C   
6311  O O   . TRP C 105 ? 0.9588 0.8398 0.8735 0.0766  -0.1475 -0.1695 169 TRP C O   
6312  C CB  . TRP C 105 ? 0.7195 0.5835 0.6394 0.0716  -0.1505 -0.1650 169 TRP C CB  
6313  C CG  . TRP C 105 ? 0.7951 0.6472 0.6975 0.0714  -0.1498 -0.1583 169 TRP C CG  
6314  C CD1 . TRP C 105 ? 0.7596 0.6089 0.6477 0.0722  -0.1466 -0.1552 169 TRP C CD1 
6315  C CD2 . TRP C 105 ? 0.8858 0.7257 0.7815 0.0713  -0.1541 -0.1546 169 TRP C CD2 
6316  N NE1 . TRP C 105 ? 0.7936 0.6303 0.6672 0.0726  -0.1487 -0.1500 169 TRP C NE1 
6317  C CE2 . TRP C 105 ? 0.9847 0.8155 0.8622 0.0718  -0.1528 -0.1490 169 TRP C CE2 
6318  C CE3 . TRP C 105 ? 1.0381 0.8728 0.9402 0.0719  -0.1599 -0.1560 169 TRP C CE3 
6319  C CZ2 . TRP C 105 ? 1.1199 0.9377 0.9869 0.0724  -0.1568 -0.1446 169 TRP C CZ2 
6320  C CZ3 . TRP C 105 ? 1.0722 0.8938 0.9638 0.0726  -0.1637 -0.1516 169 TRP C CZ3 
6321  C CH2 . TRP C 105 ? 1.0488 0.8625 0.9235 0.0726  -0.1619 -0.1457 169 TRP C CH2 
6322  N N   . SER C 106 ? 0.7424 0.6211 0.6472 0.0806  -0.1575 -0.1662 170 SER C N   
6323  C CA  . SER C 106 ? 0.8054 0.6843 0.7025 0.0815  -0.1581 -0.1648 170 SER C CA  
6324  C C   . SER C 106 ? 0.7211 0.6060 0.6178 0.0837  -0.1650 -0.1624 170 SER C C   
6325  O O   . SER C 106 ? 0.7466 0.6311 0.6422 0.0843  -0.1686 -0.1592 170 SER C O   
6326  C CB  . SER C 106 ? 0.8555 0.7212 0.7379 0.0803  -0.1560 -0.1609 170 SER C CB  
6327  O OG  . SER C 106 ? 1.0718 0.9343 0.9453 0.0821  -0.1610 -0.1595 170 SER C OG  
6328  N N   . ALA C 107 ? 0.6096 0.5008 0.5081 0.0849  -0.1668 -0.1633 171 ALA C N   
6329  C CA  . ALA C 107 ? 0.5931 0.4934 0.4946 0.0862  -0.1725 -0.1595 171 ALA C CA  
6330  C C   . ALA C 107 ? 0.6927 0.5914 0.5911 0.0857  -0.1766 -0.1573 171 ALA C C   
6331  O O   . ALA C 107 ? 0.8414 0.7363 0.7376 0.0864  -0.1748 -0.1615 171 ALA C O   
6332  C CB  . ALA C 107 ? 0.5449 0.4593 0.4561 0.0896  -0.1717 -0.1629 171 ALA C CB  
6333  N N   . SER C 108 ? 0.6873 0.5900 0.5870 0.0846  -0.1828 -0.1502 172 SER C N   
6334  C CA  . SER C 108 ? 0.6752 0.5765 0.5743 0.0834  -0.1891 -0.1462 172 SER C CA  
6335  C C   . SER C 108 ? 0.7070 0.6247 0.6152 0.0831  -0.1919 -0.1384 172 SER C C   
6336  O O   . SER C 108 ? 0.6605 0.5888 0.5733 0.0843  -0.1901 -0.1357 172 SER C O   
6337  C CB  . SER C 108 ? 0.8073 0.6921 0.6974 0.0809  -0.1957 -0.1432 172 SER C CB  
6338  O OG  . SER C 108 ? 0.9298 0.8137 0.8228 0.0782  -0.2051 -0.1361 172 SER C OG  
6339  N N   . SER C 109 ? 0.6648 0.5857 0.5757 0.0823  -0.1964 -0.1344 173 SER C N   
6340  C CA  . SER C 109 ? 0.6997 0.6387 0.6190 0.0822  -0.1977 -0.1251 173 SER C CA  
6341  C C   . SER C 109 ? 0.7723 0.7095 0.6938 0.0788  -0.2052 -0.1171 173 SER C C   
6342  O O   . SER C 109 ? 0.6880 0.6109 0.6042 0.0786  -0.2092 -0.1216 173 SER C O   
6343  C CB  . SER C 109 ? 0.8090 0.7640 0.7312 0.0886  -0.1910 -0.1302 173 SER C CB  
6344  O OG  . SER C 109 ? 0.8833 0.8357 0.8038 0.0908  -0.1910 -0.1358 173 SER C OG  
6345  N N   . CYS C 110 ? 0.8437 0.7965 0.7737 0.0765  -0.2073 -0.1045 174 CYS C N   
6346  C CA  . CYS C 110 ? 0.8295 0.7814 0.7643 0.0714  -0.2157 -0.0931 174 CYS C CA  
6347  C C   . CYS C 110 ? 0.8992 0.8765 0.8441 0.0709  -0.2130 -0.0795 174 CYS C C   
6348  O O   . CYS C 110 ? 0.9545 0.9467 0.9040 0.0728  -0.2080 -0.0774 174 CYS C O   
6349  C CB  . CYS C 110 ? 0.8719 0.8049 0.8071 0.0643  -0.2268 -0.0885 174 CYS C CB  
6350  S SG  . CYS C 110 ? 1.3830 1.3139 1.3199 0.0621  -0.2273 -0.0879 174 CYS C SG  
6351  N N   . HIS C 111 ? 0.9350 0.9182 0.8831 0.0692  -0.2163 -0.0702 175 HIS C N   
6352  C CA  . HIS C 111 ? 0.8088 0.8188 0.7655 0.0695  -0.2127 -0.0554 175 HIS C CA  
6353  C C   . HIS C 111 ? 0.8907 0.9017 0.8598 0.0590  -0.2217 -0.0369 175 HIS C C   
6354  O O   . HIS C 111 ? 1.0702 1.0643 1.0391 0.0535  -0.2315 -0.0329 175 HIS C O   
6355  C CB  . HIS C 111 ? 0.8807 0.8991 0.8317 0.0757  -0.2092 -0.0564 175 HIS C CB  
6356  C CG  . HIS C 111 ? 1.0181 1.0677 0.9734 0.0803  -0.2020 -0.0444 175 HIS C CG  
6357  N ND1 . HIS C 111 ? 0.9377 1.0006 0.9023 0.0742  -0.2049 -0.0241 175 HIS C ND1 
6358  C CD2 . HIS C 111 ? 0.8250 0.8957 0.7759 0.0916  -0.1921 -0.0502 175 HIS C CD2 
6359  C CE1 . HIS C 111 ? 0.8856 0.9791 0.8509 0.0817  -0.1956 -0.0167 175 HIS C CE1 
6360  N NE2 . HIS C 111 ? 0.8296 0.9271 0.7856 0.0932  -0.1884 -0.0338 175 HIS C NE2 
6361  N N   . ASP C 112 ? 0.9324 0.9632 0.9135 0.0562  -0.2195 -0.0255 176 ASP C N   
6362  C CA  . ASP C 112 ? 0.9484 0.9821 0.9458 0.0447  -0.2289 -0.0063 176 ASP C CA  
6363  C C   . ASP C 112 ? 0.9211 0.9754 0.9282 0.0410  -0.2285 0.0139  176 ASP C C   
6364  O O   . ASP C 112 ? 0.9085 0.9629 0.9310 0.0296  -0.2381 0.0314  176 ASP C O   
6365  C CB  . ASP C 112 ? 1.0268 1.0732 1.0361 0.0422  -0.2281 -0.0016 176 ASP C CB  
6366  C CG  . ASP C 112 ? 1.1564 1.2390 1.1700 0.0507  -0.2145 0.0026  176 ASP C CG  
6367  O OD1 . ASP C 112 ? 0.9674 1.0659 0.9736 0.0592  -0.2055 0.0016  176 ASP C OD1 
6368  O OD2 . ASP C 112 ? 1.3389 1.4341 1.3630 0.0498  -0.2137 0.0065  176 ASP C OD2 
6369  N N   . GLY C 113 ? 0.8025 0.8730 0.8006 0.0504  -0.2185 0.0120  177 GLY C N   
6370  C CA  . GLY C 113 ? 0.8132 0.9069 0.8173 0.0491  -0.2157 0.0316  177 GLY C CA  
6371  C C   . GLY C 113 ? 0.9226 1.0554 0.9291 0.0585  -0.2015 0.0379  177 GLY C C   
6372  O O   . GLY C 113 ? 1.0270 1.1835 1.0340 0.0616  -0.1958 0.0521  177 GLY C O   
6373  N N   . PHE C 114 ? 0.9456 1.0852 0.9525 0.0641  -0.1961 0.0272  178 PHE C N   
6374  C CA  . PHE C 114 ? 0.8247 0.9995 0.8319 0.0758  -0.1835 0.0293  178 PHE C CA  
6375  C C   . PHE C 114 ? 0.7668 0.9354 0.7568 0.0900  -0.1775 0.0053  178 PHE C C   
6376  O O   . PHE C 114 ? 0.7177 0.9008 0.6965 0.1022  -0.1704 0.0010  178 PHE C O   
6377  C CB  . PHE C 114 ? 0.7671 0.9596 0.7929 0.0706  -0.1833 0.0401  178 PHE C CB  
6378  C CG  . PHE C 114 ? 1.0247 1.2252 1.0715 0.0555  -0.1902 0.0651  178 PHE C CG  
6379  C CD1 . PHE C 114 ? 1.0331 1.2660 1.0881 0.0555  -0.1837 0.0871  178 PHE C CD1 
6380  C CD2 . PHE C 114 ? 1.1975 1.3728 1.2561 0.0413  -0.2041 0.0676  178 PHE C CD2 
6381  C CE1 . PHE C 114 ? 0.9559 1.1969 1.0336 0.0397  -0.1909 0.1127  178 PHE C CE1 
6382  C CE2 . PHE C 114 ? 0.8775 1.0587 0.9582 0.0263  -0.2129 0.0914  178 PHE C CE2 
6383  C CZ  . PHE C 114 ? 0.8703 1.0846 0.9619 0.0247  -0.2062 0.1146  178 PHE C CZ  
6384  N N   . GLN C 115 ? 0.7292 0.8755 0.7171 0.0884  -0.1812 -0.0099 179 GLN C N   
6385  C CA  . GLN C 115 ? 0.6564 0.7936 0.6303 0.0997  -0.1771 -0.0317 179 GLN C CA  
6386  C C   . GLN C 115 ? 0.6366 0.7375 0.6036 0.0940  -0.1839 -0.0460 179 GLN C C   
6387  O O   . GLN C 115 ? 0.6586 0.7418 0.6306 0.0828  -0.1920 -0.0401 179 GLN C O   
6388  C CB  . GLN C 115 ? 0.7234 0.8755 0.7016 0.1061  -0.1728 -0.0352 179 GLN C CB  
6389  C CG  . GLN C 115 ? 0.7231 0.9146 0.7074 0.1146  -0.1648 -0.0227 179 GLN C CG  
6390  C CD  . GLN C 115 ? 0.7966 1.0008 0.7662 0.1304  -0.1582 -0.0316 179 GLN C CD  
6391  O OE1 . GLN C 115 ? 0.8508 1.0338 0.8076 0.1349  -0.1601 -0.0490 179 GLN C OE1 
6392  N NE2 . GLN C 115 ? 0.9680 1.2076 0.9394 0.1393  -0.1507 -0.0195 179 GLN C NE2 
6393  N N   . TRP C 116 ? 0.6581 0.7484 0.6140 0.1022  -0.1810 -0.0646 180 TRP C N   
6394  C CA  . TRP C 116 ? 0.7020 0.7621 0.6527 0.0977  -0.1853 -0.0779 180 TRP C CA  
6395  C C   . TRP C 116 ? 0.7706 0.8232 0.7240 0.0954  -0.1862 -0.0814 180 TRP C C   
6396  O O   . TRP C 116 ? 0.7347 0.8006 0.6890 0.1026  -0.1818 -0.0847 180 TRP C O   
6397  C CB  . TRP C 116 ? 0.8479 0.9006 0.7887 0.1061  -0.1820 -0.0947 180 TRP C CB  
6398  C CG  . TRP C 116 ? 0.7516 0.8012 0.6877 0.1072  -0.1835 -0.0956 180 TRP C CG  
6399  C CD1 . TRP C 116 ? 0.7814 0.8482 0.7135 0.1159  -0.1805 -0.0943 180 TRP C CD1 
6400  C CD2 . TRP C 116 ? 0.7957 0.8234 0.7294 0.1011  -0.1889 -0.0989 180 TRP C CD2 
6401  N NE1 . TRP C 116 ? 0.7891 0.8457 0.7171 0.1147  -0.1840 -0.0961 180 TRP C NE1 
6402  C CE2 . TRP C 116 ? 0.8286 0.8620 0.7579 0.1061  -0.1891 -0.0991 180 TRP C CE2 
6403  C CE3 . TRP C 116 ? 0.9076 0.9123 0.8408 0.0936  -0.1939 -0.1022 180 TRP C CE3 
6404  C CZ2 . TRP C 116 ? 0.7542 0.7708 0.6805 0.1033  -0.1944 -0.1028 180 TRP C CZ2 
6405  C CZ3 . TRP C 116 ? 0.8645 0.8533 0.7938 0.0917  -0.1986 -0.1062 180 TRP C CZ3 
6406  C CH2 . TRP C 116 ? 0.6899 0.6846 0.6166 0.0962  -0.1990 -0.1064 180 TRP C CH2 
6407  N N   . THR C 117 ? 0.8661 0.8961 0.8195 0.0865  -0.1928 -0.0816 181 THR C N   
6408  C CA  . THR C 117 ? 0.7549 0.7727 0.7077 0.0845  -0.1946 -0.0863 181 THR C CA  
6409  C C   . THR C 117 ? 0.7577 0.7536 0.6991 0.0866  -0.1930 -0.1020 181 THR C C   
6410  O O   . THR C 117 ? 0.7551 0.7367 0.6915 0.0841  -0.1953 -0.1057 181 THR C O   
6411  C CB  . THR C 117 ? 0.7174 0.7239 0.6764 0.0742  -0.2041 -0.0764 181 THR C CB  
6412  O OG1 . THR C 117 ? 0.7303 0.7595 0.7039 0.0707  -0.2057 -0.0597 181 THR C OG1 
6413  C CG2 . THR C 117 ? 0.6491 0.6423 0.6050 0.0735  -0.2063 -0.0820 181 THR C CG2 
6414  N N   . VAL C 118 ? 0.6855 0.6799 0.6237 0.0914  -0.1893 -0.1105 182 VAL C N   
6415  C CA  . VAL C 118 ? 0.6937 0.6689 0.6235 0.0922  -0.1873 -0.1230 182 VAL C CA  
6416  C C   . VAL C 118 ? 0.7946 0.7568 0.7208 0.0906  -0.1885 -0.1255 182 VAL C C   
6417  O O   . VAL C 118 ? 0.8849 0.8561 0.8143 0.0940  -0.1881 -0.1242 182 VAL C O   
6418  C CB  . VAL C 118 ? 0.6453 0.6279 0.5740 0.1000  -0.1823 -0.1326 182 VAL C CB  
6419  C CG1 . VAL C 118 ? 0.7002 0.6644 0.6239 0.0992  -0.1803 -0.1436 182 VAL C CG1 
6420  C CG2 . VAL C 118 ? 0.5741 0.5663 0.5037 0.1021  -0.1817 -0.1315 182 VAL C CG2 
6421  N N   . LEU C 119 ? 0.8070 0.7482 0.7255 0.0864  -0.1900 -0.1293 183 LEU C N   
6422  C CA  . LEU C 119 ? 0.8687 0.7945 0.7804 0.0852  -0.1907 -0.1320 183 LEU C CA  
6423  C C   . LEU C 119 ? 0.7453 0.6615 0.6517 0.0872  -0.1848 -0.1415 183 LEU C C   
6424  O O   . LEU C 119 ? 0.6857 0.5954 0.5891 0.0862  -0.1823 -0.1459 183 LEU C O   
6425  C CB  . LEU C 119 ? 0.8915 0.8005 0.7965 0.0802  -0.1969 -0.1287 183 LEU C CB  
6426  C CG  . LEU C 119 ? 0.8806 0.7958 0.7931 0.0763  -0.2050 -0.1184 183 LEU C CG  
6427  C CD1 . LEU C 119 ? 0.8619 0.7661 0.7706 0.0733  -0.2099 -0.1181 183 LEU C CD1 
6428  C CD2 . LEU C 119 ? 0.8134 0.7218 0.7252 0.0743  -0.2114 -0.1142 183 LEU C CD2 
6429  N N   . SER C 120 ? 0.7310 0.6463 0.6373 0.0899  -0.1833 -0.1443 184 SER C N   
6430  C CA  . SER C 120 ? 0.7740 0.6799 0.6778 0.0904  -0.1789 -0.1515 184 SER C CA  
6431  C C   . SER C 120 ? 0.8723 0.7624 0.7684 0.0888  -0.1795 -0.1506 184 SER C C   
6432  O O   . SER C 120 ? 0.9864 0.8760 0.8810 0.0897  -0.1838 -0.1467 184 SER C O   
6433  C CB  . SER C 120 ? 0.9357 0.8535 0.8472 0.0962  -0.1779 -0.1569 184 SER C CB  
6434  O OG  . SER C 120 ? 1.4017 1.3091 1.3135 0.0954  -0.1754 -0.1631 184 SER C OG  
6435  N N   . VAL C 121 ? 0.8104 0.6885 0.7021 0.0863  -0.1751 -0.1538 185 VAL C N   
6436  C CA  . VAL C 121 ? 0.7360 0.5983 0.6190 0.0846  -0.1746 -0.1520 185 VAL C CA  
6437  C C   . VAL C 121 ? 0.6948 0.5547 0.5837 0.0852  -0.1728 -0.1558 185 VAL C C   
6438  O O   . VAL C 121 ? 0.7369 0.5991 0.6321 0.0835  -0.1685 -0.1594 185 VAL C O   
6439  C CB  . VAL C 121 ? 0.7307 0.5819 0.6036 0.0815  -0.1702 -0.1509 185 VAL C CB  
6440  C CG1 . VAL C 121 ? 0.6939 0.5292 0.5558 0.0801  -0.1688 -0.1478 185 VAL C CG1 
6441  C CG2 . VAL C 121 ? 0.8768 0.7271 0.7432 0.0817  -0.1744 -0.1485 185 VAL C CG2 
6442  N N   . ALA C 122 ? 0.6360 0.4903 0.5236 0.0875  -0.1769 -0.1551 186 ALA C N   
6443  C CA  . ALA C 122 ? 0.6165 0.4662 0.5105 0.0886  -0.1780 -0.1591 186 ALA C CA  
6444  C C   . ALA C 122 ? 0.7380 0.5707 0.6247 0.0878  -0.1809 -0.1558 186 ALA C C   
6445  O O   . ALA C 122 ? 0.8372 0.6627 0.7130 0.0873  -0.1823 -0.1508 186 ALA C O   
6446  C CB  . ALA C 122 ? 0.5959 0.4598 0.4990 0.0958  -0.1825 -0.1647 186 ALA C CB  
6447  N N   . GLY C 123 ? 0.8806 0.7058 0.7736 0.0876  -0.1831 -0.1588 187 GLY C N   
6448  C CA  . GLY C 123 ? 0.9705 0.7776 0.8582 0.0870  -0.1874 -0.1559 187 GLY C CA  
6449  C C   . GLY C 123 ? 1.0306 0.8225 0.9036 0.0822  -0.1842 -0.1472 187 GLY C C   
6450  O O   . GLY C 123 ? 0.9334 0.7194 0.8038 0.0758  -0.1771 -0.1426 187 GLY C O   
6451  N N   . ASP C 124 ? 1.3669 1.1536 1.2302 0.0862  -0.1897 -0.1450 188 ASP C N   
6452  C CA  . ASP C 124 ? 1.4080 1.1804 1.2543 0.0840  -0.1887 -0.1376 188 ASP C CA  
6453  C C   . ASP C 124 ? 1.3739 1.1504 1.2129 0.0806  -0.1809 -0.1350 188 ASP C C   
6454  O O   . ASP C 124 ? 1.2705 1.0354 1.0960 0.0778  -0.1764 -0.1292 188 ASP C O   
6455  C CB  . ASP C 124 ? 1.6652 1.4376 1.5062 0.0902  -0.1974 -0.1377 188 ASP C CB  
6456  C CG  . ASP C 124 ? 2.0104 1.7701 1.8332 0.0893  -0.1984 -0.1315 188 ASP C CG  
6457  O OD1 . ASP C 124 ? 2.4660 2.2085 2.2763 0.0863  -0.1955 -0.1262 188 ASP C OD1 
6458  O OD2 . ASP C 124 ? 1.5189 1.2857 1.3401 0.0920  -0.2027 -0.1316 188 ASP C OD2 
6459  N N   . GLY C 125 ? 1.1584 0.9515 1.0058 0.0816  -0.1796 -0.1392 189 GLY C N   
6460  C CA  . GLY C 125 ? 0.9098 0.7061 0.7501 0.0803  -0.1754 -0.1380 189 GLY C CA  
6461  C C   . GLY C 125 ? 0.9651 0.7684 0.8045 0.0834  -0.1823 -0.1383 189 GLY C C   
6462  O O   . GLY C 125 ? 0.9030 0.7021 0.7321 0.0833  -0.1831 -0.1366 189 GLY C O   
6463  N N   . PHE C 126 ? 0.8125 0.6268 0.6629 0.0867  -0.1879 -0.1402 190 PHE C N   
6464  C CA  . PHE C 126 ? 0.7593 0.5846 0.6138 0.0887  -0.1941 -0.1387 190 PHE C CA  
6465  C C   . PHE C 126 ? 0.8451 0.6893 0.7120 0.0885  -0.1917 -0.1407 190 PHE C C   
6466  O O   . PHE C 126 ? 0.8544 0.7036 0.7270 0.0881  -0.1862 -0.1447 190 PHE C O   
6467  C CB  . PHE C 126 ? 0.7161 0.5459 0.5757 0.0933  -0.2010 -0.1381 190 PHE C CB  
6468  C CG  . PHE C 126 ? 0.8286 0.6728 0.7011 0.0979  -0.2001 -0.1429 190 PHE C CG  
6469  C CD1 . PHE C 126 ? 0.9734 0.8401 0.8579 0.1018  -0.2017 -0.1428 190 PHE C CD1 
6470  C CD2 . PHE C 126 ? 0.8602 0.6952 0.7326 0.0988  -0.1983 -0.1470 190 PHE C CD2 
6471  C CE1 . PHE C 126 ? 1.1707 1.0509 1.0642 0.1083  -0.2011 -0.1481 190 PHE C CE1 
6472  C CE2 . PHE C 126 ? 0.8249 0.6708 0.7076 0.1044  -0.1995 -0.1529 190 PHE C CE2 
6473  C CZ  . PHE C 126 ? 1.0761 0.9448 0.9680 0.1102  -0.2008 -0.1541 190 PHE C CZ  
6474  N N   . VAL C 127 ? 0.7915 0.6463 0.6635 0.0888  -0.1967 -0.1373 191 VAL C N   
6475  C CA  . VAL C 127 ? 0.7918 0.6639 0.6744 0.0884  -0.1954 -0.1370 191 VAL C CA  
6476  C C   . VAL C 127 ? 0.7701 0.6634 0.6657 0.0927  -0.1976 -0.1352 191 VAL C C   
6477  O O   . VAL C 127 ? 0.7997 0.6979 0.6988 0.0936  -0.2032 -0.1304 191 VAL C O   
6478  C CB  . VAL C 127 ? 0.9969 0.8645 0.8759 0.0844  -0.1997 -0.1328 191 VAL C CB  
6479  C CG1 . VAL C 127 ? 1.2933 1.1797 1.1853 0.0835  -0.2020 -0.1285 191 VAL C CG1 
6480  C CG2 . VAL C 127 ? 0.8811 0.7367 0.7503 0.0826  -0.1951 -0.1365 191 VAL C CG2 
6481  N N   . SER C 128 ? 0.8862 0.7931 0.7889 0.0963  -0.1932 -0.1392 192 SER C N   
6482  C CA  . SER C 128 ? 0.8924 0.8240 0.8063 0.1014  -0.1936 -0.1368 192 SER C CA  
6483  C C   . SER C 128 ? 0.9663 0.9090 0.8855 0.0974  -0.1933 -0.1308 192 SER C C   
6484  O O   . SER C 128 ? 0.8207 0.7547 0.7358 0.0935  -0.1913 -0.1327 192 SER C O   
6485  C CB  . SER C 128 ? 1.0011 0.9406 0.9176 0.1087  -0.1903 -0.1448 192 SER C CB  
6486  O OG  . SER C 128 ? 1.1433 1.0697 1.0556 0.1118  -0.1922 -0.1502 192 SER C OG  
6487  N N   . ILE C 129 ? 0.8780 0.8406 0.8071 0.0985  -0.1956 -0.1228 193 ILE C N   
6488  C CA  . ILE C 129 ? 0.7848 0.7594 0.7207 0.0945  -0.1960 -0.1150 193 ILE C CA  
6489  C C   . ILE C 129 ? 0.7871 0.7888 0.7306 0.1022  -0.1915 -0.1136 193 ILE C C   
6490  O O   . ILE C 129 ? 0.8560 0.8747 0.8061 0.1076  -0.1917 -0.1104 193 ILE C O   
6491  C CB  . ILE C 129 ? 0.7119 0.6880 0.6551 0.0880  -0.2033 -0.1040 193 ILE C CB  
6492  C CG1 . ILE C 129 ? 0.7492 0.6970 0.6816 0.0822  -0.2088 -0.1066 193 ILE C CG1 
6493  C CG2 . ILE C 129 ? 0.6261 0.6179 0.5796 0.0838  -0.2045 -0.0936 193 ILE C CG2 
6494  C CD1 . ILE C 129 ? 0.8429 0.7873 0.7809 0.0770  -0.2186 -0.0983 193 ILE C CD1 
6495  N N   . LEU C 130 ? 0.7446 0.7516 0.6866 0.1041  -0.1876 -0.1163 194 LEU C N   
6496  C CA  . LEU C 130 ? 0.8157 0.8502 0.7630 0.1125  -0.1836 -0.1136 194 LEU C CA  
6497  C C   . LEU C 130 ? 0.7956 0.8459 0.7482 0.1099  -0.1824 -0.1032 194 LEU C C   
6498  O O   . LEU C 130 ? 1.0463 1.0854 0.9949 0.1054  -0.1830 -0.1046 194 LEU C O   
6499  C CB  . LEU C 130 ? 0.7945 0.8298 0.7358 0.1233  -0.1807 -0.1266 194 LEU C CB  
6500  C CG  . LEU C 130 ? 0.8588 0.8732 0.7930 0.1215  -0.1803 -0.1375 194 LEU C CG  
6501  C CD1 . LEU C 130 ? 1.1262 1.1532 1.0595 0.1275  -0.1777 -0.1406 194 LEU C CD1 
6502  C CD2 . LEU C 130 ? 0.6829 0.6861 0.6137 0.1264  -0.1817 -0.1474 194 LEU C CD2 
6503  N N   . TYR C 131 ? 0.6948 0.7722 0.6568 0.1129  -0.1808 -0.0921 195 TYR C N   
6504  C CA  . TYR C 131 ? 0.6663 0.7612 0.6354 0.1093  -0.1798 -0.0784 195 TYR C CA  
6505  C C   . TYR C 131 ? 0.6810 0.8000 0.6465 0.1219  -0.1731 -0.0800 195 TYR C C   
6506  O O   . TYR C 131 ? 0.7197 0.8607 0.6875 0.1322  -0.1693 -0.0800 195 TYR C O   
6507  C CB  . TYR C 131 ? 0.6720 0.7832 0.6565 0.1032  -0.1826 -0.0623 195 TYR C CB  
6508  C CG  . TYR C 131 ? 0.7424 0.8666 0.7369 0.0953  -0.1838 -0.0451 195 TYR C CG  
6509  C CD1 . TYR C 131 ? 0.8189 0.9196 0.8123 0.0840  -0.1911 -0.0423 195 TYR C CD1 
6510  C CD2 . TYR C 131 ? 0.7018 0.8620 0.7071 0.0995  -0.1782 -0.0308 195 TYR C CD2 
6511  C CE1 . TYR C 131 ? 0.8509 0.9611 0.8543 0.0761  -0.1942 -0.0255 195 TYR C CE1 
6512  C CE2 . TYR C 131 ? 0.8458 1.0183 0.8616 0.0910  -0.1796 -0.0124 195 TYR C CE2 
6513  C CZ  . TYR C 131 ? 0.9441 1.0903 0.9594 0.0788  -0.1883 -0.0097 195 TYR C CZ  
6514  O OH  . TYR C 131 ? 0.9196 1.0765 0.9460 0.0703  -0.1910 0.0093  195 TYR C OH  
6515  N N   . GLY C 132 ? 0.6367 0.7513 0.5954 0.1226  -0.1720 -0.0825 196 GLY C N   
6516  C CA  . GLY C 132 ? 0.7385 0.8746 0.6914 0.1354  -0.1666 -0.0844 196 GLY C CA  
6517  C C   . GLY C 132 ? 0.6874 0.8229 0.6319 0.1491  -0.1652 -0.1012 196 GLY C C   
6518  O O   . GLY C 132 ? 0.6937 0.8528 0.6350 0.1626  -0.1613 -0.1018 196 GLY C O   
6519  N N   . GLY C 133 ? 0.8019 0.9102 0.7426 0.1459  -0.1689 -0.1143 197 GLY C N   
6520  C CA  . GLY C 133 ? 0.8367 0.9392 0.7706 0.1572  -0.1699 -0.1306 197 GLY C CA  
6521  C C   . GLY C 133 ? 0.8777 0.9841 0.8141 0.1625  -0.1709 -0.1330 197 GLY C C   
6522  O O   . GLY C 133 ? 1.2477 1.3445 1.1790 0.1708  -0.1737 -0.1466 197 GLY C O   
6523  N N   . ILE C 134 ? 0.6727 0.7923 0.6180 0.1579  -0.1699 -0.1200 198 ILE C N   
6524  C CA  . ILE C 134 ? 0.9166 1.0399 0.8651 0.1631  -0.1717 -0.1222 198 ILE C CA  
6525  C C   . ILE C 134 ? 0.9403 1.0435 0.8940 0.1496  -0.1759 -0.1178 198 ILE C C   
6526  O O   . ILE C 134 ? 0.8979 0.9959 0.8565 0.1372  -0.1769 -0.1077 198 ILE C O   
6527  C CB  . ILE C 134 ? 0.8911 1.0522 0.8464 0.1736  -0.1672 -0.1126 198 ILE C CB  
6528  C CG1 . ILE C 134 ? 1.1159 1.2927 1.0847 0.1616  -0.1653 -0.0926 198 ILE C CG1 
6529  C CG2 . ILE C 134 ? 1.0890 1.2693 1.0354 0.1889  -0.1631 -0.1177 198 ILE C CG2 
6530  C CD1 . ILE C 134 ? 1.3057 1.5224 1.2850 0.1697  -0.1601 -0.0802 198 ILE C CD1 
6531  N N   . ILE C 135 ? 0.9091 0.9998 0.8606 0.1529  -0.1796 -0.1257 199 ILE C N   
6532  C CA  . ILE C 135 ? 0.8105 0.8792 0.7632 0.1421  -0.1843 -0.1235 199 ILE C CA  
6533  C C   . ILE C 135 ? 0.8273 0.9125 0.7922 0.1384  -0.1860 -0.1104 199 ILE C C   
6534  O O   . ILE C 135 ? 0.9019 1.0037 0.8718 0.1472  -0.1865 -0.1101 199 ILE C O   
6535  C CB  . ILE C 135 ? 0.9700 1.0181 0.9154 0.1470  -0.1882 -0.1355 199 ILE C CB  
6536  C CG1 . ILE C 135 ? 0.9026 0.9354 0.8395 0.1502  -0.1877 -0.1480 199 ILE C CG1 
6537  C CG2 . ILE C 135 ? 1.0976 1.1223 1.0415 0.1362  -0.1928 -0.1325 199 ILE C CG2 
6538  C CD1 . ILE C 135 ? 0.8079 0.8086 0.7386 0.1413  -0.1902 -0.1531 199 ILE C CD1 
6539  N N   . THR C 136 ? 0.9016 0.9811 0.8717 0.1255  -0.1882 -0.1002 200 THR C N   
6540  C CA  . THR C 136 ? 0.9422 1.0371 0.9272 0.1198  -0.1914 -0.0861 200 THR C CA  
6541  C C   . THR C 136 ? 0.9704 1.0418 0.9544 0.1126  -0.1995 -0.0870 200 THR C C   
6542  O O   . THR C 136 ? 1.3168 1.4004 1.3135 0.1105  -0.2039 -0.0783 200 THR C O   
6543  C CB  . THR C 136 ? 0.9876 1.0918 0.9813 0.1100  -0.1913 -0.0725 200 THR C CB  
6544  O OG1 . THR C 136 ? 0.8362 0.9111 0.8192 0.1020  -0.1939 -0.0777 200 THR C OG1 
6545  C CG2 . THR C 136 ? 1.1014 1.2359 1.0979 0.1180  -0.1832 -0.0677 200 THR C CG2 
6546  N N   . ASP C 137 ? 0.7691 0.8081 0.7383 0.1092  -0.2016 -0.0968 201 ASP C N   
6547  C CA  . ASP C 137 ? 0.9932 1.0074 0.9576 0.1027  -0.2092 -0.0973 201 ASP C CA  
6548  C C   . ASP C 137 ? 0.8529 0.8355 0.7993 0.1021  -0.2087 -0.1086 201 ASP C C   
6549  O O   . ASP C 137 ? 0.8910 0.8670 0.8307 0.1019  -0.2038 -0.1140 201 ASP C O   
6550  C CB  . ASP C 137 ? 1.0464 1.0566 1.0180 0.0914  -0.2157 -0.0867 201 ASP C CB  
6551  C CG  . ASP C 137 ? 1.2440 1.2421 1.2177 0.0875  -0.2257 -0.0837 201 ASP C CG  
6552  O OD1 . ASP C 137 ? 1.5306 1.5082 1.4916 0.0904  -0.2278 -0.0919 201 ASP C OD1 
6553  O OD2 . ASP C 137 ? 1.5234 1.5323 1.5123 0.0811  -0.2324 -0.0725 201 ASP C OD2 
6554  N N   . THR C 138 ? 0.8864 0.8508 0.8258 0.1019  -0.2139 -0.1113 202 THR C N   
6555  C CA  . THR C 138 ? 0.8306 0.7653 0.7531 0.1001  -0.2134 -0.1189 202 THR C CA  
6556  C C   . THR C 138 ? 0.9060 0.8200 0.8206 0.0939  -0.2208 -0.1157 202 THR C C   
6557  O O   . THR C 138 ? 1.0434 0.9624 0.9654 0.0926  -0.2285 -0.1096 202 THR C O   
6558  C CB  . THR C 138 ? 0.8392 0.7665 0.7558 0.1075  -0.2129 -0.1264 202 THR C CB  
6559  O OG1 . THR C 138 ? 1.4020 1.3335 1.3229 0.1109  -0.2194 -0.1234 202 THR C OG1 
6560  C CG2 . THR C 138 ? 0.8002 0.7445 0.7222 0.1155  -0.2078 -0.1318 202 THR C CG2 
6561  N N   . ILE C 139 ? 0.7530 0.6448 0.6530 0.0907  -0.2187 -0.1198 203 ILE C N   
6562  C CA  . ILE C 139 ? 0.8124 0.6818 0.6996 0.0871  -0.2250 -0.1187 203 ILE C CA  
6563  C C   . ILE C 139 ? 0.9236 0.7707 0.7929 0.0891  -0.2217 -0.1241 203 ILE C C   
6564  O O   . ILE C 139 ? 1.0521 0.8965 0.9176 0.0894  -0.2135 -0.1284 203 ILE C O   
6565  C CB  . ILE C 139 ? 0.7672 0.6314 0.6519 0.0822  -0.2259 -0.1176 203 ILE C CB  
6566  C CG1 . ILE C 139 ? 0.6775 0.5614 0.5801 0.0788  -0.2305 -0.1100 203 ILE C CG1 
6567  C CG2 . ILE C 139 ? 0.7970 0.6364 0.6649 0.0809  -0.2328 -0.1185 203 ILE C CG2 
6568  C CD1 . ILE C 139 ? 0.7686 0.6466 0.6695 0.0743  -0.2325 -0.1089 203 ILE C CD1 
6569  N N   . HIS C 140 ? 0.9653 0.7971 0.8245 0.0902  -0.2285 -0.1230 204 HIS C N   
6570  C CA  . HIS C 140 ? 0.9559 0.7674 0.7982 0.0922  -0.2257 -0.1257 204 HIS C CA  
6571  C C   . HIS C 140 ? 1.1017 0.8912 0.9238 0.0911  -0.2283 -0.1252 204 HIS C C   
6572  O O   . HIS C 140 ? 1.4284 1.2141 1.2487 0.0904  -0.2373 -0.1233 204 HIS C O   
6573  C CB  . HIS C 140 ? 0.9002 0.7111 0.7445 0.0967  -0.2309 -0.1254 204 HIS C CB  
6574  C CG  . HIS C 140 ? 0.9832 0.8158 0.8448 0.1004  -0.2286 -0.1271 204 HIS C CG  
6575  N ND1 . HIS C 140 ? 0.9637 0.7958 0.8257 0.1027  -0.2224 -0.1317 204 HIS C ND1 
6576  C CD2 . HIS C 140 ? 1.0473 0.9041 0.9268 0.1030  -0.2321 -0.1247 204 HIS C CD2 
6577  C CE1 . HIS C 140 ? 1.1134 0.9670 0.9902 0.1081  -0.2226 -0.1336 204 HIS C CE1 
6578  N NE2 . HIS C 140 ? 1.2810 1.1512 1.1683 0.1084  -0.2275 -0.1288 204 HIS C NE2 
6579  N N   . PRO C 141 ? 1.0546 0.8296 0.8614 0.0915  -0.2208 -0.1267 205 PRO C N   
6580  C CA  . PRO C 141 ? 1.0540 0.8099 0.8388 0.0925  -0.2211 -0.1264 205 PRO C CA  
6581  C C   . PRO C 141 ? 1.1965 0.9358 0.9667 0.0960  -0.2309 -0.1242 205 PRO C C   
6582  O O   . PRO C 141 ? 1.2118 0.9472 0.9818 0.0977  -0.2323 -0.1228 205 PRO C O   
6583  C CB  . PRO C 141 ? 1.0341 0.7845 0.8110 0.0916  -0.2088 -0.1265 205 PRO C CB  
6584  C CG  . PRO C 141 ? 0.9432 0.7078 0.7391 0.0897  -0.2041 -0.1280 205 PRO C CG  
6585  C CD  . PRO C 141 ? 1.0865 0.8618 0.8958 0.0916  -0.2128 -0.1281 205 PRO C CD  
6586  N N   . THR C 142 ? 1.3437 1.0720 1.1015 0.0980  -0.2391 -0.1247 206 THR C N   
6587  C CA  . THR C 142 ? 1.4758 1.1852 1.2153 0.1025  -0.2492 -0.1236 206 THR C CA  
6588  C C   . THR C 142 ? 1.6737 1.3650 1.3848 0.1065  -0.2422 -0.1235 206 THR C C   
6589  O O   . THR C 142 ? 1.9132 1.5926 1.6100 0.1088  -0.2393 -0.1205 206 THR C O   
6590  C CB  . THR C 142 ? 1.3660 1.0725 1.1082 0.1032  -0.2650 -0.1245 206 THR C CB  
6591  O OG1 . THR C 142 ? 1.9239 1.6245 1.6561 0.1041  -0.2650 -0.1276 206 THR C OG1 
6592  C CG2 . THR C 142 ? 1.1294 0.8583 0.9022 0.0984  -0.2703 -0.1222 206 THR C CG2 
6593  N N   . ASN C 143 ? 1.6410 1.3316 1.3445 0.1076  -0.2389 -0.1265 207 ASN C N   
6594  C CA  . ASN C 143 ? 1.3761 1.0536 1.0527 0.1130  -0.2318 -0.1268 207 ASN C CA  
6595  C C   . ASN C 143 ? 1.3436 1.0258 1.0189 0.1104  -0.2146 -0.1228 207 ASN C C   
6596  O O   . ASN C 143 ? 1.1024 0.7814 0.7612 0.1137  -0.2049 -0.1220 207 ASN C O   
6597  C CB  . ASN C 143 ? 1.3031 0.9821 0.9765 0.1154  -0.2336 -0.1322 207 ASN C CB  
6598  C CG  . ASN C 143 ? 1.4396 1.0994 1.0821 0.1252  -0.2397 -0.1351 207 ASN C CG  
6599  O OD1 . ASN C 143 ? 1.8157 1.4601 1.4440 0.1296  -0.2510 -0.1347 207 ASN C OD1 
6600  N ND2 . ASN C 143 ? 1.8214 1.4819 1.4526 0.1299  -0.2331 -0.1389 207 ASN C ND2 
6601  N N   . GLY C 144 ? 1.4079 1.0984 1.1018 0.1050  -0.2117 -0.1201 208 GLY C N   
6602  C CA  . GLY C 144 ? 1.3152 1.0075 1.0113 0.1013  -0.1989 -0.1155 208 GLY C CA  
6603  C C   . GLY C 144 ? 1.4353 1.1431 1.1448 0.0973  -0.1867 -0.1171 208 GLY C C   
6604  O O   . GLY C 144 ? 1.4566 1.1722 1.1694 0.0984  -0.1871 -0.1219 208 GLY C O   
6605  N N   . GLY C 145 ? 1.5084 1.2197 1.2264 0.0925  -0.1771 -0.1131 209 GLY C N   
6606  C CA  . GLY C 145 ? 1.4240 1.1500 1.1559 0.0884  -0.1658 -0.1143 209 GLY C CA  
6607  C C   . GLY C 145 ? 1.2434 0.9851 0.9962 0.0869  -0.1697 -0.1214 209 GLY C C   
6608  O O   . GLY C 145 ? 1.2791 1.0208 1.0339 0.0890  -0.1801 -0.1243 209 GLY C O   
6609  N N   . PRO C 146 ? 1.2959 1.0517 1.0647 0.0833  -0.1616 -0.1237 210 PRO C N   
6610  C CA  . PRO C 146 ? 1.1697 0.9406 0.9594 0.0818  -0.1650 -0.1294 210 PRO C CA  
6611  C C   . PRO C 146 ? 0.8967 0.6715 0.6833 0.0849  -0.1704 -0.1333 210 PRO C C   
6612  O O   . PRO C 146 ? 1.0481 0.8179 0.8204 0.0880  -0.1680 -0.1339 210 PRO C O   
6613  C CB  . PRO C 146 ? 0.9705 0.7526 0.7739 0.0780  -0.1549 -0.1305 210 PRO C CB  
6614  C CG  . PRO C 146 ? 0.9654 0.7430 0.7533 0.0793  -0.1461 -0.1270 210 PRO C CG  
6615  C CD  . PRO C 146 ? 1.1758 0.9359 0.9422 0.0819  -0.1490 -0.1212 210 PRO C CD  
6616  N N   . LEU C 147 ? 0.7200 0.5035 0.5194 0.0845  -0.1782 -0.1355 211 LEU C N   
6617  C CA  . LEU C 147 ? 0.7205 0.5092 0.5219 0.0857  -0.1831 -0.1381 211 LEU C CA  
6618  C C   . LEU C 147 ? 0.8355 0.6361 0.6465 0.0846  -0.1758 -0.1419 211 LEU C C   
6619  O O   . LEU C 147 ? 0.8678 0.6753 0.6878 0.0825  -0.1675 -0.1428 211 LEU C O   
6620  C CB  . LEU C 147 ? 0.7009 0.4983 0.5154 0.0847  -0.1925 -0.1371 211 LEU C CB  
6621  C CG  . LEU C 147 ? 0.7266 0.5167 0.5373 0.0858  -0.2012 -0.1338 211 LEU C CG  
6622  C CD1 . LEU C 147 ? 0.9605 0.7676 0.7906 0.0850  -0.2049 -0.1325 211 LEU C CD1 
6623  C CD2 . LEU C 147 ? 0.8991 0.6787 0.6992 0.0873  -0.2107 -0.1331 211 LEU C CD2 
6624  N N   . ARG C 148 ? 0.9055 0.7077 0.7156 0.0861  -0.1803 -0.1442 212 ARG C N   
6625  C CA  . ARG C 148 ? 0.9307 0.7425 0.7477 0.0863  -0.1748 -0.1482 212 ARG C CA  
6626  C C   . ARG C 148 ? 0.8868 0.7038 0.7113 0.0861  -0.1834 -0.1491 212 ARG C C   
6627  O O   . ARG C 148 ? 0.9511 0.7584 0.7679 0.0873  -0.1933 -0.1476 212 ARG C O   
6628  C CB  . ARG C 148 ? 0.9126 0.7165 0.7134 0.0905  -0.1692 -0.1503 212 ARG C CB  
6629  C CG  . ARG C 148 ? 1.2222 1.0236 1.0176 0.0896  -0.1589 -0.1471 212 ARG C CG  
6630  C CD  . ARG C 148 ? 1.2516 1.0494 1.0309 0.0947  -0.1511 -0.1477 212 ARG C CD  
6631  N NE  . ARG C 148 ? 1.2427 1.0253 0.9993 0.1013  -0.1590 -0.1486 212 ARG C NE  
6632  C CZ  . ARG C 148 ? 1.3138 1.0826 1.0528 0.1036  -0.1611 -0.1447 212 ARG C CZ  
6633  N NH1 . ARG C 148 ? 1.4858 1.2536 1.2274 0.0991  -0.1557 -0.1387 212 ARG C NH1 
6634  N NH2 . ARG C 148 ? 1.1125 0.8670 0.8309 0.1107  -0.1701 -0.1470 212 ARG C NH2 
6635  N N   . THR C 149 ? 0.8419 0.6735 0.6817 0.0846  -0.1806 -0.1509 213 THR C N   
6636  C CA  . THR C 149 ? 0.8033 0.6410 0.6511 0.0838  -0.1882 -0.1499 213 THR C CA  
6637  C C   . THR C 149 ? 0.8122 0.6467 0.6551 0.0868  -0.1880 -0.1546 213 THR C C   
6638  O O   . THR C 149 ? 0.8769 0.7103 0.7141 0.0895  -0.1797 -0.1589 213 THR C O   
6639  C CB  . THR C 149 ? 0.8207 0.6765 0.6857 0.0822  -0.1857 -0.1492 213 THR C CB  
6640  O OG1 . THR C 149 ? 0.9943 0.8565 0.8640 0.0832  -0.1767 -0.1546 213 THR C OG1 
6641  C CG2 . THR C 149 ? 0.8923 0.7540 0.7632 0.0812  -0.1867 -0.1454 213 THR C CG2 
6642  N N   . GLN C 150 ? 0.7039 0.5378 0.5501 0.0864  -0.1971 -0.1532 214 GLN C N   
6643  C CA  . GLN C 150 ? 0.7988 0.6293 0.6411 0.0901  -0.1987 -0.1583 214 GLN C CA  
6644  C C   . GLN C 150 ? 0.8274 0.6703 0.6772 0.0918  -0.1884 -0.1637 214 GLN C C   
6645  O O   . GLN C 150 ? 0.9976 0.8378 0.8419 0.0966  -0.1868 -0.1694 214 GLN C O   
6646  C CB  . GLN C 150 ? 0.9421 0.7721 0.7912 0.0878  -0.2104 -0.1543 214 GLN C CB  
6647  C CG  . GLN C 150 ? 1.0794 0.8969 0.9242 0.0855  -0.2228 -0.1490 214 GLN C CG  
6648  C CD  . GLN C 150 ? 1.0912 0.9090 0.9459 0.0814  -0.2348 -0.1426 214 GLN C CD  
6649  O OE1 . GLN C 150 ? 1.0546 0.8871 0.9221 0.0788  -0.2321 -0.1387 214 GLN C OE1 
6650  N NE2 . GLN C 150 ? 2.0971 1.8977 1.9458 0.0810  -0.2490 -0.1409 214 GLN C NE2 
6651  N N   . ALA C 151 ? 0.7484 0.6053 0.6111 0.0889  -0.1823 -0.1625 215 ALA C N   
6652  C CA  . ALA C 151 ? 0.7661 0.6347 0.6383 0.0903  -0.1750 -0.1678 215 ALA C CA  
6653  C C   . ALA C 151 ? 0.7699 0.6394 0.6436 0.0929  -0.1806 -0.1702 215 ALA C C   
6654  O O   . ALA C 151 ? 0.8279 0.6993 0.7016 0.0967  -0.1771 -0.1763 215 ALA C O   
6655  C CB  . ALA C 151 ? 0.8179 0.6852 0.6861 0.0921  -0.1654 -0.1719 215 ALA C CB  
6656  N N   . SER C 152 ? 0.8238 0.6926 0.6998 0.0908  -0.1898 -0.1646 216 SER C N   
6657  C CA  . SER C 152 ? 0.7857 0.6524 0.6626 0.0923  -0.1977 -0.1644 216 SER C CA  
6658  C C   . SER C 152 ? 0.7684 0.6398 0.6520 0.0875  -0.2046 -0.1545 216 SER C C   
6659  O O   . SER C 152 ? 0.9787 0.8502 0.8628 0.0842  -0.2052 -0.1491 216 SER C O   
6660  C CB  . SER C 152 ? 1.1381 0.9867 1.0015 0.0957  -0.2053 -0.1672 216 SER C CB  
6661  O OG  . SER C 152 ? 1.7570 1.5987 1.6210 0.0958  -0.2173 -0.1647 216 SER C OG  
6662  N N   . SER C 153 ? 0.6317 0.5079 0.5210 0.0873  -0.2097 -0.1513 217 SER C N   
6663  C CA  . SER C 153 ? 0.6525 0.5340 0.5487 0.0824  -0.2168 -0.1395 217 SER C CA  
6664  C C   . SER C 153 ? 0.6946 0.5624 0.5876 0.0779  -0.2269 -0.1329 217 SER C C   
6665  O O   . SER C 153 ? 0.9663 0.8155 0.8501 0.0795  -0.2348 -0.1369 217 SER C O   
6666  C CB  . SER C 153 ? 0.6215 0.5051 0.5211 0.0831  -0.2224 -0.1368 217 SER C CB  
6667  O OG  . SER C 153 ? 0.7982 0.6830 0.7039 0.0772  -0.2313 -0.1234 217 SER C OG  
6668  N N   . CYS C 154 ? 0.7351 0.6126 0.6359 0.0733  -0.2274 -0.1236 218 CYS C N   
6669  C CA  . CYS C 154 ? 0.8336 0.7009 0.7358 0.0681  -0.2386 -0.1157 218 CYS C CA  
6670  C C   . CYS C 154 ? 0.8045 0.6736 0.7162 0.0631  -0.2488 -0.1046 218 CYS C C   
6671  O O   . CYS C 154 ? 0.6791 0.5577 0.5940 0.0645  -0.2456 -0.1035 218 CYS C O   
6672  C CB  . CYS C 154 ? 1.0350 0.9138 0.9435 0.0656  -0.2350 -0.1101 218 CYS C CB  
6673  S SG  . CYS C 154 ? 1.3291 1.2369 1.2476 0.0680  -0.2220 -0.1077 218 CYS C SG  
6674  N N   . ILE C 155 ? 0.8825 0.7419 0.7991 0.0570  -0.2619 -0.0960 219 ILE C N   
6675  C CA  . ILE C 155 ? 0.8611 0.7169 0.7868 0.0511  -0.2743 -0.0848 219 ILE C CA  
6676  C C   . ILE C 155 ? 0.7834 0.6578 0.7278 0.0427  -0.2765 -0.0673 219 ILE C C   
6677  O O   . ILE C 155 ? 0.8721 0.7463 0.8219 0.0390  -0.2806 -0.0634 219 ILE C O   
6678  C CB  . ILE C 155 ? 0.8189 0.6442 0.7362 0.0510  -0.2917 -0.0891 219 ILE C CB  
6679  C CG1 . ILE C 155 ? 0.9651 0.7767 0.8662 0.0603  -0.2894 -0.1043 219 ILE C CG1 
6680  C CG2 . ILE C 155 ? 0.8355 0.6554 0.7655 0.0428  -0.3073 -0.0752 219 ILE C CG2 
6681  C CD1 . ILE C 155 ? 1.2386 1.0501 1.1262 0.0680  -0.2768 -0.1180 219 ILE C CD1 
6682  N N   . CYS C 156 ? 0.7943 0.6864 0.7487 0.0400  -0.2736 -0.0563 220 CYS C N   
6683  C CA  . CYS C 156 ? 0.9593 0.8726 0.9328 0.0321  -0.2750 -0.0375 220 CYS C CA  
6684  C C   . CYS C 156 ? 1.0319 0.9371 1.0154 0.0237  -0.2893 -0.0234 220 CYS C C   
6685  O O   . CYS C 156 ? 1.0539 0.9490 1.0304 0.0259  -0.2922 -0.0260 220 CYS C O   
6686  C CB  . CYS C 156 ? 1.0607 1.0066 1.0386 0.0365  -0.2586 -0.0333 220 CYS C CB  
6687  S SG  . CYS C 156 ? 1.6116 1.5644 1.5786 0.0465  -0.2438 -0.0502 220 CYS C SG  
6688  N N   . ASN C 157 ? 1.0621 0.9709 1.0632 0.0137  -0.2994 -0.0083 221 ASN C N   
6689  C CA  . ASN C 157 ? 1.1362 1.0372 1.1511 0.0032  -0.3152 0.0082  221 ASN C CA  
6690  C C   . ASN C 157 ? 1.0337 0.9568 1.0741 -0.0076 -0.3181 0.0291  221 ASN C C   
6691  O O   . ASN C 157 ? 0.9575 0.8757 1.0050 -0.0110 -0.3251 0.0285  221 ASN C O   
6692  C CB  . ASN C 157 ? 1.1395 1.0004 1.1458 0.0021  -0.3356 -0.0009 221 ASN C CB  
6693  C CG  . ASN C 157 ? 1.1045 0.9517 1.1189 -0.0055 -0.3516 0.0117  221 ASN C CG  
6694  O OD1 . ASN C 157 ? 1.1028 0.9599 1.1157 -0.0041 -0.3452 0.0171  221 ASN C OD1 
6695  N ND2 . ASN C 157 ? 1.0664 0.8895 1.0893 -0.0133 -0.3737 0.0166  221 ASN C ND2 
6696  N N   . ASP C 158 ? 1.1585 1.1076 1.2132 -0.0126 -0.3126 0.0483  222 ASP C N   
6697  C CA  . ASP C 158 ? 1.2903 1.2665 1.3722 -0.0230 -0.3136 0.0712  222 ASP C CA  
6698  C C   . ASP C 158 ? 1.1366 1.1408 1.2214 -0.0169 -0.2984 0.0675  222 ASP C C   
6699  O O   . ASP C 158 ? 1.0307 1.0465 1.1349 -0.0237 -0.3031 0.0775  222 ASP C O   
6700  C CB  . ASP C 158 ? 1.5811 1.5349 1.6800 -0.0361 -0.3372 0.0802  222 ASP C CB  
6701  C CG  . ASP C 158 ? 2.1834 2.1152 2.2868 -0.0446 -0.3542 0.0908  222 ASP C CG  
6702  O OD1 . ASP C 158 ? 2.3680 2.3100 2.4673 -0.0431 -0.3467 0.0980  222 ASP C OD1 
6703  O OD2 . ASP C 158 ? 2.7291 2.6320 2.8398 -0.0525 -0.3766 0.0917  222 ASP C OD2 
6704  N N   . GLY C 159 ? 1.1323 1.1461 1.1986 -0.0038 -0.2814 0.0526  223 GLY C N   
6705  C CA  . GLY C 159 ? 1.1631 1.2063 1.2321 0.0034  -0.2665 0.0505  223 GLY C CA  
6706  C C   . GLY C 159 ? 1.1396 1.1694 1.2024 0.0071  -0.2683 0.0351  223 GLY C C   
6707  O O   . GLY C 159 ? 1.1338 1.1848 1.1969 0.0143  -0.2568 0.0311  223 GLY C O   
6708  N N   . THR C 160 ? 0.9577 0.9523 1.0142 0.0031  -0.2835 0.0265  224 THR C N   
6709  C CA  . THR C 160 ? 0.8730 0.8487 0.9160 0.0087  -0.2849 0.0089  224 THR C CA  
6710  C C   . THR C 160 ? 0.8277 0.7763 0.8442 0.0170  -0.2825 -0.0111 224 THR C C   
6711  O O   . THR C 160 ? 0.8665 0.7983 0.8770 0.0154  -0.2892 -0.0121 224 THR C O   
6712  C CB  . THR C 160 ? 0.7860 0.7434 0.8397 0.0003  -0.3036 0.0128  224 THR C CB  
6713  O OG1 . THR C 160 ? 0.9636 0.8911 1.0137 -0.0052 -0.3203 0.0128  224 THR C OG1 
6714  C CG2 . THR C 160 ? 0.8564 0.8429 0.9403 -0.0089 -0.3064 0.0340  224 THR C CG2 
6715  N N   . CYS C 161 ? 0.8212 0.7668 0.8228 0.0259  -0.2728 -0.0265 225 CYS C N   
6716  C CA  . CYS C 161 ? 0.9105 0.8344 0.8896 0.0334  -0.2691 -0.0443 225 CYS C CA  
6717  C C   . CYS C 161 ? 0.8953 0.7931 0.8607 0.0358  -0.2758 -0.0563 225 CYS C C   
6718  O O   . CYS C 161 ? 0.9721 0.8737 0.9415 0.0354  -0.2767 -0.0553 225 CYS C O   
6719  C CB  . CYS C 161 ? 0.8062 0.7471 0.7776 0.0423  -0.2516 -0.0526 225 CYS C CB  
6720  S SG  . CYS C 161 ? 1.3416 1.3120 1.3241 0.0423  -0.2440 -0.0401 225 CYS C SG  
6721  N N   . TYR C 162 ? 0.6986 0.5713 0.6473 0.0395  -0.2801 -0.0677 226 TYR C N   
6722  C CA  . TYR C 162 ? 0.7003 0.5473 0.6322 0.0435  -0.2862 -0.0794 226 TYR C CA  
6723  C C   . TYR C 162 ? 0.6931 0.5355 0.6064 0.0527  -0.2728 -0.0944 226 TYR C C   
6724  O O   . TYR C 162 ? 0.7154 0.5598 0.6246 0.0558  -0.2667 -0.0989 226 TYR C O   
6725  C CB  . TYR C 162 ? 0.6515 0.4718 0.5793 0.0412  -0.3051 -0.0800 226 TYR C CB  
6726  C CG  . TYR C 162 ? 0.7486 0.5728 0.6982 0.0305  -0.3199 -0.0636 226 TYR C CG  
6727  C CD1 . TYR C 162 ? 0.9111 0.7296 0.8694 0.0256  -0.3323 -0.0583 226 TYR C CD1 
6728  C CD2 . TYR C 162 ? 0.7913 0.6255 0.7542 0.0247  -0.3218 -0.0523 226 TYR C CD2 
6729  C CE1 . TYR C 162 ? 1.0014 0.8250 0.9835 0.0143  -0.3465 -0.0418 226 TYR C CE1 
6730  C CE2 . TYR C 162 ? 0.8124 0.6516 0.7977 0.0135  -0.3351 -0.0347 226 TYR C CE2 
6731  C CZ  . TYR C 162 ? 0.9221 0.7564 0.9181 0.0079  -0.3474 -0.0295 226 TYR C CZ  
6732  O OH  . TYR C 162 ? 1.1090 0.9491 1.1303 -0.0043 -0.3613 -0.0111 226 TYR C OH  
6733  N N   . THR C 163 ? 0.6731 0.5099 0.5761 0.0566  -0.2684 -0.1011 227 THR C N   
6734  C CA  . THR C 163 ? 0.7750 0.6061 0.6615 0.0640  -0.2568 -0.1135 227 THR C CA  
6735  C C   . THR C 163 ? 0.7765 0.5882 0.6459 0.0681  -0.2599 -0.1203 227 THR C C   
6736  O O   . THR C 163 ? 0.9386 0.7451 0.8101 0.0657  -0.2687 -0.1160 227 THR C O   
6737  C CB  . THR C 163 ? 0.9699 0.8228 0.8626 0.0655  -0.2414 -0.1139 227 THR C CB  
6738  O OG1 . THR C 163 ? 1.3042 1.1518 1.1842 0.0713  -0.2309 -0.1248 227 THR C OG1 
6739  C CG2 . THR C 163 ? 0.7902 0.6521 0.6895 0.0641  -0.2407 -0.1090 227 THR C CG2 
6740  N N   . ILE C 164 ? 0.7136 0.5161 0.5663 0.0747  -0.2522 -0.1304 228 ILE C N   
6741  C CA  . ILE C 164 ? 0.7110 0.4956 0.5443 0.0800  -0.2537 -0.1364 228 ILE C CA  
6742  C C   . ILE C 164 ? 0.6840 0.4752 0.5114 0.0826  -0.2386 -0.1396 228 ILE C C   
6743  O O   . ILE C 164 ? 0.8804 0.6814 0.7097 0.0840  -0.2266 -0.1431 228 ILE C O   
6744  C CB  . ILE C 164 ? 0.7357 0.5025 0.5521 0.0868  -0.2588 -0.1448 228 ILE C CB  
6745  C CG1 . ILE C 164 ? 0.7121 0.4671 0.5338 0.0840  -0.2777 -0.1414 228 ILE C CG1 
6746  C CG2 . ILE C 164 ? 0.7431 0.4941 0.5356 0.0948  -0.2569 -0.1516 228 ILE C CG2 
6747  C CD1 . ILE C 164 ? 0.7131 0.4562 0.5248 0.0901  -0.2826 -0.1490 228 ILE C CD1 
6748  N N   . ILE C 165 ? 0.7260 0.5106 0.5468 0.0831  -0.2406 -0.1380 229 ILE C N   
6749  C CA  . ILE C 165 ? 0.7617 0.5499 0.5773 0.0847  -0.2285 -0.1393 229 ILE C CA  
6750  C C   . ILE C 165 ? 0.7691 0.5388 0.5611 0.0907  -0.2279 -0.1433 229 ILE C C   
6751  O O   . ILE C 165 ? 0.8417 0.5963 0.6231 0.0928  -0.2397 -0.1430 229 ILE C O   
6752  C CB  . ILE C 165 ? 0.7545 0.5535 0.5834 0.0810  -0.2296 -0.1333 229 ILE C CB  
6753  C CG1 . ILE C 165 ? 0.8302 0.6492 0.6810 0.0764  -0.2306 -0.1281 229 ILE C CG1 
6754  C CG2 . ILE C 165 ? 0.7663 0.5681 0.5915 0.0826  -0.2180 -0.1349 229 ILE C CG2 
6755  C CD1 . ILE C 165 ? 0.8179 0.6557 0.6799 0.0764  -0.2194 -0.1282 229 ILE C CD1 
6756  N N   . ALA C 166 ? 0.8635 0.6349 0.6473 0.0935  -0.2145 -0.1465 230 ALA C N   
6757  C CA  . ALA C 166 ? 0.9609 0.7183 0.7217 0.0994  -0.2107 -0.1485 230 ALA C CA  
6758  C C   . ALA C 166 ? 1.0656 0.8225 0.8245 0.0976  -0.2047 -0.1442 230 ALA C C   
6759  O O   . ALA C 166 ? 1.1344 0.9040 0.9093 0.0929  -0.1981 -0.1419 230 ALA C O   
6760  C CB  . ALA C 166 ? 0.8646 0.6250 0.6175 0.1040  -0.1996 -0.1531 230 ALA C CB  
6761  N N   . ASP C 167 ? 1.0605 0.8010 0.7982 0.1025  -0.2083 -0.1436 231 ASP C N   
6762  C CA  . ASP C 167 ? 1.1440 0.8788 0.8744 0.1022  -0.2044 -0.1392 231 ASP C CA  
6763  C C   . ASP C 167 ? 1.1423 0.8655 0.8464 0.1089  -0.1971 -0.1391 231 ASP C C   
6764  O O   . ASP C 167 ? 1.1671 0.8836 0.8553 0.1158  -0.1991 -0.1434 231 ASP C O   
6765  C CB  . ASP C 167 ? 1.4070 1.1328 1.1368 0.1021  -0.2191 -0.1372 231 ASP C CB  
6766  C CG  . ASP C 167 ? 1.4180 1.1441 1.1518 0.0998  -0.2170 -0.1326 231 ASP C CG  
6767  O OD1 . ASP C 167 ? 1.6670 1.3960 1.4004 0.0984  -0.2051 -0.1307 231 ASP C OD1 
6768  O OD2 . ASP C 167 ? 1.3356 1.0590 1.0742 0.0994  -0.2282 -0.1309 231 ASP C OD2 
6769  N N   . GLY C 168 ? 1.0632 0.7840 0.7620 0.1076  -0.1887 -0.1338 232 GLY C N   
6770  C CA  . GLY C 168 ? 1.0877 0.7977 0.7599 0.1142  -0.1820 -0.1313 232 GLY C CA  
6771  C C   . GLY C 168 ? 1.1410 0.8605 0.8157 0.1113  -0.1646 -0.1261 232 GLY C C   
6772  O O   . GLY C 168 ? 1.1748 0.9101 0.8700 0.1062  -0.1570 -0.1274 232 GLY C O   
6773  N N   . THR C 169 ? 1.3478 1.0575 1.0016 0.1147  -0.1588 -0.1196 233 THR C N   
6774  C CA  . THR C 169 ? 1.4128 1.1300 1.0697 0.1104  -0.1429 -0.1113 233 THR C CA  
6775  C C   . THR C 169 ? 1.3930 1.1247 1.0488 0.1138  -0.1301 -0.1127 233 THR C C   
6776  O O   . THR C 169 ? 1.3884 1.1351 1.0628 0.1072  -0.1184 -0.1088 233 THR C O   
6777  C CB  . THR C 169 ? 1.4287 1.1305 1.0610 0.1136  -0.1409 -0.1021 233 THR C CB  
6778  O OG1 . THR C 169 ? 1.6921 1.3801 1.3248 0.1119  -0.1543 -0.1021 233 THR C OG1 
6779  C CG2 . THR C 169 ? 1.4593 1.1681 1.0990 0.1066  -0.1257 -0.0908 233 THR C CG2 
6780  N N   . THR C 170 ? 1.3078 1.0349 0.9423 0.1249  -0.1337 -0.1187 234 THR C N   
6781  C CA  . THR C 170 ? 1.4409 1.1815 1.0711 0.1312  -0.1228 -0.1215 234 THR C CA  
6782  C C   . THR C 170 ? 1.4629 1.1970 1.0811 0.1415  -0.1349 -0.1333 234 THR C C   
6783  O O   . THR C 170 ? 1.5189 1.2363 1.1277 0.1442  -0.1510 -0.1374 234 THR C O   
6784  C CB  . THR C 170 ? 1.6474 1.3896 1.2545 0.1376  -0.1086 -0.1126 234 THR C CB  
6785  O OG1 . THR C 170 ? 1.7795 1.5389 1.3849 0.1447  -0.0973 -0.1157 234 THR C OG1 
6786  C CG2 . THR C 170 ? 1.5290 1.2497 1.1001 0.1489  -0.1176 -0.1128 234 THR C CG2 
6787  N N   . TYR C 171 ? 1.5390 1.2862 1.1584 0.1473  -0.1279 -0.1386 235 TYR C N   
6788  C CA  . TYR C 171 ? 1.5256 1.2682 1.1402 0.1556  -0.1400 -0.1505 235 TYR C CA  
6789  C C   . TYR C 171 ? 1.4363 1.1603 1.0154 0.1708  -0.1495 -0.1557 235 TYR C C   
6790  O O   . TYR C 171 ? 1.5754 1.2855 1.1486 0.1760  -0.1670 -0.1647 235 TYR C O   
6791  C CB  . TYR C 171 ? 1.7402 1.5031 1.3685 0.1574  -0.1294 -0.1546 235 TYR C CB  
6792  C CG  . TYR C 171 ? 2.2359 2.0163 1.8981 0.1430  -0.1206 -0.1495 235 TYR C CG  
6793  C CD1 . TYR C 171 ? 2.3514 2.1300 2.0360 0.1331  -0.1310 -0.1514 235 TYR C CD1 
6794  C CD2 . TYR C 171 ? 2.3628 2.1618 2.0351 0.1396  -0.1025 -0.1424 235 TYR C CD2 
6795  C CE1 . TYR C 171 ? 2.1124 1.9057 1.8258 0.1217  -0.1242 -0.1481 235 TYR C CE1 
6796  C CE2 . TYR C 171 ? 2.5627 2.3755 2.2665 0.1267  -0.0968 -0.1387 235 TYR C CE2 
6797  C CZ  . TYR C 171 ? 2.1482 1.9572 1.8710 0.1187  -0.1082 -0.1424 235 TYR C CZ  
6798  O OH  . TYR C 171 ? 2.2388 2.0603 1.9901 0.1080  -0.1039 -0.1401 235 TYR C OH  
6799  N N   . THR C 172 ? 1.3345 1.0576 0.8899 0.1779  -0.1388 -0.1494 236 THR C N   
6800  C CA  . THR C 172 ? 1.4578 1.1609 0.9762 0.1924  -0.1482 -0.1527 236 THR C CA  
6801  C C   . THR C 172 ? 1.4112 1.0921 0.9294 0.1878  -0.1688 -0.1544 236 THR C C   
6802  O O   . THR C 172 ? 1.3803 1.0421 0.8774 0.1984  -0.1856 -0.1624 236 THR C O   
6803  C CB  . THR C 172 ? 1.6445 1.3516 1.1400 0.1977  -0.1315 -0.1416 236 THR C CB  
6804  O OG1 . THR C 172 ? 1.7671 1.4669 1.2694 0.1859  -0.1315 -0.1309 236 THR C OG1 
6805  C CG2 . THR C 172 ? 1.6905 1.4254 1.1983 0.1960  -0.1086 -0.1354 236 THR C CG2 
6806  N N   . ALA C 173 ? 1.5498 1.2340 1.0930 0.1725  -0.1684 -0.1472 237 ALA C N   
6807  C CA  . ALA C 173 ? 1.4140 1.0812 0.9583 0.1679  -0.1846 -0.1462 237 ALA C CA  
6808  C C   . ALA C 173 ? 1.2878 0.9591 0.8643 0.1565  -0.1960 -0.1492 237 ALA C C   
6809  O O   . ALA C 173 ? 1.4550 1.1192 1.0402 0.1502  -0.2060 -0.1464 237 ALA C O   
6810  C CB  . ALA C 173 ? 1.5752 1.2409 1.1168 0.1620  -0.1759 -0.1346 237 ALA C CB  
6811  N N   . SER C 174 ? 1.2346 0.9179 0.8281 0.1545  -0.1946 -0.1545 238 SER C N   
6812  C CA  . SER C 174 ? 1.1768 0.8675 0.8015 0.1435  -0.2026 -0.1555 238 SER C CA  
6813  C C   . SER C 174 ? 1.1091 0.7850 0.7354 0.1434  -0.2247 -0.1590 238 SER C C   
6814  O O   . SER C 174 ? 1.1542 0.8127 0.7588 0.1532  -0.2374 -0.1646 238 SER C O   
6815  C CB  . SER C 174 ? 1.1442 0.8512 0.7858 0.1417  -0.1955 -0.1595 238 SER C CB  
6816  O OG  . SER C 174 ? 1.1121 0.8115 0.7382 0.1528  -0.2028 -0.1682 238 SER C OG  
6817  N N   . SER C 175 ? 1.1625 0.8467 0.8158 0.1323  -0.2294 -0.1554 239 SER C N   
6818  C CA  . SER C 175 ? 1.1125 0.7888 0.7758 0.1291  -0.2488 -0.1559 239 SER C CA  
6819  C C   . SER C 175 ? 1.1162 0.8093 0.8091 0.1201  -0.2484 -0.1548 239 SER C C   
6820  O O   . SER C 175 ? 1.4144 1.1248 1.1232 0.1142  -0.2348 -0.1516 239 SER C O   
6821  C CB  . SER C 175 ? 1.0955 0.7692 0.7631 0.1247  -0.2528 -0.1499 239 SER C CB  
6822  O OG  . SER C 175 ? 1.4413 1.1131 1.1251 0.1199  -0.2700 -0.1488 239 SER C OG  
6823  N N   . HIS C 176 ? 0.9871 0.6748 0.6877 0.1191  -0.2640 -0.1570 240 HIS C N   
6824  C CA  . HIS C 176 ? 0.8382 0.5416 0.5656 0.1108  -0.2641 -0.1545 240 HIS C CA  
6825  C C   . HIS C 176 ? 0.8853 0.5872 0.6300 0.1041  -0.2812 -0.1496 240 HIS C C   
6826  O O   . HIS C 176 ? 0.9075 0.5913 0.6438 0.1071  -0.2988 -0.1518 240 HIS C O   
6827  C CB  . HIS C 176 ? 0.8808 0.5824 0.6034 0.1156  -0.2638 -0.1609 240 HIS C CB  
6828  C CG  . HIS C 176 ? 0.9886 0.6940 0.6952 0.1230  -0.2469 -0.1654 240 HIS C CG  
6829  N ND1 . HIS C 176 ? 0.9304 0.6543 0.6473 0.1203  -0.2293 -0.1647 240 HIS C ND1 
6830  C CD2 . HIS C 176 ? 1.1855 0.8769 0.8639 0.1342  -0.2467 -0.1706 240 HIS C CD2 
6831  C CE1 . HIS C 176 ? 0.9705 0.6925 0.6677 0.1289  -0.2186 -0.1682 240 HIS C CE1 
6832  N NE2 . HIS C 176 ? 1.1596 0.8623 0.8321 0.1380  -0.2286 -0.1717 240 HIS C NE2 
6833  N N   . ARG C 177 ? 0.8404 0.5622 0.6103 0.0951  -0.2765 -0.1425 241 ARG C N   
6834  C CA  . ARG C 177 ? 0.8373 0.5642 0.6287 0.0876  -0.2904 -0.1356 241 ARG C CA  
6835  C C   . ARG C 177 ? 0.8053 0.5461 0.6157 0.0820  -0.2893 -0.1323 241 ARG C C   
6836  O O   . ARG C 177 ? 0.9255 0.6786 0.7384 0.0823  -0.2752 -0.1341 241 ARG C O   
6837  C CB  . ARG C 177 ? 0.8799 0.6205 0.6849 0.0833  -0.2873 -0.1290 241 ARG C CB  
6838  C CG  . ARG C 177 ? 1.0022 0.7271 0.7879 0.0890  -0.2903 -0.1317 241 ARG C CG  
6839  C CD  . ARG C 177 ? 1.0296 0.7657 0.8167 0.0890  -0.2764 -0.1299 241 ARG C CD  
6840  N NE  . ARG C 177 ? 1.2053 0.9553 1.0131 0.0843  -0.2814 -0.1234 241 ARG C NE  
6841  C CZ  . ARG C 177 ? 1.1084 0.8502 0.9122 0.0862  -0.2905 -0.1221 241 ARG C CZ  
6842  N NH1 . ARG C 177 ? 0.8379 0.5560 0.6158 0.0927  -0.2960 -0.1267 241 ARG C NH1 
6843  N NH2 . ARG C 177 ? 1.1468 0.9051 0.9720 0.0826  -0.2941 -0.1161 241 ARG C NH2 
6844  N N   . LEU C 178 ? 0.7979 0.5359 0.6221 0.0766  -0.3053 -0.1270 242 LEU C N   
6845  C CA  . LEU C 178 ? 0.8550 0.6053 0.6983 0.0703  -0.3066 -0.1212 242 LEU C CA  
6846  C C   . LEU C 178 ? 0.8337 0.6072 0.7036 0.0615  -0.3063 -0.1090 242 LEU C C   
6847  O O   . LEU C 178 ? 0.9377 0.7084 0.8177 0.0573  -0.3197 -0.1030 242 LEU C O   
6848  C CB  . LEU C 178 ? 0.8928 0.6214 0.7326 0.0704  -0.3267 -0.1228 242 LEU C CB  
6849  C CG  . LEU C 178 ? 1.0293 0.7627 0.8901 0.0621  -0.3372 -0.1140 242 LEU C CG  
6850  C CD1 . LEU C 178 ? 1.2406 0.9881 1.1044 0.0624  -0.3232 -0.1147 242 LEU C CD1 
6851  C CD2 . LEU C 178 ? 1.0493 0.7530 0.8994 0.0652  -0.3590 -0.1193 242 LEU C CD2 
6852  N N   . TYR C 179 ? 0.8589 0.6563 0.7399 0.0599  -0.2908 -0.1058 243 TYR C N   
6853  C CA  . TYR C 179 ? 0.7485 0.5721 0.6527 0.0543  -0.2874 -0.0951 243 TYR C CA  
6854  C C   . TYR C 179 ? 0.7380 0.5764 0.6630 0.0469  -0.2918 -0.0840 243 TYR C C   
6855  O O   . TYR C 179 ? 0.8153 0.6494 0.7372 0.0469  -0.2913 -0.0856 243 TYR C O   
6856  C CB  . TYR C 179 ? 0.6941 0.5348 0.5968 0.0585  -0.2693 -0.0985 243 TYR C CB  
6857  C CG  . TYR C 179 ? 0.7743 0.6078 0.6660 0.0629  -0.2668 -0.1032 243 TYR C CG  
6858  C CD1 . TYR C 179 ? 0.7997 0.6143 0.6683 0.0688  -0.2619 -0.1130 243 TYR C CD1 
6859  C CD2 . TYR C 179 ? 0.7493 0.5953 0.6537 0.0615  -0.2697 -0.0971 243 TYR C CD2 
6860  C CE1 . TYR C 179 ? 0.9907 0.7973 0.8481 0.0726  -0.2600 -0.1159 243 TYR C CE1 
6861  C CE2 . TYR C 179 ? 0.9537 0.7913 0.8472 0.0660  -0.2687 -0.1015 243 TYR C CE2 
6862  C CZ  . TYR C 179 ? 1.1639 0.9806 1.0333 0.0712  -0.2640 -0.1105 243 TYR C CZ  
6863  O OH  . TYR C 179 ? 1.3779 1.1851 1.2355 0.0754  -0.2633 -0.1134 243 TYR C OH  
6864  N N   . ARG C 180 ? 0.7338 0.5909 0.6808 0.0408  -0.2960 -0.0718 244 ARG C N   
6865  C CA  . ARG C 180 ? 0.8214 0.6991 0.7908 0.0334  -0.2975 -0.0580 244 ARG C CA  
6866  C C   . ARG C 180 ? 0.8558 0.7683 0.8392 0.0348  -0.2830 -0.0514 244 ARG C C   
6867  O O   . ARG C 180 ? 1.0769 0.9986 1.0647 0.0369  -0.2814 -0.0510 244 ARG C O   
6868  C CB  . ARG C 180 ? 0.8738 0.7435 0.8593 0.0243  -0.3175 -0.0474 244 ARG C CB  
6869  C CG  . ARG C 180 ? 1.1784 1.0752 1.1935 0.0148  -0.3198 -0.0284 244 ARG C CG  
6870  C CD  . ARG C 180 ? 1.4477 1.3328 1.4799 0.0052  -0.3421 -0.0189 244 ARG C CD  
6871  N NE  . ARG C 180 ? 2.0091 1.9276 2.0728 -0.0028 -0.3415 -0.0005 244 ARG C NE  
6872  C CZ  . ARG C 180 ? 2.2200 2.1522 2.3086 -0.0139 -0.3485 0.0178  244 ARG C CZ  
6873  N NH1 . ARG C 180 ? 2.1892 2.1011 2.2745 -0.0186 -0.3588 0.0196  244 ARG C NH1 
6874  N NH2 . ARG C 180 ? 2.2476 2.2146 2.3650 -0.0200 -0.3455 0.0349  244 ARG C NH2 
6875  N N   . LEU C 181 ? 0.8699 0.8008 0.8582 0.0354  -0.2729 -0.0473 245 LEU C N   
6876  C CA  . LEU C 181 ? 0.7102 0.6727 0.7071 0.0397  -0.2589 -0.0435 245 LEU C CA  
6877  C C   . LEU C 181 ? 0.7355 0.7244 0.7528 0.0341  -0.2583 -0.0266 245 LEU C C   
6878  O O   . LEU C 181 ? 0.7316 0.7127 0.7499 0.0290  -0.2635 -0.0216 245 LEU C O   
6879  C CB  . LEU C 181 ? 0.6492 0.6104 0.6293 0.0483  -0.2455 -0.0562 245 LEU C CB  
6880  C CG  . LEU C 181 ? 0.6959 0.6305 0.6549 0.0531  -0.2445 -0.0718 245 LEU C CG  
6881  C CD1 . LEU C 181 ? 0.8040 0.7356 0.7510 0.0583  -0.2346 -0.0816 245 LEU C CD1 
6882  C CD2 . LEU C 181 ? 0.7216 0.6596 0.6786 0.0576  -0.2412 -0.0759 245 LEU C CD2 
6883  N N   . VAL C 182 ? 0.6711 0.6916 0.7039 0.0357  -0.2518 -0.0174 246 VAL C N   
6884  C CA  . VAL C 182 ? 0.6529 0.7040 0.7045 0.0318  -0.2482 0.0001  246 VAL C CA  
6885  C C   . VAL C 182 ? 0.7027 0.7849 0.7534 0.0430  -0.2321 -0.0017 246 VAL C C   
6886  O O   . VAL C 182 ? 0.6024 0.6921 0.6531 0.0493  -0.2289 -0.0076 246 VAL C O   
6887  C CB  . VAL C 182 ? 0.6807 0.7458 0.7590 0.0213  -0.2587 0.0182  246 VAL C CB  
6888  C CG1 . VAL C 182 ? 0.7268 0.8197 0.8238 0.0151  -0.2558 0.0387  246 VAL C CG1 
6889  C CG2 . VAL C 182 ? 0.6498 0.6809 0.7281 0.0124  -0.2776 0.0164  246 VAL C CG2 
6890  N N   . ASN C 183 ? 0.7952 0.8946 0.8443 0.0464  -0.2233 0.0030  247 ASN C N   
6891  C CA  . ASN C 183 ? 0.6211 0.7496 0.6670 0.0590  -0.2091 0.0004  247 ASN C CA  
6892  C C   . ASN C 183 ? 0.6210 0.7374 0.6521 0.0691  -0.2055 -0.0190 247 ASN C C   
6893  O O   . ASN C 183 ? 0.8624 1.0011 0.8957 0.0790  -0.1983 -0.0212 247 ASN C O   
6894  C CB  . ASN C 183 ? 0.7049 0.8748 0.7733 0.0588  -0.2048 0.0193  247 ASN C CB  
6895  C CG  . ASN C 183 ? 0.9429 1.1274 1.0275 0.0480  -0.2076 0.0414  247 ASN C CG  
6896  O OD1 . ASN C 183 ? 1.4477 1.6104 1.5249 0.0419  -0.2130 0.0416  247 ASN C OD1 
6897  N ND2 . ASN C 183 ? 0.8898 1.1128 0.9973 0.0460  -0.2038 0.0610  247 ASN C ND2 
6898  N N   . GLY C 184 ? 0.5349 0.6161 0.5513 0.0668  -0.2108 -0.0324 248 GLY C N   
6899  C CA  . GLY C 184 ? 0.5410 0.6077 0.5416 0.0754  -0.2068 -0.0500 248 GLY C CA  
6900  C C   . GLY C 184 ? 0.6775 0.7337 0.6785 0.0753  -0.2120 -0.0542 248 GLY C C   
6901  O O   . GLY C 184 ? 0.7171 0.7583 0.7049 0.0812  -0.2098 -0.0674 248 GLY C O   
6902  N N   . THR C 185 ? 0.8851 0.9486 0.9019 0.0684  -0.2198 -0.0422 249 THR C N   
6903  C CA  . THR C 185 ? 0.7615 0.8134 0.7790 0.0678  -0.2270 -0.0454 249 THR C CA  
6904  C C   . THR C 185 ? 0.7814 0.8026 0.7950 0.0578  -0.2398 -0.0450 249 THR C C   
6905  O O   . THR C 185 ? 0.7950 0.8120 0.8133 0.0503  -0.2447 -0.0377 249 THR C O   
6906  C CB  . THR C 185 ? 0.8476 0.9320 0.8871 0.0691  -0.2274 -0.0338 249 THR C CB  
6907  O OG1 . THR C 185 ? 0.9755 1.0819 1.0354 0.0608  -0.2293 -0.0158 249 THR C OG1 
6908  C CG2 . THR C 185 ? 0.9652 1.0742 1.0026 0.0827  -0.2158 -0.0391 249 THR C CG2 
6909  N N   . SER C 186 ? 0.8921 0.8905 0.8952 0.0589  -0.2460 -0.0534 250 SER C N   
6910  C CA  . SER C 186 ? 0.9755 0.9440 0.9716 0.0520  -0.2590 -0.0546 250 SER C CA  
6911  C C   . SER C 186 ? 0.8148 0.7927 0.8333 0.0437  -0.2718 -0.0409 250 SER C C   
6912  O O   . SER C 186 ? 0.7492 0.7479 0.7830 0.0449  -0.2720 -0.0350 250 SER C O   
6913  C CB  . SER C 186 ? 1.1403 1.0806 1.1150 0.0568  -0.2612 -0.0676 250 SER C CB  
6914  O OG  . SER C 186 ? 1.4025 1.3506 1.3816 0.0609  -0.2621 -0.0679 250 SER C OG  
6915  N N   . ALA C 187 ? 0.9771 0.9408 0.9993 0.0353  -0.2829 -0.0355 251 ALA C N   
6916  C CA  . ALA C 187 ? 0.8885 0.8577 0.9340 0.0254  -0.2977 -0.0216 251 ALA C CA  
6917  C C   . ALA C 187 ? 0.8336 0.7662 0.8659 0.0237  -0.3141 -0.0295 251 ALA C C   
6918  O O   . ALA C 187 ? 1.1169 1.0393 1.1614 0.0151  -0.3307 -0.0219 251 ALA C O   
6919  C CB  . ALA C 187 ? 0.9038 0.8847 0.9651 0.0167  -0.2997 -0.0077 251 ALA C CB  
6920  N N   . GLY C 188 ? 0.7708 0.6829 0.7772 0.0324  -0.3098 -0.0448 252 GLY C N   
6921  C CA  . GLY C 188 ? 1.0376 0.9161 1.0276 0.0337  -0.3243 -0.0533 252 GLY C CA  
6922  C C   . GLY C 188 ? 0.9899 0.8397 0.9518 0.0385  -0.3228 -0.0657 252 GLY C C   
6923  O O   . GLY C 188 ? 0.9715 0.8273 0.9290 0.0396  -0.3114 -0.0674 252 GLY C O   
6924  N N   . TRP C 189 ? 0.8990 0.7191 0.8417 0.0423  -0.3343 -0.0744 253 TRP C N   
6925  C CA  . TRP C 189 ? 0.8507 0.6445 0.7656 0.0485  -0.3332 -0.0864 253 TRP C CA  
6926  C C   . TRP C 189 ? 0.8532 0.6160 0.7535 0.0510  -0.3526 -0.0921 253 TRP C C   
6927  O O   . TRP C 189 ? 0.9604 0.7206 0.8735 0.0470  -0.3683 -0.0869 253 TRP C O   
6928  C CB  . TRP C 189 ? 0.7825 0.5771 0.6776 0.0567  -0.3148 -0.0956 253 TRP C CB  
6929  C CG  . TRP C 189 ? 0.9191 0.7116 0.8089 0.0604  -0.3156 -0.0972 253 TRP C CG  
6930  C CD1 . TRP C 189 ? 0.9375 0.7526 0.8432 0.0597  -0.3096 -0.0918 253 TRP C CD1 
6931  C CD2 . TRP C 189 ? 0.7996 0.5654 0.6657 0.0668  -0.3239 -0.1048 253 TRP C CD2 
6932  N NE1 . TRP C 189 ? 0.7710 0.5740 0.6647 0.0646  -0.3137 -0.0957 253 TRP C NE1 
6933  C CE2 . TRP C 189 ? 0.7875 0.5611 0.6573 0.0687  -0.3222 -0.1030 253 TRP C CE2 
6934  C CE3 . TRP C 189 ? 0.8029 0.5405 0.6443 0.0723  -0.3320 -0.1130 253 TRP C CE3 
6935  C CZ2 . TRP C 189 ? 0.8295 0.5821 0.6789 0.0749  -0.3289 -0.1084 253 TRP C CZ2 
6936  C CZ3 . TRP C 189 ? 0.8922 0.6099 0.7119 0.0794  -0.3380 -0.1185 253 TRP C CZ3 
6937  C CH2 . TRP C 189 ? 0.9025 0.6270 0.7261 0.0802  -0.3366 -0.1159 253 TRP C CH2 
6938  N N   . LYS C 190 ? 0.8353 0.5753 0.7096 0.0582  -0.3523 -0.1031 254 LYS C N   
6939  C CA  . LYS C 190 ? 0.8784 0.5867 0.7318 0.0644  -0.3698 -0.1115 254 LYS C CA  
6940  C C   . LYS C 190 ? 0.9089 0.6029 0.7283 0.0764  -0.3577 -0.1240 254 LYS C C   
6941  O O   . LYS C 190 ? 0.9964 0.6991 0.8108 0.0784  -0.3415 -0.1268 254 LYS C O   
6942  C CB  . LYS C 190 ? 0.8955 0.5893 0.7556 0.0606  -0.3881 -0.1102 254 LYS C CB  
6943  C CG  . LYS C 190 ? 1.0763 0.7351 0.9119 0.0694  -0.4076 -0.1211 254 LYS C CG  
6944  C CD  . LYS C 190 ? 1.0084 0.6517 0.8594 0.0629  -0.4340 -0.1171 254 LYS C CD  
6945  C CE  . LYS C 190 ? 1.2978 0.9043 1.1195 0.0749  -0.4533 -0.1308 254 LYS C CE  
6946  N NZ  . LYS C 190 ? 1.6181 1.2043 1.4543 0.0693  -0.4845 -0.1279 254 LYS C NZ  
6947  N N   . ALA C 191 ? 0.9958 0.6698 0.7927 0.0844  -0.3648 -0.1306 255 ALA C N   
6948  C CA  . ALA C 191 ? 1.0498 0.7104 0.8138 0.0961  -0.3541 -0.1409 255 ALA C CA  
6949  C C   . ALA C 191 ? 0.9503 0.5920 0.6994 0.1025  -0.3637 -0.1490 255 ALA C C   
6950  O O   . ALA C 191 ? 0.9870 0.6118 0.7386 0.1021  -0.3857 -0.1502 255 ALA C O   
6951  C CB  . ALA C 191 ? 1.2639 0.9093 1.0063 0.1036  -0.3583 -0.1446 255 ALA C CB  
6952  N N   . LEU C 192 ? 0.9629 0.6083 0.6985 0.1083  -0.3478 -0.1546 256 LEU C N   
6953  C CA  . LEU C 192 ? 1.0569 0.6858 0.7749 0.1172  -0.3545 -0.1639 256 LEU C CA  
6954  C C   . LEU C 192 ? 1.2257 0.8360 0.9067 0.1324  -0.3534 -0.1737 256 LEU C C   
6955  O O   . LEU C 192 ? 1.1491 0.7680 0.8184 0.1355  -0.3354 -0.1729 256 LEU C O   
6956  C CB  . LEU C 192 ? 1.2586 0.9048 0.9840 0.1158  -0.3372 -0.1643 256 LEU C CB  
6957  C CG  . LEU C 192 ? 1.1029 0.7664 0.8600 0.1034  -0.3376 -0.1556 256 LEU C CG  
6958  C CD1 . LEU C 192 ? 1.1739 0.8523 0.9319 0.1050  -0.3196 -0.1582 256 LEU C CD1 
6959  C CD2 . LEU C 192 ? 0.9920 0.6393 0.7573 0.1007  -0.3614 -0.1549 256 LEU C CD2 
6960  N N   . ASP C 193 ? 1.2255 0.8103 0.8878 0.1423  -0.3733 -0.1825 257 ASP C N   
6961  C CA  . ASP C 193 ? 1.2748 0.8416 0.8988 0.1592  -0.3737 -0.1925 257 ASP C CA  
6962  C C   . ASP C 193 ? 1.3650 0.9379 0.9702 0.1702  -0.3562 -0.1996 257 ASP C C   
6963  O O   . ASP C 193 ? 1.5600 1.1238 1.1592 0.1772  -0.3647 -0.2075 257 ASP C O   
6964  C CB  . ASP C 193 ? 1.2889 0.8253 0.8987 0.1675  -0.4032 -0.2005 257 ASP C CB  
6965  C CG  . ASP C 193 ? 1.5202 1.0374 1.0873 0.1868  -0.4049 -0.2110 257 ASP C CG  
6966  O OD1 . ASP C 193 ? 1.8868 1.4156 1.4359 0.1932  -0.3821 -0.2106 257 ASP C OD1 
6967  O OD2 . ASP C 193 ? 1.5026 0.9929 1.0539 0.1960  -0.4300 -0.2192 257 ASP C OD2 
6968  N N   . THR C 194 ? 1.7113 1.2998 1.3082 0.1716  -0.3325 -0.1964 258 THR C N   
6969  C CA  . THR C 194 ? 1.6438 1.2457 1.2304 0.1787  -0.3120 -0.1999 258 THR C CA  
6970  C C   . THR C 194 ? 1.8659 1.4568 1.4130 0.1971  -0.3074 -0.2070 258 THR C C   
6971  O O   . THR C 194 ? 2.0163 1.6161 1.5508 0.2067  -0.2937 -0.2116 258 THR C O   
6972  C CB  . THR C 194 ? 1.6595 1.2880 1.2665 0.1669  -0.2882 -0.1901 258 THR C CB  
6973  O OG1 . THR C 194 ? 2.2332 1.8770 1.8380 0.1715  -0.2703 -0.1929 258 THR C OG1 
6974  C CG2 . THR C 194 ? 1.5866 1.2147 1.1813 0.1669  -0.2796 -0.1841 258 THR C CG2 
6975  N N   . THR C 195 ? 1.8919 1.4648 1.4196 0.2025  -0.3188 -0.2075 259 THR C N   
6976  C CA  . THR C 195 ? 1.8929 1.4590 1.3828 0.2183  -0.3103 -0.2103 259 THR C CA  
6977  C C   . THR C 195 ? 1.5658 1.1300 1.0290 0.2370  -0.3060 -0.2210 259 THR C C   
6978  O O   . THR C 195 ? 1.3288 0.8788 0.7872 0.2451  -0.3237 -0.2316 259 THR C O   
6979  C CB  . THR C 195 ? 2.0367 1.5782 1.5052 0.2248  -0.3294 -0.2122 259 THR C CB  
6980  O OG1 . THR C 195 ? 1.8110 1.3290 1.2760 0.2307  -0.3579 -0.2222 259 THR C OG1 
6981  C CG2 . THR C 195 ? 1.9461 1.4931 1.4368 0.2089  -0.3289 -0.2009 259 THR C CG2 
6982  N N   . GLY C 196 ? 1.5091 1.0886 0.9559 0.2437  -0.2824 -0.2174 260 GLY C N   
6983  C CA  . GLY C 196 ? 1.6662 1.2505 1.0890 0.2620  -0.2739 -0.2259 260 GLY C CA  
6984  C C   . GLY C 196 ? 1.6409 1.2510 1.0884 0.2555  -0.2565 -0.2244 260 GLY C C   
6985  O O   . GLY C 196 ? 1.8569 1.4802 1.2898 0.2682  -0.2420 -0.2280 260 GLY C O   
6986  N N   . PHE C 197 ? 1.4904 1.1091 0.9752 0.2366  -0.2581 -0.2190 261 PHE C N   
6987  C CA  . PHE C 197 ? 1.4090 1.0527 0.9189 0.2293  -0.2417 -0.2168 261 PHE C CA  
6988  C C   . PHE C 197 ? 1.3499 1.0100 0.8951 0.2076  -0.2319 -0.2049 261 PHE C C   
6989  O O   . PHE C 197 ? 1.6133 1.2683 1.1617 0.1991  -0.2338 -0.1974 261 PHE C O   
6990  C CB  . PHE C 197 ? 1.2746 0.9121 0.7892 0.2355  -0.2555 -0.2280 261 PHE C CB  
6991  C CG  . PHE C 197 ? 1.2794 0.9036 0.8170 0.2231  -0.2769 -0.2275 261 PHE C CG  
6992  C CD1 . PHE C 197 ? 1.2551 0.8950 0.8266 0.2079  -0.2723 -0.2222 261 PHE C CD1 
6993  C CD2 . PHE C 197 ? 1.3636 0.9599 0.8890 0.2270  -0.3023 -0.2321 261 PHE C CD2 
6994  C CE1 . PHE C 197 ? 1.3030 0.9329 0.8957 0.1965  -0.2910 -0.2198 261 PHE C CE1 
6995  C CE2 . PHE C 197 ? 1.2880 0.8742 0.8377 0.2143  -0.3220 -0.2296 261 PHE C CE2 
6996  C CZ  . PHE C 197 ? 1.2238 0.8275 0.8067 0.1991  -0.3155 -0.2228 261 PHE C CZ  
6997  N N   . ASN C 198 ? 1.2059 0.8855 0.7763 0.2001  -0.2218 -0.2039 262 ASN C N   
6998  C CA  . ASN C 198 ? 1.1504 0.8471 0.7526 0.1821  -0.2117 -0.1942 262 ASN C CA  
6999  C C   . ASN C 198 ? 1.3154 1.0213 0.9442 0.1750  -0.2157 -0.1968 262 ASN C C   
7000  O O   . ASN C 198 ? 1.5022 1.2108 1.1273 0.1839  -0.2161 -0.2048 262 ASN C O   
7001  C CB  . ASN C 198 ? 1.1687 0.8845 0.7708 0.1804  -0.1877 -0.1868 262 ASN C CB  
7002  C CG  . ASN C 198 ? 1.3249 1.0621 0.9600 0.1660  -0.1756 -0.1809 262 ASN C CG  
7003  O OD1 . ASN C 198 ? 1.5060 1.2607 1.1509 0.1675  -0.1639 -0.1828 262 ASN C OD1 
7004  N ND2 . ASN C 198 ? 1.2457 0.9822 0.8980 0.1532  -0.1790 -0.1742 262 ASN C ND2 
7005  N N   . PHE C 199 ? 1.1832 0.8944 0.8378 0.1602  -0.2187 -0.1902 263 PHE C N   
7006  C CA  . PHE C 199 ? 1.0765 0.7917 0.7535 0.1534  -0.2272 -0.1913 263 PHE C CA  
7007  C C   . PHE C 199 ? 1.0063 0.7417 0.7114 0.1397  -0.2161 -0.1838 263 PHE C C   
7008  O O   . PHE C 199 ? 1.2201 0.9554 0.9387 0.1301  -0.2219 -0.1774 263 PHE C O   
7009  C CB  . PHE C 199 ? 0.9995 0.6945 0.6760 0.1513  -0.2503 -0.1914 263 PHE C CB  
7010  C CG  . PHE C 199 ? 0.9799 0.6757 0.6765 0.1451  -0.2615 -0.1912 263 PHE C CG  
7011  C CD1 . PHE C 199 ? 1.0573 0.7487 0.7491 0.1532  -0.2668 -0.1994 263 PHE C CD1 
7012  C CD2 . PHE C 199 ? 1.0609 0.7620 0.7803 0.1318  -0.2672 -0.1824 263 PHE C CD2 
7013  C CE1 . PHE C 199 ? 1.0963 0.7867 0.8059 0.1472  -0.2781 -0.1980 263 PHE C CE1 
7014  C CE2 . PHE C 199 ? 1.2408 0.9435 0.9784 0.1257  -0.2771 -0.1801 263 PHE C CE2 
7015  C CZ  . PHE C 199 ? 1.1822 0.8786 0.9149 0.1329  -0.2828 -0.1875 263 PHE C CZ  
7016  N N   . GLU C 200 ? 1.0394 0.7929 0.7538 0.1398  -0.2009 -0.1849 264 GLU C N   
7017  C CA  . GLU C 200 ? 1.0370 0.8089 0.7753 0.1286  -0.1899 -0.1789 264 GLU C CA  
7018  C C   . GLU C 200 ? 0.9928 0.7769 0.7511 0.1253  -0.1902 -0.1812 264 GLU C C   
7019  O O   . GLU C 200 ? 1.1588 0.9425 0.9133 0.1324  -0.1926 -0.1879 264 GLU C O   
7020  C CB  . GLU C 200 ? 0.9422 0.7261 0.6785 0.1293  -0.1717 -0.1766 264 GLU C CB  
7021  C CG  . GLU C 200 ? 1.0782 0.8513 0.7948 0.1320  -0.1695 -0.1725 264 GLU C CG  
7022  C CD  . GLU C 200 ? 1.3655 1.1402 1.0937 0.1217  -0.1677 -0.1647 264 GLU C CD  
7023  O OE1 . GLU C 200 ? 1.3257 1.1128 1.0774 0.1134  -0.1656 -0.1630 264 GLU C OE1 
7024  O OE2 . GLU C 200 ? 1.2480 1.0111 0.9604 0.1233  -0.1690 -0.1609 264 GLU C OE2 
7025  N N   . PHE C 201 ? 0.8954 0.6904 0.6739 0.1155  -0.1882 -0.1761 265 PHE C N   
7026  C CA  . PHE C 201 ? 0.8225 0.6298 0.6189 0.1126  -0.1880 -0.1776 265 PHE C CA  
7027  C C   . PHE C 201 ? 0.7301 0.5272 0.5239 0.1159  -0.2026 -0.1807 265 PHE C C   
7028  O O   . PHE C 201 ? 1.0586 0.8598 0.8546 0.1207  -0.2020 -0.1864 265 PHE C O   
7029  C CB  . PHE C 201 ? 0.8561 0.6782 0.6578 0.1156  -0.1738 -0.1818 265 PHE C CB  
7030  C CG  . PHE C 201 ? 0.8577 0.6872 0.6612 0.1123  -0.1605 -0.1779 265 PHE C CG  
7031  C CD1 . PHE C 201 ? 0.9652 0.8009 0.7828 0.1038  -0.1582 -0.1727 265 PHE C CD1 
7032  C CD2 . PHE C 201 ? 0.8336 0.6642 0.6249 0.1181  -0.1507 -0.1789 265 PHE C CD2 
7033  C CE1 . PHE C 201 ? 1.0811 0.9209 0.9010 0.1003  -0.1478 -0.1687 265 PHE C CE1 
7034  C CE2 . PHE C 201 ? 0.8985 0.7354 0.6927 0.1138  -0.1387 -0.1732 265 PHE C CE2 
7035  C CZ  . PHE C 201 ? 0.9230 0.7627 0.7315 0.1045  -0.1382 -0.1681 265 PHE C CZ  
7036  N N   . PRO C 202 ? 0.6813 0.4647 0.4717 0.1133  -0.2168 -0.1769 266 PRO C N   
7037  C CA  . PRO C 202 ? 0.7785 0.5505 0.5689 0.1150  -0.2327 -0.1784 266 PRO C CA  
7038  C C   . PRO C 202 ? 0.7777 0.5626 0.5872 0.1096  -0.2328 -0.1754 266 PRO C C   
7039  O O   . PRO C 202 ? 0.9036 0.7033 0.7277 0.1024  -0.2264 -0.1693 266 PRO C O   
7040  C CB  . PRO C 202 ? 0.7437 0.5022 0.5328 0.1101  -0.2470 -0.1721 266 PRO C CB  
7041  C CG  . PRO C 202 ? 0.7463 0.5155 0.5415 0.1042  -0.2373 -0.1662 266 PRO C CG  
7042  C CD  . PRO C 202 ? 0.7024 0.4791 0.4896 0.1090  -0.2207 -0.1709 266 PRO C CD  
7043  N N   . THR C 203 ? 0.8893 0.6681 0.6970 0.1145  -0.2403 -0.1802 267 THR C N   
7044  C CA  . THR C 203 ? 0.9299 0.7193 0.7529 0.1108  -0.2412 -0.1776 267 THR C CA  
7045  C C   . THR C 203 ? 0.9041 0.6760 0.7265 0.1097  -0.2610 -0.1745 267 THR C C   
7046  O O   . THR C 203 ? 0.9873 0.7401 0.7954 0.1172  -0.2720 -0.1812 267 THR C O   
7047  C CB  . THR C 203 ? 0.9540 0.7544 0.7778 0.1177  -0.2306 -0.1865 267 THR C CB  
7048  O OG1 . THR C 203 ? 1.1314 0.9432 0.9701 0.1141  -0.2307 -0.1837 267 THR C OG1 
7049  C CG2 . THR C 203 ? 1.0422 0.8282 0.8504 0.1293  -0.2377 -0.1964 267 THR C CG2 
7050  N N   . CYS C 204 ? 0.8658 0.6441 0.7035 0.1005  -0.2662 -0.1638 268 CYS C N   
7051  C CA  . CYS C 204 ? 0.8067 0.5691 0.6472 0.0956  -0.2852 -0.1563 268 CYS C CA  
7052  C C   . CYS C 204 ? 0.7437 0.5086 0.5965 0.0910  -0.2930 -0.1488 268 CYS C C   
7053  O O   . CYS C 204 ? 1.1223 0.9058 0.9842 0.0895  -0.2826 -0.1464 268 CYS C O   
7054  C CB  . CYS C 204 ? 0.9609 0.7287 0.8097 0.0868  -0.2856 -0.1459 268 CYS C CB  
7055  S SG  . CYS C 204 ? 1.2891 1.0527 1.1232 0.0913  -0.2776 -0.1524 268 CYS C SG  
7056  N N   . TYR C 205 ? 0.7655 0.5110 0.6188 0.0885  -0.3125 -0.1444 269 TYR C N   
7057  C CA  . TYR C 205 ? 0.8165 0.5643 0.6838 0.0813  -0.3214 -0.1326 269 TYR C CA  
7058  C C   . TYR C 205 ? 0.9336 0.6649 0.8082 0.0727  -0.3414 -0.1215 269 TYR C C   
7059  O O   . TYR C 205 ? 1.1201 0.8370 0.9879 0.0737  -0.3493 -0.1249 269 TYR C O   
7060  C CB  . TYR C 205 ? 0.8098 0.5486 0.6709 0.0891  -0.3263 -0.1406 269 TYR C CB  
7061  C CG  . TYR C 205 ? 0.8137 0.5245 0.6593 0.0984  -0.3418 -0.1522 269 TYR C CG  
7062  C CD1 . TYR C 205 ? 0.9675 0.6555 0.8149 0.0964  -0.3643 -0.1478 269 TYR C CD1 
7063  C CD2 . TYR C 205 ? 0.8677 0.5741 0.6962 0.1097  -0.3349 -0.1672 269 TYR C CD2 
7064  C CE1 . TYR C 205 ? 1.0195 0.6792 0.8511 0.1068  -0.3812 -0.1600 269 TYR C CE1 
7065  C CE2 . TYR C 205 ? 1.0998 0.7807 0.9114 0.1207  -0.3496 -0.1788 269 TYR C CE2 
7066  C CZ  . TYR C 205 ? 1.0782 0.7350 0.8910 0.1198  -0.3735 -0.1761 269 TYR C CZ  
7067  O OH  . TYR C 205 ? 1.1582 0.7880 0.9533 0.1322  -0.3902 -0.1889 269 TYR C OH  
7068  N N   . TYR C 206 ? 0.9618 0.6949 0.8507 0.0644  -0.3504 -0.1076 270 TYR C N   
7069  C CA  . TYR C 206 ? 0.9410 0.6621 0.8425 0.0536  -0.3692 -0.0936 270 TYR C CA  
7070  C C   . TYR C 206 ? 0.9800 0.6794 0.8830 0.0525  -0.3890 -0.0903 270 TYR C C   
7071  O O   . TYR C 206 ? 1.0241 0.7317 0.9301 0.0528  -0.3849 -0.0865 270 TYR C O   
7072  C CB  . TYR C 206 ? 0.8773 0.6263 0.8002 0.0413  -0.3608 -0.0742 270 TYR C CB  
7073  C CG  . TYR C 206 ? 0.9432 0.6842 0.8844 0.0284  -0.3798 -0.0565 270 TYR C CG  
7074  C CD1 . TYR C 206 ? 1.1540 0.9013 1.1105 0.0195  -0.3858 -0.0391 270 TYR C CD1 
7075  C CD2 . TYR C 206 ? 1.1373 0.8639 1.0808 0.0250  -0.3929 -0.0566 270 TYR C CD2 
7076  C CE1 . TYR C 206 ? 1.1608 0.9019 1.1373 0.0061  -0.4038 -0.0205 270 TYR C CE1 
7077  C CE2 . TYR C 206 ? 1.3096 1.0289 1.2733 0.0121  -0.4122 -0.0397 270 TYR C CE2 
7078  C CZ  . TYR C 206 ? 1.2051 0.9324 1.1864 0.0021  -0.4171 -0.0211 270 TYR C CZ  
7079  O OH  . TYR C 206 ? 1.3846 1.1063 1.3888 -0.0121 -0.4360 -0.0021 270 TYR C OH  
7080  N N   . THR C 207 ? 1.0224 0.6924 0.9224 0.0520  -0.4118 -0.0921 271 THR C N   
7081  C CA  . THR C 207 ? 1.1439 0.7893 1.0485 0.0487  -0.4356 -0.0863 271 THR C CA  
7082  C C   . THR C 207 ? 1.1195 0.7398 1.0317 0.0413  -0.4612 -0.0803 271 THR C C   
7083  O O   . THR C 207 ? 1.2399 0.8532 1.1443 0.0449  -0.4631 -0.0887 271 THR C O   
7084  C CB  . THR C 207 ? 1.2380 0.8636 1.1220 0.0642  -0.4406 -0.1050 271 THR C CB  
7085  O OG1 . THR C 207 ? 1.8832 1.4842 1.7726 0.0606  -0.4646 -0.0981 271 THR C OG1 
7086  C CG2 . THR C 207 ? 1.1999 0.8065 1.0615 0.0784  -0.4446 -0.1258 271 THR C CG2 
7087  N N   . SER C 208 ? 1.1472 0.7537 1.0752 0.0307  -0.4815 -0.0651 272 SER C N   
7088  C CA  . SER C 208 ? 1.3223 0.8988 1.2581 0.0243  -0.5110 -0.0607 272 SER C CA  
7089  C C   . SER C 208 ? 1.2049 0.7915 1.1503 0.0176  -0.5091 -0.0563 272 SER C C   
7090  O O   . SER C 208 ? 1.2275 0.7891 1.1633 0.0227  -0.5259 -0.0672 272 SER C O   
7091  C CB  . SER C 208 ? 1.5288 1.0662 1.4395 0.0406  -0.5305 -0.0832 272 SER C CB  
7092  O OG  . SER C 208 ? 2.0775 1.5814 1.9962 0.0346  -0.5634 -0.0789 272 SER C OG  
7093  N N   . GLY C 209 ? 1.0286 0.6521 0.9915 0.0077  -0.4887 -0.0410 273 GLY C N   
7094  C CA  . GLY C 209 ? 1.0582 0.6957 1.0335 0.0007  -0.4858 -0.0346 273 GLY C CA  
7095  C C   . GLY C 209 ? 1.1039 0.7403 1.0570 0.0136  -0.4745 -0.0545 273 GLY C C   
7096  O O   . GLY C 209 ? 1.2343 0.8741 1.1944 0.0096  -0.4774 -0.0519 273 GLY C O   
7097  N N   . LYS C 210 ? 0.9944 0.6268 0.9215 0.0290  -0.4620 -0.0734 274 LYS C N   
7098  C CA  . LYS C 210 ? 1.0648 0.6962 0.9696 0.0415  -0.4504 -0.0911 274 LYS C CA  
7099  C C   . LYS C 210 ? 1.1142 0.7679 1.0068 0.0502  -0.4228 -0.0999 274 LYS C C   
7100  O O   . LYS C 210 ? 1.4702 1.1267 1.3603 0.0535  -0.4180 -0.1017 274 LYS C O   
7101  C CB  . LYS C 210 ? 1.2277 0.8216 1.1089 0.0544  -0.4704 -0.1091 274 LYS C CB  
7102  C CG  . LYS C 210 ? 1.7408 1.3132 1.6313 0.0476  -0.4965 -0.1041 274 LYS C CG  
7103  C CD  . LYS C 210 ? 1.7896 1.3222 1.6552 0.0618  -0.5196 -0.1226 274 LYS C CD  
7104  C CE  . LYS C 210 ? 1.8385 1.3444 1.7042 0.0634  -0.5421 -0.1241 274 LYS C CE  
7105  N NZ  . LYS C 210 ? 1.7498 1.2152 1.6071 0.0684  -0.5759 -0.1325 274 LYS C NZ  
7106  N N   . VAL C 211 ? 1.1231 0.7925 1.0092 0.0535  -0.4055 -0.1047 275 VAL C N   
7107  C CA  . VAL C 211 ? 0.8991 0.5877 0.7739 0.0617  -0.3804 -0.1138 275 VAL C CA  
7108  C C   . VAL C 211 ? 0.9325 0.6024 0.7802 0.0768  -0.3806 -0.1332 275 VAL C C   
7109  O O   . VAL C 211 ? 1.2375 0.8902 1.0743 0.0806  -0.3909 -0.1386 275 VAL C O   
7110  C CB  . VAL C 211 ? 0.7822 0.4988 0.6659 0.0570  -0.3614 -0.1077 275 VAL C CB  
7111  C CG1 . VAL C 211 ? 0.7305 0.4604 0.6004 0.0664  -0.3391 -0.1195 275 VAL C CG1 
7112  C CG2 . VAL C 211 ? 0.7108 0.4512 0.6206 0.0441  -0.3584 -0.0884 275 VAL C CG2 
7113  N N   . LYS C 212 ? 0.9645 0.6392 0.8015 0.0860  -0.3689 -0.1433 276 LYS C N   
7114  C CA  . LYS C 212 ? 0.9325 0.5919 0.7444 0.1018  -0.3687 -0.1611 276 LYS C CA  
7115  C C   . LYS C 212 ? 0.9327 0.6150 0.7388 0.1073  -0.3427 -0.1674 276 LYS C C   
7116  O O   . LYS C 212 ? 1.0457 0.7454 0.8612 0.1057  -0.3313 -0.1656 276 LYS C O   
7117  C CB  . LYS C 212 ? 0.9698 0.6098 0.7758 0.1088  -0.3842 -0.1677 276 LYS C CB  
7118  C CG  . LYS C 212 ? 1.0868 0.7026 0.9016 0.1015  -0.4119 -0.1598 276 LYS C CG  
7119  C CD  . LYS C 212 ? 1.2881 0.8816 1.0960 0.1092  -0.4292 -0.1670 276 LYS C CD  
7120  C CE  . LYS C 212 ? 1.6200 1.1866 1.4382 0.1007  -0.4592 -0.1581 276 LYS C CE  
7121  N NZ  . LYS C 212 ? 1.7099 1.2486 1.5189 0.1098  -0.4802 -0.1668 276 LYS C NZ  
7122  N N   . CYS C 213 ? 1.0123 0.6936 0.8031 0.1138  -0.3347 -0.1744 277 CYS C N   
7123  C CA  . CYS C 213 ? 0.9660 0.6683 0.7532 0.1170  -0.3107 -0.1781 277 CYS C CA  
7124  C C   . CYS C 213 ? 0.9122 0.6082 0.6762 0.1324  -0.3045 -0.1924 277 CYS C C   
7125  O O   . CYS C 213 ? 0.8743 0.5513 0.6194 0.1409  -0.3144 -0.1989 277 CYS C O   
7126  C CB  . CYS C 213 ? 0.9650 0.6758 0.7567 0.1097  -0.3039 -0.1706 277 CYS C CB  
7127  S SG  . CYS C 213 ? 1.5525 1.2818 1.3735 0.0932  -0.3041 -0.1534 277 CYS C SG  
7128  N N   . THR C 214 ? 0.9279 0.6417 0.6939 0.1365  -0.2877 -0.1970 278 THR C N   
7129  C CA  . THR C 214 ? 0.9745 0.6898 0.7220 0.1503  -0.2775 -0.2083 278 THR C CA  
7130  C C   . THR C 214 ? 0.9167 0.6498 0.6640 0.1478  -0.2567 -0.2054 278 THR C C   
7131  O O   . THR C 214 ? 1.2310 0.9849 0.9944 0.1412  -0.2424 -0.2015 278 THR C O   
7132  C CB  . THR C 214 ? 1.1088 0.8333 0.8603 0.1570  -0.2729 -0.2154 278 THR C CB  
7133  O OG1 . THR C 214 ? 1.1307 0.8375 0.8837 0.1583  -0.2933 -0.2169 278 THR C OG1 
7134  C CG2 . THR C 214 ? 1.1573 0.8850 0.8903 0.1726  -0.2633 -0.2269 278 THR C CG2 
7135  N N   . GLY C 215 ? 0.9399 0.6638 0.6686 0.1535  -0.2560 -0.2075 279 GLY C N   
7136  C CA  . GLY C 215 ? 0.9195 0.6577 0.6466 0.1513  -0.2372 -0.2038 279 GLY C CA  
7137  C C   . GLY C 215 ? 1.0109 0.7613 0.7277 0.1620  -0.2211 -0.2103 279 GLY C C   
7138  O O   . GLY C 215 ? 0.9084 0.6593 0.6202 0.1722  -0.2229 -0.2189 279 GLY C O   
7139  N N   . THR C 216 ? 1.0116 0.7723 0.7256 0.1598  -0.2057 -0.2057 280 THR C N   
7140  C CA  . THR C 216 ? 1.0717 0.8478 0.7793 0.1676  -0.1880 -0.2084 280 THR C CA  
7141  C C   . THR C 216 ? 1.2151 0.9849 0.9014 0.1719  -0.1823 -0.2051 280 THR C C   
7142  O O   . THR C 216 ? 1.1796 0.9475 0.8704 0.1623  -0.1806 -0.1970 280 THR C O   
7143  C CB  . THR C 216 ? 0.9659 0.7658 0.6993 0.1574  -0.1727 -0.2033 280 THR C CB  
7144  O OG1 . THR C 216 ? 1.1998 1.0076 0.9471 0.1588  -0.1758 -0.2089 280 THR C OG1 
7145  C CG2 . THR C 216 ? 0.8731 0.6893 0.6036 0.1600  -0.1532 -0.2005 280 THR C CG2 
7146  N N   . ASN C 217 ? 1.3445 1.1102 1.0062 0.1876  -0.1804 -0.2117 281 ASN C N   
7147  C CA  . ASN C 217 ? 1.1883 0.9474 0.8248 0.1945  -0.1752 -0.2089 281 ASN C CA  
7148  C C   . ASN C 217 ? 1.1669 0.9498 0.8057 0.1949  -0.1511 -0.2027 281 ASN C C   
7149  O O   . ASN C 217 ? 1.0850 0.8826 0.7190 0.2059  -0.1409 -0.2073 281 ASN C O   
7150  C CB  . ASN C 217 ? 1.2761 1.0157 0.8808 0.2131  -0.1884 -0.2194 281 ASN C CB  
7151  C CG  . ASN C 217 ? 1.2354 0.9631 0.8112 0.2207  -0.1874 -0.2167 281 ASN C CG  
7152  O OD1 . ASN C 217 ? 1.2950 1.0355 0.8697 0.2168  -0.1702 -0.2076 281 ASN C OD1 
7153  N ND2 . ASN C 217 ? 1.1473 0.8492 0.6992 0.2317  -0.2073 -0.2247 281 ASN C ND2 
7154  N N   . LEU C 218 ? 1.0243 0.8114 0.6718 0.1829  -0.1424 -0.1918 282 LEU C N   
7155  C CA  . LEU C 218 ? 1.1316 0.9406 0.7871 0.1794  -0.1209 -0.1835 282 LEU C CA  
7156  C C   . LEU C 218 ? 1.2109 1.0165 0.8374 0.1894  -0.1127 -0.1791 282 LEU C C   
7157  O O   . LEU C 218 ? 1.3478 1.1699 0.9784 0.1860  -0.0948 -0.1693 282 LEU C O   
7158  C CB  . LEU C 218 ? 1.2272 1.0416 0.9075 0.1615  -0.1162 -0.1736 282 LEU C CB  
7159  C CG  . LEU C 218 ? 1.2124 1.0382 0.9246 0.1509  -0.1179 -0.1754 282 LEU C CG  
7160  C CD1 . LEU C 218 ? 1.3162 1.1253 1.0320 0.1453  -0.1355 -0.1773 282 LEU C CD1 
7161  C CD2 . LEU C 218 ? 1.4060 1.2468 1.1399 0.1385  -0.1047 -0.1659 282 LEU C CD2 
7162  N N   . TRP C 219 ? 1.1833 0.9669 0.7804 0.2016  -0.1267 -0.1857 283 TRP C N   
7163  C CA  . TRP C 219 ? 1.2629 1.0392 0.8270 0.2131  -0.1218 -0.1823 283 TRP C CA  
7164  C C   . TRP C 219 ? 1.3174 1.0966 0.8535 0.2352  -0.1194 -0.1914 283 TRP C C   
7165  O O   . TRP C 219 ? 1.2543 1.0557 0.7863 0.2417  -0.1000 -0.1868 283 TRP C O   
7166  C CB  . TRP C 219 ? 1.1987 0.9470 0.7483 0.2111  -0.1397 -0.1823 283 TRP C CB  
7167  C CG  . TRP C 219 ? 1.2353 0.9711 0.7482 0.2237  -0.1389 -0.1800 283 TRP C CG  
7168  C CD1 . TRP C 219 ? 1.3572 1.1066 0.8522 0.2316  -0.1197 -0.1724 283 TRP C CD1 
7169  C CD2 . TRP C 219 ? 1.3334 1.0403 0.8220 0.2300  -0.1587 -0.1843 283 TRP C CD2 
7170  N NE1 . TRP C 219 ? 1.5527 1.2833 1.0122 0.2431  -0.1259 -0.1720 283 TRP C NE1 
7171  C CE2 . TRP C 219 ? 1.4516 1.1556 0.9057 0.2428  -0.1498 -0.1797 283 TRP C CE2 
7172  C CE3 . TRP C 219 ? 1.4383 1.1230 0.9315 0.2259  -0.1824 -0.1903 283 TRP C CE3 
7173  C CZ2 . TRP C 219 ? 1.4503 1.1282 0.8740 0.2523  -0.1653 -0.1828 283 TRP C CZ2 
7174  C CZ3 . TRP C 219 ? 1.4332 1.0929 0.8988 0.2344  -0.1982 -0.1930 283 TRP C CZ3 
7175  C CH2 . TRP C 219 ? 1.4210 1.0765 0.8518 0.2478  -0.1903 -0.1901 283 TRP C CH2 
7176  N N   . ASN C 220 ? 1.3507 1.1080 0.8682 0.2473  -0.1398 -0.2043 284 ASN C N   
7177  C CA  . ASN C 220 ? 1.2300 0.9832 0.7135 0.2714  -0.1419 -0.2146 284 ASN C CA  
7178  C C   . ASN C 220 ? 1.4734 1.2237 0.9609 0.2812  -0.1545 -0.2296 284 ASN C C   
7179  O O   . ASN C 220 ? 1.7590 1.4943 1.2171 0.3015  -0.1669 -0.2420 284 ASN C O   
7180  C CB  . ASN C 220 ? 1.2314 0.9543 0.6821 0.2803  -0.1589 -0.2178 284 ASN C CB  
7181  C CG  . ASN C 220 ? 1.3071 1.0045 0.7709 0.2688  -0.1840 -0.2215 284 ASN C CG  
7182  O OD1 . ASN C 220 ? 1.5632 1.2632 1.0551 0.2584  -0.1909 -0.2242 284 ASN C OD1 
7183  N ND2 . ASN C 220 ? 1.3222 0.9960 0.7664 0.2707  -0.1977 -0.2209 284 ASN C ND2 
7184  N N   . ASP C 221 ? 1.4632 1.2265 0.9854 0.2681  -0.1527 -0.2290 285 ASP C N   
7185  C CA  . ASP C 221 ? 1.4014 1.1581 0.9298 0.2749  -0.1677 -0.2423 285 ASP C CA  
7186  C C   . ASP C 221 ? 1.3637 1.1462 0.9248 0.2673  -0.1564 -0.2418 285 ASP C C   
7187  O O   . ASP C 221 ? 1.1926 0.9877 0.7842 0.2479  -0.1484 -0.2321 285 ASP C O   
7188  C CB  . ASP C 221 ? 1.5731 1.2993 1.1050 0.2668  -0.1942 -0.2455 285 ASP C CB  
7189  C CG  . ASP C 221 ? 1.8588 1.5698 1.3883 0.2768  -0.2144 -0.2593 285 ASP C CG  
7190  O OD1 . ASP C 221 ? 1.8100 1.5320 1.3311 0.2928  -0.2092 -0.2685 285 ASP C OD1 
7191  O OD2 . ASP C 221 ? 2.2172 1.9054 1.7541 0.2687  -0.2361 -0.2604 285 ASP C OD2 
7192  N N   . ALA C 222 ? 1.2660 1.0555 0.8195 0.2844  -0.1574 -0.2535 286 ALA C N   
7193  C CA  . ALA C 222 ? 1.3078 1.1202 0.8885 0.2817  -0.1495 -0.2561 286 ALA C CA  
7194  C C   . ALA C 222 ? 1.3717 1.1650 0.9613 0.2812  -0.1724 -0.2661 286 ALA C C   
7195  O O   . ALA C 222 ? 1.4224 1.2301 1.0336 0.2794  -0.1700 -0.2693 286 ALA C O   
7196  C CB  . ALA C 222 ? 1.5112 1.3480 1.0801 0.3015  -0.1339 -0.2616 286 ALA C CB  
7197  N N   . LYS C 223 ? 1.3280 1.0886 0.9012 0.2831  -0.1952 -0.2704 287 LYS C N   
7198  C CA  . LYS C 223 ? 1.3544 1.0945 0.9400 0.2767  -0.2179 -0.2750 287 LYS C CA  
7199  C C   . LYS C 223 ? 1.4031 1.1384 1.0110 0.2527  -0.2207 -0.2621 287 LYS C C   
7200  O O   . LYS C 223 ? 1.3158 1.0611 0.9272 0.2430  -0.2068 -0.2516 287 LYS C O   
7201  C CB  . LYS C 223 ? 1.3261 1.0327 0.8835 0.2922  -0.2435 -0.2868 287 LYS C CB  
7202  C CG  . LYS C 223 ? 1.3926 1.0996 0.9224 0.3194  -0.2443 -0.3016 287 LYS C CG  
7203  C CD  . LYS C 223 ? 1.5270 1.1949 1.0345 0.3314  -0.2759 -0.3136 287 LYS C CD  
7204  C CE  . LYS C 223 ? 1.6268 1.2886 1.0988 0.3617  -0.2806 -0.3300 287 LYS C CE  
7205  N NZ  . LYS C 223 ? 1.7344 1.3566 1.1914 0.3720  -0.3151 -0.3430 287 LYS C NZ  
7206  N N   . ARG C 224 ? 1.4262 1.1465 1.0490 0.2437  -0.2389 -0.2623 288 ARG C N   
7207  C CA  . ARG C 224 ? 1.2397 0.9580 0.8834 0.2227  -0.2415 -0.2502 288 ARG C CA  
7208  C C   . ARG C 224 ? 1.2301 0.9180 0.8640 0.2209  -0.2657 -0.2502 288 ARG C C   
7209  O O   . ARG C 224 ? 1.1597 0.8274 0.7883 0.2275  -0.2864 -0.2577 288 ARG C O   
7210  C CB  . ARG C 224 ? 1.2051 0.9365 0.8787 0.2107  -0.2398 -0.2464 288 ARG C CB  
7211  C CG  . ARG C 224 ? 1.2175 0.9747 0.9004 0.2165  -0.2227 -0.2507 288 ARG C CG  
7212  C CD  . ARG C 224 ? 1.1029 0.8758 0.8159 0.2021  -0.2176 -0.2445 288 ARG C CD  
7213  N NE  . ARG C 224 ? 1.1449 0.9387 0.8712 0.1914  -0.1980 -0.2355 288 ARG C NE  
7214  C CZ  . ARG C 224 ? 1.0981 0.9172 0.8394 0.1907  -0.1812 -0.2354 288 ARG C CZ  
7215  N NH1 . ARG C 224 ? 1.5754 1.4034 1.3206 0.2003  -0.1810 -0.2439 288 ARG C NH1 
7216  N NH2 . ARG C 224 ? 0.9433 0.7780 0.6972 0.1803  -0.1660 -0.2269 288 ARG C NH2 
7217  N N   . PRO C 225 ? 1.1497 0.8335 0.7818 0.2122  -0.2643 -0.2418 289 PRO C N   
7218  C CA  . PRO C 225 ? 1.1130 0.7718 0.7431 0.2067  -0.2867 -0.2394 289 PRO C CA  
7219  C C   . PRO C 225 ? 1.1165 0.7731 0.7734 0.1928  -0.2989 -0.2338 289 PRO C C   
7220  O O   . PRO C 225 ? 1.2900 0.9676 0.9688 0.1835  -0.2861 -0.2283 289 PRO C O   
7221  C CB  . PRO C 225 ? 1.0150 0.6806 0.6479 0.1964  -0.2764 -0.2290 289 PRO C CB  
7222  C CG  . PRO C 225 ? 1.0591 0.7432 0.6801 0.2042  -0.2531 -0.2299 289 PRO C CG  
7223  C CD  . PRO C 225 ? 1.0577 0.7604 0.6914 0.2066  -0.2424 -0.2336 289 PRO C CD  
7224  N N   . PHE C 226 ? 1.0147 0.6460 0.6699 0.1918  -0.3240 -0.2347 290 PHE C N   
7225  C CA  . PHE C 226 ? 0.9324 0.5607 0.6124 0.1784  -0.3369 -0.2273 290 PHE C CA  
7226  C C   . PHE C 226 ? 0.9835 0.5965 0.6710 0.1677  -0.3543 -0.2189 290 PHE C C   
7227  O O   . PHE C 226 ? 1.1352 0.7279 0.8042 0.1752  -0.3674 -0.2241 290 PHE C O   
7228  C CB  . PHE C 226 ? 0.9516 0.5637 0.6259 0.1884  -0.3531 -0.2368 290 PHE C CB  
7229  C CG  . PHE C 226 ? 1.0152 0.6294 0.7149 0.1757  -0.3613 -0.2287 290 PHE C CG  
7230  C CD1 . PHE C 226 ? 1.0240 0.6597 0.7367 0.1739  -0.3462 -0.2280 290 PHE C CD1 
7231  C CD2 . PHE C 226 ? 1.0621 0.6566 0.7731 0.1659  -0.3848 -0.2213 290 PHE C CD2 
7232  C CE1 . PHE C 226 ? 0.9932 0.6302 0.7269 0.1634  -0.3539 -0.2201 290 PHE C CE1 
7233  C CE2 . PHE C 226 ? 1.0910 0.6881 0.8249 0.1542  -0.3919 -0.2118 290 PHE C CE2 
7234  C CZ  . PHE C 226 ? 0.9664 0.5842 0.7102 0.1536  -0.3765 -0.2114 290 PHE C CZ  
7235  N N   . LEU C 227 ? 1.0270 0.6509 0.7421 0.1506  -0.3547 -0.2058 291 LEU C N   
7236  C CA  . LEU C 227 ? 0.9006 0.5186 0.6282 0.1386  -0.3665 -0.1954 291 LEU C CA  
7237  C C   . LEU C 227 ? 1.0255 0.6411 0.7779 0.1258  -0.3813 -0.1850 291 LEU C C   
7238  O O   . LEU C 227 ? 1.3945 1.0277 1.1630 0.1196  -0.3714 -0.1795 291 LEU C O   
7239  C CB  . LEU C 227 ? 0.8939 0.5363 0.6320 0.1297  -0.3459 -0.1866 291 LEU C CB  
7240  C CG  . LEU C 227 ? 0.9632 0.6065 0.7185 0.1167  -0.3547 -0.1746 291 LEU C CG  
7241  C CD1 . LEU C 227 ? 1.0094 0.6263 0.7481 0.1228  -0.3745 -0.1795 291 LEU C CD1 
7242  C CD2 . LEU C 227 ? 0.8271 0.4965 0.5929 0.1095  -0.3330 -0.1671 291 LEU C CD2 
7243  N N   . GLU C 228 ? 1.1376 0.7317 0.8936 0.1218  -0.4055 -0.1817 292 GLU C N   
7244  C CA  . GLU C 228 ? 1.1390 0.7295 0.9208 0.1079  -0.4222 -0.1691 292 GLU C CA  
7245  C C   . GLU C 228 ? 1.0377 0.6352 0.8373 0.0950  -0.4263 -0.1562 292 GLU C C   
7246  O O   . GLU C 228 ? 1.3362 0.9223 1.1225 0.1000  -0.4319 -0.1614 292 GLU C O   
7247  C CB  . GLU C 228 ? 1.3089 0.8649 1.0811 0.1149  -0.4511 -0.1768 292 GLU C CB  
7248  C CG  . GLU C 228 ? 1.7933 1.3447 1.5838 0.1070  -0.4633 -0.1690 292 GLU C CG  
7249  C CD  . GLU C 228 ? 2.2687 1.7818 2.0516 0.1127  -0.4964 -0.1758 292 GLU C CD  
7250  O OE1 . GLU C 228 ? 2.4953 1.9955 2.2680 0.1224  -0.5029 -0.1850 292 GLU C OE1 
7251  O OE2 . GLU C 228 ? 2.5302 2.0252 2.3175 0.1081  -0.5171 -0.1726 292 GLU C OE2 
7252  N N   . PHE C 229 ? 0.9716 0.5899 0.8001 0.0795  -0.4221 -0.1396 293 PHE C N   
7253  C CA  . PHE C 229 ? 1.0307 0.6572 0.8806 0.0667  -0.4287 -0.1258 293 PHE C CA  
7254  C C   . PHE C 229 ? 0.9395 0.5803 0.8203 0.0514  -0.4331 -0.1077 293 PHE C C   
7255  O O   . PHE C 229 ? 0.9514 0.6018 0.8356 0.0508  -0.4246 -0.1056 293 PHE C O   
7256  C CB  . PHE C 229 ? 1.0572 0.7070 0.9062 0.0664  -0.4071 -0.1245 293 PHE C CB  
7257  C CG  . PHE C 229 ? 0.9940 0.6748 0.8518 0.0635  -0.3817 -0.1198 293 PHE C CG  
7258  C CD1 . PHE C 229 ? 1.0271 0.7326 0.9126 0.0509  -0.3769 -0.1034 293 PHE C CD1 
7259  C CD2 . PHE C 229 ? 1.0357 0.7223 0.8745 0.0739  -0.3626 -0.1312 293 PHE C CD2 
7260  C CE1 . PHE C 229 ? 0.9151 0.6487 0.8070 0.0499  -0.3546 -0.1002 293 PHE C CE1 
7261  C CE2 . PHE C 229 ? 1.0162 0.7302 0.8641 0.0714  -0.3409 -0.1276 293 PHE C CE2 
7262  C CZ  . PHE C 229 ? 0.8912 0.6276 0.7645 0.0600  -0.3376 -0.1129 293 PHE C CZ  
7263  N N   . ASP C 230 ? 0.9650 0.6089 0.8686 0.0392  -0.4460 -0.0939 294 ASP C N   
7264  C CA  . ASP C 230 ? 1.0516 0.7123 0.9867 0.0237  -0.4497 -0.0735 294 ASP C CA  
7265  C C   . ASP C 230 ? 1.0955 0.7894 1.0529 0.0141  -0.4366 -0.0593 294 ASP C C   
7266  O O   . ASP C 230 ? 1.2068 0.9096 1.1536 0.0201  -0.4236 -0.0667 294 ASP C O   
7267  C CB  . ASP C 230 ? 1.2472 0.8810 1.1951 0.0161  -0.4814 -0.0670 294 ASP C CB  
7268  C CG  . ASP C 230 ? 1.3415 0.9611 1.2923 0.0146  -0.4988 -0.0684 294 ASP C CG  
7269  O OD1 . ASP C 230 ? 1.4760 1.1112 1.4240 0.0168  -0.4858 -0.0705 294 ASP C OD1 
7270  O OD2 . ASP C 230 ? 1.4928 1.0838 1.4489 0.0114  -0.5275 -0.0678 294 ASP C OD2 
7271  N N   . GLN C 231 ? 1.0121 0.7243 1.0001 -0.0003 -0.4407 -0.0387 295 GLN C N   
7272  C CA  . GLN C 231 ? 1.1222 0.8705 1.1318 -0.0077 -0.4264 -0.0250 295 GLN C CA  
7273  C C   . GLN C 231 ? 1.2205 0.9658 1.2344 -0.0084 -0.4346 -0.0265 295 GLN C C   
7274  O O   . GLN C 231 ? 1.3966 1.1662 1.4134 -0.0067 -0.4183 -0.0256 295 GLN C O   
7275  C CB  . GLN C 231 ? 1.1762 0.9496 1.2174 -0.0219 -0.4263 -0.0011 295 GLN C CB  
7276  C CG  . GLN C 231 ? 1.4429 1.1989 1.5063 -0.0349 -0.4540 0.0131  295 GLN C CG  
7277  C CD  . GLN C 231 ? 1.4930 1.2782 1.5865 -0.0486 -0.4497 0.0388  295 GLN C CD  
7278  O OE1 . GLN C 231 ? 1.8733 1.6839 1.9638 -0.0457 -0.4282 0.0425  295 GLN C OE1 
7279  N NE2 . GLN C 231 ? 1.4925 1.2746 1.6154 -0.0634 -0.4706 0.0571  295 GLN C NE2 
7280  N N   . SER C 232 ? 1.1741 0.8881 1.1866 -0.0096 -0.4608 -0.0304 296 SER C N   
7281  C CA  . SER C 232 ? 1.2234 0.9318 1.2391 -0.0096 -0.4714 -0.0328 296 SER C CA  
7282  C C   . SER C 232 ? 1.2297 0.9224 1.2098 0.0065  -0.4635 -0.0541 296 SER C C   
7283  O O   . SER C 232 ? 1.4219 1.1047 1.3985 0.0090  -0.4736 -0.0586 296 SER C O   
7284  C CB  . SER C 232 ? 1.2223 0.9027 1.2517 -0.0172 -0.5048 -0.0282 296 SER C CB  
7285  O OG  . SER C 232 ? 1.2575 0.8981 1.2585 -0.0065 -0.5199 -0.0454 296 SER C OG  
7286  N N   . PHE C 233 ? 1.0397 0.7312 0.9946 0.0172  -0.4457 -0.0661 297 PHE C N   
7287  C CA  . PHE C 233 ? 1.1078 0.7856 1.0287 0.0323  -0.4365 -0.0847 297 PHE C CA  
7288  C C   . PHE C 233 ? 1.0976 0.7362 0.9937 0.0423  -0.4578 -0.0993 297 PHE C C   
7289  O O   . PHE C 233 ? 1.4042 1.0321 1.2733 0.0543  -0.4523 -0.1124 297 PHE C O   
7290  C CB  . PHE C 233 ? 1.6250 1.3211 1.5468 0.0334  -0.4234 -0.0839 297 PHE C CB  
7291  C CG  . PHE C 233 ? 1.6777 1.4083 1.6088 0.0315  -0.3971 -0.0779 297 PHE C CG  
7292  C CD1 . PHE C 233 ? 1.2614 0.9993 1.1840 0.0350  -0.3814 -0.0816 297 PHE C CD1 
7293  C CD2 . PHE C 233 ? 1.9557 1.7111 1.9034 0.0273  -0.3892 -0.0696 297 PHE C CD2 
7294  C CE1 . PHE C 233 ? 1.0463 0.8139 0.9764 0.0342  -0.3593 -0.0773 297 PHE C CE1 
7295  C CE2 . PHE C 233 ? 1.7652 1.5508 1.7198 0.0273  -0.3667 -0.0655 297 PHE C CE2 
7296  C CZ  . PHE C 233 ? 1.2824 1.0732 1.2275 0.0308  -0.3521 -0.0697 297 PHE C CZ  
7297  N N   . THR C 234 ? 1.0479 0.6642 0.9518 0.0382  -0.4828 -0.0972 298 THR C N   
7298  C CA  . THR C 234 ? 1.2163 0.7936 1.0919 0.0512  -0.5030 -0.1140 298 THR C CA  
7299  C C   . THR C 234 ? 1.2655 0.8377 1.1146 0.0641  -0.4889 -0.1271 298 THR C C   
7300  O O   . THR C 234 ? 1.5150 1.0983 1.3751 0.0592  -0.4817 -0.1213 298 THR C O   
7301  C CB  . THR C 234 ? 1.1699 0.7197 1.0606 0.0443  -0.5383 -0.1097 298 THR C CB  
7302  O OG1 . THR C 234 ? 1.2179 0.7771 1.1340 0.0319  -0.5406 -0.0957 298 THR C OG1 
7303  C CG2 . THR C 234 ? 1.2041 0.7562 1.1173 0.0344  -0.5536 -0.1001 298 THR C CG2 
7304  N N   . TYR C 235 ? 1.1612 0.7196 0.9761 0.0805  -0.4836 -0.1438 299 TYR C N   
7305  C CA  . TYR C 235 ? 1.0754 0.6375 0.8672 0.0928  -0.4646 -0.1550 299 TYR C CA  
7306  C C   . TYR C 235 ? 1.1789 0.7112 0.9345 0.1118  -0.4755 -0.1736 299 TYR C C   
7307  O O   . TYR C 235 ? 1.6906 1.2061 1.4323 0.1177  -0.4879 -0.1790 299 TYR C O   
7308  C CB  . TYR C 235 ? 0.9509 0.5415 0.7397 0.0931  -0.4343 -0.1532 299 TYR C CB  
7309  C CG  . TYR C 235 ? 0.9970 0.5796 0.7616 0.1032  -0.4308 -0.1616 299 TYR C CG  
7310  C CD1 . TYR C 235 ? 1.0580 0.6448 0.8334 0.0964  -0.4356 -0.1543 299 TYR C CD1 
7311  C CD2 . TYR C 235 ? 1.0128 0.5852 0.7436 0.1199  -0.4221 -0.1759 299 TYR C CD2 
7312  C CE1 . TYR C 235 ? 1.1341 0.7125 0.8856 0.1062  -0.4326 -0.1615 299 TYR C CE1 
7313  C CE2 . TYR C 235 ? 1.0553 0.6207 0.7621 0.1294  -0.4180 -0.1820 299 TYR C CE2 
7314  C CZ  . TYR C 235 ? 1.1101 0.6772 0.8265 0.1225  -0.4238 -0.1749 299 TYR C CZ  
7315  O OH  . TYR C 235 ? 1.0773 0.6362 0.7687 0.1323  -0.4205 -0.1805 299 TYR C OH  
7316  N N   . THR C 236 ? 1.2376 0.7647 0.9770 0.1227  -0.4704 -0.1838 300 THR C N   
7317  C CA  . THR C 236 ? 1.3694 0.8759 1.0707 0.1441  -0.4733 -0.2024 300 THR C CA  
7318  C C   . THR C 236 ? 1.4463 0.9725 1.1330 0.1537  -0.4451 -0.2089 300 THR C C   
7319  O O   . THR C 236 ? 1.7553 1.2986 1.4585 0.1471  -0.4338 -0.2039 300 THR C O   
7320  C CB  . THR C 236 ? 1.2747 0.7469 0.9656 0.1533  -0.5033 -0.2127 300 THR C CB  
7321  O OG1 . THR C 236 ? 1.2345 0.7129 0.9333 0.1528  -0.4985 -0.2128 300 THR C OG1 
7322  C CG2 . THR C 236 ? 1.4700 0.9217 1.1823 0.1410  -0.5349 -0.2044 300 THR C CG2 
7323  N N   . PHE C 237 ? 1.2783 0.8028 0.9348 0.1690  -0.4339 -0.2194 301 PHE C N   
7324  C CA  . PHE C 237 ? 1.1814 0.7204 0.8216 0.1810  -0.4115 -0.2274 301 PHE C CA  
7325  C C   . PHE C 237 ? 1.2674 0.7847 0.8852 0.1992  -0.4262 -0.2430 301 PHE C C   
7326  O O   . PHE C 237 ? 1.4240 0.9126 1.0224 0.2102  -0.4492 -0.2522 301 PHE C O   
7327  C CB  . PHE C 237 ? 1.2066 0.7565 0.8260 0.1886  -0.3913 -0.2293 301 PHE C CB  
7328  C CG  . PHE C 237 ? 1.2459 0.8226 0.8864 0.1731  -0.3703 -0.2158 301 PHE C CG  
7329  C CD1 . PHE C 237 ? 1.2364 0.8106 0.8854 0.1637  -0.3767 -0.2076 301 PHE C CD1 
7330  C CD2 . PHE C 237 ? 1.1516 0.7557 0.8035 0.1689  -0.3454 -0.2122 301 PHE C CD2 
7331  C CE1 . PHE C 237 ? 1.1151 0.7130 0.7823 0.1512  -0.3587 -0.1964 301 PHE C CE1 
7332  C CE2 . PHE C 237 ? 1.3413 0.9675 1.0114 0.1561  -0.3284 -0.2012 301 PHE C CE2 
7333  C CZ  . PHE C 237 ? 1.2995 0.9223 0.9764 0.1478  -0.3350 -0.1935 301 PHE C CZ  
7334  N N   . LYS C 238 ? 1.3353 0.8657 0.9564 0.2030  -0.4144 -0.2464 302 LYS C N   
7335  C CA  . LYS C 238 ? 1.3245 0.8385 0.9242 0.2223  -0.4250 -0.2620 302 LYS C CA  
7336  C C   . LYS C 238 ? 1.2969 0.8363 0.8835 0.2339  -0.3963 -0.2678 302 LYS C C   
7337  O O   . LYS C 238 ? 1.3947 0.9628 0.9987 0.2229  -0.3723 -0.2584 302 LYS C O   
7338  C CB  . LYS C 238 ? 1.4891 0.9943 1.1093 0.2155  -0.4412 -0.2603 302 LYS C CB  
7339  C CG  . LYS C 238 ? 1.5413 1.0264 1.1830 0.1995  -0.4680 -0.2500 302 LYS C CG  
7340  C CD  . LYS C 238 ? 1.5629 1.0411 1.2240 0.1927  -0.4815 -0.2465 302 LYS C CD  
7341  C CE  . LYS C 238 ? 1.6367 1.0804 1.3042 0.1883  -0.5177 -0.2450 302 LYS C CE  
7342  N NZ  . LYS C 238 ? 1.7468 1.1717 1.4148 0.1942  -0.5357 -0.2512 302 LYS C NZ  
7343  N N   . GLU C 239 ? 1.3979 0.9273 0.9539 0.2568  -0.3991 -0.2831 303 GLU C N   
7344  C CA  . GLU C 239 ? 1.4503 1.0052 0.9962 0.2687  -0.3732 -0.2883 303 GLU C CA  
7345  C C   . GLU C 239 ? 1.5955 1.1437 1.1382 0.2818  -0.3831 -0.3004 303 GLU C C   
7346  O O   . GLU C 239 ? 1.8770 1.3953 1.4015 0.2957  -0.4089 -0.3124 303 GLU C O   
7347  C CB  . GLU C 239 ? 1.6056 1.1594 1.1166 0.2868  -0.3649 -0.2954 303 GLU C CB  
7348  C CG  . GLU C 239 ? 1.8752 1.4544 1.3715 0.3030  -0.3401 -0.3017 303 GLU C CG  
7349  C CD  . GLU C 239 ? 1.9205 1.5343 1.4323 0.2904  -0.3080 -0.2885 303 GLU C CD  
7350  O OE1 . GLU C 239 ? 2.4096 2.0265 1.9390 0.2712  -0.3046 -0.2757 303 GLU C OE1 
7351  O OE2 . GLU C 239 ? 1.7845 1.4229 1.2915 0.3001  -0.2867 -0.2909 303 GLU C OE2 
7352  N N   . PRO C 240 ? 1.3583 0.9331 0.9185 0.2782  -0.3643 -0.2981 304 PRO C N   
7353  C CA  . PRO C 240 ? 1.4391 1.0095 0.9980 0.2905  -0.3729 -0.3093 304 PRO C CA  
7354  C C   . PRO C 240 ? 1.5816 1.1476 1.1057 0.3196  -0.3732 -0.3269 304 PRO C C   
7355  O O   . PRO C 240 ? 1.5952 1.1815 1.1043 0.3285  -0.3511 -0.3274 304 PRO C O   
7356  C CB  . PRO C 240 ? 1.3840 0.9889 0.9690 0.2797  -0.3484 -0.3017 304 PRO C CB  
7357  C CG  . PRO C 240 ? 1.4277 1.0574 1.0152 0.2720  -0.3225 -0.2922 304 PRO C CG  
7358  C CD  . PRO C 240 ? 1.3154 0.9256 0.8932 0.2659  -0.3337 -0.2869 304 PRO C CD  
7359  N N   . CYS C 241 ? 1.6546 1.1939 1.1659 0.3348  -0.3986 -0.3406 305 CYS C N   
7360  C CA  . CYS C 241 ? 1.6770 1.2076 1.1526 0.3653  -0.4038 -0.3594 305 CYS C CA  
7361  C C   . CYS C 241 ? 1.5871 1.1366 1.0653 0.3793  -0.3942 -0.3690 305 CYS C C   
7362  O O   . CYS C 241 ? 1.7448 1.2721 1.2105 0.3963  -0.4163 -0.3837 305 CYS C O   
7363  C CB  . CYS C 241 ? 2.0591 1.5438 1.5167 0.3756  -0.4423 -0.3707 305 CYS C CB  
7364  S SG  . CYS C 241 ? 2.8486 2.3071 2.3094 0.3573  -0.4607 -0.3596 305 CYS C SG  
7365  N N   . LEU C 242 ? 1.4896 1.0789 0.9849 0.3724  -0.3630 -0.3610 306 LEU C N   
7366  C CA  . LEU C 242 ? 1.5412 1.1518 1.0452 0.3827  -0.3531 -0.3685 306 LEU C CA  
7367  C C   . LEU C 242 ? 1.5869 1.2408 1.0913 0.3884  -0.3180 -0.3655 306 LEU C C   
7368  O O   . LEU C 242 ? 1.5588 1.2321 1.0755 0.3716  -0.2977 -0.3510 306 LEU C O   
7369  C CB  . LEU C 242 ? 1.4756 1.0877 1.0147 0.3619  -0.3580 -0.3596 306 LEU C CB  
7370  C CG  . LEU C 242 ? 1.5219 1.0944 1.0648 0.3572  -0.3927 -0.3619 306 LEU C CG  
7371  C CD1 . LEU C 242 ? 1.8293 1.4101 1.4074 0.3340  -0.3912 -0.3488 306 LEU C CD1 
7372  C CD2 . LEU C 242 ? 1.6292 1.1792 1.1495 0.3842  -0.4147 -0.3823 306 LEU C CD2 
7373  N N   . GLY C 243 ? 1.5809 1.2498 1.0727 0.4124  -0.3118 -0.3790 307 GLY C N   
7374  C CA  . GLY C 243 ? 1.5362 1.2482 1.0283 0.4206  -0.2792 -0.3767 307 GLY C CA  
7375  C C   . GLY C 243 ? 1.6946 1.4412 1.2256 0.3996  -0.2563 -0.3634 307 GLY C C   
7376  O O   . GLY C 243 ? 2.0022 1.7861 1.5394 0.4029  -0.2292 -0.3591 307 GLY C O   
7377  N N   . PHE C 244 ? 1.5100 1.2447 1.0673 0.3785  -0.2677 -0.3565 308 PHE C N   
7378  C CA  . PHE C 244 ? 1.4706 1.2331 1.0646 0.3570  -0.2499 -0.3440 308 PHE C CA  
7379  C C   . PHE C 244 ? 1.3718 1.1410 0.9763 0.3347  -0.2362 -0.3268 308 PHE C C   
7380  O O   . PHE C 244 ? 1.3148 1.0599 0.9210 0.3199  -0.2502 -0.3199 308 PHE C O   
7381  C CB  . PHE C 244 ? 1.5659 1.3113 1.1796 0.3466  -0.2693 -0.3445 308 PHE C CB  
7382  C CG  . PHE C 244 ? 1.3215 1.0962 0.9667 0.3370  -0.2548 -0.3401 308 PHE C CG  
7383  C CD1 . PHE C 244 ? 1.3336 1.1309 0.9818 0.3541  -0.2467 -0.3508 308 PHE C CD1 
7384  C CD2 . PHE C 244 ? 1.3011 1.0804 0.9727 0.3123  -0.2510 -0.3264 308 PHE C CD2 
7385  C CE1 . PHE C 244 ? 1.1379 0.9615 0.8163 0.3456  -0.2353 -0.3475 308 PHE C CE1 
7386  C CE2 . PHE C 244 ? 1.2675 1.0719 0.9668 0.3049  -0.2399 -0.3237 308 PHE C CE2 
7387  C CZ  . PHE C 244 ? 1.1301 0.9561 0.8331 0.3213  -0.2325 -0.3344 308 PHE C CZ  
7388  N N   . LEU C 245 ? 1.2965 1.0993 0.9088 0.3325  -0.2092 -0.3198 309 LEU C N   
7389  C CA  . LEU C 245 ? 1.3262 1.1347 0.9428 0.3158  -0.1959 -0.3051 309 LEU C CA  
7390  C C   . LEU C 245 ? 1.2582 1.0786 0.9098 0.2915  -0.1893 -0.2934 309 LEU C C   
7391  O O   . LEU C 245 ? 1.4802 1.3286 1.1539 0.2889  -0.1748 -0.2921 309 LEU C O   
7392  C CB  . LEU C 245 ? 1.2843 1.1222 0.8919 0.3251  -0.1704 -0.3016 309 LEU C CB  
7393  C CG  . LEU C 245 ? 1.1903 1.0194 0.7585 0.3503  -0.1733 -0.3114 309 LEU C CG  
7394  C CD1 . LEU C 245 ? 1.2292 1.0827 0.7896 0.3508  -0.1478 -0.3004 309 LEU C CD1 
7395  C CD2 . LEU C 245 ? 1.1536 0.9396 0.6977 0.3528  -0.2003 -0.3167 309 LEU C CD2 
7396  N N   . GLY C 246 ? 1.1428 0.9430 0.7997 0.2747  -0.2005 -0.2853 310 GLY C N   
7397  C CA  . GLY C 246 ? 1.2181 1.0269 0.9059 0.2530  -0.1971 -0.2751 310 GLY C CA  
7398  C C   . GLY C 246 ? 1.1788 1.0142 0.8835 0.2406  -0.1737 -0.2637 310 GLY C C   
7399  O O   . GLY C 246 ? 1.4082 1.2629 1.1394 0.2306  -0.1650 -0.2600 310 GLY C O   
7400  N N   . ASP C 247 ? 1.1557 0.9905 0.8440 0.2419  -0.1649 -0.2585 311 ASP C N   
7401  C CA  . ASP C 247 ? 1.1102 0.9628 0.8118 0.2282  -0.1463 -0.2459 311 ASP C CA  
7402  C C   . ASP C 247 ? 1.1466 1.0329 0.8637 0.2307  -0.1250 -0.2442 311 ASP C C   
7403  O O   . ASP C 247 ? 1.1875 1.0856 0.9040 0.2444  -0.1233 -0.2533 311 ASP C O   
7404  C CB  . ASP C 247 ? 1.1516 0.9918 0.8280 0.2310  -0.1444 -0.2409 311 ASP C CB  
7405  C CG  . ASP C 247 ? 1.1069 0.9461 0.7955 0.2120  -0.1393 -0.2278 311 ASP C CG  
7406  O OD1 . ASP C 247 ? 0.9972 0.8538 0.7131 0.1987  -0.1294 -0.2213 311 ASP C OD1 
7407  O OD2 . ASP C 247 ? 1.0953 0.9153 0.7656 0.2115  -0.1463 -0.2246 311 ASP C OD2 
7408  N N   . THR C 248 ? 1.1891 1.0906 0.9213 0.2172  -0.1096 -0.2322 312 THR C N   
7409  C CA  . THR C 248 ? 1.1759 1.1102 0.9282 0.2152  -0.0890 -0.2271 312 THR C CA  
7410  C C   . THR C 248 ? 1.3699 1.3103 1.1247 0.2035  -0.0751 -0.2126 312 THR C C   
7411  O O   . THR C 248 ? 1.4324 1.3611 1.1961 0.1886  -0.0800 -0.2062 312 THR C O   
7412  C CB  . THR C 248 ? 1.1064 1.0552 0.8928 0.2054  -0.0895 -0.2286 312 THR C CB  
7413  O OG1 . THR C 248 ? 1.2569 1.1992 1.0406 0.2163  -0.1029 -0.2413 312 THR C OG1 
7414  C CG2 . THR C 248 ? 1.1127 1.0959 0.9231 0.2023  -0.0695 -0.2228 312 THR C CG2 
7415  N N   . PRO C 249 ? 1.5422 1.5017 1.2894 0.2107  -0.0576 -0.2070 313 PRO C N   
7416  C CA  . PRO C 249 ? 1.6023 1.5811 1.3414 0.2293  -0.0498 -0.2143 313 PRO C CA  
7417  C C   . PRO C 249 ? 1.3910 1.3481 1.0909 0.2491  -0.0614 -0.2248 313 PRO C C   
7418  O O   . PRO C 249 ? 1.3139 1.2415 0.9947 0.2468  -0.0752 -0.2251 313 PRO C O   
7419  C CB  . PRO C 249 ? 1.5099 1.5167 1.2552 0.2271  -0.0262 -0.2007 313 PRO C CB  
7420  C CG  . PRO C 249 ? 1.3261 1.3140 1.0587 0.2165  -0.0267 -0.1897 313 PRO C CG  
7421  C CD  . PRO C 249 ? 1.3166 1.2801 1.0604 0.2023  -0.0444 -0.1924 313 PRO C CD  
7422  N N   . ARG C 250 ? 1.2483 1.2206 0.9378 0.2689  -0.0569 -0.2339 314 ARG C N   
7423  C CA  . ARG C 250 ? 1.2449 1.1983 0.8977 0.2914  -0.0692 -0.2468 314 ARG C CA  
7424  C C   . ARG C 250 ? 1.4680 1.4512 1.1124 0.3122  -0.0537 -0.2512 314 ARG C C   
7425  O O   . ARG C 250 ? 1.6788 1.6961 1.3512 0.3080  -0.0369 -0.2460 314 ARG C O   
7426  C CB  . ARG C 250 ? 1.2397 1.1688 0.8938 0.2939  -0.0935 -0.2605 314 ARG C CB  
7427  C CG  . ARG C 250 ? 1.1039 1.0519 0.7913 0.2888  -0.0922 -0.2644 314 ARG C CG  
7428  C CD  . ARG C 250 ? 1.1051 1.0272 0.7879 0.2944  -0.1168 -0.2776 314 ARG C CD  
7429  N NE  . ARG C 250 ? 1.0191 0.9511 0.7346 0.2832  -0.1192 -0.2782 314 ARG C NE  
7430  C CZ  . ARG C 250 ? 1.1548 1.1089 0.8845 0.2927  -0.1145 -0.2857 314 ARG C CZ  
7431  N NH1 . ARG C 250 ? 1.1542 1.1255 0.8696 0.3139  -0.1058 -0.2930 314 ARG C NH1 
7432  N NH2 . ARG C 250 ? 1.2869 1.2471 1.0449 0.2821  -0.1185 -0.2862 314 ARG C NH2 
7433  N N   . GLY C 251 ? 1.5712 1.5424 1.1775 0.3354  -0.0597 -0.2609 315 GLY C N   
7434  C CA  . GLY C 251 ? 1.7464 1.7479 1.3398 0.3577  -0.0430 -0.2640 315 GLY C CA  
7435  C C   . GLY C 251 ? 1.7252 1.7375 1.3266 0.3735  -0.0493 -0.2799 315 GLY C C   
7436  O O   . GLY C 251 ? 1.8806 1.9293 1.5097 0.3726  -0.0334 -0.2770 315 GLY C O   
7437  N N   . ILE C 252 ? 1.7587 1.7379 1.3368 0.3874  -0.0744 -0.2967 316 ILE C N   
7438  C CA  . ILE C 252 ? 1.6362 1.6197 1.2076 0.4106  -0.0831 -0.3146 316 ILE C CA  
7439  C C   . ILE C 252 ? 1.6805 1.6168 1.2306 0.4171  -0.1157 -0.3293 316 ILE C C   
7440  O O   . ILE C 252 ? 2.0238 1.9291 1.5532 0.4125  -0.1279 -0.3270 316 ILE C O   
7441  C CB  . ILE C 252 ? 1.5508 1.5580 1.0928 0.4398  -0.0682 -0.3195 316 ILE C CB  
7442  C CG1 . ILE C 252 ? 1.6914 1.7255 1.2437 0.4592  -0.0648 -0.3324 316 ILE C CG1 
7443  C CG2 . ILE C 252 ? 1.3762 1.3484 0.8688 0.4590  -0.0847 -0.3291 316 ILE C CG2 
7444  C CD1 . ILE C 252 ? 1.7759 1.8573 1.3722 0.4457  -0.0402 -0.3202 316 ILE C CD1 
7445  N N   . ASP C 253 ? 1.6563 1.5864 1.2121 0.4277  -0.1308 -0.3439 317 ASP C N   
7446  C CA  . ASP C 253 ? 1.7243 1.6087 1.2615 0.4335  -0.1631 -0.3568 317 ASP C CA  
7447  C C   . ASP C 253 ? 1.8229 1.6883 1.3142 0.4621  -0.1740 -0.3701 317 ASP C C   
7448  O O   . ASP C 253 ? 2.2022 2.0935 1.6767 0.4851  -0.1589 -0.3755 317 ASP C O   
7449  C CB  . ASP C 253 ? 1.7462 1.6270 1.3036 0.4350  -0.1774 -0.3671 317 ASP C CB  
7450  C CG  . ASP C 253 ? 1.7718 1.6592 1.3694 0.4054  -0.1739 -0.3546 317 ASP C CG  
7451  O OD1 . ASP C 253 ? 1.6464 1.5232 1.2513 0.3832  -0.1726 -0.3411 317 ASP C OD1 
7452  O OD2 . ASP C 253 ? 1.7919 1.6955 1.4128 0.4058  -0.1729 -0.3590 317 ASP C OD2 
7453  N N   . THR C 254 ? 1.8310 1.6520 1.3023 0.4609  -0.2004 -0.3751 318 THR C N   
7454  C CA  . THR C 254 ? 1.9740 1.7722 1.4002 0.4859  -0.2130 -0.3868 318 THR C CA  
7455  C C   . THR C 254 ? 1.9172 1.6759 1.3275 0.5017  -0.2479 -0.4062 318 THR C C   
7456  O O   . THR C 254 ? 2.0860 1.8378 1.5206 0.4931  -0.2600 -0.4093 318 THR C O   
7457  C CB  . THR C 254 ? 2.2308 2.0075 1.6437 0.4719  -0.2162 -0.3756 318 THR C CB  
7458  O OG1 . THR C 254 ? 2.3033 2.0517 1.7384 0.4462  -0.2354 -0.3695 318 THR C OG1 
7459  C CG2 . THR C 254 ? 2.0268 1.8392 1.4498 0.4592  -0.1830 -0.3567 318 THR C CG2 
7460  N N   . THR C 255 ? 1.8119 1.5438 1.1808 0.5253  -0.2650 -0.4193 319 THR C N   
7461  C CA  . THR C 255 ? 1.8901 1.5740 1.2427 0.5359  -0.3037 -0.4357 319 THR C CA  
7462  C C   . THR C 255 ? 1.8669 1.5170 1.2331 0.5071  -0.3222 -0.4242 319 THR C C   
7463  O O   . THR C 255 ? 1.9154 1.5778 1.2932 0.4861  -0.3052 -0.4069 319 THR C O   
7464  C CB  . THR C 255 ? 1.9311 1.5961 1.2336 0.5715  -0.3174 -0.4542 319 THR C CB  
7465  O OG1 . THR C 255 ? 2.2759 1.9390 1.5578 0.5685  -0.3083 -0.4449 319 THR C OG1 
7466  C CG2 . THR C 255 ? 1.7641 1.4642 1.0515 0.6029  -0.2997 -0.4663 319 THR C CG2 
7467  N N   . ASN C 256 ? 1.7535 1.3621 1.1196 0.5060  -0.3568 -0.4329 320 ASN C N   
7468  C CA  . ASN C 256 ? 1.7520 1.3302 1.1330 0.4794  -0.3754 -0.4215 320 ASN C CA  
7469  C C   . ASN C 256 ? 1.8203 1.3719 1.1702 0.4864  -0.3886 -0.4239 320 ASN C C   
7470  O O   . ASN C 256 ? 1.9873 1.5165 1.3017 0.5140  -0.4069 -0.4415 320 ASN C O   
7471  C CB  . ASN C 256 ? 1.7681 1.3117 1.1630 0.4740  -0.4084 -0.4276 320 ASN C CB  
7472  C CG  . ASN C 256 ? 1.8152 1.3807 1.2398 0.4673  -0.3991 -0.4258 320 ASN C CG  
7473  O OD1 . ASN C 256 ? 2.0061 1.6130 1.4412 0.4689  -0.3691 -0.4222 320 ASN C OD1 
7474  N ND2 . ASN C 256 ? 1.6630 1.2003 1.1020 0.4596  -0.4258 -0.4277 320 ASN C ND2 
7475  N N   . TYR C 257 ? 2.0931 1.6464 1.4556 0.4625  -0.3804 -0.4069 321 TYR C N   
7476  C CA  . TYR C 257 ? 1.9578 1.4820 1.2960 0.4647  -0.3969 -0.4076 321 TYR C CA  
7477  C C   . TYR C 257 ? 2.1895 1.7107 1.5561 0.4313  -0.3955 -0.3878 321 TYR C C   
7478  O O   . TYR C 257 ? 2.1113 1.6621 1.5087 0.4098  -0.3718 -0.3724 321 TYR C O   
7479  C CB  . TYR C 257 ? 1.7840 1.3237 1.0844 0.4880  -0.3788 -0.4124 321 TYR C CB  
7480  C CG  . TYR C 257 ? 1.7718 1.3592 1.0852 0.4791  -0.3377 -0.3973 321 TYR C CG  
7481  C CD1 . TYR C 257 ? 1.7796 1.3767 1.1051 0.4565  -0.3224 -0.3789 321 TYR C CD1 
7482  C CD2 . TYR C 257 ? 1.7283 1.3513 1.0433 0.4932  -0.3150 -0.4013 321 TYR C CD2 
7483  C CE1 . TYR C 257 ? 1.7516 1.3902 1.0904 0.4475  -0.2865 -0.3645 321 TYR C CE1 
7484  C CE2 . TYR C 257 ? 1.8879 1.5549 1.2182 0.4836  -0.2783 -0.3863 321 TYR C CE2 
7485  C CZ  . TYR C 257 ? 1.7604 1.4336 1.1024 0.4603  -0.2648 -0.3678 321 TYR C CZ  
7486  O OH  . TYR C 257 ? 1.6757 1.3894 1.0338 0.4499  -0.2309 -0.3525 321 TYR C OH  
7487  N N   . CYS C 258 ? 2.2320 1.7177 1.5886 0.4279  -0.4220 -0.3889 322 CYS C N   
7488  C CA  . CYS C 258 ? 2.0838 1.5634 1.4690 0.3974  -0.4262 -0.3716 322 CYS C CA  
7489  C C   . CYS C 258 ? 2.0567 1.5532 1.4356 0.3898  -0.4045 -0.3596 322 CYS C C   
7490  O O   . CYS C 258 ? 1.9485 1.4404 1.3468 0.3675  -0.4075 -0.3462 322 CYS C O   
7491  C CB  . CYS C 258 ? 2.3576 1.7926 1.7435 0.3938  -0.4664 -0.3763 322 CYS C CB  
7492  S SG  . CYS C 258 ? 3.9498 3.3668 3.3567 0.3918  -0.4905 -0.3828 322 CYS C SG  
7493  N N   . ASP C 259 ? 2.0289 1.5466 1.3814 0.4086  -0.3820 -0.3637 323 ASP C N   
7494  C CA  . ASP C 259 ? 2.1672 1.7066 1.5158 0.4010  -0.3563 -0.3504 323 ASP C CA  
7495  C C   . ASP C 259 ? 1.9067 1.4854 1.2907 0.3798  -0.3250 -0.3343 323 ASP C C   
7496  O O   . ASP C 259 ? 1.8471 1.4361 1.2590 0.3705  -0.3237 -0.3334 323 ASP C O   
7497  C CB  . ASP C 259 ? 2.2895 1.8349 1.5940 0.4302  -0.3459 -0.3598 323 ASP C CB  
7498  C CG  . ASP C 259 ? 2.6126 2.1603 1.9014 0.4262  -0.3346 -0.3491 323 ASP C CG  
7499  O OD1 . ASP C 259 ? 2.7157 2.2438 2.0155 0.4089  -0.3489 -0.3418 323 ASP C OD1 
7500  O OD2 . ASP C 259 ? 3.2993 2.8695 2.5651 0.4406  -0.3110 -0.3473 323 ASP C OD2 
7501  N N   . LYS C 260 ? 1.5690 1.1681 0.9515 0.3725  -0.3013 -0.3217 324 LYS C N   
7502  C CA  . LYS C 260 ? 1.6587 1.2923 1.0733 0.3527  -0.2734 -0.3065 324 LYS C CA  
7503  C C   . LYS C 260 ? 1.6088 1.2761 1.0115 0.3669  -0.2442 -0.3058 324 LYS C C   
7504  O O   . LYS C 260 ? 1.8048 1.4723 1.1742 0.3840  -0.2377 -0.3079 324 LYS C O   
7505  C CB  . LYS C 260 ? 1.7058 1.3367 1.1329 0.3311  -0.2700 -0.2912 324 LYS C CB  
7506  C CG  . LYS C 260 ? 1.7596 1.4221 1.1970 0.3207  -0.2386 -0.2763 324 LYS C CG  
7507  C CD  . LYS C 260 ? 1.6804 1.3322 1.1087 0.3122  -0.2389 -0.2663 324 LYS C CD  
7508  C CE  . LYS C 260 ? 1.6437 1.2668 1.0829 0.2998  -0.2657 -0.2664 324 LYS C CE  
7509  N NZ  . LYS C 260 ? 1.6674 1.2792 1.0944 0.2949  -0.2676 -0.2586 324 LYS C NZ  
7510  N N   . THR C 261 ? 1.4606 1.1570 0.8908 0.3599  -0.2269 -0.3023 325 THR C N   
7511  C CA  . THR C 261 ? 1.4463 1.1788 0.8721 0.3720  -0.1992 -0.3008 325 THR C CA  
7512  C C   . THR C 261 ? 1.4970 1.2545 0.9326 0.3577  -0.1723 -0.2824 325 THR C C   
7513  O O   . THR C 261 ? 1.7252 1.4998 1.1960 0.3357  -0.1606 -0.2710 325 THR C O   
7514  C CB  . THR C 261 ? 1.5461 1.3001 1.0001 0.3701  -0.1930 -0.3047 325 THR C CB  
7515  O OG1 . THR C 261 ? 1.6678 1.3982 1.1108 0.3853  -0.2181 -0.3220 325 THR C OG1 
7516  C CG2 . THR C 261 ? 1.4069 1.2015 0.8605 0.3817  -0.1641 -0.3022 325 THR C CG2 
7517  N N   . THR C 262 ? 1.5648 1.3240 0.9683 0.3712  -0.1629 -0.2797 326 THR C N   
7518  C CA  . THR C 262 ? 1.5290 1.3042 0.9375 0.3574  -0.1416 -0.2613 326 THR C CA  
7519  C C   . THR C 262 ? 1.4853 1.3036 0.9105 0.3558  -0.1105 -0.2509 326 THR C C   
7520  O O   . THR C 262 ? 1.6056 1.4390 1.0418 0.3415  -0.0924 -0.2342 326 THR C O   
7521  C CB  . THR C 262 ? 1.6674 1.4259 1.0339 0.3717  -0.1446 -0.2607 326 THR C CB  
7522  O OG1 . THR C 262 ? 1.8831 1.6626 1.2218 0.3964  -0.1284 -0.2640 326 THR C OG1 
7523  C CG2 . THR C 262 ? 1.8295 1.5456 1.1739 0.3805  -0.1780 -0.2751 326 THR C CG2 
7524  N N   . THR C 263 ? 1.4622 1.3000 0.8904 0.3705  -0.1051 -0.2605 327 THR C N   
7525  C CA  . THR C 263 ? 1.3625 1.2435 0.8061 0.3715  -0.0761 -0.2512 327 THR C CA  
7526  C C   . THR C 263 ? 1.3397 1.2380 0.8321 0.3457  -0.0684 -0.2422 327 THR C C   
7527  O O   . THR C 263 ? 1.3955 1.2854 0.9075 0.3407  -0.0827 -0.2515 327 THR C O   
7528  C CB  . THR C 263 ? 1.3370 1.2344 0.7657 0.3988  -0.0735 -0.2657 327 THR C CB  
7529  O OG1 . THR C 263 ? 1.3534 1.2228 0.7361 0.4238  -0.0913 -0.2800 327 THR C OG1 
7530  C CG2 . THR C 263 ? 1.3976 1.3408 0.8308 0.4049  -0.0414 -0.2539 327 THR C CG2 
7531  N N   . GLU C 264 ? 1.4842 1.4058 0.9951 0.3301  -0.0465 -0.2239 328 GLU C N   
7532  C CA  . GLU C 264 ? 1.4801 1.4155 1.0365 0.3040  -0.0398 -0.2138 328 GLU C CA  
7533  C C   . GLU C 264 ? 1.4324 1.3357 0.9998 0.2868  -0.0615 -0.2160 328 GLU C C   
7534  O O   . GLU C 264 ? 1.5514 1.4590 1.1524 0.2708  -0.0646 -0.2153 328 GLU C O   
7535  C CB  . GLU C 264 ? 1.5622 1.5271 1.1474 0.3063  -0.0319 -0.2192 328 GLU C CB  
7536  C CG  . GLU C 264 ? 1.7747 1.7821 1.3668 0.3135  -0.0045 -0.2099 328 GLU C CG  
7537  C CD  . GLU C 264 ? 2.0988 2.1363 1.7388 0.2971  0.0069  -0.2036 328 GLU C CD  
7538  O OE1 . GLU C 264 ? 2.6401 2.6760 2.3065 0.2733  0.0091  -0.1917 328 GLU C OE1 
7539  O OE2 . GLU C 264 ? 1.9889 2.0514 1.6404 0.3087  0.0128  -0.2112 328 GLU C OE2 
7540  N N   . GLY C 265 ? 1.4587 1.3312 0.9974 0.2911  -0.0763 -0.2184 329 GLY C N   
7541  C CA  . GLY C 265 ? 1.5842 1.4269 1.1307 0.2772  -0.0977 -0.2205 329 GLY C CA  
7542  C C   . GLY C 265 ? 1.5775 1.4245 1.1518 0.2524  -0.0907 -0.2058 329 GLY C C   
7543  O O   . GLY C 265 ? 1.8674 1.6999 1.4594 0.2384  -0.1044 -0.2065 329 GLY C O   
7544  N N   . GLU C 266 ? 1.2893 1.1570 0.8679 0.2474  -0.0696 -0.1923 330 GLU C N   
7545  C CA  . GLU C 266 ? 1.3216 1.1911 0.9234 0.2256  -0.0637 -0.1785 330 GLU C CA  
7546  C C   . GLU C 266 ? 1.3134 1.2050 0.9568 0.2106  -0.0559 -0.1753 330 GLU C C   
7547  O O   . GLU C 266 ? 1.4057 1.3224 1.0614 0.2161  -0.0446 -0.1774 330 GLU C O   
7548  C CB  . GLU C 266 ? 1.5710 1.4485 1.1584 0.2256  -0.0470 -0.1640 330 GLU C CB  
7549  C CG  . GLU C 266 ? 1.8674 1.7396 1.4737 0.2047  -0.0451 -0.1507 330 GLU C CG  
7550  C CD  . GLU C 266 ? 2.3496 2.2192 1.9344 0.2056  -0.0346 -0.1370 330 GLU C CD  
7551  O OE1 . GLU C 266 ? 2.3869 2.2609 1.9410 0.2231  -0.0271 -0.1370 330 GLU C OE1 
7552  O OE2 . GLU C 266 ? 2.6771 2.5399 2.2747 0.1898  -0.0341 -0.1262 330 GLU C OE2 
7553  N N   . GLY C 267 ? 1.3168 1.1997 0.9814 0.1924  -0.0619 -0.1700 331 GLY C N   
7554  C CA  . GLY C 267 ? 1.4168 1.3133 1.1185 0.1789  -0.0609 -0.1700 331 GLY C CA  
7555  C C   . GLY C 267 ? 1.5488 1.4316 1.2530 0.1818  -0.0794 -0.1831 331 GLY C C   
7556  O O   . GLY C 267 ? 1.6113 1.4758 1.2904 0.1942  -0.0921 -0.1917 331 GLY C O   
7557  N N   . GLY C 268 ? 1.3296 1.2204 1.0637 0.1706  -0.0818 -0.1842 332 GLY C N   
7558  C CA  . GLY C 268 ? 1.2347 1.1139 0.9734 0.1717  -0.0987 -0.1943 332 GLY C CA  
7559  C C   . GLY C 268 ? 1.0696 0.9554 0.8393 0.1571  -0.1011 -0.1924 332 GLY C C   
7560  O O   . GLY C 268 ? 1.0383 0.9327 0.8247 0.1455  -0.0928 -0.1841 332 GLY C O   
7561  N N   . ILE C 269 ? 1.0667 0.9477 0.8431 0.1588  -0.1134 -0.2005 333 ILE C N   
7562  C CA  . ILE C 269 ? 1.1062 0.9926 0.9083 0.1475  -0.1173 -0.1998 333 ILE C CA  
7563  C C   . ILE C 269 ? 1.0255 0.8951 0.8233 0.1491  -0.1354 -0.2054 333 ILE C C   
7564  O O   . ILE C 269 ? 1.1468 1.0070 0.9296 0.1601  -0.1438 -0.2126 333 ILE C O   
7565  C CB  . ILE C 269 ? 1.1207 1.0318 0.9461 0.1472  -0.1072 -0.2024 333 ILE C CB  
7566  C CG1 . ILE C 269 ? 1.1001 1.0174 0.9516 0.1343  -0.1089 -0.1997 333 ILE C CG1 
7567  C CG2 . ILE C 269 ? 0.9028 0.8169 0.7231 0.1606  -0.1123 -0.2133 333 ILE C CG2 
7568  C CD1 . ILE C 269 ? 1.3439 1.2854 1.2214 0.1312  -0.0984 -0.2001 333 ILE C CD1 
7569  N N   . GLN C 270 ? 0.9162 0.7825 0.7274 0.1383  -0.1418 -0.2015 334 GLN C N   
7570  C CA  . GLN C 270 ? 0.9011 0.7533 0.7107 0.1373  -0.1580 -0.2031 334 GLN C CA  
7571  C C   . GLN C 270 ? 0.9254 0.7790 0.7376 0.1447  -0.1647 -0.2112 334 GLN C C   
7572  O O   . GLN C 270 ? 1.0945 0.9649 0.9223 0.1450  -0.1579 -0.2143 334 GLN C O   
7573  C CB  . GLN C 270 ? 0.9015 0.7584 0.7290 0.1255  -0.1595 -0.1972 334 GLN C CB  
7574  C CG  . GLN C 270 ? 0.9417 0.7868 0.7690 0.1227  -0.1746 -0.1954 334 GLN C CG  
7575  C CD  . GLN C 270 ? 0.9710 0.8238 0.8141 0.1131  -0.1740 -0.1893 334 GLN C CD  
7576  O OE1 . GLN C 270 ? 0.9044 0.7712 0.7604 0.1096  -0.1642 -0.1890 334 GLN C OE1 
7577  N NE2 . GLN C 270 ? 0.9766 0.8212 0.8195 0.1091  -0.1852 -0.1842 334 GLN C NE2 
7578  N N   . GLY C 271 ? 1.0490 0.8836 0.8465 0.1506  -0.1797 -0.2145 335 GLY C N   
7579  C CA  . GLY C 271 ? 1.0486 0.8795 0.8460 0.1585  -0.1895 -0.2223 335 GLY C CA  
7580  C C   . GLY C 271 ? 0.9097 0.7161 0.6957 0.1599  -0.2096 -0.2225 335 GLY C C   
7581  O O   . GLY C 271 ? 1.0803 0.8731 0.8569 0.1562  -0.2155 -0.2177 335 GLY C O   
7582  N N   . PHE C 272 ? 0.9231 0.7228 0.7103 0.1651  -0.2212 -0.2278 336 PHE C N   
7583  C CA  . PHE C 272 ? 0.9574 0.7330 0.7380 0.1643  -0.2423 -0.2263 336 PHE C CA  
7584  C C   . PHE C 272 ? 1.0690 0.8259 0.8320 0.1793  -0.2565 -0.2374 336 PHE C C   
7585  O O   . PHE C 272 ? 1.0099 0.7745 0.7642 0.1927  -0.2491 -0.2475 336 PHE C O   
7586  C CB  . PHE C 272 ? 0.9376 0.7169 0.7368 0.1540  -0.2483 -0.2192 336 PHE C CB  
7587  C CG  . PHE C 272 ? 1.0242 0.8154 0.8326 0.1591  -0.2450 -0.2252 336 PHE C CG  
7588  C CD1 . PHE C 272 ? 1.0548 0.8315 0.8593 0.1658  -0.2609 -0.2300 336 PHE C CD1 
7589  C CD2 . PHE C 272 ? 0.9360 0.7517 0.7570 0.1578  -0.2275 -0.2265 336 PHE C CD2 
7590  C CE1 . PHE C 272 ? 1.0120 0.7992 0.8245 0.1714  -0.2588 -0.2361 336 PHE C CE1 
7591  C CE2 . PHE C 272 ? 1.0170 0.8441 0.8475 0.1630  -0.2255 -0.2327 336 PHE C CE2 
7592  C CZ  . PHE C 272 ? 1.0223 0.8356 0.8481 0.1701  -0.2409 -0.2377 336 PHE C CZ  
7593  N N   . MET C 273 ? 1.1387 0.8715 0.8972 0.1769  -0.2774 -0.2348 337 MET C N   
7594  C CA  . MET C 273 ? 1.0562 0.7655 0.8013 0.1886  -0.2974 -0.2438 337 MET C CA  
7595  C C   . MET C 273 ? 1.0602 0.7535 0.8168 0.1766  -0.3162 -0.2339 337 MET C C   
7596  O O   . MET C 273 ? 1.2456 0.9412 1.0127 0.1626  -0.3159 -0.2216 337 MET C O   
7597  C CB  . MET C 273 ? 0.9800 0.6697 0.7001 0.2001  -0.3059 -0.2512 337 MET C CB  
7598  C CG  . MET C 273 ? 1.1022 0.8063 0.8070 0.2138  -0.2884 -0.2601 337 MET C CG  
7599  S SD  . MET C 273 ? 1.2936 0.9743 0.9639 0.2308  -0.2989 -0.2699 337 MET C SD  
7600  C CE  . MET C 273 ? 1.3509 1.0174 1.0249 0.2141  -0.3075 -0.2569 337 MET C CE  
7601  N N   . ILE C 274 ? 1.1338 0.8116 0.8889 0.1826  -0.3328 -0.2386 338 ILE C N   
7602  C CA  . ILE C 274 ? 1.1623 0.8240 0.9287 0.1716  -0.3518 -0.2281 338 ILE C CA  
7603  C C   . ILE C 274 ? 1.2456 0.8725 0.9965 0.1805  -0.3785 -0.2351 338 ILE C C   
7604  O O   . ILE C 274 ? 1.2269 0.8435 0.9626 0.1974  -0.3848 -0.2498 338 ILE C O   
7605  C CB  . ILE C 274 ? 1.0973 0.7694 0.8775 0.1695  -0.3503 -0.2258 338 ILE C CB  
7606  C CG1 . ILE C 274 ? 1.0138 0.7193 0.8060 0.1655  -0.3249 -0.2238 338 ILE C CG1 
7607  C CG2 . ILE C 274 ? 1.1764 0.8384 0.9708 0.1553  -0.3653 -0.2105 338 ILE C CG2 
7608  C CD1 . ILE C 274 ? 0.9499 0.6661 0.7571 0.1606  -0.3240 -0.2186 338 ILE C CD1 
7609  N N   . GLU C 275 ? 1.2161 0.8255 0.9716 0.1695  -0.3946 -0.2249 339 GLU C N   
7610  C CA  . GLU C 275 ? 1.3166 0.8904 1.0613 0.1751  -0.4235 -0.2295 339 GLU C CA  
7611  C C   . GLU C 275 ? 1.4641 1.0251 1.2264 0.1634  -0.4420 -0.2173 339 GLU C C   
7612  O O   . GLU C 275 ? 1.5506 1.1254 1.3335 0.1458  -0.4370 -0.1998 339 GLU C O   
7613  C CB  . GLU C 275 ? 1.4487 1.0109 1.1874 0.1710  -0.4304 -0.2265 339 GLU C CB  
7614  C CG  . GLU C 275 ? 1.9224 1.4471 1.6568 0.1711  -0.4636 -0.2269 339 GLU C CG  
7615  C CD  . GLU C 275 ? 2.3387 1.8361 2.0457 0.1940  -0.4805 -0.2475 339 GLU C CD  
7616  O OE1 . GLU C 275 ? 2.4795 1.9890 2.1682 0.2109  -0.4645 -0.2617 339 GLU C OE1 
7617  O OE2 . GLU C 275 ? 2.1533 1.6168 1.8577 0.1952  -0.5109 -0.2492 339 GLU C OE2 
7618  N N   . GLY C 276 ? 1.6697 1.2052 1.4234 0.1738  -0.4632 -0.2262 340 GLY C N   
7619  C CA  . GLY C 276 ? 1.7232 1.2423 1.4924 0.1631  -0.4835 -0.2139 340 GLY C CA  
7620  C C   . GLY C 276 ? 1.6373 1.1206 1.3923 0.1774  -0.5115 -0.2267 340 GLY C C   
7621  O O   . GLY C 276 ? 1.6291 1.0953 1.3621 0.1944  -0.5200 -0.2440 340 GLY C O   
7622  N N   . SER C 277 ? 1.7621 1.2333 1.5288 0.1712  -0.5265 -0.2182 341 SER C N   
7623  C CA  . SER C 277 ? 2.0084 1.4468 1.7623 0.1860  -0.5523 -0.2310 341 SER C CA  
7624  C C   . SER C 277 ? 2.0389 1.4899 1.7730 0.2095  -0.5373 -0.2535 341 SER C C   
7625  O O   . SER C 277 ? 1.8740 1.3069 1.5856 0.2290  -0.5477 -0.2724 341 SER C O   
7626  C CB  . SER C 277 ? 2.3202 1.7515 2.0910 0.1751  -0.5641 -0.2165 341 SER C CB  
7627  O OG  . SER C 277 ? 2.5513 1.9684 2.3408 0.1544  -0.5813 -0.1951 341 SER C OG  
7628  N N   . ASN C 278 ? 1.8565 1.3396 1.5998 0.2077  -0.5132 -0.2509 342 ASN C N   
7629  C CA  . ASN C 278 ? 1.6110 1.1198 1.3430 0.2242  -0.4896 -0.2671 342 ASN C CA  
7630  C C   . ASN C 278 ? 1.4435 0.9786 1.1767 0.2175  -0.4647 -0.2632 342 ASN C C   
7631  O O   . ASN C 278 ? 1.5193 1.0635 1.2680 0.1983  -0.4591 -0.2460 342 ASN C O   
7632  C CB  . ASN C 278 ? 1.6533 1.1854 1.3980 0.2230  -0.4758 -0.2646 342 ASN C CB  
7633  C CG  . ASN C 278 ? 1.5478 1.0560 1.2884 0.2337  -0.4983 -0.2718 342 ASN C CG  
7634  O OD1 . ASN C 278 ? 1.6662 1.1551 1.3886 0.2538  -0.5122 -0.2899 342 ASN C OD1 
7635  N ND2 . ASN C 278 ? 1.6284 1.1386 1.3849 0.2215  -0.5017 -0.2578 342 ASN C ND2 
7636  N N   . SER C 279 ? 1.3761 0.9238 1.0930 0.2337  -0.4500 -0.2785 343 SER C N   
7637  C CA  . SER C 279 ? 1.2847 0.8584 1.0025 0.2280  -0.4249 -0.2747 343 SER C CA  
7638  C C   . SER C 279 ? 1.3871 0.9951 1.1063 0.2366  -0.3977 -0.2824 343 SER C C   
7639  O O   . SER C 279 ? 1.3528 0.9619 1.0643 0.2534  -0.3992 -0.2960 343 SER C O   
7640  C CB  . SER C 279 ? 1.4282 0.9845 1.1251 0.2368  -0.4328 -0.2823 343 SER C CB  
7641  O OG  . SER C 279 ? 1.7241 1.2535 1.4259 0.2243  -0.4557 -0.2720 343 SER C OG  
7642  N N   . TRP C 280 ? 1.3139 0.9499 1.0445 0.2249  -0.3738 -0.2733 344 TRP C N   
7643  C CA  . TRP C 280 ? 1.0239 0.6939 0.7610 0.2294  -0.3480 -0.2779 344 TRP C CA  
7644  C C   . TRP C 280 ? 1.0676 0.7559 0.7988 0.2299  -0.3273 -0.2781 344 TRP C C   
7645  O O   . TRP C 280 ? 1.0403 0.7255 0.7724 0.2183  -0.3255 -0.2684 344 TRP C O   
7646  C CB  . TRP C 280 ? 0.8447 0.5340 0.6052 0.2148  -0.3384 -0.2667 344 TRP C CB  
7647  C CG  . TRP C 280 ? 0.8997 0.5742 0.6666 0.2143  -0.3565 -0.2651 344 TRP C CG  
7648  C CD1 . TRP C 280 ? 0.9290 0.5805 0.7006 0.2030  -0.3767 -0.2534 344 TRP C CD1 
7649  C CD2 . TRP C 280 ? 0.8953 0.5769 0.6656 0.2252  -0.3570 -0.2744 344 TRP C CD2 
7650  N NE1 . TRP C 280 ? 0.9485 0.5911 0.7247 0.2059  -0.3894 -0.2541 344 TRP C NE1 
7651  C CE2 . TRP C 280 ? 0.9553 0.6145 0.7304 0.2196  -0.3789 -0.2673 344 TRP C CE2 
7652  C CE3 . TRP C 280 ? 0.8556 0.5594 0.6267 0.2385  -0.3427 -0.2869 344 TRP C CE3 
7653  C CZ2 . TRP C 280 ? 0.9014 0.5588 0.6793 0.2282  -0.3865 -0.2735 344 TRP C CZ2 
7654  C CZ3 . TRP C 280 ? 0.8900 0.5935 0.6658 0.2470  -0.3503 -0.2936 344 TRP C CZ3 
7655  C CH2 . TRP C 280 ? 0.9094 0.5892 0.6874 0.2424  -0.3720 -0.2876 344 TRP C CH2 
7656  N N   . ILE C 281 ? 1.1785 0.8869 0.9043 0.2436  -0.3112 -0.2885 345 ILE C N   
7657  C CA  . ILE C 281 ? 1.1125 0.8451 0.8385 0.2414  -0.2873 -0.2857 345 ILE C CA  
7658  C C   . ILE C 281 ? 1.1178 0.8831 0.8629 0.2399  -0.2672 -0.2859 345 ILE C C   
7659  O O   . ILE C 281 ? 1.2057 0.9793 0.9517 0.2529  -0.2670 -0.2961 345 ILE C O   
7660  C CB  . ILE C 281 ? 1.1864 0.9157 0.8871 0.2594  -0.2844 -0.2962 345 ILE C CB  
7661  C CG1 . ILE C 281 ? 1.2027 0.8988 0.8839 0.2607  -0.3048 -0.2963 345 ILE C CG1 
7662  C CG2 . ILE C 281 ? 1.0826 0.8408 0.7866 0.2563  -0.2574 -0.2914 345 ILE C CG2 
7663  C CD1 . ILE C 281 ? 1.1822 0.8695 0.8334 0.2819  -0.3069 -0.3089 345 ILE C CD1 
7664  N N   . GLY C 282 ? 0.9993 0.7827 0.7607 0.2243  -0.2518 -0.2748 346 GLY C N   
7665  C CA  . GLY C 282 ? 0.9476 0.7620 0.7288 0.2213  -0.2329 -0.2742 346 GLY C CA  
7666  C C   . GLY C 282 ? 0.8806 0.7134 0.6578 0.2233  -0.2129 -0.2732 346 GLY C C   
7667  O O   . GLY C 282 ? 0.9696 0.7922 0.7341 0.2198  -0.2122 -0.2681 346 GLY C O   
7668  N N   . ARG C 283 ? 0.8473 0.7073 0.6362 0.2286  -0.1971 -0.2772 347 ARG C N   
7669  C CA  . ARG C 283 ? 0.9252 0.8061 0.7142 0.2291  -0.1766 -0.2737 347 ARG C CA  
7670  C C   . ARG C 283 ? 1.0772 0.9917 0.8905 0.2281  -0.1594 -0.2740 347 ARG C C   
7671  O O   . ARG C 283 ? 1.1396 1.0627 0.9660 0.2330  -0.1633 -0.2808 347 ARG C O   
7672  C CB  . ARG C 283 ? 0.9531 0.8273 0.7147 0.2469  -0.1769 -0.2811 347 ARG C CB  
7673  C CG  . ARG C 283 ? 1.1045 0.9947 0.8648 0.2653  -0.1730 -0.2927 347 ARG C CG  
7674  C CD  . ARG C 283 ? 1.1960 1.0718 0.9243 0.2850  -0.1795 -0.3017 347 ARG C CD  
7675  N NE  . ARG C 283 ? 1.1917 1.0896 0.9169 0.3047  -0.1706 -0.3120 347 ARG C NE  
7676  C CZ  . ARG C 283 ? 1.3073 1.2020 1.0047 0.3253  -0.1707 -0.3204 347 ARG C CZ  
7677  N NH1 . ARG C 283 ? 1.2761 1.1441 0.9460 0.3285  -0.1806 -0.3202 347 ARG C NH1 
7678  N NH2 . ARG C 283 ? 1.5899 1.5091 1.2871 0.3437  -0.1611 -0.3293 347 ARG C NH2 
7679  N N   . ILE C 284 ? 1.0204 0.9530 0.8402 0.2218  -0.1412 -0.2662 348 ILE C N   
7680  C CA  . ILE C 284 ? 0.9321 0.8975 0.7770 0.2197  -0.1245 -0.2647 348 ILE C CA  
7681  C C   . ILE C 284 ? 1.0111 0.9922 0.8484 0.2388  -0.1184 -0.2737 348 ILE C C   
7682  O O   . ILE C 284 ? 1.1175 1.0925 0.9299 0.2503  -0.1162 -0.2755 348 ILE C O   
7683  C CB  . ILE C 284 ? 0.8713 0.8493 0.7252 0.2071  -0.1084 -0.2526 348 ILE C CB  
7684  C CG1 . ILE C 284 ? 1.0351 0.9948 0.8925 0.1908  -0.1166 -0.2452 348 ILE C CG1 
7685  C CG2 . ILE C 284 ? 0.8057 0.8174 0.6899 0.2032  -0.0931 -0.2502 348 ILE C CG2 
7686  C CD1 . ILE C 284 ? 0.9576 0.9290 0.8322 0.1756  -0.1044 -0.2341 348 ILE C CD1 
7687  N N   . ILE C 285 ? 1.0248 1.0267 0.8831 0.2434  -0.1161 -0.2799 349 ILE C N   
7688  C CA  . ILE C 285 ? 0.9007 0.9196 0.7538 0.2636  -0.1117 -0.2901 349 ILE C CA  
7689  C C   . ILE C 285 ? 0.9602 1.0076 0.8137 0.2686  -0.0896 -0.2843 349 ILE C C   
7690  O O   . ILE C 285 ? 1.1843 1.2307 1.0125 0.2858  -0.0873 -0.2894 349 ILE C O   
7691  C CB  . ILE C 285 ? 0.8839 0.9193 0.7618 0.2671  -0.1154 -0.2981 349 ILE C CB  
7692  C CG1 . ILE C 285 ? 0.9375 0.9432 0.8104 0.2650  -0.1382 -0.3036 349 ILE C CG1 
7693  C CG2 . ILE C 285 ? 0.8327 0.8879 0.7056 0.2894  -0.1102 -0.3088 349 ILE C CG2 
7694  C CD1 . ILE C 285 ? 0.7754 0.7918 0.6675 0.2705  -0.1452 -0.3124 349 ILE C CD1 
7695  N N   . ASN C 286 ? 1.0779 1.1502 0.9596 0.2540  -0.0739 -0.2735 350 ASN C N   
7696  C CA  . ASN C 286 ? 1.1637 1.2675 1.0515 0.2566  -0.0515 -0.2652 350 ASN C CA  
7697  C C   . ASN C 286 ? 1.1598 1.2579 1.0447 0.2407  -0.0424 -0.2500 350 ASN C C   
7698  O O   . ASN C 286 ? 1.2704 1.3806 1.1834 0.2232  -0.0354 -0.2401 350 ASN C O   
7699  C CB  . ASN C 286 ? 1.2398 1.3815 1.1667 0.2532  -0.0401 -0.2640 350 ASN C CB  
7700  C CG  . ASN C 286 ? 1.3096 1.4622 1.2391 0.2718  -0.0466 -0.2790 350 ASN C CG  
7701  O OD1 . ASN C 286 ? 1.3250 1.4637 1.2617 0.2708  -0.0628 -0.2877 350 ASN C OD1 
7702  N ND2 . ASN C 286 ? 1.5713 1.7495 1.4942 0.2898  -0.0339 -0.2820 350 ASN C ND2 
7703  N N   . PRO C 287 ? 1.1946 1.2731 1.0452 0.2476  -0.0436 -0.2484 351 PRO C N   
7704  C CA  . PRO C 287 ? 1.1671 1.2325 1.0096 0.2337  -0.0392 -0.2353 351 PRO C CA  
7705  C C   . PRO C 287 ? 1.2070 1.3017 1.0721 0.2223  -0.0180 -0.2201 351 PRO C C   
7706  O O   . PRO C 287 ? 1.1813 1.2662 1.0504 0.2064  -0.0160 -0.2088 351 PRO C O   
7707  C CB  . PRO C 287 ? 1.0786 1.1258 0.8793 0.2498  -0.0422 -0.2389 351 PRO C CB  
7708  C CG  . PRO C 287 ? 1.0705 1.1086 0.8575 0.2683  -0.0562 -0.2555 351 PRO C CG  
7709  C CD  . PRO C 287 ? 1.0846 1.1550 0.9016 0.2711  -0.0481 -0.2593 351 PRO C CD  
7710  N N   . GLY C 288 ? 1.4740 1.6043 1.3545 0.2306  -0.0028 -0.2193 352 GLY C N   
7711  C CA  . GLY C 288 ? 1.5179 1.6796 1.4272 0.2182  0.0168  -0.2035 352 GLY C CA  
7712  C C   . GLY C 288 ? 1.5586 1.7232 1.5071 0.1972  0.0121  -0.1996 352 GLY C C   
7713  O O   . GLY C 288 ? 1.3559 1.5114 1.3135 0.1796  0.0134  -0.1880 352 GLY C O   
7714  N N   . SER C 289 ? 1.3575 1.5334 1.3281 0.2003  0.0053  -0.2103 353 SER C N   
7715  C CA  . SER C 289 ? 1.2406 1.4216 1.2484 0.1834  -0.0001 -0.2088 353 SER C CA  
7716  C C   . SER C 289 ? 1.0979 1.2437 1.0980 0.1749  -0.0197 -0.2145 353 SER C C   
7717  O O   . SER C 289 ? 1.0263 1.1720 1.0525 0.1611  -0.0254 -0.2131 353 SER C O   
7718  C CB  . SER C 289 ? 1.3298 1.5401 1.3661 0.1906  0.0011  -0.2173 353 SER C CB  
7719  O OG  . SER C 289 ? 1.3192 1.5264 1.3335 0.2118  -0.0051 -0.2317 353 SER C OG  
7720  N N   . LYS C 290 ? 1.0920 1.2090 1.0566 0.1838  -0.0303 -0.2208 354 LYS C N   
7721  C CA  . LYS C 290 ? 1.0432 1.1286 0.9983 0.1779  -0.0487 -0.2258 354 LYS C CA  
7722  C C   . LYS C 290 ? 1.0609 1.1473 1.0322 0.1803  -0.0615 -0.2372 354 LYS C C   
7723  O O   . LYS C 290 ? 1.2218 1.2909 1.1967 0.1720  -0.0741 -0.2388 354 LYS C O   
7724  C CB  . LYS C 290 ? 1.0602 1.1359 1.0252 0.1592  -0.0482 -0.2147 354 LYS C CB  
7725  C CG  . LYS C 290 ? 1.1064 1.1767 1.0536 0.1562  -0.0380 -0.2032 354 LYS C CG  
7726  C CD  . LYS C 290 ? 1.2849 1.3252 1.1952 0.1636  -0.0483 -0.2068 354 LYS C CD  
7727  C CE  . LYS C 290 ? 1.3725 1.4080 1.2622 0.1634  -0.0384 -0.1963 354 LYS C CE  
7728  N NZ  . LYS C 290 ? 1.2366 1.2664 1.1395 0.1458  -0.0365 -0.1849 354 LYS C NZ  
7729  N N   . LYS C 291 ? 0.9745 1.0820 0.9545 0.1928  -0.0579 -0.2449 355 LYS C N   
7730  C CA  . LYS C 291 ? 0.9633 1.0752 0.9608 0.1957  -0.0687 -0.2551 355 LYS C CA  
7731  C C   . LYS C 291 ? 0.9615 1.0494 0.9321 0.2093  -0.0844 -0.2663 355 LYS C C   
7732  O O   . LYS C 291 ? 1.0061 1.0889 0.9518 0.2236  -0.0834 -0.2704 355 LYS C O   
7733  C CB  . LYS C 291 ? 1.0891 1.2381 1.1131 0.2024  -0.0574 -0.2576 355 LYS C CB  
7734  C CG  . LYS C 291 ? 1.2361 1.4091 1.2975 0.1865  -0.0472 -0.2479 355 LYS C CG  
7735  C CD  . LYS C 291 ? 1.3765 1.5592 1.4681 0.1834  -0.0568 -0.2555 355 LYS C CD  
7736  C CE  . LYS C 291 ? 1.4159 1.6275 1.5485 0.1702  -0.0467 -0.2468 355 LYS C CE  
7737  N NZ  . LYS C 291 ? 1.7100 1.9551 1.8535 0.1749  -0.0270 -0.2394 355 LYS C NZ  
7738  N N   . GLY C 292 ? 0.9067 0.9791 0.8819 0.2051  -0.0997 -0.2710 356 GLY C N   
7739  C CA  . GLY C 292 ? 0.9943 1.0459 0.9502 0.2170  -0.1163 -0.2812 356 GLY C CA  
7740  C C   . GLY C 292 ? 0.9565 0.9745 0.8826 0.2159  -0.1273 -0.2788 356 GLY C C   
7741  O O   . GLY C 292 ? 0.9222 0.9337 0.8346 0.2119  -0.1207 -0.2716 356 GLY C O   
7742  N N   . PHE C 293 ? 0.9261 0.9228 0.8432 0.2193  -0.1451 -0.2844 357 PHE C N   
7743  C CA  . PHE C 293 ? 0.9523 0.9174 0.8442 0.2184  -0.1581 -0.2822 357 PHE C CA  
7744  C C   . PHE C 293 ? 0.9814 0.9287 0.8587 0.2322  -0.1752 -0.2923 357 PHE C C   
7745  O O   . PHE C 293 ? 1.0581 1.0075 0.9470 0.2344  -0.1835 -0.2972 357 PHE C O   
7746  C CB  . PHE C 293 ? 0.8899 0.8442 0.7893 0.2019  -0.1637 -0.2735 357 PHE C CB  
7747  C CG  . PHE C 293 ? 0.8067 0.7322 0.6851 0.1985  -0.1758 -0.2689 357 PHE C CG  
7748  C CD1 . PHE C 293 ? 0.7980 0.7025 0.6671 0.2024  -0.1941 -0.2719 357 PHE C CD1 
7749  C CD2 . PHE C 293 ? 0.8525 0.7719 0.7216 0.1911  -0.1698 -0.2608 357 PHE C CD2 
7750  C CE1 . PHE C 293 ? 0.8957 0.7747 0.7487 0.1979  -0.2061 -0.2663 357 PHE C CE1 
7751  C CE2 . PHE C 293 ? 0.8063 0.7002 0.6582 0.1877  -0.1819 -0.2563 357 PHE C CE2 
7752  C CZ  . PHE C 293 ? 0.8582 0.7326 0.7033 0.1905  -0.1999 -0.2587 357 PHE C CZ  
7753  N N   . GLU C 294 ? 0.9153 0.8441 0.7667 0.2421  -0.1817 -0.2955 358 GLU C N   
7754  C CA  . GLU C 294 ? 0.9752 0.8819 0.8100 0.2560  -0.2007 -0.3054 358 GLU C CA  
7755  C C   . GLU C 294 ? 0.9387 0.8108 0.7540 0.2506  -0.2175 -0.3005 358 GLU C C   
7756  O O   . GLU C 294 ? 0.9298 0.7960 0.7368 0.2430  -0.2127 -0.2930 358 GLU C O   
7757  C CB  . GLU C 294 ? 1.0126 0.9285 0.8341 0.2774  -0.1967 -0.3171 358 GLU C CB  
7758  C CG  . GLU C 294 ? 1.2853 1.1990 1.0850 0.2829  -0.1880 -0.3153 358 GLU C CG  
7759  C CD  . GLU C 294 ? 1.7696 1.6978 1.5555 0.3066  -0.1816 -0.3271 358 GLU C CD  
7760  O OE1 . GLU C 294 ? 2.0082 1.9368 1.7944 0.3213  -0.1910 -0.3390 358 GLU C OE1 
7761  O OE2 . GLU C 294 ? 1.5425 1.4820 1.3164 0.3116  -0.1673 -0.3244 358 GLU C OE2 
7762  N N   . ILE C 295 ? 0.9045 0.7539 0.7145 0.2538  -0.2378 -0.3040 359 ILE C N   
7763  C CA  . ILE C 295 ? 0.9521 0.7683 0.7457 0.2494  -0.2560 -0.2994 359 ILE C CA  
7764  C C   . ILE C 295 ? 0.9611 0.7545 0.7371 0.2670  -0.2758 -0.3116 359 ILE C C   
7765  O O   . ILE C 295 ? 1.0465 0.8464 0.8278 0.2778  -0.2793 -0.3206 359 ILE C O   
7766  C CB  . ILE C 295 ? 0.8825 0.6903 0.6890 0.2319  -0.2638 -0.2874 359 ILE C CB  
7767  C CG1 . ILE C 295 ? 0.9272 0.7058 0.7206 0.2246  -0.2793 -0.2798 359 ILE C CG1 
7768  C CG2 . ILE C 295 ? 0.8660 0.6701 0.6805 0.2361  -0.2759 -0.2916 359 ILE C CG2 
7769  C CD1 . ILE C 295 ? 0.8277 0.6036 0.6347 0.2061  -0.2830 -0.2650 359 ILE C CD1 
7770  N N   . TYR C 296 ? 0.9543 0.7199 0.7098 0.2703  -0.2902 -0.3122 360 TYR C N   
7771  C CA  . TYR C 296 ? 1.0030 0.7498 0.7373 0.2914  -0.3056 -0.3268 360 TYR C CA  
7772  C C   . TYR C 296 ? 1.0039 0.7106 0.7249 0.2884  -0.3324 -0.3243 360 TYR C C   
7773  O O   . TYR C 296 ? 1.0815 0.7769 0.7986 0.2767  -0.3344 -0.3148 360 TYR C O   
7774  C CB  . TYR C 296 ? 1.1066 0.8679 0.8249 0.3057  -0.2905 -0.3343 360 TYR C CB  
7775  C CG  . TYR C 296 ? 1.1844 0.9323 0.8788 0.3314  -0.3029 -0.3513 360 TYR C CG  
7776  C CD1 . TYR C 296 ? 1.2923 1.0540 0.9903 0.3481  -0.3023 -0.3636 360 TYR C CD1 
7777  C CD2 . TYR C 296 ? 1.2698 0.9916 0.9376 0.3405  -0.3160 -0.3559 360 TYR C CD2 
7778  C CE1 . TYR C 296 ? 1.2539 1.0037 0.9288 0.3740  -0.3142 -0.3804 360 TYR C CE1 
7779  C CE2 . TYR C 296 ? 1.3656 1.0740 1.0092 0.3663  -0.3286 -0.3730 360 TYR C CE2 
7780  C CZ  . TYR C 296 ? 1.3320 1.0548 0.9789 0.3834  -0.3274 -0.3853 360 TYR C CZ  
7781  O OH  . TYR C 296 ? 1.3578 1.0675 0.9792 0.4112  -0.3404 -0.4034 360 TYR C OH  
7782  N N   . LYS C 297 ? 1.0179 0.7029 0.7335 0.2987  -0.3540 -0.3324 361 LYS C N   
7783  C CA  . LYS C 297 ? 1.1095 0.7563 0.8195 0.2924  -0.3819 -0.3275 361 LYS C CA  
7784  C C   . LYS C 297 ? 1.2295 0.8467 0.9126 0.3100  -0.4012 -0.3402 361 LYS C C   
7785  O O   . LYS C 297 ? 1.4720 1.0948 1.1396 0.3326  -0.3987 -0.3566 361 LYS C O   
7786  C CB  . LYS C 297 ? 1.0951 0.7330 0.8159 0.2922  -0.3961 -0.3275 361 LYS C CB  
7787  C CG  . LYS C 297 ? 1.1090 0.7111 0.8306 0.2819  -0.4237 -0.3182 361 LYS C CG  
7788  C CD  . LYS C 297 ? 1.1733 0.7725 0.9045 0.2843  -0.4332 -0.3192 361 LYS C CD  
7789  C CE  . LYS C 297 ? 1.1472 0.7059 0.8748 0.2816  -0.4656 -0.3147 361 LYS C CE  
7790  N NZ  . LYS C 297 ? 1.2354 0.7955 0.9739 0.2821  -0.4714 -0.3132 361 LYS C NZ  
7791  N N   . PHE C 298 ? 1.2113 0.7979 0.8893 0.3002  -0.4209 -0.3326 362 PHE C N   
7792  C CA  . PHE C 298 ? 1.2380 0.7921 0.8906 0.3153  -0.4429 -0.3441 362 PHE C CA  
7793  C C   . PHE C 298 ? 1.3019 0.8163 0.9575 0.3063  -0.4755 -0.3377 362 PHE C C   
7794  O O   . PHE C 298 ? 1.3063 0.8193 0.9807 0.2830  -0.4770 -0.3192 362 PHE C O   
7795  C CB  . PHE C 298 ? 1.2371 0.7947 0.8792 0.3115  -0.4329 -0.3404 362 PHE C CB  
7796  C CG  . PHE C 298 ? 1.2760 0.8685 0.9111 0.3215  -0.4031 -0.3461 362 PHE C CG  
7797  C CD1 . PHE C 298 ? 1.3141 0.9059 0.9231 0.3477  -0.4028 -0.3637 362 PHE C CD1 
7798  C CD2 . PHE C 298 ? 1.1728 0.7984 0.8269 0.3049  -0.3758 -0.3332 362 PHE C CD2 
7799  C CE1 . PHE C 298 ? 1.2912 0.9177 0.8949 0.3561  -0.3739 -0.3664 362 PHE C CE1 
7800  C CE2 . PHE C 298 ? 1.1366 0.7933 0.7859 0.3127  -0.3492 -0.3366 362 PHE C CE2 
7801  C CZ  . PHE C 298 ? 1.0768 0.7350 0.7016 0.3376  -0.3475 -0.3522 362 PHE C CZ  
7802  N N   . LEU C 299 ? 1.3908 0.8726 1.0279 0.3248  -0.5023 -0.3525 363 LEU C N   
7803  C CA  . LEU C 299 ? 1.5113 0.9514 1.1507 0.3159  -0.5361 -0.3461 363 LEU C CA  
7804  C C   . LEU C 299 ? 1.7615 1.1844 1.3925 0.3094  -0.5451 -0.3418 363 LEU C C   
7805  O O   . LEU C 299 ? 1.6791 1.1011 1.2866 0.3266  -0.5417 -0.3555 363 LEU C O   
7806  C CB  . LEU C 299 ? 1.6275 1.0354 1.2510 0.3376  -0.5646 -0.3634 363 LEU C CB  
7807  C CG  . LEU C 299 ? 1.7318 1.1449 1.3700 0.3366  -0.5664 -0.3615 363 LEU C CG  
7808  C CD1 . LEU C 299 ? 1.5013 0.9220 1.1686 0.3059  -0.5620 -0.3356 363 LEU C CD1 
7809  C CD2 . LEU C 299 ? 1.5667 1.0178 1.2021 0.3537  -0.5395 -0.3745 363 LEU C CD2 
7810  N N   . GLY C 300 ? 1.9765 1.3884 1.6272 0.2847  -0.5552 -0.3221 364 GLY C N   
7811  C CA  . GLY C 300 ? 1.8021 1.1977 1.4498 0.2757  -0.5658 -0.3159 364 GLY C CA  
7812  C C   . GLY C 300 ? 1.6989 1.1263 1.3448 0.2713  -0.5357 -0.3122 364 GLY C C   
7813  O O   . GLY C 300 ? 1.7314 1.1952 1.3843 0.2697  -0.5058 -0.3100 364 GLY C O   
7814  N N   . THR C 301 ? 1.7315 1.1434 1.3677 0.2698  -0.5454 -0.3119 365 THR C N   
7815  C CA  . THR C 301 ? 1.5347 0.9714 1.1717 0.2614  -0.5213 -0.3045 365 THR C CA  
7816  C C   . THR C 301 ? 1.4132 0.8767 1.0301 0.2794  -0.4938 -0.3173 365 THR C C   
7817  O O   . THR C 301 ? 1.4598 0.9182 1.0552 0.3030  -0.4967 -0.3352 365 THR C O   
7818  C CB  . THR C 301 ? 1.5804 0.9911 1.2123 0.2556  -0.5419 -0.3011 365 THR C CB  
7819  O OG1 . THR C 301 ? 1.8905 1.3260 1.5256 0.2461  -0.5185 -0.2924 365 THR C OG1 
7820  C CG2 . THR C 301 ? 1.7316 1.1111 1.3304 0.2809  -0.5636 -0.3222 365 THR C CG2 
7821  N N   . LEU C 302 ? 1.3595 0.8525 0.9845 0.2680  -0.4669 -0.3071 366 LEU C N   
7822  C CA  . LEU C 302 ? 1.4103 0.9287 1.0186 0.2814  -0.4406 -0.3152 366 LEU C CA  
7823  C C   . LEU C 302 ? 1.5239 1.0251 1.1053 0.2929  -0.4485 -0.3226 366 LEU C C   
7824  O O   . LEU C 302 ? 1.6972 1.2157 1.2599 0.3058  -0.4290 -0.3290 366 LEU C O   
7825  C CB  . LEU C 302 ? 1.2950 0.8494 0.9243 0.2633  -0.4107 -0.3003 366 LEU C CB  
7826  C CG  . LEU C 302 ? 1.3901 0.9636 1.0467 0.2504  -0.4015 -0.2914 366 LEU C CG  
7827  C CD1 . LEU C 302 ? 1.4798 1.0495 1.1596 0.2264  -0.4084 -0.2732 366 LEU C CD1 
7828  C CD2 . LEU C 302 ? 1.4170 1.0289 1.0802 0.2500  -0.3689 -0.2900 366 LEU C CD2 
7829  N N   . PHE C 303 ? 1.5654 1.0326 1.1452 0.2881  -0.4777 -0.3210 367 PHE C N   
7830  C CA  . PHE C 303 ? 1.4365 0.8866 0.9947 0.2950  -0.4871 -0.3254 367 PHE C CA  
7831  C C   . PHE C 303 ? 1.4903 0.9036 1.0193 0.3185  -0.5165 -0.3444 367 PHE C C   
7832  O O   . PHE C 303 ? 1.6324 1.0260 1.1408 0.3266  -0.5296 -0.3502 367 PHE C O   
7833  C CB  . PHE C 303 ? 1.4178 0.8611 0.9981 0.2703  -0.4957 -0.3080 367 PHE C CB  
7834  C CG  . PHE C 303 ? 1.3069 0.7856 0.9142 0.2491  -0.4680 -0.2905 367 PHE C CG  
7835  C CD1 . PHE C 303 ? 1.2565 0.7662 0.8571 0.2524  -0.4365 -0.2901 367 PHE C CD1 
7836  C CD2 . PHE C 303 ? 1.5889 1.0706 1.2284 0.2266  -0.4734 -0.2742 367 PHE C CD2 
7837  C CE1 . PHE C 303 ? 1.3581 0.8988 0.9836 0.2338  -0.4125 -0.2752 367 PHE C CE1 
7838  C CE2 . PHE C 303 ? 1.7807 1.2956 1.4436 0.2091  -0.4481 -0.2592 367 PHE C CE2 
7839  C CZ  . PHE C 303 ? 1.4318 0.9749 1.0876 0.2129  -0.4186 -0.2605 367 PHE C CZ  
7840  N N   . SER C 304 ? 1.8182 1.2216 1.3448 0.3304  -0.5281 -0.3548 368 SER C N   
7841  C CA  . SER C 304 ? 1.8364 1.2089 1.3315 0.3586  -0.5528 -0.3767 368 SER C CA  
7842  C C   . SER C 304 ? 1.7730 1.1722 1.2458 0.3835  -0.5285 -0.3910 368 SER C C   
7843  O O   . SER C 304 ? 1.6199 1.0507 1.1091 0.3791  -0.5049 -0.3865 368 SER C O   
7844  C CB  . SER C 304 ? 1.8523 1.1933 1.3589 0.3568  -0.5848 -0.3794 368 SER C CB  
7845  O OG  . SER C 304 ? 2.3183 1.6227 1.7944 0.3832  -0.6145 -0.4007 368 SER C OG  
7846  N N   . VAL C 305 ? 1.8973 1.2850 1.3330 0.4102  -0.5343 -0.4080 369 VAL C N   
7847  C CA  . VAL C 305 ? 1.9488 1.3610 1.3611 0.4372  -0.5138 -0.4225 369 VAL C CA  
7848  C C   . VAL C 305 ? 1.9268 1.3279 1.3378 0.4537  -0.5296 -0.4370 369 VAL C C   
7849  O O   . VAL C 305 ? 1.7160 1.1421 1.1164 0.4736  -0.5120 -0.4475 369 VAL C O   
7850  C CB  . VAL C 305 ? 2.0007 1.4013 1.3710 0.4625  -0.5182 -0.4363 369 VAL C CB  
7851  C CG1 . VAL C 305 ? 2.1915 1.5405 1.5399 0.4793  -0.5623 -0.4533 369 VAL C CG1 
7852  C CG2 . VAL C 305 ? 2.0255 1.4601 1.3733 0.4882  -0.4904 -0.4469 369 VAL C CG2 
7853  N N   . GLN C 306 ? 2.1056 1.4695 1.5293 0.4442  -0.5632 -0.4361 370 GLN C N   
7854  C CA  . GLN C 306 ? 1.9296 1.2713 1.3511 0.4585  -0.5870 -0.4496 370 GLN C CA  
7855  C C   . GLN C 306 ? 1.7462 1.1172 1.1955 0.4483  -0.5680 -0.4420 370 GLN C C   
7856  O O   . GLN C 306 ? 1.7887 1.1549 1.2326 0.4660  -0.5770 -0.4554 370 GLN C O   
7857  C CB  . GLN C 306 ? 2.0161 1.3084 1.4477 0.4458  -0.6290 -0.4461 370 GLN C CB  
7858  C CG  . GLN C 306 ? 2.1559 1.4057 1.5559 0.4646  -0.6618 -0.4618 370 GLN C CG  
7859  C CD  . GLN C 306 ? 2.3569 1.5840 1.7244 0.5014  -0.6828 -0.4890 370 GLN C CD  
7860  O OE1 . GLN C 306 ? 2.4087 1.6587 1.7487 0.5283  -0.6633 -0.5037 370 GLN C OE1 
7861  N NE2 . GLN C 306 ? 2.3112 1.4935 1.6823 0.5030  -0.7232 -0.4954 370 GLN C NE2 
7862  N N   . THR C 307 ? 1.8181 1.2187 1.2964 0.4206  -0.5428 -0.4210 371 THR C N   
7863  C CA  . THR C 307 ? 1.8430 1.2617 1.3531 0.4036  -0.5331 -0.4097 371 THR C CA  
7864  C C   . THR C 307 ? 1.7250 1.1850 1.2375 0.4157  -0.5034 -0.4157 371 THR C C   
7865  O O   . THR C 307 ? 1.7284 1.2179 1.2284 0.4264  -0.4775 -0.4193 371 THR C O   
7866  C CB  . THR C 307 ? 1.8945 1.3224 1.4359 0.3688  -0.5245 -0.3849 371 THR C CB  
7867  O OG1 . THR C 307 ? 2.1109 1.5655 1.6494 0.3628  -0.4976 -0.3778 371 THR C OG1 
7868  C CG2 . THR C 307 ? 2.2249 1.6101 1.7714 0.3560  -0.5594 -0.3782 371 THR C CG2 
7869  N N   . VAL C 308 ? 1.7160 1.1785 1.2470 0.4122  -0.5076 -0.4148 372 VAL C N   
7870  C CA  . VAL C 308 ? 1.5672 1.0574 1.0983 0.4298  -0.4918 -0.4261 372 VAL C CA  
7871  C C   . VAL C 308 ? 1.5099 1.0389 1.0735 0.4094  -0.4642 -0.4109 372 VAL C C   
7872  O O   . VAL C 308 ? 1.3525 0.8738 0.9398 0.3861  -0.4710 -0.3960 372 VAL C O   
7873  C CB  . VAL C 308 ? 1.4559 0.9134 0.9805 0.4457  -0.5237 -0.4401 372 VAL C CB  
7874  C CG1 . VAL C 308 ? 1.3566 0.8407 0.8784 0.4680  -0.5106 -0.4545 372 VAL C CG1 
7875  C CG2 . VAL C 308 ? 1.5853 0.9984 1.0795 0.4639  -0.5563 -0.4547 372 VAL C CG2 
7876  N N   . GLY C 309 ? 1.5248 1.0957 1.0896 0.4183  -0.4335 -0.4143 373 GLY C N   
7877  C CA  . GLY C 309 ? 1.5020 1.1088 1.0964 0.4049  -0.4107 -0.4049 373 GLY C CA  
7878  C C   . GLY C 309 ? 1.8069 1.4016 1.4113 0.4099  -0.4284 -0.4111 373 GLY C C   
7879  O O   . GLY C 309 ? 2.0667 1.6399 1.6524 0.4332  -0.4489 -0.4282 373 GLY C O   
7880  N N   . ASN C 310 ? 1.5434 1.1503 1.1756 0.3893  -0.4218 -0.3977 374 ASN C N   
7881  C CA  . ASN C 310 ? 1.5247 1.1188 1.1662 0.3925  -0.4391 -0.4016 374 ASN C CA  
7882  C C   . ASN C 310 ? 1.5948 1.2286 1.2599 0.3886  -0.4160 -0.3989 374 ASN C C   
7883  O O   . ASN C 310 ? 2.0608 1.7068 1.7251 0.4077  -0.4152 -0.4127 374 ASN C O   
7884  C CB  . ASN C 310 ? 1.5769 1.1366 1.2277 0.3715  -0.4628 -0.3871 374 ASN C CB  
7885  C CG  . ASN C 310 ? 1.5122 1.0595 1.1744 0.3718  -0.4796 -0.3875 374 ASN C CG  
7886  O OD1 . ASN C 310 ? 1.2938 0.8584 0.9781 0.3552  -0.4691 -0.3749 374 ASN C OD1 
7887  N ND2 . ASN C 310 ? 1.4942 1.0102 1.1399 0.3915  -0.5067 -0.4024 374 ASN C ND2 
7888  N N   . ARG C 311 ? 1.5724 1.2265 1.2589 0.3645  -0.3980 -0.3817 375 ARG C N   
7889  C CA  . ARG C 311 ? 1.4678 1.1546 1.1791 0.3575  -0.3805 -0.3775 375 ARG C CA  
7890  C C   . ARG C 311 ? 1.3043 1.0276 1.0299 0.3439  -0.3498 -0.3674 375 ARG C C   
7891  O O   . ARG C 311 ? 1.2330 0.9514 0.9599 0.3264  -0.3455 -0.3543 375 ARG C O   
7892  C CB  . ARG C 311 ? 1.3503 1.0201 1.0765 0.3404  -0.3953 -0.3655 375 ARG C CB  
7893  C CG  . ARG C 311 ? 1.4037 1.1041 1.1540 0.3340  -0.3802 -0.3619 375 ARG C CG  
7894  C CD  . ARG C 311 ? 1.6755 1.3867 1.4250 0.3573  -0.3826 -0.3798 375 ARG C CD  
7895  N NE  . ARG C 311 ? 1.2354 0.9744 1.0084 0.3528  -0.3710 -0.3779 375 ARG C NE  
7896  C CZ  . ARG C 311 ? 1.3020 1.0286 1.0842 0.3451  -0.3844 -0.3719 375 ARG C CZ  
7897  N NH1 . ARG C 311 ? 1.2153 0.9031 0.9870 0.3397  -0.4089 -0.3654 375 ARG C NH1 
7898  N NH2 . ARG C 311 ? 1.3611 1.1140 1.1635 0.3426  -0.3737 -0.3716 375 ARG C NH2 
7899  N N   . ASN C 312 ? 1.1270 0.8868 0.8645 0.3520  -0.3294 -0.3734 376 ASN C N   
7900  C CA  . ASN C 312 ? 1.1698 0.9637 0.9232 0.3391  -0.3017 -0.3638 376 ASN C CA  
7901  C C   . ASN C 312 ? 1.1921 1.0086 0.9740 0.3271  -0.2928 -0.3579 376 ASN C C   
7902  O O   . ASN C 312 ? 1.4640 1.2963 1.2554 0.3393  -0.2919 -0.3677 376 ASN C O   
7903  C CB  . ASN C 312 ? 1.2359 1.0580 0.9823 0.3561  -0.2825 -0.3729 376 ASN C CB  
7904  C CG  . ASN C 312 ? 1.2904 1.1516 1.0593 0.3432  -0.2541 -0.3632 376 ASN C CG  
7905  O OD1 . ASN C 312 ? 1.5200 1.4097 1.3110 0.3443  -0.2433 -0.3654 376 ASN C OD1 
7906  N ND2 . ASN C 312 ? 1.1972 1.0585 0.9617 0.3304  -0.2434 -0.3522 376 ASN C ND2 
7907  N N   . TYR C 313 ? 1.0024 0.8207 0.7973 0.3047  -0.2868 -0.3428 377 TYR C N   
7908  C CA  . TYR C 313 ? 1.0304 0.8703 0.8511 0.2928  -0.2777 -0.3367 377 TYR C CA  
7909  C C   . TYR C 313 ? 0.9925 0.8663 0.8287 0.2850  -0.2519 -0.3318 377 TYR C C   
7910  O O   . TYR C 313 ? 1.0173 0.8895 0.8499 0.2733  -0.2437 -0.3222 377 TYR C O   
7911  C CB  . TYR C 313 ? 1.0172 0.8384 0.8422 0.2742  -0.2881 -0.3230 377 TYR C CB  
7912  C CG  . TYR C 313 ? 1.1939 0.9832 1.0095 0.2777  -0.3138 -0.3240 377 TYR C CG  
7913  C CD1 . TYR C 313 ? 1.0995 0.8561 0.8988 0.2738  -0.3308 -0.3186 377 TYR C CD1 
7914  C CD2 . TYR C 313 ? 1.1577 0.9489 0.9823 0.2839  -0.3224 -0.3292 377 TYR C CD2 
7915  C CE1 . TYR C 313 ? 1.1940 0.9202 0.9870 0.2751  -0.3555 -0.3173 377 TYR C CE1 
7916  C CE2 . TYR C 313 ? 1.0748 0.8352 0.8910 0.2862  -0.3467 -0.3284 377 TYR C CE2 
7917  C CZ  . TYR C 313 ? 1.1749 0.9028 0.9758 0.2812  -0.3631 -0.3218 377 TYR C CZ  
7918  O OH  . TYR C 313 ? 1.4502 1.1467 1.2445 0.2821  -0.3881 -0.3193 377 TYR C OH  
7919  N N   . GLN C 314 ? 0.8857 0.7898 0.7405 0.2911  -0.2400 -0.3379 378 GLN C N   
7920  C CA  . GLN C 314 ? 0.8876 0.8238 0.7612 0.2822  -0.2170 -0.3320 378 GLN C CA  
7921  C C   . GLN C 314 ? 0.8805 0.8236 0.7760 0.2659  -0.2161 -0.3243 378 GLN C C   
7922  O O   . GLN C 314 ? 1.1275 1.0864 1.0412 0.2692  -0.2166 -0.3295 378 GLN C O   
7923  C CB  . GLN C 314 ? 0.9442 0.9128 0.8289 0.2969  -0.2036 -0.3415 378 GLN C CB  
7924  C CG  . GLN C 314 ? 1.2921 1.2602 1.1543 0.3137  -0.1995 -0.3481 378 GLN C CG  
7925  C CD  . GLN C 314 ? 1.4637 1.4723 1.3402 0.3219  -0.1776 -0.3504 378 GLN C CD  
7926  O OE1 . GLN C 314 ? 1.6839 1.7210 1.5923 0.3110  -0.1657 -0.3456 378 GLN C OE1 
7927  N NE2 . GLN C 314 ? 1.4776 1.4927 1.3371 0.3382  -0.1716 -0.3562 378 GLN C NE2 
7928  N N   . LEU C 315 ? 0.8930 0.8244 0.7862 0.2495  -0.2157 -0.3124 379 LEU C N   
7929  C CA  . LEU C 315 ? 0.9501 0.8846 0.8598 0.2354  -0.2171 -0.3051 379 LEU C CA  
7930  C C   . LEU C 315 ? 1.0603 1.0264 0.9963 0.2290  -0.2008 -0.3041 379 LEU C C   
7931  O O   . LEU C 315 ? 1.0278 1.0036 0.9809 0.2272  -0.2039 -0.3062 379 LEU C O   
7932  C CB  . LEU C 315 ? 0.7453 0.6598 0.6451 0.2212  -0.2218 -0.2928 379 LEU C CB  
7933  C CG  . LEU C 315 ? 0.7683 0.6507 0.6478 0.2241  -0.2413 -0.2915 379 LEU C CG  
7934  C CD1 . LEU C 315 ? 0.7335 0.6007 0.6070 0.2091  -0.2444 -0.2779 379 LEU C CD1 
7935  C CD2 . LEU C 315 ? 0.7706 0.6452 0.6532 0.2302  -0.2565 -0.2960 379 LEU C CD2 
7936  N N   . LEU C 316 ? 0.9380 0.9186 0.8771 0.2254  -0.1847 -0.3004 380 LEU C N   
7937  C CA  . LEU C 316 ? 0.8851 0.8940 0.8505 0.2178  -0.1700 -0.2978 380 LEU C CA  
7938  C C   . LEU C 316 ? 0.8713 0.9048 0.8434 0.2267  -0.1552 -0.3015 380 LEU C C   
7939  O O   . LEU C 316 ? 0.8213 0.8487 0.7738 0.2334  -0.1512 -0.3013 380 LEU C O   
7940  C CB  . LEU C 316 ? 0.9192 0.9241 0.8862 0.2016  -0.1635 -0.2863 380 LEU C CB  
7941  C CG  . LEU C 316 ? 0.9987 0.9826 0.9583 0.1923  -0.1753 -0.2804 380 LEU C CG  
7942  C CD1 . LEU C 316 ? 0.9834 0.9726 0.9523 0.1781  -0.1665 -0.2714 380 LEU C CD1 
7943  C CD2 . LEU C 316 ? 1.4114 1.3963 1.3813 0.1949  -0.1864 -0.2855 380 LEU C CD2 
7944  N N   . SER C 317 ? 0.9439 1.0060 0.9439 0.2269  -0.1474 -0.3045 381 SER C N   
7945  C CA  . SER C 317 ? 0.9562 1.0480 0.9680 0.2353  -0.1323 -0.3069 381 SER C CA  
7946  C C   . SER C 317 ? 1.0115 1.1296 1.0536 0.2217  -0.1177 -0.2987 381 SER C C   
7947  O O   . SER C 317 ? 1.1590 1.2919 1.2031 0.2193  -0.1022 -0.2916 381 SER C O   
7948  C CB  . SER C 317 ? 1.2641 1.3694 1.2849 0.2514  -0.1380 -0.3197 381 SER C CB  
7949  O OG  . SER C 317 ? 1.5983 1.6761 1.5930 0.2636  -0.1549 -0.3277 381 SER C OG  
7950  N N   . ASN C 318 ? 1.1208 1.2435 1.1860 0.2129  -0.1237 -0.2994 382 ASN C N   
7951  C CA  . ASN C 318 ? 1.3317 1.4786 1.4294 0.2004  -0.1131 -0.2930 382 ASN C CA  
7952  C C   . ASN C 318 ? 1.2011 1.3367 1.2975 0.1836  -0.1091 -0.2814 382 ASN C C   
7953  O O   . ASN C 318 ? 1.6780 1.8306 1.8012 0.1724  -0.1017 -0.2754 382 ASN C O   
7954  C CB  . ASN C 318 ? 1.5361 1.6950 1.6616 0.1999  -0.1223 -0.3003 382 ASN C CB  
7955  C CG  . ASN C 318 ? 1.6220 1.8175 1.7775 0.2066  -0.1134 -0.3044 382 ASN C CG  
7956  O OD1 . ASN C 318 ? 1.8417 2.0581 2.0021 0.2086  -0.0975 -0.2991 382 ASN C OD1 
7957  N ND2 . ASN C 318 ? 1.5845 1.7893 1.7605 0.2103  -0.1234 -0.3132 382 ASN C ND2 
7958  N N   . SER C 319 ? 0.9426 1.0497 1.0097 0.1817  -0.1147 -0.2780 383 SER C N   
7959  C CA  . SER C 319 ? 0.8806 0.9749 0.9467 0.1667  -0.1143 -0.2687 383 SER C CA  
7960  C C   . SER C 319 ? 0.9022 0.9905 0.9512 0.1630  -0.1033 -0.2592 383 SER C C   
7961  O O   . SER C 319 ? 1.1939 1.2722 1.2178 0.1725  -0.1028 -0.2606 383 SER C O   
7962  C CB  . SER C 319 ? 0.8395 0.9081 0.8902 0.1650  -0.1299 -0.2707 383 SER C CB  
7963  O OG  . SER C 319 ? 1.2441 1.3114 1.2944 0.1753  -0.1411 -0.2804 383 SER C OG  
7964  N N   . THR C 320 ? 0.9586 1.0514 1.0206 0.1498  -0.0958 -0.2498 384 THR C N   
7965  C CA  . THR C 320 ? 1.0571 1.1420 1.1023 0.1454  -0.0864 -0.2398 384 THR C CA  
7966  C C   . THR C 320 ? 0.9655 1.0200 0.9838 0.1429  -0.0962 -0.2380 384 THR C C   
7967  O O   . THR C 320 ? 1.0593 1.1033 1.0825 0.1342  -0.1037 -0.2364 384 THR C O   
7968  C CB  . THR C 320 ? 1.0784 1.1773 1.1473 0.1318  -0.0758 -0.2294 384 THR C CB  
7969  O OG1 . THR C 320 ? 1.3576 1.4875 1.4538 0.1335  -0.0660 -0.2293 384 THR C OG1 
7970  C CG2 . THR C 320 ? 0.8808 0.9707 0.9300 0.1284  -0.0664 -0.2188 384 THR C CG2 
7971  N N   . ILE C 321 ? 0.8269 0.8685 0.8171 0.1512  -0.0962 -0.2382 385 ILE C N   
7972  C CA  . ILE C 321 ? 0.7755 0.7891 0.7409 0.1507  -0.1074 -0.2375 385 ILE C CA  
7973  C C   . ILE C 321 ? 0.8471 0.8495 0.7982 0.1441  -0.1019 -0.2280 385 ILE C C   
7974  O O   . ILE C 321 ? 0.8586 0.8724 0.8116 0.1429  -0.0889 -0.2220 385 ILE C O   
7975  C CB  . ILE C 321 ? 0.8035 0.8047 0.7463 0.1646  -0.1159 -0.2451 385 ILE C CB  
7976  C CG1 . ILE C 321 ? 0.9509 0.9641 0.9062 0.1736  -0.1207 -0.2551 385 ILE C CG1 
7977  C CG2 . ILE C 321 ? 0.6950 0.6692 0.6196 0.1619  -0.1300 -0.2437 385 ILE C CG2 
7978  C CD1 . ILE C 321 ? 1.2042 1.2112 1.1704 0.1684  -0.1328 -0.2575 385 ILE C CD1 
7979  N N   . GLY C 322 ? 0.9856 0.9662 0.9226 0.1401  -0.1123 -0.2259 386 GLY C N   
7980  C CA  . GLY C 322 ? 0.9338 0.9009 0.8571 0.1337  -0.1102 -0.2175 386 GLY C CA  
7981  C C   . GLY C 322 ? 0.9240 0.8675 0.8254 0.1360  -0.1232 -0.2180 386 GLY C C   
7982  O O   . GLY C 322 ? 1.1372 1.0719 1.0223 0.1461  -0.1292 -0.2232 386 GLY C O   
7983  N N   . ARG C 323 ? 0.8312 0.7646 0.7332 0.1272  -0.1284 -0.2127 387 ARG C N   
7984  C CA  . ARG C 323 ? 0.7674 0.6806 0.6525 0.1277  -0.1408 -0.2113 387 ARG C CA  
7985  C C   . ARG C 323 ? 0.7040 0.6129 0.5899 0.1319  -0.1527 -0.2165 387 ARG C C   
7986  O O   . ARG C 323 ? 0.7799 0.7007 0.6815 0.1323  -0.1529 -0.2206 387 ARG C O   
7987  C CB  . ARG C 323 ? 0.8212 0.7290 0.7093 0.1179  -0.1425 -0.2041 387 ARG C CB  
7988  C CG  . ARG C 323 ? 0.9000 0.8111 0.7893 0.1128  -0.1317 -0.1984 387 ARG C CG  
7989  C CD  . ARG C 323 ? 0.9173 0.8268 0.8151 0.1041  -0.1336 -0.1935 387 ARG C CD  
7990  N NE  . ARG C 323 ? 1.0106 0.9073 0.8984 0.1034  -0.1445 -0.1911 387 ARG C NE  
7991  C CZ  . ARG C 323 ? 0.9308 0.8299 0.8263 0.1019  -0.1518 -0.1916 387 ARG C CZ  
7992  N NH1 . ARG C 323 ? 0.7783 0.6899 0.6896 0.1017  -0.1504 -0.1956 387 ARG C NH1 
7993  N NH2 . ARG C 323 ? 0.8632 0.7530 0.7510 0.1006  -0.1606 -0.1874 387 ARG C NH2 
7994  N N   . SER C 324 ? 0.6151 0.5059 0.4844 0.1350  -0.1638 -0.2160 388 SER C N   
7995  C CA  . SER C 324 ? 0.6518 0.5343 0.5199 0.1381  -0.1772 -0.2186 388 SER C CA  
7996  C C   . SER C 324 ? 0.7003 0.5649 0.5580 0.1333  -0.1883 -0.2117 388 SER C C   
7997  O O   . SER C 324 ? 0.8812 0.7363 0.7268 0.1328  -0.1877 -0.2089 388 SER C O   
7998  C CB  . SER C 324 ? 0.7215 0.5999 0.5799 0.1506  -0.1813 -0.2277 388 SER C CB  
7999  O OG  . SER C 324 ? 0.7262 0.6012 0.5692 0.1577  -0.1757 -0.2302 388 SER C OG  
8000  N N   . GLY C 325 ? 0.6393 0.4997 0.5019 0.1299  -0.1987 -0.2081 389 GLY C N   
8001  C CA  . GLY C 325 ? 0.6139 0.4600 0.4703 0.1243  -0.2093 -0.1998 389 GLY C CA  
8002  C C   . GLY C 325 ? 0.6400 0.4803 0.5002 0.1228  -0.2222 -0.1960 389 GLY C C   
8003  O O   . GLY C 325 ? 0.6717 0.5202 0.5395 0.1256  -0.2220 -0.1995 389 GLY C O   
8004  N N   . LEU C 326 ? 0.6331 0.4593 0.4887 0.1182  -0.2338 -0.1883 390 LEU C N   
8005  C CA  . LEU C 326 ? 0.6845 0.5032 0.5438 0.1154  -0.2474 -0.1818 390 LEU C CA  
8006  C C   . LEU C 326 ? 0.8498 0.6815 0.7211 0.1060  -0.2450 -0.1696 390 LEU C C   
8007  O O   . LEU C 326 ? 0.9900 0.8321 0.8649 0.1017  -0.2358 -0.1663 390 LEU C O   
8008  C CB  . LEU C 326 ? 0.6419 0.4367 0.4913 0.1155  -0.2640 -0.1794 390 LEU C CB  
8009  C CG  . LEU C 326 ? 0.6779 0.4557 0.5118 0.1270  -0.2707 -0.1916 390 LEU C CG  
8010  C CD1 . LEU C 326 ? 0.7671 0.5237 0.5907 0.1260  -0.2838 -0.1892 390 LEU C CD1 
8011  C CD2 . LEU C 326 ? 0.7234 0.4924 0.5568 0.1330  -0.2821 -0.1960 390 LEU C CD2 
8012  N N   . TYR C 327 ? 1.0005 0.8319 0.8771 0.1039  -0.2535 -0.1629 391 TYR C N   
8013  C CA  . TYR C 327 ? 0.9105 0.7539 0.7970 0.0960  -0.2535 -0.1492 391 TYR C CA  
8014  C C   . TYR C 327 ? 0.9649 0.8005 0.8539 0.0935  -0.2670 -0.1400 391 TYR C C   
8015  O O   . TYR C 327 ? 0.9388 0.7655 0.8238 0.0994  -0.2732 -0.1463 391 TYR C O   
8016  C CB  . TYR C 327 ? 0.8701 0.7364 0.7637 0.0973  -0.2398 -0.1510 391 TYR C CB  
8017  C CG  . TYR C 327 ? 0.8316 0.7046 0.7271 0.1034  -0.2384 -0.1574 391 TYR C CG  
8018  C CD1 . TYR C 327 ? 0.8450 0.7245 0.7441 0.1024  -0.2429 -0.1489 391 TYR C CD1 
8019  C CD2 . TYR C 327 ? 0.8536 0.7284 0.7480 0.1103  -0.2321 -0.1714 391 TYR C CD2 
8020  C CE1 . TYR C 327 ? 0.8245 0.7097 0.7245 0.1089  -0.2425 -0.1554 391 TYR C CE1 
8021  C CE2 . TYR C 327 ? 0.8519 0.7337 0.7499 0.1161  -0.2317 -0.1778 391 TYR C CE2 
8022  C CZ  . TYR C 327 ? 0.8428 0.7288 0.7429 0.1156  -0.2373 -0.1704 391 TYR C CZ  
8023  O OH  . TYR C 327 ? 0.9557 0.8479 0.8584 0.1221  -0.2376 -0.1774 391 TYR C OH  
8024  N N   . GLN C 328 ? 0.9754 0.8147 0.8718 0.0847  -0.2717 -0.1243 392 GLN C N   
8025  C CA  . GLN C 328 ? 0.9638 0.7978 0.8648 0.0804  -0.2839 -0.1118 392 GLN C CA  
8026  C C   . GLN C 328 ? 0.9829 0.8411 0.8920 0.0775  -0.2757 -0.1001 392 GLN C C   
8027  O O   . GLN C 328 ? 1.2076 1.0825 1.1235 0.0728  -0.2682 -0.0915 392 GLN C O   
8028  C CB  . GLN C 328 ? 1.1336 0.9511 1.0382 0.0720  -0.2990 -0.1006 392 GLN C CB  
8029  C CG  . GLN C 328 ? 1.1176 0.9100 1.0119 0.0761  -0.3089 -0.1121 392 GLN C CG  
8030  C CD  . GLN C 328 ? 1.0659 0.8424 0.9655 0.0674  -0.3251 -0.1010 392 GLN C CD  
8031  O OE1 . GLN C 328 ? 1.3170 1.1019 1.2233 0.0610  -0.3218 -0.0940 392 GLN C OE1 
8032  N NE2 . GLN C 328 ? 1.0025 0.7551 0.8998 0.0673  -0.3440 -0.0999 392 GLN C NE2 
8033  N N   . PRO C 329 ? 0.9923 0.8534 0.8996 0.0820  -0.2768 -0.1007 393 PRO C N   
8034  C CA  . PRO C 329 ? 1.0286 0.9107 0.9407 0.0809  -0.2711 -0.0889 393 PRO C CA  
8035  C C   . PRO C 329 ? 1.0259 0.9051 0.9454 0.0710  -0.2819 -0.0675 393 PRO C C   
8036  O O   . PRO C 329 ? 1.0915 0.9474 1.0107 0.0672  -0.2970 -0.0649 393 PRO C O   
8037  C CB  . PRO C 329 ? 0.8513 0.7317 0.7572 0.0898  -0.2718 -0.0986 393 PRO C CB  
8038  C CG  . PRO C 329 ? 0.8445 0.6997 0.7449 0.0928  -0.2830 -0.1088 393 PRO C CG  
8039  C CD  . PRO C 329 ? 0.9791 0.8258 0.8786 0.0905  -0.2819 -0.1148 393 PRO C CD  
8040  N N   . ALA C 330 ? 1.0571 0.9600 0.9837 0.0671  -0.2746 -0.0521 394 ALA C N   
8041  C CA  . ALA C 330 ? 1.0490 0.9547 0.9861 0.0565  -0.2829 -0.0286 394 ALA C CA  
8042  C C   . ALA C 330 ? 1.3630 1.2845 1.2994 0.0579  -0.2805 -0.0149 394 ALA C C   
8043  O O   . ALA C 330 ? 1.9657 1.9123 1.8991 0.0646  -0.2669 -0.0154 394 ALA C O   
8044  C CB  . ALA C 330 ? 1.1208 1.0431 1.0688 0.0498  -0.2769 -0.0187 394 ALA C CB  
8045  N N   . TYR C 331 ? 1.4124 1.3179 1.3504 0.0526  -0.2948 -0.0030 395 TYR C N   
8046  C CA  . TYR C 331 ? 1.7503 1.6695 1.6885 0.0518  -0.2943 0.0152  395 TYR C CA  
8047  C C   . TYR C 331 ? 1.9168 1.8243 1.8674 0.0379  -0.3096 0.0386  395 TYR C C   
8048  O O   . TYR C 331 ? 2.1185 2.0056 2.0768 0.0301  -0.3217 0.0380  395 TYR C O   
8049  C CB  . TYR C 331 ? 1.7911 1.6997 1.7154 0.0623  -0.2974 0.0036  395 TYR C CB  
8050  C CG  . TYR C 331 ? 1.8353 1.7410 1.7500 0.0741  -0.2900 -0.0238 395 TYR C CG  
8051  C CD1 . TYR C 331 ? 1.7470 1.6775 1.6577 0.0826  -0.2738 -0.0323 395 TYR C CD1 
8052  C CD2 . TYR C 331 ? 1.6034 1.4822 1.5136 0.0773  -0.2997 -0.0410 395 TYR C CD2 
8053  C CE1 . TYR C 331 ? 1.5267 1.4548 1.4317 0.0920  -0.2679 -0.0560 395 TYR C CE1 
8054  C CE2 . TYR C 331 ? 1.6392 1.5182 1.5430 0.0875  -0.2921 -0.0643 395 TYR C CE2 
8055  C CZ  . TYR C 331 ? 1.7911 1.6947 1.6937 0.0938  -0.2764 -0.0709 395 TYR C CZ  
8056  O OH  . TYR C 331 ? 1.7866 1.6905 1.6858 0.1023  -0.2697 -0.0923 395 TYR C OH  
8057  N N   . GLU C 332 ? 1.9164 1.8365 1.8690 0.0349  -0.3098 0.0597  396 GLU C N   
8058  C CA  . GLU C 332 ? 2.5264 2.4320 2.4908 0.0214  -0.3265 0.0830  396 GLU C CA  
8059  C C   . GLU C 332 ? 3.1041 2.9681 3.0611 0.0230  -0.3466 0.0697  396 GLU C C   
8060  O O   . GLU C 332 ? 3.7044 3.5440 3.6711 0.0134  -0.3637 0.0739  396 GLU C O   
8061  C CB  . GLU C 332 ? 2.3736 2.3008 2.3383 0.0198  -0.3217 0.1076  396 GLU C CB  
8062  C CG  . GLU C 332 ? 2.4905 2.4079 2.4713 0.0034  -0.3376 0.1372  396 GLU C CG  
8063  C CD  . GLU C 332 ? 2.7002 2.5778 2.6743 0.0026  -0.3593 0.1340  396 GLU C CD  
8064  O OE1 . GLU C 332 ? 2.2842 2.1569 2.2406 0.0144  -0.3578 0.1239  396 GLU C OE1 
8065  O OE2 . GLU C 332 ? 3.3265 3.1771 3.3130 -0.0091 -0.3790 0.1409  396 GLU C OE2 
8066  N N   . SER C 333 ? 2.7806 2.6373 2.7209 0.0361  -0.3449 0.0526  397 SER C N   
8067  C CA  . SER C 333 ? 2.3173 2.1379 2.2486 0.0410  -0.3624 0.0379  397 SER C CA  
8068  C C   . SER C 333 ? 2.5631 2.3566 2.5044 0.0284  -0.3855 0.0561  397 SER C C   
8069  O O   . SER C 333 ? 2.9033 2.6996 2.8485 0.0220  -0.3909 0.0787  397 SER C O   
8070  C CB  . SER C 333 ? 2.1122 1.9196 2.0373 0.0491  -0.3611 0.0097  397 SER C CB  
8071  O OG  . SER C 333 ? 2.0707 1.9002 1.9877 0.0602  -0.3419 -0.0068 397 SER C OG  
8072  N N   . ARG C 334 ? 2.3905 2.1577 2.3357 0.0250  -0.3998 0.0467  398 ARG C N   
8073  C CA  . ARG C 334 ? 2.2207 1.9609 2.1783 0.0119  -0.4238 0.0633  398 ARG C CA  
8074  C C   . ARG C 334 ? 2.0101 1.7344 1.9745 0.0076  -0.4327 0.0543  398 ARG C C   
8075  O O   . ARG C 334 ? 2.2988 2.0382 2.2600 0.0128  -0.4177 0.0399  398 ARG C O   
8076  C CB  . ARG C 334 ? 2.5094 2.2153 2.4572 0.0168  -0.4446 0.0592  398 ARG C CB  
8077  C CG  . ARG C 334 ? 2.3643 2.0529 2.2932 0.0347  -0.4458 0.0268  398 ARG C CG  
8078  C CD  . ARG C 334 ? 2.5539 2.2055 2.4756 0.0388  -0.4704 0.0243  398 ARG C CD  
8079  N NE  . ARG C 334 ? 2.6002 2.2551 2.5254 0.0320  -0.4750 0.0488  398 ARG C NE  
8080  C CZ  . ARG C 334 ? 2.7746 2.3999 2.6943 0.0340  -0.4960 0.0520  398 ARG C CZ  
8081  N NH1 . ARG C 334 ? 2.8594 2.4497 2.7701 0.0438  -0.5149 0.0309  398 ARG C NH1 
8082  N NH2 . ARG C 334 ? 2.8358 2.4668 2.7583 0.0273  -0.4982 0.0764  398 ARG C NH2 
8083  N N   . ASP C 335 ? 2.3868 2.0793 2.3600 -0.0017 -0.4584 0.0630  399 ASP C N   
8084  C CA  . ASP C 335 ? 3.0265 2.6988 3.0054 -0.0054 -0.4717 0.0548  399 ASP C CA  
8085  C C   . ASP C 335 ? 2.9683 2.6358 2.9286 0.0107  -0.4629 0.0227  399 ASP C C   
8086  O O   . ASP C 335 ? 3.0277 2.6908 2.9897 0.0099  -0.4642 0.0143  399 ASP C O   
8087  C CB  . ASP C 335 ? 3.2304 2.8595 3.2139 -0.0113 -0.5049 0.0600  399 ASP C CB  
8088  C CG  . ASP C 335 ? 3.1779 2.8097 3.1844 -0.0307 -0.5162 0.0949  399 ASP C CG  
8089  O OD1 . ASP C 335 ? 3.1850 2.8542 3.2062 -0.0404 -0.4985 0.1156  399 ASP C OD1 
8090  O OD2 . ASP C 335 ? 2.9707 2.5676 2.9811 -0.0359 -0.5435 0.1020  399 ASP C OD2 
8091  N N   . CYS C 336 ? 2.3535 2.0230 2.2967 0.0250  -0.4538 0.0063  400 CYS C N   
8092  C CA  . CYS C 336 ? 1.8841 1.5521 1.8103 0.0410  -0.4440 -0.0227 400 CYS C CA  
8093  C C   . CYS C 336 ? 1.4452 1.1482 1.3713 0.0435  -0.4165 -0.0287 400 CYS C C   
8094  O O   . CYS C 336 ? 1.1565 0.8886 1.0856 0.0426  -0.3993 -0.0204 400 CYS C O   
8095  C CB  . CYS C 336 ? 2.0683 1.7282 1.9805 0.0541  -0.4453 -0.0353 400 CYS C CB  
8096  S SG  . CYS C 336 ? 3.0753 2.7107 2.9687 0.0726  -0.4521 -0.0678 400 CYS C SG  
8097  N N   . GLN C 337 ? 1.3029 1.0018 1.2243 0.0474  -0.4134 -0.0436 401 GLN C N   
8098  C CA  . GLN C 337 ? 1.1789 0.9055 1.0977 0.0518  -0.3894 -0.0527 401 GLN C CA  
8099  C C   . GLN C 337 ? 1.2565 0.9835 1.1592 0.0677  -0.3792 -0.0770 401 GLN C C   
8100  O O   . GLN C 337 ? 1.3104 1.0168 1.2020 0.0765  -0.3867 -0.0941 401 GLN C O   
8101  C CB  . GLN C 337 ? 1.0688 0.7937 0.9919 0.0466  -0.3898 -0.0534 401 GLN C CB  
8102  C CG  . GLN C 337 ? 0.9767 0.7282 0.8977 0.0503  -0.3665 -0.0615 401 GLN C CG  
8103  C CD  . GLN C 337 ? 1.3025 1.0866 1.2290 0.0495  -0.3480 -0.0527 401 GLN C CD  
8104  O OE1 . GLN C 337 ? 1.4274 1.2254 1.3667 0.0399  -0.3486 -0.0319 401 GLN C OE1 
8105  N NE2 . GLN C 337 ? 1.3331 1.1302 1.2501 0.0600  -0.3320 -0.0683 401 GLN C NE2 
8106  N N   . GLU C 338 ? 1.1518 0.9034 1.0539 0.0718  -0.3622 -0.0782 402 GLU C N   
8107  C CA  . GLU C 338 ? 1.1554 0.9125 1.0469 0.0854  -0.3512 -0.0992 402 GLU C CA  
8108  C C   . GLU C 338 ? 1.1058 0.8698 0.9931 0.0896  -0.3385 -0.1133 402 GLU C C   
8109  O O   . GLU C 338 ? 1.1982 0.9740 1.0917 0.0823  -0.3310 -0.1059 402 GLU C O   
8110  C CB  . GLU C 338 ? 1.4681 1.2505 1.3620 0.0876  -0.3374 -0.0955 402 GLU C CB  
8111  C CG  . GLU C 338 ? 2.0395 1.8271 1.9259 0.1008  -0.3293 -0.1153 402 GLU C CG  
8112  C CD  . GLU C 338 ? 2.1236 1.8983 2.0053 0.1072  -0.3414 -0.1174 402 GLU C CD  
8113  O OE1 . GLU C 338 ? 2.2539 2.0280 2.1386 0.1015  -0.3484 -0.1008 402 GLU C OE1 
8114  O OE2 . GLU C 338 ? 2.3293 2.0957 2.2045 0.1184  -0.3434 -0.1352 402 GLU C OE2 
8115  N N   . LEU C 339 ? 0.9471 0.7044 0.8242 0.1016  -0.3362 -0.1328 403 LEU C N   
8116  C CA  . LEU C 339 ? 0.8824 0.6456 0.7542 0.1065  -0.3240 -0.1461 403 LEU C CA  
8117  C C   . LEU C 339 ? 0.9053 0.6832 0.7743 0.1171  -0.3102 -0.1615 403 LEU C C   
8118  O O   . LEU C 339 ? 0.9657 0.7353 0.8298 0.1263  -0.3163 -0.1713 403 LEU C O   
8119  C CB  . LEU C 339 ? 0.8767 0.6140 0.7383 0.1104  -0.3375 -0.1536 403 LEU C CB  
8120  C CG  . LEU C 339 ? 0.9687 0.7091 0.8219 0.1161  -0.3267 -0.1658 403 LEU C CG  
8121  C CD1 . LEU C 339 ? 1.0780 0.8349 0.9390 0.1062  -0.3149 -0.1561 403 LEU C CD1 
8122  C CD2 . LEU C 339 ? 0.9117 0.6239 0.7517 0.1222  -0.3430 -0.1735 403 LEU C CD2 
8123  N N   . CYS C 340 ? 0.8665 0.6660 0.7399 0.1157  -0.2924 -0.1635 404 CYS C N   
8124  C CA  . CYS C 340 ? 0.8426 0.6578 0.7172 0.1237  -0.2793 -0.1765 404 CYS C CA  
8125  C C   . CYS C 340 ? 0.8575 0.6796 0.7301 0.1247  -0.2666 -0.1838 404 CYS C C   
8126  O O   . CYS C 340 ? 0.7619 0.5792 0.6323 0.1187  -0.2667 -0.1777 404 CYS C O   
8127  C CB  . CYS C 340 ? 0.9541 0.7905 0.8380 0.1207  -0.2705 -0.1708 404 CYS C CB  
8128  S SG  . CYS C 340 ? 1.3628 1.1951 1.2482 0.1187  -0.2830 -0.1585 404 CYS C SG  
8129  N N   . PHE C 341 ? 0.7437 0.5772 0.6178 0.1320  -0.2560 -0.1960 405 PHE C N   
8130  C CA  . PHE C 341 ? 0.6963 0.5383 0.5698 0.1324  -0.2427 -0.2012 405 PHE C CA  
8131  C C   . PHE C 341 ? 0.7053 0.5685 0.5897 0.1345  -0.2292 -0.2077 405 PHE C C   
8132  O O   . PHE C 341 ? 0.8582 0.7278 0.7484 0.1393  -0.2310 -0.2127 405 PHE C O   
8133  C CB  . PHE C 341 ? 0.7607 0.5893 0.6215 0.1404  -0.2455 -0.2100 405 PHE C CB  
8134  C CG  . PHE C 341 ? 0.8459 0.6767 0.7054 0.1524  -0.2459 -0.2226 405 PHE C CG  
8135  C CD1 . PHE C 341 ? 0.8946 0.7094 0.7484 0.1588  -0.2617 -0.2257 405 PHE C CD1 
8136  C CD2 . PHE C 341 ? 0.8056 0.6548 0.6709 0.1572  -0.2310 -0.2309 405 PHE C CD2 
8137  C CE1 . PHE C 341 ? 0.8757 0.6935 0.7285 0.1713  -0.2625 -0.2382 405 PHE C CE1 
8138  C CE2 . PHE C 341 ? 0.8546 0.7093 0.7211 0.1685  -0.2308 -0.2420 405 PHE C CE2 
8139  C CZ  . PHE C 341 ? 0.9027 0.7419 0.7624 0.1764  -0.2466 -0.2464 405 PHE C CZ  
8140  N N   . TRP C 342 ? 0.6176 0.4908 0.5053 0.1310  -0.2170 -0.2077 406 TRP C N   
8141  C CA  . TRP C 342 ? 0.6414 0.5337 0.5418 0.1314  -0.2055 -0.2129 406 TRP C CA  
8142  C C   . TRP C 342 ? 0.7367 0.6334 0.6365 0.1349  -0.1956 -0.2195 406 TRP C C   
8143  O O   . TRP C 342 ? 0.8839 0.7693 0.7711 0.1363  -0.1964 -0.2188 406 TRP C O   
8144  C CB  . TRP C 342 ? 0.5966 0.4979 0.5038 0.1237  -0.2001 -0.2060 406 TRP C CB  
8145  C CG  . TRP C 342 ? 0.6492 0.5433 0.5493 0.1182  -0.1977 -0.1996 406 TRP C CG  
8146  C CD1 . TRP C 342 ? 0.6759 0.5609 0.5701 0.1131  -0.2048 -0.1898 406 TRP C CD1 
8147  C CD2 . TRP C 342 ? 0.6188 0.5146 0.5175 0.1170  -0.1878 -0.2016 406 TRP C CD2 
8148  N NE1 . TRP C 342 ? 0.6015 0.4821 0.4908 0.1097  -0.2007 -0.1870 406 TRP C NE1 
8149  C CE2 . TRP C 342 ? 0.5739 0.4597 0.4642 0.1119  -0.1905 -0.1936 406 TRP C CE2 
8150  C CE3 . TRP C 342 ? 0.6684 0.5735 0.5729 0.1191  -0.1774 -0.2077 406 TRP C CE3 
8151  C CZ2 . TRP C 342 ? 0.5678 0.4513 0.4534 0.1100  -0.1835 -0.1928 406 TRP C CZ2 
8152  C CZ3 . TRP C 342 ? 0.7277 0.6310 0.6276 0.1163  -0.1696 -0.2053 406 TRP C CZ3 
8153  C CH2 . TRP C 342 ? 0.6223 0.5139 0.5117 0.1124  -0.1729 -0.1984 406 TRP C CH2 
8154  N N   . ILE C 343 ? 0.7127 0.6264 0.6262 0.1362  -0.1865 -0.2251 407 ILE C N   
8155  C CA  . ILE C 343 ? 0.6359 0.5584 0.5522 0.1392  -0.1756 -0.2300 407 ILE C CA  
8156  C C   . ILE C 343 ? 0.6263 0.5652 0.5607 0.1335  -0.1668 -0.2297 407 ILE C C   
8157  O O   . ILE C 343 ? 0.6088 0.5564 0.5557 0.1339  -0.1699 -0.2329 407 ILE C O   
8158  C CB  . ILE C 343 ? 0.6567 0.5848 0.5749 0.1500  -0.1767 -0.2396 407 ILE C CB  
8159  C CG1 . ILE C 343 ? 0.7263 0.6349 0.6263 0.1575  -0.1893 -0.2417 407 ILE C CG1 
8160  C CG2 . ILE C 343 ? 0.6215 0.5640 0.5446 0.1534  -0.1631 -0.2431 407 ILE C CG2 
8161  C CD1 . ILE C 343 ? 0.7786 0.6913 0.6799 0.1693  -0.1928 -0.2519 407 ILE C CD1 
8162  N N   . GLU C 344 ? 0.6308 0.5727 0.5661 0.1287  -0.1570 -0.2259 408 GLU C N   
8163  C CA  . GLU C 344 ? 0.6246 0.5801 0.5780 0.1224  -0.1489 -0.2250 408 GLU C CA  
8164  C C   . GLU C 344 ? 0.6213 0.5940 0.5899 0.1248  -0.1397 -0.2295 408 GLU C C   
8165  O O   . GLU C 344 ? 0.8376 0.8123 0.7991 0.1296  -0.1336 -0.2300 408 GLU C O   
8166  C CB  . GLU C 344 ? 0.6680 0.6165 0.6148 0.1155  -0.1443 -0.2174 408 GLU C CB  
8167  C CG  . GLU C 344 ? 0.8073 0.7634 0.7699 0.1080  -0.1398 -0.2152 408 GLU C CG  
8168  C CD  . GLU C 344 ? 1.0097 0.9569 0.9633 0.1025  -0.1353 -0.2076 408 GLU C CD  
8169  O OE1 . GLU C 344 ? 1.1214 1.0639 1.0758 0.0980  -0.1389 -0.2045 408 GLU C OE1 
8170  O OE2 . GLU C 344 ? 0.9789 0.9237 0.9230 0.1038  -0.1286 -0.2049 408 GLU C OE2 
8171  N N   . ILE C 345 ? 0.6765 0.6625 0.6667 0.1220  -0.1391 -0.2327 409 ILE C N   
8172  C CA  . ILE C 345 ? 0.7132 0.7185 0.7230 0.1243  -0.1323 -0.2372 409 ILE C CA  
8173  C C   . ILE C 345 ? 0.6267 0.6430 0.6590 0.1150  -0.1266 -0.2340 409 ILE C C   
8174  O O   . ILE C 345 ? 0.7963 0.8093 0.8359 0.1107  -0.1332 -0.2347 409 ILE C O   
8175  C CB  . ILE C 345 ? 0.7146 0.7259 0.7332 0.1309  -0.1410 -0.2459 409 ILE C CB  
8176  C CG1 . ILE C 345 ? 0.7595 0.7599 0.7582 0.1406  -0.1475 -0.2493 409 ILE C CG1 
8177  C CG2 . ILE C 345 ? 0.6240 0.6578 0.6695 0.1315  -0.1356 -0.2506 409 ILE C CG2 
8178  C CD1 . ILE C 345 ? 0.8234 0.8301 0.8304 0.1489  -0.1559 -0.2584 409 ILE C CD1 
8179  N N   . ALA C 346 ? 0.6082 0.6378 0.6517 0.1125  -0.1150 -0.2303 410 ALA C N   
8180  C CA  . ALA C 346 ? 0.6667 0.7076 0.7361 0.1028  -0.1106 -0.2265 410 ALA C CA  
8181  C C   . ALA C 346 ? 0.6852 0.7355 0.7783 0.1025  -0.1194 -0.2344 410 ALA C C   
8182  O O   . ALA C 346 ? 0.7629 0.8235 0.8624 0.1100  -0.1219 -0.2417 410 ALA C O   
8183  C CB  . ALA C 346 ? 0.6978 0.7567 0.7786 0.1015  -0.0964 -0.2209 410 ALA C CB  
8184  N N   . ALA C 347 ? 0.7936 0.8391 0.8985 0.0952  -0.1254 -0.2338 411 ALA C N   
8185  C CA  . ALA C 347 ? 0.7742 0.8286 0.9038 0.0946  -0.1344 -0.2415 411 ALA C CA  
8186  C C   . ALA C 347 ? 0.8067 0.8701 0.9648 0.0838  -0.1312 -0.2366 411 ALA C C   
8187  O O   . ALA C 347 ? 1.0135 1.0784 1.1721 0.0772  -0.1205 -0.2266 411 ALA C O   
8188  C CB  . ALA C 347 ? 0.6222 0.6622 0.7401 0.0977  -0.1474 -0.2468 411 ALA C CB  
8189  N N   . THR C 348 ? 0.9194 0.9884 1.1012 0.0821  -0.1412 -0.2434 412 THR C N   
8190  C CA  . THR C 348 ? 1.0465 1.1169 1.2547 0.0710  -0.1439 -0.2396 412 THR C CA  
8191  C C   . THR C 348 ? 0.8937 0.9553 1.1096 0.0731  -0.1614 -0.2499 412 THR C C   
8192  O O   . THR C 348 ? 0.8187 0.8834 1.0329 0.0820  -0.1698 -0.2600 412 THR C O   
8193  C CB  . THR C 348 ? 1.0379 1.1324 1.2812 0.0636  -0.1353 -0.2341 412 THR C CB  
8194  O OG1 . THR C 348 ? 1.0304 1.1416 1.2912 0.0699  -0.1401 -0.2437 412 THR C OG1 
8195  C CG2 . THR C 348 ? 1.2390 1.3429 1.4729 0.0622  -0.1169 -0.2226 412 THR C CG2 
8196  N N   . THR C 349 ? 0.9846 1.0341 1.2065 0.0662  -0.1676 -0.2476 413 THR C N   
8197  C CA  . THR C 349 ? 0.9753 1.0165 1.2055 0.0691  -0.1850 -0.2581 413 THR C CA  
8198  C C   . THR C 349 ? 0.9798 1.0373 1.2472 0.0659  -0.1915 -0.2634 413 THR C C   
8199  O O   . THR C 349 ? 0.9775 1.0530 1.2663 0.0595  -0.1811 -0.2567 413 THR C O   
8200  C CB  . THR C 349 ? 1.0640 1.0875 1.2919 0.0629  -0.1903 -0.2542 413 THR C CB  
8201  O OG1 . THR C 349 ? 1.1717 1.1823 1.3652 0.0677  -0.1853 -0.2507 413 THR C OG1 
8202  C CG2 . THR C 349 ? 1.0672 1.0813 1.3057 0.0664  -0.2097 -0.2657 413 THR C CG2 
8203  N N   . LYS C 350 ? 1.2049 1.2572 1.4792 0.0717  -0.2088 -0.2757 414 LYS C N   
8204  C CA  . LYS C 350 ? 1.1868 1.2515 1.4977 0.0690  -0.2192 -0.2825 414 LYS C CA  
8205  C C   . LYS C 350 ? 1.1553 1.2280 1.5023 0.0530  -0.2155 -0.2722 414 LYS C C   
8206  O O   . LYS C 350 ? 1.4519 1.5428 1.8336 0.0481  -0.2175 -0.2729 414 LYS C O   
8207  C CB  . LYS C 350 ? 1.4194 1.4707 1.7282 0.0774  -0.2406 -0.2968 414 LYS C CB  
8208  C CG  . LYS C 350 ? 1.3662 1.4275 1.7098 0.0772  -0.2556 -0.3067 414 LYS C CG  
8209  C CD  . LYS C 350 ? 1.5766 1.6199 1.9155 0.0852  -0.2780 -0.3202 414 LYS C CD  
8210  C CE  . LYS C 350 ? 1.8120 1.8627 2.1878 0.0844  -0.2957 -0.3306 414 LYS C CE  
8211  N NZ  . LYS C 350 ? 1.9641 1.9970 2.3320 0.0954  -0.3193 -0.3462 414 LYS C NZ  
8212  N N   . ALA C 351 ? 1.0411 1.1011 1.3808 0.0446  -0.2101 -0.2617 415 ALA C N   
8213  C CA  . ALA C 351 ? 0.9601 1.0272 1.3311 0.0286  -0.2044 -0.2485 415 ALA C CA  
8214  C C   . ALA C 351 ? 1.0249 1.0875 1.3763 0.0227  -0.1869 -0.2332 415 ALA C C   
8215  O O   . ALA C 351 ? 1.4253 1.4675 1.7657 0.0188  -0.1911 -0.2293 415 ALA C O   
8216  C CB  . ALA C 351 ? 0.8315 0.8828 1.2241 0.0221  -0.2240 -0.2525 415 ALA C CB  
8217  N N   . GLY C 352 ? 1.0592 1.1401 1.4053 0.0233  -0.1683 -0.2253 416 GLY C N   
8218  C CA  . GLY C 352 ? 1.1793 1.2575 1.5053 0.0192  -0.1511 -0.2109 416 GLY C CA  
8219  C C   . GLY C 352 ? 1.1431 1.2005 1.4253 0.0290  -0.1514 -0.2150 416 GLY C C   
8220  O O   . GLY C 352 ? 1.0496 1.0996 1.3173 0.0395  -0.1619 -0.2277 416 GLY C O   
8221  N N   . LEU C 353 ? 1.1952 1.2440 1.4572 0.0257  -0.1403 -0.2037 417 LEU C N   
8222  C CA  . LEU C 353 ? 1.0180 1.0466 1.2414 0.0331  -0.1412 -0.2057 417 LEU C CA  
8223  C C   . LEU C 353 ? 0.9928 1.0277 1.1906 0.0440  -0.1328 -0.2089 417 LEU C C   
8224  O O   . LEU C 353 ? 1.0303 1.0796 1.2367 0.0498  -0.1336 -0.2162 417 LEU C O   
8225  C CB  . LEU C 353 ? 0.9225 0.9335 1.1403 0.0379  -0.1593 -0.2171 417 LEU C CB  
8226  C CG  . LEU C 353 ? 1.0269 1.0323 1.2751 0.0298  -0.1731 -0.2190 417 LEU C CG  
8227  C CD1 . LEU C 353 ? 1.0435 1.0361 1.2868 0.0387  -0.1920 -0.2339 417 LEU C CD1 
8228  C CD2 . LEU C 353 ? 0.9627 0.9556 1.2165 0.0181  -0.1712 -0.2065 417 LEU C CD2 
8229  N N   . SER C 354 ? 0.9324 0.9557 1.0999 0.0468  -0.1261 -0.2036 418 SER C N   
8230  C CA  . SER C 354 ? 1.0932 1.1208 1.2377 0.0558  -0.1182 -0.2047 418 SER C CA  
8231  C C   . SER C 354 ? 1.3727 1.3837 1.4881 0.0638  -0.1257 -0.2103 418 SER C C   
8232  O O   . SER C 354 ? 2.0213 2.0223 2.1122 0.0656  -0.1207 -0.2052 418 SER C O   
8233  C CB  . SER C 354 ? 1.2565 1.2879 1.3915 0.0527  -0.1028 -0.1926 418 SER C CB  
8234  O OG  . SER C 354 ? 1.7526 1.7663 1.8744 0.0472  -0.1027 -0.1846 418 SER C OG  
8235  N N   . SER C 355 ? 1.1932 1.2020 1.3113 0.0688  -0.1378 -0.2203 419 SER C N   
8236  C CA  . SER C 355 ? 1.2604 1.2584 1.3527 0.0769  -0.1434 -0.2242 419 SER C CA  
8237  C C   . SER C 355 ? 1.1690 1.1727 1.2480 0.0838  -0.1383 -0.2253 419 SER C C   
8238  O O   . SER C 355 ? 1.0915 1.1092 1.1832 0.0846  -0.1327 -0.2264 419 SER C O   
8239  C CB  . SER C 355 ? 1.2941 1.2902 1.3911 0.0819  -0.1568 -0.2339 419 SER C CB  
8240  O OG  . SER C 355 ? 1.2161 1.2028 1.2887 0.0885  -0.1613 -0.2348 419 SER C OG  
8241  N N   . ASN C 356 ? 1.1470 1.1397 1.2011 0.0888  -0.1407 -0.2245 420 ASN C N   
8242  C CA  . ASN C 356 ? 1.0366 1.0304 1.0768 0.0958  -0.1394 -0.2262 420 ASN C CA  
8243  C C   . ASN C 356 ? 0.9324 0.9237 0.9661 0.1024  -0.1500 -0.2321 420 ASN C C   
8244  O O   . ASN C 356 ? 1.2142 1.1999 1.2446 0.1022  -0.1564 -0.2325 420 ASN C O   
8245  C CB  . ASN C 356 ? 1.1313 1.1131 1.1477 0.0960  -0.1349 -0.2191 420 ASN C CB  
8246  C CG  . ASN C 356 ? 1.1376 1.1183 1.1555 0.0894  -0.1255 -0.2115 420 ASN C CG  
8247  O OD1 . ASN C 356 ? 1.3051 1.2803 1.3278 0.0833  -0.1266 -0.2080 420 ASN C OD1 
8248  N ND2 . ASN C 356 ? 1.0012 0.9866 1.0137 0.0915  -0.1165 -0.2088 420 ASN C ND2 
8249  N N   . ASP C 357 ? 0.8299 0.8253 0.8607 0.1090  -0.1520 -0.2365 421 ASP C N   
8250  C CA  . ASP C 357 ? 0.9986 0.9893 1.0188 0.1151  -0.1617 -0.2395 421 ASP C CA  
8251  C C   . ASP C 357 ? 0.9621 0.9440 0.9630 0.1196  -0.1631 -0.2370 421 ASP C C   
8252  O O   . ASP C 357 ? 0.9753 0.9553 0.9705 0.1199  -0.1571 -0.2351 421 ASP C O   
8253  C CB  . ASP C 357 ? 1.1157 1.1168 1.1514 0.1198  -0.1681 -0.2483 421 ASP C CB  
8254  C CG  . ASP C 357 ? 1.6244 1.6221 1.6545 0.1233  -0.1779 -0.2503 421 ASP C CG  
8255  O OD1 . ASP C 357 ? 2.0546 2.0436 2.0658 0.1251  -0.1807 -0.2449 421 ASP C OD1 
8256  O OD2 . ASP C 357 ? 1.7882 1.7927 1.8331 0.1246  -0.1831 -0.2569 421 ASP C OD2 
8257  N N   . LEU C 358 ? 0.9092 0.8856 0.9001 0.1237  -0.1719 -0.2368 422 LEU C N   
8258  C CA  . LEU C 358 ? 0.8913 0.8565 0.8647 0.1267  -0.1763 -0.2331 422 LEU C CA  
8259  C C   . LEU C 358 ? 0.8238 0.7898 0.7972 0.1343  -0.1833 -0.2387 422 LEU C C   
8260  O O   . LEU C 358 ? 0.7602 0.7340 0.7430 0.1374  -0.1876 -0.2438 422 LEU C O   
8261  C CB  . LEU C 358 ? 0.7689 0.7265 0.7306 0.1244  -0.1814 -0.2254 422 LEU C CB  
8262  C CG  . LEU C 358 ? 0.8048 0.7559 0.7594 0.1184  -0.1768 -0.2182 422 LEU C CG  
8263  C CD1 . LEU C 358 ? 1.0563 1.0009 0.9992 0.1175  -0.1831 -0.2099 422 LEU C CD1 
8264  C CD2 . LEU C 358 ? 0.9918 0.9358 0.9395 0.1184  -0.1727 -0.2180 422 LEU C CD2 
8265  N N   . ILE C 359 ? 0.7916 0.7483 0.7535 0.1379  -0.1857 -0.2383 423 ILE C N   
8266  C CA  . ILE C 359 ? 0.7081 0.6591 0.6644 0.1449  -0.1957 -0.2413 423 ILE C CA  
8267  C C   . ILE C 359 ? 0.6628 0.5955 0.6009 0.1438  -0.2024 -0.2337 423 ILE C C   
8268  O O   . ILE C 359 ? 0.7908 0.7167 0.7213 0.1412  -0.1986 -0.2306 423 ILE C O   
8269  C CB  . ILE C 359 ? 0.6504 0.6093 0.6149 0.1530  -0.1945 -0.2514 423 ILE C CB  
8270  C CG1 . ILE C 359 ? 0.6755 0.6229 0.6297 0.1610  -0.2066 -0.2540 423 ILE C CG1 
8271  C CG2 . ILE C 359 ? 0.6684 0.6289 0.6309 0.1535  -0.1854 -0.2524 423 ILE C CG2 
8272  C CD1 . ILE C 359 ? 0.7007 0.6593 0.6672 0.1695  -0.2091 -0.2643 423 ILE C CD1 
8273  N N   . THR C 360 ? 0.6300 0.5547 0.5616 0.1455  -0.2132 -0.2298 424 THR C N   
8274  C CA  . THR C 360 ? 0.6697 0.5769 0.5873 0.1431  -0.2216 -0.2212 424 THR C CA  
8275  C C   . THR C 360 ? 0.7104 0.6062 0.6222 0.1502  -0.2339 -0.2243 424 THR C C   
8276  O O   . THR C 360 ? 0.8871 0.7896 0.8049 0.1557  -0.2369 -0.2298 424 THR C O   
8277  C CB  . THR C 360 ? 0.6888 0.5972 0.6048 0.1365  -0.2236 -0.2097 424 THR C CB  
8278  O OG1 . THR C 360 ? 1.0549 0.9643 0.9709 0.1399  -0.2316 -0.2079 424 THR C OG1 
8279  C CG2 . THR C 360 ? 0.6073 0.5303 0.5318 0.1329  -0.2132 -0.2103 424 THR C CG2 
8280  N N   . PHE C 361 ? 0.6844 0.5616 0.5845 0.1505  -0.2424 -0.2211 425 PHE C N   
8281  C CA  . PHE C 361 ? 0.7359 0.5972 0.6286 0.1575  -0.2567 -0.2238 425 PHE C CA  
8282  C C   . PHE C 361 ? 0.8676 0.7102 0.7518 0.1511  -0.2691 -0.2110 425 PHE C C   
8283  O O   . PHE C 361 ? 0.9969 0.8340 0.8775 0.1442  -0.2677 -0.2041 425 PHE C O   
8284  C CB  . PHE C 361 ? 0.7198 0.5741 0.6063 0.1668  -0.2574 -0.2352 425 PHE C CB  
8285  C CG  . PHE C 361 ? 0.7650 0.6389 0.6618 0.1740  -0.2462 -0.2471 425 PHE C CG  
8286  C CD1 . PHE C 361 ? 0.7504 0.6394 0.6534 0.1711  -0.2307 -0.2490 425 PHE C CD1 
8287  C CD2 . PHE C 361 ? 0.8217 0.6995 0.7235 0.1834  -0.2517 -0.2559 425 PHE C CD2 
8288  C CE1 . PHE C 361 ? 0.7664 0.6753 0.6823 0.1764  -0.2204 -0.2581 425 PHE C CE1 
8289  C CE2 . PHE C 361 ? 0.8415 0.7400 0.7563 0.1896  -0.2416 -0.2664 425 PHE C CE2 
8290  C CZ  . PHE C 361 ? 0.8468 0.7616 0.7696 0.1856  -0.2257 -0.2670 425 PHE C CZ  
8291  N N   . CYS C 362 ? 0.9142 0.7465 0.7961 0.1531  -0.2822 -0.2072 426 CYS C N   
8292  C CA  . CYS C 362 ? 0.9510 0.7641 0.8268 0.1465  -0.2959 -0.1940 426 CYS C CA  
8293  C C   . CYS C 362 ? 1.0331 0.8228 0.9004 0.1543  -0.3125 -0.2001 426 CYS C C   
8294  O O   . CYS C 362 ? 1.1399 0.9310 1.0069 0.1650  -0.3143 -0.2120 426 CYS C O   
8295  C CB  . CYS C 362 ? 0.9528 0.7730 0.8328 0.1391  -0.2974 -0.1788 426 CYS C CB  
8296  S SG  . CYS C 362 ? 1.7711 1.6159 1.6586 0.1307  -0.2793 -0.1722 426 CYS C SG  
8297  N N   . GLY C 363 ? 1.1974 0.9655 1.0584 0.1497  -0.3253 -0.1928 427 GLY C N   
8298  C CA  . GLY C 363 ? 1.0126 0.7536 0.8643 0.1571  -0.3445 -0.1984 427 GLY C CA  
8299  C C   . GLY C 363 ? 1.1175 0.8465 0.9702 0.1559  -0.3597 -0.1896 427 GLY C C   
8300  O O   . GLY C 363 ? 1.3609 1.0929 1.2193 0.1445  -0.3612 -0.1721 427 GLY C O   
8301  N N   . THR C 364 ? 1.2696 0.9863 1.1166 0.1683  -0.3705 -0.2014 428 THR C N   
8302  C CA  . THR C 364 ? 1.3117 1.0083 1.1566 0.1683  -0.3900 -0.1936 428 THR C CA  
8303  C C   . THR C 364 ? 1.3504 1.0121 1.1852 0.1740  -0.4132 -0.1984 428 THR C C   
8304  O O   . THR C 364 ? 1.3859 1.0415 1.2128 0.1838  -0.4131 -0.2136 428 THR C O   
8305  C CB  . THR C 364 ? 1.3526 1.0600 1.1993 0.1781  -0.3880 -0.2016 428 THR C CB  
8306  O OG1 . THR C 364 ? 1.7934 1.4807 1.6375 0.1763  -0.4069 -0.1909 428 THR C OG1 
8307  C CG2 . THR C 364 ? 1.4121 1.1196 1.2543 0.1953  -0.3875 -0.2243 428 THR C CG2 
8308  N N   . GLY C 365 ? 1.3488 0.9875 1.1836 0.1679  -0.4333 -0.1849 429 GLY C N   
8309  C CA  . GLY C 365 ? 1.4275 1.0291 1.2542 0.1716  -0.4593 -0.1873 429 GLY C CA  
8310  C C   . GLY C 365 ? 1.6085 1.1980 1.4248 0.1917  -0.4689 -0.2083 429 GLY C C   
8311  O O   . GLY C 365 ? 1.3654 0.9308 1.1709 0.2023  -0.4842 -0.2209 429 GLY C O   
8312  N N   . GLY C 366 ? 1.4405 1.0480 1.2602 0.1979  -0.4601 -0.2127 430 GLY C N   
8313  C CA  . GLY C 366 ? 1.3635 0.9658 1.1764 0.2174  -0.4670 -0.2324 430 GLY C CA  
8314  C C   . GLY C 366 ? 1.4588 1.0785 1.2680 0.2319  -0.4522 -0.2539 430 GLY C C   
8315  O O   . GLY C 366 ? 1.3921 1.0369 1.2066 0.2264  -0.4305 -0.2537 430 GLY C O   
8316  N N   . SER C 367 ? 1.4144 1.0211 1.2143 0.2510  -0.4640 -0.2722 431 SER C N   
8317  C CA  . SER C 367 ? 1.2905 0.9187 1.0882 0.2663  -0.4484 -0.2920 431 SER C CA  
8318  C C   . SER C 367 ? 1.2016 0.8649 1.0134 0.2674  -0.4291 -0.2949 431 SER C C   
8319  O O   . SER C 367 ? 1.1778 0.8413 0.9958 0.2630  -0.4339 -0.2872 431 SER C O   
8320  C CB  . SER C 367 ? 1.3015 0.9083 1.0851 0.2884  -0.4664 -0.3111 431 SER C CB  
8321  O OG  . SER C 367 ? 1.2682 0.9006 1.0504 0.3035  -0.4490 -0.3286 431 SER C OG  
8322  N N   . MET C 368 ? 1.1370 0.8296 0.9540 0.2731  -0.4077 -0.3055 432 MET C N   
8323  C CA  . MET C 368 ? 1.0614 0.7878 0.8944 0.2730  -0.3897 -0.3083 432 MET C CA  
8324  C C   . MET C 368 ? 1.0854 0.8320 0.9214 0.2916  -0.3809 -0.3280 432 MET C C   
8325  O O   . MET C 368 ? 1.1855 0.9275 1.0106 0.3024  -0.3808 -0.3378 432 MET C O   
8326  C CB  . MET C 368 ? 1.1584 0.9072 1.0012 0.2566  -0.3686 -0.2971 432 MET C CB  
8327  C CG  . MET C 368 ? 1.3436 1.0845 1.1888 0.2390  -0.3725 -0.2775 432 MET C CG  
8328  S SD  . MET C 368 ? 1.4617 1.2247 1.3210 0.2363  -0.3659 -0.2741 432 MET C SD  
8329  C CE  . MET C 368 ? 1.4400 1.2413 1.3146 0.2409  -0.3412 -0.2873 432 MET C CE  
8330  N N   . PRO C 369 ? 1.0543 0.8249 0.9053 0.2959  -0.3732 -0.3336 433 PRO C N   
8331  C CA  . PRO C 369 ? 1.1761 0.9707 1.0345 0.3130  -0.3641 -0.3510 433 PRO C CA  
8332  C C   . PRO C 369 ? 1.1771 1.0029 1.0455 0.3082  -0.3386 -0.3513 433 PRO C C   
8333  O O   . PRO C 369 ? 1.1103 0.9396 0.9816 0.2914  -0.3285 -0.3386 433 PRO C O   
8334  C CB  . PRO C 369 ? 1.1015 0.9100 0.9752 0.3151  -0.3659 -0.3534 433 PRO C CB  
8335  C CG  . PRO C 369 ? 1.0158 0.8247 0.8948 0.2954  -0.3616 -0.3365 433 PRO C CG  
8336  C CD  . PRO C 369 ? 1.0241 0.8023 0.8864 0.2853  -0.3724 -0.3236 433 PRO C CD  
8337  N N   . ASP C 370 ? 1.3676 1.2159 1.2413 0.3234  -0.3287 -0.3651 434 ASP C N   
8338  C CA  . ASP C 370 ? 1.1980 1.0781 1.0829 0.3200  -0.3043 -0.3650 434 ASP C CA  
8339  C C   . ASP C 370 ? 1.2703 1.1779 1.1809 0.3081  -0.2914 -0.3598 434 ASP C C   
8340  O O   . ASP C 370 ? 1.3865 1.3062 1.3114 0.3145  -0.2953 -0.3665 434 ASP C O   
8341  C CB  . ASP C 370 ? 1.6362 1.5356 1.5210 0.3410  -0.2977 -0.3805 434 ASP C CB  
8342  C CG  . ASP C 370 ? 2.0145 1.8873 1.8716 0.3554  -0.3104 -0.3878 434 ASP C CG  
8343  O OD1 . ASP C 370 ? 2.3440 2.1902 2.1847 0.3458  -0.3174 -0.3790 434 ASP C OD1 
8344  O OD2 . ASP C 370 ? 1.7860 1.6649 1.6380 0.3771  -0.3141 -0.4028 434 ASP C OD2 
8345  N N   . VAL C 371 ? 1.2042 1.1197 1.1202 0.2912  -0.2778 -0.3481 435 VAL C N   
8346  C CA  . VAL C 371 ? 1.0523 0.9917 0.9917 0.2795  -0.2663 -0.3432 435 VAL C CA  
8347  C C   . VAL C 371 ? 1.0527 1.0136 1.0019 0.2694  -0.2451 -0.3374 435 VAL C C   
8348  O O   . VAL C 371 ? 0.8765 0.8256 0.8116 0.2629  -0.2412 -0.3303 435 VAL C O   
8349  C CB  . VAL C 371 ? 0.9069 0.8297 0.8442 0.2665  -0.2762 -0.3323 435 VAL C CB  
8350  C CG1 . VAL C 371 ? 0.9484 0.8953 0.9087 0.2594  -0.2676 -0.3313 435 VAL C CG1 
8351  C CG2 . VAL C 371 ? 0.9641 0.8622 0.8894 0.2749  -0.2980 -0.3349 435 VAL C CG2 
8352  N N   . ASN C 372 ? 1.0049 0.9971 0.9795 0.2683  -0.2326 -0.3406 436 ASN C N   
8353  C CA  . ASN C 372 ? 0.9915 1.0040 0.9798 0.2567  -0.2143 -0.3337 436 ASN C CA  
8354  C C   . ASN C 372 ? 0.9023 0.9163 0.9040 0.2420  -0.2151 -0.3265 436 ASN C C   
8355  O O   . ASN C 372 ? 0.9546 0.9825 0.9754 0.2433  -0.2179 -0.3314 436 ASN C O   
8356  C CB  . ASN C 372 ? 1.0256 1.0728 1.0355 0.2649  -0.2003 -0.3409 436 ASN C CB  
8357  C CG  . ASN C 372 ? 1.3571 1.4275 1.3868 0.2514  -0.1819 -0.3326 436 ASN C CG  
8358  O OD1 . ASN C 372 ? 1.4762 1.5369 1.5045 0.2365  -0.1803 -0.3230 436 ASN C OD1 
8359  N ND2 . ASN C 372 ? 1.6429 1.7447 1.6918 0.2568  -0.1682 -0.3358 436 ASN C ND2 
8360  N N   . TRP C 373 ? 0.8986 0.8987 0.8902 0.2290  -0.2133 -0.3156 437 TRP C N   
8361  C CA  . TRP C 373 ? 0.8911 0.8925 0.8926 0.2165  -0.2141 -0.3090 437 TRP C CA  
8362  C C   . TRP C 373 ? 0.7439 0.7688 0.7688 0.2075  -0.2003 -0.3070 437 TRP C C   
8363  O O   . TRP C 373 ? 0.8195 0.8592 0.8517 0.2071  -0.1871 -0.3067 437 TRP C O   
8364  C CB  . TRP C 373 ? 0.7535 0.7307 0.7348 0.2075  -0.2197 -0.2980 437 TRP C CB  
8365  C CG  . TRP C 373 ? 0.7842 0.7366 0.7455 0.2143  -0.2358 -0.2981 437 TRP C CG  
8366  C CD1 . TRP C 373 ? 0.8931 0.8277 0.8358 0.2205  -0.2413 -0.2990 437 TRP C CD1 
8367  C CD2 . TRP C 373 ? 0.7516 0.6932 0.7096 0.2166  -0.2503 -0.2975 437 TRP C CD2 
8368  N NE1 . TRP C 373 ? 0.8148 0.7274 0.7448 0.2252  -0.2588 -0.2985 437 TRP C NE1 
8369  C CE2 . TRP C 373 ? 0.8188 0.7348 0.7568 0.2229  -0.2642 -0.2967 437 TRP C CE2 
8370  C CE3 . TRP C 373 ? 0.7386 0.6877 0.7067 0.2150  -0.2540 -0.2975 437 TRP C CE3 
8371  C CZ2 . TRP C 373 ? 0.9135 0.8130 0.8436 0.2256  -0.2803 -0.2943 437 TRP C CZ2 
8372  C CZ3 . TRP C 373 ? 0.8399 0.7733 0.7979 0.2190  -0.2693 -0.2955 437 TRP C CZ3 
8373  C CH2 . TRP C 373 ? 0.9054 0.8146 0.8453 0.2235  -0.2818 -0.2930 437 TRP C CH2 
8374  N N   . ALA D 11  ? 1.2457 1.1735 1.7352 -0.0383 -0.0772 0.1011  75  ALA D N   
8375  C CA  . ALA D 11  ? 1.2480 1.1978 1.6965 -0.0254 -0.0601 0.1035  75  ALA D CA  
8376  C C   . ALA D 11  ? 1.2727 1.2415 1.7310 -0.0255 -0.0347 0.1302  75  ALA D C   
8377  O O   . ALA D 11  ? 1.3854 1.3434 1.8663 -0.0318 -0.0273 0.1497  75  ALA D O   
8378  C CB  . ALA D 11  ? 1.0410 0.9745 1.4409 -0.0122 -0.0643 0.0941  75  ALA D CB  
8379  N N   . THR D 12  ? 1.1716 1.1678 1.6111 -0.0175 -0.0214 0.1311  76  THR D N   
8380  C CA  . THR D 12  ? 1.3066 1.3246 1.7532 -0.0152 0.0030  0.1547  76  THR D CA  
8381  C C   . THR D 12  ? 1.2874 1.3166 1.6837 0.0022  0.0143  0.1540  76  THR D C   
8382  O O   . THR D 12  ? 1.0594 1.0941 1.4288 0.0090  0.0055  0.1340  76  THR D O   
8383  C CB  . THR D 12  ? 1.5478 1.5935 2.0316 -0.0230 0.0080  0.1569  76  THR D CB  
8384  O OG1 . THR D 12  ? 1.5460 1.5814 2.0796 -0.0393 -0.0049 0.1557  76  THR D OG1 
8385  C CG2 . THR D 12  ? 1.7154 1.7865 2.2068 -0.0192 0.0351  0.1823  76  THR D CG2 
8386  N N   . PRO D 13  ? 1.3295 1.3613 1.7132 0.0099  0.0335  0.1758  77  PRO D N   
8387  C CA  . PRO D 13  ? 1.2674 1.3103 1.6044 0.0279  0.0438  0.1755  77  PRO D CA  
8388  C C   . PRO D 13  ? 1.4306 1.5004 1.7588 0.0329  0.0452  0.1634  77  PRO D C   
8389  O O   . PRO D 13  ? 1.6144 1.7042 1.9721 0.0269  0.0529  0.1704  77  PRO D O   
8390  C CB  . PRO D 13  ? 1.1834 1.2315 1.5222 0.0332  0.0668  0.2045  77  PRO D CB  
8391  C CG  . PRO D 13  ? 1.3324 1.3592 1.7078 0.0189  0.0649  0.2183  77  PRO D CG  
8392  C CD  . PRO D 13  ? 1.2907 1.3148 1.7037 0.0027  0.0465  0.2022  77  PRO D CD  
8393  N N   . LEU D 14  ? 1.5611 1.6312 1.8507 0.0437  0.0374  0.1451  78  LEU D N   
8394  C CA  . LEU D 14  ? 1.2552 1.3470 1.5320 0.0495  0.0372  0.1323  78  LEU D CA  
8395  C C   . LEU D 14  ? 1.2155 1.3314 1.4860 0.0599  0.0574  0.1484  78  LEU D C   
8396  O O   . LEU D 14  ? 1.3978 1.5132 1.6416 0.0728  0.0684  0.1593  78  LEU D O   
8397  C CB  . LEU D 14  ? 1.3511 1.4365 1.5881 0.0591  0.0263  0.1123  78  LEU D CB  
8398  C CG  . LEU D 14  ? 1.4138 1.5181 1.6378 0.0643  0.0242  0.0980  78  LEU D CG  
8399  C CD1 . LEU D 14  ? 1.3309 1.4333 1.5780 0.0521  0.0106  0.0838  78  LEU D CD1 
8400  C CD2 . LEU D 14  ? 1.4706 1.5721 1.6544 0.0762  0.0188  0.0838  78  LEU D CD2 
8401  N N   . VAL D 15  ? 1.2472 1.3842 1.5419 0.0554  0.0620  0.1496  79  VAL D N   
8402  C CA  . VAL D 15  ? 1.1848 1.3476 1.4764 0.0658  0.0813  0.1639  79  VAL D CA  
8403  C C   . VAL D 15  ? 1.1214 1.2997 1.3950 0.0730  0.0747  0.1449  79  VAL D C   
8404  O O   . VAL D 15  ? 1.3506 1.5292 1.6407 0.0635  0.0613  0.1295  79  VAL D O   
8405  C CB  . VAL D 15  ? 1.0988 1.2761 1.4392 0.0548  0.0947  0.1843  79  VAL D CB  
8406  C CG1 . VAL D 15  ? 1.0758 1.2847 1.4231 0.0614  0.1058  0.1867  79  VAL D CG1 
8407  C CG2 . VAL D 15  ? 0.9939 1.1644 1.3399 0.0563  0.1123  0.2116  79  VAL D CG2 
8408  N N   . LEU D 16  ? 1.0378 1.2271 1.2760 0.0905  0.0830  0.1454  80  LEU D N   
8409  C CA  . LEU D 16  ? 1.0275 1.2310 1.2483 0.0984  0.0774  0.1286  80  LEU D CA  
8410  C C   . LEU D 16  ? 0.8963 1.1277 1.1307 0.1046  0.0925  0.1396  80  LEU D C   
8411  O O   . LEU D 16  ? 0.8593 1.1009 1.1031 0.1090  0.1112  0.1622  80  LEU D O   
8412  C CB  . LEU D 16  ? 1.0238 1.2222 1.1984 0.1145  0.0738  0.1184  80  LEU D CB  
8413  C CG  . LEU D 16  ? 0.9094 1.0845 1.0691 0.1098  0.0573  0.1029  80  LEU D CG  
8414  C CD1 . LEU D 16  ? 0.9506 1.1225 1.0699 0.1264  0.0569  0.0981  80  LEU D CD1 
8415  C CD2 . LEU D 16  ? 0.9227 1.0949 1.0884 0.1008  0.0412  0.0816  80  LEU D CD2 
8416  N N   . GLY D 17  ? 0.7175 0.9608 0.9522 0.1056  0.0848  0.1242  81  GLY D N   
8417  C CA  . GLY D 17  ? 0.8034 1.0744 1.0495 0.1129  0.0972  0.1315  81  GLY D CA  
8418  C C   . GLY D 17  ? 0.8408 1.1245 1.0522 0.1350  0.1115  0.1398  81  GLY D C   
8419  O O   . GLY D 17  ? 0.8374 1.1119 1.0095 0.1468  0.1040  0.1276  81  GLY D O   
8420  N N   . GLU D 18  ? 0.8372 1.1424 1.0634 0.1414  0.1319  0.1605  82  GLU D N   
8421  C CA  . GLU D 18  ? 0.9772 1.2942 1.1692 0.1645  0.1470  0.1707  82  GLU D CA  
8422  C C   . GLU D 18  ? 0.9841 1.3138 1.1507 0.1795  0.1404  0.1531  82  GLU D C   
8423  O O   . GLU D 18  ? 1.0829 1.4119 1.2084 0.1992  0.1410  0.1488  82  GLU D O   
8424  C CB  . GLU D 18  ? 1.0534 1.3902 1.2689 0.1676  0.1728  0.1998  82  GLU D CB  
8425  C CG  . GLU D 18  ? 1.2067 1.5407 1.3887 0.1864  0.1896  0.2182  82  GLU D CG  
8426  C CD  . GLU D 18  ? 1.1993 1.5049 1.3755 0.1783  0.1851  0.2236  82  GLU D CD  
8427  O OE1 . GLU D 18  ? 1.2537 1.5456 1.4633 0.1563  0.1762  0.2223  82  GLU D OE1 
8428  O OE2 . GLU D 18  ? 1.1865 1.4831 1.3237 0.1955  0.1897  0.2287  82  GLU D OE2 
8429  N N   . ASN D 19  ? 1.0304 1.3701 1.2214 0.1704  0.1324  0.1419  83  ASN D N   
8430  C CA  . ASN D 19  ? 1.0345 1.3860 1.2058 0.1835  0.1257  0.1254  83  ASN D CA  
8431  C C   . ASN D 19  ? 0.9026 1.2359 1.0626 0.1760  0.1015  0.0988  83  ASN D C   
8432  O O   . ASN D 19  ? 0.9186 1.2413 1.1044 0.1572  0.0903  0.0918  83  ASN D O   
8433  C CB  . ASN D 19  ? 1.0170 1.3965 1.2207 0.1833  0.1363  0.1330  83  ASN D CB  
8434  C CG  . ASN D 19  ? 1.2259 1.6276 1.4344 0.1958  0.1625  0.1589  83  ASN D CG  
8435  O OD1 . ASN D 19  ? 1.3559 1.7557 1.5286 0.2139  0.1717  0.1665  83  ASN D OD1 
8436  N ND2 . ASN D 19  ? 1.4528 1.8763 1.7062 0.1871  0.1750  0.1731  83  ASN D ND2 
8437  N N   . LEU D 20  ? 0.7509 1.0799 0.8722 0.1912  0.0933  0.0841  84  LEU D N   
8438  C CA  . LEU D 20  ? 0.7503 1.0606 0.8586 0.1847  0.0720  0.0605  84  LEU D CA  
8439  C C   . LEU D 20  ? 0.8782 1.1968 0.9996 0.1818  0.0637  0.0480  84  LEU D C   
8440  O O   . LEU D 20  ? 0.9469 1.2868 1.0704 0.1936  0.0722  0.0520  84  LEU D O   
8441  C CB  . LEU D 20  ? 0.7002 1.0018 0.7654 0.2012  0.0654  0.0495  84  LEU D CB  
8442  C CG  . LEU D 20  ? 0.6911 0.9679 0.7425 0.1926  0.0489  0.0345  84  LEU D CG  
8443  C CD1 . LEU D 20  ? 0.7866 1.0522 0.8489 0.1822  0.0534  0.0464  84  LEU D CD1 
8444  C CD2 . LEU D 20  ? 0.7261 0.9984 0.7394 0.2101  0.0421  0.0230  84  LEU D CD2 
8445  N N   . CYS D 21  ? 1.2293 1.5307 1.3582 0.1670  0.0473  0.0332  85  CYS D N   
8446  C CA  . CYS D 21  ? 1.3299 1.6326 1.4625 0.1656  0.0359  0.0179  85  CYS D CA  
8447  C C   . CYS D 21  ? 1.2580 1.5636 1.3565 0.1842  0.0319  0.0065  85  CYS D C   
8448  O O   . CYS D 21  ? 1.0771 1.3728 1.1465 0.1927  0.0293  0.0024  85  CYS D O   
8449  C CB  . CYS D 21  ? 1.3379 1.6168 1.4749 0.1491  0.0188  0.0037  85  CYS D CB  
8450  S SG  . CYS D 21  ? 2.8906 3.1690 3.0721 0.1296  0.0192  0.0123  85  CYS D SG  
8451  N N   . SER D 22  ? 1.2312 1.5506 1.3339 0.1915  0.0309  0.0012  86  SER D N   
8452  C CA  . SER D 22  ? 1.1487 1.4660 1.2200 0.2075  0.0226  -0.0133 86  SER D CA  
8453  C C   . SER D 22  ? 0.9957 1.2863 1.0553 0.1970  0.0039  -0.0312 86  SER D C   
8454  O O   . SER D 22  ? 0.9422 1.2235 1.0209 0.1816  -0.0034 -0.0355 86  SER D O   
8455  C CB  . SER D 22  ? 1.0614 1.3980 1.1415 0.2170  0.0245  -0.0158 86  SER D CB  
8456  O OG  . SER D 22  ? 1.4473 1.8112 1.5404 0.2269  0.0438  0.0022  86  SER D OG  
8457  N N   . ILE D 23  ? 0.8422 1.1203 0.8713 0.2056  -0.0036 -0.0413 87  ILE D N   
8458  C CA  . ILE D 23  ? 0.8133 1.0668 0.8315 0.1961  -0.0198 -0.0573 87  ILE D CA  
8459  C C   . ILE D 23  ? 0.6988 0.9491 0.6945 0.2096  -0.0296 -0.0716 87  ILE D C   
8460  O O   . ILE D 23  ? 0.7029 0.9607 0.6780 0.2272  -0.0273 -0.0723 87  ILE D O   
8461  C CB  . ILE D 23  ? 0.7968 1.0360 0.8041 0.1910  -0.0218 -0.0572 87  ILE D CB  
8462  C CG1 . ILE D 23  ? 0.8075 1.0455 0.8382 0.1760  -0.0148 -0.0448 87  ILE D CG1 
8463  C CG2 . ILE D 23  ? 0.6529 0.8691 0.6479 0.1835  -0.0373 -0.0737 87  ILE D CG2 
8464  C CD1 . ILE D 23  ? 0.8008 1.0408 0.8248 0.1802  -0.0061 -0.0340 87  ILE D CD1 
8465  N N   . ASN D 24  ? 0.5621 0.8009 0.5609 0.2027  -0.0406 -0.0828 88  ASN D N   
8466  C CA  . ASN D 24  ? 0.6324 0.8619 0.6092 0.2134  -0.0525 -0.0979 88  ASN D CA  
8467  C C   . ASN D 24  ? 0.6334 0.8355 0.6020 0.2015  -0.0665 -0.1107 88  ASN D C   
8468  O O   . ASN D 24  ? 0.6496 0.8397 0.6000 0.2081  -0.0772 -0.1231 88  ASN D O   
8469  C CB  . ASN D 24  ? 0.6498 0.8918 0.6320 0.2222  -0.0525 -0.1000 88  ASN D CB  
8470  C CG  . ASN D 24  ? 0.7630 1.0335 0.7480 0.2385  -0.0382 -0.0886 88  ASN D CG  
8471  O OD1 . ASN D 24  ? 0.8410 1.1165 0.8034 0.2566  -0.0380 -0.0919 88  ASN D OD1 
8472  N ND2 . ASN D 24  ? 1.1404 1.4296 1.1536 0.2325  -0.0259 -0.0748 88  ASN D ND2 
8473  N N   . GLY D 25  ? 0.7049 0.8967 0.6870 0.1841  -0.0662 -0.1072 89  GLY D N   
8474  C CA  . GLY D 25  ? 0.6839 0.8507 0.6596 0.1725  -0.0772 -0.1173 89  GLY D CA  
8475  C C   . GLY D 25  ? 0.6968 0.8556 0.6826 0.1577  -0.0743 -0.1119 89  GLY D C   
8476  O O   . GLY D 25  ? 0.7371 0.9079 0.7348 0.1559  -0.0648 -0.1007 89  GLY D O   
8477  N N   . TRP D 26  ? 0.7091 0.8471 0.6894 0.1476  -0.0821 -0.1196 90  TRP D N   
8478  C CA  . TRP D 26  ? 0.6638 0.7943 0.6517 0.1353  -0.0796 -0.1155 90  TRP D CA  
8479  C C   . TRP D 26  ? 0.7547 0.8660 0.7440 0.1238  -0.0855 -0.1203 90  TRP D C   
8480  O O   . TRP D 26  ? 0.6994 0.7965 0.6772 0.1241  -0.0932 -0.1292 90  TRP D O   
8481  C CB  . TRP D 26  ? 0.7011 0.8286 0.6790 0.1370  -0.0807 -0.1185 90  TRP D CB  
8482  C CG  . TRP D 26  ? 0.6844 0.8297 0.6572 0.1507  -0.0752 -0.1136 90  TRP D CG  
8483  C CD1 . TRP D 26  ? 0.6702 0.8207 0.6282 0.1653  -0.0790 -0.1198 90  TRP D CD1 
8484  C CD2 . TRP D 26  ? 0.6792 0.8382 0.6596 0.1529  -0.0646 -0.1011 90  TRP D CD2 
8485  N NE1 . TRP D 26  ? 0.7311 0.8979 0.6852 0.1772  -0.0714 -0.1122 90  TRP D NE1 
8486  C CE2 . TRP D 26  ? 0.6986 0.8709 0.6658 0.1700  -0.0620 -0.1001 90  TRP D CE2 
8487  C CE3 . TRP D 26  ? 0.6128 0.7728 0.6079 0.1434  -0.0579 -0.0910 90  TRP D CE3 
8488  C CZ2 . TRP D 26  ? 0.7304 0.9162 0.6982 0.1773  -0.0517 -0.0882 90  TRP D CZ2 
8489  C CZ3 . TRP D 26  ? 0.6218 0.7948 0.6195 0.1496  -0.0482 -0.0793 90  TRP D CZ3 
8490  C CH2 . TRP D 26  ? 0.5802 0.7659 0.5642 0.1662  -0.0444 -0.0772 90  TRP D CH2 
8491  N N   . VAL D 27  ? 0.6678 0.7777 0.6705 0.1147  -0.0823 -0.1142 91  VAL D N   
8492  C CA  . VAL D 27  ? 0.6641 0.7546 0.6651 0.1051  -0.0874 -0.1184 91  VAL D CA  
8493  C C   . VAL D 27  ? 0.5952 0.6798 0.5999 0.0967  -0.0843 -0.1149 91  VAL D C   
8494  O O   . VAL D 27  ? 0.4681 0.5639 0.4835 0.0964  -0.0784 -0.1072 91  VAL D O   
8495  C CB  . VAL D 27  ? 0.6402 0.7294 0.6500 0.1041  -0.0907 -0.1185 91  VAL D CB  
8496  C CG1 . VAL D 27  ? 0.7231 0.8284 0.7364 0.1143  -0.0901 -0.1182 91  VAL D CG1 
8497  C CG2 . VAL D 27  ? 0.7887 0.8819 0.8163 0.0976  -0.0875 -0.1115 91  VAL D CG2 
8498  N N   . PRO D 28  ? 0.6065 0.6734 0.6015 0.0906  -0.0877 -0.1203 92  PRO D N   
8499  C CA  . PRO D 28  ? 0.5564 0.6175 0.5537 0.0838  -0.0849 -0.1180 92  PRO D CA  
8500  C C   . PRO D 28  ? 0.5355 0.5931 0.5426 0.0796  -0.0851 -0.1141 92  PRO D C   
8501  O O   . PRO D 28  ? 0.5603 0.6103 0.5671 0.0794  -0.0898 -0.1168 92  PRO D O   
8502  C CB  . PRO D 28  ? 0.4987 0.5425 0.4834 0.0795  -0.0878 -0.1244 92  PRO D CB  
8503  C CG  . PRO D 28  ? 0.4934 0.5291 0.4697 0.0826  -0.0931 -0.1293 92  PRO D CG  
8504  C CD  . PRO D 28  ? 0.5255 0.5776 0.5065 0.0909  -0.0933 -0.1283 92  PRO D CD  
8505  N N   . THR D 29  ? 0.5632 0.6250 0.5789 0.0768  -0.0812 -0.1087 93  THR D N   
8506  C CA  . THR D 29  ? 0.6167 0.6742 0.6436 0.0731  -0.0830 -0.1057 93  THR D CA  
8507  C C   . THR D 29  ? 0.5217 0.5651 0.5416 0.0688  -0.0837 -0.1079 93  THR D C   
8508  O O   . THR D 29  ? 0.5662 0.5999 0.5894 0.0666  -0.0876 -0.1085 93  THR D O   
8509  C CB  . THR D 29  ? 0.6386 0.7112 0.6842 0.0736  -0.0783 -0.0962 93  THR D CB  
8510  O OG1 . THR D 29  ? 0.8185 0.8999 0.8612 0.0763  -0.0721 -0.0920 93  THR D OG1 
8511  C CG2 . THR D 29  ? 0.5979 0.6846 0.6540 0.0778  -0.0773 -0.0932 93  THR D CG2 
8512  N N   . TYR D 30  ? 0.5354 0.5783 0.5462 0.0686  -0.0805 -0.1097 94  TYR D N   
8513  C CA  . TYR D 30  ? 0.5571 0.5896 0.5619 0.0654  -0.0794 -0.1113 94  TYR D CA  
8514  C C   . TYR D 30  ? 0.5882 0.6196 0.5838 0.0646  -0.0767 -0.1152 94  TYR D C   
8515  O O   . TYR D 30  ? 0.7256 0.7671 0.7222 0.0668  -0.0758 -0.1159 94  TYR D O   
8516  C CB  . TYR D 30  ? 0.4901 0.5280 0.5043 0.0651  -0.0768 -0.1062 94  TYR D CB  
8517  C CG  . TYR D 30  ? 0.5864 0.6167 0.5938 0.0637  -0.0750 -0.1085 94  TYR D CG  
8518  C CD1 . TYR D 30  ? 0.6228 0.6383 0.6244 0.0629  -0.0779 -0.1110 94  TYR D CD1 
8519  C CD2 . TYR D 30  ? 0.6000 0.6382 0.6065 0.0644  -0.0709 -0.1089 94  TYR D CD2 
8520  C CE1 . TYR D 30  ? 0.6172 0.6272 0.6119 0.0631  -0.0752 -0.1128 94  TYR D CE1 
8521  C CE2 . TYR D 30  ? 0.6696 0.7033 0.6720 0.0635  -0.0686 -0.1111 94  TYR D CE2 
8522  C CZ  . TYR D 30  ? 0.6452 0.6651 0.6413 0.0630  -0.0700 -0.1126 94  TYR D CZ  
8523  O OH  . TYR D 30  ? 0.7816 0.7980 0.7728 0.0637  -0.0667 -0.1143 94  TYR D OH  
8524  N N   . ARG D 31  ? 0.5520 0.5711 0.5394 0.0619  -0.0757 -0.1177 95  ARG D N   
8525  C CA  . ARG D 31  ? 0.5926 0.6105 0.5753 0.0595  -0.0725 -0.1205 95  ARG D CA  
8526  C C   . ARG D 31  ? 0.5769 0.5880 0.5561 0.0577  -0.0684 -0.1202 95  ARG D C   
8527  O O   . ARG D 31  ? 0.5257 0.5235 0.4962 0.0584  -0.0693 -0.1203 95  ARG D O   
8528  C CB  . ARG D 31  ? 0.6190 0.6263 0.5925 0.0587  -0.0748 -0.1237 95  ARG D CB  
8529  C CG  . ARG D 31  ? 0.8349 0.8366 0.8047 0.0547  -0.0714 -0.1259 95  ARG D CG  
8530  C CD  . ARG D 31  ? 1.0324 1.0255 0.9955 0.0546  -0.0751 -0.1288 95  ARG D CD  
8531  N NE  . ARG D 31  ? 0.8828 0.8594 0.8331 0.0563  -0.0774 -0.1284 95  ARG D NE  
8532  C CZ  . ARG D 31  ? 0.7948 0.7576 0.7346 0.0565  -0.0801 -0.1304 95  ARG D CZ  
8533  N NH1 . ARG D 31  ? 0.8308 0.7937 0.7728 0.0544  -0.0811 -0.1328 95  ARG D NH1 
8534  N NH2 . ARG D 31  ? 1.2225 1.1700 1.1492 0.0595  -0.0828 -0.1304 95  ARG D NH2 
8535  N N   . GLY D 32  ? 0.6353 0.6563 0.6210 0.0570  -0.0645 -0.1202 96  GLY D N   
8536  C CA  . GLY D 32  ? 0.6934 0.7105 0.6764 0.0562  -0.0598 -0.1201 96  GLY D CA  
8537  C C   . GLY D 32  ? 0.7196 0.7260 0.6942 0.0530  -0.0555 -0.1211 96  GLY D C   
8538  O O   . GLY D 32  ? 0.8010 0.8048 0.7749 0.0501  -0.0563 -0.1224 96  GLY D O   
8539  N N   . GLU D 33  ? 0.8014 0.8007 0.7690 0.0542  -0.0506 -0.1201 97  GLU D N   
8540  C CA  . GLU D 33  ? 0.9620 0.9499 0.9198 0.0520  -0.0445 -0.1190 97  GLU D CA  
8541  C C   . GLU D 33  ? 0.9207 0.9190 0.8911 0.0461  -0.0379 -0.1189 97  GLU D C   
8542  O O   . GLU D 33  ? 1.0550 1.0447 1.0217 0.0422  -0.0329 -0.1172 97  GLU D O   
8543  C CB  . GLU D 33  ? 1.0987 1.0751 1.0420 0.0573  -0.0409 -0.1176 97  GLU D CB  
8544  C CG  . GLU D 33  ? 1.5600 1.5163 1.4836 0.0589  -0.0383 -0.1158 97  GLU D CG  
8545  C CD  . GLU D 33  ? 1.6964 1.6404 1.6108 0.0610  -0.0480 -0.1179 97  GLU D CD  
8546  O OE1 . GLU D 33  ? 2.2795 2.2267 2.1987 0.0637  -0.0563 -0.1202 97  GLU D OE1 
8547  O OE2 . GLU D 33  ? 1.4516 1.3826 1.3549 0.0602  -0.0472 -0.1168 97  GLU D OE2 
8548  N N   . GLY D 34  ? 0.7160 0.7322 0.7023 0.0457  -0.0385 -0.1209 98  GLY D N   
8549  C CA  . GLY D 34  ? 0.7766 0.8046 0.7791 0.0403  -0.0350 -0.1225 98  GLY D CA  
8550  C C   . GLY D 34  ? 0.7325 0.7623 0.7419 0.0369  -0.0415 -0.1260 98  GLY D C   
8551  O O   . GLY D 34  ? 0.8648 0.9033 0.8895 0.0322  -0.0409 -0.1287 98  GLY D O   
8552  N N   . THR D 35  ? 0.6645 0.6866 0.6638 0.0398  -0.0482 -0.1264 99  THR D N   
8553  C CA  . THR D 35  ? 0.8008 0.8241 0.8037 0.0390  -0.0552 -0.1302 99  THR D CA  
8554  C C   . THR D 35  ? 0.8914 0.8983 0.8884 0.0338  -0.0538 -0.1297 99  THR D C   
8555  O O   . THR D 35  ? 1.2299 1.2347 1.2300 0.0325  -0.0596 -0.1334 99  THR D O   
8556  C CB  . THR D 35  ? 0.8222 0.8453 0.8174 0.0450  -0.0619 -0.1303 99  THR D CB  
8557  O OG1 . THR D 35  ? 1.0679 1.0754 1.0489 0.0459  -0.0614 -0.1274 99  THR D OG1 
8558  C CG2 . THR D 35  ? 0.8543 0.8912 0.8546 0.0500  -0.0625 -0.1290 99  THR D CG2 
8559  N N   . THR D 36  ? 0.9174 0.9114 0.9042 0.0321  -0.0464 -0.1249 100 THR D N   
8560  C CA  . THR D 36  ? 1.1104 1.0853 1.0872 0.0285  -0.0439 -0.1224 100 THR D CA  
8561  C C   . THR D 36  ? 1.0705 1.0430 1.0515 0.0232  -0.0319 -0.1173 100 THR D C   
8562  O O   . THR D 36  ? 1.3273 1.2996 1.3213 0.0158  -0.0290 -0.1169 100 THR D O   
8563  C CB  . THR D 36  ? 1.3147 1.2720 1.2689 0.0343  -0.0471 -0.1208 100 THR D CB  
8564  O OG1 . THR D 36  ? 1.5558 1.5147 1.5029 0.0395  -0.0447 -0.1189 100 THR D OG1 
8565  C CG2 . THR D 36  ? 0.9341 0.8935 0.8870 0.0383  -0.0579 -0.1253 100 THR D CG2 
8566  N N   . GLY D 37  ? 0.9139 0.8852 0.8851 0.0275  -0.0251 -0.1135 101 GLY D N   
8567  C CA  . GLY D 37  ? 1.0430 1.0154 1.0176 0.0247  -0.0120 -0.1081 101 GLY D CA  
8568  C C   . GLY D 37  ? 1.1075 1.1035 1.1030 0.0238  -0.0086 -0.1100 101 GLY D C   
8569  O O   . GLY D 37  ? 1.3134 1.3242 1.3224 0.0242  -0.0168 -0.1158 101 GLY D O   
8570  N N   . LYS D 38  ? 0.9712 0.9704 0.9680 0.0239  0.0038  -0.1051 102 LYS D N   
8571  C CA  . LYS D 38  ? 0.9668 0.9881 0.9818 0.0246  0.0079  -0.1068 102 LYS D CA  
8572  C C   . LYS D 38  ? 0.9738 0.9961 0.9743 0.0352  0.0058  -0.1081 102 LYS D C   
8573  O O   . LYS D 38  ? 1.0167 1.0220 0.9937 0.0414  0.0036  -0.1067 102 LYS D O   
8574  C CB  . LYS D 38  ? 0.9214 0.9480 0.9482 0.0196  0.0233  -0.1005 102 LYS D CB  
8575  C CG  . LYS D 38  ? 1.2935 1.3239 1.3445 0.0076  0.0243  -0.1003 102 LYS D CG  
8576  C CD  . LYS D 38  ? 1.5191 1.5642 1.5924 0.0022  0.0391  -0.0951 102 LYS D CD  
8577  C CE  . LYS D 38  ? 1.6693 1.7277 1.7785 -0.0096 0.0357  -0.0990 102 LYS D CE  
8578  N NZ  . LYS D 38  ? 1.6345 1.7152 1.7721 -0.0138 0.0484  -0.0960 102 LYS D NZ  
8579  N N   . ILE D 39  ? 0.9084 0.9498 0.9234 0.0377  0.0054  -0.1114 103 ILE D N   
8580  C CA  . ILE D 39  ? 0.7032 0.7452 0.7070 0.0473  0.0019  -0.1132 103 ILE D CA  
8581  C C   . ILE D 39  ? 0.8133 0.8570 0.8110 0.0528  0.0139  -0.1097 103 ILE D C   
8582  O O   . ILE D 39  ? 0.8176 0.8765 0.8329 0.0492  0.0235  -0.1081 103 ILE D O   
8583  C CB  . ILE D 39  ? 0.7456 0.8064 0.7666 0.0488  -0.0056 -0.1187 103 ILE D CB  
8584  C CG1 . ILE D 39  ? 0.6194 0.6836 0.6502 0.0438  -0.0152 -0.1221 103 ILE D CG1 
8585  C CG2 . ILE D 39  ? 0.7099 0.7676 0.7191 0.0582  -0.0109 -0.1200 103 ILE D CG2 
8586  C CD1 . ILE D 39  ? 0.4809 0.5383 0.5011 0.0480  -0.0249 -0.1232 103 ILE D CD1 
8587  N N   . PRO D 40  ? 0.7969 0.8258 0.7705 0.0624  0.0129  -0.1090 104 PRO D N   
8588  C CA  . PRO D 40  ? 0.7828 0.8123 0.7457 0.0716  0.0221  -0.1070 104 PRO D CA  
8589  C C   . PRO D 40  ? 0.7734 0.8251 0.7546 0.0745  0.0230  -0.1106 104 PRO D C   
8590  O O   . PRO D 40  ? 0.8354 0.8943 0.8262 0.0744  0.0124  -0.1154 104 PRO D O   
8591  C CB  . PRO D 40  ? 0.7242 0.7332 0.6606 0.0817  0.0133  -0.1093 104 PRO D CB  
8592  C CG  . PRO D 40  ? 0.7145 0.7099 0.6457 0.0763  0.0044  -0.1096 104 PRO D CG  
8593  C CD  . PRO D 40  ? 0.7172 0.7280 0.6731 0.0657  0.0015  -0.1109 104 PRO D CD  
8594  N N   . ASP D 41  ? 0.7892 0.8516 0.7745 0.0779  0.0362  -0.1077 105 ASP D N   
8595  C CA  . ASP D 41  ? 0.9859 1.0723 0.9922 0.0801  0.0382  -0.1112 105 ASP D CA  
8596  C C   . ASP D 41  ? 1.0434 1.1277 1.0393 0.0915  0.0286  -0.1167 105 ASP D C   
8597  O O   . ASP D 41  ? 1.0116 1.1126 1.0243 0.0928  0.0242  -0.1211 105 ASP D O   
8598  C CB  . ASP D 41  ? 1.3209 1.4208 1.3351 0.0817  0.0560  -0.1061 105 ASP D CB  
8599  C CG  . ASP D 41  ? 1.6469 1.7489 1.6757 0.0689  0.0662  -0.0997 105 ASP D CG  
8600  O OD1 . ASP D 41  ? 2.5949 2.6799 2.6154 0.0624  0.0601  -0.0984 105 ASP D OD1 
8601  O OD2 . ASP D 41  ? 1.6345 1.7550 1.6844 0.0653  0.0799  -0.0957 105 ASP D OD2 
8602  N N   . GLU D 42  ? 1.1513 1.2136 1.1196 0.1001  0.0242  -0.1167 106 GLU D N   
8603  C CA  . GLU D 42  ? 1.1615 1.2178 1.1192 0.1111  0.0143  -0.1218 106 GLU D CA  
8604  C C   . GLU D 42  ? 1.0196 1.0738 0.9854 0.1070  -0.0004 -0.1251 106 GLU D C   
8605  O O   . GLU D 42  ? 1.4417 1.4952 1.4064 0.1140  -0.0081 -0.1286 106 GLU D O   
8606  C CB  . GLU D 42  ? 1.3142 1.3470 1.2410 0.1227  0.0126  -0.1221 106 GLU D CB  
8607  C CG  . GLU D 42  ? 1.4706 1.4810 1.3826 0.1193  0.0042  -0.1215 106 GLU D CG  
8608  C CD  . GLU D 42  ? 2.2226 2.2226 2.1184 0.1195  0.0148  -0.1161 106 GLU D CD  
8609  O OE1 . GLU D 42  ? 2.3328 2.3461 2.2416 0.1120  0.0279  -0.1108 106 GLU D OE1 
8610  O OE2 . GLU D 42  ? 3.1122 3.0902 2.9827 0.1275  0.0096  -0.1173 106 GLU D OE2 
8611  N N   . GLN D 43  ? 0.9127 0.9653 0.8860 0.0964  -0.0038 -0.1234 107 GLN D N   
8612  C CA  . GLN D 43  ? 0.9494 1.0014 0.9299 0.0931  -0.0157 -0.1251 107 GLN D CA  
8613  C C   . GLN D 43  ? 1.0576 1.1301 1.0573 0.0936  -0.0171 -0.1277 107 GLN D C   
8614  O O   . GLN D 43  ? 1.1255 1.2158 1.1394 0.0922  -0.0093 -0.1286 107 GLN D O   
8615  C CB  . GLN D 43  ? 0.7954 0.8426 0.7786 0.0835  -0.0185 -0.1231 107 GLN D CB  
8616  C CG  . GLN D 43  ? 1.0972 1.1221 1.0607 0.0846  -0.0218 -0.1217 107 GLN D CG  
8617  C CD  . GLN D 43  ? 1.2989 1.3189 1.2654 0.0772  -0.0284 -0.1209 107 GLN D CD  
8618  O OE1 . GLN D 43  ? 1.1720 1.2028 1.1522 0.0735  -0.0328 -0.1214 107 GLN D OE1 
8619  N NE2 . GLN D 43  ? 1.1885 1.1921 1.1405 0.0767  -0.0292 -0.1197 107 GLN D NE2 
8620  N N   . MET D 44  ? 0.8064 0.8760 0.8067 0.0961  -0.0270 -0.1287 108 MET D N   
8621  C CA  . MET D 44  ? 0.6749 0.7607 0.6897 0.0978  -0.0301 -0.1308 108 MET D CA  
8622  C C   . MET D 44  ? 0.7569 0.8545 0.7860 0.0891  -0.0301 -0.1310 108 MET D C   
8623  O O   . MET D 44  ? 0.8687 0.9570 0.8935 0.0833  -0.0326 -0.1288 108 MET D O   
8624  C CB  . MET D 44  ? 0.6192 0.6942 0.6278 0.1025  -0.0399 -0.1297 108 MET D CB  
8625  C CG  . MET D 44  ? 0.7240 0.8114 0.7425 0.1065  -0.0442 -0.1308 108 MET D CG  
8626  S SD  . MET D 44  ? 1.0397 1.1398 1.0623 0.1165  -0.0410 -0.1356 108 MET D SD  
8627  C CE  . MET D 44  ? 1.0270 1.1064 1.0339 0.1264  -0.0483 -0.1348 108 MET D CE  
8628  N N   . LEU D 45  ? 0.7670 0.8848 0.8135 0.0888  -0.0281 -0.1346 109 LEU D N   
8629  C CA  . LEU D 45  ? 0.7825 0.9110 0.8430 0.0826  -0.0313 -0.1367 109 LEU D CA  
8630  C C   . LEU D 45  ? 0.8558 0.9827 0.9125 0.0869  -0.0409 -0.1365 109 LEU D C   
8631  O O   . LEU D 45  ? 1.0012 1.1314 1.0567 0.0951  -0.0443 -0.1372 109 LEU D O   
8632  C CB  . LEU D 45  ? 0.5725 0.7236 0.6552 0.0818  -0.0282 -0.1418 109 LEU D CB  
8633  C CG  . LEU D 45  ? 0.6573 0.8146 0.7487 0.0776  -0.0164 -0.1408 109 LEU D CG  
8634  C CD1 . LEU D 45  ? 0.6687 0.8512 0.7851 0.0792  -0.0142 -0.1462 109 LEU D CD1 
8635  C CD2 . LEU D 45  ? 0.5721 0.7216 0.6651 0.0668  -0.0127 -0.1379 109 LEU D CD2 
8636  N N   . THR D 46  ? 0.6840 0.8057 0.7383 0.0825  -0.0447 -0.1350 110 THR D N   
8637  C CA  . THR D 46  ? 0.7497 0.8704 0.7993 0.0874  -0.0518 -0.1332 110 THR D CA  
8638  C C   . THR D 46  ? 0.8688 1.0028 0.9277 0.0883  -0.0568 -0.1378 110 THR D C   
8639  O O   . THR D 46  ? 0.8849 1.0251 0.9540 0.0824  -0.0563 -0.1420 110 THR D O   
8640  C CB  . THR D 46  ? 0.7112 0.8160 0.7489 0.0847  -0.0532 -0.1275 110 THR D CB  
8641  O OG1 . THR D 46  ? 0.7812 0.8849 0.8206 0.0778  -0.0526 -0.1287 110 THR D OG1 
8642  C CG2 . THR D 46  ? 0.7778 0.8680 0.8063 0.0843  -0.0506 -0.1247 110 THR D CG2 
8643  N N   . ARG D 47  ? 0.8766 1.0137 0.9312 0.0967  -0.0621 -0.1367 111 ARG D N   
8644  C CA  . ARG D 47  ? 0.6162 0.7631 0.6739 0.1008  -0.0682 -0.1407 111 ARG D CA  
8645  C C   . ARG D 47  ? 0.5805 0.7217 0.6245 0.1091  -0.0708 -0.1341 111 ARG D C   
8646  O O   . ARG D 47  ? 0.6587 0.7915 0.6959 0.1118  -0.0687 -0.1278 111 ARG D O   
8647  C CB  . ARG D 47  ? 0.5108 0.6750 0.5829 0.1051  -0.0720 -0.1496 111 ARG D CB  
8648  C CG  . ARG D 47  ? 0.5868 0.7563 0.6545 0.1174  -0.0761 -0.1499 111 ARG D CG  
8649  C CD  . ARG D 47  ? 0.5945 0.7822 0.6754 0.1239  -0.0838 -0.1604 111 ARG D CD  
8650  N NE  . ARG D 47  ? 0.8018 0.9924 0.8739 0.1380  -0.0889 -0.1603 111 ARG D NE  
8651  C CZ  . ARG D 47  ? 1.1184 1.3041 1.1742 0.1478  -0.0932 -0.1565 111 ARG D CZ  
8652  N NH1 . ARG D 47  ? 1.3276 1.5072 1.3756 0.1452  -0.0932 -0.1532 111 ARG D NH1 
8653  N NH2 . ARG D 47  ? 1.1639 1.3507 1.2104 0.1612  -0.0970 -0.1555 111 ARG D NH2 
8654  N N   . GLN D 48  ? 0.4847 0.6300 0.5250 0.1135  -0.0751 -0.1352 112 GLN D N   
8655  C CA  . GLN D 48  ? 0.4693 0.6106 0.4964 0.1220  -0.0757 -0.1274 112 GLN D CA  
8656  C C   . GLN D 48  ? 0.4852 0.6126 0.5063 0.1164  -0.0702 -0.1171 112 GLN D C   
8657  O O   . GLN D 48  ? 0.5021 0.6240 0.5163 0.1213  -0.0684 -0.1082 112 GLN D O   
8658  C CB  . GLN D 48  ? 0.4365 0.5816 0.4592 0.1335  -0.0780 -0.1263 112 GLN D CB  
8659  C CG  . GLN D 48  ? 0.5318 0.6657 0.5431 0.1374  -0.0740 -0.1137 112 GLN D CG  
8660  C CD  . GLN D 48  ? 0.7616 0.8989 0.7614 0.1516  -0.0763 -0.1099 112 GLN D CD  
8661  O OE1 . GLN D 48  ? 0.9851 1.1121 0.9766 0.1546  -0.0717 -0.0973 112 GLN D OE1 
8662  N NE2 . GLN D 48  ? 0.8544 1.0026 0.8527 0.1604  -0.0824 -0.1180 112 GLN D NE2 
8663  N N   . ASN D 49  ? 0.4821 0.6036 0.5067 0.1063  -0.0681 -0.1182 113 ASN D N   
8664  C CA  . ASN D 49  ? 0.4990 0.6093 0.5197 0.1013  -0.0650 -0.1106 113 ASN D CA  
8665  C C   . ASN D 49  ? 0.5460 0.6579 0.5608 0.1065  -0.0645 -0.1037 113 ASN D C   
8666  O O   . ASN D 49  ? 0.6898 0.8098 0.7012 0.1117  -0.0670 -0.1070 113 ASN D O   
8667  C CB  . ASN D 49  ? 0.5448 0.6504 0.5680 0.0921  -0.0645 -0.1148 113 ASN D CB  
8668  C CG  . ASN D 49  ? 0.6395 0.7419 0.6672 0.0866  -0.0624 -0.1193 113 ASN D CG  
8669  O OD1 . ASN D 49  ? 0.5574 0.6485 0.5822 0.0828  -0.0602 -0.1164 113 ASN D OD1 
8670  N ND2 . ASN D 49  ? 0.5895 0.7024 0.6250 0.0867  -0.0632 -0.1264 113 ASN D ND2 
8671  N N   . PHE D 50  ? 0.5767 0.6806 0.5910 0.1053  -0.0614 -0.0942 114 PHE D N   
8672  C CA  . PHE D 50  ? 0.5461 0.6519 0.5582 0.1079  -0.0588 -0.0865 114 PHE D CA  
8673  C C   . PHE D 50  ? 0.4756 0.5714 0.4942 0.1010  -0.0564 -0.0789 114 PHE D C   
8674  O O   . PHE D 50  ? 0.5418 0.6276 0.5642 0.0952  -0.0579 -0.0806 114 PHE D O   
8675  C CB  . PHE D 50  ? 0.8239 0.9367 0.8287 0.1199  -0.0571 -0.0803 114 PHE D CB  
8676  C CG  . PHE D 50  ? 0.7621 0.8682 0.7672 0.1225  -0.0551 -0.0724 114 PHE D CG  
8677  C CD1 . PHE D 50  ? 0.7665 0.8730 0.7693 0.1268  -0.0584 -0.0778 114 PHE D CD1 
8678  C CD2 . PHE D 50  ? 0.8973 0.9969 0.9061 0.1211  -0.0501 -0.0595 114 PHE D CD2 
8679  C CE1 . PHE D 50  ? 0.7643 0.8630 0.7658 0.1304  -0.0574 -0.0709 114 PHE D CE1 
8680  C CE2 . PHE D 50  ? 0.9360 1.0271 0.9454 0.1234  -0.0489 -0.0519 114 PHE D CE2 
8681  C CZ  . PHE D 50  ? 0.7378 0.8275 0.7420 0.1286  -0.0528 -0.0578 114 PHE D CZ  
8682  N N   . VAL D 51  ? 0.4372 0.5358 0.4578 0.1022  -0.0530 -0.0708 115 VAL D N   
8683  C CA  . VAL D 51  ? 0.4157 0.5061 0.4469 0.0950  -0.0518 -0.0643 115 VAL D CA  
8684  C C   . VAL D 51  ? 0.4760 0.5698 0.5120 0.0991  -0.0459 -0.0507 115 VAL D C   
8685  O O   . VAL D 51  ? 0.6085 0.7129 0.6374 0.1078  -0.0416 -0.0461 115 VAL D O   
8686  C CB  . VAL D 51  ? 0.3983 0.4899 0.4322 0.0902  -0.0532 -0.0682 115 VAL D CB  
8687  C CG1 . VAL D 51  ? 0.3564 0.4428 0.4040 0.0842  -0.0527 -0.0614 115 VAL D CG1 
8688  C CG2 . VAL D 51  ? 0.3829 0.4686 0.4119 0.0857  -0.0579 -0.0798 115 VAL D CG2 
8689  N N   . SER D 52  ? 0.5391 0.6230 0.5871 0.0932  -0.0458 -0.0439 116 SER D N   
8690  C CA  . SER D 52  ? 0.6667 0.7512 0.7230 0.0951  -0.0394 -0.0290 116 SER D CA  
8691  C C   . SER D 52  ? 0.5805 0.6559 0.6561 0.0850  -0.0419 -0.0256 116 SER D C   
8692  O O   . SER D 52  ? 0.5162 0.5794 0.5938 0.0796  -0.0493 -0.0336 116 SER D O   
8693  C CB  . SER D 52  ? 0.6628 0.7407 0.7125 0.1008  -0.0387 -0.0243 116 SER D CB  
8694  O OG  . SER D 52  ? 0.8387 0.9150 0.8968 0.1020  -0.0317 -0.0083 116 SER D OG  
8695  N N   . CYS D 53  ? 0.6824 0.7643 0.7727 0.0831  -0.0359 -0.0143 117 CYS D N   
8696  C CA  . CYS D 53  ? 0.8343 0.9093 0.9469 0.0730  -0.0399 -0.0128 117 CYS D CA  
8697  C C   . CYS D 53  ? 0.8111 0.8789 0.9419 0.0693  -0.0367 0.0012  117 CYS D C   
8698  O O   . CYS D 53  ? 0.9996 1.0736 1.1293 0.0746  -0.0268 0.0146  117 CYS D O   
8699  C CB  . CYS D 53  ? 0.9054 0.9933 1.0273 0.0710  -0.0381 -0.0135 117 CYS D CB  
8700  S SG  . CYS D 53  ? 1.1411 1.2317 1.2423 0.0739  -0.0439 -0.0305 117 CYS D SG  
8701  N N   . SER D 54  ? 0.8074 0.8604 0.9539 0.0609  -0.0456 -0.0023 118 SER D N   
8702  C CA  . SER D 54  ? 0.8474 0.8927 1.0196 0.0542  -0.0448 0.0101  118 SER D CA  
8703  C C   . SER D 54  ? 0.8592 0.9147 1.0580 0.0469  -0.0443 0.0129  118 SER D C   
8704  O O   . SER D 54  ? 0.8429 0.9120 1.0361 0.0490  -0.0431 0.0069  118 SER D O   
8705  C CB  . SER D 54  ? 0.7811 0.8031 0.9563 0.0504  -0.0566 0.0039  118 SER D CB  
8706  O OG  . SER D 54  ? 0.8037 0.8174 0.9897 0.0442  -0.0689 -0.0079 118 SER D OG  
8707  N N   . ASP D 55  ? 1.0467 1.0960 1.2756 0.0385  -0.0456 0.0222  119 ASP D N   
8708  C CA  . ASP D 55  ? 1.1991 1.2598 1.4593 0.0310  -0.0453 0.0258  119 ASP D CA  
8709  C C   . ASP D 55  ? 0.9257 0.9753 1.1928 0.0258  -0.0624 0.0087  119 ASP D C   
8710  O O   . ASP D 55  ? 1.0807 1.1384 1.3710 0.0206  -0.0663 0.0064  119 ASP D O   
8711  C CB  . ASP D 55  ? 1.4396 1.5001 1.7332 0.0237  -0.0381 0.0447  119 ASP D CB  
8712  C CG  . ASP D 55  ? 1.6593 1.6941 1.9584 0.0194  -0.0467 0.0459  119 ASP D CG  
8713  O OD1 . ASP D 55  ? 1.8195 1.8369 2.1025 0.0209  -0.0607 0.0302  119 ASP D OD1 
8714  O OD2 . ASP D 55  ? 1.9365 1.9682 2.2561 0.0151  -0.0389 0.0632  119 ASP D OD2 
8715  N N   . LYS D 56  ? 0.7889 0.8203 1.0338 0.0288  -0.0723 -0.0034 120 LYS D N   
8716  C CA  . LYS D 56  ? 0.9814 0.9967 1.2273 0.0263  -0.0891 -0.0193 120 LYS D CA  
8717  C C   . LYS D 56  ? 0.8495 0.8671 1.0652 0.0328  -0.0917 -0.0335 120 LYS D C   
8718  O O   . LYS D 56  ? 0.9962 1.0086 1.2122 0.0320  -0.1022 -0.0454 120 LYS D O   
8719  C CB  . LYS D 56  ? 1.3359 1.3276 1.5781 0.0263  -0.0978 -0.0217 120 LYS D CB  
8720  C CG  . LYS D 56  ? 1.5286 1.5007 1.7651 0.0270  -0.1158 -0.0390 120 LYS D CG  
8721  C CD  . LYS D 56  ? 1.5998 1.5495 1.8260 0.0301  -0.1231 -0.0419 120 LYS D CD  
8722  C CE  . LYS D 56  ? 2.0449 1.9842 2.3018 0.0229  -0.1256 -0.0304 120 LYS D CE  
8723  N NZ  . LYS D 56  ? 2.1328 2.0807 2.3900 0.0232  -0.1094 -0.0124 120 LYS D NZ  
8724  N N   . GLU D 57  ? 0.6817 0.7064 0.8719 0.0395  -0.0823 -0.0320 121 GLU D N   
8725  C CA  . GLU D 57  ? 0.7009 0.7242 0.8624 0.0450  -0.0846 -0.0448 121 GLU D CA  
8726  C C   . GLU D 57  ? 0.6951 0.7295 0.8356 0.0517  -0.0739 -0.0413 121 GLU D C   
8727  O O   . GLU D 57  ? 0.8870 0.9259 1.0298 0.0538  -0.0661 -0.0302 121 GLU D O   
8728  C CB  . GLU D 57  ? 0.7103 0.7129 0.8597 0.0465  -0.0954 -0.0556 121 GLU D CB  
8729  C CG  . GLU D 57  ? 0.9212 0.9187 1.0561 0.0512  -0.0914 -0.0527 121 GLU D CG  
8730  C CD  . GLU D 57  ? 1.2805 1.2572 1.4074 0.0535  -0.1019 -0.0614 121 GLU D CD  
8731  O OE1 . GLU D 57  ? 1.4697 1.4361 1.5923 0.0537  -0.1115 -0.0725 121 GLU D OE1 
8732  O OE2 . GLU D 57  ? 1.1186 1.0890 1.2415 0.0565  -0.1005 -0.0574 121 GLU D OE2 
8733  N N   . CYS D 58  ? 0.6318 0.6692 0.7519 0.0554  -0.0743 -0.0511 122 CYS D N   
8734  C CA  . CYS D 58  ? 0.7006 0.7479 0.8023 0.0617  -0.0668 -0.0506 122 CYS D CA  
8735  C C   . CYS D 58  ? 0.6775 0.7146 0.7619 0.0643  -0.0706 -0.0596 122 CYS D C   
8736  O O   . CYS D 58  ? 0.8116 0.8385 0.8901 0.0627  -0.0772 -0.0692 122 CYS D O   
8737  C CB  . CYS D 58  ? 0.6388 0.6989 0.7329 0.0639  -0.0638 -0.0544 122 CYS D CB  
8738  S SG  . CYS D 58  ? 0.9619 1.0383 1.0738 0.0639  -0.0567 -0.0429 122 CYS D SG  
8739  N N   . ARG D 59  ? 0.5639 0.6042 0.6399 0.0694  -0.0661 -0.0563 123 ARG D N   
8740  C CA  . ARG D 59  ? 0.5298 0.5634 0.5923 0.0726  -0.0688 -0.0641 123 ARG D CA  
8741  C C   . ARG D 59  ? 0.5101 0.5564 0.5594 0.0776  -0.0643 -0.0681 123 ARG D C   
8742  O O   . ARG D 59  ? 0.5361 0.5949 0.5845 0.0811  -0.0594 -0.0632 123 ARG D O   
8743  C CB  . ARG D 59  ? 0.4731 0.4972 0.5385 0.0748  -0.0702 -0.0591 123 ARG D CB  
8744  C CG  . ARG D 59  ? 0.5345 0.5433 0.6128 0.0699  -0.0771 -0.0581 123 ARG D CG  
8745  C CD  . ARG D 59  ? 0.6632 0.6597 0.7418 0.0729  -0.0800 -0.0551 123 ARG D CD  
8746  N NE  . ARG D 59  ? 0.7069 0.6965 0.7704 0.0776  -0.0842 -0.0659 123 ARG D NE  
8747  C CZ  . ARG D 59  ? 0.8089 0.7856 0.8694 0.0769  -0.0921 -0.0749 123 ARG D CZ  
8748  N NH1 . ARG D 59  ? 0.7114 0.6802 0.7839 0.0714  -0.0984 -0.0756 123 ARG D NH1 
8749  N NH2 . ARG D 59  ? 0.7783 0.7510 0.8239 0.0828  -0.0937 -0.0835 123 ARG D NH2 
8750  N N   . ARG D 60  ? 0.4492 0.4924 0.4889 0.0784  -0.0665 -0.0774 124 ARG D N   
8751  C CA  . ARG D 60  ? 0.4319 0.4862 0.4631 0.0818  -0.0638 -0.0826 124 ARG D CA  
8752  C C   . ARG D 60  ? 0.4974 0.5515 0.5253 0.0871  -0.0638 -0.0834 124 ARG D C   
8753  O O   . ARG D 60  ? 0.6040 0.6490 0.6298 0.0870  -0.0663 -0.0874 124 ARG D O   
8754  C CB  . ARG D 60  ? 0.3830 0.4343 0.4088 0.0780  -0.0650 -0.0915 124 ARG D CB  
8755  C CG  . ARG D 60  ? 0.3998 0.4576 0.4202 0.0799  -0.0633 -0.0984 124 ARG D CG  
8756  C CD  . ARG D 60  ? 0.4250 0.4812 0.4416 0.0753  -0.0627 -0.1043 124 ARG D CD  
8757  N NE  . ARG D 60  ? 0.4163 0.4795 0.4321 0.0755  -0.0602 -0.1101 124 ARG D NE  
8758  C CZ  . ARG D 60  ? 0.5197 0.5779 0.5319 0.0718  -0.0581 -0.1143 124 ARG D CZ  
8759  N NH1 . ARG D 60  ? 0.7263 0.7713 0.7320 0.0690  -0.0591 -0.1139 124 ARG D NH1 
8760  N NH2 . ARG D 60  ? 0.5010 0.5676 0.5168 0.0712  -0.0548 -0.1185 124 ARG D NH2 
8761  N N   . PHE D 61  ? 0.4931 0.5570 0.5190 0.0933  -0.0615 -0.0798 125 PHE D N   
8762  C CA  . PHE D 61  ? 0.6436 0.7091 0.6656 0.0997  -0.0623 -0.0822 125 PHE D CA  
8763  C C   . PHE D 61  ? 0.6045 0.6823 0.6238 0.1017  -0.0624 -0.0917 125 PHE D C   
8764  O O   . PHE D 61  ? 0.5765 0.6624 0.5958 0.0999  -0.0618 -0.0947 125 PHE D O   
8765  C CB  . PHE D 61  ? 0.6746 0.7422 0.6947 0.1072  -0.0605 -0.0729 125 PHE D CB  
8766  C CG  . PHE D 61  ? 0.5945 0.6493 0.6208 0.1045  -0.0600 -0.0624 125 PHE D CG  
8767  C CD1 . PHE D 61  ? 0.6130 0.6667 0.6476 0.0983  -0.0580 -0.0564 125 PHE D CD1 
8768  C CD2 . PHE D 61  ? 0.6349 0.6787 0.6607 0.1080  -0.0621 -0.0588 125 PHE D CD2 
8769  C CE1 . PHE D 61  ? 0.8163 0.8593 0.8615 0.0946  -0.0577 -0.0465 125 PHE D CE1 
8770  C CE2 . PHE D 61  ? 0.7191 0.7495 0.7534 0.1046  -0.0624 -0.0490 125 PHE D CE2 
8771  C CZ  . PHE D 61  ? 0.8092 0.8396 0.8550 0.0972  -0.0601 -0.0425 125 PHE D CZ  
8772  N N   . PHE D 62  ? 0.5221 0.6015 0.5407 0.1055  -0.0635 -0.0968 126 PHE D N   
8773  C CA  . PHE D 62  ? 0.6124 0.7056 0.6331 0.1074  -0.0637 -0.1056 126 PHE D CA  
8774  C C   . PHE D 62  ? 0.6254 0.7229 0.6465 0.1147  -0.0652 -0.1093 126 PHE D C   
8775  O O   . PHE D 62  ? 0.6565 0.7444 0.6742 0.1187  -0.0663 -0.1053 126 PHE D O   
8776  C CB  . PHE D 62  ? 0.6600 0.7531 0.6839 0.0990  -0.0618 -0.1116 126 PHE D CB  
8777  C CG  . PHE D 62  ? 0.7100 0.7917 0.7318 0.0964  -0.0606 -0.1123 126 PHE D CG  
8778  C CD1 . PHE D 62  ? 0.7740 0.8602 0.7975 0.0998  -0.0593 -0.1174 126 PHE D CD1 
8779  C CD2 . PHE D 62  ? 0.6929 0.7598 0.7110 0.0924  -0.0615 -0.1082 126 PHE D CD2 
8780  C CE1 . PHE D 62  ? 0.6838 0.7588 0.7022 0.1001  -0.0583 -0.1182 126 PHE D CE1 
8781  C CE2 . PHE D 62  ? 0.7296 0.7844 0.7433 0.0923  -0.0621 -0.1100 126 PHE D CE2 
8782  C CZ  . PHE D 62  ? 0.7266 0.7850 0.7390 0.0968  -0.0602 -0.1149 126 PHE D CZ  
8783  N N   . VAL D 63  ? 0.7110 0.8232 0.7381 0.1165  -0.0659 -0.1176 127 VAL D N   
8784  C CA  . VAL D 63  ? 0.6396 0.7597 0.6699 0.1237  -0.0675 -0.1226 127 VAL D CA  
8785  C C   . VAL D 63  ? 0.6260 0.7523 0.6653 0.1183  -0.0640 -0.1295 127 VAL D C   
8786  O O   . VAL D 63  ? 0.6138 0.7479 0.6610 0.1117  -0.0623 -0.1336 127 VAL D O   
8787  C CB  . VAL D 63  ? 0.6101 0.7446 0.6425 0.1319  -0.0720 -0.1268 127 VAL D CB  
8788  C CG1 . VAL D 63  ? 0.7331 0.8801 0.7736 0.1382  -0.0742 -0.1348 127 VAL D CG1 
8789  C CG2 . VAL D 63  ? 0.6722 0.7994 0.6924 0.1404  -0.0739 -0.1183 127 VAL D CG2 
8790  N N   . SER D 64  ? 0.5841 0.7061 0.6216 0.1217  -0.0625 -0.1304 128 SER D N   
8791  C CA  . SER D 64  ? 0.6917 0.8194 0.7358 0.1182  -0.0571 -0.1353 128 SER D CA  
8792  C C   . SER D 64  ? 0.7453 0.8955 0.8056 0.1199  -0.0563 -0.1431 128 SER D C   
8793  O O   . SER D 64  ? 0.8898 1.0498 0.9537 0.1282  -0.0615 -0.1462 128 SER D O   
8794  C CB  . SER D 64  ? 0.8328 0.9502 0.8687 0.1241  -0.0563 -0.1347 128 SER D CB  
8795  O OG  . SER D 64  ? 1.1208 1.2464 1.1590 0.1345  -0.0596 -0.1379 128 SER D OG  
8796  N N   . MET D 65  ? 0.7436 0.9017 0.8146 0.1123  -0.0501 -0.1459 129 MET D N   
8797  C CA  . MET D 65  ? 0.8376 1.0177 0.9285 0.1130  -0.0477 -0.1529 129 MET D CA  
8798  C C   . MET D 65  ? 0.9330 1.1161 1.0255 0.1148  -0.0389 -0.1531 129 MET D C   
8799  O O   . MET D 65  ? 1.1329 1.3355 1.2442 0.1146  -0.0343 -0.1577 129 MET D O   
8800  C CB  . MET D 65  ? 0.9125 1.1026 1.0197 0.1031  -0.0468 -0.1560 129 MET D CB  
8801  C CG  . MET D 65  ? 0.9643 1.1653 1.0804 0.1062  -0.0567 -0.1617 129 MET D CG  
8802  S SD  . MET D 65  ? 1.0647 1.2539 1.1717 0.1004  -0.0616 -0.1592 129 MET D SD  
8803  C CE  . MET D 65  ? 1.0369 1.2307 1.1625 0.0862  -0.0561 -0.1617 129 MET D CE  
8804  N N   . GLY D 66  ? 1.0398 1.2041 1.1134 0.1176  -0.0369 -0.1485 130 GLY D N   
8805  C CA  . GLY D 66  ? 0.9966 1.1609 1.0668 0.1205  -0.0281 -0.1484 130 GLY D CA  
8806  C C   . GLY D 66  ? 0.9319 1.0839 0.9938 0.1123  -0.0205 -0.1438 130 GLY D C   
8807  O O   . GLY D 66  ? 0.8898 1.0355 0.9518 0.1032  -0.0218 -0.1413 130 GLY D O   
8808  N N   . TYR D 67  ? 0.7976 0.9453 0.8501 0.1171  -0.0128 -0.1427 131 TYR D N   
8809  C CA  . TYR D 67  ? 0.7585 0.8927 0.7992 0.1119  -0.0057 -0.1382 131 TYR D CA  
8810  C C   . TYR D 67  ? 0.7550 0.9062 0.8150 0.1032  0.0049  -0.1371 131 TYR D C   
8811  O O   . TYR D 67  ? 0.7717 0.9456 0.8524 0.1044  0.0089  -0.1403 131 TYR D O   
8812  C CB  . TYR D 67  ? 0.9249 1.0477 0.9459 0.1226  -0.0013 -0.1377 131 TYR D CB  
8813  C CG  . TYR D 67  ? 0.9987 1.1032 1.0026 0.1315  -0.0128 -0.1396 131 TYR D CG  
8814  C CD1 . TYR D 67  ? 1.1449 1.2276 1.1364 0.1279  -0.0214 -0.1374 131 TYR D CD1 
8815  C CD2 . TYR D 67  ? 1.0479 1.1569 1.0500 0.1437  -0.0153 -0.1437 131 TYR D CD2 
8816  C CE1 . TYR D 67  ? 1.2396 1.3052 1.2195 0.1349  -0.0323 -0.1386 131 TYR D CE1 
8817  C CE2 . TYR D 67  ? 1.4648 1.5546 1.4525 0.1515  -0.0266 -0.1452 131 TYR D CE2 
8818  C CZ  . TYR D 67  ? 1.3698 1.4379 1.3476 0.1464  -0.0350 -0.1424 131 TYR D CZ  
8819  O OH  . TYR D 67  ? 1.4088 1.4580 1.3762 0.1531  -0.0462 -0.1435 131 TYR D OH  
8820  N N   . GLY D 68  ? 0.7998 0.9396 0.8542 0.0945  0.0090  -0.1326 132 GLY D N   
8821  C CA  . GLY D 68  ? 0.8615 1.0133 0.9351 0.0840  0.0180  -0.1304 132 GLY D CA  
8822  C C   . GLY D 68  ? 0.8536 1.0164 0.9326 0.0865  0.0337  -0.1271 132 GLY D C   
8823  O O   . GLY D 68  ? 0.9356 1.1158 1.0394 0.0786  0.0423  -0.1258 132 GLY D O   
8824  N N   . THR D 69  ? 0.8682 1.0208 0.9246 0.0981  0.0372  -0.1259 133 THR D N   
8825  C CA  . THR D 69  ? 0.9927 1.1544 1.0486 0.1038  0.0533  -0.1220 133 THR D CA  
8826  C C   . THR D 69  ? 0.9646 1.1525 1.0397 0.1114  0.0561  -0.1268 133 THR D C   
8827  O O   . THR D 69  ? 0.8306 1.0377 0.9220 0.1113  0.0707  -0.1238 133 THR D O   
8828  C CB  . THR D 69  ? 0.9716 1.1092 0.9911 0.1151  0.0560  -0.1190 133 THR D CB  
8829  O OG1 . THR D 69  ? 1.1581 1.3068 1.1755 0.1237  0.0722  -0.1155 133 THR D OG1 
8830  C CG2 . THR D 69  ? 0.8731 0.9954 0.8731 0.1259  0.0404  -0.1252 133 THR D CG2 
8831  N N   . THR D 70  ? 1.3086 1.4974 1.3826 0.1182  0.0425  -0.1337 134 THR D N   
8832  C CA  . THR D 70  ? 1.2277 1.4389 1.3164 0.1278  0.0425  -0.1394 134 THR D CA  
8833  C C   . THR D 70  ? 1.1622 1.3967 1.2845 0.1197  0.0373  -0.1442 134 THR D C   
8834  O O   . THR D 70  ? 0.9497 1.2052 1.0885 0.1268  0.0355  -0.1501 134 THR D O   
8835  C CB  . THR D 70  ? 1.0887 1.2857 1.1560 0.1413  0.0298  -0.1444 134 THR D CB  
8836  O OG1 . THR D 70  ? 1.2952 1.4871 1.3668 0.1366  0.0149  -0.1474 134 THR D OG1 
8837  C CG2 . THR D 70  ? 1.3641 1.5322 1.3978 0.1474  0.0290  -0.1413 134 THR D CG2 
8838  N N   . THR D 71  ? 1.0193 1.2490 1.1504 0.1062  0.0334  -0.1427 135 THR D N   
8839  C CA  . THR D 71  ? 1.2273 1.4763 1.3888 0.0986  0.0266  -0.1482 135 THR D CA  
8840  C C   . THR D 71  ? 1.2228 1.4885 1.4129 0.0866  0.0389  -0.1451 135 THR D C   
8841  O O   . THR D 71  ? 1.2421 1.4937 1.4242 0.0782  0.0469  -0.1377 135 THR D O   
8842  C CB  . THR D 71  ? 1.1210 1.3543 1.2740 0.0933  0.0120  -0.1499 135 THR D CB  
8843  O OG1 . THR D 71  ? 0.9556 1.1758 1.0869 0.1039  0.0012  -0.1519 135 THR D OG1 
8844  C CG2 . THR D 71  ? 0.8514 1.1038 1.0345 0.0866  0.0044  -0.1565 135 THR D CG2 
8845  N N   . ASN D 72  ? 1.2165 1.5115 1.4406 0.0861  0.0403  -0.1505 136 ASN D N   
8846  C CA  . ASN D 72  ? 1.2845 1.5980 1.5440 0.0731  0.0498  -0.1484 136 ASN D CA  
8847  C C   . ASN D 72  ? 1.4099 1.7285 1.6925 0.0633  0.0353  -0.1557 136 ASN D C   
8848  O O   . ASN D 72  ? 1.7703 2.0929 2.0527 0.0702  0.0198  -0.1647 136 ASN D O   
8849  C CB  . ASN D 72  ? 1.3111 1.6560 1.5987 0.0779  0.0614  -0.1498 136 ASN D CB  
8850  C CG  . ASN D 72  ? 1.6146 1.9754 1.9358 0.0641  0.0773  -0.1432 136 ASN D CG  
8851  O OD1 . ASN D 72  ? 2.4565 2.7997 2.7711 0.0530  0.0832  -0.1352 136 ASN D OD1 
8852  N ND2 . ASN D 72  ? 1.5961 1.9902 1.9549 0.0646  0.0843  -0.1462 136 ASN D ND2 
8853  N N   . PHE D 73  ? 1.2629 1.5797 1.5633 0.0484  0.0402  -0.1518 137 PHE D N   
8854  C CA  . PHE D 73  ? 1.1885 1.5062 1.5088 0.0389  0.0260  -0.1589 137 PHE D CA  
8855  C C   . PHE D 73  ? 1.3387 1.6849 1.6950 0.0411  0.0147  -0.1713 137 PHE D C   
8856  O O   . PHE D 73  ? 1.4708 1.8144 1.8264 0.0435  -0.0031 -0.1803 137 PHE D O   
8857  C CB  . PHE D 73  ? 1.2872 1.5982 1.6236 0.0224  0.0346  -0.1520 137 PHE D CB  
8858  C CG  . PHE D 73  ? 1.7367 2.0455 2.0912 0.0135  0.0187  -0.1600 137 PHE D CG  
8859  C CD1 . PHE D 73  ? 2.1854 2.4713 2.5112 0.0162  0.0050  -0.1626 137 PHE D CD1 
8860  C CD2 . PHE D 73  ? 1.7392 2.0695 2.1407 0.0032  0.0169  -0.1654 137 PHE D CD2 
8861  C CE1 . PHE D 73  ? 2.2711 2.5545 2.6107 0.0104  -0.0102 -0.1708 137 PHE D CE1 
8862  C CE2 . PHE D 73  ? 1.6218 1.9484 2.0391 -0.0036 0.0001  -0.1745 137 PHE D CE2 
8863  C CZ  . PHE D 73  ? 1.9794 2.2822 2.3638 0.0009  -0.0135 -0.1773 137 PHE D CZ  
8864  N N   . ALA D 74  ? 1.7000 2.0738 2.0874 0.0413  0.0250  -0.1718 138 ALA D N   
8865  C CA  . ALA D 74  ? 1.8179 2.2225 2.2451 0.0434  0.0150  -0.1842 138 ALA D CA  
8866  C C   . ALA D 74  ? 1.8576 2.2637 2.2678 0.0599  -0.0025 -0.1949 138 ALA D C   
8867  O O   . ALA D 74  ? 1.8416 2.2638 2.2755 0.0623  -0.0178 -0.2071 138 ALA D O   
8868  C CB  . ALA D 74  ? 1.6462 2.0809 2.1072 0.0423  0.0319  -0.1813 138 ALA D CB  
8869  N N   . ASP D 75  ? 1.9713 2.3596 2.3405 0.0715  -0.0006 -0.1901 139 ASP D N   
8870  C CA  . ASP D 75  ? 2.0013 2.3838 2.3479 0.0866  -0.0159 -0.1971 139 ASP D CA  
8871  C C   . ASP D 75  ? 2.1962 2.5593 2.5262 0.0848  -0.0312 -0.2000 139 ASP D C   
8872  O O   . ASP D 75  ? 2.9270 3.2689 3.2412 0.0758  -0.0280 -0.1930 139 ASP D O   
8873  C CB  . ASP D 75  ? 1.9763 2.3410 2.2842 0.0977  -0.0096 -0.1900 139 ASP D CB  
8874  C CG  . ASP D 75  ? 2.3326 2.7160 2.6504 0.1050  0.0032  -0.1888 139 ASP D CG  
8875  O OD1 . ASP D 75  ? 2.6261 3.0399 2.9817 0.1041  0.0051  -0.1949 139 ASP D OD1 
8876  O OD2 . ASP D 75  ? 2.5017 2.8696 2.7898 0.1124  0.0107  -0.1824 139 ASP D OD2 
8877  N N   . LEU D 76  ? 1.9903 2.3610 2.3229 0.0949  -0.0477 -0.2104 140 LEU D N   
8878  C CA  . LEU D 76  ? 1.9489 2.2992 2.2543 0.0996  -0.0609 -0.2115 140 LEU D CA  
8879  C C   . LEU D 76  ? 1.6719 2.0117 1.9458 0.1147  -0.0623 -0.2085 140 LEU D C   
8880  O O   . LEU D 76  ? 1.4160 1.7717 1.6982 0.1251  -0.0634 -0.2134 140 LEU D O   
8881  C CB  . LEU D 76  ? 2.0796 2.4430 2.4057 0.1023  -0.0786 -0.2247 140 LEU D CB  
8882  C CG  . LEU D 76  ? 2.1035 2.4665 2.4514 0.0880  -0.0824 -0.2279 140 LEU D CG  
8883  C CD1 . LEU D 76  ? 2.1876 2.5706 2.5780 0.0740  -0.0717 -0.2280 140 LEU D CD1 
8884  C CD2 . LEU D 76  ? 1.7227 2.0905 2.0771 0.0954  -0.1035 -0.2414 140 LEU D CD2 
8885  N N   . ILE D 77  ? 1.5833 1.8963 1.8228 0.1156  -0.0619 -0.2003 141 ILE D N   
8886  C CA  . ILE D 77  ? 1.3857 1.6850 1.5957 0.1286  -0.0640 -0.1964 141 ILE D CA  
8887  C C   . ILE D 77  ? 1.3768 1.6695 1.5715 0.1393  -0.0785 -0.1997 141 ILE D C   
8888  O O   . ILE D 77  ? 1.6848 1.9762 1.8818 0.1363  -0.0861 -0.2029 141 ILE D O   
8889  C CB  . ILE D 77  ? 1.3859 1.6604 1.5690 0.1247  -0.0545 -0.1849 141 ILE D CB  
8890  C CG1 . ILE D 77  ? 1.3666 1.6301 1.5269 0.1378  -0.0560 -0.1820 141 ILE D CG1 
8891  C CG2 . ILE D 77  ? 1.6400 1.8951 1.8073 0.1177  -0.0577 -0.1800 141 ILE D CG2 
8892  C CD1 . ILE D 77  ? 1.0692 1.3178 1.2134 0.1368  -0.0455 -0.1747 141 ILE D CD1 
8893  N N   . VAL D 78  ? 1.1318 1.4188 1.3088 0.1528  -0.0818 -0.1985 142 VAL D N   
8894  C CA  . VAL D 78  ? 0.9587 1.2467 1.1267 0.1666  -0.0949 -0.2034 142 VAL D CA  
8895  C C   . VAL D 78  ? 0.7817 1.0444 0.9157 0.1740  -0.0957 -0.1934 142 VAL D C   
8896  O O   . VAL D 78  ? 0.8091 1.0584 0.9308 0.1730  -0.0884 -0.1861 142 VAL D O   
8897  C CB  . VAL D 78  ? 0.9283 1.2384 1.1138 0.1779  -0.0998 -0.2132 142 VAL D CB  
8898  C CG1 . VAL D 78  ? 0.9316 1.2396 1.1118 0.1816  -0.0906 -0.2091 142 VAL D CG1 
8899  C CG2 . VAL D 78  ? 1.2243 1.5337 1.3973 0.1944  -0.1139 -0.2183 142 VAL D CG2 
8900  N N   . SER D 79  ? 0.7675 1.0238 0.8874 0.1821  -0.1048 -0.1932 143 SER D N   
8901  C CA  . SER D 79  ? 0.7712 1.0036 0.8612 0.1872  -0.1044 -0.1819 143 SER D CA  
8902  C C   . SER D 79  ? 0.7655 0.9852 0.8407 0.1953  -0.1021 -0.1758 143 SER D C   
8903  O O   . SER D 79  ? 0.8645 1.0628 0.9216 0.1931  -0.0980 -0.1647 143 SER D O   
8904  C CB  . SER D 79  ? 0.7089 0.9409 0.7868 0.1990  -0.1145 -0.1837 143 SER D CB  
8905  O OG  . SER D 79  ? 0.8342 1.0760 0.9242 0.1930  -0.1186 -0.1905 143 SER D OG  
8906  N N   . GLU D 80  ? 0.8782 1.1110 0.9625 0.2049  -0.1056 -0.1834 144 GLU D N   
8907  C CA  . GLU D 80  ? 0.9529 1.1730 1.0225 0.2147  -0.1052 -0.1791 144 GLU D CA  
8908  C C   . GLU D 80  ? 0.8529 1.0617 0.9207 0.2058  -0.0958 -0.1736 144 GLU D C   
8909  O O   . GLU D 80  ? 0.9420 1.1328 0.9938 0.2117  -0.0958 -0.1680 144 GLU D O   
8910  C CB  . GLU D 80  ? 1.0350 1.2733 1.1150 0.2288  -0.1120 -0.1899 144 GLU D CB  
8911  C CG  . GLU D 80  ? 1.3860 1.6295 1.4597 0.2431  -0.1239 -0.1948 144 GLU D CG  
8912  C CD  . GLU D 80  ? 1.3383 1.5987 1.4282 0.2378  -0.1287 -0.2027 144 GLU D CD  
8913  O OE1 . GLU D 80  ? 1.3742 1.6485 1.4878 0.2240  -0.1236 -0.2071 144 GLU D OE1 
8914  O OE2 . GLU D 80  ? 1.4077 1.6660 1.4856 0.2483  -0.1377 -0.2043 144 GLU D OE2 
8915  N N   . GLN D 81  ? 0.6958 0.9133 0.7786 0.1923  -0.0884 -0.1753 145 GLN D N   
8916  C CA  . GLN D 81  ? 0.6630 0.8725 0.7442 0.1855  -0.0793 -0.1718 145 GLN D CA  
8917  C C   . GLN D 81  ? 0.6818 0.8685 0.7483 0.1755  -0.0760 -0.1619 145 GLN D C   
8918  O O   . GLN D 81  ? 0.9648 1.1397 1.0254 0.1705  -0.0703 -0.1583 145 GLN D O   
8919  C CB  . GLN D 81  ? 0.6662 0.8977 0.7714 0.1775  -0.0717 -0.1780 145 GLN D CB  
8920  C CG  . GLN D 81  ? 0.9902 1.2480 1.1153 0.1869  -0.0735 -0.1882 145 GLN D CG  
8921  C CD  . GLN D 81  ? 1.1935 1.4714 1.3421 0.1792  -0.0625 -0.1914 145 GLN D CD  
8922  O OE1 . GLN D 81  ? 1.3126 1.6026 1.4805 0.1676  -0.0592 -0.1930 145 GLN D OE1 
8923  N NE2 . GLN D 81  ? 1.3931 1.6742 1.5397 0.1865  -0.0566 -0.1921 145 GLN D NE2 
8924  N N   . MET D 82  ? 0.6717 0.8525 0.7317 0.1742  -0.0802 -0.1579 146 MET D N   
8925  C CA  . MET D 82  ? 0.6561 0.8214 0.7079 0.1636  -0.0769 -0.1500 146 MET D CA  
8926  C C   . MET D 82  ? 0.6559 0.7973 0.6895 0.1668  -0.0784 -0.1403 146 MET D C   
8927  O O   . MET D 82  ? 0.7951 0.9315 0.8200 0.1778  -0.0834 -0.1382 146 MET D O   
8928  C CB  . MET D 82  ? 0.7129 0.8857 0.7680 0.1610  -0.0802 -0.1509 146 MET D CB  
8929  C CG  . MET D 82  ? 0.7108 0.9032 0.7864 0.1536  -0.0789 -0.1595 146 MET D CG  
8930  S SD  . MET D 82  ? 0.8207 1.0209 0.8994 0.1534  -0.0861 -0.1632 146 MET D SD  
8931  C CE  . MET D 82  ? 0.8880 1.1050 0.9937 0.1403  -0.0824 -0.1715 146 MET D CE  
8932  N N   . ASN D 83  ? 0.6310 0.7574 0.6597 0.1572  -0.0744 -0.1344 147 ASN D N   
8933  C CA  . ASN D 83  ? 0.6741 0.7770 0.6902 0.1573  -0.0758 -0.1252 147 ASN D CA  
8934  C C   . ASN D 83  ? 0.6630 0.7582 0.6776 0.1474  -0.0737 -0.1182 147 ASN D C   
8935  O O   . ASN D 83  ? 0.6500 0.7540 0.6711 0.1392  -0.0704 -0.1212 147 ASN D O   
8936  C CB  . ASN D 83  ? 0.7761 0.8668 0.7888 0.1569  -0.0748 -0.1266 147 ASN D CB  
8937  C CG  . ASN D 83  ? 0.7016 0.7954 0.7125 0.1688  -0.0775 -0.1322 147 ASN D CG  
8938  O OD1 . ASN D 83  ? 0.8224 0.9145 0.8291 0.1781  -0.0823 -0.1307 147 ASN D OD1 
8939  N ND2 . ASN D 83  ? 0.8555 0.9537 0.8686 0.1698  -0.0741 -0.1383 147 ASN D ND2 
8940  N N   . VAL D 84  ? 0.6094 0.6881 0.6168 0.1481  -0.0752 -0.1085 148 VAL D N   
8941  C CA  . VAL D 84  ? 0.6009 0.6724 0.6084 0.1393  -0.0730 -0.1009 148 VAL D CA  
8942  C C   . VAL D 84  ? 0.6113 0.6656 0.6193 0.1318  -0.0732 -0.0985 148 VAL D C   
8943  O O   . VAL D 84  ? 0.5737 0.6117 0.5788 0.1343  -0.0765 -0.0945 148 VAL D O   
8944  C CB  . VAL D 84  ? 0.5631 0.6289 0.5653 0.1440  -0.0732 -0.0903 148 VAL D CB  
8945  C CG1 . VAL D 84  ? 0.5446 0.6085 0.5495 0.1357  -0.0697 -0.0833 148 VAL D CG1 
8946  C CG2 . VAL D 84  ? 0.5737 0.6536 0.5715 0.1549  -0.0748 -0.0931 148 VAL D CG2 
8947  N N   . TYR D 85  ? 0.5845 0.6414 0.5958 0.1231  -0.0706 -0.1015 149 TYR D N   
8948  C CA  . TYR D 85  ? 0.5997 0.6412 0.6106 0.1167  -0.0719 -0.1004 149 TYR D CA  
8949  C C   . TYR D 85  ? 0.6696 0.7082 0.6844 0.1090  -0.0709 -0.0941 149 TYR D C   
8950  O O   . TYR D 85  ? 0.7565 0.8072 0.7730 0.1078  -0.0680 -0.0924 149 TYR D O   
8951  C CB  . TYR D 85  ? 0.5668 0.6116 0.5760 0.1142  -0.0695 -0.1087 149 TYR D CB  
8952  C CG  . TYR D 85  ? 0.6920 0.7375 0.6975 0.1220  -0.0700 -0.1146 149 TYR D CG  
8953  C CD1 . TYR D 85  ? 0.8002 0.8282 0.7993 0.1264  -0.0747 -0.1154 149 TYR D CD1 
8954  C CD2 . TYR D 85  ? 0.6512 0.7156 0.6610 0.1257  -0.0663 -0.1203 149 TYR D CD2 
8955  C CE1 . TYR D 85  ? 0.7649 0.7941 0.7591 0.1355  -0.0750 -0.1214 149 TYR D CE1 
8956  C CE2 . TYR D 85  ? 0.6427 0.7106 0.6508 0.1337  -0.0658 -0.1258 149 TYR D CE2 
8957  C CZ  . TYR D 85  ? 0.7247 0.7750 0.7236 0.1391  -0.0698 -0.1262 149 TYR D CZ  
8958  O OH  . TYR D 85  ? 0.7817 0.8362 0.7777 0.1488  -0.0693 -0.1320 149 TYR D OH  
8959  N N   . SER D 86  ? 0.6738 0.6964 0.6903 0.1048  -0.0744 -0.0918 150 SER D N   
8960  C CA  . SER D 86  ? 0.6739 0.6930 0.6966 0.0973  -0.0744 -0.0868 150 SER D CA  
8961  C C   . SER D 86  ? 0.5882 0.5987 0.6085 0.0929  -0.0771 -0.0932 150 SER D C   
8962  O O   . SER D 86  ? 0.7607 0.7642 0.7741 0.0964  -0.0793 -0.0995 150 SER D O   
8963  C CB  . SER D 86  ? 0.7266 0.7340 0.7571 0.0965  -0.0771 -0.0772 150 SER D CB  
8964  O OG  . SER D 86  ? 1.1057 1.1114 1.1458 0.0892  -0.0772 -0.0724 150 SER D OG  
8965  N N   . VAL D 87  ? 0.6182 0.6289 0.6426 0.0867  -0.0770 -0.0918 151 VAL D N   
8966  C CA  . VAL D 87  ? 0.5078 0.5082 0.5283 0.0838  -0.0807 -0.0976 151 VAL D CA  
8967  C C   . VAL D 87  ? 0.5478 0.5477 0.5788 0.0779  -0.0824 -0.0925 151 VAL D C   
8968  O O   . VAL D 87  ? 0.6642 0.6744 0.7030 0.0767  -0.0785 -0.0851 151 VAL D O   
8969  C CB  . VAL D 87  ? 0.4545 0.4624 0.4653 0.0837  -0.0758 -0.1040 151 VAL D CB  
8970  C CG1 . VAL D 87  ? 0.5264 0.5466 0.5405 0.0794  -0.0718 -0.1020 151 VAL D CG1 
8971  C CG2 . VAL D 87  ? 0.4668 0.4623 0.4693 0.0835  -0.0788 -0.1092 151 VAL D CG2 
8972  N N   . LYS D 88  ? 0.6025 0.5912 0.6340 0.0754  -0.0883 -0.0962 152 LYS D N   
8973  C CA  . LYS D 88  ? 0.6352 0.6263 0.6791 0.0701  -0.0899 -0.0921 152 LYS D CA  
8974  C C   . LYS D 88  ? 0.5851 0.5870 0.6222 0.0687  -0.0850 -0.0945 152 LYS D C   
8975  O O   . LYS D 88  ? 0.6051 0.6030 0.6289 0.0700  -0.0846 -0.1012 152 LYS D O   
8976  C CB  . LYS D 88  ? 0.7097 0.6848 0.7587 0.0686  -0.1002 -0.0962 152 LYS D CB  
8977  C CG  . LYS D 88  ? 0.8601 0.8390 0.9297 0.0628  -0.1028 -0.0906 152 LYS D CG  
8978  C CD  . LYS D 88  ? 0.9386 0.9059 1.0105 0.0619  -0.1132 -0.0982 152 LYS D CD  
8979  C CE  . LYS D 88  ? 1.0851 1.0579 1.1445 0.0625  -0.1106 -0.1029 152 LYS D CE  
8980  N NZ  . LYS D 88  ? 1.0541 1.0134 1.1102 0.0642  -0.1213 -0.1113 152 LYS D NZ  
8981  N N   . LEU D 89  ? 0.5557 0.5708 0.6009 0.0667  -0.0807 -0.0886 153 LEU D N   
8982  C CA  . LEU D 89  ? 0.5526 0.5757 0.5911 0.0660  -0.0777 -0.0918 153 LEU D CA  
8983  C C   . LEU D 89  ? 0.6618 0.6735 0.6957 0.0642  -0.0835 -0.0980 153 LEU D C   
8984  O O   . LEU D 89  ? 0.5974 0.6034 0.6416 0.0624  -0.0894 -0.0972 153 LEU D O   
8985  C CB  . LEU D 89  ? 0.5705 0.6080 0.6178 0.0659  -0.0737 -0.0851 153 LEU D CB  
8986  C CG  . LEU D 89  ? 0.5029 0.5473 0.5430 0.0661  -0.0722 -0.0892 153 LEU D CG  
8987  C CD1 . LEU D 89  ? 0.4318 0.4788 0.4594 0.0678  -0.0696 -0.0949 153 LEU D CD1 
8988  C CD2 . LEU D 89  ? 0.4387 0.4974 0.4867 0.0682  -0.0683 -0.0826 153 LEU D CD2 
8989  N N   . GLY D 90  ? 0.7114 0.7196 0.7305 0.0651  -0.0818 -0.1040 154 GLY D N   
8990  C CA  . GLY D 90  ? 0.6972 0.6924 0.7067 0.0654  -0.0866 -0.1097 154 GLY D CA  
8991  C C   . GLY D 90  ? 0.8445 0.8271 0.8402 0.0688  -0.0871 -0.1144 154 GLY D C   
8992  O O   . GLY D 90  ? 0.9778 0.9491 0.9595 0.0708  -0.0885 -0.1189 154 GLY D O   
8993  N N   . ASP D 91  ? 0.9572 0.9414 0.9555 0.0708  -0.0856 -0.1129 155 ASP D N   
8994  C CA  . ASP D 91  ? 0.9216 0.8960 0.9068 0.0757  -0.0852 -0.1172 155 ASP D CA  
8995  C C   . ASP D 91  ? 0.7562 0.7421 0.7374 0.0758  -0.0758 -0.1169 155 ASP D C   
8996  O O   . ASP D 91  ? 1.0599 1.0602 1.0505 0.0731  -0.0721 -0.1137 155 ASP D O   
8997  C CB  . ASP D 91  ? 1.1659 1.1329 1.1564 0.0790  -0.0912 -0.1170 155 ASP D CB  
8998  C CG  . ASP D 91  ? 1.5486 1.4996 1.5413 0.0802  -0.1027 -0.1203 155 ASP D CG  
8999  O OD1 . ASP D 91  ? 1.4933 1.4367 1.4776 0.0810  -0.1060 -0.1243 155 ASP D OD1 
9000  O OD2 . ASP D 91  ? 1.9687 1.9138 1.9721 0.0807  -0.1092 -0.1191 155 ASP D OD2 
9001  N N   . PRO D 92  ? 0.7022 0.6823 0.6698 0.0792  -0.0719 -0.1203 156 PRO D N   
9002  C CA  . PRO D 92  ? 0.7658 0.7581 0.7335 0.0786  -0.0627 -0.1202 156 PRO D CA  
9003  C C   . PRO D 92  ? 0.8275 0.8248 0.7984 0.0835  -0.0617 -0.1206 156 PRO D C   
9004  O O   . PRO D 92  ? 1.0060 0.9919 0.9717 0.0890  -0.0672 -0.1223 156 PRO D O   
9005  C CB  . PRO D 92  ? 0.7957 0.7781 0.7475 0.0805  -0.0579 -0.1221 156 PRO D CB  
9006  C CG  . PRO D 92  ? 0.9867 0.9509 0.9262 0.0868  -0.0655 -0.1249 156 PRO D CG  
9007  C CD  . PRO D 92  ? 0.9495 0.9120 0.9007 0.0837  -0.0751 -0.1241 156 PRO D CD  
9008  N N   . PRO D 93  ? 0.7545 0.7685 0.7343 0.0824  -0.0561 -0.1201 157 PRO D N   
9009  C CA  . PRO D 93  ? 0.7722 0.7923 0.7549 0.0882  -0.0553 -0.1211 157 PRO D CA  
9010  C C   . PRO D 93  ? 0.8563 0.8725 0.8284 0.0945  -0.0504 -0.1243 157 PRO D C   
9011  O O   . PRO D 93  ? 0.7636 0.7939 0.7408 0.0959  -0.0433 -0.1255 157 PRO D O   
9012  C CB  . PRO D 93  ? 0.6627 0.7027 0.6582 0.0856  -0.0513 -0.1208 157 PRO D CB  
9013  C CG  . PRO D 93  ? 0.7174 0.7609 0.7146 0.0788  -0.0480 -0.1208 157 PRO D CG  
9014  C CD  . PRO D 93  ? 0.7573 0.7851 0.7462 0.0766  -0.0526 -0.1191 157 PRO D CD  
9015  N N   . THR D 94  ? 1.0036 1.0018 0.9614 0.0990  -0.0544 -0.1260 158 THR D N   
9016  C CA  . THR D 94  ? 0.9713 0.9636 0.9157 0.1085  -0.0513 -0.1292 158 THR D CA  
9017  C C   . THR D 94  ? 0.7922 0.7837 0.7393 0.1155  -0.0572 -0.1312 158 THR D C   
9018  O O   . THR D 94  ? 0.8459 0.8338 0.8014 0.1132  -0.0652 -0.1296 158 THR D O   
9019  C CB  . THR D 94  ? 1.0037 0.9747 0.9281 0.1137  -0.0553 -0.1316 158 THR D CB  
9020  O OG1 . THR D 94  ? 1.1323 1.0901 1.0593 0.1117  -0.0678 -0.1324 158 THR D OG1 
9021  C CG2 . THR D 94  ? 1.0662 1.0371 0.9828 0.1098  -0.0465 -0.1293 158 THR D CG2 
9022  N N   . PRO D 95  ? 0.8483 0.8429 0.7883 0.1246  -0.0526 -0.1342 159 PRO D N   
9023  C CA  . PRO D 95  ? 0.9529 0.9447 0.8927 0.1334  -0.0586 -0.1370 159 PRO D CA  
9024  C C   . PRO D 95  ? 0.9644 0.9334 0.8986 0.1366  -0.0726 -0.1388 159 PRO D C   
9025  O O   . PRO D 95  ? 1.0822 1.0484 1.0242 0.1379  -0.0796 -0.1381 159 PRO D O   
9026  C CB  . PRO D 95  ? 0.9479 0.9423 0.8747 0.1444  -0.0510 -0.1406 159 PRO D CB  
9027  C CG  . PRO D 95  ? 0.7896 0.7988 0.7205 0.1379  -0.0377 -0.1375 159 PRO D CG  
9028  C CD  . PRO D 95  ? 0.7720 0.7734 0.7040 0.1276  -0.0405 -0.1344 159 PRO D CD  
9029  N N   . ASP D 96  ? 0.9146 0.8670 0.8362 0.1379  -0.0771 -0.1410 160 ASP D N   
9030  C CA  . ASP D 96  ? 1.0677 0.9980 0.9868 0.1403  -0.0920 -0.1440 160 ASP D CA  
9031  C C   . ASP D 96  ? 1.0195 0.9494 0.9573 0.1285  -0.0981 -0.1388 160 ASP D C   
9032  O O   . ASP D 96  ? 0.9939 0.9101 0.9387 0.1286  -0.1096 -0.1393 160 ASP D O   
9033  C CB  . ASP D 96  ? 1.2146 1.1279 1.1135 0.1473  -0.0958 -0.1493 160 ASP D CB  
9034  C CG  . ASP D 96  ? 1.6274 1.5435 1.5064 0.1591  -0.0861 -0.1522 160 ASP D CG  
9035  O OD1 . ASP D 96  ? 1.5690 1.4953 1.4496 0.1648  -0.0812 -0.1528 160 ASP D OD1 
9036  O OD2 . ASP D 96  ? 2.5618 2.4702 2.4231 0.1634  -0.0829 -0.1536 160 ASP D OD2 
9037  N N   . LYS D 97  ? 0.8719 0.8168 0.8186 0.1189  -0.0902 -0.1338 161 LYS D N   
9038  C CA  . LYS D 97  ? 0.7881 0.7359 0.7515 0.1092  -0.0936 -0.1282 161 LYS D CA  
9039  C C   . LYS D 97  ? 0.8097 0.7689 0.7868 0.1069  -0.0916 -0.1227 161 LYS D C   
9040  O O   . LYS D 97  ? 0.9971 0.9546 0.9875 0.1016  -0.0958 -0.1173 161 LYS D O   
9041  C CB  . LYS D 97  ? 0.7037 0.6606 0.6683 0.1017  -0.0874 -0.1260 161 LYS D CB  
9042  C CG  . LYS D 97  ? 0.9003 0.8425 0.8534 0.1031  -0.0923 -0.1301 161 LYS D CG  
9043  C CD  . LYS D 97  ? 1.0022 0.9280 0.9614 0.1038  -0.1062 -0.1322 161 LYS D CD  
9044  C CE  . LYS D 97  ? 1.1950 1.1089 1.1461 0.1043  -0.1124 -0.1363 161 LYS D CE  
9045  N NZ  . LYS D 97  ? 1.4689 1.3669 1.4284 0.1056  -0.1276 -0.1400 161 LYS D NZ  
9046  N N   . LEU D 98  ? 0.7574 0.7286 0.7318 0.1115  -0.0849 -0.1237 162 LEU D N   
9047  C CA  . LEU D 98  ? 0.7058 0.6886 0.6903 0.1116  -0.0829 -0.1193 162 LEU D CA  
9048  C C   . LEU D 98  ? 0.6804 0.6500 0.6694 0.1146  -0.0913 -0.1164 162 LEU D C   
9049  O O   . LEU D 98  ? 1.0923 1.0459 1.0742 0.1209  -0.0983 -0.1209 162 LEU D O   
9050  C CB  . LEU D 98  ? 0.6965 0.6940 0.6778 0.1175  -0.0760 -0.1228 162 LEU D CB  
9051  C CG  . LEU D 98  ? 0.7935 0.8076 0.7765 0.1127  -0.0666 -0.1240 162 LEU D CG  
9052  C CD1 . LEU D 98  ? 0.8171 0.8510 0.8074 0.1157  -0.0613 -0.1254 162 LEU D CD1 
9053  C CD2 . LEU D 98  ? 0.9323 0.9497 0.9219 0.1032  -0.0661 -0.1198 162 LEU D CD2 
9054  N N   . LYS D 99  ? 0.5877 0.5624 0.5877 0.1106  -0.0907 -0.1087 163 LYS D N   
9055  C CA  . LYS D 99  ? 0.6395 0.6033 0.6445 0.1136  -0.0964 -0.1038 163 LYS D CA  
9056  C C   . LYS D 99  ? 0.6826 0.6606 0.6877 0.1181  -0.0911 -0.1005 163 LYS D C   
9057  O O   . LYS D 99  ? 0.6864 0.6788 0.6963 0.1147  -0.0854 -0.0957 163 LYS D O   
9058  C CB  . LYS D 99  ? 0.7846 0.7405 0.8031 0.1056  -0.0997 -0.0955 163 LYS D CB  
9059  C CG  . LYS D 99  ? 0.9540 0.9006 0.9801 0.1070  -0.1027 -0.0870 163 LYS D CG  
9060  C CD  . LYS D 99  ? 1.2393 1.1736 1.2818 0.0988  -0.1078 -0.0802 163 LYS D CD  
9061  C CE  . LYS D 99  ? 1.3627 1.2973 1.4161 0.0968  -0.1039 -0.0664 163 LYS D CE  
9062  N NZ  . LYS D 99  ? 2.2320 2.1466 2.2867 0.1013  -0.1112 -0.0640 163 LYS D NZ  
9063  N N   . PHE D 100 ? 0.7910 0.7649 0.7897 0.1275  -0.0938 -0.1042 164 PHE D N   
9064  C CA  . PHE D 100 ? 0.7196 0.7051 0.7176 0.1340  -0.0909 -0.1021 164 PHE D CA  
9065  C C   . PHE D 100 ? 0.6978 0.6778 0.7019 0.1319  -0.0915 -0.0906 164 PHE D C   
9066  O O   . PHE D 100 ? 0.6720 0.6329 0.6803 0.1299  -0.0970 -0.0851 164 PHE D O   
9067  C CB  . PHE D 100 ? 0.7004 0.6790 0.6905 0.1453  -0.0953 -0.1080 164 PHE D CB  
9068  C CG  . PHE D 100 ? 0.6660 0.6586 0.6546 0.1537  -0.0930 -0.1085 164 PHE D CG  
9069  C CD1 . PHE D 100 ? 0.6703 0.6564 0.6591 0.1572  -0.0954 -0.1002 164 PHE D CD1 
9070  C CD2 . PHE D 100 ? 0.6309 0.6434 0.6185 0.1588  -0.0884 -0.1172 164 PHE D CD2 
9071  C CE1 . PHE D 100 ? 0.5952 0.5937 0.5806 0.1670  -0.0945 -0.1015 164 PHE D CE1 
9072  C CE2 . PHE D 100 ? 0.5672 0.5939 0.5555 0.1674  -0.0879 -0.1192 164 PHE D CE2 
9073  C CZ  . PHE D 100 ? 0.5568 0.5761 0.5427 0.1721  -0.0916 -0.1118 164 PHE D CZ  
9074  N N   . GLU D 101 ? 0.7778 0.7743 0.7827 0.1328  -0.0859 -0.0868 165 GLU D N   
9075  C CA  . GLU D 101 ? 0.7603 0.7536 0.7686 0.1319  -0.0840 -0.0745 165 GLU D CA  
9076  C C   . GLU D 101 ? 0.6907 0.6845 0.6917 0.1431  -0.0846 -0.0712 165 GLU D C   
9077  O O   . GLU D 101 ? 0.6839 0.6629 0.6851 0.1450  -0.0859 -0.0611 165 GLU D O   
9078  C CB  . GLU D 101 ? 0.6822 0.6903 0.6948 0.1256  -0.0778 -0.0708 165 GLU D CB  
9079  C CG  . GLU D 101 ? 0.9739 0.9753 0.9955 0.1146  -0.0782 -0.0689 165 GLU D CG  
9080  C CD  . GLU D 101 ? 1.2129 1.1977 1.2449 0.1100  -0.0803 -0.0576 165 GLU D CD  
9081  O OE1 . GLU D 101 ? 1.5268 1.5013 1.5578 0.1151  -0.0817 -0.0508 165 GLU D OE1 
9082  O OE2 . GLU D 101 ? 1.0870 1.0689 1.1295 0.1013  -0.0809 -0.0555 165 GLU D OE2 
9083  N N   . ALA D 102 ? 0.6485 0.6590 0.6442 0.1505  -0.0837 -0.0797 166 ALA D N   
9084  C CA  . ALA D 102 ? 0.6077 0.6215 0.5956 0.1632  -0.0856 -0.0799 166 ALA D CA  
9085  C C   . ALA D 102 ? 0.6347 0.6708 0.6226 0.1690  -0.0854 -0.0925 166 ALA D C   
9086  O O   . ALA D 102 ? 0.6161 0.6646 0.6104 0.1621  -0.0825 -0.0996 166 ALA D O   
9087  C CB  . ALA D 102 ? 0.5813 0.5955 0.5648 0.1668  -0.0824 -0.0681 166 ALA D CB  
9088  N N   . VAL D 103 ? 0.6305 0.6713 0.6124 0.1817  -0.0885 -0.0950 167 VAL D N   
9089  C CA  . VAL D 103 ? 0.6397 0.7037 0.6256 0.1877  -0.0892 -0.1070 167 VAL D CA  
9090  C C   . VAL D 103 ? 0.6607 0.7383 0.6450 0.1918  -0.0889 -0.1057 167 VAL D C   
9091  O O   . VAL D 103 ? 0.8125 0.8816 0.7861 0.2001  -0.0904 -0.0975 167 VAL D O   
9092  C CB  . VAL D 103 ? 0.6428 0.7069 0.6243 0.2014  -0.0945 -0.1129 167 VAL D CB  
9093  C CG1 . VAL D 103 ? 0.9391 0.9931 0.9210 0.2004  -0.0955 -0.1172 167 VAL D CG1 
9094  C CG2 . VAL D 103 ? 0.7779 0.8255 0.7468 0.2110  -0.0981 -0.1035 167 VAL D CG2 
9095  N N   . GLY D 104 ? 0.6025 0.6997 0.5963 0.1867  -0.0872 -0.1134 168 GLY D N   
9096  C CA  . GLY D 104 ? 0.5916 0.7016 0.5836 0.1910  -0.0885 -0.1141 168 GLY D CA  
9097  C C   . GLY D 104 ? 0.5736 0.7008 0.5784 0.1821  -0.0869 -0.1222 168 GLY D C   
9098  O O   . GLY D 104 ? 0.7482 0.8756 0.7618 0.1712  -0.0831 -0.1248 168 GLY D O   
9099  N N   . TRP D 105 ? 0.5162 0.6564 0.5209 0.1873  -0.0904 -0.1263 169 TRP D N   
9100  C CA  . TRP D 105 ? 0.5195 0.6748 0.5377 0.1792  -0.0905 -0.1349 169 TRP D CA  
9101  C C   . TRP D 105 ? 0.5576 0.7097 0.5676 0.1780  -0.0898 -0.1293 169 TRP D C   
9102  O O   . TRP D 105 ? 0.7322 0.8943 0.7504 0.1728  -0.0912 -0.1358 169 TRP D O   
9103  C CB  . TRP D 105 ? 0.5491 0.7251 0.5788 0.1868  -0.0977 -0.1482 169 TRP D CB  
9104  C CG  . TRP D 105 ? 0.5886 0.7666 0.6050 0.2035  -0.1052 -0.1487 169 TRP D CG  
9105  C CD1 . TRP D 105 ? 0.5983 0.7769 0.6042 0.2093  -0.1085 -0.1474 169 TRP D CD1 
9106  C CD2 . TRP D 105 ? 0.6738 0.8522 0.6827 0.2191  -0.1108 -0.1506 169 TRP D CD2 
9107  N NE1 . TRP D 105 ? 0.6456 0.8248 0.6372 0.2273  -0.1152 -0.1480 169 TRP D NE1 
9108  C CE2 . TRP D 105 ? 0.6955 0.8742 0.6883 0.2338  -0.1171 -0.1498 169 TRP D CE2 
9109  C CE3 . TRP D 105 ? 0.7753 0.9539 0.7877 0.2237  -0.1116 -0.1533 169 TRP D CE3 
9110  C CZ2 . TRP D 105 ? 0.8103 0.9882 0.7905 0.2521  -0.1240 -0.1513 169 TRP D CZ2 
9111  C CZ3 . TRP D 105 ? 0.8514 1.0298 0.8526 0.2417  -0.1189 -0.1552 169 TRP D CZ3 
9112  C CH2 . TRP D 105 ? 0.8420 1.0195 0.8271 0.2554  -0.1250 -0.1539 169 TRP D CH2 
9113  N N   . SER D 106 ? 0.5331 0.6714 0.5275 0.1835  -0.0875 -0.1172 170 SER D N   
9114  C CA  . SER D 106 ? 0.6378 0.7730 0.6243 0.1823  -0.0845 -0.1098 170 SER D CA  
9115  C C   . SER D 106 ? 0.6663 0.7840 0.6435 0.1812  -0.0782 -0.0939 170 SER D C   
9116  O O   . SER D 106 ? 0.6487 0.7568 0.6182 0.1888  -0.0784 -0.0877 170 SER D O   
9117  C CB  . SER D 106 ? 0.6926 0.8382 0.6696 0.1964  -0.0904 -0.1143 170 SER D CB  
9118  O OG  . SER D 106 ? 0.9532 1.0944 0.9175 0.1996  -0.0864 -0.1047 170 SER D OG  
9119  N N   . ALA D 107 ? 0.6947 0.8083 0.6736 0.1721  -0.0729 -0.0873 171 ALA D N   
9120  C CA  . ALA D 107 ? 0.7053 0.8034 0.6827 0.1672  -0.0667 -0.0726 171 ALA D CA  
9121  C C   . ALA D 107 ? 0.6841 0.7831 0.6605 0.1636  -0.0611 -0.0643 171 ALA D C   
9122  O O   . ALA D 107 ? 0.7496 0.8582 0.7286 0.1602  -0.0619 -0.0709 171 ALA D O   
9123  C CB  . ALA D 107 ? 0.6168 0.7049 0.6047 0.1556  -0.0665 -0.0740 171 ALA D CB  
9124  N N   . SER D 108 ? 0.6908 0.7793 0.6647 0.1642  -0.0552 -0.0493 172 SER D N   
9125  C CA  . SER D 108 ? 0.6830 0.7724 0.6593 0.1602  -0.0484 -0.0393 172 SER D CA  
9126  C C   . SER D 108 ? 0.7770 0.8511 0.7635 0.1519  -0.0440 -0.0263 172 SER D C   
9127  O O   . SER D 108 ? 0.9155 0.9775 0.9006 0.1544  -0.0455 -0.0222 172 SER D O   
9128  C CB  . SER D 108 ? 0.6547 0.7514 0.6152 0.1748  -0.0446 -0.0324 172 SER D CB  
9129  O OG  . SER D 108 ? 0.8909 0.9857 0.8543 0.1726  -0.0351 -0.0171 172 SER D OG  
9130  N N   . SER D 109 ? 0.7473 0.8215 0.7453 0.1422  -0.0396 -0.0206 173 SER D N   
9131  C CA  . SER D 109 ? 0.7567 0.8168 0.7692 0.1329  -0.0371 -0.0096 173 SER D CA  
9132  C C   . SER D 109 ? 0.6886 0.7532 0.7136 0.1265  -0.0299 0.0009  173 SER D C   
9133  O O   . SER D 109 ? 0.6280 0.7056 0.6517 0.1266  -0.0281 -0.0031 173 SER D O   
9134  C CB  . SER D 109 ? 0.7657 0.8155 0.7878 0.1230  -0.0449 -0.0199 173 SER D CB  
9135  O OG  . SER D 109 ? 0.9538 1.0101 0.9829 0.1147  -0.0463 -0.0276 173 SER D OG  
9136  N N   . CYS D 110 ? 0.6448 0.6982 0.6833 0.1210  -0.0262 0.0143  174 CYS D N   
9137  C CA  . CYS D 110 ? 0.7588 0.8176 0.8134 0.1149  -0.0184 0.0261  174 CYS D CA  
9138  C C   . CYS D 110 ? 0.8452 0.8877 0.9215 0.1047  -0.0192 0.0357  174 CYS D C   
9139  O O   . CYS D 110 ? 0.7635 0.7905 0.8369 0.1065  -0.0224 0.0387  174 CYS D O   
9140  C CB  . CYS D 110 ? 0.7858 0.8567 0.8294 0.1265  -0.0066 0.0393  174 CYS D CB  
9141  S SG  . CYS D 110 ? 1.2302 1.2936 1.2512 0.1423  -0.0031 0.0484  174 CYS D SG  
9142  N N   . HIS D 111 ? 0.7979 0.8436 0.8969 0.0941  -0.0177 0.0396  175 HIS D N   
9143  C CA  . HIS D 111 ? 0.8103 0.8406 0.9341 0.0831  -0.0211 0.0463  175 HIS D CA  
9144  C C   . HIS D 111 ? 0.8998 0.9354 1.0411 0.0811  -0.0084 0.0670  175 HIS D C   
9145  O O   . HIS D 111 ? 1.1877 1.2410 1.3363 0.0806  -0.0007 0.0713  175 HIS D O   
9146  C CB  . HIS D 111 ? 0.7724 0.8007 0.9118 0.0723  -0.0313 0.0333  175 HIS D CB  
9147  C CG  . HIS D 111 ? 0.8071 0.8162 0.9699 0.0622  -0.0397 0.0350  175 HIS D CG  
9148  N ND1 . HIS D 111 ? 0.8609 0.8700 1.0535 0.0534  -0.0359 0.0479  175 HIS D ND1 
9149  C CD2 . HIS D 111 ? 0.7990 0.7879 0.9597 0.0604  -0.0525 0.0247  175 HIS D CD2 
9150  C CE1 . HIS D 111 ? 0.8745 0.8631 1.0843 0.0458  -0.0472 0.0451  175 HIS D CE1 
9151  N NE2 . HIS D 111 ? 0.8669 0.8425 1.0551 0.0509  -0.0575 0.0307  175 HIS D NE2 
9152  N N   . ASP D 112 ? 0.9080 0.9282 1.0565 0.0802  -0.0055 0.0808  176 ASP D N   
9153  C CA  . ASP D 112 ? 0.9969 1.0219 1.1635 0.0782  0.0090  0.1037  176 ASP D CA  
9154  C C   . ASP D 112 ? 0.9900 1.0150 1.1977 0.0623  0.0083  0.1098  176 ASP D C   
9155  O O   . ASP D 112 ? 1.0245 1.0597 1.2512 0.0597  0.0221  0.1284  176 ASP D O   
9156  C CB  . ASP D 112 ? 0.9773 0.9864 1.1337 0.0851  0.0150  0.1192  176 ASP D CB  
9157  C CG  . ASP D 112 ? 1.0571 1.0390 1.2242 0.0777  0.0024  0.1158  176 ASP D CG  
9158  O OD1 . ASP D 112 ? 0.9072 0.8824 1.0899 0.0676  -0.0112 0.1014  176 ASP D OD1 
9159  O OD2 . ASP D 112 ? 1.0576 1.0237 1.2156 0.0835  0.0059  0.1278  176 ASP D OD2 
9160  N N   . GLY D 113 ? 0.8816 0.8960 1.1029 0.0525  -0.0075 0.0942  177 GLY D N   
9161  C CA  . GLY D 113 ? 0.8732 0.8840 1.1351 0.0377  -0.0123 0.0974  177 GLY D CA  
9162  C C   . GLY D 113 ? 0.9093 0.8917 1.1838 0.0308  -0.0260 0.0944  177 GLY D C   
9163  O O   . GLY D 113 ? 0.8395 0.8141 1.1457 0.0190  -0.0359 0.0914  177 GLY D O   
9164  N N   . PHE D 114 ? 1.0792 1.0458 1.3282 0.0393  -0.0278 0.0941  178 PHE D N   
9165  C CA  . PHE D 114 ? 0.9002 0.8382 1.1552 0.0358  -0.0412 0.0905  178 PHE D CA  
9166  C C   . PHE D 114 ? 0.8412 0.7700 1.0657 0.0443  -0.0539 0.0698  178 PHE D C   
9167  O O   . PHE D 114 ? 0.9426 0.8593 1.1733 0.0400  -0.0694 0.0546  178 PHE D O   
9168  C CB  . PHE D 114 ? 0.9293 0.8538 1.1841 0.0387  -0.0317 0.1110  178 PHE D CB  
9169  C CG  . PHE D 114 ? 0.9220 0.8543 1.2090 0.0300  -0.0173 0.1341  178 PHE D CG  
9170  C CD1 . PHE D 114 ? 0.9346 0.8570 1.2647 0.0145  -0.0243 0.1380  178 PHE D CD1 
9171  C CD2 . PHE D 114 ? 0.9058 0.8559 1.1811 0.0380  0.0031  0.1518  178 PHE D CD2 
9172  C CE1 . PHE D 114 ? 1.0607 0.9923 1.4247 0.0056  -0.0098 0.1602  178 PHE D CE1 
9173  C CE2 . PHE D 114 ? 1.0038 0.9627 1.3091 0.0308  0.0186  0.1746  178 PHE D CE2 
9174  C CZ  . PHE D 114 ? 1.0555 1.0059 1.4069 0.0138  0.0128  0.1795  178 PHE D CZ  
9175  N N   . GLN D 115 ? 0.8150 0.7508 1.0070 0.0571  -0.0472 0.0692  179 GLN D N   
9176  C CA  . GLN D 115 ? 0.7879 0.7187 0.9518 0.0659  -0.0570 0.0509  179 GLN D CA  
9177  C C   . GLN D 115 ? 0.7123 0.6664 0.8517 0.0749  -0.0497 0.0445  179 GLN D C   
9178  O O   . GLN D 115 ? 0.8662 0.8375 1.0055 0.0769  -0.0372 0.0552  179 GLN D O   
9179  C CB  . GLN D 115 ? 0.8692 0.7794 1.0198 0.0736  -0.0599 0.0552  179 GLN D CB  
9180  C CG  . GLN D 115 ? 0.9651 0.8473 1.1378 0.0657  -0.0704 0.0589  179 GLN D CG  
9181  C CD  . GLN D 115 ? 0.9427 0.8135 1.1197 0.0621  -0.0881 0.0388  179 GLN D CD  
9182  O OE1 . GLN D 115 ? 1.2169 1.0970 1.3746 0.0676  -0.0922 0.0224  179 GLN D OE1 
9183  N NE2 . GLN D 115 ? 0.9384 0.7887 1.1408 0.0532  -0.0985 0.0403  179 GLN D NE2 
9184  N N   . TRP D 116 ? 0.6279 0.5828 0.7473 0.0807  -0.0574 0.0271  180 TRP D N   
9185  C CA  . TRP D 116 ? 0.6337 0.6078 0.7300 0.0901  -0.0518 0.0211  180 TRP D CA  
9186  C C   . TRP D 116 ? 0.8068 0.7786 0.8835 0.1025  -0.0477 0.0269  180 TRP D C   
9187  O O   . TRP D 116 ? 0.8074 0.7629 0.8774 0.1069  -0.0542 0.0244  180 TRP D O   
9188  C CB  . TRP D 116 ? 0.5802 0.5574 0.6650 0.0912  -0.0604 0.0012  180 TRP D CB  
9189  C CG  . TRP D 116 ? 0.5648 0.5489 0.6602 0.0826  -0.0631 -0.0064 180 TRP D CG  
9190  C CD1 . TRP D 116 ? 0.6016 0.5735 0.7099 0.0749  -0.0729 -0.0138 180 TRP D CD1 
9191  C CD2 . TRP D 116 ? 0.6307 0.6346 0.7237 0.0821  -0.0570 -0.0082 180 TRP D CD2 
9192  N NE1 . TRP D 116 ? 0.5489 0.5317 0.6625 0.0698  -0.0729 -0.0195 180 TRP D NE1 
9193  C CE2 . TRP D 116 ? 0.5725 0.5744 0.6777 0.0734  -0.0634 -0.0163 180 TRP D CE2 
9194  C CE3 . TRP D 116 ? 0.7926 0.8141 0.8738 0.0889  -0.0483 -0.0048 180 TRP D CE3 
9195  C CZ2 . TRP D 116 ? 0.5522 0.5690 0.6575 0.0714  -0.0605 -0.0201 180 TRP D CZ2 
9196  C CZ3 . TRP D 116 ? 0.7253 0.7616 0.8074 0.0866  -0.0459 -0.0091 180 TRP D CZ3 
9197  C CH2 . TRP D 116 ? 0.5999 0.6337 0.6938 0.0778  -0.0516 -0.0163 180 TRP D CH2 
9198  N N   . THR D 117 ? 0.9882 0.9764 1.0534 0.1100  -0.0377 0.0335  181 THR D N   
9199  C CA  . THR D 117 ? 0.8625 0.8515 0.9050 0.1244  -0.0351 0.0360  181 THR D CA  
9200  C C   . THR D 117 ? 0.7750 0.7795 0.8019 0.1304  -0.0396 0.0182  181 THR D C   
9201  O O   . THR D 117 ? 0.6816 0.7015 0.7110 0.1269  -0.0379 0.0121  181 THR D O   
9202  C CB  . THR D 117 ? 0.9379 0.9339 0.9757 0.1311  -0.0217 0.0546  181 THR D CB  
9203  O OG1 . THR D 117 ? 1.0049 0.9862 1.0618 0.1235  -0.0167 0.0723  181 THR D OG1 
9204  C CG2 . THR D 117 ? 0.9144 0.9111 0.9257 0.1483  -0.0202 0.0560  181 THR D CG2 
9205  N N   . VAL D 118 ? 0.7446 0.7444 0.7579 0.1390  -0.0460 0.0096  182 VAL D N   
9206  C CA  . VAL D 118 ? 0.7337 0.7488 0.7352 0.1451  -0.0501 -0.0065 182 VAL D CA  
9207  C C   . VAL D 118 ? 0.8008 0.8187 0.7834 0.1610  -0.0509 -0.0070 182 VAL D C   
9208  O O   . VAL D 118 ? 0.9241 0.9276 0.9015 0.1668  -0.0541 -0.0039 182 VAL D O   
9209  C CB  . VAL D 118 ? 0.6273 0.6389 0.6343 0.1388  -0.0585 -0.0217 182 VAL D CB  
9210  C CG1 . VAL D 118 ? 0.7068 0.7346 0.7043 0.1451  -0.0616 -0.0366 182 VAL D CG1 
9211  C CG2 . VAL D 118 ? 0.5303 0.5417 0.5518 0.1257  -0.0586 -0.0235 182 VAL D CG2 
9212  N N   . LEU D 119 ? 0.7773 0.8132 0.7497 0.1686  -0.0490 -0.0116 183 LEU D N   
9213  C CA  . LEU D 119 ? 0.8947 0.9371 0.8491 0.1850  -0.0519 -0.0160 183 LEU D CA  
9214  C C   . LEU D 119 ? 0.7623 0.8175 0.7182 0.1857  -0.0602 -0.0358 183 LEU D C   
9215  O O   . LEU D 119 ? 0.7686 0.8371 0.7307 0.1796  -0.0607 -0.0445 183 LEU D O   
9216  C CB  . LEU D 119 ? 0.8351 0.8885 0.7767 0.1951  -0.0458 -0.0091 183 LEU D CB  
9217  C CG  . LEU D 119 ? 0.8309 0.8744 0.7723 0.1947  -0.0349 0.0124  183 LEU D CG  
9218  C CD1 . LEU D 119 ? 0.9467 1.0030 0.8930 0.1901  -0.0282 0.0157  183 LEU D CD1 
9219  C CD2 . LEU D 119 ? 0.8724 0.9101 0.7920 0.2128  -0.0315 0.0233  183 LEU D CD2 
9220  N N   . SER D 120 ? 0.6715 0.7230 0.6228 0.1934  -0.0664 -0.0423 184 SER D N   
9221  C CA  . SER D 120 ? 0.6638 0.7297 0.6194 0.1947  -0.0732 -0.0600 184 SER D CA  
9222  C C   . SER D 120 ? 0.6919 0.7657 0.6355 0.2117  -0.0788 -0.0659 184 SER D C   
9223  O O   . SER D 120 ? 0.8536 0.9159 0.7840 0.2229  -0.0789 -0.0571 184 SER D O   
9224  C CB  . SER D 120 ? 0.7531 0.8104 0.7181 0.1875  -0.0763 -0.0657 184 SER D CB  
9225  O OG  . SER D 120 ? 0.8410 0.9139 0.8124 0.1879  -0.0806 -0.0814 184 SER D OG  
9226  N N   . VAL D 121 ? 0.6332 0.7263 0.5820 0.2137  -0.0839 -0.0808 185 VAL D N   
9227  C CA  . VAL D 121 ? 0.6362 0.7402 0.5780 0.2295  -0.0916 -0.0902 185 VAL D CA  
9228  C C   . VAL D 121 ? 0.7116 0.8244 0.6668 0.2283  -0.0972 -0.1041 185 VAL D C   
9229  O O   . VAL D 121 ? 0.7381 0.8633 0.7096 0.2174  -0.0969 -0.1137 185 VAL D O   
9230  C CB  . VAL D 121 ? 0.5752 0.6964 0.5171 0.2331  -0.0949 -0.0986 185 VAL D CB  
9231  C CG1 . VAL D 121 ? 0.5606 0.6942 0.4985 0.2494  -0.1051 -0.1108 185 VAL D CG1 
9232  C CG2 . VAL D 121 ? 0.6310 0.7460 0.5584 0.2367  -0.0890 -0.0858 185 VAL D CG2 
9233  N N   . ALA D 122 ? 0.7055 0.8122 0.6537 0.2399  -0.1016 -0.1048 186 ALA D N   
9234  C CA  . ALA D 122 ? 0.6943 0.8091 0.6546 0.2403  -0.1058 -0.1168 186 ALA D CA  
9235  C C   . ALA D 122 ? 0.7417 0.8648 0.6966 0.2587  -0.1147 -0.1253 186 ALA D C   
9236  O O   . ALA D 122 ? 0.6974 0.8176 0.6360 0.2726  -0.1183 -0.1216 186 ALA D O   
9237  C CB  . ALA D 122 ? 0.7221 0.8182 0.6827 0.2336  -0.1024 -0.1103 186 ALA D CB  
9238  N N   . GLY D 123 ? 0.7696 0.9038 0.7378 0.2597  -0.1179 -0.1367 187 GLY D N   
9239  C CA  . GLY D 123 ? 0.9402 1.0865 0.9086 0.2767  -0.1271 -0.1476 187 GLY D CA  
9240  C C   . GLY D 123 ? 0.9952 1.1539 0.9572 0.2911  -0.1356 -0.1538 187 GLY D C   
9241  O O   . GLY D 123 ? 0.9193 1.0986 0.8963 0.2875  -0.1387 -0.1641 187 GLY D O   
9242  N N   . ASP D 124 ? 0.9987 1.1434 0.9377 0.3086  -0.1402 -0.1477 188 ASP D N   
9243  C CA  . ASP D 124 ? 0.9684 1.1187 0.8931 0.3259  -0.1485 -0.1511 188 ASP D CA  
9244  C C   . ASP D 124 ? 0.9726 1.1290 0.8969 0.3194  -0.1460 -0.1495 188 ASP D C   
9245  O O   . ASP D 124 ? 1.0357 1.2084 0.9621 0.3285  -0.1550 -0.1611 188 ASP D O   
9246  C CB  . ASP D 124 ? 1.1503 1.2752 1.0443 0.3427  -0.1491 -0.1376 188 ASP D CB  
9247  C CG  . ASP D 124 ? 1.5436 1.6688 1.4147 0.3628  -0.1557 -0.1372 188 ASP D CG  
9248  O OD1 . ASP D 124 ? 1.7944 1.9406 1.6723 0.3739  -0.1674 -0.1540 188 ASP D OD1 
9249  O OD2 . ASP D 124 ? 1.4683 1.5722 1.3143 0.3684  -0.1494 -0.1198 188 ASP D OD2 
9250  N N   . GLY D 125 ? 0.8562 1.0000 0.7790 0.3041  -0.1350 -0.1366 189 GLY D N   
9251  C CA  . GLY D 125 ? 0.8749 1.0200 0.7914 0.3008  -0.1317 -0.1320 189 GLY D CA  
9252  C C   . GLY D 125 ? 0.9986 1.1208 0.8897 0.3057  -0.1234 -0.1115 189 GLY D C   
9253  O O   . GLY D 125 ? 0.9027 1.0251 0.7799 0.3118  -0.1216 -0.1064 189 GLY D O   
9254  N N   . PHE D 126 ? 0.9286 1.0311 0.8144 0.3035  -0.1182 -0.0997 190 PHE D N   
9255  C CA  . PHE D 126 ? 0.8209 0.9004 0.6894 0.3038  -0.1084 -0.0782 190 PHE D CA  
9256  C C   . PHE D 126 ? 0.7962 0.8689 0.6788 0.2821  -0.0982 -0.0689 190 PHE D C   
9257  O O   . PHE D 126 ? 0.7877 0.8709 0.6906 0.2672  -0.0985 -0.0786 190 PHE D O   
9258  C CB  . PHE D 126 ? 0.8091 0.8678 0.6642 0.3140  -0.1096 -0.0696 190 PHE D CB  
9259  C CG  . PHE D 126 ? 0.9318 0.9820 0.8027 0.3017  -0.1096 -0.0716 190 PHE D CG  
9260  C CD1 . PHE D 126 ? 1.0217 1.0488 0.8934 0.2909  -0.1020 -0.0559 190 PHE D CD1 
9261  C CD2 . PHE D 126 ? 1.0640 1.1293 0.9495 0.3019  -0.1175 -0.0894 190 PHE D CD2 
9262  C CE1 . PHE D 126 ? 0.8842 0.9017 0.7684 0.2815  -0.1038 -0.0590 190 PHE D CE1 
9263  C CE2 . PHE D 126 ? 1.0153 1.0724 0.9124 0.2929  -0.1172 -0.0913 190 PHE D CE2 
9264  C CZ  . PHE D 126 ? 0.9356 0.9678 0.8305 0.2834  -0.1111 -0.0767 190 PHE D CZ  
9265  N N   . VAL D 127 ? 0.7784 0.8330 0.6504 0.2808  -0.0890 -0.0495 191 VAL D N   
9266  C CA  . VAL D 127 ? 0.7686 0.8169 0.6546 0.2615  -0.0800 -0.0400 191 VAL D CA  
9267  C C   . VAL D 127 ? 0.7809 0.8054 0.6706 0.2547  -0.0768 -0.0279 191 VAL D C   
9268  O O   . VAL D 127 ? 0.9589 0.9663 0.8341 0.2643  -0.0742 -0.0142 191 VAL D O   
9269  C CB  . VAL D 127 ? 0.8307 0.8811 0.7074 0.2632  -0.0712 -0.0277 191 VAL D CB  
9270  C CG1 . VAL D 127 ? 0.9071 0.9445 0.7946 0.2478  -0.0606 -0.0113 191 VAL D CG1 
9271  C CG2 . VAL D 127 ? 1.0441 1.1166 0.9266 0.2611  -0.0744 -0.0415 191 VAL D CG2 
9272  N N   . SER D 128 ? 0.7666 0.7888 0.6750 0.2389  -0.0778 -0.0334 192 SER D N   
9273  C CA  . SER D 128 ? 0.8083 0.8074 0.7238 0.2294  -0.0754 -0.0224 192 SER D CA  
9274  C C   . SER D 128 ? 0.9374 0.9347 0.8632 0.2158  -0.0664 -0.0105 192 SER D C   
9275  O O   . SER D 128 ? 1.0841 1.0983 1.0175 0.2085  -0.0642 -0.0168 192 SER D O   
9276  C CB  . SER D 128 ? 0.7808 0.7787 0.7102 0.2205  -0.0817 -0.0354 192 SER D CB  
9277  O OG  . SER D 128 ? 0.9094 0.9109 0.8323 0.2327  -0.0896 -0.0470 192 SER D OG  
9278  N N   . ILE D 129 ? 0.9931 0.9699 0.9209 0.2121  -0.0613 0.0066  193 ILE D N   
9279  C CA  . ILE D 129 ? 1.0603 1.0353 1.0026 0.1982  -0.0529 0.0185  193 ILE D CA  
9280  C C   . ILE D 129 ? 1.1518 1.1077 1.1112 0.1855  -0.0570 0.0198  193 ILE D C   
9281  O O   . ILE D 129 ? 0.9716 0.9057 0.9279 0.1894  -0.0598 0.0273  193 ILE D O   
9282  C CB  . ILE D 129 ? 0.9559 0.9239 0.8893 0.2046  -0.0418 0.0403  193 ILE D CB  
9283  C CG1 . ILE D 129 ? 0.8397 0.8269 0.7542 0.2187  -0.0380 0.0387  193 ILE D CG1 
9284  C CG2 . ILE D 129 ? 0.8816 0.8462 0.8355 0.1890  -0.0333 0.0536  193 ILE D CG2 
9285  C CD1 . ILE D 129 ? 0.9136 0.8931 0.8118 0.2306  -0.0275 0.0593  193 ILE D CD1 
9286  N N   . LEU D 130 ? 1.0161 0.9779 0.9922 0.1714  -0.0586 0.0119  194 LEU D N   
9287  C CA  . LEU D 130 ? 0.9192 0.8615 0.9113 0.1603  -0.0638 0.0128  194 LEU D CA  
9288  C C   . LEU D 130 ? 0.8218 0.7614 0.8354 0.1448  -0.0598 0.0211  194 LEU D C   
9289  O O   . LEU D 130 ? 0.8203 0.7764 0.8407 0.1380  -0.0569 0.0162  194 LEU D O   
9290  C CB  . LEU D 130 ? 1.0102 0.9506 1.0008 0.1613  -0.0745 -0.0055 194 LEU D CB  
9291  C CG  . LEU D 130 ? 1.0274 0.9899 1.0166 0.1602  -0.0758 -0.0220 194 LEU D CG  
9292  C CD1 . LEU D 130 ? 1.4627 1.4213 1.4666 0.1468  -0.0789 -0.0282 194 LEU D CD1 
9293  C CD2 . LEU D 130 ? 0.7834 0.7487 0.7614 0.1717  -0.0822 -0.0345 194 LEU D CD2 
9294  N N   . TYR D 131 ? 0.8324 0.7503 0.8579 0.1397  -0.0601 0.0338  195 TYR D N   
9295  C CA  . TYR D 131 ? 0.8355 0.7494 0.8854 0.1255  -0.0563 0.0443  195 TYR D CA  
9296  C C   . TYR D 131 ? 0.8758 0.7732 0.9406 0.1164  -0.0690 0.0339  195 TYR D C   
9297  O O   . TYR D 131 ? 0.8515 0.7267 0.9150 0.1193  -0.0769 0.0338  195 TYR D O   
9298  C CB  . TYR D 131 ? 0.8635 0.7641 0.9192 0.1259  -0.0475 0.0672  195 TYR D CB  
9299  C CG  . TYR D 131 ? 0.9568 0.8597 1.0400 0.1121  -0.0398 0.0811  195 TYR D CG  
9300  C CD1 . TYR D 131 ? 1.0787 1.0059 1.1643 0.1107  -0.0288 0.0854  195 TYR D CD1 
9301  C CD2 . TYR D 131 ? 1.0533 0.9345 1.1621 0.1008  -0.0442 0.0896  195 TYR D CD2 
9302  C CE1 . TYR D 131 ? 1.1488 1.0808 1.2620 0.0985  -0.0214 0.0979  195 TYR D CE1 
9303  C CE2 . TYR D 131 ? 1.1801 1.0655 1.3190 0.0874  -0.0374 0.1022  195 TYR D CE2 
9304  C CZ  . TYR D 131 ? 1.2989 1.2108 1.4400 0.0865  -0.0254 0.1065  195 TYR D CZ  
9305  O OH  . TYR D 131 ? 1.4472 1.3652 1.6199 0.0740  -0.0183 0.1189  195 TYR D OH  
9306  N N   . GLY D 132 ? 0.9034 0.8110 0.9799 0.1071  -0.0717 0.0242  196 GLY D N   
9307  C CA  . GLY D 132 ? 0.9013 0.7940 0.9907 0.0994  -0.0844 0.0133  196 GLY D CA  
9308  C C   . GLY D 132 ? 0.9635 0.8475 1.0357 0.1084  -0.0948 -0.0026 196 GLY D C   
9309  O O   . GLY D 132 ? 1.0384 0.9014 1.1163 0.1070  -0.1065 -0.0085 196 GLY D O   
9310  N N   . GLY D 133 ? 0.9214 0.8219 0.9732 0.1183  -0.0910 -0.0098 197 GLY D N   
9311  C CA  . GLY D 133 ? 0.8476 0.7454 0.8841 0.1276  -0.0987 -0.0250 197 GLY D CA  
9312  C C   . GLY D 133 ? 0.7753 0.6607 0.7988 0.1398  -0.1017 -0.0225 197 GLY D C   
9313  O O   . GLY D 133 ? 0.8041 0.6915 0.8148 0.1490  -0.1067 -0.0348 197 GLY D O   
9314  N N   . ILE D 134 ? 0.7658 0.6386 0.7925 0.1403  -0.0981 -0.0061 198 ILE D N   
9315  C CA  . ILE D 134 ? 0.8816 0.7389 0.8949 0.1525  -0.1015 -0.0025 198 ILE D CA  
9316  C C   . ILE D 134 ? 0.9766 0.8464 0.9770 0.1612  -0.0911 0.0082  198 ILE D C   
9317  O O   . ILE D 134 ? 1.0615 0.9425 1.0679 0.1557  -0.0810 0.0194  198 ILE D O   
9318  C CB  . ILE D 134 ? 0.9193 0.7441 0.9446 0.1482  -0.1083 0.0074  198 ILE D CB  
9319  C CG1 . ILE D 134 ? 1.2469 1.0678 1.2884 0.1386  -0.0984 0.0287  198 ILE D CG1 
9320  C CG2 . ILE D 134 ? 0.9770 0.7888 1.0148 0.1407  -0.1206 -0.0050 198 ILE D CG2 
9321  C CD1 . ILE D 134 ? 1.4789 1.2677 1.5354 0.1334  -0.1037 0.0412  198 ILE D CD1 
9322  N N   . ILE D 135 ? 1.0876 0.9557 1.0692 0.1761  -0.0942 0.0042  199 ILE D N   
9323  C CA  . ILE D 135 ? 1.0173 0.8985 0.9826 0.1878  -0.0866 0.0108  199 ILE D CA  
9324  C C   . ILE D 135 ? 1.1132 0.9757 1.0753 0.1907  -0.0804 0.0325  199 ILE D C   
9325  O O   . ILE D 135 ? 1.3047 1.1431 1.2608 0.1971  -0.0858 0.0373  199 ILE D O   
9326  C CB  . ILE D 135 ? 0.9636 0.8522 0.9110 0.2039  -0.0931 -0.0028 199 ILE D CB  
9327  C CG1 . ILE D 135 ? 0.8384 0.7453 0.7910 0.2006  -0.0977 -0.0228 199 ILE D CG1 
9328  C CG2 . ILE D 135 ? 0.9872 0.8897 0.9175 0.2171  -0.0871 0.0023  199 ILE D CG2 
9329  C CD1 . ILE D 135 ? 0.7851 0.7198 0.7292 0.2092  -0.0959 -0.0334 199 ILE D CD1 
9330  N N   . THR D 136 ? 1.1593 1.0329 1.1242 0.1870  -0.0684 0.0458  200 THR D N   
9331  C CA  . THR D 136 ? 1.1003 0.9582 1.0642 0.1884  -0.0590 0.0695  200 THR D CA  
9332  C C   . THR D 136 ? 1.0995 0.9648 1.0366 0.2067  -0.0522 0.0768  200 THR D C   
9333  O O   . THR D 136 ? 1.2410 1.0886 1.1697 0.2130  -0.0458 0.0957  200 THR D O   
9334  C CB  . THR D 136 ? 1.0504 0.9142 1.0370 0.1727  -0.0484 0.0829  200 THR D CB  
9335  O OG1 . THR D 136 ? 1.1435 1.0367 1.1277 0.1722  -0.0435 0.0747  200 THR D OG1 
9336  C CG2 . THR D 136 ? 1.0781 0.9288 1.0922 0.1556  -0.0562 0.0787  200 THR D CG2 
9337  N N   . ASP D 137 ? 1.0191 0.9096 0.9430 0.2155  -0.0537 0.0622  201 ASP D N   
9338  C CA  . ASP D 137 ? 1.1081 1.0075 1.0059 0.2345  -0.0492 0.0664  201 ASP D CA  
9339  C C   . ASP D 137 ? 1.0919 1.0164 0.9790 0.2441  -0.0563 0.0451  201 ASP D C   
9340  O O   . ASP D 137 ? 1.2437 1.1848 1.1448 0.2338  -0.0597 0.0304  201 ASP D O   
9341  C CB  . ASP D 137 ? 1.2483 1.1540 1.1444 0.2339  -0.0340 0.0856  201 ASP D CB  
9342  C CG  . ASP D 137 ? 1.6208 1.5198 1.4876 0.2547  -0.0277 0.0995  201 ASP D CG  
9343  O OD1 . ASP D 137 ? 2.1047 2.0090 1.9494 0.2722  -0.0356 0.0877  201 ASP D OD1 
9344  O OD2 . ASP D 137 ? 1.5454 1.4339 1.4114 0.2543  -0.0145 0.1228  201 ASP D OD2 
9345  N N   . THR D 138 ? 1.2132 1.1396 1.0760 0.2642  -0.0588 0.0438  202 THR D N   
9346  C CA  . THR D 138 ? 1.2526 1.2031 1.1061 0.2753  -0.0663 0.0243  202 THR D CA  
9347  C C   . THR D 138 ? 1.2145 1.1735 1.0447 0.2925  -0.0612 0.0312  202 THR D C   
9348  O O   . THR D 138 ? 1.5229 1.4651 1.3356 0.3031  -0.0545 0.0495  202 THR D O   
9349  C CB  . THR D 138 ? 1.2871 1.2348 1.1346 0.2863  -0.0793 0.0089  202 THR D CB  
9350  O OG1 . THR D 138 ? 1.1728 1.0991 0.9991 0.3026  -0.0801 0.0206  202 THR D OG1 
9351  C CG2 . THR D 138 ? 1.1589 1.0996 1.0269 0.2719  -0.0849 0.0000  202 THR D CG2 
9352  N N   . ILE D 139 ? 1.0234 1.0075 0.8527 0.2960  -0.0648 0.0164  203 ILE D N   
9353  C CA  . ILE D 139 ? 0.9860 0.9800 0.7918 0.3147  -0.0631 0.0184  203 ILE D CA  
9354  C C   . ILE D 139 ? 1.0688 1.0798 0.8684 0.3283  -0.0774 -0.0043 203 ILE D C   
9355  O O   . ILE D 139 ? 1.0653 1.0924 0.8854 0.3175  -0.0845 -0.0224 203 ILE D O   
9356  C CB  . ILE D 139 ? 0.9357 0.9447 0.7478 0.3066  -0.0547 0.0214  203 ILE D CB  
9357  C CG1 . ILE D 139 ? 0.9677 0.9625 0.7890 0.2936  -0.0401 0.0443  203 ILE D CG1 
9358  C CG2 . ILE D 139 ? 0.8694 0.8904 0.6560 0.3278  -0.0554 0.0194  203 ILE D CG2 
9359  C CD1 . ILE D 139 ? 0.8827 0.8932 0.7138 0.2840  -0.0315 0.0473  203 ILE D CD1 
9360  N N   . HIS D 140 ? 1.0962 1.1037 0.8687 0.3521  -0.0815 -0.0030 204 HIS D N   
9361  C CA  . HIS D 140 ? 1.1670 1.1908 0.9340 0.3675  -0.0968 -0.0249 204 HIS D CA  
9362  C C   . HIS D 140 ? 1.2381 1.2777 0.9875 0.3846  -0.1009 -0.0319 204 HIS D C   
9363  O O   . HIS D 140 ? 1.1246 1.1565 0.8512 0.3952  -0.0918 -0.0160 204 HIS D O   
9364  C CB  . HIS D 140 ? 1.0829 1.0916 0.8363 0.3826  -0.1043 -0.0251 204 HIS D CB  
9365  C CG  . HIS D 140 ? 1.1894 1.1822 0.9596 0.3675  -0.1027 -0.0210 204 HIS D CG  
9366  N ND1 . HIS D 140 ? 1.3648 1.3686 1.1566 0.3589  -0.1111 -0.0386 204 HIS D ND1 
9367  C CD2 . HIS D 140 ? 1.1778 1.1438 0.9467 0.3596  -0.0934 -0.0006 204 HIS D CD2 
9368  C CE1 . HIS D 140 ? 1.3871 1.3713 1.1877 0.3478  -0.1083 -0.0308 204 HIS D CE1 
9369  N NE2 . HIS D 140 ? 1.4183 1.3788 1.2060 0.3478  -0.0983 -0.0080 204 HIS D NE2 
9370  N N   . PRO D 141 ? 1.0836 1.1455 0.8439 0.3880  -0.1147 -0.0558 205 PRO D N   
9371  C CA  . PRO D 141 ? 1.0792 1.1567 0.8266 0.4031  -0.1217 -0.0661 205 PRO D CA  
9372  C C   . PRO D 141 ? 1.2758 1.3451 0.9887 0.4334  -0.1286 -0.0646 205 PRO D C   
9373  O O   . PRO D 141 ? 1.4900 1.5551 1.1996 0.4438  -0.1380 -0.0714 205 PRO D O   
9374  C CB  . PRO D 141 ? 1.0197 1.1212 0.7952 0.3953  -0.1354 -0.0922 205 PRO D CB  
9375  C CG  . PRO D 141 ? 0.9695 1.0687 0.7715 0.3749  -0.1325 -0.0932 205 PRO D CG  
9376  C CD  . PRO D 141 ? 1.0296 1.1033 0.8156 0.3790  -0.1249 -0.0745 205 PRO D CD  
9377  N N   . THR D 142 ? 1.4152 1.4819 1.1010 0.4489  -0.1240 -0.0557 206 THR D N   
9378  C CA  . THR D 142 ? 1.7700 1.8306 1.4188 0.4809  -0.1315 -0.0559 206 THR D CA  
9379  C C   . THR D 142 ? 1.6951 1.7786 1.3461 0.4933  -0.1502 -0.0824 206 THR D C   
9380  O O   . THR D 142 ? 1.5712 1.6625 1.2238 0.5063  -0.1673 -0.1007 206 THR D O   
9381  C CB  . THR D 142 ? 1.9178 1.9621 1.5322 0.4939  -0.1151 -0.0302 206 THR D CB  
9382  O OG1 . THR D 142 ? 1.9644 2.0228 1.5811 0.4898  -0.1108 -0.0322 206 THR D OG1 
9383  C CG2 . THR D 142 ? 1.7739 1.7962 1.3930 0.4779  -0.0960 -0.0032 206 THR D CG2 
9384  N N   . ASN D 143 ? 1.7346 1.8293 1.3890 0.4879  -0.1472 -0.0848 207 ASN D N   
9385  C CA  . ASN D 143 ? 1.7937 1.9080 1.4508 0.4980  -0.1640 -0.1085 207 ASN D CA  
9386  C C   . ASN D 143 ? 1.8812 2.0154 1.5759 0.4865  -0.1811 -0.1348 207 ASN D C   
9387  O O   . ASN D 143 ? 1.8406 1.9920 1.5455 0.4907  -0.1960 -0.1557 207 ASN D O   
9388  C CB  . ASN D 143 ? 1.7697 1.8891 1.4256 0.4906  -0.1548 -0.1030 207 ASN D CB  
9389  C CG  . ASN D 143 ? 1.6792 1.8028 1.3038 0.5189  -0.1648 -0.1114 207 ASN D CG  
9390  O OD1 . ASN D 143 ? 1.8913 2.0047 1.4797 0.5470  -0.1681 -0.1068 207 ASN D OD1 
9391  N ND2 . ASN D 143 ? 1.7282 1.8654 1.3644 0.5128  -0.1700 -0.1238 207 ASN D ND2 
9392  N N   . GLY D 144 ? 1.6327 1.7644 1.3487 0.4720  -0.1787 -0.1335 208 GLY D N   
9393  C CA  . GLY D 144 ? 1.5249 1.6759 1.2776 0.4609  -0.1917 -0.1555 208 GLY D CA  
9394  C C   . GLY D 144 ? 1.5537 1.7187 1.3435 0.4320  -0.1875 -0.1621 208 GLY D C   
9395  O O   . GLY D 144 ? 1.8287 1.9903 1.6157 0.4218  -0.1772 -0.1526 208 GLY D O   
9396  N N   . GLY D 145 ? 1.6765 1.8576 1.5009 0.4195  -0.1950 -0.1779 209 GLY D N   
9397  C CA  . GLY D 145 ? 1.6359 1.8303 1.4961 0.3927  -0.1911 -0.1845 209 GLY D CA  
9398  C C   . GLY D 145 ? 1.3617 1.5414 1.2227 0.3722  -0.1719 -0.1645 209 GLY D C   
9399  O O   . GLY D 145 ? 1.3823 1.5425 1.2176 0.3785  -0.1617 -0.1456 209 GLY D O   
9400  N N   . PRO D 146 ? 1.2444 1.4327 1.1349 0.3480  -0.1669 -0.1683 210 PRO D N   
9401  C CA  . PRO D 146 ? 1.0066 1.1816 0.9020 0.3283  -0.1508 -0.1520 210 PRO D CA  
9402  C C   . PRO D 146 ? 0.8501 1.0124 0.7266 0.3265  -0.1399 -0.1357 210 PRO D C   
9403  O O   . PRO D 146 ? 1.0094 1.1786 0.8796 0.3324  -0.1441 -0.1410 210 PRO D O   
9404  C CB  . PRO D 146 ? 0.9405 1.1304 0.8701 0.3069  -0.1507 -0.1633 210 PRO D CB  
9405  C CG  . PRO D 146 ? 0.8989 1.1056 0.8365 0.3123  -0.1630 -0.1798 210 PRO D CG  
9406  C CD  . PRO D 146 ? 1.0401 1.2489 0.9583 0.3386  -0.1758 -0.1867 210 PRO D CD  
9407  N N   . LEU D 147 ? 0.6972 0.8416 0.5658 0.3195  -0.1268 -0.1166 211 LEU D N   
9408  C CA  . LEU D 147 ? 0.7336 0.8692 0.5922 0.3137  -0.1149 -0.1011 211 LEU D CA  
9409  C C   . LEU D 147 ? 0.8090 0.9526 0.6918 0.2914  -0.1114 -0.1059 211 LEU D C   
9410  O O   . LEU D 147 ? 0.7551 0.9083 0.6615 0.2793  -0.1160 -0.1187 211 LEU D O   
9411  C CB  . LEU D 147 ? 0.6901 0.8047 0.5372 0.3117  -0.1022 -0.0789 211 LEU D CB  
9412  C CG  . LEU D 147 ? 0.7599 0.8613 0.5806 0.3328  -0.1028 -0.0694 211 LEU D CG  
9413  C CD1 . LEU D 147 ? 0.9590 1.0406 0.7826 0.3236  -0.0940 -0.0535 211 LEU D CD1 
9414  C CD2 . LEU D 147 ? 0.7901 0.8878 0.5840 0.3486  -0.0973 -0.0578 211 LEU D CD2 
9415  N N   . ARG D 148 ? 0.9004 1.0404 0.7765 0.2872  -0.1027 -0.0956 212 ARG D N   
9416  C CA  . ARG D 148 ? 0.9231 1.0697 0.8175 0.2690  -0.1000 -0.0999 212 ARG D CA  
9417  C C   . ARG D 148 ? 1.0078 1.1441 0.8976 0.2611  -0.0864 -0.0816 212 ARG D C   
9418  O O   . ARG D 148 ? 1.1883 1.3200 1.0577 0.2740  -0.0807 -0.0695 212 ARG D O   
9419  C CB  . ARG D 148 ? 0.7656 0.9265 0.6595 0.2761  -0.1101 -0.1152 212 ARG D CB  
9420  C CG  . ARG D 148 ? 0.9139 1.0876 0.8201 0.2812  -0.1247 -0.1350 212 ARG D CG  
9421  C CD  . ARG D 148 ? 1.0669 1.2534 0.9755 0.2876  -0.1367 -0.1512 212 ARG D CD  
9422  N NE  . ARG D 148 ? 0.9970 1.1811 0.8763 0.3100  -0.1400 -0.1486 212 ARG D NE  
9423  C CZ  . ARG D 148 ? 1.1173 1.3030 0.9790 0.3324  -0.1499 -0.1542 212 ARG D CZ  
9424  N NH1 . ARG D 148 ? 1.0641 1.2548 0.9366 0.3352  -0.1579 -0.1631 212 ARG D NH1 
9425  N NH2 . ARG D 148 ? 1.1998 1.3823 1.0319 0.3535  -0.1517 -0.1509 212 ARG D NH2 
9426  N N   . THR D 149 ? 0.8771 1.0100 0.7859 0.2409  -0.0809 -0.0793 213 THR D N   
9427  C CA  . THR D 149 ? 0.8640 0.9885 0.7737 0.2317  -0.0690 -0.0632 213 THR D CA  
9428  C C   . THR D 149 ? 0.8349 0.9687 0.7486 0.2265  -0.0684 -0.0679 213 THR D C   
9429  O O   . THR D 149 ? 0.9600 1.1041 0.8790 0.2263  -0.0774 -0.0839 213 THR D O   
9430  C CB  . THR D 149 ? 0.9740 1.0882 0.9014 0.2138  -0.0649 -0.0588 213 THR D CB  
9431  O OG1 . THR D 149 ? 1.1234 1.2449 1.0674 0.2020  -0.0708 -0.0739 213 THR D OG1 
9432  C CG2 . THR D 149 ? 0.8705 0.9725 0.7939 0.2186  -0.0653 -0.0529 213 THR D CG2 
9433  N N   . GLN D 150 ? 0.7256 0.8555 0.6386 0.2218  -0.0582 -0.0543 214 GLN D N   
9434  C CA  . GLN D 150 ? 0.6898 0.8277 0.6069 0.2165  -0.0574 -0.0584 214 GLN D CA  
9435  C C   . GLN D 150 ? 0.6490 0.7895 0.5852 0.2001  -0.0632 -0.0720 214 GLN D C   
9436  O O   . GLN D 150 ? 0.6921 0.8398 0.6294 0.1990  -0.0671 -0.0809 214 GLN D O   
9437  C CB  . GLN D 150 ? 0.6966 0.8307 0.6159 0.2114  -0.0451 -0.0415 214 GLN D CB  
9438  C CG  . GLN D 150 ? 0.8377 0.9697 0.7392 0.2267  -0.0367 -0.0258 214 GLN D CG  
9439  C CD  . GLN D 150 ? 0.9358 1.0657 0.8446 0.2203  -0.0231 -0.0076 214 GLN D CD  
9440  O OE1 . GLN D 150 ? 0.9586 1.0829 0.8879 0.2031  -0.0206 -0.0042 214 GLN D OE1 
9441  N NE2 . GLN D 150 ? 1.3685 1.5035 1.2609 0.2351  -0.0144 0.0042  214 GLN D NE2 
9442  N N   . ALA D 151 ? 0.5735 0.7073 0.5233 0.1881  -0.0637 -0.0734 215 ALA D N   
9443  C CA  . ALA D 151 ? 0.5542 0.6892 0.5201 0.1732  -0.0670 -0.0840 215 ALA D CA  
9444  C C   . ALA D 151 ? 0.6516 0.7854 0.6214 0.1647  -0.0621 -0.0793 215 ALA D C   
9445  O O   . ALA D 151 ? 0.6428 0.7809 0.6177 0.1590  -0.0656 -0.0885 215 ALA D O   
9446  C CB  . ALA D 151 ? 0.5274 0.6733 0.4961 0.1764  -0.0766 -0.1006 215 ALA D CB  
9447  N N   . SER D 152 ? 0.7399 0.8678 0.7081 0.1644  -0.0539 -0.0644 216 SER D N   
9448  C CA  . SER D 152 ? 0.7414 0.8697 0.7142 0.1584  -0.0482 -0.0576 216 SER D CA  
9449  C C   . SER D 152 ? 0.6602 0.7799 0.6380 0.1556  -0.0400 -0.0412 216 SER D C   
9450  O O   . SER D 152 ? 0.7183 0.8334 0.6895 0.1631  -0.0380 -0.0339 216 SER D O   
9451  C CB  . SER D 152 ? 0.8224 0.9613 0.7816 0.1714  -0.0471 -0.0574 216 SER D CB  
9452  O OG  . SER D 152 ? 1.1576 1.2986 1.1203 0.1689  -0.0393 -0.0475 216 SER D OG  
9453  N N   . SER D 153 ? 0.5571 0.6742 0.5476 0.1451  -0.0359 -0.0355 217 SER D N   
9454  C CA  . SER D 153 ? 0.6212 0.7319 0.6208 0.1416  -0.0280 -0.0192 217 SER D CA  
9455  C C   . SER D 153 ? 0.6129 0.7287 0.6005 0.1554  -0.0194 -0.0054 217 SER D C   
9456  O O   . SER D 153 ? 1.0308 1.1582 1.0070 0.1655  -0.0168 -0.0058 217 SER D O   
9457  C CB  . SER D 153 ? 0.6929 0.8055 0.7079 0.1309  -0.0256 -0.0171 217 SER D CB  
9458  O OG  . SER D 153 ? 0.7933 0.9040 0.8205 0.1283  -0.0172 -0.0007 217 SER D OG  
9459  N N   . CYS D 154 ? 0.5958 0.7017 0.5841 0.1571  -0.0151 0.0068  218 CYS D N   
9460  C CA  . CYS D 154 ? 0.7077 0.8158 0.6864 0.1689  -0.0042 0.0242  218 CYS D CA  
9461  C C   . CYS D 154 ? 0.7095 0.8207 0.7070 0.1604  0.0062  0.0388  218 CYS D C   
9462  O O   . CYS D 154 ? 0.6866 0.7984 0.7027 0.1469  0.0030  0.0334  218 CYS D O   
9463  C CB  . CYS D 154 ? 1.0257 1.1195 0.9985 0.1734  -0.0037 0.0325  218 CYS D CB  
9464  S SG  . CYS D 154 ? 1.6273 1.7029 1.6189 0.1574  -0.0125 0.0268  218 CYS D SG  
9465  N N   . ILE D 155 ? 0.7616 0.8756 0.7553 0.1686  0.0189  0.0574  219 ILE D N   
9466  C CA  . ILE D 155 ? 0.7950 0.9172 0.8089 0.1615  0.0298  0.0708  219 ILE D CA  
9467  C C   . ILE D 155 ? 0.8443 0.9555 0.8750 0.1553  0.0391  0.0911  219 ILE D C   
9468  O O   . ILE D 155 ? 1.0265 1.1317 1.0422 0.1664  0.0462  0.1039  219 ILE D O   
9469  C CB  . ILE D 155 ? 0.7924 0.9330 0.7906 0.1767  0.0395  0.0760  219 ILE D CB  
9470  C CG1 . ILE D 155 ? 0.8395 0.9904 0.8310 0.1779  0.0296  0.0559  219 ILE D CG1 
9471  C CG2 . ILE D 155 ? 0.7158 0.8659 0.7354 0.1719  0.0542  0.0945  219 ILE D CG2 
9472  C CD1 . ILE D 155 ? 1.2205 1.3674 1.1905 0.1858  0.0167  0.0381  219 ILE D CD1 
9473  N N   . CYS D 156 ? 0.8171 0.9244 0.8789 0.1380  0.0381  0.0939  220 CYS D N   
9474  C CA  . CYS D 156 ? 0.9524 1.0487 1.0354 0.1304  0.0462  0.1134  220 CYS D CA  
9475  C C   . CYS D 156 ? 0.9587 1.0704 1.0665 0.1247  0.0586  0.1271  220 CYS D C   
9476  O O   . CYS D 156 ? 0.9162 1.0402 1.0360 0.1186  0.0546  0.1168  220 CYS D O   
9477  C CB  . CYS D 156 ? 0.9456 1.0218 1.0476 0.1153  0.0335  0.1062  220 CYS D CB  
9478  S SG  . CYS D 156 ? 1.6911 1.7511 1.7664 0.1222  0.0193  0.0896  220 CYS D SG  
9479  N N   . ASN D 157 ? 0.8691 0.9806 0.9840 0.1277  0.0742  0.1507  221 ASN D N   
9480  C CA  . ASN D 157 ? 0.9654 1.0926 1.1078 0.1223  0.0887  0.1674  221 ASN D CA  
9481  C C   . ASN D 157 ? 0.9724 1.0882 1.1329 0.1177  0.1011  0.1924  221 ASN D C   
9482  O O   . ASN D 157 ? 1.1391 1.2493 1.2755 0.1315  0.1115  0.2063  221 ASN D O   
9483  C CB  . ASN D 157 ? 1.1073 1.2580 1.2281 0.1397  0.1012  0.1715  221 ASN D CB  
9484  C CG  . ASN D 157 ? 1.0951 1.2678 1.2464 0.1333  0.1121  0.1805  221 ASN D CG  
9485  O OD1 . ASN D 157 ? 1.0789 1.2544 1.2596 0.1178  0.1030  0.1705  221 ASN D OD1 
9486  N ND2 . ASN D 157 ? 0.9577 1.1466 1.1010 0.1467  0.1317  0.1990  221 ASN D ND2 
9487  N N   . ASP D 158 ? 0.9638 1.0752 1.1667 0.0986  0.0994  0.1978  222 ASP D N   
9488  C CA  . ASP D 158 ? 1.2774 1.3768 1.5058 0.0907  0.1104  0.2221  222 ASP D CA  
9489  C C   . ASP D 158 ? 1.3877 1.4570 1.6001 0.0920  0.1020  0.2223  222 ASP D C   
9490  O O   . ASP D 158 ? 1.4486 1.5069 1.6573 0.0967  0.1146  0.2440  222 ASP D O   
9491  C CB  . ASP D 158 ? 1.4783 1.5940 1.7020 0.1025  0.1361  0.2487  222 ASP D CB  
9492  C CG  . ASP D 158 ? 1.7147 1.8593 1.9675 0.0977  0.1472  0.2546  222 ASP D CG  
9493  O OD1 . ASP D 158 ? 1.7592 1.9083 2.0451 0.0818  0.1357  0.2423  222 ASP D OD1 
9494  O OD2 . ASP D 158 ? 1.8496 2.0127 2.0911 0.1113  0.1676  0.2717  222 ASP D OD2 
9495  N N   . GLY D 159 ? 1.1566 1.2128 1.3582 0.0891  0.0815  0.1986  223 GLY D N   
9496  C CA  . GLY D 159 ? 1.2511 1.2787 1.4428 0.0888  0.0714  0.1966  223 GLY D CA  
9497  C C   . GLY D 159 ? 1.2475 1.2682 1.3943 0.1084  0.0726  0.1957  223 GLY D C   
9498  O O   . GLY D 159 ? 1.4672 1.4656 1.6025 0.1098  0.0618  0.1898  223 GLY D O   
9499  N N   . THR D 160 ? 1.1238 1.1632 1.2450 0.1245  0.0850  0.2011  224 THR D N   
9500  C CA  . THR D 160 ? 1.1805 1.2169 1.2572 0.1452  0.0835  0.1958  224 THR D CA  
9501  C C   . THR D 160 ? 0.9971 1.0507 1.0542 0.1521  0.0732  0.1712  224 THR D C   
9502  O O   . THR D 160 ? 0.9419 1.0152 1.0091 0.1490  0.0764  0.1671  224 THR D O   
9503  C CB  . THR D 160 ? 1.3624 1.4037 1.4182 0.1624  0.1038  0.2198  224 THR D CB  
9504  O OG1 . THR D 160 ? 1.5029 1.5708 1.5610 0.1668  0.1159  0.2241  224 THR D OG1 
9505  C CG2 . THR D 160 ? 1.3774 1.4005 1.4540 0.1550  0.1162  0.2473  224 THR D CG2 
9506  N N   . CYS D 161 ? 0.9303 0.9762 0.9614 0.1612  0.0606  0.1548  225 CYS D N   
9507  C CA  . CYS D 161 ? 0.8662 0.9263 0.8819 0.1663  0.0500  0.1316  225 CYS D CA  
9508  C C   . CYS D 161 ? 0.9230 0.9890 0.9006 0.1890  0.0511  0.1287  225 CYS D C   
9509  O O   . CYS D 161 ? 1.2176 1.2710 1.1769 0.2006  0.0540  0.1383  225 CYS D O   
9510  C CB  . CYS D 161 ? 0.9908 1.0402 1.0132 0.1560  0.0322  0.1108  225 CYS D CB  
9511  S SG  . CYS D 161 ? 1.4418 1.4815 1.5054 0.1320  0.0275  0.1114  225 CYS D SG  
9512  N N   . TYR D 162 ? 0.8637 0.9477 0.8292 0.1959  0.0477  0.1147  226 TYR D N   
9513  C CA  . TYR D 162 ? 0.8001 0.8923 0.7306 0.2186  0.0473  0.1097  226 TYR D CA  
9514  C C   . TYR D 162 ? 0.7546 0.8517 0.6776 0.2190  0.0301  0.0831  226 TYR D C   
9515  O O   . TYR D 162 ? 0.7239 0.8281 0.6632 0.2063  0.0239  0.0703  226 TYR D O   
9516  C CB  . TYR D 162 ? 0.7412 0.8520 0.6635 0.2292  0.0601  0.1189  226 TYR D CB  
9517  C CG  . TYR D 162 ? 0.7611 0.8717 0.6977 0.2262  0.0798  0.1465  226 TYR D CG  
9518  C CD1 . TYR D 162 ? 0.8697 0.9743 0.7851 0.2428  0.0929  0.1668  226 TYR D CD1 
9519  C CD2 . TYR D 162 ? 0.7033 0.8192 0.6758 0.2069  0.0850  0.1527  226 TYR D CD2 
9520  C CE1 . TYR D 162 ? 0.9190 1.0231 0.8496 0.2392  0.1124  0.1939  226 TYR D CE1 
9521  C CE2 . TYR D 162 ? 0.8099 0.9269 0.8005 0.2029  0.1030  0.1781  226 TYR D CE2 
9522  C CZ  . TYR D 162 ? 0.9982 1.1096 0.9684 0.2186  0.1176  0.1995  226 TYR D CZ  
9523  O OH  . TYR D 162 ? 1.2080 1.3208 1.1978 0.2144  0.1375  0.2271  226 TYR D OH  
9524  N N   . THR D 163 ? 0.8359 0.9285 0.7353 0.2336  0.0222  0.0750  227 THR D N   
9525  C CA  . THR D 163 ? 0.8954 0.9942 0.7889 0.2353  0.0065  0.0504  227 THR D CA  
9526  C C   . THR D 163 ? 0.8701 0.9731 0.7323 0.2592  0.0016  0.0444  227 THR D C   
9527  O O   . THR D 163 ? 1.0719 1.1678 0.9150 0.2741  0.0086  0.0585  227 THR D O   
9528  C CB  . THR D 163 ? 0.9378 1.0251 0.8459 0.2223  -0.0042 0.0399  227 THR D CB  
9529  O OG1 . THR D 163 ? 1.1505 1.2467 1.0572 0.2223  -0.0174 0.0171  227 THR D OG1 
9530  C CG2 . THR D 163 ? 0.9063 0.9782 0.8022 0.2317  -0.0043 0.0483  227 THR D CG2 
9531  N N   . ILE D 164 ? 0.7292 0.8429 0.5866 0.2630  -0.0109 0.0232  228 ILE D N   
9532  C CA  . ILE D 164 ? 0.6775 0.7963 0.5076 0.2858  -0.0188 0.0139  228 ILE D CA  
9533  C C   . ILE D 164 ? 0.7119 0.8291 0.5446 0.2857  -0.0345 -0.0048 228 ILE D C   
9534  O O   . ILE D 164 ? 0.8101 0.9320 0.6628 0.2707  -0.0428 -0.0199 228 ILE D O   
9535  C CB  . ILE D 164 ? 0.6292 0.7628 0.4501 0.2943  -0.0217 0.0042  228 ILE D CB  
9536  C CG1 . ILE D 164 ? 0.6387 0.7760 0.4520 0.3002  -0.0049 0.0239  228 ILE D CG1 
9537  C CG2 . ILE D 164 ? 0.6340 0.7724 0.4300 0.3169  -0.0343 -0.0103 228 ILE D CG2 
9538  C CD1 . ILE D 164 ? 0.6006 0.7519 0.4144 0.3011  -0.0060 0.0155  228 ILE D CD1 
9539  N N   . ILE D 165 ? 0.7440 0.8550 0.5564 0.3033  -0.0381 -0.0033 229 ILE D N   
9540  C CA  . ILE D 165 ? 0.7914 0.9024 0.6065 0.3056  -0.0527 -0.0204 229 ILE D CA  
9541  C C   . ILE D 165 ? 0.8429 0.9629 0.6365 0.3284  -0.0653 -0.0352 229 ILE D C   
9542  O O   . ILE D 165 ? 0.8418 0.9587 0.6072 0.3498  -0.0619 -0.0263 229 ILE D O   
9543  C CB  . ILE D 165 ? 0.8115 0.9059 0.6263 0.3048  -0.0500 -0.0097 229 ILE D CB  
9544  C CG1 . ILE D 165 ? 0.7558 0.8401 0.5914 0.2837  -0.0384 0.0053  229 ILE D CG1 
9545  C CG2 . ILE D 165 ? 0.8428 0.9394 0.6655 0.3047  -0.0646 -0.0283 229 ILE D CG2 
9546  C CD1 . ILE D 165 ? 0.8327 0.9088 0.6879 0.2691  -0.0443 -0.0012 229 ILE D CD1 
9547  N N   . ALA D 166 ? 0.9669 1.0979 0.7748 0.3239  -0.0800 -0.0577 230 ALA D N   
9548  C CA  . ALA D 166 ? 0.9987 1.1395 0.7933 0.3433  -0.0956 -0.0758 230 ALA D CA  
9549  C C   . ALA D 166 ? 1.0992 1.2385 0.8935 0.3516  -0.1065 -0.0850 230 ALA D C   
9550  O O   . ALA D 166 ? 1.1212 1.2580 0.9360 0.3367  -0.1065 -0.0868 230 ALA D O   
9551  C CB  . ALA D 166 ? 0.7994 0.9543 0.6124 0.3339  -0.1057 -0.0952 230 ALA D CB  
9552  N N   . ASP D 167 ? 1.3337 1.4750 1.1035 0.3771  -0.1163 -0.0917 231 ASP D N   
9553  C CA  . ASP D 167 ? 1.4253 1.5670 1.1908 0.3906  -0.1290 -0.1023 231 ASP D CA  
9554  C C   . ASP D 167 ? 1.5025 1.6590 1.2652 0.4063  -0.1484 -0.1259 231 ASP D C   
9555  O O   . ASP D 167 ? 1.4477 1.6085 1.1977 0.4152  -0.1506 -0.1292 231 ASP D O   
9556  C CB  . ASP D 167 ? 1.5631 1.6881 1.2954 0.4109  -0.1219 -0.0842 231 ASP D CB  
9557  C CG  . ASP D 167 ? 2.0081 2.1270 1.7421 0.4159  -0.1288 -0.0877 231 ASP D CG  
9558  O OD1 . ASP D 167 ? 2.0533 2.1844 1.8126 0.4074  -0.1407 -0.1064 231 ASP D OD1 
9559  O OD2 . ASP D 167 ? 2.1355 2.2373 1.8456 0.4287  -0.1218 -0.0711 231 ASP D OD2 
9560  N N   . GLY D 168 ? 1.4768 1.6414 1.2524 0.4103  -0.1631 -0.1429 232 GLY D N   
9561  C CA  . GLY D 168 ? 1.3839 1.5614 1.1562 0.4285  -0.1836 -0.1653 232 GLY D CA  
9562  C C   . GLY D 168 ? 1.4156 1.6116 1.2274 0.4142  -0.1975 -0.1883 232 GLY D C   
9563  O O   . GLY D 168 ? 1.0257 1.2264 0.8671 0.3883  -0.1905 -0.1881 232 GLY D O   
9564  N N   . THR D 169 ? 1.9329 2.1394 1.7449 0.4323  -0.2174 -0.2081 233 THR D N   
9565  C CA  . THR D 169 ? 1.8727 2.0988 1.7246 0.4218  -0.2323 -0.2307 233 THR D CA  
9566  C C   . THR D 169 ? 1.6884 1.9243 1.5632 0.4071  -0.2371 -0.2422 233 THR D C   
9567  O O   . THR D 169 ? 1.3407 1.5884 1.2543 0.3846  -0.2374 -0.2504 233 THR D O   
9568  C CB  . THR D 169 ? 1.6503 1.8854 1.4961 0.4477  -0.2541 -0.2495 233 THR D CB  
9569  O OG1 . THR D 169 ? 1.9253 2.1482 1.7445 0.4640  -0.2497 -0.2378 233 THR D OG1 
9570  C CG2 . THR D 169 ? 1.3872 1.6446 1.2795 0.4357  -0.2678 -0.2713 233 THR D CG2 
9571  N N   . THR D 170 ? 1.5881 1.8184 1.4376 0.4208  -0.2406 -0.2423 234 THR D N   
9572  C CA  . THR D 170 ? 1.5442 1.7806 1.4102 0.4103  -0.2467 -0.2534 234 THR D CA  
9573  C C   . THR D 170 ? 1.4970 1.7210 1.3295 0.4188  -0.2372 -0.2402 234 THR D C   
9574  O O   . THR D 170 ? 1.4032 1.6158 1.1986 0.4371  -0.2285 -0.2249 234 THR D O   
9575  C CB  . THR D 170 ? 1.5646 1.8153 1.4472 0.4220  -0.2733 -0.2814 234 THR D CB  
9576  O OG1 . THR D 170 ? 1.7325 1.9865 1.6326 0.4099  -0.2791 -0.2913 234 THR D OG1 
9577  C CG2 . THR D 170 ? 1.3219 1.5679 1.1652 0.4581  -0.2875 -0.2877 234 THR D CG2 
9578  N N   . TYR D 171 ? 1.4875 1.7139 1.3339 0.4058  -0.2384 -0.2460 235 TYR D N   
9579  C CA  . TYR D 171 ? 1.4292 1.6462 1.2512 0.4085  -0.2269 -0.2330 235 TYR D CA  
9580  C C   . TYR D 171 ? 1.3268 1.5404 1.1108 0.4406  -0.2379 -0.2388 235 TYR D C   
9581  O O   . TYR D 171 ? 1.2810 1.4861 1.0336 0.4516  -0.2254 -0.2232 235 TYR D O   
9582  C CB  . TYR D 171 ? 1.3695 1.5895 1.2193 0.3844  -0.2257 -0.2382 235 TYR D CB  
9583  C CG  . TYR D 171 ? 2.0707 2.2942 1.9569 0.3547  -0.2160 -0.2339 235 TYR D CG  
9584  C CD1 . TYR D 171 ? 2.0143 2.2300 1.8967 0.3431  -0.1956 -0.2126 235 TYR D CD1 
9585  C CD2 . TYR D 171 ? 2.3071 2.5415 2.2316 0.3392  -0.2274 -0.2512 235 TYR D CD2 
9586  C CE1 . TYR D 171 ? 1.6283 1.8465 1.5409 0.3186  -0.1877 -0.2096 235 TYR D CE1 
9587  C CE2 . TYR D 171 ? 2.0963 2.3343 2.0515 0.3142  -0.2173 -0.2466 235 TYR D CE2 
9588  C CZ  . TYR D 171 ? 1.8642 2.0937 1.8113 0.3050  -0.1979 -0.2263 235 TYR D CZ  
9589  O OH  . TYR D 171 ? 2.0905 2.3227 2.0647 0.2828  -0.1890 -0.2228 235 TYR D OH  
9590  N N   . THR D 172 ? 1.2661 1.4871 1.0538 0.4564  -0.2615 -0.2615 236 THR D N   
9591  C CA  . THR D 172 ? 1.2987 1.5160 1.0473 0.4917  -0.2749 -0.2690 236 THR D CA  
9592  C C   . THR D 172 ? 1.3351 1.5419 1.0445 0.5109  -0.2604 -0.2477 236 THR D C   
9593  O O   . THR D 172 ? 1.3335 1.5323 1.0004 0.5369  -0.2577 -0.2403 236 THR D O   
9594  C CB  . THR D 172 ? 1.4221 1.6499 1.1876 0.5036  -0.3041 -0.2980 236 THR D CB  
9595  O OG1 . THR D 172 ? 1.4859 1.7174 1.2568 0.5076  -0.3060 -0.2977 236 THR D OG1 
9596  C CG2 . THR D 172 ? 1.2105 1.4491 1.0261 0.4767  -0.3142 -0.3150 236 THR D CG2 
9597  N N   . ALA D 173 ? 1.3428 1.5487 1.0663 0.4976  -0.2499 -0.2368 237 ALA D N   
9598  C CA  . ALA D 173 ? 1.4089 1.6038 1.1000 0.5152  -0.2397 -0.2191 237 ALA D CA  
9599  C C   . ALA D 173 ? 1.3431 1.5273 1.0320 0.4978  -0.2119 -0.1900 237 ALA D C   
9600  O O   . ALA D 173 ? 1.3486 1.5228 1.0203 0.5058  -0.2029 -0.1750 237 ALA D O   
9601  C CB  . ALA D 173 ? 1.5065 1.7072 1.2111 0.5209  -0.2543 -0.2324 237 ALA D CB  
9602  N N   . SER D 174 ? 1.3027 1.4879 1.0089 0.4747  -0.1993 -0.1822 238 SER D N   
9603  C CA  . SER D 174 ? 1.3082 1.4849 1.0213 0.4542  -0.1756 -0.1577 238 SER D CA  
9604  C C   . SER D 174 ? 1.2659 1.4295 0.9416 0.4702  -0.1575 -0.1322 238 SER D C   
9605  O O   . SER D 174 ? 1.3387 1.5007 0.9816 0.4945  -0.1589 -0.1309 238 SER D O   
9606  C CB  . SER D 174 ? 1.3529 1.5344 1.0947 0.4264  -0.1682 -0.1574 238 SER D CB  
9607  O OG  . SER D 174 ? 1.4082 1.5905 1.1321 0.4360  -0.1668 -0.1568 238 SER D OG  
9608  N N   . SER D 175 ? 1.2006 1.3545 0.8825 0.4562  -0.1406 -0.1120 239 SER D N   
9609  C CA  . SER D 175 ? 1.3225 1.4631 0.9774 0.4652  -0.1206 -0.0845 239 SER D CA  
9610  C C   . SER D 175 ? 1.2775 1.4153 0.9583 0.4358  -0.1026 -0.0683 239 SER D C   
9611  O O   . SER D 175 ? 1.6972 1.8370 1.4101 0.4124  -0.1050 -0.0746 239 SER D O   
9612  C CB  . SER D 175 ? 1.6037 1.7318 1.2418 0.4787  -0.1205 -0.0762 239 SER D CB  
9613  O OG  . SER D 175 ? 1.7917 1.9048 1.4093 0.4831  -0.0995 -0.0472 239 SER D OG  
9614  N N   . HIS D 176 ? 1.1339 1.2677 0.8015 0.4373  -0.0845 -0.0477 240 HIS D N   
9615  C CA  . HIS D 176 ? 1.0502 1.1814 0.7438 0.4101  -0.0681 -0.0321 240 HIS D CA  
9616  C C   . HIS D 176 ? 1.0128 1.1318 0.6933 0.4129  -0.0471 -0.0028 240 HIS D C   
9617  O O   . HIS D 176 ? 1.0158 1.1342 0.6674 0.4334  -0.0379 0.0096  240 HIS D O   
9618  C CB  . HIS D 176 ? 1.0794 1.2224 0.7861 0.3995  -0.0674 -0.0390 240 HIS D CB  
9619  C CG  . HIS D 176 ? 1.0697 1.2233 0.7913 0.3954  -0.0874 -0.0666 240 HIS D CG  
9620  N ND1 . HIS D 176 ? 1.0768 1.2351 0.8325 0.3712  -0.0948 -0.0803 240 HIS D ND1 
9621  C CD2 . HIS D 176 ? 1.0910 1.2509 0.7932 0.4174  -0.1025 -0.0831 240 HIS D CD2 
9622  C CE1 . HIS D 176 ? 1.1077 1.2754 0.8661 0.3778  -0.1130 -0.1034 240 HIS D CE1 
9623  N NE2 . HIS D 176 ? 1.1968 1.3652 0.9230 0.4061  -0.1187 -0.1060 240 HIS D NE2 
9624  N N   . ARG D 177 ? 1.0178 1.1267 0.7203 0.3926  -0.0394 0.0084  241 ARG D N   
9625  C CA  . ARG D 177 ? 0.9985 1.0943 0.6972 0.3900  -0.0195 0.0371  241 ARG D CA  
9626  C C   . ARG D 177 ? 0.9573 1.0561 0.6882 0.3630  -0.0081 0.0459  241 ARG D C   
9627  O O   . ARG D 177 ? 0.9631 1.0673 0.7219 0.3423  -0.0160 0.0318  241 ARG D O   
9628  C CB  . ARG D 177 ? 0.9565 1.0344 0.6523 0.3912  -0.0206 0.0444  241 ARG D CB  
9629  C CG  . ARG D 177 ? 1.0708 1.1452 0.7334 0.4197  -0.0322 0.0360  241 ARG D CG  
9630  C CD  . ARG D 177 ? 1.3406 1.4093 1.0145 0.4151  -0.0465 0.0223  241 ARG D CD  
9631  N NE  . ARG D 177 ? 1.6045 1.6517 1.2732 0.4149  -0.0380 0.0416  241 ARG D NE  
9632  C CZ  . ARG D 177 ? 1.4109 1.4447 1.0476 0.4389  -0.0385 0.0498  241 ARG D CZ  
9633  N NH1 . ARG D 177 ? 1.2878 1.3279 0.8935 0.4663  -0.0475 0.0400  241 ARG D NH1 
9634  N NH2 . ARG D 177 ? 1.3988 1.4111 1.0338 0.4362  -0.0308 0.0676  241 ARG D NH2 
9635  N N   . LEU D 178 ? 0.9328 1.0285 0.6592 0.3644  0.0108  0.0700  242 LEU D N   
9636  C CA  . LEU D 178 ? 0.9435 1.0426 0.6997 0.3415  0.0225  0.0806  242 LEU D CA  
9637  C C   . LEU D 178 ? 0.9662 1.0472 0.7359 0.3297  0.0322  0.1003  242 LEU D C   
9638  O O   . LEU D 178 ? 1.1463 1.2177 0.8986 0.3423  0.0449  0.1214  242 LEU D O   
9639  C CB  . LEU D 178 ? 0.9861 1.0966 0.7291 0.3532  0.0373  0.0940  242 LEU D CB  
9640  C CG  . LEU D 178 ? 1.0371 1.1525 0.8046 0.3369  0.0550  0.1126  242 LEU D CG  
9641  C CD1 . LEU D 178 ? 1.1280 1.2501 0.9300 0.3115  0.0470  0.0981  242 LEU D CD1 
9642  C CD2 . LEU D 178 ? 1.1363 1.2660 0.8821 0.3563  0.0662  0.1205  242 LEU D CD2 
9643  N N   . TYR D 179 ? 0.9483 1.0233 0.7479 0.3066  0.0258  0.0934  243 TYR D N   
9644  C CA  . TYR D 179 ? 0.9156 0.9711 0.7290 0.2954  0.0315  0.1090  243 TYR D CA  
9645  C C   . TYR D 179 ? 0.9337 0.9888 0.7765 0.2757  0.0451  0.1258  243 TYR D C   
9646  O O   . TYR D 179 ? 0.9668 1.0362 0.8275 0.2641  0.0453  0.1189  243 TYR D O   
9647  C CB  . TYR D 179 ? 0.8925 0.9399 0.7193 0.2843  0.0154  0.0913  243 TYR D CB  
9648  C CG  . TYR D 179 ? 0.9359 0.9763 0.7372 0.3033  0.0047  0.0826  243 TYR D CG  
9649  C CD1 . TYR D 179 ? 0.9685 1.0229 0.7578 0.3144  -0.0094 0.0597  243 TYR D CD1 
9650  C CD2 . TYR D 179 ? 0.9604 0.9801 0.7510 0.3103  0.0080  0.0969  243 TYR D CD2 
9651  C CE1 . TYR D 179 ? 1.0341 1.0839 0.8027 0.3322  -0.0204 0.0505  243 TYR D CE1 
9652  C CE2 . TYR D 179 ? 1.0787 1.0921 0.8456 0.3288  -0.0026 0.0884  243 TYR D CE2 
9653  C CZ  . TYR D 179 ? 1.2357 1.2653 0.9923 0.3399  -0.0170 0.0647  243 TYR D CZ  
9654  O OH  . TYR D 179 ? 1.4639 1.4889 1.1994 0.3589  -0.0287 0.0552  243 TYR D OH  
9655  N N   . ARG D 180 ? 1.0360 1.0741 0.8853 0.2719  0.0557  0.1478  244 ARG D N   
9656  C CA  . ARG D 180 ? 1.0439 1.0789 0.9274 0.2509  0.0665  0.1633  244 ARG D CA  
9657  C C   . ARG D 180 ? 1.0653 1.0780 0.9690 0.2355  0.0587  0.1635  244 ARG D C   
9658  O O   . ARG D 180 ? 1.3084 1.3027 1.1960 0.2449  0.0564  0.1690  244 ARG D O   
9659  C CB  . ARG D 180 ? 1.2827 1.3182 1.1592 0.2601  0.0882  0.1921  244 ARG D CB  
9660  C CG  . ARG D 180 ? 1.4472 1.4734 1.3578 0.2415  0.1011  0.2145  244 ARG D CG  
9661  C CD  . ARG D 180 ? 1.4746 1.5031 1.3727 0.2549  0.1245  0.2440  244 ARG D CD  
9662  N NE  . ARG D 180 ? 2.0414 2.0486 1.9602 0.2437  0.1345  0.2680  244 ARG D NE  
9663  C CZ  . ARG D 180 ? 2.3698 2.3810 2.3228 0.2287  0.1503  0.2888  244 ARG D CZ  
9664  N NH1 . ARG D 180 ? 2.7598 2.7968 2.7285 0.2244  0.1587  0.2889  244 ARG D NH1 
9665  N NH2 . ARG D 180 ? 2.6434 2.6325 2.6162 0.2182  0.1574  0.3096  244 ARG D NH2 
9666  N N   . LEU D 181 ? 0.9407 0.9542 0.8777 0.2133  0.0535  0.1565  245 LEU D N   
9667  C CA  . LEU D 181 ? 0.9679 0.9608 0.9234 0.1994  0.0431  0.1522  245 LEU D CA  
9668  C C   . LEU D 181 ? 1.0227 1.0084 1.0143 0.1799  0.0505  0.1675  245 LEU D C   
9669  O O   . LEU D 181 ? 1.0264 1.0285 1.0356 0.1721  0.0584  0.1717  245 LEU D O   
9670  C CB  . LEU D 181 ? 0.8571 0.8560 0.8184 0.1917  0.0260  0.1248  245 LEU D CB  
9671  C CG  . LEU D 181 ? 0.9063 0.9172 0.8397 0.2078  0.0173  0.1065  245 LEU D CG  
9672  C CD1 . LEU D 181 ? 0.9759 0.9985 0.9213 0.1972  0.0057  0.0836  245 LEU D CD1 
9673  C CD2 . LEU D 181 ? 1.0382 1.0336 0.9516 0.2205  0.0097  0.1037  245 LEU D CD2 
9674  N N   . VAL D 182 ? 1.0783 1.0394 1.0822 0.1723  0.0469  0.1751  246 VAL D N   
9675  C CA  . VAL D 182 ? 1.0413 0.9928 1.0838 0.1525  0.0503  0.1872  246 VAL D CA  
9676  C C   . VAL D 182 ? 0.9940 0.9217 1.0481 0.1429  0.0334  0.1758  246 VAL D C   
9677  O O   . VAL D 182 ? 0.9519 0.8612 0.9863 0.1528  0.0280  0.1756  246 VAL D O   
9678  C CB  . VAL D 182 ? 1.1377 1.0785 1.1857 0.1544  0.0684  0.2183  246 VAL D CB  
9679  C CG1 . VAL D 182 ? 1.2908 1.2278 1.3856 0.1322  0.0726  0.2303  246 VAL D CG1 
9680  C CG2 . VAL D 182 ? 1.0571 1.0176 1.0813 0.1713  0.0860  0.2313  246 VAL D CG2 
9681  N N   . ASN D 183 ? 0.9891 0.9165 1.0741 0.1249  0.0247  0.1662  247 ASN D N   
9682  C CA  . ASN D 183 ? 0.9567 0.8619 1.0529 0.1164  0.0075  0.1535  247 ASN D CA  
9683  C C   . ASN D 183 ? 1.1550 1.0531 1.2192 0.1307  -0.0041 0.1369  247 ASN D C   
9684  O O   . ASN D 183 ? 1.1986 1.0728 1.2615 0.1311  -0.0149 0.1332  247 ASN D O   
9685  C CB  . ASN D 183 ? 0.9909 0.8701 1.1117 0.1067  0.0093  0.1723  247 ASN D CB  
9686  C CG  . ASN D 183 ? 1.0462 0.9338 1.2054 0.0907  0.0190  0.1867  247 ASN D CG  
9687  O OD1 . ASN D 183 ? 1.1062 1.0185 1.2742 0.0866  0.0229  0.1812  247 ASN D OD1 
9688  N ND2 . ASN D 183 ? 1.2337 1.1004 1.4178 0.0814  0.0225  0.2054  247 ASN D ND2 
9689  N N   . GLY D 184 ? 1.0766 0.9959 1.1159 0.1430  -0.0020 0.1270  248 GLY D N   
9690  C CA  . GLY D 184 ? 0.9845 0.9043 0.9988 0.1551  -0.0132 0.1083  248 GLY D CA  
9691  C C   . GLY D 184 ? 0.9874 0.9003 0.9718 0.1743  -0.0103 0.1152  248 GLY D C   
9692  O O   . GLY D 184 ? 1.0768 0.9929 1.0417 0.1855  -0.0195 0.0995  248 GLY D O   
9693  N N   . THR D 185 ? 1.0557 0.9596 1.0368 0.1788  0.0026  0.1388  249 THR D N   
9694  C CA  . THR D 185 ? 1.1853 1.0822 1.1343 0.1994  0.0063  0.1468  249 THR D CA  
9695  C C   . THR D 185 ? 1.2817 1.2000 1.2123 0.2119  0.0199  0.1554  249 THR D C   
9696  O O   . THR D 185 ? 1.1756 1.1075 1.1222 0.2033  0.0308  0.1642  249 THR D O   
9697  C CB  . THR D 185 ? 1.2030 1.0688 1.1548 0.1993  0.0098  0.1672  249 THR D CB  
9698  O OG1 . THR D 185 ? 1.2521 1.1140 1.2329 0.1837  0.0218  0.1872  249 THR D OG1 
9699  C CG2 . THR D 185 ? 1.1686 1.0126 1.1277 0.1942  -0.0075 0.1537  249 THR D CG2 
9700  N N   . SER D 186 ? 1.4998 1.4222 1.3968 0.2334  0.0181  0.1508  250 SER D N   
9701  C CA  . SER D 186 ? 1.3456 1.2862 1.2215 0.2482  0.0293  0.1577  250 SER D CA  
9702  C C   . SER D 186 ? 1.4438 1.3725 1.3158 0.2526  0.0480  0.1885  250 SER D C   
9703  O O   . SER D 186 ? 1.6976 1.6019 1.5613 0.2578  0.0497  0.2022  250 SER D O   
9704  C CB  . SER D 186 ? 1.3195 1.2678 1.1610 0.2711  0.0200  0.1425  250 SER D CB  
9705  O OG  . SER D 186 ? 1.7849 1.7110 1.6066 0.2845  0.0164  0.1486  250 SER D OG  
9706  N N   . ALA D 187 ? 1.4078 1.3536 1.2874 0.2499  0.0624  0.1999  251 ALA D N   
9707  C CA  . ALA D 187 ? 1.3131 1.2527 1.1895 0.2549  0.0833  0.2305  251 ALA D CA  
9708  C C   . ALA D 187 ? 1.2878 1.2426 1.1262 0.2806  0.0920  0.2340  251 ALA D C   
9709  O O   . ALA D 187 ? 1.1656 1.1307 1.0026 0.2849  0.1106  0.2533  251 ALA D O   
9710  C CB  . ALA D 187 ? 1.2849 1.2333 1.2010 0.2334  0.0945  0.2425  251 ALA D CB  
9711  N N   . GLY D 188 ? 1.3413 1.2983 1.1492 0.2984  0.0778  0.2145  252 GLY D N   
9712  C CA  . GLY D 188 ? 1.2810 1.2485 1.0488 0.3259  0.0824  0.2157  252 GLY D CA  
9713  C C   . GLY D 188 ? 1.2066 1.2010 0.9700 0.3299  0.0735  0.1922  252 GLY D C   
9714  O O   . GLY D 188 ? 1.1910 1.1970 0.9832 0.3103  0.0661  0.1771  252 GLY D O   
9715  N N   . TRP D 189 ? 1.1646 1.1674 0.8906 0.3564  0.0734  0.1889  253 TRP D N   
9716  C CA  . TRP D 189 ? 1.1450 1.1711 0.8638 0.3631  0.0630  0.1657  253 TRP D CA  
9717  C C   . TRP D 189 ? 1.2185 1.2525 0.8975 0.3926  0.0700  0.1717  253 TRP D C   
9718  O O   . TRP D 189 ? 1.4395 1.4610 1.0941 0.4092  0.0831  0.1937  253 TRP D O   
9719  C CB  . TRP D 189 ? 1.1869 1.2137 0.9063 0.3624  0.0394  0.1366  253 TRP D CB  
9720  C CG  . TRP D 189 ? 1.2692 1.2795 0.9591 0.3830  0.0324  0.1370  253 TRP D CG  
9721  C CD1 . TRP D 189 ? 1.2806 1.2683 0.9747 0.3784  0.0302  0.1444  253 TRP D CD1 
9722  C CD2 . TRP D 189 ? 1.1972 1.2109 0.8466 0.4140  0.0256  0.1295  253 TRP D CD2 
9723  N NE1 . TRP D 189 ? 1.2350 1.2126 0.8945 0.4037  0.0231  0.1422  253 TRP D NE1 
9724  C CE2 . TRP D 189 ? 1.2201 1.2127 0.8516 0.4262  0.0198  0.1332  253 TRP D CE2 
9725  C CE3 . TRP D 189 ? 1.2437 1.2742 0.8701 0.4332  0.0223  0.1194  253 TRP D CE3 
9726  C CZ2 . TRP D 189 ? 1.1696 1.1592 0.7615 0.4569  0.0111  0.1270  253 TRP D CZ2 
9727  C CZ3 . TRP D 189 ? 1.3739 1.4010 0.9607 0.4640  0.0130  0.1126  253 TRP D CZ3 
9728  C CH2 . TRP D 189 ? 1.2404 1.2478 0.8105 0.4756  0.0075  0.1162  253 TRP D CH2 
9729  N N   . LYS D 190 ? 1.2426 1.2964 0.9139 0.4003  0.0610  0.1520  254 LYS D N   
9730  C CA  . LYS D 190 ? 1.1609 1.2232 0.7923 0.4307  0.0637  0.1525  254 LYS D CA  
9731  C C   . LYS D 190 ? 1.1811 1.2555 0.8023 0.4406  0.0399  0.1196  254 LYS D C   
9732  O O   . LYS D 190 ? 1.2180 1.3027 0.8677 0.4210  0.0284  0.1002  254 LYS D O   
9733  C CB  . LYS D 190 ? 1.1087 1.1857 0.7446 0.4299  0.0828  0.1681  254 LYS D CB  
9734  C CG  . LYS D 190 ? 1.2142 1.3022 0.8091 0.4617  0.0843  0.1656  254 LYS D CG  
9735  C CD  . LYS D 190 ? 1.3015 1.3959 0.8879 0.4701  0.1113  0.1942  254 LYS D CD  
9736  C CE  . LYS D 190 ? 1.4167 1.5217 0.9582 0.5049  0.1108  0.1890  254 LYS D CE  
9737  N NZ  . LYS D 190 ? 1.6884 1.7985 1.2144 0.5187  0.1390  0.2194  254 LYS D NZ  
9738  N N   . ALA D 191 ? 1.2356 1.3077 0.8169 0.4711  0.0318  0.1131  255 ALA D N   
9739  C CA  . ALA D 191 ? 1.2376 1.3222 0.8100 0.4824  0.0090  0.0821  255 ALA D CA  
9740  C C   . ALA D 191 ? 1.2903 1.3930 0.8613 0.4855  0.0123  0.0770  255 ALA D C   
9741  O O   . ALA D 191 ? 1.3804 1.4855 0.9309 0.4998  0.0296  0.0960  255 ALA D O   
9742  C CB  . ALA D 191 ? 1.1358 1.2130 0.6659 0.5159  -0.0020 0.0757  255 ALA D CB  
9743  N N   . LEU D 192 ? 1.3112 1.4264 0.9046 0.4720  -0.0036 0.0521  256 LEU D N   
9744  C CA  . LEU D 192 ? 1.3265 1.4573 0.9159 0.4777  -0.0051 0.0428  256 LEU D CA  
9745  C C   . LEU D 192 ? 1.5641 1.6986 1.1222 0.5064  -0.0252 0.0205  256 LEU D C   
9746  O O   . LEU D 192 ? 1.6979 1.8305 1.2616 0.5062  -0.0452 0.0002  256 LEU D O   
9747  C CB  . LEU D 192 ? 1.1951 1.3353 0.8257 0.4474  -0.0116 0.0286  256 LEU D CB  
9748  C CG  . LEU D 192 ? 1.0778 1.2160 0.7413 0.4192  0.0058  0.0473  256 LEU D CG  
9749  C CD1 . LEU D 192 ? 1.0935 1.2401 0.7908 0.3943  -0.0040 0.0297  256 LEU D CD1 
9750  C CD2 . LEU D 192 ? 1.1852 1.3286 0.8394 0.4262  0.0282  0.0712  256 LEU D CD2 
9751  N N   . ASP D 193 ? 1.6324 1.7728 1.1583 0.5318  -0.0202 0.0242  257 ASP D N   
9752  C CA  . ASP D 193 ? 1.5330 1.6765 1.0265 0.5620  -0.0403 0.0023  257 ASP D CA  
9753  C C   . ASP D 193 ? 1.5294 1.6850 1.0440 0.5520  -0.0607 -0.0268 257 ASP D C   
9754  O O   . ASP D 193 ? 1.5307 1.6956 1.0457 0.5521  -0.0564 -0.0281 257 ASP D O   
9755  C CB  . ASP D 193 ? 1.4751 1.6191 0.9230 0.5955  -0.0273 0.0173  257 ASP D CB  
9756  C CG  . ASP D 193 ? 1.6833 1.8285 1.0939 0.6301  -0.0496 -0.0059 257 ASP D CG  
9757  O OD1 . ASP D 193 ? 1.9755 2.1207 1.3972 0.6280  -0.0753 -0.0327 257 ASP D OD1 
9758  O OD2 . ASP D 193 ? 1.6371 1.7834 1.0073 0.6603  -0.0416 0.0027  257 ASP D OD2 
9759  N N   . THR D 194 ? 1.6662 1.8214 1.1979 0.5447  -0.0828 -0.0500 258 THR D N   
9760  C CA  . THR D 194 ? 1.6286 1.7932 1.1889 0.5291  -0.1017 -0.0764 258 THR D CA  
9761  C C   . THR D 194 ? 1.6956 1.8636 1.2332 0.5563  -0.1266 -0.1024 258 THR D C   
9762  O O   . THR D 194 ? 1.6014 1.7767 1.1563 0.5490  -0.1421 -0.1237 258 THR D O   
9763  C CB  . THR D 194 ? 1.7560 1.9195 1.3568 0.4999  -0.1091 -0.0850 258 THR D CB  
9764  O OG1 . THR D 194 ? 1.7564 1.9286 1.3888 0.4802  -0.1221 -0.1055 258 THR D OG1 
9765  C CG2 . THR D 194 ? 1.6746 1.8334 1.2653 0.5148  -0.1250 -0.0963 258 THR D CG2 
9766  N N   . THR D 195 ? 2.0280 2.1894 1.5267 0.5881  -0.1308 -0.1005 259 THR D N   
9767  C CA  . THR D 195 ? 1.9352 2.0980 1.4159 0.6139  -0.1590 -0.1281 259 THR D CA  
9768  C C   . THR D 195 ? 1.6059 1.7767 1.0870 0.6201  -0.1748 -0.1497 259 THR D C   
9769  O O   . THR D 195 ? 1.3128 1.4857 0.7771 0.6276  -0.1626 -0.1399 259 THR D O   
9770  C CB  . THR D 195 ? 1.7581 1.9115 1.1862 0.6543  -0.1598 -0.1211 259 THR D CB  
9771  O OG1 . THR D 195 ? 1.6235 1.7751 1.0153 0.6739  -0.1401 -0.1008 259 THR D OG1 
9772  C CG2 . THR D 195 ? 1.5932 1.7363 1.0207 0.6509  -0.1513 -0.1057 259 THR D CG2 
9773  N N   . GLY D 196 ? 1.5365 1.7118 1.0389 0.6167  -0.2021 -0.1790 260 GLY D N   
9774  C CA  . GLY D 196 ? 1.4928 1.6736 1.0020 0.6192  -0.2205 -0.2022 260 GLY D CA  
9775  C C   . GLY D 196 ? 1.5082 1.6949 1.0662 0.5807  -0.2189 -0.2072 260 GLY D C   
9776  O O   . GLY D 196 ? 1.4956 1.6858 1.0705 0.5765  -0.2385 -0.2302 260 GLY D O   
9777  N N   . PHE D 197 ? 1.4182 1.6046 0.9983 0.5530  -0.1963 -0.1859 261 PHE D N   
9778  C CA  . PHE D 197 ? 1.1765 1.3671 0.8012 0.5170  -0.1945 -0.1899 261 PHE D CA  
9779  C C   . PHE D 197 ? 1.1557 1.3454 0.8108 0.4890  -0.1824 -0.1777 261 PHE D C   
9780  O O   . PHE D 197 ? 1.2611 1.4470 0.9060 0.4972  -0.1794 -0.1700 261 PHE D O   
9781  C CB  . PHE D 197 ? 1.0608 1.2527 0.6820 0.5112  -0.1803 -0.1794 261 PHE D CB  
9782  C CG  . PHE D 197 ? 1.0851 1.2751 0.6961 0.5069  -0.1512 -0.1485 261 PHE D CG  
9783  C CD1 . PHE D 197 ? 1.0797 1.2701 0.7235 0.4744  -0.1357 -0.1352 261 PHE D CD1 
9784  C CD2 . PHE D 197 ? 1.1168 1.3045 0.6861 0.5357  -0.1391 -0.1323 261 PHE D CD2 
9785  C CE1 . PHE D 197 ? 1.0717 1.2605 0.7104 0.4693  -0.1098 -0.1070 261 PHE D CE1 
9786  C CE2 . PHE D 197 ? 1.1287 1.3154 0.6931 0.5301  -0.1110 -0.1023 261 PHE D CE2 
9787  C CZ  . PHE D 197 ? 1.0144 1.2019 0.6153 0.4963  -0.0971 -0.0902 261 PHE D CZ  
9788  N N   . ASN D 198 ? 1.0476 1.2397 0.7381 0.4576  -0.1763 -0.1766 262 ASN D N   
9789  C CA  . ASN D 198 ? 1.0007 1.1918 0.7222 0.4301  -0.1668 -0.1679 262 ASN D CA  
9790  C C   . ASN D 198 ? 1.1710 1.3610 0.9126 0.4034  -0.1484 -0.1528 262 ASN D C   
9791  O O   . ASN D 198 ? 1.1985 1.3907 0.9458 0.3974  -0.1497 -0.1580 262 ASN D O   
9792  C CB  . ASN D 198 ? 0.8920 1.0886 0.6434 0.4195  -0.1864 -0.1904 262 ASN D CB  
9793  C CG  . ASN D 198 ? 1.0784 1.2761 0.8676 0.3870  -0.1785 -0.1866 262 ASN D CG  
9794  O OD1 . ASN D 198 ? 1.2951 1.4959 1.1099 0.3682  -0.1827 -0.1961 262 ASN D OD1 
9795  N ND2 . ASN D 198 ? 1.2075 1.4015 0.9991 0.3811  -0.1674 -0.1728 262 ASN D ND2 
9796  N N   . PHE D 199 ? 1.0475 1.2329 0.7992 0.3885  -0.1325 -0.1349 263 PHE D N   
9797  C CA  . PHE D 199 ? 0.9176 1.1007 0.6803 0.3700  -0.1136 -0.1169 263 PHE D CA  
9798  C C   . PHE D 199 ? 1.0062 1.1857 0.7981 0.3443  -0.1082 -0.1122 263 PHE D C   
9799  O O   . PHE D 199 ? 1.1627 1.3358 0.9513 0.3436  -0.0982 -0.0972 263 PHE D O   
9800  C CB  . PHE D 199 ? 0.8931 1.0726 0.6278 0.3861  -0.0961 -0.0938 263 PHE D CB  
9801  C CG  . PHE D 199 ? 0.8519 1.0311 0.5979 0.3702  -0.0771 -0.0752 263 PHE D CG  
9802  C CD1 . PHE D 199 ? 0.8301 1.0155 0.5789 0.3673  -0.0757 -0.0785 263 PHE D CD1 
9803  C CD2 . PHE D 199 ? 0.8895 1.0620 0.6439 0.3588  -0.0613 -0.0547 263 PHE D CD2 
9804  C CE1 . PHE D 199 ? 0.8118 0.9985 0.5730 0.3531  -0.0587 -0.0619 263 PHE D CE1 
9805  C CE2 . PHE D 199 ? 0.9259 1.0990 0.6945 0.3436  -0.0447 -0.0380 263 PHE D CE2 
9806  C CZ  . PHE D 199 ? 0.8488 1.0300 0.6214 0.3407  -0.0434 -0.0419 263 PHE D CZ  
9807  N N   . GLU D 200 ? 1.2089 1.3913 1.0286 0.3238  -0.1149 -0.1247 264 GLU D N   
9808  C CA  . GLU D 200 ? 1.1960 1.3756 1.0421 0.3017  -0.1118 -0.1232 264 GLU D CA  
9809  C C   . GLU D 200 ? 1.2170 1.3937 1.0827 0.2781  -0.1013 -0.1157 264 GLU D C   
9810  O O   . GLU D 200 ? 1.2605 1.4394 1.1267 0.2754  -0.1012 -0.1184 264 GLU D O   
9811  C CB  . GLU D 200 ? 1.2006 1.3864 1.0648 0.2978  -0.1286 -0.1444 264 GLU D CB  
9812  C CG  . GLU D 200 ? 1.5124 1.7016 1.3616 0.3199  -0.1409 -0.1536 264 GLU D CG  
9813  C CD  . GLU D 200 ? 1.9152 2.1020 1.7710 0.3173  -0.1389 -0.1494 264 GLU D CD  
9814  O OE1 . GLU D 200 ? 1.9529 2.1362 1.8281 0.2970  -0.1298 -0.1423 264 GLU D OE1 
9815  O OE2 . GLU D 200 ? 1.5649 1.7528 1.4051 0.3372  -0.1474 -0.1542 264 GLU D OE2 
9816  N N   . PHE D 201 ? 0.9495 1.1204 0.8302 0.2625  -0.0935 -0.1069 265 PHE D N   
9817  C CA  . PHE D 201 ? 0.7136 0.8809 0.6135 0.2408  -0.0859 -0.1020 265 PHE D CA  
9818  C C   . PHE D 201 ? 0.7333 0.9006 0.6247 0.2425  -0.0758 -0.0902 265 PHE D C   
9819  O O   . PHE D 201 ? 0.8658 1.0349 0.7662 0.2331  -0.0768 -0.0954 265 PHE D O   
9820  C CB  . PHE D 201 ? 0.7204 0.8915 0.6395 0.2279  -0.0959 -0.1192 265 PHE D CB  
9821  C CG  . PHE D 201 ? 0.8122 0.9876 0.7423 0.2275  -0.1061 -0.1322 265 PHE D CG  
9822  C CD1 . PHE D 201 ? 0.8802 1.0519 0.8203 0.2197  -0.1021 -0.1278 265 PHE D CD1 
9823  C CD2 . PHE D 201 ? 0.8459 1.0292 0.7782 0.2353  -0.1203 -0.1496 265 PHE D CD2 
9824  C CE1 . PHE D 201 ? 0.9286 1.1066 0.8801 0.2204  -0.1109 -0.1398 265 PHE D CE1 
9825  C CE2 . PHE D 201 ? 0.9870 1.1768 0.9336 0.2347  -0.1298 -0.1618 265 PHE D CE2 
9826  C CZ  . PHE D 201 ? 0.9679 1.1559 0.9240 0.2275  -0.1244 -0.1565 265 PHE D CZ  
9827  N N   . PRO D 202 ? 0.6723 0.8379 0.5470 0.2550  -0.0656 -0.0739 266 PRO D N   
9828  C CA  . PRO D 202 ? 0.7332 0.9013 0.6029 0.2566  -0.0543 -0.0614 266 PRO D CA  
9829  C C   . PRO D 202 ? 0.6534 0.8179 0.5462 0.2345  -0.0473 -0.0553 266 PRO D C   
9830  O O   . PRO D 202 ? 0.7280 0.8849 0.6351 0.2214  -0.0458 -0.0520 266 PRO D O   
9831  C CB  . PRO D 202 ? 0.7573 0.9226 0.6099 0.2706  -0.0425 -0.0423 266 PRO D CB  
9832  C CG  . PRO D 202 ? 0.6780 0.8356 0.5326 0.2694  -0.0463 -0.0429 266 PRO D CG  
9833  C CD  . PRO D 202 ? 0.7028 0.8640 0.5626 0.2684  -0.0629 -0.0651 266 PRO D CD  
9834  N N   . THR D 203 ? 0.6405 0.8100 0.5360 0.2318  -0.0441 -0.0547 267 THR D N   
9835  C CA  . THR D 203 ? 0.6993 0.8657 0.6158 0.2126  -0.0388 -0.0501 267 THR D CA  
9836  C C   . THR D 203 ? 0.6588 0.8317 0.5726 0.2179  -0.0261 -0.0348 267 THR D C   
9837  O O   . THR D 203 ? 0.7217 0.9032 0.6199 0.2328  -0.0256 -0.0364 267 THR D O   
9838  C CB  . THR D 203 ? 0.7006 0.8662 0.6277 0.2011  -0.0493 -0.0672 267 THR D CB  
9839  O OG1 . THR D 203 ? 0.7420 0.9027 0.6877 0.1834  -0.0448 -0.0626 267 THR D OG1 
9840  C CG2 . THR D 203 ? 0.8990 1.0719 0.8137 0.2126  -0.0545 -0.0760 267 THR D CG2 
9841  N N   . CYS D 204 ? 0.7847 0.9539 0.7144 0.2067  -0.0158 -0.0198 268 CYS D N   
9842  C CA  . CYS D 204 ? 0.8579 1.0339 0.7863 0.2136  -0.0009 -0.0007 268 CYS D CA  
9843  C C   . CYS D 204 ? 0.7571 0.9359 0.7097 0.1990  0.0065  0.0077  268 CYS D C   
9844  O O   . CYS D 204 ? 0.8763 1.0477 0.8478 0.1817  0.0011  0.0021  268 CYS D O   
9845  C CB  . CYS D 204 ? 0.9769 1.1459 0.9001 0.2188  0.0067  0.0143  268 CYS D CB  
9846  S SG  . CYS D 204 ? 1.4508 1.6166 1.3458 0.2377  -0.0026 0.0047  268 CYS D SG  
9847  N N   . TYR D 205 ? 0.7949 0.9852 0.7469 0.2070  0.0191  0.0214  269 TYR D N   
9848  C CA  . TYR D 205 ? 0.7717 0.9668 0.7504 0.1940  0.0280  0.0327  269 TYR D CA  
9849  C C   . TYR D 205 ? 0.7866 0.9916 0.7656 0.2037  0.0461  0.0552  269 TYR D C   
9850  O O   . TYR D 205 ? 0.8109 1.0182 0.7654 0.2218  0.0518  0.0619  269 TYR D O   
9851  C CB  . TYR D 205 ? 0.7054 0.9086 0.6909 0.1902  0.0227  0.0212  269 TYR D CB  
9852  C CG  . TYR D 205 ? 0.7017 0.9186 0.6659 0.2095  0.0251  0.0183  269 TYR D CG  
9853  C CD1 . TYR D 205 ? 0.7625 0.9954 0.7346 0.2144  0.0368  0.0290  269 TYR D CD1 
9854  C CD2 . TYR D 205 ? 0.6889 0.9033 0.6260 0.2236  0.0149  0.0043  269 TYR D CD2 
9855  C CE1 . TYR D 205 ? 0.7602 1.0056 0.7106 0.2342  0.0388  0.0257  269 TYR D CE1 
9856  C CE2 . TYR D 205 ? 0.7619 0.9872 0.6778 0.2429  0.0152  0.0002  269 TYR D CE2 
9857  C CZ  . TYR D 205 ? 0.8038 1.0443 0.7249 0.2488  0.0273  0.0109  269 TYR D CZ  
9858  O OH  . TYR D 205 ? 0.7279 0.9788 0.6257 0.2700  0.0273  0.0062  269 TYR D OH  
9859  N N   . TYR D 206 ? 0.7839 0.9950 0.7911 0.1920  0.0552  0.0672  270 TYR D N   
9860  C CA  . TYR D 206 ? 0.8766 1.0977 0.8903 0.1983  0.0743  0.0909  270 TYR D CA  
9861  C C   . TYR D 206 ? 1.0927 1.3338 1.1229 0.1985  0.0828  0.0956  270 TYR D C   
9862  O O   . TYR D 206 ? 1.3388 1.5814 1.3936 0.1835  0.0762  0.0877  270 TYR D O   
9863  C CB  . TYR D 206 ? 0.8405 1.0491 0.8787 0.1834  0.0794  0.1058  270 TYR D CB  
9864  C CG  . TYR D 206 ? 0.7501 0.9688 0.8040 0.1854  0.1001  0.1320  270 TYR D CG  
9865  C CD1 . TYR D 206 ? 0.7718 0.9978 0.8657 0.1692  0.1059  0.1410  270 TYR D CD1 
9866  C CD2 . TYR D 206 ? 0.8043 1.0258 0.8338 0.2041  0.1139  0.1479  270 TYR D CD2 
9867  C CE1 . TYR D 206 ? 0.8599 1.0969 0.9727 0.1698  0.1258  0.1659  270 TYR D CE1 
9868  C CE2 . TYR D 206 ? 0.9129 1.1441 0.9573 0.2060  0.1350  0.1739  270 TYR D CE2 
9869  C CZ  . TYR D 206 ? 0.9364 1.1760 1.0244 0.1879  0.1412  0.1831  270 TYR D CZ  
9870  O OH  . TYR D 206 ? 1.0670 1.3177 1.1751 0.1881  0.1630  0.2098  270 TYR D OH  
9871  N N   . THR D 207 ? 1.1250 1.3815 1.1402 0.2170  0.0976  0.1085  271 THR D N   
9872  C CA  . THR D 207 ? 1.0290 1.3074 1.0610 0.2193  0.1096  0.1172  271 THR D CA  
9873  C C   . THR D 207 ? 0.9299 1.2222 0.9494 0.2379  0.1315  0.1400  271 THR D C   
9874  O O   . THR D 207 ? 0.8220 1.1090 0.8067 0.2563  0.1337  0.1423  271 THR D O   
9875  C CB  . THR D 207 ? 1.0783 1.3653 1.0977 0.2266  0.0982  0.0965  271 THR D CB  
9876  O OG1 . THR D 207 ? 1.4932 1.8019 1.5335 0.2272  0.1092  0.1045  271 THR D OG1 
9877  C CG2 . THR D 207 ? 0.9606 1.2480 0.9355 0.2517  0.0944  0.0876  271 THR D CG2 
9878  N N   . SER D 208 ? 1.0994 1.4101 1.1478 0.2337  0.1479  0.1570  272 SER D N   
9879  C CA  . SER D 208 ? 1.2261 1.5551 1.2636 0.2530  0.1710  0.1789  272 SER D CA  
9880  C C   . SER D 208 ? 1.1596 1.4751 1.1754 0.2625  0.1810  0.1958  272 SER D C   
9881  O O   . SER D 208 ? 1.0415 1.3616 1.0197 0.2879  0.1898  0.2020  272 SER D O   
9882  C CB  . SER D 208 ? 1.3062 1.6499 1.3102 0.2774  0.1690  0.1667  272 SER D CB  
9883  O OG  . SER D 208 ? 1.4852 1.8510 1.4838 0.2956  0.1926  0.1877  272 SER D OG  
9884  N N   . GLY D 209 ? 1.0954 1.3926 1.1333 0.2430  0.1780  0.2020  273 GLY D N   
9885  C CA  . GLY D 209 ? 0.9761 1.2577 0.9984 0.2491  0.1870  0.2192  273 GLY D CA  
9886  C C   . GLY D 209 ? 0.9699 1.2351 0.9456 0.2661  0.1742  0.2055  273 GLY D C   
9887  O O   . GLY D 209 ? 1.2271 1.4814 1.1817 0.2776  0.1826  0.2199  273 GLY D O   
9888  N N   . LYS D 210 ? 0.8713 1.1344 0.8315 0.2682  0.1536  0.1780  274 LYS D N   
9889  C CA  . LYS D 210 ? 0.9132 1.1632 0.8329 0.2844  0.1400  0.1630  274 LYS D CA  
9890  C C   . LYS D 210 ? 0.9006 1.1384 0.8262 0.2698  0.1161  0.1367  274 LYS D C   
9891  O O   . LYS D 210 ? 1.1106 1.3544 1.0567 0.2566  0.1082  0.1242  274 LYS D O   
9892  C CB  . LYS D 210 ? 1.0619 1.3254 0.9434 0.3132  0.1420  0.1575  274 LYS D CB  
9893  C CG  . LYS D 210 ? 1.2635 1.5341 1.1236 0.3353  0.1652  0.1837  274 LYS D CG  
9894  C CD  . LYS D 210 ? 1.2693 1.5538 1.0897 0.3665  0.1679  0.1787  274 LYS D CD  
9895  C CE  . LYS D 210 ? 1.3489 1.6577 1.1869 0.3664  0.1771  0.1805  274 LYS D CE  
9896  N NZ  . LYS D 210 ? 1.4711 1.7960 1.2765 0.3977  0.1942  0.1932  274 LYS D NZ  
9897  N N   . VAL D 211 ? 0.8519 1.0724 0.7594 0.2728  0.1050  0.1288  275 VAL D N   
9898  C CA  . VAL D 211 ? 0.7809 0.9910 0.6905 0.2620  0.0832  0.1038  275 VAL D CA  
9899  C C   . VAL D 211 ? 0.8087 1.0228 0.6853 0.2816  0.0709  0.0845  275 VAL D C   
9900  O O   . VAL D 211 ? 0.8892 1.1038 0.7345 0.3042  0.0742  0.0885  275 VAL D O   
9901  C CB  . VAL D 211 ? 0.7873 0.9778 0.7002 0.2530  0.0769  0.1043  275 VAL D CB  
9902  C CG1 . VAL D 211 ? 0.8456 1.0280 0.7570 0.2455  0.0556  0.0785  275 VAL D CG1 
9903  C CG2 . VAL D 211 ? 0.7536 0.9379 0.7025 0.2316  0.0854  0.1201  275 VAL D CG2 
9904  N N   . LYS D 212 ? 0.7873 1.0032 0.6714 0.2729  0.0562  0.0634  276 LYS D N   
9905  C CA  . LYS D 212 ? 0.7709 0.9915 0.6302 0.2888  0.0436  0.0441  276 LYS D CA  
9906  C C   . LYS D 212 ? 0.7872 0.9965 0.6507 0.2777  0.0237  0.0219  276 LYS D C   
9907  O O   . LYS D 212 ? 0.8671 1.0730 0.7546 0.2573  0.0176  0.0140  276 LYS D O   
9908  C CB  . LYS D 212 ? 0.8369 1.0721 0.7017 0.2906  0.0465  0.0410  276 LYS D CB  
9909  C CG  . LYS D 212 ? 0.9882 1.2378 0.8540 0.3003  0.0682  0.0640  276 LYS D CG  
9910  C CD  . LYS D 212 ? 1.1525 1.4181 1.0232 0.3039  0.0708  0.0601  276 LYS D CD  
9911  C CE  . LYS D 212 ? 1.2819 1.5646 1.1543 0.3150  0.0943  0.0844  276 LYS D CE  
9912  N NZ  . LYS D 212 ? 1.2107 1.5114 1.0841 0.3232  0.0971  0.0801  276 LYS D NZ  
9913  N N   . CYS D 213 ? 0.8018 1.0061 0.6417 0.2924  0.0137  0.0119  277 CYS D N   
9914  C CA  . CYS D 213 ? 0.9567 1.1516 0.8017 0.2831  -0.0037 -0.0071 277 CYS D CA  
9915  C C   . CYS D 213 ? 0.9063 1.1042 0.7347 0.2957  -0.0201 -0.0291 277 CYS D C   
9916  O O   . CYS D 213 ? 0.8586 1.0612 0.6598 0.3195  -0.0215 -0.0308 277 CYS D O   
9917  C CB  . CYS D 213 ? 1.0499 1.2347 0.8887 0.2859  -0.0038 -0.0015 277 CYS D CB  
9918  S SG  . CYS D 213 ? 1.4962 1.6730 1.3587 0.2679  0.0111  0.0208  277 CYS D SG  
9919  N N   . THR D 214 ? 0.7870 0.9812 0.6320 0.2800  -0.0327 -0.0459 278 THR D N   
9920  C CA  . THR D 214 ? 0.7897 0.9839 0.6258 0.2873  -0.0503 -0.0678 278 THR D CA  
9921  C C   . THR D 214 ? 0.8199 1.0078 0.6594 0.2845  -0.0626 -0.0795 278 THR D C   
9922  O O   . THR D 214 ? 0.7946 0.9771 0.6557 0.2649  -0.0658 -0.0838 278 THR D O   
9923  C CB  . THR D 214 ? 0.8076 1.0013 0.6611 0.2716  -0.0561 -0.0786 278 THR D CB  
9924  O OG1 . THR D 214 ? 0.9150 1.1154 0.7701 0.2719  -0.0440 -0.0669 278 THR D OG1 
9925  C CG2 . THR D 214 ? 0.7518 0.9451 0.5961 0.2805  -0.0737 -0.1000 278 THR D CG2 
9926  N N   . GLY D 215 ? 0.9215 1.1107 0.7393 0.3052  -0.0700 -0.0853 279 GLY D N   
9927  C CA  . GLY D 215 ? 0.9965 1.1823 0.8198 0.3036  -0.0833 -0.0986 279 GLY D CA  
9928  C C   . GLY D 215 ? 1.1206 1.3077 0.9527 0.3007  -0.1018 -0.1220 279 GLY D C   
9929  O O   . GLY D 215 ? 1.1086 1.2968 0.9438 0.2974  -0.1053 -0.1290 279 GLY D O   
9930  N N   . THR D 216 ? 0.9861 1.1730 0.8232 0.3024  -0.1139 -0.1342 280 THR D N   
9931  C CA  . THR D 216 ? 1.0139 1.2026 0.8638 0.2991  -0.1320 -0.1562 280 THR D CA  
9932  C C   . THR D 216 ? 1.0450 1.2371 0.8811 0.3202  -0.1465 -0.1684 280 THR D C   
9933  O O   . THR D 216 ? 0.8152 1.0073 0.6502 0.3233  -0.1448 -0.1640 280 THR D O   
9934  C CB  . THR D 216 ? 0.9470 1.1335 0.8290 0.2723  -0.1317 -0.1596 280 THR D CB  
9935  O OG1 . THR D 216 ? 1.1230 1.3060 1.0157 0.2564  -0.1253 -0.1560 280 THR D OG1 
9936  C CG2 . THR D 216 ? 0.7565 0.9469 0.6558 0.2697  -0.1492 -0.1800 280 THR D CG2 
9937  N N   . ASN D 217 ? 1.1549 1.3490 0.9789 0.3363  -0.1614 -0.1838 281 ASN D N   
9938  C CA  . ASN D 217 ? 0.9891 1.1861 0.7990 0.3586  -0.1780 -0.1978 281 ASN D CA  
9939  C C   . ASN D 217 ? 0.9341 1.1345 0.7733 0.3477  -0.1965 -0.2194 281 ASN D C   
9940  O O   . ASN D 217 ? 0.8635 1.0632 0.7147 0.3425  -0.2084 -0.2338 281 ASN D O   
9941  C CB  . ASN D 217 ? 1.1596 1.3563 0.9372 0.3859  -0.1850 -0.2032 281 ASN D CB  
9942  C CG  . ASN D 217 ? 1.1501 1.3484 0.9062 0.4134  -0.2008 -0.2151 281 ASN D CG  
9943  O OD1 . ASN D 217 ? 1.0923 1.2936 0.8668 0.4100  -0.2157 -0.2301 281 ASN D OD1 
9944  N ND2 . ASN D 217 ? 1.1140 1.3111 0.8307 0.4420  -0.1976 -0.2087 281 ASN D ND2 
9945  N N   . LEU D 218 ? 0.9044 1.1084 0.7563 0.3440  -0.1987 -0.2209 282 LEU D N   
9946  C CA  . LEU D 218 ? 0.9066 1.1166 0.7918 0.3314  -0.2134 -0.2389 282 LEU D CA  
9947  C C   . LEU D 218 ? 0.9861 1.2012 0.8652 0.3532  -0.2364 -0.2596 282 LEU D C   
9948  O O   . LEU D 218 ? 1.0053 1.2274 0.9138 0.3453  -0.2508 -0.2762 282 LEU D O   
9949  C CB  . LEU D 218 ? 0.8737 1.0871 0.7785 0.3168  -0.2047 -0.2317 282 LEU D CB  
9950  C CG  . LEU D 218 ? 0.9487 1.1582 0.8723 0.2901  -0.1875 -0.2181 282 LEU D CG  
9951  C CD1 . LEU D 218 ? 1.1614 1.3644 1.0630 0.2945  -0.1699 -0.1966 282 LEU D CD1 
9952  C CD2 . LEU D 218 ? 0.8976 1.1139 0.8535 0.2736  -0.1894 -0.2243 282 LEU D CD2 
9953  N N   . TRP D 219 ? 1.1155 1.3274 0.9569 0.3813  -0.2401 -0.2587 283 TRP D N   
9954  C CA  . TRP D 219 ? 1.0550 1.2703 0.8836 0.4070  -0.2623 -0.2774 283 TRP D CA  
9955  C C   . TRP D 219 ? 1.0380 1.2503 0.8545 0.4219  -0.2793 -0.2938 283 TRP D C   
9956  O O   . TRP D 219 ? 0.9924 1.2077 0.8356 0.4155  -0.2990 -0.3149 283 TRP D O   
9957  C CB  . TRP D 219 ? 1.0640 1.2769 0.8557 0.4317  -0.2552 -0.2648 283 TRP D CB  
9958  C CG  . TRP D 219 ? 1.0827 1.2971 0.8514 0.4637  -0.2770 -0.2821 283 TRP D CG  
9959  C CD1 . TRP D 219 ? 0.9852 1.2057 0.7731 0.4692  -0.3043 -0.3095 283 TRP D CD1 
9960  C CD2 . TRP D 219 ? 1.1352 1.3442 0.8565 0.4965  -0.2744 -0.2735 283 TRP D CD2 
9961  N NE1 . TRP D 219 ? 1.0875 1.3067 0.8428 0.5033  -0.3198 -0.3196 283 TRP D NE1 
9962  C CE2 . TRP D 219 ? 1.2252 1.4370 0.9377 0.5218  -0.3025 -0.2985 283 TRP D CE2 
9963  C CE3 . TRP D 219 ? 1.1484 1.3502 0.8356 0.5072  -0.2522 -0.2479 283 TRP D CE3 
9964  C CZ2 . TRP D 219 ? 1.4182 1.6251 1.0851 0.5580  -0.3078 -0.2976 283 TRP D CZ2 
9965  C CZ3 . TRP D 219 ? 1.2302 1.4273 0.8727 0.5428  -0.2559 -0.2456 283 TRP D CZ3 
9966  C CH2 . TRP D 219 ? 1.3589 1.5579 0.9895 0.5684  -0.2831 -0.2700 283 TRP D CH2 
9967  N N   . ASN D 220 ? 1.0239 1.2302 0.8014 0.4419  -0.2718 -0.2840 284 ASN D N   
9968  C CA  . ASN D 220 ? 1.0926 1.2954 0.8486 0.4644  -0.2891 -0.2999 284 ASN D CA  
9969  C C   . ASN D 220 ? 1.2218 1.4192 0.9694 0.4587  -0.2784 -0.2919 284 ASN D C   
9970  O O   . ASN D 220 ? 1.6441 1.8378 1.3621 0.4827  -0.2866 -0.2988 284 ASN D O   
9971  C CB  . ASN D 220 ? 1.0728 1.2740 0.7824 0.5022  -0.2931 -0.2986 284 ASN D CB  
9972  C CG  . ASN D 220 ? 1.1801 1.3792 0.8616 0.5075  -0.2649 -0.2689 284 ASN D CG  
9973  O OD1 . ASN D 220 ? 1.5025 1.7010 1.1954 0.4859  -0.2436 -0.2505 284 ASN D OD1 
9974  N ND2 . ASN D 220 ? 1.0673 1.2646 0.7128 0.5365  -0.2651 -0.2641 284 ASN D ND2 
9975  N N   . ASP D 221 ? 1.1200 1.3170 0.8926 0.4287  -0.2612 -0.2786 285 ASP D N   
9976  C CA  . ASP D 221 ? 1.1442 1.3371 0.9077 0.4233  -0.2475 -0.2672 285 ASP D CA  
9977  C C   . ASP D 221 ? 1.0952 1.2855 0.8951 0.3894  -0.2416 -0.2656 285 ASP D C   
9978  O O   . ASP D 221 ? 0.9934 1.1856 0.8196 0.3655  -0.2314 -0.2572 285 ASP D O   
9979  C CB  . ASP D 221 ? 1.1718 1.3662 0.9072 0.4329  -0.2227 -0.2410 285 ASP D CB  
9980  C CG  . ASP D 221 ? 1.5048 1.6979 1.2232 0.4374  -0.2107 -0.2310 285 ASP D CG  
9981  O OD1 . ASP D 221 ? 1.6737 1.8634 1.3978 0.4354  -0.2223 -0.2448 285 ASP D OD1 
9982  O OD2 . ASP D 221 ? 1.8279 2.0235 1.5280 0.4434  -0.1894 -0.2088 285 ASP D OD2 
9983  N N   . ALA D 222 ? 1.0579 1.2427 0.8561 0.3896  -0.2485 -0.2739 286 ALA D N   
9984  C CA  . ALA D 222 ? 1.1544 1.3339 0.9795 0.3622  -0.2438 -0.2727 286 ALA D CA  
9985  C C   . ALA D 222 ? 1.1745 1.3529 0.9843 0.3603  -0.2233 -0.2537 286 ALA D C   
9986  O O   . ALA D 222 ? 1.2201 1.3937 1.0474 0.3400  -0.2177 -0.2507 286 ALA D O   
9987  C CB  . ALA D 222 ? 1.4677 1.6398 1.3042 0.3627  -0.2672 -0.2959 286 ALA D CB  
9988  N N   . LYS D 223 ? 1.1252 1.3085 0.9029 0.3823  -0.2123 -0.2412 287 LYS D N   
9989  C CA  . LYS D 223 ? 1.1976 1.3836 0.9659 0.3790  -0.1896 -0.2198 287 LYS D CA  
9990  C C   . LYS D 223 ? 1.2219 1.4119 0.9980 0.3675  -0.1711 -0.2000 287 LYS D C   
9991  O O   . LYS D 223 ? 1.3965 1.5868 1.1832 0.3632  -0.1763 -0.2038 287 LYS D O   
9992  C CB  . LYS D 223 ? 1.1046 1.2944 0.8345 0.4100  -0.1864 -0.2159 287 LYS D CB  
9993  C CG  . LYS D 223 ? 1.0730 1.2581 0.7893 0.4266  -0.2055 -0.2357 287 LYS D CG  
9994  C CD  . LYS D 223 ? 1.2042 1.3953 0.8814 0.4566  -0.1957 -0.2263 287 LYS D CD  
9995  C CE  . LYS D 223 ? 1.1674 1.3541 0.8200 0.4833  -0.2161 -0.2467 287 LYS D CE  
9996  N NZ  . LYS D 223 ? 1.3560 1.5502 0.9741 0.5087  -0.2018 -0.2342 287 LYS D NZ  
9997  N N   . ARG D 224 ? 1.2697 1.4627 1.0422 0.3625  -0.1501 -0.1794 288 ARG D N   
9998  C CA  . ARG D 224 ? 1.0812 1.2759 0.8617 0.3516  -0.1333 -0.1606 288 ARG D CA  
9999  C C   . ARG D 224 ? 1.0721 1.2721 0.8239 0.3734  -0.1185 -0.1427 288 ARG D C   
10000 O O   . ARG D 224 ? 1.0944 1.2990 0.8338 0.3818  -0.1079 -0.1332 288 ARG D O   
10001 C CB  . ARG D 224 ? 0.9761 1.1688 0.7828 0.3237  -0.1209 -0.1502 288 ARG D CB  
10002 C CG  . ARG D 224 ? 1.1061 1.2928 0.9360 0.3048  -0.1328 -0.1656 288 ARG D CG  
10003 C CD  . ARG D 224 ? 1.0023 1.1854 0.8581 0.2773  -0.1221 -0.1560 288 ARG D CD  
10004 N NE  . ARG D 224 ? 0.9107 1.0912 0.7847 0.2646  -0.1277 -0.1620 288 ARG D NE  
10005 C CZ  . ARG D 224 ? 0.9272 1.1026 0.8239 0.2461  -0.1348 -0.1721 288 ARG D CZ  
10006 N NH1 . ARG D 224 ? 1.1337 1.3036 1.0366 0.2374  -0.1376 -0.1771 288 ARG D NH1 
10007 N NH2 . ARG D 224 ? 0.7361 0.9117 0.6490 0.2365  -0.1383 -0.1763 288 ARG D NH2 
10008 N N   . PRO D 225 ? 1.0073 1.2067 0.7489 0.3828  -0.1168 -0.1371 289 PRO D N   
10009 C CA  . PRO D 225 ? 0.8583 1.0608 0.5739 0.4015  -0.1001 -0.1167 289 PRO D CA  
10010 C C   . PRO D 225 ? 0.8294 1.0340 0.5609 0.3836  -0.0781 -0.0945 289 PRO D C   
10011 O O   . PRO D 225 ? 1.0624 1.2641 0.8238 0.3569  -0.0768 -0.0947 289 PRO D O   
10012 C CB  . PRO D 225 ? 0.8914 1.0897 0.6029 0.4060  -0.1031 -0.1152 289 PRO D CB  
10013 C CG  . PRO D 225 ? 1.0085 1.2047 0.7368 0.3986  -0.1258 -0.1399 289 PRO D CG  
10014 C CD  . PRO D 225 ? 0.9107 1.1066 0.6674 0.3741  -0.1279 -0.1469 289 PRO D CD  
10015 N N   . PHE D 226 ? 0.8276 1.0375 0.5398 0.3986  -0.0610 -0.0756 290 PHE D N   
10016 C CA  . PHE D 226 ? 0.8733 1.0869 0.6029 0.3827  -0.0403 -0.0545 290 PHE D CA  
10017 C C   . PHE D 226 ? 0.9754 1.1895 0.6901 0.3944  -0.0219 -0.0305 290 PHE D C   
10018 O O   . PHE D 226 ? 1.2392 1.4543 0.9210 0.4217  -0.0214 -0.0282 290 PHE D O   
10019 C CB  . PHE D 226 ? 0.8000 1.0228 0.5282 0.3865  -0.0357 -0.0546 290 PHE D CB  
10020 C CG  . PHE D 226 ? 0.8848 1.1122 0.6403 0.3650  -0.0193 -0.0385 290 PHE D CG  
10021 C CD1 . PHE D 226 ? 0.8511 1.0744 0.6365 0.3389  -0.0261 -0.0477 290 PHE D CD1 
10022 C CD2 . PHE D 226 ? 0.8902 1.1260 0.6423 0.3714  0.0030  -0.0140 290 PHE D CD2 
10023 C CE1 . PHE D 226 ? 0.8626 1.0898 0.6730 0.3204  -0.0129 -0.0345 290 PHE D CE1 
10024 C CE2 . PHE D 226 ? 0.8832 1.1244 0.6643 0.3515  0.0167  -0.0001 290 PHE D CE2 
10025 C CZ  . PHE D 226 ? 0.9789 1.2156 0.7887 0.3264  0.0078  -0.0112 290 PHE D CZ  
10026 N N   . LEU D 227 ? 0.9684 1.1803 0.7066 0.3742  -0.0073 -0.0127 291 LEU D N   
10027 C CA  . LEU D 227 ? 0.9513 1.1603 0.6798 0.3816  0.0098  0.0110  291 LEU D CA  
10028 C C   . LEU D 227 ? 0.9979 1.2132 0.7467 0.3688  0.0313  0.0339  291 LEU D C   
10029 O O   . LEU D 227 ? 1.4310 1.6467 1.2120 0.3440  0.0313  0.0324  291 LEU D O   
10030 C CB  . LEU D 227 ? 0.9969 1.1930 0.7358 0.3697  0.0038  0.0100  291 LEU D CB  
10031 C CG  . LEU D 227 ? 0.8880 1.0768 0.6208 0.3735  0.0203  0.0347  291 LEU D CG  
10032 C CD1 . LEU D 227 ? 0.9124 1.1019 0.6032 0.4070  0.0241  0.0409  291 LEU D CD1 
10033 C CD2 . LEU D 227 ? 0.8453 1.0210 0.5936 0.3581  0.0123  0.0307  291 LEU D CD2 
10034 N N   . GLU D 228 ? 1.0080 1.2280 0.7383 0.3863  0.0495  0.0554  292 GLU D N   
10035 C CA  . GLU D 228 ? 1.1609 1.3882 0.9118 0.3760  0.0721  0.0803  292 GLU D CA  
10036 C C   . GLU D 228 ? 1.1445 1.3615 0.8883 0.3802  0.0856  0.1027  292 GLU D C   
10037 O O   . GLU D 228 ? 1.0904 1.3026 0.7989 0.4047  0.0852  0.1047  292 GLU D O   
10038 C CB  . GLU D 228 ? 1.3231 1.5678 1.0578 0.3958  0.0844  0.0875  292 GLU D CB  
10039 C CG  . GLU D 228 ? 1.7063 1.9649 1.4741 0.3788  0.0975  0.0979  292 GLU D CG  
10040 C CD  . GLU D 228 ? 1.9718 2.2493 1.7217 0.4015  0.1129  0.1084  292 GLU D CD  
10041 O OE1 . GLU D 228 ? 2.0522 2.3412 1.8087 0.4010  0.1078  0.0965  292 GLU D OE1 
10042 O OE2 . GLU D 228 ? 1.9337 2.2144 1.6618 0.4211  0.1303  0.1289  292 GLU D OE2 
10043 N N   . PHE D 229 ? 1.1112 1.3230 0.8876 0.3569  0.0959  0.1184  293 PHE D N   
10044 C CA  . PHE D 229 ? 1.0491 1.2510 0.8226 0.3595  0.1118  0.1436  293 PHE D CA  
10045 C C   . PHE D 229 ? 1.0677 1.2719 0.8817 0.3359  0.1274  0.1633  293 PHE D C   
10046 O O   . PHE D 229 ? 1.0672 1.2761 0.9133 0.3140  0.1208  0.1534  293 PHE D O   
10047 C CB  . PHE D 229 ? 1.0986 1.2805 0.8642 0.3574  0.0982  0.1356  293 PHE D CB  
10048 C CG  . PHE D 229 ? 0.9991 1.1725 0.7988 0.3287  0.0849  0.1226  293 PHE D CG  
10049 C CD1 . PHE D 229 ? 0.9950 1.1594 0.8261 0.3070  0.0937  0.1383  293 PHE D CD1 
10050 C CD2 . PHE D 229 ? 1.0094 1.1824 0.8089 0.3245  0.0633  0.0947  293 PHE D CD2 
10051 C CE1 . PHE D 229 ? 0.9278 1.0832 0.7872 0.2828  0.0806  0.1253  293 PHE D CE1 
10052 C CE2 . PHE D 229 ? 0.9136 1.0786 0.7420 0.2997  0.0523  0.0835  293 PHE D CE2 
10053 C CZ  . PHE D 229 ? 0.8279 0.9841 0.6845 0.2798  0.0608  0.0985  293 PHE D CZ  
10054 N N   . ASP D 230 ? 1.0945 1.2944 0.9078 0.3401  0.1473  0.1911  294 ASP D N   
10055 C CA  . ASP D 230 ? 1.3471 1.5488 1.2029 0.3172  0.1623  0.2113  294 ASP D CA  
10056 C C   . ASP D 230 ? 1.3867 1.5654 1.2536 0.3054  0.1636  0.2241  294 ASP D C   
10057 O O   . ASP D 230 ? 1.1852 1.3475 1.0294 0.3126  0.1504  0.2137  294 ASP D O   
10058 C CB  . ASP D 230 ? 1.4041 1.6238 1.2589 0.3294  0.1881  0.2363  294 ASP D CB  
10059 C CG  . ASP D 230 ? 1.5910 1.8042 1.4065 0.3559  0.2023  0.2555  294 ASP D CG  
10060 O OD1 . ASP D 230 ? 1.6135 1.8061 1.4076 0.3619  0.1925  0.2515  294 ASP D OD1 
10061 O OD2 . ASP D 230 ? 1.8178 2.0466 1.6229 0.3720  0.2236  0.2746  294 ASP D OD2 
10062 N N   . GLN D 231 ? 1.4812 1.6589 1.3841 0.2877  0.1788  0.2463  295 GLN D N   
10063 C CA  . GLN D 231 ? 1.3689 1.5227 1.2864 0.2745  0.1788  0.2581  295 GLN D CA  
10064 C C   . GLN D 231 ? 1.3800 1.5184 1.2595 0.2966  0.1875  0.2742  295 GLN D C   
10065 O O   . GLN D 231 ? 1.3568 1.4726 1.2311 0.2932  0.1780  0.2720  295 GLN D O   
10066 C CB  . GLN D 231 ? 1.4432 1.5978 1.4119 0.2491  0.1904  0.2764  295 GLN D CB  
10067 C CG  . GLN D 231 ? 1.6541 1.8263 1.6363 0.2535  0.2180  0.3053  295 GLN D CG  
10068 C CD  . GLN D 231 ? 1.8588 2.0316 1.8985 0.2254  0.2252  0.3195  295 GLN D CD  
10069 O OE1 . GLN D 231 ? 1.9052 2.0714 1.9745 0.2037  0.2079  0.3028  295 GLN D OE1 
10070 N NE2 . GLN D 231 ? 2.0977 2.2788 2.1539 0.2264  0.2508  0.3503  295 GLN D NE2 
10071 N N   . SER D 232 ? 1.3718 1.5219 1.2218 0.3211  0.2047  0.2891  296 SER D N   
10072 C CA  . SER D 232 ? 1.3264 1.4615 1.1358 0.3451  0.2136  0.3052  296 SER D CA  
10073 C C   . SER D 232 ? 1.4086 1.5374 1.1710 0.3686  0.1939  0.2814  296 SER D C   
10074 O O   . SER D 232 ? 1.4528 1.5710 1.1752 0.3935  0.1993  0.2915  296 SER D O   
10075 C CB  . SER D 232 ? 1.3375 1.4871 1.1332 0.3634  0.2419  0.3332  296 SER D CB  
10076 O OG  . SER D 232 ? 1.5227 1.6951 1.2958 0.3818  0.2399  0.3192  296 SER D OG  
10077 N N   . PHE D 233 ? 1.3374 1.4724 1.1056 0.3610  0.1712  0.2502  297 PHE D N   
10078 C CA  . PHE D 233 ? 1.2620 1.3947 0.9932 0.3807  0.1506  0.2246  297 PHE D CA  
10079 C C   . PHE D 233 ? 1.3048 1.4504 0.9924 0.4137  0.1542  0.2223  297 PHE D C   
10080 O O   . PHE D 233 ? 1.2286 1.3686 0.8818 0.4340  0.1386  0.2054  297 PHE D O   
10081 C CB  . PHE D 233 ? 1.3645 1.4731 1.0787 0.3860  0.1409  0.2235  297 PHE D CB  
10082 C CG  . PHE D 233 ? 1.5130 1.6092 1.2608 0.3588  0.1266  0.2118  297 PHE D CG  
10083 C CD1 . PHE D 233 ? 1.4067 1.5134 1.1830 0.3385  0.1128  0.1898  297 PHE D CD1 
10084 C CD2 . PHE D 233 ? 1.6270 1.6998 1.3754 0.3550  0.1264  0.2224  297 PHE D CD2 
10085 C CE1 . PHE D 233 ? 1.4836 1.5786 1.2881 0.3154  0.1000  0.1790  297 PHE D CE1 
10086 C CE2 . PHE D 233 ? 1.8105 1.8715 1.5879 0.3317  0.1127  0.2109  297 PHE D CE2 
10087 C CZ  . PHE D 233 ? 1.7326 1.8054 1.5376 0.3123  0.0997  0.1891  297 PHE D CZ  
10088 N N   . THR D 234 ? 1.3223 1.4854 1.0107 0.4206  0.1740  0.2385  298 THR D N   
10089 C CA  . THR D 234 ? 1.2282 1.4058 0.8776 0.4510  0.1740  0.2308  298 THR D CA  
10090 C C   . THR D 234 ? 1.2989 1.4889 0.9607 0.4421  0.1528  0.1992  298 THR D C   
10091 O O   . THR D 234 ? 1.6081 1.8068 1.3103 0.4161  0.1525  0.1954  298 THR D O   
10092 C CB  . THR D 234 ? 1.2710 1.4639 0.9125 0.4653  0.2032  0.2590  298 THR D CB  
10093 O OG1 . THR D 234 ? 1.2156 1.4226 0.9061 0.4383  0.2152  0.2688  298 THR D OG1 
10094 C CG2 . THR D 234 ? 1.3948 1.5727 1.0149 0.4794  0.2236  0.2901  298 THR D CG2 
10095 N N   . TYR D 235 ? 1.2028 1.3919 0.8308 0.4633  0.1336  0.1758  299 TYR D N   
10096 C CA  . TYR D 235 ? 1.1348 1.3301 0.7744 0.4537  0.1101  0.1441  299 TYR D CA  
10097 C C   . TYR D 235 ? 1.1336 1.3373 0.7342 0.4842  0.0993  0.1268  299 TYR D C   
10098 O O   . TYR D 235 ? 1.2802 1.4790 0.8399 0.5137  0.1014  0.1319  299 TYR D O   
10099 C CB  . TYR D 235 ? 1.0874 1.2670 0.7378 0.4395  0.0892  0.1262  299 TYR D CB  
10100 C CG  . TYR D 235 ? 1.1093 1.2792 0.7199 0.4661  0.0751  0.1146  299 TYR D CG  
10101 C CD1 . TYR D 235 ? 1.0803 1.2357 0.6690 0.4795  0.0839  0.1326  299 TYR D CD1 
10102 C CD2 . TYR D 235 ? 1.1640 1.3384 0.7594 0.4782  0.0519  0.0852  299 TYR D CD2 
10103 C CE1 . TYR D 235 ? 1.2289 1.3755 0.7803 0.5055  0.0697  0.1210  299 TYR D CE1 
10104 C CE2 . TYR D 235 ? 1.2206 1.3872 0.7819 0.5031  0.0371  0.0730  299 TYR D CE2 
10105 C CZ  . TYR D 235 ? 1.3117 1.4646 0.8501 0.5173  0.0459  0.0907  299 TYR D CZ  
10106 O OH  . TYR D 235 ? 1.4022 1.5470 0.9057 0.5437  0.0302  0.0780  299 TYR D OH  
10107 N N   . THR D 236 ? 1.1963 1.4111 0.8085 0.4780  0.0864  0.1056  300 THR D N   
10108 C CA  . THR D 236 ? 1.2627 1.4823 0.8414 0.5043  0.0696  0.0832  300 THR D CA  
10109 C C   . THR D 236 ? 1.2341 1.4529 0.8339 0.4872  0.0436  0.0519  300 THR D C   
10110 O O   . THR D 236 ? 1.3069 1.5288 0.9446 0.4585  0.0438  0.0497  300 THR D O   
10111 C CB  . THR D 236 ? 1.3084 1.5451 0.8703 0.5236  0.0831  0.0906  300 THR D CB  
10112 O OG1 . THR D 236 ? 1.3357 1.5837 0.9330 0.5005  0.0825  0.0839  300 THR D OG1 
10113 C CG2 . THR D 236 ? 1.3569 1.5982 0.9059 0.5365  0.1139  0.1255  300 THR D CG2 
10114 N N   . PHE D 237 ? 1.1372 1.3511 0.7129 0.5051  0.0211  0.0283  301 PHE D N   
10115 C CA  . PHE D 237 ? 1.0160 1.2302 0.6090 0.4927  -0.0031 -0.0011 301 PHE D CA  
10116 C C   . PHE D 237 ? 1.0091 1.2339 0.5870 0.5088  -0.0074 -0.0120 301 PHE D C   
10117 O O   . PHE D 237 ? 0.9427 1.1710 0.4827 0.5405  -0.0039 -0.0087 301 PHE D O   
10118 C CB  . PHE D 237 ? 1.0366 1.2414 0.6170 0.5025  -0.0265 -0.0223 301 PHE D CB  
10119 C CG  . PHE D 237 ? 1.1127 1.3077 0.7157 0.4818  -0.0284 -0.0195 301 PHE D CG  
10120 C CD1 . PHE D 237 ? 1.1378 1.3239 0.7227 0.4933  -0.0194 -0.0031 301 PHE D CD1 
10121 C CD2 . PHE D 237 ? 1.1346 1.3282 0.7750 0.4523  -0.0394 -0.0334 301 PHE D CD2 
10122 C CE1 . PHE D 237 ? 1.1328 1.3091 0.7377 0.4755  -0.0223 -0.0016 301 PHE D CE1 
10123 C CE2 . PHE D 237 ? 1.1717 1.3567 0.8315 0.4350  -0.0414 -0.0316 301 PHE D CE2 
10124 C CZ  . PHE D 237 ? 1.1843 1.3608 0.8266 0.4467  -0.0333 -0.0163 301 PHE D CZ  
10125 N N   . LYS D 238 ? 1.1325 1.3614 0.7390 0.4875  -0.0146 -0.0243 302 LYS D N   
10126 C CA  . LYS D 238 ? 1.1376 1.3744 0.7340 0.4995  -0.0222 -0.0381 302 LYS D CA  
10127 C C   . LYS D 238 ? 1.1757 1.4055 0.7873 0.4876  -0.0495 -0.0679 302 LYS D C   
10128 O O   . LYS D 238 ? 1.2094 1.4331 0.8517 0.4606  -0.0553 -0.0727 302 LYS D O   
10129 C CB  . LYS D 238 ? 1.0709 1.3192 0.6898 0.4844  -0.0044 -0.0241 302 LYS D CB  
10130 C CG  . LYS D 238 ? 1.2547 1.5111 0.8728 0.4870  0.0250  0.0079  302 LYS D CG  
10131 C CD  . LYS D 238 ? 1.3941 1.6640 1.0395 0.4713  0.0401  0.0189  302 LYS D CD  
10132 C CE  . LYS D 238 ? 1.4381 1.7228 1.0676 0.4909  0.0664  0.0445  302 LYS D CE  
10133 N NZ  . LYS D 238 ? 1.4448 1.7461 1.0854 0.4907  0.0732  0.0446  302 LYS D NZ  
10134 N N   . GLU D 239 ? 1.3051 1.5355 0.8954 0.5082  -0.0661 -0.0876 303 GLU D N   
10135 C CA  . GLU D 239 ? 1.3587 1.5825 0.9658 0.4966  -0.0915 -0.1150 303 GLU D CA  
10136 C C   . GLU D 239 ? 1.3984 1.6269 1.0115 0.4934  -0.0922 -0.1210 303 GLU D C   
10137 O O   . GLU D 239 ? 1.5853 1.8210 1.1709 0.5184  -0.0862 -0.1174 303 GLU D O   
10138 C CB  . GLU D 239 ? 1.5595 1.7774 1.1386 0.5235  -0.1146 -0.1362 303 GLU D CB  
10139 C CG  . GLU D 239 ? 1.7494 1.9607 1.3436 0.5162  -0.1426 -0.1661 303 GLU D CG  
10140 C CD  . GLU D 239 ? 1.9014 2.1066 1.5292 0.4903  -0.1543 -0.1761 303 GLU D CD  
10141 O OE1 . GLU D 239 ? 2.3116 2.5166 1.9463 0.4818  -0.1440 -0.1629 303 GLU D OE1 
10142 O OE2 . GLU D 239 ? 2.0822 2.2825 1.7295 0.4789  -0.1740 -0.1974 303 GLU D OE2 
10143 N N   . PRO D 240 ? 1.0612 1.2855 0.7086 0.4643  -0.0993 -0.1303 304 PRO D N   
10144 C CA  . PRO D 240 ? 1.1203 1.3473 0.7752 0.4594  -0.1004 -0.1358 304 PRO D CA  
10145 C C   . PRO D 240 ? 1.3991 1.6218 1.0308 0.4826  -0.1222 -0.1592 304 PRO D C   
10146 O O   . PRO D 240 ? 1.2879 1.5012 0.9192 0.4852  -0.1441 -0.1791 304 PRO D O   
10147 C CB  . PRO D 240 ? 1.0322 1.2516 0.7265 0.4239  -0.1059 -0.1417 304 PRO D CB  
10148 C CG  . PRO D 240 ? 0.9140 1.1257 0.6166 0.4168  -0.1179 -0.1507 304 PRO D CG  
10149 C CD  . PRO D 240 ? 1.0112 1.2269 0.6887 0.4379  -0.1095 -0.1388 304 PRO D CD  
10150 N N   . CYS D 241 ? 1.5689 1.7988 1.1831 0.4997  -0.1166 -0.1572 305 CYS D N   
10151 C CA  . CYS D 241 ? 1.4456 1.6713 1.0329 0.5261  -0.1364 -0.1784 305 CYS D CA  
10152 C C   . CYS D 241 ? 1.4941 1.7128 1.1011 0.5105  -0.1489 -0.1935 305 CYS D C   
10153 O O   . CYS D 241 ? 2.0150 2.2383 1.6076 0.5251  -0.1473 -0.1953 305 CYS D O   
10154 C CB  . CYS D 241 ? 1.6882 1.9265 1.2386 0.5596  -0.1220 -0.1667 305 CYS D CB  
10155 S SG  . CYS D 241 ? 2.5324 2.7797 2.0575 0.5787  -0.0997 -0.1416 305 CYS D SG  
10156 N N   . LEU D 242 ? 1.3619 1.5693 1.0009 0.4817  -0.1607 -0.2035 306 LEU D N   
10157 C CA  . LEU D 242 ? 1.3317 1.5297 0.9902 0.4649  -0.1720 -0.2165 306 LEU D CA  
10158 C C   . LEU D 242 ? 1.4324 1.6146 1.1093 0.4511  -0.1967 -0.2385 306 LEU D C   
10159 O O   . LEU D 242 ? 1.4742 1.6550 1.1668 0.4379  -0.1980 -0.2375 306 LEU D O   
10160 C CB  . LEU D 242 ? 1.0987 1.3013 0.7850 0.4371  -0.1529 -0.1993 306 LEU D CB  
10161 C CG  . LEU D 242 ? 1.3372 1.5562 1.0135 0.4473  -0.1299 -0.1795 306 LEU D CG  
10162 C CD1 . LEU D 242 ? 1.3342 1.5572 1.0426 0.4177  -0.1130 -0.1630 306 LEU D CD1 
10163 C CD2 . LEU D 242 ? 1.2919 1.5129 0.9466 0.4698  -0.1365 -0.1894 306 LEU D CD2 
10164 N N   . GLY D 243 ? 1.8402 2.0109 1.5162 0.4546  -0.2160 -0.2579 307 GLY D N   
10165 C CA  . GLY D 243 ? 1.6735 1.8286 1.3690 0.4423  -0.2407 -0.2797 307 GLY D CA  
10166 C C   . GLY D 243 ? 1.5897 1.7385 1.3246 0.4049  -0.2365 -0.2754 307 GLY D C   
10167 O O   . GLY D 243 ? 1.5019 1.6390 1.2576 0.3917  -0.2541 -0.2908 307 GLY D O   
10168 N N   . PHE D 244 ? 1.4307 1.5871 1.1762 0.3885  -0.2134 -0.2544 308 PHE D N   
10169 C CA  . PHE D 244 ? 1.3605 1.5125 1.1394 0.3551  -0.2059 -0.2471 308 PHE D CA  
10170 C C   . PHE D 244 ? 1.3371 1.4953 1.1266 0.3474  -0.2002 -0.2401 308 PHE D C   
10171 O O   . PHE D 244 ? 1.2131 1.3826 0.9939 0.3525  -0.1830 -0.2231 308 PHE D O   
10172 C CB  . PHE D 244 ? 1.2301 1.3872 1.0143 0.3437  -0.1857 -0.2292 308 PHE D CB  
10173 C CG  . PHE D 244 ? 1.2504 1.3967 1.0627 0.3141  -0.1846 -0.2284 308 PHE D CG  
10174 C CD1 . PHE D 244 ? 1.1987 1.3297 1.0164 0.3084  -0.1988 -0.2423 308 PHE D CD1 
10175 C CD2 . PHE D 244 ? 1.2153 1.3653 1.0467 0.2931  -0.1691 -0.2133 308 PHE D CD2 
10176 C CE1 . PHE D 244 ? 1.0408 1.1604 0.8817 0.2821  -0.1965 -0.2401 308 PHE D CE1 
10177 C CE2 . PHE D 244 ? 1.0039 1.1432 0.8578 0.2679  -0.1677 -0.2123 308 PHE D CE2 
10178 C CZ  . PHE D 244 ? 0.8760 1.0000 0.7339 0.2626  -0.1808 -0.2252 308 PHE D CZ  
10179 N N   . LEU D 245 ? 1.0837 1.2341 0.8932 0.3353  -0.2149 -0.2536 309 LEU D N   
10180 C CA  . LEU D 245 ? 1.0056 1.1617 0.8245 0.3312  -0.2140 -0.2514 309 LEU D CA  
10181 C C   . LEU D 245 ? 0.9641 1.1208 0.8085 0.3033  -0.1984 -0.2373 309 LEU D C   
10182 O O   . LEU D 245 ? 1.1518 1.2996 1.0194 0.2819  -0.2018 -0.2418 309 LEU D O   
10183 C CB  . LEU D 245 ? 1.1204 1.2700 0.9524 0.3316  -0.2378 -0.2734 309 LEU D CB  
10184 C CG  . LEU D 245 ? 0.9952 1.1423 0.8029 0.3606  -0.2580 -0.2914 309 LEU D CG  
10185 C CD1 . LEU D 245 ? 1.0510 1.1970 0.8742 0.3619  -0.2790 -0.3098 309 LEU D CD1 
10186 C CD2 . LEU D 245 ? 0.9816 1.1390 0.7524 0.3884  -0.2472 -0.2804 309 LEU D CD2 
10187 N N   . GLY D 246 ? 0.8761 1.0420 0.7151 0.3043  -0.1815 -0.2200 310 GLY D N   
10188 C CA  . GLY D 246 ? 0.8963 1.0624 0.7567 0.2800  -0.1663 -0.2059 310 GLY D CA  
10189 C C   . GLY D 246 ? 0.8315 0.9956 0.7161 0.2637  -0.1719 -0.2119 310 GLY D C   
10190 O O   . GLY D 246 ? 1.0458 1.2050 0.9523 0.2408  -0.1663 -0.2081 310 GLY D O   
10191 N N   . ASP D 247 ? 0.7884 0.9568 0.6685 0.2768  -0.1832 -0.2216 311 ASP D N   
10192 C CA  . ASP D 247 ? 0.8922 1.0633 0.7928 0.2659  -0.1863 -0.2250 311 ASP D CA  
10193 C C   . ASP D 247 ? 0.9109 1.0762 0.8402 0.2480  -0.1982 -0.2392 311 ASP D C   
10194 O O   . ASP D 247 ? 1.0064 1.1635 0.9377 0.2449  -0.2053 -0.2467 311 ASP D O   
10195 C CB  . ASP D 247 ? 0.9494 1.1274 0.8348 0.2882  -0.1959 -0.2318 311 ASP D CB  
10196 C CG  . ASP D 247 ? 1.0489 1.2327 0.9443 0.2823  -0.1890 -0.2245 311 ASP D CG  
10197 O OD1 . ASP D 247 ? 0.8172 0.9998 0.7383 0.2593  -0.1829 -0.2211 311 ASP D OD1 
10198 O OD2 . ASP D 247 ? 1.1526 1.3411 1.0281 0.3020  -0.1898 -0.2222 311 ASP D OD2 
10199 N N   . THR D 248 ? 0.8190 0.9886 0.7708 0.2362  -0.1993 -0.2417 312 THR D N   
10200 C CA  . THR D 248 ? 0.8853 1.0519 0.8679 0.2193  -0.2095 -0.2541 312 THR D CA  
10201 C C   . THR D 248 ? 0.9473 1.1243 0.9486 0.2187  -0.2162 -0.2616 312 THR D C   
10202 O O   . THR D 248 ? 1.0956 1.2787 1.0975 0.2157  -0.2046 -0.2509 312 THR D O   
10203 C CB  . THR D 248 ? 1.0525 1.2118 1.0513 0.1949  -0.1960 -0.2439 312 THR D CB  
10204 O OG1 . THR D 248 ? 1.2686 1.4183 1.2519 0.1961  -0.1923 -0.2393 312 THR D OG1 
10205 C CG2 . THR D 248 ? 1.0787 1.2354 1.1105 0.1767  -0.2035 -0.2541 312 THR D CG2 
10206 N N   . PRO D 249 ? 0.9875 1.1665 1.0060 0.2213  -0.2358 -0.2805 313 PRO D N   
10207 C CA  . PRO D 249 ? 1.0483 1.2175 1.0697 0.2225  -0.2507 -0.2939 313 PRO D CA  
10208 C C   . PRO D 249 ? 1.0676 1.2347 1.0546 0.2502  -0.2609 -0.3001 313 PRO D C   
10209 O O   . PRO D 249 ? 1.0482 1.2223 1.0105 0.2683  -0.2560 -0.2936 313 PRO D O   
10210 C CB  . PRO D 249 ? 1.0223 1.1965 1.0785 0.2153  -0.2677 -0.3113 313 PRO D CB  
10211 C CG  . PRO D 249 ? 1.0604 1.2491 1.1154 0.2267  -0.2692 -0.3125 313 PRO D CG  
10212 C CD  . PRO D 249 ? 0.9635 1.1546 0.9998 0.2253  -0.2464 -0.2912 313 PRO D CD  
10213 N N   . ARG D 250 ? 1.0800 1.2366 1.0650 0.2538  -0.2746 -0.3121 314 ARG D N   
10214 C CA  . ARG D 250 ? 1.0248 1.1773 0.9762 0.2803  -0.2847 -0.3190 314 ARG D CA  
10215 C C   . ARG D 250 ? 1.1637 1.3046 1.1272 0.2807  -0.3077 -0.3396 314 ARG D C   
10216 O O   . ARG D 250 ? 1.1782 1.3125 1.1744 0.2577  -0.3107 -0.3436 314 ARG D O   
10217 C CB  . ARG D 250 ? 0.8445 0.9939 0.7694 0.2833  -0.2657 -0.3011 314 ARG D CB  
10218 C CG  . ARG D 250 ? 0.7552 0.8947 0.6968 0.2588  -0.2556 -0.2934 314 ARG D CG  
10219 C CD  . ARG D 250 ? 0.7584 0.8949 0.6746 0.2652  -0.2420 -0.2804 314 ARG D CD  
10220 N NE  . ARG D 250 ? 0.7660 0.8971 0.6968 0.2413  -0.2263 -0.2671 314 ARG D NE  
10221 C CZ  . ARG D 250 ? 0.8702 0.9878 0.8127 0.2277  -0.2303 -0.2715 314 ARG D CZ  
10222 N NH1 . ARG D 250 ? 1.3489 1.4566 1.2918 0.2346  -0.2497 -0.2886 314 ARG D NH1 
10223 N NH2 . ARG D 250 ? 0.7697 0.8824 0.7222 0.2084  -0.2158 -0.2590 314 ARG D NH2 
10224 N N   . GLY D 251 ? 1.2201 1.3575 1.1571 0.3073  -0.3239 -0.3524 315 GLY D N   
10225 C CA  . GLY D 251 ? 1.5273 1.6533 1.4765 0.3104  -0.3497 -0.3748 315 GLY D CA  
10226 C C   . GLY D 251 ? 1.6385 1.7484 1.5823 0.3039  -0.3487 -0.3737 315 GLY D C   
10227 O O   . GLY D 251 ? 1.8617 1.9609 1.8354 0.2811  -0.3521 -0.3770 315 GLY D O   
10228 N N   . ILE D 252 ? 1.6569 1.7656 1.5620 0.3249  -0.3428 -0.3680 316 ILE D N   
10229 C CA  . ILE D 252 ? 1.6059 1.6997 1.4976 0.3295  -0.3485 -0.3726 316 ILE D CA  
10230 C C   . ILE D 252 ? 1.6440 1.7447 1.4939 0.3524  -0.3343 -0.3604 316 ILE D C   
10231 O O   . ILE D 252 ? 2.1037 2.2173 1.9319 0.3716  -0.3291 -0.3554 316 ILE D O   
10232 C CB  . ILE D 252 ? 1.7848 1.8664 1.6770 0.3450  -0.3806 -0.3997 316 ILE D CB  
10233 C CG1 . ILE D 252 ? 1.6613 1.7224 1.5587 0.3363  -0.3886 -0.4060 316 ILE D CG1 
10234 C CG2 . ILE D 252 ? 1.6927 1.7802 1.5441 0.3837  -0.3916 -0.4090 316 ILE D CG2 
10235 C CD1 . ILE D 252 ? 1.5708 1.6214 1.5126 0.3018  -0.3887 -0.4055 316 ILE D CD1 
10236 N N   . ASP D 253 ? 1.2293 1.3216 1.0680 0.3513  -0.3280 -0.3552 317 ASP D N   
10237 C CA  . ASP D 253 ? 1.1612 1.2623 0.9646 0.3716  -0.3127 -0.3423 317 ASP D CA  
10238 C C   . ASP D 253 ? 1.2546 1.3548 1.0246 0.4071  -0.3302 -0.3578 317 ASP D C   
10239 O O   . ASP D 253 ? 1.4355 1.5221 1.2089 0.4137  -0.3554 -0.3795 317 ASP D O   
10240 C CB  . ASP D 253 ? 1.4913 1.5863 1.2958 0.3587  -0.2993 -0.3312 317 ASP D CB  
10241 C CG  . ASP D 253 ? 1.5399 1.6392 1.3690 0.3288  -0.2776 -0.3120 317 ASP D CG  
10242 O OD1 . ASP D 253 ? 1.2642 1.3764 1.0977 0.3251  -0.2655 -0.3010 317 ASP D OD1 
10243 O OD2 . ASP D 253 ? 1.6205 1.7090 1.4628 0.3104  -0.2735 -0.3084 317 ASP D OD2 
10244 N N   . THR D 254 ? 1.4678 1.5820 1.2056 0.4305  -0.3169 -0.3464 318 THR D N   
10245 C CA  . THR D 254 ? 1.7211 1.8366 1.4223 0.4682  -0.3315 -0.3594 318 THR D CA  
10246 C C   . THR D 254 ? 1.6691 1.7889 1.3367 0.4897  -0.3200 -0.3511 318 THR D C   
10247 O O   . THR D 254 ? 1.7779 1.8992 1.4538 0.4742  -0.3030 -0.3372 318 THR D O   
10248 C CB  . THR D 254 ? 1.7468 1.8757 1.4331 0.4840  -0.3266 -0.3537 318 THR D CB  
10249 O OG1 . THR D 254 ? 2.1537 2.2967 1.8352 0.4773  -0.2958 -0.3262 318 THR D OG1 
10250 C CG2 . THR D 254 ? 1.4933 1.6200 1.2115 0.4674  -0.3406 -0.3647 318 THR D CG2 
10251 N N   . THR D 255 ? 1.7509 1.8731 1.3804 0.5266  -0.3297 -0.3603 319 THR D N   
10252 C CA  . THR D 255 ? 1.6908 1.8233 1.2846 0.5517  -0.3138 -0.3485 319 THR D CA  
10253 C C   . THR D 255 ? 1.5412 1.6930 1.1276 0.5519  -0.2845 -0.3216 319 THR D C   
10254 O O   . THR D 255 ? 1.4478 1.6025 1.0495 0.5394  -0.2819 -0.3169 319 THR D O   
10255 C CB  . THR D 255 ? 1.6849 1.8132 1.2377 0.5937  -0.3342 -0.3675 319 THR D CB  
10256 O OG1 . THR D 255 ? 1.7118 1.8428 1.2526 0.6096  -0.3440 -0.3741 319 THR D OG1 
10257 C CG2 . THR D 255 ? 1.6882 1.7952 1.2490 0.5938  -0.3648 -0.3948 319 THR D CG2 
10258 N N   . ASN D 256 ? 1.5173 1.6822 1.0822 0.5657  -0.2624 -0.3038 320 ASN D N   
10259 C CA  . ASN D 256 ? 1.4782 1.6606 1.0375 0.5657  -0.2336 -0.2768 320 ASN D CA  
10260 C C   . ASN D 256 ? 1.5167 1.7048 1.0380 0.6005  -0.2350 -0.2767 320 ASN D C   
10261 O O   . ASN D 256 ? 1.7016 1.8881 1.1881 0.6338  -0.2465 -0.2889 320 ASN D O   
10262 C CB  . ASN D 256 ? 1.3515 1.5478 0.9069 0.5658  -0.2077 -0.2560 320 ASN D CB  
10263 C CG  . ASN D 256 ? 1.2565 1.4474 0.8459 0.5343  -0.2055 -0.2551 320 ASN D CG  
10264 O OD1 . ASN D 256 ? 1.2713 1.4464 0.8843 0.5137  -0.2233 -0.2703 320 ASN D OD1 
10265 N ND2 . ASN D 256 ? 1.2612 1.4652 0.8532 0.5312  -0.1835 -0.2371 320 ASN D ND2 
10266 N N   . TYR D 257 ? 1.5759 1.7696 1.1019 0.5939  -0.2236 -0.2631 321 TYR D N   
10267 C CA  . TYR D 257 ? 1.4443 1.6438 0.9324 0.6267  -0.2201 -0.2580 321 TYR D CA  
10268 C C   . TYR D 257 ? 1.5883 1.7953 1.0875 0.6123  -0.1987 -0.2348 321 TYR D C   
10269 O O   . TYR D 257 ? 1.6528 1.8567 1.1897 0.5788  -0.1972 -0.2320 321 TYR D O   
10270 C CB  . TYR D 257 ? 1.5876 1.7750 1.0606 0.6470  -0.2526 -0.2863 321 TYR D CB  
10271 C CG  . TYR D 257 ? 1.7058 1.8828 1.2185 0.6183  -0.2721 -0.3021 321 TYR D CG  
10272 C CD1 . TYR D 257 ? 1.6613 1.8405 1.1847 0.6097  -0.2698 -0.2965 321 TYR D CD1 
10273 C CD2 . TYR D 257 ? 1.6241 1.7889 1.1630 0.6011  -0.2931 -0.3226 321 TYR D CD2 
10274 C CE1 . TYR D 257 ? 1.7564 1.9285 1.3175 0.5846  -0.2870 -0.3111 321 TYR D CE1 
10275 C CE2 . TYR D 257 ? 1.6537 1.8104 1.2308 0.5750  -0.3095 -0.3361 321 TYR D CE2 
10276 C CZ  . TYR D 257 ? 1.6989 1.8606 1.2875 0.5671  -0.3062 -0.3304 321 TYR D CZ  
10277 O OH  . TYR D 257 ? 1.4530 1.6090 1.0808 0.5420  -0.3214 -0.3434 321 TYR D OH  
10278 N N   . CYS D 258 ? 1.6325 1.8483 1.0975 0.6389  -0.1824 -0.2183 322 CYS D N   
10279 C CA  . CYS D 258 ? 1.7240 1.9466 1.1968 0.6270  -0.1582 -0.1921 322 CYS D CA  
10280 C C   . CYS D 258 ? 1.6865 1.9015 1.1578 0.6289  -0.1706 -0.1990 322 CYS D C   
10281 O O   . CYS D 258 ? 1.6169 1.8351 1.0893 0.6236  -0.1532 -0.1789 322 CYS D O   
10282 C CB  . CYS D 258 ? 1.8808 2.1167 1.3227 0.6505  -0.1302 -0.1663 322 CYS D CB  
10283 S SG  . CYS D 258 ? 2.8949 3.1437 2.3539 0.6377  -0.1105 -0.1534 322 CYS D SG  
10284 N N   . ASP D 259 ? 1.8419 2.0468 1.3133 0.6356  -0.2016 -0.2279 323 ASP D N   
10285 C CA  . ASP D 259 ? 2.0112 2.2099 1.4909 0.6326  -0.2175 -0.2389 323 ASP D CA  
10286 C C   . ASP D 259 ? 1.8388 2.0349 1.3714 0.5891  -0.2194 -0.2408 323 ASP D C   
10287 O O   . ASP D 259 ? 1.6712 1.8691 1.2309 0.5622  -0.2076 -0.2324 323 ASP D O   
10288 C CB  . ASP D 259 ? 2.0856 2.2758 1.5439 0.6605  -0.2508 -0.2697 323 ASP D CB  
10289 C CG  . ASP D 259 ? 2.6263 2.8135 2.0718 0.6761  -0.2635 -0.2769 323 ASP D CG  
10290 O OD1 . ASP D 259 ? 2.7521 2.9434 2.1802 0.6838  -0.2436 -0.2551 323 ASP D OD1 
10291 O OD2 . ASP D 259 ? 3.2959 3.4761 2.7496 0.6808  -0.2941 -0.3047 323 ASP D OD2 
10292 N N   . LYS D 260 ? 1.4785 1.6708 1.0240 0.5841  -0.2341 -0.2518 324 LYS D N   
10293 C CA  . LYS D 260 ? 1.4058 1.5966 0.9979 0.5472  -0.2361 -0.2541 324 LYS D CA  
10294 C C   . LYS D 260 ? 1.3124 1.4965 0.9288 0.5394  -0.2668 -0.2843 324 LYS D C   
10295 O O   . LYS D 260 ? 1.2770 1.4577 0.8767 0.5633  -0.2899 -0.3043 324 LYS D O   
10296 C CB  . LYS D 260 ? 1.3233 1.5165 0.9157 0.5457  -0.2273 -0.2418 324 LYS D CB  
10297 C CG  . LYS D 260 ? 1.4882 1.6797 1.1152 0.5263  -0.2436 -0.2566 324 LYS D CG  
10298 C CD  . LYS D 260 ? 1.5215 1.7140 1.1319 0.5431  -0.2455 -0.2539 324 LYS D CD  
10299 C CE  . LYS D 260 ? 1.3948 1.5888 0.9776 0.5533  -0.2177 -0.2242 324 LYS D CE  
10300 N NZ  . LYS D 260 ? 1.2766 1.4689 0.8364 0.5750  -0.2219 -0.2229 324 LYS D NZ  
10301 N N   . THR D 261 ? 1.3804 1.5620 1.0365 0.5061  -0.2668 -0.2869 325 THR D N   
10302 C CA  . THR D 261 ? 1.1727 1.3470 0.8563 0.4947  -0.2928 -0.3126 325 THR D CA  
10303 C C   . THR D 261 ? 1.1151 1.2913 0.8285 0.4814  -0.3052 -0.3231 325 THR D C   
10304 O O   . THR D 261 ? 1.2356 1.4143 0.9822 0.4518  -0.2946 -0.3144 325 THR D O   
10305 C CB  . THR D 261 ? 1.1007 1.2704 0.8132 0.4648  -0.2857 -0.3090 325 THR D CB  
10306 O OG1 . THR D 261 ? 1.1214 1.2905 0.8080 0.4783  -0.2762 -0.3015 325 THR D OG1 
10307 C CG2 . THR D 261 ? 1.1684 1.3290 0.9114 0.4516  -0.3114 -0.3338 325 THR D CG2 
10308 N N   . THR D 262 ? 1.2804 1.4559 0.9829 0.5042  -0.3289 -0.3430 326 THR D N   
10309 C CA  . THR D 262 ? 1.2823 1.4627 1.0098 0.4964  -0.3396 -0.3518 326 THR D CA  
10310 C C   . THR D 262 ? 1.2849 1.4635 1.0615 0.4704  -0.3577 -0.3707 326 THR D C   
10311 O O   . THR D 262 ? 1.3055 1.4905 1.1099 0.4600  -0.3653 -0.3777 326 THR D O   
10312 C CB  . THR D 262 ? 1.3230 1.5041 1.0199 0.5325  -0.3590 -0.3664 326 THR D CB  
10313 O OG1 . THR D 262 ? 1.7311 1.9057 1.4333 0.5437  -0.3901 -0.3952 326 THR D OG1 
10314 C CG2 . THR D 262 ? 1.3465 1.5271 0.9888 0.5639  -0.3437 -0.3500 326 THR D CG2 
10315 N N   . THR D 263 ? 1.4480 1.6178 1.2353 0.4607  -0.3646 -0.3788 327 THR D N   
10316 C CA  . THR D 263 ? 1.4433 1.6090 1.2760 0.4378  -0.3828 -0.3970 327 THR D CA  
10317 C C   . THR D 263 ? 1.2307 1.3994 1.0994 0.4003  -0.3619 -0.3805 327 THR D C   
10318 O O   . THR D 263 ? 1.1415 1.3071 1.0022 0.3892  -0.3406 -0.3622 327 THR D O   
10319 C CB  . THR D 263 ? 1.5822 1.7342 1.4109 0.4432  -0.3999 -0.4127 327 THR D CB  
10320 O OG1 . THR D 263 ? 1.3365 1.4851 1.1186 0.4819  -0.4114 -0.4213 327 THR D OG1 
10321 C CG2 . THR D 263 ? 1.4112 1.5582 1.2835 0.4285  -0.4263 -0.4367 327 THR D CG2 
10322 N N   . GLU D 264 ? 1.2199 1.3954 1.1282 0.3823  -0.3687 -0.3879 328 GLU D N   
10323 C CA  . GLU D 264 ? 1.3158 1.4964 1.2572 0.3497  -0.3490 -0.3726 328 GLU D CA  
10324 C C   . GLU D 264 ? 1.3075 1.4937 1.2265 0.3504  -0.3217 -0.3472 328 GLU D C   
10325 O O   . GLU D 264 ? 1.5790 1.7654 1.5130 0.3267  -0.3015 -0.3307 328 GLU D O   
10326 C CB  . GLU D 264 ? 1.3227 1.4929 1.2883 0.3235  -0.3446 -0.3707 328 GLU D CB  
10327 C CG  . GLU D 264 ? 1.5145 1.6807 1.5205 0.3102  -0.3668 -0.3916 328 GLU D CG  
10328 C CD  . GLU D 264 ? 1.5452 1.7088 1.5897 0.2748  -0.3534 -0.3822 328 GLU D CD  
10329 O OE1 . GLU D 264 ? 1.4473 1.6220 1.5112 0.2595  -0.3389 -0.3715 328 GLU D OE1 
10330 O OE2 . GLU D 264 ? 1.7724 1.9221 1.8264 0.2635  -0.3573 -0.3856 328 GLU D OE2 
10331 N N   . GLY D 265 ? 1.1973 1.3871 1.0802 0.3786  -0.3220 -0.3445 329 GLY D N   
10332 C CA  . GLY D 265 ? 1.0684 1.2616 0.9276 0.3824  -0.2976 -0.3205 329 GLY D CA  
10333 C C   . GLY D 265 ? 1.0599 1.2610 0.9430 0.3649  -0.2870 -0.3116 329 GLY D C   
10334 O O   . GLY D 265 ? 1.2318 1.4335 1.1063 0.3581  -0.2648 -0.2903 329 GLY D O   
10335 N N   . GLU D 266 ? 0.9365 1.1440 0.8513 0.3576  -0.3031 -0.3281 330 GLU D N   
10336 C CA  . GLU D 266 ? 0.9474 1.1641 0.8851 0.3439  -0.2950 -0.3221 330 GLU D CA  
10337 C C   . GLU D 266 ? 1.1514 1.3683 1.1244 0.3102  -0.2811 -0.3136 330 GLU D C   
10338 O O   . GLU D 266 ? 1.4396 1.6519 1.4342 0.2950  -0.2867 -0.3211 330 GLU D O   
10339 C CB  . GLU D 266 ? 0.9705 1.1968 0.9264 0.3535  -0.3176 -0.3430 330 GLU D CB  
10340 C CG  . GLU D 266 ? 1.0807 1.3177 1.0540 0.3453  -0.3097 -0.3368 330 GLU D CG  
10341 C CD  . GLU D 266 ? 1.6183 1.8660 1.6012 0.3618  -0.3317 -0.3563 330 GLU D CD  
10342 O OE1 . GLU D 266 ? 2.0043 2.2504 1.9806 0.3798  -0.3546 -0.3756 330 GLU D OE1 
10343 O OE2 . GLU D 266 ? 1.9834 2.2408 1.9804 0.3576  -0.3271 -0.3530 330 GLU D OE2 
10344 N N   . GLY D 267 ? 1.3500 1.5712 1.3275 0.3000  -0.2638 -0.2981 331 GLY D N   
10345 C CA  . GLY D 267 ? 1.2770 1.4962 1.2767 0.2720  -0.2462 -0.2853 331 GLY D CA  
10346 C C   . GLY D 267 ? 1.3459 1.5550 1.3193 0.2712  -0.2283 -0.2666 331 GLY D C   
10347 O O   . GLY D 267 ? 1.2157 1.4203 1.1576 0.2906  -0.2297 -0.2645 331 GLY D O   
10348 N N   . GLY D 268 ? 1.1570 1.3629 1.1434 0.2495  -0.2113 -0.2530 332 GLY D N   
10349 C CA  . GLY D 268 ? 1.1313 1.3289 1.0983 0.2467  -0.1950 -0.2359 332 GLY D CA  
10350 C C   . GLY D 268 ? 0.9504 1.1456 0.9325 0.2249  -0.1780 -0.2220 332 GLY D C   
10351 O O   . GLY D 268 ? 0.9691 1.1698 0.9709 0.2155  -0.1767 -0.2233 332 GLY D O   
10352 N N   . ILE D 269 ? 0.6825 0.8697 0.6552 0.2180  -0.1658 -0.2096 333 ILE D N   
10353 C CA  . ILE D 269 ? 0.7242 0.9074 0.7060 0.2005  -0.1502 -0.1959 333 ILE D CA  
10354 C C   . ILE D 269 ? 0.7307 0.9087 0.6917 0.2049  -0.1371 -0.1795 333 ILE D C   
10355 O O   . ILE D 269 ? 0.7079 0.8848 0.6526 0.2159  -0.1391 -0.1798 333 ILE D O   
10356 C CB  . ILE D 269 ? 0.7432 0.9216 0.7481 0.1797  -0.1501 -0.2005 333 ILE D CB  
10357 C CG1 . ILE D 269 ? 1.0068 1.1826 1.0231 0.1635  -0.1367 -0.1896 333 ILE D CG1 
10358 C CG2 . ILE D 269 ? 0.7256 0.8954 0.7219 0.1784  -0.1507 -0.2005 333 ILE D CG2 
10359 C CD1 . ILE D 269 ? 1.0785 1.2508 1.1181 0.1444  -0.1359 -0.1941 333 ILE D CD1 
10360 N N   . GLN D 270 ? 0.7028 0.8783 0.6656 0.1969  -0.1242 -0.1657 334 GLN D N   
10361 C CA  . GLN D 270 ? 0.6412 0.8131 0.5898 0.1998  -0.1116 -0.1493 334 GLN D CA  
10362 C C   . GLN D 270 ? 0.6836 0.8512 0.6312 0.1939  -0.1089 -0.1478 334 GLN D C   
10363 O O   . GLN D 270 ? 0.7751 0.9375 0.7373 0.1784  -0.1100 -0.1524 334 GLN D O   
10364 C CB  . GLN D 270 ? 0.6459 0.8135 0.6035 0.1880  -0.1010 -0.1378 334 GLN D CB  
10365 C CG  . GLN D 270 ? 0.6807 0.8444 0.6287 0.1895  -0.0881 -0.1200 334 GLN D CG  
10366 C CD  . GLN D 270 ? 0.7200 0.8776 0.6776 0.1789  -0.0807 -0.1107 334 GLN D CD  
10367 O OE1 . GLN D 270 ? 0.9257 1.0816 0.8968 0.1687  -0.0836 -0.1173 334 GLN D OE1 
10368 N NE2 . GLN D 270 ? 0.6738 0.8279 0.6249 0.1820  -0.0711 -0.0953 334 GLN D NE2 
10369 N N   . GLY D 271 ? 0.6537 0.8235 0.5834 0.2071  -0.1047 -0.1407 335 GLY D N   
10370 C CA  . GLY D 271 ? 0.6682 0.8354 0.5961 0.2035  -0.1014 -0.1384 335 GLY D CA  
10371 C C   . GLY D 271 ? 0.6689 0.8409 0.5815 0.2154  -0.0906 -0.1242 335 GLY D C   
10372 O O   . GLY D 271 ? 0.8385 1.0144 0.7392 0.2278  -0.0858 -0.1160 335 GLY D O   
10373 N N   . PHE D 272 ? 0.6281 0.7998 0.5408 0.2125  -0.0863 -0.1208 336 PHE D N   
10374 C CA  . PHE D 272 ? 0.7636 0.9423 0.6656 0.2230  -0.0743 -0.1062 336 PHE D CA  
10375 C C   . PHE D 272 ? 0.8519 1.0363 0.7387 0.2380  -0.0768 -0.1106 336 PHE D C   
10376 O O   . PHE D 272 ? 0.8160 0.9965 0.7005 0.2395  -0.0896 -0.1262 336 PHE D O   
10377 C CB  . PHE D 272 ? 0.6780 0.8544 0.5970 0.2066  -0.0628 -0.0932 336 PHE D CB  
10378 C CG  . PHE D 272 ? 0.8214 0.9918 0.7525 0.1926  -0.0672 -0.1006 336 PHE D CG  
10379 C CD1 . PHE D 272 ? 0.8333 1.0077 0.7629 0.1953  -0.0639 -0.0982 336 PHE D CD1 
10380 C CD2 . PHE D 272 ? 0.8451 1.0057 0.7877 0.1781  -0.0748 -0.1105 336 PHE D CD2 
10381 C CE1 . PHE D 272 ? 0.6512 0.8183 0.5895 0.1839  -0.0689 -0.1054 336 PHE D CE1 
10382 C CE2 . PHE D 272 ? 0.7263 0.8794 0.6772 0.1665  -0.0785 -0.1166 336 PHE D CE2 
10383 C CZ  . PHE D 272 ? 0.6533 0.8087 0.6012 0.1696  -0.0760 -0.1142 336 PHE D CZ  
10384 N N   . MET D 273 ? 0.8053 0.9987 0.6821 0.2497  -0.0642 -0.0961 337 MET D N   
10385 C CA  . MET D 273 ? 0.8740 1.0754 0.7381 0.2638  -0.0614 -0.0952 337 MET D CA  
10386 C C   . MET D 273 ? 0.8437 1.0539 0.7160 0.2611  -0.0429 -0.0746 337 MET D C   
10387 O O   . MET D 273 ? 1.0174 1.2279 0.8953 0.2572  -0.0330 -0.0607 337 MET D O   
10388 C CB  . MET D 273 ? 0.9409 1.1479 0.7764 0.2910  -0.0661 -0.1000 337 MET D CB  
10389 C CG  . MET D 273 ? 1.0388 1.2384 0.8664 0.2969  -0.0865 -0.1220 337 MET D CG  
10390 S SD  . MET D 273 ? 1.1064 1.3111 0.8982 0.3317  -0.0949 -0.1299 337 MET D SD  
10391 C CE  . MET D 273 ? 1.2340 1.4446 1.0138 0.3421  -0.0787 -0.1092 337 MET D CE  
10392 N N   . ILE D 274 ? 0.7938 1.0111 0.6680 0.2635  -0.0387 -0.0726 338 ILE D N   
10393 C CA  . ILE D 274 ? 0.7838 1.0114 0.6712 0.2596  -0.0219 -0.0542 338 ILE D CA  
10394 C C   . ILE D 274 ? 0.7843 1.0269 0.6535 0.2824  -0.0140 -0.0486 338 ILE D C   
10395 O O   . ILE D 274 ? 0.7370 0.9808 0.5941 0.2926  -0.0229 -0.0614 338 ILE D O   
10396 C CB  . ILE D 274 ? 0.7123 0.9367 0.6244 0.2395  -0.0231 -0.0562 338 ILE D CB  
10397 C CG1 . ILE D 274 ? 0.5712 0.7792 0.4957 0.2199  -0.0333 -0.0654 338 ILE D CG1 
10398 C CG2 . ILE D 274 ? 0.6762 0.9108 0.6081 0.2328  -0.0070 -0.0371 338 ILE D CG2 
10399 C CD1 . ILE D 274 ? 0.5461 0.7489 0.4924 0.2013  -0.0338 -0.0656 338 ILE D CD1 
10400 N N   . GLU D 275 ? 0.8984 1.1515 0.7648 0.2911  0.0028  -0.0291 339 GLU D N   
10401 C CA  . GLU D 275 ? 0.9631 1.2328 0.8131 0.3135  0.0147  -0.0197 339 GLU D CA  
10402 C C   . GLU D 275 ? 1.0670 1.3508 0.9433 0.3038  0.0310  -0.0033 339 GLU D C   
10403 O O   . GLU D 275 ? 1.0419 1.3248 0.9421 0.2874  0.0407  0.0111  339 GLU D O   
10404 C CB  . GLU D 275 ? 0.9736 1.2454 0.7996 0.3327  0.0232  -0.0084 339 GLU D CB  
10405 C CG  . GLU D 275 ? 1.4119 1.7020 1.2234 0.3547  0.0420  0.0089  339 GLU D CG  
10406 C CD  . GLU D 275 ? 1.7897 2.0873 1.5723 0.3804  0.0352  -0.0039 339 GLU D CD  
10407 O OE1 . GLU D 275 ? 2.0954 2.3819 1.8654 0.3838  0.0143  -0.0267 339 GLU D OE1 
10408 O OE2 . GLU D 275 ? 1.8816 2.1963 1.6545 0.3981  0.0510  0.0092  339 GLU D OE2 
10409 N N   . GLY D 276 ? 1.0337 1.3303 0.9071 0.3140  0.0328  -0.0064 340 GLY D N   
10410 C CA  . GLY D 276 ? 1.0671 1.3801 0.9674 0.3065  0.0474  0.0077  340 GLY D CA  
10411 C C   . GLY D 276 ? 1.2177 1.5477 1.1063 0.3259  0.0507  0.0048  340 GLY D C   
10412 O O   . GLY D 276 ? 1.1720 1.5030 1.0273 0.3499  0.0463  -0.0030 340 GLY D O   
10413 N N   . SER D 277 ? 1.3551 1.6987 1.2713 0.3168  0.0580  0.0106  341 SER D N   
10414 C CA  . SER D 277 ? 1.3938 1.7521 1.3039 0.3316  0.0576  0.0039  341 SER D CA  
10415 C C   . SER D 277 ? 1.3734 1.7137 1.2619 0.3355  0.0339  -0.0222 341 SER D C   
10416 O O   . SER D 277 ? 1.4583 1.7994 1.3154 0.3589  0.0281  -0.0318 341 SER D O   
10417 C CB  . SER D 277 ? 1.2709 1.6425 1.2197 0.3157  0.0641  0.0103  341 SER D CB  
10418 O OG  . SER D 277 ? 1.7648 2.1566 1.7362 0.3142  0.0868  0.0348  341 SER D OG  
10419 N N   . ASN D 278 ? 1.3173 1.6406 1.2233 0.3127  0.0204  -0.0332 342 ASN D N   
10420 C CA  . ASN D 278 ? 1.1107 1.4113 1.0005 0.3101  -0.0012 -0.0549 342 ASN D CA  
10421 C C   . ASN D 278 ? 1.0159 1.3030 0.8970 0.3056  -0.0046 -0.0546 342 ASN D C   
10422 O O   . ASN D 278 ? 0.8938 1.1823 0.7907 0.2939  0.0061  -0.0399 342 ASN D O   
10423 C CB  . ASN D 278 ? 1.1402 1.4280 1.0522 0.2875  -0.0119 -0.0643 342 ASN D CB  
10424 C CG  . ASN D 278 ? 1.1785 1.4761 1.0960 0.2931  -0.0132 -0.0690 342 ASN D CG  
10425 O OD1 . ASN D 278 ? 1.1877 1.4888 1.0832 0.3129  -0.0185 -0.0784 342 ASN D OD1 
10426 N ND2 . ASN D 278 ? 1.3570 1.6586 1.3039 0.2764  -0.0094 -0.0635 342 ASN D ND2 
10427 N N   . SER D 279 ? 0.9933 1.2670 0.8504 0.3151  -0.0203 -0.0712 343 SER D N   
10428 C CA  . SER D 279 ? 0.9383 1.1982 0.7896 0.3096  -0.0270 -0.0747 343 SER D CA  
10429 C C   . SER D 279 ? 0.9702 1.2094 0.8245 0.2958  -0.0469 -0.0943 343 SER D C   
10430 O O   . SER D 279 ? 0.9816 1.2146 0.8303 0.2988  -0.0587 -0.1085 343 SER D O   
10431 C CB  . SER D 279 ? 0.9332 1.1982 0.7542 0.3353  -0.0257 -0.0739 343 SER D CB  
10432 O OG  . SER D 279 ? 1.1113 1.3937 0.9318 0.3449  -0.0045 -0.0520 343 SER D OG  
10433 N N   . TRP D 280 ? 1.0342 1.2624 0.8980 0.2806  -0.0499 -0.0943 344 TRP D N   
10434 C CA  . TRP D 280 ? 0.7525 0.9623 0.6240 0.2646  -0.0656 -0.1098 344 TRP D CA  
10435 C C   . TRP D 280 ? 0.6500 0.8520 0.5130 0.2671  -0.0748 -0.1179 344 TRP D C   
10436 O O   . TRP D 280 ? 0.6635 0.8703 0.5233 0.2711  -0.0675 -0.1084 344 TRP D O   
10437 C CB  . TRP D 280 ? 0.7011 0.9048 0.5983 0.2400  -0.0610 -0.1035 344 TRP D CB  
10438 C CG  . TRP D 280 ? 0.8132 1.0238 0.7223 0.2360  -0.0547 -0.0979 344 TRP D CG  
10439 C CD1 . TRP D 280 ? 0.7184 0.9454 0.6379 0.2384  -0.0391 -0.0814 344 TRP D CD1 
10440 C CD2 . TRP D 280 ? 0.7441 0.9458 0.6573 0.2295  -0.0639 -0.1088 344 TRP D CD2 
10441 N NE1 . TRP D 280 ? 0.7501 0.9807 0.6813 0.2340  -0.0389 -0.0824 344 TRP D NE1 
10442 C CE2 . TRP D 280 ? 0.6878 0.9030 0.6139 0.2293  -0.0536 -0.0986 344 TRP D CE2 
10443 C CE3 . TRP D 280 ? 0.6829 0.8671 0.5918 0.2237  -0.0788 -0.1246 344 TRP D CE3 
10444 C CZ2 . TRP D 280 ? 0.6107 0.8215 0.5423 0.2252  -0.0593 -0.1054 344 TRP D CZ2 
10445 C CZ3 . TRP D 280 ? 0.6173 0.7954 0.5304 0.2192  -0.0835 -0.1300 344 TRP D CZ3 
10446 C CH2 . TRP D 280 ? 0.6382 0.8294 0.5612 0.2208  -0.0745 -0.1212 344 TRP D CH2 
10447 N N   . ILE D 281 ? 0.6531 0.8427 0.5130 0.2652  -0.0916 -0.1358 345 ILE D N   
10448 C CA  . ILE D 281 ? 0.7265 0.9079 0.5873 0.2616  -0.1019 -0.1451 345 ILE D CA  
10449 C C   . ILE D 281 ? 0.8049 0.9719 0.6848 0.2393  -0.1099 -0.1537 345 ILE D C   
10450 O O   . ILE D 281 ? 0.9105 1.0689 0.7913 0.2362  -0.1183 -0.1633 345 ILE D O   
10451 C CB  . ILE D 281 ? 0.7446 0.9251 0.5848 0.2824  -0.1162 -0.1599 345 ILE D CB  
10452 C CG1 . ILE D 281 ? 0.8195 1.0134 0.6369 0.3067  -0.1076 -0.1506 345 ILE D CG1 
10453 C CG2 . ILE D 281 ? 0.7707 0.9430 0.6186 0.2755  -0.1286 -0.1712 345 ILE D CG2 
10454 C CD1 . ILE D 281 ? 0.9565 1.1497 0.7487 0.3319  -0.1224 -0.1657 345 ILE D CD1 
10455 N N   . GLY D 282 ? 0.7380 0.9020 0.6322 0.2247  -0.1067 -0.1495 346 GLY D N   
10456 C CA  . GLY D 282 ? 0.7602 0.9113 0.6711 0.2051  -0.1132 -0.1571 346 GLY D CA  
10457 C C   . GLY D 282 ? 0.7156 0.8638 0.6276 0.2075  -0.1255 -0.1697 346 GLY D C   
10458 O O   . GLY D 282 ? 0.7365 0.8927 0.6392 0.2205  -0.1261 -0.1690 346 GLY D O   
10459 N N   . ARG D 283 ? 0.6721 0.8089 0.5961 0.1952  -0.1353 -0.1809 347 ARG D N   
10460 C CA  . ARG D 283 ? 0.6335 0.7684 0.5656 0.1944  -0.1474 -0.1934 347 ARG D CA  
10461 C C   . ARG D 283 ? 0.6097 0.7325 0.5615 0.1752  -0.1528 -0.2005 347 ARG D C   
10462 O O   . ARG D 283 ? 0.6863 0.7990 0.6408 0.1655  -0.1504 -0.1986 347 ARG D O   
10463 C CB  . ARG D 283 ? 0.7145 0.8511 0.6313 0.2145  -0.1614 -0.2063 347 ARG D CB  
10464 C CG  . ARG D 283 ? 0.6731 0.7975 0.5907 0.2135  -0.1742 -0.2191 347 ARG D CG  
10465 C CD  . ARG D 283 ? 0.7257 0.8532 0.6223 0.2380  -0.1862 -0.2296 347 ARG D CD  
10466 N NE  . ARG D 283 ? 0.8396 0.9534 0.7381 0.2383  -0.2027 -0.2452 347 ARG D NE  
10467 C CZ  . ARG D 283 ? 0.9710 1.0833 0.8542 0.2585  -0.2184 -0.2594 347 ARG D CZ  
10468 N NH1 . ARG D 283 ? 0.9692 1.0935 0.8319 0.2811  -0.2189 -0.2593 347 ARG D NH1 
10469 N NH2 . ARG D 283 ? 1.3378 1.4353 1.2251 0.2570  -0.2342 -0.2736 347 ARG D NH2 
10470 N N   . ILE D 284 ? 0.7135 0.8381 0.6797 0.1703  -0.1592 -0.2078 348 ILE D N   
10471 C CA  . ILE D 284 ? 0.7661 0.8810 0.7538 0.1526  -0.1637 -0.2142 348 ILE D CA  
10472 C C   . ILE D 284 ? 0.8143 0.9191 0.8007 0.1569  -0.1789 -0.2279 348 ILE D C   
10473 O O   . ILE D 284 ? 0.9749 1.0837 0.9521 0.1734  -0.1912 -0.2384 348 ILE D O   
10474 C CB  . ILE D 284 ? 0.7024 0.8251 0.7089 0.1468  -0.1658 -0.2181 348 ILE D CB  
10475 C CG1 . ILE D 284 ? 0.8853 1.0174 0.8888 0.1465  -0.1523 -0.2053 348 ILE D CG1 
10476 C CG2 . ILE D 284 ? 0.6574 0.7716 0.6888 0.1269  -0.1669 -0.2218 348 ILE D CG2 
10477 C CD1 . ILE D 284 ? 1.0451 1.1821 1.0698 0.1344  -0.1489 -0.2050 348 ILE D CD1 
10478 N N   . ILE D 285 ? 0.8198 0.9098 0.8138 0.1434  -0.1787 -0.2281 349 ILE D N   
10479 C CA  . ILE D 285 ? 0.8390 0.9160 0.8300 0.1474  -0.1929 -0.2400 349 ILE D CA  
10480 C C   . ILE D 285 ? 0.8647 0.9395 0.8742 0.1457  -0.2091 -0.2552 349 ILE D C   
10481 O O   . ILE D 285 ? 0.9259 0.9997 0.9266 0.1611  -0.2245 -0.2679 349 ILE D O   
10482 C CB  . ILE D 285 ? 0.8110 0.8705 0.8031 0.1343  -0.1883 -0.2353 349 ILE D CB  
10483 C CG1 . ILE D 285 ? 0.6108 0.6731 0.5848 0.1388  -0.1758 -0.2230 349 ILE D CG1 
10484 C CG2 . ILE D 285 ? 0.6914 0.7352 0.6815 0.1386  -0.2049 -0.2487 349 ILE D CG2 
10485 C CD1 . ILE D 285 ? 0.5654 0.6109 0.5383 0.1278  -0.1717 -0.2185 349 ILE D CD1 
10486 N N   . ASN D 286 ? 0.8780 0.9527 0.9138 0.1279  -0.2058 -0.2541 350 ASN D N   
10487 C CA  . ASN D 286 ? 0.9509 1.0246 1.0121 0.1227  -0.2205 -0.2679 350 ASN D CA  
10488 C C   . ASN D 286 ? 0.9252 1.0176 1.0013 0.1240  -0.2203 -0.2700 350 ASN D C   
10489 O O   . ASN D 286 ? 1.2551 1.3520 1.3534 0.1081  -0.2112 -0.2644 350 ASN D O   
10490 C CB  . ASN D 286 ? 0.9486 1.0072 1.0329 0.1007  -0.2175 -0.2657 350 ASN D CB  
10491 C CG  . ASN D 286 ? 1.2300 1.2672 1.3013 0.1005  -0.2221 -0.2670 350 ASN D CG  
10492 O OD1 . ASN D 286 ? 1.5551 1.5852 1.6099 0.0981  -0.2101 -0.2557 350 ASN D OD1 
10493 N ND2 . ASN D 286 ? 1.3863 1.4126 1.4651 0.1039  -0.2408 -0.2817 350 ASN D ND2 
10494 N N   . PRO D 287 ? 0.8670 0.9703 0.9298 0.1441  -0.2305 -0.2782 351 PRO D N   
10495 C CA  . PRO D 287 ? 0.9988 1.1200 1.0694 0.1494  -0.2303 -0.2794 351 PRO D CA  
10496 C C   . PRO D 287 ? 1.1449 1.2718 1.2536 0.1347  -0.2360 -0.2871 351 PRO D C   
10497 O O   . PRO D 287 ? 1.2904 1.4321 1.4098 0.1336  -0.2306 -0.2844 351 PRO D O   
10498 C CB  . PRO D 287 ? 0.9520 1.0779 1.0010 0.1753  -0.2460 -0.2913 351 PRO D CB  
10499 C CG  . PRO D 287 ? 0.8263 0.9404 0.8489 0.1844  -0.2457 -0.2890 351 PRO D CG  
10500 C CD  . PRO D 287 ? 0.8863 0.9843 0.9264 0.1646  -0.2453 -0.2890 351 PRO D CD  
10501 N N   . GLY D 288 ? 1.2044 1.3198 1.3347 0.1237  -0.2464 -0.2962 352 GLY D N   
10502 C CA  . GLY D 288 ? 1.2617 1.3828 1.4329 0.1067  -0.2490 -0.3012 352 GLY D CA  
10503 C C   . GLY D 288 ? 1.2336 1.3574 1.4167 0.0877  -0.2265 -0.2844 352 GLY D C   
10504 O O   . GLY D 288 ? 1.0978 1.2382 1.2938 0.0852  -0.2190 -0.2808 352 GLY D O   
10505 N N   . SER D 289 ? 1.1883 1.2950 1.3646 0.0762  -0.2162 -0.2744 353 SER D N   
10506 C CA  . SER D 289 ? 1.0495 1.1548 1.2354 0.0585  -0.1960 -0.2592 353 SER D CA  
10507 C C   . SER D 289 ? 1.2394 1.3491 1.3989 0.0638  -0.1798 -0.2452 353 SER D C   
10508 O O   . SER D 289 ? 1.2785 1.3882 1.4425 0.0523  -0.1635 -0.2333 353 SER D O   
10509 C CB  . SER D 289 ? 1.1341 1.2169 1.3233 0.0446  -0.1927 -0.2546 353 SER D CB  
10510 O OG  . SER D 289 ? 1.7386 1.8057 1.9018 0.0551  -0.2019 -0.2586 353 SER D OG  
10511 N N   . LYS D 290 ? 1.2597 1.3729 1.3921 0.0818  -0.1843 -0.2467 354 LYS D N   
10512 C CA  . LYS D 290 ? 1.0336 1.1505 1.1417 0.0881  -0.1708 -0.2339 354 LYS D CA  
10513 C C   . LYS D 290 ? 0.9023 1.0036 0.9973 0.0793  -0.1589 -0.2223 354 LYS D C   
10514 O O   . LYS D 290 ? 1.1547 1.2576 1.2382 0.0785  -0.1460 -0.2107 354 LYS D O   
10515 C CB  . LYS D 290 ? 1.1063 1.2387 1.2256 0.0851  -0.1615 -0.2286 354 LYS D CB  
10516 C CG  . LYS D 290 ? 0.9214 1.0702 1.0525 0.0953  -0.1731 -0.2399 354 LYS D CG  
10517 C CD  . LYS D 290 ? 1.3633 1.5166 1.4664 0.1159  -0.1776 -0.2403 354 LYS D CD  
10518 C CE  . LYS D 290 ? 2.0385 2.2057 2.1492 0.1290  -0.1919 -0.2533 354 LYS D CE  
10519 N NZ  . LYS D 290 ? 2.3312 2.5124 2.4579 0.1249  -0.1853 -0.2503 354 LYS D NZ  
10520 N N   . LYS D 291 ? 0.8294 0.9146 0.9265 0.0734  -0.1645 -0.2260 355 LYS D N   
10521 C CA  . LYS D 291 ? 0.8421 0.9103 0.9267 0.0660  -0.1555 -0.2166 355 LYS D CA  
10522 C C   . LYS D 291 ? 1.0225 1.0857 1.0792 0.0795  -0.1582 -0.2157 355 LYS D C   
10523 O O   . LYS D 291 ? 1.0780 1.1410 1.1269 0.0919  -0.1714 -0.2257 355 LYS D O   
10524 C CB  . LYS D 291 ? 0.9361 0.9872 1.0357 0.0536  -0.1604 -0.2207 355 LYS D CB  
10525 C CG  . LYS D 291 ? 1.3100 1.3628 1.4365 0.0369  -0.1519 -0.2166 355 LYS D CG  
10526 C CD  . LYS D 291 ? 1.6697 1.7047 1.7894 0.0253  -0.1387 -0.2045 355 LYS D CD  
10527 C CE  . LYS D 291 ? 1.5998 1.6347 1.7467 0.0089  -0.1297 -0.1999 355 LYS D CE  
10528 N NZ  . LYS D 291 ? 1.6562 1.6891 1.8312 0.0024  -0.1421 -0.2104 355 LYS D NZ  
10529 N N   . GLY D 292 ? 0.9686 1.0281 1.0110 0.0780  -0.1462 -0.2041 356 GLY D N   
10530 C CA  . GLY D 292 ? 0.7895 0.8440 0.8095 0.0884  -0.1473 -0.2022 356 GLY D CA  
10531 C C   . GLY D 292 ? 0.7795 0.8498 0.7860 0.1035  -0.1456 -0.1994 356 GLY D C   
10532 O O   . GLY D 292 ? 0.7909 0.8742 0.8006 0.1112  -0.1496 -0.2037 356 GLY D O   
10533 N N   . PHE D 293 ? 0.7013 0.7704 0.6928 0.1080  -0.1393 -0.1918 357 PHE D N   
10534 C CA  . PHE D 293 ? 0.7009 0.7846 0.6805 0.1220  -0.1359 -0.1871 357 PHE D CA  
10535 C C   . PHE D 293 ? 0.6982 0.7791 0.6622 0.1320  -0.1377 -0.1869 357 PHE D C   
10536 O O   . PHE D 293 ? 0.8775 0.9476 0.8396 0.1252  -0.1347 -0.1835 357 PHE D O   
10537 C CB  . PHE D 293 ? 0.7616 0.8517 0.7444 0.1161  -0.1228 -0.1747 357 PHE D CB  
10538 C CG  . PHE D 293 ? 0.7282 0.8324 0.7015 0.1288  -0.1178 -0.1678 357 PHE D CG  
10539 C CD1 . PHE D 293 ? 0.6996 0.8059 0.6638 0.1342  -0.1125 -0.1606 357 PHE D CD1 
10540 C CD2 . PHE D 293 ? 0.7061 0.8216 0.6803 0.1357  -0.1180 -0.1679 357 PHE D CD2 
10541 C CE1 . PHE D 293 ? 0.7472 0.8668 0.7047 0.1453  -0.1062 -0.1526 357 PHE D CE1 
10542 C CE2 . PHE D 293 ? 0.6298 0.7566 0.5939 0.1479  -0.1124 -0.1600 357 PHE D CE2 
10543 C CZ  . PHE D 293 ? 0.6214 0.7503 0.5777 0.1523  -0.1058 -0.1517 357 PHE D CZ  
10544 N N   . GLU D 294 ? 0.6083 0.6989 0.5602 0.1493  -0.1428 -0.1909 358 GLU D N   
10545 C CA  . GLU D 294 ? 0.6510 0.7423 0.5875 0.1620  -0.1443 -0.1912 358 GLU D CA  
10546 C C   . GLU D 294 ? 0.6663 0.7754 0.5928 0.1759  -0.1357 -0.1822 358 GLU D C   
10547 O O   . GLU D 294 ? 0.7868 0.9058 0.7134 0.1808  -0.1335 -0.1800 358 GLU D O   
10548 C CB  . GLU D 294 ? 0.7430 0.8262 0.6717 0.1722  -0.1601 -0.2061 358 GLU D CB  
10549 C CG  . GLU D 294 ? 0.9022 0.9934 0.8264 0.1861  -0.1701 -0.2156 358 GLU D CG  
10550 C CD  . GLU D 294 ? 1.2229 1.3034 1.1404 0.1962  -0.1884 -0.2323 358 GLU D CD  
10551 O OE1 . GLU D 294 ? 1.4771 1.5473 1.3865 0.1987  -0.1921 -0.2352 358 GLU D OE1 
10552 O OE2 . GLU D 294 ? 1.1703 1.2523 1.0907 0.2025  -0.2004 -0.2435 358 GLU D OE2 
10553 N N   . ILE D 295 ? 0.6788 0.7922 0.5979 0.1820  -0.1298 -0.1760 359 ILE D N   
10554 C CA  . ILE D 295 ? 0.7203 0.8513 0.6315 0.1953  -0.1199 -0.1657 359 ILE D CA  
10555 C C   . ILE D 295 ? 0.8484 0.9829 0.7455 0.2109  -0.1229 -0.1693 359 ILE D C   
10556 O O   . ILE D 295 ? 0.7964 0.9209 0.6938 0.2068  -0.1274 -0.1739 359 ILE D O   
10557 C CB  . ILE D 295 ? 0.6894 0.8259 0.6124 0.1845  -0.1058 -0.1508 359 ILE D CB  
10558 C CG1 . ILE D 295 ? 0.6756 0.8301 0.5935 0.1971  -0.0947 -0.1388 359 ILE D CG1 
10559 C CG2 . ILE D 295 ? 0.6929 0.8237 0.6199 0.1784  -0.1046 -0.1494 359 ILE D CG2 
10560 C CD1 . ILE D 295 ? 0.6772 0.8360 0.6102 0.1853  -0.0822 -0.1242 359 ILE D CD1 
10561 N N   . TYR D 296 ? 0.9294 1.0782 0.8126 0.2301  -0.1197 -0.1665 360 TYR D N   
10562 C CA  . TYR D 296 ? 0.7520 0.9034 0.6173 0.2496  -0.1264 -0.1743 360 TYR D CA  
10563 C C   . TYR D 296 ? 0.8047 0.9770 0.6613 0.2656  -0.1121 -0.1611 360 TYR D C   
10564 O O   . TYR D 296 ? 0.9138 1.0973 0.7685 0.2705  -0.1023 -0.1506 360 TYR D O   
10565 C CB  . TYR D 296 ? 0.7778 0.9226 0.6316 0.2605  -0.1420 -0.1894 360 TYR D CB  
10566 C CG  . TYR D 296 ? 1.0122 1.1551 0.8460 0.2814  -0.1533 -0.2015 360 TYR D CG  
10567 C CD1 . TYR D 296 ? 1.2005 1.3284 1.0346 0.2777  -0.1640 -0.2119 360 TYR D CD1 
10568 C CD2 . TYR D 296 ? 1.2493 1.4042 1.0619 0.3062  -0.1536 -0.2025 360 TYR D CD2 
10569 C CE1 . TYR D 296 ? 1.1518 1.2768 0.9663 0.2984  -0.1757 -0.2240 360 TYR D CE1 
10570 C CE2 . TYR D 296 ? 1.4491 1.6021 1.2409 0.3278  -0.1646 -0.2144 360 TYR D CE2 
10571 C CZ  . TYR D 296 ? 1.2706 1.4087 1.0639 0.3238  -0.1761 -0.2255 360 TYR D CZ  
10572 O OH  . TYR D 296 ? 1.1645 1.3000 0.9358 0.3470  -0.1881 -0.2381 360 TYR D OH  
10573 N N   . LYS D 297 ? 0.7469 0.9241 0.5987 0.2738  -0.1103 -0.1610 361 LYS D N   
10574 C CA  . LYS D 297 ? 0.9096 1.1080 0.7595 0.2854  -0.0945 -0.1467 361 LYS D CA  
10575 C C   . LYS D 297 ? 1.0403 1.2494 0.8639 0.3145  -0.0960 -0.1505 361 LYS D C   
10576 O O   . LYS D 297 ? 1.1514 1.3500 0.9590 0.3259  -0.1119 -0.1669 361 LYS D O   
10577 C CB  . LYS D 297 ? 0.7781 0.9777 0.6409 0.2775  -0.0914 -0.1443 361 LYS D CB  
10578 C CG  . LYS D 297 ? 0.7129 0.9349 0.5851 0.2823  -0.0741 -0.1282 361 LYS D CG  
10579 C CD  . LYS D 297 ? 0.6331 0.8522 0.5191 0.2728  -0.0760 -0.1302 361 LYS D CD  
10580 C CE  . LYS D 297 ? 0.7056 0.9488 0.5987 0.2835  -0.0629 -0.1195 361 LYS D CE  
10581 N NZ  . LYS D 297 ? 0.8533 1.0921 0.7605 0.2740  -0.0674 -0.1236 361 LYS D NZ  
10582 N N   . PHE D 298 ? 0.8794 1.1086 0.6985 0.3268  -0.0795 -0.1349 362 PHE D N   
10583 C CA  . PHE D 298 ? 0.8414 1.0825 0.6332 0.3566  -0.0777 -0.1358 362 PHE D CA  
10584 C C   . PHE D 298 ? 0.9288 1.1941 0.7239 0.3663  -0.0567 -0.1174 362 PHE D C   
10585 O O   . PHE D 298 ? 0.9837 1.2583 0.7989 0.3531  -0.0408 -0.0997 362 PHE D O   
10586 C CB  . PHE D 298 ? 0.8661 1.1067 0.6432 0.3661  -0.0781 -0.1343 362 PHE D CB  
10587 C CG  . PHE D 298 ? 0.9888 1.2097 0.7611 0.3620  -0.0990 -0.1531 362 PHE D CG  
10588 C CD1 . PHE D 298 ? 1.1578 1.3714 0.9064 0.3826  -0.1165 -0.1714 362 PHE D CD1 
10589 C CD2 . PHE D 298 ? 1.0129 1.2231 0.8051 0.3385  -0.1016 -0.1528 362 PHE D CD2 
10590 C CE1 . PHE D 298 ? 1.0989 1.2951 0.8474 0.3780  -0.1366 -0.1891 362 PHE D CE1 
10591 C CE2 . PHE D 298 ? 1.0531 1.2476 0.8445 0.3344  -0.1199 -0.1695 362 PHE D CE2 
10592 C CZ  . PHE D 298 ? 1.0186 1.2063 0.7899 0.3533  -0.1376 -0.1876 362 PHE D CZ  
10593 N N   . LEU D 299 ? 0.9600 1.2359 0.7365 0.3898  -0.0565 -0.1213 363 LEU D N   
10594 C CA  . LEU D 299 ? 1.0325 1.3343 0.8123 0.4014  -0.0351 -0.1031 363 LEU D CA  
10595 C C   . LEU D 299 ? 1.2103 1.5226 0.9707 0.4196  -0.0228 -0.0906 363 LEU D C   
10596 O O   . LEU D 299 ? 1.5224 1.8270 1.2527 0.4395  -0.0340 -0.1021 363 LEU D O   
10597 C CB  . LEU D 299 ? 1.1597 1.4704 0.9270 0.4208  -0.0383 -0.1113 363 LEU D CB  
10598 C CG  . LEU D 299 ? 1.2824 1.5907 1.0747 0.4030  -0.0422 -0.1154 363 LEU D CG  
10599 C CD1 . LEU D 299 ? 1.5012 1.8195 1.3304 0.3782  -0.0263 -0.0971 363 LEU D CD1 
10600 C CD2 . LEU D 299 ? 0.9696 1.2486 0.7598 0.3904  -0.0663 -0.1367 363 LEU D CD2 
10601 N N   . GLY D 300 ? 1.3141 1.6422 1.0923 0.4123  -0.0008 -0.0675 364 GLY D N   
10602 C CA  . GLY D 300 ? 1.3121 1.6494 1.0730 0.4284  0.0138  -0.0519 364 GLY D CA  
10603 C C   . GLY D 300 ? 1.1464 1.4652 0.8979 0.4228  0.0039  -0.0569 364 GLY D C   
10604 O O   . GLY D 300 ? 0.9957 1.2962 0.7604 0.4022  -0.0120 -0.0700 364 GLY D O   
10605 N N   . THR D 301 ? 1.1351 1.4591 0.8627 0.4427  0.0133  -0.0464 365 THR D N   
10606 C CA  . THR D 301 ? 1.0819 1.3920 0.8021 0.4388  0.0079  -0.0467 365 THR D CA  
10607 C C   . THR D 301 ? 1.0440 1.3339 0.7493 0.4411  -0.0196 -0.0731 365 THR D C   
10608 O O   . THR D 301 ? 1.1789 1.4650 0.8693 0.4538  -0.0347 -0.0913 365 THR D O   
10609 C CB  . THR D 301 ? 1.1073 1.4271 0.8018 0.4628  0.0249  -0.0284 365 THR D CB  
10610 O OG1 . THR D 301 ? 1.4942 1.7999 1.1846 0.4570  0.0196  -0.0280 365 THR D OG1 
10611 C CG2 . THR D 301 ? 1.1785 1.5026 0.8314 0.4990  0.0189  -0.0385 365 THR D CG2 
10612 N N   . LEU D 302 ? 0.9986 1.2759 0.7103 0.4282  -0.0258 -0.0748 366 LEU D N   
10613 C CA  . LEU D 302 ? 0.9853 1.2459 0.6874 0.4293  -0.0499 -0.0975 366 LEU D CA  
10614 C C   . LEU D 302 ? 1.0868 1.3482 0.7518 0.4605  -0.0535 -0.1000 366 LEU D C   
10615 O O   . LEU D 302 ? 1.1359 1.3854 0.7881 0.4683  -0.0746 -0.1196 366 LEU D O   
10616 C CB  . LEU D 302 ? 1.0019 1.2511 0.7295 0.4019  -0.0534 -0.0970 366 LEU D CB  
10617 C CG  . LEU D 302 ? 1.1228 1.3691 0.8863 0.3704  -0.0493 -0.0928 366 LEU D CG  
10618 C CD1 . LEU D 302 ? 1.3248 1.5785 1.1055 0.3583  -0.0285 -0.0691 366 LEU D CD1 
10619 C CD2 . LEU D 302 ? 1.1508 1.3808 0.9288 0.3515  -0.0665 -0.1086 366 LEU D CD2 
10620 N N   . PHE D 303 ? 1.0854 1.3608 0.7337 0.4787  -0.0327 -0.0797 367 PHE D N   
10621 C CA  . PHE D 303 ? 1.1141 1.3899 0.7253 0.5088  -0.0327 -0.0780 367 PHE D CA  
10622 C C   . PHE D 303 ? 1.3134 1.5980 0.8883 0.5441  -0.0330 -0.0828 367 PHE D C   
10623 O O   . PHE D 303 ? 1.5153 1.8013 1.0541 0.5739  -0.0316 -0.0804 367 PHE D O   
10624 C CB  . PHE D 303 ? 1.0215 1.3033 0.6363 0.5055  -0.0091 -0.0507 367 PHE D CB  
10625 C CG  . PHE D 303 ? 1.0719 1.3444 0.7204 0.4730  -0.0096 -0.0469 367 PHE D CG  
10626 C CD1 . PHE D 303 ? 1.0756 1.3327 0.7274 0.4644  -0.0311 -0.0658 367 PHE D CD1 
10627 C CD2 . PHE D 303 ? 1.1613 1.4404 0.8396 0.4511  0.0106  -0.0251 367 PHE D CD2 
10628 C CE1 . PHE D 303 ? 1.0252 1.2742 0.7072 0.4355  -0.0312 -0.0625 367 PHE D CE1 
10629 C CE2 . PHE D 303 ? 1.2759 1.5449 0.9838 0.4221  0.0091  -0.0225 367 PHE D CE2 
10630 C CZ  . PHE D 303 ? 1.0963 1.3505 0.8049 0.4148  -0.0114 -0.0411 367 PHE D CZ  
10631 N N   . SER D 304 ? 1.3846 1.6747 0.9677 0.5420  -0.0354 -0.0900 368 SER D N   
10632 C CA  . SER D 304 ? 1.7007 1.9963 1.2503 0.5749  -0.0419 -0.1010 368 SER D CA  
10633 C C   . SER D 304 ? 1.5908 1.8686 1.1379 0.5742  -0.0740 -0.1329 368 SER D C   
10634 O O   . SER D 304 ? 1.5051 1.7736 1.0839 0.5453  -0.0840 -0.1420 368 SER D O   
10635 C CB  . SER D 304 ? 1.7723 2.0872 1.3313 0.5763  -0.0224 -0.0873 368 SER D CB  
10636 O OG  . SER D 304 ? 1.4629 1.7858 0.9855 0.6124  -0.0245 -0.0943 368 SER D OG  
10637 N N   . VAL D 305 ? 1.4386 1.7110 0.9480 0.6067  -0.0904 -0.1495 369 VAL D N   
10638 C CA  . VAL D 305 ? 1.3295 1.5849 0.8350 0.6097  -0.1218 -0.1801 369 VAL D CA  
10639 C C   . VAL D 305 ? 1.4425 1.7014 0.9532 0.6098  -0.1232 -0.1863 369 VAL D C   
10640 O O   . VAL D 305 ? 1.3419 1.5855 0.8578 0.6053  -0.1471 -0.2094 369 VAL D O   
10641 C CB  . VAL D 305 ? 1.4255 1.6746 0.8874 0.6477  -0.1390 -0.1957 369 VAL D CB  
10642 C CG1 . VAL D 305 ? 1.7476 2.0113 1.1699 0.6859  -0.1260 -0.1878 369 VAL D CG1 
10643 C CG2 . VAL D 305 ? 1.5274 1.7568 0.9909 0.6477  -0.1738 -0.2280 369 VAL D CG2 
10644 N N   . GLN D 306 ? 1.6451 1.9242 1.1564 0.6144  -0.0970 -0.1648 370 GLN D N   
10645 C CA  . GLN D 306 ? 1.8035 2.0911 1.3169 0.6193  -0.0939 -0.1670 370 GLN D CA  
10646 C C   . GLN D 306 ? 1.6784 1.9594 1.2332 0.5828  -0.0973 -0.1698 370 GLN D C   
10647 O O   . GLN D 306 ? 1.9146 2.1939 1.4714 0.5847  -0.1049 -0.1802 370 GLN D O   
10648 C CB  . GLN D 306 ? 1.9361 2.2510 1.4424 0.6339  -0.0619 -0.1402 370 GLN D CB  
10649 C CG  . GLN D 306 ? 2.0252 2.3498 1.4833 0.6783  -0.0565 -0.1379 370 GLN D CG  
10650 C CD  . GLN D 306 ? 2.2522 2.5764 1.6846 0.7057  -0.0710 -0.1573 370 GLN D CD  
10651 O OE1 . GLN D 306 ? 2.4104 2.7139 1.8278 0.7143  -0.1009 -0.1846 370 GLN D OE1 
10652 N NE2 . GLN D 306 ? 2.6360 2.9832 2.0648 0.7196  -0.0503 -0.1434 370 GLN D NE2 
10653 N N   . THR D 307 ? 1.5976 1.8740 1.1835 0.5511  -0.0918 -0.1604 371 THR D N   
10654 C CA  . THR D 307 ? 1.4844 1.7603 1.1094 0.5176  -0.0858 -0.1543 371 THR D CA  
10655 C C   . THR D 307 ? 1.3164 1.5693 0.9570 0.4979  -0.1104 -0.1764 371 THR D C   
10656 O O   . THR D 307 ? 1.4499 1.6856 1.0831 0.4992  -0.1312 -0.1940 371 THR D O   
10657 C CB  . THR D 307 ? 1.2536 1.5365 0.9043 0.4942  -0.0662 -0.1319 371 THR D CB  
10658 O OG1 . THR D 307 ? 1.3689 1.6394 1.0133 0.4921  -0.0757 -0.1370 371 THR D OG1 
10659 C CG2 . THR D 307 ? 1.1197 1.4271 0.7623 0.5101  -0.0381 -0.1066 371 THR D CG2 
10660 N N   . VAL D 308 ? 1.2875 1.5410 0.9516 0.4794  -0.1070 -0.1744 372 VAL D N   
10661 C CA  . VAL D 308 ? 1.4093 1.6431 1.0807 0.4691  -0.1279 -0.1943 372 VAL D CA  
10662 C C   . VAL D 308 ? 1.4105 1.6318 1.1170 0.4319  -0.1290 -0.1921 372 VAL D C   
10663 O O   . VAL D 308 ? 1.1513 1.3835 0.8804 0.4146  -0.1114 -0.1750 372 VAL D O   
10664 C CB  . VAL D 308 ? 1.3436 1.5870 1.0083 0.4828  -0.1244 -0.1953 372 VAL D CB  
10665 C CG1 . VAL D 308 ? 1.2447 1.4655 0.9131 0.4751  -0.1468 -0.2160 372 VAL D CG1 
10666 C CG2 . VAL D 308 ? 1.3916 1.6504 1.0205 0.5216  -0.1201 -0.1952 372 VAL D CG2 
10667 N N   . GLY D 309 ? 1.2904 1.4888 1.0018 0.4204  -0.1500 -0.2097 373 GLY D N   
10668 C CA  . GLY D 309 ? 1.1792 1.3633 0.9197 0.3884  -0.1528 -0.2102 373 GLY D CA  
10669 C C   . GLY D 309 ? 1.2923 1.4774 1.0407 0.3833  -0.1489 -0.2081 373 GLY D C   
10670 O O   . GLY D 309 ? 1.7405 1.9272 1.4712 0.4034  -0.1550 -0.2164 373 GLY D O   
10671 N N   . ASN D 310 ? 1.1698 1.3542 0.9438 0.3581  -0.1394 -0.1977 374 ASN D N   
10672 C CA  . ASN D 310 ? 1.1518 1.3383 0.9348 0.3532  -0.1355 -0.1951 374 ASN D CA  
10673 C C   . ASN D 310 ? 1.1642 1.3283 0.9653 0.3273  -0.1442 -0.2006 374 ASN D C   
10674 O O   . ASN D 310 ? 1.6949 1.8425 1.4909 0.3281  -0.1577 -0.2131 374 ASN D O   
10675 C CB  . ASN D 310 ? 1.2477 1.4598 1.0439 0.3519  -0.1125 -0.1744 374 ASN D CB  
10676 C CG  . ASN D 310 ? 1.1594 1.3754 0.9695 0.3453  -0.1087 -0.1717 374 ASN D CG  
10677 O OD1 . ASN D 310 ? 1.2088 1.4199 1.0414 0.3228  -0.1049 -0.1657 374 ASN D OD1 
10678 N ND2 . ASN D 310 ? 1.3426 1.5673 1.1383 0.3663  -0.1106 -0.1770 374 ASN D ND2 
10679 N N   . ARG D 311 ? 0.9761 1.1387 0.7969 0.3054  -0.1365 -0.1911 375 ARG D N   
10680 C CA  . ARG D 311 ? 0.9427 1.0870 0.7807 0.2812  -0.1406 -0.1927 375 ARG D CA  
10681 C C   . ARG D 311 ? 0.8960 1.0293 0.7447 0.2638  -0.1429 -0.1929 375 ARG D C   
10682 O O   . ARG D 311 ? 0.8499 0.9953 0.7042 0.2614  -0.1328 -0.1829 375 ARG D O   
10683 C CB  . ARG D 311 ? 0.8232 0.9788 0.6784 0.2707  -0.1265 -0.1790 375 ARG D CB  
10684 C CG  . ARG D 311 ? 0.8167 0.9533 0.6867 0.2477  -0.1299 -0.1798 375 ARG D CG  
10685 C CD  . ARG D 311 ? 0.9677 1.0848 0.8276 0.2509  -0.1443 -0.1933 375 ARG D CD  
10686 N NE  . ARG D 311 ? 0.8363 0.9330 0.7059 0.2317  -0.1478 -0.1940 375 ARG D NE  
10687 C CZ  . ARG D 311 ? 0.8566 0.9554 0.7350 0.2260  -0.1428 -0.1884 375 ARG D CZ  
10688 N NH1 . ARG D 311 ? 0.9580 1.0806 0.8416 0.2360  -0.1333 -0.1810 375 ARG D NH1 
10689 N NH2 . ARG D 311 ? 0.8631 0.9407 0.7459 0.2106  -0.1470 -0.1900 375 ARG D NH2 
10690 N N   . ASN D 312 ? 0.9103 1.0206 0.7625 0.2518  -0.1559 -0.2038 376 ASN D N   
10691 C CA  . ASN D 312 ? 0.9933 1.0937 0.8582 0.2346  -0.1580 -0.2046 376 ASN D CA  
10692 C C   . ASN D 312 ? 0.8730 0.9598 0.7535 0.2120  -0.1545 -0.1999 376 ASN D C   
10693 O O   . ASN D 312 ? 0.8953 0.9645 0.7740 0.2075  -0.1624 -0.2064 376 ASN D O   
10694 C CB  . ASN D 312 ? 1.2259 1.3116 1.0850 0.2389  -0.1757 -0.2208 376 ASN D CB  
10695 C CG  . ASN D 312 ? 1.2403 1.3141 1.1171 0.2185  -0.1785 -0.2224 376 ASN D CG  
10696 O OD1 . ASN D 312 ? 1.3036 1.3591 1.1896 0.2030  -0.1823 -0.2249 376 ASN D OD1 
10697 N ND2 . ASN D 312 ? 1.0982 1.1826 0.9795 0.2191  -0.1760 -0.2205 376 ASN D ND2 
10698 N N   . TYR D 313 ? 0.7726 0.8663 0.6665 0.1992  -0.1431 -0.1887 377 TYR D N   
10699 C CA  . TYR D 313 ? 0.7283 0.8100 0.6352 0.1793  -0.1390 -0.1837 377 TYR D CA  
10700 C C   . TYR D 313 ? 0.8055 0.8775 0.7217 0.1664  -0.1421 -0.1868 377 TYR D C   
10701 O O   . TYR D 313 ? 0.8856 0.9686 0.8071 0.1657  -0.1371 -0.1826 377 TYR D O   
10702 C CB  . TYR D 313 ? 0.6884 0.7842 0.6053 0.1740  -0.1247 -0.1695 377 TYR D CB  
10703 C CG  . TYR D 313 ? 0.7149 0.8218 0.6303 0.1825  -0.1196 -0.1644 377 TYR D CG  
10704 C CD1 . TYR D 313 ? 0.7302 0.8595 0.6440 0.1958  -0.1110 -0.1568 377 TYR D CD1 
10705 C CD2 . TYR D 313 ? 0.6457 0.7414 0.5618 0.1778  -0.1228 -0.1665 377 TYR D CD2 
10706 C CE1 . TYR D 313 ? 0.7791 0.9215 0.6952 0.2034  -0.1053 -0.1515 377 TYR D CE1 
10707 C CE2 . TYR D 313 ? 0.7727 0.8808 0.6903 0.1859  -0.1187 -0.1625 377 TYR D CE2 
10708 C CZ  . TYR D 313 ? 0.7582 0.8908 0.6774 0.1983  -0.1096 -0.1549 377 TYR D CZ  
10709 O OH  . TYR D 313 ? 0.8331 0.9809 0.7577 0.2059  -0.1043 -0.1502 377 TYR D OH  
10710 N N   . GLN D 314 ? 0.8430 0.8944 0.7618 0.1561  -0.1496 -0.1935 378 GLN D N   
10711 C CA  . GLN D 314 ? 0.8177 0.8614 0.7490 0.1423  -0.1507 -0.1952 378 GLN D CA  
10712 C C   . GLN D 314 ? 0.7479 0.7871 0.6877 0.1273  -0.1402 -0.1852 378 GLN D C   
10713 O O   . GLN D 314 ? 0.8161 0.8381 0.7551 0.1188  -0.1412 -0.1853 378 GLN D O   
10714 C CB  . GLN D 314 ? 0.9756 0.9994 0.9080 0.1382  -0.1632 -0.2062 378 GLN D CB  
10715 C CG  . GLN D 314 ? 1.1232 1.1501 1.0495 0.1527  -0.1763 -0.2184 378 GLN D CG  
10716 C CD  . GLN D 314 ? 1.4037 1.4128 1.3400 0.1446  -0.1887 -0.2292 378 GLN D CD  
10717 O OE1 . GLN D 314 ? 1.8106 1.8065 1.7601 0.1258  -0.1837 -0.2245 378 GLN D OE1 
10718 N NE2 . GLN D 314 ? 1.2965 1.3035 1.2292 0.1554  -0.2026 -0.2415 378 GLN D NE2 
10719 N N   . LEU D 315 ? 0.7322 0.7857 0.6784 0.1252  -0.1307 -0.1768 379 LEU D N   
10720 C CA  . LEU D 315 ? 0.7760 0.8265 0.7288 0.1134  -0.1212 -0.1675 379 LEU D CA  
10721 C C   . LEU D 315 ? 0.8587 0.8960 0.8198 0.0990  -0.1201 -0.1680 379 LEU D C   
10722 O O   . LEU D 315 ? 1.0693 1.0938 1.0293 0.0907  -0.1164 -0.1641 379 LEU D O   
10723 C CB  . LEU D 315 ? 0.7846 0.8527 0.7423 0.1160  -0.1121 -0.1584 379 LEU D CB  
10724 C CG  . LEU D 315 ? 0.8027 0.8855 0.7552 0.1283  -0.1087 -0.1535 379 LEU D CG  
10725 C CD1 . LEU D 315 ? 0.7339 0.8309 0.6937 0.1283  -0.0990 -0.1429 379 LEU D CD1 
10726 C CD2 . LEU D 315 ? 0.6657 0.7426 0.6154 0.1283  -0.1090 -0.1523 379 LEU D CD2 
10727 N N   . LEU D 316 ? 0.7960 0.8368 0.7654 0.0970  -0.1232 -0.1728 380 LEU D N   
10728 C CA  . LEU D 316 ? 0.7523 0.7839 0.7328 0.0835  -0.1208 -0.1727 380 LEU D CA  
10729 C C   . LEU D 316 ? 0.8021 0.8263 0.7892 0.0819  -0.1308 -0.1827 380 LEU D C   
10730 O O   . LEU D 316 ? 0.7289 0.7622 0.7160 0.0916  -0.1392 -0.1903 380 LEU D O   
10731 C CB  . LEU D 316 ? 0.6218 0.6672 0.6121 0.0807  -0.1139 -0.1682 380 LEU D CB  
10732 C CG  . LEU D 316 ? 0.6015 0.6539 0.5885 0.0817  -0.1049 -0.1584 380 LEU D CG  
10733 C CD1 . LEU D 316 ? 0.7569 0.8163 0.7541 0.0760  -0.0986 -0.1548 380 LEU D CD1 
10734 C CD2 . LEU D 316 ? 0.4748 0.5140 0.4550 0.0770  -0.1015 -0.1538 380 LEU D CD2 
10735 N N   . SER D 317 ? 0.7986 0.8057 0.7913 0.0701  -0.1301 -0.1826 381 SER D N   
10736 C CA  . SER D 317 ? 0.8260 0.8240 0.8299 0.0657  -0.1395 -0.1914 381 SER D CA  
10737 C C   . SER D 317 ? 0.9128 0.9098 0.9367 0.0516  -0.1338 -0.1890 381 SER D C   
10738 O O   . SER D 317 ? 1.4174 1.4220 1.4587 0.0497  -0.1400 -0.1962 381 SER D O   
10739 C CB  . SER D 317 ? 0.9083 0.8840 0.9021 0.0650  -0.1453 -0.1939 381 SER D CB  
10740 O OG  . SER D 317 ? 1.1780 1.1562 1.1541 0.0787  -0.1499 -0.1959 381 SER D OG  
10741 N N   . ASN D 318 ? 0.9116 0.8996 0.9332 0.0424  -0.1221 -0.1794 382 ASN D N   
10742 C CA  . ASN D 318 ? 1.1476 1.1345 1.1872 0.0294  -0.1142 -0.1754 382 ASN D CA  
10743 C C   . ASN D 318 ? 1.0623 1.0701 1.1142 0.0282  -0.1067 -0.1726 382 ASN D C   
10744 O O   . ASN D 318 ? 1.3493 1.3588 1.4171 0.0183  -0.0990 -0.1691 382 ASN D O   
10745 C CB  . ASN D 318 ? 1.3877 1.3542 1.4171 0.0218  -0.1046 -0.1661 382 ASN D CB  
10746 C CG  . ASN D 318 ? 1.6930 1.6394 1.7301 0.0129  -0.1078 -0.1674 382 ASN D CG  
10747 O OD1 . ASN D 318 ? 1.9075 1.8571 1.9642 0.0094  -0.1160 -0.1750 382 ASN D OD1 
10748 N ND2 . ASN D 318 ? 1.9564 1.8812 1.9788 0.0094  -0.1017 -0.1600 382 ASN D ND2 
10749 N N   . SER D 319 ? 0.8346 0.8581 0.8799 0.0386  -0.1085 -0.1738 383 SER D N   
10750 C CA  . SER D 319 ? 0.9555 0.9953 1.0080 0.0384  -0.1008 -0.1698 383 SER D CA  
10751 C C   . SER D 319 ? 0.8065 0.8654 0.8724 0.0445  -0.1083 -0.1778 383 SER D C   
10752 O O   . SER D 319 ? 0.8223 0.8856 0.8818 0.0549  -0.1183 -0.1844 383 SER D O   
10753 C CB  . SER D 319 ? 0.8640 0.9050 0.8990 0.0442  -0.0944 -0.1621 383 SER D CB  
10754 O OG  . SER D 319 ? 1.0690 1.0933 1.0885 0.0440  -0.0939 -0.1589 383 SER D OG  
10755 N N   . THR D 320 ? 0.7409 0.8111 0.8241 0.0393  -0.1035 -0.1773 384 THR D N   
10756 C CA  . THR D 320 ? 0.7890 0.8779 0.8832 0.0465  -0.1102 -0.1845 384 THR D CA  
10757 C C   . THR D 320 ? 0.7408 0.8392 0.8189 0.0581  -0.1078 -0.1802 384 THR D C   
10758 O O   . THR D 320 ? 0.6655 0.7659 0.7402 0.0562  -0.0978 -0.1721 384 THR D O   
10759 C CB  . THR D 320 ? 0.6774 0.7775 0.7975 0.0379  -0.1058 -0.1857 384 THR D CB  
10760 O OG1 . THR D 320 ? 0.9439 1.0354 1.0821 0.0263  -0.1073 -0.1885 384 THR D OG1 
10761 C CG2 . THR D 320 ? 0.6184 0.7370 0.7494 0.0467  -0.1151 -0.1947 384 THR D CG2 
10762 N N   . ILE D 321 ? 0.6168 0.7202 0.6852 0.0706  -0.1172 -0.1856 385 ILE D N   
10763 C CA  . ILE D 321 ? 0.5718 0.6827 0.6238 0.0827  -0.1151 -0.1806 385 ILE D CA  
10764 C C   . ILE D 321 ? 0.7602 0.8871 0.8175 0.0916  -0.1188 -0.1844 385 ILE D C   
10765 O O   . ILE D 321 ? 1.0801 1.2143 1.1537 0.0911  -0.1266 -0.1941 385 ILE D O   
10766 C CB  . ILE D 321 ? 0.5105 0.6175 0.5453 0.0935  -0.1215 -0.1827 385 ILE D CB  
10767 C CG1 . ILE D 321 ? 0.5384 0.6293 0.5688 0.0861  -0.1206 -0.1813 385 ILE D CG1 
10768 C CG2 . ILE D 321 ? 0.4187 0.5323 0.4379 0.1041  -0.1162 -0.1744 385 ILE D CG2 
10769 C CD1 . ILE D 321 ? 0.5867 0.6707 0.6105 0.0797  -0.1094 -0.1703 385 ILE D CD1 
10770 N N   . GLY D 322 ? 0.6505 0.7822 0.6947 0.0998  -0.1135 -0.1767 386 GLY D N   
10771 C CA  . GLY D 322 ? 0.7227 0.8670 0.7665 0.1103  -0.1159 -0.1781 386 GLY D CA  
10772 C C   . GLY D 322 ? 0.6705 0.8163 0.6942 0.1229  -0.1128 -0.1701 386 GLY D C   
10773 O O   . GLY D 322 ? 0.6597 0.8040 0.6705 0.1317  -0.1166 -0.1711 386 GLY D O   
10774 N N   . ARG D 323 ? 0.6664 0.8150 0.6876 0.1243  -0.1054 -0.1615 387 ARG D N   
10775 C CA  . ARG D 323 ? 0.7040 0.8538 0.7085 0.1353  -0.1008 -0.1517 387 ARG D CA  
10776 C C   . ARG D 323 ? 0.5773 0.7193 0.5752 0.1309  -0.0942 -0.1430 387 ARG D C   
10777 O O   . ARG D 323 ? 0.6459 0.7796 0.6504 0.1186  -0.0913 -0.1424 387 ARG D O   
10778 C CB  . ARG D 323 ? 0.6246 0.7769 0.6290 0.1375  -0.0953 -0.1443 387 ARG D CB  
10779 C CG  . ARG D 323 ? 0.6302 0.7908 0.6441 0.1405  -0.1014 -0.1531 387 ARG D CG  
10780 C CD  . ARG D 323 ? 0.7019 0.8615 0.7199 0.1372  -0.0950 -0.1467 387 ARG D CD  
10781 N NE  . ARG D 323 ? 0.8988 1.0543 0.9026 0.1447  -0.0892 -0.1344 387 ARG D NE  
10782 C CZ  . ARG D 323 ? 0.7715 0.9179 0.7747 0.1374  -0.0810 -0.1239 387 ARG D CZ  
10783 N NH1 . ARG D 323 ? 0.6569 0.7970 0.6696 0.1241  -0.0782 -0.1249 387 ARG D NH1 
10784 N NH2 . ARG D 323 ? 0.7057 0.8486 0.6991 0.1438  -0.0760 -0.1123 387 ARG D NH2 
10785 N N   . SER D 324 ? 0.4725 0.6176 0.4570 0.1421  -0.0917 -0.1364 388 SER D N   
10786 C CA  . SER D 324 ? 0.5083 0.6496 0.4885 0.1399  -0.0853 -0.1278 388 SER D CA  
10787 C C   . SER D 324 ? 0.4685 0.6150 0.4406 0.1496  -0.0779 -0.1154 388 SER D C   
10788 O O   . SER D 324 ? 0.4991 0.6518 0.4626 0.1619  -0.0799 -0.1159 388 SER D O   
10789 C CB  . SER D 324 ? 0.5891 0.7306 0.5618 0.1458  -0.0911 -0.1346 388 SER D CB  
10790 O OG  . SER D 324 ? 0.7168 0.8638 0.6828 0.1579  -0.1010 -0.1453 388 SER D OG  
10791 N N   . GLY D 325 ? 0.3902 0.5339 0.3655 0.1445  -0.0696 -0.1041 389 GLY D N   
10792 C CA  . GLY D 325 ? 0.4147 0.5635 0.3843 0.1533  -0.0617 -0.0911 389 GLY D CA  
10793 C C   . GLY D 325 ? 0.4502 0.5982 0.4267 0.1478  -0.0537 -0.0800 389 GLY D C   
10794 O O   . GLY D 325 ? 0.5251 0.6669 0.5110 0.1362  -0.0551 -0.0830 389 GLY D O   
10795 N N   . LEU D 326 ? 0.4530 0.6073 0.4260 0.1561  -0.0450 -0.0668 390 LEU D N   
10796 C CA  . LEU D 326 ? 0.5138 0.6702 0.4978 0.1509  -0.0372 -0.0560 390 LEU D CA  
10797 C C   . LEU D 326 ? 0.6365 0.7854 0.6353 0.1404  -0.0324 -0.0459 390 LEU D C   
10798 O O   . LEU D 326 ? 0.8602 1.0032 0.8571 0.1403  -0.0333 -0.0448 390 LEU D O   
10799 C CB  . LEU D 326 ? 0.5352 0.7039 0.5103 0.1652  -0.0287 -0.0458 390 LEU D CB  
10800 C CG  . LEU D 326 ? 0.5758 0.7523 0.5339 0.1791  -0.0334 -0.0550 390 LEU D CG  
10801 C CD1 . LEU D 326 ? 0.7784 0.9648 0.7204 0.1977  -0.0255 -0.0449 390 LEU D CD1 
10802 C CD2 . LEU D 326 ? 0.5436 0.7237 0.5088 0.1753  -0.0329 -0.0565 390 LEU D CD2 
10803 N N   . TYR D 327 ? 0.7495 0.8984 0.7637 0.1320  -0.0286 -0.0397 391 TYR D N   
10804 C CA  . TYR D 327 ? 0.6771 0.8200 0.7082 0.1233  -0.0240 -0.0284 391 TYR D CA  
10805 C C   . TYR D 327 ? 0.6475 0.7972 0.6962 0.1189  -0.0183 -0.0198 391 TYR D C   
10806 O O   . TYR D 327 ? 0.8071 0.9613 0.8574 0.1178  -0.0213 -0.0264 391 TYR D O   
10807 C CB  . TYR D 327 ? 0.6232 0.7513 0.6606 0.1117  -0.0317 -0.0363 391 TYR D CB  
10808 C CG  . TYR D 327 ? 0.6793 0.8018 0.7225 0.1026  -0.0384 -0.0464 391 TYR D CG  
10809 C CD1 . TYR D 327 ? 0.7523 0.8701 0.8130 0.0936  -0.0391 -0.0430 391 TYR D CD1 
10810 C CD2 . TYR D 327 ? 0.7505 0.8711 0.7824 0.1032  -0.0447 -0.0595 391 TYR D CD2 
10811 C CE1 . TYR D 327 ? 0.6275 0.7386 0.6905 0.0871  -0.0459 -0.0525 391 TYR D CE1 
10812 C CE2 . TYR D 327 ? 0.8176 0.9308 0.8522 0.0957  -0.0502 -0.0676 391 TYR D CE2 
10813 C CZ  . TYR D 327 ? 0.7035 0.8118 0.7518 0.0885  -0.0508 -0.0643 391 TYR D CZ  
10814 O OH  . TYR D 327 ? 0.5784 0.6781 0.6257 0.0831  -0.0569 -0.0730 391 TYR D OH  
10815 N N   . GLN D 328 ? 0.6864 0.8369 0.7496 0.1164  -0.0103 -0.0048 392 GLN D N   
10816 C CA  . GLN D 328 ? 0.7128 0.8707 0.7989 0.1105  -0.0052 0.0038  392 GLN D CA  
10817 C C   . GLN D 328 ? 0.8507 0.9953 0.9593 0.0960  -0.0103 0.0047  392 GLN D C   
10818 O O   . GLN D 328 ? 1.2116 1.3462 1.3252 0.0929  -0.0091 0.0120  392 GLN D O   
10819 C CB  . GLN D 328 ? 0.7340 0.9055 0.8240 0.1188  0.0094  0.0219  392 GLN D CB  
10820 C CG  . GLN D 328 ? 0.7991 0.9828 0.8641 0.1360  0.0143  0.0215  392 GLN D CG  
10821 C CD  . GLN D 328 ? 0.9313 1.1278 0.9977 0.1459  0.0305  0.0413  392 GLN D CD  
10822 O OE1 . GLN D 328 ? 1.1196 1.3106 1.1818 0.1492  0.0372  0.0534  392 GLN D OE1 
10823 N NE2 . GLN D 328 ? 0.9907 1.2044 1.0621 0.1516  0.0376  0.0453  392 GLN D NE2 
10824 N N   . PRO D 329 ? 0.7367 0.8797 0.8574 0.0883  -0.0175 -0.0037 393 PRO D N   
10825 C CA  . PRO D 329 ? 0.7242 0.8558 0.8677 0.0761  -0.0238 -0.0038 393 PRO D CA  
10826 C C   . PRO D 329 ? 0.8277 0.9698 0.9998 0.0725  -0.0150 0.0121  393 PRO D C   
10827 O O   . PRO D 329 ? 0.8460 1.0065 1.0205 0.0790  -0.0051 0.0198  393 PRO D O   
10828 C CB  . PRO D 329 ? 0.6686 0.7971 0.8111 0.0726  -0.0339 -0.0183 393 PRO D CB  
10829 C CG  . PRO D 329 ? 0.6343 0.7777 0.7629 0.0819  -0.0297 -0.0210 393 PRO D CG  
10830 C CD  . PRO D 329 ? 0.6197 0.7686 0.7298 0.0918  -0.0221 -0.0156 393 PRO D CD  
10831 N N   . ALA D 330 ? 1.0635 1.1942 1.2577 0.0628  -0.0183 0.0170  394 ALA D N   
10832 C CA  . ALA D 330 ? 1.1355 1.2750 1.3624 0.0573  -0.0101 0.0331  394 ALA D CA  
10833 C C   . ALA D 330 ? 1.4343 1.5685 1.6926 0.0453  -0.0210 0.0277  394 ALA D C   
10834 O O   . ALA D 330 ? 1.1768 1.2911 1.4370 0.0391  -0.0337 0.0187  394 ALA D O   
10835 C CB  . ALA D 330 ? 1.2621 1.3930 1.4912 0.0570  -0.0029 0.0477  394 ALA D CB  
10836 N N   . TYR D 331 ? 1.7633 1.9161 2.0454 0.0437  -0.0164 0.0323  395 TYR D N   
10837 C CA  . TYR D 331 ? 1.6080 1.7602 1.9264 0.0330  -0.0257 0.0292  395 TYR D CA  
10838 C C   . TYR D 331 ? 1.6949 1.8703 2.0486 0.0303  -0.0122 0.0463  395 TYR D C   
10839 O O   . TYR D 331 ? 1.5302 1.7217 1.8754 0.0384  0.0047  0.0598  395 TYR D O   
10840 C CB  . TYR D 331 ? 1.3921 1.5442 1.7029 0.0344  -0.0385 0.0106  395 TYR D CB  
10841 C CG  . TYR D 331 ? 1.6628 1.8021 1.9321 0.0413  -0.0449 -0.0037 395 TYR D CG  
10842 C CD1 . TYR D 331 ? 1.5325 1.6480 1.7880 0.0384  -0.0563 -0.0135 395 TYR D CD1 
10843 C CD2 . TYR D 331 ? 1.5280 1.6791 1.7729 0.0511  -0.0395 -0.0075 395 TYR D CD2 
10844 C CE1 . TYR D 331 ? 1.7045 1.8100 1.9251 0.0442  -0.0605 -0.0254 395 TYR D CE1 
10845 C CE2 . TYR D 331 ? 1.6205 1.7600 1.8314 0.0561  -0.0452 -0.0200 395 TYR D CE2 
10846 C CZ  . TYR D 331 ? 1.9190 2.0365 2.1189 0.0521  -0.0549 -0.0283 395 TYR D CZ  
10847 O OH  . TYR D 331 ? 1.8753 1.9830 2.0448 0.0565  -0.0591 -0.0394 395 TYR D OH  
10848 N N   . GLU D 332 ? 2.0802 2.2577 2.4739 0.0198  -0.0196 0.0456  396 GLU D N   
10849 C CA  . GLU D 332 ? 2.2026 2.4056 2.6352 0.0166  -0.0077 0.0599  396 GLU D CA  
10850 C C   . GLU D 332 ? 2.4837 2.7099 2.9009 0.0280  -0.0010 0.0560  396 GLU D C   
10851 O O   . GLU D 332 ? 2.8839 3.1321 3.3042 0.0347  0.0174  0.0712  396 GLU D O   
10852 C CB  . GLU D 332 ? 2.1503 2.3511 2.6297 0.0034  -0.0212 0.0552  396 GLU D CB  
10853 C CG  . GLU D 332 ? 2.0691 2.2971 2.5983 -0.0026 -0.0087 0.0717  396 GLU D CG  
10854 C CD  . GLU D 332 ? 2.0421 2.2973 2.5755 0.0048  -0.0055 0.0663  396 GLU D CD  
10855 O OE1 . GLU D 332 ? 2.1038 2.3536 2.6287 0.0066  -0.0226 0.0461  396 GLU D OE1 
10856 O OE2 . GLU D 332 ? 1.9858 2.2674 2.5296 0.0098  0.0143  0.0825  396 GLU D OE2 
10857 N N   . SER D 333 ? 2.1791 2.3986 2.5773 0.0314  -0.0158 0.0357  397 SER D N   
10858 C CA  . SER D 333 ? 1.7829 2.0198 2.1648 0.0422  -0.0133 0.0287  397 SER D CA  
10859 C C   . SER D 333 ? 1.9280 2.1966 2.3413 0.0444  0.0021  0.0433  397 SER D C   
10860 O O   . SER D 333 ? 2.1496 2.4288 2.6050 0.0361  -0.0018 0.0443  397 SER D O   
10861 C CB  . SER D 333 ? 1.6381 1.8697 1.9712 0.0545  -0.0083 0.0253  397 SER D CB  
10862 O OG  . SER D 333 ? 1.8524 2.0577 2.1589 0.0526  -0.0221 0.0110  397 SER D OG  
10863 N N   . ARG D 334 ? 1.8347 2.1188 2.2280 0.0564  0.0193  0.0543  398 ARG D N   
10864 C CA  . ARG D 334 ? 1.9626 2.2777 2.3825 0.0604  0.0380  0.0718  398 ARG D CA  
10865 C C   . ARG D 334 ? 1.9067 2.2293 2.3002 0.0727  0.0577  0.0878  398 ARG D C   
10866 O O   . ARG D 334 ? 1.9885 2.2912 2.3497 0.0756  0.0559  0.0864  398 ARG D O   
10867 C CB  . ARG D 334 ? 2.1462 2.4826 2.5729 0.0676  0.0352  0.0622  398 ARG D CB  
10868 C CG  . ARG D 334 ? 2.1901 2.5185 2.5700 0.0806  0.0264  0.0444  398 ARG D CG  
10869 C CD  . ARG D 334 ? 2.5909 2.9429 2.9791 0.0896  0.0266  0.0383  398 ARG D CD  
10870 N NE  . ARG D 334 ? 2.8892 3.2517 3.3249 0.0789  0.0192  0.0361  398 ARG D NE  
10871 C CZ  . ARG D 334 ? 2.9009 3.2843 3.3531 0.0845  0.0169  0.0299  398 ARG D CZ  
10872 N NH1 . ARG D 334 ? 3.1109 3.5058 3.5345 0.1010  0.0214  0.0252  398 ARG D NH1 
10873 N NH2 . ARG D 334 ? 3.0542 3.4464 3.5520 0.0742  0.0087  0.0272  398 ARG D NH2 
10874 N N   . ASP D 335 ? 2.0549 2.4066 2.4618 0.0812  0.0762  0.1027  399 ASP D N   
10875 C CA  . ASP D 335 ? 2.3994 2.7610 2.7806 0.0961  0.0964  0.1192  399 ASP D CA  
10876 C C   . ASP D 335 ? 2.2685 2.6138 2.5939 0.1095  0.0892  0.1058  399 ASP D C   
10877 O O   . ASP D 335 ? 2.6153 2.9572 2.9130 0.1200  0.0998  0.1156  399 ASP D O   
10878 C CB  . ASP D 335 ? 2.6306 3.0273 3.0250 0.1080  0.1138  0.1302  399 ASP D CB  
10879 C CG  . ASP D 335 ? 2.9159 3.3333 3.3692 0.0955  0.1258  0.1482  399 ASP D CG  
10880 O OD1 . ASP D 335 ? 3.1822 3.5856 3.6638 0.0789  0.1236  0.1561  399 ASP D OD1 
10881 O OD2 . ASP D 335 ? 3.1664 3.6146 3.6394 0.1027  0.1374  0.1544  399 ASP D OD2 
10882 N N   . CYS D 336 ? 1.8010 2.1357 2.1117 0.1088  0.0706  0.0832  400 CYS D N   
10883 C CA  . CYS D 336 ? 1.5633 1.8826 1.8272 0.1191  0.0609  0.0676  400 CYS D CA  
10884 C C   . CYS D 336 ? 1.3486 1.6394 1.5949 0.1119  0.0519  0.0631  400 CYS D C   
10885 O O   . CYS D 336 ? 1.5768 1.8515 1.8407 0.0970  0.0403  0.0572  400 CYS D O   
10886 C CB  . CYS D 336 ? 1.6630 1.9801 1.9232 0.1187  0.0448  0.0470  400 CYS D CB  
10887 S SG  . CYS D 336 ? 2.3819 2.6985 2.5947 0.1379  0.0408  0.0332  400 CYS D SG  
10888 N N   . GLN D 337 ? 0.9305 1.2155 1.1416 0.1237  0.0564  0.0649  401 GLN D N   
10889 C CA  . GLN D 337 ? 0.8405 1.1005 1.0309 0.1196  0.0466  0.0575  401 GLN D CA  
10890 C C   . GLN D 337 ? 0.8214 1.0692 0.9826 0.1234  0.0312  0.0356  401 GLN D C   
10891 O O   . GLN D 337 ? 0.8533 1.1068 0.9869 0.1379  0.0322  0.0304  401 GLN D O   
10892 C CB  . GLN D 337 ? 0.9076 1.1660 1.0784 0.1296  0.0586  0.0714  401 GLN D CB  
10893 C CG  . GLN D 337 ? 0.9097 1.1440 1.0618 0.1259  0.0489  0.0643  401 GLN D CG  
10894 C CD  . GLN D 337 ? 0.8337 1.0503 1.0078 0.1074  0.0363  0.0572  401 GLN D CD  
10895 O OE1 . GLN D 337 ? 1.0080 1.2244 1.2137 0.0964  0.0399  0.0681  401 GLN D OE1 
10896 N NE2 . GLN D 337 ? 0.7256 0.9271 0.8831 0.1047  0.0214  0.0388  401 GLN D NE2 
10897 N N   . GLU D 338 ? 0.8372 1.0669 1.0044 0.1107  0.0168  0.0233  402 GLU D N   
10898 C CA  . GLU D 338 ? 0.8283 1.0446 0.9712 0.1120  0.0030  0.0041  402 GLU D CA  
10899 C C   . GLU D 338 ? 0.8269 1.0333 0.9392 0.1194  0.0020  0.0005  402 GLU D C   
10900 O O   . GLU D 338 ? 0.9752 1.1766 1.0867 0.1188  0.0071  0.0098  402 GLU D O   
10901 C CB  . GLU D 338 ? 1.1002 1.2996 1.2566 0.0976  -0.0102 -0.0060 402 GLU D CB  
10902 C CG  . GLU D 338 ? 1.4627 1.6483 1.5975 0.0979  -0.0234 -0.0245 402 GLU D CG  
10903 C CD  . GLU D 338 ? 1.8492 2.0390 1.9918 0.0973  -0.0300 -0.0330 402 GLU D CD  
10904 O OE1 . GLU D 338 ? 2.4104 2.6061 2.5810 0.0908  -0.0304 -0.0290 402 GLU D OE1 
10905 O OE2 . GLU D 338 ? 1.7426 1.9288 1.8641 0.1034  -0.0357 -0.0443 402 GLU D OE2 
10906 N N   . LEU D 339 ? 0.7461 0.9497 0.8347 0.1267  -0.0054 -0.0133 403 LEU D N   
10907 C CA  . LEU D 339 ? 0.6566 0.8522 0.7189 0.1337  -0.0090 -0.0197 403 LEU D CA  
10908 C C   . LEU D 339 ? 0.7034 0.8843 0.7538 0.1289  -0.0227 -0.0377 403 LEU D C   
10909 O O   . LEU D 339 ? 0.6888 0.8705 0.7356 0.1304  -0.0283 -0.0468 403 LEU D O   
10910 C CB  . LEU D 339 ? 0.6670 0.8766 0.7100 0.1518  -0.0024 -0.0167 403 LEU D CB  
10911 C CG  . LEU D 339 ? 0.7736 0.9764 0.7907 0.1609  -0.0072 -0.0239 403 LEU D CG  
10912 C CD1 . LEU D 339 ? 0.6712 0.8660 0.6907 0.1567  -0.0038 -0.0155 403 LEU D CD1 
10913 C CD2 . LEU D 339 ? 0.9509 1.1673 0.9481 0.1808  -0.0019 -0.0217 403 LEU D CD2 
10914 N N   . CYS D 340 ? 0.7137 0.8809 0.7583 0.1234  -0.0276 -0.0419 404 CYS D N   
10915 C CA  . CYS D 340 ? 0.6469 0.8000 0.6830 0.1174  -0.0384 -0.0565 404 CYS D CA  
10916 C C   . CYS D 340 ? 0.6092 0.7587 0.6294 0.1225  -0.0410 -0.0616 404 CYS D C   
10917 O O   . CYS D 340 ? 0.7032 0.8576 0.7196 0.1289  -0.0354 -0.0537 404 CYS D O   
10918 C CB  . CYS D 340 ? 0.7237 0.8632 0.7730 0.1039  -0.0425 -0.0576 404 CYS D CB  
10919 S SG  . CYS D 340 ? 0.9931 1.1346 1.0646 0.0968  -0.0429 -0.0539 404 CYS D SG  
10920 N N   . PHE D 341 ? 0.4863 0.6270 0.4979 0.1197  -0.0495 -0.0745 405 PHE D N   
10921 C CA  . PHE D 341 ? 0.5419 0.6802 0.5430 0.1233  -0.0530 -0.0805 405 PHE D CA  
10922 C C   . PHE D 341 ? 0.5373 0.6627 0.5399 0.1129  -0.0595 -0.0903 405 PHE D C   
10923 O O   . PHE D 341 ? 0.6626 0.7802 0.6679 0.1060  -0.0626 -0.0946 405 PHE D O   
10924 C CB  . PHE D 341 ? 0.5047 0.6514 0.4907 0.1370  -0.0558 -0.0863 405 PHE D CB  
10925 C CG  . PHE D 341 ? 0.5689 0.7114 0.5500 0.1366  -0.0634 -0.0978 405 PHE D CG  
10926 C CD1 . PHE D 341 ? 0.5205 0.6682 0.5006 0.1412  -0.0621 -0.0964 405 PHE D CD1 
10927 C CD2 . PHE D 341 ? 0.6301 0.7632 0.6087 0.1316  -0.0718 -0.1097 405 PHE D CD2 
10928 C CE1 . PHE D 341 ? 0.5577 0.6994 0.5320 0.1416  -0.0700 -0.1072 405 PHE D CE1 
10929 C CE2 . PHE D 341 ? 0.5495 0.6762 0.5239 0.1308  -0.0790 -0.1195 405 PHE D CE2 
10930 C CZ  . PHE D 341 ? 0.5831 0.7128 0.5541 0.1360  -0.0785 -0.1184 405 PHE D CZ  
10931 N N   . TRP D 342 ? 0.4877 0.6113 0.4879 0.1129  -0.0612 -0.0934 406 TRP D N   
10932 C CA  . TRP D 342 ? 0.4821 0.5959 0.4847 0.1041  -0.0654 -0.1014 406 TRP D CA  
10933 C C   . TRP D 342 ? 0.5081 0.6250 0.5055 0.1081  -0.0710 -0.1112 406 TRP D C   
10934 O O   . TRP D 342 ? 0.5834 0.7093 0.5742 0.1189  -0.0723 -0.1120 406 TRP D O   
10935 C CB  . TRP D 342 ? 0.4546 0.5640 0.4630 0.0996  -0.0627 -0.0968 406 TRP D CB  
10936 C CG  . TRP D 342 ? 0.4421 0.5593 0.4474 0.1083  -0.0605 -0.0923 406 TRP D CG  
10937 C CD1 . TRP D 342 ? 0.4509 0.5711 0.4574 0.1129  -0.0549 -0.0807 406 TRP D CD1 
10938 C CD2 . TRP D 342 ? 0.5192 0.6416 0.5200 0.1141  -0.0643 -0.0992 406 TRP D CD2 
10939 N NE1 . TRP D 342 ? 0.4395 0.5648 0.4393 0.1220  -0.0546 -0.0794 406 TRP D NE1 
10940 C CE2 . TRP D 342 ? 0.5069 0.6344 0.5032 0.1235  -0.0609 -0.0911 406 TRP D CE2 
10941 C CE3 . TRP D 342 ? 0.6489 0.7722 0.6505 0.1125  -0.0701 -0.1107 406 TRP D CE3 
10942 C CZ2 . TRP D 342 ? 0.5059 0.6391 0.4967 0.1322  -0.0645 -0.0958 406 TRP D CZ2 
10943 C CZ3 . TRP D 342 ? 0.6825 0.8133 0.6824 0.1201  -0.0738 -0.1156 406 TRP D CZ3 
10944 C CH2 . TRP D 342 ? 0.5382 0.6738 0.5318 0.1304  -0.0716 -0.1089 406 TRP D CH2 
10945 N N   . ILE D 343 ? 0.5417 0.6508 0.5424 0.0998  -0.0743 -0.1188 407 ILE D N   
10946 C CA  . ILE D 343 ? 0.5234 0.6345 0.5247 0.1008  -0.0804 -0.1289 407 ILE D CA  
10947 C C   . ILE D 343 ? 0.5725 0.6783 0.5821 0.0913  -0.0790 -0.1314 407 ILE D C   
10948 O O   . ILE D 343 ? 0.8157 0.9113 0.8264 0.0829  -0.0761 -0.1295 407 ILE D O   
10949 C CB  . ILE D 343 ? 0.5067 0.6120 0.5047 0.0996  -0.0856 -0.1357 407 ILE D CB  
10950 C CG1 . ILE D 343 ? 0.5690 0.6795 0.5578 0.1097  -0.0860 -0.1329 407 ILE D CG1 
10951 C CG2 . ILE D 343 ? 0.4377 0.5447 0.4398 0.1001  -0.0930 -0.1463 407 ILE D CG2 
10952 C CD1 . ILE D 343 ? 0.7448 0.8484 0.7289 0.1098  -0.0914 -0.1392 407 ILE D CD1 
10953 N N   . GLU D 344 ? 0.6993 0.8128 0.7142 0.0938  -0.0812 -0.1358 408 GLU D N   
10954 C CA  . GLU D 344 ? 0.5402 0.6523 0.5646 0.0863  -0.0789 -0.1380 408 GLU D CA  
10955 C C   . GLU D 344 ? 0.5499 0.6598 0.5824 0.0798  -0.0826 -0.1463 408 GLU D C   
10956 O O   . GLU D 344 ? 0.8962 1.0099 0.9298 0.0839  -0.0899 -0.1533 408 GLU D O   
10957 C CB  . GLU D 344 ? 0.4800 0.6030 0.5076 0.0934  -0.0798 -0.1385 408 GLU D CB  
10958 C CG  . GLU D 344 ? 0.5930 0.7176 0.6299 0.0885  -0.0765 -0.1395 408 GLU D CG  
10959 C CD  . GLU D 344 ? 1.0480 1.1847 1.0879 0.0977  -0.0796 -0.1422 408 GLU D CD  
10960 O OE1 . GLU D 344 ? 0.7820 0.9182 0.8211 0.0993  -0.0759 -0.1376 408 GLU D OE1 
10961 O OE2 . GLU D 344 ? 1.1988 1.3443 1.2406 0.1044  -0.0869 -0.1494 408 GLU D OE2 
10962 N N   . ILE D 345 ? 0.4977 0.6003 0.5356 0.0702  -0.0776 -0.1453 409 ILE D N   
10963 C CA  . ILE D 345 ? 0.5577 0.6555 0.6040 0.0623  -0.0790 -0.1506 409 ILE D CA  
10964 C C   . ILE D 345 ? 0.5515 0.6545 0.6125 0.0559  -0.0740 -0.1518 409 ILE D C   
10965 O O   . ILE D 345 ? 0.5194 0.6214 0.5781 0.0550  -0.0670 -0.1466 409 ILE D O   
10966 C CB  . ILE D 345 ? 0.5551 0.6364 0.5914 0.0567  -0.0758 -0.1464 409 ILE D CB  
10967 C CG1 . ILE D 345 ? 0.6137 0.6921 0.6390 0.0630  -0.0813 -0.1467 409 ILE D CG1 
10968 C CG2 . ILE D 345 ? 0.5487 0.6214 0.5928 0.0470  -0.0738 -0.1487 409 ILE D CG2 
10969 C CD1 . ILE D 345 ? 0.8268 0.8890 0.8425 0.0587  -0.0799 -0.1441 409 ILE D CD1 
10970 N N   . ALA D 346 ? 0.5103 0.6185 0.5874 0.0515  -0.0777 -0.1587 410 ALA D N   
10971 C CA  . ALA D 346 ? 0.5558 0.6699 0.6504 0.0441  -0.0714 -0.1590 410 ALA D CA  
10972 C C   . ALA D 346 ? 0.6641 0.7645 0.7519 0.0365  -0.0605 -0.1512 410 ALA D C   
10973 O O   . ALA D 346 ? 0.6255 0.7105 0.7038 0.0326  -0.0604 -0.1490 410 ALA D O   
10974 C CB  . ALA D 346 ? 0.5103 0.6302 0.6262 0.0388  -0.0776 -0.1672 410 ALA D CB  
10975 N N   . ALA D 347 ? 0.7000 0.8054 0.7906 0.0360  -0.0518 -0.1473 411 ALA D N   
10976 C CA  . ALA D 347 ? 0.6568 0.7507 0.7417 0.0302  -0.0407 -0.1405 411 ALA D CA  
10977 C C   . ALA D 347 ? 0.6811 0.7870 0.7873 0.0246  -0.0325 -0.1406 411 ALA D C   
10978 O O   . ALA D 347 ? 0.9284 1.0508 1.0567 0.0235  -0.0370 -0.1470 411 ALA D O   
10979 C CB  . ALA D 347 ? 0.7240 0.8102 0.7893 0.0362  -0.0369 -0.1352 411 ALA D CB  
10980 N N   . THR D 348 ? 0.6697 0.7675 0.7696 0.0215  -0.0205 -0.1336 412 THR D N   
10981 C CA  . THR D 348 ? 0.7280 0.8393 0.8452 0.0188  -0.0098 -0.1316 412 THR D CA  
10982 C C   . THR D 348 ? 0.7032 0.8048 0.7997 0.0237  0.0012  -0.1242 412 THR D C   
10983 O O   . THR D 348 ? 0.6475 0.7289 0.7205 0.0252  0.0018  -0.1200 412 THR D O   
10984 C CB  . THR D 348 ? 0.8014 0.9159 0.9436 0.0068  -0.0049 -0.1310 412 THR D CB  
10985 O OG1 . THR D 348 ? 0.8665 0.9587 0.9938 0.0016  0.0006  -0.1240 412 THR D OG1 
10986 C CG2 . THR D 348 ? 0.7873 0.9117 0.9517 0.0034  -0.0186 -0.1408 412 THR D CG2 
10987 N N   . THR D 349 ? 0.7059 0.8219 0.8103 0.0277  0.0085  -0.1237 413 THR D N   
10988 C CA  . THR D 349 ? 0.8156 0.9237 0.9013 0.0338  0.0192  -0.1176 413 THR D CA  
10989 C C   . THR D 349 ? 1.0106 1.1113 1.0978 0.0268  0.0330  -0.1097 413 THR D C   
10990 O O   . THR D 349 ? 1.0179 1.1252 1.1283 0.0165  0.0350  -0.1095 413 THR D O   
10991 C CB  . THR D 349 ? 0.8324 0.9603 0.9286 0.0410  0.0226  -0.1203 413 THR D CB  
10992 O OG1 . THR D 349 ? 0.9749 1.1050 1.0657 0.0481  0.0099  -0.1261 413 THR D OG1 
10993 C CG2 . THR D 349 ? 0.8800 1.0023 0.9584 0.0490  0.0344  -0.1148 413 THR D CG2 
10994 N N   . LYS D 350 ? 1.2395 1.3252 1.3014 0.0330  0.0420  -0.1032 414 LYS D N   
10995 C CA  . LYS D 350 ? 1.0794 1.1563 1.1369 0.0293  0.0577  -0.0937 414 LYS D CA  
10996 C C   . LYS D 350 ? 1.1721 1.2712 1.2642 0.0207  0.0694  -0.0909 414 LYS D C   
10997 O O   . LYS D 350 ? 1.3054 1.3983 1.4034 0.0128  0.0808  -0.0828 414 LYS D O   
10998 C CB  . LYS D 350 ? 1.3221 1.3866 1.3484 0.0419  0.0660  -0.0888 414 LYS D CB  
10999 C CG  . LYS D 350 ? 1.2669 1.3183 1.2792 0.0419  0.0830  -0.0776 414 LYS D CG  
11000 C CD  . LYS D 350 ? 1.5764 1.6220 1.5608 0.0577  0.0913  -0.0747 414 LYS D CD  
11001 C CE  . LYS D 350 ? 1.3091 1.3424 1.2768 0.0602  0.1102  -0.0624 414 LYS D CE  
11002 N NZ  . LYS D 350 ? 1.5327 1.5570 1.4670 0.0785  0.1161  -0.0609 414 LYS D NZ  
11003 N N   . ALA D 351 ? 1.1357 1.2603 1.2518 0.0222  0.0664  -0.0974 415 ALA D N   
11004 C CA  . ALA D 351 ? 1.1720 1.3210 1.3270 0.0137  0.0752  -0.0967 415 ALA D CA  
11005 C C   . ALA D 351 ? 1.2512 1.4220 1.4346 0.0118  0.0610  -0.1084 415 ALA D C   
11006 O O   . ALA D 351 ? 1.5098 1.6992 1.7006 0.0198  0.0604  -0.1130 415 ALA D O   
11007 C CB  . ALA D 351 ? 1.0756 1.2379 1.2313 0.0208  0.0929  -0.0904 415 ALA D CB  
11008 N N   . GLY D 352 ? 1.0739 1.2415 1.2714 0.0028  0.0491  -0.1134 416 GLY D N   
11009 C CA  . GLY D 352 ? 0.9636 1.1496 1.1857 0.0023  0.0338  -0.1254 416 GLY D CA  
11010 C C   . GLY D 352 ? 1.1436 1.3251 1.3419 0.0142  0.0205  -0.1316 416 GLY D C   
11011 O O   . GLY D 352 ? 1.4256 1.5876 1.5914 0.0200  0.0210  -0.1273 416 GLY D O   
11012 N N   . LEU D 353 ? 1.0288 1.2277 1.2435 0.0181  0.0085  -0.1415 417 LEU D N   
11013 C CA  . LEU D 353 ? 0.8997 1.0972 1.0947 0.0303  -0.0026 -0.1463 417 LEU D CA  
11014 C C   . LEU D 353 ? 1.0111 1.1913 1.1880 0.0307  -0.0148 -0.1482 417 LEU D C   
11015 O O   . LEU D 353 ? 1.1977 1.3600 1.3628 0.0248  -0.0125 -0.1435 417 LEU D O   
11016 C CB  . LEU D 353 ? 0.6958 0.8863 0.8660 0.0398  0.0052  -0.1408 417 LEU D CB  
11017 C CG  . LEU D 353 ? 0.8898 1.0914 1.0689 0.0404  0.0215  -0.1358 417 LEU D CG  
11018 C CD1 . LEU D 353 ? 0.9500 1.1374 1.0983 0.0500  0.0290  -0.1299 417 LEU D CD1 
11019 C CD2 . LEU D 353 ? 0.6987 0.9292 0.9073 0.0434  0.0218  -0.1420 417 LEU D CD2 
11020 N N   . SER D 354 ? 1.2397 1.4254 1.4134 0.0386  -0.0273 -0.1548 418 SER D N   
11021 C CA  . SER D 354 ? 1.3172 1.4912 1.4783 0.0396  -0.0386 -0.1573 418 SER D CA  
11022 C C   . SER D 354 ? 1.3638 1.5276 1.4981 0.0494  -0.0423 -0.1543 418 SER D C   
11023 O O   . SER D 354 ? 2.3878 2.5569 2.5190 0.0571  -0.0518 -0.1585 418 SER D O   
11024 C CB  . SER D 354 ? 1.7234 1.9120 1.9052 0.0408  -0.0512 -0.1678 418 SER D CB  
11025 O OG  . SER D 354 ? 2.2417 2.4474 2.4305 0.0504  -0.0555 -0.1729 418 SER D OG  
11026 N N   . SER D 355 ? 1.0776 1.2265 1.1927 0.0494  -0.0349 -0.1468 419 SER D N   
11027 C CA  . SER D 355 ? 1.2111 1.3484 1.3041 0.0565  -0.0393 -0.1437 419 SER D CA  
11028 C C   . SER D 355 ? 0.9277 1.0566 1.0141 0.0547  -0.0468 -0.1445 419 SER D C   
11029 O O   . SER D 355 ? 0.7639 0.8914 0.8587 0.0479  -0.0478 -0.1469 419 SER D O   
11030 C CB  . SER D 355 ? 1.4536 1.5759 1.5290 0.0573  -0.0318 -0.1372 419 SER D CB  
11031 O OG  . SER D 355 ? 1.1984 1.3109 1.2574 0.0638  -0.0365 -0.1345 419 SER D OG  
11032 N N   . ASN D 356 ? 1.0305 1.1546 1.1031 0.0614  -0.0521 -0.1425 420 ASN D N   
11033 C CA  . ASN D 356 ? 0.8257 0.9415 0.8891 0.0614  -0.0575 -0.1418 420 ASN D CA  
11034 C C   . ASN D 356 ? 0.7851 0.8850 0.8319 0.0612  -0.0549 -0.1351 420 ASN D C   
11035 O O   . ASN D 356 ? 0.9886 1.0848 1.0300 0.0638  -0.0517 -0.1316 420 ASN D O   
11036 C CB  . ASN D 356 ? 0.8191 0.9441 0.8814 0.0703  -0.0652 -0.1443 420 ASN D CB  
11037 C CG  . ASN D 356 ? 0.9197 1.0610 0.9973 0.0735  -0.0692 -0.1516 420 ASN D CG  
11038 O OD1 . ASN D 356 ? 0.9929 1.1415 1.0760 0.0760  -0.0664 -0.1518 420 ASN D OD1 
11039 N ND2 . ASN D 356 ? 1.0156 1.1627 1.1006 0.0741  -0.0768 -0.1587 420 ASN D ND2 
11040 N N   . ASP D 357 ? 0.8465 0.9368 0.8861 0.0586  -0.0572 -0.1342 421 ASP D N   
11041 C CA  . ASP D 357 ? 0.8328 0.9105 0.8592 0.0597  -0.0572 -0.1289 421 ASP D CA  
11042 C C   . ASP D 357 ? 0.7153 0.7941 0.7375 0.0635  -0.0625 -0.1280 421 ASP D C   
11043 O O   . ASP D 357 ? 1.1623 1.2494 1.1883 0.0661  -0.0666 -0.1320 421 ASP D O   
11044 C CB  . ASP D 357 ? 0.8831 0.9454 0.9015 0.0543  -0.0535 -0.1273 421 ASP D CB  
11045 C CG  . ASP D 357 ? 1.1938 1.2455 1.2023 0.0565  -0.0518 -0.1233 421 ASP D CG  
11046 O OD1 . ASP D 357 ? 1.7194 1.7706 1.7260 0.0603  -0.0555 -0.1208 421 ASP D OD1 
11047 O OD2 . ASP D 357 ? 1.2282 1.2713 1.2308 0.0550  -0.0468 -0.1226 421 ASP D OD2 
11048 N N   . LEU D 358 ? 0.6898 0.7604 0.7047 0.0646  -0.0626 -0.1231 422 LEU D N   
11049 C CA  . LEU D 358 ? 0.5810 0.6545 0.5935 0.0689  -0.0656 -0.1203 422 LEU D CA  
11050 C C   . LEU D 358 ? 0.5538 0.6180 0.5607 0.0664  -0.0674 -0.1205 422 LEU D C   
11051 O O   . LEU D 358 ? 0.6014 0.6534 0.6038 0.0623  -0.0665 -0.1204 422 LEU D O   
11052 C CB  . LEU D 358 ? 0.5543 0.6272 0.5674 0.0716  -0.0645 -0.1137 422 LEU D CB  
11053 C CG  . LEU D 358 ? 0.5749 0.6586 0.5913 0.0777  -0.0640 -0.1117 422 LEU D CG  
11054 C CD1 . LEU D 358 ? 0.5948 0.6772 0.6123 0.0804  -0.0630 -0.1032 422 LEU D CD1 
11055 C CD2 . LEU D 358 ? 0.5743 0.6688 0.5901 0.0825  -0.0666 -0.1155 422 LEU D CD2 
11056 N N   . ILE D 359 ? 0.5357 0.6057 0.5413 0.0706  -0.0704 -0.1212 423 ILE D N   
11057 C CA  . ILE D 359 ? 0.5140 0.5777 0.5150 0.0706  -0.0725 -0.1204 423 ILE D CA  
11058 C C   . ILE D 359 ? 0.5517 0.6269 0.5550 0.0776  -0.0722 -0.1155 423 ILE D C   
11059 O O   . ILE D 359 ? 0.7252 0.8114 0.7290 0.0834  -0.0719 -0.1154 423 ILE D O   
11060 C CB  . ILE D 359 ? 0.4100 0.4674 0.4060 0.0690  -0.0761 -0.1268 423 ILE D CB  
11061 C CG1 . ILE D 359 ? 0.4385 0.4929 0.4295 0.0721  -0.0790 -0.1263 423 ILE D CG1 
11062 C CG2 . ILE D 359 ? 0.4420 0.5085 0.4404 0.0727  -0.0790 -0.1316 423 ILE D CG2 
11063 C CD1 . ILE D 359 ? 0.6279 0.6679 0.6118 0.0685  -0.0819 -0.1308 423 ILE D CD1 
11064 N N   . THR D 360 ? 0.5634 0.6366 0.5687 0.0775  -0.0719 -0.1111 424 THR D N   
11065 C CA  . THR D 360 ? 0.5531 0.6382 0.5634 0.0834  -0.0695 -0.1044 424 THR D CA  
11066 C C   . THR D 360 ? 0.5005 0.5869 0.5095 0.0860  -0.0716 -0.1054 424 THR D C   
11067 O O   . THR D 360 ? 0.6996 0.7751 0.7067 0.0819  -0.0751 -0.1090 424 THR D O   
11068 C CB  . THR D 360 ? 0.6030 0.6873 0.6233 0.0806  -0.0666 -0.0964 424 THR D CB  
11069 O OG1 . THR D 360 ? 0.6871 0.7638 0.7123 0.0765  -0.0692 -0.0963 424 THR D OG1 
11070 C CG2 . THR D 360 ? 0.6846 0.7617 0.7044 0.0769  -0.0663 -0.0975 424 THR D CG2 
11071 N N   . PHE D 361 ? 0.4546 0.5545 0.4637 0.0942  -0.0694 -0.1020 425 PHE D N   
11072 C CA  . PHE D 361 ? 0.5441 0.6487 0.5530 0.0987  -0.0706 -0.1025 425 PHE D CA  
11073 C C   . PHE D 361 ? 0.5083 0.6270 0.5288 0.1026  -0.0641 -0.0919 425 PHE D C   
11074 O O   . PHE D 361 ? 0.5919 0.7189 0.6144 0.1060  -0.0585 -0.0848 425 PHE D O   
11075 C CB  . PHE D 361 ? 0.5172 0.6258 0.5137 0.1076  -0.0740 -0.1093 425 PHE D CB  
11076 C CG  . PHE D 361 ? 0.4408 0.5351 0.4293 0.1030  -0.0806 -0.1192 425 PHE D CG  
11077 C CD1 . PHE D 361 ? 0.4260 0.5178 0.4129 0.1006  -0.0816 -0.1228 425 PHE D CD1 
11078 C CD2 . PHE D 361 ? 0.4413 0.5243 0.4253 0.1006  -0.0855 -0.1244 425 PHE D CD2 
11079 C CE1 . PHE D 361 ? 0.4490 0.5283 0.4322 0.0950  -0.0866 -0.1308 425 PHE D CE1 
11080 C CE2 . PHE D 361 ? 0.4385 0.5064 0.4157 0.0956  -0.0904 -0.1320 425 PHE D CE2 
11081 C CZ  . PHE D 361 ? 0.4302 0.4969 0.4083 0.0923  -0.0905 -0.1348 425 PHE D CZ  
11082 N N   . CYS D 362 ? 0.5455 0.6674 0.5742 0.1024  -0.0646 -0.0906 426 CYS D N   
11083 C CA  . CYS D 362 ? 0.7302 0.8687 0.7729 0.1065  -0.0572 -0.0799 426 CYS D CA  
11084 C C   . CYS D 362 ? 0.6764 0.8263 0.7157 0.1160  -0.0569 -0.0817 426 CYS D C   
11085 O O   . CYS D 362 ? 0.7212 0.8633 0.7524 0.1166  -0.0642 -0.0912 426 CYS D O   
11086 C CB  . CYS D 362 ? 0.8164 0.9522 0.8798 0.0973  -0.0570 -0.0743 426 CYS D CB  
11087 S SG  . CYS D 362 ? 1.5177 1.6418 1.5823 0.0899  -0.0561 -0.0708 426 CYS D SG  
11088 N N   . GLY D 363 ? 0.6342 0.8024 0.6781 0.1245  -0.0480 -0.0721 427 GLY D N   
11089 C CA  . GLY D 363 ? 0.7233 0.9052 0.7634 0.1361  -0.0462 -0.0730 427 GLY D CA  
11090 C C   . GLY D 363 ? 0.7161 0.9052 0.7756 0.1330  -0.0463 -0.0712 427 GLY D C   
11091 O O   . GLY D 363 ? 0.8706 1.0633 0.9527 0.1246  -0.0427 -0.0631 427 GLY D O   
11092 N N   . THR D 364 ? 0.8283 1.0187 0.8796 0.1400  -0.0518 -0.0797 428 THR D N   
11093 C CA  . THR D 364 ? 0.8775 1.0795 0.9461 0.1413  -0.0517 -0.0786 428 THR D CA  
11094 C C   . THR D 364 ? 0.8836 1.1069 0.9474 0.1576  -0.0451 -0.0759 428 THR D C   
11095 O O   . THR D 364 ? 0.6746 0.8974 0.7149 0.1690  -0.0454 -0.0800 428 THR D O   
11096 C CB  . THR D 364 ? 0.9736 1.1581 1.0384 0.1362  -0.0647 -0.0912 428 THR D CB  
11097 O OG1 . THR D 364 ? 1.2817 1.4792 1.3673 0.1372  -0.0650 -0.0898 428 THR D OG1 
11098 C CG2 . THR D 364 ? 0.8765 1.0498 0.9147 0.1444  -0.0725 -0.1030 428 THR D CG2 
11099 N N   . GLY D 365 ? 0.9554 1.1977 1.0424 0.1591  -0.0394 -0.0694 429 GLY D N   
11100 C CA  . GLY D 365 ? 1.0511 1.3175 1.1376 0.1752  -0.0310 -0.0650 429 GLY D CA  
11101 C C   . GLY D 365 ? 0.9713 1.2315 1.0377 0.1857  -0.0418 -0.0797 429 GLY D C   
11102 O O   . GLY D 365 ? 0.9135 1.1858 0.9649 0.2025  -0.0384 -0.0808 429 GLY D O   
11103 N N   . GLY D 366 ? 0.8949 1.1346 0.9595 0.1767  -0.0552 -0.0910 430 GLY D N   
11104 C CA  . GLY D 366 ? 0.7927 1.0217 0.8392 0.1847  -0.0669 -0.1050 430 GLY D CA  
11105 C C   . GLY D 366 ? 0.9961 1.2071 1.0115 0.1902  -0.0735 -0.1140 430 GLY D C   
11106 O O   . GLY D 366 ? 1.0618 1.2626 1.0704 0.1836  -0.0723 -0.1121 430 GLY D O   
11107 N N   . SER D 367 ? 1.0877 1.2950 1.0853 0.2029  -0.0811 -0.1243 431 SER D N   
11108 C CA  . SER D 367 ? 0.9336 1.1192 0.9048 0.2058  -0.0908 -0.1350 431 SER D CA  
11109 C C   . SER D 367 ? 0.8488 1.0063 0.8179 0.1902  -0.1005 -0.1414 431 SER D C   
11110 O O   . SER D 367 ? 0.8277 0.9822 0.8099 0.1824  -0.1023 -0.1405 431 SER D O   
11111 C CB  . SER D 367 ? 0.9060 1.0928 0.8590 0.2238  -0.0977 -0.1449 431 SER D CB  
11112 O OG  . SER D 367 ? 1.2141 1.3783 1.1442 0.2256  -0.1085 -0.1557 431 SER D OG  
11113 N N   . MET D 368 ? 0.8752 1.0128 0.8286 0.1861  -0.1065 -0.1475 432 MET D N   
11114 C CA  . MET D 368 ? 0.7547 0.8662 0.7049 0.1721  -0.1135 -0.1519 432 MET D CA  
11115 C C   . MET D 368 ? 0.9076 0.9966 0.8372 0.1751  -0.1246 -0.1634 432 MET D C   
11116 O O   . MET D 368 ? 0.9338 1.0262 0.8527 0.1851  -0.1271 -0.1678 432 MET D O   
11117 C CB  . MET D 368 ? 0.7220 0.8311 0.6800 0.1594  -0.1076 -0.1454 432 MET D CB  
11118 C CG  . MET D 368 ? 0.8339 0.9559 0.8133 0.1522  -0.0997 -0.1352 432 MET D CG  
11119 S SD  . MET D 368 ? 0.8255 0.9266 0.8101 0.1383  -0.1051 -0.1371 432 MET D SD  
11120 C CE  . MET D 368 ? 0.7827 0.8568 0.7486 0.1305  -0.1101 -0.1433 432 MET D CE  
11121 N N   . PRO D 369 ? 0.7735 0.8382 0.6973 0.1668  -0.1317 -0.1680 433 PRO D N   
11122 C CA  . PRO D 369 ? 0.7502 0.7905 0.6570 0.1675  -0.1418 -0.1776 433 PRO D CA  
11123 C C   . PRO D 369 ? 0.8723 0.9036 0.7782 0.1585  -0.1413 -0.1779 433 PRO D C   
11124 O O   . PRO D 369 ? 0.9063 0.9475 0.8233 0.1509  -0.1333 -0.1708 433 PRO D O   
11125 C CB  . PRO D 369 ? 0.7359 0.7549 0.6392 0.1599  -0.1460 -0.1786 433 PRO D CB  
11126 C CG  . PRO D 369 ? 0.8038 0.8307 0.7221 0.1494  -0.1378 -0.1699 433 PRO D CG  
11127 C CD  . PRO D 369 ? 0.8245 0.8821 0.7574 0.1563  -0.1303 -0.1641 433 PRO D CD  
11128 N N   . ASP D 370 ? 0.9782 0.9908 0.8725 0.1597  -0.1505 -0.1865 434 ASP D N   
11129 C CA  . ASP D 370 ? 0.9317 0.9357 0.8282 0.1513  -0.1517 -0.1884 434 ASP D CA  
11130 C C   . ASP D 370 ? 0.9070 0.8945 0.8082 0.1349  -0.1478 -0.1836 434 ASP D C   
11131 O O   . ASP D 370 ? 0.9970 0.9642 0.8904 0.1317  -0.1514 -0.1849 434 ASP D O   
11132 C CB  . ASP D 370 ? 1.5241 1.5109 1.4098 0.1567  -0.1642 -0.1996 434 ASP D CB  
11133 C CG  . ASP D 370 ? 1.9556 1.9575 1.8334 0.1754  -0.1695 -0.2061 434 ASP D CG  
11134 O OD1 . ASP D 370 ? 2.0721 2.0988 1.9543 0.1824  -0.1619 -0.2010 434 ASP D OD1 
11135 O OD2 . ASP D 370 ? 2.1007 2.0886 1.9667 0.1841  -0.1813 -0.2162 434 ASP D OD2 
11136 N N   . VAL D 371 ? 0.8549 0.8507 0.7670 0.1260  -0.1403 -0.1780 435 VAL D N   
11137 C CA  . VAL D 371 ? 0.7556 0.7383 0.6720 0.1116  -0.1351 -0.1728 435 VAL D CA  
11138 C C   . VAL D 371 ? 0.7604 0.7462 0.6862 0.1038  -0.1322 -0.1724 435 VAL D C   
11139 O O   . VAL D 371 ? 0.8168 0.8217 0.7493 0.1079  -0.1296 -0.1713 435 VAL D O   
11140 C CB  . VAL D 371 ? 0.7065 0.6985 0.6290 0.1087  -0.1272 -0.1646 435 VAL D CB  
11141 C CG1 . VAL D 371 ? 0.9338 0.9099 0.8562 0.0967  -0.1230 -0.1607 435 VAL D CG1 
11142 C CG2 . VAL D 371 ? 0.7969 0.7901 0.7145 0.1168  -0.1304 -0.1653 435 VAL D CG2 
11143 N N   . ASN D 372 ? 0.8148 0.7818 0.7411 0.0933  -0.1324 -0.1728 436 ASN D N   
11144 C CA  . ASN D 372 ? 0.9437 0.9135 0.8820 0.0836  -0.1278 -0.1710 436 ASN D CA  
11145 C C   . ASN D 372 ? 0.8579 0.8265 0.7989 0.0751  -0.1175 -0.1623 436 ASN D C   
11146 O O   . ASN D 372 ? 1.0527 1.0027 0.9868 0.0694  -0.1153 -0.1594 436 ASN D O   
11147 C CB  . ASN D 372 ? 0.9689 0.9202 0.9097 0.0768  -0.1333 -0.1762 436 ASN D CB  
11148 C CG  . ASN D 372 ? 1.4639 1.4185 1.4206 0.0655  -0.1277 -0.1740 436 ASN D CG  
11149 O OD1 . ASN D 372 ? 1.5674 1.5363 1.5309 0.0631  -0.1197 -0.1687 436 ASN D OD1 
11150 N ND2 . ASN D 372 ? 1.6525 1.5937 1.6167 0.0586  -0.1322 -0.1781 436 ASN D ND2 
11151 N N   . TRP D 373 ? 0.6374 0.6241 0.5865 0.0754  -0.1117 -0.1581 437 TRP D N   
11152 C CA  . TRP D 373 ? 0.7289 0.7143 0.6803 0.0688  -0.1033 -0.1509 437 TRP D CA  
11153 C C   . TRP D 373 ? 0.6349 0.6154 0.5933 0.0590  -0.0977 -0.1491 437 TRP D C   
11154 O O   . TRP D 373 ? 0.6685 0.6515 0.6356 0.0561  -0.0999 -0.1532 437 TRP D O   
11155 C CB  . TRP D 373 ? 0.6279 0.6324 0.5855 0.0730  -0.0996 -0.1465 437 TRP D CB  
11156 C CG  . TRP D 373 ? 0.6379 0.6493 0.5919 0.0819  -0.1028 -0.1465 437 TRP D CG  
11157 C CD1 . TRP D 373 ? 0.6637 0.6890 0.6181 0.0914  -0.1060 -0.1489 437 TRP D CD1 
11158 C CD2 . TRP D 373 ? 0.5824 0.5878 0.5323 0.0832  -0.1034 -0.1442 437 TRP D CD2 
11159 N NE1 . TRP D 373 ? 0.5959 0.6257 0.5484 0.0977  -0.1070 -0.1474 437 TRP D NE1 
11160 C CE2 . TRP D 373 ? 0.5970 0.6159 0.5482 0.0928  -0.1062 -0.1451 437 TRP D CE2 
11161 C CE3 . TRP D 373 ? 0.5418 0.5332 0.4869 0.0787  -0.1023 -0.1421 437 TRP D CE3 
11162 C CZ2 . TRP D 373 ? 0.6837 0.7030 0.6353 0.0963  -0.1080 -0.1440 437 TRP D CZ2 
11163 C CZ3 . TRP D 373 ? 0.6245 0.6141 0.5675 0.0831  -0.1058 -0.1420 437 TRP D CZ3 
11164 C CH2 . TRP D 373 ? 0.6795 0.6837 0.6276 0.0911  -0.1087 -0.1430 437 TRP D CH2 
11165 C C1  . NAG E .   ? 0.9272 0.6591 0.7648 -0.0258 0.1056  0.0581  501 NAG A C1  
11166 C C2  . NAG E .   ? 0.9410 0.6619 0.7708 -0.0295 0.1238  0.0659  501 NAG A C2  
11167 C C3  . NAG E .   ? 1.1553 0.8567 0.9853 -0.0430 0.1354  0.0702  501 NAG A C3  
11168 C C4  . NAG E .   ? 1.3304 1.0036 1.1395 -0.0404 0.1291  0.0705  501 NAG A C4  
11169 C C5  . NAG E .   ? 1.0176 0.7073 0.8377 -0.0355 0.1100  0.0620  501 NAG A C5  
11170 C C6  . NAG E .   ? 1.0966 0.7585 0.8893 -0.0270 0.1033  0.0625  501 NAG A C6  
11171 C C7  . NAG E .   ? 1.0985 0.8527 0.9380 -0.0190 0.1255  0.0646  501 NAG A C7  
11172 C C8  . NAG E .   ? 0.8404 0.6210 0.6998 -0.0207 0.1296  0.0629  501 NAG A C8  
11173 N N2  . NAG E .   ? 0.9438 0.6914 0.7939 -0.0317 0.1282  0.0646  501 NAG A N2  
11174 O O3  . NAG E .   ? 1.2318 0.9147 1.0419 -0.0414 0.1520  0.0786  501 NAG A O3  
11175 O O4  . NAG E .   ? 1.2061 0.8575 1.0138 -0.0538 0.1392  0.0741  501 NAG A O4  
11176 O O5  . NAG E .   ? 1.0170 0.7242 0.8361 -0.0235 0.1018  0.0589  501 NAG A O5  
11177 O O6  . NAG E .   ? 1.6127 1.2924 1.4161 -0.0222 0.0869  0.0547  501 NAG A O6  
11178 O O7  . NAG E .   ? 1.0881 0.8283 0.9025 -0.0055 0.1194  0.0651  501 NAG A O7  
11181 C C1  . NAG H .   ? 0.7907 0.9448 1.6451 0.0630  -0.5688 -0.3273 501 NAG B C1  
11182 C C2  . NAG H .   ? 0.8707 1.0179 1.7841 0.0566  -0.6028 -0.3377 501 NAG B C2  
11183 C C3  . NAG H .   ? 0.9035 1.0804 1.9090 0.0413  -0.5969 -0.3215 501 NAG B C3  
11184 C C4  . NAG H .   ? 0.9597 1.1540 1.9818 0.0474  -0.6004 -0.3186 501 NAG B C4  
11185 C C5  . NAG H .   ? 0.9297 1.1312 1.8926 0.0533  -0.5642 -0.3073 501 NAG B C5  
11186 C C6  . NAG H .   ? 0.9003 1.1179 1.8793 0.0601  -0.5693 -0.3053 501 NAG B C6  
11187 C C7  . NAG H .   ? 1.0341 1.1309 1.8891 0.0644  -0.6338 -0.3643 501 NAG B C7  
11188 C C8  . NAG H .   ? 0.9172 0.9954 1.7556 0.0600  -0.6322 -0.3678 501 NAG B C8  
11189 N N2  . NAG H .   ? 0.9674 1.0952 1.8633 0.0528  -0.6044 -0.3431 501 NAG B N2  
11190 O O3  . NAG H .   ? 1.0885 1.2575 2.1491 0.0357  -0.6306 -0.3318 501 NAG B O3  
11191 O O4  . NAG H .   ? 0.8591 1.0798 1.9721 0.0358  -0.6021 -0.3055 501 NAG B O4  
11192 O O5  . NAG H .   ? 0.8410 1.0167 1.7175 0.0650  -0.5625 -0.3190 501 NAG B O5  
11193 O O6  . NAG H .   ? 1.2124 1.4354 2.1383 0.0662  -0.5388 -0.2960 501 NAG B O6  
11194 O O7  . NAG H .   ? 0.9898 1.0724 1.8185 0.0795  -0.6609 -0.3804 501 NAG B O7  
11196 C C1  . NAG J .   ? 0.9242 1.1726 1.0542 0.0355  -0.2046 0.0876  501 NAG C C1  
11197 C C2  . NAG J .   ? 0.8856 1.1662 1.0490 0.0266  -0.2074 0.1100  501 NAG C C2  
11198 C C3  . NAG J .   ? 0.9903 1.2905 1.1754 0.0132  -0.2094 0.1387  501 NAG C C3  
11199 C C4  . NAG J .   ? 1.1472 1.4673 1.3184 0.0220  -0.1955 0.1444  501 NAG C C4  
11200 C C5  . NAG J .   ? 0.9576 1.2400 1.0957 0.0305  -0.1959 0.1189  501 NAG C C5  
11201 C C6  . NAG J .   ? 1.0321 1.3321 1.1546 0.0410  -0.1833 0.1215  501 NAG C C6  
11202 C C7  . NAG J .   ? 1.0893 1.3387 1.2504 0.0293  -0.2200 0.0849  501 NAG C C7  
11203 C C8  . NAG J .   ? 0.8234 1.0493 0.9937 0.0211  -0.2356 0.0810  501 NAG C C8  
11204 N N2  . NAG J .   ? 0.9141 1.1720 1.0864 0.0193  -0.2213 0.1037  501 NAG C N2  
11205 O O3  . NAG J .   ? 0.8189 1.1579 1.0368 0.0064  -0.2085 0.1616  501 NAG C O3  
11206 O O4  . NAG J .   ? 1.0583 1.3908 1.2457 0.0093  -0.1980 0.1707  501 NAG C O4  
11207 O O5  . NAG J .   ? 0.8614 1.1346 0.9850 0.0428  -0.1924 0.0954  501 NAG C O5  
11208 O O6  . NAG J .   ? 1.2535 1.5204 1.3484 0.0495  -0.1841 0.0959  501 NAG C O6  
11209 O O7  . NAG J .   ? 1.1553 1.4131 1.2988 0.0451  -0.2080 0.0705  501 NAG C O7  
11211 C C1  . NAG L .   ? 1.4228 1.2960 1.6494 0.0652  0.0318  0.2213  501 NAG D C1  
11212 C C2  . NAG L .   ? 1.3903 1.2469 1.6332 0.0618  0.0466  0.2519  501 NAG D C2  
11213 C C3  . NAG L .   ? 1.5430 1.4105 1.8376 0.0429  0.0560  0.2671  501 NAG D C3  
11214 C C4  . NAG L .   ? 1.6096 1.4756 1.9401 0.0255  0.0358  0.2466  501 NAG D C4  
11215 C C5  . NAG L .   ? 1.5426 1.4223 1.8445 0.0335  0.0218  0.2164  501 NAG D C5  
11216 C C6  . NAG L .   ? 1.3784 1.2500 1.7026 0.0216  -0.0009 0.1934  501 NAG D C6  
11217 C C7  . NAG L .   ? 1.3328 1.1779 1.5038 0.0961  0.0634  0.2706  501 NAG D C7  
11218 C C8  . NAG L .   ? 1.3108 1.1694 1.4435 0.1169  0.0813  0.2837  501 NAG D C8  
11219 N N2  . NAG L .   ? 1.2940 1.1594 1.4989 0.0811  0.0638  0.2657  501 NAG D N2  
11220 O O3  . NAG L .   ? 1.4004 1.2480 1.7169 0.0365  0.0673  0.2949  501 NAG D O3  
11221 O O4  . NAG L .   ? 1.3948 1.2785 1.7718 0.0102  0.0449  0.2583  501 NAG D O4  
11222 O O5  . NAG L .   ? 1.6652 1.5308 1.9243 0.0491  0.0149  0.2068  501 NAG D O5  
11223 O O6  . NAG L .   ? 1.3769 1.2492 1.6628 0.0336  -0.0126 0.1700  501 NAG D O6  
11224 O O7  . NAG L .   ? 1.2465 1.0630 1.4152 0.0951  0.0490  0.2645  501 NAG D O7  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   65  ?   ?   ?   A . n 
A 1 2   SER 2   66  ?   ?   ?   A . n 
A 1 3   GLY 3   67  ?   ?   ?   A . n 
A 1 4   ASP 4   68  ?   ?   ?   A . n 
A 1 5   SER 5   69  ?   ?   ?   A . n 
A 1 6   GLY 6   70  ?   ?   ?   A . n 
A 1 7   SER 7   71  ?   ?   ?   A . n 
A 1 8   PRO 8   72  ?   ?   ?   A . n 
A 1 9   GLY 9   73  ?   ?   ?   A . n 
A 1 10  ILE 10  74  ?   ?   ?   A . n 
A 1 11  ALA 11  75  75  ALA ALA A . n 
A 1 12  THR 12  76  76  THR THR A . n 
A 1 13  PRO 13  77  77  PRO PRO A . n 
A 1 14  LEU 14  78  78  LEU LEU A . n 
A 1 15  VAL 15  79  79  VAL VAL A . n 
A 1 16  LEU 16  80  80  LEU LEU A . n 
A 1 17  GLY 17  81  81  GLY GLY A . n 
A 1 18  GLU 18  82  82  GLU GLU A . n 
A 1 19  ASN 19  83  83  ASN ASN A . n 
A 1 20  LEU 20  84  84  LEU LEU A . n 
A 1 21  CYS 21  85  85  CYS CYS A . n 
A 1 22  SER 22  86  86  SER SER A . n 
A 1 23  ILE 23  87  87  ILE ILE A . n 
A 1 24  ASN 24  88  88  ASN ASN A . n 
A 1 25  GLY 25  89  89  GLY GLY A . n 
A 1 26  TRP 26  90  90  TRP TRP A . n 
A 1 27  VAL 27  91  91  VAL VAL A . n 
A 1 28  PRO 28  92  92  PRO PRO A . n 
A 1 29  THR 29  93  93  THR THR A . n 
A 1 30  TYR 30  94  94  TYR TYR A . n 
A 1 31  ARG 31  95  95  ARG ARG A . n 
A 1 32  GLY 32  96  96  GLY GLY A . n 
A 1 33  GLU 33  97  97  GLU GLU A . n 
A 1 34  GLY 34  98  98  GLY GLY A . n 
A 1 35  THR 35  99  99  THR THR A . n 
A 1 36  THR 36  100 100 THR THR A . n 
A 1 37  GLY 37  101 101 GLY GLY A . n 
A 1 38  LYS 38  102 102 LYS LYS A . n 
A 1 39  ILE 39  103 103 ILE ILE A . n 
A 1 40  PRO 40  104 104 PRO PRO A . n 
A 1 41  ASP 41  105 105 ASP ASP A . n 
A 1 42  GLU 42  106 106 GLU GLU A . n 
A 1 43  GLN 43  107 107 GLN GLN A . n 
A 1 44  MET 44  108 108 MET MET A . n 
A 1 45  LEU 45  109 109 LEU LEU A . n 
A 1 46  THR 46  110 110 THR THR A . n 
A 1 47  ARG 47  111 111 ARG ARG A . n 
A 1 48  GLN 48  112 112 GLN GLN A . n 
A 1 49  ASN 49  113 113 ASN ASN A . n 
A 1 50  PHE 50  114 114 PHE PHE A . n 
A 1 51  VAL 51  115 115 VAL VAL A . n 
A 1 52  SER 52  116 116 SER SER A . n 
A 1 53  CYS 53  117 117 CYS CYS A . n 
A 1 54  SER 54  118 118 SER SER A . n 
A 1 55  ASP 55  119 119 ASP ASP A . n 
A 1 56  LYS 56  120 120 LYS LYS A . n 
A 1 57  GLU 57  121 121 GLU GLU A . n 
A 1 58  CYS 58  122 122 CYS CYS A . n 
A 1 59  ARG 59  123 123 ARG ARG A . n 
A 1 60  ARG 60  124 124 ARG ARG A . n 
A 1 61  PHE 61  125 125 PHE PHE A . n 
A 1 62  PHE 62  126 126 PHE PHE A . n 
A 1 63  VAL 63  127 127 VAL VAL A . n 
A 1 64  SER 64  128 128 SER SER A . n 
A 1 65  MET 65  129 129 MET MET A . n 
A 1 66  GLY 66  130 130 GLY GLY A . n 
A 1 67  TYR 67  131 131 TYR TYR A . n 
A 1 68  GLY 68  132 132 GLY GLY A . n 
A 1 69  THR 69  133 133 THR THR A . n 
A 1 70  THR 70  134 134 THR THR A . n 
A 1 71  THR 71  135 135 THR THR A . n 
A 1 72  ASN 72  136 136 ASN ASN A . n 
A 1 73  PHE 73  137 137 PHE PHE A . n 
A 1 74  ALA 74  138 138 ALA ALA A . n 
A 1 75  ASP 75  139 139 ASP ASP A . n 
A 1 76  LEU 76  140 140 LEU LEU A . n 
A 1 77  ILE 77  141 141 ILE ILE A . n 
A 1 78  VAL 78  142 142 VAL VAL A . n 
A 1 79  SER 79  143 143 SER SER A . n 
A 1 80  GLU 80  144 144 GLU GLU A . n 
A 1 81  GLN 81  145 145 GLN GLN A . n 
A 1 82  MET 82  146 146 MET MET A . n 
A 1 83  ASN 83  147 147 ASN ASN A . n 
A 1 84  VAL 84  148 148 VAL VAL A . n 
A 1 85  TYR 85  149 149 TYR TYR A . n 
A 1 86  SER 86  150 150 SER SER A . n 
A 1 87  VAL 87  151 151 VAL VAL A . n 
A 1 88  LYS 88  152 152 LYS LYS A . n 
A 1 89  LEU 89  153 153 LEU LEU A . n 
A 1 90  GLY 90  154 154 GLY GLY A . n 
A 1 91  ASP 91  155 155 ASP ASP A . n 
A 1 92  PRO 92  156 156 PRO PRO A . n 
A 1 93  PRO 93  157 157 PRO PRO A . n 
A 1 94  THR 94  158 158 THR THR A . n 
A 1 95  PRO 95  159 159 PRO PRO A . n 
A 1 96  ASP 96  160 160 ASP ASP A . n 
A 1 97  LYS 97  161 161 LYS LYS A . n 
A 1 98  LEU 98  162 162 LEU LEU A . n 
A 1 99  LYS 99  163 163 LYS LYS A . n 
A 1 100 PHE 100 164 164 PHE PHE A . n 
A 1 101 GLU 101 165 165 GLU GLU A . n 
A 1 102 ALA 102 166 166 ALA ALA A . n 
A 1 103 VAL 103 167 167 VAL VAL A . n 
A 1 104 GLY 104 168 168 GLY GLY A . n 
A 1 105 TRP 105 169 169 TRP TRP A . n 
A 1 106 SER 106 170 170 SER SER A . n 
A 1 107 ALA 107 171 171 ALA ALA A . n 
A 1 108 SER 108 172 172 SER SER A . n 
A 1 109 SER 109 173 173 SER SER A . n 
A 1 110 CYS 110 174 174 CYS CYS A . n 
A 1 111 HIS 111 175 175 HIS HIS A . n 
A 1 112 ASP 112 176 176 ASP ASP A . n 
A 1 113 GLY 113 177 177 GLY GLY A . n 
A 1 114 PHE 114 178 178 PHE PHE A . n 
A 1 115 GLN 115 179 179 GLN GLN A . n 
A 1 116 TRP 116 180 180 TRP TRP A . n 
A 1 117 THR 117 181 181 THR THR A . n 
A 1 118 VAL 118 182 182 VAL VAL A . n 
A 1 119 LEU 119 183 183 LEU LEU A . n 
A 1 120 SER 120 184 184 SER SER A . n 
A 1 121 VAL 121 185 185 VAL VAL A . n 
A 1 122 ALA 122 186 186 ALA ALA A . n 
A 1 123 GLY 123 187 187 GLY GLY A . n 
A 1 124 ASP 124 188 188 ASP ASP A . n 
A 1 125 GLY 125 189 189 GLY GLY A . n 
A 1 126 PHE 126 190 190 PHE PHE A . n 
A 1 127 VAL 127 191 191 VAL VAL A . n 
A 1 128 SER 128 192 192 SER SER A . n 
A 1 129 ILE 129 193 193 ILE ILE A . n 
A 1 130 LEU 130 194 194 LEU LEU A . n 
A 1 131 TYR 131 195 195 TYR TYR A . n 
A 1 132 GLY 132 196 196 GLY GLY A . n 
A 1 133 GLY 133 197 197 GLY GLY A . n 
A 1 134 ILE 134 198 198 ILE ILE A . n 
A 1 135 ILE 135 199 199 ILE ILE A . n 
A 1 136 THR 136 200 200 THR THR A . n 
A 1 137 ASP 137 201 201 ASP ASP A . n 
A 1 138 THR 138 202 202 THR THR A . n 
A 1 139 ILE 139 203 203 ILE ILE A . n 
A 1 140 HIS 140 204 204 HIS HIS A . n 
A 1 141 PRO 141 205 205 PRO PRO A . n 
A 1 142 THR 142 206 206 THR THR A . n 
A 1 143 ASN 143 207 207 ASN ASN A . n 
A 1 144 GLY 144 208 208 GLY GLY A . n 
A 1 145 GLY 145 209 209 GLY GLY A . n 
A 1 146 PRO 146 210 210 PRO PRO A . n 
A 1 147 LEU 147 211 211 LEU LEU A . n 
A 1 148 ARG 148 212 212 ARG ARG A . n 
A 1 149 THR 149 213 213 THR THR A . n 
A 1 150 GLN 150 214 214 GLN GLN A . n 
A 1 151 ALA 151 215 215 ALA ALA A . n 
A 1 152 SER 152 216 216 SER SER A . n 
A 1 153 SER 153 217 217 SER SER A . n 
A 1 154 CYS 154 218 218 CYS CYS A . n 
A 1 155 ILE 155 219 219 ILE ILE A . n 
A 1 156 CYS 156 220 220 CYS CYS A . n 
A 1 157 ASN 157 221 221 ASN ASN A . n 
A 1 158 ASP 158 222 222 ASP ASP A . n 
A 1 159 GLY 159 223 223 GLY GLY A . n 
A 1 160 THR 160 224 224 THR THR A . n 
A 1 161 CYS 161 225 225 CYS CYS A . n 
A 1 162 TYR 162 226 226 TYR TYR A . n 
A 1 163 THR 163 227 227 THR THR A . n 
A 1 164 ILE 164 228 228 ILE ILE A . n 
A 1 165 ILE 165 229 229 ILE ILE A . n 
A 1 166 ALA 166 230 230 ALA ALA A . n 
A 1 167 ASP 167 231 231 ASP ASP A . n 
A 1 168 GLY 168 232 232 GLY GLY A . n 
A 1 169 THR 169 233 233 THR THR A . n 
A 1 170 THR 170 234 234 THR THR A . n 
A 1 171 TYR 171 235 235 TYR TYR A . n 
A 1 172 THR 172 236 236 THR THR A . n 
A 1 173 ALA 173 237 237 ALA ALA A . n 
A 1 174 SER 174 238 238 SER SER A . n 
A 1 175 SER 175 239 239 SER SER A . n 
A 1 176 HIS 176 240 240 HIS HIS A . n 
A 1 177 ARG 177 241 241 ARG ARG A . n 
A 1 178 LEU 178 242 242 LEU LEU A . n 
A 1 179 TYR 179 243 243 TYR TYR A . n 
A 1 180 ARG 180 244 244 ARG ARG A . n 
A 1 181 LEU 181 245 245 LEU LEU A . n 
A 1 182 VAL 182 246 246 VAL VAL A . n 
A 1 183 ASN 183 247 247 ASN ASN A . n 
A 1 184 GLY 184 248 248 GLY GLY A . n 
A 1 185 THR 185 249 249 THR THR A . n 
A 1 186 SER 186 250 250 SER SER A . n 
A 1 187 ALA 187 251 251 ALA ALA A . n 
A 1 188 GLY 188 252 252 GLY GLY A . n 
A 1 189 TRP 189 253 253 TRP TRP A . n 
A 1 190 LYS 190 254 254 LYS LYS A . n 
A 1 191 ALA 191 255 255 ALA ALA A . n 
A 1 192 LEU 192 256 256 LEU LEU A . n 
A 1 193 ASP 193 257 257 ASP ASP A . n 
A 1 194 THR 194 258 258 THR THR A . n 
A 1 195 THR 195 259 259 THR THR A . n 
A 1 196 GLY 196 260 260 GLY GLY A . n 
A 1 197 PHE 197 261 261 PHE PHE A . n 
A 1 198 ASN 198 262 262 ASN ASN A . n 
A 1 199 PHE 199 263 263 PHE PHE A . n 
A 1 200 GLU 200 264 264 GLU GLU A . n 
A 1 201 PHE 201 265 265 PHE PHE A . n 
A 1 202 PRO 202 266 266 PRO PRO A . n 
A 1 203 THR 203 267 267 THR THR A . n 
A 1 204 CYS 204 268 268 CYS CYS A . n 
A 1 205 TYR 205 269 269 TYR TYR A . n 
A 1 206 TYR 206 270 270 TYR TYR A . n 
A 1 207 THR 207 271 271 THR THR A . n 
A 1 208 SER 208 272 272 SER SER A . n 
A 1 209 GLY 209 273 273 GLY GLY A . n 
A 1 210 LYS 210 274 274 LYS LYS A . n 
A 1 211 VAL 211 275 275 VAL VAL A . n 
A 1 212 LYS 212 276 276 LYS LYS A . n 
A 1 213 CYS 213 277 277 CYS CYS A . n 
A 1 214 THR 214 278 278 THR THR A . n 
A 1 215 GLY 215 279 279 GLY GLY A . n 
A 1 216 THR 216 280 280 THR THR A . n 
A 1 217 ASN 217 281 281 ASN ASN A . n 
A 1 218 LEU 218 282 282 LEU LEU A . n 
A 1 219 TRP 219 283 283 TRP TRP A . n 
A 1 220 ASN 220 284 284 ASN ASN A . n 
A 1 221 ASP 221 285 285 ASP ASP A . n 
A 1 222 ALA 222 286 286 ALA ALA A . n 
A 1 223 LYS 223 287 287 LYS LYS A . n 
A 1 224 ARG 224 288 288 ARG ARG A . n 
A 1 225 PRO 225 289 289 PRO PRO A . n 
A 1 226 PHE 226 290 290 PHE PHE A . n 
A 1 227 LEU 227 291 291 LEU LEU A . n 
A 1 228 GLU 228 292 292 GLU GLU A . n 
A 1 229 PHE 229 293 293 PHE PHE A . n 
A 1 230 ASP 230 294 294 ASP ASP A . n 
A 1 231 GLN 231 295 295 GLN GLN A . n 
A 1 232 SER 232 296 296 SER SER A . n 
A 1 233 PHE 233 297 297 PHE PHE A . n 
A 1 234 THR 234 298 298 THR THR A . n 
A 1 235 TYR 235 299 299 TYR TYR A . n 
A 1 236 THR 236 300 300 THR THR A . n 
A 1 237 PHE 237 301 301 PHE PHE A . n 
A 1 238 LYS 238 302 302 LYS LYS A . n 
A 1 239 GLU 239 303 303 GLU GLU A . n 
A 1 240 PRO 240 304 304 PRO PRO A . n 
A 1 241 CYS 241 305 305 CYS CYS A . n 
A 1 242 LEU 242 306 306 LEU LEU A . n 
A 1 243 GLY 243 307 307 GLY GLY A . n 
A 1 244 PHE 244 308 308 PHE PHE A . n 
A 1 245 LEU 245 309 309 LEU LEU A . n 
A 1 246 GLY 246 310 310 GLY GLY A . n 
A 1 247 ASP 247 311 311 ASP ASP A . n 
A 1 248 THR 248 312 312 THR THR A . n 
A 1 249 PRO 249 313 313 PRO PRO A . n 
A 1 250 ARG 250 314 314 ARG ARG A . n 
A 1 251 GLY 251 315 315 GLY GLY A . n 
A 1 252 ILE 252 316 316 ILE ILE A . n 
A 1 253 ASP 253 317 317 ASP ASP A . n 
A 1 254 THR 254 318 318 THR THR A . n 
A 1 255 THR 255 319 319 THR THR A . n 
A 1 256 ASN 256 320 320 ASN ASN A . n 
A 1 257 TYR 257 321 321 TYR TYR A . n 
A 1 258 CYS 258 322 322 CYS CYS A . n 
A 1 259 ASP 259 323 323 ASP ASP A . n 
A 1 260 LYS 260 324 324 LYS LYS A . n 
A 1 261 THR 261 325 325 THR THR A . n 
A 1 262 THR 262 326 326 THR THR A . n 
A 1 263 THR 263 327 327 THR THR A . n 
A 1 264 GLU 264 328 328 GLU GLU A . n 
A 1 265 GLY 265 329 329 GLY GLY A . n 
A 1 266 GLU 266 330 330 GLU GLU A . n 
A 1 267 GLY 267 331 331 GLY GLY A . n 
A 1 268 GLY 268 332 332 GLY GLY A . n 
A 1 269 ILE 269 333 333 ILE ILE A . n 
A 1 270 GLN 270 334 334 GLN GLN A . n 
A 1 271 GLY 271 335 335 GLY GLY A . n 
A 1 272 PHE 272 336 336 PHE PHE A . n 
A 1 273 MET 273 337 337 MET MET A . n 
A 1 274 ILE 274 338 338 ILE ILE A . n 
A 1 275 GLU 275 339 339 GLU GLU A . n 
A 1 276 GLY 276 340 340 GLY GLY A . n 
A 1 277 SER 277 341 341 SER SER A . n 
A 1 278 ASN 278 342 342 ASN ASN A . n 
A 1 279 SER 279 343 343 SER SER A . n 
A 1 280 TRP 280 344 344 TRP TRP A . n 
A 1 281 ILE 281 345 345 ILE ILE A . n 
A 1 282 GLY 282 346 346 GLY GLY A . n 
A 1 283 ARG 283 347 347 ARG ARG A . n 
A 1 284 ILE 284 348 348 ILE ILE A . n 
A 1 285 ILE 285 349 349 ILE ILE A . n 
A 1 286 ASN 286 350 350 ASN ASN A . n 
A 1 287 PRO 287 351 351 PRO PRO A . n 
A 1 288 GLY 288 352 352 GLY GLY A . n 
A 1 289 SER 289 353 353 SER SER A . n 
A 1 290 LYS 290 354 354 LYS LYS A . n 
A 1 291 LYS 291 355 355 LYS LYS A . n 
A 1 292 GLY 292 356 356 GLY GLY A . n 
A 1 293 PHE 293 357 357 PHE PHE A . n 
A 1 294 GLU 294 358 358 GLU GLU A . n 
A 1 295 ILE 295 359 359 ILE ILE A . n 
A 1 296 TYR 296 360 360 TYR TYR A . n 
A 1 297 LYS 297 361 361 LYS LYS A . n 
A 1 298 PHE 298 362 362 PHE PHE A . n 
A 1 299 LEU 299 363 363 LEU LEU A . n 
A 1 300 GLY 300 364 364 GLY GLY A . n 
A 1 301 THR 301 365 365 THR THR A . n 
A 1 302 LEU 302 366 366 LEU LEU A . n 
A 1 303 PHE 303 367 367 PHE PHE A . n 
A 1 304 SER 304 368 368 SER SER A . n 
A 1 305 VAL 305 369 369 VAL VAL A . n 
A 1 306 GLN 306 370 370 GLN GLN A . n 
A 1 307 THR 307 371 371 THR THR A . n 
A 1 308 VAL 308 372 372 VAL VAL A . n 
A 1 309 GLY 309 373 373 GLY GLY A . n 
A 1 310 ASN 310 374 374 ASN ASN A . n 
A 1 311 ARG 311 375 375 ARG ARG A . n 
A 1 312 ASN 312 376 376 ASN ASN A . n 
A 1 313 TYR 313 377 377 TYR TYR A . n 
A 1 314 GLN 314 378 378 GLN GLN A . n 
A 1 315 LEU 315 379 379 LEU LEU A . n 
A 1 316 LEU 316 380 380 LEU LEU A . n 
A 1 317 SER 317 381 381 SER SER A . n 
A 1 318 ASN 318 382 382 ASN ASN A . n 
A 1 319 SER 319 383 383 SER SER A . n 
A 1 320 THR 320 384 384 THR THR A . n 
A 1 321 ILE 321 385 385 ILE ILE A . n 
A 1 322 GLY 322 386 386 GLY GLY A . n 
A 1 323 ARG 323 387 387 ARG ARG A . n 
A 1 324 SER 324 388 388 SER SER A . n 
A 1 325 GLY 325 389 389 GLY GLY A . n 
A 1 326 LEU 326 390 390 LEU LEU A . n 
A 1 327 TYR 327 391 391 TYR TYR A . n 
A 1 328 GLN 328 392 392 GLN GLN A . n 
A 1 329 PRO 329 393 393 PRO PRO A . n 
A 1 330 ALA 330 394 394 ALA ALA A . n 
A 1 331 TYR 331 395 395 TYR TYR A . n 
A 1 332 GLU 332 396 396 GLU GLU A . n 
A 1 333 SER 333 397 397 SER SER A . n 
A 1 334 ARG 334 398 398 ARG ARG A . n 
A 1 335 ASP 335 399 399 ASP ASP A . n 
A 1 336 CYS 336 400 400 CYS CYS A . n 
A 1 337 GLN 337 401 401 GLN GLN A . n 
A 1 338 GLU 338 402 402 GLU GLU A . n 
A 1 339 LEU 339 403 403 LEU LEU A . n 
A 1 340 CYS 340 404 404 CYS CYS A . n 
A 1 341 PHE 341 405 405 PHE PHE A . n 
A 1 342 TRP 342 406 406 TRP TRP A . n 
A 1 343 ILE 343 407 407 ILE ILE A . n 
A 1 344 GLU 344 408 408 GLU GLU A . n 
A 1 345 ILE 345 409 409 ILE ILE A . n 
A 1 346 ALA 346 410 410 ALA ALA A . n 
A 1 347 ALA 347 411 411 ALA ALA A . n 
A 1 348 THR 348 412 412 THR THR A . n 
A 1 349 THR 349 413 413 THR THR A . n 
A 1 350 LYS 350 414 414 LYS LYS A . n 
A 1 351 ALA 351 415 415 ALA ALA A . n 
A 1 352 GLY 352 416 416 GLY GLY A . n 
A 1 353 LEU 353 417 417 LEU LEU A . n 
A 1 354 SER 354 418 418 SER SER A . n 
A 1 355 SER 355 419 419 SER SER A . n 
A 1 356 ASN 356 420 420 ASN ASN A . n 
A 1 357 ASP 357 421 421 ASP ASP A . n 
A 1 358 LEU 358 422 422 LEU LEU A . n 
A 1 359 ILE 359 423 423 ILE ILE A . n 
A 1 360 THR 360 424 424 THR THR A . n 
A 1 361 PHE 361 425 425 PHE PHE A . n 
A 1 362 CYS 362 426 426 CYS CYS A . n 
A 1 363 GLY 363 427 427 GLY GLY A . n 
A 1 364 THR 364 428 428 THR THR A . n 
A 1 365 GLY 365 429 429 GLY GLY A . n 
A 1 366 GLY 366 430 430 GLY GLY A . n 
A 1 367 SER 367 431 431 SER SER A . n 
A 1 368 MET 368 432 432 MET MET A . n 
A 1 369 PRO 369 433 433 PRO PRO A . n 
A 1 370 ASP 370 434 434 ASP ASP A . n 
A 1 371 VAL 371 435 435 VAL VAL A . n 
A 1 372 ASN 372 436 436 ASN ASN A . n 
A 1 373 TRP 373 437 437 TRP TRP A . n 
A 1 374 GLY 374 438 ?   ?   ?   A . n 
B 1 1   GLY 1   65  ?   ?   ?   B . n 
B 1 2   SER 2   66  ?   ?   ?   B . n 
B 1 3   GLY 3   67  ?   ?   ?   B . n 
B 1 4   ASP 4   68  ?   ?   ?   B . n 
B 1 5   SER 5   69  ?   ?   ?   B . n 
B 1 6   GLY 6   70  ?   ?   ?   B . n 
B 1 7   SER 7   71  ?   ?   ?   B . n 
B 1 8   PRO 8   72  ?   ?   ?   B . n 
B 1 9   GLY 9   73  ?   ?   ?   B . n 
B 1 10  ILE 10  74  ?   ?   ?   B . n 
B 1 11  ALA 11  75  75  ALA ALA B . n 
B 1 12  THR 12  76  76  THR THR B . n 
B 1 13  PRO 13  77  77  PRO PRO B . n 
B 1 14  LEU 14  78  78  LEU LEU B . n 
B 1 15  VAL 15  79  79  VAL VAL B . n 
B 1 16  LEU 16  80  80  LEU LEU B . n 
B 1 17  GLY 17  81  81  GLY GLY B . n 
B 1 18  GLU 18  82  82  GLU GLU B . n 
B 1 19  ASN 19  83  83  ASN ASN B . n 
B 1 20  LEU 20  84  84  LEU LEU B . n 
B 1 21  CYS 21  85  85  CYS CYS B . n 
B 1 22  SER 22  86  86  SER SER B . n 
B 1 23  ILE 23  87  87  ILE ILE B . n 
B 1 24  ASN 24  88  88  ASN ASN B . n 
B 1 25  GLY 25  89  89  GLY GLY B . n 
B 1 26  TRP 26  90  90  TRP TRP B . n 
B 1 27  VAL 27  91  91  VAL VAL B . n 
B 1 28  PRO 28  92  92  PRO PRO B . n 
B 1 29  THR 29  93  93  THR THR B . n 
B 1 30  TYR 30  94  94  TYR TYR B . n 
B 1 31  ARG 31  95  95  ARG ARG B . n 
B 1 32  GLY 32  96  96  GLY GLY B . n 
B 1 33  GLU 33  97  97  GLU GLU B . n 
B 1 34  GLY 34  98  98  GLY GLY B . n 
B 1 35  THR 35  99  99  THR THR B . n 
B 1 36  THR 36  100 100 THR THR B . n 
B 1 37  GLY 37  101 101 GLY GLY B . n 
B 1 38  LYS 38  102 102 LYS LYS B . n 
B 1 39  ILE 39  103 103 ILE ILE B . n 
B 1 40  PRO 40  104 104 PRO PRO B . n 
B 1 41  ASP 41  105 105 ASP ASP B . n 
B 1 42  GLU 42  106 106 GLU GLU B . n 
B 1 43  GLN 43  107 107 GLN GLN B . n 
B 1 44  MET 44  108 108 MET MET B . n 
B 1 45  LEU 45  109 109 LEU LEU B . n 
B 1 46  THR 46  110 110 THR THR B . n 
B 1 47  ARG 47  111 111 ARG ARG B . n 
B 1 48  GLN 48  112 112 GLN GLN B . n 
B 1 49  ASN 49  113 113 ASN ASN B . n 
B 1 50  PHE 50  114 114 PHE PHE B . n 
B 1 51  VAL 51  115 115 VAL VAL B . n 
B 1 52  SER 52  116 116 SER SER B . n 
B 1 53  CYS 53  117 117 CYS CYS B . n 
B 1 54  SER 54  118 118 SER SER B . n 
B 1 55  ASP 55  119 119 ASP ASP B . n 
B 1 56  LYS 56  120 120 LYS LYS B . n 
B 1 57  GLU 57  121 121 GLU GLU B . n 
B 1 58  CYS 58  122 122 CYS CYS B . n 
B 1 59  ARG 59  123 123 ARG ARG B . n 
B 1 60  ARG 60  124 124 ARG ARG B . n 
B 1 61  PHE 61  125 125 PHE PHE B . n 
B 1 62  PHE 62  126 126 PHE PHE B . n 
B 1 63  VAL 63  127 127 VAL VAL B . n 
B 1 64  SER 64  128 128 SER SER B . n 
B 1 65  MET 65  129 129 MET MET B . n 
B 1 66  GLY 66  130 130 GLY GLY B . n 
B 1 67  TYR 67  131 131 TYR TYR B . n 
B 1 68  GLY 68  132 132 GLY GLY B . n 
B 1 69  THR 69  133 133 THR THR B . n 
B 1 70  THR 70  134 134 THR THR B . n 
B 1 71  THR 71  135 135 THR THR B . n 
B 1 72  ASN 72  136 136 ASN ASN B . n 
B 1 73  PHE 73  137 137 PHE PHE B . n 
B 1 74  ALA 74  138 138 ALA ALA B . n 
B 1 75  ASP 75  139 139 ASP ASP B . n 
B 1 76  LEU 76  140 140 LEU LEU B . n 
B 1 77  ILE 77  141 141 ILE ILE B . n 
B 1 78  VAL 78  142 142 VAL VAL B . n 
B 1 79  SER 79  143 143 SER SER B . n 
B 1 80  GLU 80  144 144 GLU GLU B . n 
B 1 81  GLN 81  145 145 GLN GLN B . n 
B 1 82  MET 82  146 146 MET MET B . n 
B 1 83  ASN 83  147 147 ASN ASN B . n 
B 1 84  VAL 84  148 148 VAL VAL B . n 
B 1 85  TYR 85  149 149 TYR TYR B . n 
B 1 86  SER 86  150 150 SER SER B . n 
B 1 87  VAL 87  151 151 VAL VAL B . n 
B 1 88  LYS 88  152 152 LYS LYS B . n 
B 1 89  LEU 89  153 153 LEU LEU B . n 
B 1 90  GLY 90  154 154 GLY GLY B . n 
B 1 91  ASP 91  155 155 ASP ASP B . n 
B 1 92  PRO 92  156 156 PRO PRO B . n 
B 1 93  PRO 93  157 157 PRO PRO B . n 
B 1 94  THR 94  158 158 THR THR B . n 
B 1 95  PRO 95  159 159 PRO PRO B . n 
B 1 96  ASP 96  160 160 ASP ASP B . n 
B 1 97  LYS 97  161 161 LYS LYS B . n 
B 1 98  LEU 98  162 162 LEU LEU B . n 
B 1 99  LYS 99  163 163 LYS LYS B . n 
B 1 100 PHE 100 164 164 PHE PHE B . n 
B 1 101 GLU 101 165 165 GLU GLU B . n 
B 1 102 ALA 102 166 166 ALA ALA B . n 
B 1 103 VAL 103 167 167 VAL VAL B . n 
B 1 104 GLY 104 168 168 GLY GLY B . n 
B 1 105 TRP 105 169 169 TRP TRP B . n 
B 1 106 SER 106 170 170 SER SER B . n 
B 1 107 ALA 107 171 171 ALA ALA B . n 
B 1 108 SER 108 172 172 SER SER B . n 
B 1 109 SER 109 173 173 SER SER B . n 
B 1 110 CYS 110 174 174 CYS CYS B . n 
B 1 111 HIS 111 175 175 HIS HIS B . n 
B 1 112 ASP 112 176 176 ASP ASP B . n 
B 1 113 GLY 113 177 177 GLY GLY B . n 
B 1 114 PHE 114 178 178 PHE PHE B . n 
B 1 115 GLN 115 179 179 GLN GLN B . n 
B 1 116 TRP 116 180 180 TRP TRP B . n 
B 1 117 THR 117 181 181 THR THR B . n 
B 1 118 VAL 118 182 182 VAL VAL B . n 
B 1 119 LEU 119 183 183 LEU LEU B . n 
B 1 120 SER 120 184 184 SER SER B . n 
B 1 121 VAL 121 185 185 VAL VAL B . n 
B 1 122 ALA 122 186 186 ALA ALA B . n 
B 1 123 GLY 123 187 187 GLY GLY B . n 
B 1 124 ASP 124 188 188 ASP ASP B . n 
B 1 125 GLY 125 189 189 GLY GLY B . n 
B 1 126 PHE 126 190 190 PHE PHE B . n 
B 1 127 VAL 127 191 191 VAL VAL B . n 
B 1 128 SER 128 192 192 SER SER B . n 
B 1 129 ILE 129 193 193 ILE ILE B . n 
B 1 130 LEU 130 194 194 LEU LEU B . n 
B 1 131 TYR 131 195 195 TYR TYR B . n 
B 1 132 GLY 132 196 196 GLY GLY B . n 
B 1 133 GLY 133 197 197 GLY GLY B . n 
B 1 134 ILE 134 198 198 ILE ILE B . n 
B 1 135 ILE 135 199 199 ILE ILE B . n 
B 1 136 THR 136 200 200 THR THR B . n 
B 1 137 ASP 137 201 201 ASP ASP B . n 
B 1 138 THR 138 202 202 THR THR B . n 
B 1 139 ILE 139 203 203 ILE ILE B . n 
B 1 140 HIS 140 204 204 HIS HIS B . n 
B 1 141 PRO 141 205 205 PRO PRO B . n 
B 1 142 THR 142 206 206 THR THR B . n 
B 1 143 ASN 143 207 207 ASN ASN B . n 
B 1 144 GLY 144 208 208 GLY GLY B . n 
B 1 145 GLY 145 209 209 GLY GLY B . n 
B 1 146 PRO 146 210 210 PRO PRO B . n 
B 1 147 LEU 147 211 211 LEU LEU B . n 
B 1 148 ARG 148 212 212 ARG ARG B . n 
B 1 149 THR 149 213 213 THR THR B . n 
B 1 150 GLN 150 214 214 GLN GLN B . n 
B 1 151 ALA 151 215 215 ALA ALA B . n 
B 1 152 SER 152 216 216 SER SER B . n 
B 1 153 SER 153 217 217 SER SER B . n 
B 1 154 CYS 154 218 218 CYS CYS B . n 
B 1 155 ILE 155 219 219 ILE ILE B . n 
B 1 156 CYS 156 220 220 CYS CYS B . n 
B 1 157 ASN 157 221 221 ASN ASN B . n 
B 1 158 ASP 158 222 222 ASP ASP B . n 
B 1 159 GLY 159 223 223 GLY GLY B . n 
B 1 160 THR 160 224 224 THR THR B . n 
B 1 161 CYS 161 225 225 CYS CYS B . n 
B 1 162 TYR 162 226 226 TYR TYR B . n 
B 1 163 THR 163 227 227 THR THR B . n 
B 1 164 ILE 164 228 228 ILE ILE B . n 
B 1 165 ILE 165 229 229 ILE ILE B . n 
B 1 166 ALA 166 230 230 ALA ALA B . n 
B 1 167 ASP 167 231 231 ASP ASP B . n 
B 1 168 GLY 168 232 232 GLY GLY B . n 
B 1 169 THR 169 233 233 THR THR B . n 
B 1 170 THR 170 234 234 THR THR B . n 
B 1 171 TYR 171 235 235 TYR TYR B . n 
B 1 172 THR 172 236 236 THR THR B . n 
B 1 173 ALA 173 237 237 ALA ALA B . n 
B 1 174 SER 174 238 238 SER SER B . n 
B 1 175 SER 175 239 239 SER SER B . n 
B 1 176 HIS 176 240 240 HIS HIS B . n 
B 1 177 ARG 177 241 241 ARG ARG B . n 
B 1 178 LEU 178 242 242 LEU LEU B . n 
B 1 179 TYR 179 243 243 TYR TYR B . n 
B 1 180 ARG 180 244 244 ARG ARG B . n 
B 1 181 LEU 181 245 245 LEU LEU B . n 
B 1 182 VAL 182 246 246 VAL VAL B . n 
B 1 183 ASN 183 247 247 ASN ASN B . n 
B 1 184 GLY 184 248 248 GLY GLY B . n 
B 1 185 THR 185 249 249 THR THR B . n 
B 1 186 SER 186 250 250 SER SER B . n 
B 1 187 ALA 187 251 251 ALA ALA B . n 
B 1 188 GLY 188 252 252 GLY GLY B . n 
B 1 189 TRP 189 253 253 TRP TRP B . n 
B 1 190 LYS 190 254 254 LYS LYS B . n 
B 1 191 ALA 191 255 255 ALA ALA B . n 
B 1 192 LEU 192 256 256 LEU LEU B . n 
B 1 193 ASP 193 257 257 ASP ASP B . n 
B 1 194 THR 194 258 258 THR THR B . n 
B 1 195 THR 195 259 259 THR THR B . n 
B 1 196 GLY 196 260 260 GLY GLY B . n 
B 1 197 PHE 197 261 261 PHE PHE B . n 
B 1 198 ASN 198 262 262 ASN ASN B . n 
B 1 199 PHE 199 263 263 PHE PHE B . n 
B 1 200 GLU 200 264 264 GLU GLU B . n 
B 1 201 PHE 201 265 265 PHE PHE B . n 
B 1 202 PRO 202 266 266 PRO PRO B . n 
B 1 203 THR 203 267 267 THR THR B . n 
B 1 204 CYS 204 268 268 CYS CYS B . n 
B 1 205 TYR 205 269 269 TYR TYR B . n 
B 1 206 TYR 206 270 270 TYR TYR B . n 
B 1 207 THR 207 271 271 THR THR B . n 
B 1 208 SER 208 272 272 SER SER B . n 
B 1 209 GLY 209 273 273 GLY GLY B . n 
B 1 210 LYS 210 274 274 LYS LYS B . n 
B 1 211 VAL 211 275 275 VAL VAL B . n 
B 1 212 LYS 212 276 276 LYS LYS B . n 
B 1 213 CYS 213 277 277 CYS CYS B . n 
B 1 214 THR 214 278 278 THR THR B . n 
B 1 215 GLY 215 279 279 GLY GLY B . n 
B 1 216 THR 216 280 280 THR THR B . n 
B 1 217 ASN 217 281 281 ASN ASN B . n 
B 1 218 LEU 218 282 282 LEU LEU B . n 
B 1 219 TRP 219 283 283 TRP TRP B . n 
B 1 220 ASN 220 284 284 ASN ASN B . n 
B 1 221 ASP 221 285 285 ASP ASP B . n 
B 1 222 ALA 222 286 286 ALA ALA B . n 
B 1 223 LYS 223 287 287 LYS LYS B . n 
B 1 224 ARG 224 288 288 ARG ARG B . n 
B 1 225 PRO 225 289 289 PRO PRO B . n 
B 1 226 PHE 226 290 290 PHE PHE B . n 
B 1 227 LEU 227 291 291 LEU LEU B . n 
B 1 228 GLU 228 292 292 GLU GLU B . n 
B 1 229 PHE 229 293 293 PHE PHE B . n 
B 1 230 ASP 230 294 294 ASP ASP B . n 
B 1 231 GLN 231 295 295 GLN GLN B . n 
B 1 232 SER 232 296 296 SER SER B . n 
B 1 233 PHE 233 297 297 PHE PHE B . n 
B 1 234 THR 234 298 298 THR THR B . n 
B 1 235 TYR 235 299 299 TYR TYR B . n 
B 1 236 THR 236 300 300 THR THR B . n 
B 1 237 PHE 237 301 301 PHE PHE B . n 
B 1 238 LYS 238 302 302 LYS LYS B . n 
B 1 239 GLU 239 303 303 GLU GLU B . n 
B 1 240 PRO 240 304 304 PRO PRO B . n 
B 1 241 CYS 241 305 305 CYS CYS B . n 
B 1 242 LEU 242 306 306 LEU LEU B . n 
B 1 243 GLY 243 307 307 GLY GLY B . n 
B 1 244 PHE 244 308 308 PHE PHE B . n 
B 1 245 LEU 245 309 309 LEU LEU B . n 
B 1 246 GLY 246 310 310 GLY GLY B . n 
B 1 247 ASP 247 311 311 ASP ASP B . n 
B 1 248 THR 248 312 312 THR THR B . n 
B 1 249 PRO 249 313 313 PRO PRO B . n 
B 1 250 ARG 250 314 314 ARG ARG B . n 
B 1 251 GLY 251 315 315 GLY GLY B . n 
B 1 252 ILE 252 316 316 ILE ILE B . n 
B 1 253 ASP 253 317 317 ASP ASP B . n 
B 1 254 THR 254 318 318 THR THR B . n 
B 1 255 THR 255 319 319 THR THR B . n 
B 1 256 ASN 256 320 320 ASN ASN B . n 
B 1 257 TYR 257 321 321 TYR TYR B . n 
B 1 258 CYS 258 322 322 CYS CYS B . n 
B 1 259 ASP 259 323 323 ASP ASP B . n 
B 1 260 LYS 260 324 324 LYS LYS B . n 
B 1 261 THR 261 325 325 THR THR B . n 
B 1 262 THR 262 326 326 THR THR B . n 
B 1 263 THR 263 327 327 THR THR B . n 
B 1 264 GLU 264 328 328 GLU GLU B . n 
B 1 265 GLY 265 329 329 GLY GLY B . n 
B 1 266 GLU 266 330 330 GLU GLU B . n 
B 1 267 GLY 267 331 331 GLY GLY B . n 
B 1 268 GLY 268 332 332 GLY GLY B . n 
B 1 269 ILE 269 333 333 ILE ILE B . n 
B 1 270 GLN 270 334 334 GLN GLN B . n 
B 1 271 GLY 271 335 335 GLY GLY B . n 
B 1 272 PHE 272 336 336 PHE PHE B . n 
B 1 273 MET 273 337 337 MET MET B . n 
B 1 274 ILE 274 338 338 ILE ILE B . n 
B 1 275 GLU 275 339 339 GLU GLU B . n 
B 1 276 GLY 276 340 340 GLY GLY B . n 
B 1 277 SER 277 341 341 SER SER B . n 
B 1 278 ASN 278 342 342 ASN ASN B . n 
B 1 279 SER 279 343 343 SER SER B . n 
B 1 280 TRP 280 344 344 TRP TRP B . n 
B 1 281 ILE 281 345 345 ILE ILE B . n 
B 1 282 GLY 282 346 346 GLY GLY B . n 
B 1 283 ARG 283 347 347 ARG ARG B . n 
B 1 284 ILE 284 348 348 ILE ILE B . n 
B 1 285 ILE 285 349 349 ILE ILE B . n 
B 1 286 ASN 286 350 350 ASN ASN B . n 
B 1 287 PRO 287 351 351 PRO PRO B . n 
B 1 288 GLY 288 352 352 GLY GLY B . n 
B 1 289 SER 289 353 353 SER SER B . n 
B 1 290 LYS 290 354 354 LYS LYS B . n 
B 1 291 LYS 291 355 355 LYS LYS B . n 
B 1 292 GLY 292 356 356 GLY GLY B . n 
B 1 293 PHE 293 357 357 PHE PHE B . n 
B 1 294 GLU 294 358 358 GLU GLU B . n 
B 1 295 ILE 295 359 359 ILE ILE B . n 
B 1 296 TYR 296 360 360 TYR TYR B . n 
B 1 297 LYS 297 361 361 LYS LYS B . n 
B 1 298 PHE 298 362 362 PHE PHE B . n 
B 1 299 LEU 299 363 363 LEU LEU B . n 
B 1 300 GLY 300 364 364 GLY GLY B . n 
B 1 301 THR 301 365 365 THR THR B . n 
B 1 302 LEU 302 366 366 LEU LEU B . n 
B 1 303 PHE 303 367 367 PHE PHE B . n 
B 1 304 SER 304 368 368 SER SER B . n 
B 1 305 VAL 305 369 369 VAL VAL B . n 
B 1 306 GLN 306 370 370 GLN GLN B . n 
B 1 307 THR 307 371 371 THR THR B . n 
B 1 308 VAL 308 372 372 VAL VAL B . n 
B 1 309 GLY 309 373 373 GLY GLY B . n 
B 1 310 ASN 310 374 374 ASN ASN B . n 
B 1 311 ARG 311 375 375 ARG ARG B . n 
B 1 312 ASN 312 376 376 ASN ASN B . n 
B 1 313 TYR 313 377 377 TYR TYR B . n 
B 1 314 GLN 314 378 378 GLN GLN B . n 
B 1 315 LEU 315 379 379 LEU LEU B . n 
B 1 316 LEU 316 380 380 LEU LEU B . n 
B 1 317 SER 317 381 381 SER SER B . n 
B 1 318 ASN 318 382 382 ASN ASN B . n 
B 1 319 SER 319 383 383 SER SER B . n 
B 1 320 THR 320 384 384 THR THR B . n 
B 1 321 ILE 321 385 385 ILE ILE B . n 
B 1 322 GLY 322 386 386 GLY GLY B . n 
B 1 323 ARG 323 387 387 ARG ARG B . n 
B 1 324 SER 324 388 388 SER SER B . n 
B 1 325 GLY 325 389 389 GLY GLY B . n 
B 1 326 LEU 326 390 390 LEU LEU B . n 
B 1 327 TYR 327 391 391 TYR TYR B . n 
B 1 328 GLN 328 392 392 GLN GLN B . n 
B 1 329 PRO 329 393 393 PRO PRO B . n 
B 1 330 ALA 330 394 394 ALA ALA B . n 
B 1 331 TYR 331 395 395 TYR TYR B . n 
B 1 332 GLU 332 396 396 GLU GLU B . n 
B 1 333 SER 333 397 397 SER SER B . n 
B 1 334 ARG 334 398 398 ARG ARG B . n 
B 1 335 ASP 335 399 399 ASP ASP B . n 
B 1 336 CYS 336 400 400 CYS CYS B . n 
B 1 337 GLN 337 401 401 GLN GLN B . n 
B 1 338 GLU 338 402 402 GLU GLU B . n 
B 1 339 LEU 339 403 403 LEU LEU B . n 
B 1 340 CYS 340 404 404 CYS CYS B . n 
B 1 341 PHE 341 405 405 PHE PHE B . n 
B 1 342 TRP 342 406 406 TRP TRP B . n 
B 1 343 ILE 343 407 407 ILE ILE B . n 
B 1 344 GLU 344 408 408 GLU GLU B . n 
B 1 345 ILE 345 409 409 ILE ILE B . n 
B 1 346 ALA 346 410 410 ALA ALA B . n 
B 1 347 ALA 347 411 411 ALA ALA B . n 
B 1 348 THR 348 412 412 THR THR B . n 
B 1 349 THR 349 413 413 THR THR B . n 
B 1 350 LYS 350 414 414 LYS LYS B . n 
B 1 351 ALA 351 415 415 ALA ALA B . n 
B 1 352 GLY 352 416 416 GLY GLY B . n 
B 1 353 LEU 353 417 417 LEU LEU B . n 
B 1 354 SER 354 418 418 SER SER B . n 
B 1 355 SER 355 419 419 SER SER B . n 
B 1 356 ASN 356 420 420 ASN ASN B . n 
B 1 357 ASP 357 421 421 ASP ASP B . n 
B 1 358 LEU 358 422 422 LEU LEU B . n 
B 1 359 ILE 359 423 423 ILE ILE B . n 
B 1 360 THR 360 424 424 THR THR B . n 
B 1 361 PHE 361 425 425 PHE PHE B . n 
B 1 362 CYS 362 426 426 CYS CYS B . n 
B 1 363 GLY 363 427 427 GLY GLY B . n 
B 1 364 THR 364 428 428 THR THR B . n 
B 1 365 GLY 365 429 429 GLY GLY B . n 
B 1 366 GLY 366 430 430 GLY GLY B . n 
B 1 367 SER 367 431 431 SER SER B . n 
B 1 368 MET 368 432 432 MET MET B . n 
B 1 369 PRO 369 433 433 PRO PRO B . n 
B 1 370 ASP 370 434 434 ASP ASP B . n 
B 1 371 VAL 371 435 435 VAL VAL B . n 
B 1 372 ASN 372 436 436 ASN ASN B . n 
B 1 373 TRP 373 437 437 TRP TRP B . n 
B 1 374 GLY 374 438 ?   ?   ?   B . n 
C 1 1   GLY 1   65  ?   ?   ?   C . n 
C 1 2   SER 2   66  ?   ?   ?   C . n 
C 1 3   GLY 3   67  ?   ?   ?   C . n 
C 1 4   ASP 4   68  ?   ?   ?   C . n 
C 1 5   SER 5   69  ?   ?   ?   C . n 
C 1 6   GLY 6   70  ?   ?   ?   C . n 
C 1 7   SER 7   71  ?   ?   ?   C . n 
C 1 8   PRO 8   72  ?   ?   ?   C . n 
C 1 9   GLY 9   73  ?   ?   ?   C . n 
C 1 10  ILE 10  74  ?   ?   ?   C . n 
C 1 11  ALA 11  75  75  ALA ALA C . n 
C 1 12  THR 12  76  76  THR THR C . n 
C 1 13  PRO 13  77  77  PRO PRO C . n 
C 1 14  LEU 14  78  78  LEU LEU C . n 
C 1 15  VAL 15  79  79  VAL VAL C . n 
C 1 16  LEU 16  80  80  LEU LEU C . n 
C 1 17  GLY 17  81  81  GLY GLY C . n 
C 1 18  GLU 18  82  82  GLU GLU C . n 
C 1 19  ASN 19  83  83  ASN ASN C . n 
C 1 20  LEU 20  84  84  LEU LEU C . n 
C 1 21  CYS 21  85  85  CYS CYS C . n 
C 1 22  SER 22  86  86  SER SER C . n 
C 1 23  ILE 23  87  87  ILE ILE C . n 
C 1 24  ASN 24  88  88  ASN ASN C . n 
C 1 25  GLY 25  89  89  GLY GLY C . n 
C 1 26  TRP 26  90  90  TRP TRP C . n 
C 1 27  VAL 27  91  91  VAL VAL C . n 
C 1 28  PRO 28  92  92  PRO PRO C . n 
C 1 29  THR 29  93  93  THR THR C . n 
C 1 30  TYR 30  94  94  TYR TYR C . n 
C 1 31  ARG 31  95  95  ARG ARG C . n 
C 1 32  GLY 32  96  96  GLY GLY C . n 
C 1 33  GLU 33  97  97  GLU GLU C . n 
C 1 34  GLY 34  98  98  GLY GLY C . n 
C 1 35  THR 35  99  99  THR THR C . n 
C 1 36  THR 36  100 100 THR THR C . n 
C 1 37  GLY 37  101 101 GLY GLY C . n 
C 1 38  LYS 38  102 102 LYS LYS C . n 
C 1 39  ILE 39  103 103 ILE ILE C . n 
C 1 40  PRO 40  104 104 PRO PRO C . n 
C 1 41  ASP 41  105 105 ASP ASP C . n 
C 1 42  GLU 42  106 106 GLU GLU C . n 
C 1 43  GLN 43  107 107 GLN GLN C . n 
C 1 44  MET 44  108 108 MET MET C . n 
C 1 45  LEU 45  109 109 LEU LEU C . n 
C 1 46  THR 46  110 110 THR THR C . n 
C 1 47  ARG 47  111 111 ARG ARG C . n 
C 1 48  GLN 48  112 112 GLN GLN C . n 
C 1 49  ASN 49  113 113 ASN ASN C . n 
C 1 50  PHE 50  114 114 PHE PHE C . n 
C 1 51  VAL 51  115 115 VAL VAL C . n 
C 1 52  SER 52  116 116 SER SER C . n 
C 1 53  CYS 53  117 117 CYS CYS C . n 
C 1 54  SER 54  118 118 SER SER C . n 
C 1 55  ASP 55  119 119 ASP ASP C . n 
C 1 56  LYS 56  120 120 LYS LYS C . n 
C 1 57  GLU 57  121 121 GLU GLU C . n 
C 1 58  CYS 58  122 122 CYS CYS C . n 
C 1 59  ARG 59  123 123 ARG ARG C . n 
C 1 60  ARG 60  124 124 ARG ARG C . n 
C 1 61  PHE 61  125 125 PHE PHE C . n 
C 1 62  PHE 62  126 126 PHE PHE C . n 
C 1 63  VAL 63  127 127 VAL VAL C . n 
C 1 64  SER 64  128 128 SER SER C . n 
C 1 65  MET 65  129 129 MET MET C . n 
C 1 66  GLY 66  130 130 GLY GLY C . n 
C 1 67  TYR 67  131 131 TYR TYR C . n 
C 1 68  GLY 68  132 132 GLY GLY C . n 
C 1 69  THR 69  133 133 THR THR C . n 
C 1 70  THR 70  134 134 THR THR C . n 
C 1 71  THR 71  135 135 THR THR C . n 
C 1 72  ASN 72  136 136 ASN ASN C . n 
C 1 73  PHE 73  137 137 PHE PHE C . n 
C 1 74  ALA 74  138 138 ALA ALA C . n 
C 1 75  ASP 75  139 139 ASP ASP C . n 
C 1 76  LEU 76  140 140 LEU LEU C . n 
C 1 77  ILE 77  141 141 ILE ILE C . n 
C 1 78  VAL 78  142 142 VAL VAL C . n 
C 1 79  SER 79  143 143 SER SER C . n 
C 1 80  GLU 80  144 144 GLU GLU C . n 
C 1 81  GLN 81  145 145 GLN GLN C . n 
C 1 82  MET 82  146 146 MET MET C . n 
C 1 83  ASN 83  147 147 ASN ASN C . n 
C 1 84  VAL 84  148 148 VAL VAL C . n 
C 1 85  TYR 85  149 149 TYR TYR C . n 
C 1 86  SER 86  150 150 SER SER C . n 
C 1 87  VAL 87  151 151 VAL VAL C . n 
C 1 88  LYS 88  152 152 LYS LYS C . n 
C 1 89  LEU 89  153 153 LEU LEU C . n 
C 1 90  GLY 90  154 154 GLY GLY C . n 
C 1 91  ASP 91  155 155 ASP ASP C . n 
C 1 92  PRO 92  156 156 PRO PRO C . n 
C 1 93  PRO 93  157 157 PRO PRO C . n 
C 1 94  THR 94  158 158 THR THR C . n 
C 1 95  PRO 95  159 159 PRO PRO C . n 
C 1 96  ASP 96  160 160 ASP ASP C . n 
C 1 97  LYS 97  161 161 LYS LYS C . n 
C 1 98  LEU 98  162 162 LEU LEU C . n 
C 1 99  LYS 99  163 163 LYS LYS C . n 
C 1 100 PHE 100 164 164 PHE PHE C . n 
C 1 101 GLU 101 165 165 GLU GLU C . n 
C 1 102 ALA 102 166 166 ALA ALA C . n 
C 1 103 VAL 103 167 167 VAL VAL C . n 
C 1 104 GLY 104 168 168 GLY GLY C . n 
C 1 105 TRP 105 169 169 TRP TRP C . n 
C 1 106 SER 106 170 170 SER SER C . n 
C 1 107 ALA 107 171 171 ALA ALA C . n 
C 1 108 SER 108 172 172 SER SER C . n 
C 1 109 SER 109 173 173 SER SER C . n 
C 1 110 CYS 110 174 174 CYS CYS C . n 
C 1 111 HIS 111 175 175 HIS HIS C . n 
C 1 112 ASP 112 176 176 ASP ASP C . n 
C 1 113 GLY 113 177 177 GLY GLY C . n 
C 1 114 PHE 114 178 178 PHE PHE C . n 
C 1 115 GLN 115 179 179 GLN GLN C . n 
C 1 116 TRP 116 180 180 TRP TRP C . n 
C 1 117 THR 117 181 181 THR THR C . n 
C 1 118 VAL 118 182 182 VAL VAL C . n 
C 1 119 LEU 119 183 183 LEU LEU C . n 
C 1 120 SER 120 184 184 SER SER C . n 
C 1 121 VAL 121 185 185 VAL VAL C . n 
C 1 122 ALA 122 186 186 ALA ALA C . n 
C 1 123 GLY 123 187 187 GLY GLY C . n 
C 1 124 ASP 124 188 188 ASP ASP C . n 
C 1 125 GLY 125 189 189 GLY GLY C . n 
C 1 126 PHE 126 190 190 PHE PHE C . n 
C 1 127 VAL 127 191 191 VAL VAL C . n 
C 1 128 SER 128 192 192 SER SER C . n 
C 1 129 ILE 129 193 193 ILE ILE C . n 
C 1 130 LEU 130 194 194 LEU LEU C . n 
C 1 131 TYR 131 195 195 TYR TYR C . n 
C 1 132 GLY 132 196 196 GLY GLY C . n 
C 1 133 GLY 133 197 197 GLY GLY C . n 
C 1 134 ILE 134 198 198 ILE ILE C . n 
C 1 135 ILE 135 199 199 ILE ILE C . n 
C 1 136 THR 136 200 200 THR THR C . n 
C 1 137 ASP 137 201 201 ASP ASP C . n 
C 1 138 THR 138 202 202 THR THR C . n 
C 1 139 ILE 139 203 203 ILE ILE C . n 
C 1 140 HIS 140 204 204 HIS HIS C . n 
C 1 141 PRO 141 205 205 PRO PRO C . n 
C 1 142 THR 142 206 206 THR THR C . n 
C 1 143 ASN 143 207 207 ASN ASN C . n 
C 1 144 GLY 144 208 208 GLY GLY C . n 
C 1 145 GLY 145 209 209 GLY GLY C . n 
C 1 146 PRO 146 210 210 PRO PRO C . n 
C 1 147 LEU 147 211 211 LEU LEU C . n 
C 1 148 ARG 148 212 212 ARG ARG C . n 
C 1 149 THR 149 213 213 THR THR C . n 
C 1 150 GLN 150 214 214 GLN GLN C . n 
C 1 151 ALA 151 215 215 ALA ALA C . n 
C 1 152 SER 152 216 216 SER SER C . n 
C 1 153 SER 153 217 217 SER SER C . n 
C 1 154 CYS 154 218 218 CYS CYS C . n 
C 1 155 ILE 155 219 219 ILE ILE C . n 
C 1 156 CYS 156 220 220 CYS CYS C . n 
C 1 157 ASN 157 221 221 ASN ASN C . n 
C 1 158 ASP 158 222 222 ASP ASP C . n 
C 1 159 GLY 159 223 223 GLY GLY C . n 
C 1 160 THR 160 224 224 THR THR C . n 
C 1 161 CYS 161 225 225 CYS CYS C . n 
C 1 162 TYR 162 226 226 TYR TYR C . n 
C 1 163 THR 163 227 227 THR THR C . n 
C 1 164 ILE 164 228 228 ILE ILE C . n 
C 1 165 ILE 165 229 229 ILE ILE C . n 
C 1 166 ALA 166 230 230 ALA ALA C . n 
C 1 167 ASP 167 231 231 ASP ASP C . n 
C 1 168 GLY 168 232 232 GLY GLY C . n 
C 1 169 THR 169 233 233 THR THR C . n 
C 1 170 THR 170 234 234 THR THR C . n 
C 1 171 TYR 171 235 235 TYR TYR C . n 
C 1 172 THR 172 236 236 THR THR C . n 
C 1 173 ALA 173 237 237 ALA ALA C . n 
C 1 174 SER 174 238 238 SER SER C . n 
C 1 175 SER 175 239 239 SER SER C . n 
C 1 176 HIS 176 240 240 HIS HIS C . n 
C 1 177 ARG 177 241 241 ARG ARG C . n 
C 1 178 LEU 178 242 242 LEU LEU C . n 
C 1 179 TYR 179 243 243 TYR TYR C . n 
C 1 180 ARG 180 244 244 ARG ARG C . n 
C 1 181 LEU 181 245 245 LEU LEU C . n 
C 1 182 VAL 182 246 246 VAL VAL C . n 
C 1 183 ASN 183 247 247 ASN ASN C . n 
C 1 184 GLY 184 248 248 GLY GLY C . n 
C 1 185 THR 185 249 249 THR THR C . n 
C 1 186 SER 186 250 250 SER SER C . n 
C 1 187 ALA 187 251 251 ALA ALA C . n 
C 1 188 GLY 188 252 252 GLY GLY C . n 
C 1 189 TRP 189 253 253 TRP TRP C . n 
C 1 190 LYS 190 254 254 LYS LYS C . n 
C 1 191 ALA 191 255 255 ALA ALA C . n 
C 1 192 LEU 192 256 256 LEU LEU C . n 
C 1 193 ASP 193 257 257 ASP ASP C . n 
C 1 194 THR 194 258 258 THR THR C . n 
C 1 195 THR 195 259 259 THR THR C . n 
C 1 196 GLY 196 260 260 GLY GLY C . n 
C 1 197 PHE 197 261 261 PHE PHE C . n 
C 1 198 ASN 198 262 262 ASN ASN C . n 
C 1 199 PHE 199 263 263 PHE PHE C . n 
C 1 200 GLU 200 264 264 GLU GLU C . n 
C 1 201 PHE 201 265 265 PHE PHE C . n 
C 1 202 PRO 202 266 266 PRO PRO C . n 
C 1 203 THR 203 267 267 THR THR C . n 
C 1 204 CYS 204 268 268 CYS CYS C . n 
C 1 205 TYR 205 269 269 TYR TYR C . n 
C 1 206 TYR 206 270 270 TYR TYR C . n 
C 1 207 THR 207 271 271 THR THR C . n 
C 1 208 SER 208 272 272 SER SER C . n 
C 1 209 GLY 209 273 273 GLY GLY C . n 
C 1 210 LYS 210 274 274 LYS LYS C . n 
C 1 211 VAL 211 275 275 VAL VAL C . n 
C 1 212 LYS 212 276 276 LYS LYS C . n 
C 1 213 CYS 213 277 277 CYS CYS C . n 
C 1 214 THR 214 278 278 THR THR C . n 
C 1 215 GLY 215 279 279 GLY GLY C . n 
C 1 216 THR 216 280 280 THR THR C . n 
C 1 217 ASN 217 281 281 ASN ASN C . n 
C 1 218 LEU 218 282 282 LEU LEU C . n 
C 1 219 TRP 219 283 283 TRP TRP C . n 
C 1 220 ASN 220 284 284 ASN ASN C . n 
C 1 221 ASP 221 285 285 ASP ASP C . n 
C 1 222 ALA 222 286 286 ALA ALA C . n 
C 1 223 LYS 223 287 287 LYS LYS C . n 
C 1 224 ARG 224 288 288 ARG ARG C . n 
C 1 225 PRO 225 289 289 PRO PRO C . n 
C 1 226 PHE 226 290 290 PHE PHE C . n 
C 1 227 LEU 227 291 291 LEU LEU C . n 
C 1 228 GLU 228 292 292 GLU GLU C . n 
C 1 229 PHE 229 293 293 PHE PHE C . n 
C 1 230 ASP 230 294 294 ASP ASP C . n 
C 1 231 GLN 231 295 295 GLN GLN C . n 
C 1 232 SER 232 296 296 SER SER C . n 
C 1 233 PHE 233 297 297 PHE PHE C . n 
C 1 234 THR 234 298 298 THR THR C . n 
C 1 235 TYR 235 299 299 TYR TYR C . n 
C 1 236 THR 236 300 300 THR THR C . n 
C 1 237 PHE 237 301 301 PHE PHE C . n 
C 1 238 LYS 238 302 302 LYS LYS C . n 
C 1 239 GLU 239 303 303 GLU GLU C . n 
C 1 240 PRO 240 304 304 PRO PRO C . n 
C 1 241 CYS 241 305 305 CYS CYS C . n 
C 1 242 LEU 242 306 306 LEU LEU C . n 
C 1 243 GLY 243 307 307 GLY GLY C . n 
C 1 244 PHE 244 308 308 PHE PHE C . n 
C 1 245 LEU 245 309 309 LEU LEU C . n 
C 1 246 GLY 246 310 310 GLY GLY C . n 
C 1 247 ASP 247 311 311 ASP ASP C . n 
C 1 248 THR 248 312 312 THR THR C . n 
C 1 249 PRO 249 313 313 PRO PRO C . n 
C 1 250 ARG 250 314 314 ARG ARG C . n 
C 1 251 GLY 251 315 315 GLY GLY C . n 
C 1 252 ILE 252 316 316 ILE ILE C . n 
C 1 253 ASP 253 317 317 ASP ASP C . n 
C 1 254 THR 254 318 318 THR THR C . n 
C 1 255 THR 255 319 319 THR THR C . n 
C 1 256 ASN 256 320 320 ASN ASN C . n 
C 1 257 TYR 257 321 321 TYR TYR C . n 
C 1 258 CYS 258 322 322 CYS CYS C . n 
C 1 259 ASP 259 323 323 ASP ASP C . n 
C 1 260 LYS 260 324 324 LYS LYS C . n 
C 1 261 THR 261 325 325 THR THR C . n 
C 1 262 THR 262 326 326 THR THR C . n 
C 1 263 THR 263 327 327 THR THR C . n 
C 1 264 GLU 264 328 328 GLU GLU C . n 
C 1 265 GLY 265 329 329 GLY GLY C . n 
C 1 266 GLU 266 330 330 GLU GLU C . n 
C 1 267 GLY 267 331 331 GLY GLY C . n 
C 1 268 GLY 268 332 332 GLY GLY C . n 
C 1 269 ILE 269 333 333 ILE ILE C . n 
C 1 270 GLN 270 334 334 GLN GLN C . n 
C 1 271 GLY 271 335 335 GLY GLY C . n 
C 1 272 PHE 272 336 336 PHE PHE C . n 
C 1 273 MET 273 337 337 MET MET C . n 
C 1 274 ILE 274 338 338 ILE ILE C . n 
C 1 275 GLU 275 339 339 GLU GLU C . n 
C 1 276 GLY 276 340 340 GLY GLY C . n 
C 1 277 SER 277 341 341 SER SER C . n 
C 1 278 ASN 278 342 342 ASN ASN C . n 
C 1 279 SER 279 343 343 SER SER C . n 
C 1 280 TRP 280 344 344 TRP TRP C . n 
C 1 281 ILE 281 345 345 ILE ILE C . n 
C 1 282 GLY 282 346 346 GLY GLY C . n 
C 1 283 ARG 283 347 347 ARG ARG C . n 
C 1 284 ILE 284 348 348 ILE ILE C . n 
C 1 285 ILE 285 349 349 ILE ILE C . n 
C 1 286 ASN 286 350 350 ASN ASN C . n 
C 1 287 PRO 287 351 351 PRO PRO C . n 
C 1 288 GLY 288 352 352 GLY GLY C . n 
C 1 289 SER 289 353 353 SER SER C . n 
C 1 290 LYS 290 354 354 LYS LYS C . n 
C 1 291 LYS 291 355 355 LYS LYS C . n 
C 1 292 GLY 292 356 356 GLY GLY C . n 
C 1 293 PHE 293 357 357 PHE PHE C . n 
C 1 294 GLU 294 358 358 GLU GLU C . n 
C 1 295 ILE 295 359 359 ILE ILE C . n 
C 1 296 TYR 296 360 360 TYR TYR C . n 
C 1 297 LYS 297 361 361 LYS LYS C . n 
C 1 298 PHE 298 362 362 PHE PHE C . n 
C 1 299 LEU 299 363 363 LEU LEU C . n 
C 1 300 GLY 300 364 364 GLY GLY C . n 
C 1 301 THR 301 365 365 THR THR C . n 
C 1 302 LEU 302 366 366 LEU LEU C . n 
C 1 303 PHE 303 367 367 PHE PHE C . n 
C 1 304 SER 304 368 368 SER SER C . n 
C 1 305 VAL 305 369 369 VAL VAL C . n 
C 1 306 GLN 306 370 370 GLN GLN C . n 
C 1 307 THR 307 371 371 THR THR C . n 
C 1 308 VAL 308 372 372 VAL VAL C . n 
C 1 309 GLY 309 373 373 GLY GLY C . n 
C 1 310 ASN 310 374 374 ASN ASN C . n 
C 1 311 ARG 311 375 375 ARG ARG C . n 
C 1 312 ASN 312 376 376 ASN ASN C . n 
C 1 313 TYR 313 377 377 TYR TYR C . n 
C 1 314 GLN 314 378 378 GLN GLN C . n 
C 1 315 LEU 315 379 379 LEU LEU C . n 
C 1 316 LEU 316 380 380 LEU LEU C . n 
C 1 317 SER 317 381 381 SER SER C . n 
C 1 318 ASN 318 382 382 ASN ASN C . n 
C 1 319 SER 319 383 383 SER SER C . n 
C 1 320 THR 320 384 384 THR THR C . n 
C 1 321 ILE 321 385 385 ILE ILE C . n 
C 1 322 GLY 322 386 386 GLY GLY C . n 
C 1 323 ARG 323 387 387 ARG ARG C . n 
C 1 324 SER 324 388 388 SER SER C . n 
C 1 325 GLY 325 389 389 GLY GLY C . n 
C 1 326 LEU 326 390 390 LEU LEU C . n 
C 1 327 TYR 327 391 391 TYR TYR C . n 
C 1 328 GLN 328 392 392 GLN GLN C . n 
C 1 329 PRO 329 393 393 PRO PRO C . n 
C 1 330 ALA 330 394 394 ALA ALA C . n 
C 1 331 TYR 331 395 395 TYR TYR C . n 
C 1 332 GLU 332 396 396 GLU GLU C . n 
C 1 333 SER 333 397 397 SER SER C . n 
C 1 334 ARG 334 398 398 ARG ARG C . n 
C 1 335 ASP 335 399 399 ASP ASP C . n 
C 1 336 CYS 336 400 400 CYS CYS C . n 
C 1 337 GLN 337 401 401 GLN GLN C . n 
C 1 338 GLU 338 402 402 GLU GLU C . n 
C 1 339 LEU 339 403 403 LEU LEU C . n 
C 1 340 CYS 340 404 404 CYS CYS C . n 
C 1 341 PHE 341 405 405 PHE PHE C . n 
C 1 342 TRP 342 406 406 TRP TRP C . n 
C 1 343 ILE 343 407 407 ILE ILE C . n 
C 1 344 GLU 344 408 408 GLU GLU C . n 
C 1 345 ILE 345 409 409 ILE ILE C . n 
C 1 346 ALA 346 410 410 ALA ALA C . n 
C 1 347 ALA 347 411 411 ALA ALA C . n 
C 1 348 THR 348 412 412 THR THR C . n 
C 1 349 THR 349 413 413 THR THR C . n 
C 1 350 LYS 350 414 414 LYS LYS C . n 
C 1 351 ALA 351 415 415 ALA ALA C . n 
C 1 352 GLY 352 416 416 GLY GLY C . n 
C 1 353 LEU 353 417 417 LEU LEU C . n 
C 1 354 SER 354 418 418 SER SER C . n 
C 1 355 SER 355 419 419 SER SER C . n 
C 1 356 ASN 356 420 420 ASN ASN C . n 
C 1 357 ASP 357 421 421 ASP ASP C . n 
C 1 358 LEU 358 422 422 LEU LEU C . n 
C 1 359 ILE 359 423 423 ILE ILE C . n 
C 1 360 THR 360 424 424 THR THR C . n 
C 1 361 PHE 361 425 425 PHE PHE C . n 
C 1 362 CYS 362 426 426 CYS CYS C . n 
C 1 363 GLY 363 427 427 GLY GLY C . n 
C 1 364 THR 364 428 428 THR THR C . n 
C 1 365 GLY 365 429 429 GLY GLY C . n 
C 1 366 GLY 366 430 430 GLY GLY C . n 
C 1 367 SER 367 431 431 SER SER C . n 
C 1 368 MET 368 432 432 MET MET C . n 
C 1 369 PRO 369 433 433 PRO PRO C . n 
C 1 370 ASP 370 434 434 ASP ASP C . n 
C 1 371 VAL 371 435 435 VAL VAL C . n 
C 1 372 ASN 372 436 436 ASN ASN C . n 
C 1 373 TRP 373 437 437 TRP TRP C . n 
C 1 374 GLY 374 438 ?   ?   ?   C . n 
D 1 1   GLY 1   65  ?   ?   ?   D . n 
D 1 2   SER 2   66  ?   ?   ?   D . n 
D 1 3   GLY 3   67  ?   ?   ?   D . n 
D 1 4   ASP 4   68  ?   ?   ?   D . n 
D 1 5   SER 5   69  ?   ?   ?   D . n 
D 1 6   GLY 6   70  ?   ?   ?   D . n 
D 1 7   SER 7   71  ?   ?   ?   D . n 
D 1 8   PRO 8   72  ?   ?   ?   D . n 
D 1 9   GLY 9   73  ?   ?   ?   D . n 
D 1 10  ILE 10  74  ?   ?   ?   D . n 
D 1 11  ALA 11  75  75  ALA ALA D . n 
D 1 12  THR 12  76  76  THR THR D . n 
D 1 13  PRO 13  77  77  PRO PRO D . n 
D 1 14  LEU 14  78  78  LEU LEU D . n 
D 1 15  VAL 15  79  79  VAL VAL D . n 
D 1 16  LEU 16  80  80  LEU LEU D . n 
D 1 17  GLY 17  81  81  GLY GLY D . n 
D 1 18  GLU 18  82  82  GLU GLU D . n 
D 1 19  ASN 19  83  83  ASN ASN D . n 
D 1 20  LEU 20  84  84  LEU LEU D . n 
D 1 21  CYS 21  85  85  CYS CYS D . n 
D 1 22  SER 22  86  86  SER SER D . n 
D 1 23  ILE 23  87  87  ILE ILE D . n 
D 1 24  ASN 24  88  88  ASN ASN D . n 
D 1 25  GLY 25  89  89  GLY GLY D . n 
D 1 26  TRP 26  90  90  TRP TRP D . n 
D 1 27  VAL 27  91  91  VAL VAL D . n 
D 1 28  PRO 28  92  92  PRO PRO D . n 
D 1 29  THR 29  93  93  THR THR D . n 
D 1 30  TYR 30  94  94  TYR TYR D . n 
D 1 31  ARG 31  95  95  ARG ARG D . n 
D 1 32  GLY 32  96  96  GLY GLY D . n 
D 1 33  GLU 33  97  97  GLU GLU D . n 
D 1 34  GLY 34  98  98  GLY GLY D . n 
D 1 35  THR 35  99  99  THR THR D . n 
D 1 36  THR 36  100 100 THR THR D . n 
D 1 37  GLY 37  101 101 GLY GLY D . n 
D 1 38  LYS 38  102 102 LYS LYS D . n 
D 1 39  ILE 39  103 103 ILE ILE D . n 
D 1 40  PRO 40  104 104 PRO PRO D . n 
D 1 41  ASP 41  105 105 ASP ASP D . n 
D 1 42  GLU 42  106 106 GLU GLU D . n 
D 1 43  GLN 43  107 107 GLN GLN D . n 
D 1 44  MET 44  108 108 MET MET D . n 
D 1 45  LEU 45  109 109 LEU LEU D . n 
D 1 46  THR 46  110 110 THR THR D . n 
D 1 47  ARG 47  111 111 ARG ARG D . n 
D 1 48  GLN 48  112 112 GLN GLN D . n 
D 1 49  ASN 49  113 113 ASN ASN D . n 
D 1 50  PHE 50  114 114 PHE PHE D . n 
D 1 51  VAL 51  115 115 VAL VAL D . n 
D 1 52  SER 52  116 116 SER SER D . n 
D 1 53  CYS 53  117 117 CYS CYS D . n 
D 1 54  SER 54  118 118 SER SER D . n 
D 1 55  ASP 55  119 119 ASP ASP D . n 
D 1 56  LYS 56  120 120 LYS LYS D . n 
D 1 57  GLU 57  121 121 GLU GLU D . n 
D 1 58  CYS 58  122 122 CYS CYS D . n 
D 1 59  ARG 59  123 123 ARG ARG D . n 
D 1 60  ARG 60  124 124 ARG ARG D . n 
D 1 61  PHE 61  125 125 PHE PHE D . n 
D 1 62  PHE 62  126 126 PHE PHE D . n 
D 1 63  VAL 63  127 127 VAL VAL D . n 
D 1 64  SER 64  128 128 SER SER D . n 
D 1 65  MET 65  129 129 MET MET D . n 
D 1 66  GLY 66  130 130 GLY GLY D . n 
D 1 67  TYR 67  131 131 TYR TYR D . n 
D 1 68  GLY 68  132 132 GLY GLY D . n 
D 1 69  THR 69  133 133 THR THR D . n 
D 1 70  THR 70  134 134 THR THR D . n 
D 1 71  THR 71  135 135 THR THR D . n 
D 1 72  ASN 72  136 136 ASN ASN D . n 
D 1 73  PHE 73  137 137 PHE PHE D . n 
D 1 74  ALA 74  138 138 ALA ALA D . n 
D 1 75  ASP 75  139 139 ASP ASP D . n 
D 1 76  LEU 76  140 140 LEU LEU D . n 
D 1 77  ILE 77  141 141 ILE ILE D . n 
D 1 78  VAL 78  142 142 VAL VAL D . n 
D 1 79  SER 79  143 143 SER SER D . n 
D 1 80  GLU 80  144 144 GLU GLU D . n 
D 1 81  GLN 81  145 145 GLN GLN D . n 
D 1 82  MET 82  146 146 MET MET D . n 
D 1 83  ASN 83  147 147 ASN ASN D . n 
D 1 84  VAL 84  148 148 VAL VAL D . n 
D 1 85  TYR 85  149 149 TYR TYR D . n 
D 1 86  SER 86  150 150 SER SER D . n 
D 1 87  VAL 87  151 151 VAL VAL D . n 
D 1 88  LYS 88  152 152 LYS LYS D . n 
D 1 89  LEU 89  153 153 LEU LEU D . n 
D 1 90  GLY 90  154 154 GLY GLY D . n 
D 1 91  ASP 91  155 155 ASP ASP D . n 
D 1 92  PRO 92  156 156 PRO PRO D . n 
D 1 93  PRO 93  157 157 PRO PRO D . n 
D 1 94  THR 94  158 158 THR THR D . n 
D 1 95  PRO 95  159 159 PRO PRO D . n 
D 1 96  ASP 96  160 160 ASP ASP D . n 
D 1 97  LYS 97  161 161 LYS LYS D . n 
D 1 98  LEU 98  162 162 LEU LEU D . n 
D 1 99  LYS 99  163 163 LYS LYS D . n 
D 1 100 PHE 100 164 164 PHE PHE D . n 
D 1 101 GLU 101 165 165 GLU GLU D . n 
D 1 102 ALA 102 166 166 ALA ALA D . n 
D 1 103 VAL 103 167 167 VAL VAL D . n 
D 1 104 GLY 104 168 168 GLY GLY D . n 
D 1 105 TRP 105 169 169 TRP TRP D . n 
D 1 106 SER 106 170 170 SER SER D . n 
D 1 107 ALA 107 171 171 ALA ALA D . n 
D 1 108 SER 108 172 172 SER SER D . n 
D 1 109 SER 109 173 173 SER SER D . n 
D 1 110 CYS 110 174 174 CYS CYS D . n 
D 1 111 HIS 111 175 175 HIS HIS D . n 
D 1 112 ASP 112 176 176 ASP ASP D . n 
D 1 113 GLY 113 177 177 GLY GLY D . n 
D 1 114 PHE 114 178 178 PHE PHE D . n 
D 1 115 GLN 115 179 179 GLN GLN D . n 
D 1 116 TRP 116 180 180 TRP TRP D . n 
D 1 117 THR 117 181 181 THR THR D . n 
D 1 118 VAL 118 182 182 VAL VAL D . n 
D 1 119 LEU 119 183 183 LEU LEU D . n 
D 1 120 SER 120 184 184 SER SER D . n 
D 1 121 VAL 121 185 185 VAL VAL D . n 
D 1 122 ALA 122 186 186 ALA ALA D . n 
D 1 123 GLY 123 187 187 GLY GLY D . n 
D 1 124 ASP 124 188 188 ASP ASP D . n 
D 1 125 GLY 125 189 189 GLY GLY D . n 
D 1 126 PHE 126 190 190 PHE PHE D . n 
D 1 127 VAL 127 191 191 VAL VAL D . n 
D 1 128 SER 128 192 192 SER SER D . n 
D 1 129 ILE 129 193 193 ILE ILE D . n 
D 1 130 LEU 130 194 194 LEU LEU D . n 
D 1 131 TYR 131 195 195 TYR TYR D . n 
D 1 132 GLY 132 196 196 GLY GLY D . n 
D 1 133 GLY 133 197 197 GLY GLY D . n 
D 1 134 ILE 134 198 198 ILE ILE D . n 
D 1 135 ILE 135 199 199 ILE ILE D . n 
D 1 136 THR 136 200 200 THR THR D . n 
D 1 137 ASP 137 201 201 ASP ASP D . n 
D 1 138 THR 138 202 202 THR THR D . n 
D 1 139 ILE 139 203 203 ILE ILE D . n 
D 1 140 HIS 140 204 204 HIS HIS D . n 
D 1 141 PRO 141 205 205 PRO PRO D . n 
D 1 142 THR 142 206 206 THR THR D . n 
D 1 143 ASN 143 207 207 ASN ASN D . n 
D 1 144 GLY 144 208 208 GLY GLY D . n 
D 1 145 GLY 145 209 209 GLY GLY D . n 
D 1 146 PRO 146 210 210 PRO PRO D . n 
D 1 147 LEU 147 211 211 LEU LEU D . n 
D 1 148 ARG 148 212 212 ARG ARG D . n 
D 1 149 THR 149 213 213 THR THR D . n 
D 1 150 GLN 150 214 214 GLN GLN D . n 
D 1 151 ALA 151 215 215 ALA ALA D . n 
D 1 152 SER 152 216 216 SER SER D . n 
D 1 153 SER 153 217 217 SER SER D . n 
D 1 154 CYS 154 218 218 CYS CYS D . n 
D 1 155 ILE 155 219 219 ILE ILE D . n 
D 1 156 CYS 156 220 220 CYS CYS D . n 
D 1 157 ASN 157 221 221 ASN ASN D . n 
D 1 158 ASP 158 222 222 ASP ASP D . n 
D 1 159 GLY 159 223 223 GLY GLY D . n 
D 1 160 THR 160 224 224 THR THR D . n 
D 1 161 CYS 161 225 225 CYS CYS D . n 
D 1 162 TYR 162 226 226 TYR TYR D . n 
D 1 163 THR 163 227 227 THR THR D . n 
D 1 164 ILE 164 228 228 ILE ILE D . n 
D 1 165 ILE 165 229 229 ILE ILE D . n 
D 1 166 ALA 166 230 230 ALA ALA D . n 
D 1 167 ASP 167 231 231 ASP ASP D . n 
D 1 168 GLY 168 232 232 GLY GLY D . n 
D 1 169 THR 169 233 233 THR THR D . n 
D 1 170 THR 170 234 234 THR THR D . n 
D 1 171 TYR 171 235 235 TYR TYR D . n 
D 1 172 THR 172 236 236 THR THR D . n 
D 1 173 ALA 173 237 237 ALA ALA D . n 
D 1 174 SER 174 238 238 SER SER D . n 
D 1 175 SER 175 239 239 SER SER D . n 
D 1 176 HIS 176 240 240 HIS HIS D . n 
D 1 177 ARG 177 241 241 ARG ARG D . n 
D 1 178 LEU 178 242 242 LEU LEU D . n 
D 1 179 TYR 179 243 243 TYR TYR D . n 
D 1 180 ARG 180 244 244 ARG ARG D . n 
D 1 181 LEU 181 245 245 LEU LEU D . n 
D 1 182 VAL 182 246 246 VAL VAL D . n 
D 1 183 ASN 183 247 247 ASN ASN D . n 
D 1 184 GLY 184 248 248 GLY GLY D . n 
D 1 185 THR 185 249 249 THR THR D . n 
D 1 186 SER 186 250 250 SER SER D . n 
D 1 187 ALA 187 251 251 ALA ALA D . n 
D 1 188 GLY 188 252 252 GLY GLY D . n 
D 1 189 TRP 189 253 253 TRP TRP D . n 
D 1 190 LYS 190 254 254 LYS LYS D . n 
D 1 191 ALA 191 255 255 ALA ALA D . n 
D 1 192 LEU 192 256 256 LEU LEU D . n 
D 1 193 ASP 193 257 257 ASP ASP D . n 
D 1 194 THR 194 258 258 THR THR D . n 
D 1 195 THR 195 259 259 THR THR D . n 
D 1 196 GLY 196 260 260 GLY GLY D . n 
D 1 197 PHE 197 261 261 PHE PHE D . n 
D 1 198 ASN 198 262 262 ASN ASN D . n 
D 1 199 PHE 199 263 263 PHE PHE D . n 
D 1 200 GLU 200 264 264 GLU GLU D . n 
D 1 201 PHE 201 265 265 PHE PHE D . n 
D 1 202 PRO 202 266 266 PRO PRO D . n 
D 1 203 THR 203 267 267 THR THR D . n 
D 1 204 CYS 204 268 268 CYS CYS D . n 
D 1 205 TYR 205 269 269 TYR TYR D . n 
D 1 206 TYR 206 270 270 TYR TYR D . n 
D 1 207 THR 207 271 271 THR THR D . n 
D 1 208 SER 208 272 272 SER SER D . n 
D 1 209 GLY 209 273 273 GLY GLY D . n 
D 1 210 LYS 210 274 274 LYS LYS D . n 
D 1 211 VAL 211 275 275 VAL VAL D . n 
D 1 212 LYS 212 276 276 LYS LYS D . n 
D 1 213 CYS 213 277 277 CYS CYS D . n 
D 1 214 THR 214 278 278 THR THR D . n 
D 1 215 GLY 215 279 279 GLY GLY D . n 
D 1 216 THR 216 280 280 THR THR D . n 
D 1 217 ASN 217 281 281 ASN ASN D . n 
D 1 218 LEU 218 282 282 LEU LEU D . n 
D 1 219 TRP 219 283 283 TRP TRP D . n 
D 1 220 ASN 220 284 284 ASN ASN D . n 
D 1 221 ASP 221 285 285 ASP ASP D . n 
D 1 222 ALA 222 286 286 ALA ALA D . n 
D 1 223 LYS 223 287 287 LYS LYS D . n 
D 1 224 ARG 224 288 288 ARG ARG D . n 
D 1 225 PRO 225 289 289 PRO PRO D . n 
D 1 226 PHE 226 290 290 PHE PHE D . n 
D 1 227 LEU 227 291 291 LEU LEU D . n 
D 1 228 GLU 228 292 292 GLU GLU D . n 
D 1 229 PHE 229 293 293 PHE PHE D . n 
D 1 230 ASP 230 294 294 ASP ASP D . n 
D 1 231 GLN 231 295 295 GLN GLN D . n 
D 1 232 SER 232 296 296 SER SER D . n 
D 1 233 PHE 233 297 297 PHE PHE D . n 
D 1 234 THR 234 298 298 THR THR D . n 
D 1 235 TYR 235 299 299 TYR TYR D . n 
D 1 236 THR 236 300 300 THR THR D . n 
D 1 237 PHE 237 301 301 PHE PHE D . n 
D 1 238 LYS 238 302 302 LYS LYS D . n 
D 1 239 GLU 239 303 303 GLU GLU D . n 
D 1 240 PRO 240 304 304 PRO PRO D . n 
D 1 241 CYS 241 305 305 CYS CYS D . n 
D 1 242 LEU 242 306 306 LEU LEU D . n 
D 1 243 GLY 243 307 307 GLY GLY D . n 
D 1 244 PHE 244 308 308 PHE PHE D . n 
D 1 245 LEU 245 309 309 LEU LEU D . n 
D 1 246 GLY 246 310 310 GLY GLY D . n 
D 1 247 ASP 247 311 311 ASP ASP D . n 
D 1 248 THR 248 312 312 THR THR D . n 
D 1 249 PRO 249 313 313 PRO PRO D . n 
D 1 250 ARG 250 314 314 ARG ARG D . n 
D 1 251 GLY 251 315 315 GLY GLY D . n 
D 1 252 ILE 252 316 316 ILE ILE D . n 
D 1 253 ASP 253 317 317 ASP ASP D . n 
D 1 254 THR 254 318 318 THR THR D . n 
D 1 255 THR 255 319 319 THR THR D . n 
D 1 256 ASN 256 320 320 ASN ASN D . n 
D 1 257 TYR 257 321 321 TYR TYR D . n 
D 1 258 CYS 258 322 322 CYS CYS D . n 
D 1 259 ASP 259 323 323 ASP ASP D . n 
D 1 260 LYS 260 324 324 LYS LYS D . n 
D 1 261 THR 261 325 325 THR THR D . n 
D 1 262 THR 262 326 326 THR THR D . n 
D 1 263 THR 263 327 327 THR THR D . n 
D 1 264 GLU 264 328 328 GLU GLU D . n 
D 1 265 GLY 265 329 329 GLY GLY D . n 
D 1 266 GLU 266 330 330 GLU GLU D . n 
D 1 267 GLY 267 331 331 GLY GLY D . n 
D 1 268 GLY 268 332 332 GLY GLY D . n 
D 1 269 ILE 269 333 333 ILE ILE D . n 
D 1 270 GLN 270 334 334 GLN GLN D . n 
D 1 271 GLY 271 335 335 GLY GLY D . n 
D 1 272 PHE 272 336 336 PHE PHE D . n 
D 1 273 MET 273 337 337 MET MET D . n 
D 1 274 ILE 274 338 338 ILE ILE D . n 
D 1 275 GLU 275 339 339 GLU GLU D . n 
D 1 276 GLY 276 340 340 GLY GLY D . n 
D 1 277 SER 277 341 341 SER SER D . n 
D 1 278 ASN 278 342 342 ASN ASN D . n 
D 1 279 SER 279 343 343 SER SER D . n 
D 1 280 TRP 280 344 344 TRP TRP D . n 
D 1 281 ILE 281 345 345 ILE ILE D . n 
D 1 282 GLY 282 346 346 GLY GLY D . n 
D 1 283 ARG 283 347 347 ARG ARG D . n 
D 1 284 ILE 284 348 348 ILE ILE D . n 
D 1 285 ILE 285 349 349 ILE ILE D . n 
D 1 286 ASN 286 350 350 ASN ASN D . n 
D 1 287 PRO 287 351 351 PRO PRO D . n 
D 1 288 GLY 288 352 352 GLY GLY D . n 
D 1 289 SER 289 353 353 SER SER D . n 
D 1 290 LYS 290 354 354 LYS LYS D . n 
D 1 291 LYS 291 355 355 LYS LYS D . n 
D 1 292 GLY 292 356 356 GLY GLY D . n 
D 1 293 PHE 293 357 357 PHE PHE D . n 
D 1 294 GLU 294 358 358 GLU GLU D . n 
D 1 295 ILE 295 359 359 ILE ILE D . n 
D 1 296 TYR 296 360 360 TYR TYR D . n 
D 1 297 LYS 297 361 361 LYS LYS D . n 
D 1 298 PHE 298 362 362 PHE PHE D . n 
D 1 299 LEU 299 363 363 LEU LEU D . n 
D 1 300 GLY 300 364 364 GLY GLY D . n 
D 1 301 THR 301 365 365 THR THR D . n 
D 1 302 LEU 302 366 366 LEU LEU D . n 
D 1 303 PHE 303 367 367 PHE PHE D . n 
D 1 304 SER 304 368 368 SER SER D . n 
D 1 305 VAL 305 369 369 VAL VAL D . n 
D 1 306 GLN 306 370 370 GLN GLN D . n 
D 1 307 THR 307 371 371 THR THR D . n 
D 1 308 VAL 308 372 372 VAL VAL D . n 
D 1 309 GLY 309 373 373 GLY GLY D . n 
D 1 310 ASN 310 374 374 ASN ASN D . n 
D 1 311 ARG 311 375 375 ARG ARG D . n 
D 1 312 ASN 312 376 376 ASN ASN D . n 
D 1 313 TYR 313 377 377 TYR TYR D . n 
D 1 314 GLN 314 378 378 GLN GLN D . n 
D 1 315 LEU 315 379 379 LEU LEU D . n 
D 1 316 LEU 316 380 380 LEU LEU D . n 
D 1 317 SER 317 381 381 SER SER D . n 
D 1 318 ASN 318 382 382 ASN ASN D . n 
D 1 319 SER 319 383 383 SER SER D . n 
D 1 320 THR 320 384 384 THR THR D . n 
D 1 321 ILE 321 385 385 ILE ILE D . n 
D 1 322 GLY 322 386 386 GLY GLY D . n 
D 1 323 ARG 323 387 387 ARG ARG D . n 
D 1 324 SER 324 388 388 SER SER D . n 
D 1 325 GLY 325 389 389 GLY GLY D . n 
D 1 326 LEU 326 390 390 LEU LEU D . n 
D 1 327 TYR 327 391 391 TYR TYR D . n 
D 1 328 GLN 328 392 392 GLN GLN D . n 
D 1 329 PRO 329 393 393 PRO PRO D . n 
D 1 330 ALA 330 394 394 ALA ALA D . n 
D 1 331 TYR 331 395 395 TYR TYR D . n 
D 1 332 GLU 332 396 396 GLU GLU D . n 
D 1 333 SER 333 397 397 SER SER D . n 
D 1 334 ARG 334 398 398 ARG ARG D . n 
D 1 335 ASP 335 399 399 ASP ASP D . n 
D 1 336 CYS 336 400 400 CYS CYS D . n 
D 1 337 GLN 337 401 401 GLN GLN D . n 
D 1 338 GLU 338 402 402 GLU GLU D . n 
D 1 339 LEU 339 403 403 LEU LEU D . n 
D 1 340 CYS 340 404 404 CYS CYS D . n 
D 1 341 PHE 341 405 405 PHE PHE D . n 
D 1 342 TRP 342 406 406 TRP TRP D . n 
D 1 343 ILE 343 407 407 ILE ILE D . n 
D 1 344 GLU 344 408 408 GLU GLU D . n 
D 1 345 ILE 345 409 409 ILE ILE D . n 
D 1 346 ALA 346 410 410 ALA ALA D . n 
D 1 347 ALA 347 411 411 ALA ALA D . n 
D 1 348 THR 348 412 412 THR THR D . n 
D 1 349 THR 349 413 413 THR THR D . n 
D 1 350 LYS 350 414 414 LYS LYS D . n 
D 1 351 ALA 351 415 415 ALA ALA D . n 
D 1 352 GLY 352 416 416 GLY GLY D . n 
D 1 353 LEU 353 417 417 LEU LEU D . n 
D 1 354 SER 354 418 418 SER SER D . n 
D 1 355 SER 355 419 419 SER SER D . n 
D 1 356 ASN 356 420 420 ASN ASN D . n 
D 1 357 ASP 357 421 421 ASP ASP D . n 
D 1 358 LEU 358 422 422 LEU LEU D . n 
D 1 359 ILE 359 423 423 ILE ILE D . n 
D 1 360 THR 360 424 424 THR THR D . n 
D 1 361 PHE 361 425 425 PHE PHE D . n 
D 1 362 CYS 362 426 426 CYS CYS D . n 
D 1 363 GLY 363 427 427 GLY GLY D . n 
D 1 364 THR 364 428 428 THR THR D . n 
D 1 365 GLY 365 429 429 GLY GLY D . n 
D 1 366 GLY 366 430 430 GLY GLY D . n 
D 1 367 SER 367 431 431 SER SER D . n 
D 1 368 MET 368 432 432 MET MET D . n 
D 1 369 PRO 369 433 433 PRO PRO D . n 
D 1 370 ASP 370 434 434 ASP ASP D . n 
D 1 371 VAL 371 435 435 VAL VAL D . n 
D 1 372 ASN 372 436 436 ASN ASN D . n 
D 1 373 TRP 373 437 437 TRP TRP D . n 
D 1 374 GLY 374 438 ?   ?   ?   D . n 
# 
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 D ASN 183 D ASN 247 ? ASN 'GLYCOSYLATION SITE' 
2 B ASN 183 B ASN 247 ? ASN 'GLYCOSYLATION SITE' 
3 A ASN 183 A ASN 247 ? ASN 'GLYCOSYLATION SITE' 
4 C ASN 183 C ASN 247 ? 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   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M 
# 
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)' 10000 ? 
1 MORE         -93   ? 
1 'SSA (A^2)'  49730 ? 
# 
_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_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OD2 ? D ASP 96  ? D ASP 160 ? 1_555 CA ? G CA . ? A CA 503 ? 1_555 OD2 ? A ASP 96  ? A ASP 160 ? 1_555 91.1  ? 
2  OD2 ? D ASP 96  ? D ASP 160 ? 1_555 CA ? G CA . ? A CA 503 ? 1_555 OD2 ? B ASP 96  ? B ASP 160 ? 1_555 88.6  ? 
3  OD2 ? A ASP 96  ? A ASP 160 ? 1_555 CA ? G CA . ? A CA 503 ? 1_555 OD2 ? B ASP 96  ? B ASP 160 ? 1_555 167.8 ? 
4  OD2 ? D ASP 96  ? D ASP 160 ? 1_555 CA ? G CA . ? A CA 503 ? 1_555 OD2 ? C ASP 96  ? C ASP 160 ? 1_555 162.5 ? 
5  OD2 ? A ASP 96  ? A ASP 160 ? 1_555 CA ? G CA . ? A CA 503 ? 1_555 OD2 ? C ASP 96  ? C ASP 160 ? 1_555 91.6  ? 
6  OD2 ? B ASP 96  ? B ASP 160 ? 1_555 CA ? G CA . ? A CA 503 ? 1_555 OD2 ? C ASP 96  ? C ASP 160 ? 1_555 85.1  ? 
7  O   ? C GLY 265 ? C GLY 329 ? 1_555 CA ? K CA . ? C CA 502 ? 1_555 O   ? C ASN 217 ? C ASN 281 ? 1_555 91.1  ? 
8  O   ? C GLY 265 ? C GLY 329 ? 1_555 CA ? K CA . ? C CA 502 ? 1_555 O   ? C GLY 267 ? C GLY 331 ? 1_555 93.8  ? 
9  O   ? C ASN 217 ? C ASN 281 ? 1_555 CA ? K CA . ? C CA 502 ? 1_555 O   ? C GLY 267 ? C GLY 331 ? 1_555 90.3  ? 
10 O   ? C GLY 265 ? C GLY 329 ? 1_555 CA ? K CA . ? C CA 502 ? 1_555 O   ? C ASP 221 ? C ASP 285 ? 1_555 78.0  ? 
11 O   ? C ASN 217 ? C ASN 281 ? 1_555 CA ? K CA . ? C CA 502 ? 1_555 O   ? C ASP 221 ? C ASP 285 ? 1_555 78.0  ? 
12 O   ? C GLY 267 ? C GLY 331 ? 1_555 CA ? K CA . ? C CA 502 ? 1_555 O   ? C ASP 221 ? C ASP 285 ? 1_555 165.5 ? 
13 O   ? C GLY 265 ? C GLY 329 ? 1_555 CA ? K CA . ? C CA 502 ? 1_555 OD2 ? C ASP 247 ? C ASP 311 ? 1_555 156.1 ? 
14 O   ? C ASN 217 ? C ASN 281 ? 1_555 CA ? K CA . ? C CA 502 ? 1_555 OD2 ? C ASP 247 ? C ASP 311 ? 1_555 78.3  ? 
15 O   ? C GLY 267 ? C GLY 331 ? 1_555 CA ? K CA . ? C CA 502 ? 1_555 OD2 ? C ASP 247 ? C ASP 311 ? 1_555 107.5 ? 
16 O   ? C ASP 221 ? C ASP 285 ? 1_555 CA ? K CA . ? C CA 502 ? 1_555 OD2 ? C ASP 247 ? C ASP 311 ? 1_555 78.8  ? 
17 O   ? B GLY 267 ? B GLY 331 ? 1_555 CA ? I CA . ? B CA 502 ? 1_555 O   ? B GLY 265 ? B GLY 329 ? 1_555 92.0  ? 
18 O   ? B GLY 267 ? B GLY 331 ? 1_555 CA ? I CA . ? B CA 502 ? 1_555 O   ? B ASN 217 ? B ASN 281 ? 1_555 88.6  ? 
19 O   ? B GLY 265 ? B GLY 329 ? 1_555 CA ? I CA . ? B CA 502 ? 1_555 O   ? B ASN 217 ? B ASN 281 ? 1_555 81.8  ? 
20 O   ? B GLY 267 ? B GLY 331 ? 1_555 CA ? I CA . ? B CA 502 ? 1_555 O   ? B ASP 221 ? B ASP 285 ? 1_555 153.7 ? 
21 O   ? B GLY 265 ? B GLY 329 ? 1_555 CA ? I CA . ? B CA 502 ? 1_555 O   ? B ASP 221 ? B ASP 285 ? 1_555 69.5  ? 
22 O   ? B ASN 217 ? B ASN 281 ? 1_555 CA ? I CA . ? B CA 502 ? 1_555 O   ? B ASP 221 ? B ASP 285 ? 1_555 70.7  ? 
23 O   ? B GLY 267 ? B GLY 331 ? 1_555 CA ? I CA . ? B CA 502 ? 1_555 OD2 ? B ASP 247 ? B ASP 311 ? 1_555 113.9 ? 
24 O   ? B GLY 265 ? B GLY 329 ? 1_555 CA ? I CA . ? B CA 502 ? 1_555 OD2 ? B ASP 247 ? B ASP 311 ? 1_555 143.5 ? 
25 O   ? B ASN 217 ? B ASN 281 ? 1_555 CA ? I CA . ? B CA 502 ? 1_555 OD2 ? B ASP 247 ? B ASP 311 ? 1_555 74.0  ? 
26 O   ? B ASP 221 ? B ASP 285 ? 1_555 CA ? I CA . ? B CA 502 ? 1_555 OD2 ? B ASP 247 ? B ASP 311 ? 1_555 76.8  ? 
27 O   ? A GLY 267 ? A GLY 331 ? 1_555 CA ? F CA . ? A CA 502 ? 1_555 O   ? A GLY 265 ? A GLY 329 ? 1_555 95.8  ? 
28 O   ? A GLY 267 ? A GLY 331 ? 1_555 CA ? F CA . ? A CA 502 ? 1_555 O   ? A ASP 221 ? A ASP 285 ? 1_555 159.3 ? 
29 O   ? A GLY 265 ? A GLY 329 ? 1_555 CA ? F CA . ? A CA 502 ? 1_555 O   ? A ASP 221 ? A ASP 285 ? 1_555 72.5  ? 
30 O   ? A GLY 267 ? A GLY 331 ? 1_555 CA ? F CA . ? A CA 502 ? 1_555 O   ? A ASN 217 ? A ASN 281 ? 1_555 88.2  ? 
31 O   ? A GLY 265 ? A GLY 329 ? 1_555 CA ? F CA . ? A CA 502 ? 1_555 O   ? A ASN 217 ? A ASN 281 ? 1_555 85.4  ? 
32 O   ? A ASP 221 ? A ASP 285 ? 1_555 CA ? F CA . ? A CA 502 ? 1_555 O   ? A ASN 217 ? A ASN 281 ? 1_555 74.1  ? 
33 O   ? A GLY 267 ? A GLY 331 ? 1_555 CA ? F CA . ? A CA 502 ? 1_555 OD2 ? A ASP 247 ? A ASP 311 ? 1_555 107.3 ? 
34 O   ? A GLY 265 ? A GLY 329 ? 1_555 CA ? F CA . ? A CA 502 ? 1_555 OD2 ? A ASP 247 ? A ASP 311 ? 1_555 146.9 ? 
35 O   ? A ASP 221 ? A ASP 285 ? 1_555 CA ? F CA . ? A CA 502 ? 1_555 OD2 ? A ASP 247 ? A ASP 311 ? 1_555 77.9  ? 
36 O   ? A ASN 217 ? A ASN 281 ? 1_555 CA ? F CA . ? A CA 502 ? 1_555 OD2 ? A ASP 247 ? A ASP 311 ? 1_555 72.3  ? 
37 O   ? D GLY 267 ? D GLY 331 ? 1_555 CA ? M CA . ? D CA 502 ? 1_555 O   ? D GLY 265 ? D GLY 329 ? 1_555 91.3  ? 
38 O   ? D GLY 267 ? D GLY 331 ? 1_555 CA ? M CA . ? D CA 502 ? 1_555 O   ? D ASP 221 ? D ASP 285 ? 1_555 153.5 ? 
39 O   ? D GLY 265 ? D GLY 329 ? 1_555 CA ? M CA . ? D CA 502 ? 1_555 O   ? D ASP 221 ? D ASP 285 ? 1_555 71.8  ? 
40 O   ? D GLY 267 ? D GLY 331 ? 1_555 CA ? M CA . ? D CA 502 ? 1_555 O   ? D ASN 217 ? D ASN 281 ? 1_555 86.8  ? 
41 O   ? D GLY 265 ? D GLY 329 ? 1_555 CA ? M CA . ? D CA 502 ? 1_555 O   ? D ASN 217 ? D ASN 281 ? 1_555 82.6  ? 
42 O   ? D ASP 221 ? D ASP 285 ? 1_555 CA ? M CA . ? D CA 502 ? 1_555 O   ? D ASN 217 ? D ASN 281 ? 1_555 71.2  ? 
43 O   ? D GLY 267 ? D GLY 331 ? 1_555 CA ? M CA . ? D CA 502 ? 1_555 OD2 ? D ASP 247 ? D ASP 311 ? 1_555 107.5 ? 
44 O   ? D GLY 265 ? D GLY 329 ? 1_555 CA ? M CA . ? D CA 502 ? 1_555 OD2 ? D ASP 247 ? D ASP 311 ? 1_555 147.8 ? 
45 O   ? D ASP 221 ? D ASP 285 ? 1_555 CA ? M CA . ? D CA 502 ? 1_555 OD2 ? D ASP 247 ? D ASP 311 ? 1_555 80.5  ? 
46 O   ? D ASN 217 ? D ASN 281 ? 1_555 CA ? M CA . ? D CA 502 ? 1_555 OD2 ? D ASP 247 ? D ASP 311 ? 1_555 73.0  ? 
# 
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 2013-10-23 
2 'Structure model' 1 1 2013-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
'X-RAY DIFFRACTION' 1 ? refined 56.7746 24.0710 81.1750  0.1689 0.0357 0.0679 -0.0269 -0.0169 -0.0296 0.4694 1.2544 1.7795 -0.6868 
-0.0140 0.6741  -0.0508 -0.0167 0.0676  0.0030  0.0400 -0.0342 0.1135  0.1496  -0.0799 
'X-RAY DIFFRACTION' 2 ? refined 19.6821 66.9792 65.4586  0.1422 0.2081 0.2642 0.0724  -0.1596 -0.1697 0.9036 1.9735 0.5265 -1.2791 
0.2797  -0.5728 -0.1804 0.2114  -0.0310 -0.1924 0.2587 -0.4409 0.3198  -0.0160 0.1913  
'X-RAY DIFFRACTION' 3 ? refined 39.5530 56.6983 100.2611 0.3589 0.2054 0.2159 0.1082  -0.2025 -0.1830 1.5464 1.4096 1.3856 -0.8342 
1.0567  -0.2302 -0.2185 -0.0658 0.2843  -0.0484 0.1253 0.0247  0.2883  -0.2473 -0.1413 
'X-RAY DIFFRACTION' 4 ? refined 37.1417 34.4530 45.9320  0.2331 0.3803 0.1963 0.1646  -0.0563 -0.0775 1.3656 1.8395 1.2707 -1.2393 
0.4525  0.1439  0.3153  -0.3766 0.0612  0.4752  0.1217 -0.0326 -0.3225 -0.0915 0.0016  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.selection_details 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
'X-RAY DIFFRACTION' 1 1 A 75  A 437 ? . . . . ? 
'X-RAY DIFFRACTION' 2 1 A 501 A 501 ? . . . . ? 
'X-RAY DIFFRACTION' 3 2 B 75  B 437 ? . . . . ? 
'X-RAY DIFFRACTION' 4 2 B 501 B 501 ? . . . . ? 
'X-RAY DIFFRACTION' 5 3 C 75  C 437 ? . . . . ? 
'X-RAY DIFFRACTION' 6 3 C 501 C 501 ? . . . . ? 
'X-RAY DIFFRACTION' 7 4 D 75  D 437 ? . . . . ? 
'X-RAY DIFFRACTION' 8 4 D 501 D 501 ? . . . . ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .        ? 1 
PHASER   phasing           .        ? 2 
REFMAC   refinement        5.6.0111 ? 3 
HKL-2000 'data reduction'  .        ? 4 
HKL-2000 'data scaling'    .        ? 5 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    CH2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    TRP 
_pdbx_validate_symm_contact.auth_seq_id_1     253 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    OH 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    TYR 
_pdbx_validate_symm_contact.auth_seq_id_2     360 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   8_555 
_pdbx_validate_symm_contact.dist              2.01 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CE2 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            TRP 
_pdbx_validate_rmsd_bond.auth_seq_id_1             344 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CD2 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            TRP 
_pdbx_validate_rmsd_bond.auth_seq_id_2             344 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.482 
_pdbx_validate_rmsd_bond.bond_target_value         1.409 
_pdbx_validate_rmsd_bond.bond_deviation            0.073 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.012 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 100 ? ? -127.73 -64.68  
2  1 CYS A 174 ? ? -173.62 143.17  
3  1 THR A 206 ? ? -91.50  -66.95  
4  1 ASN A 207 ? ? -55.61  3.02    
5  1 TRP A 283 ? ? -107.47 -76.05  
6  1 CYS A 305 ? ? -103.96 58.32   
7  1 ASN A 374 ? ? -133.81 -63.33  
8  1 SER A 397 ? ? 35.81   -109.06 
9  1 LEU A 417 ? ? 79.80   143.08  
10 1 SER A 418 ? ? -118.92 62.86   
11 1 THR B 100 ? ? -131.62 -62.42  
12 1 PRO B 157 ? ? -69.29  60.71   
13 1 THR B 206 ? ? -95.07  -60.99  
14 1 ASN B 207 ? ? -59.22  7.69    
15 1 ASN B 247 ? ? 43.27   29.59   
16 1 TRP B 283 ? ? -108.36 -75.20  
17 1 CYS B 305 ? ? -103.88 54.69   
18 1 ASN B 374 ? ? -126.80 -53.81  
19 1 SER B 381 ? ? -124.38 -50.34  
20 1 SER B 397 ? ? 36.88   -109.04 
21 1 LEU B 417 ? ? 79.10   143.41  
22 1 SER B 418 ? ? -118.52 63.26   
23 1 THR C 100 ? ? -129.22 -64.90  
24 1 ASN C 207 ? ? -66.58  15.81   
25 1 ASN C 247 ? ? 39.66   33.56   
26 1 TRP C 283 ? ? -107.02 -77.53  
27 1 CYS C 305 ? ? -102.48 60.29   
28 1 ASN C 374 ? ? -128.47 -60.47  
29 1 SER C 397 ? ? 35.93   -108.51 
30 1 LEU C 417 ? ? 82.05   144.01  
31 1 SER C 418 ? ? -118.54 62.31   
32 1 THR D 100 ? ? -129.20 -64.90  
33 1 THR D 206 ? ? -93.67  -63.78  
34 1 ASN D 207 ? ? -54.70  4.40    
35 1 TRP D 283 ? ? -108.82 -75.97  
36 1 ASP D 294 ? ? -119.39 -168.22 
37 1 CYS D 305 ? ? -102.30 59.17   
38 1 ASN D 374 ? ? -128.13 -62.05  
39 1 SER D 397 ? ? 35.85   -108.84 
40 1 LEU D 417 ? ? 80.51   144.04  
41 1 SER D 418 ? ? -118.49 63.83   
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 65  ? A GLY 1   
2  1 Y 1 A SER 66  ? A SER 2   
3  1 Y 1 A GLY 67  ? A GLY 3   
4  1 Y 1 A ASP 68  ? A ASP 4   
5  1 Y 1 A SER 69  ? A SER 5   
6  1 Y 1 A GLY 70  ? A GLY 6   
7  1 Y 1 A SER 71  ? A SER 7   
8  1 Y 1 A PRO 72  ? A PRO 8   
9  1 Y 1 A GLY 73  ? A GLY 9   
10 1 Y 1 A ILE 74  ? A ILE 10  
11 1 Y 1 A GLY 438 ? A GLY 374 
12 1 Y 1 B GLY 65  ? B GLY 1   
13 1 Y 1 B SER 66  ? B SER 2   
14 1 Y 1 B GLY 67  ? B GLY 3   
15 1 Y 1 B ASP 68  ? B ASP 4   
16 1 Y 1 B SER 69  ? B SER 5   
17 1 Y 1 B GLY 70  ? B GLY 6   
18 1 Y 1 B SER 71  ? B SER 7   
19 1 Y 1 B PRO 72  ? B PRO 8   
20 1 Y 1 B GLY 73  ? B GLY 9   
21 1 Y 1 B ILE 74  ? B ILE 10  
22 1 Y 1 B GLY 438 ? B GLY 374 
23 1 Y 1 C GLY 65  ? C GLY 1   
24 1 Y 1 C SER 66  ? C SER 2   
25 1 Y 1 C GLY 67  ? C GLY 3   
26 1 Y 1 C ASP 68  ? C ASP 4   
27 1 Y 1 C SER 69  ? C SER 5   
28 1 Y 1 C GLY 70  ? C GLY 6   
29 1 Y 1 C SER 71  ? C SER 7   
30 1 Y 1 C PRO 72  ? C PRO 8   
31 1 Y 1 C GLY 73  ? C GLY 9   
32 1 Y 1 C ILE 74  ? C ILE 10  
33 1 Y 1 C GLY 438 ? C GLY 374 
34 1 Y 1 D GLY 65  ? D GLY 1   
35 1 Y 1 D SER 66  ? D SER 2   
36 1 Y 1 D GLY 67  ? D GLY 3   
37 1 Y 1 D ASP 68  ? D ASP 4   
38 1 Y 1 D SER 69  ? D SER 5   
39 1 Y 1 D GLY 70  ? D GLY 6   
40 1 Y 1 D SER 71  ? D SER 7   
41 1 Y 1 D PRO 72  ? D PRO 8   
42 1 Y 1 D GLY 73  ? D GLY 9   
43 1 Y 1 D ILE 74  ? D ILE 10  
44 1 Y 1 D GLY 438 ? D GLY 374 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE NAG 
3 'CALCIUM ION'          CA  
# 
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 
E 2 NAG 1 501 5000 NAG NAG A . 
F 3 CA  1 502 801  CA  CA  A . 
G 3 CA  1 503 805  CA  CA  A . 
H 2 NAG 1 501 5000 NAG NAG B . 
I 3 CA  1 502 802  CA  CA  B . 
J 2 NAG 1 501 5000 NAG NAG C . 
K 3 CA  1 502 803  CA  CA  C . 
L 2 NAG 1 501 5000 NAG NAG D . 
M 3 CA  1 502 804  CA  CA  D . 
# 
