data_8ZSA
# 
_entry.id   8ZSA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8ZSA         pdb_00008zsa 10.2210/pdb8zsa/pdb 
WWPDB D_1300048404 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-03-19 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8ZSA 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-05 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jun_yang96@163.com 
_pdbx_contact_author.name_first         Xiaoguang 
_pdbx_contact_author.name_last          Lei 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0380-8035 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Gao, L.'   1 ? 
'Yang, J.'  2 ? 
'Lei, X.G.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of 4VPMT2' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Gao, L.'   1 ? 
primary 'Yang, J.'  2 ? 
primary 'Lei, X.G.' 3 ? 
# 
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 4VPMT2               36956.133 4  ? ? ? ? 
2 non-polymer syn S-ADENOSYLMETHIONINE 398.437   4  ? ? ? ? 
3 non-polymer syn 4-ethenylphenol      120.149   1  ? ? ? ? 
4 water       nat water                18.015    36 ? ? ? ? 
# 
_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       
;MGSHHHHHHHHGSDYDIPTTENLYFQGSMEKQDTHVNTEKQEAYRGIDKPHLYTLGCCSLTAMASAQLDALWSQLSWPQT
PLPVLDIGCGPGDIARKVLAPRLPAGTRLVACDISPEMVDFCRQHNALPGTITYELLDVVEPRLEDTVVWRNGPFGKVFC
MLMLHLVPDNRLAVKNIHKLLVPGGEAVFSVIANMALCDAYEEMAKEPRWALYMQDVEKFVSPYQHSEDPVGEFRLLLES
EGFQVLRCDLGPQKVFFPTAETHREFLKSVCAFLYRIPEEQKDDFFDDWLQRLEKLKGTSQGVGRNGEAEYYIHLSVITA
LARKF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSHHHHHHHHGSDYDIPTTENLYFQGSMEKQDTHVNTEKQEAYRGIDKPHLYTLGCCSLTAMASAQLDALWSQLSWPQT
PLPVLDIGCGPGDIARKVLAPRLPAGTRLVACDISPEMVDFCRQHNALPGTITYELLDVVEPRLEDTVVWRNGPFGKVFC
MLMLHLVPDNRLAVKNIHKLLVPGGEAVFSVIANMALCDAYEEMAKEPRWALYMQDVEKFVSPYQHSEDPVGEFRLLLES
EGFQVLRCDLGPQKVFFPTAETHREFLKSVCAFLYRIPEEQKDDFFDDWLQRLEKLKGTSQGVGRNGEAEYYIHLSVITA
LARKF
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 S-ADENOSYLMETHIONINE SAM 
3 4-ethenylphenol      4VP 
4 water                HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  HIS n 
1 12  GLY n 
1 13  SER n 
1 14  ASP n 
1 15  TYR n 
1 16  ASP n 
1 17  ILE n 
1 18  PRO n 
1 19  THR n 
1 20  THR n 
1 21  GLU n 
1 22  ASN n 
1 23  LEU n 
1 24  TYR n 
1 25  PHE n 
1 26  GLN n 
1 27  GLY n 
1 28  SER n 
1 29  MET n 
1 30  GLU n 
1 31  LYS n 
1 32  GLN n 
1 33  ASP n 
1 34  THR n 
1 35  HIS n 
1 36  VAL n 
1 37  ASN n 
1 38  THR n 
1 39  GLU n 
1 40  LYS n 
1 41  GLN n 
1 42  GLU n 
1 43  ALA n 
1 44  TYR n 
1 45  ARG n 
1 46  GLY n 
1 47  ILE n 
1 48  ASP n 
1 49  LYS n 
1 50  PRO n 
1 51  HIS n 
1 52  LEU n 
1 53  TYR n 
1 54  THR n 
1 55  LEU n 
1 56  GLY n 
1 57  CYS n 
1 58  CYS n 
1 59  SER n 
1 60  LEU n 
1 61  THR n 
1 62  ALA n 
1 63  MET n 
1 64  ALA n 
1 65  SER n 
1 66  ALA n 
1 67  GLN n 
1 68  LEU n 
1 69  ASP n 
1 70  ALA n 
1 71  LEU n 
1 72  TRP n 
1 73  SER n 
1 74  GLN n 
1 75  LEU n 
1 76  SER n 
1 77  TRP n 
1 78  PRO n 
1 79  GLN n 
1 80  THR n 
1 81  PRO n 
1 82  LEU n 
1 83  PRO n 
1 84  VAL n 
1 85  LEU n 
1 86  ASP n 
1 87  ILE n 
1 88  GLY n 
1 89  CYS n 
1 90  GLY n 
1 91  PRO n 
1 92  GLY n 
1 93  ASP n 
1 94  ILE n 
1 95  ALA n 
1 96  ARG n 
1 97  LYS n 
1 98  VAL n 
1 99  LEU n 
1 100 ALA n 
1 101 PRO n 
1 102 ARG n 
1 103 LEU n 
1 104 PRO n 
1 105 ALA n 
1 106 GLY n 
1 107 THR n 
1 108 ARG n 
1 109 LEU n 
1 110 VAL n 
1 111 ALA n 
1 112 CYS n 
1 113 ASP n 
1 114 ILE n 
1 115 SER n 
1 116 PRO n 
1 117 GLU n 
1 118 MET n 
1 119 VAL n 
1 120 ASP n 
1 121 PHE n 
1 122 CYS n 
1 123 ARG n 
1 124 GLN n 
1 125 HIS n 
1 126 ASN n 
1 127 ALA n 
1 128 LEU n 
1 129 PRO n 
1 130 GLY n 
1 131 THR n 
1 132 ILE n 
1 133 THR n 
1 134 TYR n 
1 135 GLU n 
1 136 LEU n 
1 137 LEU n 
1 138 ASP n 
1 139 VAL n 
1 140 VAL n 
1 141 GLU n 
1 142 PRO n 
1 143 ARG n 
1 144 LEU n 
1 145 GLU n 
1 146 ASP n 
1 147 THR n 
1 148 VAL n 
1 149 VAL n 
1 150 TRP n 
1 151 ARG n 
1 152 ASN n 
1 153 GLY n 
1 154 PRO n 
1 155 PHE n 
1 156 GLY n 
1 157 LYS n 
1 158 VAL n 
1 159 PHE n 
1 160 CYS n 
1 161 MET n 
1 162 LEU n 
1 163 MET n 
1 164 LEU n 
1 165 HIS n 
1 166 LEU n 
1 167 VAL n 
1 168 PRO n 
1 169 ASP n 
1 170 ASN n 
1 171 ARG n 
1 172 LEU n 
1 173 ALA n 
1 174 VAL n 
1 175 LYS n 
1 176 ASN n 
1 177 ILE n 
1 178 HIS n 
1 179 LYS n 
1 180 LEU n 
1 181 LEU n 
1 182 VAL n 
1 183 PRO n 
1 184 GLY n 
1 185 GLY n 
1 186 GLU n 
1 187 ALA n 
1 188 VAL n 
1 189 PHE n 
1 190 SER n 
1 191 VAL n 
1 192 ILE n 
1 193 ALA n 
1 194 ASN n 
1 195 MET n 
1 196 ALA n 
1 197 LEU n 
1 198 CYS n 
1 199 ASP n 
1 200 ALA n 
1 201 TYR n 
1 202 GLU n 
1 203 GLU n 
1 204 MET n 
1 205 ALA n 
1 206 LYS n 
1 207 GLU n 
1 208 PRO n 
1 209 ARG n 
1 210 TRP n 
1 211 ALA n 
1 212 LEU n 
1 213 TYR n 
1 214 MET n 
1 215 GLN n 
1 216 ASP n 
1 217 VAL n 
1 218 GLU n 
1 219 LYS n 
1 220 PHE n 
1 221 VAL n 
1 222 SER n 
1 223 PRO n 
1 224 TYR n 
1 225 GLN n 
1 226 HIS n 
1 227 SER n 
1 228 GLU n 
1 229 ASP n 
1 230 PRO n 
1 231 VAL n 
1 232 GLY n 
1 233 GLU n 
1 234 PHE n 
1 235 ARG n 
1 236 LEU n 
1 237 LEU n 
1 238 LEU n 
1 239 GLU n 
1 240 SER n 
1 241 GLU n 
1 242 GLY n 
1 243 PHE n 
1 244 GLN n 
1 245 VAL n 
1 246 LEU n 
1 247 ARG n 
1 248 CYS n 
1 249 ASP n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 GLN n 
1 254 LYS n 
1 255 VAL n 
1 256 PHE n 
1 257 PHE n 
1 258 PRO n 
1 259 THR n 
1 260 ALA n 
1 261 GLU n 
1 262 THR n 
1 263 HIS n 
1 264 ARG n 
1 265 GLU n 
1 266 PHE n 
1 267 LEU n 
1 268 LYS n 
1 269 SER n 
1 270 VAL n 
1 271 CYS n 
1 272 ALA n 
1 273 PHE n 
1 274 LEU n 
1 275 TYR n 
1 276 ARG n 
1 277 ILE n 
1 278 PRO n 
1 279 GLU n 
1 280 GLU n 
1 281 GLN n 
1 282 LYS n 
1 283 ASP n 
1 284 ASP n 
1 285 PHE n 
1 286 PHE n 
1 287 ASP n 
1 288 ASP n 
1 289 TRP n 
1 290 LEU n 
1 291 GLN n 
1 292 ARG n 
1 293 LEU n 
1 294 GLU n 
1 295 LYS n 
1 296 LEU n 
1 297 LYS n 
1 298 GLY n 
1 299 THR n 
1 300 SER n 
1 301 GLN n 
1 302 GLY n 
1 303 VAL n 
1 304 GLY n 
1 305 ARG n 
1 306 ASN n 
1 307 GLY n 
1 308 GLU n 
1 309 ALA n 
1 310 GLU n 
1 311 TYR n 
1 312 TYR n 
1 313 ILE n 
1 314 HIS n 
1 315 LEU n 
1 316 SER n 
1 317 VAL n 
1 318 ILE n 
1 319 THR n 
1 320 ALA n 
1 321 LEU n 
1 322 ALA n 
1 323 ARG n 
1 324 LYS n 
1 325 PHE n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   325 
_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                    ? 
_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      'Locusta migratoria' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     7004 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
4VP non-polymer         . 4-ethenylphenol      ? 'C8 H8 O'         120.149 
ALA 'L-peptide linking' y ALANINE              ? 'C3 H7 N O2'      89.093  
ARG 'L-peptide linking' y ARGININE             ? 'C6 H15 N4 O2 1'  175.209 
ASN 'L-peptide linking' y ASPARAGINE           ? 'C4 H8 N2 O3'     132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'      ? 'C4 H7 N O4'      133.103 
CYS 'L-peptide linking' y CYSTEINE             ? 'C3 H7 N O2 S'    121.158 
GLN 'L-peptide linking' y GLUTAMINE            ? 'C5 H10 N2 O3'    146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'      ? 'C5 H9 N O4'      147.129 
GLY 'peptide linking'   y GLYCINE              ? 'C2 H5 N O2'      75.067  
HIS 'L-peptide linking' y HISTIDINE            ? 'C6 H10 N3 O2 1'  156.162 
HOH non-polymer         . WATER                ? 'H2 O'            18.015  
ILE 'L-peptide linking' y ISOLEUCINE           ? 'C6 H13 N O2'     131.173 
LEU 'L-peptide linking' y LEUCINE              ? 'C6 H13 N O2'     131.173 
LYS 'L-peptide linking' y LYSINE               ? 'C6 H15 N2 O2 1'  147.195 
MET 'L-peptide linking' y METHIONINE           ? 'C5 H11 N O2 S'   149.211 
PHE 'L-peptide linking' y PHENYLALANINE        ? 'C9 H11 N O2'     165.189 
PRO 'L-peptide linking' y PROLINE              ? 'C5 H9 N O2'      115.130 
SAM non-polymer         . S-ADENOSYLMETHIONINE ? 'C15 H22 N6 O5 S' 398.437 
SER 'L-peptide linking' y SERINE               ? 'C3 H7 N O3'      105.093 
THR 'L-peptide linking' y THREONINE            ? 'C4 H9 N O3'      119.119 
TRP 'L-peptide linking' y TRYPTOPHAN           ? 'C11 H12 N2 O2'   204.225 
TYR 'L-peptide linking' y TYROSINE             ? 'C9 H11 N O3'     181.189 
VAL 'L-peptide linking' y VALINE               ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   -27 ?   ?   ?   A . n 
A 1 2   GLY 2   -26 ?   ?   ?   A . n 
A 1 3   SER 3   -25 ?   ?   ?   A . n 
A 1 4   HIS 4   -24 ?   ?   ?   A . n 
A 1 5   HIS 5   -23 ?   ?   ?   A . n 
A 1 6   HIS 6   -22 ?   ?   ?   A . n 
A 1 7   HIS 7   -21 ?   ?   ?   A . n 
A 1 8   HIS 8   -20 ?   ?   ?   A . n 
A 1 9   HIS 9   -19 ?   ?   ?   A . n 
A 1 10  HIS 10  -18 ?   ?   ?   A . n 
A 1 11  HIS 11  -17 ?   ?   ?   A . n 
A 1 12  GLY 12  -16 ?   ?   ?   A . n 
A 1 13  SER 13  -15 ?   ?   ?   A . n 
A 1 14  ASP 14  -14 ?   ?   ?   A . n 
A 1 15  TYR 15  -13 ?   ?   ?   A . n 
A 1 16  ASP 16  -12 ?   ?   ?   A . n 
A 1 17  ILE 17  -11 ?   ?   ?   A . n 
A 1 18  PRO 18  -10 ?   ?   ?   A . n 
A 1 19  THR 19  -9  ?   ?   ?   A . n 
A 1 20  THR 20  -8  ?   ?   ?   A . n 
A 1 21  GLU 21  -7  ?   ?   ?   A . n 
A 1 22  ASN 22  -6  ?   ?   ?   A . n 
A 1 23  LEU 23  -5  ?   ?   ?   A . n 
A 1 24  TYR 24  -4  ?   ?   ?   A . n 
A 1 25  PHE 25  -3  ?   ?   ?   A . n 
A 1 26  GLN 26  -2  ?   ?   ?   A . n 
A 1 27  GLY 27  -1  ?   ?   ?   A . n 
A 1 28  SER 28  0   ?   ?   ?   A . n 
A 1 29  MET 29  1   ?   ?   ?   A . n 
A 1 30  GLU 30  2   ?   ?   ?   A . n 
A 1 31  LYS 31  3   ?   ?   ?   A . n 
A 1 32  GLN 32  4   ?   ?   ?   A . n 
A 1 33  ASP 33  5   ?   ?   ?   A . n 
A 1 34  THR 34  6   ?   ?   ?   A . n 
A 1 35  HIS 35  7   ?   ?   ?   A . n 
A 1 36  VAL 36  8   ?   ?   ?   A . n 
A 1 37  ASN 37  9   ?   ?   ?   A . n 
A 1 38  THR 38  10  ?   ?   ?   A . n 
A 1 39  GLU 39  11  ?   ?   ?   A . n 
A 1 40  LYS 40  12  ?   ?   ?   A . n 
A 1 41  GLN 41  13  ?   ?   ?   A . n 
A 1 42  GLU 42  14  14  GLU GLU A . n 
A 1 43  ALA 43  15  15  ALA ALA A . n 
A 1 44  TYR 44  16  16  TYR TYR A . n 
A 1 45  ARG 45  17  17  ARG ARG A . n 
A 1 46  GLY 46  18  18  GLY GLY A . n 
A 1 47  ILE 47  19  19  ILE ILE A . n 
A 1 48  ASP 48  20  20  ASP ASP A . n 
A 1 49  LYS 49  21  21  LYS LYS A . n 
A 1 50  PRO 50  22  22  PRO PRO A . n 
A 1 51  HIS 51  23  23  HIS HIS A . n 
A 1 52  LEU 52  24  24  LEU LEU A . n 
A 1 53  TYR 53  25  25  TYR TYR A . n 
A 1 54  THR 54  26  26  THR THR A . n 
A 1 55  LEU 55  27  27  LEU LEU A . n 
A 1 56  GLY 56  28  28  GLY GLY A . n 
A 1 57  CYS 57  29  29  CYS CYS A . n 
A 1 58  CYS 58  30  30  CYS CYS A . n 
A 1 59  SER 59  31  31  SER SER A . n 
A 1 60  LEU 60  32  32  LEU LEU A . n 
A 1 61  THR 61  33  33  THR THR A . n 
A 1 62  ALA 62  34  34  ALA ALA A . n 
A 1 63  MET 63  35  35  MET MET A . n 
A 1 64  ALA 64  36  36  ALA ALA A . n 
A 1 65  SER 65  37  37  SER SER A . n 
A 1 66  ALA 66  38  38  ALA ALA A . n 
A 1 67  GLN 67  39  39  GLN GLN A . n 
A 1 68  LEU 68  40  40  LEU LEU A . n 
A 1 69  ASP 69  41  41  ASP ASP A . n 
A 1 70  ALA 70  42  42  ALA ALA A . n 
A 1 71  LEU 71  43  43  LEU LEU A . n 
A 1 72  TRP 72  44  44  TRP TRP A . n 
A 1 73  SER 73  45  45  SER SER A . n 
A 1 74  GLN 74  46  46  GLN GLN A . n 
A 1 75  LEU 75  47  47  LEU LEU A . n 
A 1 76  SER 76  48  48  SER SER A . n 
A 1 77  TRP 77  49  49  TRP TRP A . n 
A 1 78  PRO 78  50  50  PRO PRO A . n 
A 1 79  GLN 79  51  51  GLN GLN A . n 
A 1 80  THR 80  52  52  THR THR A . n 
A 1 81  PRO 81  53  53  PRO PRO A . n 
A 1 82  LEU 82  54  54  LEU LEU A . n 
A 1 83  PRO 83  55  55  PRO PRO A . n 
A 1 84  VAL 84  56  56  VAL VAL A . n 
A 1 85  LEU 85  57  57  LEU LEU A . n 
A 1 86  ASP 86  58  58  ASP ASP A . n 
A 1 87  ILE 87  59  59  ILE ILE A . n 
A 1 88  GLY 88  60  60  GLY GLY A . n 
A 1 89  CYS 89  61  61  CYS CYS A . n 
A 1 90  GLY 90  62  62  GLY GLY A . n 
A 1 91  PRO 91  63  63  PRO PRO A . n 
A 1 92  GLY 92  64  64  GLY GLY A . n 
A 1 93  ASP 93  65  65  ASP ASP A . n 
A 1 94  ILE 94  66  66  ILE ILE A . n 
A 1 95  ALA 95  67  67  ALA ALA A . n 
A 1 96  ARG 96  68  68  ARG ARG A . n 
A 1 97  LYS 97  69  69  LYS LYS A . n 
A 1 98  VAL 98  70  70  VAL VAL A . n 
A 1 99  LEU 99  71  71  LEU LEU A . n 
A 1 100 ALA 100 72  72  ALA ALA A . n 
A 1 101 PRO 101 73  73  PRO PRO A . n 
A 1 102 ARG 102 74  74  ARG ARG A . n 
A 1 103 LEU 103 75  75  LEU LEU A . n 
A 1 104 PRO 104 76  76  PRO PRO A . n 
A 1 105 ALA 105 77  77  ALA ALA A . n 
A 1 106 GLY 106 78  78  GLY GLY A . n 
A 1 107 THR 107 79  79  THR THR A . n 
A 1 108 ARG 108 80  80  ARG ARG A . n 
A 1 109 LEU 109 81  81  LEU LEU A . n 
A 1 110 VAL 110 82  82  VAL VAL A . n 
A 1 111 ALA 111 83  83  ALA ALA A . n 
A 1 112 CYS 112 84  84  CYS CYS A . n 
A 1 113 ASP 113 85  85  ASP ASP A . n 
A 1 114 ILE 114 86  86  ILE ILE A . n 
A 1 115 SER 115 87  87  SER SER A . n 
A 1 116 PRO 116 88  88  PRO PRO A . n 
A 1 117 GLU 117 89  89  GLU GLU A . n 
A 1 118 MET 118 90  90  MET MET A . n 
A 1 119 VAL 119 91  91  VAL VAL A . n 
A 1 120 ASP 120 92  92  ASP ASP A . n 
A 1 121 PHE 121 93  93  PHE PHE A . n 
A 1 122 CYS 122 94  94  CYS CYS A . n 
A 1 123 ARG 123 95  95  ARG ARG A . n 
A 1 124 GLN 124 96  96  GLN GLN A . n 
A 1 125 HIS 125 97  97  HIS HIS A . n 
A 1 126 ASN 126 98  98  ASN ASN A . n 
A 1 127 ALA 127 99  99  ALA ALA A . n 
A 1 128 LEU 128 100 100 LEU LEU A . n 
A 1 129 PRO 129 101 101 PRO PRO A . n 
A 1 130 GLY 130 102 102 GLY GLY A . n 
A 1 131 THR 131 103 103 THR THR A . n 
A 1 132 ILE 132 104 104 ILE ILE A . n 
A 1 133 THR 133 105 105 THR THR A . n 
A 1 134 TYR 134 106 106 TYR TYR A . n 
A 1 135 GLU 135 107 107 GLU GLU A . n 
A 1 136 LEU 136 108 108 LEU LEU A . n 
A 1 137 LEU 137 109 109 LEU LEU A . n 
A 1 138 ASP 138 110 110 ASP ASP A . n 
A 1 139 VAL 139 111 111 VAL VAL A . n 
A 1 140 VAL 140 112 112 VAL VAL A . n 
A 1 141 GLU 141 113 113 GLU GLU A . n 
A 1 142 PRO 142 114 114 PRO PRO A . n 
A 1 143 ARG 143 115 115 ARG ARG A . n 
A 1 144 LEU 144 116 116 LEU LEU A . n 
A 1 145 GLU 145 117 117 GLU GLU A . n 
A 1 146 ASP 146 118 118 ASP ASP A . n 
A 1 147 THR 147 119 119 THR THR A . n 
A 1 148 VAL 148 120 120 VAL VAL A . n 
A 1 149 VAL 149 121 121 VAL VAL A . n 
A 1 150 TRP 150 122 122 TRP TRP A . n 
A 1 151 ARG 151 123 123 ARG ARG A . n 
A 1 152 ASN 152 124 124 ASN ASN A . n 
A 1 153 GLY 153 125 125 GLY GLY A . n 
A 1 154 PRO 154 126 126 PRO PRO A . n 
A 1 155 PHE 155 127 127 PHE PHE A . n 
A 1 156 GLY 156 128 128 GLY GLY A . n 
A 1 157 LYS 157 129 129 LYS LYS A . n 
A 1 158 VAL 158 130 130 VAL VAL A . n 
A 1 159 PHE 159 131 131 PHE PHE A . n 
A 1 160 CYS 160 132 132 CYS CYS A . n 
A 1 161 MET 161 133 133 MET MET A . n 
A 1 162 LEU 162 134 134 LEU LEU A . n 
A 1 163 MET 163 135 135 MET MET A . n 
A 1 164 LEU 164 136 136 LEU LEU A . n 
A 1 165 HIS 165 137 137 HIS HIS A . n 
A 1 166 LEU 166 138 138 LEU LEU A . n 
A 1 167 VAL 167 139 139 VAL VAL A . n 
A 1 168 PRO 168 140 140 PRO PRO A . n 
A 1 169 ASP 169 141 141 ASP ASP A . n 
A 1 170 ASN 170 142 142 ASN ASN A . n 
A 1 171 ARG 171 143 143 ARG ARG A . n 
A 1 172 LEU 172 144 144 LEU LEU A . n 
A 1 173 ALA 173 145 145 ALA ALA A . n 
A 1 174 VAL 174 146 146 VAL VAL A . n 
A 1 175 LYS 175 147 147 LYS LYS A . n 
A 1 176 ASN 176 148 148 ASN ASN A . n 
A 1 177 ILE 177 149 149 ILE ILE A . n 
A 1 178 HIS 178 150 150 HIS HIS A . n 
A 1 179 LYS 179 151 151 LYS LYS A . n 
A 1 180 LEU 180 152 152 LEU LEU A . n 
A 1 181 LEU 181 153 153 LEU LEU A . n 
A 1 182 VAL 182 154 154 VAL VAL A . n 
A 1 183 PRO 183 155 155 PRO PRO A . n 
A 1 184 GLY 184 156 156 GLY GLY A . n 
A 1 185 GLY 185 157 157 GLY GLY A . n 
A 1 186 GLU 186 158 158 GLU GLU A . n 
A 1 187 ALA 187 159 159 ALA ALA A . n 
A 1 188 VAL 188 160 160 VAL VAL A . n 
A 1 189 PHE 189 161 161 PHE PHE A . n 
A 1 190 SER 190 162 162 SER SER A . n 
A 1 191 VAL 191 163 163 VAL VAL A . n 
A 1 192 ILE 192 164 164 ILE ILE A . n 
A 1 193 ALA 193 165 165 ALA ALA A . n 
A 1 194 ASN 194 166 166 ASN ASN A . n 
A 1 195 MET 195 167 167 MET MET A . n 
A 1 196 ALA 196 168 168 ALA ALA A . n 
A 1 197 LEU 197 169 169 LEU LEU A . n 
A 1 198 CYS 198 170 170 CYS CYS A . n 
A 1 199 ASP 199 171 171 ASP ASP A . n 
A 1 200 ALA 200 172 172 ALA ALA A . n 
A 1 201 TYR 201 173 173 TYR TYR A . n 
A 1 202 GLU 202 174 174 GLU GLU A . n 
A 1 203 GLU 203 175 175 GLU GLU A . n 
A 1 204 MET 204 176 176 MET MET A . n 
A 1 205 ALA 205 177 177 ALA ALA A . n 
A 1 206 LYS 206 178 178 LYS LYS A . n 
A 1 207 GLU 207 179 179 GLU GLU A . n 
A 1 208 PRO 208 180 180 PRO PRO A . n 
A 1 209 ARG 209 181 181 ARG ARG A . n 
A 1 210 TRP 210 182 182 TRP TRP A . n 
A 1 211 ALA 211 183 183 ALA ALA A . n 
A 1 212 LEU 212 184 184 LEU LEU A . n 
A 1 213 TYR 213 185 185 TYR TYR A . n 
A 1 214 MET 214 186 186 MET MET A . n 
A 1 215 GLN 215 187 187 GLN GLN A . n 
A 1 216 ASP 216 188 188 ASP ASP A . n 
A 1 217 VAL 217 189 189 VAL VAL A . n 
A 1 218 GLU 218 190 190 GLU GLU A . n 
A 1 219 LYS 219 191 191 LYS LYS A . n 
A 1 220 PHE 220 192 192 PHE PHE A . n 
A 1 221 VAL 221 193 193 VAL VAL A . n 
A 1 222 SER 222 194 194 SER SER A . n 
A 1 223 PRO 223 195 195 PRO PRO A . n 
A 1 224 TYR 224 196 196 TYR TYR A . n 
A 1 225 GLN 225 197 197 GLN GLN A . n 
A 1 226 HIS 226 198 198 HIS HIS A . n 
A 1 227 SER 227 199 199 SER SER A . n 
A 1 228 GLU 228 200 200 GLU GLU A . n 
A 1 229 ASP 229 201 201 ASP ASP A . n 
A 1 230 PRO 230 202 202 PRO PRO A . n 
A 1 231 VAL 231 203 203 VAL VAL A . n 
A 1 232 GLY 232 204 204 GLY GLY A . n 
A 1 233 GLU 233 205 205 GLU GLU A . n 
A 1 234 PHE 234 206 206 PHE PHE A . n 
A 1 235 ARG 235 207 207 ARG ARG A . n 
A 1 236 LEU 236 208 208 LEU LEU A . n 
A 1 237 LEU 237 209 209 LEU LEU A . n 
A 1 238 LEU 238 210 210 LEU LEU A . n 
A 1 239 GLU 239 211 211 GLU GLU A . n 
A 1 240 SER 240 212 212 SER SER A . n 
A 1 241 GLU 241 213 213 GLU GLU A . n 
A 1 242 GLY 242 214 214 GLY GLY A . n 
A 1 243 PHE 243 215 215 PHE PHE A . n 
A 1 244 GLN 244 216 216 GLN GLN A . n 
A 1 245 VAL 245 217 217 VAL VAL A . n 
A 1 246 LEU 246 218 218 LEU LEU A . n 
A 1 247 ARG 247 219 219 ARG ARG A . n 
A 1 248 CYS 248 220 220 CYS CYS A . n 
A 1 249 ASP 249 221 221 ASP ASP A . n 
A 1 250 LEU 250 222 222 LEU LEU A . n 
A 1 251 GLY 251 223 223 GLY GLY A . n 
A 1 252 PRO 252 224 224 PRO PRO A . n 
A 1 253 GLN 253 225 225 GLN GLN A . n 
A 1 254 LYS 254 226 226 LYS LYS A . n 
A 1 255 VAL 255 227 227 VAL VAL A . n 
A 1 256 PHE 256 228 228 PHE PHE A . n 
A 1 257 PHE 257 229 229 PHE PHE A . n 
A 1 258 PRO 258 230 230 PRO PRO A . n 
A 1 259 THR 259 231 231 THR THR A . n 
A 1 260 ALA 260 232 232 ALA ALA A . n 
A 1 261 GLU 261 233 233 GLU GLU A . n 
A 1 262 THR 262 234 234 THR THR A . n 
A 1 263 HIS 263 235 235 HIS HIS A . n 
A 1 264 ARG 264 236 236 ARG ARG A . n 
A 1 265 GLU 265 237 237 GLU GLU A . n 
A 1 266 PHE 266 238 238 PHE PHE A . n 
A 1 267 LEU 267 239 239 LEU LEU A . n 
A 1 268 LYS 268 240 240 LYS LYS A . n 
A 1 269 SER 269 241 241 SER SER A . n 
A 1 270 VAL 270 242 242 VAL VAL A . n 
A 1 271 CYS 271 243 243 CYS CYS A . n 
A 1 272 ALA 272 244 244 ALA ALA A . n 
A 1 273 PHE 273 245 245 PHE PHE A . n 
A 1 274 LEU 274 246 246 LEU LEU A . n 
A 1 275 TYR 275 247 247 TYR TYR A . n 
A 1 276 ARG 276 248 248 ARG ARG A . n 
A 1 277 ILE 277 249 249 ILE ILE A . n 
A 1 278 PRO 278 250 250 PRO PRO A . n 
A 1 279 GLU 279 251 251 GLU GLU A . n 
A 1 280 GLU 280 252 252 GLU GLU A . n 
A 1 281 GLN 281 253 253 GLN GLN A . n 
A 1 282 LYS 282 254 254 LYS LYS A . n 
A 1 283 ASP 283 255 255 ASP ASP A . n 
A 1 284 ASP 284 256 256 ASP ASP A . n 
A 1 285 PHE 285 257 257 PHE PHE A . n 
A 1 286 PHE 286 258 258 PHE PHE A . n 
A 1 287 ASP 287 259 259 ASP ASP A . n 
A 1 288 ASP 288 260 260 ASP ASP A . n 
A 1 289 TRP 289 261 261 TRP TRP A . n 
A 1 290 LEU 290 262 262 LEU LEU A . n 
A 1 291 GLN 291 263 263 GLN GLN A . n 
A 1 292 ARG 292 264 264 ARG ARG A . n 
A 1 293 LEU 293 265 265 LEU LEU A . n 
A 1 294 GLU 294 266 266 GLU GLU A . n 
A 1 295 LYS 295 267 267 LYS LYS A . n 
A 1 296 LEU 296 268 268 LEU LEU A . n 
A 1 297 LYS 297 269 269 LYS LYS A . n 
A 1 298 GLY 298 270 270 GLY GLY A . n 
A 1 299 THR 299 271 271 THR THR A . n 
A 1 300 SER 300 272 272 SER SER A . n 
A 1 301 GLN 301 273 273 GLN GLN A . n 
A 1 302 GLY 302 274 274 GLY GLY A . n 
A 1 303 VAL 303 275 275 VAL VAL A . n 
A 1 304 GLY 304 276 276 GLY GLY A . n 
A 1 305 ARG 305 277 277 ARG ARG A . n 
A 1 306 ASN 306 278 278 ASN ASN A . n 
A 1 307 GLY 307 279 279 GLY GLY A . n 
A 1 308 GLU 308 280 280 GLU GLU A . n 
A 1 309 ALA 309 281 281 ALA ALA A . n 
A 1 310 GLU 310 282 282 GLU GLU A . n 
A 1 311 TYR 311 283 283 TYR TYR A . n 
A 1 312 TYR 312 284 284 TYR TYR A . n 
A 1 313 ILE 313 285 285 ILE ILE A . n 
A 1 314 HIS 314 286 286 HIS HIS A . n 
A 1 315 LEU 315 287 287 LEU LEU A . n 
A 1 316 SER 316 288 288 SER SER A . n 
A 1 317 VAL 317 289 289 VAL VAL A . n 
A 1 318 ILE 318 290 290 ILE ILE A . n 
A 1 319 THR 319 291 291 THR THR A . n 
A 1 320 ALA 320 292 292 ALA ALA A . n 
A 1 321 LEU 321 293 293 LEU LEU A . n 
A 1 322 ALA 322 294 294 ALA ALA A . n 
A 1 323 ARG 323 295 295 ARG ARG A . n 
A 1 324 LYS 324 296 296 LYS LYS A . n 
A 1 325 PHE 325 297 297 PHE PHE A . n 
B 1 1   MET 1   -27 ?   ?   ?   B . n 
B 1 2   GLY 2   -26 ?   ?   ?   B . n 
B 1 3   SER 3   -25 ?   ?   ?   B . n 
B 1 4   HIS 4   -24 ?   ?   ?   B . n 
B 1 5   HIS 5   -23 ?   ?   ?   B . n 
B 1 6   HIS 6   -22 ?   ?   ?   B . n 
B 1 7   HIS 7   -21 ?   ?   ?   B . n 
B 1 8   HIS 8   -20 ?   ?   ?   B . n 
B 1 9   HIS 9   -19 ?   ?   ?   B . n 
B 1 10  HIS 10  -18 ?   ?   ?   B . n 
B 1 11  HIS 11  -17 ?   ?   ?   B . n 
B 1 12  GLY 12  -16 ?   ?   ?   B . n 
B 1 13  SER 13  -15 ?   ?   ?   B . n 
B 1 14  ASP 14  -14 ?   ?   ?   B . n 
B 1 15  TYR 15  -13 ?   ?   ?   B . n 
B 1 16  ASP 16  -12 ?   ?   ?   B . n 
B 1 17  ILE 17  -11 ?   ?   ?   B . n 
B 1 18  PRO 18  -10 ?   ?   ?   B . n 
B 1 19  THR 19  -9  ?   ?   ?   B . n 
B 1 20  THR 20  -8  ?   ?   ?   B . n 
B 1 21  GLU 21  -7  ?   ?   ?   B . n 
B 1 22  ASN 22  -6  ?   ?   ?   B . n 
B 1 23  LEU 23  -5  ?   ?   ?   B . n 
B 1 24  TYR 24  -4  ?   ?   ?   B . n 
B 1 25  PHE 25  -3  ?   ?   ?   B . n 
B 1 26  GLN 26  -2  ?   ?   ?   B . n 
B 1 27  GLY 27  -1  ?   ?   ?   B . n 
B 1 28  SER 28  0   ?   ?   ?   B . n 
B 1 29  MET 29  1   ?   ?   ?   B . n 
B 1 30  GLU 30  2   ?   ?   ?   B . n 
B 1 31  LYS 31  3   ?   ?   ?   B . n 
B 1 32  GLN 32  4   ?   ?   ?   B . n 
B 1 33  ASP 33  5   ?   ?   ?   B . n 
B 1 34  THR 34  6   ?   ?   ?   B . n 
B 1 35  HIS 35  7   ?   ?   ?   B . n 
B 1 36  VAL 36  8   ?   ?   ?   B . n 
B 1 37  ASN 37  9   ?   ?   ?   B . n 
B 1 38  THR 38  10  ?   ?   ?   B . n 
B 1 39  GLU 39  11  ?   ?   ?   B . n 
B 1 40  LYS 40  12  ?   ?   ?   B . n 
B 1 41  GLN 41  13  ?   ?   ?   B . n 
B 1 42  GLU 42  14  14  GLU GLU B . n 
B 1 43  ALA 43  15  15  ALA ALA B . n 
B 1 44  TYR 44  16  16  TYR TYR B . n 
B 1 45  ARG 45  17  17  ARG ARG B . n 
B 1 46  GLY 46  18  18  GLY GLY B . n 
B 1 47  ILE 47  19  19  ILE ILE B . n 
B 1 48  ASP 48  20  20  ASP ASP B . n 
B 1 49  LYS 49  21  21  LYS LYS B . n 
B 1 50  PRO 50  22  22  PRO PRO B . n 
B 1 51  HIS 51  23  23  HIS HIS B . n 
B 1 52  LEU 52  24  24  LEU LEU B . n 
B 1 53  TYR 53  25  25  TYR TYR B . n 
B 1 54  THR 54  26  26  THR THR B . n 
B 1 55  LEU 55  27  27  LEU LEU B . n 
B 1 56  GLY 56  28  28  GLY GLY B . n 
B 1 57  CYS 57  29  29  CYS CYS B . n 
B 1 58  CYS 58  30  30  CYS CYS B . n 
B 1 59  SER 59  31  31  SER SER B . n 
B 1 60  LEU 60  32  32  LEU LEU B . n 
B 1 61  THR 61  33  33  THR THR B . n 
B 1 62  ALA 62  34  34  ALA ALA B . n 
B 1 63  MET 63  35  35  MET MET B . n 
B 1 64  ALA 64  36  36  ALA ALA B . n 
B 1 65  SER 65  37  37  SER SER B . n 
B 1 66  ALA 66  38  38  ALA ALA B . n 
B 1 67  GLN 67  39  39  GLN GLN B . n 
B 1 68  LEU 68  40  40  LEU LEU B . n 
B 1 69  ASP 69  41  41  ASP ASP B . n 
B 1 70  ALA 70  42  42  ALA ALA B . n 
B 1 71  LEU 71  43  43  LEU LEU B . n 
B 1 72  TRP 72  44  44  TRP TRP B . n 
B 1 73  SER 73  45  45  SER SER B . n 
B 1 74  GLN 74  46  46  GLN GLN B . n 
B 1 75  LEU 75  47  47  LEU LEU B . n 
B 1 76  SER 76  48  48  SER SER B . n 
B 1 77  TRP 77  49  49  TRP TRP B . n 
B 1 78  PRO 78  50  50  PRO PRO B . n 
B 1 79  GLN 79  51  51  GLN GLN B . n 
B 1 80  THR 80  52  52  THR THR B . n 
B 1 81  PRO 81  53  53  PRO PRO B . n 
B 1 82  LEU 82  54  54  LEU LEU B . n 
B 1 83  PRO 83  55  55  PRO PRO B . n 
B 1 84  VAL 84  56  56  VAL VAL B . n 
B 1 85  LEU 85  57  57  LEU LEU B . n 
B 1 86  ASP 86  58  58  ASP ASP B . n 
B 1 87  ILE 87  59  59  ILE ILE B . n 
B 1 88  GLY 88  60  60  GLY GLY B . n 
B 1 89  CYS 89  61  61  CYS CYS B . n 
B 1 90  GLY 90  62  62  GLY GLY B . n 
B 1 91  PRO 91  63  63  PRO PRO B . n 
B 1 92  GLY 92  64  64  GLY GLY B . n 
B 1 93  ASP 93  65  65  ASP ASP B . n 
B 1 94  ILE 94  66  66  ILE ILE B . n 
B 1 95  ALA 95  67  67  ALA ALA B . n 
B 1 96  ARG 96  68  68  ARG ARG B . n 
B 1 97  LYS 97  69  69  LYS LYS B . n 
B 1 98  VAL 98  70  70  VAL VAL B . n 
B 1 99  LEU 99  71  71  LEU LEU B . n 
B 1 100 ALA 100 72  72  ALA ALA B . n 
B 1 101 PRO 101 73  73  PRO PRO B . n 
B 1 102 ARG 102 74  74  ARG ARG B . n 
B 1 103 LEU 103 75  75  LEU LEU B . n 
B 1 104 PRO 104 76  76  PRO PRO B . n 
B 1 105 ALA 105 77  77  ALA ALA B . n 
B 1 106 GLY 106 78  78  GLY GLY B . n 
B 1 107 THR 107 79  79  THR THR B . n 
B 1 108 ARG 108 80  80  ARG ARG B . n 
B 1 109 LEU 109 81  81  LEU LEU B . n 
B 1 110 VAL 110 82  82  VAL VAL B . n 
B 1 111 ALA 111 83  83  ALA ALA B . n 
B 1 112 CYS 112 84  84  CYS CYS B . n 
B 1 113 ASP 113 85  85  ASP ASP B . n 
B 1 114 ILE 114 86  86  ILE ILE B . n 
B 1 115 SER 115 87  87  SER SER B . n 
B 1 116 PRO 116 88  88  PRO PRO B . n 
B 1 117 GLU 117 89  89  GLU GLU B . n 
B 1 118 MET 118 90  90  MET MET B . n 
B 1 119 VAL 119 91  91  VAL VAL B . n 
B 1 120 ASP 120 92  92  ASP ASP B . n 
B 1 121 PHE 121 93  93  PHE PHE B . n 
B 1 122 CYS 122 94  94  CYS CYS B . n 
B 1 123 ARG 123 95  95  ARG ARG B . n 
B 1 124 GLN 124 96  96  GLN GLN B . n 
B 1 125 HIS 125 97  97  HIS HIS B . n 
B 1 126 ASN 126 98  98  ASN ASN B . n 
B 1 127 ALA 127 99  99  ALA ALA B . n 
B 1 128 LEU 128 100 100 LEU LEU B . n 
B 1 129 PRO 129 101 101 PRO PRO B . n 
B 1 130 GLY 130 102 102 GLY GLY B . n 
B 1 131 THR 131 103 103 THR THR B . n 
B 1 132 ILE 132 104 104 ILE ILE B . n 
B 1 133 THR 133 105 105 THR THR B . n 
B 1 134 TYR 134 106 106 TYR TYR B . n 
B 1 135 GLU 135 107 107 GLU GLU B . n 
B 1 136 LEU 136 108 108 LEU LEU B . n 
B 1 137 LEU 137 109 109 LEU LEU B . n 
B 1 138 ASP 138 110 110 ASP ASP B . n 
B 1 139 VAL 139 111 111 VAL VAL B . n 
B 1 140 VAL 140 112 112 VAL VAL B . n 
B 1 141 GLU 141 113 113 GLU GLU B . n 
B 1 142 PRO 142 114 114 PRO PRO B . n 
B 1 143 ARG 143 115 115 ARG ARG B . n 
B 1 144 LEU 144 116 116 LEU LEU B . n 
B 1 145 GLU 145 117 117 GLU GLU B . n 
B 1 146 ASP 146 118 118 ASP ASP B . n 
B 1 147 THR 147 119 119 THR THR B . n 
B 1 148 VAL 148 120 120 VAL VAL B . n 
B 1 149 VAL 149 121 121 VAL VAL B . n 
B 1 150 TRP 150 122 122 TRP TRP B . n 
B 1 151 ARG 151 123 123 ARG ARG B . n 
B 1 152 ASN 152 124 124 ASN ASN B . n 
B 1 153 GLY 153 125 125 GLY GLY B . n 
B 1 154 PRO 154 126 126 PRO PRO B . n 
B 1 155 PHE 155 127 127 PHE PHE B . n 
B 1 156 GLY 156 128 128 GLY GLY B . n 
B 1 157 LYS 157 129 129 LYS LYS B . n 
B 1 158 VAL 158 130 130 VAL VAL B . n 
B 1 159 PHE 159 131 131 PHE PHE B . n 
B 1 160 CYS 160 132 132 CYS CYS B . n 
B 1 161 MET 161 133 133 MET MET B . n 
B 1 162 LEU 162 134 134 LEU LEU B . n 
B 1 163 MET 163 135 135 MET MET B . n 
B 1 164 LEU 164 136 136 LEU LEU B . n 
B 1 165 HIS 165 137 137 HIS HIS B . n 
B 1 166 LEU 166 138 138 LEU LEU B . n 
B 1 167 VAL 167 139 139 VAL VAL B . n 
B 1 168 PRO 168 140 140 PRO PRO B . n 
B 1 169 ASP 169 141 141 ASP ASP B . n 
B 1 170 ASN 170 142 142 ASN ASN B . n 
B 1 171 ARG 171 143 143 ARG ARG B . n 
B 1 172 LEU 172 144 144 LEU LEU B . n 
B 1 173 ALA 173 145 145 ALA ALA B . n 
B 1 174 VAL 174 146 146 VAL VAL B . n 
B 1 175 LYS 175 147 147 LYS LYS B . n 
B 1 176 ASN 176 148 148 ASN ASN B . n 
B 1 177 ILE 177 149 149 ILE ILE B . n 
B 1 178 HIS 178 150 150 HIS HIS B . n 
B 1 179 LYS 179 151 151 LYS LYS B . n 
B 1 180 LEU 180 152 152 LEU LEU B . n 
B 1 181 LEU 181 153 153 LEU LEU B . n 
B 1 182 VAL 182 154 154 VAL VAL B . n 
B 1 183 PRO 183 155 155 PRO PRO B . n 
B 1 184 GLY 184 156 156 GLY GLY B . n 
B 1 185 GLY 185 157 157 GLY GLY B . n 
B 1 186 GLU 186 158 158 GLU GLU B . n 
B 1 187 ALA 187 159 159 ALA ALA B . n 
B 1 188 VAL 188 160 160 VAL VAL B . n 
B 1 189 PHE 189 161 161 PHE PHE B . n 
B 1 190 SER 190 162 162 SER SER B . n 
B 1 191 VAL 191 163 163 VAL VAL B . n 
B 1 192 ILE 192 164 164 ILE ILE B . n 
B 1 193 ALA 193 165 165 ALA ALA B . n 
B 1 194 ASN 194 166 166 ASN ASN B . n 
B 1 195 MET 195 167 167 MET MET B . n 
B 1 196 ALA 196 168 168 ALA ALA B . n 
B 1 197 LEU 197 169 169 LEU LEU B . n 
B 1 198 CYS 198 170 170 CYS CYS B . n 
B 1 199 ASP 199 171 171 ASP ASP B . n 
B 1 200 ALA 200 172 172 ALA ALA B . n 
B 1 201 TYR 201 173 173 TYR TYR B . n 
B 1 202 GLU 202 174 174 GLU GLU B . n 
B 1 203 GLU 203 175 175 GLU GLU B . n 
B 1 204 MET 204 176 176 MET MET B . n 
B 1 205 ALA 205 177 177 ALA ALA B . n 
B 1 206 LYS 206 178 178 LYS LYS B . n 
B 1 207 GLU 207 179 179 GLU GLU B . n 
B 1 208 PRO 208 180 180 PRO PRO B . n 
B 1 209 ARG 209 181 181 ARG ARG B . n 
B 1 210 TRP 210 182 182 TRP TRP B . n 
B 1 211 ALA 211 183 183 ALA ALA B . n 
B 1 212 LEU 212 184 184 LEU LEU B . n 
B 1 213 TYR 213 185 185 TYR TYR B . n 
B 1 214 MET 214 186 186 MET MET B . n 
B 1 215 GLN 215 187 187 GLN GLN B . n 
B 1 216 ASP 216 188 188 ASP ASP B . n 
B 1 217 VAL 217 189 189 VAL VAL B . n 
B 1 218 GLU 218 190 190 GLU GLU B . n 
B 1 219 LYS 219 191 191 LYS LYS B . n 
B 1 220 PHE 220 192 192 PHE PHE B . n 
B 1 221 VAL 221 193 193 VAL VAL B . n 
B 1 222 SER 222 194 194 SER SER B . n 
B 1 223 PRO 223 195 195 PRO PRO B . n 
B 1 224 TYR 224 196 196 TYR TYR B . n 
B 1 225 GLN 225 197 197 GLN GLN B . n 
B 1 226 HIS 226 198 198 HIS HIS B . n 
B 1 227 SER 227 199 199 SER SER B . n 
B 1 228 GLU 228 200 200 GLU GLU B . n 
B 1 229 ASP 229 201 201 ASP ASP B . n 
B 1 230 PRO 230 202 202 PRO PRO B . n 
B 1 231 VAL 231 203 203 VAL VAL B . n 
B 1 232 GLY 232 204 204 GLY GLY B . n 
B 1 233 GLU 233 205 205 GLU GLU B . n 
B 1 234 PHE 234 206 206 PHE PHE B . n 
B 1 235 ARG 235 207 207 ARG ARG B . n 
B 1 236 LEU 236 208 208 LEU LEU B . n 
B 1 237 LEU 237 209 209 LEU LEU B . n 
B 1 238 LEU 238 210 210 LEU LEU B . n 
B 1 239 GLU 239 211 211 GLU GLU B . n 
B 1 240 SER 240 212 212 SER SER B . n 
B 1 241 GLU 241 213 213 GLU GLU B . n 
B 1 242 GLY 242 214 214 GLY GLY B . n 
B 1 243 PHE 243 215 215 PHE PHE B . n 
B 1 244 GLN 244 216 216 GLN GLN B . n 
B 1 245 VAL 245 217 217 VAL VAL B . n 
B 1 246 LEU 246 218 218 LEU LEU B . n 
B 1 247 ARG 247 219 219 ARG ARG B . n 
B 1 248 CYS 248 220 220 CYS CYS B . n 
B 1 249 ASP 249 221 221 ASP ASP B . n 
B 1 250 LEU 250 222 222 LEU LEU B . n 
B 1 251 GLY 251 223 223 GLY GLY B . n 
B 1 252 PRO 252 224 224 PRO PRO B . n 
B 1 253 GLN 253 225 225 GLN GLN B . n 
B 1 254 LYS 254 226 226 LYS LYS B . n 
B 1 255 VAL 255 227 227 VAL VAL B . n 
B 1 256 PHE 256 228 228 PHE PHE B . n 
B 1 257 PHE 257 229 229 PHE PHE B . n 
B 1 258 PRO 258 230 230 PRO PRO B . n 
B 1 259 THR 259 231 231 THR THR B . n 
B 1 260 ALA 260 232 232 ALA ALA B . n 
B 1 261 GLU 261 233 233 GLU GLU B . n 
B 1 262 THR 262 234 234 THR THR B . n 
B 1 263 HIS 263 235 235 HIS HIS B . n 
B 1 264 ARG 264 236 236 ARG ARG B . n 
B 1 265 GLU 265 237 237 GLU GLU B . n 
B 1 266 PHE 266 238 238 PHE PHE B . n 
B 1 267 LEU 267 239 239 LEU LEU B . n 
B 1 268 LYS 268 240 240 LYS LYS B . n 
B 1 269 SER 269 241 241 SER SER B . n 
B 1 270 VAL 270 242 242 VAL VAL B . n 
B 1 271 CYS 271 243 243 CYS CYS B . n 
B 1 272 ALA 272 244 244 ALA ALA B . n 
B 1 273 PHE 273 245 245 PHE PHE B . n 
B 1 274 LEU 274 246 246 LEU LEU B . n 
B 1 275 TYR 275 247 247 TYR TYR B . n 
B 1 276 ARG 276 248 248 ARG ARG B . n 
B 1 277 ILE 277 249 249 ILE ILE B . n 
B 1 278 PRO 278 250 250 PRO PRO B . n 
B 1 279 GLU 279 251 251 GLU GLU B . n 
B 1 280 GLU 280 252 252 GLU GLU B . n 
B 1 281 GLN 281 253 253 GLN GLN B . n 
B 1 282 LYS 282 254 254 LYS LYS B . n 
B 1 283 ASP 283 255 255 ASP ASP B . n 
B 1 284 ASP 284 256 256 ASP ASP B . n 
B 1 285 PHE 285 257 257 PHE PHE B . n 
B 1 286 PHE 286 258 258 PHE PHE B . n 
B 1 287 ASP 287 259 259 ASP ASP B . n 
B 1 288 ASP 288 260 260 ASP ASP B . n 
B 1 289 TRP 289 261 261 TRP TRP B . n 
B 1 290 LEU 290 262 262 LEU LEU B . n 
B 1 291 GLN 291 263 263 GLN GLN B . n 
B 1 292 ARG 292 264 264 ARG ARG B . n 
B 1 293 LEU 293 265 265 LEU LEU B . n 
B 1 294 GLU 294 266 266 GLU GLU B . n 
B 1 295 LYS 295 267 267 LYS LYS B . n 
B 1 296 LEU 296 268 268 LEU LEU B . n 
B 1 297 LYS 297 269 269 LYS LYS B . n 
B 1 298 GLY 298 270 270 GLY GLY B . n 
B 1 299 THR 299 271 271 THR THR B . n 
B 1 300 SER 300 272 272 SER SER B . n 
B 1 301 GLN 301 273 273 GLN GLN B . n 
B 1 302 GLY 302 274 274 GLY GLY B . n 
B 1 303 VAL 303 275 275 VAL VAL B . n 
B 1 304 GLY 304 276 276 GLY GLY B . n 
B 1 305 ARG 305 277 277 ARG ARG B . n 
B 1 306 ASN 306 278 278 ASN ASN B . n 
B 1 307 GLY 307 279 279 GLY GLY B . n 
B 1 308 GLU 308 280 280 GLU GLU B . n 
B 1 309 ALA 309 281 281 ALA ALA B . n 
B 1 310 GLU 310 282 282 GLU GLU B . n 
B 1 311 TYR 311 283 283 TYR TYR B . n 
B 1 312 TYR 312 284 284 TYR TYR B . n 
B 1 313 ILE 313 285 285 ILE ILE B . n 
B 1 314 HIS 314 286 286 HIS HIS B . n 
B 1 315 LEU 315 287 287 LEU LEU B . n 
B 1 316 SER 316 288 288 SER SER B . n 
B 1 317 VAL 317 289 289 VAL VAL B . n 
B 1 318 ILE 318 290 290 ILE ILE B . n 
B 1 319 THR 319 291 291 THR THR B . n 
B 1 320 ALA 320 292 292 ALA ALA B . n 
B 1 321 LEU 321 293 293 LEU LEU B . n 
B 1 322 ALA 322 294 294 ALA ALA B . n 
B 1 323 ARG 323 295 295 ARG ARG B . n 
B 1 324 LYS 324 296 296 LYS LYS B . n 
B 1 325 PHE 325 297 297 PHE PHE B . n 
C 1 1   MET 1   -27 ?   ?   ?   C . n 
C 1 2   GLY 2   -26 ?   ?   ?   C . n 
C 1 3   SER 3   -25 ?   ?   ?   C . n 
C 1 4   HIS 4   -24 ?   ?   ?   C . n 
C 1 5   HIS 5   -23 ?   ?   ?   C . n 
C 1 6   HIS 6   -22 ?   ?   ?   C . n 
C 1 7   HIS 7   -21 ?   ?   ?   C . n 
C 1 8   HIS 8   -20 ?   ?   ?   C . n 
C 1 9   HIS 9   -19 ?   ?   ?   C . n 
C 1 10  HIS 10  -18 ?   ?   ?   C . n 
C 1 11  HIS 11  -17 ?   ?   ?   C . n 
C 1 12  GLY 12  -16 ?   ?   ?   C . n 
C 1 13  SER 13  -15 ?   ?   ?   C . n 
C 1 14  ASP 14  -14 ?   ?   ?   C . n 
C 1 15  TYR 15  -13 ?   ?   ?   C . n 
C 1 16  ASP 16  -12 ?   ?   ?   C . n 
C 1 17  ILE 17  -11 ?   ?   ?   C . n 
C 1 18  PRO 18  -10 ?   ?   ?   C . n 
C 1 19  THR 19  -9  ?   ?   ?   C . n 
C 1 20  THR 20  -8  ?   ?   ?   C . n 
C 1 21  GLU 21  -7  ?   ?   ?   C . n 
C 1 22  ASN 22  -6  ?   ?   ?   C . n 
C 1 23  LEU 23  -5  ?   ?   ?   C . n 
C 1 24  TYR 24  -4  ?   ?   ?   C . n 
C 1 25  PHE 25  -3  ?   ?   ?   C . n 
C 1 26  GLN 26  -2  ?   ?   ?   C . n 
C 1 27  GLY 27  -1  ?   ?   ?   C . n 
C 1 28  SER 28  0   ?   ?   ?   C . n 
C 1 29  MET 29  1   ?   ?   ?   C . n 
C 1 30  GLU 30  2   ?   ?   ?   C . n 
C 1 31  LYS 31  3   ?   ?   ?   C . n 
C 1 32  GLN 32  4   ?   ?   ?   C . n 
C 1 33  ASP 33  5   ?   ?   ?   C . n 
C 1 34  THR 34  6   ?   ?   ?   C . n 
C 1 35  HIS 35  7   ?   ?   ?   C . n 
C 1 36  VAL 36  8   ?   ?   ?   C . n 
C 1 37  ASN 37  9   ?   ?   ?   C . n 
C 1 38  THR 38  10  ?   ?   ?   C . n 
C 1 39  GLU 39  11  ?   ?   ?   C . n 
C 1 40  LYS 40  12  ?   ?   ?   C . n 
C 1 41  GLN 41  13  ?   ?   ?   C . n 
C 1 42  GLU 42  14  ?   ?   ?   C . n 
C 1 43  ALA 43  15  15  ALA ALA C . n 
C 1 44  TYR 44  16  16  TYR TYR C . n 
C 1 45  ARG 45  17  17  ARG ARG C . n 
C 1 46  GLY 46  18  18  GLY GLY C . n 
C 1 47  ILE 47  19  19  ILE ILE C . n 
C 1 48  ASP 48  20  20  ASP ASP C . n 
C 1 49  LYS 49  21  21  LYS LYS C . n 
C 1 50  PRO 50  22  22  PRO PRO C . n 
C 1 51  HIS 51  23  23  HIS HIS C . n 
C 1 52  LEU 52  24  24  LEU LEU C . n 
C 1 53  TYR 53  25  25  TYR TYR C . n 
C 1 54  THR 54  26  26  THR THR C . n 
C 1 55  LEU 55  27  27  LEU LEU C . n 
C 1 56  GLY 56  28  28  GLY GLY C . n 
C 1 57  CYS 57  29  29  CYS CYS C . n 
C 1 58  CYS 58  30  30  CYS CYS C . n 
C 1 59  SER 59  31  31  SER SER C . n 
C 1 60  LEU 60  32  32  LEU LEU C . n 
C 1 61  THR 61  33  33  THR THR C . n 
C 1 62  ALA 62  34  34  ALA ALA C . n 
C 1 63  MET 63  35  35  MET MET C . n 
C 1 64  ALA 64  36  36  ALA ALA C . n 
C 1 65  SER 65  37  37  SER SER C . n 
C 1 66  ALA 66  38  38  ALA ALA C . n 
C 1 67  GLN 67  39  39  GLN GLN C . n 
C 1 68  LEU 68  40  40  LEU LEU C . n 
C 1 69  ASP 69  41  41  ASP ASP C . n 
C 1 70  ALA 70  42  42  ALA ALA C . n 
C 1 71  LEU 71  43  43  LEU LEU C . n 
C 1 72  TRP 72  44  44  TRP TRP C . n 
C 1 73  SER 73  45  45  SER SER C . n 
C 1 74  GLN 74  46  46  GLN GLN C . n 
C 1 75  LEU 75  47  47  LEU LEU C . n 
C 1 76  SER 76  48  48  SER SER C . n 
C 1 77  TRP 77  49  49  TRP TRP C . n 
C 1 78  PRO 78  50  50  PRO PRO C . n 
C 1 79  GLN 79  51  51  GLN GLN C . n 
C 1 80  THR 80  52  52  THR THR C . n 
C 1 81  PRO 81  53  53  PRO PRO C . n 
C 1 82  LEU 82  54  54  LEU LEU C . n 
C 1 83  PRO 83  55  55  PRO PRO C . n 
C 1 84  VAL 84  56  56  VAL VAL C . n 
C 1 85  LEU 85  57  57  LEU LEU C . n 
C 1 86  ASP 86  58  58  ASP ASP C . n 
C 1 87  ILE 87  59  59  ILE ILE C . n 
C 1 88  GLY 88  60  60  GLY GLY C . n 
C 1 89  CYS 89  61  61  CYS CYS C . n 
C 1 90  GLY 90  62  62  GLY GLY C . n 
C 1 91  PRO 91  63  63  PRO PRO C . n 
C 1 92  GLY 92  64  64  GLY GLY C . n 
C 1 93  ASP 93  65  65  ASP ASP C . n 
C 1 94  ILE 94  66  66  ILE ILE C . n 
C 1 95  ALA 95  67  67  ALA ALA C . n 
C 1 96  ARG 96  68  68  ARG ARG C . n 
C 1 97  LYS 97  69  69  LYS LYS C . n 
C 1 98  VAL 98  70  70  VAL VAL C . n 
C 1 99  LEU 99  71  71  LEU LEU C . n 
C 1 100 ALA 100 72  72  ALA ALA C . n 
C 1 101 PRO 101 73  73  PRO PRO C . n 
C 1 102 ARG 102 74  74  ARG ARG C . n 
C 1 103 LEU 103 75  75  LEU LEU C . n 
C 1 104 PRO 104 76  76  PRO PRO C . n 
C 1 105 ALA 105 77  77  ALA ALA C . n 
C 1 106 GLY 106 78  78  GLY GLY C . n 
C 1 107 THR 107 79  79  THR THR C . n 
C 1 108 ARG 108 80  80  ARG ARG C . n 
C 1 109 LEU 109 81  81  LEU LEU C . n 
C 1 110 VAL 110 82  82  VAL VAL C . n 
C 1 111 ALA 111 83  83  ALA ALA C . n 
C 1 112 CYS 112 84  84  CYS CYS C . n 
C 1 113 ASP 113 85  85  ASP ASP C . n 
C 1 114 ILE 114 86  86  ILE ILE C . n 
C 1 115 SER 115 87  87  SER SER C . n 
C 1 116 PRO 116 88  88  PRO PRO C . n 
C 1 117 GLU 117 89  89  GLU GLU C . n 
C 1 118 MET 118 90  90  MET MET C . n 
C 1 119 VAL 119 91  91  VAL VAL C . n 
C 1 120 ASP 120 92  92  ASP ASP C . n 
C 1 121 PHE 121 93  93  PHE PHE C . n 
C 1 122 CYS 122 94  94  CYS CYS C . n 
C 1 123 ARG 123 95  95  ARG ARG C . n 
C 1 124 GLN 124 96  96  GLN GLN C . n 
C 1 125 HIS 125 97  97  HIS HIS C . n 
C 1 126 ASN 126 98  98  ASN ASN C . n 
C 1 127 ALA 127 99  99  ALA ALA C . n 
C 1 128 LEU 128 100 100 LEU LEU C . n 
C 1 129 PRO 129 101 101 PRO PRO C . n 
C 1 130 GLY 130 102 102 GLY GLY C . n 
C 1 131 THR 131 103 103 THR THR C . n 
C 1 132 ILE 132 104 104 ILE ILE C . n 
C 1 133 THR 133 105 105 THR THR C . n 
C 1 134 TYR 134 106 106 TYR TYR C . n 
C 1 135 GLU 135 107 107 GLU GLU C . n 
C 1 136 LEU 136 108 108 LEU LEU C . n 
C 1 137 LEU 137 109 109 LEU LEU C . n 
C 1 138 ASP 138 110 110 ASP ASP C . n 
C 1 139 VAL 139 111 111 VAL VAL C . n 
C 1 140 VAL 140 112 112 VAL VAL C . n 
C 1 141 GLU 141 113 113 GLU GLU C . n 
C 1 142 PRO 142 114 114 PRO PRO C . n 
C 1 143 ARG 143 115 115 ARG ARG C . n 
C 1 144 LEU 144 116 116 LEU LEU C . n 
C 1 145 GLU 145 117 117 GLU GLU C . n 
C 1 146 ASP 146 118 118 ASP ASP C . n 
C 1 147 THR 147 119 119 THR THR C . n 
C 1 148 VAL 148 120 120 VAL VAL C . n 
C 1 149 VAL 149 121 121 VAL VAL C . n 
C 1 150 TRP 150 122 122 TRP TRP C . n 
C 1 151 ARG 151 123 123 ARG ARG C . n 
C 1 152 ASN 152 124 124 ASN ASN C . n 
C 1 153 GLY 153 125 125 GLY GLY C . n 
C 1 154 PRO 154 126 126 PRO PRO C . n 
C 1 155 PHE 155 127 127 PHE PHE C . n 
C 1 156 GLY 156 128 128 GLY GLY C . n 
C 1 157 LYS 157 129 129 LYS LYS C . n 
C 1 158 VAL 158 130 130 VAL VAL C . n 
C 1 159 PHE 159 131 131 PHE PHE C . n 
C 1 160 CYS 160 132 132 CYS CYS C . n 
C 1 161 MET 161 133 133 MET MET C . n 
C 1 162 LEU 162 134 134 LEU LEU C . n 
C 1 163 MET 163 135 135 MET MET C . n 
C 1 164 LEU 164 136 136 LEU LEU C . n 
C 1 165 HIS 165 137 137 HIS HIS C . n 
C 1 166 LEU 166 138 138 LEU LEU C . n 
C 1 167 VAL 167 139 139 VAL VAL C . n 
C 1 168 PRO 168 140 140 PRO PRO C . n 
C 1 169 ASP 169 141 141 ASP ASP C . n 
C 1 170 ASN 170 142 142 ASN ASN C . n 
C 1 171 ARG 171 143 143 ARG ARG C . n 
C 1 172 LEU 172 144 144 LEU LEU C . n 
C 1 173 ALA 173 145 145 ALA ALA C . n 
C 1 174 VAL 174 146 146 VAL VAL C . n 
C 1 175 LYS 175 147 147 LYS LYS C . n 
C 1 176 ASN 176 148 148 ASN ASN C . n 
C 1 177 ILE 177 149 149 ILE ILE C . n 
C 1 178 HIS 178 150 150 HIS HIS C . n 
C 1 179 LYS 179 151 151 LYS LYS C . n 
C 1 180 LEU 180 152 152 LEU LEU C . n 
C 1 181 LEU 181 153 153 LEU LEU C . n 
C 1 182 VAL 182 154 154 VAL VAL C . n 
C 1 183 PRO 183 155 155 PRO PRO C . n 
C 1 184 GLY 184 156 156 GLY GLY C . n 
C 1 185 GLY 185 157 157 GLY GLY C . n 
C 1 186 GLU 186 158 158 GLU GLU C . n 
C 1 187 ALA 187 159 159 ALA ALA C . n 
C 1 188 VAL 188 160 160 VAL VAL C . n 
C 1 189 PHE 189 161 161 PHE PHE C . n 
C 1 190 SER 190 162 162 SER SER C . n 
C 1 191 VAL 191 163 163 VAL VAL C . n 
C 1 192 ILE 192 164 164 ILE ILE C . n 
C 1 193 ALA 193 165 165 ALA ALA C . n 
C 1 194 ASN 194 166 166 ASN ASN C . n 
C 1 195 MET 195 167 167 MET MET C . n 
C 1 196 ALA 196 168 168 ALA ALA C . n 
C 1 197 LEU 197 169 169 LEU LEU C . n 
C 1 198 CYS 198 170 170 CYS CYS C . n 
C 1 199 ASP 199 171 171 ASP ASP C . n 
C 1 200 ALA 200 172 172 ALA ALA C . n 
C 1 201 TYR 201 173 173 TYR TYR C . n 
C 1 202 GLU 202 174 174 GLU GLU C . n 
C 1 203 GLU 203 175 175 GLU GLU C . n 
C 1 204 MET 204 176 176 MET MET C . n 
C 1 205 ALA 205 177 177 ALA ALA C . n 
C 1 206 LYS 206 178 178 LYS LYS C . n 
C 1 207 GLU 207 179 179 GLU GLU C . n 
C 1 208 PRO 208 180 180 PRO PRO C . n 
C 1 209 ARG 209 181 181 ARG ARG C . n 
C 1 210 TRP 210 182 182 TRP TRP C . n 
C 1 211 ALA 211 183 183 ALA ALA C . n 
C 1 212 LEU 212 184 184 LEU LEU C . n 
C 1 213 TYR 213 185 185 TYR TYR C . n 
C 1 214 MET 214 186 186 MET MET C . n 
C 1 215 GLN 215 187 187 GLN GLN C . n 
C 1 216 ASP 216 188 188 ASP ASP C . n 
C 1 217 VAL 217 189 189 VAL VAL C . n 
C 1 218 GLU 218 190 190 GLU GLU C . n 
C 1 219 LYS 219 191 191 LYS LYS C . n 
C 1 220 PHE 220 192 192 PHE PHE C . n 
C 1 221 VAL 221 193 193 VAL VAL C . n 
C 1 222 SER 222 194 194 SER SER C . n 
C 1 223 PRO 223 195 195 PRO PRO C . n 
C 1 224 TYR 224 196 196 TYR TYR C . n 
C 1 225 GLN 225 197 197 GLN GLN C . n 
C 1 226 HIS 226 198 198 HIS HIS C . n 
C 1 227 SER 227 199 199 SER SER C . n 
C 1 228 GLU 228 200 200 GLU GLU C . n 
C 1 229 ASP 229 201 201 ASP ASP C . n 
C 1 230 PRO 230 202 202 PRO PRO C . n 
C 1 231 VAL 231 203 203 VAL VAL C . n 
C 1 232 GLY 232 204 204 GLY GLY C . n 
C 1 233 GLU 233 205 205 GLU GLU C . n 
C 1 234 PHE 234 206 206 PHE PHE C . n 
C 1 235 ARG 235 207 207 ARG ARG C . n 
C 1 236 LEU 236 208 208 LEU LEU C . n 
C 1 237 LEU 237 209 209 LEU LEU C . n 
C 1 238 LEU 238 210 210 LEU LEU C . n 
C 1 239 GLU 239 211 211 GLU GLU C . n 
C 1 240 SER 240 212 212 SER SER C . n 
C 1 241 GLU 241 213 213 GLU GLU C . n 
C 1 242 GLY 242 214 214 GLY GLY C . n 
C 1 243 PHE 243 215 215 PHE PHE C . n 
C 1 244 GLN 244 216 216 GLN GLN C . n 
C 1 245 VAL 245 217 217 VAL VAL C . n 
C 1 246 LEU 246 218 218 LEU LEU C . n 
C 1 247 ARG 247 219 219 ARG ARG C . n 
C 1 248 CYS 248 220 220 CYS CYS C . n 
C 1 249 ASP 249 221 221 ASP ASP C . n 
C 1 250 LEU 250 222 222 LEU LEU C . n 
C 1 251 GLY 251 223 223 GLY GLY C . n 
C 1 252 PRO 252 224 224 PRO PRO C . n 
C 1 253 GLN 253 225 225 GLN GLN C . n 
C 1 254 LYS 254 226 226 LYS LYS C . n 
C 1 255 VAL 255 227 227 VAL VAL C . n 
C 1 256 PHE 256 228 228 PHE PHE C . n 
C 1 257 PHE 257 229 229 PHE PHE C . n 
C 1 258 PRO 258 230 230 PRO PRO C . n 
C 1 259 THR 259 231 231 THR THR C . n 
C 1 260 ALA 260 232 232 ALA ALA C . n 
C 1 261 GLU 261 233 233 GLU GLU C . n 
C 1 262 THR 262 234 234 THR THR C . n 
C 1 263 HIS 263 235 235 HIS HIS C . n 
C 1 264 ARG 264 236 236 ARG ARG C . n 
C 1 265 GLU 265 237 237 GLU GLU C . n 
C 1 266 PHE 266 238 238 PHE PHE C . n 
C 1 267 LEU 267 239 239 LEU LEU C . n 
C 1 268 LYS 268 240 240 LYS LYS C . n 
C 1 269 SER 269 241 241 SER SER C . n 
C 1 270 VAL 270 242 242 VAL VAL C . n 
C 1 271 CYS 271 243 243 CYS CYS C . n 
C 1 272 ALA 272 244 244 ALA ALA C . n 
C 1 273 PHE 273 245 245 PHE PHE C . n 
C 1 274 LEU 274 246 246 LEU LEU C . n 
C 1 275 TYR 275 247 247 TYR TYR C . n 
C 1 276 ARG 276 248 248 ARG ARG C . n 
C 1 277 ILE 277 249 249 ILE ILE C . n 
C 1 278 PRO 278 250 250 PRO PRO C . n 
C 1 279 GLU 279 251 251 GLU GLU C . n 
C 1 280 GLU 280 252 252 GLU GLU C . n 
C 1 281 GLN 281 253 253 GLN GLN C . n 
C 1 282 LYS 282 254 254 LYS LYS C . n 
C 1 283 ASP 283 255 255 ASP ASP C . n 
C 1 284 ASP 284 256 256 ASP ASP C . n 
C 1 285 PHE 285 257 257 PHE PHE C . n 
C 1 286 PHE 286 258 258 PHE PHE C . n 
C 1 287 ASP 287 259 259 ASP ASP C . n 
C 1 288 ASP 288 260 260 ASP ASP C . n 
C 1 289 TRP 289 261 261 TRP TRP C . n 
C 1 290 LEU 290 262 262 LEU LEU C . n 
C 1 291 GLN 291 263 263 GLN GLN C . n 
C 1 292 ARG 292 264 264 ARG ARG C . n 
C 1 293 LEU 293 265 265 LEU LEU C . n 
C 1 294 GLU 294 266 266 GLU GLU C . n 
C 1 295 LYS 295 267 267 LYS LYS C . n 
C 1 296 LEU 296 268 268 LEU LEU C . n 
C 1 297 LYS 297 269 269 LYS LYS C . n 
C 1 298 GLY 298 270 270 GLY GLY C . n 
C 1 299 THR 299 271 271 THR THR C . n 
C 1 300 SER 300 272 272 SER SER C . n 
C 1 301 GLN 301 273 273 GLN GLN C . n 
C 1 302 GLY 302 274 274 GLY GLY C . n 
C 1 303 VAL 303 275 275 VAL VAL C . n 
C 1 304 GLY 304 276 276 GLY GLY C . n 
C 1 305 ARG 305 277 277 ARG ARG C . n 
C 1 306 ASN 306 278 278 ASN ASN C . n 
C 1 307 GLY 307 279 279 GLY GLY C . n 
C 1 308 GLU 308 280 280 GLU GLU C . n 
C 1 309 ALA 309 281 281 ALA ALA C . n 
C 1 310 GLU 310 282 282 GLU GLU C . n 
C 1 311 TYR 311 283 283 TYR TYR C . n 
C 1 312 TYR 312 284 284 TYR TYR C . n 
C 1 313 ILE 313 285 285 ILE ILE C . n 
C 1 314 HIS 314 286 286 HIS HIS C . n 
C 1 315 LEU 315 287 287 LEU LEU C . n 
C 1 316 SER 316 288 288 SER SER C . n 
C 1 317 VAL 317 289 289 VAL VAL C . n 
C 1 318 ILE 318 290 290 ILE ILE C . n 
C 1 319 THR 319 291 291 THR THR C . n 
C 1 320 ALA 320 292 292 ALA ALA C . n 
C 1 321 LEU 321 293 293 LEU LEU C . n 
C 1 322 ALA 322 294 294 ALA ALA C . n 
C 1 323 ARG 323 295 295 ARG ARG C . n 
C 1 324 LYS 324 296 296 LYS LYS C . n 
C 1 325 PHE 325 297 297 PHE PHE C . n 
D 1 1   MET 1   -27 ?   ?   ?   D . n 
D 1 2   GLY 2   -26 ?   ?   ?   D . n 
D 1 3   SER 3   -25 ?   ?   ?   D . n 
D 1 4   HIS 4   -24 ?   ?   ?   D . n 
D 1 5   HIS 5   -23 ?   ?   ?   D . n 
D 1 6   HIS 6   -22 ?   ?   ?   D . n 
D 1 7   HIS 7   -21 ?   ?   ?   D . n 
D 1 8   HIS 8   -20 ?   ?   ?   D . n 
D 1 9   HIS 9   -19 ?   ?   ?   D . n 
D 1 10  HIS 10  -18 ?   ?   ?   D . n 
D 1 11  HIS 11  -17 ?   ?   ?   D . n 
D 1 12  GLY 12  -16 ?   ?   ?   D . n 
D 1 13  SER 13  -15 ?   ?   ?   D . n 
D 1 14  ASP 14  -14 ?   ?   ?   D . n 
D 1 15  TYR 15  -13 ?   ?   ?   D . n 
D 1 16  ASP 16  -12 ?   ?   ?   D . n 
D 1 17  ILE 17  -11 ?   ?   ?   D . n 
D 1 18  PRO 18  -10 ?   ?   ?   D . n 
D 1 19  THR 19  -9  ?   ?   ?   D . n 
D 1 20  THR 20  -8  ?   ?   ?   D . n 
D 1 21  GLU 21  -7  ?   ?   ?   D . n 
D 1 22  ASN 22  -6  ?   ?   ?   D . n 
D 1 23  LEU 23  -5  ?   ?   ?   D . n 
D 1 24  TYR 24  -4  ?   ?   ?   D . n 
D 1 25  PHE 25  -3  ?   ?   ?   D . n 
D 1 26  GLN 26  -2  ?   ?   ?   D . n 
D 1 27  GLY 27  -1  ?   ?   ?   D . n 
D 1 28  SER 28  0   ?   ?   ?   D . n 
D 1 29  MET 29  1   ?   ?   ?   D . n 
D 1 30  GLU 30  2   ?   ?   ?   D . n 
D 1 31  LYS 31  3   ?   ?   ?   D . n 
D 1 32  GLN 32  4   ?   ?   ?   D . n 
D 1 33  ASP 33  5   ?   ?   ?   D . n 
D 1 34  THR 34  6   ?   ?   ?   D . n 
D 1 35  HIS 35  7   ?   ?   ?   D . n 
D 1 36  VAL 36  8   ?   ?   ?   D . n 
D 1 37  ASN 37  9   ?   ?   ?   D . n 
D 1 38  THR 38  10  ?   ?   ?   D . n 
D 1 39  GLU 39  11  ?   ?   ?   D . n 
D 1 40  LYS 40  12  ?   ?   ?   D . n 
D 1 41  GLN 41  13  ?   ?   ?   D . n 
D 1 42  GLU 42  14  14  GLU GLU D . n 
D 1 43  ALA 43  15  15  ALA ALA D . n 
D 1 44  TYR 44  16  16  TYR TYR D . n 
D 1 45  ARG 45  17  17  ARG ARG D . n 
D 1 46  GLY 46  18  18  GLY GLY D . n 
D 1 47  ILE 47  19  19  ILE ILE D . n 
D 1 48  ASP 48  20  20  ASP ASP D . n 
D 1 49  LYS 49  21  21  LYS LYS D . n 
D 1 50  PRO 50  22  22  PRO PRO D . n 
D 1 51  HIS 51  23  23  HIS HIS D . n 
D 1 52  LEU 52  24  24  LEU LEU D . n 
D 1 53  TYR 53  25  25  TYR TYR D . n 
D 1 54  THR 54  26  26  THR THR D . n 
D 1 55  LEU 55  27  27  LEU LEU D . n 
D 1 56  GLY 56  28  28  GLY GLY D . n 
D 1 57  CYS 57  29  29  CYS CYS D . n 
D 1 58  CYS 58  30  30  CYS CYS D . n 
D 1 59  SER 59  31  31  SER SER D . n 
D 1 60  LEU 60  32  32  LEU LEU D . n 
D 1 61  THR 61  33  33  THR THR D . n 
D 1 62  ALA 62  34  34  ALA ALA D . n 
D 1 63  MET 63  35  35  MET MET D . n 
D 1 64  ALA 64  36  36  ALA ALA D . n 
D 1 65  SER 65  37  37  SER SER D . n 
D 1 66  ALA 66  38  38  ALA ALA D . n 
D 1 67  GLN 67  39  39  GLN GLN D . n 
D 1 68  LEU 68  40  40  LEU LEU D . n 
D 1 69  ASP 69  41  41  ASP ASP D . n 
D 1 70  ALA 70  42  42  ALA ALA D . n 
D 1 71  LEU 71  43  43  LEU LEU D . n 
D 1 72  TRP 72  44  44  TRP TRP D . n 
D 1 73  SER 73  45  45  SER SER D . n 
D 1 74  GLN 74  46  46  GLN GLN D . n 
D 1 75  LEU 75  47  47  LEU LEU D . n 
D 1 76  SER 76  48  48  SER SER D . n 
D 1 77  TRP 77  49  49  TRP TRP D . n 
D 1 78  PRO 78  50  50  PRO PRO D . n 
D 1 79  GLN 79  51  51  GLN GLN D . n 
D 1 80  THR 80  52  52  THR THR D . n 
D 1 81  PRO 81  53  53  PRO PRO D . n 
D 1 82  LEU 82  54  54  LEU LEU D . n 
D 1 83  PRO 83  55  55  PRO PRO D . n 
D 1 84  VAL 84  56  56  VAL VAL D . n 
D 1 85  LEU 85  57  57  LEU LEU D . n 
D 1 86  ASP 86  58  58  ASP ASP D . n 
D 1 87  ILE 87  59  59  ILE ILE D . n 
D 1 88  GLY 88  60  60  GLY GLY D . n 
D 1 89  CYS 89  61  61  CYS CYS D . n 
D 1 90  GLY 90  62  62  GLY GLY D . n 
D 1 91  PRO 91  63  63  PRO PRO D . n 
D 1 92  GLY 92  64  64  GLY GLY D . n 
D 1 93  ASP 93  65  65  ASP ASP D . n 
D 1 94  ILE 94  66  66  ILE ILE D . n 
D 1 95  ALA 95  67  67  ALA ALA D . n 
D 1 96  ARG 96  68  68  ARG ARG D . n 
D 1 97  LYS 97  69  69  LYS LYS D . n 
D 1 98  VAL 98  70  70  VAL VAL D . n 
D 1 99  LEU 99  71  71  LEU LEU D . n 
D 1 100 ALA 100 72  72  ALA ALA D . n 
D 1 101 PRO 101 73  73  PRO PRO D . n 
D 1 102 ARG 102 74  74  ARG ARG D . n 
D 1 103 LEU 103 75  75  LEU LEU D . n 
D 1 104 PRO 104 76  76  PRO PRO D . n 
D 1 105 ALA 105 77  77  ALA ALA D . n 
D 1 106 GLY 106 78  78  GLY GLY D . n 
D 1 107 THR 107 79  79  THR THR D . n 
D 1 108 ARG 108 80  80  ARG ARG D . n 
D 1 109 LEU 109 81  81  LEU LEU D . n 
D 1 110 VAL 110 82  82  VAL VAL D . n 
D 1 111 ALA 111 83  83  ALA ALA D . n 
D 1 112 CYS 112 84  84  CYS CYS D . n 
D 1 113 ASP 113 85  85  ASP ASP D . n 
D 1 114 ILE 114 86  86  ILE ILE D . n 
D 1 115 SER 115 87  87  SER SER D . n 
D 1 116 PRO 116 88  88  PRO PRO D . n 
D 1 117 GLU 117 89  89  GLU GLU D . n 
D 1 118 MET 118 90  90  MET MET D . n 
D 1 119 VAL 119 91  91  VAL VAL D . n 
D 1 120 ASP 120 92  92  ASP ASP D . n 
D 1 121 PHE 121 93  93  PHE PHE D . n 
D 1 122 CYS 122 94  94  CYS CYS D . n 
D 1 123 ARG 123 95  95  ARG ARG D . n 
D 1 124 GLN 124 96  96  GLN GLN D . n 
D 1 125 HIS 125 97  97  HIS HIS D . n 
D 1 126 ASN 126 98  98  ASN ASN D . n 
D 1 127 ALA 127 99  99  ALA ALA D . n 
D 1 128 LEU 128 100 100 LEU LEU D . n 
D 1 129 PRO 129 101 101 PRO PRO D . n 
D 1 130 GLY 130 102 102 GLY GLY D . n 
D 1 131 THR 131 103 103 THR THR D . n 
D 1 132 ILE 132 104 104 ILE ILE D . n 
D 1 133 THR 133 105 105 THR THR D . n 
D 1 134 TYR 134 106 106 TYR TYR D . n 
D 1 135 GLU 135 107 107 GLU GLU D . n 
D 1 136 LEU 136 108 108 LEU LEU D . n 
D 1 137 LEU 137 109 109 LEU LEU D . n 
D 1 138 ASP 138 110 110 ASP ASP D . n 
D 1 139 VAL 139 111 111 VAL VAL D . n 
D 1 140 VAL 140 112 112 VAL VAL D . n 
D 1 141 GLU 141 113 113 GLU GLU D . n 
D 1 142 PRO 142 114 114 PRO PRO D . n 
D 1 143 ARG 143 115 115 ARG ARG D . n 
D 1 144 LEU 144 116 116 LEU LEU D . n 
D 1 145 GLU 145 117 117 GLU GLU D . n 
D 1 146 ASP 146 118 118 ASP ASP D . n 
D 1 147 THR 147 119 119 THR THR D . n 
D 1 148 VAL 148 120 120 VAL VAL D . n 
D 1 149 VAL 149 121 121 VAL VAL D . n 
D 1 150 TRP 150 122 122 TRP TRP D . n 
D 1 151 ARG 151 123 123 ARG ARG D . n 
D 1 152 ASN 152 124 124 ASN ASN D . n 
D 1 153 GLY 153 125 125 GLY GLY D . n 
D 1 154 PRO 154 126 126 PRO PRO D . n 
D 1 155 PHE 155 127 127 PHE PHE D . n 
D 1 156 GLY 156 128 128 GLY GLY D . n 
D 1 157 LYS 157 129 129 LYS LYS D . n 
D 1 158 VAL 158 130 130 VAL VAL D . n 
D 1 159 PHE 159 131 131 PHE PHE D . n 
D 1 160 CYS 160 132 132 CYS CYS D . n 
D 1 161 MET 161 133 133 MET MET D . n 
D 1 162 LEU 162 134 134 LEU LEU D . n 
D 1 163 MET 163 135 135 MET MET D . n 
D 1 164 LEU 164 136 136 LEU LEU D . n 
D 1 165 HIS 165 137 137 HIS HIS D . n 
D 1 166 LEU 166 138 138 LEU LEU D . n 
D 1 167 VAL 167 139 139 VAL VAL D . n 
D 1 168 PRO 168 140 140 PRO PRO D . n 
D 1 169 ASP 169 141 141 ASP ASP D . n 
D 1 170 ASN 170 142 142 ASN ASN D . n 
D 1 171 ARG 171 143 143 ARG ARG D . n 
D 1 172 LEU 172 144 144 LEU LEU D . n 
D 1 173 ALA 173 145 145 ALA ALA D . n 
D 1 174 VAL 174 146 146 VAL VAL D . n 
D 1 175 LYS 175 147 147 LYS LYS D . n 
D 1 176 ASN 176 148 148 ASN ASN D . n 
D 1 177 ILE 177 149 149 ILE ILE D . n 
D 1 178 HIS 178 150 150 HIS HIS D . n 
D 1 179 LYS 179 151 151 LYS LYS D . n 
D 1 180 LEU 180 152 152 LEU LEU D . n 
D 1 181 LEU 181 153 153 LEU LEU D . n 
D 1 182 VAL 182 154 154 VAL VAL D . n 
D 1 183 PRO 183 155 155 PRO PRO D . n 
D 1 184 GLY 184 156 156 GLY GLY D . n 
D 1 185 GLY 185 157 157 GLY GLY D . n 
D 1 186 GLU 186 158 158 GLU GLU D . n 
D 1 187 ALA 187 159 159 ALA ALA D . n 
D 1 188 VAL 188 160 160 VAL VAL D . n 
D 1 189 PHE 189 161 161 PHE PHE D . n 
D 1 190 SER 190 162 162 SER SER D . n 
D 1 191 VAL 191 163 163 VAL VAL D . n 
D 1 192 ILE 192 164 164 ILE ILE D . n 
D 1 193 ALA 193 165 165 ALA ALA D . n 
D 1 194 ASN 194 166 166 ASN ASN D . n 
D 1 195 MET 195 167 167 MET MET D . n 
D 1 196 ALA 196 168 168 ALA ALA D . n 
D 1 197 LEU 197 169 169 LEU LEU D . n 
D 1 198 CYS 198 170 170 CYS CYS D . n 
D 1 199 ASP 199 171 171 ASP ASP D . n 
D 1 200 ALA 200 172 172 ALA ALA D . n 
D 1 201 TYR 201 173 173 TYR TYR D . n 
D 1 202 GLU 202 174 174 GLU GLU D . n 
D 1 203 GLU 203 175 175 GLU GLU D . n 
D 1 204 MET 204 176 176 MET MET D . n 
D 1 205 ALA 205 177 177 ALA ALA D . n 
D 1 206 LYS 206 178 178 LYS LYS D . n 
D 1 207 GLU 207 179 179 GLU GLU D . n 
D 1 208 PRO 208 180 180 PRO PRO D . n 
D 1 209 ARG 209 181 181 ARG ARG D . n 
D 1 210 TRP 210 182 182 TRP TRP D . n 
D 1 211 ALA 211 183 183 ALA ALA D . n 
D 1 212 LEU 212 184 184 LEU LEU D . n 
D 1 213 TYR 213 185 185 TYR TYR D . n 
D 1 214 MET 214 186 186 MET MET D . n 
D 1 215 GLN 215 187 187 GLN GLN D . n 
D 1 216 ASP 216 188 188 ASP ASP D . n 
D 1 217 VAL 217 189 189 VAL VAL D . n 
D 1 218 GLU 218 190 190 GLU GLU D . n 
D 1 219 LYS 219 191 191 LYS LYS D . n 
D 1 220 PHE 220 192 192 PHE PHE D . n 
D 1 221 VAL 221 193 193 VAL VAL D . n 
D 1 222 SER 222 194 194 SER SER D . n 
D 1 223 PRO 223 195 195 PRO PRO D . n 
D 1 224 TYR 224 196 196 TYR TYR D . n 
D 1 225 GLN 225 197 197 GLN GLN D . n 
D 1 226 HIS 226 198 198 HIS HIS D . n 
D 1 227 SER 227 199 199 SER SER D . n 
D 1 228 GLU 228 200 200 GLU GLU D . n 
D 1 229 ASP 229 201 201 ASP ASP D . n 
D 1 230 PRO 230 202 202 PRO PRO D . n 
D 1 231 VAL 231 203 203 VAL VAL D . n 
D 1 232 GLY 232 204 204 GLY GLY D . n 
D 1 233 GLU 233 205 205 GLU GLU D . n 
D 1 234 PHE 234 206 206 PHE PHE D . n 
D 1 235 ARG 235 207 207 ARG ARG D . n 
D 1 236 LEU 236 208 208 LEU LEU D . n 
D 1 237 LEU 237 209 209 LEU LEU D . n 
D 1 238 LEU 238 210 210 LEU LEU D . n 
D 1 239 GLU 239 211 211 GLU GLU D . n 
D 1 240 SER 240 212 212 SER SER D . n 
D 1 241 GLU 241 213 213 GLU GLU D . n 
D 1 242 GLY 242 214 214 GLY GLY D . n 
D 1 243 PHE 243 215 215 PHE PHE D . n 
D 1 244 GLN 244 216 216 GLN GLN D . n 
D 1 245 VAL 245 217 217 VAL VAL D . n 
D 1 246 LEU 246 218 218 LEU LEU D . n 
D 1 247 ARG 247 219 219 ARG ARG D . n 
D 1 248 CYS 248 220 220 CYS CYS D . n 
D 1 249 ASP 249 221 221 ASP ASP D . n 
D 1 250 LEU 250 222 222 LEU LEU D . n 
D 1 251 GLY 251 223 223 GLY GLY D . n 
D 1 252 PRO 252 224 224 PRO PRO D . n 
D 1 253 GLN 253 225 225 GLN GLN D . n 
D 1 254 LYS 254 226 226 LYS LYS D . n 
D 1 255 VAL 255 227 227 VAL VAL D . n 
D 1 256 PHE 256 228 228 PHE PHE D . n 
D 1 257 PHE 257 229 229 PHE PHE D . n 
D 1 258 PRO 258 230 230 PRO PRO D . n 
D 1 259 THR 259 231 231 THR THR D . n 
D 1 260 ALA 260 232 232 ALA ALA D . n 
D 1 261 GLU 261 233 233 GLU GLU D . n 
D 1 262 THR 262 234 234 THR THR D . n 
D 1 263 HIS 263 235 235 HIS HIS D . n 
D 1 264 ARG 264 236 236 ARG ARG D . n 
D 1 265 GLU 265 237 237 GLU GLU D . n 
D 1 266 PHE 266 238 238 PHE PHE D . n 
D 1 267 LEU 267 239 239 LEU LEU D . n 
D 1 268 LYS 268 240 240 LYS LYS D . n 
D 1 269 SER 269 241 241 SER SER D . n 
D 1 270 VAL 270 242 242 VAL VAL D . n 
D 1 271 CYS 271 243 243 CYS CYS D . n 
D 1 272 ALA 272 244 244 ALA ALA D . n 
D 1 273 PHE 273 245 245 PHE PHE D . n 
D 1 274 LEU 274 246 246 LEU LEU D . n 
D 1 275 TYR 275 247 247 TYR TYR D . n 
D 1 276 ARG 276 248 248 ARG ARG D . n 
D 1 277 ILE 277 249 249 ILE ILE D . n 
D 1 278 PRO 278 250 250 PRO PRO D . n 
D 1 279 GLU 279 251 251 GLU GLU D . n 
D 1 280 GLU 280 252 252 GLU GLU D . n 
D 1 281 GLN 281 253 253 GLN GLN D . n 
D 1 282 LYS 282 254 254 LYS LYS D . n 
D 1 283 ASP 283 255 255 ASP ASP D . n 
D 1 284 ASP 284 256 256 ASP ASP D . n 
D 1 285 PHE 285 257 257 PHE PHE D . n 
D 1 286 PHE 286 258 258 PHE PHE D . n 
D 1 287 ASP 287 259 259 ASP ASP D . n 
D 1 288 ASP 288 260 260 ASP ASP D . n 
D 1 289 TRP 289 261 261 TRP TRP D . n 
D 1 290 LEU 290 262 262 LEU LEU D . n 
D 1 291 GLN 291 263 263 GLN GLN D . n 
D 1 292 ARG 292 264 264 ARG ARG D . n 
D 1 293 LEU 293 265 265 LEU LEU D . n 
D 1 294 GLU 294 266 266 GLU GLU D . n 
D 1 295 LYS 295 267 267 LYS LYS D . n 
D 1 296 LEU 296 268 268 LEU LEU D . n 
D 1 297 LYS 297 269 269 LYS LYS D . n 
D 1 298 GLY 298 270 270 GLY GLY D . n 
D 1 299 THR 299 271 271 THR THR D . n 
D 1 300 SER 300 272 272 SER SER D . n 
D 1 301 GLN 301 273 273 GLN GLN D . n 
D 1 302 GLY 302 274 274 GLY GLY D . n 
D 1 303 VAL 303 275 275 VAL VAL D . n 
D 1 304 GLY 304 276 276 GLY GLY D . n 
D 1 305 ARG 305 277 277 ARG ARG D . n 
D 1 306 ASN 306 278 278 ASN ASN D . n 
D 1 307 GLY 307 279 279 GLY GLY D . n 
D 1 308 GLU 308 280 280 GLU GLU D . n 
D 1 309 ALA 309 281 281 ALA ALA D . n 
D 1 310 GLU 310 282 282 GLU GLU D . n 
D 1 311 TYR 311 283 283 TYR TYR D . n 
D 1 312 TYR 312 284 284 TYR TYR D . n 
D 1 313 ILE 313 285 285 ILE ILE D . n 
D 1 314 HIS 314 286 286 HIS HIS D . n 
D 1 315 LEU 315 287 287 LEU LEU D . n 
D 1 316 SER 316 288 288 SER SER D . n 
D 1 317 VAL 317 289 289 VAL VAL D . n 
D 1 318 ILE 318 290 290 ILE ILE D . n 
D 1 319 THR 319 291 291 THR THR D . n 
D 1 320 ALA 320 292 292 ALA ALA D . n 
D 1 321 LEU 321 293 293 LEU LEU D . n 
D 1 322 ALA 322 294 294 ALA ALA D . n 
D 1 323 ARG 323 295 295 ARG ARG D . n 
D 1 324 LYS 324 296 296 LYS LYS D . n 
D 1 325 PHE 325 297 297 PHE PHE D . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 4VP ? ? 4VP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 SAM ? ? SAM ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
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 SAM 1  301 301 SAM SAM A . 
F 2 SAM 1  301 301 SAM SAM B . 
G 2 SAM 1  301 301 SAM SAM C . 
H 3 4VP 1  302 302 4VP 4VP C . 
I 2 SAM 1  301 301 SAM SAM D . 
J 4 HOH 1  401 1   HOH HOH A . 
J 4 HOH 2  402 5   HOH HOH A . 
J 4 HOH 3  403 8   HOH HOH A . 
J 4 HOH 4  404 2   HOH HOH A . 
J 4 HOH 5  405 27  HOH HOH A . 
J 4 HOH 6  406 4   HOH HOH A . 
J 4 HOH 7  407 29  HOH HOH A . 
J 4 HOH 8  408 6   HOH HOH A . 
J 4 HOH 9  409 7   HOH HOH A . 
J 4 HOH 10 410 36  HOH HOH A . 
J 4 HOH 11 411 9   HOH HOH A . 
J 4 HOH 12 412 28  HOH HOH A . 
J 4 HOH 13 413 3   HOH HOH A . 
J 4 HOH 14 414 26  HOH HOH A . 
K 4 HOH 1  401 13  HOH HOH B . 
K 4 HOH 2  402 21  HOH HOH B . 
K 4 HOH 3  403 11  HOH HOH B . 
K 4 HOH 4  404 18  HOH HOH B . 
K 4 HOH 5  405 20  HOH HOH B . 
K 4 HOH 6  406 14  HOH HOH B . 
K 4 HOH 7  407 10  HOH HOH B . 
K 4 HOH 8  408 17  HOH HOH B . 
K 4 HOH 9  409 19  HOH HOH B . 
K 4 HOH 10 410 22  HOH HOH B . 
L 4 HOH 1  401 30  HOH HOH C . 
M 4 HOH 1  401 12  HOH HOH D . 
M 4 HOH 2  402 33  HOH HOH D . 
M 4 HOH 3  403 16  HOH HOH D . 
M 4 HOH 4  404 23  HOH HOH D . 
M 4 HOH 5  405 32  HOH HOH D . 
M 4 HOH 6  406 24  HOH HOH D . 
M 4 HOH 7  407 15  HOH HOH D . 
M 4 HOH 8  408 25  HOH HOH D . 
M 4 HOH 9  409 34  HOH HOH D . 
M 4 HOH 10 410 35  HOH HOH D . 
M 4 HOH 11 411 31  HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A LYS 21  ? CG  ? A LYS 49  CG  
2   1 Y 1 A LYS 21  ? CD  ? A LYS 49  CD  
3   1 Y 1 A LYS 21  ? CE  ? A LYS 49  CE  
4   1 Y 1 A LYS 21  ? NZ  ? A LYS 49  NZ  
5   1 Y 1 A LEU 184 ? CG  ? A LEU 212 CG  
6   1 Y 1 A LEU 184 ? CD1 ? A LEU 212 CD1 
7   1 Y 1 A LEU 184 ? CD2 ? A LEU 212 CD2 
8   1 Y 1 A GLU 200 ? CG  ? A GLU 228 CG  
9   1 Y 1 A GLU 200 ? CD  ? A GLU 228 CD  
10  1 Y 1 A GLU 200 ? OE1 ? A GLU 228 OE1 
11  1 Y 1 A GLU 200 ? OE2 ? A GLU 228 OE2 
12  1 Y 1 A LEU 208 ? CG  ? A LEU 236 CG  
13  1 Y 1 A LEU 208 ? CD1 ? A LEU 236 CD1 
14  1 Y 1 A LEU 208 ? CD2 ? A LEU 236 CD2 
15  1 Y 1 A ARG 277 ? CG  ? A ARG 305 CG  
16  1 Y 1 A ARG 277 ? CD  ? A ARG 305 CD  
17  1 Y 1 A ARG 277 ? NE  ? A ARG 305 NE  
18  1 Y 1 A ARG 277 ? CZ  ? A ARG 305 CZ  
19  1 Y 1 A ARG 277 ? NH1 ? A ARG 305 NH1 
20  1 Y 1 A ARG 277 ? NH2 ? A ARG 305 NH2 
21  1 Y 1 A ASN 278 ? CG  ? A ASN 306 CG  
22  1 Y 1 A ASN 278 ? OD1 ? A ASN 306 OD1 
23  1 Y 1 A ASN 278 ? ND2 ? A ASN 306 ND2 
24  1 Y 1 A GLU 280 ? CG  ? A GLU 308 CG  
25  1 Y 1 A GLU 280 ? CD  ? A GLU 308 CD  
26  1 Y 1 A GLU 280 ? OE1 ? A GLU 308 OE1 
27  1 Y 1 A GLU 280 ? OE2 ? A GLU 308 OE2 
28  1 Y 1 B LYS 21  ? CG  ? B LYS 49  CG  
29  1 Y 1 B LYS 21  ? CD  ? B LYS 49  CD  
30  1 Y 1 B LYS 21  ? CE  ? B LYS 49  CE  
31  1 Y 1 B LYS 21  ? NZ  ? B LYS 49  NZ  
32  1 Y 1 B LEU 184 ? CG  ? B LEU 212 CG  
33  1 Y 1 B LEU 184 ? CD1 ? B LEU 212 CD1 
34  1 Y 1 B LEU 184 ? CD2 ? B LEU 212 CD2 
35  1 Y 1 B GLU 200 ? CG  ? B GLU 228 CG  
36  1 Y 1 B GLU 200 ? CD  ? B GLU 228 CD  
37  1 Y 1 B GLU 200 ? OE1 ? B GLU 228 OE1 
38  1 Y 1 B GLU 200 ? OE2 ? B GLU 228 OE2 
39  1 Y 1 B LYS 267 ? CG  ? B LYS 295 CG  
40  1 Y 1 B LYS 267 ? CD  ? B LYS 295 CD  
41  1 Y 1 B LYS 267 ? CE  ? B LYS 295 CE  
42  1 Y 1 B LYS 267 ? NZ  ? B LYS 295 NZ  
43  1 Y 1 B LYS 269 ? CG  ? B LYS 297 CG  
44  1 Y 1 B LYS 269 ? CD  ? B LYS 297 CD  
45  1 Y 1 B LYS 269 ? CE  ? B LYS 297 CE  
46  1 Y 1 B LYS 269 ? NZ  ? B LYS 297 NZ  
47  1 Y 1 B ARG 277 ? CG  ? B ARG 305 CG  
48  1 Y 1 B ARG 277 ? CD  ? B ARG 305 CD  
49  1 Y 1 B ARG 277 ? NE  ? B ARG 305 NE  
50  1 Y 1 B ARG 277 ? CZ  ? B ARG 305 CZ  
51  1 Y 1 B ARG 277 ? NH1 ? B ARG 305 NH1 
52  1 Y 1 B ARG 277 ? NH2 ? B ARG 305 NH2 
53  1 Y 1 B ASN 278 ? CG  ? B ASN 306 CG  
54  1 Y 1 B ASN 278 ? OD1 ? B ASN 306 OD1 
55  1 Y 1 B ASN 278 ? ND2 ? B ASN 306 ND2 
56  1 Y 1 B GLU 280 ? CG  ? B GLU 308 CG  
57  1 Y 1 B GLU 280 ? CD  ? B GLU 308 CD  
58  1 Y 1 B GLU 280 ? OE1 ? B GLU 308 OE1 
59  1 Y 1 B GLU 280 ? OE2 ? B GLU 308 OE2 
60  1 Y 1 C LYS 21  ? CG  ? C LYS 49  CG  
61  1 Y 1 C LYS 21  ? CD  ? C LYS 49  CD  
62  1 Y 1 C LYS 21  ? CE  ? C LYS 49  CE  
63  1 Y 1 C LYS 21  ? NZ  ? C LYS 49  NZ  
64  1 Y 1 C ASP 141 ? CG  ? C ASP 169 CG  
65  1 Y 1 C ASP 141 ? OD1 ? C ASP 169 OD1 
66  1 Y 1 C ASP 141 ? OD2 ? C ASP 169 OD2 
67  1 Y 1 C LYS 147 ? CG  ? C LYS 175 CG  
68  1 Y 1 C LYS 147 ? CD  ? C LYS 175 CD  
69  1 Y 1 C LYS 147 ? CE  ? C LYS 175 CE  
70  1 Y 1 C LYS 147 ? NZ  ? C LYS 175 NZ  
71  1 Y 1 C LEU 184 ? CG  ? C LEU 212 CG  
72  1 Y 1 C LEU 184 ? CD1 ? C LEU 212 CD1 
73  1 Y 1 C LEU 184 ? CD2 ? C LEU 212 CD2 
74  1 Y 1 C GLN 187 ? CG  ? C GLN 215 CG  
75  1 Y 1 C GLN 187 ? CD  ? C GLN 215 CD  
76  1 Y 1 C GLN 187 ? OE1 ? C GLN 215 OE1 
77  1 Y 1 C GLN 187 ? NE2 ? C GLN 215 NE2 
78  1 Y 1 C GLU 200 ? CG  ? C GLU 228 CG  
79  1 Y 1 C GLU 200 ? CD  ? C GLU 228 CD  
80  1 Y 1 C GLU 200 ? OE1 ? C GLU 228 OE1 
81  1 Y 1 C GLU 200 ? OE2 ? C GLU 228 OE2 
82  1 Y 1 C GLU 252 ? CG  ? C GLU 280 CG  
83  1 Y 1 C GLU 252 ? CD  ? C GLU 280 CD  
84  1 Y 1 C GLU 252 ? OE1 ? C GLU 280 OE1 
85  1 Y 1 C GLU 252 ? OE2 ? C GLU 280 OE2 
86  1 Y 1 C GLN 253 ? CG  ? C GLN 281 CG  
87  1 Y 1 C GLN 253 ? CD  ? C GLN 281 CD  
88  1 Y 1 C GLN 253 ? OE1 ? C GLN 281 OE1 
89  1 Y 1 C GLN 253 ? NE2 ? C GLN 281 NE2 
90  1 Y 1 C ASP 256 ? CG  ? C ASP 284 CG  
91  1 Y 1 C ASP 256 ? OD1 ? C ASP 284 OD1 
92  1 Y 1 C ASP 256 ? OD2 ? C ASP 284 OD2 
93  1 Y 1 C ARG 277 ? CG  ? C ARG 305 CG  
94  1 Y 1 C ARG 277 ? CD  ? C ARG 305 CD  
95  1 Y 1 C ARG 277 ? NE  ? C ARG 305 NE  
96  1 Y 1 C ARG 277 ? CZ  ? C ARG 305 CZ  
97  1 Y 1 C ARG 277 ? NH1 ? C ARG 305 NH1 
98  1 Y 1 C ARG 277 ? NH2 ? C ARG 305 NH2 
99  1 Y 1 C ASN 278 ? CG  ? C ASN 306 CG  
100 1 Y 1 C ASN 278 ? OD1 ? C ASN 306 OD1 
101 1 Y 1 C ASN 278 ? ND2 ? C ASN 306 ND2 
102 1 Y 1 C GLU 280 ? CG  ? C GLU 308 CG  
103 1 Y 1 C GLU 280 ? CD  ? C GLU 308 CD  
104 1 Y 1 C GLU 280 ? OE1 ? C GLU 308 OE1 
105 1 Y 1 C GLU 280 ? OE2 ? C GLU 308 OE2 
106 1 Y 1 D LYS 21  ? CG  ? D LYS 49  CG  
107 1 Y 1 D LYS 21  ? CD  ? D LYS 49  CD  
108 1 Y 1 D LYS 21  ? CE  ? D LYS 49  CE  
109 1 Y 1 D LYS 21  ? NZ  ? D LYS 49  NZ  
110 1 Y 1 D GLN 46  ? CG  ? D GLN 74  CG  
111 1 Y 1 D GLN 46  ? CD  ? D GLN 74  CD  
112 1 Y 1 D GLN 46  ? OE1 ? D GLN 74  OE1 
113 1 Y 1 D GLN 46  ? NE2 ? D GLN 74  NE2 
114 1 Y 1 D LYS 147 ? CG  ? D LYS 175 CG  
115 1 Y 1 D LYS 147 ? CD  ? D LYS 175 CD  
116 1 Y 1 D LYS 147 ? CE  ? D LYS 175 CE  
117 1 Y 1 D LYS 147 ? NZ  ? D LYS 175 NZ  
118 1 Y 1 D GLU 175 ? CG  ? D GLU 203 CG  
119 1 Y 1 D GLU 175 ? CD  ? D GLU 203 CD  
120 1 Y 1 D GLU 175 ? OE1 ? D GLU 203 OE1 
121 1 Y 1 D GLU 175 ? OE2 ? D GLU 203 OE2 
122 1 Y 1 D GLU 179 ? CG  ? D GLU 207 CG  
123 1 Y 1 D GLU 179 ? CD  ? D GLU 207 CD  
124 1 Y 1 D GLU 179 ? OE1 ? D GLU 207 OE1 
125 1 Y 1 D GLU 179 ? OE2 ? D GLU 207 OE2 
126 1 Y 1 D LEU 184 ? CG  ? D LEU 212 CG  
127 1 Y 1 D LEU 184 ? CD1 ? D LEU 212 CD1 
128 1 Y 1 D LEU 184 ? CD2 ? D LEU 212 CD2 
129 1 Y 1 D MET 186 ? CG  ? D MET 214 CG  
130 1 Y 1 D MET 186 ? SD  ? D MET 214 SD  
131 1 Y 1 D MET 186 ? CE  ? D MET 214 CE  
132 1 Y 1 D GLN 187 ? CG  ? D GLN 215 CG  
133 1 Y 1 D GLN 187 ? CD  ? D GLN 215 CD  
134 1 Y 1 D GLN 187 ? OE1 ? D GLN 215 OE1 
135 1 Y 1 D GLN 187 ? NE2 ? D GLN 215 NE2 
136 1 Y 1 D LYS 191 ? CG  ? D LYS 219 CG  
137 1 Y 1 D LYS 191 ? CD  ? D LYS 219 CD  
138 1 Y 1 D LYS 191 ? CE  ? D LYS 219 CE  
139 1 Y 1 D LYS 191 ? NZ  ? D LYS 219 NZ  
140 1 Y 1 D GLU 200 ? CG  ? D GLU 228 CG  
141 1 Y 1 D GLU 200 ? CD  ? D GLU 228 CD  
142 1 Y 1 D GLU 200 ? OE1 ? D GLU 228 OE1 
143 1 Y 1 D GLU 200 ? OE2 ? D GLU 228 OE2 
144 1 Y 1 D ARG 207 ? CG  ? D ARG 235 CG  
145 1 Y 1 D ARG 207 ? CD  ? D ARG 235 CD  
146 1 Y 1 D ARG 207 ? NE  ? D ARG 235 NE  
147 1 Y 1 D ARG 207 ? CZ  ? D ARG 235 CZ  
148 1 Y 1 D ARG 207 ? NH1 ? D ARG 235 NH1 
149 1 Y 1 D ARG 207 ? NH2 ? D ARG 235 NH2 
150 1 Y 1 D LEU 208 ? CG  ? D LEU 236 CG  
151 1 Y 1 D LEU 208 ? CD1 ? D LEU 236 CD1 
152 1 Y 1 D LEU 208 ? CD2 ? D LEU 236 CD2 
153 1 Y 1 D GLU 211 ? CG  ? D GLU 239 CG  
154 1 Y 1 D GLU 211 ? CD  ? D GLU 239 CD  
155 1 Y 1 D GLU 211 ? OE1 ? D GLU 239 OE1 
156 1 Y 1 D GLU 211 ? OE2 ? D GLU 239 OE2 
157 1 Y 1 D GLU 252 ? CG  ? D GLU 280 CG  
158 1 Y 1 D GLU 252 ? CD  ? D GLU 280 CD  
159 1 Y 1 D GLU 252 ? OE1 ? D GLU 280 OE1 
160 1 Y 1 D GLU 252 ? OE2 ? D GLU 280 OE2 
161 1 Y 1 D GLN 253 ? CG  ? D GLN 281 CG  
162 1 Y 1 D GLN 253 ? CD  ? D GLN 281 CD  
163 1 Y 1 D GLN 253 ? OE1 ? D GLN 281 OE1 
164 1 Y 1 D GLN 253 ? NE2 ? D GLN 281 NE2 
165 1 Y 1 D LYS 254 ? CG  ? D LYS 282 CG  
166 1 Y 1 D LYS 254 ? CD  ? D LYS 282 CD  
167 1 Y 1 D LYS 254 ? CE  ? D LYS 282 CE  
168 1 Y 1 D LYS 254 ? NZ  ? D LYS 282 NZ  
169 1 Y 1 D ASP 256 ? CG  ? D ASP 284 CG  
170 1 Y 1 D ASP 256 ? OD1 ? D ASP 284 OD1 
171 1 Y 1 D ASP 256 ? OD2 ? D ASP 284 OD2 
172 1 Y 1 D GLN 263 ? CG  ? D GLN 291 CG  
173 1 Y 1 D GLN 263 ? CD  ? D GLN 291 CD  
174 1 Y 1 D GLN 263 ? OE1 ? D GLN 291 OE1 
175 1 Y 1 D GLN 263 ? NE2 ? D GLN 291 NE2 
176 1 Y 1 D LYS 267 ? CG  ? D LYS 295 CG  
177 1 Y 1 D LYS 267 ? CD  ? D LYS 295 CD  
178 1 Y 1 D LYS 267 ? CE  ? D LYS 295 CE  
179 1 Y 1 D LYS 267 ? NZ  ? D LYS 295 NZ  
180 1 Y 1 D LYS 269 ? CG  ? D LYS 297 CG  
181 1 Y 1 D LYS 269 ? CD  ? D LYS 297 CD  
182 1 Y 1 D LYS 269 ? CE  ? D LYS 297 CE  
183 1 Y 1 D LYS 269 ? NZ  ? D LYS 297 NZ  
184 1 Y 1 D ARG 277 ? CG  ? D ARG 305 CG  
185 1 Y 1 D ARG 277 ? CD  ? D ARG 305 CD  
186 1 Y 1 D ARG 277 ? NE  ? D ARG 305 NE  
187 1 Y 1 D ARG 277 ? CZ  ? D ARG 305 CZ  
188 1 Y 1 D ARG 277 ? NH1 ? D ARG 305 NH1 
189 1 Y 1 D ARG 277 ? NH2 ? D ARG 305 NH2 
190 1 Y 1 D ASN 278 ? CG  ? D ASN 306 CG  
191 1 Y 1 D ASN 278 ? OD1 ? D ASN 306 OD1 
192 1 Y 1 D ASN 278 ? ND2 ? D ASN 306 ND2 
193 1 Y 1 D GLU 280 ? CG  ? D GLU 308 CG  
194 1 Y 1 D GLU 280 ? CD  ? D GLU 308 CD  
195 1 Y 1 D GLU 280 ? OE1 ? D GLU 308 OE1 
196 1 Y 1 D GLU 280 ? OE2 ? D GLU 308 OE2 
197 1 Y 1 D LYS 296 ? CG  ? D LYS 324 CG  
198 1 Y 1 D LYS 296 ? CD  ? D LYS 324 CD  
199 1 Y 1 D LYS 296 ? CE  ? D LYS 324 CE  
200 1 Y 1 D LYS 296 ? NZ  ? D LYS 324 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZSA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     101.525 
_cell.length_a_esd                 ? 
_cell.length_b                     101.525 
_cell.length_b_esd                 ? 
_cell.length_c                     326.778 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        24 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8ZSA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                170 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 65' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZSA 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.29 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          62.60 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.1 MMT buffer, 25% PEG1500, pH7.0-7.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-01-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZSA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.40 
_reflns.d_resolution_low                               50 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     38865 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.9 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          10.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.360 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.955 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    3.40 
_reflns_shell.d_res_low                                     3.46 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1303 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.629 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          87.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8ZSA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            3.42 
_refine.ls_d_res_low                             29.62 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     38865 
_refine.ls_number_reflns_R_free                  3144 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    76.16 
_refine.ls_percent_reflns_R_free                 8.09 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2152 
_refine.ls_R_factor_R_free                       0.2477 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2124 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.38 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 25.18 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.44 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.42 
_refine_hist.d_res_low                        29.62 
_refine_hist.number_atoms_solvent             36 
_refine_hist.number_atoms_total               8964 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        8811 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         117 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.002 ? 9168  ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.520 ? 12498 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 5.853 ? 1231  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.041 ? 1393  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 1608  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 3.42 3.47 . . 45  523  25.00  . . . . 0.3069 . . . . . . . . . . . 0.3115 
'X-RAY DIFFRACTION' 3.47 3.53 . . 70  753  35.00  . . . . 0.3309 . . . . . . . . . . . 0.3777 
'X-RAY DIFFRACTION' 3.53 3.59 . . 85  967  46.00  . . . . 0.2909 . . . . . . . . . . . 0.3217 
'X-RAY DIFFRACTION' 3.59 3.65 . . 97  1083 52.00  . . . . 0.3113 . . . . . . . . . . . 0.3928 
'X-RAY DIFFRACTION' 3.65 3.72 . . 105 1144 53.00  . . . . 0.2978 . . . . . . . . . . . 0.3150 
'X-RAY DIFFRACTION' 3.72 3.80 . . 108 1171 56.00  . . . . 0.2746 . . . . . . . . . . . 0.2958 
'X-RAY DIFFRACTION' 3.80 3.88 . . 104 1231 57.00  . . . . 0.2625 . . . . . . . . . . . 0.3085 
'X-RAY DIFFRACTION' 3.88 3.97 . . 113 1276 61.00  . . . . 0.2471 . . . . . . . . . . . 0.3088 
'X-RAY DIFFRACTION' 3.97 4.07 . . 131 1478 67.00  . . . . 0.2215 . . . . . . . . . . . 0.2878 
'X-RAY DIFFRACTION' 4.07 4.18 . . 133 1546 73.00  . . . . 0.2124 . . . . . . . . . . . 0.2269 
'X-RAY DIFFRACTION' 4.18 4.30 . . 135 1651 78.00  . . . . 0.2096 . . . . . . . . . . . 0.2558 
'X-RAY DIFFRACTION' 4.30 4.44 . . 164 1878 87.00  . . . . 0.1957 . . . . . . . . . . . 0.2167 
'X-RAY DIFFRACTION' 4.44 4.60 . . 183 2000 93.00  . . . . 0.1967 . . . . . . . . . . . 0.2338 
'X-RAY DIFFRACTION' 4.60 4.78 . . 172 2006 96.00  . . . . 0.2034 . . . . . . . . . . . 0.2063 
'X-RAY DIFFRACTION' 4.78 5.00 . . 195 2116 99.00  . . . . 0.2056 . . . . . . . . . . . 0.2131 
'X-RAY DIFFRACTION' 5.00 5.26 . . 186 2129 100.00 . . . . 0.2152 . . . . . . . . . . . 0.3166 
'X-RAY DIFFRACTION' 5.26 5.59 . . 187 2149 100.00 . . . . 0.2130 . . . . . . . . . . . 0.2327 
'X-RAY DIFFRACTION' 5.59 6.02 . . 198 2103 100.00 . . . . 0.2280 . . . . . . . . . . . 0.2797 
'X-RAY DIFFRACTION' 6.02 6.61 . . 196 2134 100.00 . . . . 0.2232 . . . . . . . . . . . 0.2629 
'X-RAY DIFFRACTION' 6.62 7.55 . . 182 2115 100.00 . . . . 0.1991 . . . . . . . . . . . 0.2141 
'X-RAY DIFFRACTION' 7.56 9.47 . . 176 2143 100.00 . . . . 0.1586 . . . . . . . . . . . 0.2023 
# 
_struct.entry_id                     8ZSA 
_struct.title                        'Crystal structure of 4VPMT2' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8ZSA 
_struct_keywords.text            'methyltransferase, 4-vinylanisole biosynthesis, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 1 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 2 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    PDB 
_struct_ref.db_code                    8ZSA 
_struct_ref.pdbx_db_accession          8ZSA 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8ZSA A 1 ? 325 ? 8ZSA -27 ? 297 ? -27 297 
2 1 8ZSA B 1 ? 325 ? 8ZSA -27 ? 297 ? -27 297 
3 1 8ZSA C 1 ? 325 ? 8ZSA -27 ? 297 ? -27 297 
4 1 8ZSA D 1 ? 325 ? 8ZSA -27 ? 297 ? -27 297 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2430  ? 
1 MORE         -16   ? 
1 'SSA (A^2)'  22410 ? 
2 'ABSA (A^2)' 2420  ? 
2 MORE         -13   ? 
2 'SSA (A^2)'  22440 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E,G,H,J,L 
2 1 B,D,F,I,K,M   
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 49  ? THR A 54  ? LYS A 21  THR A 26  1 ? 6  
HELX_P HELX_P2  AA2 GLY A 56  ? TRP A 72  ? GLY A 28  TRP A 44  1 ? 17 
HELX_P HELX_P3  AA3 GLY A 92  ? VAL A 98  ? GLY A 64  VAL A 70  1 ? 7  
HELX_P HELX_P4  AA4 VAL A 98  ? LEU A 103 ? VAL A 70  LEU A 75  1 ? 6  
HELX_P HELX_P5  AA5 SER A 115 ? ARG A 123 ? SER A 87  ARG A 95  1 ? 9  
HELX_P HELX_P6  AA6 ARG A 143 ? ASP A 146 ? ARG A 115 ASP A 118 5 ? 4  
HELX_P HELX_P7  AA7 THR A 147 ? GLY A 153 ? THR A 119 GLY A 125 1 ? 7  
HELX_P HELX_P8  AA8 MET A 163 ? VAL A 167 ? MET A 135 VAL A 139 5 ? 5  
HELX_P HELX_P9  AA9 ASP A 169 ? LEU A 180 ? ASP A 141 LEU A 152 1 ? 12 
HELX_P HELX_P10 AB1 ALA A 196 ? ALA A 205 ? ALA A 168 ALA A 177 1 ? 10 
HELX_P HELX_P11 AB2 TRP A 210 ? GLN A 215 ? TRP A 182 GLN A 187 5 ? 6  
HELX_P HELX_P12 AB3 ASP A 216 ? VAL A 221 ? ASP A 188 VAL A 193 5 ? 6  
HELX_P HELX_P13 AB4 ASP A 229 ? SER A 240 ? ASP A 201 SER A 212 1 ? 12 
HELX_P HELX_P14 AB5 THR A 259 ? VAL A 270 ? THR A 231 VAL A 242 1 ? 12 
HELX_P HELX_P15 AB6 PRO A 278 ? LYS A 297 ? PRO A 250 LYS A 269 1 ? 20 
HELX_P HELX_P16 AB7 LYS B 49  ? LEU B 55  ? LYS B 21  LEU B 27  5 ? 7  
HELX_P HELX_P17 AB8 GLY B 56  ? TRP B 72  ? GLY B 28  TRP B 44  1 ? 17 
HELX_P HELX_P18 AB9 GLY B 92  ? VAL B 98  ? GLY B 64  VAL B 70  1 ? 7  
HELX_P HELX_P19 AC1 VAL B 98  ? LEU B 103 ? VAL B 70  LEU B 75  1 ? 6  
HELX_P HELX_P20 AC2 SER B 115 ? ASN B 126 ? SER B 87  ASN B 98  1 ? 12 
HELX_P HELX_P21 AC3 ARG B 143 ? ASP B 146 ? ARG B 115 ASP B 118 5 ? 4  
HELX_P HELX_P22 AC4 THR B 147 ? GLY B 153 ? THR B 119 GLY B 125 1 ? 7  
HELX_P HELX_P23 AC5 MET B 163 ? VAL B 167 ? MET B 135 VAL B 139 5 ? 5  
HELX_P HELX_P24 AC6 ASP B 169 ? LEU B 180 ? ASP B 141 LEU B 152 1 ? 12 
HELX_P HELX_P25 AC7 ALA B 196 ? LYS B 206 ? ALA B 168 LYS B 178 1 ? 11 
HELX_P HELX_P26 AC8 ASP B 216 ? VAL B 221 ? ASP B 188 VAL B 193 5 ? 6  
HELX_P HELX_P27 AC9 ASP B 229 ? SER B 240 ? ASP B 201 SER B 212 1 ? 12 
HELX_P HELX_P28 AD1 ALA B 260 ? VAL B 270 ? ALA B 232 VAL B 242 1 ? 11 
HELX_P HELX_P29 AD2 PHE B 273 ? ILE B 277 ? PHE B 245 ILE B 249 5 ? 5  
HELX_P HELX_P30 AD3 PRO B 278 ? LYS B 297 ? PRO B 250 LYS B 269 1 ? 20 
HELX_P HELX_P31 AD4 LYS C 49  ? THR C 54  ? LYS C 21  THR C 26  1 ? 6  
HELX_P HELX_P32 AD5 GLY C 56  ? TRP C 72  ? GLY C 28  TRP C 44  1 ? 17 
HELX_P HELX_P33 AD6 SER C 73  ? LEU C 75  ? SER C 45  LEU C 47  5 ? 3  
HELX_P HELX_P34 AD7 GLY C 92  ? LYS C 97  ? GLY C 64  LYS C 69  1 ? 6  
HELX_P HELX_P35 AD8 LEU C 99  ? LEU C 103 ? LEU C 71  LEU C 75  5 ? 5  
HELX_P HELX_P36 AD9 SER C 115 ? HIS C 125 ? SER C 87  HIS C 97  1 ? 11 
HELX_P HELX_P37 AE1 ARG C 143 ? ASP C 146 ? ARG C 115 ASP C 118 5 ? 4  
HELX_P HELX_P38 AE2 THR C 147 ? ASN C 152 ? THR C 119 ASN C 124 1 ? 6  
HELX_P HELX_P39 AE3 ASP C 169 ? LEU C 180 ? ASP C 141 LEU C 152 1 ? 12 
HELX_P HELX_P40 AE4 ALA C 196 ? LYS C 206 ? ALA C 168 LYS C 178 1 ? 11 
HELX_P HELX_P41 AE5 ASP C 216 ? VAL C 221 ? ASP C 188 VAL C 193 5 ? 6  
HELX_P HELX_P42 AE6 ASP C 229 ? SER C 240 ? ASP C 201 SER C 212 1 ? 12 
HELX_P HELX_P43 AE7 THR C 259 ? VAL C 270 ? THR C 231 VAL C 242 1 ? 12 
HELX_P HELX_P44 AE8 PHE C 273 ? ILE C 277 ? PHE C 245 ILE C 249 5 ? 5  
HELX_P HELX_P45 AE9 PRO C 278 ? LEU C 296 ? PRO C 250 LEU C 268 1 ? 19 
HELX_P HELX_P46 AF1 LYS D 49  ? THR D 54  ? LYS D 21  THR D 26  1 ? 6  
HELX_P HELX_P47 AF2 GLY D 56  ? ALA D 70  ? GLY D 28  ALA D 42  1 ? 15 
HELX_P HELX_P48 AF3 LEU D 71  ? LEU D 75  ? LEU D 43  LEU D 47  5 ? 5  
HELX_P HELX_P49 AF4 GLY D 92  ? VAL D 98  ? GLY D 64  VAL D 70  1 ? 7  
HELX_P HELX_P50 AF5 VAL D 98  ? LEU D 103 ? VAL D 70  LEU D 75  1 ? 6  
HELX_P HELX_P51 AF6 SER D 115 ? ASN D 126 ? SER D 87  ASN D 98  1 ? 12 
HELX_P HELX_P52 AF7 ARG D 143 ? ASP D 146 ? ARG D 115 ASP D 118 5 ? 4  
HELX_P HELX_P53 AF8 THR D 147 ? GLY D 153 ? THR D 119 GLY D 125 1 ? 7  
HELX_P HELX_P54 AF9 MET D 163 ? VAL D 167 ? MET D 135 VAL D 139 5 ? 5  
HELX_P HELX_P55 AG1 ASP D 169 ? LEU D 180 ? ASP D 141 LEU D 152 1 ? 12 
HELX_P HELX_P56 AG2 ALA D 196 ? LYS D 206 ? ALA D 168 LYS D 178 1 ? 11 
HELX_P HELX_P57 AG3 ASP D 216 ? PHE D 220 ? ASP D 188 PHE D 192 5 ? 5  
HELX_P HELX_P58 AG4 ASP D 229 ? SER D 240 ? ASP D 201 SER D 212 1 ? 12 
HELX_P HELX_P59 AG5 GLU D 261 ? VAL D 270 ? GLU D 233 VAL D 242 1 ? 10 
HELX_P HELX_P60 AG6 PRO D 278 ? LYS D 297 ? PRO D 250 LYS D 269 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_conn.id                            disulf1 
_struct_conn.conn_type_id                  disulf 
_struct_conn.pdbx_leaving_atom_flag        ? 
_struct_conn.pdbx_PDB_id                   ? 
_struct_conn.ptnr1_label_asym_id           A 
_struct_conn.ptnr1_label_comp_id           CYS 
_struct_conn.ptnr1_label_seq_id            58 
_struct_conn.ptnr1_label_atom_id           SG 
_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                1_555 
_struct_conn.ptnr2_label_asym_id           C 
_struct_conn.ptnr2_label_comp_id           CYS 
_struct_conn.ptnr2_label_seq_id            58 
_struct_conn.ptnr2_label_atom_id           SG 
_struct_conn.pdbx_ptnr2_label_alt_id       ? 
_struct_conn.pdbx_ptnr2_PDB_ins_code       ? 
_struct_conn.ptnr1_auth_asym_id            A 
_struct_conn.ptnr1_auth_comp_id            CYS 
_struct_conn.ptnr1_auth_seq_id             30 
_struct_conn.ptnr2_auth_asym_id            C 
_struct_conn.ptnr2_auth_comp_id            CYS 
_struct_conn.ptnr2_auth_seq_id             30 
_struct_conn.ptnr2_symmetry                1_555 
_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               2.028 
_struct_conn.pdbx_value_order              ? 
_struct_conn.pdbx_role                     ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       58 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     C 
_pdbx_modification_feature.modified_residue_label_seq_id      58 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        30 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      C 
_pdbx_modification_feature.modified_residue_auth_seq_id       30 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
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 GLY 153 A . ? GLY 125 A PRO 154 A ? PRO 126 A 1 0.71 
2 GLY 153 B . ? GLY 125 B PRO 154 B ? PRO 126 B 1 1.09 
3 GLY 153 C . ? GLY 125 C PRO 154 C ? PRO 126 C 1 2.17 
4 GLY 153 D . ? GLY 125 D PRO 154 D ? PRO 126 D 1 1.74 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2 ? 
AA2 ? 7 ? 
AA3 ? 7 ? 
AA4 ? 7 ? 
AA5 ? 7 ? 
AA6 ? 7 ? 
AA7 ? 7 ? 
AA8 ? 7 ? 
AA9 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? parallel      
AA5 3 4 ? parallel      
AA5 4 5 ? parallel      
AA5 5 6 ? anti-parallel 
AA5 6 7 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? parallel      
AA6 3 4 ? parallel      
AA6 4 5 ? parallel      
AA6 5 6 ? anti-parallel 
AA6 6 7 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? parallel      
AA7 3 4 ? parallel      
AA7 4 5 ? parallel      
AA7 5 6 ? anti-parallel 
AA7 6 7 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? parallel      
AA8 3 4 ? parallel      
AA8 4 5 ? parallel      
AA8 5 6 ? anti-parallel 
AA8 6 7 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? parallel      
AA9 3 4 ? parallel      
AA9 4 5 ? parallel      
AA9 5 6 ? anti-parallel 
AA9 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 SER A 76  ? PRO A 78  ? SER A 48  PRO A 50  
AA1 2 SER B 76  ? PRO B 78  ? SER B 48  PRO B 50  
AA2 1 ILE A 132 ? LEU A 136 ? ILE A 104 LEU A 108 
AA2 2 LEU A 109 ? ASP A 113 ? LEU A 81  ASP A 85  
AA2 3 VAL A 84  ? ILE A 87  ? VAL A 56  ILE A 59  
AA2 4 PHE A 155 ? CYS A 160 ? PHE A 127 CYS A 132 
AA2 5 LEU A 181 ? MET A 195 ? LEU A 153 MET A 167 
AA2 6 ALA A 309 ? ARG A 323 ? ALA A 281 ARG A 295 
AA2 7 ARG A 247 ? LYS A 254 ? ARG A 219 LYS A 226 
AA3 1 ILE A 132 ? LEU A 136 ? ILE A 104 LEU A 108 
AA3 2 LEU A 109 ? ASP A 113 ? LEU A 81  ASP A 85  
AA3 3 VAL A 84  ? ILE A 87  ? VAL A 56  ILE A 59  
AA3 4 PHE A 155 ? CYS A 160 ? PHE A 127 CYS A 132 
AA3 5 LEU A 181 ? MET A 195 ? LEU A 153 MET A 167 
AA3 6 ALA A 309 ? ARG A 323 ? ALA A 281 ARG A 295 
AA3 7 THR A 299 ? VAL A 303 ? THR A 271 VAL A 275 
AA4 1 ILE B 132 ? LEU B 136 ? ILE B 104 LEU B 108 
AA4 2 LEU B 109 ? ASP B 113 ? LEU B 81  ASP B 85  
AA4 3 VAL B 84  ? ILE B 87  ? VAL B 56  ILE B 59  
AA4 4 PHE B 155 ? MET B 161 ? PHE B 127 MET B 133 
AA4 5 LEU B 181 ? MET B 195 ? LEU B 153 MET B 167 
AA4 6 ALA B 309 ? ARG B 323 ? ALA B 281 ARG B 295 
AA4 7 ARG B 247 ? LYS B 254 ? ARG B 219 LYS B 226 
AA5 1 ILE B 132 ? LEU B 136 ? ILE B 104 LEU B 108 
AA5 2 LEU B 109 ? ASP B 113 ? LEU B 81  ASP B 85  
AA5 3 VAL B 84  ? ILE B 87  ? VAL B 56  ILE B 59  
AA5 4 PHE B 155 ? MET B 161 ? PHE B 127 MET B 133 
AA5 5 LEU B 181 ? MET B 195 ? LEU B 153 MET B 167 
AA5 6 ALA B 309 ? ARG B 323 ? ALA B 281 ARG B 295 
AA5 7 THR B 299 ? VAL B 303 ? THR B 271 VAL B 275 
AA6 1 ILE C 132 ? LEU C 136 ? ILE C 104 LEU C 108 
AA6 2 LEU C 109 ? ASP C 113 ? LEU C 81  ASP C 85  
AA6 3 VAL C 84  ? ILE C 87  ? VAL C 56  ILE C 59  
AA6 4 PHE C 155 ? MET C 161 ? PHE C 127 MET C 133 
AA6 5 LEU C 181 ? MET C 195 ? LEU C 153 MET C 167 
AA6 6 ALA C 309 ? ARG C 323 ? ALA C 281 ARG C 295 
AA6 7 ARG C 247 ? PHE C 257 ? ARG C 219 PHE C 229 
AA7 1 ILE C 132 ? LEU C 136 ? ILE C 104 LEU C 108 
AA7 2 LEU C 109 ? ASP C 113 ? LEU C 81  ASP C 85  
AA7 3 VAL C 84  ? ILE C 87  ? VAL C 56  ILE C 59  
AA7 4 PHE C 155 ? MET C 161 ? PHE C 127 MET C 133 
AA7 5 LEU C 181 ? MET C 195 ? LEU C 153 MET C 167 
AA7 6 ALA C 309 ? ARG C 323 ? ALA C 281 ARG C 295 
AA7 7 THR C 299 ? VAL C 303 ? THR C 271 VAL C 275 
AA8 1 ILE D 132 ? LEU D 136 ? ILE D 104 LEU D 108 
AA8 2 LEU D 109 ? ASP D 113 ? LEU D 81  ASP D 85  
AA8 3 VAL D 84  ? ILE D 87  ? VAL D 56  ILE D 59  
AA8 4 PHE D 155 ? CYS D 160 ? PHE D 127 CYS D 132 
AA8 5 LEU D 181 ? MET D 195 ? LEU D 153 MET D 167 
AA8 6 ALA D 309 ? ARG D 323 ? ALA D 281 ARG D 295 
AA8 7 ARG D 247 ? LYS D 254 ? ARG D 219 LYS D 226 
AA9 1 ILE D 132 ? LEU D 136 ? ILE D 104 LEU D 108 
AA9 2 LEU D 109 ? ASP D 113 ? LEU D 81  ASP D 85  
AA9 3 VAL D 84  ? ILE D 87  ? VAL D 56  ILE D 59  
AA9 4 PHE D 155 ? CYS D 160 ? PHE D 127 CYS D 132 
AA9 5 LEU D 181 ? MET D 195 ? LEU D 153 MET D 167 
AA9 6 ALA D 309 ? ARG D 323 ? ALA D 281 ARG D 295 
AA9 7 THR D 299 ? VAL D 303 ? THR D 271 VAL D 275 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 77  ? N TRP A 49  O TRP B 77  ? O TRP B 49  
AA2 1 2 O GLU A 135 ? O GLU A 107 N ALA A 111 ? N ALA A 83  
AA2 2 3 O VAL A 110 ? O VAL A 82  N VAL A 84  ? N VAL A 56  
AA2 3 4 N LEU A 85  ? N LEU A 57  O PHE A 159 ? O PHE A 131 
AA2 4 5 N CYS A 160 ? N CYS A 132 O VAL A 188 ? O VAL A 160 
AA2 5 6 N VAL A 191 ? N VAL A 163 O ILE A 318 ? O ILE A 290 
AA2 6 7 O VAL A 317 ? O VAL A 289 N GLY A 251 ? N GLY A 223 
AA3 1 2 O GLU A 135 ? O GLU A 107 N ALA A 111 ? N ALA A 83  
AA3 2 3 O VAL A 110 ? O VAL A 82  N VAL A 84  ? N VAL A 56  
AA3 3 4 N LEU A 85  ? N LEU A 57  O PHE A 159 ? O PHE A 131 
AA3 4 5 N CYS A 160 ? N CYS A 132 O VAL A 188 ? O VAL A 160 
AA3 5 6 N VAL A 191 ? N VAL A 163 O ILE A 318 ? O ILE A 290 
AA3 6 7 O GLU A 310 ? O GLU A 282 N GLY A 302 ? N GLY A 274 
AA4 1 2 O THR B 133 ? O THR B 105 N ALA B 111 ? N ALA B 83  
AA4 2 3 O VAL B 110 ? O VAL B 82  N VAL B 84  ? N VAL B 56  
AA4 3 4 N LEU B 85  ? N LEU B 57  O PHE B 159 ? O PHE B 131 
AA4 4 5 N CYS B 160 ? N CYS B 132 O VAL B 188 ? O VAL B 160 
AA4 5 6 N VAL B 191 ? N VAL B 163 O ILE B 318 ? O ILE B 290 
AA4 6 7 O VAL B 317 ? O VAL B 289 N GLY B 251 ? N GLY B 223 
AA5 1 2 O THR B 133 ? O THR B 105 N ALA B 111 ? N ALA B 83  
AA5 2 3 O VAL B 110 ? O VAL B 82  N VAL B 84  ? N VAL B 56  
AA5 3 4 N LEU B 85  ? N LEU B 57  O PHE B 159 ? O PHE B 131 
AA5 4 5 N CYS B 160 ? N CYS B 132 O VAL B 188 ? O VAL B 160 
AA5 5 6 N VAL B 191 ? N VAL B 163 O ILE B 318 ? O ILE B 290 
AA5 6 7 O GLU B 310 ? O GLU B 282 N GLY B 302 ? N GLY B 274 
AA6 1 2 O THR C 133 ? O THR C 105 N ALA C 111 ? N ALA C 83  
AA6 2 3 O VAL C 110 ? O VAL C 82  N VAL C 84  ? N VAL C 56  
AA6 3 4 N LEU C 85  ? N LEU C 57  O PHE C 159 ? O PHE C 131 
AA6 4 5 N CYS C 160 ? N CYS C 132 O VAL C 188 ? O VAL C 160 
AA6 5 6 N VAL C 191 ? N VAL C 163 O ILE C 318 ? O ILE C 290 
AA6 6 7 O LEU C 315 ? O LEU C 287 N GLN C 253 ? N GLN C 225 
AA7 1 2 O THR C 133 ? O THR C 105 N ALA C 111 ? N ALA C 83  
AA7 2 3 O VAL C 110 ? O VAL C 82  N VAL C 84  ? N VAL C 56  
AA7 3 4 N LEU C 85  ? N LEU C 57  O PHE C 159 ? O PHE C 131 
AA7 4 5 N CYS C 160 ? N CYS C 132 O VAL C 188 ? O VAL C 160 
AA7 5 6 N VAL C 191 ? N VAL C 163 O ILE C 318 ? O ILE C 290 
AA7 6 7 O GLU C 310 ? O GLU C 282 N GLY C 302 ? N GLY C 274 
AA8 1 2 O GLU D 135 ? O GLU D 107 N ALA D 111 ? N ALA D 83  
AA8 2 3 O VAL D 110 ? O VAL D 82  N ASP D 86  ? N ASP D 58  
AA8 3 4 N LEU D 85  ? N LEU D 57  O PHE D 159 ? O PHE D 131 
AA8 4 5 N CYS D 160 ? N CYS D 132 O VAL D 188 ? O VAL D 160 
AA8 5 6 N VAL D 191 ? N VAL D 163 O ILE D 318 ? O ILE D 290 
AA8 6 7 O THR D 319 ? O THR D 291 N ASP D 249 ? N ASP D 221 
AA9 1 2 O GLU D 135 ? O GLU D 107 N ALA D 111 ? N ALA D 83  
AA9 2 3 O VAL D 110 ? O VAL D 82  N ASP D 86  ? N ASP D 58  
AA9 3 4 N LEU D 85  ? N LEU D 57  O PHE D 159 ? O PHE D 131 
AA9 4 5 N CYS D 160 ? N CYS D 132 O VAL D 188 ? O VAL D 160 
AA9 5 6 N VAL D 191 ? N VAL D 163 O ILE D 318 ? O ILE D 290 
AA9 6 7 O GLU D 310 ? O GLU D 282 N GLY D 302 ? N GLY D 274 
# 
_pdbx_entry_details.entry_id                   8ZSA 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ALA A 15  ? ? 55.53   -110.88 
2  1 ARG A 17  ? ? 57.75   -161.54 
3  1 GLN A 51  ? ? -57.26  -72.92  
4  1 HIS A 97  ? ? -104.76 -71.79  
5  1 ASN A 98  ? ? -79.15  30.18   
6  1 THR A 103 ? ? -138.70 -62.36  
7  1 MET A 133 ? ? -87.46  -141.45 
8  1 TRP A 182 ? ? -103.50 -81.36  
9  1 ALA A 183 ? ? 37.84   -62.74  
10 1 ALA B 15  ? ? 56.60   -109.39 
11 1 ARG B 17  ? ? 59.06   -156.60 
12 1 LYS B 21  ? ? 53.89   70.71   
13 1 ARG B 115 ? ? -101.25 76.74   
14 1 MET B 135 ? ? -154.67 -26.86  
15 1 ALA B 165 ? ? -65.11  -71.53  
16 1 ASP B 188 ? ? -99.85  51.47   
17 1 ARG C 17  ? ? -90.10  59.57   
18 1 PRO C 63  ? ? -82.32  32.50   
19 1 ILE C 66  ? ? -88.00  31.61   
20 1 ALA C 67  ? ? -135.27 -50.24  
21 1 GLN C 96  ? ? -91.76  -62.49  
22 1 HIS C 97  ? ? -82.28  -79.28  
23 1 ASN C 98  ? ? -75.97  45.03   
24 1 THR C 103 ? ? -137.14 -71.77  
25 1 ARG C 115 ? ? -114.71 79.44   
26 1 MET C 135 ? ? -157.39 -33.08  
27 1 ASP C 188 ? ? -109.80 49.05   
28 1 ARG C 219 ? ? -170.03 136.65  
29 1 ALA D 15  ? ? 57.66   -112.23 
30 1 ARG D 17  ? ? 57.80   87.48   
31 1 LYS D 21  ? ? 54.87   70.23   
32 1 ASP D 85  ? ? -175.75 142.91  
33 1 THR D 103 ? ? -136.35 -53.97  
34 1 MET D 133 ? ? -83.77  -135.12 
35 1 MET D 135 ? ? -149.38 -33.82  
36 1 ASP D 188 ? ? -99.55  46.34   
37 1 ASP D 201 ? ? -152.17 83.32   
38 1 LEU D 287 ? ? -171.58 149.03  
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         2.3352 
_pdbx_refine_tls.origin_y         2.0404 
_pdbx_refine_tls.origin_z         8.2938 
_pdbx_refine_tls.T[1][1]          0.4775 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          0.1134 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0823 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2977 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0104 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.2852 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.6833 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0860 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.1107 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.8657 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.2704 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          1.0009 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.1339 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.1324 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          -0.0447 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0455 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.1826 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0590 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          0.1747 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.1083 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.2274 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET -27 ? A MET 1  
2   1 Y 1 A GLY -26 ? A GLY 2  
3   1 Y 1 A SER -25 ? A SER 3  
4   1 Y 1 A HIS -24 ? A HIS 4  
5   1 Y 1 A HIS -23 ? A HIS 5  
6   1 Y 1 A HIS -22 ? A HIS 6  
7   1 Y 1 A HIS -21 ? A HIS 7  
8   1 Y 1 A HIS -20 ? A HIS 8  
9   1 Y 1 A HIS -19 ? A HIS 9  
10  1 Y 1 A HIS -18 ? A HIS 10 
11  1 Y 1 A HIS -17 ? A HIS 11 
12  1 Y 1 A GLY -16 ? A GLY 12 
13  1 Y 1 A SER -15 ? A SER 13 
14  1 Y 1 A ASP -14 ? A ASP 14 
15  1 Y 1 A TYR -13 ? A TYR 15 
16  1 Y 1 A ASP -12 ? A ASP 16 
17  1 Y 1 A ILE -11 ? A ILE 17 
18  1 Y 1 A PRO -10 ? A PRO 18 
19  1 Y 1 A THR -9  ? A THR 19 
20  1 Y 1 A THR -8  ? A THR 20 
21  1 Y 1 A GLU -7  ? A GLU 21 
22  1 Y 1 A ASN -6  ? A ASN 22 
23  1 Y 1 A LEU -5  ? A LEU 23 
24  1 Y 1 A TYR -4  ? A TYR 24 
25  1 Y 1 A PHE -3  ? A PHE 25 
26  1 Y 1 A GLN -2  ? A GLN 26 
27  1 Y 1 A GLY -1  ? A GLY 27 
28  1 Y 1 A SER 0   ? A SER 28 
29  1 Y 1 A MET 1   ? A MET 29 
30  1 Y 1 A GLU 2   ? A GLU 30 
31  1 Y 1 A LYS 3   ? A LYS 31 
32  1 Y 1 A GLN 4   ? A GLN 32 
33  1 Y 1 A ASP 5   ? A ASP 33 
34  1 Y 1 A THR 6   ? A THR 34 
35  1 Y 1 A HIS 7   ? A HIS 35 
36  1 Y 1 A VAL 8   ? A VAL 36 
37  1 Y 1 A ASN 9   ? A ASN 37 
38  1 Y 1 A THR 10  ? A THR 38 
39  1 Y 1 A GLU 11  ? A GLU 39 
40  1 Y 1 A LYS 12  ? A LYS 40 
41  1 Y 1 A GLN 13  ? A GLN 41 
42  1 Y 1 B MET -27 ? B MET 1  
43  1 Y 1 B GLY -26 ? B GLY 2  
44  1 Y 1 B SER -25 ? B SER 3  
45  1 Y 1 B HIS -24 ? B HIS 4  
46  1 Y 1 B HIS -23 ? B HIS 5  
47  1 Y 1 B HIS -22 ? B HIS 6  
48  1 Y 1 B HIS -21 ? B HIS 7  
49  1 Y 1 B HIS -20 ? B HIS 8  
50  1 Y 1 B HIS -19 ? B HIS 9  
51  1 Y 1 B HIS -18 ? B HIS 10 
52  1 Y 1 B HIS -17 ? B HIS 11 
53  1 Y 1 B GLY -16 ? B GLY 12 
54  1 Y 1 B SER -15 ? B SER 13 
55  1 Y 1 B ASP -14 ? B ASP 14 
56  1 Y 1 B TYR -13 ? B TYR 15 
57  1 Y 1 B ASP -12 ? B ASP 16 
58  1 Y 1 B ILE -11 ? B ILE 17 
59  1 Y 1 B PRO -10 ? B PRO 18 
60  1 Y 1 B THR -9  ? B THR 19 
61  1 Y 1 B THR -8  ? B THR 20 
62  1 Y 1 B GLU -7  ? B GLU 21 
63  1 Y 1 B ASN -6  ? B ASN 22 
64  1 Y 1 B LEU -5  ? B LEU 23 
65  1 Y 1 B TYR -4  ? B TYR 24 
66  1 Y 1 B PHE -3  ? B PHE 25 
67  1 Y 1 B GLN -2  ? B GLN 26 
68  1 Y 1 B GLY -1  ? B GLY 27 
69  1 Y 1 B SER 0   ? B SER 28 
70  1 Y 1 B MET 1   ? B MET 29 
71  1 Y 1 B GLU 2   ? B GLU 30 
72  1 Y 1 B LYS 3   ? B LYS 31 
73  1 Y 1 B GLN 4   ? B GLN 32 
74  1 Y 1 B ASP 5   ? B ASP 33 
75  1 Y 1 B THR 6   ? B THR 34 
76  1 Y 1 B HIS 7   ? B HIS 35 
77  1 Y 1 B VAL 8   ? B VAL 36 
78  1 Y 1 B ASN 9   ? B ASN 37 
79  1 Y 1 B THR 10  ? B THR 38 
80  1 Y 1 B GLU 11  ? B GLU 39 
81  1 Y 1 B LYS 12  ? B LYS 40 
82  1 Y 1 B GLN 13  ? B GLN 41 
83  1 Y 1 C MET -27 ? C MET 1  
84  1 Y 1 C GLY -26 ? C GLY 2  
85  1 Y 1 C SER -25 ? C SER 3  
86  1 Y 1 C HIS -24 ? C HIS 4  
87  1 Y 1 C HIS -23 ? C HIS 5  
88  1 Y 1 C HIS -22 ? C HIS 6  
89  1 Y 1 C HIS -21 ? C HIS 7  
90  1 Y 1 C HIS -20 ? C HIS 8  
91  1 Y 1 C HIS -19 ? C HIS 9  
92  1 Y 1 C HIS -18 ? C HIS 10 
93  1 Y 1 C HIS -17 ? C HIS 11 
94  1 Y 1 C GLY -16 ? C GLY 12 
95  1 Y 1 C SER -15 ? C SER 13 
96  1 Y 1 C ASP -14 ? C ASP 14 
97  1 Y 1 C TYR -13 ? C TYR 15 
98  1 Y 1 C ASP -12 ? C ASP 16 
99  1 Y 1 C ILE -11 ? C ILE 17 
100 1 Y 1 C PRO -10 ? C PRO 18 
101 1 Y 1 C THR -9  ? C THR 19 
102 1 Y 1 C THR -8  ? C THR 20 
103 1 Y 1 C GLU -7  ? C GLU 21 
104 1 Y 1 C ASN -6  ? C ASN 22 
105 1 Y 1 C LEU -5  ? C LEU 23 
106 1 Y 1 C TYR -4  ? C TYR 24 
107 1 Y 1 C PHE -3  ? C PHE 25 
108 1 Y 1 C GLN -2  ? C GLN 26 
109 1 Y 1 C GLY -1  ? C GLY 27 
110 1 Y 1 C SER 0   ? C SER 28 
111 1 Y 1 C MET 1   ? C MET 29 
112 1 Y 1 C GLU 2   ? C GLU 30 
113 1 Y 1 C LYS 3   ? C LYS 31 
114 1 Y 1 C GLN 4   ? C GLN 32 
115 1 Y 1 C ASP 5   ? C ASP 33 
116 1 Y 1 C THR 6   ? C THR 34 
117 1 Y 1 C HIS 7   ? C HIS 35 
118 1 Y 1 C VAL 8   ? C VAL 36 
119 1 Y 1 C ASN 9   ? C ASN 37 
120 1 Y 1 C THR 10  ? C THR 38 
121 1 Y 1 C GLU 11  ? C GLU 39 
122 1 Y 1 C LYS 12  ? C LYS 40 
123 1 Y 1 C GLN 13  ? C GLN 41 
124 1 Y 1 C GLU 14  ? C GLU 42 
125 1 Y 1 D MET -27 ? D MET 1  
126 1 Y 1 D GLY -26 ? D GLY 2  
127 1 Y 1 D SER -25 ? D SER 3  
128 1 Y 1 D HIS -24 ? D HIS 4  
129 1 Y 1 D HIS -23 ? D HIS 5  
130 1 Y 1 D HIS -22 ? D HIS 6  
131 1 Y 1 D HIS -21 ? D HIS 7  
132 1 Y 1 D HIS -20 ? D HIS 8  
133 1 Y 1 D HIS -19 ? D HIS 9  
134 1 Y 1 D HIS -18 ? D HIS 10 
135 1 Y 1 D HIS -17 ? D HIS 11 
136 1 Y 1 D GLY -16 ? D GLY 12 
137 1 Y 1 D SER -15 ? D SER 13 
138 1 Y 1 D ASP -14 ? D ASP 14 
139 1 Y 1 D TYR -13 ? D TYR 15 
140 1 Y 1 D ASP -12 ? D ASP 16 
141 1 Y 1 D ILE -11 ? D ILE 17 
142 1 Y 1 D PRO -10 ? D PRO 18 
143 1 Y 1 D THR -9  ? D THR 19 
144 1 Y 1 D THR -8  ? D THR 20 
145 1 Y 1 D GLU -7  ? D GLU 21 
146 1 Y 1 D ASN -6  ? D ASN 22 
147 1 Y 1 D LEU -5  ? D LEU 23 
148 1 Y 1 D TYR -4  ? D TYR 24 
149 1 Y 1 D PHE -3  ? D PHE 25 
150 1 Y 1 D GLN -2  ? D GLN 26 
151 1 Y 1 D GLY -1  ? D GLY 27 
152 1 Y 1 D SER 0   ? D SER 28 
153 1 Y 1 D MET 1   ? D MET 29 
154 1 Y 1 D GLU 2   ? D GLU 30 
155 1 Y 1 D LYS 3   ? D LYS 31 
156 1 Y 1 D GLN 4   ? D GLN 32 
157 1 Y 1 D ASP 5   ? D ASP 33 
158 1 Y 1 D THR 6   ? D THR 34 
159 1 Y 1 D HIS 7   ? D HIS 35 
160 1 Y 1 D VAL 8   ? D VAL 36 
161 1 Y 1 D ASN 9   ? D ASN 37 
162 1 Y 1 D THR 10  ? D THR 38 
163 1 Y 1 D GLU 11  ? D GLU 39 
164 1 Y 1 D LYS 12  ? D LYS 40 
165 1 Y 1 D GLN 13  ? D GLN 41 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
4VP C2     C N N 1   
4VP C3     C N N 2   
4VP "C1'"  C Y N 3   
4VP "C6'"  C Y N 4   
4VP "C5'"  C Y N 5   
4VP "C4'"  C Y N 6   
4VP "O4'"  O N N 7   
4VP "C3'"  C Y N 8   
4VP "C2'"  C Y N 9   
4VP H1     H N N 10  
4VP H2     H N N 11  
4VP H3     H N N 12  
4VP H4     H N N 13  
4VP H5     H N N 14  
4VP H6     H N N 15  
4VP H7     H N N 16  
4VP H8     H N N 17  
ALA N      N N N 18  
ALA CA     C N S 19  
ALA C      C N N 20  
ALA O      O N N 21  
ALA CB     C N N 22  
ALA OXT    O N N 23  
ALA H      H N N 24  
ALA H2     H N N 25  
ALA HA     H N N 26  
ALA HB1    H N N 27  
ALA HB2    H N N 28  
ALA HB3    H N N 29  
ALA HXT    H N N 30  
ARG N      N N N 31  
ARG CA     C N S 32  
ARG C      C N N 33  
ARG O      O N N 34  
ARG CB     C N N 35  
ARG CG     C N N 36  
ARG CD     C N N 37  
ARG NE     N N N 38  
ARG CZ     C N N 39  
ARG NH1    N N N 40  
ARG NH2    N N N 41  
ARG OXT    O N N 42  
ARG H      H N N 43  
ARG H2     H N N 44  
ARG HA     H N N 45  
ARG HB2    H N N 46  
ARG HB3    H N N 47  
ARG HG2    H N N 48  
ARG HG3    H N N 49  
ARG HD2    H N N 50  
ARG HD3    H N N 51  
ARG HE     H N N 52  
ARG HH11   H N N 53  
ARG HH12   H N N 54  
ARG HH21   H N N 55  
ARG HH22   H N N 56  
ARG HXT    H N N 57  
ASN N      N N N 58  
ASN CA     C N S 59  
ASN C      C N N 60  
ASN O      O N N 61  
ASN CB     C N N 62  
ASN CG     C N N 63  
ASN OD1    O N N 64  
ASN ND2    N N N 65  
ASN OXT    O N N 66  
ASN H      H N N 67  
ASN H2     H N N 68  
ASN HA     H N N 69  
ASN HB2    H N N 70  
ASN HB3    H N N 71  
ASN HD21   H N N 72  
ASN HD22   H N N 73  
ASN HXT    H N N 74  
ASP N      N N N 75  
ASP CA     C N S 76  
ASP C      C N N 77  
ASP O      O N N 78  
ASP CB     C N N 79  
ASP CG     C N N 80  
ASP OD1    O N N 81  
ASP OD2    O N N 82  
ASP OXT    O N N 83  
ASP H      H N N 84  
ASP H2     H N N 85  
ASP HA     H N N 86  
ASP HB2    H N N 87  
ASP HB3    H N N 88  
ASP HD2    H N N 89  
ASP HXT    H N N 90  
CYS N      N N N 91  
CYS CA     C N R 92  
CYS C      C N N 93  
CYS O      O N N 94  
CYS CB     C N N 95  
CYS SG     S N N 96  
CYS OXT    O N N 97  
CYS H      H N N 98  
CYS H2     H N N 99  
CYS HA     H N N 100 
CYS HB2    H N N 101 
CYS HB3    H N N 102 
CYS HG     H N N 103 
CYS HXT    H N N 104 
GLN N      N N N 105 
GLN CA     C N S 106 
GLN C      C N N 107 
GLN O      O N N 108 
GLN CB     C N N 109 
GLN CG     C N N 110 
GLN CD     C N N 111 
GLN OE1    O N N 112 
GLN NE2    N N N 113 
GLN OXT    O N N 114 
GLN H      H N N 115 
GLN H2     H N N 116 
GLN HA     H N N 117 
GLN HB2    H N N 118 
GLN HB3    H N N 119 
GLN HG2    H N N 120 
GLN HG3    H N N 121 
GLN HE21   H N N 122 
GLN HE22   H N N 123 
GLN HXT    H N N 124 
GLU N      N N N 125 
GLU CA     C N S 126 
GLU C      C N N 127 
GLU O      O N N 128 
GLU CB     C N N 129 
GLU CG     C N N 130 
GLU CD     C N N 131 
GLU OE1    O N N 132 
GLU OE2    O N N 133 
GLU OXT    O N N 134 
GLU H      H N N 135 
GLU H2     H N N 136 
GLU HA     H N N 137 
GLU HB2    H N N 138 
GLU HB3    H N N 139 
GLU HG2    H N N 140 
GLU HG3    H N N 141 
GLU HE2    H N N 142 
GLU HXT    H N N 143 
GLY N      N N N 144 
GLY CA     C N N 145 
GLY C      C N N 146 
GLY O      O N N 147 
GLY OXT    O N N 148 
GLY H      H N N 149 
GLY H2     H N N 150 
GLY HA2    H N N 151 
GLY HA3    H N N 152 
GLY HXT    H N N 153 
HIS N      N N N 154 
HIS CA     C N S 155 
HIS C      C N N 156 
HIS O      O N N 157 
HIS CB     C N N 158 
HIS CG     C Y N 159 
HIS ND1    N Y N 160 
HIS CD2    C Y N 161 
HIS CE1    C Y N 162 
HIS NE2    N Y N 163 
HIS OXT    O N N 164 
HIS H      H N N 165 
HIS H2     H N N 166 
HIS HA     H N N 167 
HIS HB2    H N N 168 
HIS HB3    H N N 169 
HIS HD1    H N N 170 
HIS HD2    H N N 171 
HIS HE1    H N N 172 
HIS HE2    H N N 173 
HIS HXT    H N N 174 
HOH O      O N N 175 
HOH H1     H N N 176 
HOH H2     H N N 177 
ILE N      N N N 178 
ILE CA     C N S 179 
ILE C      C N N 180 
ILE O      O N N 181 
ILE CB     C N S 182 
ILE CG1    C N N 183 
ILE CG2    C N N 184 
ILE CD1    C N N 185 
ILE OXT    O N N 186 
ILE H      H N N 187 
ILE H2     H N N 188 
ILE HA     H N N 189 
ILE HB     H N N 190 
ILE HG12   H N N 191 
ILE HG13   H N N 192 
ILE HG21   H N N 193 
ILE HG22   H N N 194 
ILE HG23   H N N 195 
ILE HD11   H N N 196 
ILE HD12   H N N 197 
ILE HD13   H N N 198 
ILE HXT    H N N 199 
LEU N      N N N 200 
LEU CA     C N S 201 
LEU C      C N N 202 
LEU O      O N N 203 
LEU CB     C N N 204 
LEU CG     C N N 205 
LEU CD1    C N N 206 
LEU CD2    C N N 207 
LEU OXT    O N N 208 
LEU H      H N N 209 
LEU H2     H N N 210 
LEU HA     H N N 211 
LEU HB2    H N N 212 
LEU HB3    H N N 213 
LEU HG     H N N 214 
LEU HD11   H N N 215 
LEU HD12   H N N 216 
LEU HD13   H N N 217 
LEU HD21   H N N 218 
LEU HD22   H N N 219 
LEU HD23   H N N 220 
LEU HXT    H N N 221 
LYS N      N N N 222 
LYS CA     C N S 223 
LYS C      C N N 224 
LYS O      O N N 225 
LYS CB     C N N 226 
LYS CG     C N N 227 
LYS CD     C N N 228 
LYS CE     C N N 229 
LYS NZ     N N N 230 
LYS OXT    O N N 231 
LYS H      H N N 232 
LYS H2     H N N 233 
LYS HA     H N N 234 
LYS HB2    H N N 235 
LYS HB3    H N N 236 
LYS HG2    H N N 237 
LYS HG3    H N N 238 
LYS HD2    H N N 239 
LYS HD3    H N N 240 
LYS HE2    H N N 241 
LYS HE3    H N N 242 
LYS HZ1    H N N 243 
LYS HZ2    H N N 244 
LYS HZ3    H N N 245 
LYS HXT    H N N 246 
MET N      N N N 247 
MET CA     C N S 248 
MET C      C N N 249 
MET O      O N N 250 
MET CB     C N N 251 
MET CG     C N N 252 
MET SD     S N N 253 
MET CE     C N N 254 
MET OXT    O N N 255 
MET H      H N N 256 
MET H2     H N N 257 
MET HA     H N N 258 
MET HB2    H N N 259 
MET HB3    H N N 260 
MET HG2    H N N 261 
MET HG3    H N N 262 
MET HE1    H N N 263 
MET HE2    H N N 264 
MET HE3    H N N 265 
MET HXT    H N N 266 
PHE N      N N N 267 
PHE CA     C N S 268 
PHE C      C N N 269 
PHE O      O N N 270 
PHE CB     C N N 271 
PHE CG     C Y N 272 
PHE CD1    C Y N 273 
PHE CD2    C Y N 274 
PHE CE1    C Y N 275 
PHE CE2    C Y N 276 
PHE CZ     C Y N 277 
PHE OXT    O N N 278 
PHE H      H N N 279 
PHE H2     H N N 280 
PHE HA     H N N 281 
PHE HB2    H N N 282 
PHE HB3    H N N 283 
PHE HD1    H N N 284 
PHE HD2    H N N 285 
PHE HE1    H N N 286 
PHE HE2    H N N 287 
PHE HZ     H N N 288 
PHE HXT    H N N 289 
PRO N      N N N 290 
PRO CA     C N S 291 
PRO C      C N N 292 
PRO O      O N N 293 
PRO CB     C N N 294 
PRO CG     C N N 295 
PRO CD     C N N 296 
PRO OXT    O N N 297 
PRO H      H N N 298 
PRO HA     H N N 299 
PRO HB2    H N N 300 
PRO HB3    H N N 301 
PRO HG2    H N N 302 
PRO HG3    H N N 303 
PRO HD2    H N N 304 
PRO HD3    H N N 305 
PRO HXT    H N N 306 
SAM N      N N N 307 
SAM CA     C N S 308 
SAM C      C N N 309 
SAM O      O N N 310 
SAM OXT    O N N 311 
SAM CB     C N N 312 
SAM CG     C N N 313 
SAM SD     S N S 314 
SAM CE     C N N 315 
SAM "C5'"  C N N 316 
SAM "C4'"  C N S 317 
SAM "O4'"  O N N 318 
SAM "C3'"  C N S 319 
SAM "O3'"  O N N 320 
SAM "C2'"  C N R 321 
SAM "O2'"  O N N 322 
SAM "C1'"  C N R 323 
SAM N9     N Y N 324 
SAM C8     C Y N 325 
SAM N7     N Y N 326 
SAM C5     C Y N 327 
SAM C6     C Y N 328 
SAM N6     N N N 329 
SAM N1     N Y N 330 
SAM C2     C Y N 331 
SAM N3     N Y N 332 
SAM C4     C Y N 333 
SAM HN1    H N N 334 
SAM HN2    H N N 335 
SAM HA     H N N 336 
SAM HB1    H N N 337 
SAM HB2    H N N 338 
SAM HG1    H N N 339 
SAM HG2    H N N 340 
SAM HE1    H N N 341 
SAM HE2    H N N 342 
SAM HE3    H N N 343 
SAM "H5'1" H N N 344 
SAM "H5'2" H N N 345 
SAM "H4'"  H N N 346 
SAM "H3'"  H N N 347 
SAM "HO3'" H N N 348 
SAM "H2'"  H N N 349 
SAM "HO2'" H N N 350 
SAM "H1'"  H N N 351 
SAM H8     H N N 352 
SAM HN61   H N N 353 
SAM HN62   H N N 354 
SAM H2     H N N 355 
SER N      N N N 356 
SER CA     C N S 357 
SER C      C N N 358 
SER O      O N N 359 
SER CB     C N N 360 
SER OG     O N N 361 
SER OXT    O N N 362 
SER H      H N N 363 
SER H2     H N N 364 
SER HA     H N N 365 
SER HB2    H N N 366 
SER HB3    H N N 367 
SER HG     H N N 368 
SER HXT    H N N 369 
THR N      N N N 370 
THR CA     C N S 371 
THR C      C N N 372 
THR O      O N N 373 
THR CB     C N R 374 
THR OG1    O N N 375 
THR CG2    C N N 376 
THR OXT    O N N 377 
THR H      H N N 378 
THR H2     H N N 379 
THR HA     H N N 380 
THR HB     H N N 381 
THR HG1    H N N 382 
THR HG21   H N N 383 
THR HG22   H N N 384 
THR HG23   H N N 385 
THR HXT    H N N 386 
TRP N      N N N 387 
TRP CA     C N S 388 
TRP C      C N N 389 
TRP O      O N N 390 
TRP CB     C N N 391 
TRP CG     C Y N 392 
TRP CD1    C Y N 393 
TRP CD2    C Y N 394 
TRP NE1    N Y N 395 
TRP CE2    C Y N 396 
TRP CE3    C Y N 397 
TRP CZ2    C Y N 398 
TRP CZ3    C Y N 399 
TRP CH2    C Y N 400 
TRP OXT    O N N 401 
TRP H      H N N 402 
TRP H2     H N N 403 
TRP HA     H N N 404 
TRP HB2    H N N 405 
TRP HB3    H N N 406 
TRP HD1    H N N 407 
TRP HE1    H N N 408 
TRP HE3    H N N 409 
TRP HZ2    H N N 410 
TRP HZ3    H N N 411 
TRP HH2    H N N 412 
TRP HXT    H N N 413 
TYR N      N N N 414 
TYR CA     C N S 415 
TYR C      C N N 416 
TYR O      O N N 417 
TYR CB     C N N 418 
TYR CG     C Y N 419 
TYR CD1    C Y N 420 
TYR CD2    C Y N 421 
TYR CE1    C Y N 422 
TYR CE2    C Y N 423 
TYR CZ     C Y N 424 
TYR OH     O N N 425 
TYR OXT    O N N 426 
TYR H      H N N 427 
TYR H2     H N N 428 
TYR HA     H N N 429 
TYR HB2    H N N 430 
TYR HB3    H N N 431 
TYR HD1    H N N 432 
TYR HD2    H N N 433 
TYR HE1    H N N 434 
TYR HE2    H N N 435 
TYR HH     H N N 436 
TYR HXT    H N N 437 
VAL N      N N N 438 
VAL CA     C N S 439 
VAL C      C N N 440 
VAL O      O N N 441 
VAL CB     C N N 442 
VAL CG1    C N N 443 
VAL CG2    C N N 444 
VAL OXT    O N N 445 
VAL H      H N N 446 
VAL H2     H N N 447 
VAL HA     H N N 448 
VAL HB     H N N 449 
VAL HG11   H N N 450 
VAL HG12   H N N 451 
VAL HG13   H N N 452 
VAL HG21   H N N 453 
VAL HG22   H N N 454 
VAL HG23   H N N 455 
VAL HXT    H N N 456 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
4VP "O4'" "C4'"  sing N N 1   
4VP "C4'" "C3'"  doub Y N 2   
4VP "C4'" "C5'"  sing Y N 3   
4VP "C3'" "C2'"  sing Y N 4   
4VP "C5'" "C6'"  doub Y N 5   
4VP "C2'" "C1'"  doub Y N 6   
4VP "C6'" "C1'"  sing Y N 7   
4VP "C1'" C3     sing N N 8   
4VP C3    C2     doub N N 9   
4VP C2    H1     sing N N 10  
4VP C2    H2     sing N N 11  
4VP C3    H3     sing N N 12  
4VP "C6'" H4     sing N N 13  
4VP "C5'" H5     sing N N 14  
4VP "O4'" H6     sing N N 15  
4VP "C3'" H7     sing N N 16  
4VP "C2'" H8     sing N N 17  
ALA N     CA     sing N N 18  
ALA N     H      sing N N 19  
ALA N     H2     sing N N 20  
ALA CA    C      sing N N 21  
ALA CA    CB     sing N N 22  
ALA CA    HA     sing N N 23  
ALA C     O      doub N N 24  
ALA C     OXT    sing N N 25  
ALA CB    HB1    sing N N 26  
ALA CB    HB2    sing N N 27  
ALA CB    HB3    sing N N 28  
ALA OXT   HXT    sing N N 29  
ARG N     CA     sing N N 30  
ARG N     H      sing N N 31  
ARG N     H2     sing N N 32  
ARG CA    C      sing N N 33  
ARG CA    CB     sing N N 34  
ARG CA    HA     sing N N 35  
ARG C     O      doub N N 36  
ARG C     OXT    sing N N 37  
ARG CB    CG     sing N N 38  
ARG CB    HB2    sing N N 39  
ARG CB    HB3    sing N N 40  
ARG CG    CD     sing N N 41  
ARG CG    HG2    sing N N 42  
ARG CG    HG3    sing N N 43  
ARG CD    NE     sing N N 44  
ARG CD    HD2    sing N N 45  
ARG CD    HD3    sing N N 46  
ARG NE    CZ     sing N N 47  
ARG NE    HE     sing N N 48  
ARG CZ    NH1    sing N N 49  
ARG CZ    NH2    doub N N 50  
ARG NH1   HH11   sing N N 51  
ARG NH1   HH12   sing N N 52  
ARG NH2   HH21   sing N N 53  
ARG NH2   HH22   sing N N 54  
ARG OXT   HXT    sing N N 55  
ASN N     CA     sing N N 56  
ASN N     H      sing N N 57  
ASN N     H2     sing N N 58  
ASN CA    C      sing N N 59  
ASN CA    CB     sing N N 60  
ASN CA    HA     sing N N 61  
ASN C     O      doub N N 62  
ASN C     OXT    sing N N 63  
ASN CB    CG     sing N N 64  
ASN CB    HB2    sing N N 65  
ASN CB    HB3    sing N N 66  
ASN CG    OD1    doub N N 67  
ASN CG    ND2    sing N N 68  
ASN ND2   HD21   sing N N 69  
ASN ND2   HD22   sing N N 70  
ASN OXT   HXT    sing N N 71  
ASP N     CA     sing N N 72  
ASP N     H      sing N N 73  
ASP N     H2     sing N N 74  
ASP CA    C      sing N N 75  
ASP CA    CB     sing N N 76  
ASP CA    HA     sing N N 77  
ASP C     O      doub N N 78  
ASP C     OXT    sing N N 79  
ASP CB    CG     sing N N 80  
ASP CB    HB2    sing N N 81  
ASP CB    HB3    sing N N 82  
ASP CG    OD1    doub N N 83  
ASP CG    OD2    sing N N 84  
ASP OD2   HD2    sing N N 85  
ASP OXT   HXT    sing N N 86  
CYS N     CA     sing N N 87  
CYS N     H      sing N N 88  
CYS N     H2     sing N N 89  
CYS CA    C      sing N N 90  
CYS CA    CB     sing N N 91  
CYS CA    HA     sing N N 92  
CYS C     O      doub N N 93  
CYS C     OXT    sing N N 94  
CYS CB    SG     sing N N 95  
CYS CB    HB2    sing N N 96  
CYS CB    HB3    sing N N 97  
CYS SG    HG     sing N N 98  
CYS OXT   HXT    sing N N 99  
GLN N     CA     sing N N 100 
GLN N     H      sing N N 101 
GLN N     H2     sing N N 102 
GLN CA    C      sing N N 103 
GLN CA    CB     sing N N 104 
GLN CA    HA     sing N N 105 
GLN C     O      doub N N 106 
GLN C     OXT    sing N N 107 
GLN CB    CG     sing N N 108 
GLN CB    HB2    sing N N 109 
GLN CB    HB3    sing N N 110 
GLN CG    CD     sing N N 111 
GLN CG    HG2    sing N N 112 
GLN CG    HG3    sing N N 113 
GLN CD    OE1    doub N N 114 
GLN CD    NE2    sing N N 115 
GLN NE2   HE21   sing N N 116 
GLN NE2   HE22   sing N N 117 
GLN OXT   HXT    sing N N 118 
GLU N     CA     sing N N 119 
GLU N     H      sing N N 120 
GLU N     H2     sing N N 121 
GLU CA    C      sing N N 122 
GLU CA    CB     sing N N 123 
GLU CA    HA     sing N N 124 
GLU C     O      doub N N 125 
GLU C     OXT    sing N N 126 
GLU CB    CG     sing N N 127 
GLU CB    HB2    sing N N 128 
GLU CB    HB3    sing N N 129 
GLU CG    CD     sing N N 130 
GLU CG    HG2    sing N N 131 
GLU CG    HG3    sing N N 132 
GLU CD    OE1    doub N N 133 
GLU CD    OE2    sing N N 134 
GLU OE2   HE2    sing N N 135 
GLU OXT   HXT    sing N N 136 
GLY N     CA     sing N N 137 
GLY N     H      sing N N 138 
GLY N     H2     sing N N 139 
GLY CA    C      sing N N 140 
GLY CA    HA2    sing N N 141 
GLY CA    HA3    sing N N 142 
GLY C     O      doub N N 143 
GLY C     OXT    sing N N 144 
GLY OXT   HXT    sing N N 145 
HIS N     CA     sing N N 146 
HIS N     H      sing N N 147 
HIS N     H2     sing N N 148 
HIS CA    C      sing N N 149 
HIS CA    CB     sing N N 150 
HIS CA    HA     sing N N 151 
HIS C     O      doub N N 152 
HIS C     OXT    sing N N 153 
HIS CB    CG     sing N N 154 
HIS CB    HB2    sing N N 155 
HIS CB    HB3    sing N N 156 
HIS CG    ND1    sing Y N 157 
HIS CG    CD2    doub Y N 158 
HIS ND1   CE1    doub Y N 159 
HIS ND1   HD1    sing N N 160 
HIS CD2   NE2    sing Y N 161 
HIS CD2   HD2    sing N N 162 
HIS CE1   NE2    sing Y N 163 
HIS CE1   HE1    sing N N 164 
HIS NE2   HE2    sing N N 165 
HIS OXT   HXT    sing N N 166 
HOH O     H1     sing N N 167 
HOH O     H2     sing N N 168 
ILE N     CA     sing N N 169 
ILE N     H      sing N N 170 
ILE N     H2     sing N N 171 
ILE CA    C      sing N N 172 
ILE CA    CB     sing N N 173 
ILE CA    HA     sing N N 174 
ILE C     O      doub N N 175 
ILE C     OXT    sing N N 176 
ILE CB    CG1    sing N N 177 
ILE CB    CG2    sing N N 178 
ILE CB    HB     sing N N 179 
ILE CG1   CD1    sing N N 180 
ILE CG1   HG12   sing N N 181 
ILE CG1   HG13   sing N N 182 
ILE CG2   HG21   sing N N 183 
ILE CG2   HG22   sing N N 184 
ILE CG2   HG23   sing N N 185 
ILE CD1   HD11   sing N N 186 
ILE CD1   HD12   sing N N 187 
ILE CD1   HD13   sing N N 188 
ILE OXT   HXT    sing N N 189 
LEU N     CA     sing N N 190 
LEU N     H      sing N N 191 
LEU N     H2     sing N N 192 
LEU CA    C      sing N N 193 
LEU CA    CB     sing N N 194 
LEU CA    HA     sing N N 195 
LEU C     O      doub N N 196 
LEU C     OXT    sing N N 197 
LEU CB    CG     sing N N 198 
LEU CB    HB2    sing N N 199 
LEU CB    HB3    sing N N 200 
LEU CG    CD1    sing N N 201 
LEU CG    CD2    sing N N 202 
LEU CG    HG     sing N N 203 
LEU CD1   HD11   sing N N 204 
LEU CD1   HD12   sing N N 205 
LEU CD1   HD13   sing N N 206 
LEU CD2   HD21   sing N N 207 
LEU CD2   HD22   sing N N 208 
LEU CD2   HD23   sing N N 209 
LEU OXT   HXT    sing N N 210 
LYS N     CA     sing N N 211 
LYS N     H      sing N N 212 
LYS N     H2     sing N N 213 
LYS CA    C      sing N N 214 
LYS CA    CB     sing N N 215 
LYS CA    HA     sing N N 216 
LYS C     O      doub N N 217 
LYS C     OXT    sing N N 218 
LYS CB    CG     sing N N 219 
LYS CB    HB2    sing N N 220 
LYS CB    HB3    sing N N 221 
LYS CG    CD     sing N N 222 
LYS CG    HG2    sing N N 223 
LYS CG    HG3    sing N N 224 
LYS CD    CE     sing N N 225 
LYS CD    HD2    sing N N 226 
LYS CD    HD3    sing N N 227 
LYS CE    NZ     sing N N 228 
LYS CE    HE2    sing N N 229 
LYS CE    HE3    sing N N 230 
LYS NZ    HZ1    sing N N 231 
LYS NZ    HZ2    sing N N 232 
LYS NZ    HZ3    sing N N 233 
LYS OXT   HXT    sing N N 234 
MET N     CA     sing N N 235 
MET N     H      sing N N 236 
MET N     H2     sing N N 237 
MET CA    C      sing N N 238 
MET CA    CB     sing N N 239 
MET CA    HA     sing N N 240 
MET C     O      doub N N 241 
MET C     OXT    sing N N 242 
MET CB    CG     sing N N 243 
MET CB    HB2    sing N N 244 
MET CB    HB3    sing N N 245 
MET CG    SD     sing N N 246 
MET CG    HG2    sing N N 247 
MET CG    HG3    sing N N 248 
MET SD    CE     sing N N 249 
MET CE    HE1    sing N N 250 
MET CE    HE2    sing N N 251 
MET CE    HE3    sing N N 252 
MET OXT   HXT    sing N N 253 
PHE N     CA     sing N N 254 
PHE N     H      sing N N 255 
PHE N     H2     sing N N 256 
PHE CA    C      sing N N 257 
PHE CA    CB     sing N N 258 
PHE CA    HA     sing N N 259 
PHE C     O      doub N N 260 
PHE C     OXT    sing N N 261 
PHE CB    CG     sing N N 262 
PHE CB    HB2    sing N N 263 
PHE CB    HB3    sing N N 264 
PHE CG    CD1    doub Y N 265 
PHE CG    CD2    sing Y N 266 
PHE CD1   CE1    sing Y N 267 
PHE CD1   HD1    sing N N 268 
PHE CD2   CE2    doub Y N 269 
PHE CD2   HD2    sing N N 270 
PHE CE1   CZ     doub Y N 271 
PHE CE1   HE1    sing N N 272 
PHE CE2   CZ     sing Y N 273 
PHE CE2   HE2    sing N N 274 
PHE CZ    HZ     sing N N 275 
PHE OXT   HXT    sing N N 276 
PRO N     CA     sing N N 277 
PRO N     CD     sing N N 278 
PRO N     H      sing N N 279 
PRO CA    C      sing N N 280 
PRO CA    CB     sing N N 281 
PRO CA    HA     sing N N 282 
PRO C     O      doub N N 283 
PRO C     OXT    sing N N 284 
PRO CB    CG     sing N N 285 
PRO CB    HB2    sing N N 286 
PRO CB    HB3    sing N N 287 
PRO CG    CD     sing N N 288 
PRO CG    HG2    sing N N 289 
PRO CG    HG3    sing N N 290 
PRO CD    HD2    sing N N 291 
PRO CD    HD3    sing N N 292 
PRO OXT   HXT    sing N N 293 
SAM N     CA     sing N N 294 
SAM N     HN1    sing N N 295 
SAM N     HN2    sing N N 296 
SAM CA    C      sing N N 297 
SAM CA    CB     sing N N 298 
SAM CA    HA     sing N N 299 
SAM C     O      doub N N 300 
SAM C     OXT    sing N N 301 
SAM CB    CG     sing N N 302 
SAM CB    HB1    sing N N 303 
SAM CB    HB2    sing N N 304 
SAM CG    SD     sing N N 305 
SAM CG    HG1    sing N N 306 
SAM CG    HG2    sing N N 307 
SAM SD    CE     sing N N 308 
SAM SD    "C5'"  sing N N 309 
SAM CE    HE1    sing N N 310 
SAM CE    HE2    sing N N 311 
SAM CE    HE3    sing N N 312 
SAM "C5'" "C4'"  sing N N 313 
SAM "C5'" "H5'1" sing N N 314 
SAM "C5'" "H5'2" sing N N 315 
SAM "C4'" "O4'"  sing N N 316 
SAM "C4'" "C3'"  sing N N 317 
SAM "C4'" "H4'"  sing N N 318 
SAM "O4'" "C1'"  sing N N 319 
SAM "C3'" "O3'"  sing N N 320 
SAM "C3'" "C2'"  sing N N 321 
SAM "C3'" "H3'"  sing N N 322 
SAM "O3'" "HO3'" sing N N 323 
SAM "C2'" "O2'"  sing N N 324 
SAM "C2'" "C1'"  sing N N 325 
SAM "C2'" "H2'"  sing N N 326 
SAM "O2'" "HO2'" sing N N 327 
SAM "C1'" N9     sing N N 328 
SAM "C1'" "H1'"  sing N N 329 
SAM N9    C8     sing Y N 330 
SAM N9    C4     sing Y N 331 
SAM C8    N7     doub Y N 332 
SAM C8    H8     sing N N 333 
SAM N7    C5     sing Y N 334 
SAM C5    C6     sing Y N 335 
SAM C5    C4     doub Y N 336 
SAM C6    N6     sing N N 337 
SAM C6    N1     doub Y N 338 
SAM N6    HN61   sing N N 339 
SAM N6    HN62   sing N N 340 
SAM N1    C2     sing Y N 341 
SAM C2    N3     doub Y N 342 
SAM C2    H2     sing N N 343 
SAM N3    C4     sing Y N 344 
SER N     CA     sing N N 345 
SER N     H      sing N N 346 
SER N     H2     sing N N 347 
SER CA    C      sing N N 348 
SER CA    CB     sing N N 349 
SER CA    HA     sing N N 350 
SER C     O      doub N N 351 
SER C     OXT    sing N N 352 
SER CB    OG     sing N N 353 
SER CB    HB2    sing N N 354 
SER CB    HB3    sing N N 355 
SER OG    HG     sing N N 356 
SER OXT   HXT    sing N N 357 
THR N     CA     sing N N 358 
THR N     H      sing N N 359 
THR N     H2     sing N N 360 
THR CA    C      sing N N 361 
THR CA    CB     sing N N 362 
THR CA    HA     sing N N 363 
THR C     O      doub N N 364 
THR C     OXT    sing N N 365 
THR CB    OG1    sing N N 366 
THR CB    CG2    sing N N 367 
THR CB    HB     sing N N 368 
THR OG1   HG1    sing N N 369 
THR CG2   HG21   sing N N 370 
THR CG2   HG22   sing N N 371 
THR CG2   HG23   sing N N 372 
THR OXT   HXT    sing N N 373 
TRP N     CA     sing N N 374 
TRP N     H      sing N N 375 
TRP N     H2     sing N N 376 
TRP CA    C      sing N N 377 
TRP CA    CB     sing N N 378 
TRP CA    HA     sing N N 379 
TRP C     O      doub N N 380 
TRP C     OXT    sing N N 381 
TRP CB    CG     sing N N 382 
TRP CB    HB2    sing N N 383 
TRP CB    HB3    sing N N 384 
TRP CG    CD1    doub Y N 385 
TRP CG    CD2    sing Y N 386 
TRP CD1   NE1    sing Y N 387 
TRP CD1   HD1    sing N N 388 
TRP CD2   CE2    doub Y N 389 
TRP CD2   CE3    sing Y N 390 
TRP NE1   CE2    sing Y N 391 
TRP NE1   HE1    sing N N 392 
TRP CE2   CZ2    sing Y N 393 
TRP CE3   CZ3    doub Y N 394 
TRP CE3   HE3    sing N N 395 
TRP CZ2   CH2    doub Y N 396 
TRP CZ2   HZ2    sing N N 397 
TRP CZ3   CH2    sing Y N 398 
TRP CZ3   HZ3    sing N N 399 
TRP CH2   HH2    sing N N 400 
TRP OXT   HXT    sing N N 401 
TYR N     CA     sing N N 402 
TYR N     H      sing N N 403 
TYR N     H2     sing N N 404 
TYR CA    C      sing N N 405 
TYR CA    CB     sing N N 406 
TYR CA    HA     sing N N 407 
TYR C     O      doub N N 408 
TYR C     OXT    sing N N 409 
TYR CB    CG     sing N N 410 
TYR CB    HB2    sing N N 411 
TYR CB    HB3    sing N N 412 
TYR CG    CD1    doub Y N 413 
TYR CG    CD2    sing Y N 414 
TYR CD1   CE1    sing Y N 415 
TYR CD1   HD1    sing N N 416 
TYR CD2   CE2    doub Y N 417 
TYR CD2   HD2    sing N N 418 
TYR CE1   CZ     doub Y N 419 
TYR CE1   HE1    sing N N 420 
TYR CE2   CZ     sing Y N 421 
TYR CE2   HE2    sing N N 422 
TYR CZ    OH     sing N N 423 
TYR OH    HH     sing N N 424 
TYR OXT   HXT    sing N N 425 
VAL N     CA     sing N N 426 
VAL N     H      sing N N 427 
VAL N     H2     sing N N 428 
VAL CA    C      sing N N 429 
VAL CA    CB     sing N N 430 
VAL CA    HA     sing N N 431 
VAL C     O      doub N N 432 
VAL C     OXT    sing N N 433 
VAL CB    CG1    sing N N 434 
VAL CB    CG2    sing N N 435 
VAL CB    HB     sing N N 436 
VAL CG1   HG11   sing N N 437 
VAL CG1   HG12   sing N N 438 
VAL CG1   HG13   sing N N 439 
VAL CG2   HG21   sing N N 440 
VAL CG2   HG22   sing N N 441 
VAL CG2   HG23   sing N N 442 
VAL OXT   HXT    sing N N 443 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           '22193073 and 92253305' 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8ZSA 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009850 
_atom_sites.fract_transf_matrix[1][2]   0.005687 
_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]   0.011374 
_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]   0.003060 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N     . GLU A 1 42  ? -5.339  38.004  18.392  1.00 50.53  ? 14  GLU A N     1 
ATOM   2    C CA    . GLU A 1 42  ? -3.951  38.238  18.769  1.00 52.83  ? 14  GLU A CA    1 
ATOM   3    C C     . GLU A 1 42  ? -3.872  38.998  20.092  1.00 58.04  ? 14  GLU A C     1 
ATOM   4    O O     . GLU A 1 42  ? -4.900  39.364  20.663  1.00 60.32  ? 14  GLU A O     1 
ATOM   5    C CB    . GLU A 1 42  ? -3.218  39.009  17.667  1.00 59.14  ? 14  GLU A CB    1 
ATOM   6    C CG    . GLU A 1 42  ? -1.710  38.825  17.681  1.00 57.62  ? 14  GLU A CG    1 
ATOM   7    C CD    . GLU A 1 42  ? -0.963  40.015  17.120  1.00 55.90  ? 14  GLU A CD    1 
ATOM   8    O OE1   . GLU A 1 42  ? -1.501  40.690  16.217  1.00 57.99  ? 14  GLU A OE1   1 
ATOM   9    O OE2   . GLU A 1 42  ? 0.163   40.279  17.592  1.00 52.10  ? 14  GLU A OE2   1 
ATOM   10   N N     . ALA A 1 43  ? -2.644  39.227  20.567  1.00 63.73  ? 15  ALA A N     1 
ATOM   11   C CA    . ALA A 1 43  ? -2.379  39.920  21.823  1.00 64.70  ? 15  ALA A CA    1 
ATOM   12   C C     . ALA A 1 43  ? -3.102  39.242  22.976  1.00 63.33  ? 15  ALA A C     1 
ATOM   13   O O     . ALA A 1 43  ? -2.750  38.123  23.364  1.00 63.08  ? 15  ALA A O     1 
ATOM   14   C CB    . ALA A 1 43  ? -2.780  41.394  21.728  1.00 62.95  ? 15  ALA A CB    1 
ATOM   15   N N     . TYR A 1 44  ? -4.112  39.906  23.530  1.00 58.33  ? 16  TYR A N     1 
ATOM   16   C CA    . TYR A 1 44  ? -4.907  39.312  24.599  1.00 64.71  ? 16  TYR A CA    1 
ATOM   17   C C     . TYR A 1 44  ? -5.721  38.166  24.012  1.00 67.18  ? 16  TYR A C     1 
ATOM   18   O O     . TYR A 1 44  ? -6.689  38.395  23.279  1.00 68.18  ? 16  TYR A O     1 
ATOM   19   C CB    . TYR A 1 44  ? -5.805  40.360  25.252  1.00 62.78  ? 16  TYR A CB    1 
ATOM   20   C CG    . TYR A 1 44  ? -5.073  41.580  25.783  1.00 63.33  ? 16  TYR A CG    1 
ATOM   21   C CD1   . TYR A 1 44  ? -3.691  41.584  25.935  1.00 58.59  ? 16  TYR A CD1   1 
ATOM   22   C CD2   . TYR A 1 44  ? -5.772  42.724  26.143  1.00 68.30  ? 16  TYR A CD2   1 
ATOM   23   C CE1   . TYR A 1 44  ? -3.028  42.696  26.415  1.00 62.26  ? 16  TYR A CE1   1 
ATOM   24   C CE2   . TYR A 1 44  ? -5.118  43.839  26.625  1.00 69.99  ? 16  TYR A CE2   1 
ATOM   25   C CZ    . TYR A 1 44  ? -3.748  43.820  26.761  1.00 70.65  ? 16  TYR A CZ    1 
ATOM   26   O OH    . TYR A 1 44  ? -3.095  44.931  27.244  1.00 71.50  ? 16  TYR A OH    1 
ATOM   27   N N     . ARG A 1 45  ? -5.313  36.933  24.325  1.00 57.81  ? 17  ARG A N     1 
ATOM   28   C CA    . ARG A 1 45  ? -5.818  35.732  23.667  1.00 52.30  ? 17  ARG A CA    1 
ATOM   29   C C     . ARG A 1 45  ? -5.569  35.816  22.166  1.00 55.93  ? 17  ARG A C     1 
ATOM   30   O O     . ARG A 1 45  ? -4.728  36.601  21.715  1.00 60.42  ? 17  ARG A O     1 
ATOM   31   C CB    . ARG A 1 45  ? -7.306  35.519  23.965  1.00 56.02  ? 17  ARG A CB    1 
ATOM   32   C CG    . ARG A 1 45  ? -7.611  35.183  25.421  1.00 64.35  ? 17  ARG A CG    1 
ATOM   33   C CD    . ARG A 1 45  ? -6.487  34.373  26.057  1.00 58.02  ? 17  ARG A CD    1 
ATOM   34   N NE    . ARG A 1 45  ? -6.883  33.796  27.336  1.00 53.01  ? 17  ARG A NE    1 
ATOM   35   C CZ    . ARG A 1 45  ? -6.117  32.998  28.067  1.00 56.92  ? 17  ARG A CZ    1 
ATOM   36   N NH1   . ARG A 1 45  ? -4.909  32.639  27.664  1.00 57.11  ? 17  ARG A NH1   1 
ATOM   37   N NH2   . ARG A 1 45  ? -6.577  32.543  29.229  1.00 58.11  ? 17  ARG A NH2   1 
ATOM   38   N N     . GLY A 1 46  ? -6.280  35.012  21.384  1.00 55.01  ? 18  GLY A N     1 
ATOM   39   C CA    . GLY A 1 46  ? -6.077  35.015  19.950  1.00 44.88  ? 18  GLY A CA    1 
ATOM   40   C C     . GLY A 1 46  ? -7.280  35.510  19.179  1.00 41.17  ? 18  GLY A C     1 
ATOM   41   O O     . GLY A 1 46  ? -7.713  36.654  19.349  1.00 48.23  ? 18  GLY A O     1 
ATOM   42   N N     . ILE A 1 47  ? -7.826  34.654  18.325  1.00 38.93  ? 19  ILE A N     1 
ATOM   43   C CA    . ILE A 1 47  ? -9.009  34.970  17.535  1.00 41.01  ? 19  ILE A CA    1 
ATOM   44   C C     . ILE A 1 47  ? -10.213 34.415  18.284  1.00 42.44  ? 19  ILE A C     1 
ATOM   45   O O     . ILE A 1 47  ? -10.512 33.220  18.209  1.00 43.64  ? 19  ILE A O     1 
ATOM   46   C CB    . ILE A 1 47  ? -8.914  34.406  16.115  1.00 38.51  ? 19  ILE A CB    1 
ATOM   47   C CG1   . ILE A 1 47  ? -7.581  34.798  15.473  1.00 43.12  ? 19  ILE A CG1   1 
ATOM   48   C CG2   . ILE A 1 47  ? -10.090 34.874  15.273  1.00 39.05  ? 19  ILE A CG2   1 
ATOM   49   C CD1   . ILE A 1 47  ? -7.404  36.292  15.304  1.00 48.97  ? 19  ILE A CD1   1 
ATOM   50   N N     . ASP A 1 48  ? -10.905 35.282  19.017  1.00 46.58  ? 20  ASP A N     1 
ATOM   51   C CA    . ASP A 1 48  ? -12.182 34.903  19.597  1.00 44.76  ? 20  ASP A CA    1 
ATOM   52   C C     . ASP A 1 48  ? -13.239 34.830  18.496  1.00 50.74  ? 20  ASP A C     1 
ATOM   53   O O     . ASP A 1 48  ? -12.968 35.077  17.316  1.00 53.42  ? 20  ASP A O     1 
ATOM   54   C CB    . ASP A 1 48  ? -12.583 35.883  20.697  1.00 46.25  ? 20  ASP A CB    1 
ATOM   55   C CG    . ASP A 1 48  ? -12.325 37.327  20.317  1.00 52.61  ? 20  ASP A CG    1 
ATOM   56   O OD1   . ASP A 1 48  ? -12.126 37.605  19.116  1.00 56.19  ? 20  ASP A OD1   1 
ATOM   57   O OD2   . ASP A 1 48  ? -12.321 38.187  21.223  1.00 59.58  ? 20  ASP A OD2   1 
ATOM   58   N N     . LYS A 1 49  ? -14.465 34.492  18.894  1.00 50.40  ? 21  LYS A N     1 
ATOM   59   C CA    . LYS A 1 49  ? -15.564 34.254  17.964  1.00 55.46  ? 21  LYS A CA    1 
ATOM   60   C C     . LYS A 1 49  ? -15.160 33.201  16.938  1.00 48.44  ? 21  LYS A C     1 
ATOM   61   O O     . LYS A 1 49  ? -14.961 33.525  15.759  1.00 41.60  ? 21  LYS A O     1 
ATOM   62   C CB    . LYS A 1 49  ? -15.986 35.552  17.268  1.00 50.27  ? 21  LYS A CB    1 
ATOM   63   N N     . PRO A 1 50  ? -15.016 31.935  17.344  1.00 44.40  ? 22  PRO A N     1 
ATOM   64   C CA    . PRO A 1 50  ? -14.630 30.897  16.376  1.00 38.67  ? 22  PRO A CA    1 
ATOM   65   C C     . PRO A 1 50  ? -15.721 30.572  15.376  1.00 40.55  ? 22  PRO A C     1 
ATOM   66   O O     . PRO A 1 50  ? -15.418 29.990  14.327  1.00 39.00  ? 22  PRO A O     1 
ATOM   67   C CB    . PRO A 1 50  ? -14.317 29.688  17.266  1.00 38.02  ? 22  PRO A CB    1 
ATOM   68   C CG    . PRO A 1 50  ? -15.149 29.909  18.483  1.00 47.11  ? 22  PRO A CG    1 
ATOM   69   C CD    . PRO A 1 50  ? -15.157 31.393  18.707  1.00 48.72  ? 22  PRO A CD    1 
ATOM   70   N N     . HIS A 1 51  ? -16.976 30.921  15.669  1.00 46.59  ? 23  HIS A N     1 
ATOM   71   C CA    . HIS A 1 51  ? -18.060 30.657  14.730  1.00 45.54  ? 23  HIS A CA    1 
ATOM   72   C C     . HIS A 1 51  ? -17.836 31.386  13.413  1.00 45.15  ? 23  HIS A C     1 
ATOM   73   O O     . HIS A 1 51  ? -18.037 30.815  12.335  1.00 46.70  ? 23  HIS A O     1 
ATOM   74   C CB    . HIS A 1 51  ? -19.398 31.067  15.348  1.00 47.65  ? 23  HIS A CB    1 
ATOM   75   C CG    . HIS A 1 51  ? -20.072 29.971  16.113  1.00 54.17  ? 23  HIS A CG    1 
ATOM   76   N ND1   . HIS A 1 51  ? -19.453 29.290  17.140  1.00 55.28  ? 23  HIS A ND1   1 
ATOM   77   C CD2   . HIS A 1 51  ? -21.313 29.440  16.003  1.00 56.83  ? 23  HIS A CD2   1 
ATOM   78   C CE1   . HIS A 1 51  ? -20.283 28.386  17.628  1.00 55.86  ? 23  HIS A CE1   1 
ATOM   79   N NE2   . HIS A 1 51  ? -21.418 28.456  16.957  1.00 59.12  ? 23  HIS A NE2   1 
ATOM   80   N N     . LEU A 1 52  ? -17.410 32.649  13.480  1.00 45.13  ? 24  LEU A N     1 
ATOM   81   C CA    . LEU A 1 52  ? -17.183 33.425  12.268  1.00 40.91  ? 24  LEU A CA    1 
ATOM   82   C C     . LEU A 1 52  ? -15.979 32.932  11.477  1.00 39.83  ? 24  LEU A C     1 
ATOM   83   O O     . LEU A 1 52  ? -15.884 33.219  10.279  1.00 46.23  ? 24  LEU A O     1 
ATOM   84   C CB    . LEU A 1 52  ? -17.003 34.902  12.617  1.00 41.82  ? 24  LEU A CB    1 
ATOM   85   C CG    . LEU A 1 52  ? -18.229 35.604  13.203  1.00 43.11  ? 24  LEU A CG    1 
ATOM   86   C CD1   . LEU A 1 52  ? -17.939 37.076  13.455  1.00 49.86  ? 24  LEU A CD1   1 
ATOM   87   C CD2   . LEU A 1 52  ? -19.430 35.439  12.285  1.00 46.21  ? 24  LEU A CD2   1 
ATOM   88   N N     . TYR A 1 53  ? -15.063 32.196  12.110  1.00 38.96  ? 25  TYR A N     1 
ATOM   89   C CA    . TYR A 1 53  ? -13.857 31.772  11.409  1.00 38.03  ? 25  TYR A CA    1 
ATOM   90   C C     . TYR A 1 53  ? -14.077 30.512  10.581  1.00 39.47  ? 25  TYR A C     1 
ATOM   91   O O     . TYR A 1 53  ? -13.464 30.366  9.517   1.00 40.85  ? 25  TYR A O     1 
ATOM   92   C CB    . TYR A 1 53  ? -12.712 31.555  12.399  1.00 37.63  ? 25  TYR A CB    1 
ATOM   93   C CG    . TYR A 1 53  ? -11.361 31.470  11.727  1.00 37.52  ? 25  TYR A CG    1 
ATOM   94   C CD1   . TYR A 1 53  ? -10.619 32.615  11.471  1.00 39.04  ? 25  TYR A CD1   1 
ATOM   95   C CD2   . TYR A 1 53  ? -10.833 30.248  11.337  1.00 39.17  ? 25  TYR A CD2   1 
ATOM   96   C CE1   . TYR A 1 53  ? -9.387  32.543  10.851  1.00 39.90  ? 25  TYR A CE1   1 
ATOM   97   C CE2   . TYR A 1 53  ? -9.602  30.165  10.717  1.00 41.38  ? 25  TYR A CE2   1 
ATOM   98   C CZ    . TYR A 1 53  ? -8.883  31.315  10.477  1.00 39.90  ? 25  TYR A CZ    1 
ATOM   99   O OH    . TYR A 1 53  ? -7.658  31.237  9.858   1.00 40.35  ? 25  TYR A OH    1 
ATOM   100  N N     . THR A 1 54  ? -14.936 29.595  11.035  1.00 37.90  ? 26  THR A N     1 
ATOM   101  C CA    . THR A 1 54  ? -15.232 28.405  10.244  1.00 36.81  ? 26  THR A CA    1 
ATOM   102  C C     . THR A 1 54  ? -15.949 28.729  8.942   1.00 39.11  ? 26  THR A C     1 
ATOM   103  O O     . THR A 1 54  ? -16.121 27.832  8.111   1.00 50.11  ? 26  THR A O     1 
ATOM   104  C CB    . THR A 1 54  ? -16.069 27.412  11.051  1.00 36.83  ? 26  THR A CB    1 
ATOM   105  O OG1   . THR A 1 54  ? -17.146 28.100  11.701  1.00 41.43  ? 26  THR A OG1   1 
ATOM   106  C CG2   . THR A 1 54  ? -15.209 26.711  12.085  1.00 37.46  ? 26  THR A CG2   1 
ATOM   107  N N     . LEU A 1 55  ? -16.375 29.979  8.749   1.00 38.19  ? 27  LEU A N     1 
ATOM   108  C CA    . LEU A 1 55  ? -16.915 30.390  7.460   1.00 39.72  ? 27  LEU A CA    1 
ATOM   109  C C     . LEU A 1 55  ? -15.875 30.284  6.355   1.00 42.67  ? 27  LEU A C     1 
ATOM   110  O O     . LEU A 1 55  ? -16.240 30.165  5.180   1.00 49.71  ? 27  LEU A O     1 
ATOM   111  C CB    . LEU A 1 55  ? -17.443 31.820  7.554   1.00 40.03  ? 27  LEU A CB    1 
ATOM   112  C CG    . LEU A 1 55  ? -18.674 31.995  8.443   1.00 40.68  ? 27  LEU A CG    1 
ATOM   113  C CD1   . LEU A 1 55  ? -19.003 33.466  8.611   1.00 42.39  ? 27  LEU A CD1   1 
ATOM   114  C CD2   . LEU A 1 55  ? -19.861 31.233  7.878   1.00 41.02  ? 27  LEU A CD2   1 
ATOM   115  N N     . GLY A 1 56  ? -14.592 30.329  6.705   1.00 39.76  ? 28  GLY A N     1 
ATOM   116  C CA    . GLY A 1 56  ? -13.508 30.114  5.775   1.00 39.16  ? 28  GLY A CA    1 
ATOM   117  C C     . GLY A 1 56  ? -12.940 28.715  5.771   1.00 42.63  ? 28  GLY A C     1 
ATOM   118  O O     . GLY A 1 56  ? -11.973 28.460  5.047   1.00 44.12  ? 28  GLY A O     1 
ATOM   119  N N     . CYS A 1 57  ? -13.503 27.802  6.568   1.00 40.31  ? 29  CYS A N     1 
ATOM   120  C CA    . CYS A 1 57  ? -13.080 26.404  6.544   1.00 44.69  ? 29  CYS A CA    1 
ATOM   121  C C     . CYS A 1 57  ? -13.149 25.818  5.140   1.00 51.93  ? 29  CYS A C     1 
ATOM   122  O O     . CYS A 1 57  ? -12.141 25.356  4.596   1.00 50.70  ? 29  CYS A O     1 
ATOM   123  C CB    . CYS A 1 57  ? -13.937 25.581  7.506   1.00 54.35  ? 29  CYS A CB    1 
ATOM   124  S SG    . CYS A 1 57  ? -13.504 23.835  7.559   1.00 61.85  ? 29  CYS A SG    1 
ATOM   125  N N     . CYS A 1 58  ? -14.336 25.842  4.529   1.00 61.21  ? 30  CYS A N     1 
ATOM   126  C CA    . CYS A 1 58  ? -14.544 25.242  3.213   1.00 60.37  ? 30  CYS A CA    1 
ATOM   127  C C     . CYS A 1 58  ? -13.561 25.745  2.156   1.00 55.65  ? 30  CYS A C     1 
ATOM   128  O O     . CYS A 1 58  ? -13.448 25.143  1.085   1.00 55.54  ? 30  CYS A O     1 
ATOM   129  C CB    . CYS A 1 58  ? -15.986 25.472  2.742   1.00 66.56  ? 30  CYS A CB    1 
ATOM   130  S SG    . CYS A 1 58  ? -17.349 25.068  3.908   1.00 102.34 ? 30  CYS A SG    1 
ATOM   131  N N     . SER A 1 59  ? -12.841 26.830  2.441   1.00 60.21  ? 31  SER A N     1 
ATOM   132  C CA    . SER A 1 59  ? -11.802 27.344  1.556   1.00 48.70  ? 31  SER A CA    1 
ATOM   133  C C     . SER A 1 59  ? -10.400 27.162  2.118   1.00 37.21  ? 31  SER A C     1 
ATOM   134  O O     . SER A 1 59  ? -9.508  26.677  1.413   1.00 33.92  ? 31  SER A O     1 
ATOM   135  C CB    . SER A 1 59  ? -12.049 28.829  1.260   1.00 43.33  ? 31  SER A CB    1 
ATOM   136  O OG    . SER A 1 59  ? -13.217 29.006  0.478   1.00 44.80  ? 31  SER A OG    1 
ATOM   137  N N     . LEU A 1 60  ? -10.177 27.549  3.378   1.00 45.35  ? 32  LEU A N     1 
ATOM   138  C CA    . LEU A 1 60  ? -8.855  27.397  3.980   1.00 35.45  ? 32  LEU A CA    1 
ATOM   139  C C     . LEU A 1 60  ? -8.462  25.933  4.118   1.00 40.53  ? 32  LEU A C     1 
ATOM   140  O O     . LEU A 1 60  ? -7.267  25.613  4.131   1.00 35.37  ? 32  LEU A O     1 
ATOM   141  C CB    . LEU A 1 60  ? -8.812  28.083  5.346   1.00 35.90  ? 32  LEU A CB    1 
ATOM   142  C CG    . LEU A 1 60  ? -8.888  29.610  5.367   1.00 34.63  ? 32  LEU A CG    1 
ATOM   143  C CD1   . LEU A 1 60  ? -8.926  30.118  6.798   1.00 34.86  ? 32  LEU A CD1   1 
ATOM   144  C CD2   . LEU A 1 60  ? -7.714  30.216  4.614   1.00 34.60  ? 32  LEU A CD2   1 
ATOM   145  N N     . THR A 1 61  ? -9.442  25.034  4.235   1.00 42.21  ? 33  THR A N     1 
ATOM   146  C CA    . THR A 1 61  ? -9.137  23.608  4.272   1.00 41.76  ? 33  THR A CA    1 
ATOM   147  C C     . THR A 1 61  ? -8.472  23.166  2.976   1.00 42.85  ? 33  THR A C     1 
ATOM   148  O O     . THR A 1 61  ? -7.443  22.481  2.993   1.00 43.12  ? 33  THR A O     1 
ATOM   149  C CB    . THR A 1 61  ? -10.412 22.800  4.524   1.00 42.60  ? 33  THR A CB    1 
ATOM   150  O OG1   . THR A 1 61  ? -10.961 23.153  5.800   1.00 49.31  ? 33  THR A OG1   1 
ATOM   151  C CG2   . THR A 1 61  ? -10.120 21.309  4.498   1.00 44.33  ? 33  THR A CG2   1 
ATOM   152  N N     . ALA A 1 62  ? -9.043  23.565  1.836   1.00 43.91  ? 34  ALA A N     1 
ATOM   153  C CA    . ALA A 1 62  ? -8.478  23.180  0.548   1.00 40.67  ? 34  ALA A CA    1 
ATOM   154  C C     . ALA A 1 62  ? -7.118  23.825  0.307   1.00 42.73  ? 34  ALA A C     1 
ATOM   155  O O     . ALA A 1 62  ? -6.272  23.239  -0.378  1.00 44.95  ? 34  ALA A O     1 
ATOM   156  C CB    . ALA A 1 62  ? -9.444  23.546  -0.578  1.00 41.88  ? 34  ALA A CB    1 
ATOM   157  N N     . MET A 1 63  ? -6.888  25.020  0.856   1.00 40.77  ? 35  MET A N     1 
ATOM   158  C CA    . MET A 1 63  ? -5.624  25.711  0.619   1.00 38.20  ? 35  MET A CA    1 
ATOM   159  C C     . MET A 1 63  ? -4.460  24.979  1.275   1.00 41.65  ? 35  MET A C     1 
ATOM   160  O O     . MET A 1 63  ? -3.467  24.655  0.614   1.00 49.53  ? 35  MET A O     1 
ATOM   161  C CB    . MET A 1 63  ? -5.706  27.150  1.125   1.00 38.37  ? 35  MET A CB    1 
ATOM   162  C CG    . MET A 1 63  ? -4.400  27.912  0.990   1.00 41.28  ? 35  MET A CG    1 
ATOM   163  S SD    . MET A 1 63  ? -4.393  29.441  1.938   1.00 44.12  ? 35  MET A SD    1 
ATOM   164  C CE    . MET A 1 63  ? -5.916  30.181  1.361   1.00 45.44  ? 35  MET A CE    1 
ATOM   165  N N     . ALA A 1 64  ? -4.558  24.719  2.581   1.00 41.84  ? 36  ALA A N     1 
ATOM   166  C CA    . ALA A 1 64  ? -3.499  23.982  3.262   1.00 38.98  ? 36  ALA A CA    1 
ATOM   167  C C     . ALA A 1 64  ? -3.428  22.539  2.784   1.00 42.12  ? 36  ALA A C     1 
ATOM   168  O O     . ALA A 1 64  ? -2.349  21.936  2.799   1.00 43.41  ? 36  ALA A O     1 
ATOM   169  C CB    . ALA A 1 64  ? -3.710  24.024  4.774   1.00 43.46  ? 36  ALA A CB    1 
ATOM   170  N N     . SER A 1 65  ? -4.561  21.970  2.366   1.00 45.26  ? 37  SER A N     1 
ATOM   171  C CA    . SER A 1 65  ? -4.543  20.624  1.811   1.00 47.29  ? 37  SER A CA    1 
ATOM   172  C C     . SER A 1 65  ? -3.752  20.582  0.511   1.00 49.45  ? 37  SER A C     1 
ATOM   173  O O     . SER A 1 65  ? -3.229  19.528  0.132   1.00 54.74  ? 37  SER A O     1 
ATOM   174  C CB    . SER A 1 65  ? -5.971  20.126  1.588   1.00 47.09  ? 37  SER A CB    1 
ATOM   175  O OG    . SER A 1 65  ? -5.999  18.763  1.201   1.00 51.11  ? 37  SER A OG    1 
ATOM   176  N N     . ALA A 1 66  ? -3.640  21.717  -0.180  1.00 48.15  ? 38  ALA A N     1 
ATOM   177  C CA    . ALA A 1 66  ? -2.834  21.759  -1.392  1.00 45.55  ? 38  ALA A CA    1 
ATOM   178  C C     . ALA A 1 66  ? -1.370  22.028  -1.069  1.00 45.92  ? 38  ALA A C     1 
ATOM   179  O O     . ALA A 1 66  ? -0.479  21.488  -1.733  1.00 51.25  ? 38  ALA A O     1 
ATOM   180  C CB    . ALA A 1 66  ? -3.387  22.812  -2.350  1.00 44.82  ? 38  ALA A CB    1 
ATOM   181  N N     . GLN A 1 67  ? -1.105  22.847  -0.047  1.00 44.13  ? 39  GLN A N     1 
ATOM   182  C CA    . GLN A 1 67  ? 0.273   23.094  0.370   1.00 45.02  ? 39  GLN A CA    1 
ATOM   183  C C     . GLN A 1 67  ? 0.923   21.819  0.890   1.00 46.95  ? 39  GLN A C     1 
ATOM   184  O O     . GLN A 1 67  ? 2.061   21.495  0.531   1.00 50.43  ? 39  GLN A O     1 
ATOM   185  C CB    . GLN A 1 67  ? 0.314   24.182  1.443   1.00 46.49  ? 39  GLN A CB    1 
ATOM   186  C CG    . GLN A 1 67  ? 0.096   25.594  0.937   1.00 51.57  ? 39  GLN A CG    1 
ATOM   187  C CD    . GLN A 1 67  ? -0.015  26.598  2.069   1.00 49.67  ? 39  GLN A CD    1 
ATOM   188  O OE1   . GLN A 1 67  ? 0.268   27.783  1.896   1.00 52.20  ? 39  GLN A OE1   1 
ATOM   189  N NE2   . GLN A 1 67  ? -0.421  26.123  3.241   1.00 45.82  ? 39  GLN A NE2   1 
ATOM   190  N N     . LEU A 1 68  ? 0.211   21.080  1.745   1.00 47.94  ? 40  LEU A N     1 
ATOM   191  C CA    . LEU A 1 68  ? 0.785   19.883  2.348   1.00 50.18  ? 40  LEU A CA    1 
ATOM   192  C C     . LEU A 1 68  ? 1.028   18.788  1.317   1.00 57.75  ? 40  LEU A C     1 
ATOM   193  O O     . LEU A 1 68  ? 1.969   18.001  1.464   1.00 59.48  ? 40  LEU A O     1 
ATOM   194  C CB    . LEU A 1 68  ? -0.126  19.374  3.464   1.00 45.44  ? 40  LEU A CB    1 
ATOM   195  C CG    . LEU A 1 68  ? -0.096  20.198  4.752   1.00 40.48  ? 40  LEU A CG    1 
ATOM   196  C CD1   . LEU A 1 68  ? -1.070  19.637  5.772   1.00 40.60  ? 40  LEU A CD1   1 
ATOM   197  C CD2   . LEU A 1 68  ? 1.312   20.256  5.324   1.00 41.00  ? 40  LEU A CD2   1 
ATOM   198  N N     . ASP A 1 69  ? 0.198   18.722  0.272   1.00 54.06  ? 41  ASP A N     1 
ATOM   199  C CA    . ASP A 1 69  ? 0.396   17.711  -0.761  1.00 55.50  ? 41  ASP A CA    1 
ATOM   200  C C     . ASP A 1 69  ? 1.699   17.928  -1.520  1.00 57.31  ? 41  ASP A C     1 
ATOM   201  O O     . ASP A 1 69  ? 2.289   16.965  -2.022  1.00 60.33  ? 41  ASP A O     1 
ATOM   202  C CB    . ASP A 1 69  ? -0.786  17.706  -1.730  1.00 59.74  ? 41  ASP A CB    1 
ATOM   203  C CG    . ASP A 1 69  ? -2.022  17.057  -1.138  1.00 64.37  ? 41  ASP A CG    1 
ATOM   204  O OD1   . ASP A 1 69  ? -1.899  16.383  -0.093  1.00 63.44  ? 41  ASP A OD1   1 
ATOM   205  O OD2   . ASP A 1 69  ? -3.117  17.219  -1.718  1.00 63.54  ? 41  ASP A OD2   1 
ATOM   206  N N     . ALA A 1 70  ? 2.164   19.175  -1.612  1.00 53.96  ? 42  ALA A N     1 
ATOM   207  C CA    . ALA A 1 70  ? 3.422   19.450  -2.295  1.00 52.32  ? 42  ALA A CA    1 
ATOM   208  C C     . ALA A 1 70  ? 4.629   19.059  -1.452  1.00 56.49  ? 42  ALA A C     1 
ATOM   209  O O     . ALA A 1 70  ? 5.702   18.788  -2.003  1.00 61.81  ? 42  ALA A O     1 
ATOM   210  C CB    . ALA A 1 70  ? 3.505   20.931  -2.671  1.00 49.38  ? 42  ALA A CB    1 
ATOM   211  N N     . LEU A 1 71  ? 4.477   19.018  -0.128  1.00 57.31  ? 43  LEU A N     1 
ATOM   212  C CA    . LEU A 1 71  ? 5.580   18.713  0.771   1.00 49.97  ? 43  LEU A CA    1 
ATOM   213  C C     . LEU A 1 71  ? 5.503   17.324  1.384   1.00 49.65  ? 43  LEU A C     1 
ATOM   214  O O     . LEU A 1 71  ? 6.498   16.870  1.961   1.00 52.99  ? 43  LEU A O     1 
ATOM   215  C CB    . LEU A 1 71  ? 5.641   19.744  1.908   1.00 47.31  ? 43  LEU A CB    1 
ATOM   216  C CG    . LEU A 1 71  ? 5.844   21.208  1.528   1.00 52.10  ? 43  LEU A CG    1 
ATOM   217  C CD1   . LEU A 1 71  ? 5.874   22.073  2.778   1.00 46.29  ? 43  LEU A CD1   1 
ATOM   218  C CD2   . LEU A 1 71  ? 7.114   21.377  0.719   1.00 56.67  ? 43  LEU A CD2   1 
ATOM   219  N N     . TRP A 1 72  ? 4.362   16.638  1.275   1.00 52.02  ? 44  TRP A N     1 
ATOM   220  C CA    . TRP A 1 72  ? 4.162   15.418  2.051   1.00 50.32  ? 44  TRP A CA    1 
ATOM   221  C C     . TRP A 1 72  ? 5.120   14.310  1.634   1.00 54.29  ? 44  TRP A C     1 
ATOM   222  O O     . TRP A 1 72  ? 5.466   13.453  2.455   1.00 53.58  ? 44  TRP A O     1 
ATOM   223  C CB    . TRP A 1 72  ? 2.716   14.941  1.925   1.00 47.29  ? 44  TRP A CB    1 
ATOM   224  C CG    . TRP A 1 72  ? 2.265   14.199  3.132   1.00 44.07  ? 44  TRP A CG    1 
ATOM   225  C CD1   . TRP A 1 72  ? 2.230   12.847  3.302   1.00 43.74  ? 44  TRP A CD1   1 
ATOM   226  C CD2   . TRP A 1 72  ? 1.804   14.772  4.359   1.00 44.92  ? 44  TRP A CD2   1 
ATOM   227  N NE1   . TRP A 1 72  ? 1.766   12.542  4.560   1.00 43.85  ? 44  TRP A NE1   1 
ATOM   228  C CE2   . TRP A 1 72  ? 1.497   13.708  5.228   1.00 47.54  ? 44  TRP A CE2   1 
ATOM   229  C CE3   . TRP A 1 72  ? 1.615   16.084  4.805   1.00 44.86  ? 44  TRP A CE3   1 
ATOM   230  C CZ2   . TRP A 1 72  ? 1.015   13.915  6.518   1.00 50.73  ? 44  TRP A CZ2   1 
ATOM   231  C CZ3   . TRP A 1 72  ? 1.135   16.287  6.084   1.00 46.41  ? 44  TRP A CZ3   1 
ATOM   232  C CH2   . TRP A 1 72  ? 0.839   15.209  6.926   1.00 48.20  ? 44  TRP A CH2   1 
ATOM   233  N N     . SER A 1 73  ? 5.558   14.306  0.373   1.00 55.60  ? 45  SER A N     1 
ATOM   234  C CA    . SER A 1 73  ? 6.526   13.306  -0.061  1.00 55.37  ? 45  SER A CA    1 
ATOM   235  C C     . SER A 1 73  ? 7.886   13.524  0.588   1.00 56.04  ? 45  SER A C     1 
ATOM   236  O O     . SER A 1 73  ? 8.623   12.558  0.818   1.00 58.61  ? 45  SER A O     1 
ATOM   237  C CB    . SER A 1 73  ? 6.656   13.327  -1.584  1.00 54.58  ? 45  SER A CB    1 
ATOM   238  O OG    . SER A 1 73  ? 7.143   14.579  -2.035  1.00 61.75  ? 45  SER A OG    1 
ATOM   239  N N     . GLN A 1 74  ? 8.232   14.773  0.896   1.00 52.61  ? 46  GLN A N     1 
ATOM   240  C CA    . GLN A 1 74  ? 9.516   15.099  1.503   1.00 50.48  ? 46  GLN A CA    1 
ATOM   241  C C     . GLN A 1 74  ? 9.541   14.877  3.010   1.00 50.40  ? 46  GLN A C     1 
ATOM   242  O O     . GLN A 1 74  ? 10.569  15.148  3.640   1.00 50.29  ? 46  GLN A O     1 
ATOM   243  C CB    . GLN A 1 74  ? 9.885   16.554  1.201   1.00 51.22  ? 46  GLN A CB    1 
ATOM   244  C CG    . GLN A 1 74  ? 10.050  16.867  -0.275  1.00 57.80  ? 46  GLN A CG    1 
ATOM   245  C CD    . GLN A 1 74  ? 10.277  18.345  -0.528  1.00 62.20  ? 46  GLN A CD    1 
ATOM   246  O OE1   . GLN A 1 74  ? 9.547   18.975  -1.293  1.00 60.91  ? 46  GLN A OE1   1 
ATOM   247  N NE2   . GLN A 1 74  ? 11.293  18.906  0.118   1.00 60.54  ? 46  GLN A NE2   1 
ATOM   248  N N     . LEU A 1 75  ? 8.450   14.401  3.601   1.00 44.48  ? 47  LEU A N     1 
ATOM   249  C CA    . LEU A 1 75  ? 8.376   14.199  5.042   1.00 49.85  ? 47  LEU A CA    1 
ATOM   250  C C     . LEU A 1 75  ? 8.746   12.758  5.372   1.00 47.01  ? 47  LEU A C     1 
ATOM   251  O O     . LEU A 1 75  ? 8.146   11.819  4.837   1.00 46.31  ? 47  LEU A O     1 
ATOM   252  C CB    . LEU A 1 75  ? 6.978   14.530  5.563   1.00 44.73  ? 47  LEU A CB    1 
ATOM   253  C CG    . LEU A 1 75  ? 6.533   15.990  5.454   1.00 36.92  ? 47  LEU A CG    1 
ATOM   254  C CD1   . LEU A 1 75  ? 5.040   16.116  5.706   1.00 40.03  ? 47  LEU A CD1   1 
ATOM   255  C CD2   . LEU A 1 75  ? 7.313   16.870  6.415   1.00 36.60  ? 47  LEU A CD2   1 
ATOM   256  N N     . SER A 1 76  ? 9.732   12.588  6.246   1.00 45.39  ? 48  SER A N     1 
ATOM   257  C CA    . SER A 1 76  ? 10.156  11.278  6.712   1.00 44.21  ? 48  SER A CA    1 
ATOM   258  C C     . SER A 1 76  ? 9.588   11.012  8.101   1.00 42.60  ? 48  SER A C     1 
ATOM   259  O O     . SER A 1 76  ? 9.463   11.921  8.924   1.00 41.90  ? 48  SER A O     1 
ATOM   260  C CB    . SER A 1 76  ? 11.682  11.176  6.732   1.00 52.75  ? 48  SER A CB    1 
ATOM   261  O OG    . SER A 1 76  ? 12.244  12.093  7.655   1.00 63.74  ? 48  SER A OG    1 
ATOM   262  N N     . TRP A 1 77  ? 9.248   9.752   8.357   1.00 45.56  ? 49  TRP A N     1 
ATOM   263  C CA    . TRP A 1 77  ? 8.518   9.381   9.557   1.00 43.46  ? 49  TRP A CA    1 
ATOM   264  C C     . TRP A 1 77  ? 9.206   8.232   10.277  1.00 40.84  ? 49  TRP A C     1 
ATOM   265  O O     . TRP A 1 77  ? 9.804   7.360   9.638   1.00 46.08  ? 49  TRP A O     1 
ATOM   266  C CB    . TRP A 1 77  ? 7.078   8.976   9.209   1.00 42.30  ? 49  TRP A CB    1 
ATOM   267  C CG    . TRP A 1 77  ? 6.302   10.073  8.558   1.00 39.80  ? 49  TRP A CG    1 
ATOM   268  C CD1   . TRP A 1 77  ? 6.192   10.315  7.220   1.00 39.90  ? 49  TRP A CD1   1 
ATOM   269  C CD2   . TRP A 1 77  ? 5.519   11.077  9.213   1.00 39.41  ? 49  TRP A CD2   1 
ATOM   270  N NE1   . TRP A 1 77  ? 5.394   11.410  7.001   1.00 42.17  ? 49  TRP A NE1   1 
ATOM   271  C CE2   . TRP A 1 77  ? 4.966   11.896  8.209   1.00 40.75  ? 49  TRP A CE2   1 
ATOM   272  C CE3   . TRP A 1 77  ? 5.233   11.364  10.551  1.00 40.21  ? 49  TRP A CE3   1 
ATOM   273  C CZ2   . TRP A 1 77  ? 4.144   12.981  8.499   1.00 42.03  ? 49  TRP A CZ2   1 
ATOM   274  C CZ3   . TRP A 1 77  ? 4.416   12.441  10.837  1.00 41.49  ? 49  TRP A CZ3   1 
ATOM   275  C CH2   . TRP A 1 77  ? 3.883   13.238  9.817   1.00 42.69  ? 49  TRP A CH2   1 
ATOM   276  N N     . PRO A 1 78  ? 9.134   8.203   11.604  1.00 38.53  ? 50  PRO A N     1 
ATOM   277  C CA    . PRO A 1 78  ? 9.733   7.098   12.356  1.00 42.03  ? 50  PRO A CA    1 
ATOM   278  C C     . PRO A 1 78  ? 8.884   5.837   12.282  1.00 45.14  ? 50  PRO A C     1 
ATOM   279  O O     . PRO A 1 78  ? 7.692   5.870   11.968  1.00 48.05  ? 50  PRO A O     1 
ATOM   280  C CB    . PRO A 1 78  ? 9.791   7.637   13.789  1.00 41.35  ? 50  PRO A CB    1 
ATOM   281  C CG    . PRO A 1 78  ? 8.656   8.596   13.864  1.00 42.58  ? 50  PRO A CG    1 
ATOM   282  C CD    . PRO A 1 78  ? 8.514   9.205   12.490  1.00 41.46  ? 50  PRO A CD    1 
ATOM   283  N N     . GLN A 1 79  ? 9.534   4.710   12.573  1.00 42.84  ? 51  GLN A N     1 
ATOM   284  C CA    . GLN A 1 79  ? 8.858   3.419   12.635  1.00 43.81  ? 51  GLN A CA    1 
ATOM   285  C C     . GLN A 1 79  ? 7.720   3.460   13.645  1.00 46.37  ? 51  GLN A C     1 
ATOM   286  O O     . GLN A 1 79  ? 6.544   3.472   13.267  1.00 46.53  ? 51  GLN A O     1 
ATOM   287  C CB    . GLN A 1 79  ? 9.849   2.312   12.998  1.00 51.27  ? 51  GLN A CB    1 
ATOM   288  C CG    . GLN A 1 79  ? 10.596  1.728   11.815  1.00 46.88  ? 51  GLN A CG    1 
ATOM   289  C CD    . GLN A 1 79  ? 9.704   0.908   10.905  1.00 46.83  ? 51  GLN A CD    1 
ATOM   290  O OE1   . GLN A 1 79  ? 9.952   0.802   9.705   1.00 49.97  ? 51  GLN A OE1   1 
ATOM   291  N NE2   . GLN A 1 79  ? 8.661   0.315   11.474  1.00 45.12  ? 51  GLN A NE2   1 
ATOM   292  N N     . THR A 1 80  ? 8.061   3.475   14.925  1.00 46.59  ? 52  THR A N     1 
ATOM   293  C CA    . THR A 1 80  ? 7.062   3.681   15.964  1.00 45.81  ? 52  THR A CA    1 
ATOM   294  C C     . THR A 1 80  ? 6.612   5.135   15.930  1.00 48.66  ? 52  THR A C     1 
ATOM   295  O O     . THR A 1 80  ? 7.451   6.035   16.071  1.00 49.91  ? 52  THR A O     1 
ATOM   296  C CB    . THR A 1 80  ? 7.627   3.326   17.335  1.00 46.85  ? 52  THR A CB    1 
ATOM   297  O OG1   . THR A 1 80  ? 8.045   1.955   17.340  1.00 50.61  ? 52  THR A OG1   1 
ATOM   298  C CG2   . THR A 1 80  ? 6.574   3.534   18.413  1.00 52.36  ? 52  THR A CG2   1 
ATOM   299  N N     . PRO A 1 81  ? 5.323   5.413   15.731  1.00 46.58  ? 53  PRO A N     1 
ATOM   300  C CA    . PRO A 1 81  ? 4.884   6.805   15.577  1.00 45.15  ? 53  PRO A CA    1 
ATOM   301  C C     . PRO A 1 81  ? 5.152   7.633   16.826  1.00 43.09  ? 53  PRO A C     1 
ATOM   302  O O     . PRO A 1 81  ? 5.193   7.120   17.946  1.00 45.09  ? 53  PRO A O     1 
ATOM   303  C CB    . PRO A 1 81  ? 3.380   6.679   15.310  1.00 44.34  ? 53  PRO A CB    1 
ATOM   304  C CG    . PRO A 1 81  ? 3.186   5.290   14.811  1.00 43.11  ? 53  PRO A CG    1 
ATOM   305  C CD    . PRO A 1 81  ? 4.244   4.449   15.459  1.00 44.68  ? 53  PRO A CD    1 
ATOM   306  N N     . LEU A 1 82  ? 5.341   8.928   16.613  1.00 35.60  ? 54  LEU A N     1 
ATOM   307  C CA    . LEU A 1 82  ? 5.502   9.915   17.666  1.00 35.62  ? 54  LEU A CA    1 
ATOM   308  C C     . LEU A 1 82  ? 4.359   10.919  17.603  1.00 36.11  ? 54  LEU A C     1 
ATOM   309  O O     . LEU A 1 82  ? 3.726   11.085  16.554  1.00 37.81  ? 54  LEU A O     1 
ATOM   310  C CB    . LEU A 1 82  ? 6.847   10.646  17.536  1.00 34.71  ? 54  LEU A CB    1 
ATOM   311  C CG    . LEU A 1 82  ? 8.104   9.799   17.735  1.00 35.35  ? 54  LEU A CG    1 
ATOM   312  C CD1   . LEU A 1 82  ? 9.355   10.644  17.540  1.00 34.17  ? 54  LEU A CD1   1 
ATOM   313  C CD2   . LEU A 1 82  ? 8.099   9.152   19.110  1.00 39.98  ? 54  LEU A CD2   1 
ATOM   314  N N     . PRO A 1 83  ? 4.052   11.593  18.711  1.00 28.28  ? 55  PRO A N     1 
ATOM   315  C CA    . PRO A 1 83  ? 2.987   12.602  18.678  1.00 34.51  ? 55  PRO A CA    1 
ATOM   316  C C     . PRO A 1 83  ? 3.348   13.756  17.753  1.00 33.70  ? 55  PRO A C     1 
ATOM   317  O O     . PRO A 1 83  ? 4.503   14.176  17.672  1.00 40.11  ? 55  PRO A O     1 
ATOM   318  C CB    . PRO A 1 83  ? 2.877   13.061  20.138  1.00 39.88  ? 55  PRO A CB    1 
ATOM   319  C CG    . PRO A 1 83  ? 3.571   12.020  20.945  1.00 39.94  ? 55  PRO A CG    1 
ATOM   320  C CD    . PRO A 1 83  ? 4.598   11.394  20.065  1.00 37.92  ? 55  PRO A CD    1 
ATOM   321  N N     . VAL A 1 84  ? 2.340   14.260  17.046  1.00 31.13  ? 56  VAL A N     1 
ATOM   322  C CA    . VAL A 1 84  ? 2.496   15.368  16.113  1.00 28.21  ? 56  VAL A CA    1 
ATOM   323  C C     . VAL A 1 84  ? 1.736   16.568  16.661  1.00 43.29  ? 56  VAL A C     1 
ATOM   324  O O     . VAL A 1 84  ? 0.617   16.429  17.166  1.00 36.31  ? 56  VAL A O     1 
ATOM   325  C CB    . VAL A 1 84  ? 2.003   14.985  14.703  1.00 27.93  ? 56  VAL A CB    1 
ATOM   326  C CG1   . VAL A 1 84  ? 1.873   16.213  13.827  1.00 32.55  ? 56  VAL A CG1   1 
ATOM   327  C CG2   . VAL A 1 84  ? 2.956   13.987  14.071  1.00 31.61  ? 56  VAL A CG2   1 
ATOM   328  N N     . LEU A 1 85  ? 2.350   17.744  16.568  1.00 33.56  ? 57  LEU A N     1 
ATOM   329  C CA    . LEU A 1 85  ? 1.818   18.962  17.158  1.00 29.29  ? 57  LEU A CA    1 
ATOM   330  C C     . LEU A 1 85  ? 1.382   19.938  16.073  1.00 52.65  ? 57  LEU A C     1 
ATOM   331  O O     . LEU A 1 85  ? 2.063   20.095  15.055  1.00 37.74  ? 57  LEU A O     1 
ATOM   332  C CB    . LEU A 1 85  ? 2.861   19.622  18.063  1.00 29.69  ? 57  LEU A CB    1 
ATOM   333  C CG    . LEU A 1 85  ? 2.472   20.942  18.727  1.00 31.91  ? 57  LEU A CG    1 
ATOM   334  C CD1   . LEU A 1 85  ? 1.327   20.727  19.701  1.00 37.29  ? 57  LEU A CD1   1 
ATOM   335  C CD2   . LEU A 1 85  ? 3.670   21.558  19.429  1.00 30.74  ? 57  LEU A CD2   1 
ATOM   336  N N     . ASP A 1 86  ? 0.243   20.591  16.298  1.00 38.68  ? 58  ASP A N     1 
ATOM   337  C CA    . ASP A 1 86  ? -0.250  21.654  15.430  1.00 40.84  ? 58  ASP A CA    1 
ATOM   338  C C     . ASP A 1 86  ? -0.407  22.919  16.261  1.00 41.50  ? 58  ASP A C     1 
ATOM   339  O O     . ASP A 1 86  ? -1.216  22.956  17.195  1.00 39.63  ? 58  ASP A O     1 
ATOM   340  C CB    . ASP A 1 86  ? -1.579  21.269  14.776  1.00 44.27  ? 58  ASP A CB    1 
ATOM   341  C CG    . ASP A 1 86  ? -2.067  22.314  13.785  1.00 55.40  ? 58  ASP A CG    1 
ATOM   342  O OD1   . ASP A 1 86  ? -1.245  23.145  13.341  1.00 55.59  ? 58  ASP A OD1   1 
ATOM   343  O OD2   . ASP A 1 86  ? -3.271  22.305  13.450  1.00 56.47  ? 58  ASP A OD2   1 
ATOM   344  N N     . ILE A 1 87  ? 0.360   23.950  15.920  1.00 48.27  ? 59  ILE A N     1 
ATOM   345  C CA    . ILE A 1 87  ? 0.385   25.203  16.664  1.00 31.58  ? 59  ILE A CA    1 
ATOM   346  C C     . ILE A 1 87  ? -0.492  26.215  15.942  1.00 37.57  ? 59  ILE A C     1 
ATOM   347  O O     . ILE A 1 87  ? -0.393  26.372  14.718  1.00 42.70  ? 59  ILE A O     1 
ATOM   348  C CB    . ILE A 1 87  ? 1.823   25.724  16.819  1.00 31.81  ? 59  ILE A CB    1 
ATOM   349  C CG1   . ILE A 1 87  ? 2.641   24.758  17.678  1.00 31.57  ? 59  ILE A CG1   1 
ATOM   350  C CG2   . ILE A 1 87  ? 1.829   27.117  17.426  1.00 37.39  ? 59  ILE A CG2   1 
ATOM   351  C CD1   . ILE A 1 87  ? 4.084   25.162  17.847  1.00 31.95  ? 59  ILE A CD1   1 
ATOM   352  N N     . GLY A 1 88  ? -1.347  26.903  16.695  1.00 39.61  ? 60  GLY A N     1 
ATOM   353  C CA    . GLY A 1 88  ? -2.293  27.832  16.108  1.00 36.95  ? 60  GLY A CA    1 
ATOM   354  C C     . GLY A 1 88  ? -3.293  27.120  15.223  1.00 38.09  ? 60  GLY A C     1 
ATOM   355  O O     . GLY A 1 88  ? -3.484  27.489  14.061  1.00 42.04  ? 60  GLY A O     1 
ATOM   356  N N     . CYS A 1 89  ? -3.938  26.088  15.770  1.00 37.26  ? 61  CYS A N     1 
ATOM   357  C CA    . CYS A 1 89  ? -4.810  25.225  14.984  1.00 38.22  ? 61  CYS A CA    1 
ATOM   358  C C     . CYS A 1 89  ? -6.136  25.878  14.620  1.00 40.02  ? 61  CYS A C     1 
ATOM   359  O O     . CYS A 1 89  ? -6.849  25.344  13.764  1.00 40.09  ? 61  CYS A O     1 
ATOM   360  C CB    . CYS A 1 89  ? -5.071  23.925  15.744  1.00 39.63  ? 61  CYS A CB    1 
ATOM   361  S SG    . CYS A 1 89  ? -5.943  24.146  17.310  1.00 36.94  ? 61  CYS A SG    1 
ATOM   362  N N     . GLY A 1 90  ? -6.481  27.006  15.235  1.00 38.61  ? 62  GLY A N     1 
ATOM   363  C CA    . GLY A 1 90  ? -7.741  27.658  14.976  1.00 38.67  ? 62  GLY A CA    1 
ATOM   364  C C     . GLY A 1 90  ? -8.917  26.833  15.462  1.00 37.03  ? 62  GLY A C     1 
ATOM   365  O O     . GLY A 1 90  ? -8.879  26.233  16.540  1.00 39.03  ? 62  GLY A O     1 
ATOM   366  N N     . PRO A 1 91  ? -9.991  26.787  14.664  1.00 37.62  ? 63  PRO A N     1 
ATOM   367  C CA    . PRO A 1 91  ? -11.160 25.976  15.035  1.00 34.28  ? 63  PRO A CA    1 
ATOM   368  C C     . PRO A 1 91  ? -10.968 24.489  14.774  1.00 37.67  ? 63  PRO A C     1 
ATOM   369  O O     . PRO A 1 91  ? -11.939 23.728  14.780  1.00 34.91  ? 63  PRO A O     1 
ATOM   370  C CB    . PRO A 1 91  ? -12.276 26.555  14.154  1.00 34.87  ? 63  PRO A CB    1 
ATOM   371  C CG    . PRO A 1 91  ? -11.565 27.103  12.970  1.00 34.67  ? 63  PRO A CG    1 
ATOM   372  C CD    . PRO A 1 91  ? -10.228 27.589  13.452  1.00 34.94  ? 63  PRO A CD    1 
ATOM   373  N N     . GLY A 1 92  ? -9.729  24.065  14.542  1.00 37.82  ? 64  GLY A N     1 
ATOM   374  C CA    . GLY A 1 92  ? -9.430  22.652  14.415  1.00 34.56  ? 64  GLY A CA    1 
ATOM   375  C C     . GLY A 1 92  ? -9.886  22.000  13.129  1.00 34.01  ? 64  GLY A C     1 
ATOM   376  O O     . GLY A 1 92  ? -10.250 20.820  13.136  1.00 36.02  ? 64  GLY A O     1 
ATOM   377  N N     . ASP A 1 93  ? -9.868  22.732  12.016  1.00 35.29  ? 65  ASP A N     1 
ATOM   378  C CA    . ASP A 1 93  ? -10.281 22.152  10.744  1.00 36.00  ? 65  ASP A CA    1 
ATOM   379  C C     . ASP A 1 93  ? -9.101  21.608  9.949   1.00 36.15  ? 65  ASP A C     1 
ATOM   380  O O     . ASP A 1 93  ? -9.202  20.531  9.352   1.00 37.22  ? 65  ASP A O     1 
ATOM   381  C CB    . ASP A 1 93  ? -11.041 23.190  9.920   1.00 36.69  ? 65  ASP A CB    1 
ATOM   382  C CG    . ASP A 1 93  ? -12.341 23.609  10.575  1.00 44.75  ? 65  ASP A CG    1 
ATOM   383  O OD1   . ASP A 1 93  ? -13.307 22.817  10.550  1.00 51.25  ? 65  ASP A OD1   1 
ATOM   384  O OD2   . ASP A 1 93  ? -12.403 24.736  11.103  1.00 45.46  ? 65  ASP A OD2   1 
ATOM   385  N N     . ILE A 1 94  ? -7.984  22.338  9.924   1.00 34.91  ? 66  ILE A N     1 
ATOM   386  C CA    . ILE A 1 94  ? -6.756  21.792  9.354   1.00 33.33  ? 66  ILE A CA    1 
ATOM   387  C C     . ILE A 1 94  ? -6.297  20.584  10.160  1.00 35.73  ? 66  ILE A C     1 
ATOM   388  O O     . ILE A 1 94  ? -5.794  19.599  9.606   1.00 37.01  ? 66  ILE A O     1 
ATOM   389  C CB    . ILE A 1 94  ? -5.672  22.885  9.286   1.00 35.78  ? 66  ILE A CB    1 
ATOM   390  C CG1   . ILE A 1 94  ? -5.899  23.786  8.071   1.00 38.69  ? 66  ILE A CG1   1 
ATOM   391  C CG2   . ILE A 1 94  ? -4.276  22.278  9.244   1.00 37.87  ? 66  ILE A CG2   1 
ATOM   392  C CD1   . ILE A 1 94  ? -4.975  24.979  8.020   1.00 41.35  ? 66  ILE A CD1   1 
ATOM   393  N N     . ALA A 1 95  ? -6.488  20.631  11.480  1.00 39.84  ? 67  ALA A N     1 
ATOM   394  C CA    . ALA A 1 95  ? -6.086  19.516  12.330  1.00 31.33  ? 67  ALA A CA    1 
ATOM   395  C C     . ALA A 1 95  ? -6.922  18.273  12.052  1.00 29.77  ? 67  ALA A C     1 
ATOM   396  O O     . ALA A 1 95  ? -6.384  17.162  11.981  1.00 32.40  ? 67  ALA A O     1 
ATOM   397  C CB    . ALA A 1 95  ? -6.191  19.915  13.802  1.00 32.57  ? 67  ALA A CB    1 
ATOM   398  N N     . ARG A 1 96  ? -8.234  18.436  11.886  1.00 30.21  ? 68  ARG A N     1 
ATOM   399  C CA    . ARG A 1 96  ? -9.122  17.290  11.728  1.00 30.25  ? 68  ARG A CA    1 
ATOM   400  C C     . ARG A 1 96  ? -9.244  16.837  10.276  1.00 39.68  ? 68  ARG A C     1 
ATOM   401  O O     . ARG A 1 96  ? -9.096  15.646  9.984   1.00 40.50  ? 68  ARG A O     1 
ATOM   402  C CB    . ARG A 1 96  ? -10.509 17.614  12.291  1.00 31.99  ? 68  ARG A CB    1 
ATOM   403  C CG    . ARG A 1 96  ? -11.607 16.707  11.752  1.00 35.82  ? 68  ARG A CG    1 
ATOM   404  C CD    . ARG A 1 96  ? -11.475 15.287  12.282  1.00 42.32  ? 68  ARG A CD    1 
ATOM   405  N NE    . ARG A 1 96  ? -12.307 14.353  11.532  1.00 50.61  ? 68  ARG A NE    1 
ATOM   406  C CZ    . ARG A 1 96  ? -12.995 13.356  12.070  1.00 61.13  ? 68  ARG A CZ    1 
ATOM   407  N NH1   . ARG A 1 96  ? -12.998 13.144  13.376  1.00 63.60  ? 68  ARG A NH1   1 
ATOM   408  N NH2   . ARG A 1 96  ? -13.698 12.551  11.279  1.00 64.73  ? 68  ARG A NH2   1 
ATOM   409  N N     . LYS A 1 97  ? -9.518  17.763  9.361   1.00 40.37  ? 69  LYS A N     1 
ATOM   410  C CA    . LYS A 1 97  ? -9.862  17.404  7.992   1.00 35.92  ? 69  LYS A CA    1 
ATOM   411  C C     . LYS A 1 97  ? -8.659  17.299  7.064   1.00 34.00  ? 69  LYS A C     1 
ATOM   412  O O     . LYS A 1 97  ? -8.799  16.765  5.959   1.00 39.24  ? 69  LYS A O     1 
ATOM   413  C CB    . LYS A 1 97  ? -10.857 18.420  7.421   1.00 35.23  ? 69  LYS A CB    1 
ATOM   414  C CG    . LYS A 1 97  ? -12.179 18.466  8.169   1.00 34.25  ? 69  LYS A CG    1 
ATOM   415  C CD    . LYS A 1 97  ? -13.089 19.552  7.628   1.00 40.72  ? 69  LYS A CD    1 
ATOM   416  C CE    . LYS A 1 97  ? -14.347 19.678  8.469   1.00 59.95  ? 69  LYS A CE    1 
ATOM   417  N NZ    . LYS A 1 97  ? -15.183 20.835  8.048   1.00 78.29  ? 69  LYS A NZ    1 
ATOM   418  N N     . VAL A 1 98  ? -7.488  17.784  7.474   1.00 40.02  ? 70  VAL A N     1 
ATOM   419  C CA    . VAL A 1 98  ? -6.322  17.785  6.596   1.00 29.49  ? 70  VAL A CA    1 
ATOM   420  C C     . VAL A 1 98  ? -5.199  16.959  7.209   1.00 33.30  ? 70  VAL A C     1 
ATOM   421  O O     . VAL A 1 98  ? -4.749  15.970  6.619   1.00 42.46  ? 70  VAL A O     1 
ATOM   422  C CB    . VAL A 1 98  ? -5.848  19.220  6.304   1.00 29.70  ? 70  VAL A CB    1 
ATOM   423  C CG1   . VAL A 1 98  ? -4.663  19.200  5.353   1.00 34.59  ? 70  VAL A CG1   1 
ATOM   424  C CG2   . VAL A 1 98  ? -6.982  20.048  5.731   1.00 32.45  ? 70  VAL A CG2   1 
ATOM   425  N N     . LEU A 1 99  ? -4.738  17.360  8.396   1.00 31.66  ? 71  LEU A N     1 
ATOM   426  C CA    . LEU A 1 99  ? -3.593  16.697  9.015   1.00 28.52  ? 71  LEU A CA    1 
ATOM   427  C C     . LEU A 1 99  ? -3.921  15.259  9.400   1.00 41.18  ? 71  LEU A C     1 
ATOM   428  O O     . LEU A 1 99  ? -3.201  14.327  9.023   1.00 34.81  ? 71  LEU A O     1 
ATOM   429  C CB    . LEU A 1 99  ? -3.129  17.486  10.239  1.00 31.69  ? 71  LEU A CB    1 
ATOM   430  C CG    . LEU A 1 99  ? -2.374  18.788  9.972   1.00 29.80  ? 71  LEU A CG    1 
ATOM   431  C CD1   . LEU A 1 99  ? -2.102  19.524  11.272  1.00 34.42  ? 71  LEU A CD1   1 
ATOM   432  C CD2   . LEU A 1 99  ? -1.077  18.498  9.240   1.00 34.04  ? 71  LEU A CD2   1 
ATOM   433  N N     . ALA A 1 100 ? -5.003  15.062  10.153  1.00 34.34  ? 72  ALA A N     1 
ATOM   434  C CA    . ALA A 1 100 ? -5.330  13.728  10.650  1.00 28.47  ? 72  ALA A CA    1 
ATOM   435  C C     . ALA A 1 100 ? -5.499  12.682  9.552   1.00 39.44  ? 72  ALA A C     1 
ATOM   436  O O     . ALA A 1 100 ? -4.972  11.569  9.722   1.00 42.08  ? 72  ALA A O     1 
ATOM   437  C CB    . ALA A 1 100 ? -6.585  13.800  11.531  1.00 28.84  ? 72  ALA A CB    1 
ATOM   438  N N     . PRO A 1 101 ? -6.196  12.938  8.436   1.00 38.69  ? 73  PRO A N     1 
ATOM   439  C CA    . PRO A 1 101 ? -6.310  11.893  7.405   1.00 41.37  ? 73  PRO A CA    1 
ATOM   440  C C     . PRO A 1 101 ? -4.995  11.557  6.723   1.00 40.94  ? 73  PRO A C     1 
ATOM   441  O O     . PRO A 1 101 ? -4.903  10.499  6.088   1.00 42.43  ? 73  PRO A O     1 
ATOM   442  C CB    . PRO A 1 101 ? -7.311  12.488  6.403   1.00 44.06  ? 73  PRO A CB    1 
ATOM   443  C CG    . PRO A 1 101 ? -8.038  13.540  7.159   1.00 44.07  ? 73  PRO A CG    1 
ATOM   444  C CD    . PRO A 1 101 ? -7.038  14.104  8.111   1.00 40.87  ? 73  PRO A CD    1 
ATOM   445  N N     . ARG A 1 102 ? -3.981  12.413  6.829   1.00 41.07  ? 74  ARG A N     1 
ATOM   446  C CA    . ARG A 1 102 ? -2.728  12.220  6.115   1.00 36.89  ? 74  ARG A CA    1 
ATOM   447  C C     . ARG A 1 102 ? -1.610  11.667  6.990   1.00 37.03  ? 74  ARG A C     1 
ATOM   448  O O     . ARG A 1 102 ? -0.571  11.266  6.457   1.00 41.60  ? 74  ARG A O     1 
ATOM   449  C CB    . ARG A 1 102 ? -2.279  13.542  5.481   1.00 37.31  ? 74  ARG A CB    1 
ATOM   450  C CG    . ARG A 1 102 ? -3.120  13.957  4.286   1.00 41.08  ? 74  ARG A CG    1 
ATOM   451  C CD    . ARG A 1 102 ? -2.870  15.402  3.889   1.00 43.52  ? 74  ARG A CD    1 
ATOM   452  N NE    . ARG A 1 102 ? -3.553  15.741  2.646   1.00 48.73  ? 74  ARG A NE    1 
ATOM   453  C CZ    . ARG A 1 102 ? -4.840  16.047  2.559   1.00 50.70  ? 74  ARG A CZ    1 
ATOM   454  N NH1   . ARG A 1 102 ? -5.620  16.067  3.628   1.00 44.88  ? 74  ARG A NH1   1 
ATOM   455  N NH2   . ARG A 1 102 ? -5.359  16.338  1.370   1.00 56.04  ? 74  ARG A NH2   1 
ATOM   456  N N     . LEU A 1 103 ? -1.798  11.627  8.308   1.00 38.17  ? 75  LEU A N     1 
ATOM   457  C CA    . LEU A 1 103 ? -0.782  11.093  9.197   1.00 35.65  ? 75  LEU A CA    1 
ATOM   458  C C     . LEU A 1 103 ? -0.736  9.569   9.104   1.00 38.68  ? 75  LEU A C     1 
ATOM   459  O O     . LEU A 1 103 ? -1.724  8.929   8.737   1.00 35.96  ? 75  LEU A O     1 
ATOM   460  C CB    . LEU A 1 103 ? -1.061  11.515  10.638  1.00 33.41  ? 75  LEU A CB    1 
ATOM   461  C CG    . LEU A 1 103 ? -0.934  13.004  10.964  1.00 30.57  ? 75  LEU A CG    1 
ATOM   462  C CD1   . LEU A 1 103 ? -1.478  13.296  12.353  1.00 32.99  ? 75  LEU A CD1   1 
ATOM   463  C CD2   . LEU A 1 103 ? 0.511   13.457  10.844  1.00 32.67  ? 75  LEU A CD2   1 
ATOM   464  N N     . PRO A 1 104 ? 0.410   8.966   9.423   1.00 36.04  ? 76  PRO A N     1 
ATOM   465  C CA    . PRO A 1 104 ? 0.477   7.502   9.489   1.00 31.49  ? 76  PRO A CA    1 
ATOM   466  C C     . PRO A 1 104 ? -0.461  6.957   10.556  1.00 36.14  ? 76  PRO A C     1 
ATOM   467  O O     . PRO A 1 104 ? -0.886  7.665   11.472  1.00 42.83  ? 76  PRO A O     1 
ATOM   468  C CB    . PRO A 1 104 ? 1.944   7.224   9.844   1.00 32.12  ? 76  PRO A CB    1 
ATOM   469  C CG    . PRO A 1 104 ? 2.679   8.454   9.431   1.00 35.22  ? 76  PRO A CG    1 
ATOM   470  C CD    . PRO A 1 104 ? 1.727   9.592   9.634   1.00 40.45  ? 76  PRO A CD    1 
ATOM   471  N N     . ALA A 1 105 ? -0.788  5.674   10.422  1.00 32.77  ? 77  ALA A N     1 
ATOM   472  C CA    . ALA A 1 105 ? -1.687  5.034   11.372  1.00 32.12  ? 77  ALA A CA    1 
ATOM   473  C C     . ALA A 1 105 ? -1.060  4.996   12.759  1.00 34.19  ? 77  ALA A C     1 
ATOM   474  O O     . ALA A 1 105 ? 0.143   4.763   12.912  1.00 31.55  ? 77  ALA A O     1 
ATOM   475  C CB    . ALA A 1 105 ? -2.031  3.620   10.907  1.00 38.48  ? 77  ALA A CB    1 
ATOM   476  N N     . GLY A 1 106 ? -1.885  5.232   13.777  1.00 35.84  ? 78  GLY A N     1 
ATOM   477  C CA    . GLY A 1 106 ? -1.418  5.256   15.145  1.00 40.45  ? 78  GLY A CA    1 
ATOM   478  C C     . GLY A 1 106 ? -0.708  6.524   15.565  1.00 42.04  ? 78  GLY A C     1 
ATOM   479  O O     . GLY A 1 106 ? -0.199  6.582   16.692  1.00 40.06  ? 78  GLY A O     1 
ATOM   480  N N     . THR A 1 107 ? -0.653  7.537   14.704  1.00 40.01  ? 79  THR A N     1 
ATOM   481  C CA    . THR A 1 107 ? -0.004  8.797   15.044  1.00 37.74  ? 79  THR A CA    1 
ATOM   482  C C     . THR A 1 107 ? -0.991  9.692   15.783  1.00 41.28  ? 79  THR A C     1 
ATOM   483  O O     . THR A 1 107 ? -2.025  10.076  15.227  1.00 42.42  ? 79  THR A O     1 
ATOM   484  C CB    . THR A 1 107 ? 0.511   9.491   13.786  1.00 37.00  ? 79  THR A CB    1 
ATOM   485  O OG1   . THR A 1 107 ? 1.429   8.629   13.102  1.00 39.37  ? 79  THR A OG1   1 
ATOM   486  C CG2   . THR A 1 107 ? 1.214   10.788  14.146  1.00 38.10  ? 79  THR A CG2   1 
ATOM   487  N N     . ARG A 1 108 ? -0.676  10.020  17.033  1.00 41.08  ? 80  ARG A N     1 
ATOM   488  C CA    . ARG A 1 108 ? -1.535  10.882  17.830  1.00 39.90  ? 80  ARG A CA    1 
ATOM   489  C C     . ARG A 1 108 ? -1.229  12.344  17.531  1.00 40.96  ? 80  ARG A C     1 
ATOM   490  O O     . ARG A 1 108 ? -0.071  12.725  17.335  1.00 39.08  ? 80  ARG A O     1 
ATOM   491  C CB    . ARG A 1 108 ? -1.353  10.591  19.321  1.00 39.67  ? 80  ARG A CB    1 
ATOM   492  C CG    . ARG A 1 108 ? -2.462  11.148  20.199  1.00 51.92  ? 80  ARG A CG    1 
ATOM   493  C CD    . ARG A 1 108 ? -2.210  10.866  21.674  1.00 64.57  ? 80  ARG A CD    1 
ATOM   494  N NE    . ARG A 1 108 ? -0.924  11.376  22.133  1.00 62.90  ? 80  ARG A NE    1 
ATOM   495  C CZ    . ARG A 1 108 ? -0.750  12.069  23.250  1.00 51.31  ? 80  ARG A CZ    1 
ATOM   496  N NH1   . ARG A 1 108 ? -1.764  12.355  24.051  1.00 45.04  ? 80  ARG A NH1   1 
ATOM   497  N NH2   . ARG A 1 108 ? 0.471   12.488  23.572  1.00 42.44  ? 80  ARG A NH2   1 
ATOM   498  N N     . LEU A 1 109 ? -2.277  13.162  17.492  1.00 44.04  ? 81  LEU A N     1 
ATOM   499  C CA    . LEU A 1 109 ? -2.169  14.568  17.133  1.00 42.28  ? 81  LEU A CA    1 
ATOM   500  C C     . LEU A 1 109 ? -2.509  15.448  18.330  1.00 43.19  ? 81  LEU A C     1 
ATOM   501  O O     . LEU A 1 109 ? -3.441  15.155  19.085  1.00 42.87  ? 81  LEU A O     1 
ATOM   502  C CB    . LEU A 1 109 ? -3.095  14.901  15.957  1.00 38.69  ? 81  LEU A CB    1 
ATOM   503  C CG    . LEU A 1 109 ? -3.148  16.353  15.478  1.00 35.99  ? 81  LEU A CG    1 
ATOM   504  C CD1   . LEU A 1 109 ? -1.774  16.831  15.036  1.00 37.63  ? 81  LEU A CD1   1 
ATOM   505  C CD2   . LEU A 1 109 ? -4.157  16.507  14.351  1.00 33.70  ? 81  LEU A CD2   1 
ATOM   506  N N     . VAL A 1 110 ? -1.743  16.522  18.500  1.00 48.87  ? 82  VAL A N     1 
ATOM   507  C CA    . VAL A 1 110 ? -1.974  17.511  19.546  1.00 29.75  ? 82  VAL A CA    1 
ATOM   508  C C     . VAL A 1 110 ? -2.096  18.870  18.874  1.00 29.97  ? 82  VAL A C     1 
ATOM   509  O O     . VAL A 1 110 ? -1.179  19.301  18.165  1.00 56.29  ? 82  VAL A O     1 
ATOM   510  C CB    . VAL A 1 110 ? -0.847  17.516  20.591  1.00 29.90  ? 82  VAL A CB    1 
ATOM   511  C CG1   . VAL A 1 110 ? -1.116  18.569  21.656  1.00 30.88  ? 82  VAL A CG1   1 
ATOM   512  C CG2   . VAL A 1 110 ? -0.700  16.140  21.222  1.00 32.60  ? 82  VAL A CG2   1 
ATOM   513  N N     . ALA A 1 111 ? -3.224  19.540  19.088  1.00 31.18  ? 83  ALA A N     1 
ATOM   514  C CA    . ALA A 1 111 ? -3.497  20.837  18.483  1.00 33.08  ? 83  ALA A CA    1 
ATOM   515  C C     . ALA A 1 111 ? -3.678  21.875  19.580  1.00 36.48  ? 83  ALA A C     1 
ATOM   516  O O     . ALA A 1 111 ? -4.453  21.662  20.518  1.00 37.23  ? 83  ALA A O     1 
ATOM   517  C CB    . ALA A 1 111 ? -4.738  20.778  17.592  1.00 30.73  ? 83  ALA A CB    1 
ATOM   518  N N     . CYS A 1 112 ? -2.968  22.994  19.459  1.00 37.09  ? 84  CYS A N     1 
ATOM   519  C CA    . CYS A 1 112 ? -3.013  24.048  20.458  1.00 33.76  ? 84  CYS A CA    1 
ATOM   520  C C     . CYS A 1 112 ? -3.362  25.377  19.804  1.00 35.15  ? 84  CYS A C     1 
ATOM   521  O O     . CYS A 1 112 ? -3.193  25.569  18.596  1.00 38.20  ? 84  CYS A O     1 
ATOM   522  C CB    . CYS A 1 112 ? -1.682  24.172  21.213  1.00 33.89  ? 84  CYS A CB    1 
ATOM   523  S SG    . CYS A 1 112 ? -0.211  24.036  20.178  1.00 40.66  ? 84  CYS A SG    1 
ATOM   524  N N     . ASP A 1 113 ? -3.852  26.298  20.630  1.00 35.45  ? 85  ASP A N     1 
ATOM   525  C CA    . ASP A 1 113 ? -4.228  27.634  20.193  1.00 34.30  ? 85  ASP A CA    1 
ATOM   526  C C     . ASP A 1 113 ? -4.322  28.516  21.429  1.00 35.21  ? 85  ASP A C     1 
ATOM   527  O O     . ASP A 1 113 ? -4.875  28.096  22.448  1.00 35.45  ? 85  ASP A O     1 
ATOM   528  C CB    . ASP A 1 113 ? -5.562  27.616  19.435  1.00 34.33  ? 85  ASP A CB    1 
ATOM   529  C CG    . ASP A 1 113 ? -5.779  28.862  18.600  1.00 37.09  ? 85  ASP A CG    1 
ATOM   530  O OD1   . ASP A 1 113 ? -6.101  29.922  19.177  1.00 38.38  ? 85  ASP A OD1   1 
ATOM   531  O OD2   . ASP A 1 113 ? -5.633  28.779  17.363  1.00 38.82  ? 85  ASP A OD2   1 
ATOM   532  N N     . ILE A 1 114 ? -3.773  29.730  21.338  1.00 35.78  ? 86  ILE A N     1 
ATOM   533  C CA    . ILE A 1 114 ? -3.775  30.613  22.501  1.00 36.75  ? 86  ILE A CA    1 
ATOM   534  C C     . ILE A 1 114 ? -5.195  31.033  22.861  1.00 37.41  ? 86  ILE A C     1 
ATOM   535  O O     . ILE A 1 114 ? -5.488  31.315  24.029  1.00 38.92  ? 86  ILE A O     1 
ATOM   536  C CB    . ILE A 1 114 ? -2.869  31.836  22.263  1.00 37.30  ? 86  ILE A CB    1 
ATOM   537  C CG1   . ILE A 1 114 ? -2.491  32.483  23.597  1.00 40.35  ? 86  ILE A CG1   1 
ATOM   538  C CG2   . ILE A 1 114 ? -3.551  32.855  21.368  1.00 37.74  ? 86  ILE A CG2   1 
ATOM   539  C CD1   . ILE A 1 114 ? -1.822  33.835  23.456  1.00 52.34  ? 86  ILE A CD1   1 
ATOM   540  N N     . SER A 1 115 ? -6.095  31.068  21.886  1.00 37.26  ? 87  SER A N     1 
ATOM   541  C CA    . SER A 1 115 ? -7.468  31.477  22.143  1.00 38.15  ? 87  SER A CA    1 
ATOM   542  C C     . SER A 1 115 ? -8.253  30.305  22.717  1.00 37.67  ? 87  SER A C     1 
ATOM   543  O O     . SER A 1 115 ? -8.289  29.236  22.098  1.00 36.82  ? 87  SER A O     1 
ATOM   544  C CB    . SER A 1 115 ? -8.126  31.975  20.864  1.00 40.26  ? 87  SER A CB    1 
ATOM   545  O OG    . SER A 1 115 ? -9.532  32.057  21.013  1.00 38.56  ? 87  SER A OG    1 
ATOM   546  N N     . PRO A 1 116 ? -8.872  30.450  23.890  1.00 38.42  ? 88  PRO A N     1 
ATOM   547  C CA    . PRO A 1 116 ? -9.701  29.363  24.426  1.00 38.25  ? 88  PRO A CA    1 
ATOM   548  C C     . PRO A 1 116 ? -10.874 29.038  23.517  1.00 40.97  ? 88  PRO A C     1 
ATOM   549  O O     . PRO A 1 116 ? -11.029 27.892  23.087  1.00 43.61  ? 88  PRO A O     1 
ATOM   550  C CB    . PRO A 1 116 ? -10.176 29.914  25.776  1.00 39.34  ? 88  PRO A CB    1 
ATOM   551  C CG    . PRO A 1 116 ? -9.167  30.943  26.145  1.00 39.81  ? 88  PRO A CG    1 
ATOM   552  C CD    . PRO A 1 116 ? -8.709  31.552  24.852  1.00 44.12  ? 88  PRO A CD    1 
ATOM   553  N N     . GLU A 1 117 ? -11.688 30.048  23.205  1.00 38.90  ? 89  GLU A N     1 
ATOM   554  C CA    . GLU A 1 117 ? -12.888 29.897  22.386  1.00 39.01  ? 89  GLU A CA    1 
ATOM   555  C C     . GLU A 1 117 ? -12.657 28.996  21.178  1.00 38.16  ? 89  GLU A C     1 
ATOM   556  O O     . GLU A 1 117 ? -13.544 28.227  20.794  1.00 37.82  ? 89  GLU A O     1 
ATOM   557  C CB    . GLU A 1 117 ? -13.384 31.269  21.926  1.00 45.88  ? 89  GLU A CB    1 
ATOM   558  C CG    . GLU A 1 117 ? -13.593 32.258  23.058  1.00 43.29  ? 89  GLU A CG    1 
ATOM   559  C CD    . GLU A 1 117 ? -12.372 33.123  23.305  1.00 44.25  ? 89  GLU A CD    1 
ATOM   560  O OE1   . GLU A 1 117 ? -11.495 33.186  22.418  1.00 51.34  ? 89  GLU A OE1   1 
ATOM   561  O OE2   . GLU A 1 117 ? -12.287 33.738  24.389  1.00 42.17  ? 89  GLU A OE2   1 
ATOM   562  N N     . MET A 1 118 ? -11.466 29.077  20.581  1.00 38.36  ? 90  MET A N     1 
ATOM   563  C CA    . MET A 1 118 ? -11.120 28.160  19.499  1.00 36.36  ? 90  MET A CA    1 
ATOM   564  C C     . MET A 1 118 ? -10.996 26.728  20.005  1.00 35.72  ? 90  MET A C     1 
ATOM   565  O O     . MET A 1 118 ? -11.578 25.807  19.422  1.00 42.25  ? 90  MET A O     1 
ATOM   566  C CB    . MET A 1 118 ? -9.828  28.607  18.815  1.00 35.92  ? 90  MET A CB    1 
ATOM   567  C CG    . MET A 1 118 ? -9.924  29.958  18.135  1.00 36.53  ? 90  MET A CG    1 
ATOM   568  S SD    . MET A 1 118 ? -10.748 29.811  16.538  1.00 39.00  ? 90  MET A SD    1 
ATOM   569  C CE    . MET A 1 118 ? -9.688  30.816  15.503  1.00 42.03  ? 90  MET A CE    1 
ATOM   570  N N     . VAL A 1 119 ? -10.253 26.517  21.096  1.00 35.67  ? 91  VAL A N     1 
ATOM   571  C CA    . VAL A 1 119 ? -9.993  25.146  21.527  1.00 35.06  ? 91  VAL A CA    1 
ATOM   572  C C     . VAL A 1 119 ? -11.271 24.483  22.029  1.00 35.52  ? 91  VAL A C     1 
ATOM   573  O O     . VAL A 1 119 ? -11.428 23.265  21.906  1.00 42.64  ? 91  VAL A O     1 
ATOM   574  C CB    . VAL A 1 119 ? -8.866  25.091  22.583  1.00 35.01  ? 91  VAL A CB    1 
ATOM   575  C CG1   . VAL A 1 119 ? -7.659  25.903  22.124  1.00 34.86  ? 91  VAL A CG1   1 
ATOM   576  C CG2   . VAL A 1 119 ? -9.348  25.522  23.960  1.00 35.88  ? 91  VAL A CG2   1 
ATOM   577  N N     . ASP A 1 120 ? -12.213 25.258  22.576  1.00 36.33  ? 92  ASP A N     1 
ATOM   578  C CA    . ASP A 1 120 ? -13.500 24.672  22.938  1.00 36.76  ? 92  ASP A CA    1 
ATOM   579  C C     . ASP A 1 120 ? -14.353 24.389  21.709  1.00 36.62  ? 92  ASP A C     1 
ATOM   580  O O     . ASP A 1 120 ? -15.119 23.418  21.701  1.00 36.60  ? 92  ASP A O     1 
ATOM   581  C CB    . ASP A 1 120 ? -14.262 25.576  23.908  1.00 42.41  ? 92  ASP A CB    1 
ATOM   582  C CG    . ASP A 1 120 ? -13.438 25.965  25.116  1.00 48.00  ? 92  ASP A CG    1 
ATOM   583  O OD1   . ASP A 1 120 ? -12.539 26.819  24.984  1.00 49.13  ? 92  ASP A OD1   1 
ATOM   584  O OD2   . ASP A 1 120 ? -13.687 25.409  26.206  1.00 51.86  ? 92  ASP A OD2   1 
ATOM   585  N N     . PHE A 1 121 ? -14.242 25.219  20.670  1.00 36.62  ? 93  PHE A N     1 
ATOM   586  C CA    . PHE A 1 121 ? -14.937 24.925  19.423  1.00 36.48  ? 93  PHE A CA    1 
ATOM   587  C C     . PHE A 1 121 ? -14.413 23.631  18.813  1.00 35.52  ? 93  PHE A C     1 
ATOM   588  O O     . PHE A 1 121 ? -15.180 22.844  18.247  1.00 38.14  ? 93  PHE A O     1 
ATOM   589  C CB    . PHE A 1 121 ? -14.781 26.101  18.451  1.00 36.69  ? 93  PHE A CB    1 
ATOM   590  C CG    . PHE A 1 121 ? -15.608 25.980  17.196  1.00 36.77  ? 93  PHE A CG    1 
ATOM   591  C CD1   . PHE A 1 121 ? -15.245 25.114  16.174  1.00 35.99  ? 93  PHE A CD1   1 
ATOM   592  C CD2   . PHE A 1 121 ? -16.753 26.744  17.040  1.00 37.73  ? 93  PHE A CD2   1 
ATOM   593  C CE1   . PHE A 1 121 ? -16.011 25.009  15.031  1.00 36.17  ? 93  PHE A CE1   1 
ATOM   594  C CE2   . PHE A 1 121 ? -17.521 26.645  15.897  1.00 38.48  ? 93  PHE A CE2   1 
ATOM   595  C CZ    . PHE A 1 121 ? -17.150 25.776  14.891  1.00 37.12  ? 93  PHE A CZ    1 
ATOM   596  N N     . CYS A 1 122 ? -13.106 23.390  18.934  1.00 34.82  ? 94  CYS A N     1 
ATOM   597  C CA    . CYS A 1 122 ? -12.514 22.161  18.417  1.00 33.96  ? 94  CYS A CA    1 
ATOM   598  C C     . CYS A 1 122 ? -13.072 20.938  19.135  1.00 33.96  ? 94  CYS A C     1 
ATOM   599  O O     . CYS A 1 122 ? -13.638 20.035  18.508  1.00 45.58  ? 94  CYS A O     1 
ATOM   600  C CB    . CYS A 1 122 ? -10.994 22.211  18.567  1.00 33.38  ? 94  CYS A CB    1 
ATOM   601  S SG    . CYS A 1 122 ? -10.167 23.613  17.806  1.00 33.42  ? 94  CYS A SG    1 
ATOM   602  N N     . ARG A 1 123 ? -12.924 20.898  20.462  1.00 34.22  ? 95  ARG A N     1 
ATOM   603  C CA    . ARG A 1 123 ? -13.335 19.745  21.258  1.00 34.26  ? 95  ARG A CA    1 
ATOM   604  C C     . ARG A 1 123 ? -14.828 19.456  21.169  1.00 34.88  ? 95  ARG A C     1 
ATOM   605  O O     . ARG A 1 123 ? -15.274 18.439  21.710  1.00 34.97  ? 95  ARG A O     1 
ATOM   606  C CB    . ARG A 1 123 ? -12.928 19.961  22.721  1.00 34.60  ? 95  ARG A CB    1 
ATOM   607  C CG    . ARG A 1 123 ? -11.484 20.413  22.893  1.00 34.18  ? 95  ARG A CG    1 
ATOM   608  C CD    . ARG A 1 123 ? -10.819 19.853  24.138  1.00 34.17  ? 95  ARG A CD    1 
ATOM   609  N NE    . ARG A 1 123 ? -10.928 20.775  25.264  1.00 36.15  ? 95  ARG A NE    1 
ATOM   610  C CZ    . ARG A 1 123 ? -9.934  21.074  26.090  1.00 38.13  ? 95  ARG A CZ    1 
ATOM   611  N NH1   . ARG A 1 123 ? -8.729  20.548  25.940  1.00 38.05  ? 95  ARG A NH1   1 
ATOM   612  N NH2   . ARG A 1 123 ? -10.151 21.929  27.085  1.00 36.53  ? 95  ARG A NH2   1 
ATOM   613  N N     . GLN A 1 124 ? -15.605 20.308  20.501  1.00 36.15  ? 96  GLN A N     1 
ATOM   614  C CA    . GLN A 1 124 ? -17.044 20.111  20.383  1.00 37.30  ? 96  GLN A CA    1 
ATOM   615  C C     . GLN A 1 124 ? -17.502 19.773  18.972  1.00 39.55  ? 96  GLN A C     1 
ATOM   616  O O     . GLN A 1 124 ? -18.449 19.000  18.818  1.00 42.25  ? 96  GLN A O     1 
ATOM   617  C CB    . GLN A 1 124 ? -17.793 21.359  20.869  1.00 40.30  ? 96  GLN A CB    1 
ATOM   618  C CG    . GLN A 1 124 ? -19.218 21.089  21.332  1.00 45.54  ? 96  GLN A CG    1 
ATOM   619  C CD    . GLN A 1 124 ? -20.211 22.112  20.817  1.00 54.37  ? 96  GLN A CD    1 
ATOM   620  O OE1   . GLN A 1 124 ? -20.329 22.328  19.612  1.00 52.16  ? 96  GLN A OE1   1 
ATOM   621  N NE2   . GLN A 1 124 ? -20.928 22.753  21.733  1.00 58.67  ? 96  GLN A NE2   1 
ATOM   622  N N     . HIS A 1 125 ? -16.857 20.323  17.941  1.00 39.89  ? 97  HIS A N     1 
ATOM   623  C CA    . HIS A 1 125 ? -17.213 19.992  16.566  1.00 37.22  ? 97  HIS A CA    1 
ATOM   624  C C     . HIS A 1 125 ? -16.191 19.057  15.931  1.00 39.48  ? 97  HIS A C     1 
ATOM   625  O O     . HIS A 1 125 ? -16.474 17.874  15.717  1.00 41.16  ? 97  HIS A O     1 
ATOM   626  C CB    . HIS A 1 125 ? -17.357 21.257  15.715  1.00 35.65  ? 97  HIS A CB    1 
ATOM   627  C CG    . HIS A 1 125 ? -18.276 22.283  16.300  1.00 36.94  ? 97  HIS A CG    1 
ATOM   628  N ND1   . HIS A 1 125 ? -17.871 23.187  17.258  1.00 46.01  ? 97  HIS A ND1   1 
ATOM   629  C CD2   . HIS A 1 125 ? -19.582 22.549  16.061  1.00 40.76  ? 97  HIS A CD2   1 
ATOM   630  C CE1   . HIS A 1 125 ? -18.887 23.967  17.582  1.00 48.90  ? 97  HIS A CE1   1 
ATOM   631  N NE2   . HIS A 1 125 ? -19.938 23.599  16.871  1.00 45.85  ? 97  HIS A NE2   1 
ATOM   632  N N     . ASN A 1 126 ? -15.000 19.574  15.626  1.00 41.28  ? 98  ASN A N     1 
ATOM   633  C CA    . ASN A 1 126 ? -13.967 18.778  14.971  1.00 37.92  ? 98  ASN A CA    1 
ATOM   634  C C     . ASN A 1 126 ? -13.247 17.872  15.962  1.00 37.23  ? 98  ASN A C     1 
ATOM   635  O O     . ASN A 1 126 ? -12.065 17.565  15.781  1.00 40.41  ? 98  ASN A O     1 
ATOM   636  C CB    . ASN A 1 126 ? -12.952 19.683  14.268  1.00 34.35  ? 98  ASN A CB    1 
ATOM   637  C CG    . ASN A 1 126 ? -13.604 20.842  13.541  1.00 39.05  ? 98  ASN A CG    1 
ATOM   638  O OD1   . ASN A 1 126 ? -14.333 21.634  14.138  1.00 45.21  ? 98  ASN A OD1   1 
ATOM   639  N ND2   . ASN A 1 126 ? -13.340 20.950  12.244  1.00 41.43  ? 98  ASN A ND2   1 
ATOM   640  N N     . ALA A 1 127 ? -13.945 17.441  17.008  1.00 33.29  ? 99  ALA A N     1 
ATOM   641  C CA    . ALA A 1 127 ? -13.347 16.563  18.005  1.00 36.63  ? 99  ALA A CA    1 
ATOM   642  C C     . ALA A 1 127 ? -13.179 15.164  17.428  1.00 42.20  ? 99  ALA A C     1 
ATOM   643  O O     . ALA A 1 127 ? -14.165 14.500  17.091  1.00 35.99  ? 99  ALA A O     1 
ATOM   644  C CB    . ALA A 1 127 ? -14.210 16.526  19.263  1.00 49.73  ? 99  ALA A CB    1 
ATOM   645  N N     . LEU A 1 128 ? -11.931 14.719  17.310  1.00 45.59  ? 100 LEU A N     1 
ATOM   646  C CA    . LEU A 1 128 ? -11.629 13.384  16.809  1.00 47.09  ? 100 LEU A CA    1 
ATOM   647  C C     . LEU A 1 128 ? -11.052 12.556  17.948  1.00 45.58  ? 100 LEU A C     1 
ATOM   648  O O     . LEU A 1 128 ? -9.891  12.766  18.333  1.00 48.29  ? 100 LEU A O     1 
ATOM   649  C CB    . LEU A 1 128 ? -10.646 13.453  15.639  1.00 44.29  ? 100 LEU A CB    1 
ATOM   650  C CG    . LEU A 1 128 ? -10.017 12.166  15.096  1.00 39.67  ? 100 LEU A CG    1 
ATOM   651  C CD1   . LEU A 1 128 ? -11.034 11.037  14.987  1.00 41.87  ? 100 LEU A CD1   1 
ATOM   652  C CD2   . LEU A 1 128 ? -9.364  12.429  13.748  1.00 44.86  ? 100 LEU A CD2   1 
ATOM   653  N N     . PRO A 1 129 ? -11.811 11.624  18.519  1.00 41.83  ? 101 PRO A N     1 
ATOM   654  C CA    . PRO A 1 129 ? -11.305 10.861  19.665  1.00 41.98  ? 101 PRO A CA    1 
ATOM   655  C C     . PRO A 1 129 ? -10.199 9.900   19.263  1.00 44.92  ? 101 PRO A C     1 
ATOM   656  O O     . PRO A 1 129 ? -10.125 9.436   18.122  1.00 49.37  ? 101 PRO A O     1 
ATOM   657  C CB    . PRO A 1 129 ? -12.542 10.101  20.162  1.00 40.97  ? 101 PRO A CB    1 
ATOM   658  C CG    . PRO A 1 129 ? -13.714 10.804  19.536  1.00 42.76  ? 101 PRO A CG    1 
ATOM   659  C CD    . PRO A 1 129 ? -13.215 11.306  18.222  1.00 39.63  ? 101 PRO A CD    1 
ATOM   660  N N     . GLY A 1 130 ? -9.329  9.604   20.227  1.00 45.65  ? 102 GLY A N     1 
ATOM   661  C CA    . GLY A 1 130 ? -8.247  8.663   20.015  1.00 46.98  ? 102 GLY A CA    1 
ATOM   662  C C     . GLY A 1 130 ? -7.164  9.117   19.064  1.00 44.32  ? 102 GLY A C     1 
ATOM   663  O O     . GLY A 1 130 ? -6.262  8.331   18.759  1.00 44.87  ? 102 GLY A O     1 
ATOM   664  N N     . THR A 1 131 ? -7.220  10.358  18.584  1.00 42.11  ? 103 THR A N     1 
ATOM   665  C CA    . THR A 1 131 ? -6.219  10.857  17.651  1.00 43.58  ? 103 THR A CA    1 
ATOM   666  C C     . THR A 1 131 ? -5.823  12.288  17.986  1.00 46.74  ? 103 THR A C     1 
ATOM   667  O O     . THR A 1 131 ? -4.661  12.558  18.307  1.00 51.67  ? 103 THR A O     1 
ATOM   668  C CB    . THR A 1 131 ? -6.737  10.782  16.212  1.00 41.66  ? 103 THR A CB    1 
ATOM   669  O OG1   . THR A 1 131 ? -7.241  9.467   15.948  1.00 34.55  ? 103 THR A OG1   1 
ATOM   670  C CG2   . THR A 1 131 ? -5.622  11.102  15.228  1.00 41.50  ? 103 THR A CG2   1 
ATOM   671  N N     . ILE A 1 132 ? -6.778  13.209  17.916  1.00 38.12  ? 104 ILE A N     1 
ATOM   672  C CA    . ILE A 1 132 ? -6.520  14.628  18.126  1.00 41.72  ? 104 ILE A CA    1 
ATOM   673  C C     . ILE A 1 132 ? -6.888  14.994  19.555  1.00 37.49  ? 104 ILE A C     1 
ATOM   674  O O     . ILE A 1 132 ? -7.981  14.660  20.031  1.00 35.00  ? 104 ILE A O     1 
ATOM   675  C CB    . ILE A 1 132 ? -7.301  15.490  17.121  1.00 35.50  ? 104 ILE A CB    1 
ATOM   676  C CG1   . ILE A 1 132 ? -7.280  14.837  15.740  1.00 37.45  ? 104 ILE A CG1   1 
ATOM   677  C CG2   . ILE A 1 132 ? -6.713  16.887  17.060  1.00 44.14  ? 104 ILE A CG2   1 
ATOM   678  C CD1   . ILE A 1 132 ? -7.852  15.706  14.652  1.00 38.71  ? 104 ILE A CD1   1 
ATOM   679  N N     . THR A 1 133 ? -5.975  15.676  20.241  1.00 36.54  ? 105 THR A N     1 
ATOM   680  C CA    . THR A 1 133 ? -6.201  16.192  21.590  1.00 37.20  ? 105 THR A CA    1 
ATOM   681  C C     . THR A 1 133 ? -6.017  17.706  21.531  1.00 41.25  ? 105 THR A C     1 
ATOM   682  O O     . THR A 1 133 ? -4.888  18.198  21.444  1.00 43.62  ? 105 THR A O     1 
ATOM   683  C CB    . THR A 1 133 ? -5.250  15.547  22.598  1.00 40.07  ? 105 THR A CB    1 
ATOM   684  O OG1   . THR A 1 133 ? -3.928  16.070  22.417  1.00 48.08  ? 105 THR A OG1   1 
ATOM   685  C CG2   . THR A 1 133 ? -5.219  14.037  22.416  1.00 39.83  ? 105 THR A CG2   1 
ATOM   686  N N     . TYR A 1 134 ? -7.124  18.444  21.564  1.00 39.74  ? 106 TYR A N     1 
ATOM   687  C CA    . TYR A 1 134 ? -7.071  19.895  21.452  1.00 33.41  ? 106 TYR A CA    1 
ATOM   688  C C     . TYR A 1 134 ? -6.746  20.511  22.806  1.00 32.59  ? 106 TYR A C     1 
ATOM   689  O O     . TYR A 1 134 ? -7.414  20.223  23.803  1.00 35.31  ? 106 TYR A O     1 
ATOM   690  C CB    . TYR A 1 134 ? -8.396  20.437  20.926  1.00 32.45  ? 106 TYR A CB    1 
ATOM   691  C CG    . TYR A 1 134 ? -8.766  19.931  19.553  1.00 32.03  ? 106 TYR A CG    1 
ATOM   692  C CD1   . TYR A 1 134 ? -8.137  20.425  18.417  1.00 37.56  ? 106 TYR A CD1   1 
ATOM   693  C CD2   . TYR A 1 134 ? -9.746  18.963  19.390  1.00 32.03  ? 106 TYR A CD2   1 
ATOM   694  C CE1   . TYR A 1 134 ? -8.479  19.970  17.156  1.00 38.22  ? 106 TYR A CE1   1 
ATOM   695  C CE2   . TYR A 1 134 ? -10.091 18.499  18.137  1.00 31.74  ? 106 TYR A CE2   1 
ATOM   696  C CZ    . TYR A 1 134 ? -9.455  19.006  17.023  1.00 36.23  ? 106 TYR A CZ    1 
ATOM   697  O OH    . TYR A 1 134 ? -9.802  18.539  15.776  1.00 40.23  ? 106 TYR A OH    1 
ATOM   698  N N     . GLU A 1 135 ? -5.715  21.356  22.843  1.00 32.65  ? 107 GLU A N     1 
ATOM   699  C CA    . GLU A 1 135 ? -5.247  21.930  24.094  1.00 33.23  ? 107 GLU A CA    1 
ATOM   700  C C     . GLU A 1 135 ? -4.992  23.420  23.918  1.00 33.72  ? 107 GLU A C     1 
ATOM   701  O O     . GLU A 1 135 ? -5.072  23.968  22.816  1.00 33.56  ? 107 GLU A O     1 
ATOM   702  C CB    . GLU A 1 135 ? -3.980  21.241  24.586  1.00 33.07  ? 107 GLU A CB    1 
ATOM   703  C CG    . GLU A 1 135 ? -4.084  19.739  24.555  1.00 39.19  ? 107 GLU A CG    1 
ATOM   704  C CD    . GLU A 1 135 ? -4.319  19.167  25.923  1.00 44.63  ? 107 GLU A CD    1 
ATOM   705  O OE1   . GLU A 1 135 ? -4.583  19.955  26.854  1.00 45.88  ? 107 GLU A OE1   1 
ATOM   706  O OE2   . GLU A 1 135 ? -4.263  17.926  26.073  1.00 46.60  ? 107 GLU A OE2   1 
ATOM   707  N N     . LEU A 1 136 ? -4.660  24.072  25.027  1.00 34.39  ? 108 LEU A N     1 
ATOM   708  C CA    . LEU A 1 136 ? -4.361  25.495  25.050  1.00 35.02  ? 108 LEU A CA    1 
ATOM   709  C C     . LEU A 1 136 ? -2.861  25.696  25.210  1.00 34.95  ? 108 LEU A C     1 
ATOM   710  O O     . LEU A 1 136 ? -2.215  25.000  25.998  1.00 34.87  ? 108 LEU A O     1 
ATOM   711  C CB    . LEU A 1 136 ? -5.115  26.186  26.191  1.00 36.02  ? 108 LEU A CB    1 
ATOM   712  C CG    . LEU A 1 136 ? -4.954  27.698  26.372  1.00 36.89  ? 108 LEU A CG    1 
ATOM   713  C CD1   . LEU A 1 136 ? -6.270  28.324  26.799  1.00 37.73  ? 108 LEU A CD1   1 
ATOM   714  C CD2   . LEU A 1 136 ? -3.866  28.019  27.393  1.00 37.37  ? 108 LEU A CD2   1 
ATOM   715  N N     . LEU A 1 137 ? -2.312  26.652  24.462  1.00 35.05  ? 109 LEU A N     1 
ATOM   716  C CA    . LEU A 1 137 ? -0.890  26.960  24.548  1.00 35.11  ? 109 LEU A CA    1 
ATOM   717  C C     . LEU A 1 137 ? -0.607  28.263  23.817  1.00 35.50  ? 109 LEU A C     1 
ATOM   718  O O     . LEU A 1 137 ? -1.206  28.537  22.774  1.00 35.29  ? 109 LEU A O     1 
ATOM   719  C CB    . LEU A 1 137 ? -0.034  25.833  23.954  1.00 34.22  ? 109 LEU A CB    1 
ATOM   720  C CG    . LEU A 1 137 ? 1.478   26.061  23.929  1.00 34.27  ? 109 LEU A CG    1 
ATOM   721  C CD1   . LEU A 1 137 ? 2.044   26.029  25.339  1.00 34.86  ? 109 LEU A CD1   1 
ATOM   722  C CD2   . LEU A 1 137 ? 2.164   25.026  23.050  1.00 33.41  ? 109 LEU A CD2   1 
ATOM   723  N N     . ASP A 1 138 ? 0.306   29.056  24.372  1.00 36.15  ? 110 ASP A N     1 
ATOM   724  C CA    . ASP A 1 138 ? 0.860   30.224  23.700  1.00 36.56  ? 110 ASP A CA    1 
ATOM   725  C C     . ASP A 1 138 ? 2.247   29.843  23.193  1.00 36.11  ? 110 ASP A C     1 
ATOM   726  O O     . ASP A 1 138 ? 3.094   29.401  23.975  1.00 41.42  ? 110 ASP A O     1 
ATOM   727  C CB    . ASP A 1 138 ? 0.928   31.419  24.653  1.00 37.74  ? 110 ASP A CB    1 
ATOM   728  C CG    . ASP A 1 138 ? 1.362   32.704  23.964  1.00 38.30  ? 110 ASP A CG    1 
ATOM   729  O OD1   . ASP A 1 138 ? 1.703   32.668  22.763  1.00 38.21  ? 110 ASP A OD1   1 
ATOM   730  O OD2   . ASP A 1 138 ? 1.355   33.761  24.630  1.00 39.35  ? 110 ASP A OD2   1 
ATOM   731  N N     . VAL A 1 139 ? 2.474   30.009  21.887  1.00 35.70  ? 111 VAL A N     1 
ATOM   732  C CA    . VAL A 1 139 ? 3.710   29.532  21.273  1.00 35.23  ? 111 VAL A CA    1 
ATOM   733  C C     . VAL A 1 139 ? 4.934   30.261  21.817  1.00 35.97  ? 111 VAL A C     1 
ATOM   734  O O     . VAL A 1 139 ? 6.057   29.759  21.696  1.00 39.19  ? 111 VAL A O     1 
ATOM   735  C CB    . VAL A 1 139 ? 3.621   29.657  19.735  1.00 35.89  ? 111 VAL A CB    1 
ATOM   736  C CG1   . VAL A 1 139 ? 3.690   31.116  19.306  1.00 43.63  ? 111 VAL A CG1   1 
ATOM   737  C CG2   . VAL A 1 139 ? 4.705   28.827  19.053  1.00 34.14  ? 111 VAL A CG2   1 
ATOM   738  N N     . VAL A 1 140 ? 4.747   31.430  22.426  1.00 36.94  ? 112 VAL A N     1 
ATOM   739  C CA    . VAL A 1 140 ? 5.853   32.164  23.031  1.00 37.80  ? 112 VAL A CA    1 
ATOM   740  C C     . VAL A 1 140 ? 5.665   32.194  24.542  1.00 38.46  ? 112 VAL A C     1 
ATOM   741  O O     . VAL A 1 140 ? 5.824   33.241  25.180  1.00 39.52  ? 112 VAL A O     1 
ATOM   742  C CB    . VAL A 1 140 ? 5.964   33.585  22.451  1.00 38.56  ? 112 VAL A CB    1 
ATOM   743  C CG1   . VAL A 1 140 ? 6.579   33.539  21.062  1.00 38.06  ? 112 VAL A CG1   1 
ATOM   744  C CG2   . VAL A 1 140 ? 4.595   34.249  22.406  1.00 38.87  ? 112 VAL A CG2   1 
ATOM   745  N N     . GLU A 1 141 ? 5.337   31.045  25.119  1.00 41.15  ? 113 GLU A N     1 
ATOM   746  C CA    . GLU A 1 141 ? 5.070   30.973  26.551  1.00 42.70  ? 113 GLU A CA    1 
ATOM   747  C C     . GLU A 1 141 ? 6.361   31.159  27.340  1.00 42.14  ? 113 GLU A C     1 
ATOM   748  O O     . GLU A 1 141 ? 7.382   30.548  27.000  1.00 40.92  ? 113 GLU A O     1 
ATOM   749  C CB    . GLU A 1 141 ? 4.427   29.633  26.903  1.00 42.17  ? 113 GLU A CB    1 
ATOM   750  C CG    . GLU A 1 141 ? 3.035   29.745  27.498  1.00 41.83  ? 113 GLU A CG    1 
ATOM   751  C CD    . GLU A 1 141 ? 3.061   30.018  28.989  1.00 51.74  ? 113 GLU A CD    1 
ATOM   752  O OE1   . GLU A 1 141 ? 4.150   29.920  29.594  1.00 52.00  ? 113 GLU A OE1   1 
ATOM   753  O OE2   . GLU A 1 141 ? 1.993   30.332  29.556  1.00 63.48  ? 113 GLU A OE2   1 
ATOM   754  N N     . PRO A 1 142 ? 6.365   31.996  28.382  1.00 42.31  ? 114 PRO A N     1 
ATOM   755  C CA    . PRO A 1 142 ? 7.573   32.102  29.220  1.00 43.59  ? 114 PRO A CA    1 
ATOM   756  C C     . PRO A 1 142 ? 7.973   30.780  29.852  1.00 45.82  ? 114 PRO A C     1 
ATOM   757  O O     . PRO A 1 142 ? 9.131   30.359  29.731  1.00 47.17  ? 114 PRO A O     1 
ATOM   758  C CB    . PRO A 1 142 ? 7.169   33.146  30.270  1.00 43.85  ? 114 PRO A CB    1 
ATOM   759  C CG    . PRO A 1 142 ? 6.124   33.969  29.595  1.00 45.31  ? 114 PRO A CG    1 
ATOM   760  C CD    . PRO A 1 142 ? 5.355   33.009  28.730  1.00 43.04  ? 114 PRO A CD    1 
ATOM   761  N N     . ARG A 1 143 ? 7.040   30.109  30.522  1.00 43.79  ? 115 ARG A N     1 
ATOM   762  C CA    . ARG A 1 143 ? 7.283   28.806  31.134  1.00 42.44  ? 115 ARG A CA    1 
ATOM   763  C C     . ARG A 1 143 ? 6.593   27.744  30.284  1.00 43.06  ? 115 ARG A C     1 
ATOM   764  O O     . ARG A 1 143 ? 5.484   27.298  30.581  1.00 42.97  ? 115 ARG A O     1 
ATOM   765  C CB    . ARG A 1 143 ? 6.795   28.776  32.575  1.00 46.68  ? 115 ARG A CB    1 
ATOM   766  C CG    . ARG A 1 143 ? 6.942   30.093  33.312  1.00 48.00  ? 115 ARG A CG    1 
ATOM   767  C CD    . ARG A 1 143 ? 6.542   29.926  34.761  1.00 47.08  ? 115 ARG A CD    1 
ATOM   768  N NE    . ARG A 1 143 ? 7.318   28.852  35.372  1.00 48.12  ? 115 ARG A NE    1 
ATOM   769  C CZ    . ARG A 1 143 ? 8.442   29.028  36.052  1.00 50.01  ? 115 ARG A CZ    1 
ATOM   770  N NH1   . ARG A 1 143 ? 8.953   30.234  36.246  1.00 52.82  ? 115 ARG A NH1   1 
ATOM   771  N NH2   . ARG A 1 143 ? 9.076   27.967  36.539  1.00 49.87  ? 115 ARG A NH2   1 
ATOM   772  N N     . LEU A 1 144 ? 7.270   27.339  29.208  1.00 43.37  ? 116 LEU A N     1 
ATOM   773  C CA    . LEU A 1 144 ? 6.738   26.284  28.353  1.00 45.78  ? 116 LEU A CA    1 
ATOM   774  C C     . LEU A 1 144 ? 6.656   24.965  29.109  1.00 46.10  ? 116 LEU A C     1 
ATOM   775  O O     . LEU A 1 144 ? 5.685   24.212  28.962  1.00 44.01  ? 116 LEU A O     1 
ATOM   776  C CB    . LEU A 1 144 ? 7.618   26.131  27.112  1.00 47.02  ? 116 LEU A CB    1 
ATOM   777  C CG    . LEU A 1 144 ? 7.050   25.611  25.784  1.00 40.32  ? 116 LEU A CG    1 
ATOM   778  C CD1   . LEU A 1 144 ? 8.164   25.551  24.761  1.00 40.98  ? 116 LEU A CD1   1 
ATOM   779  C CD2   . LEU A 1 144 ? 6.367   24.260  25.888  1.00 37.08  ? 116 LEU A CD2   1 
ATOM   780  N N     . GLU A 1 145 ? 7.662   24.676  29.935  1.00 45.90  ? 117 GLU A N     1 
ATOM   781  C CA    . GLU A 1 145 ? 7.783   23.383  30.594  1.00 47.72  ? 117 GLU A CA    1 
ATOM   782  C C     . GLU A 1 145 ? 6.678   23.119  31.608  1.00 45.78  ? 117 GLU A C     1 
ATOM   783  O O     . GLU A 1 145 ? 6.604   22.005  32.139  1.00 45.52  ? 117 GLU A O     1 
ATOM   784  C CB    . GLU A 1 145 ? 9.148   23.285  31.277  1.00 51.58  ? 117 GLU A CB    1 
ATOM   785  C CG    . GLU A 1 145 ? 10.260  22.821  30.353  1.00 54.15  ? 117 GLU A CG    1 
ATOM   786  C CD    . GLU A 1 145 ? 10.906  23.976  29.606  1.00 62.99  ? 117 GLU A CD    1 
ATOM   787  O OE1   . GLU A 1 145 ? 11.003  25.080  30.183  1.00 61.06  ? 117 GLU A OE1   1 
ATOM   788  O OE2   . GLU A 1 145 ? 11.311  23.781  28.439  1.00 63.99  ? 117 GLU A OE2   1 
ATOM   789  N N     . ASP A 1 146 ? 5.822   24.100  31.887  1.00 42.96  ? 118 ASP A N     1 
ATOM   790  C CA    . ASP A 1 146 ? 4.732   23.944  32.839  1.00 41.68  ? 118 ASP A CA    1 
ATOM   791  C C     . ASP A 1 146 ? 3.382   23.744  32.162  1.00 42.65  ? 118 ASP A C     1 
ATOM   792  O O     . ASP A 1 146 ? 2.351   23.775  32.841  1.00 45.37  ? 118 ASP A O     1 
ATOM   793  C CB    . ASP A 1 146 ? 4.673   25.155  33.772  1.00 47.73  ? 118 ASP A CB    1 
ATOM   794  C CG    . ASP A 1 146 ? 5.923   25.300  34.619  1.00 52.84  ? 118 ASP A CG    1 
ATOM   795  O OD1   . ASP A 1 146 ? 7.029   25.371  34.042  1.00 53.39  ? 118 ASP A OD1   1 
ATOM   796  O OD2   . ASP A 1 146 ? 5.800   25.346  35.861  1.00 53.48  ? 118 ASP A OD2   1 
ATOM   797  N N     . THR A 1 147 ? 3.362   23.540  30.849  1.00 44.61  ? 119 THR A N     1 
ATOM   798  C CA    . THR A 1 147 ? 2.126   23.370  30.101  1.00 39.61  ? 119 THR A CA    1 
ATOM   799  C C     . THR A 1 147 ? 1.864   21.895  29.815  1.00 35.11  ? 119 THR A C     1 
ATOM   800  O O     . THR A 1 147 ? 2.761   21.051  29.882  1.00 36.73  ? 119 THR A O     1 
ATOM   801  C CB    . THR A 1 147 ? 2.169   24.153  28.785  1.00 35.60  ? 119 THR A CB    1 
ATOM   802  O OG1   . THR A 1 147 ? 3.151   23.577  27.916  1.00 34.91  ? 119 THR A OG1   1 
ATOM   803  C CG2   . THR A 1 147 ? 2.518   25.610  29.044  1.00 45.00  ? 119 THR A CG2   1 
ATOM   804  N N     . VAL A 1 148 ? 0.605   21.597  29.490  1.00 34.83  ? 120 VAL A N     1 
ATOM   805  C CA    . VAL A 1 148 ? 0.218   20.227  29.167  1.00 34.13  ? 120 VAL A CA    1 
ATOM   806  C C     . VAL A 1 148 ? 0.855   19.790  27.854  1.00 33.29  ? 120 VAL A C     1 
ATOM   807  O O     . VAL A 1 148 ? 1.253   18.629  27.696  1.00 37.55  ? 120 VAL A O     1 
ATOM   808  C CB    . VAL A 1 148 ? -1.318  20.111  29.127  1.00 34.17  ? 120 VAL A CB    1 
ATOM   809  C CG1   . VAL A 1 148 ? -1.751  18.797  28.501  1.00 33.44  ? 120 VAL A CG1   1 
ATOM   810  C CG2   . VAL A 1 148 ? -1.903  20.253  30.522  1.00 35.02  ? 120 VAL A CG2   1 
ATOM   811  N N     . VAL A 1 149 ? 0.982   20.715  26.900  1.00 33.18  ? 121 VAL A N     1 
ATOM   812  C CA    . VAL A 1 149 ? 1.486   20.365  25.574  1.00 32.93  ? 121 VAL A CA    1 
ATOM   813  C C     . VAL A 1 149 ? 2.950   19.943  25.644  1.00 40.79  ? 121 VAL A C     1 
ATOM   814  O O     . VAL A 1 149 ? 3.381   19.033  24.925  1.00 37.19  ? 121 VAL A O     1 
ATOM   815  C CB    . VAL A 1 149 ? 1.274   21.540  24.601  1.00 32.50  ? 121 VAL A CB    1 
ATOM   816  C CG1   . VAL A 1 149 ? 1.984   21.285  23.280  1.00 31.87  ? 121 VAL A CG1   1 
ATOM   817  C CG2   . VAL A 1 149 ? -0.212  21.773  24.373  1.00 32.56  ? 121 VAL A CG2   1 
ATOM   818  N N     . TRP A 1 150 ? 3.736   20.585  26.513  1.00 33.38  ? 122 TRP A N     1 
ATOM   819  C CA    . TRP A 1 150 ? 5.145   20.221  26.635  1.00 36.09  ? 122 TRP A CA    1 
ATOM   820  C C     . TRP A 1 150 ? 5.307   18.793  27.137  1.00 38.12  ? 122 TRP A C     1 
ATOM   821  O O     . TRP A 1 150 ? 6.186   18.058  26.671  1.00 42.50  ? 122 TRP A O     1 
ATOM   822  C CB    . TRP A 1 150 ? 5.868   21.193  27.568  1.00 40.54  ? 122 TRP A CB    1 
ATOM   823  C CG    . TRP A 1 150 ? 7.229   20.715  27.996  1.00 46.03  ? 122 TRP A CG    1 
ATOM   824  C CD1   . TRP A 1 150 ? 7.550   20.107  29.176  1.00 47.40  ? 122 TRP A CD1   1 
ATOM   825  C CD2   . TRP A 1 150 ? 8.448   20.802  27.246  1.00 47.29  ? 122 TRP A CD2   1 
ATOM   826  N NE1   . TRP A 1 150 ? 8.892   19.813  29.207  1.00 45.87  ? 122 TRP A NE1   1 
ATOM   827  C CE2   . TRP A 1 150 ? 9.465   20.229  28.034  1.00 47.81  ? 122 TRP A CE2   1 
ATOM   828  C CE3   . TRP A 1 150 ? 8.777   21.311  25.986  1.00 50.50  ? 122 TRP A CE3   1 
ATOM   829  C CZ2   . TRP A 1 150 ? 10.789  20.150  27.604  1.00 53.54  ? 122 TRP A CZ2   1 
ATOM   830  C CZ3   . TRP A 1 150 ? 10.092  21.231  25.560  1.00 51.54  ? 122 TRP A CZ3   1 
ATOM   831  C CH2   . TRP A 1 150 ? 11.081  20.655  26.367  1.00 53.29  ? 122 TRP A CH2   1 
ATOM   832  N N     . ARG A 1 151 ? 4.468   18.382  28.086  1.00 37.41  ? 123 ARG A N     1 
ATOM   833  C CA    . ARG A 1 151 ? 4.601   17.061  28.684  1.00 35.01  ? 123 ARG A CA    1 
ATOM   834  C C     . ARG A 1 151 ? 3.943   15.968  27.855  1.00 38.50  ? 123 ARG A C     1 
ATOM   835  O O     . ARG A 1 151 ? 4.153   14.785  28.143  1.00 42.13  ? 123 ARG A O     1 
ATOM   836  C CB    . ARG A 1 151 ? 4.035   17.083  30.104  1.00 33.59  ? 123 ARG A CB    1 
ATOM   837  C CG    . ARG A 1 151 ? 4.805   18.038  30.999  1.00 34.44  ? 123 ARG A CG    1 
ATOM   838  C CD    . ARG A 1 151 ? 4.403   17.961  32.456  1.00 35.22  ? 123 ARG A CD    1 
ATOM   839  N NE    . ARG A 1 151 ? 5.087   18.995  33.224  1.00 40.24  ? 123 ARG A NE    1 
ATOM   840  C CZ    . ARG A 1 151 ? 4.861   19.260  34.503  1.00 48.53  ? 123 ARG A CZ    1 
ATOM   841  N NH1   . ARG A 1 151 ? 4.006   18.547  35.215  1.00 53.65  ? 123 ARG A NH1   1 
ATOM   842  N NH2   . ARG A 1 151 ? 5.518   20.259  35.084  1.00 50.56  ? 123 ARG A NH2   1 
ATOM   843  N N     . ASN A 1 152 ? 3.157   16.329  26.839  1.00 36.95  ? 124 ASN A N     1 
ATOM   844  C CA    . ASN A 1 152 ? 2.751   15.363  25.829  1.00 39.94  ? 124 ASN A CA    1 
ATOM   845  C C     . ASN A 1 152 ? 3.880   15.042  24.862  1.00 41.65  ? 124 ASN A C     1 
ATOM   846  O O     . ASN A 1 152 ? 3.803   14.036  24.148  1.00 42.27  ? 124 ASN A O     1 
ATOM   847  C CB    . ASN A 1 152 ? 1.546   15.880  25.040  1.00 39.45  ? 124 ASN A CB    1 
ATOM   848  C CG    . ASN A 1 152 ? 0.259   15.820  25.833  1.00 45.54  ? 124 ASN A CG    1 
ATOM   849  O OD1   . ASN A 1 152 ? -0.349  14.759  25.973  1.00 56.33  ? 124 ASN A OD1   1 
ATOM   850  N ND2   . ASN A 1 152 ? -0.170  16.963  26.349  1.00 46.87  ? 124 ASN A ND2   1 
ATOM   851  N N     . GLY A 1 153 ? 4.922   15.870  24.829  1.00 40.53  ? 125 GLY A N     1 
ATOM   852  C CA    . GLY A 1 153 ? 6.021   15.687  23.916  1.00 39.33  ? 125 GLY A CA    1 
ATOM   853  C C     . GLY A 1 153 ? 6.981   14.604  24.361  1.00 40.39  ? 125 GLY A C     1 
ATOM   854  O O     . GLY A 1 153 ? 6.714   13.849  25.301  1.00 44.93  ? 125 GLY A O     1 
ATOM   855  N N     . PRO A 1 154 ? 8.132   14.507  23.683  1.00 36.21  ? 126 PRO A N     1 
ATOM   856  C CA    . PRO A 1 154 ? 8.578   15.343  22.562  1.00 34.06  ? 126 PRO A CA    1 
ATOM   857  C C     . PRO A 1 154 ? 7.861   14.969  21.271  1.00 39.86  ? 126 PRO A C     1 
ATOM   858  O O     . PRO A 1 154 ? 7.318   13.873  21.157  1.00 44.64  ? 126 PRO A O     1 
ATOM   859  C CB    . PRO A 1 154 ? 10.080  15.057  22.513  1.00 30.63  ? 126 PRO A CB    1 
ATOM   860  C CG    . PRO A 1 154 ? 10.184  13.618  22.940  1.00 35.55  ? 126 PRO A CG    1 
ATOM   861  C CD    . PRO A 1 154 ? 9.072   13.402  23.947  1.00 37.93  ? 126 PRO A CD    1 
ATOM   862  N N     . PHE A 1 155 ? 7.829   15.861  20.285  1.00 38.42  ? 127 PHE A N     1 
ATOM   863  C CA    . PHE A 1 155 ? 7.042   15.660  19.078  1.00 35.87  ? 127 PHE A CA    1 
ATOM   864  C C     . PHE A 1 155 ? 7.949   15.379  17.888  1.00 40.05  ? 127 PHE A C     1 
ATOM   865  O O     . PHE A 1 155 ? 9.038   15.953  17.772  1.00 29.26  ? 127 PHE A O     1 
ATOM   866  C CB    . PHE A 1 155 ? 6.166   16.881  18.786  1.00 34.43  ? 127 PHE A CB    1 
ATOM   867  C CG    . PHE A 1 155 ? 5.117   17.135  19.828  1.00 33.87  ? 127 PHE A CG    1 
ATOM   868  C CD1   . PHE A 1 155 ? 3.887   16.500  19.768  1.00 31.90  ? 127 PHE A CD1   1 
ATOM   869  C CD2   . PHE A 1 155 ? 5.361   18.014  20.869  1.00 36.47  ? 127 PHE A CD2   1 
ATOM   870  C CE1   . PHE A 1 155 ? 2.923   16.736  20.731  1.00 34.54  ? 127 PHE A CE1   1 
ATOM   871  C CE2   . PHE A 1 155 ? 4.402   18.256  21.832  1.00 37.33  ? 127 PHE A CE2   1 
ATOM   872  C CZ    . PHE A 1 155 ? 3.182   17.616  21.764  1.00 38.74  ? 127 PHE A CZ    1 
ATOM   873  N N     . GLY A 1 156 ? 7.490   14.487  17.011  1.00 36.92  ? 128 GLY A N     1 
ATOM   874  C CA    . GLY A 1 156 ? 8.203   14.179  15.790  1.00 30.87  ? 128 GLY A CA    1 
ATOM   875  C C     . GLY A 1 156 ? 8.083   15.289  14.768  1.00 36.87  ? 128 GLY A C     1 
ATOM   876  O O     . GLY A 1 156 ? 9.089   15.754  14.229  1.00 41.91  ? 128 GLY A O     1 
ATOM   877  N N     . LYS A 1 157 ? 6.854   15.731  14.503  1.00 42.75  ? 129 LYS A N     1 
ATOM   878  C CA    . LYS A 1 157 ? 6.592   16.805  13.556  1.00 41.39  ? 129 LYS A CA    1 
ATOM   879  C C     . LYS A 1 157 ? 5.737   17.876  14.217  1.00 34.46  ? 129 LYS A C     1 
ATOM   880  O O     . LYS A 1 157 ? 4.904   17.586  15.080  1.00 28.60  ? 129 LYS A O     1 
ATOM   881  C CB    . LYS A 1 157 ? 5.892   16.283  12.291  1.00 37.95  ? 129 LYS A CB    1 
ATOM   882  C CG    . LYS A 1 157 ? 6.561   15.064  11.687  1.00 37.93  ? 129 LYS A CG    1 
ATOM   883  C CD    . LYS A 1 157 ? 7.981   15.383  11.263  1.00 45.13  ? 129 LYS A CD    1 
ATOM   884  C CE    . LYS A 1 157 ? 8.786   14.121  11.022  1.00 49.76  ? 129 LYS A CE    1 
ATOM   885  N NZ    . LYS A 1 157 ? 9.994   14.056  11.893  1.00 43.91  ? 129 LYS A NZ    1 
ATOM   886  N N     . VAL A 1 158 ? 5.955   19.123  13.803  1.00 39.51  ? 130 VAL A N     1 
ATOM   887  C CA    . VAL A 1 158 ? 5.215   20.271  14.312  1.00 33.39  ? 130 VAL A CA    1 
ATOM   888  C C     . VAL A 1 158 ? 4.776   21.115  13.125  1.00 29.86  ? 130 VAL A C     1 
ATOM   889  O O     . VAL A 1 158 ? 5.617   21.665  12.405  1.00 29.51  ? 130 VAL A O     1 
ATOM   890  C CB    . VAL A 1 158 ? 6.048   21.110  15.295  1.00 30.71  ? 130 VAL A CB    1 
ATOM   891  C CG1   . VAL A 1 158 ? 5.371   22.444  15.555  1.00 30.26  ? 130 VAL A CG1   1 
ATOM   892  C CG2   . VAL A 1 158 ? 6.246   20.355  16.599  1.00 31.40  ? 130 VAL A CG2   1 
ATOM   893  N N     . PHE A 1 159 ? 3.466   21.209  12.917  1.00 32.81  ? 131 PHE A N     1 
ATOM   894  C CA    . PHE A 1 159 ? 2.892   22.021  11.852  1.00 29.45  ? 131 PHE A CA    1 
ATOM   895  C C     . PHE A 1 159 ? 2.471   23.368  12.423  1.00 41.68  ? 131 PHE A C     1 
ATOM   896  O O     . PHE A 1 159 ? 1.585   23.433  13.283  1.00 48.62  ? 131 PHE A O     1 
ATOM   897  C CB    . PHE A 1 159 ? 1.697   21.318  11.208  1.00 35.65  ? 131 PHE A CB    1 
ATOM   898  C CG    . PHE A 1 159 ? 2.032   19.996  10.581  1.00 29.06  ? 131 PHE A CG    1 
ATOM   899  C CD1   . PHE A 1 159 ? 2.525   19.934  9.289   1.00 35.46  ? 131 PHE A CD1   1 
ATOM   900  C CD2   . PHE A 1 159 ? 1.850   18.816  11.279  1.00 28.43  ? 131 PHE A CD2   1 
ATOM   901  C CE1   . PHE A 1 159 ? 2.832   18.720  8.705   1.00 33.88  ? 131 PHE A CE1   1 
ATOM   902  C CE2   . PHE A 1 159 ? 2.156   17.599  10.700  1.00 31.94  ? 131 PHE A CE2   1 
ATOM   903  C CZ    . PHE A 1 159 ? 2.647   17.551  9.413   1.00 33.34  ? 131 PHE A CZ    1 
ATOM   904  N N     . CYS A 1 160 ? 3.105   24.436  11.950  1.00 36.37  ? 132 CYS A N     1 
ATOM   905  C CA    . CYS A 1 160 ? 2.752   25.804  12.325  1.00 35.89  ? 132 CYS A CA    1 
ATOM   906  C C     . CYS A 1 160 ? 2.247   26.492  11.062  1.00 43.00  ? 132 CYS A C     1 
ATOM   907  O O     . CYS A 1 160 ? 3.040   26.893  10.204  1.00 42.51  ? 132 CYS A O     1 
ATOM   908  C CB    . CYS A 1 160 ? 3.945   26.536  12.936  1.00 35.27  ? 132 CYS A CB    1 
ATOM   909  S SG    . CYS A 1 160 ? 3.836   28.340  12.879  1.00 47.05  ? 132 CYS A SG    1 
ATOM   910  N N     . MET A 1 161 ? 0.927   26.616  10.942  1.00 42.38  ? 133 MET A N     1 
ATOM   911  C CA    . MET A 1 161 ? 0.328   27.165  9.732   1.00 46.59  ? 133 MET A CA    1 
ATOM   912  C C     . MET A 1 161 ? 0.226   28.684  9.795   1.00 46.23  ? 133 MET A C     1 
ATOM   913  O O     . MET A 1 161 ? 1.130   29.355  10.304  1.00 48.22  ? 133 MET A O     1 
ATOM   914  C CB    . MET A 1 161 ? -1.050  26.545  9.493   1.00 47.34  ? 133 MET A CB    1 
ATOM   915  C CG    . MET A 1 161 ? -1.024  25.034  9.305   1.00 50.26  ? 133 MET A CG    1 
ATOM   916  S SD    . MET A 1 161 ? 0.169   24.514  8.054   1.00 49.34  ? 133 MET A SD    1 
ATOM   917  C CE    . MET A 1 161 ? -0.353  22.825  7.766   1.00 43.80  ? 133 MET A CE    1 
ATOM   918  N N     . LEU A 1 162 ? -0.874  29.235  9.280   1.00 46.65  ? 134 LEU A N     1 
ATOM   919  C CA    . LEU A 1 162 ? -1.022  30.680  9.153   1.00 38.81  ? 134 LEU A CA    1 
ATOM   920  C C     . LEU A 1 162 ? -1.233  31.348  10.507  1.00 37.85  ? 134 LEU A C     1 
ATOM   921  O O     . LEU A 1 162 ? -2.295  31.923  10.764  1.00 39.04  ? 134 LEU A O     1 
ATOM   922  C CB    . LEU A 1 162 ? -2.184  31.010  8.215   1.00 33.73  ? 134 LEU A CB    1 
ATOM   923  C CG    . LEU A 1 162 ? -2.163  30.280  6.871   1.00 34.22  ? 134 LEU A CG    1 
ATOM   924  C CD1   . LEU A 1 162 ? -3.573  30.118  6.322   1.00 34.49  ? 134 LEU A CD1   1 
ATOM   925  C CD2   . LEU A 1 162 ? -1.267  30.997  5.875   1.00 33.59  ? 134 LEU A CD2   1 
ATOM   926  N N     . MET A 1 163 ? -0.222  31.285  11.373  1.00 38.07  ? 135 MET A N     1 
ATOM   927  C CA    . MET A 1 163 ? -0.302  31.909  12.689  1.00 36.23  ? 135 MET A CA    1 
ATOM   928  C C     . MET A 1 163 ? 0.966   32.628  13.117  1.00 37.81  ? 135 MET A C     1 
ATOM   929  O O     . MET A 1 163 ? 0.904   33.421  14.063  1.00 40.90  ? 135 MET A O     1 
ATOM   930  C CB    . MET A 1 163 ? -0.672  30.866  13.755  1.00 41.26  ? 135 MET A CB    1 
ATOM   931  C CG    . MET A 1 163 ? 0.402   29.818  14.051  1.00 46.83  ? 135 MET A CG    1 
ATOM   932  S SD    . MET A 1 163 ? 1.692   30.327  15.207  1.00 44.14  ? 135 MET A SD    1 
ATOM   933  C CE    . MET A 1 163 ? 0.717   30.697  16.659  1.00 39.82  ? 135 MET A CE    1 
ATOM   934  N N     . LEU A 1 164 ? 2.111   32.395  12.471  1.00 38.43  ? 136 LEU A N     1 
ATOM   935  C CA    . LEU A 1 164 ? 3.354   33.032  12.889  1.00 35.98  ? 136 LEU A CA    1 
ATOM   936  C C     . LEU A 1 164 ? 3.374   34.529  12.611  1.00 36.13  ? 136 LEU A C     1 
ATOM   937  O O     . LEU A 1 164 ? 4.246   35.226  13.140  1.00 37.10  ? 136 LEU A O     1 
ATOM   938  C CB    . LEU A 1 164 ? 4.543   32.356  12.205  1.00 34.68  ? 136 LEU A CB    1 
ATOM   939  C CG    . LEU A 1 164 ? 5.759   32.128  13.104  1.00 34.79  ? 136 LEU A CG    1 
ATOM   940  C CD1   . LEU A 1 164 ? 5.368   31.316  14.328  1.00 34.47  ? 136 LEU A CD1   1 
ATOM   941  C CD2   . LEU A 1 164 ? 6.873   31.438  12.340  1.00 34.37  ? 136 LEU A CD2   1 
ATOM   942  N N     . HIS A 1 165 ? 2.443   35.039  11.802  1.00 36.34  ? 137 HIS A N     1 
ATOM   943  C CA    . HIS A 1 165 ? 2.330   36.476  11.601  1.00 37.85  ? 137 HIS A CA    1 
ATOM   944  C C     . HIS A 1 165 ? 1.602   37.160  12.750  1.00 41.62  ? 137 HIS A C     1 
ATOM   945  O O     . HIS A 1 165 ? 1.720   38.380  12.905  1.00 42.98  ? 137 HIS A O     1 
ATOM   946  C CB    . HIS A 1 165 ? 1.612   36.762  10.282  1.00 37.38  ? 137 HIS A CB    1 
ATOM   947  C CG    . HIS A 1 165 ? 0.200   36.271  10.247  1.00 37.07  ? 137 HIS A CG    1 
ATOM   948  N ND1   . HIS A 1 165 ? -0.132  34.979  9.901   1.00 36.54  ? 137 HIS A ND1   1 
ATOM   949  C CD2   . HIS A 1 165 ? -0.969  36.908  10.491  1.00 37.66  ? 137 HIS A CD2   1 
ATOM   950  C CE1   . HIS A 1 165 ? -1.445  34.835  9.954   1.00 40.51  ? 137 HIS A CE1   1 
ATOM   951  N NE2   . HIS A 1 165 ? -1.976  35.992  10.308  1.00 37.07  ? 137 HIS A NE2   1 
ATOM   952  N N     . LEU A 1 166 ? 0.849   36.403  13.548  1.00 39.30  ? 138 LEU A N     1 
ATOM   953  C CA    . LEU A 1 166 ? 0.252   36.895  14.784  1.00 38.74  ? 138 LEU A CA    1 
ATOM   954  C C     . LEU A 1 166 ? 1.222   36.856  15.958  1.00 43.34  ? 138 LEU A C     1 
ATOM   955  O O     . LEU A 1 166 ? 0.820   37.145  17.089  1.00 48.59  ? 138 LEU A O     1 
ATOM   956  C CB    . LEU A 1 166 ? -1.005  36.084  15.122  1.00 38.84  ? 138 LEU A CB    1 
ATOM   957  C CG    . LEU A 1 166 ? -2.372  36.715  14.834  1.00 43.18  ? 138 LEU A CG    1 
ATOM   958  C CD1   . LEU A 1 166 ? -2.451  37.240  13.418  1.00 48.34  ? 138 LEU A CD1   1 
ATOM   959  C CD2   . LEU A 1 166 ? -3.488  35.717  15.088  1.00 42.64  ? 138 LEU A CD2   1 
ATOM   960  N N     . VAL A 1 167 ? 2.482   36.508  15.722  1.00 40.47  ? 139 VAL A N     1 
ATOM   961  C CA    . VAL A 1 167 ? 3.480   36.431  16.785  1.00 42.08  ? 139 VAL A CA    1 
ATOM   962  C C     . VAL A 1 167 ? 4.544   37.493  16.537  1.00 47.63  ? 139 VAL A C     1 
ATOM   963  O O     . VAL A 1 167 ? 5.327   37.368  15.586  1.00 50.13  ? 139 VAL A O     1 
ATOM   964  C CB    . VAL A 1 167 ? 4.099   35.030  16.867  1.00 41.40  ? 139 VAL A CB    1 
ATOM   965  C CG1   . VAL A 1 167 ? 5.113   34.968  17.994  1.00 48.88  ? 139 VAL A CG1   1 
ATOM   966  C CG2   . VAL A 1 167 ? 3.008   33.984  17.056  1.00 38.17  ? 139 VAL A CG2   1 
ATOM   967  N N     . PRO A 1 168 ? 4.600   38.556  17.344  1.00 47.39  ? 140 PRO A N     1 
ATOM   968  C CA    . PRO A 1 168 ? 5.627   39.586  17.113  1.00 49.65  ? 140 PRO A CA    1 
ATOM   969  C C     . PRO A 1 168 ? 7.045   39.070  17.283  1.00 58.28  ? 140 PRO A C     1 
ATOM   970  O O     . PRO A 1 168 ? 7.943   39.469  16.530  1.00 61.39  ? 140 PRO A O     1 
ATOM   971  C CB    . PRO A 1 168 ? 5.286   40.657  18.159  1.00 49.47  ? 140 PRO A CB    1 
ATOM   972  C CG    . PRO A 1 168 ? 3.840   40.446  18.462  1.00 46.41  ? 140 PRO A CG    1 
ATOM   973  C CD    . PRO A 1 168 ? 3.625   38.965  18.369  1.00 49.25  ? 140 PRO A CD    1 
ATOM   974  N N     . ASP A 1 169 ? 7.272   38.190  18.255  1.00 56.24  ? 141 ASP A N     1 
ATOM   975  C CA    . ASP A 1 169 ? 8.599   37.644  18.539  1.00 56.79  ? 141 ASP A CA    1 
ATOM   976  C C     . ASP A 1 169 ? 8.707   36.298  17.827  1.00 56.61  ? 141 ASP A C     1 
ATOM   977  O O     . ASP A 1 169 ? 8.367   35.252  18.380  1.00 58.19  ? 141 ASP A O     1 
ATOM   978  C CB    . ASP A 1 169 ? 8.814   37.512  20.043  1.00 60.34  ? 141 ASP A CB    1 
ATOM   979  C CG    . ASP A 1 169 ? 10.269  37.278  20.411  1.00 62.41  ? 141 ASP A CG    1 
ATOM   980  O OD1   . ASP A 1 169 ? 11.056  36.869  19.532  1.00 60.11  ? 141 ASP A OD1   1 
ATOM   981  O OD2   . ASP A 1 169 ? 10.622  37.497  21.590  1.00 62.14  ? 141 ASP A OD2   1 
ATOM   982  N N     . ASN A 1 170 ? 9.195   36.330  16.585  1.00 54.47  ? 142 ASN A N     1 
ATOM   983  C CA    . ASN A 1 170 ? 9.285   35.101  15.803  1.00 53.27  ? 142 ASN A CA    1 
ATOM   984  C C     . ASN A 1 170 ? 10.392  34.188  16.315  1.00 52.97  ? 142 ASN A C     1 
ATOM   985  O O     . ASN A 1 170 ? 10.207  32.968  16.389  1.00 51.62  ? 142 ASN A O     1 
ATOM   986  C CB    . ASN A 1 170 ? 9.504   35.425  14.326  1.00 51.90  ? 142 ASN A CB    1 
ATOM   987  C CG    . ASN A 1 170 ? 8.203   35.626  13.575  1.00 50.31  ? 142 ASN A CG    1 
ATOM   988  O OD1   . ASN A 1 170 ? 7.317   36.348  14.027  1.00 54.52  ? 142 ASN A OD1   1 
ATOM   989  N ND2   . ASN A 1 170 ? 8.079   34.977  12.424  1.00 43.02  ? 142 ASN A ND2   1 
ATOM   990  N N     . ARG A 1 171 ? 11.548  34.754  16.671  1.00 52.13  ? 143 ARG A N     1 
ATOM   991  C CA    . ARG A 1 171 ? 12.672  33.918  17.081  1.00 55.45  ? 143 ARG A CA    1 
ATOM   992  C C     . ARG A 1 171 ? 12.365  33.167  18.371  1.00 54.82  ? 143 ARG A C     1 
ATOM   993  O O     . ARG A 1 171 ? 12.784  32.016  18.541  1.00 56.09  ? 143 ARG A O     1 
ATOM   994  C CB    . ARG A 1 171 ? 13.938  34.764  17.231  1.00 58.31  ? 143 ARG A CB    1 
ATOM   995  C CG    . ARG A 1 171 ? 15.153  33.973  17.699  1.00 56.33  ? 143 ARG A CG    1 
ATOM   996  C CD    . ARG A 1 171 ? 16.446  34.513  17.111  1.00 52.12  ? 143 ARG A CD    1 
ATOM   997  N NE    . ARG A 1 171 ? 16.330  35.899  16.678  1.00 62.48  ? 143 ARG A NE    1 
ATOM   998  C CZ    . ARG A 1 171 ? 16.913  36.391  15.594  1.00 71.37  ? 143 ARG A CZ    1 
ATOM   999  N NH1   . ARG A 1 171 ? 17.662  35.634  14.810  1.00 68.43  ? 143 ARG A NH1   1 
ATOM   1000 N NH2   . ARG A 1 171 ? 16.736  37.674  15.288  1.00 75.66  ? 143 ARG A NH2   1 
ATOM   1001 N N     . LEU A 1 172 ? 11.625  33.793  19.291  1.00 52.37  ? 144 LEU A N     1 
ATOM   1002 C CA    . LEU A 1 172 ? 11.220  33.084  20.500  1.00 51.89  ? 144 LEU A CA    1 
ATOM   1003 C C     . LEU A 1 172 ? 10.280  31.931  20.173  1.00 46.34  ? 144 LEU A C     1 
ATOM   1004 O O     . LEU A 1 172 ? 10.318  30.889  20.838  1.00 43.07  ? 144 LEU A O     1 
ATOM   1005 C CB    . LEU A 1 172 ? 10.560  34.056  21.480  1.00 52.78  ? 144 LEU A CB    1 
ATOM   1006 C CG    . LEU A 1 172 ? 9.980   33.478  22.775  1.00 46.98  ? 144 LEU A CG    1 
ATOM   1007 C CD1   . LEU A 1 172 ? 11.004  32.616  23.500  1.00 39.37  ? 144 LEU A CD1   1 
ATOM   1008 C CD2   . LEU A 1 172 ? 9.471   34.589  23.680  1.00 50.04  ? 144 LEU A CD2   1 
ATOM   1009 N N     . ALA A 1 173 ? 9.443   32.090  19.145  1.00 47.55  ? 145 ALA A N     1 
ATOM   1010 C CA    . ALA A 1 173 ? 8.535   31.015  18.763  1.00 43.97  ? 145 ALA A CA    1 
ATOM   1011 C C     . ALA A 1 173 ? 9.280   29.880  18.070  1.00 49.65  ? 145 ALA A C     1 
ATOM   1012 O O     . ALA A 1 173 ? 8.940   28.706  18.255  1.00 45.50  ? 145 ALA A O     1 
ATOM   1013 C CB    . ALA A 1 173 ? 7.422   31.559  17.869  1.00 43.33  ? 145 ALA A CB    1 
ATOM   1014 N N     . VAL A 1 174 ? 10.298  30.207  17.267  1.00 48.12  ? 146 VAL A N     1 
ATOM   1015 C CA    . VAL A 1 174 ? 11.113  29.166  16.645  1.00 40.82  ? 146 VAL A CA    1 
ATOM   1016 C C     . VAL A 1 174 ? 11.920  28.416  17.698  1.00 43.22  ? 146 VAL A C     1 
ATOM   1017 O O     . VAL A 1 174 ? 12.140  27.204  17.576  1.00 42.94  ? 146 VAL A O     1 
ATOM   1018 C CB    . VAL A 1 174 ? 12.018  29.773  15.557  1.00 41.42  ? 146 VAL A CB    1 
ATOM   1019 C CG1   . VAL A 1 174 ? 12.823  28.687  14.859  1.00 45.22  ? 146 VAL A CG1   1 
ATOM   1020 C CG2   . VAL A 1 174 ? 11.189  30.551  14.545  1.00 47.33  ? 146 VAL A CG2   1 
ATOM   1021 N N     . LYS A 1 175 ? 12.370  29.112  18.746  1.00 43.90  ? 147 LYS A N     1 
ATOM   1022 C CA    . LYS A 1 175 ? 13.066  28.452  19.849  1.00 40.70  ? 147 LYS A CA    1 
ATOM   1023 C C     . LYS A 1 175 ? 12.179  27.404  20.509  1.00 44.53  ? 147 LYS A C     1 
ATOM   1024 O O     . LYS A 1 175 ? 12.566  26.238  20.649  1.00 47.30  ? 147 LYS A O     1 
ATOM   1025 C CB    . LYS A 1 175 ? 13.512  29.483  20.886  1.00 39.07  ? 147 LYS A CB    1 
ATOM   1026 C CG    . LYS A 1 175 ? 14.685  30.346  20.483  1.00 43.10  ? 147 LYS A CG    1 
ATOM   1027 C CD    . LYS A 1 175 ? 15.610  30.594  21.668  1.00 42.70  ? 147 LYS A CD    1 
ATOM   1028 C CE    . LYS A 1 175 ? 16.380  31.898  21.505  1.00 44.69  ? 147 LYS A CE    1 
ATOM   1029 N NZ    . LYS A 1 175 ? 17.351  31.830  20.377  1.00 51.39  ? 147 LYS A NZ    1 
ATOM   1030 N N     . ASN A 1 176 ? 10.985  27.815  20.942  1.00 42.77  ? 148 ASN A N     1 
ATOM   1031 C CA    . ASN A 1 176 ? 10.085  26.904  21.639  1.00 41.88  ? 148 ASN A CA    1 
ATOM   1032 C C     . ASN A 1 176 ? 9.671   25.730  20.761  1.00 38.90  ? 148 ASN A C     1 
ATOM   1033 O O     . ASN A 1 176 ? 9.461   24.621  21.266  1.00 40.70  ? 148 ASN A O     1 
ATOM   1034 C CB    . ASN A 1 176 ? 8.860   27.673  22.134  1.00 41.84  ? 148 ASN A CB    1 
ATOM   1035 C CG    . ASN A 1 176 ? 9.167   28.539  23.346  1.00 41.37  ? 148 ASN A CG    1 
ATOM   1036 O OD1   . ASN A 1 176 ? 10.227  28.409  23.961  1.00 43.06  ? 148 ASN A OD1   1 
ATOM   1037 N ND2   . ASN A 1 176 ? 8.242   29.424  23.695  1.00 42.65  ? 148 ASN A ND2   1 
ATOM   1038 N N     . ILE A 1 177 ? 9.545   25.951  19.452  1.00 35.36  ? 149 ILE A N     1 
ATOM   1039 C CA    . ILE A 1 177 ? 9.318   24.840  18.534  1.00 38.18  ? 149 ILE A CA    1 
ATOM   1040 C C     . ILE A 1 177 ? 10.552  23.945  18.477  1.00 44.84  ? 149 ILE A C     1 
ATOM   1041 O O     . ILE A 1 177 ? 10.443  22.718  18.359  1.00 51.11  ? 149 ILE A O     1 
ATOM   1042 C CB    . ILE A 1 177 ? 8.928   25.377  17.144  1.00 35.52  ? 149 ILE A CB    1 
ATOM   1043 C CG1   . ILE A 1 177 ? 7.536   26.011  17.186  1.00 32.58  ? 149 ILE A CG1   1 
ATOM   1044 C CG2   . ILE A 1 177 ? 8.958   24.274  16.096  1.00 33.79  ? 149 ILE A CG2   1 
ATOM   1045 C CD1   . ILE A 1 177 ? 7.169   26.763  15.923  1.00 34.42  ? 149 ILE A CD1   1 
ATOM   1046 N N     . HIS A 1 178 ? 11.745  24.541  18.574  1.00 46.10  ? 150 HIS A N     1 
ATOM   1047 C CA    . HIS A 1 178 ? 12.972  23.751  18.585  1.00 45.70  ? 150 HIS A CA    1 
ATOM   1048 C C     . HIS A 1 178 ? 13.093  22.916  19.855  1.00 47.43  ? 150 HIS A C     1 
ATOM   1049 O O     . HIS A 1 178 ? 13.661  21.819  19.819  1.00 48.66  ? 150 HIS A O     1 
ATOM   1050 C CB    . HIS A 1 178 ? 14.189  24.667  18.424  1.00 44.63  ? 150 HIS A CB    1 
ATOM   1051 C CG    . HIS A 1 178 ? 15.494  23.936  18.336  1.00 47.30  ? 150 HIS A CG    1 
ATOM   1052 N ND1   . HIS A 1 178 ? 16.251  23.628  19.446  1.00 49.57  ? 150 HIS A ND1   1 
ATOM   1053 C CD2   . HIS A 1 178 ? 16.178  23.455  17.270  1.00 48.33  ? 150 HIS A CD2   1 
ATOM   1054 C CE1   . HIS A 1 178 ? 17.344  22.989  19.068  1.00 53.29  ? 150 HIS A CE1   1 
ATOM   1055 N NE2   . HIS A 1 178 ? 17.323  22.869  17.753  1.00 53.48  ? 150 HIS A NE2   1 
ATOM   1056 N N     . LYS A 1 179 ? 12.568  23.412  20.980  1.00 46.55  ? 151 LYS A N     1 
ATOM   1057 C CA    . LYS A 1 179 ? 12.552  22.612  22.202  1.00 44.91  ? 151 LYS A CA    1 
ATOM   1058 C C     . LYS A 1 179 ? 11.607  21.424  22.085  1.00 43.62  ? 151 LYS A C     1 
ATOM   1059 O O     . LYS A 1 179 ? 11.881  20.357  22.646  1.00 45.21  ? 151 LYS A O     1 
ATOM   1060 C CB    . LYS A 1 179 ? 12.143  23.470  23.400  1.00 44.75  ? 151 LYS A CB    1 
ATOM   1061 C CG    . LYS A 1 179 ? 13.173  24.482  23.866  1.00 45.85  ? 151 LYS A CG    1 
ATOM   1062 C CD    . LYS A 1 179 ? 12.652  25.232  25.085  1.00 51.27  ? 151 LYS A CD    1 
ATOM   1063 C CE    . LYS A 1 179 ? 13.649  26.258  25.593  1.00 63.75  ? 151 LYS A CE    1 
ATOM   1064 N NZ    . LYS A 1 179 ? 13.114  27.001  26.770  1.00 69.21  ? 151 LYS A NZ    1 
ATOM   1065 N N     . LEU A 1 180 ? 10.497  21.588  21.364  1.00 43.57  ? 152 LEU A N     1 
ATOM   1066 C CA    . LEU A 1 180 ? 9.455   20.571  21.312  1.00 33.07  ? 152 LEU A CA    1 
ATOM   1067 C C     . LEU A 1 180 ? 9.775   19.433  20.353  1.00 40.94  ? 152 LEU A C     1 
ATOM   1068 O O     . LEU A 1 180 ? 9.146   18.373  20.441  1.00 39.70  ? 152 LEU A O     1 
ATOM   1069 C CB    . LEU A 1 180 ? 8.125   21.214  20.913  1.00 33.66  ? 152 LEU A CB    1 
ATOM   1070 C CG    . LEU A 1 180 ? 7.442   22.069  21.981  1.00 33.82  ? 152 LEU A CG    1 
ATOM   1071 C CD1   . LEU A 1 180 ? 6.392   22.969  21.355  1.00 33.10  ? 152 LEU A CD1   1 
ATOM   1072 C CD2   . LEU A 1 180 ? 6.818   21.183  23.044  1.00 39.62  ? 152 LEU A CD2   1 
ATOM   1073 N N     . LEU A 1 181 ? 10.728  19.622  19.446  1.00 38.33  ? 153 LEU A N     1 
ATOM   1074 C CA    . LEU A 1 181 ? 11.031  18.625  18.430  1.00 42.80  ? 153 LEU A CA    1 
ATOM   1075 C C     . LEU A 1 181 ? 12.117  17.673  18.909  1.00 42.83  ? 153 LEU A C     1 
ATOM   1076 O O     . LEU A 1 181 ? 13.052  18.076  19.608  1.00 41.13  ? 153 LEU A O     1 
ATOM   1077 C CB    . LEU A 1 181 ? 11.472  19.299  17.130  1.00 41.94  ? 153 LEU A CB    1 
ATOM   1078 C CG    . LEU A 1 181 ? 10.376  19.981  16.313  1.00 39.14  ? 153 LEU A CG    1 
ATOM   1079 C CD1   . LEU A 1 181 ? 10.982  20.888  15.256  1.00 43.07  ? 153 LEU A CD1   1 
ATOM   1080 C CD2   . LEU A 1 181 ? 9.474   18.940  15.675  1.00 43.79  ? 153 LEU A CD2   1 
ATOM   1081 N N     . VAL A 1 182 ? 11.983  16.406  18.532  1.00 45.91  ? 154 VAL A N     1 
ATOM   1082 C CA    . VAL A 1 182 ? 13.046  15.426  18.735  1.00 43.82  ? 154 VAL A CA    1 
ATOM   1083 C C     . VAL A 1 182 ? 14.164  15.763  17.756  1.00 45.46  ? 154 VAL A C     1 
ATOM   1084 O O     . VAL A 1 182 ? 13.892  16.313  16.679  1.00 45.45  ? 154 VAL A O     1 
ATOM   1085 C CB    . VAL A 1 182 ? 12.540  13.987  18.537  1.00 36.35  ? 154 VAL A CB    1 
ATOM   1086 C CG1   . VAL A 1 182 ? 11.479  13.649  19.564  1.00 36.51  ? 154 VAL A CG1   1 
ATOM   1087 C CG2   . VAL A 1 182 ? 11.994  13.801  17.131  1.00 35.44  ? 154 VAL A CG2   1 
ATOM   1088 N N     . PRO A 1 183 ? 15.425  15.491  18.093  1.00 40.39  ? 155 PRO A N     1 
ATOM   1089 C CA    . PRO A 1 183 ? 16.506  15.686  17.116  1.00 40.78  ? 155 PRO A CA    1 
ATOM   1090 C C     . PRO A 1 183 ? 16.234  14.893  15.847  1.00 43.99  ? 155 PRO A C     1 
ATOM   1091 O O     . PRO A 1 183 ? 16.075  13.671  15.878  1.00 50.33  ? 155 PRO A O     1 
ATOM   1092 C CB    . PRO A 1 183 ? 17.744  15.174  17.859  1.00 42.98  ? 155 PRO A CB    1 
ATOM   1093 C CG    . PRO A 1 183 ? 17.422  15.397  19.292  1.00 48.48  ? 155 PRO A CG    1 
ATOM   1094 C CD    . PRO A 1 183 ? 15.943  15.143  19.426  1.00 45.17  ? 155 PRO A CD    1 
ATOM   1095 N N     . GLY A 1 184 ? 16.171  15.604  14.725  1.00 46.94  ? 156 GLY A N     1 
ATOM   1096 C CA    . GLY A 1 184 ? 15.760  15.029  13.465  1.00 45.28  ? 156 GLY A CA    1 
ATOM   1097 C C     . GLY A 1 184 ? 14.306  15.262  13.118  1.00 50.04  ? 156 GLY A C     1 
ATOM   1098 O O     . GLY A 1 184 ? 13.897  14.955  11.991  1.00 55.11  ? 156 GLY A O     1 
ATOM   1099 N N     . GLY A 1 185 ? 13.516  15.788  14.051  1.00 48.84  ? 157 GLY A N     1 
ATOM   1100 C CA    . GLY A 1 185 ? 12.131  16.091  13.753  1.00 47.02  ? 157 GLY A CA    1 
ATOM   1101 C C     . GLY A 1 185 ? 12.000  17.297  12.845  1.00 41.40  ? 157 GLY A C     1 
ATOM   1102 O O     . GLY A 1 185 ? 12.863  18.173  12.798  1.00 46.31  ? 157 GLY A O     1 
ATOM   1103 N N     . GLU A 1 186 ? 10.891  17.344  12.116  1.00 45.60  ? 158 GLU A N     1 
ATOM   1104 C CA    . GLU A 1 186 ? 10.670  18.357  11.097  1.00 48.32  ? 158 GLU A CA    1 
ATOM   1105 C C     . GLU A 1 186 ? 9.601   19.349  11.535  1.00 45.01  ? 158 GLU A C     1 
ATOM   1106 O O     . GLU A 1 186 ? 8.720   19.032  12.340  1.00 42.32  ? 158 GLU A O     1 
ATOM   1107 C CB    . GLU A 1 186 ? 10.265  17.713  9.768   1.00 49.89  ? 158 GLU A CB    1 
ATOM   1108 C CG    . GLU A 1 186 ? 11.288  16.727  9.229   1.00 52.53  ? 158 GLU A CG    1 
ATOM   1109 C CD    . GLU A 1 186 ? 10.743  15.875  8.100   1.00 57.72  ? 158 GLU A CD    1 
ATOM   1110 O OE1   . GLU A 1 186 ? 9.571   15.452  8.187   1.00 58.67  ? 158 GLU A OE1   1 
ATOM   1111 O OE2   . GLU A 1 186 ? 11.486  15.625  7.128   1.00 59.28  ? 158 GLU A OE2   1 
ATOM   1112 N N     . ALA A 1 187 ? 9.690   20.561  10.989  1.00 42.14  ? 159 ALA A N     1 
ATOM   1113 C CA    . ALA A 1 187 ? 8.716   21.615  11.228  1.00 35.43  ? 159 ALA A CA    1 
ATOM   1114 C C     . ALA A 1 187 ? 8.228   22.152  9.891   1.00 36.94  ? 159 ALA A C     1 
ATOM   1115 O O     . ALA A 1 187 ? 9.022   22.348  8.965   1.00 38.62  ? 159 ALA A O     1 
ATOM   1116 C CB    . ALA A 1 187 ? 9.311   22.752  12.067  1.00 34.45  ? 159 ALA A CB    1 
ATOM   1117 N N     . VAL A 1 188 ? 6.923   22.382  9.790   1.00 34.21  ? 160 VAL A N     1 
ATOM   1118 C CA    . VAL A 1 188 ? 6.293   22.856  8.563   1.00 29.74  ? 160 VAL A CA    1 
ATOM   1119 C C     . VAL A 1 188 ? 5.690   24.223  8.854   1.00 39.04  ? 160 VAL A C     1 
ATOM   1120 O O     . VAL A 1 188 ? 4.760   24.339  9.662   1.00 39.15  ? 160 VAL A O     1 
ATOM   1121 C CB    . VAL A 1 188 ? 5.228   21.881  8.047   1.00 29.30  ? 160 VAL A CB    1 
ATOM   1122 C CG1   . VAL A 1 188 ? 4.501   22.471  6.849   1.00 31.64  ? 160 VAL A CG1   1 
ATOM   1123 C CG2   . VAL A 1 188 ? 5.862   20.546  7.691   1.00 28.92  ? 160 VAL A CG2   1 
ATOM   1124 N N     . PHE A 1 189 ? 6.214   25.254  8.199   1.00 37.18  ? 161 PHE A N     1 
ATOM   1125 C CA    . PHE A 1 189 ? 5.756   26.622  8.395   1.00 37.81  ? 161 PHE A CA    1 
ATOM   1126 C C     . PHE A 1 189 ? 4.902   27.076  7.219   1.00 40.59  ? 161 PHE A C     1 
ATOM   1127 O O     . PHE A 1 189 ? 5.182   26.739  6.065   1.00 43.06  ? 161 PHE A O     1 
ATOM   1128 C CB    . PHE A 1 189 ? 6.938   27.578  8.570   1.00 35.60  ? 161 PHE A CB    1 
ATOM   1129 C CG    . PHE A 1 189 ? 7.762   27.308  9.795   1.00 36.33  ? 161 PHE A CG    1 
ATOM   1130 C CD1   . PHE A 1 189 ? 8.840   26.439  9.745   1.00 38.39  ? 161 PHE A CD1   1 
ATOM   1131 C CD2   . PHE A 1 189 ? 7.459   27.926  10.997  1.00 35.91  ? 161 PHE A CD2   1 
ATOM   1132 C CE1   . PHE A 1 189 ? 9.600   26.191  10.872  1.00 41.20  ? 161 PHE A CE1   1 
ATOM   1133 C CE2   . PHE A 1 189 ? 8.215   27.682  12.128  1.00 38.77  ? 161 PHE A CE2   1 
ATOM   1134 C CZ    . PHE A 1 189 ? 9.287   26.814  12.066  1.00 42.21  ? 161 PHE A CZ    1 
ATOM   1135 N N     . SER A 1 190 ? 3.855   27.842  7.526   1.00 39.62  ? 162 SER A N     1 
ATOM   1136 C CA    . SER A 1 190 ? 3.014   28.493  6.524   1.00 34.52  ? 162 SER A CA    1 
ATOM   1137 C C     . SER A 1 190 ? 2.867   29.960  6.934   1.00 33.95  ? 162 SER A C     1 
ATOM   1138 O O     . SER A 1 190 ? 1.779   30.429  7.274   1.00 37.67  ? 162 SER A O     1 
ATOM   1139 C CB    . SER A 1 190 ? 1.660   27.796  6.393   1.00 41.28  ? 162 SER A CB    1 
ATOM   1140 O OG    . SER A 1 190 ? 0.896   28.356  5.339   1.00 40.92  ? 162 SER A OG    1 
ATOM   1141 N N     . VAL A 1 191 ? 3.982   30.681  6.906   1.00 33.20  ? 163 VAL A N     1 
ATOM   1142 C CA    . VAL A 1 191 ? 4.030   32.057  7.384   1.00 34.02  ? 163 VAL A CA    1 
ATOM   1143 C C     . VAL A 1 191 ? 3.500   32.992  6.308   1.00 34.56  ? 163 VAL A C     1 
ATOM   1144 O O     . VAL A 1 191 ? 3.815   32.844  5.121   1.00 37.14  ? 163 VAL A O     1 
ATOM   1145 C CB    . VAL A 1 191 ? 5.467   32.432  7.788   1.00 34.37  ? 163 VAL A CB    1 
ATOM   1146 C CG1   . VAL A 1 191 ? 5.511   33.831  8.385   1.00 35.30  ? 163 VAL A CG1   1 
ATOM   1147 C CG2   . VAL A 1 191 ? 6.024   31.408  8.761   1.00 35.49  ? 163 VAL A CG2   1 
ATOM   1148 N N     . ILE A 1 192 ? 2.687   33.960  6.720   1.00 35.17  ? 164 ILE A N     1 
ATOM   1149 C CA    . ILE A 1 192 ? 2.209   35.008  5.825   1.00 35.86  ? 164 ILE A CA    1 
ATOM   1150 C C     . ILE A 1 192 ? 3.254   36.117  5.811   1.00 36.64  ? 164 ILE A C     1 
ATOM   1151 O O     . ILE A 1 192 ? 3.466   36.797  6.818   1.00 37.16  ? 164 ILE A O     1 
ATOM   1152 C CB    . ILE A 1 192 ? 0.836   35.538  6.252   1.00 36.26  ? 164 ILE A CB    1 
ATOM   1153 C CG1   . ILE A 1 192 ? -0.235  34.466  6.049   1.00 35.61  ? 164 ILE A CG1   1 
ATOM   1154 C CG2   . ILE A 1 192 ? 0.487   36.794  5.473   1.00 37.17  ? 164 ILE A CG2   1 
ATOM   1155 C CD1   . ILE A 1 192 ? -1.604  34.863  6.551   1.00 36.01  ? 164 ILE A CD1   1 
ATOM   1156 N N     . ALA A 1 193 ? 3.916   36.292  4.667   1.00 40.12  ? 165 ALA A N     1 
ATOM   1157 C CA    . ALA A 1 193 ? 4.940   37.319  4.522   1.00 39.18  ? 165 ALA A CA    1 
ATOM   1158 C C     . ALA A 1 193 ? 4.332   38.707  4.659   1.00 45.26  ? 165 ALA A C     1 
ATOM   1159 O O     . ALA A 1 193 ? 4.621   39.428  5.619   1.00 52.18  ? 165 ALA A O     1 
ATOM   1160 C CB    . ALA A 1 193 ? 5.650   37.184  3.174   1.00 43.85  ? 165 ALA A CB    1 
ATOM   1161 N N     . ASN A 1 194 ? 3.485   39.084  3.705   1.00 47.22  ? 166 ASN A N     1 
ATOM   1162 C CA    . ASN A 1 194 ? 2.846   40.390  3.711   1.00 44.75  ? 166 ASN A CA    1 
ATOM   1163 C C     . ASN A 1 194 ? 1.421   40.257  3.197   1.00 43.36  ? 166 ASN A C     1 
ATOM   1164 O O     . ASN A 1 194 ? 1.078   39.307  2.489   1.00 44.95  ? 166 ASN A O     1 
ATOM   1165 C CB    . ASN A 1 194 ? 3.625   41.403  2.860   1.00 47.64  ? 166 ASN A CB    1 
ATOM   1166 C CG    . ASN A 1 194 ? 3.593   41.070  1.380   1.00 53.78  ? 166 ASN A CG    1 
ATOM   1167 O OD1   . ASN A 1 194 ? 2.603   41.324  0.694   1.00 54.25  ? 166 ASN A OD1   1 
ATOM   1168 N ND2   . ASN A 1 194 ? 4.681   40.493  0.880   1.00 56.41  ? 166 ASN A ND2   1 
ATOM   1169 N N     . MET A 1 195 ? 0.592   41.231  3.563   1.00 49.45  ? 167 MET A N     1 
ATOM   1170 C CA    . MET A 1 195 ? -0.779  41.291  3.078   1.00 53.38  ? 167 MET A CA    1 
ATOM   1171 C C     . MET A 1 195 ? -1.309  42.697  3.311   1.00 52.84  ? 167 MET A C     1 
ATOM   1172 O O     . MET A 1 195 ? -0.767  43.457  4.117   1.00 52.68  ? 167 MET A O     1 
ATOM   1173 C CB    . MET A 1 195 ? -1.672  40.255  3.767   1.00 42.90  ? 167 MET A CB    1 
ATOM   1174 C CG    . MET A 1 195 ? -1.509  40.189  5.274   1.00 45.34  ? 167 MET A CG    1 
ATOM   1175 S SD    . MET A 1 195 ? -2.434  38.812  5.974   1.00 50.42  ? 167 MET A SD    1 
ATOM   1176 C CE    . MET A 1 195 ? -3.902  38.849  4.952   1.00 43.35  ? 167 MET A CE    1 
ATOM   1177 N N     . ALA A 1 196 ? -2.384  43.031  2.595   1.00 46.51  ? 168 ALA A N     1 
ATOM   1178 C CA    . ALA A 1 196 ? -2.957  44.366  2.702   1.00 50.51  ? 168 ALA A CA    1 
ATOM   1179 C C     . ALA A 1 196 ? -3.651  44.600  4.037   1.00 52.53  ? 168 ALA A C     1 
ATOM   1180 O O     . ALA A 1 196 ? -3.879  45.757  4.406   1.00 55.54  ? 168 ALA A O     1 
ATOM   1181 C CB    . ALA A 1 196 ? -3.936  44.615  1.556   1.00 52.32  ? 168 ALA A CB    1 
ATOM   1182 N N     . LEU A 1 197 ? -3.998  43.534  4.767   1.00 48.09  ? 169 LEU A N     1 
ATOM   1183 C CA    . LEU A 1 197 ? -4.575  43.719  6.095   1.00 49.29  ? 169 LEU A CA    1 
ATOM   1184 C C     . LEU A 1 197 ? -3.597  44.422  7.026   1.00 55.32  ? 169 LEU A C     1 
ATOM   1185 O O     . LEU A 1 197 ? -4.011  45.207  7.887   1.00 55.86  ? 169 LEU A O     1 
ATOM   1186 C CB    . LEU A 1 197 ? -4.988  42.375  6.702   1.00 49.36  ? 169 LEU A CB    1 
ATOM   1187 C CG    . LEU A 1 197 ? -6.081  41.512  6.066   1.00 43.68  ? 169 LEU A CG    1 
ATOM   1188 C CD1   . LEU A 1 197 ? -6.394  40.317  6.961   1.00 45.18  ? 169 LEU A CD1   1 
ATOM   1189 C CD2   . LEU A 1 197 ? -7.338  42.292  5.772   1.00 45.59  ? 169 LEU A CD2   1 
ATOM   1190 N N     . CYS A 1 198 ? -2.299  44.154  6.866   1.00 56.08  ? 170 CYS A N     1 
ATOM   1191 C CA    . CYS A 1 198 ? -1.299  44.761  7.738   1.00 56.58  ? 170 CYS A CA    1 
ATOM   1192 C C     . CYS A 1 198 ? -1.132  46.246  7.444   1.00 57.65  ? 170 CYS A C     1 
ATOM   1193 O O     . CYS A 1 198 ? -1.023  47.059  8.370   1.00 57.39  ? 170 CYS A O     1 
ATOM   1194 C CB    . CYS A 1 198 ? 0.035   44.033  7.585   1.00 58.06  ? 170 CYS A CB    1 
ATOM   1195 S SG    . CYS A 1 198 ? 0.083   42.380  8.314   1.00 62.88  ? 170 CYS A SG    1 
ATOM   1196 N N     . ASP A 1 199 ? -1.101  46.621  6.162   1.00 59.49  ? 171 ASP A N     1 
ATOM   1197 C CA    . ASP A 1 199 ? -0.964  48.031  5.811   1.00 57.61  ? 171 ASP A CA    1 
ATOM   1198 C C     . ASP A 1 199 ? -2.206  48.820  6.203   1.00 58.23  ? 171 ASP A C     1 
ATOM   1199 O O     . ASP A 1 199 ? -2.105  49.980  6.619   1.00 58.55  ? 171 ASP A O     1 
ATOM   1200 C CB    . ASP A 1 199 ? -0.680  48.177  4.317   1.00 57.86  ? 171 ASP A CB    1 
ATOM   1201 C CG    . ASP A 1 199 ? 0.647   47.567  3.915   1.00 66.27  ? 171 ASP A CG    1 
ATOM   1202 O OD1   . ASP A 1 199 ? 1.608   47.658  4.709   1.00 64.76  ? 171 ASP A OD1   1 
ATOM   1203 O OD2   . ASP A 1 199 ? 0.730   46.997  2.806   1.00 69.75  ? 171 ASP A OD2   1 
ATOM   1204 N N     . ALA A 1 200 ? -3.387  48.208  6.077   1.00 54.78  ? 172 ALA A N     1 
ATOM   1205 C CA    . ALA A 1 200 ? -4.607  48.859  6.541   1.00 52.75  ? 172 ALA A CA    1 
ATOM   1206 C C     . ALA A 1 200 ? -4.559  49.119  8.039   1.00 53.32  ? 172 ALA A C     1 
ATOM   1207 O O     . ALA A 1 200 ? -5.167  50.081  8.523   1.00 54.04  ? 172 ALA A O     1 
ATOM   1208 C CB    . ALA A 1 200 ? -5.827  48.011  6.183   1.00 51.23  ? 172 ALA A CB    1 
ATOM   1209 N N     . TYR A 1 201 ? -3.843  48.278  8.787   1.00 56.72  ? 173 TYR A N     1 
ATOM   1210 C CA    . TYR A 1 201 ? -3.641  48.537  10.208  1.00 55.32  ? 173 TYR A CA    1 
ATOM   1211 C C     . TYR A 1 201 ? -2.743  49.750  10.417  1.00 55.95  ? 173 TYR A C     1 
ATOM   1212 O O     . TYR A 1 201 ? -3.037  50.618  11.247  1.00 58.22  ? 173 TYR A O     1 
ATOM   1213 C CB    . TYR A 1 201 ? -3.039  47.305  10.888  1.00 53.23  ? 173 TYR A CB    1 
ATOM   1214 C CG    . TYR A 1 201 ? -4.048  46.252  11.292  1.00 50.57  ? 173 TYR A CG    1 
ATOM   1215 C CD1   . TYR A 1 201 ? -5.390  46.570  11.452  1.00 49.85  ? 173 TYR A CD1   1 
ATOM   1216 C CD2   . TYR A 1 201 ? -3.653  44.940  11.520  1.00 49.38  ? 173 TYR A CD2   1 
ATOM   1217 C CE1   . TYR A 1 201 ? -6.312  45.609  11.824  1.00 47.48  ? 173 TYR A CE1   1 
ATOM   1218 C CE2   . TYR A 1 201 ? -4.567  43.972  11.892  1.00 49.87  ? 173 TYR A CE2   1 
ATOM   1219 C CZ    . TYR A 1 201 ? -5.894  44.312  12.043  1.00 50.37  ? 173 TYR A CZ    1 
ATOM   1220 O OH    . TYR A 1 201 ? -6.805  43.352  12.413  1.00 53.09  ? 173 TYR A OH    1 
ATOM   1221 N N     . GLU A 1 202 ? -1.642  49.831  9.665   1.00 51.82  ? 174 GLU A N     1 
ATOM   1222 C CA    . GLU A 1 202 ? -0.698  50.927  9.852   1.00 53.28  ? 174 GLU A CA    1 
ATOM   1223 C C     . GLU A 1 202 ? -1.278  52.261  9.398   1.00 58.03  ? 174 GLU A C     1 
ATOM   1224 O O     . GLU A 1 202 ? -0.914  53.309  9.943   1.00 60.43  ? 174 GLU A O     1 
ATOM   1225 C CB    . GLU A 1 202 ? 0.605   50.632  9.111   1.00 53.62  ? 174 GLU A CB    1 
ATOM   1226 C CG    . GLU A 1 202 ? 1.441   49.535  9.751   1.00 57.09  ? 174 GLU A CG    1 
ATOM   1227 C CD    . GLU A 1 202 ? 2.577   49.073  8.861   1.00 64.80  ? 174 GLU A CD    1 
ATOM   1228 O OE1   . GLU A 1 202 ? 2.388   49.026  7.627   1.00 67.00  ? 174 GLU A OE1   1 
ATOM   1229 O OE2   . GLU A 1 202 ? 3.662   48.759  9.396   1.00 67.51  ? 174 GLU A OE2   1 
ATOM   1230 N N     . GLU A 1 203 ? -2.174  52.248  8.410   1.00 58.07  ? 175 GLU A N     1 
ATOM   1231 C CA    . GLU A 1 203 ? -2.799  53.495  7.982   1.00 59.54  ? 175 GLU A CA    1 
ATOM   1232 C C     . GLU A 1 203 ? -3.833  53.969  8.996   1.00 60.39  ? 175 GLU A C     1 
ATOM   1233 O O     . GLU A 1 203 ? -3.949  55.172  9.256   1.00 65.66  ? 175 GLU A O     1 
ATOM   1234 C CB    . GLU A 1 203 ? -3.434  53.324  6.603   1.00 59.28  ? 175 GLU A CB    1 
ATOM   1235 C CG    . GLU A 1 203 ? -2.433  53.153  5.472   1.00 61.86  ? 175 GLU A CG    1 
ATOM   1236 C CD    . GLU A 1 203 ? -3.077  53.248  4.100   1.00 67.97  ? 175 GLU A CD    1 
ATOM   1237 O OE1   . GLU A 1 203 ? -4.302  53.481  4.029   1.00 71.23  ? 175 GLU A OE1   1 
ATOM   1238 O OE2   . GLU A 1 203 ? -2.357  53.089  3.092   1.00 71.96  ? 175 GLU A OE2   1 
ATOM   1239 N N     . MET A 1 204 ? -4.588  53.037  9.583   1.00 55.67  ? 176 MET A N     1 
ATOM   1240 C CA    . MET A 1 204 ? -5.567  53.413  10.598  1.00 56.25  ? 176 MET A CA    1 
ATOM   1241 C C     . MET A 1 204 ? -4.896  53.876  11.883  1.00 60.47  ? 176 MET A C     1 
ATOM   1242 O O     . MET A 1 204 ? -5.487  54.650  12.645  1.00 62.76  ? 176 MET A O     1 
ATOM   1243 C CB    . MET A 1 204 ? -6.505  52.241  10.887  1.00 53.18  ? 176 MET A CB    1 
ATOM   1244 C CG    . MET A 1 204 ? -7.456  51.909  9.751   1.00 54.25  ? 176 MET A CG    1 
ATOM   1245 S SD    . MET A 1 204 ? -8.478  50.468  10.102  1.00 51.57  ? 176 MET A SD    1 
ATOM   1246 C CE    . MET A 1 204 ? -9.540  51.115  11.390  1.00 52.85  ? 176 MET A CE    1 
ATOM   1247 N N     . ALA A 1 205 ? -3.667  53.419  12.140  1.00 60.53  ? 177 ALA A N     1 
ATOM   1248 C CA    . ALA A 1 205 ? -2.960  53.810  13.353  1.00 60.56  ? 177 ALA A CA    1 
ATOM   1249 C C     . ALA A 1 205 ? -2.608  55.291  13.371  1.00 63.38  ? 177 ALA A C     1 
ATOM   1250 O O     . ALA A 1 205 ? -2.322  55.833  14.443  1.00 66.43  ? 177 ALA A O     1 
ATOM   1251 C CB    . ALA A 1 205 ? -1.690  52.973  13.515  1.00 58.23  ? 177 ALA A CB    1 
ATOM   1252 N N     . LYS A 1 206 ? -2.621  55.955  12.216  1.00 62.46  ? 178 LYS A N     1 
ATOM   1253 C CA    . LYS A 1 206 ? -2.325  57.378  12.143  1.00 65.82  ? 178 LYS A CA    1 
ATOM   1254 C C     . LYS A 1 206 ? -3.546  58.255  12.384  1.00 73.32  ? 178 LYS A C     1 
ATOM   1255 O O     . LYS A 1 206 ? -3.392  59.472  12.537  1.00 73.31  ? 178 LYS A O     1 
ATOM   1256 C CB    . LYS A 1 206 ? -1.710  57.721  10.782  1.00 62.50  ? 178 LYS A CB    1 
ATOM   1257 C CG    . LYS A 1 206 ? -0.341  57.100  10.551  1.00 63.85  ? 178 LYS A CG    1 
ATOM   1258 C CD    . LYS A 1 206 ? 0.180   57.406  9.157   1.00 66.78  ? 178 LYS A CD    1 
ATOM   1259 C CE    . LYS A 1 206 ? 1.516   56.726  8.907   1.00 57.35  ? 178 LYS A CE    1 
ATOM   1260 N NZ    . LYS A 1 206 ? 1.990   56.929  7.510   1.00 66.29  ? 178 LYS A NZ    1 
ATOM   1261 N N     . GLU A 1 207 ? -4.739  57.678  12.422  1.00 71.88  ? 179 GLU A N     1 
ATOM   1262 C CA    . GLU A 1 207 ? -5.946  58.452  12.694  1.00 73.06  ? 179 GLU A CA    1 
ATOM   1263 C C     . GLU A 1 207 ? -6.004  58.812  14.172  1.00 73.00  ? 179 GLU A C     1 
ATOM   1264 O O     . GLU A 1 207 ? -6.013  57.908  15.017  1.00 75.45  ? 179 GLU A O     1 
ATOM   1265 C CB    . GLU A 1 207 ? -7.192  57.660  12.300  1.00 72.13  ? 179 GLU A CB    1 
ATOM   1266 C CG    . GLU A 1 207 ? -7.306  57.355  10.817  1.00 75.05  ? 179 GLU A CG    1 
ATOM   1267 C CD    . GLU A 1 207 ? -8.606  56.662  10.457  1.00 73.49  ? 179 GLU A CD    1 
ATOM   1268 O OE1   . GLU A 1 207 ? -9.580  56.780  11.230  1.00 70.69  ? 179 GLU A OE1   1 
ATOM   1269 O OE2   . GLU A 1 207 ? -8.654  56.002  9.398   1.00 71.93  ? 179 GLU A OE2   1 
ATOM   1270 N N     . PRO A 1 208 ? -6.036  60.099  14.534  1.00 73.21  ? 180 PRO A N     1 
ATOM   1271 C CA    . PRO A 1 208 ? -6.250  60.451  15.949  1.00 71.49  ? 180 PRO A CA    1 
ATOM   1272 C C     . PRO A 1 208 ? -7.530  59.863  16.509  1.00 69.82  ? 180 PRO A C     1 
ATOM   1273 O O     . PRO A 1 208 ? -7.620  59.612  17.718  1.00 70.23  ? 180 PRO A O     1 
ATOM   1274 C CB    . PRO A 1 208 ? -6.299  61.985  15.922  1.00 76.57  ? 180 PRO A CB    1 
ATOM   1275 C CG    . PRO A 1 208 ? -5.522  62.366  14.706  1.00 73.37  ? 180 PRO A CG    1 
ATOM   1276 C CD    . PRO A 1 208 ? -5.783  61.284  13.696  1.00 70.74  ? 180 PRO A CD    1 
ATOM   1277 N N     . ARG A 1 209 ? -8.529  59.657  15.648  1.00 70.39  ? 181 ARG A N     1 
ATOM   1278 C CA    . ARG A 1 209 ? -9.737  58.924  16.009  1.00 64.42  ? 181 ARG A CA    1 
ATOM   1279 C C     . ARG A 1 209 ? -9.416  57.597  16.685  1.00 63.73  ? 181 ARG A C     1 
ATOM   1280 O O     . ARG A 1 209 ? -10.064 57.218  17.667  1.00 62.20  ? 181 ARG A O     1 
ATOM   1281 C CB    . ARG A 1 209 ? -10.562 58.699  14.744  1.00 66.11  ? 181 ARG A CB    1 
ATOM   1282 C CG    . ARG A 1 209 ? -11.851 57.925  14.887  1.00 62.82  ? 181 ARG A CG    1 
ATOM   1283 C CD    . ARG A 1 209 ? -12.396 57.730  13.487  1.00 62.55  ? 181 ARG A CD    1 
ATOM   1284 N NE    . ARG A 1 209 ? -13.491 56.778  13.380  1.00 64.43  ? 181 ARG A NE    1 
ATOM   1285 C CZ    . ARG A 1 209 ? -13.972 56.343  12.223  1.00 68.78  ? 181 ARG A CZ    1 
ATOM   1286 N NH1   . ARG A 1 209 ? -13.473 56.754  11.069  1.00 65.30  ? 181 ARG A NH1   1 
ATOM   1287 N NH2   . ARG A 1 209 ? -14.975 55.471  12.224  1.00 73.73  ? 181 ARG A NH2   1 
ATOM   1288 N N     . TRP A 1 210 ? -8.419  56.877  16.173  1.00 68.13  ? 182 TRP A N     1 
ATOM   1289 C CA    . TRP A 1 210 ? -8.060  55.578  16.726  1.00 66.08  ? 182 TRP A CA    1 
ATOM   1290 C C     . TRP A 1 210 ? -6.796  55.695  17.568  1.00 66.07  ? 182 TRP A C     1 
ATOM   1291 O O     . TRP A 1 210 ? -6.881  55.780  18.796  1.00 67.76  ? 182 TRP A O     1 
ATOM   1292 C CB    . TRP A 1 210 ? -7.892  54.557  15.600  1.00 63.57  ? 182 TRP A CB    1 
ATOM   1293 C CG    . TRP A 1 210 ? -9.137  54.414  14.774  1.00 58.32  ? 182 TRP A CG    1 
ATOM   1294 C CD1   . TRP A 1 210 ? -9.264  54.652  13.438  1.00 59.54  ? 182 TRP A CD1   1 
ATOM   1295 C CD2   . TRP A 1 210 ? -10.436 54.022  15.237  1.00 57.47  ? 182 TRP A CD2   1 
ATOM   1296 N NE1   . TRP A 1 210 ? -10.559 54.426  13.037  1.00 63.65  ? 182 TRP A NE1   1 
ATOM   1297 C CE2   . TRP A 1 210 ? -11.298 54.038  14.123  1.00 57.49  ? 182 TRP A CE2   1 
ATOM   1298 C CE3   . TRP A 1 210 ? -10.953 53.653  16.484  1.00 57.59  ? 182 TRP A CE3   1 
ATOM   1299 C CZ2   . TRP A 1 210 ? -12.646 53.701  14.218  1.00 57.85  ? 182 TRP A CZ2   1 
ATOM   1300 C CZ3   . TRP A 1 210 ? -12.291 53.319  16.575  1.00 57.73  ? 182 TRP A CZ3   1 
ATOM   1301 C CH2   . TRP A 1 210 ? -13.122 53.345  15.450  1.00 57.75  ? 182 TRP A CH2   1 
ATOM   1302 N N     . ALA A 1 211 ? -5.630  55.692  16.912  1.00 66.54  ? 183 ALA A N     1 
ATOM   1303 C CA    . ALA A 1 211 ? -4.326  55.994  17.505  1.00 66.55  ? 183 ALA A CA    1 
ATOM   1304 C C     . ALA A 1 211 ? -4.128  55.468  18.923  1.00 68.45  ? 183 ALA A C     1 
ATOM   1305 O O     . ALA A 1 211 ? -3.233  54.651  19.166  1.00 71.81  ? 183 ALA A O     1 
ATOM   1306 C CB    . ALA A 1 211 ? -4.085  57.506  17.494  1.00 69.36  ? 183 ALA A CB    1 
ATOM   1307 N N     . LEU A 1 212 ? -4.942  55.956  19.866  1.00 71.50  ? 184 LEU A N     1 
ATOM   1308 C CA    . LEU A 1 212 ? -4.798  55.578  21.269  1.00 69.29  ? 184 LEU A CA    1 
ATOM   1309 C C     . LEU A 1 212 ? -4.820  54.066  21.451  1.00 69.34  ? 184 LEU A C     1 
ATOM   1310 O O     . LEU A 1 212 ? -4.021  53.513  22.216  1.00 72.23  ? 184 LEU A O     1 
ATOM   1311 C CB    . LEU A 1 212 ? -5.904  56.232  22.100  1.00 67.21  ? 184 LEU A CB    1 
ATOM   1312 N N     . TYR A 1 213 ? -5.726  53.377  20.757  1.00 64.46  ? 185 TYR A N     1 
ATOM   1313 C CA    . TYR A 1 213 ? -5.778  51.923  20.832  1.00 61.14  ? 185 TYR A CA    1 
ATOM   1314 C C     . TYR A 1 213 ? -4.714  51.245  19.980  1.00 60.67  ? 185 TYR A C     1 
ATOM   1315 O O     . TYR A 1 213 ? -4.472  50.047  20.164  1.00 64.65  ? 185 TYR A O     1 
ATOM   1316 C CB    . TYR A 1 213 ? -7.154  51.394  20.402  1.00 56.79  ? 185 TYR A CB    1 
ATOM   1317 C CG    . TYR A 1 213 ? -8.356  52.129  20.961  1.00 59.32  ? 185 TYR A CG    1 
ATOM   1318 C CD1   . TYR A 1 213 ? -8.739  53.370  20.465  1.00 62.00  ? 185 TYR A CD1   1 
ATOM   1319 C CD2   . TYR A 1 213 ? -9.116  51.569  21.979  1.00 60.78  ? 185 TYR A CD2   1 
ATOM   1320 C CE1   . TYR A 1 213 ? -9.841  54.033  20.972  1.00 60.90  ? 185 TYR A CE1   1 
ATOM   1321 C CE2   . TYR A 1 213 ? -10.218 52.225  22.492  1.00 62.36  ? 185 TYR A CE2   1 
ATOM   1322 C CZ    . TYR A 1 213 ? -10.576 53.456  21.986  1.00 59.80  ? 185 TYR A CZ    1 
ATOM   1323 O OH    . TYR A 1 213 ? -11.673 54.111  22.496  1.00 60.81  ? 185 TYR A OH    1 
ATOM   1324 N N     . MET A 1 214 ? -4.076  51.969  19.063  1.00 58.15  ? 186 MET A N     1 
ATOM   1325 C CA    . MET A 1 214 ? -3.164  51.369  18.097  1.00 57.15  ? 186 MET A CA    1 
ATOM   1326 C C     . MET A 1 214 ? -1.735  51.868  18.281  1.00 59.07  ? 186 MET A C     1 
ATOM   1327 O O     . MET A 1 214 ? -0.985  51.997  17.311  1.00 56.09  ? 186 MET A O     1 
ATOM   1328 C CB    . MET A 1 214 ? -3.650  51.636  16.673  1.00 56.73  ? 186 MET A CB    1 
ATOM   1329 C CG    . MET A 1 214 ? -5.041  51.090  16.398  1.00 52.94  ? 186 MET A CG    1 
ATOM   1330 S SD    . MET A 1 214 ? -5.587  51.340  14.702  1.00 55.35  ? 186 MET A SD    1 
ATOM   1331 C CE    . MET A 1 214 ? -4.707  50.016  13.882  1.00 53.92  ? 186 MET A CE    1 
ATOM   1332 N N     . GLN A 1 215 ? -1.346  52.151  19.526  1.00 63.37  ? 187 GLN A N     1 
ATOM   1333 C CA    . GLN A 1 215 ? 0.021   52.572  19.807  1.00 67.62  ? 187 GLN A CA    1 
ATOM   1334 C C     . GLN A 1 215 ? 1.033   51.470  19.526  1.00 68.18  ? 187 GLN A C     1 
ATOM   1335 O O     . GLN A 1 215 ? 2.209   51.768  19.292  1.00 68.47  ? 187 GLN A O     1 
ATOM   1336 C CB    . GLN A 1 215 ? 0.139   53.026  21.263  1.00 67.86  ? 187 GLN A CB    1 
ATOM   1337 C CG    . GLN A 1 215 ? -0.727  54.225  21.610  1.00 73.10  ? 187 GLN A CG    1 
ATOM   1338 C CD    . GLN A 1 215 ? -0.828  54.456  23.104  1.00 83.42  ? 187 GLN A CD    1 
ATOM   1339 O OE1   . GLN A 1 215 ? -0.117  53.830  23.891  1.00 91.13  ? 187 GLN A OE1   1 
ATOM   1340 N NE2   . GLN A 1 215 ? -1.719  55.356  23.505  1.00 84.06  ? 187 GLN A NE2   1 
ATOM   1341 N N     . ASP A 1 216 ? 0.602   50.210  19.541  1.00 68.59  ? 188 ASP A N     1 
ATOM   1342 C CA    . ASP A 1 216 ? 1.486   49.077  19.297  1.00 63.88  ? 188 ASP A CA    1 
ATOM   1343 C C     . ASP A 1 216 ? 1.153   48.421  17.963  1.00 64.09  ? 188 ASP A C     1 
ATOM   1344 O O     . ASP A 1 216 ? 1.020   47.196  17.883  1.00 60.78  ? 188 ASP A O     1 
ATOM   1345 C CB    . ASP A 1 216 ? 1.370   48.063  20.436  1.00 60.68  ? 188 ASP A CB    1 
ATOM   1346 C CG    . ASP A 1 216 ? -0.073  47.754  20.792  1.00 59.39  ? 188 ASP A CG    1 
ATOM   1347 O OD1   . ASP A 1 216 ? -0.968  48.509  20.355  1.00 59.74  ? 188 ASP A OD1   1 
ATOM   1348 O OD2   . ASP A 1 216 ? -0.313  46.760  21.508  1.00 59.26  ? 188 ASP A OD2   1 
ATOM   1349 N N     . VAL A 1 217 ? 1.019   49.232  16.910  1.00 63.03  ? 189 VAL A N     1 
ATOM   1350 C CA    . VAL A 1 217 ? 0.572   48.710  15.622  1.00 57.32  ? 189 VAL A CA    1 
ATOM   1351 C C     . VAL A 1 217 ? 1.607   47.768  15.016  1.00 60.86  ? 189 VAL A C     1 
ATOM   1352 O O     . VAL A 1 217 ? 1.246   46.778  14.369  1.00 61.31  ? 189 VAL A O     1 
ATOM   1353 C CB    . VAL A 1 217 ? 0.225   49.872  14.670  1.00 58.50  ? 189 VAL A CB    1 
ATOM   1354 C CG1   . VAL A 1 217 ? 1.448   50.741  14.400  1.00 65.02  ? 189 VAL A CG1   1 
ATOM   1355 C CG2   . VAL A 1 217 ? -0.365  49.342  13.370  1.00 58.35  ? 189 VAL A CG2   1 
ATOM   1356 N N     . GLU A 1 218 ? 2.898   48.038  15.225  1.00 64.89  ? 190 GLU A N     1 
ATOM   1357 C CA    . GLU A 1 218 ? 3.934   47.186  14.652  1.00 62.49  ? 190 GLU A CA    1 
ATOM   1358 C C     . GLU A 1 218 ? 3.927   45.783  15.245  1.00 59.40  ? 190 GLU A C     1 
ATOM   1359 O O     . GLU A 1 218 ? 4.405   44.848  14.595  1.00 57.73  ? 190 GLU A O     1 
ATOM   1360 C CB    . GLU A 1 218 ? 5.313   47.825  14.836  1.00 65.32  ? 190 GLU A CB    1 
ATOM   1361 C CG    . GLU A 1 218 ? 5.788   47.908  16.281  1.00 67.85  ? 190 GLU A CG    1 
ATOM   1362 C CD    . GLU A 1 218 ? 5.184   49.081  17.037  1.00 72.67  ? 190 GLU A CD    1 
ATOM   1363 O OE1   . GLU A 1 218 ? 4.277   49.746  16.493  1.00 71.09  ? 190 GLU A OE1   1 
ATOM   1364 O OE2   . GLU A 1 218 ? 5.619   49.338  18.179  1.00 75.07  ? 190 GLU A OE2   1 
ATOM   1365 N N     . LYS A 1 219 ? 3.397   45.613  16.458  1.00 56.82  ? 191 LYS A N     1 
ATOM   1366 C CA    . LYS A 1 219 ? 3.272   44.283  17.037  1.00 54.76  ? 191 LYS A CA    1 
ATOM   1367 C C     . LYS A 1 219 ? 2.020   43.551  16.573  1.00 54.71  ? 191 LYS A C     1 
ATOM   1368 O O     . LYS A 1 219 ? 1.864   42.367  16.888  1.00 56.81  ? 191 LYS A O     1 
ATOM   1369 C CB    . LYS A 1 219 ? 3.295   44.362  18.566  1.00 52.74  ? 191 LYS A CB    1 
ATOM   1370 C CG    . LYS A 1 219 ? 4.684   44.596  19.137  1.00 49.08  ? 191 LYS A CG    1 
ATOM   1371 C CD    . LYS A 1 219 ? 4.700   44.502  20.652  1.00 47.05  ? 191 LYS A CD    1 
ATOM   1372 C CE    . LYS A 1 219 ? 6.117   44.640  21.189  1.00 49.90  ? 191 LYS A CE    1 
ATOM   1373 N NZ    . LYS A 1 219 ? 6.165   44.600  22.676  1.00 53.88  ? 191 LYS A NZ    1 
ATOM   1374 N N     . PHE A 1 220 ? 1.131   44.217  15.838  1.00 51.98  ? 192 PHE A N     1 
ATOM   1375 C CA    . PHE A 1 220 ? 0.006   43.564  15.185  1.00 49.13  ? 192 PHE A CA    1 
ATOM   1376 C C     . PHE A 1 220 ? 0.243   43.364  13.694  1.00 45.64  ? 192 PHE A C     1 
ATOM   1377 O O     . PHE A 1 220 ? -0.689  43.005  12.967  1.00 44.53  ? 192 PHE A O     1 
ATOM   1378 C CB    . PHE A 1 220 ? -1.278  44.365  15.407  1.00 51.52  ? 192 PHE A CB    1 
ATOM   1379 C CG    . PHE A 1 220 ? -1.834  44.250  16.797  1.00 49.10  ? 192 PHE A CG    1 
ATOM   1380 C CD1   . PHE A 1 220 ? -1.267  44.952  17.848  1.00 49.57  ? 192 PHE A CD1   1 
ATOM   1381 C CD2   . PHE A 1 220 ? -2.926  43.438  17.053  1.00 51.98  ? 192 PHE A CD2   1 
ATOM   1382 C CE1   . PHE A 1 220 ? -1.780  44.846  19.127  1.00 51.97  ? 192 PHE A CE1   1 
ATOM   1383 C CE2   . PHE A 1 220 ? -3.443  43.327  18.329  1.00 52.40  ? 192 PHE A CE2   1 
ATOM   1384 C CZ    . PHE A 1 220 ? -2.870  44.033  19.367  1.00 52.38  ? 192 PHE A CZ    1 
ATOM   1385 N N     . VAL A 1 221 ? 1.468   43.589  13.226  1.00 45.83  ? 193 VAL A N     1 
ATOM   1386 C CA    . VAL A 1 221 ? 1.832   43.450  11.823  1.00 46.58  ? 193 VAL A CA    1 
ATOM   1387 C C     . VAL A 1 221 ? 2.873   42.347  11.704  1.00 49.74  ? 193 VAL A C     1 
ATOM   1388 O O     . VAL A 1 221 ? 3.738   42.204  12.576  1.00 52.31  ? 193 VAL A O     1 
ATOM   1389 C CB    . VAL A 1 221 ? 2.364   44.781  11.249  1.00 46.92  ? 193 VAL A CB    1 
ATOM   1390 C CG1   . VAL A 1 221 ? 2.812   44.613  9.811   1.00 50.83  ? 193 VAL A CG1   1 
ATOM   1391 C CG2   . VAL A 1 221 ? 1.297   45.856  11.342  1.00 52.57  ? 193 VAL A CG2   1 
ATOM   1392 N N     . SER A 1 222 ? 2.774   41.559  10.637  1.00 51.16  ? 194 SER A N     1 
ATOM   1393 C CA    . SER A 1 222 ? 3.750   40.508  10.392  1.00 47.38  ? 194 SER A CA    1 
ATOM   1394 C C     . SER A 1 222 ? 5.155   41.105  10.328  1.00 48.98  ? 194 SER A C     1 
ATOM   1395 O O     . SER A 1 222 ? 5.356   42.156  9.709   1.00 54.61  ? 194 SER A O     1 
ATOM   1396 C CB    . SER A 1 222 ? 3.433   39.776  9.087   1.00 44.87  ? 194 SER A CB    1 
ATOM   1397 O OG    . SER A 1 222 ? 4.536   38.999  8.654   1.00 44.01  ? 194 SER A OG    1 
ATOM   1398 N N     . PRO A 1 223 ? 6.146   40.471  10.962  1.00 49.82  ? 195 PRO A N     1 
ATOM   1399 C CA    . PRO A 1 223 ? 7.510   41.021  10.916  1.00 54.19  ? 195 PRO A CA    1 
ATOM   1400 C C     . PRO A 1 223 ? 8.119   41.008  9.527   1.00 52.46  ? 195 PRO A C     1 
ATOM   1401 O O     . PRO A 1 223 ? 9.047   41.784  9.269   1.00 54.46  ? 195 PRO A O     1 
ATOM   1402 C CB    . PRO A 1 223 ? 8.292   40.116  11.878  1.00 52.29  ? 195 PRO A CB    1 
ATOM   1403 C CG    . PRO A 1 223 ? 7.504   38.855  11.958  1.00 50.63  ? 195 PRO A CG    1 
ATOM   1404 C CD    . PRO A 1 223 ? 6.068   39.202  11.706  1.00 47.14  ? 195 PRO A CD    1 
ATOM   1405 N N     . TYR A 1 224 ? 7.628   40.157  8.627   1.00 49.53  ? 196 TYR A N     1 
ATOM   1406 C CA    . TYR A 1 224 ? 8.094   40.112  7.249   1.00 54.60  ? 196 TYR A CA    1 
ATOM   1407 C C     . TYR A 1 224 ? 7.240   40.968  6.321   1.00 58.18  ? 196 TYR A C     1 
ATOM   1408 O O     . TYR A 1 224 ? 7.264   40.760  5.102   1.00 57.24  ? 196 TYR A O     1 
ATOM   1409 C CB    . TYR A 1 224 ? 8.129   38.664  6.759   1.00 51.64  ? 196 TYR A CB    1 
ATOM   1410 C CG    . TYR A 1 224 ? 8.780   37.724  7.746   1.00 56.19  ? 196 TYR A CG    1 
ATOM   1411 C CD1   . TYR A 1 224 ? 10.159  37.698  7.906   1.00 58.15  ? 196 TYR A CD1   1 
ATOM   1412 C CD2   . TYR A 1 224 ? 8.014   36.873  8.532   1.00 56.40  ? 196 TYR A CD2   1 
ATOM   1413 C CE1   . TYR A 1 224 ? 10.758  36.845  8.813   1.00 52.29  ? 196 TYR A CE1   1 
ATOM   1414 C CE2   . TYR A 1 224 ? 8.603   36.017  9.441   1.00 52.53  ? 196 TYR A CE2   1 
ATOM   1415 C CZ    . TYR A 1 224 ? 9.975   36.007  9.578   1.00 50.79  ? 196 TYR A CZ    1 
ATOM   1416 O OH    . TYR A 1 224 ? 10.565  35.157  10.482  1.00 53.97  ? 196 TYR A OH    1 
ATOM   1417 N N     . GLN A 1 225 ? 6.489   41.922  6.874   1.00 58.31  ? 197 GLN A N     1 
ATOM   1418 C CA    . GLN A 1 225 ? 5.644   42.785  6.054   1.00 53.65  ? 197 GLN A CA    1 
ATOM   1419 C C     . GLN A 1 225 ? 6.487   43.700  5.176   1.00 55.75  ? 197 GLN A C     1 
ATOM   1420 O O     . GLN A 1 225 ? 6.334   43.722  3.949   1.00 60.19  ? 197 GLN A O     1 
ATOM   1421 C CB    . GLN A 1 225 ? 4.716   43.608  6.948   1.00 50.45  ? 197 GLN A CB    1 
ATOM   1422 C CG    . GLN A 1 225 ? 3.786   44.535  6.189   1.00 52.85  ? 197 GLN A CG    1 
ATOM   1423 C CD    . GLN A 1 225 ? 2.720   43.781  5.423   1.00 57.78  ? 197 GLN A CD    1 
ATOM   1424 O OE1   . GLN A 1 225 ? 2.326   42.681  5.808   1.00 55.14  ? 197 GLN A OE1   1 
ATOM   1425 N NE2   . GLN A 1 225 ? 2.251   44.367  4.327   1.00 61.89  ? 197 GLN A NE2   1 
ATOM   1426 N N     . HIS A 1 226 ? 7.382   44.468  5.791   1.00 56.71  ? 198 HIS A N     1 
ATOM   1427 C CA    . HIS A 1 226 ? 8.234   45.406  5.077   1.00 61.54  ? 198 HIS A CA    1 
ATOM   1428 C C     . HIS A 1 226 ? 9.572   44.798  4.677   1.00 65.80  ? 198 HIS A C     1 
ATOM   1429 O O     . HIS A 1 226 ? 10.469  45.532  4.250   1.00 74.62  ? 198 HIS A O     1 
ATOM   1430 C CB    . HIS A 1 226 ? 8.464   46.658  5.927   1.00 61.54  ? 198 HIS A CB    1 
ATOM   1431 C CG    . HIS A 1 226 ? 7.202   47.280  6.439   1.00 62.68  ? 198 HIS A CG    1 
ATOM   1432 N ND1   . HIS A 1 226 ? 6.207   47.740  5.604   1.00 68.06  ? 198 HIS A ND1   1 
ATOM   1433 C CD2   . HIS A 1 226 ? 6.772   47.514  7.701   1.00 62.69  ? 198 HIS A CD2   1 
ATOM   1434 C CE1   . HIS A 1 226 ? 5.219   48.232  6.330   1.00 64.69  ? 198 HIS A CE1   1 
ATOM   1435 N NE2   . HIS A 1 226 ? 5.537   48.107  7.606   1.00 63.75  ? 198 HIS A NE2   1 
ATOM   1436 N N     . SER A 1 227 ? 9.725   43.483  4.803   1.00 62.70  ? 199 SER A N     1 
ATOM   1437 C CA    . SER A 1 227 ? 10.979  42.835  4.445   1.00 66.47  ? 199 SER A CA    1 
ATOM   1438 C C     . SER A 1 227 ? 11.157  42.826  2.931   1.00 68.16  ? 199 SER A C     1 
ATOM   1439 O O     . SER A 1 227 ? 10.230  42.493  2.187   1.00 64.61  ? 199 SER A O     1 
ATOM   1440 C CB    . SER A 1 227 ? 11.013  41.409  4.991   1.00 68.35  ? 199 SER A CB    1 
ATOM   1441 O OG    . SER A 1 227 ? 12.153  40.710  4.522   1.00 69.13  ? 199 SER A OG    1 
ATOM   1442 N N     . GLU A 1 228 ? 12.356  43.197  2.477   1.00 72.27  ? 200 GLU A N     1 
ATOM   1443 C CA    . GLU A 1 228 ? 12.662  43.176  1.053   1.00 69.98  ? 200 GLU A CA    1 
ATOM   1444 C C     . GLU A 1 228 ? 12.926  41.769  0.533   1.00 64.03  ? 200 GLU A C     1 
ATOM   1445 O O     . GLU A 1 228 ? 12.875  41.553  -0.683  1.00 61.14  ? 200 GLU A O     1 
ATOM   1446 C CB    . GLU A 1 228 ? 13.869  44.069  0.760   1.00 69.41  ? 200 GLU A CB    1 
ATOM   1447 N N     . ASP A 1 229 ? 13.206  40.816  1.420   1.00 64.29  ? 201 ASP A N     1 
ATOM   1448 C CA    . ASP A 1 229 ? 13.431  39.426  1.025   1.00 63.12  ? 201 ASP A CA    1 
ATOM   1449 C C     . ASP A 1 229 ? 12.919  38.530  2.141   1.00 63.95  ? 201 ASP A C     1 
ATOM   1450 O O     . ASP A 1 229 ? 13.672  38.140  3.045   1.00 63.50  ? 201 ASP A O     1 
ATOM   1451 C CB    . ASP A 1 229 ? 14.906  39.151  0.737   1.00 61.64  ? 201 ASP A CB    1 
ATOM   1452 C CG    . ASP A 1 229 ? 15.156  37.726  0.282   1.00 63.84  ? 201 ASP A CG    1 
ATOM   1453 O OD1   . ASP A 1 229 ? 14.208  37.081  -0.214  1.00 64.40  ? 201 ASP A OD1   1 
ATOM   1454 O OD2   . ASP A 1 229 ? 16.302  37.250  0.421   1.00 66.58  ? 201 ASP A OD2   1 
ATOM   1455 N N     . PRO A 1 230 ? 11.627  38.188  2.118   1.00 59.19  ? 202 PRO A N     1 
ATOM   1456 C CA    . PRO A 1 230 ? 11.072  37.389  3.224   1.00 58.83  ? 202 PRO A CA    1 
ATOM   1457 C C     . PRO A 1 230 ? 11.632  35.979  3.296   1.00 57.01  ? 202 PRO A C     1 
ATOM   1458 O O     . PRO A 1 230 ? 11.887  35.479  4.399   1.00 60.33  ? 202 PRO A O     1 
ATOM   1459 C CB    . PRO A 1 230 ? 9.563   37.386  2.934   1.00 58.61  ? 202 PRO A CB    1 
ATOM   1460 C CG    . PRO A 1 230 ? 9.334   38.534  2.002   1.00 57.47  ? 202 PRO A CG    1 
ATOM   1461 C CD    . PRO A 1 230 ? 10.586  38.671  1.197   1.00 60.02  ? 202 PRO A CD    1 
ATOM   1462 N N     . VAL A 1 231 ? 11.823  35.319  2.151   1.00 50.51  ? 203 VAL A N     1 
ATOM   1463 C CA    . VAL A 1 231 ? 12.330  33.948  2.158   1.00 49.35  ? 203 VAL A CA    1 
ATOM   1464 C C     . VAL A 1 231 ? 13.738  33.903  2.738   1.00 57.85  ? 203 VAL A C     1 
ATOM   1465 O O     . VAL A 1 231 ? 14.097  32.968  3.464   1.00 60.27  ? 203 VAL A O     1 
ATOM   1466 C CB    . VAL A 1 231 ? 12.279  33.353  0.738   1.00 52.60  ? 203 VAL A CB    1 
ATOM   1467 C CG1   . VAL A 1 231 ? 13.000  32.013  0.686   1.00 57.55  ? 203 VAL A CG1   1 
ATOM   1468 C CG2   . VAL A 1 231 ? 10.841  33.198  0.285   1.00 47.00  ? 203 VAL A CG2   1 
ATOM   1469 N N     . GLY A 1 232 ? 14.551  34.917  2.441   1.00 55.69  ? 204 GLY A N     1 
ATOM   1470 C CA    . GLY A 1 232 ? 15.905  34.942  2.971   1.00 59.64  ? 204 GLY A CA    1 
ATOM   1471 C C     . GLY A 1 232 ? 15.938  35.133  4.476   1.00 59.73  ? 204 GLY A C     1 
ATOM   1472 O O     . GLY A 1 232 ? 16.673  34.441  5.186   1.00 57.33  ? 204 GLY A O     1 
ATOM   1473 N N     . GLU A 1 233 ? 15.138  36.075  4.984   1.00 61.01  ? 205 GLU A N     1 
ATOM   1474 C CA    . GLU A 1 233 ? 15.134  36.339  6.419   1.00 62.17  ? 205 GLU A CA    1 
ATOM   1475 C C     . GLU A 1 233 ? 14.564  35.161  7.201   1.00 58.74  ? 205 GLU A C     1 
ATOM   1476 O O     . GLU A 1 233 ? 15.037  34.856  8.302   1.00 59.22  ? 205 GLU A O     1 
ATOM   1477 C CB    . GLU A 1 233 ? 14.348  37.614  6.723   1.00 60.89  ? 205 GLU A CB    1 
ATOM   1478 C CG    . GLU A 1 233 ? 15.063  38.893  6.325   1.00 64.88  ? 205 GLU A CG    1 
ATOM   1479 C CD    . GLU A 1 233 ? 14.369  40.134  6.847   1.00 73.49  ? 205 GLU A CD    1 
ATOM   1480 O OE1   . GLU A 1 233 ? 13.563  40.011  7.794   1.00 76.29  ? 205 GLU A OE1   1 
ATOM   1481 O OE2   . GLU A 1 233 ? 14.630  41.234  6.315   1.00 83.21  ? 205 GLU A OE2   1 
ATOM   1482 N N     . PHE A 1 234 ? 13.548  34.488  6.654   1.00 56.36  ? 206 PHE A N     1 
ATOM   1483 C CA    . PHE A 1 234 ? 12.994  33.334  7.352   1.00 52.69  ? 206 PHE A CA    1 
ATOM   1484 C C     . PHE A 1 234 ? 13.913  32.124  7.259   1.00 56.90  ? 206 PHE A C     1 
ATOM   1485 O O     . PHE A 1 234 ? 13.986  31.333  8.206   1.00 58.17  ? 206 PHE A O     1 
ATOM   1486 C CB    . PHE A 1 234 ? 11.606  32.991  6.810   1.00 48.34  ? 206 PHE A CB    1 
ATOM   1487 C CG    . PHE A 1 234 ? 10.829  32.062  7.697   1.00 43.28  ? 206 PHE A CG    1 
ATOM   1488 C CD1   . PHE A 1 234 ? 10.621  32.374  9.031   1.00 39.18  ? 206 PHE A CD1   1 
ATOM   1489 C CD2   . PHE A 1 234 ? 10.310  30.877  7.204   1.00 42.20  ? 206 PHE A CD2   1 
ATOM   1490 C CE1   . PHE A 1 234 ? 9.912   31.523  9.856   1.00 34.69  ? 206 PHE A CE1   1 
ATOM   1491 C CE2   . PHE A 1 234 ? 9.597   30.021  8.025   1.00 37.52  ? 206 PHE A CE2   1 
ATOM   1492 C CZ    . PHE A 1 234 ? 9.399   30.346  9.353   1.00 34.40  ? 206 PHE A CZ    1 
ATOM   1493 N N     . ARG A 1 235 ? 14.618  31.959  6.136   1.00 56.18  ? 207 ARG A N     1 
ATOM   1494 C CA    . ARG A 1 235 ? 15.619  30.900  6.056   1.00 59.88  ? 207 ARG A CA    1 
ATOM   1495 C C     . ARG A 1 235 ? 16.778  31.174  7.005   1.00 59.21  ? 207 ARG A C     1 
ATOM   1496 O O     . ARG A 1 235 ? 17.330  30.246  7.608   1.00 60.97  ? 207 ARG A O     1 
ATOM   1497 C CB    . ARG A 1 235 ? 16.124  30.745  4.620   1.00 57.85  ? 207 ARG A CB    1 
ATOM   1498 C CG    . ARG A 1 235 ? 17.199  29.676  4.465   1.00 58.87  ? 207 ARG A CG    1 
ATOM   1499 C CD    . ARG A 1 235 ? 17.668  29.523  3.025   1.00 60.65  ? 207 ARG A CD    1 
ATOM   1500 N NE    . ARG A 1 235 ? 16.816  28.623  2.257   1.00 65.15  ? 207 ARG A NE    1 
ATOM   1501 C CZ    . ARG A 1 235 ? 16.221  28.943  1.116   1.00 66.75  ? 207 ARG A CZ    1 
ATOM   1502 N NH1   . ARG A 1 235 ? 16.369  30.139  0.571   1.00 65.03  ? 207 ARG A NH1   1 
ATOM   1503 N NH2   . ARG A 1 235 ? 15.466  28.036  0.502   1.00 63.85  ? 207 ARG A NH2   1 
ATOM   1504 N N     . LEU A 1 236 ? 17.155  32.445  7.157   1.00 56.88  ? 208 LEU A N     1 
ATOM   1505 C CA    . LEU A 1 236 ? 18.226  32.791  8.086   1.00 51.80  ? 208 LEU A CA    1 
ATOM   1506 C C     . LEU A 1 236 ? 17.784  32.603  9.532   1.00 51.23  ? 208 LEU A C     1 
ATOM   1507 O O     . LEU A 1 236 ? 18.574  32.163  10.375  1.00 51.53  ? 208 LEU A O     1 
ATOM   1508 C CB    . LEU A 1 236 ? 18.685  34.228  7.845   1.00 46.54  ? 208 LEU A CB    1 
ATOM   1509 N N     . LEU A 1 237 ? 16.524  32.927  9.837   1.00 51.81  ? 209 LEU A N     1 
ATOM   1510 C CA    . LEU A 1 237 ? 16.040  32.795  11.208  1.00 44.92  ? 209 LEU A CA    1 
ATOM   1511 C C     . LEU A 1 237 ? 15.981  31.336  11.639  1.00 49.39  ? 209 LEU A C     1 
ATOM   1512 O O     . LEU A 1 237 ? 16.365  31.000  12.766  1.00 55.27  ? 209 LEU A O     1 
ATOM   1513 C CB    . LEU A 1 237 ? 14.666  33.447  11.349  1.00 42.40  ? 209 LEU A CB    1 
ATOM   1514 C CG    . LEU A 1 237 ? 14.029  33.303  12.733  1.00 41.39  ? 209 LEU A CG    1 
ATOM   1515 C CD1   . LEU A 1 237 ? 14.867  34.015  13.780  1.00 47.03  ? 209 LEU A CD1   1 
ATOM   1516 C CD2   . LEU A 1 237 ? 12.600  33.823  12.738  1.00 44.63  ? 209 LEU A CD2   1 
ATOM   1517 N N     . LEU A 1 238 ? 15.499  30.455  10.760  1.00 51.14  ? 210 LEU A N     1 
ATOM   1518 C CA    . LEU A 1 238 ? 15.413  29.039  11.103  1.00 51.13  ? 210 LEU A CA    1 
ATOM   1519 C C     . LEU A 1 238 ? 16.799  28.442  11.312  1.00 53.53  ? 210 LEU A C     1 
ATOM   1520 O O     . LEU A 1 238 ? 17.043  27.734  12.296  1.00 51.66  ? 210 LEU A O     1 
ATOM   1521 C CB    . LEU A 1 238 ? 14.656  28.281  10.012  1.00 44.28  ? 210 LEU A CB    1 
ATOM   1522 C CG    . LEU A 1 238 ? 13.164  28.592  9.879   1.00 37.40  ? 210 LEU A CG    1 
ATOM   1523 C CD1   . LEU A 1 238 ? 12.537  27.755  8.776   1.00 33.14  ? 210 LEU A CD1   1 
ATOM   1524 C CD2   . LEU A 1 238 ? 12.451  28.365  11.200  1.00 42.17  ? 210 LEU A CD2   1 
ATOM   1525 N N     . GLU A 1 239 ? 17.727  28.727  10.395  1.00 53.55  ? 211 GLU A N     1 
ATOM   1526 C CA    . GLU A 1 239 ? 19.078  28.193  10.520  1.00 52.67  ? 211 GLU A CA    1 
ATOM   1527 C C     . GLU A 1 239 ? 19.816  28.795  11.708  1.00 52.90  ? 211 GLU A C     1 
ATOM   1528 O O     . GLU A 1 239 ? 20.734  28.166  12.247  1.00 57.19  ? 211 GLU A O     1 
ATOM   1529 C CB    . GLU A 1 239 ? 19.858  28.435  9.228   1.00 51.64  ? 211 GLU A CB    1 
ATOM   1530 C CG    . GLU A 1 239 ? 19.347  27.628  8.047   1.00 55.36  ? 211 GLU A CG    1 
ATOM   1531 C CD    . GLU A 1 239 ? 19.867  28.141  6.719   1.00 62.24  ? 211 GLU A CD    1 
ATOM   1532 O OE1   . GLU A 1 239 ? 20.442  29.249  6.694   1.00 65.74  ? 211 GLU A OE1   1 
ATOM   1533 O OE2   . GLU A 1 239 ? 19.699  27.436  5.701   1.00 64.87  ? 211 GLU A OE2   1 
ATOM   1534 N N     . SER A 1 240 ? 19.435  29.999  12.133  1.00 49.71  ? 212 SER A N     1 
ATOM   1535 C CA    . SER A 1 240 ? 20.022  30.609  13.319  1.00 46.90  ? 212 SER A CA    1 
ATOM   1536 C C     . SER A 1 240 ? 19.502  30.001  14.613  1.00 50.05  ? 212 SER A C     1 
ATOM   1537 O O     . SER A 1 240 ? 19.889  30.460  15.694  1.00 50.69  ? 212 SER A O     1 
ATOM   1538 C CB    . SER A 1 240 ? 19.766  32.119  13.323  1.00 49.34  ? 212 SER A CB    1 
ATOM   1539 O OG    . SER A 1 240 ? 18.402  32.408  13.574  1.00 51.16  ? 212 SER A OG    1 
ATOM   1540 N N     . GLU A 1 241 ? 18.636  28.987  14.534  1.00 52.35  ? 213 GLU A N     1 
ATOM   1541 C CA    . GLU A 1 241 ? 18.113  28.312  15.715  1.00 50.88  ? 213 GLU A CA    1 
ATOM   1542 C C     . GLU A 1 241 ? 18.371  26.810  15.678  1.00 53.05  ? 213 GLU A C     1 
ATOM   1543 O O     . GLU A 1 241 ? 17.738  26.056  16.425  1.00 51.48  ? 213 GLU A O     1 
ATOM   1544 C CB    . GLU A 1 241 ? 16.618  28.591  15.873  1.00 50.35  ? 213 GLU A CB    1 
ATOM   1545 C CG    . GLU A 1 241 ? 16.312  30.022  16.263  1.00 52.06  ? 213 GLU A CG    1 
ATOM   1546 C CD    . GLU A 1 241 ? 16.951  30.396  17.582  1.00 56.17  ? 213 GLU A CD    1 
ATOM   1547 O OE1   . GLU A 1 241 ? 16.919  29.564  18.513  1.00 52.45  ? 213 GLU A OE1   1 
ATOM   1548 O OE2   . GLU A 1 241 ? 17.481  31.522  17.689  1.00 62.06  ? 213 GLU A OE2   1 
ATOM   1549 N N     . GLY A 1 242 ? 19.289  26.360  14.826  1.00 55.54  ? 214 GLY A N     1 
ATOM   1550 C CA    . GLY A 1 242 ? 19.627  24.955  14.752  1.00 54.69  ? 214 GLY A CA    1 
ATOM   1551 C C     . GLY A 1 242 ? 18.764  24.132  13.826  1.00 53.56  ? 214 GLY A C     1 
ATOM   1552 O O     . GLY A 1 242 ? 18.594  22.930  14.062  1.00 53.58  ? 214 GLY A O     1 
ATOM   1553 N N     . PHE A 1 243 ? 18.216  24.734  12.775  1.00 50.27  ? 215 PHE A N     1 
ATOM   1554 C CA    . PHE A 1 243 ? 17.338  24.043  11.844  1.00 50.71  ? 215 PHE A CA    1 
ATOM   1555 C C     . PHE A 1 243 ? 18.005  23.899  10.483  1.00 49.05  ? 215 PHE A C     1 
ATOM   1556 O O     . PHE A 1 243 ? 18.833  24.723  10.085  1.00 50.66  ? 215 PHE A O     1 
ATOM   1557 C CB    . PHE A 1 243 ? 16.007  24.783  11.685  1.00 48.92  ? 215 PHE A CB    1 
ATOM   1558 C CG    . PHE A 1 243 ? 15.031  24.525  12.794  1.00 44.97  ? 215 PHE A CG    1 
ATOM   1559 C CD1   . PHE A 1 243 ? 14.199  23.419  12.758  1.00 44.98  ? 215 PHE A CD1   1 
ATOM   1560 C CD2   . PHE A 1 243 ? 14.942  25.388  13.872  1.00 45.58  ? 215 PHE A CD2   1 
ATOM   1561 C CE1   . PHE A 1 243 ? 13.299  23.177  13.775  1.00 45.34  ? 215 PHE A CE1   1 
ATOM   1562 C CE2   . PHE A 1 243 ? 14.043  25.152  14.894  1.00 45.75  ? 215 PHE A CE2   1 
ATOM   1563 C CZ    . PHE A 1 243 ? 13.220  24.044  14.845  1.00 43.80  ? 215 PHE A CZ    1 
ATOM   1564 N N     . GLN A 1 244 ? 17.631  22.838  9.773   1.00 47.89  ? 216 GLN A N     1 
ATOM   1565 C CA    . GLN A 1 244 ? 18.067  22.605  8.398   1.00 47.28  ? 216 GLN A CA    1 
ATOM   1566 C C     . GLN A 1 244 ? 16.895  22.938  7.483   1.00 48.86  ? 216 GLN A C     1 
ATOM   1567 O O     . GLN A 1 244 ? 15.940  22.165  7.373   1.00 52.94  ? 216 GLN A O     1 
ATOM   1568 C CB    . GLN A 1 244 ? 18.532  21.165  8.206   1.00 51.18  ? 216 GLN A CB    1 
ATOM   1569 C CG    . GLN A 1 244 ? 18.977  20.848  6.786   1.00 55.52  ? 216 GLN A CG    1 
ATOM   1570 C CD    . GLN A 1 244 ? 19.212  19.366  6.563   1.00 60.54  ? 216 GLN A CD    1 
ATOM   1571 O OE1   . GLN A 1 244 ? 18.693  18.526  7.298   1.00 64.37  ? 216 GLN A OE1   1 
ATOM   1572 N NE2   . GLN A 1 244 ? 19.992  19.038  5.539   1.00 60.34  ? 216 GLN A NE2   1 
ATOM   1573 N N     . VAL A 1 245 ? 16.965  24.096  6.829   1.00 45.47  ? 217 VAL A N     1 
ATOM   1574 C CA    . VAL A 1 245 ? 15.903  24.533  5.930   1.00 46.37  ? 217 VAL A CA    1 
ATOM   1575 C C     . VAL A 1 245 ? 15.950  23.695  4.659   1.00 50.27  ? 217 VAL A C     1 
ATOM   1576 O O     . VAL A 1 245 ? 16.818  23.893  3.801   1.00 54.27  ? 217 VAL A O     1 
ATOM   1577 C CB    . VAL A 1 245 ? 16.020  26.034  5.611   1.00 52.20  ? 217 VAL A CB    1 
ATOM   1578 C CG1   . VAL A 1 245 ? 14.946  26.452  4.618   1.00 58.98  ? 217 VAL A CG1   1 
ATOM   1579 C CG2   . VAL A 1 245 ? 15.921  26.853  6.887   1.00 47.74  ? 217 VAL A CG2   1 
ATOM   1580 N N     . LEU A 1 246 ? 15.016  22.750  4.532   1.00 52.54  ? 218 LEU A N     1 
ATOM   1581 C CA    . LEU A 1 246 ? 14.999  21.868  3.371   1.00 51.51  ? 218 LEU A CA    1 
ATOM   1582 C C     . LEU A 1 246 ? 14.330  22.513  2.165   1.00 55.81  ? 218 LEU A C     1 
ATOM   1583 O O     . LEU A 1 246 ? 14.676  22.185  1.024   1.00 68.29  ? 218 LEU A O     1 
ATOM   1584 C CB    . LEU A 1 246 ? 14.289  20.557  3.714   1.00 49.08  ? 218 LEU A CB    1 
ATOM   1585 C CG    . LEU A 1 246 ? 14.881  19.715  4.845   1.00 50.17  ? 218 LEU A CG    1 
ATOM   1586 C CD1   . LEU A 1 246 ? 14.047  18.463  5.071   1.00 48.38  ? 218 LEU A CD1   1 
ATOM   1587 C CD2   . LEU A 1 246 ? 16.324  19.350  4.536   1.00 57.08  ? 218 LEU A CD2   1 
ATOM   1588 N N     . ARG A 1 247 ? 13.385  23.422  2.389   1.00 54.34  ? 219 ARG A N     1 
ATOM   1589 C CA    . ARG A 1 247 ? 12.614  24.002  1.299   1.00 57.03  ? 219 ARG A CA    1 
ATOM   1590 C C     . ARG A 1 247 ? 11.908  25.248  1.814   1.00 57.20  ? 219 ARG A C     1 
ATOM   1591 O O     . ARG A 1 247 ? 11.342  25.231  2.909   1.00 54.01  ? 219 ARG A O     1 
ATOM   1592 C CB    . ARG A 1 247 ? 11.602  22.985  0.753   1.00 56.37  ? 219 ARG A CB    1 
ATOM   1593 C CG    . ARG A 1 247 ? 10.879  23.400  -0.513  1.00 62.23  ? 219 ARG A CG    1 
ATOM   1594 C CD    . ARG A 1 247 ? 10.076  22.228  -1.055  1.00 63.79  ? 219 ARG A CD    1 
ATOM   1595 N NE    . ARG A 1 247 ? 9.218   22.598  -2.174  1.00 76.03  ? 219 ARG A NE    1 
ATOM   1596 C CZ    . ARG A 1 247 ? 8.942   21.801  -3.197  1.00 72.86  ? 219 ARG A CZ    1 
ATOM   1597 N NH1   . ARG A 1 247 ? 9.444   20.579  -3.276  1.00 69.11  ? 219 ARG A NH1   1 
ATOM   1598 N NH2   . ARG A 1 247 ? 8.143   22.241  -4.165  1.00 71.42  ? 219 ARG A NH2   1 
ATOM   1599 N N     . CYS A 1 248 ? 11.951  26.322  1.026   1.00 59.99  ? 220 CYS A N     1 
ATOM   1600 C CA    . CYS A 1 248 ? 11.413  27.607  1.470   1.00 58.72  ? 220 CYS A CA    1 
ATOM   1601 C C     . CYS A 1 248 ? 11.045  28.427  0.240   1.00 60.64  ? 220 CYS A C     1 
ATOM   1602 O O     . CYS A 1 248 ? 11.934  28.862  -0.498  1.00 62.57  ? 220 CYS A O     1 
ATOM   1603 C CB    . CYS A 1 248 ? 12.428  28.339  2.341   1.00 56.44  ? 220 CYS A CB    1 
ATOM   1604 S SG    . CYS A 1 248 ? 11.764  29.737  3.269   1.00 65.38  ? 220 CYS A SG    1 
ATOM   1605 N N     . ASP A 1 249 ? 9.747   28.644  0.029   1.00 57.88  ? 221 ASP A N     1 
ATOM   1606 C CA    . ASP A 1 249 ? 9.259   29.358  -1.143  1.00 55.26  ? 221 ASP A CA    1 
ATOM   1607 C C     . ASP A 1 249 ? 8.190   30.360  -0.727  1.00 49.43  ? 221 ASP A C     1 
ATOM   1608 O O     . ASP A 1 249 ? 7.620   30.277  0.364   1.00 49.18  ? 221 ASP A O     1 
ATOM   1609 C CB    . ASP A 1 249 ? 8.695   28.394  -2.196  1.00 62.47  ? 221 ASP A CB    1 
ATOM   1610 C CG    . ASP A 1 249 ? 9.649   27.260  -2.517  1.00 69.17  ? 221 ASP A CG    1 
ATOM   1611 O OD1   . ASP A 1 249 ? 10.729  27.531  -3.083  1.00 70.69  ? 221 ASP A OD1   1 
ATOM   1612 O OD2   . ASP A 1 249 ? 9.320   26.097  -2.201  1.00 67.56  ? 221 ASP A OD2   1 
ATOM   1613 N N     . LEU A 1 250 ? 7.921   31.311  -1.621  1.00 48.14  ? 222 LEU A N     1 
ATOM   1614 C CA    . LEU A 1 250 ? 6.938   32.364  -1.396  1.00 44.01  ? 222 LEU A CA    1 
ATOM   1615 C C     . LEU A 1 250 ? 6.017   32.464  -2.602  1.00 39.58  ? 222 LEU A C     1 
ATOM   1616 O O     . LEU A 1 250 ? 6.485   32.478  -3.745  1.00 38.40  ? 222 LEU A O     1 
ATOM   1617 C CB    . LEU A 1 250 ? 7.620   33.713  -1.141  1.00 42.56  ? 222 LEU A CB    1 
ATOM   1618 C CG    . LEU A 1 250 ? 6.729   34.954  -1.048  1.00 43.73  ? 222 LEU A CG    1 
ATOM   1619 C CD1   . LEU A 1 250 ? 5.811   34.886  0.162   1.00 47.52  ? 222 LEU A CD1   1 
ATOM   1620 C CD2   . LEU A 1 250 ? 7.577   36.216  -1.007  1.00 45.00  ? 222 LEU A CD2   1 
ATOM   1621 N N     . GLY A 1 251 ? 4.713   32.542  -2.346  1.00 40.81  ? 223 GLY A N     1 
ATOM   1622 C CA    . GLY A 1 251 ? 3.735   32.655  -3.402  1.00 42.94  ? 223 GLY A CA    1 
ATOM   1623 C C     . GLY A 1 251 ? 2.455   33.324  -2.943  1.00 43.14  ? 223 GLY A C     1 
ATOM   1624 O O     . GLY A 1 251 ? 2.178   33.431  -1.744  1.00 46.84  ? 223 GLY A O     1 
ATOM   1625 N N     . PRO A 1 252 ? 1.653   33.796  -3.891  1.00 40.66  ? 224 PRO A N     1 
ATOM   1626 C CA    . PRO A 1 252 ? 0.373   34.416  -3.541  1.00 40.33  ? 224 PRO A CA    1 
ATOM   1627 C C     . PRO A 1 252 ? -0.724  33.378  -3.352  1.00 40.58  ? 224 PRO A C     1 
ATOM   1628 O O     . PRO A 1 252 ? -0.677  32.270  -3.889  1.00 40.40  ? 224 PRO A O     1 
ATOM   1629 C CB    . PRO A 1 252 ? 0.083   35.313  -4.748  1.00 44.07  ? 224 PRO A CB    1 
ATOM   1630 C CG    . PRO A 1 252 ? 0.694   34.569  -5.890  1.00 44.14  ? 224 PRO A CG    1 
ATOM   1631 C CD    . PRO A 1 252 ? 1.926   33.877  -5.338  1.00 41.28  ? 224 PRO A CD    1 
ATOM   1632 N N     . GLN A 1 253 ? -1.729  33.764  -2.567  1.00 43.43  ? 225 GLN A N     1 
ATOM   1633 C CA    . GLN A 1 253 ? -2.855  32.895  -2.260  1.00 38.76  ? 225 GLN A CA    1 
ATOM   1634 C C     . GLN A 1 253 ? -4.148  33.695  -2.288  1.00 39.35  ? 225 GLN A C     1 
ATOM   1635 O O     . GLN A 1 253 ? -4.162  34.896  -2.004  1.00 41.91  ? 225 GLN A O     1 
ATOM   1636 C CB    . GLN A 1 253 ? -2.701  32.222  -0.887  1.00 40.80  ? 225 GLN A CB    1 
ATOM   1637 C CG    . GLN A 1 253 ? -1.543  31.242  -0.780  1.00 42.46  ? 225 GLN A CG    1 
ATOM   1638 C CD    . GLN A 1 253 ? -1.800  29.948  -1.526  1.00 47.73  ? 225 GLN A CD    1 
ATOM   1639 O OE1   . GLN A 1 253 ? -2.949  29.561  -1.744  1.00 48.33  ? 225 GLN A OE1   1 
ATOM   1640 N NE2   . GLN A 1 253 ? -0.729  29.268  -1.917  1.00 51.82  ? 225 GLN A NE2   1 
ATOM   1641 N N     . LYS A 1 254 ? -5.236  33.012  -2.634  1.00 42.33  ? 226 LYS A N     1 
ATOM   1642 C CA    . LYS A 1 254 ? -6.579  33.571  -2.578  1.00 45.52  ? 226 LYS A CA    1 
ATOM   1643 C C     . LYS A 1 254 ? -7.430  32.743  -1.625  1.00 42.87  ? 226 LYS A C     1 
ATOM   1644 O O     . LYS A 1 254 ? -7.276  31.521  -1.545  1.00 41.61  ? 226 LYS A O     1 
ATOM   1645 C CB    . LYS A 1 254 ? -7.240  33.603  -3.963  1.00 46.82  ? 226 LYS A CB    1 
ATOM   1646 C CG    . LYS A 1 254 ? -6.605  34.559  -4.959  1.00 48.84  ? 226 LYS A CG    1 
ATOM   1647 C CD    . LYS A 1 254 ? -7.403  34.587  -6.257  1.00 56.61  ? 226 LYS A CD    1 
ATOM   1648 C CE    . LYS A 1 254 ? -6.781  35.515  -7.287  1.00 63.89  ? 226 LYS A CE    1 
ATOM   1649 N NZ    . LYS A 1 254 ? -7.607  35.589  -8.525  1.00 49.26  ? 226 LYS A NZ    1 
ATOM   1650 N N     . VAL A 1 255 ? -8.323  33.412  -0.902  1.00 43.35  ? 227 VAL A N     1 
ATOM   1651 C CA    . VAL A 1 255 ? -9.260  32.757  0.003   1.00 41.22  ? 227 VAL A CA    1 
ATOM   1652 C C     . VAL A 1 255 ? -10.655 32.976  -0.564  1.00 45.27  ? 227 VAL A C     1 
ATOM   1653 O O     . VAL A 1 255 ? -11.155 34.107  -0.587  1.00 47.37  ? 227 VAL A O     1 
ATOM   1654 C CB    . VAL A 1 255 ? -9.151  33.295  1.436   1.00 40.71  ? 227 VAL A CB    1 
ATOM   1655 C CG1   . VAL A 1 255 ? -10.064 32.510  2.365   1.00 40.47  ? 227 VAL A CG1   1 
ATOM   1656 C CG2   . VAL A 1 255 ? -7.711  33.246  1.918   1.00 43.70  ? 227 VAL A CG2   1 
ATOM   1657 N N     . PHE A 1 256 ? -11.288 31.898  -1.017  1.00 44.75  ? 228 PHE A N     1 
ATOM   1658 C CA    . PHE A 1 256 ? -12.566 31.988  -1.708  1.00 45.08  ? 228 PHE A CA    1 
ATOM   1659 C C     . PHE A 1 256 ? -13.725 32.021  -0.720  1.00 45.04  ? 228 PHE A C     1 
ATOM   1660 O O     . PHE A 1 256 ? -13.717 31.318  0.293   1.00 46.39  ? 228 PHE A O     1 
ATOM   1661 C CB    . PHE A 1 256 ? -12.737 30.810  -2.670  1.00 44.55  ? 228 PHE A CB    1 
ATOM   1662 C CG    . PHE A 1 256 ? -14.096 30.739  -3.303  1.00 48.50  ? 228 PHE A CG    1 
ATOM   1663 C CD1   . PHE A 1 256 ? -14.413 31.546  -4.382  1.00 52.54  ? 228 PHE A CD1   1 
ATOM   1664 C CD2   . PHE A 1 256 ? -15.058 29.865  -2.821  1.00 50.07  ? 228 PHE A CD2   1 
ATOM   1665 C CE1   . PHE A 1 256 ? -15.662 31.485  -4.966  1.00 56.34  ? 228 PHE A CE1   1 
ATOM   1666 C CE2   . PHE A 1 256 ? -16.309 29.800  -3.402  1.00 49.56  ? 228 PHE A CE2   1 
ATOM   1667 C CZ    . PHE A 1 256 ? -16.612 30.611  -4.476  1.00 55.98  ? 228 PHE A CZ    1 
ATOM   1668 N N     . PHE A 1 257 ? -14.726 32.844  -1.029  1.00 45.01  ? 229 PHE A N     1 
ATOM   1669 C CA    . PHE A 1 257 ? -15.972 32.881  -0.278  1.00 46.22  ? 229 PHE A CA    1 
ATOM   1670 C C     . PHE A 1 257 ? -17.133 32.913  -1.264  1.00 47.08  ? 229 PHE A C     1 
ATOM   1671 O O     . PHE A 1 257 ? -17.159 33.769  -2.166  1.00 48.86  ? 229 PHE A O     1 
ATOM   1672 C CB    . PHE A 1 257 ? -16.033 34.087  0.667   1.00 47.56  ? 229 PHE A CB    1 
ATOM   1673 C CG    . PHE A 1 257 ? -15.015 34.042  1.767   1.00 45.34  ? 229 PHE A CG    1 
ATOM   1674 C CD1   . PHE A 1 257 ? -15.297 33.396  2.959   1.00 43.03  ? 229 PHE A CD1   1 
ATOM   1675 C CD2   . PHE A 1 257 ? -13.778 34.642  1.611   1.00 43.47  ? 229 PHE A CD2   1 
ATOM   1676 C CE1   . PHE A 1 257 ? -14.365 33.348  3.973   1.00 39.41  ? 229 PHE A CE1   1 
ATOM   1677 C CE2   . PHE A 1 257 ? -12.843 34.599  2.624   1.00 39.32  ? 229 PHE A CE2   1 
ATOM   1678 C CZ    . PHE A 1 257 ? -13.136 33.949  3.805   1.00 38.94  ? 229 PHE A CZ    1 
ATOM   1679 N N     . PRO A 1 258 ? -18.105 32.007  -1.133  1.00 46.05  ? 230 PRO A N     1 
ATOM   1680 C CA    . PRO A 1 258 ? -19.184 31.960  -2.133  1.00 55.36  ? 230 PRO A CA    1 
ATOM   1681 C C     . PRO A 1 258 ? -20.168 33.107  -2.011  1.00 56.72  ? 230 PRO A C     1 
ATOM   1682 O O     . PRO A 1 258 ? -20.645 33.616  -3.033  1.00 61.16  ? 230 PRO A O     1 
ATOM   1683 C CB    . PRO A 1 258 ? -19.847 30.604  -1.859  1.00 59.71  ? 230 PRO A CB    1 
ATOM   1684 C CG    . PRO A 1 258 ? -19.573 30.340  -0.415  1.00 50.39  ? 230 PRO A CG    1 
ATOM   1685 C CD    . PRO A 1 258 ? -18.232 30.948  -0.117  1.00 47.80  ? 230 PRO A CD    1 
ATOM   1686 N N     . THR A 1 259 ? -20.489 33.530  -0.794  1.00 51.68  ? 231 THR A N     1 
ATOM   1687 C CA    . THR A 1 259 ? -21.465 34.584  -0.569  1.00 54.38  ? 231 THR A CA    1 
ATOM   1688 C C     . THR A 1 259 ? -20.768 35.897  -0.229  1.00 55.73  ? 231 THR A C     1 
ATOM   1689 O O     . THR A 1 259 ? -19.555 35.955  -0.015  1.00 56.52  ? 231 THR A O     1 
ATOM   1690 C CB    . THR A 1 259 ? -22.435 34.195  0.550   1.00 58.08  ? 231 THR A CB    1 
ATOM   1691 O OG1   . THR A 1 259 ? -21.774 34.304  1.815   1.00 64.00  ? 231 THR A OG1   1 
ATOM   1692 C CG2   . THR A 1 259 ? -22.915 32.765  0.361   1.00 58.82  ? 231 THR A CG2   1 
ATOM   1693 N N     . ALA A 1 260 ? -21.565 36.965  -0.178  1.00 54.82  ? 232 ALA A N     1 
ATOM   1694 C CA    . ALA A 1 260 ? -21.021 38.285  0.119   1.00 54.28  ? 232 ALA A CA    1 
ATOM   1695 C C     . ALA A 1 260 ? -20.771 38.472  1.611   1.00 55.88  ? 232 ALA A C     1 
ATOM   1696 O O     . ALA A 1 260 ? -19.728 39.005  2.004   1.00 49.21  ? 232 ALA A O     1 
ATOM   1697 C CB    . ALA A 1 260 ? -21.964 39.370  -0.400  1.00 57.54  ? 232 ALA A CB    1 
ATOM   1698 N N     . GLU A 1 261 ? -21.709 38.036  2.454   1.00 59.52  ? 233 GLU A N     1 
ATOM   1699 C CA    . GLU A 1 261 ? -21.597 38.313  3.881   1.00 62.67  ? 233 GLU A CA    1 
ATOM   1700 C C     . GLU A 1 261 ? -20.585 37.406  4.572   1.00 59.92  ? 233 GLU A C     1 
ATOM   1701 O O     . GLU A 1 261 ? -19.915 37.846  5.513   1.00 62.93  ? 233 GLU A O     1 
ATOM   1702 C CB    . GLU A 1 261 ? -22.966 38.195  4.553   1.00 67.35  ? 233 GLU A CB    1 
ATOM   1703 C CG    . GLU A 1 261 ? -22.969 38.648  6.006   1.00 71.84  ? 233 GLU A CG    1 
ATOM   1704 C CD    . GLU A 1 261 ? -24.363 38.846  6.562   1.00 79.13  ? 233 GLU A CD    1 
ATOM   1705 O OE1   . GLU A 1 261 ? -25.332 38.792  5.776   1.00 84.19  ? 233 GLU A OE1   1 
ATOM   1706 O OE2   . GLU A 1 261 ? -24.492 39.058  7.787   1.00 80.47  ? 233 GLU A OE2   1 
ATOM   1707 N N     . THR A 1 262 ? -20.451 36.151  4.132   1.00 58.35  ? 234 THR A N     1 
ATOM   1708 C CA    . THR A 1 262 ? -19.407 35.297  4.690   1.00 53.60  ? 234 THR A CA    1 
ATOM   1709 C C     . THR A 1 262 ? -18.015 35.819  4.364   1.00 54.01  ? 234 THR A C     1 
ATOM   1710 O O     . THR A 1 262 ? -17.066 35.524  5.098   1.00 51.12  ? 234 THR A O     1 
ATOM   1711 C CB    . THR A 1 262 ? -19.554 33.859  4.190   1.00 46.13  ? 234 THR A CB    1 
ATOM   1712 O OG1   . THR A 1 262 ? -19.529 33.841  2.757   1.00 56.29  ? 234 THR A OG1   1 
ATOM   1713 C CG2   . THR A 1 262 ? -20.855 33.258  4.685   1.00 43.30  ? 234 THR A CG2   1 
ATOM   1714 N N     . HIS A 1 263 ? -17.872 36.579  3.277   1.00 54.89  ? 235 HIS A N     1 
ATOM   1715 C CA    . HIS A 1 263 ? -16.639 37.327  3.060   1.00 48.57  ? 235 HIS A CA    1 
ATOM   1716 C C     . HIS A 1 263 ? -16.488 38.430  4.099   1.00 50.42  ? 235 HIS A C     1 
ATOM   1717 O O     . HIS A 1 263 ? -15.381 38.694  4.581   1.00 48.36  ? 235 HIS A O     1 
ATOM   1718 C CB    . HIS A 1 263 ? -16.626 37.909  1.647   1.00 47.30  ? 235 HIS A CB    1 
ATOM   1719 C CG    . HIS A 1 263 ? -15.466 38.815  1.376   1.00 43.66  ? 235 HIS A CG    1 
ATOM   1720 N ND1   . HIS A 1 263 ? -14.157 38.394  1.459   1.00 43.07  ? 235 HIS A ND1   1 
ATOM   1721 C CD2   . HIS A 1 263 ? -15.420 40.121  1.024   1.00 44.67  ? 235 HIS A CD2   1 
ATOM   1722 C CE1   . HIS A 1 263 ? -13.353 39.401  1.169   1.00 43.05  ? 235 HIS A CE1   1 
ATOM   1723 N NE2   . HIS A 1 263 ? -14.094 40.461  0.901   1.00 44.26  ? 235 HIS A NE2   1 
ATOM   1724 N N     . ARG A 1 264 ? -17.598 39.076  4.463   1.00 51.18  ? 236 ARG A N     1 
ATOM   1725 C CA    . ARG A 1 264 ? -17.571 40.142  5.458   1.00 49.16  ? 236 ARG A CA    1 
ATOM   1726 C C     . ARG A 1 264 ? -17.465 39.582  6.871   1.00 50.54  ? 236 ARG A C     1 
ATOM   1727 O O     . ARG A 1 264 ? -16.649 40.050  7.672   1.00 50.65  ? 236 ARG A O     1 
ATOM   1728 C CB    . ARG A 1 264 ? -18.823 41.012  5.314   1.00 55.53  ? 236 ARG A CB    1 
ATOM   1729 C CG    . ARG A 1 264 ? -18.818 42.288  6.140   1.00 52.05  ? 236 ARG A CG    1 
ATOM   1730 C CD    . ARG A 1 264 ? -20.033 43.144  5.807   1.00 49.60  ? 236 ARG A CD    1 
ATOM   1731 N NE    . ARG A 1 264 ? -20.069 44.386  6.571   1.00 56.64  ? 236 ARG A NE    1 
ATOM   1732 C CZ    . ARG A 1 264 ? -20.538 44.495  7.807   1.00 64.06  ? 236 ARG A CZ    1 
ATOM   1733 N NH1   . ARG A 1 264 ? -21.019 43.449  8.459   1.00 64.35  ? 236 ARG A NH1   1 
ATOM   1734 N NH2   . ARG A 1 264 ? -20.526 45.684  8.403   1.00 57.45  ? 236 ARG A NH2   1 
ATOM   1735 N N     . GLU A 1 265 ? -18.283 38.574  7.193   1.00 54.46  ? 237 GLU A N     1 
ATOM   1736 C CA    . GLU A 1 265 ? -18.288 38.022  8.544   1.00 52.22  ? 237 GLU A CA    1 
ATOM   1737 C C     . GLU A 1 265 ? -16.963 37.357  8.892   1.00 49.46  ? 237 GLU A C     1 
ATOM   1738 O O     . GLU A 1 265 ? -16.558 37.361  10.061  1.00 49.72  ? 237 GLU A O     1 
ATOM   1739 C CB    . GLU A 1 265 ? -19.434 37.022  8.705   1.00 50.96  ? 237 GLU A CB    1 
ATOM   1740 C CG    . GLU A 1 265 ? -20.823 37.635  8.645   1.00 57.70  ? 237 GLU A CG    1 
ATOM   1741 C CD    . GLU A 1 265 ? -21.039 38.710  9.693   1.00 70.03  ? 237 GLU A CD    1 
ATOM   1742 O OE1   . GLU A 1 265 ? -20.569 38.531  10.837  1.00 67.33  ? 237 GLU A OE1   1 
ATOM   1743 O OE2   . GLU A 1 265 ? -21.681 39.733  9.373   1.00 75.64  ? 237 GLU A OE2   1 
ATOM   1744 N N     . PHE A 1 266 ? -16.278 36.775  7.905   1.00 45.73  ? 238 PHE A N     1 
ATOM   1745 C CA    . PHE A 1 266 ? -14.970 36.186  8.174   1.00 41.22  ? 238 PHE A CA    1 
ATOM   1746 C C     . PHE A 1 266 ? -13.951 37.257  8.538   1.00 41.89  ? 238 PHE A C     1 
ATOM   1747 O O     . PHE A 1 266 ? -13.116 37.051  9.427   1.00 42.38  ? 238 PHE A O     1 
ATOM   1748 C CB    . PHE A 1 266 ? -14.487 35.383  6.968   1.00 40.40  ? 238 PHE A CB    1 
ATOM   1749 C CG    . PHE A 1 266 ? -13.142 34.743  7.168   1.00 39.32  ? 238 PHE A CG    1 
ATOM   1750 C CD1   . PHE A 1 266 ? -13.023 33.550  7.861   1.00 38.51  ? 238 PHE A CD1   1 
ATOM   1751 C CD2   . PHE A 1 266 ? -11.995 35.339  6.669   1.00 39.20  ? 238 PHE A CD2   1 
ATOM   1752 C CE1   . PHE A 1 266 ? -11.786 32.962  8.048   1.00 37.60  ? 238 PHE A CE1   1 
ATOM   1753 C CE2   . PHE A 1 266 ? -10.757 34.756  6.852   1.00 38.30  ? 238 PHE A CE2   1 
ATOM   1754 C CZ    . PHE A 1 266 ? -10.652 33.566  7.543   1.00 37.50  ? 238 PHE A CZ    1 
ATOM   1755 N N     . LEU A 1 267 ? -14.002 38.406  7.862   1.00 44.67  ? 239 LEU A N     1 
ATOM   1756 C CA    . LEU A 1 267 ? -13.067 39.483  8.157   1.00 42.74  ? 239 LEU A CA    1 
ATOM   1757 C C     . LEU A 1 267 ? -13.310 40.096  9.530   1.00 44.46  ? 239 LEU A C     1 
ATOM   1758 O O     . LEU A 1 267 ? -12.403 40.729  10.080  1.00 45.96  ? 239 LEU A O     1 
ATOM   1759 C CB    . LEU A 1 267 ? -13.147 40.554  7.068   1.00 43.59  ? 239 LEU A CB    1 
ATOM   1760 C CG    . LEU A 1 267 ? -12.458 40.168  5.757   1.00 42.95  ? 239 LEU A CG    1 
ATOM   1761 C CD1   . LEU A 1 267 ? -12.750 41.177  4.657   1.00 43.91  ? 239 LEU A CD1   1 
ATOM   1762 C CD2   . LEU A 1 267 ? -10.958 40.012  5.964   1.00 42.20  ? 239 LEU A CD2   1 
ATOM   1763 N N     . LYS A 1 268 ? -14.510 39.924  10.092  1.00 43.92  ? 240 LYS A N     1 
ATOM   1764 C CA    . LYS A 1 268 ? -14.747 40.339  11.472  1.00 44.54  ? 240 LYS A CA    1 
ATOM   1765 C C     . LYS A 1 268 ? -13.853 39.570  12.436  1.00 43.62  ? 240 LYS A C     1 
ATOM   1766 O O     . LYS A 1 268 ? -13.343 40.136  13.410  1.00 44.01  ? 240 LYS A O     1 
ATOM   1767 C CB    . LYS A 1 268 ? -16.216 40.134  11.843  1.00 45.18  ? 240 LYS A CB    1 
ATOM   1768 C CG    . LYS A 1 268 ? -17.131 41.299  11.516  1.00 48.83  ? 240 LYS A CG    1 
ATOM   1769 C CD    . LYS A 1 268 ? -18.536 41.063  12.055  1.00 57.93  ? 240 LYS A CD    1 
ATOM   1770 C CE    . LYS A 1 268 ? -19.450 42.244  11.763  1.00 68.62  ? 240 LYS A CE    1 
ATOM   1771 N NZ    . LYS A 1 268 ? -20.839 42.006  12.246  1.00 74.01  ? 240 LYS A NZ    1 
ATOM   1772 N N     . SER A 1 269 ? -13.648 38.277  12.175  1.00 42.46  ? 241 SER A N     1 
ATOM   1773 C CA    . SER A 1 269 ? -12.917 37.435  13.116  1.00 41.63  ? 241 SER A CA    1 
ATOM   1774 C C     . SER A 1 269 ? -11.422 37.731  13.091  1.00 41.22  ? 241 SER A C     1 
ATOM   1775 O O     . SER A 1 269 ? -10.779 37.785  14.146  1.00 42.65  ? 241 SER A O     1 
ATOM   1776 C CB    . SER A 1 269 ? -13.172 35.961  12.802  1.00 43.46  ? 241 SER A CB    1 
ATOM   1777 O OG    . SER A 1 269 ? -12.380 35.529  11.709  1.00 39.81  ? 241 SER A OG    1 
ATOM   1778 N N     . VAL A 1 270 ? -10.854 37.933  11.904  1.00 40.97  ? 242 VAL A N     1 
ATOM   1779 C CA    . VAL A 1 270 ? -9.410  38.082  11.760  1.00 40.54  ? 242 VAL A CA    1 
ATOM   1780 C C     . VAL A 1 270 ? -8.989  39.526  12.001  1.00 43.91  ? 242 VAL A C     1 
ATOM   1781 O O     . VAL A 1 270 ? -7.827  39.888  11.784  1.00 48.60  ? 242 VAL A O     1 
ATOM   1782 C CB    . VAL A 1 270 ? -8.942  37.596  10.377  1.00 39.84  ? 242 VAL A CB    1 
ATOM   1783 C CG1   . VAL A 1 270 ? -9.417  36.173  10.130  1.00 38.94  ? 242 VAL A CG1   1 
ATOM   1784 C CG2   . VAL A 1 270 ? -9.449  38.528  9.287   1.00 41.75  ? 242 VAL A CG2   1 
ATOM   1785 N N     . CYS A 1 271 ? -9.923  40.362  12.452  1.00 42.65  ? 243 CYS A N     1 
ATOM   1786 C CA    . CYS A 1 271 ? -9.616  41.743  12.812  1.00 43.79  ? 243 CYS A CA    1 
ATOM   1787 C C     . CYS A 1 271 ? -9.117  41.756  14.253  1.00 51.34  ? 243 CYS A C     1 
ATOM   1788 O O     . CYS A 1 271 ? -9.899  41.577  15.192  1.00 49.81  ? 243 CYS A O     1 
ATOM   1789 C CB    . CYS A 1 271 ? -10.839 42.638  12.637  1.00 44.99  ? 243 CYS A CB    1 
ATOM   1790 S SG    . CYS A 1 271 ? -10.505 44.392  12.915  1.00 48.22  ? 243 CYS A SG    1 
ATOM   1791 N N     . ALA A 1 272 ? -7.813  41.977  14.426  1.00 55.35  ? 244 ALA A N     1 
ATOM   1792 C CA    . ALA A 1 272 ? -7.173  41.782  15.721  1.00 54.59  ? 244 ALA A CA    1 
ATOM   1793 C C     . ALA A 1 272 ? -7.409  42.928  16.696  1.00 49.62  ? 244 ALA A C     1 
ATOM   1794 O O     . ALA A 1 272 ? -7.168  42.753  17.895  1.00 52.67  ? 244 ALA A O     1 
ATOM   1795 C CB    . ALA A 1 272 ? -5.668  41.578  15.535  1.00 58.55  ? 244 ALA A CB    1 
ATOM   1796 N N     . PHE A 1 273 ? -7.868  44.087  16.226  1.00 47.66  ? 245 PHE A N     1 
ATOM   1797 C CA    . PHE A 1 273 ? -8.020  45.252  17.088  1.00 47.61  ? 245 PHE A CA    1 
ATOM   1798 C C     . PHE A 1 273 ? -9.428  45.428  17.642  1.00 48.39  ? 245 PHE A C     1 
ATOM   1799 O O     . PHE A 1 273 ? -9.624  46.277  18.518  1.00 49.59  ? 245 PHE A O     1 
ATOM   1800 C CB    . PHE A 1 273 ? -7.622  46.527  16.337  1.00 48.56  ? 245 PHE A CB    1 
ATOM   1801 C CG    . PHE A 1 273 ? -6.142  46.750  16.256  1.00 48.40  ? 245 PHE A CG    1 
ATOM   1802 C CD1   . PHE A 1 273 ? -5.469  47.396  17.279  1.00 49.25  ? 245 PHE A CD1   1 
ATOM   1803 C CD2   . PHE A 1 273 ? -5.423  46.324  15.152  1.00 47.50  ? 245 PHE A CD2   1 
ATOM   1804 C CE1   . PHE A 1 273 ? -4.107  47.608  17.208  1.00 49.20  ? 245 PHE A CE1   1 
ATOM   1805 C CE2   . PHE A 1 273 ? -4.060  46.533  15.074  1.00 47.44  ? 245 PHE A CE2   1 
ATOM   1806 C CZ    . PHE A 1 273 ? -3.401  47.176  16.104  1.00 48.30  ? 245 PHE A CZ    1 
ATOM   1807 N N     . LEU A 1 274 ? -10.406 44.655  17.165  1.00 47.81  ? 246 LEU A N     1 
ATOM   1808 C CA    . LEU A 1 274 ? -11.793 44.882  17.558  1.00 48.66  ? 246 LEU A CA    1 
ATOM   1809 C C     . LEU A 1 274 ? -12.045 44.617  19.037  1.00 48.99  ? 246 LEU A C     1 
ATOM   1810 O O     . LEU A 1 274 ? -13.001 45.166  19.595  1.00 50.12  ? 246 LEU A O     1 
ATOM   1811 C CB    . LEU A 1 274 ? -12.729 44.020  16.712  1.00 47.97  ? 246 LEU A CB    1 
ATOM   1812 C CG    . LEU A 1 274 ? -13.097 44.612  15.351  1.00 48.32  ? 246 LEU A CG    1 
ATOM   1813 C CD1   . LEU A 1 274 ? -13.952 43.642  14.550  1.00 47.60  ? 246 LEU A CD1   1 
ATOM   1814 C CD2   . LEU A 1 274 ? -13.804 45.948  15.521  1.00 49.98  ? 246 LEU A CD2   1 
ATOM   1815 N N     . TYR A 1 275 ? -11.218 43.796  19.687  1.00 49.91  ? 247 TYR A N     1 
ATOM   1816 C CA    . TYR A 1 275 ? -11.416 43.525  21.105  1.00 51.53  ? 247 TYR A CA    1 
ATOM   1817 C C     . TYR A 1 275 ? -11.065 44.717  21.987  1.00 55.48  ? 247 TYR A C     1 
ATOM   1818 O O     . TYR A 1 275 ? -11.415 44.712  23.172  1.00 59.13  ? 247 TYR A O     1 
ATOM   1819 C CB    . TYR A 1 275 ? -10.597 42.300  21.527  1.00 50.56  ? 247 TYR A CB    1 
ATOM   1820 C CG    . TYR A 1 275 ? -9.138  42.592  21.795  1.00 51.41  ? 247 TYR A CG    1 
ATOM   1821 C CD1   . TYR A 1 275 ? -8.205  42.568  20.769  1.00 48.70  ? 247 TYR A CD1   1 
ATOM   1822 C CD2   . TYR A 1 275 ? -8.691  42.879  23.078  1.00 57.23  ? 247 TYR A CD2   1 
ATOM   1823 C CE1   . TYR A 1 275 ? -6.871  42.834  21.010  1.00 49.76  ? 247 TYR A CE1   1 
ATOM   1824 C CE2   . TYR A 1 275 ? -7.365  43.148  23.326  1.00 57.70  ? 247 TYR A CE2   1 
ATOM   1825 C CZ    . TYR A 1 275 ? -6.458  43.122  22.291  1.00 56.69  ? 247 TYR A CZ    1 
ATOM   1826 O OH    . TYR A 1 275 ? -5.133  43.388  22.545  1.00 64.23  ? 247 TYR A OH    1 
ATOM   1827 N N     . ARG A 1 276 ? -10.382 45.728  21.447  1.00 52.75  ? 248 ARG A N     1 
ATOM   1828 C CA    . ARG A 1 276 ? -10.028 46.916  22.212  1.00 53.69  ? 248 ARG A CA    1 
ATOM   1829 C C     . ARG A 1 276 ? -11.032 48.049  22.057  1.00 62.09  ? 248 ARG A C     1 
ATOM   1830 O O     . ARG A 1 276 ? -11.058 48.954  22.899  1.00 63.81  ? 248 ARG A O     1 
ATOM   1831 C CB    . ARG A 1 276 ? -8.646  47.429  21.792  1.00 51.77  ? 248 ARG A CB    1 
ATOM   1832 C CG    . ARG A 1 276 ? -7.493  46.493  22.098  1.00 52.89  ? 248 ARG A CG    1 
ATOM   1833 C CD    . ARG A 1 276 ? -6.168  47.134  21.715  1.00 54.18  ? 248 ARG A CD    1 
ATOM   1834 N NE    . ARG A 1 276 ? -5.027  46.281  22.023  1.00 56.84  ? 248 ARG A NE    1 
ATOM   1835 C CZ    . ARG A 1 276 ? -3.760  46.651  21.893  1.00 56.14  ? 248 ARG A CZ    1 
ATOM   1836 N NH1   . ARG A 1 276 ? -3.433  47.857  21.458  1.00 55.24  ? 248 ARG A NH1   1 
ATOM   1837 N NH2   . ARG A 1 276 ? -2.797  45.789  22.206  1.00 59.01  ? 248 ARG A NH2   1 
ATOM   1838 N N     . ILE A 1 277 ? -11.853 48.021  21.012  1.00 60.32  ? 249 ILE A N     1 
ATOM   1839 C CA    . ILE A 1 277 ? -12.721 49.144  20.668  1.00 61.40  ? 249 ILE A CA    1 
ATOM   1840 C C     . ILE A 1 277 ? -14.071 48.997  21.361  1.00 66.46  ? 249 ILE A C     1 
ATOM   1841 O O     . ILE A 1 277 ? -14.658 47.906  21.346  1.00 65.84  ? 249 ILE A O     1 
ATOM   1842 C CB    . ILE A 1 277 ? -12.895 49.253  19.145  1.00 56.92  ? 249 ILE A CB    1 
ATOM   1843 C CG1   . ILE A 1 277 ? -11.532 49.342  18.457  1.00 53.49  ? 249 ILE A CG1   1 
ATOM   1844 C CG2   . ILE A 1 277 ? -13.739 50.460  18.791  1.00 67.59  ? 249 ILE A CG2   1 
ATOM   1845 C CD1   . ILE A 1 277 ? -10.688 50.506  18.924  1.00 54.66  ? 249 ILE A CD1   1 
ATOM   1846 N N     . PRO A 1 278 ? -14.591 50.051  21.986  1.00 64.37  ? 250 PRO A N     1 
ATOM   1847 C CA    . PRO A 1 278 ? -15.952 49.994  22.534  1.00 69.64  ? 250 PRO A CA    1 
ATOM   1848 C C     . PRO A 1 278 ? -16.986 49.846  21.426  1.00 72.90  ? 250 PRO A C     1 
ATOM   1849 O O     . PRO A 1 278 ? -16.702 50.007  20.238  1.00 78.85  ? 250 PRO A O     1 
ATOM   1850 C CB    . PRO A 1 278 ? -16.103 51.330  23.268  1.00 76.47  ? 250 PRO A CB    1 
ATOM   1851 C CG    . PRO A 1 278 ? -14.702 51.782  23.534  1.00 72.48  ? 250 PRO A CG    1 
ATOM   1852 C CD    . PRO A 1 278 ? -13.884 51.280  22.382  1.00 62.96  ? 250 PRO A CD    1 
ATOM   1853 N N     . GLU A 1 279 ? -18.221 49.551  21.845  1.00 74.00  ? 251 GLU A N     1 
ATOM   1854 C CA    . GLU A 1 279 ? -19.256 49.157  20.892  1.00 84.85  ? 251 GLU A CA    1 
ATOM   1855 C C     . GLU A 1 279 ? -19.632 50.294  19.948  1.00 88.21  ? 251 GLU A C     1 
ATOM   1856 O O     . GLU A 1 279 ? -19.841 50.063  18.750  1.00 87.11  ? 251 GLU A O     1 
ATOM   1857 C CB    . GLU A 1 279 ? -20.493 48.653  21.634  1.00 84.18  ? 251 GLU A CB    1 
ATOM   1858 C CG    . GLU A 1 279 ? -21.617 48.212  20.707  1.00 92.66  ? 251 GLU A CG    1 
ATOM   1859 C CD    . GLU A 1 279 ? -21.186 47.122  19.743  1.00 99.16  ? 251 GLU A CD    1 
ATOM   1860 O OE1   . GLU A 1 279 ? -20.354 46.273  20.129  1.00 101.38 ? 251 GLU A OE1   1 
ATOM   1861 O OE2   . GLU A 1 279 ? -21.676 47.120  18.593  1.00 93.95  ? 251 GLU A OE2   1 
ATOM   1862 N N     . GLU A 1 280 ? -19.726 51.524  20.459  1.00 85.94  ? 252 GLU A N     1 
ATOM   1863 C CA    . GLU A 1 280 ? -20.160 52.635  19.617  1.00 85.38  ? 252 GLU A CA    1 
ATOM   1864 C C     . GLU A 1 280 ? -19.195 52.904  18.470  1.00 84.54  ? 252 GLU A C     1 
ATOM   1865 O O     . GLU A 1 280 ? -19.564 53.597  17.515  1.00 89.51  ? 252 GLU A O     1 
ATOM   1866 C CB    . GLU A 1 280 ? -20.334 53.905  20.453  1.00 91.89  ? 252 GLU A CB    1 
ATOM   1867 C CG    . GLU A 1 280 ? -19.040 54.473  21.011  1.00 90.20  ? 252 GLU A CG    1 
ATOM   1868 C CD    . GLU A 1 280 ? -18.734 53.970  22.406  1.00 86.41  ? 252 GLU A CD    1 
ATOM   1869 O OE1   . GLU A 1 280 ? -19.193 52.862  22.755  1.00 87.71  ? 252 GLU A OE1   1 
ATOM   1870 O OE2   . GLU A 1 280 ? -18.036 54.685  23.156  1.00 80.86  ? 252 GLU A OE2   1 
ATOM   1871 N N     . GLN A 1 281 ? -17.976 52.371  18.536  1.00 78.78  ? 253 GLN A N     1 
ATOM   1872 C CA    . GLN A 1 281 ? -16.998 52.532  17.472  1.00 74.01  ? 253 GLN A CA    1 
ATOM   1873 C C     . GLN A 1 281 ? -16.516 51.208  16.895  1.00 69.68  ? 253 GLN A C     1 
ATOM   1874 O O     . GLN A 1 281 ? -15.697 51.219  15.969  1.00 66.62  ? 253 GLN A O     1 
ATOM   1875 C CB    . GLN A 1 281 ? -15.799 53.349  17.975  1.00 69.91  ? 253 GLN A CB    1 
ATOM   1876 C CG    . GLN A 1 281 ? -16.149 54.783  18.346  1.00 73.09  ? 253 GLN A CG    1 
ATOM   1877 C CD    . GLN A 1 281 ? -14.933 55.613  18.711  1.00 72.47  ? 253 GLN A CD    1 
ATOM   1878 O OE1   . GLN A 1 281 ? -13.984 55.721  17.934  1.00 73.95  ? 253 GLN A OE1   1 
ATOM   1879 N NE2   . GLN A 1 281 ? -14.957 56.208  19.899  1.00 67.34  ? 253 GLN A NE2   1 
ATOM   1880 N N     . LYS A 1 282 ? -16.993 50.072  17.415  1.00 73.41  ? 254 LYS A N     1 
ATOM   1881 C CA    . LYS A 1 282 ? -16.644 48.775  16.839  1.00 68.06  ? 254 LYS A CA    1 
ATOM   1882 C C     . LYS A 1 282 ? -17.060 48.696  15.377  1.00 63.67  ? 254 LYS A C     1 
ATOM   1883 O O     . LYS A 1 282 ? -16.237 48.434  14.493  1.00 65.05  ? 254 LYS A O     1 
ATOM   1884 C CB    . LYS A 1 282 ? -17.300 47.644  17.632  1.00 71.33  ? 254 LYS A CB    1 
ATOM   1885 C CG    . LYS A 1 282 ? -16.540 47.175  18.857  1.00 69.10  ? 254 LYS A CG    1 
ATOM   1886 C CD    . LYS A 1 282 ? -17.197 45.931  19.435  1.00 66.96  ? 254 LYS A CD    1 
ATOM   1887 C CE    . LYS A 1 282 ? -16.401 45.353  20.589  1.00 58.75  ? 254 LYS A CE    1 
ATOM   1888 N NZ    . LYS A 1 282 ? -17.128 44.231  21.245  1.00 68.48  ? 254 LYS A NZ    1 
ATOM   1889 N N     . ASP A 1 283 ? -18.348 48.915  15.107  1.00 65.81  ? 255 ASP A N     1 
ATOM   1890 C CA    . ASP A 1 283 ? -18.850 48.856  13.740  1.00 62.61  ? 255 ASP A CA    1 
ATOM   1891 C C     . ASP A 1 283 ? -18.233 49.930  12.856  1.00 62.50  ? 255 ASP A C     1 
ATOM   1892 O O     . ASP A 1 283 ? -18.296 49.821  11.627  1.00 62.47  ? 255 ASP A O     1 
ATOM   1893 C CB    . ASP A 1 283 ? -20.374 48.986  13.743  1.00 69.89  ? 255 ASP A CB    1 
ATOM   1894 C CG    . ASP A 1 283 ? -21.046 47.907  14.571  1.00 79.19  ? 255 ASP A CG    1 
ATOM   1895 O OD1   . ASP A 1 283 ? -20.445 46.826  14.744  1.00 85.60  ? 255 ASP A OD1   1 
ATOM   1896 O OD2   . ASP A 1 283 ? -22.174 48.143  15.055  1.00 80.05  ? 255 ASP A OD2   1 
ATOM   1897 N N     . ASP A 1 284 ? -17.640 50.962  13.455  1.00 61.18  ? 256 ASP A N     1 
ATOM   1898 C CA    . ASP A 1 284 ? -16.947 52.003  12.708  1.00 63.51  ? 256 ASP A CA    1 
ATOM   1899 C C     . ASP A 1 284 ? -15.501 51.628  12.415  1.00 57.57  ? 256 ASP A C     1 
ATOM   1900 O O     . ASP A 1 284 ? -14.988 51.941  11.336  1.00 55.99  ? 256 ASP A O     1 
ATOM   1901 C CB    . ASP A 1 284 ? -17.000 53.322  13.481  1.00 70.27  ? 256 ASP A CB    1 
ATOM   1902 C CG    . ASP A 1 284 ? -18.417 53.806  13.706  1.00 72.71  ? 256 ASP A CG    1 
ATOM   1903 O OD1   . ASP A 1 284 ? -19.333 53.302  13.022  1.00 65.87  ? 256 ASP A OD1   1 
ATOM   1904 O OD2   . ASP A 1 284 ? -18.613 54.688  14.570  1.00 77.09  ? 256 ASP A OD2   1 
ATOM   1905 N N     . PHE A 1 285 ? -14.832 50.966  13.364  1.00 56.61  ? 257 PHE A N     1 
ATOM   1906 C CA    . PHE A 1 285 ? -13.495 50.446  13.101  1.00 53.98  ? 257 PHE A CA    1 
ATOM   1907 C C     . PHE A 1 285 ? -13.519 49.420  11.977  1.00 52.64  ? 257 PHE A C     1 
ATOM   1908 O O     . PHE A 1 285 ? -12.560 49.323  11.204  1.00 51.98  ? 257 PHE A O     1 
ATOM   1909 C CB    . PHE A 1 285 ? -12.912 49.836  14.381  1.00 53.36  ? 257 PHE A CB    1 
ATOM   1910 C CG    . PHE A 1 285 ? -11.436 49.538  14.306  1.00 52.42  ? 257 PHE A CG    1 
ATOM   1911 C CD1   . PHE A 1 285 ? -10.966 48.412  13.649  1.00 50.88  ? 257 PHE A CD1   1 
ATOM   1912 C CD2   . PHE A 1 285 ? -10.519 50.388  14.902  1.00 53.17  ? 257 PHE A CD2   1 
ATOM   1913 C CE1   . PHE A 1 285 ? -9.612  48.143  13.584  1.00 50.10  ? 257 PHE A CE1   1 
ATOM   1914 C CE2   . PHE A 1 285 ? -9.164  50.124  14.840  1.00 52.41  ? 257 PHE A CE2   1 
ATOM   1915 C CZ    . PHE A 1 285 ? -8.711  49.001  14.179  1.00 50.88  ? 257 PHE A CZ    1 
ATOM   1916 N N     . PHE A 1 286 ? -14.611 48.662  11.861  1.00 52.84  ? 258 PHE A N     1 
ATOM   1917 C CA    . PHE A 1 286 ? -14.708 47.645  10.820  1.00 51.15  ? 258 PHE A CA    1 
ATOM   1918 C C     . PHE A 1 286 ? -14.869 48.277  9.442   1.00 54.15  ? 258 PHE A C     1 
ATOM   1919 O O     . PHE A 1 286 ? -14.136 47.939  8.504   1.00 54.39  ? 258 PHE A O     1 
ATOM   1920 C CB    . PHE A 1 286 ? -15.872 46.702  11.120  1.00 50.83  ? 258 PHE A CB    1 
ATOM   1921 C CG    . PHE A 1 286 ? -15.824 45.421  10.345  1.00 49.45  ? 258 PHE A CG    1 
ATOM   1922 C CD1   . PHE A 1 286 ? -14.650 44.693  10.258  1.00 48.16  ? 258 PHE A CD1   1 
ATOM   1923 C CD2   . PHE A 1 286 ? -16.950 44.948  9.693   1.00 49.54  ? 258 PHE A CD2   1 
ATOM   1924 C CE1   . PHE A 1 286 ? -14.600 43.513  9.541   1.00 46.97  ? 258 PHE A CE1   1 
ATOM   1925 C CE2   . PHE A 1 286 ? -16.907 43.770  8.974   1.00 49.33  ? 258 PHE A CE2   1 
ATOM   1926 C CZ    . PHE A 1 286 ? -15.730 43.052  8.896   1.00 47.08  ? 258 PHE A CZ    1 
ATOM   1927 N N     . ASP A 1 287 ? -15.830 49.194  9.297   1.00 54.34  ? 259 ASP A N     1 
ATOM   1928 C CA    . ASP A 1 287 ? -16.049 49.837  8.004   1.00 56.20  ? 259 ASP A CA    1 
ATOM   1929 C C     . ASP A 1 287 ? -14.842 50.669  7.589   1.00 55.81  ? 259 ASP A C     1 
ATOM   1930 O O     . ASP A 1 287 ? -14.483 50.709  6.406   1.00 55.70  ? 259 ASP A O     1 
ATOM   1931 C CB    . ASP A 1 287 ? -17.310 50.699  8.051   1.00 63.32  ? 259 ASP A CB    1 
ATOM   1932 C CG    . ASP A 1 287 ? -18.580 49.871  8.074   1.00 71.85  ? 259 ASP A CG    1 
ATOM   1933 O OD1   . ASP A 1 287 ? -18.679 48.952  8.914   1.00 72.73  ? 259 ASP A OD1   1 
ATOM   1934 O OD2   . ASP A 1 287 ? -19.480 50.140  7.251   1.00 78.49  ? 259 ASP A OD2   1 
ATOM   1935 N N     . ASP A 1 288 ? -14.208 51.347  8.549   1.00 55.01  ? 260 ASP A N     1 
ATOM   1936 C CA    . ASP A 1 288 ? -12.947 52.026  8.267   1.00 56.93  ? 260 ASP A CA    1 
ATOM   1937 C C     . ASP A 1 288 ? -11.896 51.038  7.777   1.00 54.01  ? 260 ASP A C     1 
ATOM   1938 O O     . ASP A 1 288 ? -11.112 51.344  6.871   1.00 53.06  ? 260 ASP A O     1 
ATOM   1939 C CB    . ASP A 1 288 ? -12.460 52.751  9.522   1.00 55.71  ? 260 ASP A CB    1 
ATOM   1940 C CG    . ASP A 1 288 ? -11.453 53.838  9.216   1.00 61.57  ? 260 ASP A CG    1 
ATOM   1941 O OD1   . ASP A 1 288 ? -11.552 54.461  8.138   1.00 71.64  ? 260 ASP A OD1   1 
ATOM   1942 O OD2   . ASP A 1 288 ? -10.555 54.065  10.054  1.00 59.25  ? 260 ASP A OD2   1 
ATOM   1943 N N     . TRP A 1 289 ? -11.876 49.841  8.365   1.00 56.15  ? 261 TRP A N     1 
ATOM   1944 C CA    . TRP A 1 289 ? -10.929 48.808  7.959   1.00 50.36  ? 261 TRP A CA    1 
ATOM   1945 C C     . TRP A 1 289 ? -11.271 48.257  6.581   1.00 49.83  ? 261 TRP A C     1 
ATOM   1946 O O     . TRP A 1 289 ? -10.411 48.198  5.695   1.00 49.88  ? 261 TRP A O     1 
ATOM   1947 C CB    . TRP A 1 289 ? -10.923 47.691  9.002   1.00 49.64  ? 261 TRP A CB    1 
ATOM   1948 C CG    . TRP A 1 289 ? -9.764  46.755  8.928   1.00 49.77  ? 261 TRP A CG    1 
ATOM   1949 C CD1   . TRP A 1 289 ? -8.442  47.081  8.839   1.00 48.49  ? 261 TRP A CD1   1 
ATOM   1950 C CD2   . TRP A 1 289 ? -9.826  45.326  8.953   1.00 46.58  ? 261 TRP A CD2   1 
ATOM   1951 N NE1   . TRP A 1 289 ? -7.677  45.939  8.803   1.00 46.48  ? 261 TRP A NE1   1 
ATOM   1952 C CE2   . TRP A 1 289 ? -8.504  44.849  8.870   1.00 45.69  ? 261 TRP A CE2   1 
ATOM   1953 C CE3   . TRP A 1 289 ? -10.873 44.403  9.034   1.00 46.11  ? 261 TRP A CE3   1 
ATOM   1954 C CZ2   . TRP A 1 289 ? -8.202  43.491  8.868   1.00 51.10  ? 261 TRP A CZ2   1 
ATOM   1955 C CZ3   . TRP A 1 289 ? -10.572 43.057  9.028   1.00 44.77  ? 261 TRP A CZ3   1 
ATOM   1956 C CH2   . TRP A 1 289 ? -9.248  42.612  8.945   1.00 50.76  ? 261 TRP A CH2   1 
ATOM   1957 N N     . LEU A 1 290 ? -12.530 47.852  6.382   1.00 49.92  ? 262 LEU A N     1 
ATOM   1958 C CA    . LEU A 1 290 ? -12.924 47.222  5.125   1.00 49.43  ? 262 LEU A CA    1 
ATOM   1959 C C     . LEU A 1 290 ? -12.750 48.172  3.946   1.00 51.22  ? 262 LEU A C     1 
ATOM   1960 O O     . LEU A 1 290 ? -12.344 47.751  2.856   1.00 49.74  ? 262 LEU A O     1 
ATOM   1961 C CB    . LEU A 1 290 ? -14.373 46.742  5.211   1.00 49.64  ? 262 LEU A CB    1 
ATOM   1962 C CG    . LEU A 1 290 ? -14.670 45.512  6.073   1.00 48.63  ? 262 LEU A CG    1 
ATOM   1963 C CD1   . LEU A 1 290 ? -15.983 44.871  5.650   1.00 48.71  ? 262 LEU A CD1   1 
ATOM   1964 C CD2   . LEU A 1 290 ? -13.532 44.507  6.005   1.00 47.15  ? 262 LEU A CD2   1 
ATOM   1965 N N     . GLN A 1 291 ? -13.060 49.456  4.142   1.00 58.06  ? 263 GLN A N     1 
ATOM   1966 C CA    . GLN A 1 291 ? -12.877 50.433  3.073   1.00 57.50  ? 263 GLN A CA    1 
ATOM   1967 C C     . GLN A 1 291 ? -11.409 50.545  2.682   1.00 55.17  ? 263 GLN A C     1 
ATOM   1968 O O     . GLN A 1 291 ? -11.074 50.565  1.491   1.00 55.43  ? 263 GLN A O     1 
ATOM   1969 C CB    . GLN A 1 291 ? -13.424 51.793  3.505   1.00 56.28  ? 263 GLN A CB    1 
ATOM   1970 C CG    . GLN A 1 291 ? -12.706 52.980  2.884   1.00 57.29  ? 263 GLN A CG    1 
ATOM   1971 C CD    . GLN A 1 291 ? -13.237 54.308  3.382   1.00 66.45  ? 263 GLN A CD    1 
ATOM   1972 O OE1   . GLN A 1 291 ? -13.277 54.561  4.587   1.00 62.98  ? 263 GLN A OE1   1 
ATOM   1973 N NE2   . GLN A 1 291 ? -13.646 55.168  2.455   1.00 75.71  ? 263 GLN A NE2   1 
ATOM   1974 N N     . ARG A 1 292 ? -10.518 50.605  3.673   1.00 51.93  ? 264 ARG A N     1 
ATOM   1975 C CA    . ARG A 1 292 ? -9.087  50.683  3.409   1.00 51.51  ? 264 ARG A CA    1 
ATOM   1976 C C     . ARG A 1 292 ? -8.523  49.403  2.809   1.00 51.67  ? 264 ARG A C     1 
ATOM   1977 O O     . ARG A 1 292 ? -7.340  49.380  2.452   1.00 53.31  ? 264 ARG A O     1 
ATOM   1978 C CB    . ARG A 1 292 ? -8.334  51.015  4.698   1.00 54.96  ? 264 ARG A CB    1 
ATOM   1979 C CG    . ARG A 1 292 ? -7.165  51.964  4.506   1.00 60.25  ? 264 ARG A CG    1 
ATOM   1980 C CD    . ARG A 1 292 ? -6.835  52.698  5.793   1.00 58.24  ? 264 ARG A CD    1 
ATOM   1981 N NE    . ARG A 1 292 ? -7.510  53.987  5.883   1.00 54.83  ? 264 ARG A NE    1 
ATOM   1982 C CZ    . ARG A 1 292 ? -8.617  54.202  6.579   1.00 62.77  ? 264 ARG A CZ    1 
ATOM   1983 N NH1   . ARG A 1 292 ? -9.210  53.229  7.250   1.00 58.21  ? 264 ARG A NH1   1 
ATOM   1984 N NH2   . ARG A 1 292 ? -9.142  55.424  6.602   1.00 75.80  ? 264 ARG A NH2   1 
ATOM   1985 N N     . LEU A 1 293 ? -9.325  48.346  2.691   1.00 50.42  ? 265 LEU A N     1 
ATOM   1986 C CA    . LEU A 1 293 ? -8.840  47.088  2.139   1.00 48.31  ? 265 LEU A CA    1 
ATOM   1987 C C     . LEU A 1 293 ? -8.929  47.060  0.618   1.00 55.00  ? 265 LEU A C     1 
ATOM   1988 O O     . LEU A 1 293 ? -7.947  46.735  -0.056  1.00 59.06  ? 265 LEU A O     1 
ATOM   1989 C CB    . LEU A 1 293 ? -9.614  45.914  2.739   1.00 48.16  ? 265 LEU A CB    1 
ATOM   1990 C CG    . LEU A 1 293 ? -9.219  45.635  4.186   1.00 46.46  ? 265 LEU A CG    1 
ATOM   1991 C CD1   . LEU A 1 293 ? -10.012 44.471  4.763   1.00 45.65  ? 265 LEU A CD1   1 
ATOM   1992 C CD2   . LEU A 1 293 ? -7.720  45.406  4.283   1.00 45.77  ? 265 LEU A CD2   1 
ATOM   1993 N N     . GLU A 1 294 ? -10.096 47.392  0.062   1.00 53.63  ? 266 GLU A N     1 
ATOM   1994 C CA    . GLU A 1 294 ? -10.208 47.481  -1.388  1.00 55.03  ? 266 GLU A CA    1 
ATOM   1995 C C     . GLU A 1 294 ? -9.418  48.656  -1.948  1.00 58.41  ? 266 GLU A C     1 
ATOM   1996 O O     . GLU A 1 294 ? -9.070  48.642  -3.134  1.00 63.46  ? 266 GLU A O     1 
ATOM   1997 C CB    . GLU A 1 294 ? -11.676 47.571  -1.803  1.00 60.41  ? 266 GLU A CB    1 
ATOM   1998 C CG    . GLU A 1 294 ? -12.407 46.240  -1.707  1.00 64.21  ? 266 GLU A CG    1 
ATOM   1999 C CD    . GLU A 1 294 ? -13.873 46.340  -2.079  1.00 77.42  ? 266 GLU A CD    1 
ATOM   2000 O OE1   . GLU A 1 294 ? -14.308 47.428  -2.513  1.00 81.11  ? 266 GLU A OE1   1 
ATOM   2001 O OE2   . GLU A 1 294 ? -14.592 45.327  -1.938  1.00 78.96  ? 266 GLU A OE2   1 
ATOM   2002 N N     . LYS A 1 295 ? -9.130  49.669  -1.126  1.00 58.06  ? 267 LYS A N     1 
ATOM   2003 C CA    . LYS A 1 295 ? -8.127  50.661  -1.499  1.00 58.59  ? 267 LYS A CA    1 
ATOM   2004 C C     . LYS A 1 295 ? -6.779  49.996  -1.739  1.00 56.13  ? 267 LYS A C     1 
ATOM   2005 O O     . LYS A 1 295 ? -6.158  50.179  -2.793  1.00 53.02  ? 267 LYS A O     1 
ATOM   2006 C CB    . LYS A 1 295 ? -8.006  51.727  -0.409  1.00 60.99  ? 267 LYS A CB    1 
ATOM   2007 C CG    . LYS A 1 295 ? -6.909  52.746  -0.680  1.00 69.02  ? 267 LYS A CG    1 
ATOM   2008 C CD    . LYS A 1 295 ? -6.732  53.713  0.478   1.00 70.60  ? 267 LYS A CD    1 
ATOM   2009 C CE    . LYS A 1 295 ? -5.543  54.631  0.241   1.00 76.12  ? 267 LYS A CE    1 
ATOM   2010 N NZ    . LYS A 1 295 ? -5.326  55.578  1.368   1.00 77.68  ? 267 LYS A NZ    1 
ATOM   2011 N N     . LEU A 1 296 ? -6.311  49.216  -0.766  1.00 55.41  ? 268 LEU A N     1 
ATOM   2012 C CA    . LEU A 1 296 ? -5.060  48.481  -0.883  1.00 54.16  ? 268 LEU A CA    1 
ATOM   2013 C C     . LEU A 1 296 ? -5.204  47.199  -1.693  1.00 54.87  ? 268 LEU A C     1 
ATOM   2014 O O     . LEU A 1 296 ? -4.202  46.508  -1.909  1.00 52.06  ? 268 LEU A O     1 
ATOM   2015 C CB    . LEU A 1 296 ? -4.515  48.162  0.511   1.00 52.77  ? 268 LEU A CB    1 
ATOM   2016 C CG    . LEU A 1 296 ? -4.154  49.385  1.359   1.00 53.10  ? 268 LEU A CG    1 
ATOM   2017 C CD1   . LEU A 1 296 ? -3.979  49.000  2.819   1.00 61.60  ? 268 LEU A CD1   1 
ATOM   2018 C CD2   . LEU A 1 296 ? -2.902  50.066  0.825   1.00 55.19  ? 268 LEU A CD2   1 
ATOM   2019 N N     . LYS A 1 297 ? -6.422  46.868  -2.128  1.00 55.80  ? 269 LYS A N     1 
ATOM   2020 C CA    . LYS A 1 297 ? -6.675  45.741  -3.029  1.00 54.33  ? 269 LYS A CA    1 
ATOM   2021 C C     . LYS A 1 297 ? -6.208  44.417  -2.428  1.00 49.86  ? 269 LYS A C     1 
ATOM   2022 O O     . LYS A 1 297 ? -5.590  43.591  -3.102  1.00 46.44  ? 269 LYS A O     1 
ATOM   2023 C CB    . LYS A 1 297 ? -6.034  45.981  -4.398  1.00 57.00  ? 269 LYS A CB    1 
ATOM   2024 C CG    . LYS A 1 297 ? -6.570  47.218  -5.105  1.00 61.37  ? 269 LYS A CG    1 
ATOM   2025 C CD    . LYS A 1 297 ? -5.956  47.399  -6.483  1.00 63.39  ? 269 LYS A CD    1 
ATOM   2026 C CE    . LYS A 1 297 ? -6.464  48.675  -7.138  1.00 68.18  ? 269 LYS A CE    1 
ATOM   2027 N NZ    . LYS A 1 297 ? -5.868  48.891  -8.485  1.00 74.35  ? 269 LYS A NZ    1 
ATOM   2028 N N     . GLY A 1 298 ? -6.508  44.213  -1.148  1.00 48.65  ? 270 GLY A N     1 
ATOM   2029 C CA    . GLY A 1 298 ? -6.250  42.941  -0.504  1.00 47.89  ? 270 GLY A CA    1 
ATOM   2030 C C     . GLY A 1 298 ? -7.424  42.000  -0.660  1.00 49.93  ? 270 GLY A C     1 
ATOM   2031 O O     . GLY A 1 298 ? -7.258  40.777  -0.714  1.00 50.49  ? 270 GLY A O     1 
ATOM   2032 N N     . THR A 1 299 ? -8.622  42.571  -0.725  1.00 48.51  ? 271 THR A N     1 
ATOM   2033 C CA    . THR A 1 299 ? -9.839  41.843  -1.039  1.00 51.57  ? 271 THR A CA    1 
ATOM   2034 C C     . THR A 1 299 ? -10.282 42.191  -2.454  1.00 57.60  ? 271 THR A C     1 
ATOM   2035 O O     . THR A 1 299 ? -9.931  43.242  -2.997  1.00 56.97  ? 271 THR A O     1 
ATOM   2036 C CB    . THR A 1 299 ? -10.957 42.172  -0.044  1.00 45.54  ? 271 THR A CB    1 
ATOM   2037 O OG1   . THR A 1 299 ? -11.352 43.540  -0.202  1.00 50.58  ? 271 THR A OG1   1 
ATOM   2038 C CG2   . THR A 1 299 ? -10.480 41.953  1.383   1.00 43.81  ? 271 THR A CG2   1 
ATOM   2039 N N     . SER A 1 300 ? -11.057 41.292  -3.053  1.00 56.15  ? 272 SER A N     1 
ATOM   2040 C CA    . SER A 1 300 ? -11.534 41.501  -4.412  1.00 59.71  ? 272 SER A CA    1 
ATOM   2041 C C     . SER A 1 300 ? -12.809 40.698  -4.619  1.00 60.15  ? 272 SER A C     1 
ATOM   2042 O O     . SER A 1 300 ? -13.163 39.832  -3.816  1.00 60.51  ? 272 SER A O     1 
ATOM   2043 C CB    . SER A 1 300 ? -10.471 41.114  -5.445  1.00 61.11  ? 272 SER A CB    1 
ATOM   2044 O OG    . SER A 1 300 ? -11.067 40.655  -6.646  1.00 64.70  ? 272 SER A OG    1 
ATOM   2045 N N     . GLN A 1 301 ? -13.494 41.002  -5.718  1.00 64.24  ? 273 GLN A N     1 
ATOM   2046 C CA    . GLN A 1 301 ? -14.727 40.331  -6.098  1.00 61.70  ? 273 GLN A CA    1 
ATOM   2047 C C     . GLN A 1 301 ? -14.660 39.961  -7.572  1.00 63.97  ? 273 GLN A C     1 
ATOM   2048 O O     . GLN A 1 301 ? -14.239 40.770  -8.405  1.00 66.14  ? 273 GLN A O     1 
ATOM   2049 C CB    . GLN A 1 301 ? -15.948 41.218  -5.830  1.00 59.75  ? 273 GLN A CB    1 
ATOM   2050 C CG    . GLN A 1 301 ? -17.279 40.534  -6.078  1.00 61.41  ? 273 GLN A CG    1 
ATOM   2051 C CD    . GLN A 1 301 ? -18.334 41.492  -6.594  1.00 69.58  ? 273 GLN A CD    1 
ATOM   2052 O OE1   . GLN A 1 301 ? -18.822 42.350  -5.859  1.00 71.16  ? 273 GLN A OE1   1 
ATOM   2053 N NE2   . GLN A 1 301 ? -18.688 41.351  -7.866  1.00 72.43  ? 273 GLN A NE2   1 
ATOM   2054 N N     . GLY A 1 302 ? -15.072 38.736  -7.889  1.00 67.15  ? 274 GLY A N     1 
ATOM   2055 C CA    . GLY A 1 302 ? -15.002 38.256  -9.255  1.00 69.90  ? 274 GLY A CA    1 
ATOM   2056 C C     . GLY A 1 302 ? -16.308 37.700  -9.783  1.00 69.26  ? 274 GLY A C     1 
ATOM   2057 O O     . GLY A 1 302 ? -17.380 37.972  -9.232  1.00 68.66  ? 274 GLY A O     1 
ATOM   2058 N N     . VAL A 1 303 ? -16.228 36.921  -10.860 1.00 70.88  ? 275 VAL A N     1 
ATOM   2059 C CA    . VAL A 1 303 ? -17.392 36.305  -11.482 1.00 69.19  ? 275 VAL A CA    1 
ATOM   2060 C C     . VAL A 1 303 ? -17.122 34.817  -11.649 1.00 73.01  ? 275 VAL A C     1 
ATOM   2061 O O     . VAL A 1 303 ? -15.972 34.384  -11.766 1.00 78.62  ? 275 VAL A O     1 
ATOM   2062 C CB    . VAL A 1 303 ? -17.731 36.952  -12.842 1.00 64.46  ? 275 VAL A CB    1 
ATOM   2063 C CG1   . VAL A 1 303 ? -18.371 38.317  -12.635 1.00 59.40  ? 275 VAL A CG1   1 
ATOM   2064 C CG2   . VAL A 1 303 ? -16.481 37.066  -13.702 1.00 63.79  ? 275 VAL A CG2   1 
ATOM   2065 N N     . GLY A 1 304 ? -18.196 34.032  -11.660 1.00 75.04  ? 276 GLY A N     1 
ATOM   2066 C CA    . GLY A 1 304 ? -18.068 32.592  -11.764 1.00 80.57  ? 276 GLY A CA    1 
ATOM   2067 C C     . GLY A 1 304 ? -18.500 32.032  -13.103 1.00 84.96  ? 276 GLY A C     1 
ATOM   2068 O O     . GLY A 1 304 ? -19.169 32.717  -13.884 1.00 80.40  ? 276 GLY A O     1 
ATOM   2069 N N     . ARG A 1 305 ? -18.116 30.782  -13.380 1.00 90.24  ? 277 ARG A N     1 
ATOM   2070 C CA    . ARG A 1 305 ? -18.543 30.132  -14.615 1.00 87.51  ? 277 ARG A CA    1 
ATOM   2071 C C     . ARG A 1 305 ? -20.057 29.984  -14.668 1.00 82.51  ? 277 ARG A C     1 
ATOM   2072 O O     . ARG A 1 305 ? -20.654 30.078  -15.748 1.00 77.38  ? 277 ARG A O     1 
ATOM   2073 C CB    . ARG A 1 305 ? -17.868 28.767  -14.752 1.00 81.54  ? 277 ARG A CB    1 
ATOM   2074 N N     . ASN A 1 306 ? -20.694 29.753  -13.522 1.00 86.38  ? 278 ASN A N     1 
ATOM   2075 C CA    . ASN A 1 306 ? -22.147 29.733  -13.436 1.00 80.29  ? 278 ASN A CA    1 
ATOM   2076 C C     . ASN A 1 306 ? -22.749 31.130  -13.369 1.00 78.74  ? 278 ASN A C     1 
ATOM   2077 O O     . ASN A 1 306 ? -23.978 31.257  -13.343 1.00 75.54  ? 278 ASN A O     1 
ATOM   2078 C CB    . ASN A 1 306 ? -22.591 28.920  -12.216 1.00 74.35  ? 278 ASN A CB    1 
ATOM   2079 N N     . GLY A 1 307 ? -21.920 32.174  -13.339 1.00 79.16  ? 279 GLY A N     1 
ATOM   2080 C CA    . GLY A 1 307 ? -22.392 33.539  -13.288 1.00 76.08  ? 279 GLY A CA    1 
ATOM   2081 C C     . GLY A 1 307 ? -22.497 34.135  -11.901 1.00 76.47  ? 279 GLY A C     1 
ATOM   2082 O O     . GLY A 1 307 ? -22.749 35.341  -11.782 1.00 71.11  ? 279 GLY A O     1 
ATOM   2083 N N     . GLU A 1 308 ? -22.306 33.339  -10.853 1.00 76.05  ? 280 GLU A N     1 
ATOM   2084 C CA    . GLU A 1 308 ? -22.452 33.828  -9.492  1.00 71.71  ? 280 GLU A CA    1 
ATOM   2085 C C     . GLU A 1 308 ? -21.248 34.677  -9.087  1.00 74.43  ? 280 GLU A C     1 
ATOM   2086 O O     . GLU A 1 308 ? -20.176 34.619  -9.695  1.00 74.62  ? 280 GLU A O     1 
ATOM   2087 C CB    . GLU A 1 308 ? -22.624 32.663  -8.518  1.00 80.23  ? 280 GLU A CB    1 
ATOM   2088 N N     . ALA A 1 309 ? -21.442 35.470  -8.036  1.00 72.85  ? 281 ALA A N     1 
ATOM   2089 C CA    . ALA A 1 309 ? -20.404 36.374  -7.561  1.00 65.17  ? 281 ALA A CA    1 
ATOM   2090 C C     . ALA A 1 309 ? -19.410 35.639  -6.672  1.00 65.38  ? 281 ALA A C     1 
ATOM   2091 O O     . ALA A 1 309 ? -19.793 34.850  -5.802  1.00 58.13  ? 281 ALA A O     1 
ATOM   2092 C CB    . ALA A 1 309 ? -21.024 37.544  -6.797  1.00 53.67  ? 281 ALA A CB    1 
ATOM   2093 N N     . GLU A 1 310 ? -18.126 35.907  -6.894  1.00 67.95  ? 282 GLU A N     1 
ATOM   2094 C CA    . GLU A 1 310 ? -17.040 35.293  -6.145  1.00 62.51  ? 282 GLU A CA    1 
ATOM   2095 C C     . GLU A 1 310 ? -16.305 36.364  -5.352  1.00 58.84  ? 282 GLU A C     1 
ATOM   2096 O O     . GLU A 1 310 ? -16.088 37.474  -5.846  1.00 60.58  ? 282 GLU A O     1 
ATOM   2097 C CB    . GLU A 1 310 ? -16.068 34.572  -7.083  1.00 64.17  ? 282 GLU A CB    1 
ATOM   2098 C CG    . GLU A 1 310 ? -16.651 33.341  -7.758  1.00 68.47  ? 282 GLU A CG    1 
ATOM   2099 C CD    . GLU A 1 310 ? -15.687 32.703  -8.740  1.00 70.45  ? 282 GLU A CD    1 
ATOM   2100 O OE1   . GLU A 1 310 ? -14.755 33.399  -9.194  1.00 72.81  ? 282 GLU A OE1   1 
ATOM   2101 O OE2   . GLU A 1 310 ? -15.863 31.507  -9.057  1.00 68.15  ? 282 GLU A OE2   1 
ATOM   2102 N N     . TYR A 1 311 ? -15.922 36.029  -4.123  1.00 54.87  ? 283 TYR A N     1 
ATOM   2103 C CA    . TYR A 1 311 ? -15.252 36.959  -3.225  1.00 50.76  ? 283 TYR A CA    1 
ATOM   2104 C C     . TYR A 1 311 ? -13.933 36.355  -2.763  1.00 46.27  ? 283 TYR A C     1 
ATOM   2105 O O     . TYR A 1 311 ? -13.850 35.151  -2.504  1.00 48.12  ? 283 TYR A O     1 
ATOM   2106 C CB    . TYR A 1 311 ? -16.141 37.298  -2.022  1.00 49.72  ? 283 TYR A CB    1 
ATOM   2107 C CG    . TYR A 1 311 ? -17.435 37.983  -2.409  1.00 51.61  ? 283 TYR A CG    1 
ATOM   2108 C CD1   . TYR A 1 311 ? -18.520 37.250  -2.874  1.00 57.23  ? 283 TYR A CD1   1 
ATOM   2109 C CD2   . TYR A 1 311 ? -17.567 39.362  -2.321  1.00 52.69  ? 283 TYR A CD2   1 
ATOM   2110 C CE1   . TYR A 1 311 ? -19.701 37.870  -3.235  1.00 60.37  ? 283 TYR A CE1   1 
ATOM   2111 C CE2   . TYR A 1 311 ? -18.746 39.992  -2.679  1.00 58.32  ? 283 TYR A CE2   1 
ATOM   2112 C CZ    . TYR A 1 311 ? -19.809 39.241  -3.136  1.00 59.28  ? 283 TYR A CZ    1 
ATOM   2113 O OH    . TYR A 1 311 ? -20.984 39.861  -3.494  1.00 53.59  ? 283 TYR A OH    1 
ATOM   2114 N N     . TYR A 1 312 ? -12.904 37.194  -2.659  1.00 43.16  ? 284 TYR A N     1 
ATOM   2115 C CA    . TYR A 1 312 ? -11.549 36.707  -2.447  1.00 44.03  ? 284 TYR A CA    1 
ATOM   2116 C C     . TYR A 1 312 ? -10.839 37.532  -1.384  1.00 47.08  ? 284 TYR A C     1 
ATOM   2117 O O     . TYR A 1 312 ? -11.245 38.647  -1.050  1.00 45.90  ? 284 TYR A O     1 
ATOM   2118 C CB    . TYR A 1 312 ? -10.737 36.741  -3.748  1.00 47.97  ? 284 TYR A CB    1 
ATOM   2119 C CG    . TYR A 1 312 ? -11.203 35.749  -4.785  1.00 49.06  ? 284 TYR A CG    1 
ATOM   2120 C CD1   . TYR A 1 312 ? -12.180 36.089  -5.710  1.00 53.59  ? 284 TYR A CD1   1 
ATOM   2121 C CD2   . TYR A 1 312 ? -10.666 34.471  -4.839  1.00 52.04  ? 284 TYR A CD2   1 
ATOM   2122 C CE1   . TYR A 1 312 ? -12.609 35.184  -6.660  1.00 58.04  ? 284 TYR A CE1   1 
ATOM   2123 C CE2   . TYR A 1 312 ? -11.087 33.559  -5.785  1.00 55.12  ? 284 TYR A CE2   1 
ATOM   2124 C CZ    . TYR A 1 312 ? -12.059 33.920  -6.693  1.00 59.04  ? 284 TYR A CZ    1 
ATOM   2125 O OH    . TYR A 1 312 ? -12.482 33.013  -7.638  1.00 64.87  ? 284 TYR A OH    1 
ATOM   2126 N N     . ILE A 1 313 ? -9.760  36.952  -0.857  1.00 47.03  ? 285 ILE A N     1 
ATOM   2127 C CA    . ILE A 1 313 ? -8.821  37.635  0.029   1.00 40.53  ? 285 ILE A CA    1 
ATOM   2128 C C     . ILE A 1 313 ? -7.417  37.275  -0.435  1.00 41.44  ? 285 ILE A C     1 
ATOM   2129 O O     . ILE A 1 313 ? -7.079  36.090  -0.526  1.00 41.36  ? 285 ILE A O     1 
ATOM   2130 C CB    . ILE A 1 313 ? -9.012  37.246  1.505   1.00 39.65  ? 285 ILE A CB    1 
ATOM   2131 C CG1   . ILE A 1 313 ? -10.372 37.725  2.013   1.00 40.44  ? 285 ILE A CG1   1 
ATOM   2132 C CG2   . ILE A 1 313 ? -7.882  37.811  2.354   1.00 39.60  ? 285 ILE A CG2   1 
ATOM   2133 C CD1   . ILE A 1 313 ? -10.690 37.270  3.418   1.00 40.11  ? 285 ILE A CD1   1 
ATOM   2134 N N     . HIS A 1 314 ? -6.602  38.283  -0.728  1.00 43.59  ? 286 HIS A N     1 
ATOM   2135 C CA    . HIS A 1 314 ? -5.281  38.071  -1.301  1.00 46.97  ? 286 HIS A CA    1 
ATOM   2136 C C     . HIS A 1 314 ? -4.194  38.316  -0.264  1.00 45.78  ? 286 HIS A C     1 
ATOM   2137 O O     . HIS A 1 314 ? -4.306  39.226  0.565   1.00 45.58  ? 286 HIS A O     1 
ATOM   2138 C CB    . HIS A 1 314 ? -5.066  38.977  -2.516  1.00 50.77  ? 286 HIS A CB    1 
ATOM   2139 C CG    . HIS A 1 314 ? -6.194  38.930  -3.497  1.00 51.13  ? 286 HIS A CG    1 
ATOM   2140 N ND1   . HIS A 1 314 ? -6.301  37.945  -4.455  1.00 51.44  ? 286 HIS A ND1   1 
ATOM   2141 C CD2   . HIS A 1 314 ? -7.268  39.737  -3.663  1.00 51.97  ? 286 HIS A CD2   1 
ATOM   2142 C CE1   . HIS A 1 314 ? -7.393  38.149  -5.170  1.00 53.34  ? 286 HIS A CE1   1 
ATOM   2143 N NE2   . HIS A 1 314 ? -7.997  39.230  -4.710  1.00 54.39  ? 286 HIS A NE2   1 
ATOM   2144 N N     . LEU A 1 315 ? -3.136  37.505  -0.331  1.00 39.65  ? 287 LEU A N     1 
ATOM   2145 C CA    . LEU A 1 315 ? -2.046  37.549  0.638   1.00 40.21  ? 287 LEU A CA    1 
ATOM   2146 C C     . LEU A 1 315 ? -0.891  36.645  0.211   1.00 39.72  ? 287 LEU A C     1 
ATOM   2147 O O     . LEU A 1 315 ? -1.098  35.679  -0.527  1.00 38.84  ? 287 LEU A O     1 
ATOM   2148 C CB    . LEU A 1 315 ? -2.578  37.165  2.021   1.00 38.21  ? 287 LEU A CB    1 
ATOM   2149 C CG    . LEU A 1 315 ? -3.234  35.788  2.136   1.00 37.06  ? 287 LEU A CG    1 
ATOM   2150 C CD1   . LEU A 1 315 ? -2.253  34.767  2.648   1.00 36.18  ? 287 LEU A CD1   1 
ATOM   2151 C CD2   . LEU A 1 315 ? -4.466  35.844  3.024   1.00 37.26  ? 287 LEU A CD2   1 
ATOM   2152 N N     . SER A 1 316 ? 0.326   36.951  0.654   1.00 42.01  ? 288 SER A N     1 
ATOM   2153 C CA    . SER A 1 316 ? 1.501   36.164  0.299   1.00 44.68  ? 288 SER A CA    1 
ATOM   2154 C C     . SER A 1 316 ? 1.847   35.201  1.429   1.00 43.65  ? 288 SER A C     1 
ATOM   2155 O O     . SER A 1 316 ? 1.742   35.550  2.608   1.00 43.18  ? 288 SER A O     1 
ATOM   2156 C CB    . SER A 1 316 ? 2.694   37.070  -0.014  1.00 45.42  ? 288 SER A CB    1 
ATOM   2157 O OG    . SER A 1 316 ? 2.398   37.940  -1.093  1.00 47.92  ? 288 SER A OG    1 
ATOM   2158 N N     . VAL A 1 317 ? 2.248   33.983  1.065   1.00 42.05  ? 289 VAL A N     1 
ATOM   2159 C CA    . VAL A 1 317 ? 2.524   32.925  2.031   1.00 34.71  ? 289 VAL A CA    1 
ATOM   2160 C C     . VAL A 1 317 ? 3.935   32.401  1.813   1.00 35.94  ? 289 VAL A C     1 
ATOM   2161 O O     . VAL A 1 317 ? 4.307   32.058  0.685   1.00 45.49  ? 289 VAL A O     1 
ATOM   2162 C CB    . VAL A 1 317 ? 1.512   31.767  1.928   1.00 35.44  ? 289 VAL A CB    1 
ATOM   2163 C CG1   . VAL A 1 317 ? 1.909   30.631  2.863   1.00 44.54  ? 289 VAL A CG1   1 
ATOM   2164 C CG2   . VAL A 1 317 ? 0.120   32.246  2.255   1.00 34.39  ? 289 VAL A CG2   1 
ATOM   2165 N N     . ILE A 1 318 ? 4.714   32.338  2.888   1.00 35.35  ? 290 ILE A N     1 
ATOM   2166 C CA    . ILE A 1 318 ? 5.981   31.618  2.890   1.00 37.94  ? 290 ILE A CA    1 
ATOM   2167 C C     . ILE A 1 318 ? 5.720   30.200  3.374   1.00 39.94  ? 290 ILE A C     1 
ATOM   2168 O O     . ILE A 1 318 ? 5.153   29.997  4.455   1.00 44.45  ? 290 ILE A O     1 
ATOM   2169 C CB    . ILE A 1 318 ? 7.020   32.315  3.784   1.00 38.13  ? 290 ILE A CB    1 
ATOM   2170 C CG1   . ILE A 1 318 ? 7.155   33.793  3.422   1.00 37.26  ? 290 ILE A CG1   1 
ATOM   2171 C CG2   . ILE A 1 318 ? 8.367   31.619  3.670   1.00 43.35  ? 290 ILE A CG2   1 
ATOM   2172 C CD1   . ILE A 1 318 ? 7.856   34.605  4.492   1.00 39.97  ? 290 ILE A CD1   1 
ATOM   2173 N N     . THR A 1 319 ? 6.123   29.217  2.577   1.00 36.57  ? 291 THR A N     1 
ATOM   2174 C CA    . THR A 1 319 ? 6.025   27.813  2.948   1.00 40.73  ? 291 THR A CA    1 
ATOM   2175 C C     . THR A 1 319 ? 7.423   27.288  3.238   1.00 46.31  ? 291 THR A C     1 
ATOM   2176 O O     . THR A 1 319 ? 8.346   27.507  2.447   1.00 53.02  ? 291 THR A O     1 
ATOM   2177 C CB    . THR A 1 319 ? 5.363   26.992  1.840   1.00 40.97  ? 291 THR A CB    1 
ATOM   2178 O OG1   . THR A 1 319 ? 4.128   27.610  1.461   1.00 48.66  ? 291 THR A OG1   1 
ATOM   2179 C CG2   . THR A 1 319 ? 5.080   25.582  2.327   1.00 40.07  ? 291 THR A CG2   1 
ATOM   2180 N N     . ALA A 1 320 ? 7.579   26.602  4.369   1.00 44.88  ? 292 ALA A N     1 
ATOM   2181 C CA    . ALA A 1 320 ? 8.894   26.173  4.818   1.00 41.25  ? 292 ALA A CA    1 
ATOM   2182 C C     . ALA A 1 320 ? 8.841   24.734  5.310   1.00 41.71  ? 292 ALA A C     1 
ATOM   2183 O O     . ALA A 1 320 ? 7.791   24.227  5.713   1.00 43.48  ? 292 ALA A O     1 
ATOM   2184 C CB    . ALA A 1 320 ? 9.434   27.086  5.927   1.00 39.69  ? 292 ALA A CB    1 
ATOM   2185 N N     . LEU A 1 321 ? 10.003  24.085  5.267   1.00 41.46  ? 293 LEU A N     1 
ATOM   2186 C CA    . LEU A 1 321 ? 10.183  22.726  5.772   1.00 38.69  ? 293 LEU A CA    1 
ATOM   2187 C C     . LEU A 1 321 ? 11.567  22.655  6.402   1.00 39.66  ? 293 LEU A C     1 
ATOM   2188 O O     . LEU A 1 321 ? 12.575  22.749  5.696   1.00 46.44  ? 293 LEU A O     1 
ATOM   2189 C CB    . LEU A 1 321 ? 10.034  21.690  4.657   1.00 40.33  ? 293 LEU A CB    1 
ATOM   2190 C CG    . LEU A 1 321 ? 10.460  20.261  4.999   1.00 38.04  ? 293 LEU A CG    1 
ATOM   2191 C CD1   . LEU A 1 321 ? 9.617   19.703  6.134   1.00 42.73  ? 293 LEU A CD1   1 
ATOM   2192 C CD2   . LEU A 1 321 ? 10.381  19.365  3.773   1.00 44.26  ? 293 LEU A CD2   1 
ATOM   2193 N N     . ALA A 1 322 ? 11.617  22.495  7.718   1.00 30.56  ? 294 ALA A N     1 
ATOM   2194 C CA    . ALA A 1 322 ? 12.865  22.507  8.469   1.00 33.84  ? 294 ALA A CA    1 
ATOM   2195 C C     . ALA A 1 322 ? 13.078  21.158  9.150   1.00 60.39  ? 294 ALA A C     1 
ATOM   2196 O O     . ALA A 1 322 ? 12.255  20.246  9.046   1.00 55.36  ? 294 ALA A O     1 
ATOM   2197 C CB    . ALA A 1 322 ? 12.870  23.644  9.494   1.00 40.51  ? 294 ALA A CB    1 
ATOM   2198 N N     . ARG A 1 323 ? 14.205  21.041  9.850   1.00 52.08  ? 295 ARG A N     1 
ATOM   2199 C CA    . ARG A 1 323 ? 14.534  19.825  10.584  1.00 51.83  ? 295 ARG A CA    1 
ATOM   2200 C C     . ARG A 1 323 ? 15.526  20.166  11.686  1.00 52.51  ? 295 ARG A C     1 
ATOM   2201 O O     . ARG A 1 323 ? 16.524  20.849  11.435  1.00 52.01  ? 295 ARG A O     1 
ATOM   2202 C CB    . ARG A 1 323 ? 15.112  18.751  9.655   1.00 52.58  ? 295 ARG A CB    1 
ATOM   2203 C CG    . ARG A 1 323 ? 15.447  17.444  10.361  1.00 56.59  ? 295 ARG A CG    1 
ATOM   2204 C CD    . ARG A 1 323 ? 16.100  16.444  9.420   1.00 57.13  ? 295 ARG A CD    1 
ATOM   2205 N NE    . ARG A 1 323 ? 15.193  16.009  8.365   1.00 64.40  ? 295 ARG A NE    1 
ATOM   2206 C CZ    . ARG A 1 323 ? 15.583  15.486  7.211   1.00 70.69  ? 295 ARG A CZ    1 
ATOM   2207 N NH1   . ARG A 1 323 ? 16.864  15.329  6.920   1.00 69.39  ? 295 ARG A NH1   1 
ATOM   2208 N NH2   . ARG A 1 323 ? 14.663  15.109  6.326   1.00 66.45  ? 295 ARG A NH2   1 
ATOM   2209 N N     . LYS A 1 324 ? 15.250  19.689  12.897  1.00 52.66  ? 296 LYS A N     1 
ATOM   2210 C CA    . LYS A 1 324 ? 16.123  19.931  14.036  1.00 48.80  ? 296 LYS A CA    1 
ATOM   2211 C C     . LYS A 1 324 ? 17.349  19.026  13.974  1.00 49.28  ? 296 LYS A C     1 
ATOM   2212 O O     . LYS A 1 324 ? 17.280  17.880  13.522  1.00 45.30  ? 296 LYS A O     1 
ATOM   2213 C CB    . LYS A 1 324 ? 15.365  19.702  15.346  1.00 46.29  ? 296 LYS A CB    1 
ATOM   2214 C CG    . LYS A 1 324 ? 16.203  19.881  16.605  1.00 47.62  ? 296 LYS A CG    1 
ATOM   2215 C CD    . LYS A 1 324 ? 15.392  19.618  17.863  1.00 43.88  ? 296 LYS A CD    1 
ATOM   2216 C CE    . LYS A 1 324 ? 16.256  19.744  19.109  1.00 44.86  ? 296 LYS A CE    1 
ATOM   2217 N NZ    . LYS A 1 324 ? 15.462  19.604  20.361  1.00 43.62  ? 296 LYS A NZ    1 
ATOM   2218 N N     . PHE A 1 325 ? 18.479  19.557  14.431  1.00 55.21  ? 297 PHE A N     1 
ATOM   2219 C CA    . PHE A 1 325 ? 19.721  18.792  14.476  1.00 55.62  ? 297 PHE A CA    1 
ATOM   2220 C C     . PHE A 1 325 ? 19.826  17.983  15.767  1.00 54.85  ? 297 PHE A C     1 
ATOM   2221 O O     . PHE A 1 325 ? 19.657  18.517  16.864  1.00 54.91  ? 297 PHE A O     1 
ATOM   2222 C CB    . PHE A 1 325 ? 20.927  19.722  14.339  1.00 51.55  ? 297 PHE A CB    1 
ATOM   2223 C CG    . PHE A 1 325 ? 21.331  19.980  12.918  1.00 50.83  ? 297 PHE A CG    1 
ATOM   2224 C CD1   . PHE A 1 325 ? 22.089  19.054  12.221  1.00 52.57  ? 297 PHE A CD1   1 
ATOM   2225 C CD2   . PHE A 1 325 ? 20.951  21.147  12.276  1.00 52.92  ? 297 PHE A CD2   1 
ATOM   2226 C CE1   . PHE A 1 325 ? 22.462  19.287  10.911  1.00 56.41  ? 297 PHE A CE1   1 
ATOM   2227 C CE2   . PHE A 1 325 ? 21.321  21.386  10.965  1.00 57.80  ? 297 PHE A CE2   1 
ATOM   2228 C CZ    . PHE A 1 325 ? 22.077  20.454  10.282  1.00 59.97  ? 297 PHE A CZ    1 
ATOM   2229 N N     . GLU B 1 42  ? 36.282  -12.435 -1.648  1.00 65.66  ? 14  GLU B N     1 
ATOM   2230 C CA    . GLU B 1 42  ? 37.020  -11.222 -1.974  1.00 72.60  ? 14  GLU B CA    1 
ATOM   2231 C C     . GLU B 1 42  ? 37.781  -11.378 -3.288  1.00 78.68  ? 14  GLU B C     1 
ATOM   2232 O O     . GLU B 1 42  ? 37.897  -12.485 -3.815  1.00 80.28  ? 14  GLU B O     1 
ATOM   2233 C CB    . GLU B 1 42  ? 37.988  -10.869 -0.844  1.00 79.65  ? 14  GLU B CB    1 
ATOM   2234 C CG    . GLU B 1 42  ? 38.405  -9.409  -0.818  1.00 79.26  ? 14  GLU B CG    1 
ATOM   2235 C CD    . GLU B 1 42  ? 39.769  -9.204  -0.198  1.00 80.53  ? 14  GLU B CD    1 
ATOM   2236 O OE1   . GLU B 1 42  ? 39.999  -9.705  0.923   1.00 82.49  ? 14  GLU B OE1   1 
ATOM   2237 O OE2   . GLU B 1 42  ? 40.616  -8.550  -0.843  1.00 75.25  ? 14  GLU B OE2   1 
ATOM   2238 N N     . ALA B 1 43  ? 38.290  -10.256 -3.804  1.00 84.23  ? 15  ALA B N     1 
ATOM   2239 C CA    . ALA B 1 43  ? 39.087  -10.223 -5.027  1.00 84.83  ? 15  ALA B CA    1 
ATOM   2240 C C     . ALA B 1 43  ? 38.322  -10.832 -6.193  1.00 83.59  ? 15  ALA B C     1 
ATOM   2241 O O     . ALA B 1 43  ? 37.354  -10.241 -6.683  1.00 86.63  ? 15  ALA B O     1 
ATOM   2242 C CB    . ALA B 1 43  ? 40.421  -10.946 -4.823  1.00 81.95  ? 15  ALA B CB    1 
ATOM   2243 N N     . TYR B 1 44  ? 38.749  -12.009 -6.643  1.00 80.74  ? 16  TYR B N     1 
ATOM   2244 C CA    . TYR B 1 44  ? 38.051  -12.713 -7.714  1.00 80.38  ? 16  TYR B CA    1 
ATOM   2245 C C     . TYR B 1 44  ? 36.717  -13.215 -7.170  1.00 74.00  ? 16  TYR B C     1 
ATOM   2246 O O     . TYR B 1 44  ? 36.680  -14.182 -6.396  1.00 77.25  ? 16  TYR B O     1 
ATOM   2247 C CB    . TYR B 1 44  ? 38.894  -13.869 -8.249  1.00 79.34  ? 16  TYR B CB    1 
ATOM   2248 C CG    . TYR B 1 44  ? 40.217  -13.479 -8.891  1.00 77.81  ? 16  TYR B CG    1 
ATOM   2249 C CD1   . TYR B 1 44  ? 40.649  -12.158 -8.921  1.00 74.48  ? 16  TYR B CD1   1 
ATOM   2250 C CD2   . TYR B 1 44  ? 41.037  -14.444 -9.466  1.00 80.71  ? 16  TYR B CD2   1 
ATOM   2251 C CE1   . TYR B 1 44  ? 41.857  -11.811 -9.500  1.00 82.04  ? 16  TYR B CE1   1 
ATOM   2252 C CE2   . TYR B 1 44  ? 42.247  -14.108 -10.045 1.00 85.02  ? 16  TYR B CE2   1 
ATOM   2253 C CZ    . TYR B 1 44  ? 42.651  -12.789 -10.061 1.00 90.63  ? 16  TYR B CZ    1 
ATOM   2254 O OH    . TYR B 1 44  ? 43.852  -12.443 -10.638 1.00 94.99  ? 16  TYR B OH    1 
ATOM   2255 N N     . ARG B 1 45  ? 35.634  -12.550 -7.563  1.00 63.28  ? 17  ARG B N     1 
ATOM   2256 C CA    . ARG B 1 45  ? 34.305  -12.774 -6.986  1.00 58.98  ? 17  ARG B CA    1 
ATOM   2257 C C     . ARG B 1 45  ? 34.389  -12.489 -5.475  1.00 64.05  ? 17  ARG B C     1 
ATOM   2258 O O     . ARG B 1 45  ? 35.251  -11.725 -5.026  1.00 70.69  ? 17  ARG B O     1 
ATOM   2259 C CB    . ARG B 1 45  ? 33.800  -14.155 -7.367  1.00 58.28  ? 17  ARG B CB    1 
ATOM   2260 C CG    . ARG B 1 45  ? 33.506  -14.315 -8.870  1.00 59.05  ? 17  ARG B CG    1 
ATOM   2261 C CD    . ARG B 1 45  ? 32.968  -13.012 -9.476  1.00 58.93  ? 17  ARG B CD    1 
ATOM   2262 N NE    . ARG B 1 45  ? 32.289  -13.243 -10.746 1.00 56.49  ? 17  ARG B NE    1 
ATOM   2263 C CZ    . ARG B 1 45  ? 31.238  -12.545 -11.165 1.00 54.34  ? 17  ARG B CZ    1 
ATOM   2264 N NH1   . ARG B 1 45  ? 30.737  -11.547 -10.450 1.00 49.59  ? 17  ARG B NH1   1 
ATOM   2265 N NH2   . ARG B 1 45  ? 30.650  -12.878 -12.311 1.00 52.28  ? 17  ARG B NH2   1 
ATOM   2266 N N     . GLY B 1 46  ? 33.485  -13.058 -4.676  1.00 56.02  ? 18  GLY B N     1 
ATOM   2267 C CA    . GLY B 1 46  ? 33.494  -12.808 -3.249  1.00 52.91  ? 18  GLY B CA    1 
ATOM   2268 C C     . GLY B 1 46  ? 33.752  -14.062 -2.441  1.00 54.15  ? 18  GLY B C     1 
ATOM   2269 O O     . GLY B 1 46  ? 34.837  -14.645 -2.528  1.00 63.27  ? 18  GLY B O     1 
ATOM   2270 N N     . ILE B 1 47  ? 32.763  -14.505 -1.671  1.00 52.29  ? 19  ILE B N     1 
ATOM   2271 C CA    . ILE B 1 47  ? 32.885  -15.696 -0.838  1.00 56.07  ? 19  ILE B CA    1 
ATOM   2272 C C     . ILE B 1 47  ? 32.177  -16.832 -1.567  1.00 56.41  ? 19  ILE B C     1 
ATOM   2273 O O     . ILE B 1 47  ? 30.946  -16.926 -1.554  1.00 58.61  ? 19  ILE B O     1 
ATOM   2274 C CB    . ILE B 1 47  ? 32.308  -15.473 0.563   1.00 51.93  ? 19  ILE B CB    1 
ATOM   2275 C CG1   . ILE B 1 47  ? 32.996  -14.285 1.241   1.00 53.92  ? 19  ILE B CG1   1 
ATOM   2276 C CG2   . ILE B 1 47  ? 32.441  -16.733 1.408   1.00 49.21  ? 19  ILE B CG2   1 
ATOM   2277 C CD1   . ILE B 1 47  ? 34.509  -14.342 1.203   1.00 58.20  ? 19  ILE B CD1   1 
ATOM   2278 N N     . ASP B 1 48  ? 32.951  -17.699 -2.215  1.00 59.52  ? 20  ASP B N     1 
ATOM   2279 C CA    . ASP B 1 48  ? 32.377  -18.894 -2.813  1.00 60.45  ? 20  ASP B CA    1 
ATOM   2280 C C     . ASP B 1 48  ? 32.025  -19.897 -1.715  1.00 63.17  ? 20  ASP B C     1 
ATOM   2281 O O     . ASP B 1 48  ? 32.260  -19.669 -0.524  1.00 64.40  ? 20  ASP B O     1 
ATOM   2282 C CB    . ASP B 1 48  ? 33.337  -19.497 -3.837  1.00 65.43  ? 20  ASP B CB    1 
ATOM   2283 C CG    . ASP B 1 48  ? 34.773  -19.518 -3.353  1.00 71.14  ? 20  ASP B CG    1 
ATOM   2284 O OD1   . ASP B 1 48  ? 34.996  -19.374 -2.133  1.00 70.77  ? 20  ASP B OD1   1 
ATOM   2285 O OD2   . ASP B 1 48  ? 35.681  -19.678 -4.197  1.00 73.03  ? 20  ASP B OD2   1 
ATOM   2286 N N     . LYS B 1 49  ? 31.456  -21.029 -2.131  1.00 62.19  ? 21  LYS B N     1 
ATOM   2287 C CA    . LYS B 1 49  ? 30.930  -22.036 -1.217  1.00 53.99  ? 21  LYS B CA    1 
ATOM   2288 C C     . LYS B 1 49  ? 29.942  -21.394 -0.249  1.00 51.35  ? 21  LYS B C     1 
ATOM   2289 O O     . LYS B 1 49  ? 30.247  -21.241 0.941   1.00 51.06  ? 21  LYS B O     1 
ATOM   2290 C CB    . LYS B 1 49  ? 32.062  -22.729 -0.453  1.00 54.18  ? 21  LYS B CB    1 
ATOM   2291 N N     . PRO B 1 50  ? 28.758  -20.990 -0.720  1.00 50.33  ? 22  PRO B N     1 
ATOM   2292 C CA    . PRO B 1 50  ? 27.767  -20.410 0.197   1.00 48.86  ? 22  PRO B CA    1 
ATOM   2293 C C     . PRO B 1 50  ? 27.230  -21.407 1.202   1.00 49.00  ? 22  PRO B C     1 
ATOM   2294 O O     . PRO B 1 50  ? 26.728  -20.992 2.254   1.00 49.93  ? 22  PRO B O     1 
ATOM   2295 C CB    . PRO B 1 50  ? 26.659  -19.923 -0.745  1.00 48.07  ? 22  PRO B CB    1 
ATOM   2296 C CG    . PRO B 1 50  ? 26.791  -20.792 -1.949  1.00 56.05  ? 22  PRO B CG    1 
ATOM   2297 C CD    . PRO B 1 50  ? 28.263  -21.041 -2.106  1.00 58.44  ? 22  PRO B CD    1 
ATOM   2298 N N     . HIS B 1 51  ? 27.316  -22.706 0.906   1.00 52.45  ? 23  HIS B N     1 
ATOM   2299 C CA    . HIS B 1 51  ? 26.846  -23.720 1.843   1.00 52.74  ? 23  HIS B CA    1 
ATOM   2300 C C     . HIS B 1 51  ? 27.604  -23.640 3.161   1.00 52.78  ? 23  HIS B C     1 
ATOM   2301 O O     . HIS B 1 51  ? 27.015  -23.796 4.237   1.00 52.25  ? 23  HIS B O     1 
ATOM   2302 C CB    . HIS B 1 51  ? 26.998  -25.109 1.221   1.00 56.43  ? 23  HIS B CB    1 
ATOM   2303 C CG    . HIS B 1 51  ? 25.827  -25.533 0.391   1.00 64.38  ? 23  HIS B CG    1 
ATOM   2304 N ND1   . HIS B 1 51  ? 25.139  -26.706 0.617   1.00 69.86  ? 23  HIS B ND1   1 
ATOM   2305 C CD2   . HIS B 1 51  ? 25.227  -24.944 -0.671  1.00 64.66  ? 23  HIS B CD2   1 
ATOM   2306 C CE1   . HIS B 1 51  ? 24.164  -26.819 -0.267  1.00 70.26  ? 23  HIS B CE1   1 
ATOM   2307 N NE2   . HIS B 1 51  ? 24.195  -25.763 -1.060  1.00 68.28  ? 23  HIS B NE2   1 
ATOM   2308 N N     . LEU B 1 52  ? 28.910  -23.387 3.097   1.00 51.28  ? 24  LEU B N     1 
ATOM   2309 C CA    . LEU B 1 52  ? 29.740  -23.322 4.291   1.00 51.51  ? 24  LEU B CA    1 
ATOM   2310 C C     . LEU B 1 52  ? 29.569  -22.024 5.067   1.00 50.11  ? 24  LEU B C     1 
ATOM   2311 O O     . LEU B 1 52  ? 30.096  -21.915 6.179   1.00 50.19  ? 24  LEU B O     1 
ATOM   2312 C CB    . LEU B 1 52  ? 31.213  -23.501 3.914   1.00 52.87  ? 24  LEU B CB    1 
ATOM   2313 C CG    . LEU B 1 52  ? 31.599  -24.862 3.331   1.00 54.53  ? 24  LEU B CG    1 
ATOM   2314 C CD1   . LEU B 1 52  ? 33.097  -24.933 3.073   1.00 55.88  ? 24  LEU B CD1   1 
ATOM   2315 C CD2   . LEU B 1 52  ? 31.154  -25.993 4.244   1.00 54.99  ? 24  LEU B CD2   1 
ATOM   2316 N N     . TYR B 1 53  ? 28.852  -21.042 4.519   1.00 48.91  ? 25  TYR B N     1 
ATOM   2317 C CA    . TYR B 1 53  ? 28.678  -19.772 5.211   1.00 47.64  ? 25  TYR B CA    1 
ATOM   2318 C C     . TYR B 1 53  ? 27.391  -19.711 6.022   1.00 46.55  ? 25  TYR B C     1 
ATOM   2319 O O     . TYR B 1 53  ? 27.365  -19.061 7.074   1.00 46.00  ? 25  TYR B O     1 
ATOM   2320 C CB    . TYR B 1 53  ? 28.711  -18.610 4.214   1.00 47.00  ? 25  TYR B CB    1 
ATOM   2321 C CG    . TYR B 1 53  ? 28.894  -17.262 4.874   1.00 46.02  ? 25  TYR B CG    1 
ATOM   2322 C CD1   . TYR B 1 53  ? 30.161  -16.765 5.146   1.00 46.56  ? 25  TYR B CD1   1 
ATOM   2323 C CD2   . TYR B 1 53  ? 27.799  -16.497 5.242   1.00 44.65  ? 25  TYR B CD2   1 
ATOM   2324 C CE1   . TYR B 1 53  ? 30.330  -15.535 5.754   1.00 45.75  ? 25  TYR B CE1   1 
ATOM   2325 C CE2   . TYR B 1 53  ? 27.955  -15.269 5.849   1.00 45.90  ? 25  TYR B CE2   1 
ATOM   2326 C CZ    . TYR B 1 53  ? 29.220  -14.792 6.104   1.00 46.32  ? 25  TYR B CZ    1 
ATOM   2327 O OH    . TYR B 1 53  ? 29.371  -13.567 6.712   1.00 48.50  ? 25  TYR B OH    1 
ATOM   2328 N N     . THR B 1 54  ? 26.322  -20.371 5.569   1.00 46.45  ? 26  THR B N     1 
ATOM   2329 C CA    . THR B 1 54  ? 25.095  -20.427 6.358   1.00 45.58  ? 26  THR B CA    1 
ATOM   2330 C C     . THR B 1 54  ? 25.266  -21.194 7.658   1.00 46.07  ? 26  THR B C     1 
ATOM   2331 O O     . THR B 1 54  ? 24.318  -21.258 8.447   1.00 45.44  ? 26  THR B O     1 
ATOM   2332 C CB    . THR B 1 54  ? 23.960  -21.054 5.550   1.00 45.58  ? 26  THR B CB    1 
ATOM   2333 O OG1   . THR B 1 54  ? 24.425  -22.252 4.916   1.00 48.26  ? 26  THR B OG1   1 
ATOM   2334 C CG2   . THR B 1 54  ? 23.452  -20.083 4.506   1.00 44.75  ? 26  THR B CG2   1 
ATOM   2335 N N     . LEU B 1 55  ? 26.435  -21.784 7.898   1.00 47.24  ? 27  LEU B N     1 
ATOM   2336 C CA    . LEU B 1 55  ? 26.717  -22.363 9.201   1.00 47.72  ? 27  LEU B CA    1 
ATOM   2337 C C     . LEU B 1 55  ? 26.777  -21.300 10.289  1.00 46.79  ? 27  LEU B C     1 
ATOM   2338 O O     . LEU B 1 55  ? 26.574  -21.617 11.466  1.00 52.63  ? 27  LEU B O     1 
ATOM   2339 C CB    . LEU B 1 55  ? 28.027  -23.144 9.142   1.00 49.26  ? 27  LEU B CB    1 
ATOM   2340 C CG    . LEU B 1 55  ? 27.959  -24.406 8.277   1.00 50.42  ? 27  LEU B CG    1 
ATOM   2341 C CD1   . LEU B 1 55  ? 29.329  -25.032 8.118   1.00 51.96  ? 27  LEU B CD1   1 
ATOM   2342 C CD2   . LEU B 1 55  ? 26.975  -25.411 8.850   1.00 50.57  ? 27  LEU B CD2   1 
ATOM   2343 N N     . GLY B 1 56  ? 27.047  -20.051 9.923   1.00 46.04  ? 28  GLY B N     1 
ATOM   2344 C CA    . GLY B 1 56  ? 27.058  -18.962 10.877  1.00 48.16  ? 28  GLY B CA    1 
ATOM   2345 C C     . GLY B 1 56  ? 25.766  -18.178 10.840  1.00 48.23  ? 28  GLY B C     1 
ATOM   2346 O O     . GLY B 1 56  ? 25.714  -17.036 11.302  1.00 46.11  ? 28  GLY B O     1 
ATOM   2347 N N     . CYS B 1 57  ? 24.719  -18.781 10.273  1.00 47.21  ? 29  CYS B N     1 
ATOM   2348 C CA    . CYS B 1 57  ? 23.407  -18.142 10.245  1.00 49.64  ? 29  CYS B CA    1 
ATOM   2349 C C     . CYS B 1 57  ? 22.926  -17.817 11.651  1.00 56.74  ? 29  CYS B C     1 
ATOM   2350 O O     . CYS B 1 57  ? 22.621  -16.663 11.966  1.00 55.00  ? 29  CYS B O     1 
ATOM   2351 C CB    . CYS B 1 57  ? 22.398  -19.044 9.534   1.00 59.40  ? 29  CYS B CB    1 
ATOM   2352 S SG    . CYS B 1 57  ? 20.868  -18.223 9.068   1.00 52.76  ? 29  CYS B SG    1 
ATOM   2353 N N     . CYS B 1 58  ? 22.878  -18.832 12.520  1.00 64.32  ? 30  CYS B N     1 
ATOM   2354 C CA    . CYS B 1 58  ? 22.269  -18.678 13.839  1.00 63.07  ? 30  CYS B CA    1 
ATOM   2355 C C     . CYS B 1 58  ? 22.873  -17.513 14.611  1.00 60.67  ? 30  CYS B C     1 
ATOM   2356 O O     . CYS B 1 58  ? 22.162  -16.793 15.319  1.00 61.84  ? 30  CYS B O     1 
ATOM   2357 C CB    . CYS B 1 58  ? 22.428  -19.976 14.630  1.00 67.09  ? 30  CYS B CB    1 
ATOM   2358 S SG    . CYS B 1 58  ? 22.428  -21.461 13.601  1.00 84.73  ? 30  CYS B SG    1 
ATOM   2359 N N     . SER B 1 59  ? 24.183  -17.307 14.479  1.00 58.92  ? 31  SER B N     1 
ATOM   2360 C CA    . SER B 1 59  ? 24.871  -16.259 15.220  1.00 53.73  ? 31  SER B CA    1 
ATOM   2361 C C     . SER B 1 59  ? 24.855  -14.924 14.482  1.00 49.42  ? 31  SER B C     1 
ATOM   2362 O O     . SER B 1 59  ? 24.509  -13.894 15.069  1.00 49.05  ? 31  SER B O     1 
ATOM   2363 C CB    . SER B 1 59  ? 26.312  -16.686 15.510  1.00 54.73  ? 31  SER B CB    1 
ATOM   2364 O OG    . SER B 1 59  ? 26.343  -17.798 16.387  1.00 56.77  ? 31  SER B OG    1 
ATOM   2365 N N     . LEU B 1 60  ? 25.226  -14.925 13.199  1.00 52.19  ? 32  LEU B N     1 
ATOM   2366 C CA    . LEU B 1 60  ? 25.283  -13.674 12.448  1.00 47.94  ? 32  LEU B CA    1 
ATOM   2367 C C     . LEU B 1 60  ? 23.904  -13.050 12.284  1.00 47.64  ? 32  LEU B C     1 
ATOM   2368 O O     . LEU B 1 60  ? 23.786  -11.820 12.237  1.00 46.22  ? 32  LEU B O     1 
ATOM   2369 C CB    . LEU B 1 60  ? 25.925  -13.908 11.081  1.00 50.39  ? 32  LEU B CB    1 
ATOM   2370 C CG    . LEU B 1 60  ? 27.407  -14.288 11.095  1.00 46.16  ? 32  LEU B CG    1 
ATOM   2371 C CD1   . LEU B 1 60  ? 27.905  -14.571 9.686   1.00 45.85  ? 32  LEU B CD1   1 
ATOM   2372 C CD2   . LEU B 1 60  ? 28.235  -13.197 11.756  1.00 43.82  ? 32  LEU B CD2   1 
ATOM   2373 N N     . THR B 1 61  ? 22.855  -13.871 12.191  1.00 54.40  ? 33  THR B N     1 
ATOM   2374 C CA    . THR B 1 61  ? 21.499  -13.335 12.127  1.00 47.36  ? 33  THR B CA    1 
ATOM   2375 C C     . THR B 1 61  ? 21.171  -12.542 13.384  1.00 49.24  ? 33  THR B C     1 
ATOM   2376 O O     . THR B 1 61  ? 20.745  -11.384 13.309  1.00 50.59  ? 33  THR B O     1 
ATOM   2377 C CB    . THR B 1 61  ? 20.490  -14.468 11.930  1.00 52.84  ? 33  THR B CB    1 
ATOM   2378 O OG1   . THR B 1 61  ? 20.728  -15.113 10.673  1.00 57.33  ? 33  THR B OG1   1 
ATOM   2379 C CG2   . THR B 1 61  ? 19.067  -13.940 11.969  1.00 56.75  ? 33  THR B CG2   1 
ATOM   2380 N N     . ALA B 1 62  ? 21.379  -13.149 14.555  1.00 51.06  ? 34  ALA B N     1 
ATOM   2381 C CA    . ALA B 1 62  ? 21.051  -12.479 15.809  1.00 54.17  ? 34  ALA B CA    1 
ATOM   2382 C C     . ALA B 1 62  ? 21.959  -11.284 16.073  1.00 52.73  ? 34  ALA B C     1 
ATOM   2383 O O     . ALA B 1 62  ? 21.534  -10.320 16.719  1.00 53.71  ? 34  ALA B O     1 
ATOM   2384 C CB    . ALA B 1 62  ? 21.132  -13.471 16.970  1.00 57.61  ? 34  ALA B CB    1 
ATOM   2385 N N     . MET B 1 63  ? 23.203  -11.325 15.589  1.00 50.96  ? 35  MET B N     1 
ATOM   2386 C CA    . MET B 1 63  ? 24.120  -10.213 15.822  1.00 50.44  ? 35  MET B CA    1 
ATOM   2387 C C     . MET B 1 63  ? 23.667  -8.961  15.082  1.00 51.29  ? 35  MET B C     1 
ATOM   2388 O O     . MET B 1 63  ? 23.557  -7.882  15.677  1.00 52.40  ? 35  MET B O     1 
ATOM   2389 C CB    . MET B 1 63  ? 25.537  -10.601 15.404  1.00 47.94  ? 35  MET B CB    1 
ATOM   2390 C CG    . MET B 1 63  ? 26.542  -9.471  15.546  1.00 47.81  ? 35  MET B CG    1 
ATOM   2391 S SD    . MET B 1 63  ? 28.087  -9.816  14.690  1.00 43.22  ? 35  MET B SD    1 
ATOM   2392 C CE    . MET B 1 63  ? 28.475  -11.425 15.368  1.00 50.63  ? 35  MET B CE    1 
ATOM   2393 N N     . ALA B 1 64  ? 23.407  -9.083  13.779  1.00 49.20  ? 36  ALA B N     1 
ATOM   2394 C CA    . ALA B 1 64  ? 22.879  -7.952  13.026  1.00 43.07  ? 36  ALA B CA    1 
ATOM   2395 C C     . ALA B 1 64  ? 21.479  -7.579  13.492  1.00 46.73  ? 36  ALA B C     1 
ATOM   2396 O O     . ALA B 1 64  ? 21.117  -6.397  13.479  1.00 50.08  ? 36  ALA B O     1 
ATOM   2397 C CB    . ALA B 1 64  ? 22.869  -8.270  11.533  1.00 45.61  ? 36  ALA B CB    1 
ATOM   2398 N N     . SER B 1 65  ? 20.682  -8.569  13.902  1.00 50.65  ? 37  SER B N     1 
ATOM   2399 C CA    . SER B 1 65  ? 19.364  -8.277  14.449  1.00 52.92  ? 37  SER B CA    1 
ATOM   2400 C C     . SER B 1 65  ? 19.468  -7.475  15.739  1.00 51.98  ? 37  SER B C     1 
ATOM   2401 O O     . SER B 1 65  ? 18.549  -6.723  16.079  1.00 51.50  ? 37  SER B O     1 
ATOM   2402 C CB    . SER B 1 65  ? 18.594  -9.576  14.687  1.00 54.92  ? 37  SER B CB    1 
ATOM   2403 O OG    . SER B 1 65  ? 17.250  -9.326  15.058  1.00 62.26  ? 37  SER B OG    1 
ATOM   2404 N N     . ALA B 1 66  ? 20.578  -7.612  16.464  1.00 50.05  ? 38  ALA B N     1 
ATOM   2405 C CA    . ALA B 1 66  ? 20.764  -6.825  17.676  1.00 52.44  ? 38  ALA B CA    1 
ATOM   2406 C C     . ALA B 1 66  ? 21.343  -5.451  17.362  1.00 48.63  ? 38  ALA B C     1 
ATOM   2407 O O     . ALA B 1 66  ? 20.963  -4.458  17.992  1.00 50.01  ? 38  ALA B O     1 
ATOM   2408 C CB    . ALA B 1 66  ? 21.659  -7.577  18.662  1.00 58.38  ? 38  ALA B CB    1 
ATOM   2409 N N     . GLN B 1 67  ? 22.260  -5.374  16.392  1.00 46.18  ? 39  GLN B N     1 
ATOM   2410 C CA    . GLN B 1 67  ? 22.809  -4.081  15.994  1.00 46.73  ? 39  GLN B CA    1 
ATOM   2411 C C     . GLN B 1 67  ? 21.725  -3.176  15.426  1.00 47.79  ? 39  GLN B C     1 
ATOM   2412 O O     . GLN B 1 67  ? 21.686  -1.977  15.724  1.00 48.68  ? 39  GLN B O     1 
ATOM   2413 C CB    . GLN B 1 67  ? 23.926  -4.272  14.970  1.00 51.79  ? 39  GLN B CB    1 
ATOM   2414 C CG    . GLN B 1 67  ? 25.223  -4.823  15.530  1.00 53.54  ? 39  GLN B CG    1 
ATOM   2415 C CD    . GLN B 1 67  ? 26.222  -5.162  14.438  1.00 52.09  ? 39  GLN B CD    1 
ATOM   2416 O OE1   . GLN B 1 67  ? 25.848  -5.419  13.294  1.00 45.40  ? 39  GLN B OE1   1 
ATOM   2417 N NE2   . GLN B 1 67  ? 27.504  -5.156  14.787  1.00 55.28  ? 39  GLN B NE2   1 
ATOM   2418 N N     . LEU B 1 68  ? 20.834  -3.734  14.602  1.00 46.63  ? 40  LEU B N     1 
ATOM   2419 C CA    . LEU B 1 68  ? 19.782  -2.928  13.992  1.00 45.29  ? 40  LEU B CA    1 
ATOM   2420 C C     . LEU B 1 68  ? 18.766  -2.451  15.021  1.00 53.63  ? 40  LEU B C     1 
ATOM   2421 O O     . LEU B 1 68  ? 18.235  -1.342  14.895  1.00 55.14  ? 40  LEU B O     1 
ATOM   2422 C CB    . LEU B 1 68  ? 19.083  -3.724  12.890  1.00 40.11  ? 40  LEU B CB    1 
ATOM   2423 C CG    . LEU B 1 68  ? 19.866  -3.887  11.589  1.00 36.36  ? 40  LEU B CG    1 
ATOM   2424 C CD1   . LEU B 1 68  ? 19.075  -4.712  10.594  1.00 39.71  ? 40  LEU B CD1   1 
ATOM   2425 C CD2   . LEU B 1 68  ? 20.228  -2.533  11.000  1.00 38.89  ? 40  LEU B CD2   1 
ATOM   2426 N N     . ASP B 1 69  ? 18.484  -3.267  16.040  1.00 53.82  ? 41  ASP B N     1 
ATOM   2427 C CA    . ASP B 1 69  ? 17.513  -2.873  17.056  1.00 49.83  ? 41  ASP B CA    1 
ATOM   2428 C C     . ASP B 1 69  ? 17.969  -1.636  17.817  1.00 49.50  ? 41  ASP B C     1 
ATOM   2429 O O     . ASP B 1 69  ? 17.135  -0.861  18.299  1.00 48.08  ? 41  ASP B O     1 
ATOM   2430 C CB    . ASP B 1 69  ? 17.265  -4.030  18.023  1.00 54.45  ? 41  ASP B CB    1 
ATOM   2431 C CG    . ASP B 1 69  ? 16.401  -5.122  17.420  1.00 60.43  ? 41  ASP B CG    1 
ATOM   2432 O OD1   . ASP B 1 69  ? 15.784  -4.877  16.361  1.00 62.10  ? 41  ASP B OD1   1 
ATOM   2433 O OD2   . ASP B 1 69  ? 16.346  -6.229  17.998  1.00 60.84  ? 41  ASP B OD2   1 
ATOM   2434 N N     . ALA B 1 70  ? 19.282  -1.432  17.937  1.00 49.57  ? 42  ALA B N     1 
ATOM   2435 C CA    . ALA B 1 70  ? 19.782  -0.248  18.625  1.00 49.39  ? 42  ALA B CA    1 
ATOM   2436 C C     . ALA B 1 70  ? 19.643  1.001   17.765  1.00 51.77  ? 42  ALA B C     1 
ATOM   2437 O O     . ALA B 1 70  ? 19.550  2.112   18.300  1.00 53.84  ? 42  ALA B O     1 
ATOM   2438 C CB    . ALA B 1 70  ? 21.240  -0.453  19.035  1.00 48.37  ? 42  ALA B CB    1 
ATOM   2439 N N     . LEU B 1 71  ? 19.618  0.844   16.441  1.00 52.72  ? 43  LEU B N     1 
ATOM   2440 C CA    . LEU B 1 71  ? 19.527  1.974   15.527  1.00 51.15  ? 43  LEU B CA    1 
ATOM   2441 C C     . LEU B 1 71  ? 18.135  2.184   14.951  1.00 48.95  ? 43  LEU B C     1 
ATOM   2442 O O     . LEU B 1 71  ? 17.839  3.290   14.487  1.00 49.00  ? 43  LEU B O     1 
ATOM   2443 C CB    . LEU B 1 71  ? 20.504  1.798   14.358  1.00 47.60  ? 43  LEU B CB    1 
ATOM   2444 C CG    . LEU B 1 71  ? 22.000  1.722   14.652  1.00 53.38  ? 43  LEU B CG    1 
ATOM   2445 C CD1   . LEU B 1 71  ? 22.771  1.524   13.359  1.00 46.12  ? 43  LEU B CD1   1 
ATOM   2446 C CD2   . LEU B 1 71  ? 22.465  2.975   15.367  1.00 59.11  ? 43  LEU B CD2   1 
ATOM   2447 N N     . TRP B 1 72  ? 17.279  1.159   14.978  1.00 46.95  ? 44  TRP B N     1 
ATOM   2448 C CA    . TRP B 1 72  ? 16.047  1.186   14.196  1.00 45.41  ? 44  TRP B CA    1 
ATOM   2449 C C     . TRP B 1 72  ? 15.116  2.324   14.595  1.00 54.01  ? 44  TRP B C     1 
ATOM   2450 O O     . TRP B 1 72  ? 14.277  2.733   13.786  1.00 54.37  ? 44  TRP B O     1 
ATOM   2451 C CB    . TRP B 1 72  ? 15.319  -0.152  14.317  1.00 45.14  ? 44  TRP B CB    1 
ATOM   2452 C CG    . TRP B 1 72  ? 14.489  -0.467  13.121  1.00 43.10  ? 44  TRP B CG    1 
ATOM   2453 C CD1   . TRP B 1 72  ? 13.147  -0.281  12.980  1.00 41.83  ? 44  TRP B CD1   1 
ATOM   2454 C CD2   . TRP B 1 72  ? 14.953  -1.006  11.878  1.00 43.73  ? 44  TRP B CD2   1 
ATOM   2455 N NE1   . TRP B 1 72  ? 12.743  -0.681  11.730  1.00 43.47  ? 44  TRP B NE1   1 
ATOM   2456 C CE2   . TRP B 1 72  ? 13.835  -1.129  11.033  1.00 47.32  ? 44  TRP B CE2   1 
ATOM   2457 C CE3   . TRP B 1 72  ? 16.207  -1.402  11.401  1.00 40.26  ? 44  TRP B CE3   1 
ATOM   2458 C CZ2   . TRP B 1 72  ? 13.931  -1.629  9.736   1.00 45.05  ? 44  TRP B CZ2   1 
ATOM   2459 C CZ3   . TRP B 1 72  ? 16.300  -1.898  10.115  1.00 40.39  ? 44  TRP B CZ3   1 
ATOM   2460 C CH2   . TRP B 1 72  ? 15.169  -2.009  9.297   1.00 41.78  ? 44  TRP B CH2   1 
ATOM   2461 N N     . SER B 1 73  ? 15.242  2.846   15.817  1.00 56.57  ? 45  SER B N     1 
ATOM   2462 C CA    . SER B 1 73  ? 14.423  3.986   16.210  1.00 54.06  ? 45  SER B CA    1 
ATOM   2463 C C     . SER B 1 73  ? 14.869  5.264   15.511  1.00 50.24  ? 45  SER B C     1 
ATOM   2464 O O     . SER B 1 73  ? 14.038  6.132   15.219  1.00 49.56  ? 45  SER B O     1 
ATOM   2465 C CB    . SER B 1 73  ? 14.468  4.170   17.727  1.00 54.28  ? 45  SER B CB    1 
ATOM   2466 O OG    . SER B 1 73  ? 15.782  4.470   18.164  1.00 56.45  ? 45  SER B OG    1 
ATOM   2467 N N     . GLN B 1 74  ? 16.165  5.394   15.227  1.00 50.22  ? 46  GLN B N     1 
ATOM   2468 C CA    . GLN B 1 74  ? 16.709  6.590   14.596  1.00 49.15  ? 46  GLN B CA    1 
ATOM   2469 C C     . GLN B 1 74  ? 16.486  6.631   13.090  1.00 45.54  ? 46  GLN B C     1 
ATOM   2470 O O     . GLN B 1 74  ? 16.932  7.585   12.443  1.00 46.56  ? 46  GLN B O     1 
ATOM   2471 C CB    . GLN B 1 74  ? 18.207  6.703   14.889  1.00 46.13  ? 46  GLN B CB    1 
ATOM   2472 C CG    . GLN B 1 74  ? 18.550  6.850   16.360  1.00 50.40  ? 46  GLN B CG    1 
ATOM   2473 C CD    . GLN B 1 74  ? 20.045  6.828   16.610  1.00 56.13  ? 46  GLN B CD    1 
ATOM   2474 O OE1   . GLN B 1 74  ? 20.544  6.020   17.393  1.00 60.92  ? 46  GLN B OE1   1 
ATOM   2475 N NE2   . GLN B 1 74  ? 20.769  7.717   15.940  1.00 50.69  ? 46  GLN B NE2   1 
ATOM   2476 N N     . LEU B 1 75  ? 15.818  5.634   12.517  1.00 37.88  ? 47  LEU B N     1 
ATOM   2477 C CA    . LEU B 1 75  ? 15.595  5.582   11.079  1.00 37.93  ? 47  LEU B CA    1 
ATOM   2478 C C     . LEU B 1 75  ? 14.253  6.215   10.735  1.00 54.14  ? 47  LEU B C     1 
ATOM   2479 O O     . LEU B 1 75  ? 13.220  5.847   11.305  1.00 50.52  ? 47  LEU B O     1 
ATOM   2480 C CB    . LEU B 1 75  ? 15.645  4.139   10.575  1.00 35.84  ? 47  LEU B CB    1 
ATOM   2481 C CG    . LEU B 1 75  ? 17.004  3.440   10.649  1.00 30.19  ? 47  LEU B CG    1 
ATOM   2482 C CD1   . LEU B 1 75  ? 16.850  1.948   10.414  1.00 33.65  ? 47  LEU B CD1   1 
ATOM   2483 C CD2   . LEU B 1 75  ? 17.971  4.043   9.647   1.00 31.68  ? 47  LEU B CD2   1 
ATOM   2484 N N     . SER B 1 76  ? 14.275  7.164   9.805   1.00 42.81  ? 48  SER B N     1 
ATOM   2485 C CA    . SER B 1 76  ? 13.079  7.843   9.330   1.00 43.48  ? 48  SER B CA    1 
ATOM   2486 C C     . SER B 1 76  ? 12.721  7.332   7.942   1.00 40.93  ? 48  SER B C     1 
ATOM   2487 O O     . SER B 1 76  ? 13.596  7.167   7.087   1.00 50.04  ? 48  SER B O     1 
ATOM   2488 C CB    . SER B 1 76  ? 13.286  9.359   9.299   1.00 50.06  ? 48  SER B CB    1 
ATOM   2489 O OG    . SER B 1 76  ? 14.286  9.721   8.361   1.00 60.55  ? 48  SER B OG    1 
ATOM   2490 N N     . TRP B 1 77  ? 11.431  7.090   7.719   1.00 40.79  ? 49  TRP B N     1 
ATOM   2491 C CA    . TRP B 1 77  ? 10.967  6.456   6.497   1.00 41.73  ? 49  TRP B CA    1 
ATOM   2492 C C     . TRP B 1 77  ? 10.021  7.376   5.735   1.00 36.82  ? 49  TRP B C     1 
ATOM   2493 O O     . TRP B 1 77  ? 9.288   8.162   6.343   1.00 45.38  ? 49  TRP B O     1 
ATOM   2494 C CB    . TRP B 1 77  ? 10.249  5.139   6.812   1.00 42.18  ? 49  TRP B CB    1 
ATOM   2495 C CG    . TRP B 1 77  ? 11.128  4.136   7.486   1.00 39.96  ? 49  TRP B CG    1 
ATOM   2496 C CD1   . TRP B 1 77  ? 11.286  3.961   8.830   1.00 40.82  ? 49  TRP B CD1   1 
ATOM   2497 C CD2   . TRP B 1 77  ? 11.971  3.167   6.853   1.00 42.35  ? 49  TRP B CD2   1 
ATOM   2498 N NE1   . TRP B 1 77  ? 12.177  2.944   9.073   1.00 40.22  ? 49  TRP B NE1   1 
ATOM   2499 C CE2   . TRP B 1 77  ? 12.611  2.439   7.876   1.00 39.94  ? 49  TRP B CE2   1 
ATOM   2500 C CE3   . TRP B 1 77  ? 12.247  2.844   5.521   1.00 39.58  ? 49  TRP B CE3   1 
ATOM   2501 C CZ2   . TRP B 1 77  ? 13.510  1.409   7.609   1.00 38.28  ? 49  TRP B CZ2   1 
ATOM   2502 C CZ3   . TRP B 1 77  ? 13.139  1.820   5.258   1.00 39.43  ? 49  TRP B CZ3   1 
ATOM   2503 C CH2   . TRP B 1 77  ? 13.760  1.116   6.297   1.00 42.01  ? 49  TRP B CH2   1 
ATOM   2504 N N     . PRO B 1 78  ? 10.012  7.303   4.408   1.00 34.64  ? 50  PRO B N     1 
ATOM   2505 C CA    . PRO B 1 78  ? 9.053   8.091   3.630   1.00 40.83  ? 50  PRO B CA    1 
ATOM   2506 C C     . PRO B 1 78  ? 7.655   7.493   3.693   1.00 42.09  ? 50  PRO B C     1 
ATOM   2507 O O     . PRO B 1 78  ? 7.460   6.323   4.028   1.00 41.49  ? 50  PRO B O     1 
ATOM   2508 C CB    . PRO B 1 78  ? 9.616   8.030   2.206   1.00 38.64  ? 50  PRO B CB    1 
ATOM   2509 C CG    . PRO B 1 78  ? 10.366  6.744   2.162   1.00 40.62  ? 50  PRO B CG    1 
ATOM   2510 C CD    . PRO B 1 78  ? 10.914  6.516   3.548   1.00 43.73  ? 50  PRO B CD    1 
ATOM   2511 N N     . GLN B 1 79  ? 6.672   8.335   3.369   1.00 44.37  ? 51  GLN B N     1 
ATOM   2512 C CA    . GLN B 1 79  ? 5.274   7.918   3.337   1.00 44.37  ? 51  GLN B CA    1 
ATOM   2513 C C     . GLN B 1 79  ? 5.076   6.771   2.354   1.00 43.68  ? 51  GLN B C     1 
ATOM   2514 O O     . GLN B 1 79  ? 4.782   5.641   2.759   1.00 43.60  ? 51  GLN B O     1 
ATOM   2515 C CB    . GLN B 1 79  ? 4.371   9.097   2.968   1.00 48.81  ? 51  GLN B CB    1 
ATOM   2516 C CG    . GLN B 1 79  ? 3.967   9.970   4.146   1.00 48.80  ? 51  GLN B CG    1 
ATOM   2517 C CD    . GLN B 1 79  ? 3.041   9.254   5.112   1.00 49.73  ? 51  GLN B CD    1 
ATOM   2518 O OE1   . GLN B 1 79  ? 2.285   8.365   4.722   1.00 47.33  ? 51  GLN B OE1   1 
ATOM   2519 N NE2   . GLN B 1 79  ? 3.091   9.646   6.379   1.00 50.37  ? 51  GLN B NE2   1 
ATOM   2520 N N     . THR B 1 80  ? 5.227   7.052   1.066   1.00 42.80  ? 52  THR B N     1 
ATOM   2521 C CA    . THR B 1 80  ? 5.213   5.998   0.061   1.00 41.83  ? 52  THR B CA    1 
ATOM   2522 C C     . THR B 1 80  ? 6.553   5.273   0.085   1.00 45.40  ? 52  THR B C     1 
ATOM   2523 O O     . THR B 1 80  ? 7.597   5.922   -0.043  1.00 46.56  ? 52  THR B O     1 
ATOM   2524 C CB    . THR B 1 80  ? 4.945   6.574   -1.322  1.00 40.63  ? 52  THR B CB    1 
ATOM   2525 O OG1   . THR B 1 80  ? 3.693   7.272   -1.315  1.00 42.61  ? 52  THR B OG1   1 
ATOM   2526 C CG2   . THR B 1 80  ? 4.891   5.461   -2.358  1.00 42.76  ? 52  THR B CG2   1 
ATOM   2527 N N     . PRO B 1 81  ? 6.573   3.951   0.258   1.00 41.15  ? 53  PRO B N     1 
ATOM   2528 C CA    . PRO B 1 81  ? 7.850   3.251   0.440   1.00 37.47  ? 53  PRO B CA    1 
ATOM   2529 C C     . PRO B 1 81  ? 8.741   3.347   -0.789  1.00 37.94  ? 53  PRO B C     1 
ATOM   2530 O O     . PRO B 1 81  ? 8.271   3.405   -1.927  1.00 42.21  ? 53  PRO B O     1 
ATOM   2531 C CB    . PRO B 1 81  ? 7.429   1.800   0.703   1.00 39.84  ? 53  PRO B CB    1 
ATOM   2532 C CG    . PRO B 1 81  ? 6.010   1.874   1.144   1.00 42.76  ? 53  PRO B CG    1 
ATOM   2533 C CD    . PRO B 1 81  ? 5.413   3.071   0.470   1.00 44.45  ? 53  PRO B CD    1 
ATOM   2534 N N     . LEU B 1 82  ? 10.044  3.369   -0.540  1.00 35.44  ? 54  LEU B N     1 
ATOM   2535 C CA    . LEU B 1 82  ? 11.068  3.286   -1.566  1.00 34.48  ? 54  LEU B CA    1 
ATOM   2536 C C     . LEU B 1 82  ? 11.811  1.960   -1.458  1.00 35.71  ? 54  LEU B C     1 
ATOM   2537 O O     . LEU B 1 82  ? 11.823  1.328   -0.395  1.00 37.95  ? 54  LEU B O     1 
ATOM   2538 C CB    . LEU B 1 82  ? 12.066  4.447   -1.444  1.00 34.28  ? 54  LEU B CB    1 
ATOM   2539 C CG    . LEU B 1 82  ? 11.525  5.852   -1.705  1.00 33.04  ? 54  LEU B CG    1 
ATOM   2540 C CD1   . LEU B 1 82  ? 12.621  6.892   -1.519  1.00 31.99  ? 54  LEU B CD1   1 
ATOM   2541 C CD2   . LEU B 1 82  ? 10.926  5.942   -3.099  1.00 34.82  ? 54  LEU B CD2   1 
ATOM   2542 N N     . PRO B 1 83  ? 12.428  1.495   -2.544  1.00 31.24  ? 55  PRO B N     1 
ATOM   2543 C CA    . PRO B 1 83  ? 13.201  0.250   -2.467  1.00 31.73  ? 55  PRO B CA    1 
ATOM   2544 C C     . PRO B 1 83  ? 14.399  0.393   -1.539  1.00 33.76  ? 55  PRO B C     1 
ATOM   2545 O O     . PRO B 1 83  ? 15.018  1.455   -1.440  1.00 32.74  ? 55  PRO B O     1 
ATOM   2546 C CB    . PRO B 1 83  ? 13.641  0.005   -3.916  1.00 32.96  ? 55  PRO B CB    1 
ATOM   2547 C CG    . PRO B 1 83  ? 12.761  0.866   -4.756  1.00 37.17  ? 55  PRO B CG    1 
ATOM   2548 C CD    . PRO B 1 83  ? 12.344  2.023   -3.916  1.00 31.74  ? 55  PRO B CD    1 
ATOM   2549 N N     . VAL B 1 84  ? 14.718  -0.701  -0.851  1.00 31.93  ? 56  VAL B N     1 
ATOM   2550 C CA    . VAL B 1 84  ? 15.807  -0.752  0.115   1.00 32.02  ? 56  VAL B CA    1 
ATOM   2551 C C     . VAL B 1 84  ? 16.849  -1.742  -0.386  1.00 32.83  ? 56  VAL B C     1 
ATOM   2552 O O     . VAL B 1 84  ? 16.506  -2.820  -0.883  1.00 37.94  ? 56  VAL B O     1 
ATOM   2553 C CB    . VAL B 1 84  ? 15.295  -1.143  1.517   1.00 31.61  ? 56  VAL B CB    1 
ATOM   2554 C CG1   . VAL B 1 84  ? 16.448  -1.490  2.437   1.00 32.62  ? 56  VAL B CG1   1 
ATOM   2555 C CG2   . VAL B 1 84  ? 14.468  -0.014  2.106   1.00 32.56  ? 56  VAL B CG2   1 
ATOM   2556 N N     . LEU B 1 85  ? 18.121  -1.372  -0.259  1.00 33.17  ? 57  LEU B N     1 
ATOM   2557 C CA    . LEU B 1 85  ? 19.226  -2.145  -0.807  1.00 34.04  ? 57  LEU B CA    1 
ATOM   2558 C C     . LEU B 1 85  ? 20.090  -2.718  0.309   1.00 34.31  ? 57  LEU B C     1 
ATOM   2559 O O     . LEU B 1 85  ? 20.386  -2.033  1.294   1.00 33.98  ? 57  LEU B O     1 
ATOM   2560 C CB    . LEU B 1 85  ? 20.082  -1.278  -1.733  1.00 34.43  ? 57  LEU B CB    1 
ATOM   2561 C CG    . LEU B 1 85  ? 21.317  -1.924  -2.360  1.00 35.43  ? 57  LEU B CG    1 
ATOM   2562 C CD1   . LEU B 1 85  ? 20.910  -3.044  -3.303  1.00 35.94  ? 57  LEU B CD1   1 
ATOM   2563 C CD2   . LEU B 1 85  ? 22.146  -0.881  -3.088  1.00 35.77  ? 57  LEU B CD2   1 
ATOM   2564 N N     . ASP B 1 86  ? 20.491  -3.978  0.148   1.00 35.00  ? 58  ASP B N     1 
ATOM   2565 C CA    . ASP B 1 86  ? 21.443  -4.636  1.039   1.00 35.48  ? 58  ASP B CA    1 
ATOM   2566 C C     . ASP B 1 86  ? 22.667  -5.020  0.217   1.00 36.48  ? 58  ASP B C     1 
ATOM   2567 O O     . ASP B 1 86  ? 22.600  -5.928  -0.618  1.00 37.06  ? 58  ASP B O     1 
ATOM   2568 C CB    . ASP B 1 86  ? 20.827  -5.864  1.709   1.00 39.28  ? 58  ASP B CB    1 
ATOM   2569 C CG    . ASP B 1 86  ? 21.758  -6.502  2.730   1.00 50.90  ? 58  ASP B CG    1 
ATOM   2570 O OD1   . ASP B 1 86  ? 22.714  -5.827  3.171   1.00 50.82  ? 58  ASP B OD1   1 
ATOM   2571 O OD2   . ASP B 1 86  ? 21.534  -7.678  3.092   1.00 48.16  ? 58  ASP B OD2   1 
ATOM   2572 N N     . ILE B 1 87  ? 23.778  -4.332  0.456   1.00 36.77  ? 59  ILE B N     1 
ATOM   2573 C CA    . ILE B 1 87  ? 25.017  -4.568  -0.274  1.00 37.79  ? 59  ILE B CA    1 
ATOM   2574 C C     . ILE B 1 87  ? 25.833  -5.610  0.477   1.00 42.11  ? 59  ILE B C     1 
ATOM   2575 O O     . ILE B 1 87  ? 26.029  -5.500  1.693   1.00 45.03  ? 59  ILE B O     1 
ATOM   2576 C CB    . ILE B 1 87  ? 25.809  -3.261  -0.445  1.00 37.85  ? 59  ILE B CB    1 
ATOM   2577 C CG1   . ILE B 1 87  ? 25.013  -2.267  -1.290  1.00 37.26  ? 59  ILE B CG1   1 
ATOM   2578 C CG2   . ILE B 1 87  ? 27.153  -3.533  -1.092  1.00 39.01  ? 59  ILE B CG2   1 
ATOM   2579 C CD1   . ILE B 1 87  ? 25.690  -0.928  -1.458  1.00 37.32  ? 59  ILE B CD1   1 
ATOM   2580 N N     . GLY B 1 88  ? 26.311  -6.621  -0.245  1.00 42.89  ? 60  GLY B N     1 
ATOM   2581 C CA    . GLY B 1 88  ? 27.035  -7.708  0.380   1.00 43.02  ? 60  GLY B CA    1 
ATOM   2582 C C     . GLY B 1 88  ? 26.151  -8.494  1.324   1.00 41.69  ? 60  GLY B C     1 
ATOM   2583 O O     . GLY B 1 88  ? 26.463  -8.640  2.509   1.00 44.49  ? 60  GLY B O     1 
ATOM   2584 N N     . CYS B 1 89  ? 25.031  -8.998  0.804   1.00 44.02  ? 61  CYS B N     1 
ATOM   2585 C CA    . CYS B 1 89  ? 24.064  -9.693  1.643   1.00 47.38  ? 61  CYS B CA    1 
ATOM   2586 C C     . CYS B 1 89  ? 24.523  -11.091 2.027   1.00 49.21  ? 61  CYS B C     1 
ATOM   2587 O O     . CYS B 1 89  ? 23.967  -11.676 2.964   1.00 48.24  ? 61  CYS B O     1 
ATOM   2588 C CB    . CYS B 1 89  ? 22.718  -9.775  0.928   1.00 44.25  ? 61  CYS B CB    1 
ATOM   2589 S SG    . CYS B 1 89  ? 22.755  -10.771 -0.578  1.00 39.52  ? 61  CYS B SG    1 
ATOM   2590 N N     . GLY B 1 90  ? 25.518  -11.637 1.334   1.00 46.69  ? 62  GLY B N     1 
ATOM   2591 C CA    . GLY B 1 90  ? 25.950  -12.993 1.566   1.00 47.03  ? 62  GLY B CA    1 
ATOM   2592 C C     . GLY B 1 90  ? 24.908  -13.991 1.107   1.00 44.62  ? 62  GLY B C     1 
ATOM   2593 O O     . GLY B 1 90  ? 24.261  -13.816 0.070   1.00 43.76  ? 62  GLY B O     1 
ATOM   2594 N N     . PRO B 1 91  ? 24.715  -15.060 1.884   1.00 42.95  ? 63  PRO B N     1 
ATOM   2595 C CA    . PRO B 1 91  ? 23.721  -16.077 1.514   1.00 42.72  ? 63  PRO B CA    1 
ATOM   2596 C C     . PRO B 1 91  ? 22.281  -15.619 1.672   1.00 41.59  ? 63  PRO B C     1 
ATOM   2597 O O     . PRO B 1 91  ? 21.369  -16.428 1.467   1.00 42.64  ? 63  PRO B O     1 
ATOM   2598 C CB    . PRO B 1 91  ? 24.037  -17.234 2.468   1.00 43.45  ? 63  PRO B CB    1 
ATOM   2599 C CG    . PRO B 1 91  ? 24.644  -16.578 3.655   1.00 43.04  ? 63  PRO B CG    1 
ATOM   2600 C CD    . PRO B 1 91  ? 25.403  -15.386 3.144   1.00 42.81  ? 63  PRO B CD    1 
ATOM   2601 N N     . GLY B 1 92  ? 22.045  -14.359 2.026   1.00 44.09  ? 64  GLY B N     1 
ATOM   2602 C CA    . GLY B 1 92  ? 20.697  -13.832 2.073   1.00 44.57  ? 64  GLY B CA    1 
ATOM   2603 C C     . GLY B 1 92  ? 19.941  -14.098 3.352   1.00 42.37  ? 64  GLY B C     1 
ATOM   2604 O O     . GLY B 1 92  ? 18.707  -14.077 3.342   1.00 43.34  ? 64  GLY B O     1 
ATOM   2605 N N     . ASP B 1 93  ? 20.639  -14.347 4.458   1.00 42.44  ? 65  ASP B N     1 
ATOM   2606 C CA    . ASP B 1 93  ? 19.959  -14.594 5.722   1.00 43.99  ? 65  ASP B CA    1 
ATOM   2607 C C     . ASP B 1 93  ? 19.645  -13.303 6.467   1.00 42.62  ? 65  ASP B C     1 
ATOM   2608 O O     . ASP B 1 93  ? 18.569  -13.181 7.061   1.00 44.35  ? 65  ASP B O     1 
ATOM   2609 C CB    . ASP B 1 93  ? 20.801  -15.523 6.598   1.00 46.61  ? 65  ASP B CB    1 
ATOM   2610 C CG    . ASP B 1 93  ? 20.946  -16.908 5.997   1.00 48.75  ? 65  ASP B CG    1 
ATOM   2611 O OD1   . ASP B 1 93  ? 19.976  -17.692 6.068   1.00 55.28  ? 65  ASP B OD1   1 
ATOM   2612 O OD2   . ASP B 1 93  ? 22.033  -17.217 5.465   1.00 45.24  ? 65  ASP B OD2   1 
ATOM   2613 N N     . ILE B 1 94  ? 20.563  -12.335 6.449   1.00 40.16  ? 66  ILE B N     1 
ATOM   2614 C CA    . ILE B 1 94  ? 20.255  -11.019 7.002   1.00 36.67  ? 66  ILE B CA    1 
ATOM   2615 C C     . ILE B 1 94  ? 19.170  -10.343 6.174   1.00 36.07  ? 66  ILE B C     1 
ATOM   2616 O O     . ILE B 1 94  ? 18.290  -9.659  6.710   1.00 38.62  ? 66  ILE B O     1 
ATOM   2617 C CB    . ILE B 1 94  ? 21.532  -10.160 7.084   1.00 40.80  ? 66  ILE B CB    1 
ATOM   2618 C CG1   . ILE B 1 94  ? 22.352  -10.539 8.319   1.00 46.01  ? 66  ILE B CG1   1 
ATOM   2619 C CG2   . ILE B 1 94  ? 21.200  -8.672  7.096   1.00 42.06  ? 66  ILE B CG2   1 
ATOM   2620 C CD1   . ILE B 1 94  ? 23.691  -9.844  8.392   1.00 48.58  ? 66  ILE B CD1   1 
ATOM   2621 N N     . ALA B 1 95  ? 19.202  -10.546 4.855   1.00 39.95  ? 67  ALA B N     1 
ATOM   2622 C CA    . ALA B 1 95  ? 18.209  -9.929  3.982   1.00 37.36  ? 67  ALA B CA    1 
ATOM   2623 C C     . ALA B 1 95  ? 16.818  -10.501 4.224   1.00 35.44  ? 67  ALA B C     1 
ATOM   2624 O O     . ALA B 1 95  ? 15.835  -9.753  4.276   1.00 34.69  ? 67  ALA B O     1 
ATOM   2625 C CB    . ALA B 1 95  ? 18.620  -10.106 2.520   1.00 36.32  ? 67  ALA B CB    1 
ATOM   2626 N N     . ARG B 1 96  ? 16.711  -11.820 4.386   1.00 36.10  ? 68  ARG B N     1 
ATOM   2627 C CA    . ARG B 1 96  ? 15.406  -12.456 4.531   1.00 36.00  ? 68  ARG B CA    1 
ATOM   2628 C C     . ARG B 1 96  ? 14.897  -12.445 5.969   1.00 35.55  ? 68  ARG B C     1 
ATOM   2629 O O     . ARG B 1 96  ? 13.723  -12.140 6.203   1.00 37.17  ? 68  ARG B O     1 
ATOM   2630 C CB    . ARG B 1 96  ? 15.461  -13.897 4.015   1.00 37.01  ? 68  ARG B CB    1 
ATOM   2631 C CG    . ARG B 1 96  ? 14.352  -14.786 4.564   1.00 39.25  ? 68  ARG B CG    1 
ATOM   2632 C CD    . ARG B 1 96  ? 12.998  -14.403 3.984   1.00 44.99  ? 68  ARG B CD    1 
ATOM   2633 N NE    . ARG B 1 96  ? 11.895  -14.989 4.737   1.00 55.95  ? 68  ARG B NE    1 
ATOM   2634 C CZ    . ARG B 1 96  ? 10.804  -15.506 4.189   1.00 64.73  ? 68  ARG B CZ    1 
ATOM   2635 N NH1   . ARG B 1 96  ? 10.643  -15.549 2.876   1.00 66.73  ? 68  ARG B NH1   1 
ATOM   2636 N NH2   . ARG B 1 96  ? 9.848   -15.990 4.978   1.00 58.64  ? 68  ARG B NH2   1 
ATOM   2637 N N     . LYS B 1 97  ? 15.755  -12.765 6.937   1.00 37.90  ? 69  LYS B N     1 
ATOM   2638 C CA    . LYS B 1 97  ? 15.315  -12.998 8.307   1.00 35.66  ? 69  LYS B CA    1 
ATOM   2639 C C     . LYS B 1 97  ? 15.424  -11.776 9.210   1.00 34.90  ? 69  LYS B C     1 
ATOM   2640 O O     . LYS B 1 97  ? 14.741  -11.728 10.239  1.00 37.36  ? 69  LYS B O     1 
ATOM   2641 C CB    . LYS B 1 97  ? 16.121  -14.148 8.922   1.00 38.98  ? 69  LYS B CB    1 
ATOM   2642 C CG    . LYS B 1 97  ? 15.946  -15.464 8.184   1.00 42.38  ? 69  LYS B CG    1 
ATOM   2643 C CD    . LYS B 1 97  ? 16.842  -16.549 8.743   1.00 46.17  ? 69  LYS B CD    1 
ATOM   2644 C CE    . LYS B 1 97  ? 16.741  -17.810 7.904   1.00 60.78  ? 69  LYS B CE    1 
ATOM   2645 N NZ    . LYS B 1 97  ? 17.721  -18.836 8.344   1.00 72.30  ? 69  LYS B NZ    1 
ATOM   2646 N N     . VAL B 1 98  ? 16.254  -10.795 8.862   1.00 34.69  ? 70  VAL B N     1 
ATOM   2647 C CA    . VAL B 1 98  ? 16.477  -9.614  9.694   1.00 34.09  ? 70  VAL B CA    1 
ATOM   2648 C C     . VAL B 1 98  ? 15.864  -8.367  9.061   1.00 33.33  ? 70  VAL B C     1 
ATOM   2649 O O     . VAL B 1 98  ? 15.045  -7.685  9.680   1.00 41.88  ? 70  VAL B O     1 
ATOM   2650 C CB    . VAL B 1 98  ? 17.981  -9.412  9.984   1.00 34.56  ? 70  VAL B CB    1 
ATOM   2651 C CG1   . VAL B 1 98  ? 18.189  -8.202  10.876  1.00 37.71  ? 70  VAL B CG1   1 
ATOM   2652 C CG2   . VAL B 1 98  ? 18.569  -10.654 10.621  1.00 41.50  ? 70  VAL B CG2   1 
ATOM   2653 N N     . LEU B 1 99  ? 16.252  -8.052  7.824   1.00 33.44  ? 71  LEU B N     1 
ATOM   2654 C CA    . LEU B 1 99  ? 15.799  -6.813  7.199   1.00 32.81  ? 71  LEU B CA    1 
ATOM   2655 C C     . LEU B 1 99  ? 14.338  -6.902  6.777   1.00 32.43  ? 71  LEU B C     1 
ATOM   2656 O O     . LEU B 1 99  ? 13.530  -6.032  7.124   1.00 38.28  ? 71  LEU B O     1 
ATOM   2657 C CB    . LEU B 1 99  ? 16.685  -6.478  5.999   1.00 33.14  ? 71  LEU B CB    1 
ATOM   2658 C CG    . LEU B 1 99  ? 18.090  -5.972  6.325   1.00 33.44  ? 71  LEU B CG    1 
ATOM   2659 C CD1   . LEU B 1 99  ? 18.906  -5.785  5.056   1.00 33.90  ? 71  LEU B CD1   1 
ATOM   2660 C CD2   . LEU B 1 99  ? 18.011  -4.676  7.111   1.00 32.81  ? 71  LEU B CD2   1 
ATOM   2661 N N     . ALA B 1 100 ? 13.982  -7.946  6.028   1.00 32.91  ? 72  ALA B N     1 
ATOM   2662 C CA    . ALA B 1 100 ? 12.636  -8.038  5.469   1.00 32.69  ? 72  ALA B CA    1 
ATOM   2663 C C     . ALA B 1 100 ? 11.522  -7.958  6.509   1.00 37.59  ? 72  ALA B C     1 
ATOM   2664 O O     . ALA B 1 100 ? 10.526  -7.263  6.244   1.00 40.43  ? 72  ALA B O     1 
ATOM   2665 C CB    . ALA B 1 100 ? 12.510  -9.321  4.636   1.00 33.44  ? 72  ALA B CB    1 
ATOM   2666 N N     . PRO B 1 101 ? 11.597  -8.618  7.672   1.00 36.84  ? 73  PRO B N     1 
ATOM   2667 C CA    . PRO B 1 101 ? 10.513  -8.450  8.653   1.00 39.09  ? 73  PRO B CA    1 
ATOM   2668 C C     . PRO B 1 101 ? 10.445  -7.055  9.251   1.00 38.60  ? 73  PRO B C     1 
ATOM   2669 O O     . PRO B 1 101 ? 9.345   -6.580  9.558   1.00 40.83  ? 73  PRO B O     1 
ATOM   2670 C CB    . PRO B 1 101 ? 10.836  -9.502  9.725   1.00 44.61  ? 73  PRO B CB    1 
ATOM   2671 C CG    . PRO B 1 101 ? 11.715  -10.488 9.045   1.00 42.66  ? 73  PRO B CG    1 
ATOM   2672 C CD    . PRO B 1 101 ? 12.525  -9.691  8.075   1.00 37.57  ? 73  PRO B CD    1 
ATOM   2673 N N     . ARG B 1 102 ? 11.583  -6.382  9.424   1.00 36.86  ? 74  ARG B N     1 
ATOM   2674 C CA    . ARG B 1 102 ? 11.615  -5.102  10.120  1.00 35.78  ? 74  ARG B CA    1 
ATOM   2675 C C     . ARG B 1 102 ? 11.256  -3.918  9.232   1.00 38.98  ? 74  ARG B C     1 
ATOM   2676 O O     . ARG B 1 102 ? 11.075  -2.811  9.751   1.00 43.77  ? 74  ARG B O     1 
ATOM   2677 C CB    . ARG B 1 102 ? 12.999  -4.883  10.736  1.00 31.37  ? 74  ARG B CB    1 
ATOM   2678 C CG    . ARG B 1 102 ? 13.252  -5.726  11.972  1.00 38.55  ? 74  ARG B CG    1 
ATOM   2679 C CD    . ARG B 1 102 ? 14.720  -5.744  12.358  1.00 42.84  ? 74  ARG B CD    1 
ATOM   2680 N NE    . ARG B 1 102 ? 14.922  -6.389  13.650  1.00 52.14  ? 74  ARG B NE    1 
ATOM   2681 C CZ    . ARG B 1 102 ? 14.954  -7.702  13.835  1.00 52.49  ? 74  ARG B CZ    1 
ATOM   2682 N NH1   . ARG B 1 102 ? 14.800  -8.547  12.829  1.00 47.40  ? 74  ARG B NH1   1 
ATOM   2683 N NH2   . ARG B 1 102 ? 15.144  -8.180  15.062  1.00 56.09  ? 74  ARG B NH2   1 
ATOM   2684 N N     . LEU B 1 103 ? 11.138  -4.115  7.921   1.00 38.39  ? 75  LEU B N     1 
ATOM   2685 C CA    . LEU B 1 103 ? 10.833  -3.016  7.023   1.00 42.24  ? 75  LEU B CA    1 
ATOM   2686 C C     . LEU B 1 103 ? 9.371   -2.597  7.153   1.00 37.80  ? 75  LEU B C     1 
ATOM   2687 O O     . LEU B 1 103 ? 8.529   -3.372  7.615   1.00 41.61  ? 75  LEU B O     1 
ATOM   2688 C CB    . LEU B 1 103 ? 11.131  -3.413  5.579   1.00 33.01  ? 75  LEU B CB    1 
ATOM   2689 C CG    . LEU B 1 103 ? 12.596  -3.654  5.217   1.00 30.91  ? 75  LEU B CG    1 
ATOM   2690 C CD1   . LEU B 1 103 ? 12.710  -4.271  3.832   1.00 32.75  ? 75  LEU B CD1   1 
ATOM   2691 C CD2   . LEU B 1 103 ? 13.388  -2.361  5.302   1.00 33.93  ? 75  LEU B CD2   1 
ATOM   2692 N N     . PRO B 1 104 ? 9.045   -1.365  6.761   1.00 38.06  ? 76  PRO B N     1 
ATOM   2693 C CA    . PRO B 1 104 ? 7.635   -0.973  6.669   1.00 37.78  ? 76  PRO B CA    1 
ATOM   2694 C C     . PRO B 1 104 ? 6.908   -1.798  5.617   1.00 43.34  ? 76  PRO B C     1 
ATOM   2695 O O     . PRO B 1 104 ? 7.517   -2.429  4.749   1.00 47.04  ? 76  PRO B O     1 
ATOM   2696 C CB    . PRO B 1 104 ? 7.697   0.507   6.269   1.00 38.31  ? 76  PRO B CB    1 
ATOM   2697 C CG    . PRO B 1 104 ? 9.060   0.959   6.666   1.00 40.07  ? 76  PRO B CG    1 
ATOM   2698 C CD    . PRO B 1 104 ? 9.953   -0.232  6.508   1.00 39.40  ? 76  PRO B CD    1 
ATOM   2699 N N     . ALA B 1 105 ? 5.580   -1.790  5.706   1.00 39.91  ? 77  ALA B N     1 
ATOM   2700 C CA    . ALA B 1 105 ? 4.769   -2.552  4.767   1.00 39.63  ? 77  ALA B CA    1 
ATOM   2701 C C     . ALA B 1 105 ? 4.926   -2.004  3.354   1.00 41.13  ? 77  ALA B C     1 
ATOM   2702 O O     . ALA B 1 105 ? 5.077   -0.796  3.150   1.00 42.06  ? 77  ALA B O     1 
ATOM   2703 C CB    . ALA B 1 105 ? 3.300   -2.518  5.187   1.00 43.40  ? 77  ALA B CB    1 
ATOM   2704 N N     . GLY B 1 106 ? 4.896   -2.905  2.374   1.00 44.87  ? 78  GLY B N     1 
ATOM   2705 C CA    . GLY B 1 106 ? 5.046   -2.511  0.989   1.00 45.88  ? 78  GLY B CA    1 
ATOM   2706 C C     . GLY B 1 106 ? 6.438   -2.083  0.586   1.00 45.06  ? 78  GLY B C     1 
ATOM   2707 O O     . GLY B 1 106 ? 6.626   -1.637  -0.550  1.00 47.17  ? 78  GLY B O     1 
ATOM   2708 N N     . THR B 1 107 ? 7.420   -2.202  1.477   1.00 45.91  ? 79  THR B N     1 
ATOM   2709 C CA    . THR B 1 107 ? 8.797   -1.821  1.179   1.00 40.59  ? 79  THR B CA    1 
ATOM   2710 C C     . THR B 1 107 ? 9.494   -2.993  0.501   1.00 39.05  ? 79  THR B C     1 
ATOM   2711 O O     . THR B 1 107 ? 9.691   -4.046  1.116   1.00 39.90  ? 79  THR B O     1 
ATOM   2712 C CB    . THR B 1 107 ? 9.539   -1.414  2.451   1.00 39.32  ? 79  THR B CB    1 
ATOM   2713 O OG1   . THR B 1 107 ? 8.844   -0.336  3.092   1.00 41.88  ? 79  THR B OG1   1 
ATOM   2714 C CG2   . THR B 1 107 ? 10.954  -0.969  2.119   1.00 36.84  ? 79  THR B CG2   1 
ATOM   2715 N N     . ARG B 1 108 ? 9.865   -2.813  -0.762  1.00 40.42  ? 80  ARG B N     1 
ATOM   2716 C CA    . ARG B 1 108 ? 10.587  -3.844  -1.488  1.00 38.81  ? 80  ARG B CA    1 
ATOM   2717 C C     . ARG B 1 108 ? 12.060  -3.826  -1.101  1.00 36.47  ? 80  ARG B C     1 
ATOM   2718 O O     . ARG B 1 108 ? 12.616  -2.788  -0.733  1.00 32.59  ? 80  ARG B O     1 
ATOM   2719 C CB    . ARG B 1 108 ? 10.435  -3.647  -2.996  1.00 39.48  ? 80  ARG B CB    1 
ATOM   2720 C CG    . ARG B 1 108 ? 9.084   -4.080  -3.543  1.00 44.75  ? 80  ARG B CG    1 
ATOM   2721 C CD    . ARG B 1 108 ? 8.910   -3.662  -4.995  1.00 52.54  ? 80  ARG B CD    1 
ATOM   2722 N NE    . ARG B 1 108 ? 9.012   -2.217  -5.155  1.00 66.03  ? 80  ARG B NE    1 
ATOM   2723 C CZ    . ARG B 1 108 ? 8.377   -1.517  -6.086  1.00 73.54  ? 80  ARG B CZ    1 
ATOM   2724 N NH1   . ARG B 1 108 ? 7.578   -2.099  -6.964  1.00 68.56  ? 80  ARG B NH1   1 
ATOM   2725 N NH2   . ARG B 1 108 ? 8.551   -0.199  -6.138  1.00 71.41  ? 80  ARG B NH2   1 
ATOM   2726 N N     . LEU B 1 109 ? 12.690  -4.994  -1.191  1.00 42.28  ? 81  LEU B N     1 
ATOM   2727 C CA    . LEU B 1 109 ? 14.079  -5.173  -0.795  1.00 37.29  ? 81  LEU B CA    1 
ATOM   2728 C C     . LEU B 1 109 ? 14.894  -5.694  -1.970  1.00 34.18  ? 81  LEU B C     1 
ATOM   2729 O O     . LEU B 1 109 ? 14.434  -6.554  -2.728  1.00 34.70  ? 81  LEU B O     1 
ATOM   2730 C CB    . LEU B 1 109 ? 14.192  -6.142  0.389   1.00 33.42  ? 81  LEU B CB    1 
ATOM   2731 C CG    . LEU B 1 109 ? 15.605  -6.497  0.861   1.00 33.87  ? 81  LEU B CG    1 
ATOM   2732 C CD1   . LEU B 1 109 ? 16.359  -5.252  1.301   1.00 33.48  ? 81  LEU B CD1   1 
ATOM   2733 C CD2   . LEU B 1 109 ? 15.555  -7.517  1.985   1.00 34.02  ? 81  LEU B CD2   1 
ATOM   2734 N N     . VAL B 1 110 ? 16.105  -5.163  -2.116  1.00 34.39  ? 82  VAL B N     1 
ATOM   2735 C CA    . VAL B 1 110 ? 17.049  -5.605  -3.135  1.00 35.27  ? 82  VAL B CA    1 
ATOM   2736 C C     . VAL B 1 110 ? 18.344  -5.982  -2.432  1.00 35.68  ? 82  VAL B C     1 
ATOM   2737 O O     . VAL B 1 110 ? 18.920  -5.166  -1.704  1.00 35.32  ? 82  VAL B O     1 
ATOM   2738 C CB    . VAL B 1 110 ? 17.306  -4.524  -4.199  1.00 35.31  ? 82  VAL B CB    1 
ATOM   2739 C CG1   . VAL B 1 110 ? 18.270  -5.041  -5.256  1.00 36.33  ? 82  VAL B CG1   1 
ATOM   2740 C CG2   . VAL B 1 110 ? 15.999  -4.083  -4.836  1.00 34.93  ? 82  VAL B CG2   1 
ATOM   2741 N N     . ALA B 1 111 ? 18.797  -7.214  -2.642  1.00 36.51  ? 83  ALA B N     1 
ATOM   2742 C CA    . ALA B 1 111 ? 20.034  -7.709  -2.058  1.00 37.08  ? 83  ALA B CA    1 
ATOM   2743 C C     . ALA B 1 111 ? 20.975  -8.143  -3.171  1.00 38.13  ? 83  ALA B C     1 
ATOM   2744 O O     . ALA B 1 111 ? 20.557  -8.801  -4.128  1.00 38.64  ? 83  ALA B O     1 
ATOM   2745 C CB    . ALA B 1 111 ? 19.768  -8.875  -1.103  1.00 37.22  ? 83  ALA B CB    1 
ATOM   2746 N N     . CYS B 1 112 ? 22.246  -7.768  -3.047  1.00 38.53  ? 84  CYS B N     1 
ATOM   2747 C CA    . CYS B 1 112 ? 23.230  -8.069  -4.075  1.00 39.59  ? 84  CYS B CA    1 
ATOM   2748 C C     . CYS B 1 112 ? 24.508  -8.582  -3.431  1.00 46.78  ? 84  CYS B C     1 
ATOM   2749 O O     . CYS B 1 112 ? 24.749  -8.398  -2.235  1.00 50.99  ? 84  CYS B O     1 
ATOM   2750 C CB    . CYS B 1 112 ? 23.535  -6.841  -4.943  1.00 39.51  ? 84  CYS B CB    1 
ATOM   2751 S SG    . CYS B 1 112 ? 23.752  -5.307  -4.016  1.00 38.59  ? 84  CYS B SG    1 
ATOM   2752 N N     . ASP B 1 113 ? 25.330  -9.229  -4.253  1.00 44.99  ? 85  ASP B N     1 
ATOM   2753 C CA    . ASP B 1 113 ? 26.610  -9.770  -3.820  1.00 45.91  ? 85  ASP B CA    1 
ATOM   2754 C C     . ASP B 1 113 ? 27.481  -9.952  -5.054  1.00 49.19  ? 85  ASP B C     1 
ATOM   2755 O O     . ASP B 1 113 ? 26.984  -10.342 -6.113  1.00 50.80  ? 85  ASP B O     1 
ATOM   2756 C CB    . ASP B 1 113 ? 26.433  -11.103 -3.083  1.00 46.25  ? 85  ASP B CB    1 
ATOM   2757 C CG    . ASP B 1 113 ? 27.484  -11.324 -2.013  1.00 50.08  ? 85  ASP B CG    1 
ATOM   2758 O OD1   . ASP B 1 113 ? 27.317  -10.790 -0.897  1.00 50.70  ? 85  ASP B OD1   1 
ATOM   2759 O OD2   . ASP B 1 113 ? 28.476  -12.033 -2.288  1.00 52.92  ? 85  ASP B OD2   1 
ATOM   2760 N N     . ILE B 1 114 ? 28.777  -9.661  -4.915  1.00 52.27  ? 86  ILE B N     1 
ATOM   2761 C CA    . ILE B 1 114 ? 29.686  -9.837  -6.041  1.00 45.46  ? 86  ILE B CA    1 
ATOM   2762 C C     . ILE B 1 114 ? 29.871  -11.311 -6.374  1.00 46.58  ? 86  ILE B C     1 
ATOM   2763 O O     . ILE B 1 114 ? 30.255  -11.646 -7.500  1.00 47.59  ? 86  ILE B O     1 
ATOM   2764 C CB    . ILE B 1 114 ? 31.045  -9.166  -5.756  1.00 45.99  ? 86  ILE B CB    1 
ATOM   2765 C CG1   . ILE B 1 114 ? 31.842  -8.995  -7.051  1.00 47.10  ? 86  ILE B CG1   1 
ATOM   2766 C CG2   . ILE B 1 114 ? 31.845  -9.981  -4.761  1.00 46.65  ? 86  ILE B CG2   1 
ATOM   2767 C CD1   . ILE B 1 114 ? 33.233  -8.435  -6.844  1.00 50.42  ? 86  ILE B CD1   1 
ATOM   2768 N N     . SER B 1 115 ? 29.588  -12.204 -5.428  1.00 46.69  ? 87  SER B N     1 
ATOM   2769 C CA    . SER B 1 115 ? 29.759  -13.633 -5.643  1.00 47.60  ? 87  SER B CA    1 
ATOM   2770 C C     . SER B 1 115 ? 28.513  -14.210 -6.298  1.00 47.39  ? 87  SER B C     1 
ATOM   2771 O O     . SER B 1 115 ? 27.423  -14.117 -5.717  1.00 50.55  ? 87  SER B O     1 
ATOM   2772 C CB    . SER B 1 115 ? 30.029  -14.342 -4.327  1.00 52.51  ? 87  SER B CB    1 
ATOM   2773 O OG    . SER B 1 115 ? 29.875  -15.744 -4.461  1.00 59.02  ? 87  SER B OG    1 
ATOM   2774 N N     . PRO B 1 116 ? 28.616  -14.801 -7.492  1.00 48.44  ? 88  PRO B N     1 
ATOM   2775 C CA    . PRO B 1 116 ? 27.435  -15.439 -8.096  1.00 48.40  ? 88  PRO B CA    1 
ATOM   2776 C C     . PRO B 1 116 ? 26.971  -16.674 -7.348  1.00 49.83  ? 88  PRO B C     1 
ATOM   2777 O O     . PRO B 1 116 ? 25.814  -17.080 -7.515  1.00 48.28  ? 88  PRO B O     1 
ATOM   2778 C CB    . PRO B 1 116 ? 27.908  -15.793 -9.514  1.00 49.73  ? 88  PRO B CB    1 
ATOM   2779 C CG    . PRO B 1 116 ? 29.139  -14.964 -9.739  1.00 50.10  ? 88  PRO B CG    1 
ATOM   2780 C CD    . PRO B 1 116 ? 29.776  -14.818 -8.395  1.00 49.73  ? 88  PRO B CD    1 
ATOM   2781 N N     . GLU B 1 117 ? 27.833  -17.286 -6.533  1.00 51.31  ? 89  GLU B N     1 
ATOM   2782 C CA    . GLU B 1 117 ? 27.414  -18.439 -5.745  1.00 51.54  ? 89  GLU B CA    1 
ATOM   2783 C C     . GLU B 1 117 ? 26.438  -18.028 -4.650  1.00 50.09  ? 89  GLU B C     1 
ATOM   2784 O O     . GLU B 1 117 ? 25.492  -18.764 -4.345  1.00 49.95  ? 89  GLU B O     1 
ATOM   2785 C CB    . GLU B 1 117 ? 28.631  -19.143 -5.142  1.00 53.88  ? 89  GLU B CB    1 
ATOM   2786 C CG    . GLU B 1 117 ? 29.710  -19.553 -6.145  1.00 59.19  ? 89  GLU B CG    1 
ATOM   2787 C CD    . GLU B 1 117 ? 30.591  -18.395 -6.580  1.00 62.51  ? 89  GLU B CD    1 
ATOM   2788 O OE1   . GLU B 1 117 ? 31.110  -17.677 -5.700  1.00 66.94  ? 89  GLU B OE1   1 
ATOM   2789 O OE2   . GLU B 1 117 ? 30.765  -18.201 -7.802  1.00 62.73  ? 89  GLU B OE2   1 
ATOM   2790 N N     . MET B 1 118 ? 26.655  -16.858 -4.044  1.00 50.28  ? 90  MET B N     1 
ATOM   2791 C CA    . MET B 1 118 ? 25.699  -16.329 -3.076  1.00 45.63  ? 90  MET B CA    1 
ATOM   2792 C C     . MET B 1 118 ? 24.344  -16.074 -3.727  1.00 44.92  ? 90  MET B C     1 
ATOM   2793 O O     . MET B 1 118 ? 23.302  -16.474 -3.196  1.00 44.42  ? 90  MET B O     1 
ATOM   2794 C CB    . MET B 1 118 ? 26.241  -15.043 -2.449  1.00 45.33  ? 90  MET B CB    1 
ATOM   2795 C CG    . MET B 1 118 ? 27.443  -15.230 -1.537  1.00 46.63  ? 90  MET B CG    1 
ATOM   2796 S SD    . MET B 1 118 ? 27.158  -16.484 -0.276  1.00 45.65  ? 90  MET B SD    1 
ATOM   2797 C CE    . MET B 1 118 ? 28.449  -16.090 0.899   1.00 45.88  ? 90  MET B CE    1 
ATOM   2798 N N     . VAL B 1 119 ? 24.342  -15.408 -4.885  1.00 44.95  ? 91  VAL B N     1 
ATOM   2799 C CA    . VAL B 1 119 ? 23.088  -15.059 -5.550  1.00 44.32  ? 91  VAL B CA    1 
ATOM   2800 C C     . VAL B 1 119 ? 22.304  -16.314 -5.911  1.00 44.98  ? 91  VAL B C     1 
ATOM   2801 O O     . VAL B 1 119 ? 21.074  -16.353 -5.783  1.00 44.36  ? 91  VAL B O     1 
ATOM   2802 C CB    . VAL B 1 119 ? 23.370  -14.190 -6.789  1.00 44.46  ? 91  VAL B CB    1 
ATOM   2803 C CG1   . VAL B 1 119 ? 22.070  -13.693 -7.396  1.00 43.76  ? 91  VAL B CG1   1 
ATOM   2804 C CG2   . VAL B 1 119 ? 24.275  -13.027 -6.422  1.00 44.02  ? 91  VAL B CG2   1 
ATOM   2805 N N     . ASP B 1 120 ? 22.999  -17.358 -6.366  1.00 46.34  ? 92  ASP B N     1 
ATOM   2806 C CA    . ASP B 1 120 ? 22.320  -18.606 -6.698  1.00 47.13  ? 92  ASP B CA    1 
ATOM   2807 C C     . ASP B 1 120 ? 21.765  -19.279 -5.449  1.00 46.78  ? 92  ASP B C     1 
ATOM   2808 O O     . ASP B 1 120 ? 20.691  -19.890 -5.490  1.00 46.80  ? 92  ASP B O     1 
ATOM   2809 C CB    . ASP B 1 120 ? 23.277  -19.543 -7.434  1.00 52.00  ? 92  ASP B CB    1 
ATOM   2810 C CG    . ASP B 1 120 ? 23.515  -19.121 -8.870  1.00 50.93  ? 92  ASP B CG    1 
ATOM   2811 O OD1   . ASP B 1 120 ? 22.733  -18.295 -9.386  1.00 48.53  ? 92  ASP B OD1   1 
ATOM   2812 O OD2   . ASP B 1 120 ? 24.485  -19.615 -9.483  1.00 62.45  ? 92  ASP B OD2   1 
ATOM   2813 N N     . PHE B 1 121 ? 22.485  -19.177 -4.330  1.00 46.54  ? 93  PHE B N     1 
ATOM   2814 C CA    . PHE B 1 121 ? 22.010  -19.759 -3.081  1.00 46.22  ? 93  PHE B CA    1 
ATOM   2815 C C     . PHE B 1 121 ? 20.812  -18.995 -2.532  1.00 44.81  ? 93  PHE B C     1 
ATOM   2816 O O     . PHE B 1 121 ? 19.924  -19.597 -1.916  1.00 44.65  ? 93  PHE B O     1 
ATOM   2817 C CB    . PHE B 1 121 ? 23.150  -19.786 -2.060  1.00 46.41  ? 93  PHE B CB    1 
ATOM   2818 C CG    . PHE B 1 121 ? 22.834  -20.552 -0.804  1.00 46.39  ? 93  PHE B CG    1 
ATOM   2819 C CD1   . PHE B 1 121 ? 22.167  -19.948 0.250   1.00 45.19  ? 93  PHE B CD1   1 
ATOM   2820 C CD2   . PHE B 1 121 ? 23.215  -21.877 -0.675  1.00 47.66  ? 93  PHE B CD2   1 
ATOM   2821 C CE1   . PHE B 1 121 ? 21.880  -20.652 1.401   1.00 45.24  ? 93  PHE B CE1   1 
ATOM   2822 C CE2   . PHE B 1 121 ? 22.932  -22.586 0.476   1.00 47.71  ? 93  PHE B CE2   1 
ATOM   2823 C CZ    . PHE B 1 121 ? 22.264  -21.972 1.515   1.00 46.49  ? 93  PHE B CZ    1 
ATOM   2824 N N     . CYS B 1 122 ? 20.765  -17.680 -2.751  1.00 43.86  ? 94  CYS B N     1 
ATOM   2825 C CA    . CYS B 1 122 ? 19.688  -16.865 -2.196  1.00 42.56  ? 94  CYS B CA    1 
ATOM   2826 C C     . CYS B 1 122 ? 18.355  -17.174 -2.865  1.00 42.51  ? 94  CYS B C     1 
ATOM   2827 O O     . CYS B 1 122 ? 17.334  -17.343 -2.188  1.00 42.29  ? 94  CYS B O     1 
ATOM   2828 C CB    . CYS B 1 122 ? 20.022  -15.381 -2.349  1.00 41.70  ? 94  CYS B CB    1 
ATOM   2829 S SG    . CYS B 1 122 ? 21.408  -14.796 -1.360  1.00 41.57  ? 94  CYS B SG    1 
ATOM   2830 N N     . ARG B 1 123 ? 18.344  -17.249 -4.197  1.00 43.13  ? 95  ARG B N     1 
ATOM   2831 C CA    . ARG B 1 123 ? 17.096  -17.377 -4.941  1.00 43.11  ? 95  ARG B CA    1 
ATOM   2832 C C     . ARG B 1 123 ? 16.386  -18.704 -4.701  1.00 43.80  ? 95  ARG B C     1 
ATOM   2833 O O     . ARG B 1 123 ? 15.239  -18.854 -5.135  1.00 51.34  ? 95  ARG B O     1 
ATOM   2834 C CB    . ARG B 1 123 ? 17.360  -17.187 -6.436  1.00 43.78  ? 95  ARG B CB    1 
ATOM   2835 C CG    . ARG B 1 123 ? 17.731  -15.760 -6.812  1.00 43.04  ? 95  ARG B CG    1 
ATOM   2836 C CD    . ARG B 1 123 ? 17.937  -15.608 -8.310  1.00 43.79  ? 95  ARG B CD    1 
ATOM   2837 N NE    . ARG B 1 123 ? 18.308  -14.244 -8.672  1.00 43.15  ? 95  ARG B NE    1 
ATOM   2838 C CZ    . ARG B 1 123 ? 19.218  -13.932 -9.585  1.00 43.80  ? 95  ARG B CZ    1 
ATOM   2839 N NH1   . ARG B 1 123 ? 19.874  -14.864 -10.255 1.00 45.11  ? 95  ARG B NH1   1 
ATOM   2840 N NH2   . ARG B 1 123 ? 19.474  -12.650 -9.833  1.00 43.19  ? 95  ARG B NH2   1 
ATOM   2841 N N     . GLN B 1 124 ? 17.025  -19.659 -4.027  1.00 45.27  ? 96  GLN B N     1 
ATOM   2842 C CA    . GLN B 1 124 ? 16.385  -20.921 -3.674  1.00 45.26  ? 96  GLN B CA    1 
ATOM   2843 C C     . GLN B 1 124 ? 15.941  -20.968 -2.217  1.00 46.39  ? 96  GLN B C     1 
ATOM   2844 O O     . GLN B 1 124 ? 14.782  -21.283 -1.931  1.00 50.08  ? 96  GLN B O     1 
ATOM   2845 C CB    . GLN B 1 124 ? 17.326  -22.100 -3.951  1.00 48.89  ? 96  GLN B CB    1 
ATOM   2846 C CG    . GLN B 1 124 ? 17.478  -22.471 -5.413  1.00 59.71  ? 96  GLN B CG    1 
ATOM   2847 C CD    . GLN B 1 124 ? 18.475  -23.597 -5.616  1.00 69.55  ? 96  GLN B CD    1 
ATOM   2848 O OE1   . GLN B 1 124 ? 18.764  -24.357 -4.691  1.00 67.67  ? 96  GLN B OE1   1 
ATOM   2849 N NE2   . GLN B 1 124 ? 19.003  -23.710 -6.829  1.00 75.09  ? 96  GLN B NE2   1 
ATOM   2850 N N     . HIS B 1 125 ? 16.843  -20.652 -1.288  1.00 45.27  ? 97  HIS B N     1 
ATOM   2851 C CA    . HIS B 1 125 ? 16.608  -20.898 0.128   1.00 46.60  ? 97  HIS B CA    1 
ATOM   2852 C C     . HIS B 1 125 ? 16.050  -19.696 0.880   1.00 45.23  ? 97  HIS B C     1 
ATOM   2853 O O     . HIS B 1 125 ? 15.395  -19.885 1.910   1.00 49.90  ? 97  HIS B O     1 
ATOM   2854 C CB    . HIS B 1 125 ? 17.907  -21.360 0.796   1.00 46.73  ? 97  HIS B CB    1 
ATOM   2855 C CG    . HIS B 1 125 ? 18.458  -22.625 0.216   1.00 47.78  ? 97  HIS B CG    1 
ATOM   2856 N ND1   . HIS B 1 125 ? 19.211  -22.647 -0.938  1.00 49.73  ? 97  HIS B ND1   1 
ATOM   2857 C CD2   . HIS B 1 125 ? 18.356  -23.912 0.623   1.00 50.66  ? 97  HIS B CD2   1 
ATOM   2858 C CE1   . HIS B 1 125 ? 19.554  -23.893 -1.214  1.00 52.39  ? 97  HIS B CE1   1 
ATOM   2859 N NE2   . HIS B 1 125 ? 19.048  -24.680 -0.282  1.00 54.75  ? 97  HIS B NE2   1 
ATOM   2860 N N     . ASN B 1 126 ? 16.293  -18.477 0.403   1.00 41.53  ? 98  ASN B N     1 
ATOM   2861 C CA    . ASN B 1 126 ? 15.689  -17.302 1.018   1.00 43.31  ? 98  ASN B CA    1 
ATOM   2862 C C     . ASN B 1 126 ? 14.775  -16.602 0.022   1.00 42.06  ? 98  ASN B C     1 
ATOM   2863 O O     . ASN B 1 126 ? 14.837  -15.380 -0.142  1.00 42.53  ? 98  ASN B O     1 
ATOM   2864 C CB    . ASN B 1 126 ? 16.764  -16.345 1.536   1.00 41.63  ? 98  ASN B CB    1 
ATOM   2865 C CG    . ASN B 1 126 ? 17.535  -16.918 2.710   1.00 44.43  ? 98  ASN B CG    1 
ATOM   2866 O OD1   . ASN B 1 126 ? 18.762  -17.000 2.682   1.00 45.81  ? 98  ASN B OD1   1 
ATOM   2867 N ND2   . ASN B 1 126 ? 16.814  -17.323 3.749   1.00 46.42  ? 98  ASN B ND2   1 
ATOM   2868 N N     . ALA B 1 127 ? 13.921  -17.375 -0.644  1.00 43.97  ? 99  ALA B N     1 
ATOM   2869 C CA    . ALA B 1 127 ? 13.000  -16.828 -1.630  1.00 45.71  ? 99  ALA B CA    1 
ATOM   2870 C C     . ALA B 1 127 ? 11.833  -16.154 -0.921  1.00 49.97  ? 99  ALA B C     1 
ATOM   2871 O O     . ALA B 1 127 ? 11.149  -16.780 -0.104  1.00 53.19  ? 99  ALA B O     1 
ATOM   2872 C CB    . ALA B 1 127 ? 12.501  -17.931 -2.560  1.00 51.68  ? 99  ALA B CB    1 
ATOM   2873 N N     . LEU B 1 128 ? 11.610  -14.880 -1.229  1.00 51.96  ? 100 LEU B N     1 
ATOM   2874 C CA    . LEU B 1 128 ? 10.465  -14.128 -0.713  1.00 50.50  ? 100 LEU B CA    1 
ATOM   2875 C C     . LEU B 1 128 ? 9.862   -13.355 -1.874  1.00 48.06  ? 100 LEU B C     1 
ATOM   2876 O O     . LEU B 1 128 ? 10.158  -12.171 -2.078  1.00 50.80  ? 100 LEU B O     1 
ATOM   2877 C CB    . LEU B 1 128 ? 10.877  -13.202 0.433   1.00 47.40  ? 100 LEU B CB    1 
ATOM   2878 C CG    . LEU B 1 128 ? 9.759   -12.420 1.128   1.00 44.56  ? 100 LEU B CG    1 
ATOM   2879 C CD1   . LEU B 1 128 ? 8.600   -13.335 1.494   1.00 49.16  ? 100 LEU B CD1   1 
ATOM   2880 C CD2   . LEU B 1 128 ? 10.290  -11.707 2.362   1.00 48.94  ? 100 LEU B CD2   1 
ATOM   2881 N N     . PRO B 1 129 ? 9.018   -14.006 -2.676  1.00 44.45  ? 101 PRO B N     1 
ATOM   2882 C CA    . PRO B 1 129 ? 8.476   -13.348 -3.870  1.00 46.39  ? 101 PRO B CA    1 
ATOM   2883 C C     . PRO B 1 129 ? 7.649   -12.123 -3.512  1.00 49.37  ? 101 PRO B C     1 
ATOM   2884 O O     . PRO B 1 129 ? 6.970   -12.079 -2.485  1.00 50.89  ? 101 PRO B O     1 
ATOM   2885 C CB    . PRO B 1 129 ? 7.610   -14.438 -4.514  1.00 52.58  ? 101 PRO B CB    1 
ATOM   2886 C CG    . PRO B 1 129 ? 8.161   -15.724 -3.987  1.00 51.71  ? 101 PRO B CG    1 
ATOM   2887 C CD    . PRO B 1 129 ? 8.620   -15.421 -2.592  1.00 48.32  ? 101 PRO B CD    1 
ATOM   2888 N N     . GLY B 1 130 ? 7.723   -11.113 -4.380  1.00 47.91  ? 102 GLY B N     1 
ATOM   2889 C CA    . GLY B 1 130 ? 7.031   -9.862  -4.171  1.00 53.50  ? 102 GLY B CA    1 
ATOM   2890 C C     . GLY B 1 130 ? 7.729   -8.883  -3.254  1.00 52.00  ? 102 GLY B C     1 
ATOM   2891 O O     . GLY B 1 130 ? 7.400   -7.690  -3.281  1.00 54.08  ? 102 GLY B O     1 
ATOM   2892 N N     . THR B 1 131 ? 8.683   -9.340  -2.444  1.00 49.00  ? 103 THR B N     1 
ATOM   2893 C CA    . THR B 1 131 ? 9.400   -8.471  -1.518  1.00 46.22  ? 103 THR B CA    1 
ATOM   2894 C C     . THR B 1 131 ? 10.885  -8.393  -1.843  1.00 45.11  ? 103 THR B C     1 
ATOM   2895 O O     . THR B 1 131 ? 11.383  -7.310  -2.167  1.00 48.98  ? 103 THR B O     1 
ATOM   2896 C CB    . THR B 1 131 ? 9.197   -8.951  -0.074  1.00 47.69  ? 103 THR B CB    1 
ATOM   2897 O OG1   . THR B 1 131 ? 7.810   -8.859  0.275   1.00 56.04  ? 103 THR B OG1   1 
ATOM   2898 C CG2   . THR B 1 131 ? 10.016  -8.104  0.891   1.00 41.75  ? 103 THR B CG2   1 
ATOM   2899 N N     . ILE B 1 132 ? 11.608  -9.507  -1.772  1.00 45.18  ? 104 ILE B N     1 
ATOM   2900 C CA    . ILE B 1 132 ? 13.059  -9.517  -1.921  1.00 37.19  ? 104 ILE B CA    1 
ATOM   2901 C C     . ILE B 1 132 ? 13.422  -9.945  -3.335  1.00 36.40  ? 104 ILE B C     1 
ATOM   2902 O O     . ILE B 1 132 ? 12.840  -10.890 -3.883  1.00 37.03  ? 104 ILE B O     1 
ATOM   2903 C CB    . ILE B 1 132 ? 13.715  -10.447 -0.883  1.00 35.85  ? 104 ILE B CB    1 
ATOM   2904 C CG1   . ILE B 1 132 ? 13.275  -10.069 0.530   1.00 38.92  ? 104 ILE B CG1   1 
ATOM   2905 C CG2   . ILE B 1 132 ? 15.228  -10.381 -0.990  1.00 36.28  ? 104 ILE B CG2   1 
ATOM   2906 C CD1   . ILE B 1 132 ? 13.817  -10.994 1.595   1.00 40.17  ? 104 ILE B CD1   1 
ATOM   2907 N N     . THR B 1 133 ? 14.384  -9.242  -3.928  1.00 36.51  ? 105 THR B N     1 
ATOM   2908 C CA    . THR B 1 133 ? 14.985  -9.620  -5.198  1.00 37.43  ? 105 THR B CA    1 
ATOM   2909 C C     . THR B 1 133 ? 16.497  -9.649  -5.028  1.00 37.85  ? 105 THR B C     1 
ATOM   2910 O O     . THR B 1 133 ? 17.071  -8.774  -4.373  1.00 37.30  ? 105 THR B O     1 
ATOM   2911 C CB    . THR B 1 133 ? 14.599  -8.648  -6.322  1.00 37.30  ? 105 THR B CB    1 
ATOM   2912 O OG1   . THR B 1 133 ? 15.170  -7.360  -6.061  1.00 37.60  ? 105 THR B OG1   1 
ATOM   2913 C CG2   . THR B 1 133 ? 13.086  -8.517  -6.425  1.00 36.89  ? 105 THR B CG2   1 
ATOM   2914 N N     . TYR B 1 134 ? 17.138  -10.657 -5.612  1.00 38.91  ? 106 TYR B N     1 
ATOM   2915 C CA    . TYR B 1 134 ? 18.572  -10.859 -5.470  1.00 39.50  ? 106 TYR B CA    1 
ATOM   2916 C C     . TYR B 1 134 ? 19.276  -10.584 -6.792  1.00 40.24  ? 106 TYR B C     1 
ATOM   2917 O O     . TYR B 1 134 ? 18.815  -11.018 -7.853  1.00 40.83  ? 106 TYR B O     1 
ATOM   2918 C CB    . TYR B 1 134 ? 18.877  -12.278 -4.988  1.00 40.27  ? 106 TYR B CB    1 
ATOM   2919 C CG    . TYR B 1 134 ? 18.318  -12.572 -3.614  1.00 39.64  ? 106 TYR B CG    1 
ATOM   2920 C CD1   . TYR B 1 134 ? 18.940  -12.086 -2.472  1.00 39.14  ? 106 TYR B CD1   1 
ATOM   2921 C CD2   . TYR B 1 134 ? 17.168  -13.333 -3.459  1.00 39.63  ? 106 TYR B CD2   1 
ATOM   2922 C CE1   . TYR B 1 134 ? 18.434  -12.351 -1.215  1.00 38.64  ? 106 TYR B CE1   1 
ATOM   2923 C CE2   . TYR B 1 134 ? 16.654  -13.603 -2.205  1.00 39.13  ? 106 TYR B CE2   1 
ATOM   2924 C CZ    . TYR B 1 134 ? 17.291  -13.111 -1.087  1.00 38.63  ? 106 TYR B CZ    1 
ATOM   2925 O OH    . TYR B 1 134 ? 16.783  -13.375 0.164   1.00 38.19  ? 106 TYR B OH    1 
ATOM   2926 N N     . GLU B 1 135 ? 20.394  -9.860  -6.723  1.00 40.28  ? 107 GLU B N     1 
ATOM   2927 C CA    . GLU B 1 135 ? 21.090  -9.395  -7.914  1.00 40.92  ? 107 GLU B CA    1 
ATOM   2928 C C     . GLU B 1 135 ? 22.589  -9.614  -7.762  1.00 41.71  ? 107 GLU B C     1 
ATOM   2929 O O     . GLU B 1 135 ? 23.086  -9.986  -6.695  1.00 41.66  ? 107 GLU B O     1 
ATOM   2930 C CB    . GLU B 1 135 ? 20.820  -7.908  -8.181  1.00 40.13  ? 107 GLU B CB    1 
ATOM   2931 C CG    . GLU B 1 135 ? 19.369  -7.468  -8.038  1.00 39.19  ? 107 GLU B CG    1 
ATOM   2932 C CD    . GLU B 1 135 ? 18.444  -8.097  -9.063  1.00 39.66  ? 107 GLU B CD    1 
ATOM   2933 O OE1   . GLU B 1 135 ? 18.940  -8.742  -10.012 1.00 40.72  ? 107 GLU B OE1   1 
ATOM   2934 O OE2   . GLU B 1 135 ? 17.212  -7.942  -8.919  1.00 39.04  ? 107 GLU B OE2   1 
ATOM   2935 N N     . LEU B 1 136 ? 23.308  -9.372  -8.855  1.00 42.50  ? 108 LEU B N     1 
ATOM   2936 C CA    . LEU B 1 136 ? 24.764  -9.338  -8.868  1.00 43.30  ? 108 LEU B CA    1 
ATOM   2937 C C     . LEU B 1 136 ? 25.227  -7.889  -8.900  1.00 42.82  ? 108 LEU B C     1 
ATOM   2938 O O     . LEU B 1 136 ? 24.721  -7.091  -9.697  1.00 42.53  ? 108 LEU B O     1 
ATOM   2939 C CB    . LEU B 1 136 ? 25.323  -10.085 -10.079 1.00 44.70  ? 108 LEU B CB    1 
ATOM   2940 C CG    . LEU B 1 136 ? 25.484  -11.601 -9.992  1.00 45.65  ? 108 LEU B CG    1 
ATOM   2941 C CD1   . LEU B 1 136 ? 25.766  -12.179 -11.367 1.00 46.97  ? 108 LEU B CD1   1 
ATOM   2942 C CD2   . LEU B 1 136 ? 26.609  -11.944 -9.033  1.00 46.03  ? 108 LEU B CD2   1 
ATOM   2943 N N     . LEU B 1 137 ? 26.186  -7.550  -8.041  1.00 42.81  ? 109 LEU B N     1 
ATOM   2944 C CA    . LEU B 1 137 ? 26.723  -6.197  -8.025  1.00 42.49  ? 109 LEU B CA    1 
ATOM   2945 C C     . LEU B 1 137 ? 28.038  -6.172  -7.264  1.00 43.00  ? 109 LEU B C     1 
ATOM   2946 O O     . LEU B 1 137 ? 28.158  -6.780  -6.198  1.00 42.89  ? 109 LEU B O     1 
ATOM   2947 C CB    . LEU B 1 137 ? 25.738  -5.205  -7.393  1.00 41.13  ? 109 LEU B CB    1 
ATOM   2948 C CG    . LEU B 1 137 ? 26.230  -3.757  -7.328  1.00 40.81  ? 109 LEU B CG    1 
ATOM   2949 C CD1   . LEU B 1 137 ? 26.299  -3.155  -8.722  1.00 41.27  ? 109 LEU B CD1   1 
ATOM   2950 C CD2   . LEU B 1 137 ? 25.345  -2.921  -6.421  1.00 39.54  ? 109 LEU B CD2   1 
ATOM   2951 N N     . ASP B 1 138 ? 29.017  -5.472  -7.827  1.00 43.63  ? 110 ASP B N     1 
ATOM   2952 C CA    . ASP B 1 138 ? 30.240  -5.112  -7.126  1.00 44.05  ? 110 ASP B CA    1 
ATOM   2953 C C     . ASP B 1 138 ? 30.086  -3.677  -6.641  1.00 43.15  ? 110 ASP B C     1 
ATOM   2954 O O     . ASP B 1 138 ? 29.785  -2.781  -7.435  1.00 44.34  ? 110 ASP B O     1 
ATOM   2955 C CB    . ASP B 1 138 ? 31.458  -5.250  -8.043  1.00 45.47  ? 110 ASP B CB    1 
ATOM   2956 C CG    . ASP B 1 138 ? 32.776  -5.045  -7.314  1.00 46.11  ? 110 ASP B CG    1 
ATOM   2957 O OD1   . ASP B 1 138 ? 32.761  -4.696  -6.115  1.00 45.44  ? 110 ASP B OD1   1 
ATOM   2958 O OD2   . ASP B 1 138 ? 33.837  -5.237  -7.945  1.00 47.37  ? 110 ASP B OD2   1 
ATOM   2959 N N     . VAL B 1 139 ? 30.280  -3.463  -5.336  1.00 42.68  ? 111 VAL B N     1 
ATOM   2960 C CA    . VAL B 1 139 ? 30.030  -2.152  -4.747  1.00 41.80  ? 111 VAL B CA    1 
ATOM   2961 C C     . VAL B 1 139 ? 30.952  -1.086  -5.325  1.00 42.39  ? 111 VAL B C     1 
ATOM   2962 O O     . VAL B 1 139 ? 30.643  0.108   -5.248  1.00 41.78  ? 111 VAL B O     1 
ATOM   2963 C CB    . VAL B 1 139 ? 30.158  -2.228  -3.209  1.00 41.38  ? 111 VAL B CB    1 
ATOM   2964 C CG1   . VAL B 1 139 ? 31.614  -2.380  -2.798  1.00 42.44  ? 111 VAL B CG1   1 
ATOM   2965 C CG2   . VAL B 1 139 ? 29.522  -1.011  -2.548  1.00 40.31  ? 111 VAL B CG2   1 
ATOM   2966 N N     . VAL B 1 140 ? 32.076  -1.486  -5.916  1.00 43.64  ? 112 VAL B N     1 
ATOM   2967 C CA    . VAL B 1 140 ? 32.995  -0.542  -6.541  1.00 44.37  ? 112 VAL B CA    1 
ATOM   2968 C C     . VAL B 1 140 ? 32.988  -0.759  -8.048  1.00 45.07  ? 112 VAL B C     1 
ATOM   2969 O O     . VAL B 1 140 ? 34.042  -0.760  -8.692  1.00 48.62  ? 112 VAL B O     1 
ATOM   2970 C CB    . VAL B 1 140 ? 34.414  -0.680  -5.963  1.00 45.40  ? 112 VAL B CB    1 
ATOM   2971 C CG1   . VAL B 1 140 ? 34.491  -0.017  -4.601  1.00 44.78  ? 112 VAL B CG1   1 
ATOM   2972 C CG2   . VAL B 1 140 ? 34.808  -2.146  -5.866  1.00 46.17  ? 112 VAL B CG2   1 
ATOM   2973 N N     . GLU B 1 141 ? 31.801  -0.939  -8.615  1.00 49.93  ? 113 GLU B N     1 
ATOM   2974 C CA    . GLU B 1 141 ? 31.687  -1.175  -10.049 1.00 50.80  ? 113 GLU B CA    1 
ATOM   2975 C C     . GLU B 1 141 ? 32.033  0.095   -10.817 1.00 50.96  ? 113 GLU B C     1 
ATOM   2976 O O     . GLU B 1 141 ? 31.504  1.167   -10.499 1.00 49.99  ? 113 GLU B O     1 
ATOM   2977 C CB    . GLU B 1 141 ? 30.275  -1.637  -10.405 1.00 49.84  ? 113 GLU B CB    1 
ATOM   2978 C CG    . GLU B 1 141 ? 30.212  -3.031  -11.008 1.00 54.45  ? 113 GLU B CG    1 
ATOM   2979 C CD    . GLU B 1 141 ? 30.484  -3.034  -12.501 1.00 61.16  ? 113 GLU B CD    1 
ATOM   2980 O OE1   . GLU B 1 141 ? 30.505  -1.941  -13.106 1.00 53.22  ? 113 GLU B OE1   1 
ATOM   2981 O OE2   . GLU B 1 141 ? 30.678  -4.130  -13.070 1.00 79.61  ? 113 GLU B OE2   1 
ATOM   2982 N N     . PRO B 1 142 ? 32.919  0.022   -11.815 1.00 54.52  ? 114 PRO B N     1 
ATOM   2983 C CA    . PRO B 1 142 ? 33.208  1.226   -12.616 1.00 46.94  ? 114 PRO B CA    1 
ATOM   2984 C C     . PRO B 1 142 ? 31.976  1.796   -13.298 1.00 46.16  ? 114 PRO B C     1 
ATOM   2985 O O     . PRO B 1 142 ? 31.691  2.993   -13.167 1.00 45.56  ? 114 PRO B O     1 
ATOM   2986 C CB    . PRO B 1 142 ? 34.248  0.722   -13.626 1.00 48.54  ? 114 PRO B CB    1 
ATOM   2987 C CG    . PRO B 1 142 ? 34.905  -0.431  -12.942 1.00 49.07  ? 114 PRO B CG    1 
ATOM   2988 C CD    . PRO B 1 142 ? 33.817  -1.096  -12.147 1.00 55.48  ? 114 PRO B CD    1 
ATOM   2989 N N     . ARG B 1 143 ? 31.229  0.963   -14.022 1.00 50.05  ? 115 ARG B N     1 
ATOM   2990 C CA    . ARG B 1 143 ? 30.004  1.394   -14.692 1.00 45.56  ? 115 ARG B CA    1 
ATOM   2991 C C     . ARG B 1 143 ? 28.812  0.941   -13.854 1.00 44.32  ? 115 ARG B C     1 
ATOM   2992 O O     . ARG B 1 143 ? 28.124  -0.032  -14.165 1.00 44.33  ? 115 ARG B O     1 
ATOM   2993 C CB    . ARG B 1 143 ? 29.944  0.846   -16.113 1.00 46.56  ? 115 ARG B CB    1 
ATOM   2994 C CG    . ARG B 1 143 ? 31.294  0.752   -16.796 1.00 48.05  ? 115 ARG B CG    1 
ATOM   2995 C CD    . ARG B 1 143 ? 31.129  0.339   -18.241 1.00 49.03  ? 115 ARG B CD    1 
ATOM   2996 N NE    . ARG B 1 143 ? 30.202  1.232   -18.925 1.00 48.53  ? 115 ARG B NE    1 
ATOM   2997 C CZ    . ARG B 1 143 ? 30.565  2.306   -19.613 1.00 50.53  ? 115 ARG B CZ    1 
ATOM   2998 N NH1   . ARG B 1 143 ? 31.837  2.650   -19.739 1.00 56.54  ? 115 ARG B NH1   1 
ATOM   2999 N NH2   . ARG B 1 143 ? 29.628  3.056   -20.183 1.00 48.51  ? 115 ARG B NH2   1 
ATOM   3000 N N     . LEU B 1 144 ? 28.576  1.675   -12.765 1.00 46.52  ? 116 LEU B N     1 
ATOM   3001 C CA    . LEU B 1 144 ? 27.452  1.368   -11.887 1.00 42.84  ? 116 LEU B CA    1 
ATOM   3002 C C     . LEU B 1 144 ? 26.129  1.503   -12.629 1.00 41.67  ? 116 LEU B C     1 
ATOM   3003 O O     . LEU B 1 144 ? 25.226  0.675   -12.464 1.00 41.26  ? 116 LEU B O     1 
ATOM   3004 C CB    . LEU B 1 144 ? 27.482  2.295   -10.669 1.00 42.08  ? 116 LEU B CB    1 
ATOM   3005 C CG    . LEU B 1 144 ? 26.861  1.892   -9.325  1.00 40.33  ? 116 LEU B CG    1 
ATOM   3006 C CD1   . LEU B 1 144 ? 27.066  3.012   -8.318  1.00 39.93  ? 116 LEU B CD1   1 
ATOM   3007 C CD2   . LEU B 1 144 ? 25.386  1.542   -9.417  1.00 39.53  ? 116 LEU B CD2   1 
ATOM   3008 N N     . GLU B 1 145 ? 26.007  2.532   -13.470 1.00 41.80  ? 117 GLU B N     1 
ATOM   3009 C CA    . GLU B 1 145 ? 24.739  2.861   -14.106 1.00 41.32  ? 117 GLU B CA    1 
ATOM   3010 C C     . GLU B 1 145 ? 24.244  1.773   -15.050 1.00 41.90  ? 117 GLU B C     1 
ATOM   3011 O O     . GLU B 1 145 ? 23.067  1.792   -15.426 1.00 41.48  ? 117 GLU B O     1 
ATOM   3012 C CB    . GLU B 1 145 ? 24.879  4.182   -14.862 1.00 41.56  ? 117 GLU B CB    1 
ATOM   3013 C CG    . GLU B 1 145 ? 24.680  5.412   -13.992 1.00 40.68  ? 117 GLU B CG    1 
ATOM   3014 C CD    . GLU B 1 145 ? 25.971  5.870   -13.337 1.00 48.06  ? 117 GLU B CD    1 
ATOM   3015 O OE1   . GLU B 1 145 ? 27.042  5.720   -13.966 1.00 53.97  ? 117 GLU B OE1   1 
ATOM   3016 O OE2   . GLU B 1 145 ? 25.918  6.378   -12.198 1.00 49.30  ? 117 GLU B OE2   1 
ATOM   3017 N N     . ASP B 1 146 ? 25.099  0.827   -15.434 1.00 42.91  ? 118 ASP B N     1 
ATOM   3018 C CA    . ASP B 1 146 ? 24.734  -0.228  -16.367 1.00 43.64  ? 118 ASP B CA    1 
ATOM   3019 C C     . ASP B 1 146 ? 24.286  -1.506  -15.668 1.00 43.38  ? 118 ASP B C     1 
ATOM   3020 O O     . ASP B 1 146 ? 24.064  -2.520  -16.338 1.00 44.09  ? 118 ASP B O     1 
ATOM   3021 C CB    . ASP B 1 146 ? 25.905  -0.526  -17.305 1.00 45.07  ? 118 ASP B CB    1 
ATOM   3022 C CG    . ASP B 1 146 ? 26.279  0.667   -18.167 1.00 45.50  ? 118 ASP B CG    1 
ATOM   3023 O OD1   . ASP B 1 146 ? 26.566  1.744   -17.603 1.00 44.97  ? 118 ASP B OD1   1 
ATOM   3024 O OD2   . ASP B 1 146 ? 26.285  0.528   -19.407 1.00 46.44  ? 118 ASP B OD2   1 
ATOM   3025 N N     . THR B 1 147 ? 24.142  -1.483  -14.348 1.00 42.45  ? 119 THR B N     1 
ATOM   3026 C CA    . THR B 1 147 ? 23.754  -2.658  -13.584 1.00 42.22  ? 119 THR B CA    1 
ATOM   3027 C C     . THR B 1 147 ? 22.253  -2.664  -13.321 1.00 41.27  ? 119 THR B C     1 
ATOM   3028 O O     . THR B 1 147 ? 21.585  -1.627  -13.346 1.00 40.55  ? 119 THR B O     1 
ATOM   3029 C CB    . THR B 1 147 ? 24.511  -2.722  -12.254 1.00 41.88  ? 119 THR B CB    1 
ATOM   3030 O OG1   . THR B 1 147 ? 24.112  -1.626  -11.422 1.00 40.78  ? 119 THR B OG1   1 
ATOM   3031 C CG2   . THR B 1 147 ? 26.012  -2.654  -12.490 1.00 44.61  ? 119 THR B CG2   1 
ATOM   3032 N N     . VAL B 1 148 ? 21.727  -3.865  -13.069 1.00 41.35  ? 120 VAL B N     1 
ATOM   3033 C CA    . VAL B 1 148 ? 20.309  -4.012  -12.752 1.00 40.56  ? 120 VAL B CA    1 
ATOM   3034 C C     . VAL B 1 148 ? 19.978  -3.309  -11.442 1.00 39.36  ? 120 VAL B C     1 
ATOM   3035 O O     . VAL B 1 148 ? 18.889  -2.741  -11.288 1.00 38.58  ? 120 VAL B O     1 
ATOM   3036 C CB    . VAL B 1 148 ? 19.933  -5.508  -12.709 1.00 41.04  ? 120 VAL B CB    1 
ATOM   3037 C CG1   . VAL B 1 148 ? 18.549  -5.706  -12.122 1.00 40.21  ? 120 VAL B CG1   1 
ATOM   3038 C CG2   . VAL B 1 148 ? 20.014  -6.120  -14.098 1.00 42.23  ? 120 VAL B CG2   1 
ATOM   3039 N N     . VAL B 1 149 ? 20.914  -3.313  -10.490 1.00 39.26  ? 121 VAL B N     1 
ATOM   3040 C CA    . VAL B 1 149 ? 20.663  -2.706  -9.185  1.00 38.23  ? 121 VAL B CA    1 
ATOM   3041 C C     . VAL B 1 149 ? 20.460  -1.203  -9.319  1.00 37.66  ? 121 VAL B C     1 
ATOM   3042 O O     . VAL B 1 149 ? 19.580  -0.621  -8.671  1.00 38.45  ? 121 VAL B O     1 
ATOM   3043 C CB    . VAL B 1 149 ? 21.812  -3.036  -8.213  1.00 38.43  ? 121 VAL B CB    1 
ATOM   3044 C CG1   . VAL B 1 149 ? 21.671  -2.240  -6.923  1.00 37.48  ? 121 VAL B CG1   1 
ATOM   3045 C CG2   . VAL B 1 149 ? 21.848  -4.522  -7.921  1.00 38.91  ? 121 VAL B CG2   1 
ATOM   3046 N N     . TRP B 1 150 ? 21.266  -0.548  -10.160 1.00 38.25  ? 122 TRP B N     1 
ATOM   3047 C CA    . TRP B 1 150 ? 21.171  0.903   -10.294 1.00 37.83  ? 122 TRP B CA    1 
ATOM   3048 C C     . TRP B 1 150 ? 19.803  1.326   -10.812 1.00 37.34  ? 122 TRP B C     1 
ATOM   3049 O O     . TRP B 1 150 ? 19.257  2.348   -10.381 1.00 37.74  ? 122 TRP B O     1 
ATOM   3050 C CB    . TRP B 1 150 ? 22.269  1.424   -11.221 1.00 38.71  ? 122 TRP B CB    1 
ATOM   3051 C CG    . TRP B 1 150 ? 22.038  2.838   -11.671 1.00 38.47  ? 122 TRP B CG    1 
ATOM   3052 C CD1   . TRP B 1 150 ? 21.530  3.246   -12.871 1.00 38.78  ? 122 TRP B CD1   1 
ATOM   3053 C CD2   . TRP B 1 150 ? 22.291  4.031   -10.918 1.00 38.94  ? 122 TRP B CD2   1 
ATOM   3054 N NE1   . TRP B 1 150 ? 21.459  4.617   -12.915 1.00 38.48  ? 122 TRP B NE1   1 
ATOM   3055 C CE2   . TRP B 1 150 ? 21.920  5.123   -11.728 1.00 37.97  ? 122 TRP B CE2   1 
ATOM   3056 C CE3   . TRP B 1 150 ? 22.800  4.282   -9.640  1.00 38.98  ? 122 TRP B CE3   1 
ATOM   3057 C CZ2   . TRP B 1 150 ? 22.042  6.444   -11.301 1.00 38.02  ? 122 TRP B CZ2   1 
ATOM   3058 C CZ3   . TRP B 1 150 ? 22.919  5.594   -9.218  1.00 38.00  ? 122 TRP B CZ3   1 
ATOM   3059 C CH2   . TRP B 1 150 ? 22.542  6.658   -10.046 1.00 39.10  ? 122 TRP B CH2   1 
ATOM   3060 N N     . ARG B 1 151 ? 19.233  0.554   -11.732 1.00 37.82  ? 123 ARG B N     1 
ATOM   3061 C CA    . ARG B 1 151 ? 17.967  0.922   -12.347 1.00 37.54  ? 123 ARG B CA    1 
ATOM   3062 C C     . ARG B 1 151 ? 16.760  0.446   -11.553 1.00 36.80  ? 123 ARG B C     1 
ATOM   3063 O O     . ARG B 1 151 ? 15.631  0.821   -11.887 1.00 36.50  ? 123 ARG B O     1 
ATOM   3064 C CB    . ARG B 1 151 ? 17.921  0.390   -13.779 1.00 38.53  ? 123 ARG B CB    1 
ATOM   3065 C CG    . ARG B 1 151 ? 19.039  0.981   -14.614 1.00 39.30  ? 123 ARG B CG    1 
ATOM   3066 C CD    . ARG B 1 151 ? 18.965  0.611   -16.072 1.00 40.33  ? 123 ARG B CD    1 
ATOM   3067 N NE    . ARG B 1 151 ? 20.158  1.078   -16.766 1.00 41.15  ? 123 ARG B NE    1 
ATOM   3068 C CZ    . ARG B 1 151 ? 20.451  0.791   -18.026 1.00 42.24  ? 123 ARG B CZ    1 
ATOM   3069 N NH1   . ARG B 1 151 ? 19.640  0.063   -18.773 1.00 44.66  ? 123 ARG B NH1   1 
ATOM   3070 N NH2   . ARG B 1 151 ? 21.585  1.250   -18.549 1.00 43.00  ? 123 ARG B NH2   1 
ATOM   3071 N N     . ASN B 1 152 ? 16.967  -0.366  -10.518 1.00 36.57  ? 124 ASN B N     1 
ATOM   3072 C CA    . ASN B 1 152 ? 15.934  -0.580  -9.517  1.00 35.77  ? 124 ASN B CA    1 
ATOM   3073 C C     . ASN B 1 152 ? 15.853  0.569   -8.524  1.00 36.16  ? 124 ASN B C     1 
ATOM   3074 O O     . ASN B 1 152 ? 14.882  0.646   -7.764  1.00 43.08  ? 124 ASN B O     1 
ATOM   3075 C CB    . ASN B 1 152 ? 16.180  -1.888  -8.761  1.00 37.42  ? 124 ASN B CB    1 
ATOM   3076 C CG    . ASN B 1 152 ? 15.859  -3.112  -9.592  1.00 43.70  ? 124 ASN B CG    1 
ATOM   3077 O OD1   . ASN B 1 152 ? 14.695  -3.478  -9.757  1.00 59.80  ? 124 ASN B OD1   1 
ATOM   3078 N ND2   . ASN B 1 152 ? 16.892  -3.758  -10.115 1.00 38.29  ? 124 ASN B ND2   1 
ATOM   3079 N N     . GLY B 1 153 ? 16.843  1.458   -8.517  1.00 37.16  ? 125 GLY B N     1 
ATOM   3080 C CA    . GLY B 1 153 ? 16.866  2.578   -7.611  1.00 36.88  ? 125 GLY B CA    1 
ATOM   3081 C C     . GLY B 1 153 ? 16.034  3.743   -8.108  1.00 39.87  ? 125 GLY B C     1 
ATOM   3082 O O     . GLY B 1 153 ? 15.261  3.621   -9.063  1.00 46.61  ? 125 GLY B O     1 
ATOM   3083 N N     . PRO B 1 154 ? 16.178  4.908   -7.462  1.00 36.76  ? 126 PRO B N     1 
ATOM   3084 C CA    . PRO B 1 154 ? 17.070  5.200   -6.333  1.00 34.13  ? 126 PRO B CA    1 
ATOM   3085 C C     . PRO B 1 154 ? 16.544  4.596   -5.037  1.00 36.56  ? 126 PRO B C     1 
ATOM   3086 O O     . PRO B 1 154 ? 15.353  4.322   -4.917  1.00 39.65  ? 126 PRO B O     1 
ATOM   3087 C CB    . PRO B 1 154 ? 17.085  6.730   -6.307  1.00 36.07  ? 126 PRO B CB    1 
ATOM   3088 C CG    . PRO B 1 154 ? 15.706  7.111   -6.768  1.00 39.64  ? 126 PRO B CG    1 
ATOM   3089 C CD    . PRO B 1 154 ? 15.294  6.049   -7.767  1.00 42.64  ? 126 PRO B CD    1 
ATOM   3090 N N     . PHE B 1 155 ? 17.407  4.369   -4.053  1.00 33.72  ? 127 PHE B N     1 
ATOM   3091 C CA    . PHE B 1 155 ? 17.041  3.638   -2.851  1.00 34.92  ? 127 PHE B CA    1 
ATOM   3092 C C     . PHE B 1 155 ? 16.913  4.585   -1.665  1.00 31.82  ? 127 PHE B C     1 
ATOM   3093 O O     . PHE B 1 155 ? 17.648  5.571   -1.551  1.00 35.39  ? 127 PHE B O     1 
ATOM   3094 C CB    . PHE B 1 155 ? 18.070  2.547   -2.539  1.00 34.98  ? 127 PHE B CB    1 
ATOM   3095 C CG    . PHE B 1 155 ? 18.141  1.469   -3.582  1.00 33.44  ? 127 PHE B CG    1 
ATOM   3096 C CD1   . PHE B 1 155 ? 17.280  0.384   -3.540  1.00 33.37  ? 127 PHE B CD1   1 
ATOM   3097 C CD2   . PHE B 1 155 ? 19.067  1.543   -4.607  1.00 34.17  ? 127 PHE B CD2   1 
ATOM   3098 C CE1   . PHE B 1 155 ? 17.344  -0.607  -4.503  1.00 34.04  ? 127 PHE B CE1   1 
ATOM   3099 C CE2   . PHE B 1 155 ? 19.137  0.557   -5.571  1.00 34.84  ? 127 PHE B CE2   1 
ATOM   3100 C CZ    . PHE B 1 155 ? 18.274  -0.519  -5.519  1.00 34.77  ? 127 PHE B CZ    1 
ATOM   3101 N N     . GLY B 1 156 ? 15.966  4.274   -0.784  1.00 31.17  ? 128 GLY B N     1 
ATOM   3102 C CA    . GLY B 1 156 ? 15.763  5.057   0.418   1.00 30.76  ? 128 GLY B CA    1 
ATOM   3103 C C     . GLY B 1 156 ? 16.819  4.780   1.467   1.00 31.06  ? 128 GLY B C     1 
ATOM   3104 O O     . GLY B 1 156 ? 17.462  5.704   1.970   1.00 36.51  ? 128 GLY B O     1 
ATOM   3105 N N     . LYS B 1 157 ? 17.005  3.506   1.805   1.00 31.89  ? 129 LYS B N     1 
ATOM   3106 C CA    . LYS B 1 157 ? 18.016  3.086   2.763   1.00 31.85  ? 129 LYS B CA    1 
ATOM   3107 C C     . LYS B 1 157 ? 18.909  2.031   2.128   1.00 33.51  ? 129 LYS B C     1 
ATOM   3108 O O     . LYS B 1 157 ? 18.472  1.260   1.268   1.00 34.40  ? 129 LYS B O     1 
ATOM   3109 C CB    . LYS B 1 157 ? 17.386  2.533   4.052   1.00 30.97  ? 129 LYS B CB    1 
ATOM   3110 C CG    . LYS B 1 157 ? 16.283  3.407   4.621   1.00 35.86  ? 129 LYS B CG    1 
ATOM   3111 C CD    . LYS B 1 157 ? 16.813  4.781   4.987   1.00 43.14  ? 129 LYS B CD    1 
ATOM   3112 C CE    . LYS B 1 157 ? 15.683  5.769   5.203   1.00 43.84  ? 129 LYS B CE    1 
ATOM   3113 N NZ    . LYS B 1 157 ? 15.782  6.941   4.289   1.00 39.44  ? 129 LYS B NZ    1 
ATOM   3114 N N     . VAL B 1 158 ? 20.169  2.007   2.555   1.00 34.97  ? 130 VAL B N     1 
ATOM   3115 C CA    . VAL B 1 158 ? 21.160  1.060   2.056   1.00 33.34  ? 130 VAL B CA    1 
ATOM   3116 C C     . VAL B 1 158 ? 21.871  0.455   3.258   1.00 33.62  ? 130 VAL B C     1 
ATOM   3117 O O     . VAL B 1 158 ? 22.568  1.164   3.995   1.00 33.72  ? 130 VAL B O     1 
ATOM   3118 C CB    . VAL B 1 158 ? 22.165  1.717   1.100   1.00 33.93  ? 130 VAL B CB    1 
ATOM   3119 C CG1   . VAL B 1 158 ? 23.344  0.790   0.857   1.00 34.84  ? 130 VAL B CG1   1 
ATOM   3120 C CG2   . VAL B 1 158 ? 21.490  2.066   -0.215  1.00 33.82  ? 130 VAL B CG2   1 
ATOM   3121 N N     . PHE B 1 159 ? 21.695  -0.848  3.460   1.00 33.83  ? 131 PHE B N     1 
ATOM   3122 C CA    . PHE B 1 159 ? 22.375  -1.568  4.527   1.00 34.22  ? 131 PHE B CA    1 
ATOM   3123 C C     . PHE B 1 159 ? 23.648  -2.205  3.987   1.00 37.18  ? 131 PHE B C     1 
ATOM   3124 O O     . PHE B 1 159 ? 23.624  -2.882  2.954   1.00 42.56  ? 131 PHE B O     1 
ATOM   3125 C CB    . PHE B 1 159 ? 21.461  -2.635  5.131   1.00 33.97  ? 131 PHE B CB    1 
ATOM   3126 C CG    . PHE B 1 159 ? 20.211  -2.083  5.752   1.00 33.09  ? 131 PHE B CG    1 
ATOM   3127 C CD1   . PHE B 1 159 ? 20.200  -1.683  7.077   1.00 35.48  ? 131 PHE B CD1   1 
ATOM   3128 C CD2   . PHE B 1 159 ? 19.048  -1.960  5.011   1.00 32.81  ? 131 PHE B CD2   1 
ATOM   3129 C CE1   . PHE B 1 159 ? 19.051  -1.173  7.654   1.00 37.19  ? 131 PHE B CE1   1 
ATOM   3130 C CE2   . PHE B 1 159 ? 17.896  -1.450  5.583   1.00 32.00  ? 131 PHE B CE2   1 
ATOM   3131 C CZ    . PHE B 1 159 ? 17.898  -1.057  6.905   1.00 36.18  ? 131 PHE B CZ    1 
ATOM   3132 N N     . CYS B 1 160 ? 24.758  -1.981  4.687   1.00 37.11  ? 132 CYS B N     1 
ATOM   3133 C CA    . CYS B 1 160 ? 26.069  -2.496  4.297   1.00 38.15  ? 132 CYS B CA    1 
ATOM   3134 C C     . CYS B 1 160 ? 26.681  -3.152  5.530   1.00 38.63  ? 132 CYS B C     1 
ATOM   3135 O O     . CYS B 1 160 ? 27.251  -2.469  6.386   1.00 42.32  ? 132 CYS B O     1 
ATOM   3136 C CB    . CYS B 1 160 ? 26.951  -1.377  3.750   1.00 38.50  ? 132 CYS B CB    1 
ATOM   3137 S SG    . CYS B 1 160 ? 28.708  -1.767  3.650   1.00 47.59  ? 132 CYS B SG    1 
ATOM   3138 N N     . MET B 1 161 ? 26.558  -4.474  5.623   1.00 38.65  ? 133 MET B N     1 
ATOM   3139 C CA    . MET B 1 161 ? 26.928  -5.219  6.820   1.00 40.48  ? 133 MET B CA    1 
ATOM   3140 C C     . MET B 1 161 ? 28.119  -6.120  6.522   1.00 42.17  ? 133 MET B C     1 
ATOM   3141 O O     . MET B 1 161 ? 28.024  -7.017  5.677   1.00 46.90  ? 133 MET B O     1 
ATOM   3142 C CB    . MET B 1 161 ? 25.750  -6.052  7.327   1.00 40.73  ? 133 MET B CB    1 
ATOM   3143 C CG    . MET B 1 161 ? 24.396  -5.377  7.181   1.00 40.16  ? 133 MET B CG    1 
ATOM   3144 S SD    . MET B 1 161 ? 24.024  -4.261  8.545   1.00 42.07  ? 133 MET B SD    1 
ATOM   3145 C CE    . MET B 1 161 ? 24.325  -5.331  9.949   1.00 46.30  ? 133 MET B CE    1 
ATOM   3146 N N     . LEU B 1 162 ? 29.230  -5.878  7.219   1.00 39.75  ? 134 LEU B N     1 
ATOM   3147 C CA    . LEU B 1 162 ? 30.400  -6.757  7.222   1.00 40.99  ? 134 LEU B CA    1 
ATOM   3148 C C     . LEU B 1 162 ? 30.876  -7.063  5.799   1.00 41.65  ? 134 LEU B C     1 
ATOM   3149 O O     . LEU B 1 162 ? 30.846  -8.200  5.331   1.00 42.19  ? 134 LEU B O     1 
ATOM   3150 C CB    . LEU B 1 162 ? 30.094  -8.053  7.978   1.00 41.23  ? 134 LEU B CB    1 
ATOM   3151 C CG    . LEU B 1 162 ? 29.401  -7.931  9.336   1.00 40.56  ? 134 LEU B CG    1 
ATOM   3152 C CD1   . LEU B 1 162 ? 28.970  -9.298  9.837   1.00 40.83  ? 134 LEU B CD1   1 
ATOM   3153 C CD2   . LEU B 1 162 ? 30.317  -7.258  10.343  1.00 40.95  ? 134 LEU B CD2   1 
ATOM   3154 N N     . MET B 1 163 ? 31.331  -6.012  5.119   1.00 45.47  ? 135 MET B N     1 
ATOM   3155 C CA    . MET B 1 163 ? 31.763  -6.188  3.738   1.00 43.87  ? 135 MET B CA    1 
ATOM   3156 C C     . MET B 1 163 ? 32.782  -5.141  3.304   1.00 43.32  ? 135 MET B C     1 
ATOM   3157 O O     . MET B 1 163 ? 33.593  -5.404  2.411   1.00 46.27  ? 135 MET B O     1 
ATOM   3158 C CB    . MET B 1 163 ? 30.544  -6.191  2.808   1.00 41.53  ? 135 MET B CB    1 
ATOM   3159 C CG    . MET B 1 163 ? 29.956  -4.829  2.478   1.00 40.68  ? 135 MET B CG    1 
ATOM   3160 S SD    . MET B 1 163 ? 30.746  -4.017  1.078   1.00 46.64  ? 135 MET B SD    1 
ATOM   3161 C CE    . MET B 1 163 ? 30.287  -5.133  -0.242  1.00 42.84  ? 135 MET B CE    1 
ATOM   3162 N N     . LEU B 1 164 ? 32.759  -3.955  3.918   1.00 42.29  ? 136 LEU B N     1 
ATOM   3163 C CA    . LEU B 1 164 ? 33.723  -2.927  3.540   1.00 42.85  ? 136 LEU B CA    1 
ATOM   3164 C C     . LEU B 1 164 ? 35.150  -3.298  3.922   1.00 46.91  ? 136 LEU B C     1 
ATOM   3165 O O     . LEU B 1 164 ? 36.093  -2.692  3.401   1.00 51.79  ? 136 LEU B O     1 
ATOM   3166 C CB    . LEU B 1 164 ? 33.350  -1.582  4.160   1.00 42.03  ? 136 LEU B CB    1 
ATOM   3167 C CG    . LEU B 1 164 ? 32.180  -0.874  3.479   1.00 40.95  ? 136 LEU B CG    1 
ATOM   3168 C CD1   . LEU B 1 164 ? 31.763  0.355   4.261   1.00 42.59  ? 136 LEU B CD1   1 
ATOM   3169 C CD2   . LEU B 1 164 ? 32.551  -0.504  2.053   1.00 41.41  ? 136 LEU B CD2   1 
ATOM   3170 N N     . HIS B 1 165 ? 35.330  -4.271  4.814   1.00 48.08  ? 137 HIS B N     1 
ATOM   3171 C CA    . HIS B 1 165 ? 36.658  -4.791  5.108   1.00 47.87  ? 137 HIS B CA    1 
ATOM   3172 C C     . HIS B 1 165 ? 37.189  -5.696  4.004   1.00 49.10  ? 137 HIS B C     1 
ATOM   3173 O O     . HIS B 1 165 ? 38.371  -6.054  4.032   1.00 53.16  ? 137 HIS B O     1 
ATOM   3174 C CB    . HIS B 1 165 ? 36.640  -5.536  6.445   1.00 46.05  ? 137 HIS B CB    1 
ATOM   3175 C CG    . HIS B 1 165 ? 35.788  -6.767  6.442   1.00 45.71  ? 137 HIS B CG    1 
ATOM   3176 N ND1   . HIS B 1 165 ? 36.314  -8.037  6.353   1.00 46.75  ? 137 HIS B ND1   1 
ATOM   3177 C CD2   . HIS B 1 165 ? 34.444  -6.920  6.511   1.00 46.58  ? 137 HIS B CD2   1 
ATOM   3178 C CE1   . HIS B 1 165 ? 35.332  -8.921  6.379   1.00 47.15  ? 137 HIS B CE1   1 
ATOM   3179 N NE2   . HIS B 1 165 ? 34.187  -8.269  6.469   1.00 51.92  ? 137 HIS B NE2   1 
ATOM   3180 N N     . LEU B 1 166 ? 36.347  -6.067  3.039   1.00 46.45  ? 138 LEU B N     1 
ATOM   3181 C CA    . LEU B 1 166 ? 36.768  -6.801  1.853   1.00 50.44  ? 138 LEU B CA    1 
ATOM   3182 C C     . LEU B 1 166 ? 37.008  -5.902  0.648   1.00 53.18  ? 138 LEU B C     1 
ATOM   3183 O O     . LEU B 1 166 ? 37.526  -6.379  -0.367  1.00 59.29  ? 138 LEU B O     1 
ATOM   3184 C CB    . LEU B 1 166 ? 35.722  -7.865  1.490   1.00 55.09  ? 138 LEU B CB    1 
ATOM   3185 C CG    . LEU B 1 166 ? 36.022  -9.319  1.864   1.00 58.65  ? 138 LEU B CG    1 
ATOM   3186 C CD1   . LEU B 1 166 ? 36.456  -9.437  3.307   1.00 62.92  ? 138 LEU B CD1   1 
ATOM   3187 C CD2   . LEU B 1 166 ? 34.810  -10.198 1.601   1.00 54.11  ? 138 LEU B CD2   1 
ATOM   3188 N N     . VAL B 1 167 ? 36.651  -4.624  0.732   1.00 49.09  ? 139 VAL B N     1 
ATOM   3189 C CA    . VAL B 1 167 ? 36.778  -3.690  -0.384  1.00 51.39  ? 139 VAL B CA    1 
ATOM   3190 C C     . VAL B 1 167 ? 37.992  -2.809  -0.118  1.00 53.75  ? 139 VAL B C     1 
ATOM   3191 O O     . VAL B 1 167 ? 37.938  -1.949  0.780   1.00 53.72  ? 139 VAL B O     1 
ATOM   3192 C CB    . VAL B 1 167 ? 35.507  -2.850  -0.559  1.00 49.09  ? 139 VAL B CB    1 
ATOM   3193 C CG1   . VAL B 1 167 ? 35.645  -1.933  -1.759  1.00 52.09  ? 139 VAL B CG1   1 
ATOM   3194 C CG2   . VAL B 1 167 ? 34.294  -3.755  -0.705  1.00 46.39  ? 139 VAL B CG2   1 
ATOM   3195 N N     . PRO B 1 168 ? 39.100  -2.979  -0.848  1.00 50.95  ? 140 PRO B N     1 
ATOM   3196 C CA    . PRO B 1 168 ? 40.276  -2.126  -0.604  1.00 49.84  ? 140 PRO B CA    1 
ATOM   3197 C C     . PRO B 1 168 ? 40.008  -0.646  -0.816  1.00 50.08  ? 140 PRO B C     1 
ATOM   3198 O O     . PRO B 1 168 ? 40.490  0.184   -0.036  1.00 51.45  ? 140 PRO B O     1 
ATOM   3199 C CB    . PRO B 1 168 ? 41.301  -2.668  -1.609  1.00 55.03  ? 140 PRO B CB    1 
ATOM   3200 C CG    . PRO B 1 168 ? 40.909  -4.098  -1.786  1.00 57.74  ? 140 PRO B CG    1 
ATOM   3201 C CD    . PRO B 1 168 ? 39.406  -4.080  -1.778  1.00 52.59  ? 140 PRO B CD    1 
ATOM   3202 N N     . ASP B 1 169 ? 39.254  -0.291  -1.855  1.00 52.31  ? 141 ASP B N     1 
ATOM   3203 C CA    . ASP B 1 169 ? 38.946  1.107   -2.154  1.00 51.74  ? 141 ASP B CA    1 
ATOM   3204 C C     . ASP B 1 169 ? 37.633  1.452   -1.463  1.00 50.15  ? 141 ASP B C     1 
ATOM   3205 O O     . ASP B 1 169 ? 36.550  1.328   -2.037  1.00 50.11  ? 141 ASP B O     1 
ATOM   3206 C CB    . ASP B 1 169 ? 38.872  1.334   -3.659  1.00 56.89  ? 141 ASP B CB    1 
ATOM   3207 C CG    . ASP B 1 169 ? 38.915  2.805   -4.034  1.00 65.97  ? 141 ASP B CG    1 
ATOM   3208 O OD1   . ASP B 1 169 ? 38.653  3.658   -3.159  1.00 63.87  ? 141 ASP B OD1   1 
ATOM   3209 O OD2   . ASP B 1 169 ? 39.209  3.108   -5.210  1.00 68.09  ? 141 ASP B OD2   1 
ATOM   3210 N N     . ASN B 1 170 ? 37.732  1.905   -0.213  1.00 54.03  ? 142 ASN B N     1 
ATOM   3211 C CA    . ASN B 1 170 ? 36.536  2.157   0.583   1.00 50.26  ? 142 ASN B CA    1 
ATOM   3212 C C     . ASN B 1 170 ? 35.851  3.467   0.214   1.00 44.36  ? 142 ASN B C     1 
ATOM   3213 O O     . ASN B 1 170 ? 34.626  3.570   0.336   1.00 43.94  ? 142 ASN B O     1 
ATOM   3214 C CB    . ASN B 1 170 ? 36.885  2.144   2.072   1.00 48.85  ? 142 ASN B CB    1 
ATOM   3215 C CG    . ASN B 1 170 ? 36.470  0.855   2.753   1.00 45.24  ? 142 ASN B CG    1 
ATOM   3216 O OD1   . ASN B 1 170 ? 35.431  0.794   3.410   1.00 44.18  ? 142 ASN B OD1   1 
ATOM   3217 N ND2   . ASN B 1 170 ? 37.271  -0.189  2.583   1.00 46.98  ? 142 ASN B ND2   1 
ATOM   3218 N N     . ARG B 1 171 ? 36.607  4.474   -0.231  1.00 46.19  ? 143 ARG B N     1 
ATOM   3219 C CA    . ARG B 1 171 ? 35.976  5.731   -0.619  1.00 47.47  ? 143 ARG B CA    1 
ATOM   3220 C C     . ARG B 1 171 ? 35.167  5.568   -1.900  1.00 45.42  ? 143 ARG B C     1 
ATOM   3221 O O     . ARG B 1 171 ? 34.108  6.188   -2.055  1.00 44.78  ? 143 ARG B O     1 
ATOM   3222 C CB    . ARG B 1 171 ? 37.026  6.831   -0.779  1.00 50.85  ? 143 ARG B CB    1 
ATOM   3223 C CG    . ARG B 1 171 ? 36.442  8.167   -1.224  1.00 47.87  ? 143 ARG B CG    1 
ATOM   3224 C CD    . ARG B 1 171 ? 37.224  9.355   -0.687  1.00 45.02  ? 143 ARG B CD    1 
ATOM   3225 N NE    . ARG B 1 171 ? 38.597  9.018   -0.336  1.00 55.91  ? 143 ARG B NE    1 
ATOM   3226 C CZ    . ARG B 1 171 ? 39.251  9.539   0.692   1.00 67.77  ? 143 ARG B CZ    1 
ATOM   3227 N NH1   . ARG B 1 171 ? 38.684  10.427  1.493   1.00 66.83  ? 143 ARG B NH1   1 
ATOM   3228 N NH2   . ARG B 1 171 ? 40.506  9.161   0.923   1.00 68.59  ? 143 ARG B NH2   1 
ATOM   3229 N N     . LEU B 1 172 ? 35.645  4.734   -2.827  1.00 45.16  ? 144 LEU B N     1 
ATOM   3230 C CA    . LEU B 1 172 ? 34.883  4.476   -4.045  1.00 45.05  ? 144 LEU B CA    1 
ATOM   3231 C C     . LEU B 1 172 ? 33.565  3.782   -3.727  1.00 42.85  ? 144 LEU B C     1 
ATOM   3232 O O     . LEU B 1 172 ? 32.545  4.041   -4.376  1.00 43.84  ? 144 LEU B O     1 
ATOM   3233 C CB    . LEU B 1 172 ? 35.717  3.640   -5.016  1.00 47.02  ? 144 LEU B CB    1 
ATOM   3234 C CG    . LEU B 1 172 ? 35.045  3.197   -6.319  1.00 45.17  ? 144 LEU B CG    1 
ATOM   3235 C CD1   . LEU B 1 172 ? 34.426  4.382   -7.044  1.00 45.83  ? 144 LEU B CD1   1 
ATOM   3236 C CD2   . LEU B 1 172 ? 36.036  2.471   -7.215  1.00 49.17  ? 144 LEU B CD2   1 
ATOM   3237 N N     . ALA B 1 173 ? 33.565  2.902   -2.722  1.00 42.70  ? 145 ALA B N     1 
ATOM   3238 C CA    . ALA B 1 173 ? 32.329  2.237   -2.326  1.00 41.66  ? 145 ALA B CA    1 
ATOM   3239 C C     . ALA B 1 173 ? 31.363  3.216   -1.670  1.00 40.50  ? 145 ALA B C     1 
ATOM   3240 O O     . ALA B 1 173 ? 30.146  3.117   -1.863  1.00 39.61  ? 145 ALA B O     1 
ATOM   3241 C CB    . ALA B 1 173 ? 32.635  1.071   -1.388  1.00 41.90  ? 145 ALA B CB    1 
ATOM   3242 N N     . VAL B 1 174 ? 31.885  4.166   -0.891  1.00 40.85  ? 146 VAL B N     1 
ATOM   3243 C CA    . VAL B 1 174 ? 31.028  5.182   -0.287  1.00 39.60  ? 146 VAL B CA    1 
ATOM   3244 C C     . VAL B 1 174 ? 30.468  6.108   -1.359  1.00 41.61  ? 146 VAL B C     1 
ATOM   3245 O O     . VAL B 1 174 ? 29.298  6.507   -1.307  1.00 41.09  ? 146 VAL B O     1 
ATOM   3246 C CB    . VAL B 1 174 ? 31.801  5.959   0.794   1.00 39.92  ? 146 VAL B CB    1 
ATOM   3247 C CG1   . VAL B 1 174 ? 31.010  7.173   1.254   1.00 39.10  ? 146 VAL B CG1   1 
ATOM   3248 C CG2   . VAL B 1 174 ? 32.121  5.053   1.971   1.00 40.06  ? 146 VAL B CG2   1 
ATOM   3249 N N     . LYS B 1 175 ? 31.290  6.458   -2.354  1.00 42.11  ? 147 LYS B N     1 
ATOM   3250 C CA    . LYS B 1 175 ? 30.808  7.278   -3.461  1.00 42.24  ? 147 LYS B CA    1 
ATOM   3251 C C     . LYS B 1 175 ? 29.703  6.568   -4.233  1.00 40.77  ? 147 LYS B C     1 
ATOM   3252 O O     . LYS B 1 175 ? 28.710  7.191   -4.627  1.00 39.71  ? 147 LYS B O     1 
ATOM   3253 C CB    . LYS B 1 175 ? 31.967  7.634   -4.393  1.00 41.27  ? 147 LYS B CB    1 
ATOM   3254 C CG    . LYS B 1 175 ? 31.535  8.320   -5.679  1.00 47.12  ? 147 LYS B CG    1 
ATOM   3255 C CD    . LYS B 1 175 ? 32.704  8.512   -6.629  1.00 55.02  ? 147 LYS B CD    1 
ATOM   3256 C CE    . LYS B 1 175 ? 32.228  8.995   -7.990  1.00 56.45  ? 147 LYS B CE    1 
ATOM   3257 N NZ    . LYS B 1 175 ? 33.353  9.151   -8.953  1.00 50.07  ? 147 LYS B NZ    1 
ATOM   3258 N N     . ASN B 1 176 ? 29.857  5.260   -4.455  1.00 41.47  ? 148 ASN B N     1 
ATOM   3259 C CA    . ASN B 1 176 ? 28.838  4.511   -5.183  1.00 39.68  ? 148 ASN B CA    1 
ATOM   3260 C C     . ASN B 1 176 ? 27.573  4.328   -4.355  1.00 40.23  ? 148 ASN B C     1 
ATOM   3261 O O     . ASN B 1 176 ? 26.468  4.326   -4.909  1.00 39.49  ? 148 ASN B O     1 
ATOM   3262 C CB    . ASN B 1 176 ? 29.397  3.158   -5.621  1.00 40.26  ? 148 ASN B CB    1 
ATOM   3263 C CG    . ASN B 1 176 ? 30.203  3.251   -6.902  1.00 41.34  ? 148 ASN B CG    1 
ATOM   3264 O OD1   . ASN B 1 176 ? 30.159  4.263   -7.602  1.00 41.41  ? 148 ASN B OD1   1 
ATOM   3265 N ND2   . ASN B 1 176 ? 30.940  2.194   -7.219  1.00 48.03  ? 148 ASN B ND2   1 
ATOM   3266 N N     . ILE B 1 177 ? 27.708  4.168   -3.036  1.00 37.99  ? 149 ILE B N     1 
ATOM   3267 C CA    . ILE B 1 177 ? 26.532  4.160   -2.172  1.00 36.93  ? 149 ILE B CA    1 
ATOM   3268 C C     . ILE B 1 177 ? 25.853  5.523   -2.199  1.00 42.54  ? 149 ILE B C     1 
ATOM   3269 O O     . ILE B 1 177 ? 24.619  5.621   -2.193  1.00 42.39  ? 149 ILE B O     1 
ATOM   3270 C CB    . ILE B 1 177 ? 26.923  3.745   -0.741  1.00 36.87  ? 149 ILE B CB    1 
ATOM   3271 C CG1   . ILE B 1 177 ? 27.306  2.265   -0.696  1.00 37.39  ? 149 ILE B CG1   1 
ATOM   3272 C CG2   . ILE B 1 177 ? 25.787  4.021   0.234   1.00 35.84  ? 149 ILE B CG2   1 
ATOM   3273 C CD1   . ILE B 1 177 ? 27.922  1.835   0.618   1.00 37.59  ? 149 ILE B CD1   1 
ATOM   3274 N N     . HIS B 1 178 ? 26.647  6.596   -2.247  1.00 42.22  ? 150 HIS B N     1 
ATOM   3275 C CA    . HIS B 1 178 ? 26.088  7.942   -2.302  1.00 42.44  ? 150 HIS B CA    1 
ATOM   3276 C C     . HIS B 1 178 ? 25.292  8.170   -3.581  1.00 43.28  ? 150 HIS B C     1 
ATOM   3277 O O     . HIS B 1 178 ? 24.294  8.900   -3.567  1.00 41.93  ? 150 HIS B O     1 
ATOM   3278 C CB    . HIS B 1 178 ? 27.211  8.972   -2.176  1.00 44.66  ? 150 HIS B CB    1 
ATOM   3279 C CG    . HIS B 1 178 ? 26.733  10.388  -2.108  1.00 46.34  ? 150 HIS B CG    1 
ATOM   3280 N ND1   . HIS B 1 178 ? 26.562  11.171  -3.230  1.00 47.42  ? 150 HIS B ND1   1 
ATOM   3281 C CD2   . HIS B 1 178 ? 26.393  11.165  -1.052  1.00 48.40  ? 150 HIS B CD2   1 
ATOM   3282 C CE1   . HIS B 1 178 ? 26.137  12.368  -2.868  1.00 49.93  ? 150 HIS B CE1   1 
ATOM   3283 N NE2   . HIS B 1 178 ? 26.026  12.391  -1.552  1.00 51.46  ? 150 HIS B NE2   1 
ATOM   3284 N N     . LYS B 1 179 ? 25.713  7.557   -4.691  1.00 40.69  ? 151 LYS B N     1 
ATOM   3285 C CA    . LYS B 1 179 ? 24.957  7.680   -5.934  1.00 38.12  ? 151 LYS B CA    1 
ATOM   3286 C C     . LYS B 1 179 ? 23.612  6.971   -5.851  1.00 38.56  ? 151 LYS B C     1 
ATOM   3287 O O     . LYS B 1 179 ? 22.650  7.393   -6.502  1.00 39.76  ? 151 LYS B O     1 
ATOM   3288 C CB    . LYS B 1 179 ? 25.759  7.115   -7.107  1.00 37.88  ? 151 LYS B CB    1 
ATOM   3289 C CG    . LYS B 1 179 ? 26.944  7.954   -7.548  1.00 39.87  ? 151 LYS B CG    1 
ATOM   3290 C CD    . LYS B 1 179 ? 27.614  7.320   -8.759  1.00 42.31  ? 151 LYS B CD    1 
ATOM   3291 C CE    . LYS B 1 179 ? 28.802  8.133   -9.240  1.00 48.45  ? 151 LYS B CE    1 
ATOM   3292 N NZ    . LYS B 1 179 ? 29.461  7.490   -10.412 1.00 51.18  ? 151 LYS B NZ    1 
ATOM   3293 N N     . LEU B 1 180 ? 23.526  5.899   -5.062  1.00 35.76  ? 152 LEU B N     1 
ATOM   3294 C CA    . LEU B 1 180 ? 22.323  5.079   -5.019  1.00 35.19  ? 152 LEU B CA    1 
ATOM   3295 C C     . LEU B 1 180 ? 21.252  5.636   -4.092  1.00 34.24  ? 152 LEU B C     1 
ATOM   3296 O O     . LEU B 1 180 ? 20.089  5.230   -4.198  1.00 33.76  ? 152 LEU B O     1 
ATOM   3297 C CB    . LEU B 1 180 ? 22.684  3.656   -4.587  1.00 35.47  ? 152 LEU B CB    1 
ATOM   3298 C CG    . LEU B 1 180 ? 23.404  2.800   -5.630  1.00 36.43  ? 152 LEU B CG    1 
ATOM   3299 C CD1   . LEU B 1 180 ? 24.068  1.603   -4.975  1.00 36.83  ? 152 LEU B CD1   1 
ATOM   3300 C CD2   . LEU B 1 180 ? 22.433  2.348   -6.706  1.00 36.43  ? 152 LEU B CD2   1 
ATOM   3301 N N     . LEU B 1 181 ? 21.608  6.551   -3.197  1.00 34.02  ? 153 LEU B N     1 
ATOM   3302 C CA    . LEU B 1 181 ? 20.679  7.052   -2.195  1.00 33.99  ? 153 LEU B CA    1 
ATOM   3303 C C     . LEU B 1 181 ? 19.956  8.300   -2.682  1.00 47.35  ? 153 LEU B C     1 
ATOM   3304 O O     . LEU B 1 181 ? 20.514  9.124   -3.412  1.00 45.17  ? 153 LEU B O     1 
ATOM   3305 C CB    . LEU B 1 181 ? 21.411  7.359   -0.889  1.00 33.20  ? 153 LEU B CB    1 
ATOM   3306 C CG    . LEU B 1 181 ? 21.839  6.149   -0.058  1.00 33.32  ? 153 LEU B CG    1 
ATOM   3307 C CD1   . LEU B 1 181 ? 22.841  6.559   1.006   1.00 36.23  ? 153 LEU B CD1   1 
ATOM   3308 C CD2   . LEU B 1 181 ? 20.622  5.496   0.574   1.00 33.69  ? 153 LEU B CD2   1 
ATOM   3309 N N     . VAL B 1 182 ? 18.700  8.428   -2.268  1.00 41.98  ? 154 VAL B N     1 
ATOM   3310 C CA    . VAL B 1 182 ? 17.913  9.632   -2.518  1.00 41.49  ? 154 VAL B CA    1 
ATOM   3311 C C     . VAL B 1 182 ? 18.404  10.716  -1.568  1.00 43.10  ? 154 VAL B C     1 
ATOM   3312 O O     . VAL B 1 182 ? 18.916  10.395  -0.484  1.00 44.24  ? 154 VAL B O     1 
ATOM   3313 C CB    . VAL B 1 182 ? 16.408  9.369   -2.338  1.00 41.37  ? 154 VAL B CB    1 
ATOM   3314 C CG1   . VAL B 1 182 ? 15.925  8.325   -3.327  1.00 40.92  ? 154 VAL B CG1   1 
ATOM   3315 C CG2   . VAL B 1 182 ? 16.110  8.929   -0.913  1.00 40.50  ? 154 VAL B CG2   1 
ATOM   3316 N N     . PRO B 1 183 ? 18.302  11.994  -1.932  1.00 40.55  ? 155 PRO B N     1 
ATOM   3317 C CA    . PRO B 1 183 ? 18.645  13.064  -0.982  1.00 44.06  ? 155 PRO B CA    1 
ATOM   3318 C C     . PRO B 1 183 ? 17.838  12.926  0.299   1.00 43.59  ? 155 PRO B C     1 
ATOM   3319 O O     . PRO B 1 183 ? 16.606  12.947  0.287   1.00 46.44  ? 155 PRO B O     1 
ATOM   3320 C CB    . PRO B 1 183 ? 18.287  14.340  -1.750  1.00 43.61  ? 155 PRO B CB    1 
ATOM   3321 C CG    . PRO B 1 183 ? 18.459  13.961  -3.178  1.00 45.60  ? 155 PRO B CG    1 
ATOM   3322 C CD    . PRO B 1 183 ? 18.019  12.523  -3.277  1.00 40.65  ? 155 PRO B CD    1 
ATOM   3323 N N     . GLY B 1 184 ? 18.549  12.778  1.415   1.00 44.63  ? 156 GLY B N     1 
ATOM   3324 C CA    . GLY B 1 184 ? 17.930  12.450  2.678   1.00 43.65  ? 156 GLY B CA    1 
ATOM   3325 C C     . GLY B 1 184 ? 17.918  10.974  3.005   1.00 48.20  ? 156 GLY B C     1 
ATOM   3326 O O     . GLY B 1 184 ? 17.556  10.607  4.131   1.00 53.64  ? 156 GLY B O     1 
ATOM   3327 N N     . GLY B 1 185 ? 18.297  10.118  2.058   1.00 38.96  ? 157 GLY B N     1 
ATOM   3328 C CA    . GLY B 1 185 ? 18.379  8.701   2.341   1.00 42.23  ? 157 GLY B CA    1 
ATOM   3329 C C     . GLY B 1 185 ? 19.498  8.385   3.315   1.00 47.16  ? 157 GLY B C     1 
ATOM   3330 O O     . GLY B 1 185 ? 20.495  9.101   3.413   1.00 47.11  ? 157 GLY B O     1 
ATOM   3331 N N     . GLU B 1 186 ? 19.326  7.287   4.044   1.00 44.45  ? 158 GLU B N     1 
ATOM   3332 C CA    . GLU B 1 186 ? 20.226  6.922   5.126   1.00 45.11  ? 158 GLU B CA    1 
ATOM   3333 C C     . GLU B 1 186 ? 20.957  5.626   4.800   1.00 40.79  ? 158 GLU B C     1 
ATOM   3334 O O     . GLU B 1 186 ? 20.431  4.751   4.108   1.00 39.77  ? 158 GLU B O     1 
ATOM   3335 C CB    . GLU B 1 186 ? 19.461  6.773   6.445   1.00 48.41  ? 158 GLU B CB    1 
ATOM   3336 C CG    . GLU B 1 186 ? 18.695  8.024   6.847   1.00 52.01  ? 158 GLU B CG    1 
ATOM   3337 C CD    . GLU B 1 186 ? 17.712  7.774   7.972   1.00 57.76  ? 158 GLU B CD    1 
ATOM   3338 O OE1   . GLU B 1 186 ? 17.055  6.711   7.964   1.00 57.13  ? 158 GLU B OE1   1 
ATOM   3339 O OE2   . GLU B 1 186 ? 17.592  8.643   8.862   1.00 59.50  ? 158 GLU B OE2   1 
ATOM   3340 N N     . ALA B 1 187 ? 22.181  5.514   5.312   1.00 40.73  ? 159 ALA B N     1 
ATOM   3341 C CA    . ALA B 1 187 ? 23.016  4.338   5.124   1.00 34.08  ? 159 ALA B CA    1 
ATOM   3342 C C     . ALA B 1 187 ? 23.374  3.743   6.478   1.00 34.45  ? 159 ALA B C     1 
ATOM   3343 O O     . ALA B 1 187 ? 23.640  4.474   7.437   1.00 37.90  ? 159 ALA B O     1 
ATOM   3344 C CB    . ALA B 1 187 ? 24.291  4.681   4.347   1.00 34.08  ? 159 ALA B CB    1 
ATOM   3345 N N     . VAL B 1 188 ? 23.376  2.415   6.552   1.00 33.63  ? 160 VAL B N     1 
ATOM   3346 C CA    . VAL B 1 188 ? 23.689  1.686   7.775   1.00 33.85  ? 160 VAL B CA    1 
ATOM   3347 C C     . VAL B 1 188 ? 24.923  0.841   7.499   1.00 34.79  ? 160 VAL B C     1 
ATOM   3348 O O     . VAL B 1 188 ? 24.878  -0.086  6.679   1.00 39.24  ? 160 VAL B O     1 
ATOM   3349 C CB    . VAL B 1 188 ? 22.517  0.815   8.244   1.00 33.33  ? 160 VAL B CB    1 
ATOM   3350 C CG1   . VAL B 1 188 ? 22.933  -0.041  9.430   1.00 33.70  ? 160 VAL B CG1   1 
ATOM   3351 C CG2   . VAL B 1 188 ? 21.321  1.684   8.599   1.00 32.50  ? 160 VAL B CG2   1 
ATOM   3352 N N     . PHE B 1 189 ? 26.021  1.153   8.178   1.00 35.40  ? 161 PHE B N     1 
ATOM   3353 C CA    . PHE B 1 189 ? 27.279  0.447   7.998   1.00 36.41  ? 161 PHE B CA    1 
ATOM   3354 C C     . PHE B 1 189 ? 27.552  -0.471  9.182   1.00 36.76  ? 161 PHE B C     1 
ATOM   3355 O O     . PHE B 1 189 ? 27.197  -0.169  10.324  1.00 37.63  ? 161 PHE B O     1 
ATOM   3356 C CB    . PHE B 1 189 ? 28.446  1.425   7.833   1.00 37.06  ? 161 PHE B CB    1 
ATOM   3357 C CG    . PHE B 1 189 ? 28.352  2.281   6.606   1.00 37.09  ? 161 PHE B CG    1 
ATOM   3358 C CD1   . PHE B 1 189 ? 28.850  1.833   5.395   1.00 37.47  ? 161 PHE B CD1   1 
ATOM   3359 C CD2   . PHE B 1 189 ? 27.776  3.539   6.664   1.00 42.83  ? 161 PHE B CD2   1 
ATOM   3360 C CE1   . PHE B 1 189 ? 28.770  2.618   4.262   1.00 37.40  ? 161 PHE B CE1   1 
ATOM   3361 C CE2   . PHE B 1 189 ? 27.692  4.330   5.534   1.00 42.57  ? 161 PHE B CE2   1 
ATOM   3362 C CZ    . PHE B 1 189 ? 28.190  3.869   4.331   1.00 38.15  ? 161 PHE B CZ    1 
ATOM   3363 N N     . SER B 1 190 ? 28.191  -1.609  8.887   1.00 37.50  ? 162 SER B N     1 
ATOM   3364 C CA    . SER B 1 190 ? 28.684  -2.544  9.899   1.00 38.09  ? 162 SER B CA    1 
ATOM   3365 C C     . SER B 1 190 ? 30.087  -2.948  9.446   1.00 39.29  ? 162 SER B C     1 
ATOM   3366 O O     . SER B 1 190 ? 30.303  -4.024  8.886   1.00 42.16  ? 162 SER B O     1 
ATOM   3367 C CB    . SER B 1 190 ? 27.760  -3.748  10.063  1.00 39.85  ? 162 SER B CB    1 
ATOM   3368 O OG    . SER B 1 190 ? 28.179  -4.574  11.136  1.00 42.92  ? 162 SER B OG    1 
ATOM   3369 N N     . VAL B 1 191 ? 31.048  -2.063  9.683   1.00 39.80  ? 163 VAL B N     1 
ATOM   3370 C CA    . VAL B 1 191 ? 32.402  -2.221  9.168   1.00 40.97  ? 163 VAL B CA    1 
ATOM   3371 C C     . VAL B 1 191 ? 33.261  -2.896  10.226  1.00 41.89  ? 163 VAL B C     1 
ATOM   3372 O O     . VAL B 1 191 ? 33.227  -2.516  11.402  1.00 41.78  ? 163 VAL B O     1 
ATOM   3373 C CB    . VAL B 1 191 ? 32.995  -0.861  8.765   1.00 41.15  ? 163 VAL B CB    1 
ATOM   3374 C CG1   . VAL B 1 191 ? 34.358  -1.044  8.116   1.00 42.43  ? 163 VAL B CG1   1 
ATOM   3375 C CG2   . VAL B 1 191 ? 32.040  -0.129  7.841   1.00 40.20  ? 163 VAL B CG2   1 
ATOM   3376 N N     . ILE B 1 192 ? 34.033  -3.897  9.811   1.00 42.88  ? 164 ILE B N     1 
ATOM   3377 C CA    . ILE B 1 192 ? 34.974  -4.564  10.705  1.00 43.95  ? 164 ILE B CA    1 
ATOM   3378 C C     . ILE B 1 192 ? 36.253  -3.734  10.746  1.00 44.90  ? 164 ILE B C     1 
ATOM   3379 O O     . ILE B 1 192 ? 36.977  -3.642  9.753   1.00 45.57  ? 164 ILE B O     1 
ATOM   3380 C CB    . ILE B 1 192 ? 35.261  -6.002  10.259  1.00 44.71  ? 164 ILE B CB    1 
ATOM   3381 C CG1   . ILE B 1 192 ? 34.007  -6.866  10.401  1.00 43.89  ? 164 ILE B CG1   1 
ATOM   3382 C CG2   . ILE B 1 192 ? 36.403  -6.588  11.071  1.00 46.01  ? 164 ILE B CG2   1 
ATOM   3383 C CD1   . ILE B 1 192 ? 34.165  -8.266  9.849   1.00 44.61  ? 164 ILE B CD1   1 
ATOM   3384 N N     . ALA B 1 193 ? 36.529  -3.124  11.899  1.00 45.03  ? 165 ALA B N     1 
ATOM   3385 C CA    . ALA B 1 193 ? 37.731  -2.318  12.068  1.00 48.16  ? 165 ALA B CA    1 
ATOM   3386 C C     . ALA B 1 193 ? 38.977  -3.186  11.963  1.00 54.92  ? 165 ALA B C     1 
ATOM   3387 O O     . ALA B 1 193 ? 39.712  -3.111  10.973  1.00 63.37  ? 165 ALA B O     1 
ATOM   3388 C CB    . ALA B 1 193 ? 37.704  -1.585  13.410  1.00 50.24  ? 165 ALA B CB    1 
ATOM   3389 N N     . ASN B 1 194 ? 39.219  -4.014  12.976  1.00 54.97  ? 166 ASN B N     1 
ATOM   3390 C CA    . ASN B 1 194 ? 40.367  -4.904  12.988  1.00 56.92  ? 166 ASN B CA    1 
ATOM   3391 C C     . ASN B 1 194 ? 39.940  -6.270  13.505  1.00 55.33  ? 166 ASN B C     1 
ATOM   3392 O O     . ASN B 1 194 ? 38.961  -6.399  14.244  1.00 53.08  ? 166 ASN B O     1 
ATOM   3393 C CB    . ASN B 1 194 ? 41.510  -4.344  13.847  1.00 59.32  ? 166 ASN B CB    1 
ATOM   3394 C CG    . ASN B 1 194 ? 41.172  -4.320  15.327  1.00 62.99  ? 166 ASN B CG    1 
ATOM   3395 O OD1   . ASN B 1 194 ? 41.251  -5.340  16.013  1.00 62.82  ? 166 ASN B OD1   1 
ATOM   3396 N ND2   . ASN B 1 194 ? 40.790  -3.150  15.827  1.00 67.03  ? 166 ASN B ND2   1 
ATOM   3397 N N     . MET B 1 195 ? 40.692  -7.292  13.104  1.00 60.33  ? 167 MET B N     1 
ATOM   3398 C CA    . MET B 1 195 ? 40.468  -8.642  13.597  1.00 60.55  ? 167 MET B CA    1 
ATOM   3399 C C     . MET B 1 195 ? 41.746  -9.442  13.398  1.00 60.52  ? 167 MET B C     1 
ATOM   3400 O O     . MET B 1 195 ? 42.629  -9.053  12.630  1.00 59.70  ? 167 MET B O     1 
ATOM   3401 C CB    . MET B 1 195 ? 39.289  -9.318  12.889  1.00 55.29  ? 167 MET B CB    1 
ATOM   3402 C CG    . MET B 1 195 ? 39.296  -9.182  11.376  1.00 58.78  ? 167 MET B CG    1 
ATOM   3403 S SD    . MET B 1 195 ? 37.781  -9.832  10.647  1.00 54.20  ? 167 MET B SD    1 
ATOM   3404 C CE    . MET B 1 195 ? 37.487  -11.249 11.699  1.00 52.79  ? 167 MET B CE    1 
ATOM   3405 N N     . ALA B 1 196 ? 41.830  -10.573 14.102  1.00 60.13  ? 168 ALA B N     1 
ATOM   3406 C CA    . ALA B 1 196 ? 43.019  -11.413 14.037  1.00 63.05  ? 168 ALA B CA    1 
ATOM   3407 C C     . ALA B 1 196 ? 43.125  -12.195 12.733  1.00 62.99  ? 168 ALA B C     1 
ATOM   3408 O O     . ALA B 1 196 ? 44.205  -12.712 12.426  1.00 63.88  ? 168 ALA B O     1 
ATOM   3409 C CB    . ALA B 1 196 ? 43.046  -12.383 15.218  1.00 62.01  ? 168 ALA B CB    1 
ATOM   3410 N N     . LEU B 1 197 ? 42.036  -12.303 11.966  1.00 60.29  ? 169 LEU B N     1 
ATOM   3411 C CA    . LEU B 1 197 ? 42.128  -12.955 10.664  1.00 59.53  ? 169 LEU B CA    1 
ATOM   3412 C C     . LEU B 1 197 ? 43.041  -12.179 9.726   1.00 68.03  ? 169 LEU B C     1 
ATOM   3413 O O     . LEU B 1 197 ? 43.701  -12.773 8.866   1.00 73.12  ? 169 LEU B O     1 
ATOM   3414 C CB    . LEU B 1 197 ? 40.742  -13.101 10.029  1.00 60.33  ? 169 LEU B CB    1 
ATOM   3415 C CG    . LEU B 1 197 ? 39.650  -13.952 10.688  1.00 54.78  ? 169 LEU B CG    1 
ATOM   3416 C CD1   . LEU B 1 197 ? 38.438  -14.055 9.769   1.00 62.20  ? 169 LEU B CD1   1 
ATOM   3417 C CD2   . LEU B 1 197 ? 40.137  -15.327 11.075  1.00 57.58  ? 169 LEU B CD2   1 
ATOM   3418 N N     . CYS B 1 198 ? 43.092  -10.853 9.878   1.00 69.03  ? 170 CYS B N     1 
ATOM   3419 C CA    . CYS B 1 198 ? 43.925  -10.023 9.016   1.00 67.82  ? 170 CYS B CA    1 
ATOM   3420 C C     . CYS B 1 198 ? 45.399  -10.124 9.390   1.00 74.52  ? 170 CYS B C     1 
ATOM   3421 O O     . CYS B 1 198 ? 46.258  -10.236 8.509   1.00 74.66  ? 170 CYS B O     1 
ATOM   3422 C CB    . CYS B 1 198 ? 43.459  -8.569  9.083   1.00 62.59  ? 170 CYS B CB    1 
ATOM   3423 S SG    . CYS B 1 198 ? 41.899  -8.243  8.232   1.00 60.46  ? 170 CYS B SG    1 
ATOM   3424 N N     . ASP B 1 199 ? 45.712  -10.077 10.688  1.00 76.39  ? 171 ASP B N     1 
ATOM   3425 C CA    . ASP B 1 199 ? 47.098  -10.237 11.114  1.00 72.81  ? 171 ASP B CA    1 
ATOM   3426 C C     . ASP B 1 199 ? 47.616  -11.636 10.812  1.00 71.00  ? 171 ASP B C     1 
ATOM   3427 O O     . ASP B 1 199 ? 48.811  -11.809 10.548  1.00 73.70  ? 171 ASP B O     1 
ATOM   3428 C CB    . ASP B 1 199 ? 47.232  -9.926  12.605  1.00 74.54  ? 171 ASP B CB    1 
ATOM   3429 C CG    . ASP B 1 199 ? 46.928  -8.476  12.925  1.00 78.82  ? 171 ASP B CG    1 
ATOM   3430 O OD1   . ASP B 1 199 ? 47.298  -7.598  12.117  1.00 75.49  ? 171 ASP B OD1   1 
ATOM   3431 O OD2   . ASP B 1 199 ? 46.319  -8.214  13.983  1.00 79.09  ? 171 ASP B OD2   1 
ATOM   3432 N N     . ALA B 1 200 ? 46.738  -12.642 10.844  1.00 66.08  ? 172 ALA B N     1 
ATOM   3433 C CA    . ALA B 1 200 ? 47.134  -13.976 10.407  1.00 72.02  ? 172 ALA B CA    1 
ATOM   3434 C C     . ALA B 1 200 ? 47.472  -13.991 8.924   1.00 77.06  ? 172 ALA B C     1 
ATOM   3435 O O     . ALA B 1 200 ? 48.316  -14.781 8.486   1.00 78.35  ? 172 ALA B O     1 
ATOM   3436 C CB    . ALA B 1 200 ? 46.025  -14.982 10.712  1.00 69.28  ? 172 ALA B CB    1 
ATOM   3437 N N     . TYR B 1 201 ? 46.826  -13.126 8.138   1.00 77.52  ? 173 TYR B N     1 
ATOM   3438 C CA    . TYR B 1 201 ? 47.167  -13.012 6.724   1.00 80.97  ? 173 TYR B CA    1 
ATOM   3439 C C     . TYR B 1 201 ? 48.530  -12.357 6.541   1.00 79.96  ? 173 TYR B C     1 
ATOM   3440 O O     . TYR B 1 201 ? 49.343  -12.814 5.730   1.00 77.96  ? 173 TYR B O     1 
ATOM   3441 C CB    . TYR B 1 201 ? 46.093  -12.211 5.987   1.00 78.07  ? 173 TYR B CB    1 
ATOM   3442 C CG    . TYR B 1 201 ? 44.870  -13.006 5.591   1.00 74.17  ? 173 TYR B CG    1 
ATOM   3443 C CD1   . TYR B 1 201 ? 44.917  -14.390 5.486   1.00 74.35  ? 173 TYR B CD1   1 
ATOM   3444 C CD2   . TYR B 1 201 ? 43.666  -12.369 5.319   1.00 69.51  ? 173 TYR B CD2   1 
ATOM   3445 C CE1   . TYR B 1 201 ? 43.798  -15.117 5.123   1.00 72.19  ? 173 TYR B CE1   1 
ATOM   3446 C CE2   . TYR B 1 201 ? 42.544  -13.085 4.956   1.00 72.12  ? 173 TYR B CE2   1 
ATOM   3447 C CZ    . TYR B 1 201 ? 42.615  -14.457 4.859   1.00 73.38  ? 173 TYR B CZ    1 
ATOM   3448 O OH    . TYR B 1 201 ? 41.496  -15.170 4.497   1.00 71.00  ? 173 TYR B OH    1 
ATOM   3449 N N     . GLU B 1 202 ? 48.799  -11.284 7.291   1.00 78.96  ? 174 GLU B N     1 
ATOM   3450 C CA    . GLU B 1 202 ? 50.055  -10.560 7.130   1.00 80.96  ? 174 GLU B CA    1 
ATOM   3451 C C     . GLU B 1 202 ? 51.250  -11.388 7.581   1.00 88.47  ? 174 GLU B C     1 
ATOM   3452 O O     . GLU B 1 202 ? 52.354  -11.220 7.049   1.00 91.53  ? 174 GLU B O     1 
ATOM   3453 C CB    . GLU B 1 202 ? 50.000  -9.241  7.902   1.00 77.19  ? 174 GLU B CB    1 
ATOM   3454 C CG    . GLU B 1 202 ? 49.079  -8.202  7.285   1.00 73.45  ? 174 GLU B CG    1 
ATOM   3455 C CD    . GLU B 1 202 ? 48.839  -7.017  8.200   1.00 72.26  ? 174 GLU B CD    1 
ATOM   3456 O OE1   . GLU B 1 202 ? 48.772  -7.219  9.431   1.00 74.23  ? 174 GLU B OE1   1 
ATOM   3457 O OE2   . GLU B 1 202 ? 48.720  -5.884  7.688   1.00 71.74  ? 174 GLU B OE2   1 
ATOM   3458 N N     . GLU B 1 203 ? 51.059  -12.282 8.553   1.00 86.97  ? 175 GLU B N     1 
ATOM   3459 C CA    . GLU B 1 203 ? 52.164  -13.117 9.008   1.00 88.67  ? 175 GLU B CA    1 
ATOM   3460 C C     . GLU B 1 203 ? 52.461  -14.237 8.018   1.00 89.63  ? 175 GLU B C     1 
ATOM   3461 O O     . GLU B 1 203 ? 53.629  -14.572 7.789   1.00 88.75  ? 175 GLU B O     1 
ATOM   3462 C CB    . GLU B 1 203 ? 51.855  -13.691 10.392  1.00 88.61  ? 175 GLU B CB    1 
ATOM   3463 C CG    . GLU B 1 203 ? 51.817  -12.649 11.499  1.00 92.69  ? 175 GLU B CG    1 
ATOM   3464 C CD    . GLU B 1 203 ? 51.758  -13.267 12.884  1.00 96.06  ? 175 GLU B CD    1 
ATOM   3465 O OE1   . GLU B 1 203 ? 51.791  -14.511 12.986  1.00 96.19  ? 175 GLU B OE1   1 
ATOM   3466 O OE2   . GLU B 1 203 ? 51.673  -12.507 13.872  1.00 96.68  ? 175 GLU B OE2   1 
ATOM   3467 N N     . MET B 1 204 ? 51.421  -14.823 7.419   1.00 89.12  ? 176 MET B N     1 
ATOM   3468 C CA    . MET B 1 204 ? 51.634  -15.873 6.428   1.00 88.75  ? 176 MET B CA    1 
ATOM   3469 C C     . MET B 1 204 ? 52.265  -15.327 5.155   1.00 91.67  ? 176 MET B C     1 
ATOM   3470 O O     . MET B 1 204 ? 52.942  -16.069 4.434   1.00 91.92  ? 176 MET B O     1 
ATOM   3471 C CB    . MET B 1 204 ? 50.313  -16.568 6.099   1.00 86.72  ? 176 MET B CB    1 
ATOM   3472 C CG    . MET B 1 204 ? 49.752  -17.416 7.224   1.00 85.50  ? 176 MET B CG    1 
ATOM   3473 S SD    . MET B 1 204 ? 48.175  -18.173 6.787   1.00 86.28  ? 176 MET B SD    1 
ATOM   3474 C CE    . MET B 1 204 ? 48.706  -19.359 5.555   1.00 73.53  ? 176 MET B CE    1 
ATOM   3475 N N     . ALA B 1 205 ? 52.053  -14.041 4.860   1.00 91.93  ? 177 ALA B N     1 
ATOM   3476 C CA    . ALA B 1 205 ? 52.615  -13.457 3.647   1.00 89.59  ? 177 ALA B CA    1 
ATOM   3477 C C     . ALA B 1 205 ? 54.135  -13.387 3.706   1.00 93.94  ? 177 ALA B C     1 
ATOM   3478 O O     . ALA B 1 205 ? 54.794  -13.383 2.659   1.00 94.96  ? 177 ALA B O     1 
ATOM   3479 C CB    . ALA B 1 205 ? 52.027  -12.066 3.412   1.00 88.15  ? 177 ALA B CB    1 
ATOM   3480 N N     . LYS B 1 206 ? 54.708  -13.329 4.909   1.00 93.51  ? 178 LYS B N     1 
ATOM   3481 C CA    . LYS B 1 206 ? 56.156  -13.305 5.062   1.00 90.89  ? 178 LYS B CA    1 
ATOM   3482 C C     . LYS B 1 206 ? 56.797  -14.669 4.852   1.00 88.59  ? 178 LYS B C     1 
ATOM   3483 O O     . LYS B 1 206 ? 58.022  -14.745 4.711   1.00 87.58  ? 178 LYS B O     1 
ATOM   3484 C CB    . LYS B 1 206 ? 56.531  -12.772 6.446   1.00 85.71  ? 178 LYS B CB    1 
ATOM   3485 C CG    . LYS B 1 206 ? 56.154  -11.318 6.668   1.00 86.82  ? 178 LYS B CG    1 
ATOM   3486 C CD    . LYS B 1 206 ? 56.466  -10.878 8.086   1.00 90.17  ? 178 LYS B CD    1 
ATOM   3487 C CE    . LYS B 1 206 ? 56.020  -9.446  8.328   1.00 87.80  ? 178 LYS B CE    1 
ATOM   3488 N NZ    . LYS B 1 206 ? 56.225  -9.034  9.744   1.00 86.90  ? 178 LYS B NZ    1 
ATOM   3489 N N     . GLU B 1 207 ? 56.011  -15.735 4.829   1.00 91.09  ? 179 GLU B N     1 
ATOM   3490 C CA    . GLU B 1 207 ? 56.564  -17.063 4.608   1.00 90.35  ? 179 GLU B CA    1 
ATOM   3491 C C     . GLU B 1 207 ? 56.929  -17.231 3.137   1.00 92.22  ? 179 GLU B C     1 
ATOM   3492 O O     . GLU B 1 207 ? 56.079  -17.009 2.266   1.00 92.28  ? 179 GLU B O     1 
ATOM   3493 C CB    . GLU B 1 207 ? 55.558  -18.135 5.025   1.00 90.78  ? 179 GLU B CB    1 
ATOM   3494 C CG    . GLU B 1 207 ? 55.231  -18.147 6.510   1.00 95.01  ? 179 GLU B CG    1 
ATOM   3495 C CD    . GLU B 1 207 ? 54.270  -19.260 6.886   1.00 100.32 ? 179 GLU B CD    1 
ATOM   3496 O OE1   . GLU B 1 207 ? 54.159  -20.238 6.116   1.00 100.57 ? 179 GLU B OE1   1 
ATOM   3497 O OE2   . GLU B 1 207 ? 53.623  -19.155 7.950   1.00 96.57  ? 179 GLU B OE2   1 
ATOM   3498 N N     . PRO B 1 208 ? 58.172  -17.601 2.817   1.00 94.75  ? 180 PRO B N     1 
ATOM   3499 C CA    . PRO B 1 208 ? 58.496  -17.951 1.423   1.00 95.84  ? 180 PRO B CA    1 
ATOM   3500 C C     . PRO B 1 208 ? 57.638  -19.081 0.892   1.00 91.67  ? 180 PRO B C     1 
ATOM   3501 O O     . PRO B 1 208 ? 57.474  -19.209 -0.327  1.00 90.13  ? 180 PRO B O     1 
ATOM   3502 C CB    . PRO B 1 208 ? 59.973  -18.359 1.496   1.00 92.92  ? 180 PRO B CB    1 
ATOM   3503 C CG    . PRO B 1 208 ? 60.498  -17.654 2.704   1.00 88.26  ? 180 PRO B CG    1 
ATOM   3504 C CD    . PRO B 1 208 ? 59.361  -17.618 3.686   1.00 86.23  ? 180 PRO B CD    1 
ATOM   3505 N N     . ARG B 1 209 ? 57.092  -19.904 1.788   1.00 89.23  ? 181 ARG B N     1 
ATOM   3506 C CA    . ARG B 1 209 ? 56.156  -20.956 1.415   1.00 90.66  ? 181 ARG B CA    1 
ATOM   3507 C C     . ARG B 1 209 ? 54.933  -20.404 0.689   1.00 91.71  ? 181 ARG B C     1 
ATOM   3508 O O     . ARG B 1 209 ? 54.314  -21.115 -0.111  1.00 84.99  ? 181 ARG B O     1 
ATOM   3509 C CB    . ARG B 1 209 ? 55.753  -21.704 2.687   1.00 91.67  ? 181 ARG B CB    1 
ATOM   3510 C CG    . ARG B 1 209 ? 54.821  -22.888 2.549   1.00 91.14  ? 181 ARG B CG    1 
ATOM   3511 C CD    . ARG B 1 209 ? 54.512  -23.390 3.954   1.00 86.44  ? 181 ARG B CD    1 
ATOM   3512 N NE    . ARG B 1 209 ? 53.459  -24.395 4.006   1.00 91.51  ? 181 ARG B NE    1 
ATOM   3513 C CZ    . ARG B 1 209 ? 52.904  -24.826 5.131   1.00 89.43  ? 181 ARG B CZ    1 
ATOM   3514 N NH1   . ARG B 1 209 ? 53.262  -24.339 6.308   1.00 80.49  ? 181 ARG B NH1   1 
ATOM   3515 N NH2   . ARG B 1 209 ? 51.958  -25.758 5.073   1.00 93.13  ? 181 ARG B NH2   1 
ATOM   3516 N N     . TRP B 1 210 ? 54.576  -19.141 0.933   1.00 94.90  ? 182 TRP B N     1 
ATOM   3517 C CA    . TRP B 1 210 ? 53.336  -18.589 0.399   1.00 95.00  ? 182 TRP B CA    1 
ATOM   3518 C C     . TRP B 1 210 ? 53.531  -17.298 -0.384  1.00 93.63  ? 182 TRP B C     1 
ATOM   3519 O O     . TRP B 1 210 ? 52.707  -16.970 -1.246  1.00 91.98  ? 182 TRP B O     1 
ATOM   3520 C CB    . TRP B 1 210 ? 52.338  -18.326 1.528   1.00 92.49  ? 182 TRP B CB    1 
ATOM   3521 C CG    . TRP B 1 210 ? 52.048  -19.506 2.405   1.00 89.28  ? 182 TRP B CG    1 
ATOM   3522 C CD1   . TRP B 1 210 ? 52.220  -19.586 3.756   1.00 86.54  ? 182 TRP B CD1   1 
ATOM   3523 C CD2   . TRP B 1 210 ? 51.486  -20.759 1.997   1.00 90.95  ? 182 TRP B CD2   1 
ATOM   3524 N NE1   . TRP B 1 210 ? 51.824  -20.820 4.212   1.00 89.28  ? 182 TRP B NE1   1 
ATOM   3525 C CE2   . TRP B 1 210 ? 51.367  -21.558 3.152   1.00 89.79  ? 182 TRP B CE2   1 
ATOM   3526 C CE3   . TRP B 1 210 ? 51.081  -21.286 0.768   1.00 89.62  ? 182 TRP B CE3   1 
ATOM   3527 C CZ2   . TRP B 1 210 ? 50.859  -22.854 3.112   1.00 86.89  ? 182 TRP B CZ2   1 
ATOM   3528 C CZ3   . TRP B 1 210 ? 50.580  -22.571 0.731   1.00 87.00  ? 182 TRP B CZ3   1 
ATOM   3529 C CH2   . TRP B 1 210 ? 50.473  -23.342 1.895   1.00 85.80  ? 182 TRP B CH2   1 
ATOM   3530 N N     . ALA B 1 211 ? 54.611  -16.568 -0.096  1.00 93.70  ? 183 ALA B N     1 
ATOM   3531 C CA    . ALA B 1 211 ? 54.805  -15.181 -0.519  1.00 90.11  ? 183 ALA B CA    1 
ATOM   3532 C C     . ALA B 1 211 ? 54.399  -14.894 -1.962  1.00 90.74  ? 183 ALA B C     1 
ATOM   3533 O O     . ALA B 1 211 ? 53.993  -13.771 -2.280  1.00 90.96  ? 183 ALA B O     1 
ATOM   3534 C CB    . ALA B 1 211 ? 56.267  -14.779 -0.311  1.00 91.35  ? 183 ALA B CB    1 
ATOM   3535 N N     . LEU B 1 212 ? 54.500  -15.894 -2.842  1.00 90.72  ? 184 LEU B N     1 
ATOM   3536 C CA    . LEU B 1 212 ? 54.109  -15.696 -4.234  1.00 92.28  ? 184 LEU B CA    1 
ATOM   3537 C C     . LEU B 1 212 ? 52.619  -15.392 -4.349  1.00 96.22  ? 184 LEU B C     1 
ATOM   3538 O O     . LEU B 1 212 ? 52.214  -14.470 -5.067  1.00 93.44  ? 184 LEU B O     1 
ATOM   3539 C CB    . LEU B 1 212 ? 54.472  -16.929 -5.063  1.00 76.69  ? 184 LEU B CB    1 
ATOM   3540 N N     . TYR B 1 213 ? 51.785  -16.160 -3.645  1.00 92.23  ? 185 TYR B N     1 
ATOM   3541 C CA    . TYR B 1 213 ? 50.343  -15.954 -3.712  1.00 89.47  ? 185 TYR B CA    1 
ATOM   3542 C C     . TYR B 1 213 ? 49.886  -14.732 -2.927  1.00 89.18  ? 185 TYR B C     1 
ATOM   3543 O O     . TYR B 1 213 ? 48.766  -14.258 -3.145  1.00 89.24  ? 185 TYR B O     1 
ATOM   3544 C CB    . TYR B 1 213 ? 49.603  -17.186 -3.189  1.00 87.43  ? 185 TYR B CB    1 
ATOM   3545 C CG    . TYR B 1 213 ? 49.948  -18.482 -3.886  1.00 88.94  ? 185 TYR B CG    1 
ATOM   3546 C CD1   . TYR B 1 213 ? 49.280  -18.871 -5.040  1.00 90.20  ? 185 TYR B CD1   1 
ATOM   3547 C CD2   . TYR B 1 213 ? 50.933  -19.322 -3.385  1.00 92.24  ? 185 TYR B CD2   1 
ATOM   3548 C CE1   . TYR B 1 213 ? 49.586  -20.058 -5.677  1.00 91.53  ? 185 TYR B CE1   1 
ATOM   3549 C CE2   . TYR B 1 213 ? 51.247  -20.511 -4.016  1.00 94.52  ? 185 TYR B CE2   1 
ATOM   3550 C CZ    . TYR B 1 213 ? 50.570  -20.874 -5.161  1.00 93.47  ? 185 TYR B CZ    1 
ATOM   3551 O OH    . TYR B 1 213 ? 50.877  -22.055 -5.795  1.00 94.83  ? 185 TYR B OH    1 
ATOM   3552 N N     . MET B 1 214 ? 50.711  -14.216 -2.022  1.00 88.10  ? 186 MET B N     1 
ATOM   3553 C CA    . MET B 1 214 ? 50.288  -13.198 -1.070  1.00 88.61  ? 186 MET B CA    1 
ATOM   3554 C C     . MET B 1 214 ? 51.079  -11.907 -1.240  1.00 87.01  ? 186 MET B C     1 
ATOM   3555 O O     . MET B 1 214 ? 51.426  -11.238 -0.265  1.00 82.92  ? 186 MET B O     1 
ATOM   3556 C CB    . MET B 1 214 ? 50.409  -13.722 0.358   1.00 86.80  ? 186 MET B CB    1 
ATOM   3557 C CG    . MET B 1 214 ? 49.583  -14.971 0.618   1.00 82.73  ? 186 MET B CG    1 
ATOM   3558 S SD    . MET B 1 214 ? 49.679  -15.550 2.321   1.00 84.43  ? 186 MET B SD    1 
ATOM   3559 C CE    . MET B 1 214 ? 48.541  -14.421 3.114   1.00 82.87  ? 186 MET B CE    1 
ATOM   3560 N N     . GLN B 1 215 ? 51.371  -11.539 -2.490  1.00 86.57  ? 187 GLN B N     1 
ATOM   3561 C CA    . GLN B 1 215 ? 52.047  -10.270 -2.737  1.00 91.74  ? 187 GLN B CA    1 
ATOM   3562 C C     . GLN B 1 215 ? 51.133  -9.085  -2.452  1.00 92.57  ? 187 GLN B C     1 
ATOM   3563 O O     . GLN B 1 215 ? 51.603  -8.038  -1.992  1.00 93.29  ? 187 GLN B O     1 
ATOM   3564 C CB    . GLN B 1 215 ? 52.553  -10.213 -4.178  1.00 93.74  ? 187 GLN B CB    1 
ATOM   3565 C CG    . GLN B 1 215 ? 53.595  -11.266 -4.514  1.00 90.33  ? 187 GLN B CG    1 
ATOM   3566 C CD    . GLN B 1 215 ? 53.854  -11.370 -6.004  1.00 101.23 ? 187 GLN B CD    1 
ATOM   3567 O OE1   . GLN B 1 215 ? 53.389  -10.541 -6.787  1.00 108.23 ? 187 GLN B OE1   1 
ATOM   3568 N NE2   . GLN B 1 215 ? 54.601  -12.393 -6.405  1.00 99.05  ? 187 GLN B NE2   1 
ATOM   3569 N N     . ASP B 1 216 ? 49.839  -9.229  -2.712  1.00 89.25  ? 188 ASP B N     1 
ATOM   3570 C CA    . ASP B 1 216 ? 48.855  -8.175  -2.465  1.00 88.12  ? 188 ASP B CA    1 
ATOM   3571 C C     . ASP B 1 216 ? 48.106  -8.421  -1.162  1.00 86.94  ? 188 ASP B C     1 
ATOM   3572 O O     . ASP B 1 216 ? 46.876  -8.412  -1.118  1.00 87.62  ? 188 ASP B O     1 
ATOM   3573 C CB    . ASP B 1 216 ? 47.887  -8.078  -3.638  1.00 89.09  ? 188 ASP B CB    1 
ATOM   3574 C CG    . ASP B 1 216 ? 47.308  -9.425  -4.029  1.00 91.77  ? 188 ASP B CG    1 
ATOM   3575 O OD1   . ASP B 1 216 ? 47.848  -10.459 -3.581  1.00 91.25  ? 188 ASP B OD1   1 
ATOM   3576 O OD2   . ASP B 1 216 ? 46.313  -9.450  -4.784  1.00 92.97  ? 188 ASP B OD2   1 
ATOM   3577 N N     . VAL B 1 217 ? 48.851  -8.645  -0.077  1.00 86.22  ? 189 VAL B N     1 
ATOM   3578 C CA    . VAL B 1 217 ? 48.220  -8.972  1.198   1.00 83.03  ? 189 VAL B CA    1 
ATOM   3579 C C     . VAL B 1 217 ? 47.469  -7.771  1.762   1.00 80.15  ? 189 VAL B C     1 
ATOM   3580 O O     . VAL B 1 217 ? 46.412  -7.930  2.384   1.00 78.04  ? 189 VAL B O     1 
ATOM   3581 C CB    . VAL B 1 217 ? 49.269  -9.510  2.190   1.00 84.43  ? 189 VAL B CB    1 
ATOM   3582 C CG1   . VAL B 1 217 ? 50.347  -8.468  2.462   1.00 90.73  ? 189 VAL B CG1   1 
ATOM   3583 C CG2   . VAL B 1 217 ? 48.603  -9.956  3.485   1.00 79.38  ? 189 VAL B CG2   1 
ATOM   3584 N N     . GLU B 1 218 ? 47.979  -6.555  1.542   1.00 78.62  ? 190 GLU B N     1 
ATOM   3585 C CA    . GLU B 1 218 ? 47.329  -5.367  2.085   1.00 73.33  ? 190 GLU B CA    1 
ATOM   3586 C C     . GLU B 1 218 ? 45.953  -5.128  1.477   1.00 73.96  ? 190 GLU B C     1 
ATOM   3587 O O     . GLU B 1 218 ? 45.120  -4.470  2.108   1.00 74.94  ? 190 GLU B O     1 
ATOM   3588 C CB    . GLU B 1 218 ? 48.213  -4.135  1.876   1.00 83.61  ? 190 GLU B CB    1 
ATOM   3589 C CG    . GLU B 1 218 ? 48.385  -3.712  0.421   1.00 100.87 ? 190 GLU B CG    1 
ATOM   3590 C CD    . GLU B 1 218 ? 49.434  -4.529  -0.316  1.00 103.21 ? 190 GLU B CD    1 
ATOM   3591 O OE1   . GLU B 1 218 ? 49.931  -5.525  0.253   1.00 94.47  ? 190 GLU B OE1   1 
ATOM   3592 O OE2   . GLU B 1 218 ? 49.763  -4.171  -1.467  1.00 104.01 ? 190 GLU B OE2   1 
ATOM   3593 N N     . LYS B 1 219 ? 45.696  -5.644  0.275   1.00 75.17  ? 191 LYS B N     1 
ATOM   3594 C CA    . LYS B 1 219 ? 44.372  -5.532  -0.321  1.00 74.44  ? 191 LYS B CA    1 
ATOM   3595 C C     . LYS B 1 219 ? 43.397  -6.576  0.208   1.00 78.71  ? 191 LYS B C     1 
ATOM   3596 O O     . LYS B 1 219 ? 42.190  -6.440  -0.017  1.00 77.49  ? 191 LYS B O     1 
ATOM   3597 C CB    . LYS B 1 219 ? 44.467  -5.628  -1.847  1.00 70.97  ? 191 LYS B CB    1 
ATOM   3598 C CG    . LYS B 1 219 ? 45.012  -4.365  -2.500  1.00 71.13  ? 191 LYS B CG    1 
ATOM   3599 C CD    . LYS B 1 219 ? 44.965  -4.441  -4.017  1.00 75.67  ? 191 LYS B CD    1 
ATOM   3600 C CE    . LYS B 1 219 ? 45.440  -3.136  -4.641  1.00 83.70  ? 191 LYS B CE    1 
ATOM   3601 N NZ    . LYS B 1 219 ? 45.469  -3.196  -6.128  1.00 85.35  ? 191 LYS B NZ    1 
ATOM   3602 N N     . PHE B 1 220 ? 43.885  -7.603  0.904   1.00 73.93  ? 192 PHE B N     1 
ATOM   3603 C CA    . PHE B 1 220 ? 43.034  -8.572  1.580   1.00 70.37  ? 192 PHE B CA    1 
ATOM   3604 C C     . PHE B 1 220 ? 42.848  -8.251  3.057   1.00 63.91  ? 192 PHE B C     1 
ATOM   3605 O O     . PHE B 1 220 ? 42.291  -9.070  3.795   1.00 64.77  ? 192 PHE B O     1 
ATOM   3606 C CB    . PHE B 1 220 ? 43.606  -9.983  1.426   1.00 69.04  ? 192 PHE B CB    1 
ATOM   3607 C CG    . PHE B 1 220 ? 43.428  -10.567 0.054   1.00 69.53  ? 192 PHE B CG    1 
ATOM   3608 C CD1   . PHE B 1 220 ? 44.261  -10.196 -0.988  1.00 74.71  ? 192 PHE B CD1   1 
ATOM   3609 C CD2   . PHE B 1 220 ? 42.432  -11.498 -0.190  1.00 73.42  ? 192 PHE B CD2   1 
ATOM   3610 C CE1   . PHE B 1 220 ? 44.099  -10.739 -2.250  1.00 78.95  ? 192 PHE B CE1   1 
ATOM   3611 C CE2   . PHE B 1 220 ? 42.265  -12.043 -1.449  1.00 72.84  ? 192 PHE B CE2   1 
ATOM   3612 C CZ    . PHE B 1 220 ? 43.099  -11.664 -2.480  1.00 75.54  ? 192 PHE B CZ    1 
ATOM   3613 N N     . VAL B 1 221 ? 43.302  -7.083  3.502   1.00 60.61  ? 193 VAL B N     1 
ATOM   3614 C CA    . VAL B 1 221 ? 43.214  -6.667  4.895   1.00 54.52  ? 193 VAL B CA    1 
ATOM   3615 C C     . VAL B 1 221 ? 42.297  -5.455  4.980   1.00 58.46  ? 193 VAL B C     1 
ATOM   3616 O O     . VAL B 1 221 ? 42.287  -4.611  4.076   1.00 64.12  ? 193 VAL B O     1 
ATOM   3617 C CB    . VAL B 1 221 ? 44.610  -6.350  5.473   1.00 55.11  ? 193 VAL B CB    1 
ATOM   3618 C CG1   . VAL B 1 221 ? 44.511  -5.852  6.902   1.00 54.67  ? 193 VAL B CG1   1 
ATOM   3619 C CG2   . VAL B 1 221 ? 45.496  -7.581  5.408   1.00 64.39  ? 193 VAL B CG2   1 
ATOM   3620 N N     . SER B 1 222 ? 41.515  -5.384  6.053   1.00 56.45  ? 194 SER B N     1 
ATOM   3621 C CA    . SER B 1 222 ? 40.654  -4.233  6.272   1.00 52.43  ? 194 SER B CA    1 
ATOM   3622 C C     . SER B 1 222 ? 41.493  -2.959  6.333   1.00 54.10  ? 194 SER B C     1 
ATOM   3623 O O     . SER B 1 222 ? 42.569  -2.954  6.943   1.00 57.20  ? 194 SER B O     1 
ATOM   3624 C CB    . SER B 1 222 ? 39.857  -4.401  7.566   1.00 51.70  ? 194 SER B CB    1 
ATOM   3625 O OG    . SER B 1 222 ? 39.265  -3.178  7.967   1.00 55.77  ? 194 SER B OG    1 
ATOM   3626 N N     . PRO B 1 223 ? 41.042  -1.866  5.711   1.00 54.30  ? 195 PRO B N     1 
ATOM   3627 C CA    . PRO B 1 223 ? 41.846  -0.634  5.740   1.00 57.70  ? 195 PRO B CA    1 
ATOM   3628 C C     . PRO B 1 223 ? 41.960  -0.030  7.127   1.00 56.84  ? 195 PRO B C     1 
ATOM   3629 O O     . PRO B 1 223 ? 42.936  0.678   7.404   1.00 61.51  ? 195 PRO B O     1 
ATOM   3630 C CB    . PRO B 1 223 ? 41.102  0.299   4.776   1.00 53.94  ? 195 PRO B CB    1 
ATOM   3631 C CG    . PRO B 1 223 ? 39.709  -0.221  4.729   1.00 51.41  ? 195 PRO B CG    1 
ATOM   3632 C CD    . PRO B 1 223 ? 39.768  -1.697  4.992   1.00 49.36  ? 195 PRO B CD    1 
ATOM   3633 N N     . TYR B 1 224 ? 40.994  -0.288  8.008   1.00 53.13  ? 196 TYR B N     1 
ATOM   3634 C CA    . TYR B 1 224 ? 41.026  0.203   9.377   1.00 55.51  ? 196 TYR B CA    1 
ATOM   3635 C C     . TYR B 1 224 ? 41.694  -0.779  10.331  1.00 66.51  ? 196 TYR B C     1 
ATOM   3636 O O     . TYR B 1 224 ? 41.517  -0.666  11.550  1.00 68.94  ? 196 TYR B O     1 
ATOM   3637 C CB    . TYR B 1 224 ? 39.605  0.524   9.845   1.00 52.93  ? 196 TYR B CB    1 
ATOM   3638 C CG    . TYR B 1 224 ? 38.821  1.327   8.835   1.00 53.02  ? 196 TYR B CG    1 
ATOM   3639 C CD1   . TYR B 1 224 ? 39.051  2.686   8.670   1.00 60.77  ? 196 TYR B CD1   1 
ATOM   3640 C CD2   . TYR B 1 224 ? 37.864  0.722   8.030   1.00 50.66  ? 196 TYR B CD2   1 
ATOM   3641 C CE1   . TYR B 1 224 ? 38.342  3.424   7.741   1.00 55.83  ? 196 TYR B CE1   1 
ATOM   3642 C CE2   . TYR B 1 224 ? 37.152  1.451   7.098   1.00 51.14  ? 196 TYR B CE2   1 
ATOM   3643 C CZ    . TYR B 1 224 ? 37.394  2.801   6.958   1.00 51.31  ? 196 TYR B CZ    1 
ATOM   3644 O OH    . TYR B 1 224 ? 36.687  3.530   6.032   1.00 50.41  ? 196 TYR B OH    1 
ATOM   3645 N N     . GLN B 1 225 ? 42.454  -1.739  9.799   1.00 65.80  ? 197 GLN B N     1 
ATOM   3646 C CA    . GLN B 1 225 ? 43.149  -2.707  10.641  1.00 66.69  ? 197 GLN B CA    1 
ATOM   3647 C C     . GLN B 1 225 ? 44.186  -2.020  11.519  1.00 71.75  ? 197 GLN B C     1 
ATOM   3648 O O     . GLN B 1 225 ? 44.127  -2.091  12.752  1.00 74.37  ? 197 GLN B O     1 
ATOM   3649 C CB    . GLN B 1 225 ? 43.808  -3.775  9.767   1.00 63.52  ? 197 GLN B CB    1 
ATOM   3650 C CG    . GLN B 1 225 ? 44.537  -4.859  10.541  1.00 64.87  ? 197 GLN B CG    1 
ATOM   3651 C CD    . GLN B 1 225 ? 43.589  -5.786  11.273  1.00 67.66  ? 197 GLN B CD    1 
ATOM   3652 O OE1   . GLN B 1 225 ? 42.453  -5.992  10.848  1.00 65.57  ? 197 GLN B OE1   1 
ATOM   3653 N NE2   . GLN B 1 225 ? 44.050  -6.347  12.384  1.00 70.85  ? 197 GLN B NE2   1 
ATOM   3654 N N     . HIS B 1 226 ? 45.151  -1.346  10.894  1.00 70.52  ? 198 HIS B N     1 
ATOM   3655 C CA    . HIS B 1 226 ? 46.211  -0.647  11.605  1.00 70.19  ? 198 HIS B CA    1 
ATOM   3656 C C     . HIS B 1 226 ? 45.830  0.784   11.964  1.00 71.43  ? 198 HIS B C     1 
ATOM   3657 O O     . HIS B 1 226 ? 46.709  1.584   12.303  1.00 75.67  ? 198 HIS B O     1 
ATOM   3658 C CB    . HIS B 1 226 ? 47.496  -0.659  10.774  1.00 68.12  ? 198 HIS B CB    1 
ATOM   3659 C CG    . HIS B 1 226 ? 47.896  -2.022  10.303  1.00 70.62  ? 198 HIS B CG    1 
ATOM   3660 N ND1   . HIS B 1 226 ? 48.176  -3.057  11.170  1.00 73.56  ? 198 HIS B ND1   1 
ATOM   3661 C CD2   . HIS B 1 226 ? 48.058  -2.522  9.055   1.00 70.27  ? 198 HIS B CD2   1 
ATOM   3662 C CE1   . HIS B 1 226 ? 48.494  -4.135  10.476  1.00 74.02  ? 198 HIS B CE1   1 
ATOM   3663 N NE2   . HIS B 1 226 ? 48.431  -3.837  9.191   1.00 72.28  ? 198 HIS B NE2   1 
ATOM   3664 N N     . SER B 1 227 ? 44.545  1.121   11.895  1.00 71.93  ? 199 SER B N     1 
ATOM   3665 C CA    . SER B 1 227 ? 44.103  2.465   12.238  1.00 73.69  ? 199 SER B CA    1 
ATOM   3666 C C     . SER B 1 227 ? 44.131  2.661   13.749  1.00 77.64  ? 199 SER B C     1 
ATOM   3667 O O     . SER B 1 227 ? 43.618  1.830   14.504  1.00 77.19  ? 199 SER B O     1 
ATOM   3668 C CB    . SER B 1 227 ? 42.696  2.714   11.698  1.00 71.97  ? 199 SER B CB    1 
ATOM   3669 O OG    . SER B 1 227 ? 42.182  3.951   12.161  1.00 71.76  ? 199 SER B OG    1 
ATOM   3670 N N     . GLU B 1 228 ? 44.739  3.764   14.189  1.00 79.07  ? 200 GLU B N     1 
ATOM   3671 C CA    . GLU B 1 228 ? 44.744  4.102   15.607  1.00 77.80  ? 200 GLU B CA    1 
ATOM   3672 C C     . GLU B 1 228 ? 43.412  4.673   16.071  1.00 78.86  ? 200 GLU B C     1 
ATOM   3673 O O     . GLU B 1 228 ? 43.142  4.683   17.277  1.00 77.93  ? 200 GLU B O     1 
ATOM   3674 C CB    . GLU B 1 228 ? 45.868  5.097   15.909  1.00 70.85  ? 200 GLU B CB    1 
ATOM   3675 N N     . ASP B 1 229 ? 42.579  5.144   15.145  1.00 71.06  ? 201 ASP B N     1 
ATOM   3676 C CA    . ASP B 1 229 ? 41.252  5.666   15.477  1.00 67.33  ? 201 ASP B CA    1 
ATOM   3677 C C     . ASP B 1 229 ? 40.305  5.328   14.337  1.00 66.06  ? 201 ASP B C     1 
ATOM   3678 O O     . ASP B 1 229 ? 40.046  6.151   13.451  1.00 66.97  ? 201 ASP B O     1 
ATOM   3679 C CB    . ASP B 1 229 ? 41.295  7.174   15.727  1.00 68.34  ? 201 ASP B CB    1 
ATOM   3680 C CG    . ASP B 1 229 ? 39.941  7.742   16.108  1.00 71.98  ? 201 ASP B CG    1 
ATOM   3681 O OD1   . ASP B 1 229 ? 39.083  6.971   16.588  1.00 72.05  ? 201 ASP B OD1   1 
ATOM   3682 O OD2   . ASP B 1 229 ? 39.734  8.960   15.927  1.00 75.22  ? 201 ASP B OD2   1 
ATOM   3683 N N     . PRO B 1 230 ? 39.771  4.102   14.321  1.00 61.78  ? 202 PRO B N     1 
ATOM   3684 C CA    . PRO B 1 230 ? 38.877  3.715   13.215  1.00 58.88  ? 202 PRO B CA    1 
ATOM   3685 C C     . PRO B 1 230 ? 37.599  4.533   13.155  1.00 56.13  ? 202 PRO B C     1 
ATOM   3686 O O     . PRO B 1 230 ? 37.117  4.839   12.056  1.00 56.85  ? 202 PRO B O     1 
ATOM   3687 C CB    . PRO B 1 230 ? 38.589  2.233   13.500  1.00 62.02  ? 202 PRO B CB    1 
ATOM   3688 C CG    . PRO B 1 230 ? 39.685  1.782   14.407  1.00 62.26  ? 202 PRO B CG    1 
ATOM   3689 C CD    . PRO B 1 230 ? 40.075  2.976   15.219  1.00 65.92  ? 202 PRO B CD    1 
ATOM   3690 N N     . VAL B 1 231 ? 37.032  4.895   14.308  1.00 57.63  ? 203 VAL B N     1 
ATOM   3691 C CA    . VAL B 1 231 ? 35.804  5.686   14.320  1.00 56.93  ? 203 VAL B CA    1 
ATOM   3692 C C     . VAL B 1 231 ? 36.050  7.060   13.710  1.00 55.89  ? 203 VAL B C     1 
ATOM   3693 O O     . VAL B 1 231 ? 35.214  7.584   12.963  1.00 57.73  ? 203 VAL B O     1 
ATOM   3694 C CB    . VAL B 1 231 ? 35.251  5.791   15.754  1.00 60.22  ? 203 VAL B CB    1 
ATOM   3695 C CG1   . VAL B 1 231 ? 34.116  6.803   15.822  1.00 56.78  ? 203 VAL B CG1   1 
ATOM   3696 C CG2   . VAL B 1 231 ? 34.778  4.432   16.234  1.00 56.62  ? 203 VAL B CG2   1 
ATOM   3697 N N     . GLY B 1 232 ? 37.203  7.660   14.007  1.00 59.35  ? 204 GLY B N     1 
ATOM   3698 C CA    . GLY B 1 232 ? 37.511  8.963   13.442  1.00 59.69  ? 204 GLY B CA    1 
ATOM   3699 C C     . GLY B 1 232 ? 37.717  8.917   11.940  1.00 58.64  ? 204 GLY B C     1 
ATOM   3700 O O     . GLY B 1 232 ? 37.230  9.786   11.211  1.00 57.04  ? 204 GLY B O     1 
ATOM   3701 N N     . GLU B 1 233 ? 38.438  7.903   11.454  1.00 60.13  ? 205 GLU B N     1 
ATOM   3702 C CA    . GLU B 1 233 ? 38.681  7.794   10.019  1.00 60.04  ? 205 GLU B CA    1 
ATOM   3703 C C     . GLU B 1 233 ? 37.395  7.506   9.257   1.00 57.21  ? 205 GLU B C     1 
ATOM   3704 O O     . GLU B 1 233 ? 37.179  8.050   8.167   1.00 55.63  ? 205 GLU B O     1 
ATOM   3705 C CB    . GLU B 1 233 ? 39.722  6.711   9.738   1.00 57.02  ? 205 GLU B CB    1 
ATOM   3706 C CG    . GLU B 1 233 ? 41.140  7.093   10.126  1.00 64.58  ? 205 GLU B CG    1 
ATOM   3707 C CD    . GLU B 1 233 ? 42.170  6.102   9.618   1.00 73.46  ? 205 GLU B CD    1 
ATOM   3708 O OE1   . GLU B 1 233 ? 41.852  5.345   8.676   1.00 75.87  ? 205 GLU B OE1   1 
ATOM   3709 O OE2   . GLU B 1 233 ? 43.296  6.080   10.159  1.00 73.70  ? 205 GLU B OE2   1 
ATOM   3710 N N     . PHE B 1 234 ? 36.526  6.656   9.809   1.00 53.15  ? 206 PHE B N     1 
ATOM   3711 C CA    . PHE B 1 234 ? 35.288  6.330   9.110   1.00 50.77  ? 206 PHE B CA    1 
ATOM   3712 C C     . PHE B 1 234 ? 34.306  7.494   9.147   1.00 54.61  ? 206 PHE B C     1 
ATOM   3713 O O     . PHE B 1 234 ? 33.586  7.732   8.171   1.00 57.77  ? 206 PHE B O     1 
ATOM   3714 C CB    . PHE B 1 234 ? 34.653  5.074   9.703   1.00 49.88  ? 206 PHE B CB    1 
ATOM   3715 C CG    . PHE B 1 234 ? 33.602  4.462   8.823   1.00 48.71  ? 206 PHE B CG    1 
ATOM   3716 C CD1   . PHE B 1 234 ? 33.905  4.085   7.525   1.00 47.98  ? 206 PHE B CD1   1 
ATOM   3717 C CD2   . PHE B 1 234 ? 32.310  4.276   9.285   1.00 45.40  ? 206 PHE B CD2   1 
ATOM   3718 C CE1   . PHE B 1 234 ? 32.942  3.526   6.707   1.00 42.01  ? 206 PHE B CE1   1 
ATOM   3719 C CE2   . PHE B 1 234 ? 31.343  3.717   8.470   1.00 40.30  ? 206 PHE B CE2   1 
ATOM   3720 C CZ    . PHE B 1 234 ? 31.659  3.343   7.180   1.00 39.43  ? 206 PHE B CZ    1 
ATOM   3721 N N     . ARG B 1 235 ? 34.256  8.226   10.263  1.00 55.32  ? 207 ARG B N     1 
ATOM   3722 C CA    . ARG B 1 235 ? 33.400  9.408   10.321  1.00 56.81  ? 207 ARG B CA    1 
ATOM   3723 C C     . ARG B 1 235 ? 33.867  10.469  9.333   1.00 56.54  ? 207 ARG B C     1 
ATOM   3724 O O     . ARG B 1 235 ? 33.046  11.141  8.697   1.00 55.65  ? 207 ARG B O     1 
ATOM   3725 C CB    . ARG B 1 235 ? 33.365  9.976   11.740  1.00 56.92  ? 207 ARG B CB    1 
ATOM   3726 C CG    . ARG B 1 235 ? 32.517  11.236  11.866  1.00 57.31  ? 207 ARG B CG    1 
ATOM   3727 C CD    . ARG B 1 235 ? 32.450  11.758  13.294  1.00 61.48  ? 207 ARG B CD    1 
ATOM   3728 N NE    . ARG B 1 235 ? 31.398  11.113  14.071  1.00 68.31  ? 207 ARG B NE    1 
ATOM   3729 C CZ    . ARG B 1 235 ? 31.590  10.494  15.228  1.00 71.17  ? 207 ARG B CZ    1 
ATOM   3730 N NH1   . ARG B 1 235 ? 32.790  10.422  15.783  1.00 73.25  ? 207 ARG B NH1   1 
ATOM   3731 N NH2   . ARG B 1 235 ? 30.552  9.940   15.848  1.00 64.96  ? 207 ARG B NH2   1 
ATOM   3732 N N     . LEU B 1 236 ? 35.184  10.629  9.184   1.00 56.02  ? 208 LEU B N     1 
ATOM   3733 C CA    . LEU B 1 236 ? 35.703  11.590  8.217   1.00 54.06  ? 208 LEU B CA    1 
ATOM   3734 C C     . LEU B 1 236 ? 35.435  11.135  6.788   1.00 53.40  ? 208 LEU B C     1 
ATOM   3735 O O     . LEU B 1 236 ? 35.092  11.952  5.926   1.00 54.08  ? 208 LEU B O     1 
ATOM   3736 C CB    . LEU B 1 236 ? 37.199  11.805  8.437   1.00 50.64  ? 208 LEU B CB    1 
ATOM   3737 C CG    . LEU B 1 236 ? 37.869  12.765  7.452   1.00 52.53  ? 208 LEU B CG    1 
ATOM   3738 C CD1   . LEU B 1 236 ? 37.233  14.145  7.535   1.00 52.85  ? 208 LEU B CD1   1 
ATOM   3739 C CD2   . LEU B 1 236 ? 39.368  12.843  7.694   1.00 56.07  ? 208 LEU B CD2   1 
ATOM   3740 N N     . LEU B 1 237 ? 35.584  9.835   6.520   1.00 52.48  ? 209 LEU B N     1 
ATOM   3741 C CA    . LEU B 1 237 ? 35.387  9.332   5.164   1.00 49.97  ? 209 LEU B CA    1 
ATOM   3742 C C     . LEU B 1 237 ? 33.948  9.525   4.705   1.00 49.92  ? 209 LEU B C     1 
ATOM   3743 O O     . LEU B 1 237 ? 33.701  9.893   3.550   1.00 53.41  ? 209 LEU B O     1 
ATOM   3744 C CB    . LEU B 1 237 ? 35.779  7.858   5.087   1.00 50.20  ? 209 LEU B CB    1 
ATOM   3745 C CG    . LEU B 1 237 ? 35.552  7.198   3.726   1.00 45.86  ? 209 LEU B CG    1 
ATOM   3746 C CD1   . LEU B 1 237 ? 36.428  7.851   2.671   1.00 50.48  ? 209 LEU B CD1   1 
ATOM   3747 C CD2   . LEU B 1 237 ? 35.812  5.702   3.793   1.00 44.46  ? 209 LEU B CD2   1 
ATOM   3748 N N     . LEU B 1 238 ? 32.983  9.282   5.594   1.00 49.35  ? 210 LEU B N     1 
ATOM   3749 C CA    . LEU B 1 238 ? 31.584  9.481   5.231   1.00 50.24  ? 210 LEU B CA    1 
ATOM   3750 C C     . LEU B 1 238 ? 31.278  10.956  5.005   1.00 54.66  ? 210 LEU B C     1 
ATOM   3751 O O     . LEU B 1 238 ? 30.620  11.315  4.022   1.00 58.10  ? 210 LEU B O     1 
ATOM   3752 C CB    . LEU B 1 238 ? 30.673  8.902   6.313   1.00 49.90  ? 210 LEU B CB    1 
ATOM   3753 C CG    . LEU B 1 238 ? 30.666  7.378   6.453   1.00 45.22  ? 210 LEU B CG    1 
ATOM   3754 C CD1   . LEU B 1 238 ? 29.688  6.942   7.533   1.00 37.54  ? 210 LEU B CD1   1 
ATOM   3755 C CD2   . LEU B 1 238 ? 30.336  6.719   5.123   1.00 44.03  ? 210 LEU B CD2   1 
ATOM   3756 N N     . GLU B 1 239 ? 31.755  11.825  5.899   1.00 56.05  ? 211 GLU B N     1 
ATOM   3757 C CA    . GLU B 1 239 ? 31.480  13.251  5.761   1.00 54.77  ? 211 GLU B CA    1 
ATOM   3758 C C     . GLU B 1 239 ? 32.190  13.851  4.554   1.00 51.32  ? 211 GLU B C     1 
ATOM   3759 O O     . GLU B 1 239 ? 31.709  14.835  3.981   1.00 50.31  ? 211 GLU B O     1 
ATOM   3760 C CB    . GLU B 1 239 ? 31.881  13.985  7.040   1.00 56.37  ? 211 GLU B CB    1 
ATOM   3761 C CG    . GLU B 1 239 ? 30.996  13.662  8.234   1.00 60.46  ? 211 GLU B CG    1 
ATOM   3762 C CD    . GLU B 1 239 ? 31.614  14.080  9.555   1.00 69.49  ? 211 GLU B CD    1 
ATOM   3763 O OE1   . GLU B 1 239 ? 32.822  14.399  9.572   1.00 68.43  ? 211 GLU B OE1   1 
ATOM   3764 O OE2   . GLU B 1 239 ? 30.893  14.086  10.575  1.00 69.07  ? 211 GLU B OE2   1 
ATOM   3765 N N     . SER B 1 240 ? 33.326  13.277  4.150   1.00 50.74  ? 212 SER B N     1 
ATOM   3766 C CA    . SER B 1 240 ? 34.039  13.770  2.978   1.00 51.56  ? 212 SER B CA    1 
ATOM   3767 C C     . SER B 1 240 ? 33.337  13.424  1.672   1.00 52.36  ? 212 SER B C     1 
ATOM   3768 O O     . SER B 1 240 ? 33.730  13.946  0.623   1.00 59.58  ? 212 SER B O     1 
ATOM   3769 C CB    . SER B 1 240 ? 35.465  13.217  2.957   1.00 54.59  ? 212 SER B CB    1 
ATOM   3770 O OG    . SER B 1 240 ? 35.474  11.834  2.645   1.00 56.70  ? 212 SER B OG    1 
ATOM   3771 N N     . GLU B 1 241 ? 32.319  12.566  1.708   1.00 53.20  ? 213 GLU B N     1 
ATOM   3772 C CA    . GLU B 1 241 ? 31.566  12.188  0.520   1.00 54.01  ? 213 GLU B CA    1 
ATOM   3773 C C     . GLU B 1 241 ? 30.133  12.703  0.549   1.00 54.82  ? 213 GLU B C     1 
ATOM   3774 O O     . GLU B 1 241 ? 29.303  12.244  -0.244  1.00 52.71  ? 213 GLU B O     1 
ATOM   3775 C CB    . GLU B 1 241 ? 31.579  10.668  0.348   1.00 53.57  ? 213 GLU B CB    1 
ATOM   3776 C CG    . GLU B 1 241 ? 32.937  10.108  -0.042  1.00 56.09  ? 213 GLU B CG    1 
ATOM   3777 C CD    . GLU B 1 241 ? 33.428  10.655  -1.368  1.00 68.52  ? 213 GLU B CD    1 
ATOM   3778 O OE1   . GLU B 1 241 ? 32.615  10.748  -2.312  1.00 67.96  ? 213 GLU B OE1   1 
ATOM   3779 O OE2   . GLU B 1 241 ? 34.625  10.998  -1.467  1.00 73.50  ? 213 GLU B OE2   1 
ATOM   3780 N N     . GLY B 1 242 ? 29.822  13.640  1.442   1.00 58.41  ? 214 GLY B N     1 
ATOM   3781 C CA    . GLY B 1 242 ? 28.504  14.244  1.484   1.00 59.83  ? 214 GLY B CA    1 
ATOM   3782 C C     . GLY B 1 242 ? 27.507  13.497  2.346   1.00 59.01  ? 214 GLY B C     1 
ATOM   3783 O O     . GLY B 1 242 ? 26.333  13.379  1.982   1.00 58.87  ? 214 GLY B O     1 
ATOM   3784 N N     . PHE B 1 243 ? 27.957  12.993  3.492   1.00 55.12  ? 215 PHE B N     1 
ATOM   3785 C CA    . PHE B 1 243 ? 27.099  12.269  4.416   1.00 50.38  ? 215 PHE B CA    1 
ATOM   3786 C C     . PHE B 1 243 ? 27.087  12.962  5.770   1.00 49.43  ? 215 PHE B C     1 
ATOM   3787 O O     . PHE B 1 243 ? 28.073  13.582  6.180   1.00 51.63  ? 215 PHE B O     1 
ATOM   3788 C CB    . PHE B 1 243 ? 27.558  10.815  4.589   1.00 47.06  ? 215 PHE B CB    1 
ATOM   3789 C CG    . PHE B 1 243 ? 27.144  9.910   3.467   1.00 45.09  ? 215 PHE B CG    1 
ATOM   3790 C CD1   . PHE B 1 243 ? 25.882  9.342   3.447   1.00 44.08  ? 215 PHE B CD1   1 
ATOM   3791 C CD2   . PHE B 1 243 ? 28.019  9.621   2.434   1.00 49.48  ? 215 PHE B CD2   1 
ATOM   3792 C CE1   . PHE B 1 243 ? 25.498  8.506   2.416   1.00 42.23  ? 215 PHE B CE1   1 
ATOM   3793 C CE2   . PHE B 1 243 ? 27.642  8.785   1.400   1.00 48.67  ? 215 PHE B CE2   1 
ATOM   3794 C CZ    . PHE B 1 243 ? 26.379  8.227   1.391   1.00 41.37  ? 215 PHE B CZ    1 
ATOM   3795 N N     . GLN B 1 244 ? 25.954  12.853  6.460   1.00 49.34  ? 216 GLN B N     1 
ATOM   3796 C CA    . GLN B 1 244 ? 25.801  13.359  7.819   1.00 50.97  ? 216 GLN B CA    1 
ATOM   3797 C C     . GLN B 1 244 ? 25.871  12.174  8.774   1.00 49.48  ? 216 GLN B C     1 
ATOM   3798 O O     . GLN B 1 244 ? 24.924  11.386  8.867   1.00 48.13  ? 216 GLN B O     1 
ATOM   3799 C CB    . GLN B 1 244 ? 24.485  14.117  7.977   1.00 54.56  ? 216 GLN B CB    1 
ATOM   3800 C CG    . GLN B 1 244 ? 24.252  14.663  9.378   1.00 59.64  ? 216 GLN B CG    1 
ATOM   3801 C CD    . GLN B 1 244 ? 22.844  15.193  9.573   1.00 60.10  ? 216 GLN B CD    1 
ATOM   3802 O OE1   . GLN B 1 244 ? 21.923  14.822  8.846   1.00 62.61  ? 216 GLN B OE1   1 
ATOM   3803 N NE2   . GLN B 1 244 ? 22.671  16.062  10.561  1.00 57.22  ? 216 GLN B NE2   1 
ATOM   3804 N N     . VAL B 1 245 ? 26.993  12.045  9.478   1.00 47.80  ? 217 VAL B N     1 
ATOM   3805 C CA    . VAL B 1 245 ? 27.192  10.928  10.396  1.00 48.01  ? 217 VAL B CA    1 
ATOM   3806 C C     . VAL B 1 245 ? 26.314  11.155  11.624  1.00 49.17  ? 217 VAL B C     1 
ATOM   3807 O O     . VAL B 1 245 ? 26.604  12.018  12.457  1.00 51.98  ? 217 VAL B O     1 
ATOM   3808 C CB    . VAL B 1 245 ? 28.666  10.773  10.785  1.00 50.79  ? 217 VAL B CB    1 
ATOM   3809 C CG1   . VAL B 1 245 ? 28.829  9.663   11.813  1.00 51.38  ? 217 VAL B CG1   1 
ATOM   3810 C CG2   . VAL B 1 245 ? 29.511  10.490  9.552   1.00 49.71  ? 217 VAL B CG2   1 
ATOM   3811 N N     . LEU B 1 246 ? 25.234  10.378  11.737  1.00 52.02  ? 218 LEU B N     1 
ATOM   3812 C CA    . LEU B 1 246 ? 24.325  10.522  12.868  1.00 44.88  ? 218 LEU B CA    1 
ATOM   3813 C C     . LEU B 1 246 ? 24.808  9.762   14.095  1.00 44.30  ? 218 LEU B C     1 
ATOM   3814 O O     . LEU B 1 246 ? 24.536  10.184  15.224  1.00 52.48  ? 218 LEU B O     1 
ATOM   3815 C CB    . LEU B 1 246 ? 22.925  10.043  12.481  1.00 40.85  ? 218 LEU B CB    1 
ATOM   3816 C CG    . LEU B 1 246 ? 22.248  10.755  11.309  1.00 47.69  ? 218 LEU B CG    1 
ATOM   3817 C CD1   . LEU B 1 246 ? 20.883  10.143  11.030  1.00 50.66  ? 218 LEU B CD1   1 
ATOM   3818 C CD2   . LEU B 1 246 ? 22.123  12.245  11.586  1.00 52.95  ? 218 LEU B CD2   1 
ATOM   3819 N N     . ARG B 1 247 ? 25.521  8.655   13.902  1.00 46.70  ? 219 ARG B N     1 
ATOM   3820 C CA    . ARG B 1 247 ? 25.956  7.824   15.014  1.00 46.62  ? 219 ARG B CA    1 
ATOM   3821 C C     . ARG B 1 247 ? 27.110  6.951   14.542  1.00 48.45  ? 219 ARG B C     1 
ATOM   3822 O O     . ARG B 1 247 ? 27.096  6.458   13.412  1.00 43.97  ? 219 ARG B O     1 
ATOM   3823 C CB    . ARG B 1 247 ? 24.797  6.970   15.540  1.00 49.27  ? 219 ARG B CB    1 
ATOM   3824 C CG    . ARG B 1 247 ? 25.086  6.217   16.824  1.00 61.36  ? 219 ARG B CG    1 
ATOM   3825 C CD    . ARG B 1 247 ? 23.808  5.601   17.369  1.00 67.30  ? 219 ARG B CD    1 
ATOM   3826 N NE    . ARG B 1 247 ? 24.045  4.743   18.523  1.00 74.64  ? 219 ARG B NE    1 
ATOM   3827 C CZ    . ARG B 1 247 ? 23.216  4.632   19.552  1.00 72.03  ? 219 ARG B CZ    1 
ATOM   3828 N NH1   . ARG B 1 247 ? 22.088  5.321   19.609  1.00 73.09  ? 219 ARG B NH1   1 
ATOM   3829 N NH2   . ARG B 1 247 ? 23.528  3.810   20.551  1.00 67.64  ? 219 ARG B NH2   1 
ATOM   3830 N N     . CYS B 1 248 ? 28.107  6.771   15.409  1.00 51.17  ? 220 CYS B N     1 
ATOM   3831 C CA    . CYS B 1 248 ? 29.321  6.052   15.025  1.00 51.08  ? 220 CYS B CA    1 
ATOM   3832 C C     . CYS B 1 248 ? 30.018  5.569   16.291  1.00 55.58  ? 220 CYS B C     1 
ATOM   3833 O O     . CYS B 1 248 ? 30.515  6.387   17.071  1.00 58.74  ? 220 CYS B O     1 
ATOM   3834 C CB    . CYS B 1 248 ? 30.235  6.949   14.199  1.00 48.83  ? 220 CYS B CB    1 
ATOM   3835 S SG    . CYS B 1 248 ? 31.579  6.090   13.354  1.00 59.01  ? 220 CYS B SG    1 
ATOM   3836 N N     . ASP B 1 249 ? 30.059  4.251   16.488  1.00 54.73  ? 221 ASP B N     1 
ATOM   3837 C CA    . ASP B 1 249 ? 30.677  3.655   17.663  1.00 52.40  ? 221 ASP B CA    1 
ATOM   3838 C C     . ASP B 1 249 ? 31.515  2.455   17.240  1.00 48.58  ? 221 ASP B C     1 
ATOM   3839 O O     . ASP B 1 249 ? 31.401  1.951   16.120  1.00 50.71  ? 221 ASP B O     1 
ATOM   3840 C CB    . ASP B 1 249 ? 29.629  3.231   18.700  1.00 57.54  ? 221 ASP B CB    1 
ATOM   3841 C CG    . ASP B 1 249 ? 28.635  4.334   19.010  1.00 61.60  ? 221 ASP B CG    1 
ATOM   3842 O OD1   . ASP B 1 249 ? 29.049  5.368   19.574  1.00 64.16  ? 221 ASP B OD1   1 
ATOM   3843 O OD2   . ASP B 1 249 ? 27.439  4.165   18.688  1.00 59.76  ? 221 ASP B OD2   1 
ATOM   3844 N N     . LEU B 1 250 ? 32.363  1.996   18.160  1.00 44.06  ? 222 LEU B N     1 
ATOM   3845 C CA    . LEU B 1 250 ? 33.207  0.827   17.950  1.00 41.85  ? 222 LEU B CA    1 
ATOM   3846 C C     . LEU B 1 250 ? 33.066  -0.107  19.141  1.00 42.53  ? 222 LEU B C     1 
ATOM   3847 O O     . LEU B 1 250 ? 33.144  0.335   20.292  1.00 46.31  ? 222 LEU B O     1 
ATOM   3848 C CB    . LEU B 1 250 ? 34.676  1.224   17.761  1.00 43.10  ? 222 LEU B CB    1 
ATOM   3849 C CG    . LEU B 1 250 ? 35.701  0.090   17.672  1.00 44.23  ? 222 LEU B CG    1 
ATOM   3850 C CD1   . LEU B 1 250 ? 35.463  -0.766  16.439  1.00 44.61  ? 222 LEU B CD1   1 
ATOM   3851 C CD2   . LEU B 1 250 ? 37.116  0.647   17.672  1.00 45.54  ? 222 LEU B CD2   1 
ATOM   3852 N N     . GLY B 1 251 ? 32.861  -1.392  18.864  1.00 44.94  ? 223 GLY B N     1 
ATOM   3853 C CA    . GLY B 1 251 ? 32.720  -2.383  19.903  1.00 44.52  ? 223 GLY B CA    1 
ATOM   3854 C C     . GLY B 1 251 ? 33.090  -3.773  19.428  1.00 45.30  ? 223 GLY B C     1 
ATOM   3855 O O     . GLY B 1 251 ? 33.074  -4.071  18.229  1.00 48.07  ? 223 GLY B O     1 
ATOM   3856 N N     . PRO B 1 252 ? 33.436  -4.653  20.362  1.00 43.80  ? 224 PRO B N     1 
ATOM   3857 C CA    . PRO B 1 252 ? 33.790  -6.025  19.994  1.00 45.06  ? 224 PRO B CA    1 
ATOM   3858 C C     . PRO B 1 252 ? 32.556  -6.888  19.775  1.00 46.73  ? 224 PRO B C     1 
ATOM   3859 O O     . PRO B 1 252 ? 31.458  -6.592  20.249  1.00 46.21  ? 224 PRO B O     1 
ATOM   3860 C CB    . PRO B 1 252 ? 34.594  -6.511  21.203  1.00 49.73  ? 224 PRO B CB    1 
ATOM   3861 C CG    . PRO B 1 252 ? 33.988  -5.768  22.348  1.00 48.51  ? 224 PRO B CG    1 
ATOM   3862 C CD    . PRO B 1 252 ? 33.577  -4.415  21.809  1.00 44.25  ? 224 PRO B CD    1 
ATOM   3863 N N     . GLN B 1 253 ? 32.760  -7.977  19.036  1.00 46.94  ? 225 GLN B N     1 
ATOM   3864 C CA    . GLN B 1 253 ? 31.692  -8.913  18.719  1.00 44.54  ? 225 GLN B CA    1 
ATOM   3865 C C     . GLN B 1 253 ? 32.220  -10.339 18.765  1.00 44.88  ? 225 GLN B C     1 
ATOM   3866 O O     . GLN B 1 253 ? 33.358  -10.602 18.366  1.00 46.12  ? 225 GLN B O     1 
ATOM   3867 C CB    . GLN B 1 253 ? 31.087  -8.635  17.334  1.00 45.84  ? 225 GLN B CB    1 
ATOM   3868 C CG    . GLN B 1 253 ? 30.384  -7.293  17.201  1.00 44.19  ? 225 GLN B CG    1 
ATOM   3869 C CD    . GLN B 1 253 ? 29.080  -7.237  17.971  1.00 51.83  ? 225 GLN B CD    1 
ATOM   3870 O OE1   . GLN B 1 253 ? 28.463  -8.266  18.245  1.00 55.69  ? 225 GLN B OE1   1 
ATOM   3871 N NE2   . GLN B 1 253 ? 28.649  -6.029  18.318  1.00 49.15  ? 225 GLN B NE2   1 
ATOM   3872 N N     . LYS B 1 254 ? 31.386  -11.250 19.256  1.00 48.21  ? 226 LYS B N     1 
ATOM   3873 C CA    . LYS B 1 254 ? 31.659  -12.678 19.230  1.00 47.71  ? 226 LYS B CA    1 
ATOM   3874 C C     . LYS B 1 254 ? 30.678  -13.362 18.287  1.00 46.12  ? 226 LYS B C     1 
ATOM   3875 O O     . LYS B 1 254 ? 29.516  -12.962 18.178  1.00 51.22  ? 226 LYS B O     1 
ATOM   3876 C CB    . LYS B 1 254 ? 31.545  -13.296 20.628  1.00 55.33  ? 226 LYS B CB    1 
ATOM   3877 C CG    . LYS B 1 254 ? 32.594  -12.833 21.626  1.00 57.22  ? 226 LYS B CG    1 
ATOM   3878 C CD    . LYS B 1 254 ? 32.438  -13.575 22.948  1.00 60.93  ? 226 LYS B CD    1 
ATOM   3879 C CE    . LYS B 1 254 ? 33.441  -13.098 23.988  1.00 63.90  ? 226 LYS B CE    1 
ATOM   3880 N NZ    . LYS B 1 254 ? 33.318  -13.864 25.260  1.00 56.93  ? 226 LYS B NZ    1 
ATOM   3881 N N     . VAL B 1 255 ? 31.153  -14.398 17.603  1.00 45.49  ? 227 VAL B N     1 
ATOM   3882 C CA    . VAL B 1 255 ? 30.325  -15.187 16.697  1.00 46.07  ? 227 VAL B CA    1 
ATOM   3883 C C     . VAL B 1 255 ? 30.251  -16.596 17.270  1.00 53.73  ? 227 VAL B C     1 
ATOM   3884 O O     . VAL B 1 255 ? 31.245  -17.334 17.257  1.00 53.68  ? 227 VAL B O     1 
ATOM   3885 C CB    . VAL B 1 255 ? 30.875  -15.199 15.265  1.00 45.49  ? 227 VAL B CB    1 
ATOM   3886 C CG1   . VAL B 1 255 ? 29.915  -15.930 14.339  1.00 46.30  ? 227 VAL B CG1   1 
ATOM   3887 C CG2   . VAL B 1 255 ? 31.123  -13.782 14.778  1.00 44.84  ? 227 VAL B CG2   1 
ATOM   3888 N N     . PHE B 1 256 ? 29.076  -16.971 17.767  1.00 53.74  ? 228 PHE B N     1 
ATOM   3889 C CA    . PHE B 1 256 ? 28.905  -18.240 18.460  1.00 51.09  ? 228 PHE B CA    1 
ATOM   3890 C C     . PHE B 1 256 ? 28.738  -19.391 17.474  1.00 53.65  ? 228 PHE B C     1 
ATOM   3891 O O     . PHE B 1 256 ? 28.104  -19.245 16.426  1.00 53.89  ? 228 PHE B O     1 
ATOM   3892 C CB    . PHE B 1 256 ? 27.693  -18.167 19.390  1.00 46.42  ? 228 PHE B CB    1 
ATOM   3893 C CG    . PHE B 1 256 ? 27.331  -19.478 20.022  1.00 50.93  ? 228 PHE B CG    1 
ATOM   3894 C CD1   . PHE B 1 256 ? 28.033  -19.952 21.116  1.00 56.36  ? 228 PHE B CD1   1 
ATOM   3895 C CD2   . PHE B 1 256 ? 26.279  -20.233 19.527  1.00 50.32  ? 228 PHE B CD2   1 
ATOM   3896 C CE1   . PHE B 1 256 ? 27.699  -21.158 21.699  1.00 61.47  ? 228 PHE B CE1   1 
ATOM   3897 C CE2   . PHE B 1 256 ? 25.941  -21.440 20.106  1.00 52.32  ? 228 PHE B CE2   1 
ATOM   3898 C CZ    . PHE B 1 256 ? 26.652  -21.903 21.194  1.00 61.48  ? 228 PHE B CZ    1 
ATOM   3899 N N     . PHE B 1 257 ? 29.317  -20.544 17.821  1.00 53.15  ? 229 PHE B N     1 
ATOM   3900 C CA    . PHE B 1 257 ? 29.144  -21.772 17.056  1.00 50.91  ? 229 PHE B CA    1 
ATOM   3901 C C     . PHE B 1 257 ? 28.940  -22.917 18.042  1.00 50.37  ? 229 PHE B C     1 
ATOM   3902 O O     . PHE B 1 257 ? 29.690  -23.023 19.030  1.00 51.33  ? 229 PHE B O     1 
ATOM   3903 C CB    . PHE B 1 257 ? 30.331  -22.066 16.136  1.00 50.06  ? 229 PHE B CB    1 
ATOM   3904 C CG    . PHE B 1 257 ? 30.513  -21.056 15.043  1.00 51.93  ? 229 PHE B CG    1 
ATOM   3905 C CD1   . PHE B 1 257 ? 31.305  -19.938 15.237  1.00 49.95  ? 229 PHE B CD1   1 
ATOM   3906 C CD2   . PHE B 1 257 ? 29.878  -21.219 13.823  1.00 53.67  ? 229 PHE B CD2   1 
ATOM   3907 C CE1   . PHE B 1 257 ? 31.470  -19.010 14.231  1.00 48.40  ? 229 PHE B CE1   1 
ATOM   3908 C CE2   . PHE B 1 257 ? 30.037  -20.292 12.813  1.00 48.20  ? 229 PHE B CE2   1 
ATOM   3909 C CZ    . PHE B 1 257 ? 30.834  -19.185 13.018  1.00 48.00  ? 229 PHE B CZ    1 
ATOM   3910 N N     . PRO B 1 258 ? 27.953  -23.780 17.812  1.00 49.60  ? 230 PRO B N     1 
ATOM   3911 C CA    . PRO B 1 258 ? 27.666  -24.850 18.776  1.00 56.70  ? 230 PRO B CA    1 
ATOM   3912 C C     . PRO B 1 258 ? 28.647  -26.010 18.704  1.00 60.20  ? 230 PRO B C     1 
ATOM   3913 O O     . PRO B 1 258 ? 29.130  -26.481 19.739  1.00 63.52  ? 230 PRO B O     1 
ATOM   3914 C CB    . PRO B 1 258 ? 26.250  -25.290 18.390  1.00 59.81  ? 230 PRO B CB    1 
ATOM   3915 C CG    . PRO B 1 258 ? 26.137  -24.964 16.940  1.00 49.57  ? 230 PRO B CG    1 
ATOM   3916 C CD    . PRO B 1 258 ? 26.970  -23.734 16.715  1.00 48.80  ? 230 PRO B CD    1 
ATOM   3917 N N     . THR B 1 259 ? 28.946  -26.484 17.498  1.00 55.67  ? 231 THR B N     1 
ATOM   3918 C CA    . THR B 1 259 ? 29.821  -27.630 17.311  1.00 55.77  ? 231 THR B CA    1 
ATOM   3919 C C     . THR B 1 259 ? 31.248  -27.163 17.040  1.00 57.06  ? 231 THR B C     1 
ATOM   3920 O O     . THR B 1 259 ? 31.541  -25.968 16.963  1.00 55.69  ? 231 THR B O     1 
ATOM   3921 C CB    . THR B 1 259 ? 29.318  -28.516 16.170  1.00 58.22  ? 231 THR B CB    1 
ATOM   3922 O OG1   . THR B 1 259 ? 29.618  -27.896 14.915  1.00 62.46  ? 231 THR B OG1   1 
ATOM   3923 C CG2   . THR B 1 259 ? 27.817  -28.719 16.278  1.00 59.01  ? 231 THR B CG2   1 
ATOM   3924 N N     . ALA B 1 260 ? 32.150  -28.132 16.888  1.00 65.08  ? 232 ALA B N     1 
ATOM   3925 C CA    . ALA B 1 260 ? 33.550  -27.838 16.613  1.00 61.59  ? 232 ALA B CA    1 
ATOM   3926 C C     . ALA B 1 260 ? 33.829  -27.685 15.124  1.00 57.49  ? 232 ALA B C     1 
ATOM   3927 O O     . ALA B 1 260 ? 34.653  -26.851 14.733  1.00 57.45  ? 232 ALA B O     1 
ATOM   3928 C CB    . ALA B 1 260 ? 34.444  -28.933 17.199  1.00 67.63  ? 232 ALA B CB    1 
ATOM   3929 N N     . GLU B 1 261 ? 33.157  -28.470 14.279  1.00 61.43  ? 233 GLU B N     1 
ATOM   3930 C CA    . GLU B 1 261 ? 33.449  -28.421 12.851  1.00 61.67  ? 233 GLU B CA    1 
ATOM   3931 C C     . GLU B 1 261 ? 32.711  -27.289 12.147  1.00 60.01  ? 233 GLU B C     1 
ATOM   3932 O O     . GLU B 1 261 ? 33.243  -26.720 11.187  1.00 66.05  ? 233 GLU B O     1 
ATOM   3933 C CB    . GLU B 1 261 ? 33.125  -29.764 12.193  1.00 62.97  ? 233 GLU B CB    1 
ATOM   3934 C CG    . GLU B 1 261 ? 33.576  -29.848 10.741  1.00 66.09  ? 233 GLU B CG    1 
ATOM   3935 C CD    . GLU B 1 261 ? 33.588  -31.263 10.194  1.00 74.93  ? 233 GLU B CD    1 
ATOM   3936 O OE1   . GLU B 1 261 ? 33.401  -32.215 10.981  1.00 78.00  ? 233 GLU B OE1   1 
ATOM   3937 O OE2   . GLU B 1 261 ? 33.785  -31.423 8.970   1.00 70.68  ? 233 GLU B OE2   1 
ATOM   3938 N N     . THR B 1 262 ? 31.502  -26.938 12.597  1.00 59.96  ? 234 THR B N     1 
ATOM   3939 C CA    . THR B 1 262 ? 30.836  -25.766 12.035  1.00 56.60  ? 234 THR B CA    1 
ATOM   3940 C C     . THR B 1 262 ? 31.612  -24.491 12.341  1.00 52.82  ? 234 THR B C     1 
ATOM   3941 O O     . THR B 1 262 ? 31.519  -23.512 11.592  1.00 51.95  ? 234 THR B O     1 
ATOM   3942 C CB    . THR B 1 262 ? 29.401  -25.653 12.553  1.00 52.13  ? 234 THR B CB    1 
ATOM   3943 O OG1   . THR B 1 262 ? 29.406  -25.605 13.986  1.00 56.27  ? 234 THR B OG1   1 
ATOM   3944 C CG2   . THR B 1 262 ? 28.563  -26.835 12.078  1.00 52.63  ? 234 THR B CG2   1 
ATOM   3945 N N     . HIS B 1 263 ? 32.376  -24.482 13.435  1.00 53.40  ? 235 HIS B N     1 
ATOM   3946 C CA    . HIS B 1 263 ? 33.337  -23.408 13.656  1.00 53.31  ? 235 HIS B CA    1 
ATOM   3947 C C     . HIS B 1 263 ? 34.462  -23.468 12.630  1.00 54.35  ? 235 HIS B C     1 
ATOM   3948 O O     . HIS B 1 263 ? 34.908  -22.432 12.125  1.00 53.92  ? 235 HIS B O     1 
ATOM   3949 C CB    . HIS B 1 263 ? 33.899  -23.496 15.074  1.00 53.89  ? 235 HIS B CB    1 
ATOM   3950 C CG    . HIS B 1 263 ? 34.986  -22.508 15.359  1.00 54.08  ? 235 HIS B CG    1 
ATOM   3951 N ND1   . HIS B 1 263 ? 34.785  -21.146 15.312  1.00 52.84  ? 235 HIS B ND1   1 
ATOM   3952 C CD2   . HIS B 1 263 ? 36.287  -22.685 15.689  1.00 55.45  ? 235 HIS B CD2   1 
ATOM   3953 C CE1   . HIS B 1 263 ? 35.914  -20.526 15.607  1.00 53.44  ? 235 HIS B CE1   1 
ATOM   3954 N NE2   . HIS B 1 263 ? 36.842  -21.437 15.838  1.00 55.02  ? 235 HIS B NE2   1 
ATOM   3955 N N     . ARG B 1 264 ? 34.925  -24.677 12.305  1.00 55.80  ? 236 ARG B N     1 
ATOM   3956 C CA    . ARG B 1 264 ? 35.994  -24.834 11.325  1.00 56.96  ? 236 ARG B CA    1 
ATOM   3957 C C     . ARG B 1 264 ? 35.479  -24.628 9.906   1.00 56.42  ? 236 ARG B C     1 
ATOM   3958 O O     . ARG B 1 264 ? 36.067  -23.869 9.126   1.00 56.39  ? 236 ARG B O     1 
ATOM   3959 C CB    . ARG B 1 264 ? 36.633  -26.216 11.472  1.00 58.78  ? 236 ARG B CB    1 
ATOM   3960 C CG    . ARG B 1 264 ? 37.871  -26.437 10.621  1.00 60.23  ? 236 ARG B CG    1 
ATOM   3961 C CD    . ARG B 1 264 ? 38.518  -27.768 10.965  1.00 62.08  ? 236 ARG B CD    1 
ATOM   3962 N NE    . ARG B 1 264 ? 39.710  -28.043 10.172  1.00 68.33  ? 236 ARG B NE    1 
ATOM   3963 C CZ    . ARG B 1 264 ? 39.696  -28.596 8.967   1.00 69.67  ? 236 ARG B CZ    1 
ATOM   3964 N NH1   . ARG B 1 264 ? 38.563  -28.954 8.384   1.00 64.14  ? 236 ARG B NH1   1 
ATOM   3965 N NH2   . ARG B 1 264 ? 40.847  -28.797 8.331   1.00 66.12  ? 236 ARG B NH2   1 
ATOM   3966 N N     . GLU B 1 265 ? 34.378  -25.300 9.552   1.00 56.06  ? 237 GLU B N     1 
ATOM   3967 C CA    . GLU B 1 265 ? 33.857  -25.211 8.190   1.00 55.70  ? 237 GLU B CA    1 
ATOM   3968 C C     . GLU B 1 265 ? 33.470  -23.785 7.823   1.00 54.18  ? 237 GLU B C     1 
ATOM   3969 O O     . GLU B 1 265 ? 33.580  -23.397 6.655   1.00 54.13  ? 237 GLU B O     1 
ATOM   3970 C CB    . GLU B 1 265 ? 32.658  -26.143 8.019   1.00 55.57  ? 237 GLU B CB    1 
ATOM   3971 C CG    . GLU B 1 265 ? 32.983  -27.626 8.080   1.00 57.22  ? 237 GLU B CG    1 
ATOM   3972 C CD    . GLU B 1 265 ? 33.998  -28.052 7.038   1.00 62.24  ? 237 GLU B CD    1 
ATOM   3973 O OE1   . GLU B 1 265 ? 33.922  -27.558 5.894   1.00 58.35  ? 237 GLU B OE1   1 
ATOM   3974 O OE2   . GLU B 1 265 ? 34.869  -28.888 7.362   1.00 73.15  ? 237 GLU B OE2   1 
ATOM   3975 N N     . PHE B 1 266 ? 33.008  -22.994 8.794   1.00 52.99  ? 238 PHE B N     1 
ATOM   3976 C CA    . PHE B 1 266 ? 32.719  -21.593 8.510   1.00 51.64  ? 238 PHE B CA    1 
ATOM   3977 C C     . PHE B 1 266 ? 33.994  -20.821 8.202   1.00 52.15  ? 238 PHE B C     1 
ATOM   3978 O O     . PHE B 1 266 ? 34.011  -19.973 7.302   1.00 51.64  ? 238 PHE B O     1 
ATOM   3979 C CB    . PHE B 1 266 ? 31.981  -20.949 9.682   1.00 50.40  ? 238 PHE B CB    1 
ATOM   3980 C CG    . PHE B 1 266 ? 31.666  -19.495 9.467   1.00 49.06  ? 238 PHE B CG    1 
ATOM   3981 C CD1   . PHE B 1 266 ? 30.583  -19.114 8.694   1.00 48.01  ? 238 PHE B CD1   1 
ATOM   3982 C CD2   . PHE B 1 266 ? 32.463  -18.510 10.028  1.00 48.96  ? 238 PHE B CD2   1 
ATOM   3983 C CE1   . PHE B 1 266 ? 30.295  -17.779 8.490   1.00 46.85  ? 238 PHE B CE1   1 
ATOM   3984 C CE2   . PHE B 1 266 ? 32.180  -17.173 9.827   1.00 47.81  ? 238 PHE B CE2   1 
ATOM   3985 C CZ    . PHE B 1 266 ? 31.094  -16.807 9.057   1.00 46.76  ? 238 PHE B CZ    1 
ATOM   3986 N N     . LEU B 1 267 ? 35.072  -21.099 8.939   1.00 53.24  ? 239 LEU B N     1 
ATOM   3987 C CA    . LEU B 1 267 ? 36.337  -20.420 8.690   1.00 53.91  ? 239 LEU B CA    1 
ATOM   3988 C C     . LEU B 1 267 ? 36.938  -20.800 7.343   1.00 54.94  ? 239 LEU B C     1 
ATOM   3989 O O     . LEU B 1 267 ? 37.789  -20.066 6.830   1.00 55.28  ? 239 LEU B O     1 
ATOM   3990 C CB    . LEU B 1 267 ? 37.325  -20.722 9.817   1.00 54.98  ? 239 LEU B CB    1 
ATOM   3991 C CG    . LEU B 1 267 ? 37.071  -19.954 11.117  1.00 54.08  ? 239 LEU B CG    1 
ATOM   3992 C CD1   . LEU B 1 267 ? 37.975  -20.451 12.236  1.00 55.31  ? 239 LEU B CD1   1 
ATOM   3993 C CD2   . LEU B 1 267 ? 37.247  -18.459 10.902  1.00 53.19  ? 239 LEU B CD2   1 
ATOM   3994 N N     . LYS B 1 268 ? 36.518  -21.927 6.762   1.00 55.52  ? 240 LYS B N     1 
ATOM   3995 C CA    . LYS B 1 268 ? 36.932  -22.256 5.402   1.00 56.43  ? 240 LYS B CA    1 
ATOM   3996 C C     . LYS B 1 268 ? 36.392  -21.240 4.405   1.00 55.30  ? 240 LYS B C     1 
ATOM   3997 O O     . LYS B 1 268 ? 37.077  -20.878 3.441   1.00 55.88  ? 240 LYS B O     1 
ATOM   3998 C CB    . LYS B 1 268 ? 36.460  -23.661 5.027   1.00 57.24  ? 240 LYS B CB    1 
ATOM   3999 C CG    . LYS B 1 268 ? 37.410  -24.783 5.406   1.00 59.05  ? 240 LYS B CG    1 
ATOM   4000 C CD    . LYS B 1 268 ? 36.920  -26.118 4.863   1.00 59.91  ? 240 LYS B CD    1 
ATOM   4001 C CE    . LYS B 1 268 ? 37.875  -27.249 5.213   1.00 64.31  ? 240 LYS B CE    1 
ATOM   4002 N NZ    . LYS B 1 268 ? 37.378  -28.565 4.723   1.00 63.34  ? 240 LYS B NZ    1 
ATOM   4003 N N     . SER B 1 269 ? 35.164  -20.766 4.622   1.00 53.75  ? 241 SER B N     1 
ATOM   4004 C CA    . SER B 1 269 ? 34.516  -19.889 3.653   1.00 52.70  ? 241 SER B CA    1 
ATOM   4005 C C     . SER B 1 269 ? 35.075  -18.472 3.701   1.00 52.13  ? 241 SER B C     1 
ATOM   4006 O O     . SER B 1 269 ? 35.240  -17.834 2.655   1.00 52.06  ? 241 SER B O     1 
ATOM   4007 C CB    . SER B 1 269 ? 33.006  -19.873 3.893   1.00 51.34  ? 241 SER B CB    1 
ATOM   4008 O OG    . SER B 1 269 ? 32.671  -19.022 4.975   1.00 50.19  ? 241 SER B OG    1 
ATOM   4009 N N     . VAL B 1 270 ? 35.378  -17.966 4.895   1.00 51.79  ? 242 VAL B N     1 
ATOM   4010 C CA    . VAL B 1 270 ? 35.818  -16.583 5.049   1.00 52.40  ? 242 VAL B CA    1 
ATOM   4011 C C     . VAL B 1 270 ? 37.322  -16.475 4.830   1.00 57.46  ? 242 VAL B C     1 
ATOM   4012 O O     . VAL B 1 270 ? 37.919  -15.419 5.070   1.00 62.55  ? 242 VAL B O     1 
ATOM   4013 C CB    . VAL B 1 270 ? 35.419  -16.025 6.428   1.00 50.24  ? 242 VAL B CB    1 
ATOM   4014 C CG1   . VAL B 1 270 ? 33.922  -16.186 6.650   1.00 49.88  ? 242 VAL B CG1   1 
ATOM   4015 C CG2   . VAL B 1 270 ? 36.204  -16.716 7.531   1.00 51.28  ? 242 VAL B CG2   1 
ATOM   4016 N N     . CYS B 1 271 ? 37.945  -17.558 4.371   1.00 57.90  ? 243 CYS B N     1 
ATOM   4017 C CA    . CYS B 1 271 ? 39.363  -17.549 4.023   1.00 60.23  ? 243 CYS B CA    1 
ATOM   4018 C C     . CYS B 1 271 ? 39.489  -17.115 2.566   1.00 64.13  ? 243 CYS B C     1 
ATOM   4019 O O     . CYS B 1 271 ? 39.169  -17.881 1.651   1.00 61.99  ? 243 CYS B O     1 
ATOM   4020 C CB    . CYS B 1 271 ? 39.990  -18.921 4.255   1.00 60.38  ? 243 CYS B CB    1 
ATOM   4021 S SG    . CYS B 1 271 ? 41.782  -18.969 4.012   1.00 62.92  ? 243 CYS B SG    1 
ATOM   4022 N N     . ALA B 1 272 ? 39.958  -15.886 2.352   1.00 68.19  ? 244 ALA B N     1 
ATOM   4023 C CA    . ALA B 1 272 ? 39.935  -15.272 1.031   1.00 68.33  ? 244 ALA B CA    1 
ATOM   4024 C C     . ALA B 1 272 ? 41.093  -15.693 0.136   1.00 63.90  ? 244 ALA B C     1 
ATOM   4025 O O     . ALA B 1 272 ? 41.109  -15.310 -1.039  1.00 68.02  ? 244 ALA B O     1 
ATOM   4026 C CB    . ALA B 1 272 ? 39.928  -13.747 1.166   1.00 72.81  ? 244 ALA B CB    1 
ATOM   4027 N N     . PHE B 1 273 ? 42.055  -16.462 0.643   1.00 60.01  ? 245 PHE B N     1 
ATOM   4028 C CA    . PHE B 1 273 ? 43.222  -16.842 -0.142  1.00 66.01  ? 245 PHE B CA    1 
ATOM   4029 C C     . PHE B 1 273 ? 43.171  -18.272 -0.665  1.00 73.81  ? 245 PHE B C     1 
ATOM   4030 O O     . PHE B 1 273 ? 44.067  -18.667 -1.419  1.00 77.48  ? 245 PHE B O     1 
ATOM   4031 C CB    . PHE B 1 273 ? 44.501  -16.666 0.687   1.00 63.49  ? 245 PHE B CB    1 
ATOM   4032 C CG    . PHE B 1 273 ? 44.988  -15.250 0.765   1.00 65.72  ? 245 PHE B CG    1 
ATOM   4033 C CD1   . PHE B 1 273 ? 45.800  -14.728 -0.229  1.00 71.46  ? 245 PHE B CD1   1 
ATOM   4034 C CD2   . PHE B 1 273 ? 44.644  -14.444 1.834   1.00 69.58  ? 245 PHE B CD2   1 
ATOM   4035 C CE1   . PHE B 1 273 ? 46.256  -13.425 -0.157  1.00 75.98  ? 245 PHE B CE1   1 
ATOM   4036 C CE2   . PHE B 1 273 ? 45.095  -13.142 1.912   1.00 71.75  ? 245 PHE B CE2   1 
ATOM   4037 C CZ    . PHE B 1 273 ? 45.903  -12.632 0.915   1.00 75.79  ? 245 PHE B CZ    1 
ATOM   4038 N N     . LEU B 1 274 ? 42.155  -19.053 -0.293  1.00 73.90  ? 246 LEU B N     1 
ATOM   4039 C CA    . LEU B 1 274 ? 42.141  -20.466 -0.660  1.00 71.03  ? 246 LEU B CA    1 
ATOM   4040 C C     . LEU B 1 274 ? 41.899  -20.672 -2.150  1.00 73.20  ? 246 LEU B C     1 
ATOM   4041 O O     . LEU B 1 274 ? 42.334  -21.685 -2.710  1.00 68.07  ? 246 LEU B O     1 
ATOM   4042 C CB    . LEU B 1 274 ? 41.084  -21.211 0.155   1.00 66.08  ? 246 LEU B CB    1 
ATOM   4043 C CG    . LEU B 1 274 ? 41.532  -21.660 1.546   1.00 62.11  ? 246 LEU B CG    1 
ATOM   4044 C CD1   . LEU B 1 274 ? 40.381  -22.296 2.309   1.00 68.23  ? 246 LEU B CD1   1 
ATOM   4045 C CD2   . LEU B 1 274 ? 42.711  -22.616 1.445   1.00 63.94  ? 246 LEU B CD2   1 
ATOM   4046 N N     . TYR B 1 275 ? 41.215  -19.735 -2.809  1.00 76.04  ? 247 TYR B N     1 
ATOM   4047 C CA    . TYR B 1 275 ? 40.945  -19.880 -4.235  1.00 75.13  ? 247 TYR B CA    1 
ATOM   4048 C C     . TYR B 1 275 ? 42.202  -19.758 -5.087  1.00 74.16  ? 247 TYR B C     1 
ATOM   4049 O O     . TYR B 1 275 ? 42.157  -20.094 -6.275  1.00 70.99  ? 247 TYR B O     1 
ATOM   4050 C CB    . TYR B 1 275 ? 39.900  -18.851 -4.679  1.00 68.94  ? 247 TYR B CB    1 
ATOM   4051 C CG    . TYR B 1 275 ? 40.449  -17.467 -4.949  1.00 71.24  ? 247 TYR B CG    1 
ATOM   4052 C CD1   . TYR B 1 275 ? 40.586  -16.541 -3.924  1.00 72.16  ? 247 TYR B CD1   1 
ATOM   4053 C CD2   . TYR B 1 275 ? 40.812  -17.080 -6.232  1.00 77.33  ? 247 TYR B CD2   1 
ATOM   4054 C CE1   . TYR B 1 275 ? 41.083  -15.273 -4.168  1.00 75.21  ? 247 TYR B CE1   1 
ATOM   4055 C CE2   . TYR B 1 275 ? 41.311  -15.820 -6.483  1.00 79.31  ? 247 TYR B CE2   1 
ATOM   4056 C CZ    . TYR B 1 275 ? 41.442  -14.919 -5.450  1.00 78.66  ? 247 TYR B CZ    1 
ATOM   4057 O OH    . TYR B 1 275 ? 41.938  -13.661 -5.704  1.00 81.11  ? 247 TYR B OH    1 
ATOM   4058 N N     . ARG B 1 276 ? 43.314  -19.294 -4.515  1.00 75.05  ? 248 ARG B N     1 
ATOM   4059 C CA    . ARG B 1 276 ? 44.575  -19.184 -5.237  1.00 79.12  ? 248 ARG B CA    1 
ATOM   4060 C C     . ARG B 1 276 ? 45.498  -20.376 -5.026  1.00 83.01  ? 248 ARG B C     1 
ATOM   4061 O O     . ARG B 1 276 ? 46.391  -20.600 -5.852  1.00 81.89  ? 248 ARG B O     1 
ATOM   4062 C CB    . ARG B 1 276 ? 45.319  -17.910 -4.819  1.00 78.00  ? 248 ARG B CB    1 
ATOM   4063 C CG    . ARG B 1 276 ? 44.622  -16.615 -5.194  1.00 84.74  ? 248 ARG B CG    1 
ATOM   4064 C CD    . ARG B 1 276 ? 45.473  -15.414 -4.810  1.00 87.06  ? 248 ARG B CD    1 
ATOM   4065 N NE    . ARG B 1 276 ? 44.848  -14.152 -5.188  1.00 89.65  ? 248 ARG B NE    1 
ATOM   4066 C CZ    . ARG B 1 276 ? 45.424  -12.964 -5.059  1.00 84.34  ? 248 ARG B CZ    1 
ATOM   4067 N NH1   . ARG B 1 276 ? 46.640  -12.837 -4.552  1.00 82.33  ? 248 ARG B NH1   1 
ATOM   4068 N NH2   . ARG B 1 276 ? 44.763  -11.877 -5.446  1.00 84.06  ? 248 ARG B NH2   1 
ATOM   4069 N N     . ILE B 1 277 ? 45.307  -21.139 -3.955  1.00 81.89  ? 249 ILE B N     1 
ATOM   4070 C CA    . ILE B 1 277 ? 46.229  -22.208 -3.581  1.00 84.49  ? 249 ILE B CA    1 
ATOM   4071 C C     . ILE B 1 277 ? 45.816  -23.511 -4.256  1.00 91.64  ? 249 ILE B C     1 
ATOM   4072 O O     . ILE B 1 277 ? 44.625  -23.854 -4.260  1.00 90.53  ? 249 ILE B O     1 
ATOM   4073 C CB    . ILE B 1 277 ? 46.285  -22.376 -2.055  1.00 80.55  ? 249 ILE B CB    1 
ATOM   4074 C CG1   . ILE B 1 277 ? 46.586  -21.037 -1.380  1.00 75.19  ? 249 ILE B CG1   1 
ATOM   4075 C CG2   . ILE B 1 277 ? 47.331  -23.405 -1.669  1.00 89.20  ? 249 ILE B CG2   1 
ATOM   4076 C CD1   . ILE B 1 277 ? 47.891  -20.414 -1.817  1.00 76.23  ? 249 ILE B CD1   1 
ATOM   4077 N N     . PRO B 1 278 ? 46.749  -24.256 -4.845  1.00 93.95  ? 250 PRO B N     1 
ATOM   4078 C CA    . PRO B 1 278 ? 46.414  -25.580 -5.384  1.00 92.20  ? 250 PRO B CA    1 
ATOM   4079 C C     . PRO B 1 278 ? 46.026  -26.547 -4.274  1.00 96.38  ? 250 PRO B C     1 
ATOM   4080 O O     . PRO B 1 278 ? 46.211  -26.289 -3.083  1.00 96.74  ? 250 PRO B O     1 
ATOM   4081 C CB    . PRO B 1 278 ? 47.701  -26.020 -6.088  1.00 85.88  ? 250 PRO B CB    1 
ATOM   4082 C CG    . PRO B 1 278 ? 48.448  -24.753 -6.353  1.00 84.35  ? 250 PRO B CG    1 
ATOM   4083 C CD    . PRO B 1 278 ? 48.108  -23.832 -5.221  1.00 85.95  ? 250 PRO B CD    1 
ATOM   4084 N N     . GLU B 1 279 ? 45.492  -27.698 -4.695  1.00 97.06  ? 251 GLU B N     1 
ATOM   4085 C CA    . GLU B 1 279 ? 44.890  -28.635 -3.749  1.00 102.46 ? 251 GLU B CA    1 
ATOM   4086 C C     . GLU B 1 279 ? 45.921  -29.229 -2.795  1.00 104.47 ? 251 GLU B C     1 
ATOM   4087 O O     . GLU B 1 279 ? 45.625  -29.438 -1.612  1.00 102.42 ? 251 GLU B O     1 
ATOM   4088 C CB    . GLU B 1 279 ? 44.161  -29.746 -4.506  1.00 101.99 ? 251 GLU B CB    1 
ATOM   4089 C CG    . GLU B 1 279 ? 43.477  -30.770 -3.608  1.00 109.10 ? 251 GLU B CG    1 
ATOM   4090 C CD    . GLU B 1 279 ? 42.446  -30.149 -2.682  1.00 110.74 ? 251 GLU B CD    1 
ATOM   4091 O OE1   . GLU B 1 279 ? 41.791  -29.164 -3.086  1.00 109.42 ? 251 GLU B OE1   1 
ATOM   4092 O OE2   . GLU B 1 279 ? 42.294  -30.647 -1.546  1.00 98.24  ? 251 GLU B OE2   1 
ATOM   4093 N N     . GLU B 1 280 ? 47.132  -29.512 -3.283  1.00 101.29 ? 252 GLU B N     1 
ATOM   4094 C CA    . GLU B 1 280 ? 48.134  -30.149 -2.435  1.00 100.97 ? 252 GLU B CA    1 
ATOM   4095 C C     . GLU B 1 280 ? 48.561  -29.266 -1.270  1.00 98.85  ? 252 GLU B C     1 
ATOM   4096 O O     . GLU B 1 280 ? 49.119  -29.776 -0.293  1.00 96.65  ? 252 GLU B O     1 
ATOM   4097 C CB    . GLU B 1 280 ? 49.363  -30.540 -3.259  1.00 106.46 ? 252 GLU B CB    1 
ATOM   4098 C CG    . GLU B 1 280 ? 50.172  -29.362 -3.777  1.00 110.01 ? 252 GLU B CG    1 
ATOM   4099 C CD    . GLU B 1 280 ? 49.740  -28.919 -5.160  1.00 107.34 ? 252 GLU B CD    1 
ATOM   4100 O OE1   . GLU B 1 280 ? 48.563  -29.135 -5.515  1.00 112.53 ? 252 GLU B OE1   1 
ATOM   4101 O OE2   . GLU B 1 280 ? 50.581  -28.355 -5.891  1.00 107.35 ? 252 GLU B OE2   1 
ATOM   4102 N N     . GLN B 1 281 ? 48.312  -27.959 -1.350  1.00 98.15  ? 253 GLN B N     1 
ATOM   4103 C CA    . GLN B 1 281 ? 48.645  -27.039 -0.274  1.00 95.25  ? 253 GLN B CA    1 
ATOM   4104 C C     . GLN B 1 281 ? 47.431  -26.305 0.278   1.00 91.40  ? 253 GLN B C     1 
ATOM   4105 O O     . GLN B 1 281 ? 47.592  -25.455 1.163   1.00 88.57  ? 253 GLN B O     1 
ATOM   4106 C CB    . GLN B 1 281 ? 49.696  -26.026 -0.749  1.00 96.51  ? 253 GLN B CB    1 
ATOM   4107 C CG    . GLN B 1 281 ? 51.038  -26.659 -1.093  1.00 100.66 ? 253 GLN B CG    1 
ATOM   4108 C CD    . GLN B 1 281 ? 52.105  -25.636 -1.431  1.00 105.85 ? 253 GLN B CD    1 
ATOM   4109 O OE1   . GLN B 1 281 ? 52.382  -24.727 -0.650  1.00 108.08 ? 253 GLN B OE1   1 
ATOM   4110 N NE2   . GLN B 1 281 ? 52.712  -25.782 -2.604  1.00 106.65 ? 253 GLN B NE2   1 
ATOM   4111 N N     . LYS B 1 282 ? 46.226  -26.600 -0.219  1.00 95.49  ? 254 LYS B N     1 
ATOM   4112 C CA    . LYS B 1 282 ? 45.017  -26.022 0.361   1.00 89.52  ? 254 LYS B CA    1 
ATOM   4113 C C     . LYS B 1 282 ? 44.849  -26.450 1.813   1.00 85.84  ? 254 LYS B C     1 
ATOM   4114 O O     . LYS B 1 282 ? 44.693  -25.611 2.707   1.00 82.87  ? 254 LYS B O     1 
ATOM   4115 C CB    . LYS B 1 282 ? 43.789  -26.431 -0.455  1.00 93.07  ? 254 LYS B CB    1 
ATOM   4116 C CG    . LYS B 1 282 ? 43.502  -25.570 -1.674  1.00 87.93  ? 254 LYS B CG    1 
ATOM   4117 C CD    . LYS B 1 282 ? 42.167  -25.956 -2.293  1.00 87.98  ? 254 LYS B CD    1 
ATOM   4118 C CE    . LYS B 1 282 ? 41.778  -25.023 -3.427  1.00 84.16  ? 254 LYS B CE    1 
ATOM   4119 N NZ    . LYS B 1 282 ? 40.544  -25.485 -4.121  1.00 84.84  ? 254 LYS B NZ    1 
ATOM   4120 N N     . ASP B 1 283 ? 44.875  -27.762 2.064   1.00 85.95  ? 255 ASP B N     1 
ATOM   4121 C CA    . ASP B 1 283 ? 44.721  -28.270 3.422   1.00 75.01  ? 255 ASP B CA    1 
ATOM   4122 C C     . ASP B 1 283 ? 45.886  -27.881 4.321   1.00 71.37  ? 255 ASP B C     1 
ATOM   4123 O O     . ASP B 1 283 ? 45.753  -27.941 5.547   1.00 71.00  ? 255 ASP B O     1 
ATOM   4124 C CB    . ASP B 1 283 ? 44.566  -29.791 3.398   1.00 76.03  ? 255 ASP B CB    1 
ATOM   4125 C CG    . ASP B 1 283 ? 43.341  -30.238 2.624   1.00 86.97  ? 255 ASP B CG    1 
ATOM   4126 O OD1   . ASP B 1 283 ? 42.406  -29.425 2.465   1.00 95.38  ? 255 ASP B OD1   1 
ATOM   4127 O OD2   . ASP B 1 283 ? 43.312  -31.404 2.175   1.00 88.19  ? 255 ASP B OD2   1 
ATOM   4128 N N     . ASP B 1 284 ? 47.021  -27.490 3.744   1.00 75.20  ? 256 ASP B N     1 
ATOM   4129 C CA    . ASP B 1 284 ? 48.146  -27.004 4.529   1.00 76.98  ? 256 ASP B CA    1 
ATOM   4130 C C     . ASP B 1 284 ? 48.119  -25.493 4.709   1.00 72.22  ? 256 ASP B C     1 
ATOM   4131 O O     . ASP B 1 284 ? 48.686  -24.981 5.682   1.00 71.92  ? 256 ASP B O     1 
ATOM   4132 C CB    . ASP B 1 284 ? 49.464  -27.428 3.876   1.00 88.33  ? 256 ASP B CB    1 
ATOM   4133 C CG    . ASP B 1 284 ? 49.659  -28.933 3.884   1.00 96.29  ? 256 ASP B CG    1 
ATOM   4134 O OD1   . ASP B 1 284 ? 48.996  -29.615 4.695   1.00 91.76  ? 256 ASP B OD1   1 
ATOM   4135 O OD2   . ASP B 1 284 ? 50.475  -29.434 3.081   1.00 98.91  ? 256 ASP B OD2   1 
ATOM   4136 N N     . PHE B 1 285 ? 47.473  -24.769 3.792   1.00 77.93  ? 257 PHE B N     1 
ATOM   4137 C CA    . PHE B 1 285 ? 47.279  -23.334 3.977   1.00 75.46  ? 257 PHE B CA    1 
ATOM   4138 C C     . PHE B 1 285 ? 46.249  -23.062 5.065   1.00 70.98  ? 257 PHE B C     1 
ATOM   4139 O O     . PHE B 1 285 ? 46.406  -22.127 5.859   1.00 69.53  ? 257 PHE B O     1 
ATOM   4140 C CB    . PHE B 1 285 ? 46.857  -22.693 2.651   1.00 77.35  ? 257 PHE B CB    1 
ATOM   4141 C CG    . PHE B 1 285 ? 46.788  -21.188 2.685   1.00 76.56  ? 257 PHE B CG    1 
ATOM   4142 C CD1   . PHE B 1 285 ? 45.699  -20.534 3.242   1.00 72.93  ? 257 PHE B CD1   1 
ATOM   4143 C CD2   . PHE B 1 285 ? 47.813  -20.426 2.148   1.00 80.03  ? 257 PHE B CD2   1 
ATOM   4144 C CE1   . PHE B 1 285 ? 45.639  -19.154 3.270   1.00 73.83  ? 257 PHE B CE1   1 
ATOM   4145 C CE2   . PHE B 1 285 ? 47.757  -19.046 2.172   1.00 72.95  ? 257 PHE B CE2   1 
ATOM   4146 C CZ    . PHE B 1 285 ? 46.670  -18.410 2.735   1.00 70.80  ? 257 PHE B CZ    1 
ATOM   4147 N N     . PHE B 1 286 ? 45.187  -23.869 5.115   1.00 67.98  ? 258 PHE B N     1 
ATOM   4148 C CA    . PHE B 1 286 ? 44.153  -23.692 6.130   1.00 65.14  ? 258 PHE B CA    1 
ATOM   4149 C C     . PHE B 1 286 ? 44.699  -23.965 7.527   1.00 66.17  ? 258 PHE B C     1 
ATOM   4150 O O     . PHE B 1 286 ? 44.453  -23.194 8.462   1.00 64.75  ? 258 PHE B O     1 
ATOM   4151 C CB    . PHE B 1 286 ? 42.968  -24.608 5.826   1.00 64.62  ? 258 PHE B CB    1 
ATOM   4152 C CG    . PHE B 1 286 ? 41.730  -24.278 6.605   1.00 62.82  ? 258 PHE B CG    1 
ATOM   4153 C CD1   . PHE B 1 286 ? 41.283  -22.971 6.704   1.00 61.21  ? 258 PHE B CD1   1 
ATOM   4154 C CD2   . PHE B 1 286 ? 41.014  -25.276 7.244   1.00 62.82  ? 258 PHE B CD2   1 
ATOM   4155 C CE1   . PHE B 1 286 ? 40.141  -22.667 7.423   1.00 61.87  ? 258 PHE B CE1   1 
ATOM   4156 C CE2   . PHE B 1 286 ? 39.874  -24.980 7.964   1.00 61.25  ? 258 PHE B CE2   1 
ATOM   4157 C CZ    . PHE B 1 286 ? 39.437  -23.673 8.055   1.00 59.66  ? 258 PHE B CZ    1 
ATOM   4158 N N     . ASP B 1 287 ? 45.440  -25.065 7.685   1.00 71.98  ? 259 ASP B N     1 
ATOM   4159 C CA    . ASP B 1 287 ? 45.992  -25.411 8.992   1.00 68.43  ? 259 ASP B CA    1 
ATOM   4160 C C     . ASP B 1 287 ? 47.008  -24.377 9.459   1.00 68.76  ? 259 ASP B C     1 
ATOM   4161 O O     . ASP B 1 287 ? 47.054  -24.031 10.645  1.00 70.22  ? 259 ASP B O     1 
ATOM   4162 C CB    . ASP B 1 287 ? 46.626  -26.799 8.931   1.00 70.47  ? 259 ASP B CB    1 
ATOM   4163 C CG    . ASP B 1 287 ? 45.596  -27.905 8.881   1.00 74.04  ? 259 ASP B CG    1 
ATOM   4164 O OD1   . ASP B 1 287 ? 44.642  -27.804 8.080   1.00 69.11  ? 259 ASP B OD1   1 
ATOM   4165 O OD2   . ASP B 1 287 ? 45.752  -28.886 9.634   1.00 87.42  ? 259 ASP B OD2   1 
ATOM   4166 N N     . ASP B 1 288 ? 47.840  -23.879 8.541   1.00 70.91  ? 260 ASP B N     1 
ATOM   4167 C CA    . ASP B 1 288 ? 48.752  -22.792 8.880   1.00 74.16  ? 260 ASP B CA    1 
ATOM   4168 C C     . ASP B 1 288 ? 47.981  -21.557 9.325   1.00 73.22  ? 260 ASP B C     1 
ATOM   4169 O O     . ASP B 1 288 ? 48.410  -20.836 10.234  1.00 75.25  ? 260 ASP B O     1 
ATOM   4170 C CB    . ASP B 1 288 ? 49.644  -22.472 7.680   1.00 80.36  ? 260 ASP B CB    1 
ATOM   4171 C CG    . ASP B 1 288 ? 50.897  -21.715 8.067   1.00 86.29  ? 260 ASP B CG    1 
ATOM   4172 O OD1   . ASP B 1 288 ? 51.404  -21.935 9.187   1.00 89.79  ? 260 ASP B OD1   1 
ATOM   4173 O OD2   . ASP B 1 288 ? 51.374  -20.898 7.252   1.00 88.19  ? 260 ASP B OD2   1 
ATOM   4174 N N     . TRP B 1 289 ? 46.830  -21.305 8.698   1.00 72.96  ? 261 TRP B N     1 
ATOM   4175 C CA    . TRP B 1 289 ? 46.000  -20.163 9.067   1.00 72.26  ? 261 TRP B CA    1 
ATOM   4176 C C     . TRP B 1 289 ? 45.358  -20.366 10.434  1.00 70.76  ? 261 TRP B C     1 
ATOM   4177 O O     . TRP B 1 289 ? 45.436  -19.490 11.303  1.00 71.13  ? 261 TRP B O     1 
ATOM   4178 C CB    . TRP B 1 289 ? 44.931  -19.943 7.996   1.00 73.03  ? 261 TRP B CB    1 
ATOM   4179 C CG    . TRP B 1 289 ? 44.248  -18.615 8.058   1.00 68.43  ? 261 TRP B CG    1 
ATOM   4180 C CD1   . TRP B 1 289 ? 44.837  -17.390 8.167   1.00 67.72  ? 261 TRP B CD1   1 
ATOM   4181 C CD2   . TRP B 1 289 ? 42.837  -18.379 8.007   1.00 60.37  ? 261 TRP B CD2   1 
ATOM   4182 N NE1   . TRP B 1 289 ? 43.879  -16.405 8.189   1.00 66.47  ? 261 TRP B NE1   1 
ATOM   4183 C CE2   . TRP B 1 289 ? 42.643  -16.987 8.093   1.00 64.22  ? 261 TRP B CE2   1 
ATOM   4184 C CE3   . TRP B 1 289 ? 41.718  -19.211 7.900   1.00 58.61  ? 261 TRP B CE3   1 
ATOM   4185 C CZ2   . TRP B 1 289 ? 41.376  -16.410 8.071   1.00 68.41  ? 261 TRP B CZ2   1 
ATOM   4186 C CZ3   . TRP B 1 289 ? 40.463  -18.636 7.881   1.00 56.84  ? 261 TRP B CZ3   1 
ATOM   4187 C CH2   . TRP B 1 289 ? 40.301  -17.249 7.967   1.00 63.66  ? 261 TRP B CH2   1 
ATOM   4188 N N     . LEU B 1 290 ? 44.720  -21.522 10.641  1.00 68.07  ? 262 LEU B N     1 
ATOM   4189 C CA    . LEU B 1 290 ? 43.988  -21.759 11.883  1.00 66.89  ? 262 LEU B CA    1 
ATOM   4190 C C     . LEU B 1 290 ? 44.921  -21.769 13.088  1.00 74.28  ? 262 LEU B C     1 
ATOM   4191 O O     . LEU B 1 290 ? 44.551  -21.301 14.171  1.00 72.48  ? 262 LEU B O     1 
ATOM   4192 C CB    . LEU B 1 290 ? 43.218  -23.076 11.793  1.00 62.98  ? 262 LEU B CB    1 
ATOM   4193 C CG    . LEU B 1 290 ? 41.995  -23.117 10.873  1.00 61.67  ? 262 LEU B CG    1 
ATOM   4194 C CD1   . LEU B 1 290 ? 41.074  -24.262 11.264  1.00 61.59  ? 262 LEU B CD1   1 
ATOM   4195 C CD2   . LEU B 1 290 ? 41.247  -21.793 10.895  1.00 59.79  ? 262 LEU B CD2   1 
ATOM   4196 N N     . GLN B 1 291 ? 46.133  -22.304 12.920  1.00 80.12  ? 263 GLN B N     1 
ATOM   4197 C CA    . GLN B 1 291 ? 47.090  -22.322 14.022  1.00 80.67  ? 263 GLN B CA    1 
ATOM   4198 C C     . GLN B 1 291 ? 47.480  -20.908 14.433  1.00 79.54  ? 263 GLN B C     1 
ATOM   4199 O O     . GLN B 1 291 ? 47.563  -20.600 15.628  1.00 75.33  ? 263 GLN B O     1 
ATOM   4200 C CB    . GLN B 1 291 ? 48.327  -23.130 13.626  1.00 81.55  ? 263 GLN B CB    1 
ATOM   4201 C CG    . GLN B 1 291 ? 49.616  -22.666 14.285  1.00 93.44  ? 263 GLN B CG    1 
ATOM   4202 C CD    . GLN B 1 291 ? 50.824  -23.459 13.824  1.00 100.87 ? 263 GLN B CD    1 
ATOM   4203 O OE1   . GLN B 1 291 ? 51.101  -23.548 12.627  1.00 97.00  ? 263 GLN B OE1   1 
ATOM   4204 N NE2   . GLN B 1 291 ? 51.549  -24.040 14.772  1.00 101.82 ? 263 GLN B NE2   1 
ATOM   4205 N N     . ARG B 1 292 ? 47.710  -20.031 13.455  1.00 80.94  ? 264 ARG B N     1 
ATOM   4206 C CA    . ARG B 1 292 ? 48.063  -18.646 13.732  1.00 80.86  ? 264 ARG B CA    1 
ATOM   4207 C C     . ARG B 1 292 ? 46.914  -17.852 14.339  1.00 80.06  ? 264 ARG B C     1 
ATOM   4208 O O     . ARG B 1 292 ? 47.150  -16.756 14.860  1.00 80.10  ? 264 ARG B O     1 
ATOM   4209 C CB    . ARG B 1 292 ? 48.530  -17.963 12.446  1.00 80.10  ? 264 ARG B CB    1 
ATOM   4210 C CG    . ARG B 1 292 ? 49.715  -17.030 12.622  1.00 78.06  ? 264 ARG B CG    1 
ATOM   4211 C CD    . ARG B 1 292 ? 50.461  -16.856 11.310  1.00 82.16  ? 264 ARG B CD    1 
ATOM   4212 N NE    . ARG B 1 292 ? 51.561  -17.801 11.167  1.00 84.95  ? 264 ARG B NE    1 
ATOM   4213 C CZ    . ARG B 1 292 ? 51.493  -18.924 10.466  1.00 87.24  ? 264 ARG B CZ    1 
ATOM   4214 N NH1   . ARG B 1 292 ? 50.379  -19.290 9.856   1.00 84.43  ? 264 ARG B NH1   1 
ATOM   4215 N NH2   . ARG B 1 292 ? 52.569  -19.701 10.379  1.00 91.86  ? 264 ARG B NH2   1 
ATOM   4216 N N     . LEU B 1 293 ? 45.686  -18.371 14.287  1.00 79.31  ? 265 LEU B N     1 
ATOM   4217 C CA    . LEU B 1 293 ? 44.539  -17.624 14.792  1.00 75.36  ? 265 LEU B CA    1 
ATOM   4218 C C     . LEU B 1 293 ? 44.465  -17.679 16.312  1.00 71.93  ? 265 LEU B C     1 
ATOM   4219 O O     . LEU B 1 293 ? 44.352  -16.640 16.972  1.00 69.50  ? 265 LEU B O     1 
ATOM   4220 C CB    . LEU B 1 293 ? 43.250  -18.158 14.170  1.00 73.47  ? 265 LEU B CB    1 
ATOM   4221 C CG    . LEU B 1 293 ? 43.092  -17.769 12.702  1.00 68.67  ? 265 LEU B CG    1 
ATOM   4222 C CD1   . LEU B 1 293 ? 41.814  -18.349 12.112  1.00 60.97  ? 265 LEU B CD1   1 
ATOM   4223 C CD2   . LEU B 1 293 ? 43.149  -16.260 12.554  1.00 67.69  ? 265 LEU B CD2   1 
ATOM   4224 N N     . GLU B 1 294 ? 44.516  -18.883 16.885  1.00 73.55  ? 266 GLU B N     1 
ATOM   4225 C CA    . GLU B 1 294 ? 44.583  -19.001 18.335  1.00 74.17  ? 266 GLU B CA    1 
ATOM   4226 C C     . GLU B 1 294 ? 45.878  -18.426 18.891  1.00 73.92  ? 266 GLU B C     1 
ATOM   4227 O O     . GLU B 1 294 ? 45.917  -18.033 20.062  1.00 71.45  ? 266 GLU B O     1 
ATOM   4228 C CB    . GLU B 1 294 ? 44.425  -20.461 18.757  1.00 82.52  ? 266 GLU B CB    1 
ATOM   4229 C CG    . GLU B 1 294 ? 43.003  -20.982 18.630  1.00 87.57  ? 266 GLU B CG    1 
ATOM   4230 C CD    . GLU B 1 294 ? 42.882  -22.449 18.987  1.00 101.29 ? 266 GLU B CD    1 
ATOM   4231 O OE1   . GLU B 1 294 ? 43.891  -23.042 19.426  1.00 95.25  ? 266 GLU B OE1   1 
ATOM   4232 O OE2   . GLU B 1 294 ? 41.776  -23.008 18.830  1.00 108.83 ? 266 GLU B OE2   1 
ATOM   4233 N N     . LYS B 1 295 ? 46.936  -18.370 18.078  1.00 76.33  ? 267 LYS B N     1 
ATOM   4234 C CA    . LYS B 1 295 ? 48.138  -17.648 18.477  1.00 74.34  ? 267 LYS B CA    1 
ATOM   4235 C C     . LYS B 1 295 ? 47.836  -16.167 18.674  1.00 74.96  ? 267 LYS B C     1 
ATOM   4236 O O     . LYS B 1 295 ? 48.197  -15.575 19.698  1.00 68.24  ? 267 LYS B O     1 
ATOM   4237 C CB    . LYS B 1 295 ? 49.238  -17.843 17.432  1.00 77.92  ? 267 LYS B CB    1 
ATOM   4238 N N     . LEU B 1 296 ? 47.161  -15.555 17.702  1.00 76.51  ? 268 LEU B N     1 
ATOM   4239 C CA    . LEU B 1 296 ? 46.744  -14.163 17.802  1.00 72.92  ? 268 LEU B CA    1 
ATOM   4240 C C     . LEU B 1 296 ? 45.462  -13.984 18.607  1.00 71.63  ? 268 LEU B C     1 
ATOM   4241 O O     . LEU B 1 296 ? 45.020  -12.844 18.788  1.00 63.86  ? 268 LEU B O     1 
ATOM   4242 C CB    . LEU B 1 296 ? 46.568  -13.569 16.402  1.00 68.15  ? 268 LEU B CB    1 
ATOM   4243 C CG    . LEU B 1 296 ? 47.846  -13.519 15.562  1.00 69.90  ? 268 LEU B CG    1 
ATOM   4244 C CD1   . LEU B 1 296 ? 47.522  -13.274 14.098  1.00 79.26  ? 268 LEU B CD1   1 
ATOM   4245 C CD2   . LEU B 1 296 ? 48.796  -12.455 16.092  1.00 74.50  ? 268 LEU B CD2   1 
ATOM   4246 N N     . LYS B 1 297 ? 44.860  -15.078 19.081  1.00 72.58  ? 269 LYS B N     1 
ATOM   4247 C CA    . LYS B 1 297 ? 43.684  -15.035 19.953  1.00 65.83  ? 269 LYS B CA    1 
ATOM   4248 C C     . LYS B 1 297 ? 42.514  -14.310 19.287  1.00 64.38  ? 269 LYS B C     1 
ATOM   4249 O O     . LYS B 1 297 ? 41.939  -13.368 19.837  1.00 58.79  ? 269 LYS B O     1 
ATOM   4250 C CB    . LYS B 1 297 ? 44.027  -14.401 21.304  1.00 59.15  ? 269 LYS B CB    1 
ATOM   4251 N N     . GLY B 1 298 ? 42.162  -14.762 18.086  1.00 68.84  ? 270 GLY B N     1 
ATOM   4252 C CA    . GLY B 1 298 ? 40.983  -14.262 17.407  1.00 62.32  ? 270 GLY B CA    1 
ATOM   4253 C C     . GLY B 1 298 ? 39.821  -15.219 17.557  1.00 58.05  ? 270 GLY B C     1 
ATOM   4254 O O     . GLY B 1 298 ? 38.657  -14.809 17.595  1.00 55.93  ? 270 GLY B O     1 
ATOM   4255 N N     . THR B 1 299 ? 40.137  -16.507 17.638  1.00 61.31  ? 271 THR B N     1 
ATOM   4256 C CA    . THR B 1 299 ? 39.171  -17.552 17.928  1.00 58.88  ? 271 THR B CA    1 
ATOM   4257 C C     . THR B 1 299 ? 39.380  -18.052 19.351  1.00 59.18  ? 271 THR B C     1 
ATOM   4258 O O     . THR B 1 299 ? 40.471  -17.943 19.917  1.00 60.57  ? 271 THR B O     1 
ATOM   4259 C CB    . THR B 1 299 ? 39.299  -18.716 16.939  1.00 56.42  ? 271 THR B CB    1 
ATOM   4260 O OG1   . THR B 1 299 ? 40.554  -19.378 17.139  1.00 65.10  ? 271 THR B OG1   1 
ATOM   4261 C CG2   . THR B 1 299 ? 39.226  -18.208 15.507  1.00 58.04  ? 271 THR B CG2   1 
ATOM   4262 N N     . SER B 1 300 ? 38.317  -18.601 19.931  1.00 57.35  ? 272 SER B N     1 
ATOM   4263 C CA    . SER B 1 300 ? 38.380  -19.089 21.299  1.00 60.90  ? 272 SER B CA    1 
ATOM   4264 C C     . SER B 1 300 ? 37.335  -20.176 21.499  1.00 62.61  ? 272 SER B C     1 
ATOM   4265 O O     . SER B 1 300 ? 36.417  -20.347 20.694  1.00 59.91  ? 272 SER B O     1 
ATOM   4266 C CB    . SER B 1 300 ? 38.179  -17.954 22.308  1.00 61.25  ? 272 SER B CB    1 
ATOM   4267 O OG    . SER B 1 300 ? 37.556  -18.426 23.490  1.00 71.99  ? 272 SER B OG    1 
ATOM   4268 N N     . GLN B 1 301 ? 37.493  -20.911 22.597  1.00 66.61  ? 273 GLN B N     1 
ATOM   4269 C CA    . GLN B 1 301 ? 36.580  -21.975 22.983  1.00 65.12  ? 273 GLN B CA    1 
ATOM   4270 C C     . GLN B 1 301 ? 36.136  -21.746 24.420  1.00 69.19  ? 273 GLN B C     1 
ATOM   4271 O O     . GLN B 1 301 ? 36.940  -21.355 25.271  1.00 69.28  ? 273 GLN B O     1 
ATOM   4272 C CB    . GLN B 1 301 ? 37.241  -23.352 22.837  1.00 63.98  ? 273 GLN B CB    1 
ATOM   4273 C CG    . GLN B 1 301 ? 36.308  -24.526 23.070  1.00 67.25  ? 273 GLN B CG    1 
ATOM   4274 C CD    . GLN B 1 301 ? 37.024  -25.724 23.662  1.00 77.64  ? 273 GLN B CD    1 
ATOM   4275 O OE1   . GLN B 1 301 ? 37.818  -26.382 22.989  1.00 79.60  ? 273 GLN B OE1   1 
ATOM   4276 N NE2   . GLN B 1 301 ? 36.745  -26.015 24.928  1.00 77.28  ? 273 GLN B NE2   1 
ATOM   4277 N N     . GLY B 1 302 ? 34.849  -21.981 24.684  1.00 73.24  ? 274 GLY B N     1 
ATOM   4278 C CA    . GLY B 1 302 ? 34.280  -21.751 25.995  1.00 71.89  ? 274 GLY B CA    1 
ATOM   4279 C C     . GLY B 1 302 ? 33.406  -22.910 26.442  1.00 71.06  ? 274 GLY B C     1 
ATOM   4280 O O     . GLY B 1 302 ? 33.187  -23.874 25.706  1.00 70.23  ? 274 GLY B O     1 
ATOM   4281 N N     . VAL B 1 303 ? 32.916  -22.787 27.672  1.00 72.73  ? 275 VAL B N     1 
ATOM   4282 C CA    . VAL B 1 303 ? 32.031  -23.776 28.272  1.00 71.46  ? 275 VAL B CA    1 
ATOM   4283 C C     . VAL B 1 303 ? 30.647  -23.161 28.425  1.00 72.26  ? 275 VAL B C     1 
ATOM   4284 O O     . VAL B 1 303 ? 30.493  -21.939 28.515  1.00 70.69  ? 275 VAL B O     1 
ATOM   4285 C CB    . VAL B 1 303 ? 32.561  -24.274 29.633  1.00 68.03  ? 275 VAL B CB    1 
ATOM   4286 C CG1   . VAL B 1 303 ? 33.717  -25.240 29.430  1.00 62.23  ? 275 VAL B CG1   1 
ATOM   4287 C CG2   . VAL B 1 303 ? 32.987  -23.099 30.499  1.00 74.01  ? 275 VAL B CG2   1 
ATOM   4288 N N     . GLY B 1 304 ? 29.631  -24.023 28.454  1.00 70.53  ? 276 GLY B N     1 
ATOM   4289 C CA    . GLY B 1 304 ? 28.254  -23.600 28.554  1.00 69.87  ? 276 GLY B CA    1 
ATOM   4290 C C     . GLY B 1 304 ? 27.635  -23.954 29.897  1.00 73.18  ? 276 GLY B C     1 
ATOM   4291 O O     . GLY B 1 304 ? 28.186  -24.711 30.696  1.00 73.73  ? 276 GLY B O     1 
ATOM   4292 N N     . ARG B 1 305 ? 26.453  -23.377 30.133  1.00 75.65  ? 277 ARG B N     1 
ATOM   4293 C CA    . ARG B 1 305 ? 25.719  -23.670 31.359  1.00 73.49  ? 277 ARG B CA    1 
ATOM   4294 C C     . ARG B 1 305 ? 25.241  -25.115 31.394  1.00 70.76  ? 277 ARG B C     1 
ATOM   4295 O O     . ARG B 1 305 ? 25.046  -25.677 32.477  1.00 68.93  ? 277 ARG B O     1 
ATOM   4296 C CB    . ARG B 1 305 ? 24.534  -22.716 31.506  1.00 69.94  ? 277 ARG B CB    1 
ATOM   4297 N N     . ASN B 1 306 ? 25.042  -25.727 30.229  1.00 75.66  ? 278 ASN B N     1 
ATOM   4298 C CA    . ASN B 1 306 ? 24.701  -27.139 30.136  1.00 74.01  ? 278 ASN B CA    1 
ATOM   4299 C C     . ASN B 1 306 ? 25.930  -28.037 30.094  1.00 71.81  ? 278 ASN B C     1 
ATOM   4300 O O     . ASN B 1 306 ? 25.783  -29.262 30.038  1.00 62.47  ? 278 ASN B O     1 
ATOM   4301 C CB    . ASN B 1 306 ? 23.835  -27.391 28.897  1.00 68.92  ? 278 ASN B CB    1 
ATOM   4302 N N     . GLY B 1 307 ? 27.131  -27.461 30.118  1.00 72.27  ? 279 GLY B N     1 
ATOM   4303 C CA    . GLY B 1 307 ? 28.358  -28.226 30.096  1.00 71.57  ? 279 GLY B CA    1 
ATOM   4304 C C     . GLY B 1 307 ? 28.953  -28.462 28.726  1.00 77.97  ? 279 GLY B C     1 
ATOM   4305 O O     . GLY B 1 307 ? 30.034  -29.058 28.634  1.00 80.12  ? 279 GLY B O     1 
ATOM   4306 N N     . GLU B 1 308 ? 28.294  -28.014 27.661  1.00 74.10  ? 280 GLU B N     1 
ATOM   4307 C CA    . GLU B 1 308 ? 28.781  -28.252 26.313  1.00 68.86  ? 280 GLU B CA    1 
ATOM   4308 C C     . GLU B 1 308 ? 29.847  -27.227 25.932  1.00 71.89  ? 280 GLU B C     1 
ATOM   4309 O O     . GLU B 1 308 ? 29.968  -26.158 26.536  1.00 70.78  ? 280 GLU B O     1 
ATOM   4310 C CB    . GLU B 1 308 ? 27.629  -28.208 25.309  1.00 67.88  ? 280 GLU B CB    1 
ATOM   4311 N N     . ALA B 1 309 ? 30.625  -27.573 24.909  1.00 71.25  ? 281 ALA B N     1 
ATOM   4312 C CA    . ALA B 1 309 ? 31.689  -26.702 24.432  1.00 58.65  ? 281 ALA B CA    1 
ATOM   4313 C C     . ALA B 1 309 ? 31.124  -25.614 23.528  1.00 61.49  ? 281 ALA B C     1 
ATOM   4314 O O     . ALA B 1 309 ? 30.217  -25.858 22.727  1.00 57.37  ? 281 ALA B O     1 
ATOM   4315 C CB    . ALA B 1 309 ? 32.747  -27.510 23.681  1.00 57.45  ? 281 ALA B CB    1 
ATOM   4316 N N     . GLU B 1 310 ? 31.668  -24.407 23.663  1.00 65.34  ? 282 GLU B N     1 
ATOM   4317 C CA    . GLU B 1 310 ? 31.236  -23.248 22.895  1.00 62.61  ? 282 GLU B CA    1 
ATOM   4318 C C     . GLU B 1 310 ? 32.428  -22.687 22.135  1.00 62.92  ? 282 GLU B C     1 
ATOM   4319 O O     . GLU B 1 310 ? 33.513  -22.537 22.704  1.00 68.78  ? 282 GLU B O     1 
ATOM   4320 C CB    . GLU B 1 310 ? 30.638  -22.179 23.812  1.00 63.65  ? 282 GLU B CB    1 
ATOM   4321 C CG    . GLU B 1 310 ? 29.315  -22.571 24.449  1.00 67.24  ? 282 GLU B CG    1 
ATOM   4322 C CD    . GLU B 1 310 ? 28.804  -21.518 25.414  1.00 69.05  ? 282 GLU B CD    1 
ATOM   4323 O OE1   . GLU B 1 310 ? 29.624  -20.708 25.896  1.00 70.34  ? 282 GLU B OE1   1 
ATOM   4324 O OE2   . GLU B 1 310 ? 27.585  -21.500 25.688  1.00 68.21  ? 282 GLU B OE2   1 
ATOM   4325 N N     . TYR B 1 311 ? 32.227  -22.375 20.857  1.00 58.17  ? 283 TYR B N     1 
ATOM   4326 C CA    . TYR B 1 311 ? 33.289  -21.887 19.987  1.00 56.32  ? 283 TYR B CA    1 
ATOM   4327 C C     . TYR B 1 311 ? 32.959  -20.478 19.514  1.00 51.22  ? 283 TYR B C     1 
ATOM   4328 O O     . TYR B 1 311 ? 31.805  -20.177 19.192  1.00 51.60  ? 283 TYR B O     1 
ATOM   4329 C CB    . TYR B 1 311 ? 33.491  -22.825 18.792  1.00 54.98  ? 283 TYR B CB    1 
ATOM   4330 C CG    . TYR B 1 311 ? 33.923  -24.219 19.194  1.00 58.76  ? 283 TYR B CG    1 
ATOM   4331 C CD1   . TYR B 1 311 ? 32.995  -25.162 19.617  1.00 60.44  ? 283 TYR B CD1   1 
ATOM   4332 C CD2   . TYR B 1 311 ? 35.262  -24.588 19.165  1.00 63.09  ? 283 TYR B CD2   1 
ATOM   4333 C CE1   . TYR B 1 311 ? 33.385  -26.434 19.992  1.00 62.80  ? 283 TYR B CE1   1 
ATOM   4334 C CE2   . TYR B 1 311 ? 35.661  -25.858 19.538  1.00 68.56  ? 283 TYR B CE2   1 
ATOM   4335 C CZ    . TYR B 1 311 ? 34.719  -26.776 19.950  1.00 63.67  ? 283 TYR B CZ    1 
ATOM   4336 O OH    . TYR B 1 311 ? 35.112  -28.042 20.322  1.00 59.51  ? 283 TYR B OH    1 
ATOM   4337 N N     . TYR B 1 312 ? 33.976  -19.618 19.468  1.00 51.45  ? 284 TYR B N     1 
ATOM   4338 C CA    . TYR B 1 312 ? 33.778  -18.194 19.247  1.00 50.28  ? 284 TYR B CA    1 
ATOM   4339 C C     . TYR B 1 312 ? 34.746  -17.663 18.198  1.00 50.77  ? 284 TYR B C     1 
ATOM   4340 O O     . TYR B 1 312 ? 35.773  -18.276 17.895  1.00 52.32  ? 284 TYR B O     1 
ATOM   4341 C CB    . TYR B 1 312 ? 33.956  -17.401 20.549  1.00 51.90  ? 284 TYR B CB    1 
ATOM   4342 C CG    . TYR B 1 312 ? 32.868  -17.641 21.567  1.00 54.68  ? 284 TYR B CG    1 
ATOM   4343 C CD1   . TYR B 1 312 ? 32.982  -18.657 22.506  1.00 59.50  ? 284 TYR B CD1   1 
ATOM   4344 C CD2   . TYR B 1 312 ? 31.727  -16.851 21.591  1.00 56.55  ? 284 TYR B CD2   1 
ATOM   4345 C CE1   . TYR B 1 312 ? 31.988  -18.881 23.440  1.00 63.86  ? 284 TYR B CE1   1 
ATOM   4346 C CE2   . TYR B 1 312 ? 30.728  -17.067 22.520  1.00 56.63  ? 284 TYR B CE2   1 
ATOM   4347 C CZ    . TYR B 1 312 ? 30.863  -18.082 23.442  1.00 61.69  ? 284 TYR B CZ    1 
ATOM   4348 O OH    . TYR B 1 312 ? 29.870  -18.300 24.369  1.00 60.66  ? 284 TYR B OH    1 
ATOM   4349 N N     . ILE B 1 313 ? 34.395  -16.500 17.648  1.00 49.52  ? 285 ILE B N     1 
ATOM   4350 C CA    . ILE B 1 313 ? 35.255  -15.724 16.760  1.00 49.73  ? 285 ILE B CA    1 
ATOM   4351 C C     . ILE B 1 313 ? 35.180  -14.271 17.208  1.00 48.87  ? 285 ILE B C     1 
ATOM   4352 O O     . ILE B 1 313 ? 34.097  -13.674 17.201  1.00 47.55  ? 285 ILE B O     1 
ATOM   4353 C CB    . ILE B 1 313 ? 34.845  -15.853 15.282  1.00 49.29  ? 285 ILE B CB    1 
ATOM   4354 C CG1   . ILE B 1 313 ? 35.028  -17.288 14.788  1.00 50.33  ? 285 ILE B CG1   1 
ATOM   4355 C CG2   . ILE B 1 313 ? 35.645  -14.888 14.422  1.00 49.40  ? 285 ILE B CG2   1 
ATOM   4356 C CD1   . ILE B 1 313 ? 34.521  -17.514 13.379  1.00 49.97  ? 285 ILE B CD1   1 
ATOM   4357 N N     . HIS B 1 314 ? 36.319  -13.705 17.595  1.00 49.70  ? 286 HIS B N     1 
ATOM   4358 C CA    . HIS B 1 314 ? 36.373  -12.352 18.129  1.00 49.13  ? 286 HIS B CA    1 
ATOM   4359 C C     . HIS B 1 314 ? 36.852  -11.365 17.072  1.00 48.95  ? 286 HIS B C     1 
ATOM   4360 O O     . HIS B 1 314 ? 37.711  -11.679 16.244  1.00 49.85  ? 286 HIS B O     1 
ATOM   4361 C CB    . HIS B 1 314 ? 37.288  -12.286 19.353  1.00 50.21  ? 286 HIS B CB    1 
ATOM   4362 C CG    . HIS B 1 314 ? 37.002  -13.340 20.375  1.00 52.35  ? 286 HIS B CG    1 
ATOM   4363 N ND1   . HIS B 1 314 ? 36.021  -13.198 21.333  1.00 55.52  ? 286 HIS B ND1   1 
ATOM   4364 C CD2   . HIS B 1 314 ? 37.563  -14.554 20.588  1.00 58.79  ? 286 HIS B CD2   1 
ATOM   4365 C CE1   . HIS B 1 314 ? 35.992  -14.278 22.093  1.00 64.30  ? 286 HIS B CE1   1 
ATOM   4366 N NE2   . HIS B 1 314 ? 36.917  -15.116 21.661  1.00 61.97  ? 286 HIS B NE2   1 
ATOM   4367 N N     . LEU B 1 315 ? 36.294  -10.158 17.125  1.00 47.86  ? 287 LEU B N     1 
ATOM   4368 C CA    . LEU B 1 315 ? 36.547  -9.123  16.132  1.00 47.52  ? 287 LEU B CA    1 
ATOM   4369 C C     . LEU B 1 315 ? 35.852  -7.841  16.573  1.00 46.38  ? 287 LEU B C     1 
ATOM   4370 O O     . LEU B 1 315 ? 34.931  -7.867  17.394  1.00 45.65  ? 287 LEU B O     1 
ATOM   4371 C CB    . LEU B 1 315 ? 36.075  -9.568  14.742  1.00 47.10  ? 287 LEU B CB    1 
ATOM   4372 C CG    . LEU B 1 315 ? 34.603  -9.969  14.607  1.00 45.89  ? 287 LEU B CG    1 
ATOM   4373 C CD1   . LEU B 1 315 ? 33.764  -8.827  14.089  1.00 44.59  ? 287 LEU B CD1   1 
ATOM   4374 C CD2   . LEU B 1 315 ? 34.448  -11.195 13.720  1.00 46.27  ? 287 LEU B CD2   1 
ATOM   4375 N N     . SER B 1 316 ? 36.313  -6.718  16.024  1.00 46.34  ? 288 SER B N     1 
ATOM   4376 C CA    . SER B 1 316 ? 35.785  -5.398  16.345  1.00 45.42  ? 288 SER B CA    1 
ATOM   4377 C C     . SER B 1 316 ? 34.985  -4.855  15.168  1.00 44.34  ? 288 SER B C     1 
ATOM   4378 O O     . SER B 1 316 ? 35.390  -5.001  14.011  1.00 45.53  ? 288 SER B O     1 
ATOM   4379 C CB    . SER B 1 316 ? 36.914  -4.426  16.702  1.00 46.28  ? 288 SER B CB    1 
ATOM   4380 O OG    . SER B 1 316 ? 37.644  -4.885  17.826  1.00 52.13  ? 288 SER B OG    1 
ATOM   4381 N N     . VAL B 1 317 ? 33.851  -4.222  15.468  1.00 43.14  ? 289 VAL B N     1 
ATOM   4382 C CA    . VAL B 1 317 ? 32.922  -3.735  14.455  1.00 42.06  ? 289 VAL B CA    1 
ATOM   4383 C C     . VAL B 1 317 ? 32.657  -2.255  14.685  1.00 41.45  ? 289 VAL B C     1 
ATOM   4384 O O     . VAL B 1 317 ? 32.421  -1.831  15.821  1.00 44.51  ? 289 VAL B O     1 
ATOM   4385 C CB    . VAL B 1 317 ? 31.592  -4.515  14.473  1.00 42.23  ? 289 VAL B CB    1 
ATOM   4386 C CG1   . VAL B 1 317 ? 30.605  -3.914  13.481  1.00 47.44  ? 289 VAL B CG1   1 
ATOM   4387 C CG2   . VAL B 1 317 ? 31.827  -5.968  14.151  1.00 41.81  ? 289 VAL B CG2   1 
ATOM   4388 N N     . ILE B 1 318 ? 32.690  -1.475  13.607  1.00 41.18  ? 290 ILE B N     1 
ATOM   4389 C CA    . ILE B 1 318 ? 32.201  -0.103  13.622  1.00 40.68  ? 290 ILE B CA    1 
ATOM   4390 C C     . ILE B 1 318 ? 30.753  -0.108  13.154  1.00 41.16  ? 290 ILE B C     1 
ATOM   4391 O O     . ILE B 1 318 ? 30.435  -0.665  12.096  1.00 44.47  ? 290 ILE B O     1 
ATOM   4392 C CB    . ILE B 1 318 ? 33.060  0.805   12.727  1.00 40.97  ? 290 ILE B CB    1 
ATOM   4393 C CG1   . ILE B 1 318 ? 34.543  0.663   13.068  1.00 42.81  ? 290 ILE B CG1   1 
ATOM   4394 C CG2   . ILE B 1 318 ? 32.619  2.255   12.862  1.00 40.37  ? 290 ILE B CG2   1 
ATOM   4395 C CD1   . ILE B 1 318 ? 35.459  1.215   11.997  1.00 51.23  ? 290 ILE B CD1   1 
ATOM   4396 N N     . THR B 1 319 ? 29.873  0.501   13.941  1.00 38.48  ? 291 THR B N     1 
ATOM   4397 C CA    . THR B 1 319 ? 28.477  0.683   13.572  1.00 37.83  ? 291 THR B CA    1 
ATOM   4398 C C     . THR B 1 319 ? 28.257  2.149   13.228  1.00 40.39  ? 291 THR B C     1 
ATOM   4399 O O     . THR B 1 319 ? 28.681  3.034   13.979  1.00 50.85  ? 291 THR B O     1 
ATOM   4400 C CB    . THR B 1 319 ? 27.542  0.252   14.705  1.00 40.78  ? 291 THR B CB    1 
ATOM   4401 O OG1   . THR B 1 319 ? 27.886  -1.073  15.130  1.00 46.82  ? 291 THR B OG1   1 
ATOM   4402 C CG2   . THR B 1 319 ? 26.097  0.263   14.235  1.00 39.76  ? 291 THR B CG2   1 
ATOM   4403 N N     . ALA B 1 320 ? 27.605  2.406   12.096  1.00 36.95  ? 292 ALA B N     1 
ATOM   4404 C CA    . ALA B 1 320 ? 27.465  3.766   11.599  1.00 37.29  ? 292 ALA B CA    1 
ATOM   4405 C C     . ALA B 1 320 ? 26.081  3.978   11.005  1.00 39.04  ? 292 ALA B C     1 
ATOM   4406 O O     . ALA B 1 320 ? 25.458  3.050   10.483  1.00 39.47  ? 292 ALA B O     1 
ATOM   4407 C CB    . ALA B 1 320 ? 28.533  4.091   10.549  1.00 40.53  ? 292 ALA B CB    1 
ATOM   4408 N N     . LEU B 1 321 ? 25.613  5.222   11.090  1.00 37.91  ? 293 LEU B N     1 
ATOM   4409 C CA    . LEU B 1 321 ? 24.339  5.638   10.510  1.00 37.30  ? 293 LEU B CA    1 
ATOM   4410 C C     . LEU B 1 321 ? 24.551  7.000   9.866   1.00 41.65  ? 293 LEU B C     1 
ATOM   4411 O O     . LEU B 1 321 ? 24.679  8.007   10.568  1.00 50.54  ? 293 LEU B O     1 
ATOM   4412 C CB    . LEU B 1 321 ? 23.236  5.699   11.568  1.00 39.05  ? 293 LEU B CB    1 
ATOM   4413 C CG    . LEU B 1 321 ? 21.925  6.364   11.144  1.00 38.38  ? 293 LEU B CG    1 
ATOM   4414 C CD1   . LEU B 1 321 ? 21.280  5.604   9.997   1.00 41.91  ? 293 LEU B CD1   1 
ATOM   4415 C CD2   . LEU B 1 321 ? 20.970  6.481   12.323  1.00 42.95  ? 293 LEU B CD2   1 
ATOM   4416 N N     . ALA B 1 322 ? 24.598  7.031   8.539   1.00 37.45  ? 294 ALA B N     1 
ATOM   4417 C CA    . ALA B 1 322 ? 24.824  8.255   7.786   1.00 38.52  ? 294 ALA B CA    1 
ATOM   4418 C C     . ALA B 1 322 ? 23.553  8.667   7.055   1.00 43.42  ? 294 ALA B C     1 
ATOM   4419 O O     . ALA B 1 322 ? 22.550  7.951   7.044   1.00 49.13  ? 294 ALA B O     1 
ATOM   4420 C CB    . ALA B 1 322 ? 25.980  8.076   6.794   1.00 42.29  ? 294 ALA B CB    1 
ATOM   4421 N N     . ARG B 1 323 ? 23.607  9.847   6.439   1.00 45.46  ? 295 ARG B N     1 
ATOM   4422 C CA    . ARG B 1 323 ? 22.485  10.363  5.667   1.00 45.44  ? 295 ARG B CA    1 
ATOM   4423 C C     . ARG B 1 323 ? 23.010  11.227  4.532   1.00 48.94  ? 295 ARG B C     1 
ATOM   4424 O O     . ARG B 1 323 ? 23.800  12.147  4.764   1.00 49.52  ? 295 ARG B O     1 
ATOM   4425 C CB    . ARG B 1 323 ? 21.527  11.174  6.547   1.00 44.51  ? 295 ARG B CB    1 
ATOM   4426 C CG    . ARG B 1 323 ? 20.327  11.728  5.793   1.00 50.64  ? 295 ARG B CG    1 
ATOM   4427 C CD    . ARG B 1 323 ? 19.439  12.569  6.694   1.00 55.83  ? 295 ARG B CD    1 
ATOM   4428 N NE    . ARG B 1 323 ? 18.822  11.772  7.747   1.00 58.51  ? 295 ARG B NE    1 
ATOM   4429 C CZ    . ARG B 1 323 ? 18.351  12.268  8.883   1.00 60.08  ? 295 ARG B CZ    1 
ATOM   4430 N NH1   . ARG B 1 323 ? 18.416  13.561  9.153   1.00 65.62  ? 295 ARG B NH1   1 
ATOM   4431 N NH2   . ARG B 1 323 ? 17.799  11.445  9.770   1.00 57.54  ? 295 ARG B NH2   1 
ATOM   4432 N N     . LYS B 1 324 ? 22.571  10.928  3.312   1.00 47.02  ? 296 LYS B N     1 
ATOM   4433 C CA    . LYS B 1 324 ? 22.945  11.738  2.162   1.00 47.29  ? 296 LYS B CA    1 
ATOM   4434 C C     . LYS B 1 324 ? 22.249  13.092  2.223   1.00 49.28  ? 296 LYS B C     1 
ATOM   4435 O O     . LYS B 1 324 ? 21.100  13.199  2.661   1.00 46.13  ? 296 LYS B O     1 
ATOM   4436 C CB    . LYS B 1 324 ? 22.587  11.017  0.861   1.00 45.15  ? 296 LYS B CB    1 
ATOM   4437 C CG    . LYS B 1 324 ? 22.887  11.817  -0.399  1.00 43.91  ? 296 LYS B CG    1 
ATOM   4438 C CD    . LYS B 1 324 ? 22.495  11.065  -1.660  1.00 40.96  ? 296 LYS B CD    1 
ATOM   4439 C CE    . LYS B 1 324 ? 22.744  11.916  -2.897  1.00 46.42  ? 296 LYS B CE    1 
ATOM   4440 N NZ    . LYS B 1 324 ? 22.479  11.174  -4.160  1.00 42.45  ? 296 LYS B NZ    1 
ATOM   4441 N N     . PHE B 1 325 ? 22.954  14.130  1.787   1.00 56.16  ? 297 PHE B N     1 
ATOM   4442 C CA    . PHE B 1 325 ? 22.404  15.479  1.786   1.00 59.05  ? 297 PHE B CA    1 
ATOM   4443 C C     . PHE B 1 325 ? 21.604  15.745  0.514   1.00 60.69  ? 297 PHE B C     1 
ATOM   4444 O O     . PHE B 1 325 ? 21.994  15.327  -0.577  1.00 59.23  ? 297 PHE B O     1 
ATOM   4445 C CB    . PHE B 1 325 ? 23.522  16.512  1.931   1.00 57.02  ? 297 PHE B CB    1 
ATOM   4446 C CG    . PHE B 1 325 ? 23.882  16.813  3.356   1.00 53.93  ? 297 PHE B CG    1 
ATOM   4447 C CD1   . PHE B 1 325 ? 23.111  17.680  4.111   1.00 59.38  ? 297 PHE B CD1   1 
ATOM   4448 C CD2   . PHE B 1 325 ? 24.992  16.228  3.940   1.00 53.12  ? 297 PHE B CD2   1 
ATOM   4449 C CE1   . PHE B 1 325 ? 23.440  17.959  5.424   1.00 64.41  ? 297 PHE B CE1   1 
ATOM   4450 C CE2   . PHE B 1 325 ? 25.328  16.502  5.252   1.00 57.38  ? 297 PHE B CE2   1 
ATOM   4451 C CZ    . PHE B 1 325 ? 24.551  17.369  5.995   1.00 59.58  ? 297 PHE B CZ    1 
ATOM   4452 N N     . ALA C 1 43  ? -37.335 19.771  -15.727 1.00 61.88  ? 15  ALA C N     1 
ATOM   4453 C CA    . ALA C 1 43  ? -37.255 18.703  -14.736 1.00 63.56  ? 15  ALA C CA    1 
ATOM   4454 C C     . ALA C 1 43  ? -36.138 18.965  -13.731 1.00 77.17  ? 15  ALA C C     1 
ATOM   4455 O O     . ALA C 1 43  ? -35.632 20.083  -13.630 1.00 88.76  ? 15  ALA C O     1 
ATOM   4456 C CB    . ALA C 1 43  ? -37.050 17.362  -15.418 1.00 63.32  ? 15  ALA C CB    1 
ATOM   4457 N N     . TYR C 1 44  ? -35.749 17.929  -12.991 1.00 70.88  ? 16  TYR C N     1 
ATOM   4458 C CA    . TYR C 1 44  ? -34.739 18.060  -11.942 1.00 66.37  ? 16  TYR C CA    1 
ATOM   4459 C C     . TYR C 1 44  ? -33.362 17.782  -12.531 1.00 64.51  ? 16  TYR C C     1 
ATOM   4460 O O     . TYR C 1 44  ? -32.938 16.629  -12.637 1.00 64.02  ? 16  TYR C O     1 
ATOM   4461 C CB    . TYR C 1 44  ? -35.034 17.123  -10.777 1.00 63.90  ? 16  TYR C CB    1 
ATOM   4462 C CG    . TYR C 1 44  ? -34.206 17.432  -9.549  1.00 63.55  ? 16  TYR C CG    1 
ATOM   4463 C CD1   . TYR C 1 44  ? -34.313 18.660  -8.912  1.00 71.38  ? 16  TYR C CD1   1 
ATOM   4464 C CD2   . TYR C 1 44  ? -33.305 16.504  -9.037  1.00 56.20  ? 16  TYR C CD2   1 
ATOM   4465 C CE1   . TYR C 1 44  ? -33.558 18.957  -7.793  1.00 71.49  ? 16  TYR C CE1   1 
ATOM   4466 C CE2   . TYR C 1 44  ? -32.543 16.792  -7.914  1.00 56.67  ? 16  TYR C CE2   1 
ATOM   4467 C CZ    . TYR C 1 44  ? -32.674 18.021  -7.299  1.00 61.24  ? 16  TYR C CZ    1 
ATOM   4468 O OH    . TYR C 1 44  ? -31.923 18.320  -6.184  1.00 54.72  ? 16  TYR C OH    1 
ATOM   4469 N N     . ARG C 1 45  ? -32.659 18.846  -12.915 1.00 65.32  ? 17  ARG C N     1 
ATOM   4470 C CA    . ARG C 1 45  ? -31.239 18.753  -13.249 1.00 63.70  ? 17  ARG C CA    1 
ATOM   4471 C C     . ARG C 1 45  ? -30.402 18.993  -11.995 1.00 64.95  ? 17  ARG C C     1 
ATOM   4472 O O     . ARG C 1 45  ? -29.604 19.924  -11.903 1.00 66.43  ? 17  ARG C O     1 
ATOM   4473 C CB    . ARG C 1 45  ? -30.878 19.735  -14.359 1.00 67.96  ? 17  ARG C CB    1 
ATOM   4474 C CG    . ARG C 1 45  ? -31.515 19.419  -15.696 1.00 76.34  ? 17  ARG C CG    1 
ATOM   4475 C CD    . ARG C 1 45  ? -30.767 18.290  -16.415 1.00 77.84  ? 17  ARG C CD    1 
ATOM   4476 N NE    . ARG C 1 45  ? -29.433 18.629  -16.907 1.00 76.37  ? 17  ARG C NE    1 
ATOM   4477 C CZ    . ARG C 1 45  ? -29.116 19.687  -17.646 1.00 76.70  ? 17  ARG C CZ    1 
ATOM   4478 N NH1   . ARG C 1 45  ? -30.029 20.557  -18.049 1.00 79.35  ? 17  ARG C NH1   1 
ATOM   4479 N NH2   . ARG C 1 45  ? -27.850 19.863  -18.017 1.00 68.57  ? 17  ARG C NH2   1 
ATOM   4480 N N     . GLY C 1 46  ? -30.633 18.131  -11.009 1.00 64.07  ? 18  GLY C N     1 
ATOM   4481 C CA    . GLY C 1 46  ? -29.936 18.158  -9.743  1.00 57.75  ? 18  GLY C CA    1 
ATOM   4482 C C     . GLY C 1 46  ? -30.061 19.493  -9.040  1.00 57.61  ? 18  GLY C C     1 
ATOM   4483 O O     . GLY C 1 46  ? -31.041 20.231  -9.197  1.00 60.35  ? 18  GLY C O     1 
ATOM   4484 N N     . ILE C 1 47  ? -29.041 19.812  -8.252  1.00 56.78  ? 19  ILE C N     1 
ATOM   4485 C CA    . ILE C 1 47  ? -28.985 21.057  -7.497  1.00 56.70  ? 19  ILE C CA    1 
ATOM   4486 C C     . ILE C 1 47  ? -28.181 22.074  -8.294  1.00 53.58  ? 19  ILE C C     1 
ATOM   4487 O O     . ILE C 1 47  ? -27.000 21.851  -8.587  1.00 54.15  ? 19  ILE C O     1 
ATOM   4488 C CB    . ILE C 1 47  ? -28.371 20.845  -6.105  1.00 48.97  ? 19  ILE C CB    1 
ATOM   4489 C CG1   . ILE C 1 47  ? -29.021 19.649  -5.409  1.00 55.78  ? 19  ILE C CG1   1 
ATOM   4490 C CG2   . ILE C 1 47  ? -28.492 22.113  -5.279  1.00 49.16  ? 19  ILE C CG2   1 
ATOM   4491 C CD1   . ILE C 1 47  ? -28.920 19.691  -3.902  1.00 49.10  ? 19  ILE C CD1   1 
ATOM   4492 N N     . ASP C 1 48  ? -28.821 23.183  -8.652  1.00 53.29  ? 20  ASP C N     1 
ATOM   4493 C CA    . ASP C 1 48  ? -28.116 24.321  -9.215  1.00 48.90  ? 20  ASP C CA    1 
ATOM   4494 C C     . ASP C 1 48  ? -27.581 25.169  -8.064  1.00 57.26  ? 20  ASP C C     1 
ATOM   4495 O O     . ASP C 1 48  ? -27.575 24.739  -6.908  1.00 62.32  ? 20  ASP C O     1 
ATOM   4496 C CB    . ASP C 1 48  ? -29.033 25.126  -10.133 1.00 50.47  ? 20  ASP C CB    1 
ATOM   4497 C CG    . ASP C 1 48  ? -30.398 25.366  -9.522  1.00 61.57  ? 20  ASP C CG    1 
ATOM   4498 O OD1   . ASP C 1 48  ? -30.630 24.916  -8.380  1.00 66.27  ? 20  ASP C OD1   1 
ATOM   4499 O OD2   . ASP C 1 48  ? -31.237 26.016  -10.179 1.00 65.95  ? 20  ASP C OD2   1 
ATOM   4500 N N     . LYS C 1 49  ? -27.150 26.387  -8.370  1.00 55.58  ? 21  LYS C N     1 
ATOM   4501 C CA    . LYS C 1 49  ? -26.603 27.314  -7.385  1.00 57.23  ? 21  LYS C CA    1 
ATOM   4502 C C     . LYS C 1 49  ? -25.561 26.630  -6.488  1.00 60.29  ? 21  LYS C C     1 
ATOM   4503 O O     . LYS C 1 49  ? -25.757 26.518  -5.283  1.00 55.19  ? 21  LYS C O     1 
ATOM   4504 C CB    . LYS C 1 49  ? -27.715 27.923  -6.546  1.00 48.58  ? 21  LYS C CB    1 
ATOM   4505 N N     . PRO C 1 50  ? -24.450 26.155  -7.066  1.00 54.95  ? 22  PRO C N     1 
ATOM   4506 C CA    . PRO C 1 50  ? -23.449 25.461  -6.242  1.00 48.09  ? 22  PRO C CA    1 
ATOM   4507 C C     . PRO C 1 50  ? -22.780 26.361  -5.223  1.00 58.43  ? 22  PRO C C     1 
ATOM   4508 O O     . PRO C 1 50  ? -22.188 25.849  -4.265  1.00 57.02  ? 22  PRO C O     1 
ATOM   4509 C CB    . PRO C 1 50  ? -22.442 24.943  -7.278  1.00 43.29  ? 22  PRO C CB    1 
ATOM   4510 C CG    . PRO C 1 50  ? -22.578 25.884  -8.425  1.00 50.58  ? 22  PRO C CG    1 
ATOM   4511 C CD    . PRO C 1 50  ? -24.033 26.249  -8.476  1.00 56.04  ? 22  PRO C CD    1 
ATOM   4512 N N     . HIS C 1 51  ? -22.857 27.682  -5.398  1.00 59.54  ? 23  HIS C N     1 
ATOM   4513 C CA    . HIS C 1 51  ? -22.266 28.594  -4.426  1.00 59.10  ? 23  HIS C CA    1 
ATOM   4514 C C     . HIS C 1 51  ? -22.941 28.463  -3.068  1.00 57.32  ? 23  HIS C C     1 
ATOM   4515 O O     . HIS C 1 51  ? -22.282 28.552  -2.026  1.00 58.77  ? 23  HIS C O     1 
ATOM   4516 C CB    . HIS C 1 51  ? -22.361 30.032  -4.937  1.00 60.61  ? 23  HIS C CB    1 
ATOM   4517 C CG    . HIS C 1 51  ? -21.194 30.454  -5.774  1.00 71.84  ? 23  HIS C CG    1 
ATOM   4518 N ND1   . HIS C 1 51  ? -20.783 29.750  -6.885  1.00 78.77  ? 23  HIS C ND1   1 
ATOM   4519 C CD2   . HIS C 1 51  ? -20.349 31.506  -5.661  1.00 73.68  ? 23  HIS C CD2   1 
ATOM   4520 C CE1   . HIS C 1 51  ? -19.736 30.350  -7.422  1.00 75.58  ? 23  HIS C CE1   1 
ATOM   4521 N NE2   . HIS C 1 51  ? -19.452 31.418  -6.698  1.00 76.64  ? 23  HIS C NE2   1 
ATOM   4522 N N     . LEU C 1 52  ? -24.256 28.239  -3.058  1.00 56.51  ? 24  LEU C N     1 
ATOM   4523 C CA    . LEU C 1 52  ? -24.978 28.133  -1.796  1.00 51.88  ? 24  LEU C CA    1 
ATOM   4524 C C     . LEU C 1 52  ? -24.761 26.789  -1.114  1.00 52.57  ? 24  LEU C C     1 
ATOM   4525 O O     . LEU C 1 52  ? -24.883 26.698  0.113   1.00 50.86  ? 24  LEU C O     1 
ATOM   4526 C CB    . LEU C 1 52  ? -26.472 28.365  -2.024  1.00 46.53  ? 24  LEU C CB    1 
ATOM   4527 C CG    . LEU C 1 52  ? -26.866 29.780  -2.447  1.00 47.23  ? 24  LEU C CG    1 
ATOM   4528 C CD1   . LEU C 1 52  ? -28.376 29.904  -2.580  1.00 49.32  ? 24  LEU C CD1   1 
ATOM   4529 C CD2   . LEU C 1 52  ? -26.322 30.800  -1.461  1.00 50.52  ? 24  LEU C CD2   1 
ATOM   4530 N N     . TYR C 1 53  ? -24.439 25.741  -1.876  1.00 51.96  ? 25  TYR C N     1 
ATOM   4531 C CA    . TYR C 1 53  ? -24.305 24.421  -1.271  1.00 47.31  ? 25  TYR C CA    1 
ATOM   4532 C C     . TYR C 1 53  ? -22.998 24.268  -0.503  1.00 47.45  ? 25  TYR C C     1 
ATOM   4533 O O     . TYR C 1 53  ? -22.963 23.587  0.528   1.00 44.11  ? 25  TYR C O     1 
ATOM   4534 C CB    . TYR C 1 53  ? -24.427 23.328  -2.332  1.00 47.33  ? 25  TYR C CB    1 
ATOM   4535 C CG    . TYR C 1 53  ? -24.590 21.957  -1.720  1.00 44.65  ? 25  TYR C CG    1 
ATOM   4536 C CD1   . TYR C 1 53  ? -25.842 21.476  -1.366  1.00 43.09  ? 25  TYR C CD1   1 
ATOM   4537 C CD2   . TYR C 1 53  ? -23.487 21.149  -1.483  1.00 44.26  ? 25  TYR C CD2   1 
ATOM   4538 C CE1   . TYR C 1 53  ? -25.990 20.228  -0.794  1.00 43.19  ? 25  TYR C CE1   1 
ATOM   4539 C CE2   . TYR C 1 53  ? -23.624 19.900  -0.916  1.00 42.23  ? 25  TYR C CE2   1 
ATOM   4540 C CZ    . TYR C 1 53  ? -24.876 19.443  -0.574  1.00 43.97  ? 25  TYR C CZ    1 
ATOM   4541 O OH    . TYR C 1 53  ? -25.005 18.197  -0.007  1.00 52.01  ? 25  TYR C OH    1 
ATOM   4542 N N     . THR C 1 54  ? -21.914 24.886  -0.981  1.00 45.92  ? 26  THR C N     1 
ATOM   4543 C CA    . THR C 1 54  ? -20.641 24.789  -0.273  1.00 40.80  ? 26  THR C CA    1 
ATOM   4544 C C     . THR C 1 54  ? -20.684 25.433  1.105   1.00 47.87  ? 26  THR C C     1 
ATOM   4545 O O     . THR C 1 54  ? -19.727 25.277  1.870   1.00 57.69  ? 26  THR C O     1 
ATOM   4546 C CB    . THR C 1 54  ? -19.518 25.419  -1.097  1.00 41.62  ? 26  THR C CB    1 
ATOM   4547 O OG1   . THR C 1 54  ? -19.932 26.704  -1.577  1.00 51.69  ? 26  THR C OG1   1 
ATOM   4548 C CG2   . THR C 1 54  ? -19.161 24.527  -2.270  1.00 46.20  ? 26  THR C CG2   1 
ATOM   4549 N N     . LEU C 1 55  ? -21.760 26.149  1.439   1.00 49.03  ? 27  LEU C N     1 
ATOM   4550 C CA    . LEU C 1 55  ? -21.931 26.648  2.796   1.00 44.27  ? 27  LEU C CA    1 
ATOM   4551 C C     . LEU C 1 55  ? -22.101 25.517  3.801   1.00 44.74  ? 27  LEU C C     1 
ATOM   4552 O O     . LEU C 1 55  ? -21.872 25.725  4.997   1.00 47.88  ? 27  LEU C O     1 
ATOM   4553 C CB    . LEU C 1 55  ? -23.130 27.594  2.856   1.00 42.93  ? 27  LEU C CB    1 
ATOM   4554 C CG    . LEU C 1 55  ? -22.936 28.926  2.128   1.00 43.65  ? 27  LEU C CG    1 
ATOM   4555 C CD1   . LEU C 1 55  ? -24.237 29.703  2.072   1.00 43.95  ? 27  LEU C CD1   1 
ATOM   4556 C CD2   . LEU C 1 55  ? -21.844 29.750  2.794   1.00 48.61  ? 27  LEU C CD2   1 
ATOM   4557 N N     . GLY C 1 56  ? -22.496 24.332  3.343   1.00 42.99  ? 28  GLY C N     1 
ATOM   4558 C CA    . GLY C 1 56  ? -22.560 23.149  4.170   1.00 41.60  ? 28  GLY C CA    1 
ATOM   4559 C C     . GLY C 1 56  ? -21.349 22.251  4.090   1.00 52.34  ? 28  GLY C C     1 
ATOM   4560 O O     . GLY C 1 56  ? -21.299 21.242  4.800   1.00 56.01  ? 28  GLY C O     1 
ATOM   4561 N N     . CYS C 1 57  ? -20.373 22.583  3.239   1.00 51.03  ? 29  CYS C N     1 
ATOM   4562 C CA    . CYS C 1 57  ? -19.141 21.802  3.159   1.00 55.19  ? 29  CYS C CA    1 
ATOM   4563 C C     . CYS C 1 57  ? -18.438 21.720  4.507   1.00 69.23  ? 29  CYS C C     1 
ATOM   4564 O O     . CYS C 1 57  ? -18.149 20.623  4.999   1.00 64.72  ? 29  CYS C O     1 
ATOM   4565 C CB    . CYS C 1 57  ? -18.203 22.397  2.111   1.00 55.78  ? 29  CYS C CB    1 
ATOM   4566 S SG    . CYS C 1 57  ? -16.634 21.522  1.987   1.00 58.44  ? 29  CYS C SG    1 
ATOM   4567 N N     . CYS C 1 58  ? -18.159 22.873  5.125   1.00 79.51  ? 30  CYS C N     1 
ATOM   4568 C CA    . CYS C 1 58  ? -17.456 22.894  6.408   1.00 76.35  ? 30  CYS C CA    1 
ATOM   4569 C C     . CYS C 1 58  ? -18.103 22.008  7.472   1.00 70.47  ? 30  CYS C C     1 
ATOM   4570 O O     . CYS C 1 58  ? -17.464 21.743  8.494   1.00 70.23  ? 30  CYS C O     1 
ATOM   4571 C CB    . CYS C 1 58  ? -17.340 24.336  6.930   1.00 78.24  ? 30  CYS C CB    1 
ATOM   4572 S SG    . CYS C 1 58  ? -16.764 25.635  5.765   1.00 107.64 ? 30  CYS C SG    1 
ATOM   4573 N N     . SER C 1 59  ? -19.330 21.537  7.256   1.00 73.90  ? 31  SER C N     1 
ATOM   4574 C CA    . SER C 1 59  ? -19.995 20.599  8.155   1.00 55.58  ? 31  SER C CA    1 
ATOM   4575 C C     . SER C 1 59  ? -20.242 19.233  7.533   1.00 49.86  ? 31  SER C C     1 
ATOM   4576 O O     . SER C 1 59  ? -20.061 18.214  8.204   1.00 44.98  ? 31  SER C O     1 
ATOM   4577 C CB    . SER C 1 59  ? -21.332 21.175  8.634   1.00 47.95  ? 31  SER C CB    1 
ATOM   4578 O OG    . SER C 1 59  ? -21.136 22.316  9.452   1.00 52.51  ? 31  SER C OG    1 
ATOM   4579 N N     . LEU C 1 60  ? -20.663 19.186  6.265   1.00 61.20  ? 32  LEU C N     1 
ATOM   4580 C CA    . LEU C 1 60  ? -20.877 17.903  5.601   1.00 55.08  ? 32  LEU C CA    1 
ATOM   4581 C C     . LEU C 1 60  ? -19.569 17.157  5.379   1.00 55.70  ? 32  LEU C C     1 
ATOM   4582 O O     . LEU C 1 60  ? -19.566 15.922  5.325   1.00 53.64  ? 32  LEU C O     1 
ATOM   4583 C CB    . LEU C 1 60  ? -21.595 18.108  4.266   1.00 46.75  ? 32  LEU C CB    1 
ATOM   4584 C CG    . LEU C 1 60  ? -23.061 18.540  4.312   1.00 44.03  ? 32  LEU C CG    1 
ATOM   4585 C CD1   . LEU C 1 60  ? -23.586 18.787  2.908   1.00 40.93  ? 32  LEU C CD1   1 
ATOM   4586 C CD2   . LEU C 1 60  ? -23.903 17.494  5.024   1.00 47.04  ? 32  LEU C CD2   1 
ATOM   4587 N N     . THR C 1 61  ? -18.456 17.881  5.238   1.00 61.27  ? 33  THR C N     1 
ATOM   4588 C CA    . THR C 1 61  ? -17.160 17.226  5.089   1.00 61.68  ? 33  THR C CA    1 
ATOM   4589 C C     . THR C 1 61  ? -16.819 16.409  6.327   1.00 59.34  ? 33  THR C C     1 
ATOM   4590 O O     . THR C 1 61  ? -16.385 15.256  6.225   1.00 57.00  ? 33  THR C O     1 
ATOM   4591 C CB    . THR C 1 61  ? -16.073 18.267  4.810   1.00 64.35  ? 33  THR C CB    1 
ATOM   4592 O OG1   . THR C 1 61  ? -16.348 18.927  3.568   1.00 68.74  ? 33  THR C OG1   1 
ATOM   4593 C CG2   . THR C 1 61  ? -14.702 17.614  4.742   1.00 59.50  ? 33  THR C CG2   1 
ATOM   4594 N N     . ALA C 1 62  ? -17.026 16.988  7.512   1.00 60.18  ? 34  ALA C N     1 
ATOM   4595 C CA    . ALA C 1 62  ? -16.735 16.271  8.747   1.00 61.92  ? 34  ALA C CA    1 
ATOM   4596 C C     . ALA C 1 62  ? -17.693 15.106  8.965   1.00 58.91  ? 34  ALA C C     1 
ATOM   4597 O O     . ALA C 1 62  ? -17.305 14.092  9.555   1.00 60.10  ? 34  ALA C O     1 
ATOM   4598 C CB    . ALA C 1 62  ? -16.788 17.230  9.936   1.00 67.16  ? 34  ALA C CB    1 
ATOM   4599 N N     . MET C 1 63  ? -18.937 15.228  8.499   1.00 54.57  ? 35  MET C N     1 
ATOM   4600 C CA    . MET C 1 63  ? -19.916 14.168  8.721   1.00 58.62  ? 35  MET C CA    1 
ATOM   4601 C C     . MET C 1 63  ? -19.586 12.930  7.896   1.00 59.82  ? 35  MET C C     1 
ATOM   4602 O O     . MET C 1 63  ? -19.505 11.819  8.432   1.00 64.34  ? 35  MET C O     1 
ATOM   4603 C CB    . MET C 1 63  ? -21.321 14.669  8.395   1.00 60.45  ? 35  MET C CB    1 
ATOM   4604 C CG    . MET C 1 63  ? -22.397 13.607  8.557   1.00 67.36  ? 35  MET C CG    1 
ATOM   4605 S SD    . MET C 1 63  ? -23.961 14.084  7.803   1.00 71.75  ? 35  MET C SD    1 
ATOM   4606 C CE    . MET C 1 63  ? -24.192 15.705  8.527   1.00 60.52  ? 35  MET C CE    1 
ATOM   4607 N N     . ALA C 1 64  ? -19.404 13.101  6.585   1.00 59.28  ? 36  ALA C N     1 
ATOM   4608 C CA    . ALA C 1 64  ? -19.061 11.964  5.739   1.00 56.97  ? 36  ALA C CA    1 
ATOM   4609 C C     . ALA C 1 64  ? -17.679 11.417  6.069   1.00 55.15  ? 36  ALA C C     1 
ATOM   4610 O O     . ALA C 1 64  ? -17.430 10.219  5.894   1.00 53.02  ? 36  ALA C O     1 
ATOM   4611 C CB    . ALA C 1 64  ? -19.142 12.360  4.267   1.00 60.13  ? 36  ALA C CB    1 
ATOM   4612 N N     . SER C 1 65  ? -16.772 12.274  6.543   1.00 61.49  ? 37  SER C N     1 
ATOM   4613 C CA    . SER C 1 65  ? -15.482 11.789  7.021   1.00 63.15  ? 37  SER C CA    1 
ATOM   4614 C C     . SER C 1 65  ? -15.647 10.891  8.238   1.00 63.75  ? 37  SER C C     1 
ATOM   4615 O O     . SER C 1 65  ? -14.882 9.935   8.413   1.00 65.45  ? 37  SER C O     1 
ATOM   4616 C CB    . SER C 1 65  ? -14.564 12.967  7.352   1.00 63.58  ? 37  SER C CB    1 
ATOM   4617 O OG    . SER C 1 65  ? -13.257 12.527  7.675   1.00 66.76  ? 37  SER C OG    1 
ATOM   4618 N N     . ALA C 1 66  ? -16.638 11.177  9.085   1.00 61.20  ? 38  ALA C N     1 
ATOM   4619 C CA    . ALA C 1 66  ? -16.871 10.345  10.260  1.00 60.86  ? 38  ALA C CA    1 
ATOM   4620 C C     . ALA C 1 66  ? -17.516 9.018   9.879   1.00 60.23  ? 38  ALA C C     1 
ATOM   4621 O O     . ALA C 1 66  ? -17.202 7.978   10.470  1.00 60.57  ? 38  ALA C O     1 
ATOM   4622 C CB    . ALA C 1 66  ? -17.740 11.095  11.269  1.00 62.60  ? 38  ALA C CB    1 
ATOM   4623 N N     . GLN C 1 67  ? -18.421 9.034   8.897   1.00 65.64  ? 39  GLN C N     1 
ATOM   4624 C CA    . GLN C 1 67  ? -19.068 7.798   8.469   1.00 66.31  ? 39  GLN C CA    1 
ATOM   4625 C C     . GLN C 1 67  ? -18.063 6.834   7.851   1.00 67.21  ? 39  GLN C C     1 
ATOM   4626 O O     . GLN C 1 67  ? -18.098 5.629   8.125   1.00 65.45  ? 39  GLN C O     1 
ATOM   4627 C CB    . GLN C 1 67  ? -20.188 8.103   7.475   1.00 64.50  ? 39  GLN C CB    1 
ATOM   4628 C CG    . GLN C 1 67  ? -21.424 8.737   8.089   1.00 73.07  ? 39  GLN C CG    1 
ATOM   4629 C CD    . GLN C 1 67  ? -22.394 9.243   7.039   1.00 73.17  ? 39  GLN C CD    1 
ATOM   4630 O OE1   . GLN C 1 67  ? -22.005 9.540   5.909   1.00 70.31  ? 39  GLN C OE1   1 
ATOM   4631 N NE2   . GLN C 1 67  ? -23.667 9.341   7.407   1.00 71.57  ? 39  GLN C NE2   1 
ATOM   4632 N N     . LEU C 1 68  ? -17.159 7.348   7.013   1.00 70.59  ? 40  LEU C N     1 
ATOM   4633 C CA    . LEU C 1 68  ? -16.190 6.480   6.351   1.00 63.75  ? 40  LEU C CA    1 
ATOM   4634 C C     . LEU C 1 68  ? -15.213 5.875   7.350   1.00 66.08  ? 40  LEU C C     1 
ATOM   4635 O O     . LEU C 1 68  ? -14.785 4.726   7.188   1.00 65.86  ? 40  LEU C O     1 
ATOM   4636 C CB    . LEU C 1 68  ? -15.438 7.257   5.271   1.00 61.44  ? 40  LEU C CB    1 
ATOM   4637 C CG    . LEU C 1 68  ? -16.221 7.551   3.990   1.00 59.23  ? 40  LEU C CG    1 
ATOM   4638 C CD1   . LEU C 1 68  ? -15.369 8.343   3.014   1.00 54.08  ? 40  LEU C CD1   1 
ATOM   4639 C CD2   . LEU C 1 68  ? -16.711 6.261   3.354   1.00 54.18  ? 40  LEU C CD2   1 
ATOM   4640 N N     . ASP C 1 69  ? -14.847 6.631   8.389   1.00 67.95  ? 41  ASP C N     1 
ATOM   4641 C CA    . ASP C 1 69  ? -13.944 6.098   9.403   1.00 69.32  ? 41  ASP C CA    1 
ATOM   4642 C C     . ASP C 1 69  ? -14.554 4.901   10.118  1.00 64.98  ? 41  ASP C C     1 
ATOM   4643 O O     . ASP C 1 69  ? -13.826 4.010   10.571  1.00 67.38  ? 41  ASP C O     1 
ATOM   4644 C CB    . ASP C 1 69  ? -13.579 7.190   10.409  1.00 68.94  ? 41  ASP C CB    1 
ATOM   4645 C CG    . ASP C 1 69  ? -12.595 8.197   9.844   1.00 72.73  ? 41  ASP C CG    1 
ATOM   4646 O OD1   . ASP C 1 69  ? -12.012 7.925   8.773   1.00 71.48  ? 41  ASP C OD1   1 
ATOM   4647 O OD2   . ASP C 1 69  ? -12.404 9.260   10.472  1.00 70.33  ? 41  ASP C OD2   1 
ATOM   4648 N N     . ALA C 1 70  ? -15.884 4.857   10.225  1.00 60.18  ? 42  ALA C N     1 
ATOM   4649 C CA    . ALA C 1 70  ? -16.540 3.719   10.854  1.00 54.79  ? 42  ALA C CA    1 
ATOM   4650 C C     . ALA C 1 70  ? -16.581 2.499   9.945   1.00 57.97  ? 42  ALA C C     1 
ATOM   4651 O O     . ALA C 1 70  ? -16.815 1.388   10.431  1.00 62.34  ? 42  ALA C O     1 
ATOM   4652 C CB    . ALA C 1 70  ? -17.959 4.098   11.281  1.00 57.23  ? 42  ALA C CB    1 
ATOM   4653 N N     . LEU C 1 71  ? -16.354 2.677   8.642   1.00 67.44  ? 43  LEU C N     1 
ATOM   4654 C CA    . LEU C 1 71  ? -16.411 1.580   7.687   1.00 65.37  ? 43  LEU C CA    1 
ATOM   4655 C C     . LEU C 1 71  ? -15.086 1.287   7.001   1.00 63.85  ? 43  LEU C C     1 
ATOM   4656 O O     . LEU C 1 71  ? -14.963 0.230   6.372   1.00 63.88  ? 43  LEU C O     1 
ATOM   4657 C CB    . LEU C 1 71  ? -17.463 1.865   6.603   1.00 58.47  ? 43  LEU C CB    1 
ATOM   4658 C CG    . LEU C 1 71  ? -18.914 2.052   7.042   1.00 68.21  ? 43  LEU C CG    1 
ATOM   4659 C CD1   . LEU C 1 71  ? -19.793 2.337   5.835   1.00 61.66  ? 43  LEU C CD1   1 
ATOM   4660 C CD2   . LEU C 1 71  ? -19.410 0.833   7.794   1.00 72.44  ? 43  LEU C CD2   1 
ATOM   4661 N N     . TRP C 1 72  ? -14.096 2.178   7.102   1.00 66.92  ? 44  TRP C N     1 
ATOM   4662 C CA    . TRP C 1 72  ? -12.883 2.043   6.303   1.00 66.10  ? 44  TRP C CA    1 
ATOM   4663 C C     . TRP C 1 72  ? -12.068 0.811   6.673   1.00 68.39  ? 44  TRP C C     1 
ATOM   4664 O O     . TRP C 1 72  ? -11.242 0.367   5.868   1.00 66.16  ? 44  TRP C O     1 
ATOM   4665 C CB    . TRP C 1 72  ? -12.019 3.297   6.442   1.00 65.38  ? 44  TRP C CB    1 
ATOM   4666 C CG    . TRP C 1 72  ? -11.178 3.560   5.236   1.00 66.21  ? 44  TRP C CG    1 
ATOM   4667 C CD1   . TRP C 1 72  ? -9.877  3.200   5.048   1.00 66.46  ? 44  TRP C CD1   1 
ATOM   4668 C CD2   . TRP C 1 72  ? -11.585 4.235   4.040   1.00 65.74  ? 44  TRP C CD2   1 
ATOM   4669 N NE1   . TRP C 1 72  ? -9.447  3.613   3.810   1.00 69.55  ? 44  TRP C NE1   1 
ATOM   4670 C CE2   . TRP C 1 72  ? -10.477 4.251   3.172   1.00 63.33  ? 44  TRP C CE2   1 
ATOM   4671 C CE3   . TRP C 1 72  ? -12.779 4.832   3.622   1.00 65.14  ? 44  TRP C CE3   1 
ATOM   4672 C CZ2   . TRP C 1 72  ? -10.527 4.838   1.909   1.00 61.26  ? 44  TRP C CZ2   1 
ATOM   4673 C CZ3   . TRP C 1 72  ? -12.827 5.412   2.369   1.00 66.63  ? 44  TRP C CZ3   1 
ATOM   4674 C CH2   . TRP C 1 72  ? -11.708 5.412   1.527   1.00 62.21  ? 44  TRP C CH2   1 
ATOM   4675 N N     . SER C 1 73  ? -12.277 0.248   7.865   1.00 75.57  ? 45  SER C N     1 
ATOM   4676 C CA    . SER C 1 73  ? -11.551 -0.959  8.243   1.00 77.53  ? 45  SER C CA    1 
ATOM   4677 C C     . SER C 1 73  ? -12.093 -2.188  7.524   1.00 72.58  ? 45  SER C C     1 
ATOM   4678 O O     . SER C 1 73  ? -11.358 -3.163  7.328   1.00 70.90  ? 45  SER C O     1 
ATOM   4679 C CB    . SER C 1 73  ? -11.616 -1.160  9.757   1.00 79.98  ? 45  SER C CB    1 
ATOM   4680 O OG    . SER C 1 73  ? -12.952 -1.346  10.190  1.00 78.28  ? 45  SER C OG    1 
ATOM   4681 N N     . GLN C 1 74  ? -13.362 -2.160  7.124   1.00 71.17  ? 46  GLN C N     1 
ATOM   4682 C CA    . GLN C 1 74  ? -14.009 -3.290  6.472   1.00 71.84  ? 46  GLN C CA    1 
ATOM   4683 C C     . GLN C 1 74  ? -13.849 -3.274  4.957   1.00 74.23  ? 46  GLN C C     1 
ATOM   4684 O O     . GLN C 1 74  ? -14.433 -4.123  4.276   1.00 71.78  ? 46  GLN C O     1 
ATOM   4685 C CB    . GLN C 1 74  ? -15.497 -3.316  6.830   1.00 72.93  ? 46  GLN C CB    1 
ATOM   4686 C CG    . GLN C 1 74  ? -15.780 -3.488  8.312   1.00 77.31  ? 46  GLN C CG    1 
ATOM   4687 C CD    . GLN C 1 74  ? -17.254 -3.347  8.641   1.00 83.61  ? 46  GLN C CD    1 
ATOM   4688 O OE1   . GLN C 1 74  ? -17.638 -2.536  9.485   1.00 83.15  ? 46  GLN C OE1   1 
ATOM   4689 N NE2   . GLN C 1 74  ? -18.089 -4.137  7.975   1.00 77.32  ? 46  GLN C NE2   1 
ATOM   4690 N N     . LEU C 1 75  ? -13.077 -2.336  4.415   1.00 75.27  ? 47  LEU C N     1 
ATOM   4691 C CA    . LEU C 1 75  ? -12.923 -2.180  2.975   1.00 73.44  ? 47  LEU C CA    1 
ATOM   4692 C C     . LEU C 1 75  ? -11.669 -2.909  2.510   1.00 69.89  ? 47  LEU C C     1 
ATOM   4693 O O     . LEU C 1 75  ? -10.556 -2.560  2.916   1.00 70.42  ? 47  LEU C O     1 
ATOM   4694 C CB    . LEU C 1 75  ? -12.850 -0.703  2.590   1.00 71.53  ? 47  LEU C CB    1 
ATOM   4695 C CG    . LEU C 1 75  ? -14.104 0.141   2.817   1.00 65.30  ? 47  LEU C CG    1 
ATOM   4696 C CD1   . LEU C 1 75  ? -13.781 1.616   2.657   1.00 56.02  ? 47  LEU C CD1   1 
ATOM   4697 C CD2   . LEU C 1 75  ? -15.216 -0.274  1.868   1.00 65.58  ? 47  LEU C CD2   1 
ATOM   4698 N N     . SER C 1 76  ? -11.852 -3.915  1.661   1.00 63.91  ? 48  SER C N     1 
ATOM   4699 C CA    . SER C 1 76  ? -10.739 -4.596  1.021   1.00 71.10  ? 48  SER C CA    1 
ATOM   4700 C C     . SER C 1 76  ? -10.344 -3.859  -0.252  1.00 73.08  ? 48  SER C C     1 
ATOM   4701 O O     . SER C 1 76  ? -11.168 -3.200  -0.891  1.00 77.44  ? 48  SER C O     1 
ATOM   4702 C CB    . SER C 1 76  ? -11.101 -6.047  0.698   1.00 71.65  ? 48  SER C CB    1 
ATOM   4703 O OG    . SER C 1 76  ? -12.164 -6.112  -0.237  1.00 69.15  ? 48  SER C OG    1 
ATOM   4704 N N     . TRP C 1 77  ? -9.068  -3.971  -0.615  1.00 74.32  ? 49  TRP C N     1 
ATOM   4705 C CA    . TRP C 1 77  ? -8.557  -3.279  -1.786  1.00 77.13  ? 49  TRP C CA    1 
ATOM   4706 C C     . TRP C 1 77  ? -7.751  -4.231  -2.659  1.00 81.54  ? 49  TRP C C     1 
ATOM   4707 O O     . TRP C 1 77  ? -7.059  -5.117  -2.142  1.00 81.01  ? 49  TRP C O     1 
ATOM   4708 C CB    . TRP C 1 77  ? -7.685  -2.082  -1.382  1.00 73.83  ? 49  TRP C CB    1 
ATOM   4709 C CG    . TRP C 1 77  ? -8.432  -1.036  -0.616  1.00 72.12  ? 49  TRP C CG    1 
ATOM   4710 C CD1   . TRP C 1 77  ? -8.495  -0.900  0.740   1.00 72.08  ? 49  TRP C CD1   1 
ATOM   4711 C CD2   . TRP C 1 77  ? -9.238  0.013   -1.163  1.00 76.10  ? 49  TRP C CD2   1 
ATOM   4712 N NE1   . TRP C 1 77  ? -9.283  0.176   1.071   1.00 73.69  ? 49  TRP C NE1   1 
ATOM   4713 C CE2   . TRP C 1 77  ? -9.752  0.753   -0.080  1.00 76.90  ? 49  TRP C CE2   1 
ATOM   4714 C CE3   . TRP C 1 77  ? -9.572  0.402   -2.465  1.00 75.49  ? 49  TRP C CE3   1 
ATOM   4715 C CZ2   . TRP C 1 77  ? -10.583 1.858   -0.258  1.00 73.90  ? 49  TRP C CZ2   1 
ATOM   4716 C CZ3   . TRP C 1 77  ? -10.396 1.498   -2.639  1.00 71.08  ? 49  TRP C CZ3   1 
ATOM   4717 C CH2   . TRP C 1 77  ? -10.892 2.214   -1.543  1.00 67.13  ? 49  TRP C CH2   1 
ATOM   4718 N N     . PRO C 1 78  ? -7.820  -4.076  -3.977  1.00 85.20  ? 50  PRO C N     1 
ATOM   4719 C CA    . PRO C 1 78  ? -7.043  -4.941  -4.868  1.00 86.58  ? 50  PRO C CA    1 
ATOM   4720 C C     . PRO C 1 78  ? -5.574  -4.548  -4.896  1.00 88.33  ? 50  PRO C C     1 
ATOM   4721 O O     . PRO C 1 78  ? -5.181  -3.453  -4.487  1.00 84.01  ? 50  PRO C O     1 
ATOM   4722 C CB    . PRO C 1 78  ? -7.698  -4.718  -6.235  1.00 83.42  ? 50  PRO C CB    1 
ATOM   4723 C CG    . PRO C 1 78  ? -8.240  -3.332  -6.158  1.00 84.05  ? 50  PRO C CG    1 
ATOM   4724 C CD    . PRO C 1 78  ? -8.643  -3.106  -4.721  1.00 85.51  ? 50  PRO C CD    1 
ATOM   4725 N N     . GLN C 1 79  ? -4.757  -5.480  -5.394  1.00 93.21  ? 51  GLN C N     1 
ATOM   4726 C CA    . GLN C 1 79  ? -3.320  -5.239  -5.475  1.00 88.29  ? 51  GLN C CA    1 
ATOM   4727 C C     . GLN C 1 79  ? -3.010  -4.117  -6.460  1.00 81.79  ? 51  GLN C C     1 
ATOM   4728 O O     . GLN C 1 79  ? -2.330  -3.144  -6.114  1.00 77.18  ? 51  GLN C O     1 
ATOM   4729 C CB    . GLN C 1 79  ? -2.594  -6.525  -5.871  1.00 85.67  ? 51  GLN C CB    1 
ATOM   4730 C CG    . GLN C 1 79  ? -2.338  -7.471  -4.708  1.00 87.14  ? 51  GLN C CG    1 
ATOM   4731 C CD    . GLN C 1 79  ? -1.370  -6.901  -3.690  1.00 93.67  ? 51  GLN C CD    1 
ATOM   4732 O OE1   . GLN C 1 79  ? -0.490  -6.108  -4.027  1.00 100.92 ? 51  GLN C OE1   1 
ATOM   4733 N NE2   . GLN C 1 79  ? -1.529  -7.301  -2.434  1.00 85.91  ? 51  GLN C NE2   1 
ATOM   4734 N N     . THR C 1 80  ? -3.499  -4.238  -7.692  1.00 79.98  ? 52  THR C N     1 
ATOM   4735 C CA    . THR C 1 80  ? -3.398  -3.156  -8.660  1.00 77.14  ? 52  THR C CA    1 
ATOM   4736 C C     . THR C 1 80  ? -4.621  -2.259  -8.530  1.00 76.07  ? 52  THR C C     1 
ATOM   4737 O O     . THR C 1 80  ? -5.751  -2.760  -8.613  1.00 73.57  ? 52  THR C O     1 
ATOM   4738 C CB    . THR C 1 80  ? -3.297  -3.699  -10.075 1.00 76.85  ? 52  THR C CB    1 
ATOM   4739 O OG1   . THR C 1 80  ? -2.159  -4.565  -10.175 1.00 77.76  ? 52  THR C OG1   1 
ATOM   4740 C CG2   . THR C 1 80  ? -3.145  -2.558  -11.072 1.00 79.44  ? 52  THR C CG2   1 
ATOM   4741 N N     . PRO C 1 81  ? -4.452  -0.955  -8.314  1.00 73.85  ? 53  PRO C N     1 
ATOM   4742 C CA    . PRO C 1 81  ? -5.612  -0.094  -8.051  1.00 73.43  ? 53  PRO C CA    1 
ATOM   4743 C C     . PRO C 1 81  ? -6.576  -0.049  -9.229  1.00 68.15  ? 53  PRO C C     1 
ATOM   4744 O O     . PRO C 1 81  ? -6.171  -0.058  -10.393 1.00 65.36  ? 53  PRO C O     1 
ATOM   4745 C CB    . PRO C 1 81  ? -4.985  1.281   -7.791  1.00 72.28  ? 53  PRO C CB    1 
ATOM   4746 C CG    . PRO C 1 81  ? -3.577  1.003   -7.398  1.00 67.26  ? 53  PRO C CG    1 
ATOM   4747 C CD    . PRO C 1 81  ? -3.173  -0.254  -8.110  1.00 71.67  ? 53  PRO C CD    1 
ATOM   4748 N N     . LEU C 1 82  ? -7.862  -0.004  -8.907  1.00 61.42  ? 54  LEU C N     1 
ATOM   4749 C CA    . LEU C 1 82  ? -8.944  0.186   -9.857  1.00 53.39  ? 54  LEU C CA    1 
ATOM   4750 C C     . LEU C 1 82  ? -9.590  1.548   -9.644  1.00 53.67  ? 54  LEU C C     1 
ATOM   4751 O O     . LEU C 1 82  ? -9.520  2.112   -8.547  1.00 56.57  ? 54  LEU C O     1 
ATOM   4752 C CB    . LEU C 1 82  ? -10.002 -0.916  -9.706  1.00 51.43  ? 54  LEU C CB    1 
ATOM   4753 C CG    . LEU C 1 82  ? -9.567  -2.344  -10.038 1.00 53.13  ? 54  LEU C CG    1 
ATOM   4754 C CD1   . LEU C 1 82  ? -10.709 -3.319  -9.794  1.00 43.71  ? 54  LEU C CD1   1 
ATOM   4755 C CD2   . LEU C 1 82  ? -9.077  -2.433  -11.474 1.00 57.62  ? 54  LEU C CD2   1 
ATOM   4756 N N     . PRO C 1 83  ? -10.220 2.117   -10.673 1.00 53.53  ? 55  PRO C N     1 
ATOM   4757 C CA    . PRO C 1 83  ? -10.871 3.420   -10.497 1.00 50.70  ? 55  PRO C CA    1 
ATOM   4758 C C     . PRO C 1 83  ? -11.992 3.350   -9.471  1.00 48.05  ? 55  PRO C C     1 
ATOM   4759 O O     . PRO C 1 83  ? -12.683 2.338   -9.336  1.00 49.29  ? 55  PRO C O     1 
ATOM   4760 C CB    . PRO C 1 83  ? -11.410 3.749   -11.895 1.00 52.91  ? 55  PRO C CB    1 
ATOM   4761 C CG    . PRO C 1 83  ? -10.686 2.846   -12.832 1.00 56.33  ? 55  PRO C CG    1 
ATOM   4762 C CD    . PRO C 1 83  ? -10.302 1.628   -12.060 1.00 54.41  ? 55  PRO C CD    1 
ATOM   4763 N N     . VAL C 1 84  ? -12.157 4.444   -8.733  1.00 44.67  ? 56  VAL C N     1 
ATOM   4764 C CA    . VAL C 1 84  ? -13.193 4.570   -7.716  1.00 46.12  ? 56  VAL C CA    1 
ATOM   4765 C C     . VAL C 1 84  ? -14.153 5.669   -8.149  1.00 49.84  ? 56  VAL C C     1 
ATOM   4766 O O     . VAL C 1 84  ? -13.726 6.722   -8.636  1.00 54.99  ? 56  VAL C O     1 
ATOM   4767 C CB    . VAL C 1 84  ? -12.588 4.870   -6.328  1.00 43.79  ? 56  VAL C CB    1 
ATOM   4768 C CG1   . VAL C 1 84  ? -13.665 5.306   -5.354  1.00 43.68  ? 56  VAL C CG1   1 
ATOM   4769 C CG2   . VAL C 1 84  ? -11.858 3.646   -5.800  1.00 48.71  ? 56  VAL C CG2   1 
ATOM   4770 N N     . LEU C 1 85  ? -15.450 5.418   -7.984  1.00 48.29  ? 57  LEU C N     1 
ATOM   4771 C CA    . LEU C 1 85  ? -16.495 6.296   -8.491  1.00 46.50  ? 57  LEU C CA    1 
ATOM   4772 C C     . LEU C 1 85  ? -17.286 6.890   -7.334  1.00 51.42  ? 57  LEU C C     1 
ATOM   4773 O O     . LEU C 1 85  ? -17.670 6.172   -6.405  1.00 51.08  ? 57  LEU C O     1 
ATOM   4774 C CB    . LEU C 1 85  ? -17.427 5.534   -9.437  1.00 42.70  ? 57  LEU C CB    1 
ATOM   4775 C CG    . LEU C 1 85  ? -18.593 6.299   -10.061 1.00 40.67  ? 57  LEU C CG    1 
ATOM   4776 C CD1   . LEU C 1 85  ? -18.085 7.384   -10.990 1.00 40.64  ? 57  LEU C CD1   1 
ATOM   4777 C CD2   . LEU C 1 85  ? -19.501 5.342   -10.809 1.00 41.94  ? 57  LEU C CD2   1 
ATOM   4778 N N     . ASP C 1 86  ? -17.526 8.199   -7.395  1.00 47.12  ? 58  ASP C N     1 
ATOM   4779 C CA    . ASP C 1 86  ? -18.377 8.901   -6.439  1.00 47.26  ? 58  ASP C CA    1 
ATOM   4780 C C     . ASP C 1 86  ? -19.548 9.497   -7.209  1.00 48.31  ? 58  ASP C C     1 
ATOM   4781 O O     . ASP C 1 86  ? -19.378 10.472  -7.949  1.00 48.81  ? 58  ASP C O     1 
ATOM   4782 C CB    . ASP C 1 86  ? -17.599 9.986   -5.694  1.00 49.58  ? 58  ASP C CB    1 
ATOM   4783 C CG    . ASP C 1 86  ? -18.423 10.650  -4.603  1.00 64.28  ? 58  ASP C CG    1 
ATOM   4784 O OD1   . ASP C 1 86  ? -19.438 10.057  -4.176  1.00 65.89  ? 58  ASP C OD1   1 
ATOM   4785 O OD2   . ASP C 1 86  ? -18.057 11.765  -4.171  1.00 62.69  ? 58  ASP C OD2   1 
ATOM   4786 N N     . ILE C 1 87  ? -20.729 8.912   -7.040  1.00 47.55  ? 59  ILE C N     1 
ATOM   4787 C CA    . ILE C 1 87  ? -21.918 9.333   -7.770  1.00 42.60  ? 59  ILE C CA    1 
ATOM   4788 C C     . ILE C 1 87  ? -22.644 10.388  -6.949  1.00 47.09  ? 59  ILE C C     1 
ATOM   4789 O O     . ILE C 1 87  ? -22.751 10.272  -5.721  1.00 51.33  ? 59  ILE C O     1 
ATOM   4790 C CB    . ILE C 1 87  ? -22.830 8.129   -8.069  1.00 42.52  ? 59  ILE C CB    1 
ATOM   4791 C CG1   . ILE C 1 87  ? -22.072 7.081   -8.881  1.00 42.49  ? 59  ILE C CG1   1 
ATOM   4792 C CG2   . ILE C 1 87  ? -24.045 8.566   -8.865  1.00 43.88  ? 59  ILE C CG2   1 
ATOM   4793 C CD1   . ILE C 1 87  ? -22.872 5.826   -9.153  1.00 43.53  ? 59  ILE C CD1   1 
ATOM   4794 N N     . GLY C 1 88  ? -23.148 11.421  -7.623  1.00 45.59  ? 60  GLY C N     1 
ATOM   4795 C CA    . GLY C 1 88  ? -23.786 12.529  -6.939  1.00 44.13  ? 60  GLY C CA    1 
ATOM   4796 C C     . GLY C 1 88  ? -22.830 13.211  -5.985  1.00 49.34  ? 60  GLY C C     1 
ATOM   4797 O O     . GLY C 1 88  ? -23.103 13.322  -4.787  1.00 56.68  ? 60  GLY C O     1 
ATOM   4798 N N     . CYS C 1 89  ? -21.696 13.670  -6.515  1.00 45.78  ? 61  CYS C N     1 
ATOM   4799 C CA    . CYS C 1 89  ? -20.607 14.167  -5.685  1.00 50.03  ? 61  CYS C CA    1 
ATOM   4800 C C     . CYS C 1 89  ? -20.837 15.581  -5.171  1.00 50.43  ? 61  CYS C C     1 
ATOM   4801 O O     . CYS C 1 89  ? -20.161 15.995  -4.223  1.00 52.73  ? 61  CYS C O     1 
ATOM   4802 C CB    . CYS C 1 89  ? -19.294 14.116  -6.467  1.00 49.72  ? 61  CYS C CB    1 
ATOM   4803 S SG    . CYS C 1 89  ? -19.280 15.150  -7.950  1.00 47.72  ? 61  CYS C SG    1 
ATOM   4804 N N     . GLY C 1 90  ? -21.761 16.329  -5.767  1.00 48.62  ? 62  GLY C N     1 
ATOM   4805 C CA    . GLY C 1 90  ? -21.981 17.702  -5.381  1.00 50.37  ? 62  GLY C CA    1 
ATOM   4806 C C     . GLY C 1 90  ? -20.866 18.605  -5.866  1.00 46.20  ? 62  GLY C C     1 
ATOM   4807 O O     . GLY C 1 90  ? -20.350 18.447  -6.976  1.00 44.46  ? 62  GLY C O     1 
ATOM   4808 N N     . PRO C 1 91  ? -20.472 19.578  -5.040  1.00 47.84  ? 63  PRO C N     1 
ATOM   4809 C CA    . PRO C 1 91  ? -19.389 20.488  -5.438  1.00 44.26  ? 63  PRO C CA    1 
ATOM   4810 C C     . PRO C 1 91  ? -18.003 19.909  -5.195  1.00 47.49  ? 63  PRO C C     1 
ATOM   4811 O O     . PRO C 1 91  ? -17.059 20.647  -4.897  1.00 45.91  ? 63  PRO C O     1 
ATOM   4812 C CB    . PRO C 1 91  ? -19.640 21.725  -4.570  1.00 45.46  ? 63  PRO C CB    1 
ATOM   4813 C CG    . PRO C 1 91  ? -20.305 21.182  -3.355  1.00 48.97  ? 63  PRO C CG    1 
ATOM   4814 C CD    . PRO C 1 91  ? -21.156 20.033  -3.818  1.00 51.33  ? 63  PRO C CD    1 
ATOM   4815 N N     . GLY C 1 92  ? -17.873 18.590  -5.322  1.00 50.39  ? 64  GLY C N     1 
ATOM   4816 C CA    . GLY C 1 92  ? -16.569 17.949  -5.261  1.00 50.64  ? 64  GLY C CA    1 
ATOM   4817 C C     . GLY C 1 92  ? -15.873 18.066  -3.927  1.00 47.61  ? 64  GLY C C     1 
ATOM   4818 O O     . GLY C 1 92  ? -14.641 17.993  -3.867  1.00 47.93  ? 64  GLY C O     1 
ATOM   4819 N N     . ASP C 1 93  ? -16.630 18.238  -2.847  1.00 47.71  ? 65  ASP C N     1 
ATOM   4820 C CA    . ASP C 1 93  ? -16.033 18.420  -1.532  1.00 45.94  ? 65  ASP C CA    1 
ATOM   4821 C C     . ASP C 1 93  ? -15.809 17.100  -0.807  1.00 46.89  ? 65  ASP C C     1 
ATOM   4822 O O     . ASP C 1 93  ? -14.787 16.932  -0.132  1.00 48.79  ? 65  ASP C O     1 
ATOM   4823 C CB    . ASP C 1 93  ? -16.910 19.342  -0.687  1.00 50.76  ? 65  ASP C CB    1 
ATOM   4824 C CG    . ASP C 1 93  ? -16.846 20.783  -1.149  1.00 52.32  ? 65  ASP C CG    1 
ATOM   4825 O OD1   . ASP C 1 93  ? -15.723 21.297  -1.336  1.00 51.83  ? 65  ASP C OD1   1 
ATOM   4826 O OD2   . ASP C 1 93  ? -17.914 21.411  -1.300  1.00 51.74  ? 65  ASP C OD2   1 
ATOM   4827 N N     . ILE C 1 94  ? -16.736 16.153  -0.942  1.00 49.53  ? 66  ILE C N     1 
ATOM   4828 C CA    . ILE C 1 94  ? -16.593 14.838  -0.326  1.00 48.73  ? 66  ILE C CA    1 
ATOM   4829 C C     . ILE C 1 94  ? -15.834 13.944  -1.298  1.00 48.36  ? 66  ILE C C     1 
ATOM   4830 O O     . ILE C 1 94  ? -16.055 12.729  -1.358  1.00 50.35  ? 66  ILE C O     1 
ATOM   4831 C CB    . ILE C 1 94  ? -17.963 14.242  0.048   1.00 54.89  ? 66  ILE C CB    1 
ATOM   4832 C CG1   . ILE C 1 94  ? -18.851 15.308  0.688   1.00 56.97  ? 66  ILE C CG1   1 
ATOM   4833 C CG2   . ILE C 1 94  ? -17.807 13.097  1.039   1.00 58.61  ? 66  ILE C CG2   1 
ATOM   4834 C CD1   . ILE C 1 94  ? -18.258 15.938  1.927   1.00 58.72  ? 66  ILE C CD1   1 
ATOM   4835 N N     . ALA C 1 95  ? -14.940 14.546  -2.078  1.00 46.03  ? 67  ALA C N     1 
ATOM   4836 C CA    . ALA C 1 95  ? -14.119 13.805  -3.024  1.00 42.48  ? 67  ALA C CA    1 
ATOM   4837 C C     . ALA C 1 95  ? -12.678 14.286  -2.936  1.00 44.35  ? 67  ALA C C     1 
ATOM   4838 O O     . ALA C 1 95  ? -11.754 13.479  -2.804  1.00 53.15  ? 67  ALA C O     1 
ATOM   4839 C CB    . ALA C 1 95  ? -14.656 13.964  -4.448  1.00 40.32  ? 67  ALA C CB    1 
ATOM   4840 N N     . ARG C 1 96  ? -12.480 15.603  -3.002  1.00 39.75  ? 68  ARG C N     1 
ATOM   4841 C CA    . ARG C 1 96  ? -11.136 16.155  -2.894  1.00 39.48  ? 68  ARG C CA    1 
ATOM   4842 C C     . ARG C 1 96  ? -10.645 16.138  -1.451  1.00 44.50  ? 68  ARG C C     1 
ATOM   4843 O O     . ARG C 1 96  ? -9.462  15.884  -1.198  1.00 52.88  ? 68  ARG C O     1 
ATOM   4844 C CB    . ARG C 1 96  ? -11.111 17.576  -3.468  1.00 40.88  ? 68  ARG C CB    1 
ATOM   4845 C CG    . ARG C 1 96  ? -9.985  18.473  -2.960  1.00 44.25  ? 68  ARG C CG    1 
ATOM   4846 C CD    . ARG C 1 96  ? -8.616  17.933  -3.347  1.00 45.64  ? 68  ARG C CD    1 
ATOM   4847 N NE    . ARG C 1 96  ? -7.546  18.874  -3.042  1.00 52.31  ? 68  ARG C NE    1 
ATOM   4848 C CZ    . ARG C 1 96  ? -6.308  18.521  -2.727  1.00 55.36  ? 68  ARG C CZ    1 
ATOM   4849 N NH1   . ARG C 1 96  ? -5.947  17.250  -2.659  1.00 55.13  ? 68  ARG C NH1   1 
ATOM   4850 N NH2   . ARG C 1 96  ? -5.410  19.467  -2.469  1.00 55.19  ? 68  ARG C NH2   1 
ATOM   4851 N N     . LYS C 1 97  ? -11.539 16.380  -0.494  1.00 40.60  ? 69  LYS C N     1 
ATOM   4852 C CA    . LYS C 1 97  ? -11.140 16.537  0.896   1.00 43.04  ? 69  LYS C CA    1 
ATOM   4853 C C     . LYS C 1 97  ? -11.431 15.318  1.761   1.00 43.70  ? 69  LYS C C     1 
ATOM   4854 O O     . LYS C 1 97  ? -10.821 15.181  2.828   1.00 43.42  ? 69  LYS C O     1 
ATOM   4855 C CB    . LYS C 1 97  ? -11.831 17.764  1.501   1.00 42.70  ? 69  LYS C CB    1 
ATOM   4856 C CG    . LYS C 1 97  ? -11.789 18.979  0.588   1.00 40.75  ? 69  LYS C CG    1 
ATOM   4857 C CD    . LYS C 1 97  ? -11.717 20.275  1.371   1.00 34.19  ? 69  LYS C CD    1 
ATOM   4858 C CE    . LYS C 1 97  ? -12.430 21.396  0.636   1.00 40.34  ? 69  LYS C CE    1 
ATOM   4859 N NZ    . LYS C 1 97  ? -13.072 22.355  1.577   1.00 55.46  ? 69  LYS C NZ    1 
ATOM   4860 N N     . VAL C 1 98  ? -12.330 14.433  1.337   1.00 45.34  ? 70  VAL C N     1 
ATOM   4861 C CA    . VAL C 1 98  ? -12.705 13.252  2.113   1.00 43.69  ? 70  VAL C CA    1 
ATOM   4862 C C     . VAL C 1 98  ? -12.192 11.971  1.459   1.00 45.39  ? 70  VAL C C     1 
ATOM   4863 O O     . VAL C 1 98  ? -11.418 11.226  2.059   1.00 47.55  ? 70  VAL C O     1 
ATOM   4864 C CB    . VAL C 1 98  ? -14.232 13.194  2.340   1.00 48.07  ? 70  VAL C CB    1 
ATOM   4865 C CG1   . VAL C 1 98  ? -14.619 11.880  2.995   1.00 45.50  ? 70  VAL C CG1   1 
ATOM   4866 C CG2   . VAL C 1 98  ? -14.686 14.364  3.190   1.00 53.75  ? 70  VAL C CG2   1 
ATOM   4867 N N     . LEU C 1 99  ? -12.611 11.702  0.223   1.00 41.65  ? 71  LEU C N     1 
ATOM   4868 C CA    . LEU C 1 99  ? -12.288 10.441  -0.437  1.00 46.54  ? 71  LEU C CA    1 
ATOM   4869 C C     . LEU C 1 99  ? -10.818 10.342  -0.827  1.00 49.09  ? 71  LEU C C     1 
ATOM   4870 O O     . LEU C 1 99  ? -10.090 9.490   -0.306  1.00 52.40  ? 71  LEU C O     1 
ATOM   4871 C CB    . LEU C 1 99  ? -13.160 10.250  -1.679  1.00 46.58  ? 71  LEU C CB    1 
ATOM   4872 C CG    . LEU C 1 99  ? -14.615 9.847   -1.441  1.00 46.18  ? 71  LEU C CG    1 
ATOM   4873 C CD1   . LEU C 1 99  ? -15.377 9.809   -2.755  1.00 46.48  ? 71  LEU C CD1   1 
ATOM   4874 C CD2   . LEU C 1 99  ? -14.688 8.504   -0.734  1.00 45.33  ? 71  LEU C CD2   1 
ATOM   4875 N N     . ALA C 1 100 ? -10.381 11.202  -1.745  1.00 47.58  ? 72  ALA C N     1 
ATOM   4876 C CA    . ALA C 1 100 ? -9.032  11.103  -2.300  1.00 48.10  ? 72  ALA C CA    1 
ATOM   4877 C C     . ALA C 1 100 ? -7.912  11.106  -1.263  1.00 51.52  ? 72  ALA C C     1 
ATOM   4878 O O     . ALA C 1 100 ? -6.926  10.379  -1.471  1.00 55.01  ? 72  ALA C O     1 
ATOM   4879 C CB    . ALA C 1 100 ? -8.815  12.232  -3.318  1.00 46.87  ? 72  ALA C CB    1 
ATOM   4880 N N     . PRO C 1 101 ? -7.966  11.881  -0.169  1.00 50.87  ? 73  PRO C N     1 
ATOM   4881 C CA    . PRO C 1 101 ? -6.861  11.820  0.804   1.00 49.71  ? 73  PRO C CA    1 
ATOM   4882 C C     . PRO C 1 101 ? -6.594  10.428  1.354   1.00 49.11  ? 73  PRO C C     1 
ATOM   4883 O O     . PRO C 1 101 ? -5.426  10.045  1.501   1.00 50.12  ? 73  PRO C O     1 
ATOM   4884 C CB    . PRO C 1 101 ? -7.322  12.785  1.903   1.00 52.15  ? 73  PRO C CB    1 
ATOM   4885 C CG    . PRO C 1 101 ? -8.112  13.797  1.170   1.00 52.52  ? 73  PRO C CG    1 
ATOM   4886 C CD    . PRO C 1 101 ? -8.862  13.018  0.119   1.00 50.91  ? 73  PRO C CD    1 
ATOM   4887 N N     . ARG C 1 102 ? -7.636  9.655   1.661   1.00 45.86  ? 74  ARG C N     1 
ATOM   4888 C CA    . ARG C 1 102 ? -7.464  8.330   2.242   1.00 51.17  ? 74  ARG C CA    1 
ATOM   4889 C C     . ARG C 1 102 ? -7.462  7.221   1.196   1.00 54.17  ? 74  ARG C C     1 
ATOM   4890 O O     . ARG C 1 102 ? -7.636  6.049   1.550   1.00 56.74  ? 74  ARG C O     1 
ATOM   4891 C CB    . ARG C 1 102 ? -8.557  8.053   3.279   1.00 53.06  ? 74  ARG C CB    1 
ATOM   4892 C CG    . ARG C 1 102 ? -9.967  8.362   2.808   1.00 53.65  ? 74  ARG C CG    1 
ATOM   4893 C CD    . ARG C 1 102 ? -10.865 8.800   3.954   1.00 55.72  ? 74  ARG C CD    1 
ATOM   4894 N NE    . ARG C 1 102 ? -10.547 10.141  4.426   1.00 55.22  ? 74  ARG C NE    1 
ATOM   4895 C CZ    . ARG C 1 102 ? -10.890 10.617  5.615   1.00 57.11  ? 74  ARG C CZ    1 
ATOM   4896 N NH1   . ARG C 1 102 ? -11.550 9.879   6.493   1.00 58.90  ? 74  ARG C NH1   1 
ATOM   4897 N NH2   . ARG C 1 102 ? -10.569 11.869  5.930   1.00 52.21  ? 74  ARG C NH2   1 
ATOM   4898 N N     . LEU C 1 103 ? -7.273  7.558   -0.073  1.00 50.75  ? 75  LEU C N     1 
ATOM   4899 C CA    . LEU C 1 103 ? -7.355  6.469   -1.033  1.00 53.12  ? 75  LEU C CA    1 
ATOM   4900 C C     . LEU C 1 103 ? -5.997  5.799   -1.211  1.00 53.10  ? 75  LEU C C     1 
ATOM   4901 O O     . LEU C 1 103 ? -4.954  6.445   -1.057  1.00 49.57  ? 75  LEU C O     1 
ATOM   4902 C CB    . LEU C 1 103 ? -7.848  6.982   -2.384  1.00 54.14  ? 75  LEU C CB    1 
ATOM   4903 C CG    . LEU C 1 103 ? -9.364  7.114   -2.549  1.00 51.39  ? 75  LEU C CG    1 
ATOM   4904 C CD1   . LEU C 1 103 ? -9.736  7.197   -4.019  1.00 46.69  ? 75  LEU C CD1   1 
ATOM   4905 C CD2   . LEU C 1 103 ? -10.090 5.960   -1.872  1.00 57.16  ? 75  LEU C CD2   1 
ATOM   4906 N N     . PRO C 1 104 ? -5.995  4.491   -1.508  1.00 59.31  ? 76  PRO C N     1 
ATOM   4907 C CA    . PRO C 1 104 ? -4.739  3.808   -1.850  1.00 60.10  ? 76  PRO C CA    1 
ATOM   4908 C C     . PRO C 1 104 ? -3.970  4.545   -2.934  1.00 56.59  ? 76  PRO C C     1 
ATOM   4909 O O     . PRO C 1 104 ? -4.520  4.821   -4.003  1.00 62.25  ? 76  PRO C O     1 
ATOM   4910 C CB    . PRO C 1 104 ? -5.213  2.434   -2.334  1.00 58.56  ? 76  PRO C CB    1 
ATOM   4911 C CG    . PRO C 1 104 ? -6.479  2.193   -1.580  1.00 64.05  ? 76  PRO C CG    1 
ATOM   4912 C CD    . PRO C 1 104 ? -7.105  3.543   -1.304  1.00 61.84  ? 76  PRO C CD    1 
ATOM   4913 N N     . ALA C 1 105 ? -2.709  4.879   -2.662  1.00 55.79  ? 77  ALA C N     1 
ATOM   4914 C CA    . ALA C 1 105 ? -1.912  5.646   -3.611  1.00 57.87  ? 77  ALA C CA    1 
ATOM   4915 C C     . ALA C 1 105 ? -1.825  4.921   -4.948  1.00 62.54  ? 77  ALA C C     1 
ATOM   4916 O O     . ALA C 1 105 ? -1.539  3.722   -5.005  1.00 60.25  ? 77  ALA C O     1 
ATOM   4917 C CB    . ALA C 1 105 ? -0.513  5.894   -3.046  1.00 59.06  ? 77  ALA C CB    1 
ATOM   4918 N N     . GLY C 1 106 ? -2.078  5.658   -6.028  1.00 60.34  ? 78  GLY C N     1 
ATOM   4919 C CA    . GLY C 1 106 ? -2.198  5.096   -7.352  1.00 58.75  ? 78  GLY C CA    1 
ATOM   4920 C C     . GLY C 1 106 ? -3.626  4.955   -7.837  1.00 63.20  ? 78  GLY C C     1 
ATOM   4921 O O     . GLY C 1 106 ? -3.850  4.875   -9.051  1.00 67.78  ? 78  GLY C O     1 
ATOM   4922 N N     . THR C 1 107 ? -4.592  4.924   -6.922  1.00 63.66  ? 79  THR C N     1 
ATOM   4923 C CA    . THR C 1 107 ? -5.995  4.860   -7.304  1.00 62.22  ? 79  THR C CA    1 
ATOM   4924 C C     . THR C 1 107 ? -6.448  6.195   -7.881  1.00 62.20  ? 79  THR C C     1 
ATOM   4925 O O     . THR C 1 107 ? -6.017  7.263   -7.436  1.00 60.48  ? 79  THR C O     1 
ATOM   4926 C CB    . THR C 1 107 ? -6.857  4.490   -6.094  1.00 60.87  ? 79  THR C CB    1 
ATOM   4927 O OG1   . THR C 1 107 ? -6.311  3.330   -5.453  1.00 61.61  ? 79  THR C OG1   1 
ATOM   4928 C CG2   . THR C 1 107 ? -8.287  4.201   -6.513  1.00 61.51  ? 79  THR C CG2   1 
ATOM   4929 N N     . ARG C 1 108 ? -7.317  6.131   -8.885  1.00 58.49  ? 80  ARG C N     1 
ATOM   4930 C CA    . ARG C 1 108 ? -7.869  7.312   -9.530  1.00 55.13  ? 80  ARG C CA    1 
ATOM   4931 C C     . ARG C 1 108 ? -9.359  7.407   -9.230  1.00 53.70  ? 80  ARG C C     1 
ATOM   4932 O O     . ARG C 1 108 ? -10.078 6.404   -9.278  1.00 51.93  ? 80  ARG C O     1 
ATOM   4933 C CB    . ARG C 1 108 ? -7.624  7.269   -11.041 1.00 54.02  ? 80  ARG C CB    1 
ATOM   4934 C CG    . ARG C 1 108 ? -8.521  8.182   -11.857 1.00 61.90  ? 80  ARG C CG    1 
ATOM   4935 C CD    . ARG C 1 108 ? -8.046  8.260   -13.297 1.00 67.22  ? 80  ARG C CD    1 
ATOM   4936 N NE    . ARG C 1 108 ? -8.673  7.245   -14.134 1.00 79.94  ? 80  ARG C NE    1 
ATOM   4937 C CZ    . ARG C 1 108 ? -9.831  7.403   -14.760 1.00 70.24  ? 80  ARG C CZ    1 
ATOM   4938 N NH1   . ARG C 1 108 ? -10.518 8.530   -14.669 1.00 67.74  ? 80  ARG C NH1   1 
ATOM   4939 N NH2   . ARG C 1 108 ? -10.311 6.406   -15.498 1.00 66.00  ? 80  ARG C NH2   1 
ATOM   4940 N N     . LEU C 1 109 ? -9.816  8.615   -8.912  1.00 49.69  ? 81  LEU C N     1 
ATOM   4941 C CA    . LEU C 1 109 ? -11.202 8.860   -8.542  1.00 42.30  ? 81  LEU C CA    1 
ATOM   4942 C C     . LEU C 1 109 ? -11.964 9.478   -9.708  1.00 44.53  ? 81  LEU C C     1 
ATOM   4943 O O     . LEU C 1 109 ? -11.428 10.311  -10.445 1.00 51.17  ? 81  LEU C O     1 
ATOM   4944 C CB    . LEU C 1 109 ? -11.281 9.779   -7.320  1.00 37.00  ? 81  LEU C CB    1 
ATOM   4945 C CG    . LEU C 1 109 ? -12.663 10.076  -6.732  1.00 37.60  ? 81  LEU C CG    1 
ATOM   4946 C CD1   . LEU C 1 109 ? -13.334 8.804   -6.250  1.00 41.64  ? 81  LEU C CD1   1 
ATOM   4947 C CD2   . LEU C 1 109 ? -12.555 11.082  -5.598  1.00 38.62  ? 81  LEU C CD2   1 
ATOM   4948 N N     . VAL C 1 110 ? -13.213 9.055   -9.875  1.00 42.34  ? 82  VAL C N     1 
ATOM   4949 C CA    . VAL C 1 110 ? -14.130 9.636   -10.848 1.00 37.79  ? 82  VAL C CA    1 
ATOM   4950 C C     . VAL C 1 110 ? -15.373 10.078  -10.092 1.00 44.73  ? 82  VAL C C     1 
ATOM   4951 O O     . VAL C 1 110 ? -16.060 9.250   -9.482  1.00 52.28  ? 82  VAL C O     1 
ATOM   4952 C CB    . VAL C 1 110 ? -14.489 8.646   -11.967 1.00 41.26  ? 82  VAL C CB    1 
ATOM   4953 C CG1   . VAL C 1 110 ? -15.456 9.286   -12.952 1.00 42.32  ? 82  VAL C CG1   1 
ATOM   4954 C CG2   . VAL C 1 110 ? -13.233 8.169   -12.680 1.00 50.74  ? 82  VAL C CG2   1 
ATOM   4955 N N     . ALA C 1 111 ? -15.652 11.376  -10.114 1.00 42.07  ? 83  ALA C N     1 
ATOM   4956 C CA    . ALA C 1 111 ? -16.814 11.939  -9.441  1.00 44.84  ? 83  ALA C CA    1 
ATOM   4957 C C     . ALA C 1 111 ? -17.779 12.483  -10.483 1.00 44.70  ? 83  ALA C C     1 
ATOM   4958 O O     . ALA C 1 111 ? -17.361 13.170  -11.421 1.00 44.89  ? 83  ALA C O     1 
ATOM   4959 C CB    . ALA C 1 111 ? -16.400 13.039  -8.462  1.00 40.86  ? 83  ALA C CB    1 
ATOM   4960 N N     . CYS C 1 112 ? -19.063 12.173  -10.323 1.00 42.18  ? 84  CYS C N     1 
ATOM   4961 C CA    . CYS C 1 112 ? -20.062 12.578  -11.300 1.00 41.70  ? 84  CYS C CA    1 
ATOM   4962 C C     . CYS C 1 112 ? -21.314 13.075  -10.598 1.00 42.76  ? 84  CYS C C     1 
ATOM   4963 O O     . CYS C 1 112 ? -21.793 12.456  -9.644  1.00 47.43  ? 84  CYS C O     1 
ATOM   4964 C CB    . CYS C 1 112 ? -20.426 11.425  -12.245 1.00 42.57  ? 84  CYS C CB    1 
ATOM   4965 S SG    . CYS C 1 112 ? -20.843 9.878   -11.417 1.00 42.54  ? 84  CYS C SG    1 
ATOM   4966 N N     . ASP C 1 113 ? -21.833 14.198  -11.080 1.00 42.90  ? 85  ASP C N     1 
ATOM   4967 C CA    . ASP C 1 113 ? -23.125 14.725  -10.677 1.00 43.73  ? 85  ASP C CA    1 
ATOM   4968 C C     . ASP C 1 113 ? -24.027 14.788  -11.902 1.00 45.17  ? 85  ASP C C     1 
ATOM   4969 O O     . ASP C 1 113 ? -23.583 14.608  -13.039 1.00 45.46  ? 85  ASP C O     1 
ATOM   4970 C CB    . ASP C 1 113 ? -22.985 16.112  -10.039 1.00 45.40  ? 85  ASP C CB    1 
ATOM   4971 C CG    . ASP C 1 113 ? -24.064 16.393  -9.015  1.00 47.09  ? 85  ASP C CG    1 
ATOM   4972 O OD1   . ASP C 1 113 ? -23.976 15.847  -7.896  1.00 49.86  ? 85  ASP C OD1   1 
ATOM   4973 O OD2   . ASP C 1 113 ? -25.003 17.154  -9.330  1.00 47.94  ? 85  ASP C OD2   1 
ATOM   4974 N N     . ILE C 1 114 ? -25.312 15.042  -11.665 1.00 46.16  ? 86  ILE C N     1 
ATOM   4975 C CA    . ILE C 1 114 ? -26.251 15.190  -12.769 1.00 47.66  ? 86  ILE C CA    1 
ATOM   4976 C C     . ILE C 1 114 ? -26.331 16.630  -13.266 1.00 48.09  ? 86  ILE C C     1 
ATOM   4977 O O     . ILE C 1 114 ? -26.678 16.856  -14.435 1.00 51.42  ? 86  ILE C O     1 
ATOM   4978 C CB    . ILE C 1 114 ? -27.647 14.682  -12.362 1.00 48.72  ? 86  ILE C CB    1 
ATOM   4979 C CG1   . ILE C 1 114 ? -28.597 14.659  -13.562 1.00 50.38  ? 86  ILE C CG1   1 
ATOM   4980 C CG2   . ILE C 1 114 ? -28.221 15.535  -11.257 1.00 48.66  ? 86  ILE C CG2   1 
ATOM   4981 C CD1   . ILE C 1 114 ? -29.956 14.076  -13.252 1.00 51.57  ? 86  ILE C CD1   1 
ATOM   4982 N N     . SER C 1 115 ? -25.991 17.612  -12.424 1.00 47.35  ? 87  SER C N     1 
ATOM   4983 C CA    . SER C 1 115 ? -26.113 19.017  -12.792 1.00 49.19  ? 87  SER C CA    1 
ATOM   4984 C C     . SER C 1 115 ? -24.785 19.553  -13.295 1.00 47.01  ? 87  SER C C     1 
ATOM   4985 O O     . SER C 1 115 ? -23.751 19.336  -12.647 1.00 45.72  ? 87  SER C O     1 
ATOM   4986 C CB    . SER C 1 115 ? -26.576 19.845  -11.598 1.00 51.63  ? 87  SER C CB    1 
ATOM   4987 O OG    . SER C 1 115 ? -25.479 20.248  -10.801 1.00 52.92  ? 87  SER C OG    1 
ATOM   4988 N N     . PRO C 1 116 ? -24.772 20.238  -14.442 1.00 47.79  ? 88  PRO C N     1 
ATOM   4989 C CA    . PRO C 1 116 ? -23.523 20.869  -14.900 1.00 47.11  ? 88  PRO C CA    1 
ATOM   4990 C C     . PRO C 1 116 ? -22.937 21.849  -13.902 1.00 47.25  ? 88  PRO C C     1 
ATOM   4991 O O     . PRO C 1 116 ? -21.712 21.896  -13.737 1.00 48.43  ? 88  PRO C O     1 
ATOM   4992 C CB    . PRO C 1 116 ? -23.958 21.575  -16.187 1.00 49.38  ? 88  PRO C CB    1 
ATOM   4993 C CG    . PRO C 1 116 ? -25.021 20.701  -16.731 1.00 55.73  ? 88  PRO C CG    1 
ATOM   4994 C CD    . PRO C 1 116 ? -25.757 20.128  -15.531 1.00 49.33  ? 88  PRO C CD    1 
ATOM   4995 N N     . GLU C 1 117 ? -23.786 22.638  -13.239 1.00 47.18  ? 89  GLU C N     1 
ATOM   4996 C CA    . GLU C 1 117 ? -23.308 23.666  -12.320 1.00 46.52  ? 89  GLU C CA    1 
ATOM   4997 C C     . GLU C 1 117 ? -22.394 23.083  -11.250 1.00 46.59  ? 89  GLU C C     1 
ATOM   4998 O O     . GLU C 1 117 ? -21.343 23.656  -10.940 1.00 47.65  ? 89  GLU C O     1 
ATOM   4999 C CB    . GLU C 1 117 ? -24.497 24.383  -11.678 1.00 47.97  ? 89  GLU C CB    1 
ATOM   5000 C CG    . GLU C 1 117 ? -25.542 24.855  -12.678 1.00 48.95  ? 89  GLU C CG    1 
ATOM   5001 C CD    . GLU C 1 117 ? -26.625 23.823  -12.928 1.00 53.56  ? 89  GLU C CD    1 
ATOM   5002 O OE1   . GLU C 1 117 ? -27.009 23.118  -11.971 1.00 60.69  ? 89  GLU C OE1   1 
ATOM   5003 O OE2   . GLU C 1 117 ? -27.091 23.719  -14.082 1.00 50.86  ? 89  GLU C OE2   1 
ATOM   5004 N N     . MET C 1 118 ? -22.775 21.941  -10.675 1.00 47.52  ? 90  MET C N     1 
ATOM   5005 C CA    . MET C 1 118 ? -21.888 21.262  -9.736  1.00 43.79  ? 90  MET C CA    1 
ATOM   5006 C C     . MET C 1 118 ? -20.656 20.720  -10.447 1.00 42.32  ? 90  MET C C     1 
ATOM   5007 O O     . MET C 1 118 ? -19.523 20.961  -10.017 1.00 44.02  ? 90  MET C O     1 
ATOM   5008 C CB    . MET C 1 118 ? -22.636 20.140  -9.017  1.00 43.03  ? 90  MET C CB    1 
ATOM   5009 C CG    . MET C 1 118 ? -23.808 20.616  -8.182  1.00 48.05  ? 90  MET C CG    1 
ATOM   5010 S SD    . MET C 1 118 ? -23.338 20.954  -6.478  1.00 42.63  ? 90  MET C SD    1 
ATOM   5011 C CE    . MET C 1 118 ? -24.643 22.076  -5.986  1.00 53.27  ? 90  MET C CE    1 
ATOM   5012 N N     . VAL C 1 119 ? -20.860 19.996  -11.552 1.00 42.92  ? 91  VAL C N     1 
ATOM   5013 C CA    . VAL C 1 119 ? -19.745 19.476  -12.333 1.00 42.44  ? 91  VAL C CA    1 
ATOM   5014 C C     . VAL C 1 119 ? -18.828 20.599  -12.798 1.00 42.24  ? 91  VAL C C     1 
ATOM   5015 O O     . VAL C 1 119 ? -17.633 20.375  -13.010 1.00 41.52  ? 91  VAL C O     1 
ATOM   5016 C CB    . VAL C 1 119 ? -20.284 18.643  -13.519 1.00 43.40  ? 91  VAL C CB    1 
ATOM   5017 C CG1   . VAL C 1 119 ? -19.151 18.145  -14.410 1.00 43.06  ? 91  VAL C CG1   1 
ATOM   5018 C CG2   . VAL C 1 119 ? -21.112 17.472  -13.006 1.00 43.60  ? 91  VAL C CG2   1 
ATOM   5019 N N     . ASP C 1 120 ? -19.352 21.818  -12.932 1.00 42.92  ? 92  ASP C N     1 
ATOM   5020 C CA    . ASP C 1 120 ? -18.521 22.972  -13.256 1.00 42.79  ? 92  ASP C CA    1 
ATOM   5021 C C     . ASP C 1 120 ? -17.863 23.574  -12.021 1.00 41.83  ? 92  ASP C C     1 
ATOM   5022 O O     . ASP C 1 120 ? -16.725 24.049  -12.098 1.00 41.27  ? 92  ASP C O     1 
ATOM   5023 C CB    . ASP C 1 120 ? -19.353 24.037  -13.973 1.00 45.17  ? 92  ASP C CB    1 
ATOM   5024 C CG    . ASP C 1 120 ? -19.739 23.622  -15.376 1.00 49.58  ? 92  ASP C CG    1 
ATOM   5025 O OD1   . ASP C 1 120 ? -19.131 22.662  -15.893 1.00 51.78  ? 92  ASP C OD1   1 
ATOM   5026 O OD2   . ASP C 1 120 ? -20.650 24.247  -15.958 1.00 46.23  ? 92  ASP C OD2   1 
ATOM   5027 N N     . PHE C 1 121 ? -18.560 23.568  -10.882 1.00 41.71  ? 93  PHE C N     1 
ATOM   5028 C CA    . PHE C 1 121 ? -17.967 24.076  -9.649  1.00 40.86  ? 93  PHE C CA    1 
ATOM   5029 C C     . PHE C 1 121 ? -16.766 23.236  -9.232  1.00 41.93  ? 93  PHE C C     1 
ATOM   5030 O O     . PHE C 1 121 ? -15.764 23.770  -8.743  1.00 48.08  ? 93  PHE C O     1 
ATOM   5031 C CB    . PHE C 1 121 ? -19.015 24.104  -8.535  1.00 41.06  ? 93  PHE C CB    1 
ATOM   5032 C CG    . PHE C 1 121 ? -18.621 24.939  -7.347  1.00 40.79  ? 93  PHE C CG    1 
ATOM   5033 C CD1   . PHE C 1 121 ? -17.866 24.395  -6.322  1.00 42.29  ? 93  PHE C CD1   1 
ATOM   5034 C CD2   . PHE C 1 121 ? -19.018 26.262  -7.250  1.00 47.05  ? 93  PHE C CD2   1 
ATOM   5035 C CE1   . PHE C 1 121 ? -17.501 25.158  -5.230  1.00 45.72  ? 93  PHE C CE1   1 
ATOM   5036 C CE2   . PHE C 1 121 ? -18.660 27.030  -6.157  1.00 52.12  ? 93  PHE C CE2   1 
ATOM   5037 C CZ    . PHE C 1 121 ? -17.901 26.477  -5.145  1.00 48.28  ? 93  PHE C CZ    1 
ATOM   5038 N N     . CYS C 1 122 ? -16.850 21.917  -9.421  1.00 43.01  ? 94  CYS C N     1 
ATOM   5039 C CA    . CYS C 1 122 ? -15.759 21.029  -9.032  1.00 41.29  ? 94  CYS C CA    1 
ATOM   5040 C C     . CYS C 1 122 ? -14.503 21.309  -9.847  1.00 42.26  ? 94  CYS C C     1 
ATOM   5041 O O     . CYS C 1 122 ? -13.428 21.562  -9.292  1.00 47.20  ? 94  CYS C O     1 
ATOM   5042 C CB    . CYS C 1 122 ? -16.182 19.570  -9.204  1.00 41.68  ? 94  CYS C CB    1 
ATOM   5043 S SG    . CYS C 1 122 ? -17.724 19.103  -8.412  1.00 47.47  ? 94  CYS C SG    1 
ATOM   5044 N N     . ARG C 1 123 ? -14.626 21.264  -11.177 1.00 38.87  ? 95  ARG C N     1 
ATOM   5045 C CA    . ARG C 1 123 ? -13.475 21.417  -12.060 1.00 38.74  ? 95  ARG C CA    1 
ATOM   5046 C C     . ARG C 1 123 ? -12.747 22.735  -11.845 1.00 39.86  ? 95  ARG C C     1 
ATOM   5047 O O     . ARG C 1 123 ? -11.591 22.867  -12.262 1.00 41.36  ? 95  ARG C O     1 
ATOM   5048 C CB    . ARG C 1 123 ? -13.929 21.305  -13.514 1.00 39.75  ? 95  ARG C CB    1 
ATOM   5049 C CG    . ARG C 1 123 ? -14.702 20.037  -13.814 1.00 40.12  ? 95  ARG C CG    1 
ATOM   5050 C CD    . ARG C 1 123 ? -15.194 20.003  -15.251 1.00 41.27  ? 95  ARG C CD    1 
ATOM   5051 N NE    . ARG C 1 123 ? -14.942 18.720  -15.893 1.00 42.74  ? 95  ARG C NE    1 
ATOM   5052 C CZ    . ARG C 1 123 ? -15.611 18.268  -16.944 1.00 42.38  ? 95  ARG C CZ    1 
ATOM   5053 N NH1   . ARG C 1 123 ? -16.585 18.972  -17.498 1.00 43.43  ? 95  ARG C NH1   1 
ATOM   5054 N NH2   . ARG C 1 123 ? -15.302 17.077  -17.446 1.00 45.06  ? 95  ARG C NH2   1 
ATOM   5055 N N     . GLN C 1 124 ? -13.392 23.711  -11.211 1.00 40.91  ? 96  GLN C N     1 
ATOM   5056 C CA    . GLN C 1 124 ? -12.755 24.987  -10.909 1.00 46.19  ? 96  GLN C CA    1 
ATOM   5057 C C     . GLN C 1 124 ? -12.105 24.970  -9.527  1.00 49.40  ? 96  GLN C C     1 
ATOM   5058 O O     . GLN C 1 124 ? -10.883 25.105  -9.406  1.00 52.07  ? 96  GLN C O     1 
ATOM   5059 C CB    . GLN C 1 124 ? -13.782 26.120  -11.013 1.00 48.32  ? 96  GLN C CB    1 
ATOM   5060 C CG    . GLN C 1 124 ? -13.252 27.486  -10.616 1.00 52.13  ? 96  GLN C CG    1 
ATOM   5061 C CD    . GLN C 1 124 ? -14.120 28.617  -11.135 1.00 66.25  ? 96  GLN C CD    1 
ATOM   5062 O OE1   . GLN C 1 124 ? -13.633 29.538  -11.790 1.00 80.52  ? 96  GLN C OE1   1 
ATOM   5063 N NE2   . GLN C 1 124 ? -15.416 28.551  -10.845 1.00 64.82  ? 96  GLN C NE2   1 
ATOM   5064 N N     . HIS C 1 125 ? -12.910 24.793  -8.479  1.00 45.76  ? 97  HIS C N     1 
ATOM   5065 C CA    . HIS C 1 125 ? -12.410 24.868  -7.111  1.00 41.62  ? 97  HIS C CA    1 
ATOM   5066 C C     . HIS C 1 125 ? -11.767 23.561  -6.659  1.00 45.56  ? 97  HIS C C     1 
ATOM   5067 O O     . HIS C 1 125 ? -10.538 23.442  -6.656  1.00 56.60  ? 97  HIS C O     1 
ATOM   5068 C CB    . HIS C 1 125 ? -13.536 25.276  -6.159  1.00 43.11  ? 97  HIS C CB    1 
ATOM   5069 C CG    . HIS C 1 125 ? -14.268 26.512  -6.586  1.00 47.58  ? 97  HIS C CG    1 
ATOM   5070 N ND1   . HIS C 1 125 ? -15.256 26.500  -7.546  1.00 52.08  ? 97  HIS C ND1   1 
ATOM   5071 C CD2   . HIS C 1 125 ? -14.145 27.801  -6.189  1.00 48.61  ? 97  HIS C CD2   1 
ATOM   5072 C CE1   . HIS C 1 125 ? -15.716 27.727  -7.718  1.00 52.04  ? 97  HIS C CE1   1 
ATOM   5073 N NE2   . HIS C 1 125 ? -15.057 28.535  -6.907  1.00 47.84  ? 97  HIS C NE2   1 
ATOM   5074 N N     . ASN C 1 126 ? -12.576 22.573  -6.276  1.00 41.25  ? 98  ASN C N     1 
ATOM   5075 C CA    . ASN C 1 126 ? -12.035 21.319  -5.760  1.00 42.22  ? 98  ASN C CA    1 
ATOM   5076 C C     . ASN C 1 126 ? -11.477 20.425  -6.862  1.00 44.94  ? 98  ASN C C     1 
ATOM   5077 O O     . ASN C 1 126 ? -11.728 19.218  -6.866  1.00 46.30  ? 98  ASN C O     1 
ATOM   5078 C CB    . ASN C 1 126 ? -13.103 20.561  -4.973  1.00 40.31  ? 98  ASN C CB    1 
ATOM   5079 C CG    . ASN C 1 126 ? -13.887 21.457  -4.037  1.00 51.04  ? 98  ASN C CG    1 
ATOM   5080 O OD1   . ASN C 1 126 ? -14.531 22.415  -4.468  1.00 58.43  ? 98  ASN C OD1   1 
ATOM   5081 N ND2   . ASN C 1 126 ? -13.834 21.150  -2.746  1.00 50.41  ? 98  ASN C ND2   1 
ATOM   5082 N N     . ALA C 1 127 ? -10.712 20.997  -7.787  1.00 44.28  ? 99  ALA C N     1 
ATOM   5083 C CA    . ALA C 1 127 ? -10.122 20.237  -8.880  1.00 43.08  ? 99  ALA C CA    1 
ATOM   5084 C C     . ALA C 1 127 ? -8.786  19.657  -8.433  1.00 46.82  ? 99  ALA C C     1 
ATOM   5085 O O     . ALA C 1 127 ? -7.868  20.402  -8.077  1.00 46.93  ? 99  ALA C O     1 
ATOM   5086 C CB    . ALA C 1 127 ? -9.940  21.117  -10.115 1.00 48.33  ? 99  ALA C CB    1 
ATOM   5087 N N     . LEU C 1 128 ? -8.680  18.331  -8.455  1.00 49.78  ? 100 LEU C N     1 
ATOM   5088 C CA    . LEU C 1 128 ? -7.450  17.633  -8.080  1.00 51.46  ? 100 LEU C CA    1 
ATOM   5089 C C     . LEU C 1 128 ? -6.931  16.897  -9.306  1.00 51.76  ? 100 LEU C C     1 
ATOM   5090 O O     . LEU C 1 128 ? -7.430  15.807  -9.638  1.00 53.60  ? 100 LEU C O     1 
ATOM   5091 C CB    . LEU C 1 128 ? -7.702  16.662  -6.925  1.00 55.04  ? 100 LEU C CB    1 
ATOM   5092 C CG    . LEU C 1 128 ? -6.584  15.702  -6.505  1.00 53.52  ? 100 LEU C CG    1 
ATOM   5093 C CD1   . LEU C 1 128 ? -5.233  16.402  -6.460  1.00 52.28  ? 100 LEU C CD1   1 
ATOM   5094 C CD2   . LEU C 1 128 ? -6.908  15.064  -5.161  1.00 54.14  ? 100 LEU C CD2   1 
ATOM   5095 N N     . PRO C 1 129 ? -5.950  17.450  -10.015 1.00 53.37  ? 101 PRO C N     1 
ATOM   5096 C CA    . PRO C 1 129 ? -5.473  16.813  -11.247 1.00 50.71  ? 101 PRO C CA    1 
ATOM   5097 C C     . PRO C 1 129 ? -4.731  15.516  -10.965 1.00 49.43  ? 101 PRO C C     1 
ATOM   5098 O O     . PRO C 1 129 ? -4.217  15.279  -9.869  1.00 52.74  ? 101 PRO C O     1 
ATOM   5099 C CB    . PRO C 1 129 ? -4.534  17.863  -11.855 1.00 39.98  ? 101 PRO C CB    1 
ATOM   5100 C CG    . PRO C 1 129 ? -4.868  19.147  -11.151 1.00 47.39  ? 101 PRO C CG    1 
ATOM   5101 C CD    . PRO C 1 129 ? -5.307  18.752  -9.781  1.00 52.08  ? 101 PRO C CD    1 
ATOM   5102 N N     . GLY C 1 130 ? -4.681  14.667  -11.991 1.00 43.54  ? 102 GLY C N     1 
ATOM   5103 C CA    . GLY C 1 130 ? -4.037  13.376  -11.887 1.00 42.69  ? 102 GLY C CA    1 
ATOM   5104 C C     . GLY C 1 130 ? -4.721  12.386  -10.974 1.00 46.37  ? 102 GLY C C     1 
ATOM   5105 O O     . GLY C 1 130 ? -4.212  11.272  -10.806 1.00 55.68  ? 102 GLY C O     1 
ATOM   5106 N N     . THR C 1 131 ? -5.856  12.750  -10.380 1.00 41.38  ? 103 THR C N     1 
ATOM   5107 C CA    . THR C 1 131 ? -6.556  11.867  -9.457  1.00 42.37  ? 103 THR C CA    1 
ATOM   5108 C C     . THR C 1 131 ? -8.056  11.895  -9.714  1.00 46.97  ? 103 THR C C     1 
ATOM   5109 O O     . THR C 1 131 ? -8.624  10.928  -10.230 1.00 50.27  ? 103 THR C O     1 
ATOM   5110 C CB    . THR C 1 131 ? -6.266  12.264  -8.007  1.00 48.90  ? 103 THR C CB    1 
ATOM   5111 O OG1   . THR C 1 131 ? -4.853  12.401  -7.817  1.00 51.12  ? 103 THR C OG1   1 
ATOM   5112 C CG2   . THR C 1 131 ? -6.801  11.212  -7.047  1.00 50.50  ? 103 THR C CG2   1 
ATOM   5113 N N     . ILE C 1 132 ? -8.703  12.999  -9.360  1.00 47.37  ? 104 ILE C N     1 
ATOM   5114 C CA    . ILE C 1 132 ? -10.153 13.113  -9.453  1.00 47.59  ? 104 ILE C CA    1 
ATOM   5115 C C     . ILE C 1 132 ? -10.531 13.698  -10.804 1.00 44.82  ? 104 ILE C C     1 
ATOM   5116 O O     . ILE C 1 132 ? -10.003 14.739  -11.216 1.00 43.93  ? 104 ILE C O     1 
ATOM   5117 C CB    . ILE C 1 132 ? -10.710 13.970  -8.307  1.00 45.33  ? 104 ILE C CB    1 
ATOM   5118 C CG1   . ILE C 1 132 ? -9.984  13.636  -7.005  1.00 47.14  ? 104 ILE C CG1   1 
ATOM   5119 C CG2   . ILE C 1 132 ? -12.210 13.760  -8.168  1.00 43.76  ? 104 ILE C CG2   1 
ATOM   5120 C CD1   . ILE C 1 132 ? -10.573 14.306  -5.805  1.00 46.78  ? 104 ILE C CD1   1 
ATOM   5121 N N     . THR C 1 133 ? -11.448 13.026  -11.494 1.00 44.79  ? 105 THR C N     1 
ATOM   5122 C CA    . THR C 1 133 ? -12.020 13.506  -12.744 1.00 42.18  ? 105 THR C CA    1 
ATOM   5123 C C     . THR C 1 133 ? -13.509 13.724  -12.523 1.00 42.48  ? 105 THR C C     1 
ATOM   5124 O O     . THR C 1 133 ? -14.216 12.806  -12.092 1.00 43.40  ? 105 THR C O     1 
ATOM   5125 C CB    . THR C 1 133 ? -11.778 12.512  -13.882 1.00 47.11  ? 105 THR C CB    1 
ATOM   5126 O OG1   . THR C 1 133 ? -12.656 11.389  -13.733 1.00 58.36  ? 105 THR C OG1   1 
ATOM   5127 C CG2   . THR C 1 133 ? -10.336 12.025  -13.867 1.00 45.43  ? 105 THR C CG2   1 
ATOM   5128 N N     . TYR C 1 134 ? -13.981 14.936  -12.808 1.00 40.87  ? 106 TYR C N     1 
ATOM   5129 C CA    . TYR C 1 134 ? -15.377 15.305  -12.601 1.00 39.33  ? 106 TYR C CA    1 
ATOM   5130 C C     . TYR C 1 134 ? -16.108 15.259  -13.938 1.00 40.56  ? 106 TYR C C     1 
ATOM   5131 O O     . TYR C 1 134 ? -15.825 16.058  -14.836 1.00 43.25  ? 106 TYR C O     1 
ATOM   5132 C CB    . TYR C 1 134 ? -15.488 16.688  -11.965 1.00 39.12  ? 106 TYR C CB    1 
ATOM   5133 C CG    . TYR C 1 134 ? -14.826 16.805  -10.611 1.00 38.02  ? 106 TYR C CG    1 
ATOM   5134 C CD1   . TYR C 1 134 ? -15.407 16.242  -9.482  1.00 38.37  ? 106 TYR C CD1   1 
ATOM   5135 C CD2   . TYR C 1 134 ? -13.629 17.490  -10.458 1.00 43.44  ? 106 TYR C CD2   1 
ATOM   5136 C CE1   . TYR C 1 134 ? -14.810 16.354  -8.241  1.00 41.68  ? 106 TYR C CE1   1 
ATOM   5137 C CE2   . TYR C 1 134 ? -13.024 17.606  -9.221  1.00 41.65  ? 106 TYR C CE2   1 
ATOM   5138 C CZ    . TYR C 1 134 ? -13.619 17.036  -8.117  1.00 43.07  ? 106 TYR C CZ    1 
ATOM   5139 O OH    . TYR C 1 134 ? -13.020 17.150  -6.883  1.00 54.50  ? 106 TYR C OH    1 
ATOM   5140 N N     . GLU C 1 135 ? -17.045 14.327  -14.067 1.00 41.21  ? 107 GLU C N     1 
ATOM   5141 C CA    . GLU C 1 135 ? -17.882 14.195  -15.251 1.00 42.52  ? 107 GLU C CA    1 
ATOM   5142 C C     . GLU C 1 135 ? -19.349 14.362  -14.867 1.00 43.29  ? 107 GLU C C     1 
ATOM   5143 O O     . GLU C 1 135 ? -19.692 14.576  -13.703 1.00 42.81  ? 107 GLU C O     1 
ATOM   5144 C CB    . GLU C 1 135 ? -17.646 12.851  -15.946 1.00 42.84  ? 107 GLU C CB    1 
ATOM   5145 C CG    . GLU C 1 135 ? -16.422 12.826  -16.849 1.00 42.66  ? 107 GLU C CG    1 
ATOM   5146 C CD    . GLU C 1 135 ? -15.200 12.248  -16.165 1.00 52.12  ? 107 GLU C CD    1 
ATOM   5147 O OE1   . GLU C 1 135 ? -14.880 12.689  -15.043 1.00 61.18  ? 107 GLU C OE1   1 
ATOM   5148 O OE2   . GLU C 1 135 ? -14.556 11.352  -16.752 1.00 55.72  ? 107 GLU C OE2   1 
ATOM   5149 N N     . LEU C 1 136 ? -20.217 14.268  -15.868 1.00 44.58  ? 108 LEU C N     1 
ATOM   5150 C CA    . LEU C 1 136 ? -21.654 14.415  -15.690 1.00 45.56  ? 108 LEU C CA    1 
ATOM   5151 C C     . LEU C 1 136 ? -22.332 13.071  -15.918 1.00 46.29  ? 108 LEU C C     1 
ATOM   5152 O O     . LEU C 1 136 ? -22.017 12.364  -16.881 1.00 46.74  ? 108 LEU C O     1 
ATOM   5153 C CB    . LEU C 1 136 ? -22.211 15.479  -16.646 1.00 46.66  ? 108 LEU C CB    1 
ATOM   5154 C CG    . LEU C 1 136 ? -23.714 15.607  -16.912 1.00 48.09  ? 108 LEU C CG    1 
ATOM   5155 C CD1   . LEU C 1 136 ? -24.046 17.052  -17.237 1.00 48.66  ? 108 LEU C CD1   1 
ATOM   5156 C CD2   . LEU C 1 136 ? -24.169 14.711  -18.060 1.00 49.29  ? 108 LEU C CD2   1 
ATOM   5157 N N     . LEU C 1 137 ? -23.264 12.722  -15.033 1.00 46.48  ? 109 LEU C N     1 
ATOM   5158 C CA    . LEU C 1 137 ? -23.937 11.435  -15.126 1.00 47.20  ? 109 LEU C CA    1 
ATOM   5159 C C     . LEU C 1 137 ? -25.223 11.463  -14.312 1.00 47.80  ? 109 LEU C C     1 
ATOM   5160 O O     . LEU C 1 137 ? -25.255 12.009  -13.206 1.00 47.08  ? 109 LEU C O     1 
ATOM   5161 C CB    . LEU C 1 137 ? -23.032 10.299  -14.634 1.00 46.23  ? 109 LEU C CB    1 
ATOM   5162 C CG    . LEU C 1 137 ? -23.654 8.901   -14.637 1.00 46.94  ? 109 LEU C CG    1 
ATOM   5163 C CD1   . LEU C 1 137 ? -23.852 8.404   -16.060 1.00 48.16  ? 109 LEU C CD1   1 
ATOM   5164 C CD2   . LEU C 1 137 ? -22.808 7.927   -13.834 1.00 45.86  ? 109 LEU C CD2   1 
ATOM   5165 N N     . ASP C 1 138 ? -26.274 10.872  -14.873 1.00 49.18  ? 110 ASP C N     1 
ATOM   5166 C CA    . ASP C 1 138 ? -27.515 10.610  -14.158 1.00 49.91  ? 110 ASP C CA    1 
ATOM   5167 C C     . ASP C 1 138 ? -27.508 9.140   -13.755 1.00 49.83  ? 110 ASP C C     1 
ATOM   5168 O O     . ASP C 1 138 ? -27.373 8.263   -14.613 1.00 50.41  ? 110 ASP C O     1 
ATOM   5169 C CB    . ASP C 1 138 ? -28.727 10.935  -15.033 1.00 51.66  ? 110 ASP C CB    1 
ATOM   5170 C CG    . ASP C 1 138 ? -30.046 10.824  -14.283 1.00 52.52  ? 110 ASP C CG    1 
ATOM   5171 O OD1   . ASP C 1 138 ? -30.046 10.393  -13.111 1.00 51.81  ? 110 ASP C OD1   1 
ATOM   5172 O OD2   . ASP C 1 138 ? -31.091 11.175  -14.873 1.00 53.98  ? 110 ASP C OD2   1 
ATOM   5173 N N     . VAL C 1 139 ? -27.651 8.875   -12.453 1.00 49.18  ? 111 VAL C N     1 
ATOM   5174 C CA    . VAL C 1 139 ? -27.508 7.514   -11.946 1.00 48.96  ? 111 VAL C CA    1 
ATOM   5175 C C     . VAL C 1 139 ? -28.568 6.580   -12.517 1.00 50.54  ? 111 VAL C C     1 
ATOM   5176 O O     . VAL C 1 139 ? -28.373 5.359   -12.537 1.00 50.64  ? 111 VAL C O     1 
ATOM   5177 C CB    . VAL C 1 139 ? -27.540 7.515   -10.400 1.00 48.07  ? 111 VAL C CB    1 
ATOM   5178 C CG1   . VAL C 1 139 ? -28.942 7.807   -9.888  1.00 49.77  ? 111 VAL C CG1   1 
ATOM   5179 C CG2   . VAL C 1 139 ? -27.008 6.200   -9.842  1.00 47.50  ? 111 VAL C CG2   1 
ATOM   5180 N N     . VAL C 1 140 ? -29.686 7.122   -12.997 1.00 51.87  ? 112 VAL C N     1 
ATOM   5181 C CA    . VAL C 1 140 ? -30.719 6.314   -13.637 1.00 53.55  ? 112 VAL C CA    1 
ATOM   5182 C C     . VAL C 1 140 ? -30.743 6.624   -15.128 1.00 54.52  ? 112 VAL C C     1 
ATOM   5183 O O     . VAL C 1 140 ? -31.812 6.820   -15.718 1.00 56.06  ? 112 VAL C O     1 
ATOM   5184 C CB    . VAL C 1 140 ? -32.096 6.553   -12.995 1.00 54.57  ? 112 VAL C CB    1 
ATOM   5185 C CG1   . VAL C 1 140 ? -32.195 5.802   -11.679 1.00 54.02  ? 112 VAL C CG1   1 
ATOM   5186 C CG2   . VAL C 1 140 ? -32.332 8.040   -12.777 1.00 54.40  ? 112 VAL C CG2   1 
ATOM   5187 N N     . GLU C 1 141 ? -29.568 6.661   -15.743 1.00 53.71  ? 113 GLU C N     1 
ATOM   5188 C CA    . GLU C 1 141 ? -29.477 6.974   -17.163 1.00 54.59  ? 113 GLU C CA    1 
ATOM   5189 C C     . GLU C 1 141 ? -29.988 5.796   -17.985 1.00 56.03  ? 113 GLU C C     1 
ATOM   5190 O O     . GLU C 1 141 ? -29.592 4.652   -17.729 1.00 55.73  ? 113 GLU C O     1 
ATOM   5191 C CB    . GLU C 1 141 ? -28.035 7.298   -17.546 1.00 53.34  ? 113 GLU C CB    1 
ATOM   5192 C CG    . GLU C 1 141 ? -27.810 8.738   -17.980 1.00 53.16  ? 113 GLU C CG    1 
ATOM   5193 C CD    . GLU C 1 141 ? -28.179 8.978   -19.430 1.00 62.28  ? 113 GLU C CD    1 
ATOM   5194 O OE1   . GLU C 1 141 ? -28.440 7.991   -20.151 1.00 60.75  ? 113 GLU C OE1   1 
ATOM   5195 O OE2   . GLU C 1 141 ? -28.206 10.154  -19.850 1.00 76.48  ? 113 GLU C OE2   1 
ATOM   5196 N N     . PRO C 1 142 ? -30.871 6.025   -18.961 1.00 57.68  ? 114 PRO C N     1 
ATOM   5197 C CA    . PRO C 1 142 ? -31.323 4.906   -19.804 1.00 59.16  ? 114 PRO C CA    1 
ATOM   5198 C C     . PRO C 1 142 ? -30.188 4.224   -20.545 1.00 58.76  ? 114 PRO C C     1 
ATOM   5199 O O     . PRO C 1 142 ? -30.165 2.991   -20.646 1.00 59.23  ? 114 PRO C O     1 
ATOM   5200 C CB    . PRO C 1 142 ? -32.306 5.579   -20.772 1.00 60.87  ? 114 PRO C CB    1 
ATOM   5201 C CG    . PRO C 1 142 ? -32.792 6.781   -20.036 1.00 60.50  ? 114 PRO C CG    1 
ATOM   5202 C CD    . PRO C 1 142 ? -31.613 7.265   -19.240 1.00 58.41  ? 114 PRO C CD    1 
ATOM   5203 N N     . ARG C 1 143 ? -29.239 4.998   -21.062 1.00 57.96  ? 115 ARG C N     1 
ATOM   5204 C CA    . ARG C 1 143 ? -28.108 4.480   -21.824 1.00 57.62  ? 115 ARG C CA    1 
ATOM   5205 C C     . ARG C 1 143 ? -26.830 4.759   -21.041 1.00 55.60  ? 115 ARG C C     1 
ATOM   5206 O O     . ARG C 1 143 ? -26.088 5.699   -21.329 1.00 54.87  ? 115 ARG C O     1 
ATOM   5207 C CB    . ARG C 1 143 ? -28.064 5.105   -23.202 1.00 58.61  ? 115 ARG C CB    1 
ATOM   5208 C CG    . ARG C 1 143 ? -29.427 5.405   -23.791 1.00 60.46  ? 115 ARG C CG    1 
ATOM   5209 C CD    . ARG C 1 143 ? -29.277 5.805   -25.238 1.00 61.54  ? 115 ARG C CD    1 
ATOM   5210 N NE    . ARG C 1 143 ? -28.427 4.840   -25.923 1.00 61.61  ? 115 ARG C NE    1 
ATOM   5211 C CZ    . ARG C 1 143 ? -28.869 3.747   -26.526 1.00 63.02  ? 115 ARG C CZ    1 
ATOM   5212 N NH1   . ARG C 1 143 ? -30.160 3.457   -26.576 1.00 64.54  ? 115 ARG C NH1   1 
ATOM   5213 N NH2   . ARG C 1 143 ? -27.994 2.918   -27.085 1.00 62.98  ? 115 ARG C NH2   1 
ATOM   5214 N N     . LEU C 1 144 ? -26.574 3.918   -20.038 1.00 54.77  ? 116 LEU C N     1 
ATOM   5215 C CA    . LEU C 1 144 ? -25.371 4.080   -19.229 1.00 52.93  ? 116 LEU C CA    1 
ATOM   5216 C C     . LEU C 1 144 ? -24.119 3.849   -20.067 1.00 52.56  ? 116 LEU C C     1 
ATOM   5217 O O     . LEU C 1 144 ? -23.115 4.554   -19.908 1.00 51.34  ? 116 LEU C O     1 
ATOM   5218 C CB    . LEU C 1 144 ? -25.415 3.115   -18.042 1.00 52.34  ? 116 LEU C CB    1 
ATOM   5219 C CG    . LEU C 1 144 ? -24.704 3.427   -16.717 1.00 50.58  ? 116 LEU C CG    1 
ATOM   5220 C CD1   . LEU C 1 144 ? -24.917 2.281   -15.744 1.00 50.43  ? 116 LEU C CD1   1 
ATOM   5221 C CD2   . LEU C 1 144 ? -23.221 3.713   -16.870 1.00 49.31  ? 116 LEU C CD2   1 
ATOM   5222 N N     . GLU C 1 145 ? -24.171 2.882   -20.986 1.00 53.69  ? 117 GLU C N     1 
ATOM   5223 C CA    . GLU C 1 145 ? -22.987 2.479   -21.733 1.00 53.44  ? 117 GLU C CA    1 
ATOM   5224 C C     . GLU C 1 145 ? -22.483 3.562   -22.679 1.00 53.47  ? 117 GLU C C     1 
ATOM   5225 O O     . GLU C 1 145 ? -21.348 3.467   -23.158 1.00 52.99  ? 117 GLU C O     1 
ATOM   5226 C CB    . GLU C 1 145 ? -23.283 1.202   -22.520 1.00 54.86  ? 117 GLU C CB    1 
ATOM   5227 C CG    . GLU C 1 145 ? -23.123 -0.071  -21.707 1.00 54.52  ? 117 GLU C CG    1 
ATOM   5228 C CD    . GLU C 1 145 ? -24.402 -0.462  -20.988 1.00 57.26  ? 117 GLU C CD    1 
ATOM   5229 O OE1   . GLU C 1 145 ? -25.494 -0.222  -21.544 1.00 61.52  ? 117 GLU C OE1   1 
ATOM   5230 O OE2   . GLU C 1 145 ? -24.316 -1.003  -19.864 1.00 54.39  ? 117 GLU C OE2   1 
ATOM   5231 N N     . ASP C 1 146 ? -23.290 4.583   -22.960 1.00 54.08  ? 118 ASP C N     1 
ATOM   5232 C CA    . ASP C 1 146 ? -22.895 5.675   -23.837 1.00 54.22  ? 118 ASP C CA    1 
ATOM   5233 C C     . ASP C 1 146 ? -22.347 6.875   -23.074 1.00 52.76  ? 118 ASP C C     1 
ATOM   5234 O O     . ASP C 1 146 ? -22.198 7.953   -23.659 1.00 52.91  ? 118 ASP C O     1 
ATOM   5235 C CB    . ASP C 1 146 ? -24.076 6.107   -24.709 1.00 55.93  ? 118 ASP C CB    1 
ATOM   5236 C CG    . ASP C 1 146 ? -24.528 5.015   -25.660 1.00 57.54  ? 118 ASP C CG    1 
ATOM   5237 O OD1   . ASP C 1 146 ? -24.828 3.898   -25.189 1.00 57.72  ? 118 ASP C OD1   1 
ATOM   5238 O OD2   . ASP C 1 146 ? -24.585 5.274   -26.879 1.00 58.70  ? 118 ASP C OD2   1 
ATOM   5239 N N     . THR C 1 147 ? -22.043 6.716   -21.790 1.00 51.44  ? 119 THR C N     1 
ATOM   5240 C CA    . THR C 1 147 ? -21.528 7.800   -20.968 1.00 50.09  ? 119 THR C CA    1 
ATOM   5241 C C     . THR C 1 147 ? -20.028 7.643   -20.747 1.00 48.77  ? 119 THR C C     1 
ATOM   5242 O O     . THR C 1 147 ? -19.469 6.548   -20.845 1.00 48.67  ? 119 THR C O     1 
ATOM   5243 C CB    . THR C 1 147 ? -22.249 7.852   -19.619 1.00 49.57  ? 119 THR C CB    1 
ATOM   5244 O OG1   . THR C 1 147 ? -21.931 6.680   -18.858 1.00 48.97  ? 119 THR C OG1   1 
ATOM   5245 C CG2   . THR C 1 147 ? -23.755 7.927   -19.821 1.00 50.99  ? 119 THR C CG2   1 
ATOM   5246 N N     . VAL C 1 148 ? -19.379 8.770   -20.447 1.00 47.82  ? 120 VAL C N     1 
ATOM   5247 C CA    . VAL C 1 148 ? -17.944 8.758   -20.183 1.00 46.59  ? 120 VAL C CA    1 
ATOM   5248 C C     . VAL C 1 148 ? -17.641 7.969   -18.916 1.00 45.53  ? 120 VAL C C     1 
ATOM   5249 O O     . VAL C 1 148 ? -16.647 7.235   -18.846 1.00 44.96  ? 120 VAL C O     1 
ATOM   5250 C CB    . VAL C 1 148 ? -17.410 10.200  -20.095 1.00 45.94  ? 120 VAL C CB    1 
ATOM   5251 C CG1   . VAL C 1 148 ? -16.013 10.215  -19.514 1.00 44.57  ? 120 VAL C CG1   1 
ATOM   5252 C CG2   . VAL C 1 148 ? -17.429 10.864  -21.464 1.00 46.96  ? 120 VAL C CG2   1 
ATOM   5253 N N     . VAL C 1 149 ? -18.498 8.099   -17.900 1.00 45.34  ? 121 VAL C N     1 
ATOM   5254 C CA    . VAL C 1 149 ? -18.274 7.415   -16.629 1.00 44.39  ? 121 VAL C CA    1 
ATOM   5255 C C     . VAL C 1 149 ? -18.230 5.906   -16.829 1.00 44.82  ? 121 VAL C C     1 
ATOM   5256 O O     . VAL C 1 149 ? -17.421 5.206   -16.208 1.00 43.99  ? 121 VAL C O     1 
ATOM   5257 C CB    . VAL C 1 149 ? -19.359 7.820   -15.612 1.00 44.38  ? 121 VAL C CB    1 
ATOM   5258 C CG1   . VAL C 1 149 ? -19.277 6.955   -14.366 1.00 43.64  ? 121 VAL C CG1   1 
ATOM   5259 C CG2   . VAL C 1 149 ? -19.226 9.292   -15.253 1.00 43.80  ? 121 VAL C CG2   1 
ATOM   5260 N N     . TRP C 1 150 ? -19.086 5.383   -17.710 1.00 46.21  ? 122 TRP C N     1 
ATOM   5261 C CA    . TRP C 1 150 ? -19.138 3.941   -17.923 1.00 46.80  ? 122 TRP C CA    1 
ATOM   5262 C C     . TRP C 1 150 ? -17.824 3.399   -18.465 1.00 46.45  ? 122 TRP C C     1 
ATOM   5263 O O     . TRP C 1 150 ? -17.466 2.248   -18.189 1.00 47.98  ? 122 TRP C O     1 
ATOM   5264 C CB    . TRP C 1 150 ? -20.277 3.589   -18.877 1.00 48.50  ? 122 TRP C CB    1 
ATOM   5265 C CG    . TRP C 1 150 ? -20.206 2.185   -19.391 1.00 49.32  ? 122 TRP C CG    1 
ATOM   5266 C CD1   . TRP C 1 150 ? -19.760 1.781   -20.617 1.00 50.13  ? 122 TRP C CD1   1 
ATOM   5267 C CD2   . TRP C 1 150 ? -20.577 0.995   -18.687 1.00 49.48  ? 122 TRP C CD2   1 
ATOM   5268 N NE1   . TRP C 1 150 ? -19.839 0.414   -20.722 1.00 50.80  ? 122 TRP C NE1   1 
ATOM   5269 C CE2   . TRP C 1 150 ? -20.337 -0.093  -19.550 1.00 50.42  ? 122 TRP C CE2   1 
ATOM   5270 C CE3   . TRP C 1 150 ? -21.093 0.743   -17.412 1.00 48.98  ? 122 TRP C CE3   1 
ATOM   5271 C CZ2   . TRP C 1 150 ? -20.595 -1.411  -19.180 1.00 52.98  ? 122 TRP C CZ2   1 
ATOM   5272 C CZ3   . TRP C 1 150 ? -21.348 -0.566  -17.046 1.00 49.43  ? 122 TRP C CZ3   1 
ATOM   5273 C CH2   . TRP C 1 150 ? -21.099 -1.626  -17.926 1.00 52.65  ? 122 TRP C CH2   1 
ATOM   5274 N N     . ARG C 1 151 ? -17.089 4.204   -19.227 1.00 46.30  ? 123 ARG C N     1 
ATOM   5275 C CA    . ARG C 1 151 ? -15.910 3.714   -19.921 1.00 46.22  ? 123 ARG C CA    1 
ATOM   5276 C C     . ARG C 1 151 ? -14.609 4.078   -19.225 1.00 49.20  ? 123 ARG C C     1 
ATOM   5277 O O     . ARG C 1 151 ? -13.544 3.632   -19.663 1.00 52.23  ? 123 ARG C O     1 
ATOM   5278 C CB    . ARG C 1 151 ? -15.916 4.231   -21.353 1.00 47.25  ? 123 ARG C CB    1 
ATOM   5279 C CG    . ARG C 1 151 ? -17.160 3.758   -22.053 1.00 48.81  ? 123 ARG C CG    1 
ATOM   5280 C CD    . ARG C 1 151 ? -17.137 4.053   -23.510 1.00 49.98  ? 123 ARG C CD    1 
ATOM   5281 N NE    . ARG C 1 151 ? -18.416 3.725   -24.118 1.00 51.53  ? 123 ARG C NE    1 
ATOM   5282 C CZ    . ARG C 1 151 ? -18.710 3.976   -25.383 1.00 52.84  ? 123 ARG C CZ    1 
ATOM   5283 N NH1   . ARG C 1 151 ? -17.810 4.483   -26.205 1.00 52.82  ? 123 ARG C NH1   1 
ATOM   5284 N NH2   . ARG C 1 151 ? -19.930 3.699   -25.835 1.00 54.28  ? 123 ARG C NH2   1 
ATOM   5285 N N     . ASN C 1 152 ? -14.670 4.877   -18.162 1.00 49.52  ? 124 ASN C N     1 
ATOM   5286 C CA    . ASN C 1 152 ? -13.572 4.929   -17.211 1.00 51.34  ? 124 ASN C CA    1 
ATOM   5287 C C     . ASN C 1 152 ? -13.580 3.732   -16.275 1.00 50.22  ? 124 ASN C C     1 
ATOM   5288 O O     . ASN C 1 152 ? -12.611 3.536   -15.534 1.00 54.60  ? 124 ASN C O     1 
ATOM   5289 C CB    . ASN C 1 152 ? -13.631 6.222   -16.394 1.00 56.36  ? 124 ASN C CB    1 
ATOM   5290 C CG    . ASN C 1 152 ? -13.223 7.438   -17.199 1.00 58.52  ? 124 ASN C CG    1 
ATOM   5291 O OD1   . ASN C 1 152 ? -12.037 7.681   -17.422 1.00 63.35  ? 124 ASN C OD1   1 
ATOM   5292 N ND2   . ASN C 1 152 ? -14.207 8.210   -17.639 1.00 56.80  ? 124 ASN C ND2   1 
ATOM   5293 N N     . GLY C 1 153 ? -14.644 2.934   -16.297 1.00 45.77  ? 125 GLY C N     1 
ATOM   5294 C CA    . GLY C 1 153 ? -14.745 1.759   -15.470 1.00 45.66  ? 125 GLY C CA    1 
ATOM   5295 C C     . GLY C 1 153 ? -14.117 0.543   -16.118 1.00 47.84  ? 125 GLY C C     1 
ATOM   5296 O O     . GLY C 1 153 ? -13.412 0.644   -17.128 1.00 54.35  ? 125 GLY C O     1 
ATOM   5297 N N     . PRO C 1 154 ? -14.363 -0.643  -15.547 1.00 47.47  ? 126 PRO C N     1 
ATOM   5298 C CA    . PRO C 1 154 ? -15.213 -0.917  -14.380 1.00 47.08  ? 126 PRO C CA    1 
ATOM   5299 C C     . PRO C 1 154 ? -14.564 -0.446  -13.082 1.00 46.45  ? 126 PRO C C     1 
ATOM   5300 O O     . PRO C 1 154 ? -13.342 -0.408  -12.968 1.00 46.90  ? 126 PRO C O     1 
ATOM   5301 C CB    . PRO C 1 154 ? -15.382 -2.437  -14.438 1.00 47.69  ? 126 PRO C CB    1 
ATOM   5302 C CG    . PRO C 1 154 ? -14.082 -2.922  -15.014 1.00 47.65  ? 126 PRO C CG    1 
ATOM   5303 C CD    . PRO C 1 154 ? -13.632 -1.848  -15.982 1.00 51.12  ? 126 PRO C CD    1 
ATOM   5304 N N     . PHE C 1 155 ? -15.364 -0.071  -12.091 1.00 46.98  ? 127 PHE C N     1 
ATOM   5305 C CA    . PHE C 1 155 ? -14.863 0.564   -10.882 1.00 48.39  ? 127 PHE C CA    1 
ATOM   5306 C C     . PHE C 1 155 ? -14.722 -0.453  -9.759  1.00 51.35  ? 127 PHE C C     1 
ATOM   5307 O O     . PHE C 1 155 ? -15.556 -1.351  -9.608  1.00 52.61  ? 127 PHE C O     1 
ATOM   5308 C CB    . PHE C 1 155 ? -15.791 1.699   -10.445 1.00 50.22  ? 127 PHE C CB    1 
ATOM   5309 C CG    . PHE C 1 155 ? -15.840 2.845   -11.414 1.00 46.77  ? 127 PHE C CG    1 
ATOM   5310 C CD1   . PHE C 1 155 ? -14.923 3.879   -11.333 1.00 48.71  ? 127 PHE C CD1   1 
ATOM   5311 C CD2   . PHE C 1 155 ? -16.800 2.884   -12.412 1.00 43.17  ? 127 PHE C CD2   1 
ATOM   5312 C CE1   . PHE C 1 155 ? -14.964 4.932   -12.227 1.00 46.80  ? 127 PHE C CE1   1 
ATOM   5313 C CE2   . PHE C 1 155 ? -16.846 3.934   -13.307 1.00 45.77  ? 127 PHE C CE2   1 
ATOM   5314 C CZ    . PHE C 1 155 ? -15.927 4.960   -13.215 1.00 47.16  ? 127 PHE C CZ    1 
ATOM   5315 N N     . GLY C 1 156 ? -13.654 -0.306  -8.973  1.00 44.84  ? 128 GLY C N     1 
ATOM   5316 C CA    . GLY C 1 156 ? -13.474 -1.176  -7.823  1.00 49.96  ? 128 GLY C CA    1 
ATOM   5317 C C     . GLY C 1 156 ? -14.473 -0.882  -6.720  1.00 55.23  ? 128 GLY C C     1 
ATOM   5318 O O     . GLY C 1 156 ? -15.154 -1.783  -6.225  1.00 56.58  ? 128 GLY C O     1 
ATOM   5319 N N     . LYS C 1 157 ? -14.577 0.384   -6.324  1.00 55.45  ? 129 LYS C N     1 
ATOM   5320 C CA    . LYS C 1 157 ? -15.522 0.814   -5.306  1.00 57.56  ? 129 LYS C CA    1 
ATOM   5321 C C     . LYS C 1 157 ? -16.362 1.961   -5.848  1.00 56.02  ? 129 LYS C C     1 
ATOM   5322 O O     . LYS C 1 157 ? -15.927 2.709   -6.727  1.00 57.62  ? 129 LYS C O     1 
ATOM   5323 C CB    . LYS C 1 157 ? -14.807 1.252   -4.017  1.00 58.02  ? 129 LYS C CB    1 
ATOM   5324 C CG    . LYS C 1 157 ? -13.738 0.282   -3.542  1.00 63.27  ? 129 LYS C CG    1 
ATOM   5325 C CD    . LYS C 1 157 ? -14.334 -1.077  -3.218  1.00 65.79  ? 129 LYS C CD    1 
ATOM   5326 C CE    . LYS C 1 157 ? -13.253 -2.135  -3.076  1.00 67.88  ? 129 LYS C CE    1 
ATOM   5327 N NZ    . LYS C 1 157 ? -13.444 -3.257  -4.038  1.00 65.58  ? 129 LYS C NZ    1 
ATOM   5328 N N     . VAL C 1 158 ? -17.577 2.089   -5.318  1.00 54.92  ? 130 VAL C N     1 
ATOM   5329 C CA    . VAL C 1 158 ? -18.499 3.153   -5.701  1.00 50.53  ? 130 VAL C CA    1 
ATOM   5330 C C     . VAL C 1 158 ? -19.086 3.753   -4.432  1.00 52.02  ? 130 VAL C C     1 
ATOM   5331 O O     . VAL C 1 158 ? -19.736 3.049   -3.651  1.00 51.71  ? 130 VAL C O     1 
ATOM   5332 C CB    . VAL C 1 158 ? -19.618 2.648   -6.629  1.00 43.83  ? 130 VAL C CB    1 
ATOM   5333 C CG1   . VAL C 1 158 ? -20.713 3.694   -6.751  1.00 41.07  ? 130 VAL C CG1   1 
ATOM   5334 C CG2   . VAL C 1 158 ? -19.056 2.315   -8.000  1.00 49.03  ? 130 VAL C CG2   1 
ATOM   5335 N N     . PHE C 1 159 ? -18.856 5.046   -4.227  1.00 50.86  ? 131 PHE C N     1 
ATOM   5336 C CA    . PHE C 1 159 ? -19.399 5.769   -3.086  1.00 44.82  ? 131 PHE C CA    1 
ATOM   5337 C C     . PHE C 1 159 ? -20.652 6.532   -3.496  1.00 46.68  ? 131 PHE C C     1 
ATOM   5338 O O     . PHE C 1 159 ? -20.724 7.090   -4.595  1.00 50.54  ? 131 PHE C O     1 
ATOM   5339 C CB    . PHE C 1 159 ? -18.366 6.732   -2.502  1.00 48.88  ? 131 PHE C CB    1 
ATOM   5340 C CG    . PHE C 1 159 ? -17.165 6.049   -1.914  1.00 46.45  ? 131 PHE C CG    1 
ATOM   5341 C CD1   . PHE C 1 159 ? -17.165 5.642   -0.590  1.00 50.44  ? 131 PHE C CD1   1 
ATOM   5342 C CD2   . PHE C 1 159 ? -16.038 5.812   -2.681  1.00 46.88  ? 131 PHE C CD2   1 
ATOM   5343 C CE1   . PHE C 1 159 ? -16.063 5.013   -0.042  1.00 47.73  ? 131 PHE C CE1   1 
ATOM   5344 C CE2   . PHE C 1 159 ? -14.933 5.183   -2.136  1.00 48.22  ? 131 PHE C CE2   1 
ATOM   5345 C CZ    . PHE C 1 159 ? -14.946 4.784   -0.817  1.00 45.88  ? 131 PHE C CZ    1 
ATOM   5346 N N     . CYS C 1 160 ? -21.636 6.554   -2.598  1.00 48.66  ? 132 CYS C N     1 
ATOM   5347 C CA    . CYS C 1 160 ? -22.928 7.193   -2.849  1.00 48.27  ? 132 CYS C CA    1 
ATOM   5348 C C     . CYS C 1 160 ? -23.387 7.826   -1.540  1.00 51.19  ? 132 CYS C C     1 
ATOM   5349 O O     . CYS C 1 160 ? -23.845 7.126   -0.631  1.00 53.91  ? 132 CYS C O     1 
ATOM   5350 C CB    . CYS C 1 160 ? -23.944 6.185   -3.371  1.00 43.90  ? 132 CYS C CB    1 
ATOM   5351 S SG    . CYS C 1 160 ? -25.657 6.683   -3.148  1.00 54.17  ? 132 CYS C SG    1 
ATOM   5352 N N     . MET C 1 161 ? -23.265 9.149   -1.445  1.00 50.28  ? 133 MET C N     1 
ATOM   5353 C CA    . MET C 1 161 ? -23.539 9.878   -0.213  1.00 49.99  ? 133 MET C CA    1 
ATOM   5354 C C     . MET C 1 161 ? -24.655 10.884  -0.446  1.00 53.91  ? 133 MET C C     1 
ATOM   5355 O O     . MET C 1 161 ? -24.503 11.804  -1.257  1.00 57.91  ? 133 MET C O     1 
ATOM   5356 C CB    . MET C 1 161 ? -22.282 10.589  0.295   1.00 53.89  ? 133 MET C CB    1 
ATOM   5357 C CG    . MET C 1 161 ? -20.978 9.899   -0.065  1.00 59.65  ? 133 MET C CG    1 
ATOM   5358 S SD    . MET C 1 161 ? -20.680 8.423   0.926   1.00 62.94  ? 133 MET C SD    1 
ATOM   5359 C CE    . MET C 1 161 ? -20.693 9.121   2.575   1.00 56.14  ? 133 MET C CE    1 
ATOM   5360 N N     . LEU C 1 162 ? -25.765 10.707  0.269   1.00 52.50  ? 134 LEU C N     1 
ATOM   5361 C CA    . LEU C 1 162 ? -26.856 11.681  0.341   1.00 50.75  ? 134 LEU C CA    1 
ATOM   5362 C C     . LEU C 1 162 ? -27.308 12.121  -1.054  1.00 50.67  ? 134 LEU C C     1 
ATOM   5363 O O     . LEU C 1 162 ? -27.130 13.265  -1.468  1.00 54.81  ? 134 LEU C O     1 
ATOM   5364 C CB    . LEU C 1 162 ? -26.436 12.891  1.183   1.00 49.55  ? 134 LEU C CB    1 
ATOM   5365 C CG    . LEU C 1 162 ? -25.697 12.600  2.490   1.00 46.27  ? 134 LEU C CG    1 
ATOM   5366 C CD1   . LEU C 1 162 ? -25.099 13.875  3.061   1.00 47.88  ? 134 LEU C CD1   1 
ATOM   5367 C CD2   . LEU C 1 162 ? -26.625 11.943  3.497   1.00 41.41  ? 134 LEU C CD2   1 
ATOM   5368 N N     . MET C 1 163 ? -27.921 11.177  -1.768  1.00 48.44  ? 135 MET C N     1 
ATOM   5369 C CA    . MET C 1 163 ? -28.359 11.474  -3.126  1.00 48.86  ? 135 MET C CA    1 
ATOM   5370 C C     . MET C 1 163 ? -29.479 10.540  -3.574  1.00 51.00  ? 135 MET C C     1 
ATOM   5371 O O     . MET C 1 163 ? -30.364 10.952  -4.331  1.00 55.24  ? 135 MET C O     1 
ATOM   5372 C CB    . MET C 1 163 ? -27.161 11.410  -4.079  1.00 49.52  ? 135 MET C CB    1 
ATOM   5373 C CG    . MET C 1 163 ? -27.478 11.108  -5.534  1.00 54.02  ? 135 MET C CG    1 
ATOM   5374 S SD    . MET C 1 163 ? -27.474 9.346   -5.889  1.00 51.79  ? 135 MET C SD    1 
ATOM   5375 C CE    . MET C 1 163 ? -25.722 9.007   -5.804  1.00 50.75  ? 135 MET C CE    1 
ATOM   5376 N N     . LEU C 1 164 ? -29.461 9.288   -3.107  1.00 46.22  ? 136 LEU C N     1 
ATOM   5377 C CA    . LEU C 1 164 ? -30.506 8.334   -3.473  1.00 47.54  ? 136 LEU C CA    1 
ATOM   5378 C C     . LEU C 1 164 ? -31.894 8.750   -3.001  1.00 48.78  ? 136 LEU C C     1 
ATOM   5379 O O     . LEU C 1 164 ? -32.882 8.161   -3.456  1.00 50.11  ? 136 LEU C O     1 
ATOM   5380 C CB    . LEU C 1 164 ? -30.171 6.940   -2.931  1.00 47.18  ? 136 LEU C CB    1 
ATOM   5381 C CG    . LEU C 1 164 ? -29.812 5.870   -3.972  1.00 47.43  ? 136 LEU C CG    1 
ATOM   5382 C CD1   . LEU C 1 164 ? -28.622 6.256   -4.820  1.00 46.53  ? 136 LEU C CD1   1 
ATOM   5383 C CD2   . LEU C 1 164 ? -29.567 4.532   -3.292  1.00 47.18  ? 136 LEU C CD2   1 
ATOM   5384 N N     . HIS C 1 165 ? -32.002 9.740   -2.116  1.00 48.46  ? 137 HIS C N     1 
ATOM   5385 C CA    . HIS C 1 165 ? -33.304 10.285  -1.758  1.00 49.72  ? 137 HIS C CA    1 
ATOM   5386 C C     . HIS C 1 165 ? -33.822 11.273  -2.798  1.00 50.62  ? 137 HIS C C     1 
ATOM   5387 O O     . HIS C 1 165 ? -34.995 11.658  -2.732  1.00 51.93  ? 137 HIS C O     1 
ATOM   5388 C CB    . HIS C 1 165 ? -33.219 10.949  -0.385  1.00 49.12  ? 137 HIS C CB    1 
ATOM   5389 C CG    . HIS C 1 165 ? -32.194 12.033  -0.303  1.00 49.41  ? 137 HIS C CG    1 
ATOM   5390 N ND1   . HIS C 1 165 ? -30.852 11.782  -0.116  1.00 53.05  ? 137 HIS C ND1   1 
ATOM   5391 C CD2   . HIS C 1 165 ? -32.325 13.380  -0.323  1.00 50.89  ? 137 HIS C CD2   1 
ATOM   5392 C CE1   . HIS C 1 165 ? -30.195 12.927  -0.069  1.00 59.85  ? 137 HIS C CE1   1 
ATOM   5393 N NE2   . HIS C 1 165 ? -31.066 13.912  -0.188  1.00 58.31  ? 137 HIS C NE2   1 
ATOM   5394 N N     . LEU C 1 166 ? -32.975 11.690  -3.744  1.00 50.02  ? 138 LEU C N     1 
ATOM   5395 C CA    . LEU C 1 166 ? -33.376 12.467  -4.914  1.00 50.92  ? 138 LEU C CA    1 
ATOM   5396 C C     . LEU C 1 166 ? -33.678 11.608  -6.135  1.00 51.84  ? 138 LEU C C     1 
ATOM   5397 O O     . LEU C 1 166 ? -34.138 12.144  -7.148  1.00 52.82  ? 138 LEU C O     1 
ATOM   5398 C CB    . LEU C 1 166 ? -32.288 13.491  -5.281  1.00 53.01  ? 138 LEU C CB    1 
ATOM   5399 C CG    . LEU C 1 166 ? -32.309 14.895  -4.662  1.00 57.16  ? 138 LEU C CG    1 
ATOM   5400 C CD1   . LEU C 1 166 ? -32.635 14.859  -3.195  1.00 57.19  ? 138 LEU C CD1   1 
ATOM   5401 C CD2   . LEU C 1 166 ? -30.950 15.550  -4.851  1.00 58.24  ? 138 LEU C CD2   1 
ATOM   5402 N N     . VAL C 1 167 ? -33.437 10.302  -6.068  1.00 51.63  ? 139 VAL C N     1 
ATOM   5403 C CA    . VAL C 1 167 ? -33.660 9.398   -7.191  1.00 52.52  ? 139 VAL C CA    1 
ATOM   5404 C C     . VAL C 1 167 ? -34.933 8.600   -6.899  1.00 53.96  ? 139 VAL C C     1 
ATOM   5405 O O     . VAL C 1 167 ? -34.907 7.722   -6.023  1.00 53.63  ? 139 VAL C O     1 
ATOM   5406 C CB    . VAL C 1 167 ? -32.462 8.467   -7.408  1.00 51.41  ? 139 VAL C CB    1 
ATOM   5407 C CG1   . VAL C 1 167 ? -32.506 7.874   -8.797  1.00 52.27  ? 139 VAL C CG1   1 
ATOM   5408 C CG2   . VAL C 1 167 ? -31.161 9.225   -7.180  1.00 49.78  ? 139 VAL C CG2   1 
ATOM   5409 N N     . PRO C 1 168 ? -36.048 8.880   -7.579  1.00 55.59  ? 140 PRO C N     1 
ATOM   5410 C CA    . PRO C 1 168 ? -37.271 8.098   -7.312  1.00 57.08  ? 140 PRO C CA    1 
ATOM   5411 C C     . PRO C 1 168 ? -37.099 6.609   -7.559  1.00 57.26  ? 140 PRO C C     1 
ATOM   5412 O O     . PRO C 1 168 ? -37.360 5.799   -6.660  1.00 57.30  ? 140 PRO C O     1 
ATOM   5413 C CB    . PRO C 1 168 ? -38.288 8.733   -8.270  1.00 58.77  ? 140 PRO C CB    1 
ATOM   5414 C CG    . PRO C 1 168 ? -37.809 10.142  -8.417  1.00 58.05  ? 140 PRO C CG    1 
ATOM   5415 C CD    . PRO C 1 168 ? -36.311 10.014  -8.479  1.00 56.24  ? 140 PRO C CD    1 
ATOM   5416 N N     . ASP C 1 169 ? -36.662 6.223   -8.756  1.00 57.44  ? 141 ASP C N     1 
ATOM   5417 C CA    . ASP C 1 169 ? -36.442 4.817   -9.090  1.00 57.69  ? 141 ASP C CA    1 
ATOM   5418 C C     . ASP C 1 169 ? -35.124 4.379   -8.466  1.00 55.86  ? 141 ASP C C     1 
ATOM   5419 O O     . ASP C 1 169 ? -34.050 4.523   -9.054  1.00 54.88  ? 141 ASP C O     1 
ATOM   5420 C CB    . ASP C 1 169 ? -36.445 4.613   -10.600 1.00 58.64  ? 141 ASP C CB    1 
ATOM   5421 N N     . ASN C 1 170 ? -35.209 3.832   -7.253  1.00 55.45  ? 142 ASN C N     1 
ATOM   5422 C CA    . ASN C 1 170 ? -34.012 3.418   -6.531  1.00 53.78  ? 142 ASN C CA    1 
ATOM   5423 C C     . ASN C 1 170 ? -33.478 2.076   -7.010  1.00 53.82  ? 142 ASN C C     1 
ATOM   5424 O O     . ASN C 1 170 ? -32.259 1.872   -7.027  1.00 57.07  ? 142 ASN C O     1 
ATOM   5425 C CB    . ASN C 1 170 ? -34.304 3.364   -5.032  1.00 53.41  ? 142 ASN C CB    1 
ATOM   5426 C CG    . ASN C 1 170 ? -34.053 4.686   -4.347  1.00 55.36  ? 142 ASN C CG    1 
ATOM   5427 O OD1   . ASN C 1 170 ? -34.954 5.509   -4.213  1.00 65.28  ? 142 ASN C OD1   1 
ATOM   5428 N ND2   . ASN C 1 170 ? -32.828 4.888   -3.890  1.00 50.83  ? 142 ASN C ND2   1 
ATOM   5429 N N     . ARG C 1 171 ? -34.360 1.151   -7.396  1.00 56.12  ? 143 ARG C N     1 
ATOM   5430 C CA    . ARG C 1 171 ? -33.893 -0.141  -7.886  1.00 56.31  ? 143 ARG C CA    1 
ATOM   5431 C C     . ARG C 1 171 ? -33.173 -0.004  -9.221  1.00 56.19  ? 143 ARG C C     1 
ATOM   5432 O O     . ARG C 1 171 ? -32.241 -0.766  -9.503  1.00 55.60  ? 143 ARG C O     1 
ATOM   5433 C CB    . ARG C 1 171 ? -35.067 -1.115  -7.993  1.00 58.15  ? 143 ARG C CB    1 
ATOM   5434 C CG    . ARG C 1 171 ? -34.695 -2.488  -8.529  1.00 59.31  ? 143 ARG C CG    1 
ATOM   5435 C CD    . ARG C 1 171 ? -35.566 -3.576  -7.923  1.00 59.79  ? 143 ARG C CD    1 
ATOM   5436 N NE    . ARG C 1 171 ? -36.828 -3.055  -7.412  1.00 63.55  ? 143 ARG C NE    1 
ATOM   5437 C CZ    . ARG C 1 171 ? -37.426 -3.491  -6.312  1.00 70.53  ? 143 ARG C CZ    1 
ATOM   5438 N NH1   . ARG C 1 171 ? -36.897 -4.453  -5.573  1.00 70.41  ? 143 ARG C NH1   1 
ATOM   5439 N NH2   . ARG C 1 171 ? -38.580 -2.945  -5.939  1.00 65.80  ? 143 ARG C NH2   1 
ATOM   5440 N N     . LEU C 1 172 ? -33.579 0.962   -10.048 1.00 56.19  ? 144 LEU C N     1 
ATOM   5441 C CA    . LEU C 1 172 ? -32.859 1.217   -11.292 1.00 55.87  ? 144 LEU C CA    1 
ATOM   5442 C C     . LEU C 1 172 ? -31.464 1.765   -11.015 1.00 53.96  ? 144 LEU C C     1 
ATOM   5443 O O     . LEU C 1 172 ? -30.498 1.389   -11.689 1.00 53.47  ? 144 LEU C O     1 
ATOM   5444 C CB    . LEU C 1 172 ? -33.653 2.184   -12.169 1.00 57.01  ? 144 LEU C CB    1 
ATOM   5445 C CG    . LEU C 1 172 ? -32.984 2.663   -13.461 1.00 56.95  ? 144 LEU C CG    1 
ATOM   5446 C CD1   . LEU C 1 172 ? -32.483 1.488   -14.292 1.00 57.36  ? 144 LEU C CD1   1 
ATOM   5447 C CD2   . LEU C 1 172 ? -33.932 3.535   -14.270 1.00 58.32  ? 144 LEU C CD2   1 
ATOM   5448 N N     . ALA C 1 173 ? -31.339 2.651   -10.024 1.00 52.93  ? 145 ALA C N     1 
ATOM   5449 C CA    . ALA C 1 173 ? -30.033 3.208   -9.692  1.00 51.18  ? 145 ALA C CA    1 
ATOM   5450 C C     . ALA C 1 173 ? -29.116 2.162   -9.071  1.00 50.20  ? 145 ALA C C     1 
ATOM   5451 O O     . ALA C 1 173 ? -27.901 2.199   -9.290  1.00 49.10  ? 145 ALA C O     1 
ATOM   5452 C CB    . ALA C 1 173 ? -30.193 4.401   -8.751  1.00 50.49  ? 145 ALA C CB    1 
ATOM   5453 N N     . VAL C 1 174 ? -29.673 1.228   -8.297  1.00 50.64  ? 146 VAL C N     1 
ATOM   5454 C CA    . VAL C 1 174 ? -28.860 0.156   -7.732  1.00 49.88  ? 146 VAL C CA    1 
ATOM   5455 C C     . VAL C 1 174 ? -28.381 -0.783  -8.833  1.00 50.37  ? 146 VAL C C     1 
ATOM   5456 O O     . VAL C 1 174 ? -27.233 -1.242  -8.821  1.00 49.42  ? 146 VAL C O     1 
ATOM   5457 C CB    . VAL C 1 174 ? -29.648 -0.595  -6.643  1.00 50.39  ? 146 VAL C CB    1 
ATOM   5458 C CG1   . VAL C 1 174 ? -28.918 -1.863  -6.228  1.00 49.93  ? 146 VAL C CG1   1 
ATOM   5459 C CG2   . VAL C 1 174 ? -29.879 0.306   -5.440  1.00 49.69  ? 146 VAL C CG2   1 
ATOM   5460 N N     . LYS C 1 175 ? -29.248 -1.074  -9.806  1.00 51.93  ? 147 LYS C N     1 
ATOM   5461 C CA    . LYS C 1 175 ? -28.855 -1.938  -10.915 1.00 52.58  ? 147 LYS C CA    1 
ATOM   5462 C C     . LYS C 1 175 ? -27.751 -1.298  -11.748 1.00 51.73  ? 147 LYS C C     1 
ATOM   5463 O O     . LYS C 1 175 ? -26.854 -1.992  -12.241 1.00 51.47  ? 147 LYS C O     1 
ATOM   5464 C CB    . LYS C 1 175 ? -30.069 -2.258  -11.788 1.00 54.54  ? 147 LYS C CB    1 
ATOM   5465 N N     . ASN C 1 176 ? -27.799 0.026   -11.916 1.00 51.35  ? 148 ASN C N     1 
ATOM   5466 C CA    . ASN C 1 176 ? -26.739 0.717   -12.644 1.00 50.54  ? 148 ASN C CA    1 
ATOM   5467 C C     . ASN C 1 176 ? -25.435 0.712   -11.855 1.00 48.81  ? 148 ASN C C     1 
ATOM   5468 O O     . ASN C 1 176 ? -24.352 0.588   -12.437 1.00 48.25  ? 148 ASN C O     1 
ATOM   5469 C CB    . ASN C 1 176 ? -27.169 2.147   -12.969 1.00 50.66  ? 148 ASN C CB    1 
ATOM   5470 C CG    . ASN C 1 176 ? -28.030 2.226   -14.214 1.00 52.32  ? 148 ASN C CG    1 
ATOM   5471 O OD1   . ASN C 1 176 ? -28.114 1.269   -14.986 1.00 53.28  ? 148 ASN C OD1   1 
ATOM   5472 N ND2   . ASN C 1 176 ? -28.671 3.370   -14.421 1.00 52.74  ? 148 ASN C ND2   1 
ATOM   5473 N N     . ILE C 1 177 ? -25.519 0.852   -10.530 1.00 48.02  ? 149 ILE C N     1 
ATOM   5474 C CA    . ILE C 1 177 ? -24.324 0.741   -9.699  1.00 46.50  ? 149 ILE C CA    1 
ATOM   5475 C C     . ILE C 1 177 ? -23.771 -0.677  -9.758  1.00 46.57  ? 149 ILE C C     1 
ATOM   5476 O O     . ILE C 1 177 ? -22.550 -0.880  -9.735  1.00 45.79  ? 149 ILE C O     1 
ATOM   5477 C CB    . ILE C 1 177 ? -24.642 1.177   -8.256  1.00 45.82  ? 149 ILE C CB    1 
ATOM   5478 C CG1   . ILE C 1 177 ? -24.875 2.688   -8.194  1.00 45.51  ? 149 ILE C CG1   1 
ATOM   5479 C CG2   . ILE C 1 177 ? -23.522 0.783   -7.307  1.00 44.47  ? 149 ILE C CG2   1 
ATOM   5480 C CD1   . ILE C 1 177 ? -25.424 3.169   -6.870  1.00 45.18  ? 149 ILE C CD1   1 
ATOM   5481 N N     . HIS C 1 178 ? -24.651 -1.677  -9.856  1.00 48.99  ? 150 HIS C N     1 
ATOM   5482 C CA    . HIS C 1 178 ? -24.200 -3.059  -9.979  1.00 51.05  ? 150 HIS C CA    1 
ATOM   5483 C C     . HIS C 1 178 ? -23.460 -3.285  -11.292 1.00 50.35  ? 150 HIS C C     1 
ATOM   5484 O O     . HIS C 1 178 ? -22.493 -4.054  -11.341 1.00 50.66  ? 150 HIS C O     1 
ATOM   5485 C CB    . HIS C 1 178 ? -25.395 -4.006  -9.859  1.00 54.74  ? 150 HIS C CB    1 
ATOM   5486 C CG    . HIS C 1 178 ? -25.025 -5.456  -9.878  1.00 59.81  ? 150 HIS C CG    1 
ATOM   5487 N ND1   . HIS C 1 178 ? -24.941 -6.188  -11.043 1.00 65.64  ? 150 HIS C ND1   1 
ATOM   5488 C CD2   . HIS C 1 178 ? -24.718 -6.311  -8.874  1.00 61.01  ? 150 HIS C CD2   1 
ATOM   5489 C CE1   . HIS C 1 178 ? -24.599 -7.431  -10.756 1.00 65.11  ? 150 HIS C CE1   1 
ATOM   5490 N NE2   . HIS C 1 178 ? -24.457 -7.532  -9.447  1.00 66.56  ? 150 HIS C NE2   1 
ATOM   5491 N N     . LYS C 1 179 ? -23.899 -2.624  -12.368 1.00 49.13  ? 151 LYS C N     1 
ATOM   5492 C CA    . LYS C 1 179 ? -23.194 -2.729  -13.642 1.00 49.43  ? 151 LYS C CA    1 
ATOM   5493 C C     . LYS C 1 179 ? -21.789 -2.148  -13.543 1.00 47.93  ? 151 LYS C C     1 
ATOM   5494 O O     . LYS C 1 179 ? -20.837 -2.701  -14.105 1.00 52.33  ? 151 LYS C O     1 
ATOM   5495 C CB    . LYS C 1 179 ? -23.976 -2.010  -14.742 1.00 50.55  ? 151 LYS C CB    1 
ATOM   5496 C CG    . LYS C 1 179 ? -25.270 -2.677  -15.170 1.00 52.33  ? 151 LYS C CG    1 
ATOM   5497 C CD    . LYS C 1 179 ? -25.937 -1.859  -16.267 1.00 53.39  ? 151 LYS C CD    1 
ATOM   5498 C CE    . LYS C 1 179 ? -27.251 -2.471  -16.715 1.00 56.15  ? 151 LYS C CE    1 
ATOM   5499 N NZ    . LYS C 1 179 ? -27.908 -1.641  -17.764 1.00 60.27  ? 151 LYS C NZ    1 
ATOM   5500 N N     . LEU C 1 180 ? -21.643 -1.030  -12.831 1.00 46.86  ? 152 LEU C N     1 
ATOM   5501 C CA    . LEU C 1 180 ? -20.382 -0.302  -12.792 1.00 45.55  ? 152 LEU C CA    1 
ATOM   5502 C C     . LEU C 1 180 ? -19.330 -0.975  -11.922 1.00 48.35  ? 152 LEU C C     1 
ATOM   5503 O O     . LEU C 1 180 ? -18.145 -0.644  -12.041 1.00 48.78  ? 152 LEU C O     1 
ATOM   5504 C CB    . LEU C 1 180 ? -20.628 1.123   -12.292 1.00 44.89  ? 152 LEU C CB    1 
ATOM   5505 C CG    . LEU C 1 180 ? -21.322 2.060   -13.282 1.00 45.76  ? 152 LEU C CG    1 
ATOM   5506 C CD1   . LEU C 1 180 ? -21.896 3.271   -12.568 1.00 45.38  ? 152 LEU C CD1   1 
ATOM   5507 C CD2   . LEU C 1 180 ? -20.358 2.488   -14.376 1.00 45.60  ? 152 LEU C CD2   1 
ATOM   5508 N N     . LEU C 1 181 ? -19.726 -1.903  -11.058 1.00 52.36  ? 153 LEU C N     1 
ATOM   5509 C CA    . LEU C 1 181 ? -18.799 -2.539  -10.135 1.00 54.36  ? 153 LEU C CA    1 
ATOM   5510 C C     . LEU C 1 181 ? -18.217 -3.816  -10.728 1.00 58.54  ? 153 LEU C C     1 
ATOM   5511 O O     . LEU C 1 181 ? -18.870 -4.526  -11.498 1.00 56.04  ? 153 LEU C O     1 
ATOM   5512 C CB    . LEU C 1 181 ? -19.490 -2.857  -8.809  1.00 51.64  ? 153 LEU C CB    1 
ATOM   5513 C CG    . LEU C 1 181 ? -19.763 -1.672  -7.885  1.00 47.00  ? 153 LEU C CG    1 
ATOM   5514 C CD1   . LEU C 1 181 ? -20.744 -2.060  -6.792  1.00 54.71  ? 153 LEU C CD1   1 
ATOM   5515 C CD2   . LEU C 1 181 ? -18.460 -1.177  -7.283  1.00 55.72  ? 153 LEU C CD2   1 
ATOM   5516 N N     . VAL C 1 182 ? -16.972 -4.098  -10.358 1.00 59.91  ? 154 VAL C N     1 
ATOM   5517 C CA    . VAL C 1 182 ? -16.329 -5.365  -10.692 1.00 59.77  ? 154 VAL C CA    1 
ATOM   5518 C C     . VAL C 1 182 ? -16.882 -6.426  -9.749  1.00 66.12  ? 154 VAL C C     1 
ATOM   5519 O O     . VAL C 1 182 ? -17.288 -6.097  -8.624  1.00 69.76  ? 154 VAL C O     1 
ATOM   5520 C CB    . VAL C 1 182 ? -14.798 -5.266  -10.588 1.00 53.14  ? 154 VAL C CB    1 
ATOM   5521 C CG1   . VAL C 1 182 ? -14.264 -4.233  -11.561 1.00 50.75  ? 154 VAL C CG1   1 
ATOM   5522 C CG2   . VAL C 1 182 ? -14.379 -4.922  -9.167  1.00 55.26  ? 154 VAL C CG2   1 
ATOM   5523 N N     . PRO C 1 183 ? -16.952 -7.691  -10.163 1.00 69.17  ? 155 PRO C N     1 
ATOM   5524 C CA    . PRO C 1 183 ? -17.352 -8.753  -9.228  1.00 73.00  ? 155 PRO C CA    1 
ATOM   5525 C C     . PRO C 1 183 ? -16.408 -8.804  -8.037  1.00 75.34  ? 155 PRO C C     1 
ATOM   5526 O O     . PRO C 1 183 ? -15.212 -9.069  -8.178  1.00 74.47  ? 155 PRO C O     1 
ATOM   5527 C CB    . PRO C 1 183 ? -17.267 -10.022 -10.082 1.00 77.02  ? 155 PRO C CB    1 
ATOM   5528 C CG    . PRO C 1 183 ? -17.505 -9.541  -11.473 1.00 77.48  ? 155 PRO C CG    1 
ATOM   5529 C CD    . PRO C 1 183 ? -16.858 -8.182  -11.548 1.00 71.19  ? 155 PRO C CD    1 
ATOM   5530 N N     . GLY C 1 184 ? -16.957 -8.540  -6.854  1.00 78.61  ? 156 GLY C N     1 
ATOM   5531 C CA    . GLY C 1 184 ? -16.171 -8.392  -5.650  1.00 75.14  ? 156 GLY C CA    1 
ATOM   5532 C C     . GLY C 1 184 ? -15.992 -6.961  -5.194  1.00 70.83  ? 156 GLY C C     1 
ATOM   5533 O O     . GLY C 1 184 ? -15.484 -6.738  -4.088  1.00 72.90  ? 156 GLY C O     1 
ATOM   5534 N N     . GLY C 1 185 ? -16.387 -5.990  -6.012  1.00 67.82  ? 157 GLY C N     1 
ATOM   5535 C CA    . GLY C 1 185 ? -16.329 -4.603  -5.608  1.00 65.33  ? 157 GLY C CA    1 
ATOM   5536 C C     . GLY C 1 185 ? -17.358 -4.279  -4.543  1.00 69.16  ? 157 GLY C C     1 
ATOM   5537 O O     . GLY C 1 185 ? -18.302 -5.028  -4.288  1.00 70.20  ? 157 GLY C O     1 
ATOM   5538 N N     . GLU C 1 186 ? -17.170 -3.125  -3.910  1.00 67.50  ? 158 GLU C N     1 
ATOM   5539 C CA    . GLU C 1 186 ? -17.988 -2.716  -2.780  1.00 67.28  ? 158 GLU C CA    1 
ATOM   5540 C C     . GLU C 1 186 ? -18.626 -1.359  -3.046  1.00 63.88  ? 158 GLU C C     1 
ATOM   5541 O O     . GLU C 1 186 ? -18.037 -0.492  -3.697  1.00 59.90  ? 158 GLU C O     1 
ATOM   5542 C CB    . GLU C 1 186 ? -17.155 -2.663  -1.495  1.00 67.51  ? 158 GLU C CB    1 
ATOM   5543 C CG    . GLU C 1 186 ? -16.490 -3.986  -1.149  1.00 69.89  ? 158 GLU C CG    1 
ATOM   5544 C CD    . GLU C 1 186 ? -15.414 -3.843  -0.092  1.00 79.71  ? 158 GLU C CD    1 
ATOM   5545 O OE1   . GLU C 1 186 ? -14.661 -2.848  -0.139  1.00 79.84  ? 158 GLU C OE1   1 
ATOM   5546 O OE2   . GLU C 1 186 ? -15.319 -4.727  0.786   1.00 84.01  ? 158 GLU C OE2   1 
ATOM   5547 N N     . ALA C 1 187 ? -19.841 -1.186  -2.530  1.00 64.85  ? 159 ALA C N     1 
ATOM   5548 C CA    . ALA C 1 187 ? -20.600 0.048   -2.677  1.00 55.93  ? 159 ALA C CA    1 
ATOM   5549 C C     . ALA C 1 187 ? -20.936 0.596   -1.298  1.00 55.89  ? 159 ALA C C     1 
ATOM   5550 O O     . ALA C 1 187 ? -21.481 -0.125  -0.456  1.00 54.17  ? 159 ALA C O     1 
ATOM   5551 C CB    . ALA C 1 187 ? -21.879 -0.184  -3.486  1.00 52.61  ? 159 ALA C CB    1 
ATOM   5552 N N     . VAL C 1 188 ? -20.612 1.865   -1.073  1.00 53.80  ? 160 VAL C N     1 
ATOM   5553 C CA    . VAL C 1 188 ? -20.839 2.530   0.205   1.00 46.69  ? 160 VAL C CA    1 
ATOM   5554 C C     . VAL C 1 188 ? -21.992 3.506   0.018   1.00 46.39  ? 160 VAL C C     1 
ATOM   5555 O O     . VAL C 1 188 ? -21.848 4.531   -0.660  1.00 53.28  ? 160 VAL C O     1 
ATOM   5556 C CB    . VAL C 1 188 ? -19.579 3.247   0.706   1.00 42.84  ? 160 VAL C CB    1 
ATOM   5557 C CG1   . VAL C 1 188 ? -19.890 4.053   1.958   1.00 46.87  ? 160 VAL C CG1   1 
ATOM   5558 C CG2   . VAL C 1 188 ? -18.469 2.242   0.972   1.00 42.60  ? 160 VAL C CG2   1 
ATOM   5559 N N     . PHE C 1 189 ? -23.137 3.193   0.616   1.00 47.58  ? 161 PHE C N     1 
ATOM   5560 C CA    . PHE C 1 189 ? -24.323 4.028   0.511   1.00 48.67  ? 161 PHE C CA    1 
ATOM   5561 C C     . PHE C 1 189 ? -24.452 4.944   1.722   1.00 49.70  ? 161 PHE C C     1 
ATOM   5562 O O     . PHE C 1 189 ? -23.965 4.641   2.814   1.00 47.85  ? 161 PHE C O     1 
ATOM   5563 C CB    . PHE C 1 189 ? -25.586 3.175   0.375   1.00 49.20  ? 161 PHE C CB    1 
ATOM   5564 C CG    . PHE C 1 189 ? -25.646 2.379   -0.895  1.00 48.92  ? 161 PHE C CG    1 
ATOM   5565 C CD1   . PHE C 1 189 ? -25.100 1.108   -0.961  1.00 52.78  ? 161 PHE C CD1   1 
ATOM   5566 C CD2   . PHE C 1 189 ? -26.248 2.904   -2.026  1.00 48.04  ? 161 PHE C CD2   1 
ATOM   5567 C CE1   . PHE C 1 189 ? -25.157 0.376   -2.130  1.00 53.31  ? 161 PHE C CE1   1 
ATOM   5568 C CE2   . PHE C 1 189 ? -26.306 2.178   -3.198  1.00 47.71  ? 161 PHE C CE2   1 
ATOM   5569 C CZ    . PHE C 1 189 ? -25.760 0.912   -3.250  1.00 49.52  ? 161 PHE C CZ    1 
ATOM   5570 N N     . SER C 1 190 ? -25.121 6.082   1.507   1.00 50.98  ? 162 SER C N     1 
ATOM   5571 C CA    . SER C 1 190 ? -25.460 7.036   2.561   1.00 48.00  ? 162 SER C CA    1 
ATOM   5572 C C     . SER C 1 190 ? -26.804 7.652   2.166   1.00 48.15  ? 162 SER C C     1 
ATOM   5573 O O     . SER C 1 190 ? -26.894 8.792   1.704   1.00 51.64  ? 162 SER C O     1 
ATOM   5574 C CB    . SER C 1 190 ? -24.380 8.099   2.753   1.00 51.04  ? 162 SER C CB    1 
ATOM   5575 O OG    . SER C 1 190 ? -24.688 8.953   3.840   1.00 54.55  ? 162 SER C OG    1 
ATOM   5576 N N     . VAL C 1 191 ? -27.859 6.871   2.336   1.00 44.68  ? 163 VAL C N     1 
ATOM   5577 C CA    . VAL C 1 191 ? -29.203 7.259   1.925   1.00 44.57  ? 163 VAL C CA    1 
ATOM   5578 C C     . VAL C 1 191 ? -29.915 7.908   3.100   1.00 46.37  ? 163 VAL C C     1 
ATOM   5579 O O     . VAL C 1 191 ? -29.790 7.461   4.247   1.00 47.34  ? 163 VAL C O     1 
ATOM   5580 C CB    . VAL C 1 191 ? -29.985 6.037   1.406   1.00 45.65  ? 163 VAL C CB    1 
ATOM   5581 C CG1   . VAL C 1 191 ? -31.342 6.459   0.867   1.00 47.15  ? 163 VAL C CG1   1 
ATOM   5582 C CG2   . VAL C 1 191 ? -29.177 5.306   0.343   1.00 45.29  ? 163 VAL C CG2   1 
ATOM   5583 N N     . ILE C 1 192 ? -30.661 8.971   2.818   1.00 47.12  ? 164 ILE C N     1 
ATOM   5584 C CA    . ILE C 1 192 ? -31.485 9.632   3.822   1.00 48.84  ? 164 ILE C CA    1 
ATOM   5585 C C     . ILE C 1 192 ? -32.837 8.927   3.848   1.00 52.50  ? 164 ILE C C     1 
ATOM   5586 O O     . ILE C 1 192 ? -33.597 8.983   2.878   1.00 55.64  ? 164 ILE C O     1 
ATOM   5587 C CB    . ILE C 1 192 ? -31.642 11.129  3.533   1.00 46.34  ? 164 ILE C CB    1 
ATOM   5588 C CG1   . ILE C 1 192 ? -30.302 11.847  3.701   1.00 45.86  ? 164 ILE C CG1   1 
ATOM   5589 C CG2   . ILE C 1 192 ? -32.690 11.733  4.450   1.00 50.71  ? 164 ILE C CG2   1 
ATOM   5590 C CD1   . ILE C 1 192 ? -30.340 13.310  3.322   1.00 47.00  ? 164 ILE C CD1   1 
ATOM   5591 N N     . ALA C 1 193 ? -33.133 8.253   4.962   1.00 53.69  ? 165 ALA C N     1 
ATOM   5592 C CA    . ALA C 1 193 ? -34.394 7.531   5.082   1.00 57.54  ? 165 ALA C CA    1 
ATOM   5593 C C     . ALA C 1 193 ? -35.575 8.493   5.104   1.00 61.97  ? 165 ALA C C     1 
ATOM   5594 O O     . ALA C 1 193 ? -36.432 8.466   4.214   1.00 68.50  ? 165 ALA C O     1 
ATOM   5595 C CB    . ALA C 1 193 ? -34.382 6.660   6.340   1.00 65.16  ? 165 ALA C CB    1 
ATOM   5596 N N     . ASN C 1 194 ? -35.633 9.356   6.115   1.00 65.90  ? 166 ASN C N     1 
ATOM   5597 C CA    . ASN C 1 194 ? -36.715 10.319  6.248   1.00 65.87  ? 166 ASN C CA    1 
ATOM   5598 C C     . ASN C 1 194 ? -36.172 11.616  6.828   1.00 64.66  ? 166 ASN C C     1 
ATOM   5599 O O     . ASN C 1 194 ? -35.204 11.616  7.592   1.00 62.16  ? 166 ASN C O     1 
ATOM   5600 C CB    . ASN C 1 194 ? -37.849 9.773   7.130   1.00 64.82  ? 166 ASN C CB    1 
ATOM   5601 C CG    . ASN C 1 194 ? -37.432 9.601   8.580   1.00 69.38  ? 166 ASN C CG    1 
ATOM   5602 O OD1   . ASN C 1 194 ? -37.391 10.563  9.347   1.00 76.39  ? 166 ASN C OD1   1 
ATOM   5603 N ND2   . ASN C 1 194 ? -37.118 8.368   8.960   1.00 68.30  ? 166 ASN C ND2   1 
ATOM   5604 N N     . MET C 1 195 ? -36.807 12.723  6.453   1.00 61.54  ? 167 MET C N     1 
ATOM   5605 C CA    . MET C 1 195 ? -36.436 14.028  6.980   1.00 63.71  ? 167 MET C CA    1 
ATOM   5606 C C     . MET C 1 195 ? -37.642 14.948  6.874   1.00 64.65  ? 167 MET C C     1 
ATOM   5607 O O     . MET C 1 195 ? -38.557 14.709  6.083   1.00 68.62  ? 167 MET C O     1 
ATOM   5608 C CB    . MET C 1 195 ? -35.233 14.617  6.237   1.00 63.12  ? 167 MET C CB    1 
ATOM   5609 C CG    . MET C 1 195 ? -35.314 14.507  4.723   1.00 67.96  ? 167 MET C CG    1 
ATOM   5610 S SD    . MET C 1 195 ? -33.782 15.032  3.931   1.00 71.44  ? 167 MET C SD    1 
ATOM   5611 C CE    . MET C 1 195 ? -33.329 16.416  4.970   1.00 60.80  ? 167 MET C CE    1 
ATOM   5612 N N     . ALA C 1 196 ? -37.629 16.008  7.683   1.00 62.48  ? 168 ALA C N     1 
ATOM   5613 C CA    . ALA C 1 196 ? -38.757 16.930  7.714   1.00 65.64  ? 168 ALA C CA    1 
ATOM   5614 C C     . ALA C 1 196 ? -38.815 17.844  6.497   1.00 66.61  ? 168 ALA C C     1 
ATOM   5615 O O     . ALA C 1 196 ? -39.847 18.488  6.281   1.00 68.31  ? 168 ALA C O     1 
ATOM   5616 C CB    . ALA C 1 196 ? -38.716 17.771  8.989   1.00 75.11  ? 168 ALA C CB    1 
ATOM   5617 N N     . LEU C 1 197 ? -37.741 17.925  5.705   1.00 69.53  ? 169 LEU C N     1 
ATOM   5618 C CA    . LEU C 1 197 ? -37.823 18.661  4.447   1.00 73.47  ? 169 LEU C CA    1 
ATOM   5619 C C     . LEU C 1 197 ? -38.832 18.022  3.505   1.00 72.19  ? 169 LEU C C     1 
ATOM   5620 O O     . LEU C 1 197 ? -39.422 18.708  2.663   1.00 66.04  ? 169 LEU C O     1 
ATOM   5621 C CB    . LEU C 1 197 ? -36.452 18.730  3.766   1.00 75.55  ? 169 LEU C CB    1 
ATOM   5622 C CG    . LEU C 1 197 ? -35.276 19.463  4.418   1.00 66.93  ? 169 LEU C CG    1 
ATOM   5623 C CD1   . LEU C 1 197 ? -34.087 19.501  3.466   1.00 65.05  ? 169 LEU C CD1   1 
ATOM   5624 C CD2   . LEU C 1 197 ? -35.643 20.860  4.854   1.00 68.42  ? 169 LEU C CD2   1 
ATOM   5625 N N     . CYS C 1 198 ? -39.043 16.710  3.634   1.00 78.11  ? 170 CYS C N     1 
ATOM   5626 C CA    . CYS C 1 198 ? -39.964 16.000  2.756   1.00 74.95  ? 170 CYS C CA    1 
ATOM   5627 C C     . CYS C 1 198 ? -41.406 16.127  3.232   1.00 78.70  ? 170 CYS C C     1 
ATOM   5628 O O     . CYS C 1 198 ? -42.321 16.264  2.413   1.00 81.82  ? 170 CYS C O     1 
ATOM   5629 C CB    . CYS C 1 198 ? -39.561 14.529  2.660   1.00 75.35  ? 170 CYS C CB    1 
ATOM   5630 S SG    . CYS C 1 198 ? -38.053 14.233  1.706   1.00 72.15  ? 170 CYS C SG    1 
ATOM   5631 N N     . ASP C 1 199 ? -41.632 16.075  4.549   1.00 81.57  ? 171 ASP C N     1 
ATOM   5632 C CA    . ASP C 1 199 ? -42.980 16.280  5.070   1.00 76.96  ? 171 ASP C CA    1 
ATOM   5633 C C     . ASP C 1 199 ? -43.460 17.701  4.803   1.00 74.99  ? 171 ASP C C     1 
ATOM   5634 O O     . ASP C 1 199 ? -44.648 17.923  4.546   1.00 76.94  ? 171 ASP C O     1 
ATOM   5635 C CB    . ASP C 1 199 ? -43.025 15.970  6.566   1.00 71.27  ? 171 ASP C CB    1 
ATOM   5636 C CG    . ASP C 1 199 ? -42.810 14.500  6.865   1.00 74.14  ? 171 ASP C CG    1 
ATOM   5637 O OD1   . ASP C 1 199 ? -43.281 13.657  6.073   1.00 82.66  ? 171 ASP C OD1   1 
ATOM   5638 O OD2   . ASP C 1 199 ? -42.175 14.187  7.894   1.00 68.07  ? 171 ASP C OD2   1 
ATOM   5639 N N     . ALA C 1 200 ? -42.550 18.677  4.860   1.00 78.64  ? 172 ALA C N     1 
ATOM   5640 C CA    . ALA C 1 200 ? -42.914 20.044  4.506   1.00 79.48  ? 172 ALA C CA    1 
ATOM   5641 C C     . ALA C 1 200 ? -43.286 20.153  3.034   1.00 79.48  ? 172 ALA C C     1 
ATOM   5642 O O     . ALA C 1 200 ? -44.126 20.981  2.665   1.00 79.34  ? 172 ALA C O     1 
ATOM   5643 C CB    . ALA C 1 200 ? -41.769 21.000  4.841   1.00 82.83  ? 172 ALA C CB    1 
ATOM   5644 N N     . TYR C 1 201 ? -42.672 19.330  2.181   1.00 81.85  ? 173 TYR C N     1 
ATOM   5645 C CA    . TYR C 1 201 ? -43.062 19.288  0.776   1.00 80.53  ? 173 TYR C CA    1 
ATOM   5646 C C     . TYR C 1 201 ? -44.492 18.784  0.627   1.00 82.76  ? 173 TYR C C     1 
ATOM   5647 O O     . TYR C 1 201 ? -45.315 19.402  -0.057  1.00 86.46  ? 173 TYR C O     1 
ATOM   5648 C CB    . TYR C 1 201 ? -42.100 18.395  -0.009  1.00 79.91  ? 173 TYR C CB    1 
ATOM   5649 C CG    . TYR C 1 201 ? -40.814 19.064  -0.440  1.00 73.75  ? 173 TYR C CG    1 
ATOM   5650 C CD1   . TYR C 1 201 ? -40.729 20.444  -0.565  1.00 69.82  ? 173 TYR C CD1   1 
ATOM   5651 C CD2   . TYR C 1 201 ? -39.683 18.309  -0.724  1.00 73.92  ? 173 TYR C CD2   1 
ATOM   5652 C CE1   . TYR C 1 201 ? -39.551 21.054  -0.960  1.00 71.33  ? 173 TYR C CE1   1 
ATOM   5653 C CE2   . TYR C 1 201 ? -38.504 18.908  -1.119  1.00 72.75  ? 173 TYR C CE2   1 
ATOM   5654 C CZ    . TYR C 1 201 ? -38.443 20.280  -1.236  1.00 70.56  ? 173 TYR C CZ    1 
ATOM   5655 O OH    . TYR C 1 201 ? -37.268 20.877  -1.629  1.00 67.42  ? 173 TYR C OH    1 
ATOM   5656 N N     . GLU C 1 202 ? -44.806 17.659  1.275   1.00 83.43  ? 174 GLU C N     1 
ATOM   5657 C CA    . GLU C 1 202 ? -46.121 17.048  1.118   1.00 86.81  ? 174 GLU C CA    1 
ATOM   5658 C C     . GLU C 1 202 ? -47.226 17.918  1.704   1.00 87.23  ? 174 GLU C C     1 
ATOM   5659 O O     . GLU C 1 202 ? -48.374 17.843  1.251   1.00 85.79  ? 174 GLU C O     1 
ATOM   5660 C CB    . GLU C 1 202 ? -46.130 15.663  1.764   1.00 87.99  ? 174 GLU C CB    1 
ATOM   5661 C CG    . GLU C 1 202 ? -45.286 14.635  1.026   1.00 85.54  ? 174 GLU C CG    1 
ATOM   5662 C CD    . GLU C 1 202 ? -45.092 13.356  1.819   1.00 87.59  ? 174 GLU C CD    1 
ATOM   5663 O OE1   . GLU C 1 202 ? -44.996 13.434  3.062   1.00 83.75  ? 174 GLU C OE1   1 
ATOM   5664 O OE2   . GLU C 1 202 ? -45.032 12.274  1.198   1.00 90.24  ? 174 GLU C OE2   1 
ATOM   5665 N N     . GLU C 1 203 ? -46.908 18.743  2.703   1.00 86.46  ? 175 GLU C N     1 
ATOM   5666 C CA    . GLU C 1 203 ? -47.911 19.651  3.249   1.00 86.59  ? 175 GLU C CA    1 
ATOM   5667 C C     . GLU C 1 203 ? -48.128 20.852  2.335   1.00 87.47  ? 175 GLU C C     1 
ATOM   5668 O O     . GLU C 1 203 ? -49.253 21.349  2.217   1.00 93.34  ? 175 GLU C O     1 
ATOM   5669 C CB    . GLU C 1 203 ? -47.506 20.109  4.651   1.00 90.27  ? 175 GLU C CB    1 
ATOM   5670 C CG    . GLU C 1 203 ? -47.556 19.009  5.703   1.00 89.79  ? 175 GLU C CG    1 
ATOM   5671 C CD    . GLU C 1 203 ? -47.410 19.542  7.117   1.00 96.11  ? 175 GLU C CD    1 
ATOM   5672 O OE1   . GLU C 1 203 ? -47.316 20.776  7.285   1.00 98.12  ? 175 GLU C OE1   1 
ATOM   5673 O OE2   . GLU C 1 203 ? -47.387 18.725  8.062   1.00 96.39  ? 175 GLU C OE2   1 
ATOM   5674 N N     . MET C 1 204 ? -47.066 21.328  1.680   1.00 87.94  ? 176 MET C N     1 
ATOM   5675 C CA    . MET C 1 204 ? -47.207 22.431  0.737   1.00 91.14  ? 176 MET C CA    1 
ATOM   5676 C C     . MET C 1 204 ? -47.897 22.007  -0.552  1.00 91.23  ? 176 MET C C     1 
ATOM   5677 O O     . MET C 1 204 ? -48.451 22.860  -1.252  1.00 89.21  ? 176 MET C O     1 
ATOM   5678 C CB    . MET C 1 204 ? -45.839 23.034  0.411   1.00 91.63  ? 176 MET C CB    1 
ATOM   5679 C CG    . MET C 1 204 ? -45.199 23.797  1.557   1.00 90.89  ? 176 MET C CG    1 
ATOM   5680 S SD    . MET C 1 204 ? -43.583 24.462  1.116   1.00 87.03  ? 176 MET C SD    1 
ATOM   5681 C CE    . MET C 1 204 ? -44.055 25.730  -0.056  1.00 85.40  ? 176 MET C CE    1 
ATOM   5682 N N     . ALA C 1 205 ? -47.870 20.713  -0.883  1.00 92.85  ? 177 ALA C N     1 
ATOM   5683 C CA    . ALA C 1 205 ? -48.533 20.250  -2.097  1.00 93.87  ? 177 ALA C CA    1 
ATOM   5684 C C     . ALA C 1 205 ? -50.049 20.335  -1.977  1.00 103.30 ? 177 ALA C C     1 
ATOM   5685 O O     . ALA C 1 205 ? -50.744 20.441  -2.994  1.00 104.32 ? 177 ALA C O     1 
ATOM   5686 C CB    . ALA C 1 205 ? -48.104 18.819  -2.419  1.00 88.87  ? 177 ALA C CB    1 
ATOM   5687 N N     . LYS C 1 206 ? -50.578 20.290  -0.752  1.00 101.22 ? 178 LYS C N     1 
ATOM   5688 C CA    . LYS C 1 206 ? -52.017 20.387  -0.547  1.00 99.31  ? 178 LYS C CA    1 
ATOM   5689 C C     . LYS C 1 206 ? -52.542 21.805  -0.716  1.00 106.42 ? 178 LYS C C     1 
ATOM   5690 O O     . LYS C 1 206 ? -53.755 21.987  -0.864  1.00 118.56 ? 178 LYS C O     1 
ATOM   5691 C CB    . LYS C 1 206 ? -52.392 19.869  0.843   1.00 92.66  ? 178 LYS C CB    1 
ATOM   5692 C CG    . LYS C 1 206 ? -52.160 18.381  1.039   1.00 89.06  ? 178 LYS C CG    1 
ATOM   5693 C CD    . LYS C 1 206 ? -52.481 17.960  2.463   1.00 87.45  ? 178 LYS C CD    1 
ATOM   5694 C CE    . LYS C 1 206 ? -52.176 16.488  2.688   1.00 92.24  ? 178 LYS C CE    1 
ATOM   5695 N NZ    . LYS C 1 206 ? -52.385 16.089  4.107   1.00 88.23  ? 178 LYS C NZ    1 
ATOM   5696 N N     . GLU C 1 207 ? -51.670 22.801  -0.695  1.00 105.76 ? 179 GLU C N     1 
ATOM   5697 C CA    . GLU C 1 207 ? -52.101 24.183  -0.859  1.00 108.87 ? 179 GLU C CA    1 
ATOM   5698 C C     . GLU C 1 207 ? -52.508 24.431  -2.305  1.00 109.14 ? 179 GLU C C     1 
ATOM   5699 O O     . GLU C 1 207 ? -51.707 24.177  -3.215  1.00 108.83 ? 179 GLU C O     1 
ATOM   5700 C CB    . GLU C 1 207 ? -50.982 25.140  -0.454  1.00 107.78 ? 179 GLU C CB    1 
ATOM   5701 C CG    . GLU C 1 207 ? -50.599 25.079  1.016   1.00 107.53 ? 179 GLU C CG    1 
ATOM   5702 C CD    . GLU C 1 207 ? -49.528 26.091  1.380   1.00 103.81 ? 179 GLU C CD    1 
ATOM   5703 O OE1   . GLU C 1 207 ? -49.358 27.077  0.631   1.00 104.18 ? 179 GLU C OE1   1 
ATOM   5704 O OE2   . GLU C 1 207 ? -48.850 25.898  2.412   1.00 100.04 ? 179 GLU C OE2   1 
ATOM   5705 N N     . PRO C 1 208 ? -53.730 24.903  -2.571  1.00 112.52 ? 180 PRO C N     1 
ATOM   5706 C CA    . PRO C 1 208 ? -54.068 25.330  -3.941  1.00 115.19 ? 180 PRO C CA    1 
ATOM   5707 C C     . PRO C 1 208 ? -53.142 26.413  -4.463  1.00 112.75 ? 180 PRO C C     1 
ATOM   5708 O O     . PRO C 1 208 ? -53.001 26.566  -5.682  1.00 109.46 ? 180 PRO C O     1 
ATOM   5709 C CB    . PRO C 1 208 ? -55.506 25.846  -3.801  1.00 113.33 ? 180 PRO C CB    1 
ATOM   5710 C CG    . PRO C 1 208 ? -56.047 25.137  -2.605  1.00 110.05 ? 180 PRO C CG    1 
ATOM   5711 C CD    . PRO C 1 208 ? -54.888 24.973  -1.664  1.00 108.23 ? 180 PRO C CD    1 
ATOM   5712 N N     . ARG C 1 209 ? -52.520 27.170  -3.559  1.00 112.04 ? 181 ARG C N     1 
ATOM   5713 C CA    . ARG C 1 209 ? -51.519 28.166  -3.921  1.00 106.25 ? 181 ARG C CA    1 
ATOM   5714 C C     . ARG C 1 209 ? -50.372 27.558  -4.721  1.00 102.60 ? 181 ARG C C     1 
ATOM   5715 O O     . ARG C 1 209 ? -49.784 28.232  -5.575  1.00 93.06  ? 181 ARG C O     1 
ATOM   5716 C CB    . ARG C 1 209 ? -51.005 28.812  -2.634  1.00 100.97 ? 181 ARG C CB    1 
ATOM   5717 C CG    . ARG C 1 209 ? -49.977 29.913  -2.758  1.00 94.50  ? 181 ARG C CG    1 
ATOM   5718 C CD    . ARG C 1 209 ? -49.580 30.316  -1.346  1.00 93.51  ? 181 ARG C CD    1 
ATOM   5719 N NE    . ARG C 1 209 ? -48.439 31.219  -1.282  1.00 96.09  ? 181 ARG C NE    1 
ATOM   5720 C CZ    . ARG C 1 209 ? -47.824 31.554  -0.156  1.00 96.00  ? 181 ARG C CZ    1 
ATOM   5721 N NH1   . ARG C 1 209 ? -48.212 31.071  1.013   1.00 94.44  ? 181 ARG C NH1   1 
ATOM   5722 N NH2   . ARG C 1 209 ? -46.792 32.390  -0.204  1.00 94.81  ? 181 ARG C NH2   1 
ATOM   5723 N N     . TRP C 1 210 ? -50.047 26.287  -4.469  1.00 105.55 ? 182 TRP C N     1 
ATOM   5724 C CA    . TRP C 1 210 ? -48.910 25.637  -5.099  1.00 100.01 ? 182 TRP C CA    1 
ATOM   5725 C C     . TRP C 1 210 ? -49.266 24.400  -5.909  1.00 99.10  ? 182 TRP C C     1 
ATOM   5726 O O     . TRP C 1 210 ? -48.439 23.966  -6.718  1.00 94.66  ? 182 TRP C O     1 
ATOM   5727 C CB    . TRP C 1 210 ? -47.877 25.216  -4.039  1.00 99.42  ? 182 TRP C CB    1 
ATOM   5728 C CG    . TRP C 1 210 ? -47.424 26.321  -3.125  1.00 97.29  ? 182 TRP C CG    1 
ATOM   5729 C CD1   . TRP C 1 210 ? -47.487 26.327  -1.761  1.00 94.91  ? 182 TRP C CD1   1 
ATOM   5730 C CD2   . TRP C 1 210 ? -46.818 27.567  -3.501  1.00 95.93  ? 182 TRP C CD2   1 
ATOM   5731 N NE1   . TRP C 1 210 ? -46.976 27.501  -1.265  1.00 93.06  ? 182 TRP C NE1   1 
ATOM   5732 C CE2   . TRP C 1 210 ? -46.556 28.278  -2.312  1.00 92.38  ? 182 TRP C CE2   1 
ATOM   5733 C CE3   . TRP C 1 210 ? -46.478 28.152  -4.725  1.00 94.91  ? 182 TRP C CE3   1 
ATOM   5734 C CZ2   . TRP C 1 210 ? -45.969 29.542  -2.311  1.00 90.50  ? 182 TRP C CZ2   1 
ATOM   5735 C CZ3   . TRP C 1 210 ? -45.896 29.409  -4.721  1.00 90.61  ? 182 TRP C CZ3   1 
ATOM   5736 C CH2   . TRP C 1 210 ? -45.649 30.089  -3.523  1.00 89.29  ? 182 TRP C CH2   1 
ATOM   5737 N N     . ALA C 1 211 ? -50.465 23.833  -5.728  1.00 101.78 ? 183 ALA C N     1 
ATOM   5738 C CA    . ALA C 1 211 ? -50.745 22.468  -6.171  1.00 100.43 ? 183 ALA C CA    1 
ATOM   5739 C C     . ALA C 1 211 ? -50.398 22.233  -7.636  1.00 99.75  ? 183 ALA C C     1 
ATOM   5740 O O     . ALA C 1 211 ? -50.075 21.103  -8.021  1.00 100.40 ? 183 ALA C O     1 
ATOM   5741 C CB    . ALA C 1 211 ? -52.217 22.123  -5.922  1.00 102.54 ? 183 ALA C CB    1 
ATOM   5742 N N     . LEU C 1 212 ? -50.442 23.280  -8.464  1.00 98.04  ? 184 LEU C N     1 
ATOM   5743 C CA    . LEU C 1 212 ? -50.118 23.105  -9.877  1.00 91.93  ? 184 LEU C CA    1 
ATOM   5744 C C     . LEU C 1 212 ? -48.658 22.708  -10.065 1.00 94.23  ? 184 LEU C C     1 
ATOM   5745 O O     . LEU C 1 212 ? -48.335 21.894  -10.938 1.00 91.42  ? 184 LEU C O     1 
ATOM   5746 C CB    . LEU C 1 212 ? -50.431 24.383  -10.653 1.00 78.49  ? 184 LEU C CB    1 
ATOM   5747 N N     . TYR C 1 213 ? -47.763 23.263  -9.246  1.00 94.38  ? 185 TYR C N     1 
ATOM   5748 C CA    . TYR C 1 213 ? -46.342 22.964  -9.362  1.00 92.74  ? 185 TYR C CA    1 
ATOM   5749 C C     . TYR C 1 213 ? -45.937 21.697  -8.621  1.00 90.20  ? 185 TYR C C     1 
ATOM   5750 O O     . TYR C 1 213 ? -44.851 21.167  -8.878  1.00 89.96  ? 185 TYR C O     1 
ATOM   5751 C CB    . TYR C 1 213 ? -45.510 24.135  -8.832  1.00 90.93  ? 185 TYR C CB    1 
ATOM   5752 C CG    . TYR C 1 213 ? -45.818 25.467  -9.475  1.00 91.06  ? 185 TYR C CG    1 
ATOM   5753 C CD1   . TYR C 1 213 ? -45.202 25.846  -10.660 1.00 95.32  ? 185 TYR C CD1   1 
ATOM   5754 C CD2   . TYR C 1 213 ? -46.719 26.349  -8.893  1.00 89.86  ? 185 TYR C CD2   1 
ATOM   5755 C CE1   . TYR C 1 213 ? -45.476 27.065  -11.250 1.00 97.48  ? 185 TYR C CE1   1 
ATOM   5756 C CE2   . TYR C 1 213 ? -47.000 27.570  -9.475  1.00 92.28  ? 185 TYR C CE2   1 
ATOM   5757 C CZ    . TYR C 1 213 ? -46.376 27.922  -10.654 1.00 95.70  ? 185 TYR C CZ    1 
ATOM   5758 O OH    . TYR C 1 213 ? -46.653 29.137  -11.238 1.00 95.54  ? 185 TYR C OH    1 
ATOM   5759 N N     . MET C 1 214 ? -46.773 21.201  -7.714  1.00 87.46  ? 186 MET C N     1 
ATOM   5760 C CA    . MET C 1 214 ? -46.412 20.098  -6.835  1.00 82.12  ? 186 MET C CA    1 
ATOM   5761 C C     . MET C 1 214 ? -47.341 18.906  -7.030  1.00 87.29  ? 186 MET C C     1 
ATOM   5762 O O     . MET C 1 214 ? -47.712 18.221  -6.075  1.00 89.75  ? 186 MET C O     1 
ATOM   5763 C CB    . MET C 1 214 ? -46.414 20.553  -5.378  1.00 85.79  ? 186 MET C CB    1 
ATOM   5764 C CG    . MET C 1 214 ? -45.446 21.693  -5.099  1.00 87.98  ? 186 MET C CG    1 
ATOM   5765 S SD    . MET C 1 214 ? -45.387 22.182  -3.366  1.00 97.05  ? 186 MET C SD    1 
ATOM   5766 C CE    . MET C 1 214 ? -44.343 20.893  -2.697  1.00 88.54  ? 186 MET C CE    1 
ATOM   5767 N N     . GLN C 1 215 ? -47.729 18.644  -8.280  1.00 91.56  ? 187 GLN C N     1 
ATOM   5768 C CA    . GLN C 1 215 ? -48.563 17.484  -8.572  1.00 90.52  ? 187 GLN C CA    1 
ATOM   5769 C C     . GLN C 1 215 ? -47.785 16.178  -8.482  1.00 92.49  ? 187 GLN C C     1 
ATOM   5770 O O     . GLN C 1 215 ? -48.395 15.118  -8.301  1.00 97.37  ? 187 GLN C O     1 
ATOM   5771 C CB    . GLN C 1 215 ? -49.192 17.621  -9.959  1.00 87.47  ? 187 GLN C CB    1 
ATOM   5772 N N     . ASP C 1 216 ? -46.459 16.230  -8.603  1.00 90.45  ? 188 ASP C N     1 
ATOM   5773 C CA    . ASP C 1 216 ? -45.624 15.040  -8.491  1.00 88.97  ? 188 ASP C CA    1 
ATOM   5774 C C     . ASP C 1 216 ? -44.816 15.086  -7.201  1.00 84.24  ? 188 ASP C C     1 
ATOM   5775 O O     . ASP C 1 216 ? -43.600 14.869  -7.215  1.00 84.37  ? 188 ASP C O     1 
ATOM   5776 C CB    . ASP C 1 216 ? -44.692 14.923  -9.698  1.00 88.89  ? 188 ASP C CB    1 
ATOM   5777 C CG    . ASP C 1 216 ? -43.951 16.215  -9.988  1.00 86.36  ? 188 ASP C CG    1 
ATOM   5778 O OD1   . ASP C 1 216 ? -44.349 17.265  -9.440  1.00 84.01  ? 188 ASP C OD1   1 
ATOM   5779 O OD2   . ASP C 1 216 ? -42.970 16.180  -10.759 1.00 90.83  ? 188 ASP C OD2   1 
ATOM   5780 N N     . VAL C 1 217 ? -45.487 15.366  -6.081  1.00 79.12  ? 189 VAL C N     1 
ATOM   5781 C CA    . VAL C 1 217 ? -44.777 15.571  -4.823  1.00 75.32  ? 189 VAL C CA    1 
ATOM   5782 C C     . VAL C 1 217 ? -44.134 14.277  -4.336  1.00 82.13  ? 189 VAL C C     1 
ATOM   5783 O O     . VAL C 1 217 ? -43.071 14.307  -3.703  1.00 85.61  ? 189 VAL C O     1 
ATOM   5784 C CB    . VAL C 1 217 ? -45.730 16.171  -3.769  1.00 70.61  ? 189 VAL C CB    1 
ATOM   5785 C CG1   . VAL C 1 217 ? -46.871 15.211  -3.457  1.00 77.10  ? 189 VAL C CG1   1 
ATOM   5786 C CG2   . VAL C 1 217 ? -44.969 16.544  -2.504  1.00 74.63  ? 189 VAL C CG2   1 
ATOM   5787 N N     . GLU C 1 218 ? -44.741 13.124  -4.633  1.00 84.69  ? 190 GLU C N     1 
ATOM   5788 C CA    . GLU C 1 218 ? -44.183 11.857  -4.172  1.00 83.45  ? 190 GLU C CA    1 
ATOM   5789 C C     . GLU C 1 218 ? -42.876 11.508  -4.872  1.00 79.88  ? 190 GLU C C     1 
ATOM   5790 O O     . GLU C 1 218 ? -42.147 10.634  -4.393  1.00 77.97  ? 190 GLU C O     1 
ATOM   5791 C CB    . GLU C 1 218 ? -45.196 10.725  -4.364  1.00 84.37  ? 190 GLU C CB    1 
ATOM   5792 C CG    . GLU C 1 218 ? -45.487 10.367  -5.815  1.00 88.61  ? 190 GLU C CG    1 
ATOM   5793 C CD    . GLU C 1 218 ? -46.495 11.299  -6.464  1.00 90.45  ? 190 GLU C CD    1 
ATOM   5794 O OE1   . GLU C 1 218 ? -46.865 12.317  -5.840  1.00 85.80  ? 190 GLU C OE1   1 
ATOM   5795 O OE2   . GLU C 1 218 ? -46.921 11.011  -7.602  1.00 93.03  ? 190 GLU C OE2   1 
ATOM   5796 N N     . LYS C 1 219 ? -42.564 12.163  -5.988  1.00 79.39  ? 191 LYS C N     1 
ATOM   5797 C CA    . LYS C 1 219 ? -41.290 11.973  -6.665  1.00 76.58  ? 191 LYS C CA    1 
ATOM   5798 C C     . LYS C 1 219 ? -40.224 12.957  -6.200  1.00 76.08  ? 191 LYS C C     1 
ATOM   5799 O O     . LYS C 1 219 ? -39.072 12.855  -6.635  1.00 78.00  ? 191 LYS C O     1 
ATOM   5800 C CB    . LYS C 1 219 ? -41.479 12.075  -8.183  1.00 68.91  ? 191 LYS C CB    1 
ATOM   5801 C CG    . LYS C 1 219 ? -42.184 10.867  -8.782  1.00 64.00  ? 191 LYS C CG    1 
ATOM   5802 C CD    . LYS C 1 219 ? -42.264 10.943  -10.296 1.00 64.95  ? 191 LYS C CD    1 
ATOM   5803 C CE    . LYS C 1 219 ? -42.917 9.692   -10.867 1.00 67.29  ? 191 LYS C CE    1 
ATOM   5804 N NZ    . LYS C 1 219 ? -43.077 9.762   -12.346 1.00 69.12  ? 191 LYS C NZ    1 
ATOM   5805 N N     . PHE C 1 220 ? -40.581 13.905  -5.331  1.00 71.69  ? 192 PHE C N     1 
ATOM   5806 C CA    . PHE C 1 220 ? -39.624 14.787  -4.676  1.00 68.63  ? 192 PHE C CA    1 
ATOM   5807 C C     . PHE C 1 220 ? -39.419 14.417  -3.211  1.00 65.02  ? 192 PHE C C     1 
ATOM   5808 O O     . PHE C 1 220 ? -38.909 15.228  -2.432  1.00 66.19  ? 192 PHE C O     1 
ATOM   5809 C CB    . PHE C 1 220 ? -40.069 16.245  -4.794  1.00 67.05  ? 192 PHE C CB    1 
ATOM   5810 C CG    . PHE C 1 220 ? -39.897 16.824  -6.168  1.00 68.80  ? 192 PHE C CG    1 
ATOM   5811 C CD1   . PHE C 1 220 ? -40.814 16.556  -7.170  1.00 76.27  ? 192 PHE C CD1   1 
ATOM   5812 C CD2   . PHE C 1 220 ? -38.818 17.643  -6.455  1.00 72.11  ? 192 PHE C CD2   1 
ATOM   5813 C CE1   . PHE C 1 220 ? -40.655 17.092  -8.434  1.00 81.28  ? 192 PHE C CE1   1 
ATOM   5814 C CE2   . PHE C 1 220 ? -38.653 18.181  -7.716  1.00 73.81  ? 192 PHE C CE2   1 
ATOM   5815 C CZ    . PHE C 1 220 ? -39.573 17.906  -8.707  1.00 80.05  ? 192 PHE C CZ    1 
ATOM   5816 N N     . VAL C 1 221 ? -39.816 13.209  -2.824  1.00 60.94  ? 193 VAL C N     1 
ATOM   5817 C CA    . VAL C 1 221 ? -39.706 12.728  -1.454  1.00 58.06  ? 193 VAL C CA    1 
ATOM   5818 C C     . VAL C 1 221 ? -38.942 11.412  -1.472  1.00 61.02  ? 193 VAL C C     1 
ATOM   5819 O O     . VAL C 1 221 ? -39.094 10.612  -2.401  1.00 71.81  ? 193 VAL C O     1 
ATOM   5820 C CB    . VAL C 1 221 ? -41.099 12.551  -0.809  1.00 65.69  ? 193 VAL C CB    1 
ATOM   5821 C CG1   . VAL C 1 221 ? -40.984 11.966  0.586   1.00 74.20  ? 193 VAL C CG1   1 
ATOM   5822 C CG2   . VAL C 1 221 ? -41.833 13.881  -0.764  1.00 74.14  ? 193 VAL C CG2   1 
ATOM   5823 N N     . SER C 1 222 ? -38.106 11.201  -0.459  1.00 55.56  ? 194 SER C N     1 
ATOM   5824 C CA    . SER C 1 222 ? -37.387 9.942   -0.344  1.00 55.45  ? 194 SER C CA    1 
ATOM   5825 C C     . SER C 1 222 ? -38.381 8.784   -0.286  1.00 62.93  ? 194 SER C C     1 
ATOM   5826 O O     . SER C 1 222 ? -39.431 8.898   0.356   1.00 65.71  ? 194 SER C O     1 
ATOM   5827 C CB    . SER C 1 222 ? -36.503 9.941   0.903   1.00 54.45  ? 194 SER C CB    1 
ATOM   5828 O OG    . SER C 1 222 ? -36.051 8.633   1.210   1.00 57.11  ? 194 SER C OG    1 
ATOM   5829 N N     . PRO C 1 223 ? -38.094 7.663   -0.953  1.00 62.77  ? 195 PRO C N     1 
ATOM   5830 C CA    . PRO C 1 223 ? -39.041 6.538   -0.914  1.00 65.09  ? 195 PRO C CA    1 
ATOM   5831 C C     . PRO C 1 223 ? -39.137 5.898   0.455   1.00 71.11  ? 195 PRO C C     1 
ATOM   5832 O O     . PRO C 1 223 ? -40.187 5.341   0.797   1.00 76.00  ? 195 PRO C O     1 
ATOM   5833 C CB    . PRO C 1 223 ? -38.476 5.562   -1.953  1.00 60.99  ? 195 PRO C CB    1 
ATOM   5834 C CG    . PRO C 1 223 ? -37.034 5.889   -2.032  1.00 58.83  ? 195 PRO C CG    1 
ATOM   5835 C CD    . PRO C 1 223 ? -36.875 7.346   -1.715  1.00 55.55  ? 195 PRO C CD    1 
ATOM   5836 N N     . TYR C 1 224 ? -38.071 5.961   1.248   1.00 67.00  ? 196 TYR C N     1 
ATOM   5837 C CA    . TYR C 1 224 ? -38.063 5.429   2.602   1.00 68.98  ? 196 TYR C CA    1 
ATOM   5838 C C     . TYR C 1 224 ? -38.613 6.420   3.620   1.00 71.75  ? 196 TYR C C     1 
ATOM   5839 O O     . TYR C 1 224 ? -38.448 6.206   4.826   1.00 74.89  ? 196 TYR C O     1 
ATOM   5840 C CB    . TYR C 1 224 ? -36.640 5.015   2.983   1.00 67.64  ? 196 TYR C CB    1 
ATOM   5841 C CG    . TYR C 1 224 ? -35.938 4.249   1.886   1.00 67.02  ? 196 TYR C CG    1 
ATOM   5842 C CD1   . TYR C 1 224 ? -36.250 2.920   1.628   1.00 68.98  ? 196 TYR C CD1   1 
ATOM   5843 C CD2   . TYR C 1 224 ? -34.974 4.861   1.095   1.00 66.33  ? 196 TYR C CD2   1 
ATOM   5844 C CE1   . TYR C 1 224 ? -35.614 2.220   0.619   1.00 72.62  ? 196 TYR C CE1   1 
ATOM   5845 C CE2   . TYR C 1 224 ? -34.334 4.170   0.085   1.00 65.94  ? 196 TYR C CE2   1 
ATOM   5846 C CZ    . TYR C 1 224 ? -34.657 2.850   -0.149  1.00 66.32  ? 196 TYR C CZ    1 
ATOM   5847 O OH    . TYR C 1 224 ? -34.022 2.159   -1.154  1.00 64.87  ? 196 TYR C OH    1 
ATOM   5848 N N     . GLN C 1 225 ? -39.253 7.496   3.153   1.00 70.04  ? 197 GLN C N     1 
ATOM   5849 C CA    . GLN C 1 225 ? -39.834 8.480   4.060   1.00 70.09  ? 197 GLN C CA    1 
ATOM   5850 C C     . GLN C 1 225 ? -40.895 7.844   4.949   1.00 74.24  ? 197 GLN C C     1 
ATOM   5851 O O     . GLN C 1 225 ? -40.841 7.952   6.179   1.00 78.99  ? 197 GLN C O     1 
ATOM   5852 C CB    . GLN C 1 225 ? -40.435 9.634   3.256   1.00 68.22  ? 197 GLN C CB    1 
ATOM   5853 C CG    . GLN C 1 225 ? -40.998 10.771  4.092   1.00 67.04  ? 197 GLN C CG    1 
ATOM   5854 C CD    . GLN C 1 225 ? -39.914 11.602  4.747   1.00 69.23  ? 197 GLN C CD    1 
ATOM   5855 O OE1   . GLN C 1 225 ? -38.799 11.701  4.237   1.00 69.50  ? 197 GLN C OE1   1 
ATOM   5856 N NE2   . GLN C 1 225 ? -40.236 12.205  5.886   1.00 74.31  ? 197 GLN C NE2   1 
ATOM   5857 N N     . HIS C 1 226 ? -41.870 7.174   4.337   1.00 74.37  ? 198 HIS C N     1 
ATOM   5858 C CA    . HIS C 1 226 ? -42.958 6.532   5.058   1.00 78.63  ? 198 HIS C CA    1 
ATOM   5859 C C     . HIS C 1 226 ? -42.687 5.058   5.335   1.00 79.27  ? 198 HIS C C     1 
ATOM   5860 O O     . HIS C 1 226 ? -43.626 4.307   5.622   1.00 83.51  ? 198 HIS C O     1 
ATOM   5861 C CB    . HIS C 1 226 ? -44.268 6.691   4.283   1.00 78.39  ? 198 HIS C CB    1 
ATOM   5862 C CG    . HIS C 1 226 ? -44.585 8.109   3.922   1.00 80.43  ? 198 HIS C CG    1 
ATOM   5863 N ND1   . HIS C 1 226 ? -44.772 9.094   4.868   1.00 80.28  ? 198 HIS C ND1   1 
ATOM   5864 C CD2   . HIS C 1 226 ? -44.744 8.709   2.718   1.00 79.71  ? 198 HIS C CD2   1 
ATOM   5865 C CE1   . HIS C 1 226 ? -45.034 10.239  4.262   1.00 81.50  ? 198 HIS C CE1   1 
ATOM   5866 N NE2   . HIS C 1 226 ? -45.023 10.032  2.958   1.00 84.33  ? 198 HIS C NE2   1 
ATOM   5867 N N     . SER C 1 227 ? -41.430 4.630   5.256   1.00 77.45  ? 199 SER C N     1 
ATOM   5868 C CA    . SER C 1 227 ? -41.082 3.240   5.509   1.00 81.51  ? 199 SER C CA    1 
ATOM   5869 C C     . SER C 1 227 ? -41.033 2.975   7.008   1.00 86.80  ? 199 SER C C     1 
ATOM   5870 O O     . SER C 1 227 ? -40.348 3.684   7.752   1.00 91.87  ? 199 SER C O     1 
ATOM   5871 C CB    . SER C 1 227 ? -39.736 2.902   4.868   1.00 81.77  ? 199 SER C CB    1 
ATOM   5872 O OG    . SER C 1 227 ? -39.302 1.606   5.244   1.00 81.87  ? 199 SER C OG    1 
ATOM   5873 N N     . GLU C 1 228 ? -41.765 1.950   7.451   1.00 86.23  ? 200 GLU C N     1 
ATOM   5874 C CA    . GLU C 1 228 ? -41.731 1.565   8.857   1.00 89.51  ? 200 GLU C CA    1 
ATOM   5875 C C     . GLU C 1 228 ? -40.428 0.872   9.232   1.00 91.08  ? 200 GLU C C     1 
ATOM   5876 O O     . GLU C 1 228 ? -40.115 0.770   10.422  1.00 91.44  ? 200 GLU C O     1 
ATOM   5877 C CB    . GLU C 1 228 ? -42.919 0.658   9.184   1.00 94.06  ? 200 GLU C CB    1 
ATOM   5878 N N     . ASP C 1 229 ? -39.669 0.396   8.247   1.00 87.15  ? 201 ASP C N     1 
ATOM   5879 C CA    . ASP C 1 229 ? -38.372 -0.237  8.492   1.00 85.35  ? 201 ASP C CA    1 
ATOM   5880 C C     . ASP C 1 229 ? -37.458 0.072   7.317   1.00 81.76  ? 201 ASP C C     1 
ATOM   5881 O O     . ASP C 1 229 ? -37.321 -0.725  6.382   1.00 79.59  ? 201 ASP C O     1 
ATOM   5882 C CB    . ASP C 1 229 ? -38.519 -1.746  8.691   1.00 87.01  ? 201 ASP C CB    1 
ATOM   5883 C CG    . ASP C 1 229 ? -37.196 -2.430  8.982   1.00 86.07  ? 201 ASP C CG    1 
ATOM   5884 O OD1   . ASP C 1 229 ? -36.255 -1.744  9.435   1.00 90.83  ? 201 ASP C OD1   1 
ATOM   5885 O OD2   . ASP C 1 229 ? -37.095 -3.654  8.753   1.00 79.38  ? 201 ASP C OD2   1 
ATOM   5886 N N     . PRO C 1 230 ? -36.816 1.244   7.327   1.00 80.46  ? 202 PRO C N     1 
ATOM   5887 C CA    . PRO C 1 230 ? -35.959 1.612   6.185   1.00 74.15  ? 202 PRO C CA    1 
ATOM   5888 C C     . PRO C 1 230 ? -34.756 0.700   6.011   1.00 73.88  ? 202 PRO C C     1 
ATOM   5889 O O     . PRO C 1 230 ? -34.362 0.417   4.872   1.00 76.25  ? 202 PRO C O     1 
ATOM   5890 C CB    . PRO C 1 230 ? -35.537 3.052   6.512   1.00 74.83  ? 202 PRO C CB    1 
ATOM   5891 C CG    . PRO C 1 230 ? -36.528 3.541   7.517   1.00 77.39  ? 202 PRO C CG    1 
ATOM   5892 C CD    . PRO C 1 230 ? -36.958 2.341   8.298   1.00 80.97  ? 202 PRO C CD    1 
ATOM   5893 N N     . VAL C 1 231 ? -34.159 0.234   7.109   1.00 72.53  ? 203 VAL C N     1 
ATOM   5894 C CA    . VAL C 1 231 ? -32.994 -0.642  7.006   1.00 70.47  ? 203 VAL C CA    1 
ATOM   5895 C C     . VAL C 1 231 ? -33.374 -1.965  6.353   1.00 71.53  ? 203 VAL C C     1 
ATOM   5896 O O     . VAL C 1 231 ? -32.610 -2.521  5.554   1.00 71.23  ? 203 VAL C O     1 
ATOM   5897 C CB    . VAL C 1 231 ? -32.363 -0.852  8.395   1.00 75.49  ? 203 VAL C CB    1 
ATOM   5898 C CG1   . VAL C 1 231 ? -31.302 -1.941  8.348   1.00 69.99  ? 203 VAL C CG1   1 
ATOM   5899 C CG2   . VAL C 1 231 ? -31.764 0.446   8.897   1.00 76.35  ? 203 VAL C CG2   1 
ATOM   5900 N N     . GLY C 1 232 ? -34.560 -2.484  6.669   1.00 75.57  ? 204 GLY C N     1 
ATOM   5901 C CA    . GLY C 1 232 ? -34.983 -3.742  6.075   1.00 78.95  ? 204 GLY C CA    1 
ATOM   5902 C C     . GLY C 1 232 ? -35.229 -3.628  4.582   1.00 75.74  ? 204 GLY C C     1 
ATOM   5903 O O     . GLY C 1 232 ? -34.773 -4.467  3.799   1.00 75.50  ? 204 GLY C O     1 
ATOM   5904 N N     . GLU C 1 233 ? -35.955 -2.586  4.167   1.00 74.20  ? 205 GLU C N     1 
ATOM   5905 C CA    . GLU C 1 233 ? -36.261 -2.413  2.751   1.00 67.49  ? 205 GLU C CA    1 
ATOM   5906 C C     . GLU C 1 233 ? -34.996 -2.196  1.931   1.00 69.26  ? 205 GLU C C     1 
ATOM   5907 O O     . GLU C 1 233 ? -34.866 -2.730  0.823   1.00 71.54  ? 205 GLU C O     1 
ATOM   5908 C CB    . GLU C 1 233 ? -37.225 -1.243  2.558   1.00 66.91  ? 205 GLU C CB    1 
ATOM   5909 C CG    . GLU C 1 233 ? -38.640 -1.512  3.035   1.00 74.76  ? 205 GLU C CG    1 
ATOM   5910 C CD    . GLU C 1 233 ? -39.597 -0.398  2.662   1.00 84.30  ? 205 GLU C CD    1 
ATOM   5911 O OE1   . GLU C 1 233 ? -39.268 0.387   1.747   1.00 84.24  ? 205 GLU C OE1   1 
ATOM   5912 O OE2   . GLU C 1 233 ? -40.678 -0.306  3.282   1.00 86.73  ? 205 GLU C OE2   1 
ATOM   5913 N N     . PHE C 1 234 ? -34.049 -1.416  2.458   1.00 70.07  ? 206 PHE C N     1 
ATOM   5914 C CA    . PHE C 1 234 ? -32.824 -1.149  1.713   1.00 62.56  ? 206 PHE C CA    1 
ATOM   5915 C C     . PHE C 1 234 ? -31.950 -2.393  1.624   1.00 63.19  ? 206 PHE C C     1 
ATOM   5916 O O     . PHE C 1 234 ? -31.363 -2.670  0.572   1.00 63.99  ? 206 PHE C O     1 
ATOM   5917 C CB    . PHE C 1 234 ? -32.055 0.005   2.355   1.00 58.08  ? 206 PHE C CB    1 
ATOM   5918 C CG    . PHE C 1 234 ? -31.021 0.614   1.452   1.00 55.29  ? 206 PHE C CG    1 
ATOM   5919 C CD1   . PHE C 1 234 ? -31.384 1.151   0.229   1.00 53.16  ? 206 PHE C CD1   1 
ATOM   5920 C CD2   . PHE C 1 234 ? -29.687 0.640   1.820   1.00 56.60  ? 206 PHE C CD2   1 
ATOM   5921 C CE1   . PHE C 1 234 ? -30.438 1.710   -0.608  1.00 49.88  ? 206 PHE C CE1   1 
ATOM   5922 C CE2   . PHE C 1 234 ? -28.734 1.198   0.986   1.00 48.38  ? 206 PHE C CE2   1 
ATOM   5923 C CZ    . PHE C 1 234 ? -29.111 1.733   -0.229  1.00 46.28  ? 206 PHE C CZ    1 
ATOM   5924 N N     . ARG C 1 235 ? -31.846 -3.152  2.719   1.00 68.42  ? 207 ARG C N     1 
ATOM   5925 C CA    . ARG C 1 235 ? -31.091 -4.400  2.677   1.00 69.62  ? 207 ARG C CA    1 
ATOM   5926 C C     . ARG C 1 235 ? -31.722 -5.389  1.706   1.00 68.23  ? 207 ARG C C     1 
ATOM   5927 O O     . ARG C 1 235 ? -31.015 -6.109  0.992   1.00 71.33  ? 207 ARG C O     1 
ATOM   5928 C CB    . ARG C 1 235 ? -30.994 -5.012  4.076   1.00 72.32  ? 207 ARG C CB    1 
ATOM   5929 C CG    . ARG C 1 235 ? -30.238 -6.334  4.113   1.00 72.89  ? 207 ARG C CG    1 
ATOM   5930 C CD    . ARG C 1 235 ? -30.152 -6.912  5.519   1.00 74.06  ? 207 ARG C CD    1 
ATOM   5931 N NE    . ARG C 1 235 ? -29.026 -6.377  6.274   1.00 72.41  ? 207 ARG C NE    1 
ATOM   5932 C CZ    . ARG C 1 235 ? -29.128 -5.792  7.460   1.00 74.04  ? 207 ARG C CZ    1 
ATOM   5933 N NH1   . ARG C 1 235 ? -30.297 -5.647  8.062   1.00 67.86  ? 207 ARG C NH1   1 
ATOM   5934 N NH2   . ARG C 1 235 ? -28.028 -5.344  8.058   1.00 79.42  ? 207 ARG C NH2   1 
ATOM   5935 N N     . LEU C 1 236 ? -33.055 -5.436  1.663   1.00 68.54  ? 208 LEU C N     1 
ATOM   5936 C CA    . LEU C 1 236 ? -33.731 -6.301  0.703   1.00 73.26  ? 208 LEU C CA    1 
ATOM   5937 C C     . LEU C 1 236 ? -33.545 -5.794  -0.721  1.00 73.60  ? 208 LEU C C     1 
ATOM   5938 O O     . LEU C 1 236 ? -33.422 -6.591  -1.658  1.00 74.25  ? 208 LEU C O     1 
ATOM   5939 C CB    . LEU C 1 236 ? -35.217 -6.408  1.047   1.00 76.51  ? 208 LEU C CB    1 
ATOM   5940 C CG    . LEU C 1 236 ? -36.071 -7.251  0.096   1.00 81.44  ? 208 LEU C CG    1 
ATOM   5941 C CD1   . LEU C 1 236 ? -35.560 -8.683  0.041   1.00 81.01  ? 208 LEU C CD1   1 
ATOM   5942 C CD2   . LEU C 1 236 ? -37.534 -7.216  0.508   1.00 91.77  ? 208 LEU C CD2   1 
ATOM   5943 N N     . LEU C 1 237 ? -33.517 -4.471  -0.903  1.00 72.67  ? 209 LEU C N     1 
ATOM   5944 C CA    . LEU C 1 237 ? -33.340 -3.916  -2.240  1.00 71.29  ? 209 LEU C CA    1 
ATOM   5945 C C     . LEU C 1 237 ? -31.946 -4.208  -2.781  1.00 68.06  ? 209 LEU C C     1 
ATOM   5946 O O     . LEU C 1 237 ? -31.788 -4.532  -3.963  1.00 70.65  ? 209 LEU C O     1 
ATOM   5947 C CB    . LEU C 1 237 ? -33.602 -2.410  -2.226  1.00 65.57  ? 209 LEU C CB    1 
ATOM   5948 C CG    . LEU C 1 237 ? -33.388 -1.708  -3.568  1.00 60.83  ? 209 LEU C CG    1 
ATOM   5949 C CD1   . LEU C 1 237 ? -34.383 -2.223  -4.593  1.00 62.57  ? 209 LEU C CD1   1 
ATOM   5950 C CD2   . LEU C 1 237 ? -33.492 -0.200  -3.420  1.00 61.37  ? 209 LEU C CD2   1 
ATOM   5951 N N     . LEU C 1 238 ? -30.922 -4.098  -1.931  1.00 64.12  ? 210 LEU C N     1 
ATOM   5952 C CA    . LEU C 1 238 ? -29.562 -4.377  -2.378  1.00 60.89  ? 210 LEU C CA    1 
ATOM   5953 C C     . LEU C 1 238 ? -29.378 -5.855  -2.699  1.00 67.27  ? 210 LEU C C     1 
ATOM   5954 O O     . LEU C 1 238 ? -28.805 -6.202  -3.738  1.00 71.69  ? 210 LEU C O     1 
ATOM   5955 C CB    . LEU C 1 238 ? -28.558 -3.928  -1.317  1.00 60.65  ? 210 LEU C CB    1 
ATOM   5956 C CG    . LEU C 1 238 ? -28.440 -2.419  -1.099  1.00 54.49  ? 210 LEU C CG    1 
ATOM   5957 C CD1   . LEU C 1 238 ? -27.404 -2.111  -0.030  1.00 45.85  ? 210 LEU C CD1   1 
ATOM   5958 C CD2   . LEU C 1 238 ? -28.099 -1.720  -2.403  1.00 54.84  ? 210 LEU C CD2   1 
ATOM   5959 N N     . GLU C 1 239 ? -29.866 -6.739  -1.825  1.00 70.15  ? 211 GLU C N     1 
ATOM   5960 C CA    . GLU C 1 239 ? -29.712 -8.173  -2.051  1.00 72.55  ? 211 GLU C CA    1 
ATOM   5961 C C     . GLU C 1 239 ? -30.558 -8.679  -3.213  1.00 72.71  ? 211 GLU C C     1 
ATOM   5962 O O     . GLU C 1 239 ? -30.209 -9.700  -3.814  1.00 76.41  ? 211 GLU C O     1 
ATOM   5963 C CB    . GLU C 1 239 ? -30.054 -8.945  -0.776  1.00 77.87  ? 211 GLU C CB    1 
ATOM   5964 C CG    . GLU C 1 239 ? -29.023 -8.777  0.328   1.00 82.01  ? 211 GLU C CG    1 
ATOM   5965 C CD    . GLU C 1 239 ? -29.535 -9.218  1.683   1.00 84.30  ? 211 GLU C CD    1 
ATOM   5966 O OE1   . GLU C 1 239 ? -30.760 -9.421  1.821   1.00 85.04  ? 211 GLU C OE1   1 
ATOM   5967 O OE2   . GLU C 1 239 ? -28.710 -9.360  2.610   1.00 81.10  ? 211 GLU C OE2   1 
ATOM   5968 N N     . SER C 1 240 ? -31.653 -7.994  -3.546  1.00 72.71  ? 212 SER C N     1 
ATOM   5969 C CA    . SER C 1 240 ? -32.437 -8.358  -4.721  1.00 71.06  ? 212 SER C CA    1 
ATOM   5970 C C     . SER C 1 240 ? -31.753 -7.974  -6.027  1.00 67.00  ? 212 SER C C     1 
ATOM   5971 O O     . SER C 1 240 ? -32.292 -8.271  -7.099  1.00 66.07  ? 212 SER C O     1 
ATOM   5972 C CB    . SER C 1 240 ? -33.823 -7.709  -4.658  1.00 73.73  ? 212 SER C CB    1 
ATOM   5973 O OG    . SER C 1 240 ? -33.746 -6.313  -4.893  1.00 70.48  ? 212 SER C OG    1 
ATOM   5974 N N     . GLU C 1 241 ? -30.590 -7.324  -5.963  1.00 69.59  ? 213 GLU C N     1 
ATOM   5975 C CA    . GLU C 1 241 ? -29.837 -6.931  -7.148  1.00 66.16  ? 213 GLU C CA    1 
ATOM   5976 C C     . GLU C 1 241 ? -28.460 -7.585  -7.189  1.00 65.63  ? 213 GLU C C     1 
ATOM   5977 O O     . GLU C 1 241 ? -27.586 -7.136  -7.936  1.00 61.99  ? 213 GLU C O     1 
ATOM   5978 C CB    . GLU C 1 241 ? -29.706 -5.408  -7.217  1.00 63.98  ? 213 GLU C CB    1 
ATOM   5979 C CG    . GLU C 1 241 ? -31.025 -4.684  -7.438  1.00 62.61  ? 213 GLU C CG    1 
ATOM   5980 C CD    . GLU C 1 241 ? -31.702 -5.088  -8.733  1.00 69.46  ? 213 GLU C CD    1 
ATOM   5981 O OE1   . GLU C 1 241 ? -31.001 -5.216  -9.759  1.00 69.54  ? 213 GLU C OE1   1 
ATOM   5982 O OE2   . GLU C 1 241 ? -32.935 -5.281  -8.723  1.00 75.78  ? 213 GLU C OE2   1 
ATOM   5983 N N     . GLY C 1 242 ? -28.249 -8.633  -6.397  1.00 69.38  ? 214 GLY C N     1 
ATOM   5984 C CA    . GLY C 1 242 ? -26.991 -9.352  -6.407  1.00 72.14  ? 214 GLY C CA    1 
ATOM   5985 C C     . GLY C 1 242 ? -25.936 -8.837  -5.458  1.00 70.68  ? 214 GLY C C     1 
ATOM   5986 O O     . GLY C 1 242 ? -24.756 -9.163  -5.635  1.00 72.32  ? 214 GLY C O     1 
ATOM   5987 N N     . PHE C 1 243 ? -26.313 -8.050  -4.457  1.00 71.02  ? 215 PHE C N     1 
ATOM   5988 C CA    . PHE C 1 243 ? -25.363 -7.491  -3.508  1.00 72.87  ? 215 PHE C CA    1 
ATOM   5989 C C     . PHE C 1 243 ? -25.340 -8.307  -2.221  1.00 78.05  ? 215 PHE C C     1 
ATOM   5990 O O     . PHE C 1 243 ? -26.303 -8.993  -1.869  1.00 77.73  ? 215 PHE C O     1 
ATOM   5991 C CB    . PHE C 1 243 ? -25.702 -6.033  -3.188  1.00 70.94  ? 215 PHE C CB    1 
ATOM   5992 C CG    . PHE C 1 243 ? -25.248 -5.060  -4.238  1.00 68.05  ? 215 PHE C CG    1 
ATOM   5993 C CD1   . PHE C 1 243 ? -23.948 -4.583  -4.243  1.00 66.12  ? 215 PHE C CD1   1 
ATOM   5994 C CD2   . PHE C 1 243 ? -26.123 -4.618  -5.215  1.00 66.60  ? 215 PHE C CD2   1 
ATOM   5995 C CE1   . PHE C 1 243 ? -23.528 -3.687  -5.206  1.00 61.96  ? 215 PHE C CE1   1 
ATOM   5996 C CE2   . PHE C 1 243 ? -25.709 -3.721  -6.182  1.00 60.44  ? 215 PHE C CE2   1 
ATOM   5997 C CZ    . PHE C 1 243 ? -24.410 -3.255  -6.177  1.00 58.24  ? 215 PHE C CZ    1 
ATOM   5998 N N     . GLN C 1 244 ? -24.214 -8.220  -1.519  1.00 78.40  ? 216 GLN C N     1 
ATOM   5999 C CA    . GLN C 1 244 ? -24.033 -8.844  -0.212  1.00 82.31  ? 216 GLN C CA    1 
ATOM   6000 C C     . GLN C 1 244 ? -23.937 -7.721  0.816   1.00 79.51  ? 216 GLN C C     1 
ATOM   6001 O O     . GLN C 1 244 ? -22.878 -7.110  0.984   1.00 79.37  ? 216 GLN C O     1 
ATOM   6002 C CB    . GLN C 1 244 ? -22.790 -9.730  -0.193  1.00 84.43  ? 216 GLN C CB    1 
ATOM   6003 C CG    . GLN C 1 244 ? -22.516 -10.388 1.151   1.00 88.82  ? 216 GLN C CG    1 
ATOM   6004 C CD    . GLN C 1 244 ? -21.159 -11.064 1.201   1.00 88.42  ? 216 GLN C CD    1 
ATOM   6005 O OE1   . GLN C 1 244 ? -20.264 -10.745 0.418   1.00 88.80  ? 216 GLN C OE1   1 
ATOM   6006 N NE2   . GLN C 1 244 ? -20.999 -12.003 2.127   1.00 90.04  ? 216 GLN C NE2   1 
ATOM   6007 N N     . VAL C 1 245 ? -25.050 -7.446  1.495   1.00 74.11  ? 217 VAL C N     1 
ATOM   6008 C CA    . VAL C 1 245 ? -25.104 -6.374  2.483   1.00 74.13  ? 217 VAL C CA    1 
ATOM   6009 C C     . VAL C 1 245 ? -24.219 -6.742  3.666   1.00 72.64  ? 217 VAL C C     1 
ATOM   6010 O O     . VAL C 1 245 ? -24.588 -7.581  4.496   1.00 77.33  ? 217 VAL C O     1 
ATOM   6011 C CB    . VAL C 1 245 ? -26.550 -6.100  2.933   1.00 72.16  ? 217 VAL C CB    1 
ATOM   6012 C CG1   . VAL C 1 245 ? -26.576 -5.029  4.015   1.00 68.75  ? 217 VAL C CG1   1 
ATOM   6013 C CG2   . VAL C 1 245 ? -27.406 -5.689  1.745   1.00 68.22  ? 217 VAL C CG2   1 
ATOM   6014 N N     . LEU C 1 246 ? -23.042 -6.119  3.747   1.00 71.67  ? 218 LEU C N     1 
ATOM   6015 C CA    . LEU C 1 246 ? -22.100 -6.422  4.816   1.00 72.44  ? 218 LEU C CA    1 
ATOM   6016 C C     . LEU C 1 246 ? -22.426 -5.697  6.114   1.00 75.00  ? 218 LEU C C     1 
ATOM   6017 O O     . LEU C 1 246 ? -22.022 -6.162  7.184   1.00 82.12  ? 218 LEU C O     1 
ATOM   6018 C CB    . LEU C 1 246 ? -20.675 -6.062  4.382   1.00 67.23  ? 218 LEU C CB    1 
ATOM   6019 C CG    . LEU C 1 246 ? -20.131 -6.745  3.127   1.00 69.98  ? 218 LEU C CG    1 
ATOM   6020 C CD1   . LEU C 1 246 ? -18.714 -6.274  2.837   1.00 65.96  ? 218 LEU C CD1   1 
ATOM   6021 C CD2   . LEU C 1 246 ? -20.180 -8.257  3.269   1.00 76.30  ? 218 LEU C CD2   1 
ATOM   6022 N N     . ARG C 1 247 ? -23.147 -4.580  6.044   1.00 74.73  ? 219 ARG C N     1 
ATOM   6023 C CA    . ARG C 1 247 ? -23.417 -3.758  7.216   1.00 76.34  ? 219 ARG C CA    1 
ATOM   6024 C C     . ARG C 1 247 ? -24.457 -2.714  6.841   1.00 72.05  ? 219 ARG C C     1 
ATOM   6025 O O     . ARG C 1 247 ? -24.377 -2.118  5.765   1.00 70.19  ? 219 ARG C O     1 
ATOM   6026 C CB    . ARG C 1 247 ? -22.130 -3.088  7.716   1.00 72.17  ? 219 ARG C CB    1 
ATOM   6027 C CG    . ARG C 1 247 ? -22.247 -2.351  9.036   1.00 75.57  ? 219 ARG C CG    1 
ATOM   6028 C CD    . ARG C 1 247 ? -20.866 -1.918  9.499   1.00 80.15  ? 219 ARG C CD    1 
ATOM   6029 N NE    . ARG C 1 247 ? -20.898 -1.061  10.678  1.00 93.17  ? 219 ARG C NE    1 
ATOM   6030 C CZ    . ARG C 1 247 ? -19.976 -1.073  11.632  1.00 91.80  ? 219 ARG C CZ    1 
ATOM   6031 N NH1   . ARG C 1 247 ? -18.937 -1.890  11.578  1.00 86.70  ? 219 ARG C NH1   1 
ATOM   6032 N NH2   . ARG C 1 247 ? -20.100 -0.243  12.664  1.00 92.37  ? 219 ARG C NH2   1 
ATOM   6033 N N     . CYS C 1 248 ? -25.431 -2.504  7.725   1.00 68.23  ? 220 CYS C N     1 
ATOM   6034 C CA    . CYS C 1 248 ? -26.512 -1.562  7.451   1.00 69.65  ? 220 CYS C CA    1 
ATOM   6035 C C     . CYS C 1 248 ? -27.078 -1.059  8.770   1.00 74.36  ? 220 CYS C C     1 
ATOM   6036 O O     . CYS C 1 248 ? -27.518 -1.860  9.600   1.00 80.30  ? 220 CYS C O     1 
ATOM   6037 C CB    . CYS C 1 248 ? -27.608 -2.215  6.606   1.00 68.06  ? 220 CYS C CB    1 
ATOM   6038 S SG    . CYS C 1 248 ? -28.794 -1.051  5.897   1.00 72.52  ? 220 CYS C SG    1 
ATOM   6039 N N     . ASP C 1 249 ? -27.069 0.260   8.957   1.00 74.06  ? 221 ASP C N     1 
ATOM   6040 C CA    . ASP C 1 249 ? -27.548 0.876   10.185  1.00 74.83  ? 221 ASP C CA    1 
ATOM   6041 C C     . ASP C 1 249 ? -28.320 2.145   9.850   1.00 69.80  ? 221 ASP C C     1 
ATOM   6042 O O     . ASP C 1 249 ? -28.191 2.707   8.760   1.00 69.19  ? 221 ASP C O     1 
ATOM   6043 C CB    . ASP C 1 249 ? -26.395 1.204   11.144  1.00 78.18  ? 221 ASP C CB    1 
ATOM   6044 C CG    . ASP C 1 249 ? -25.469 0.025   11.370  1.00 84.82  ? 221 ASP C CG    1 
ATOM   6045 O OD1   . ASP C 1 249 ? -25.915 -0.977  11.969  1.00 88.35  ? 221 ASP C OD1   1 
ATOM   6046 O OD2   . ASP C 1 249 ? -24.296 0.099   10.946  1.00 85.06  ? 221 ASP C OD2   1 
ATOM   6047 N N     . LEU C 1 250 ? -29.128 2.590   10.810  1.00 69.81  ? 222 LEU C N     1 
ATOM   6048 C CA    . LEU C 1 250 ? -29.896 3.823   10.693  1.00 62.98  ? 222 LEU C CA    1 
ATOM   6049 C C     . LEU C 1 250 ? -29.636 4.678   11.922  1.00 59.83  ? 222 LEU C C     1 
ATOM   6050 O O     . LEU C 1 250 ? -29.722 4.188   13.052  1.00 60.96  ? 222 LEU C O     1 
ATOM   6051 C CB    . LEU C 1 250 ? -31.395 3.539   10.553  1.00 58.86  ? 222 LEU C CB    1 
ATOM   6052 C CG    . LEU C 1 250 ? -32.345 4.738   10.529  1.00 58.38  ? 222 LEU C CG    1 
ATOM   6053 C CD1   . LEU C 1 250 ? -32.111 5.594   9.295   1.00 58.81  ? 222 LEU C CD1   1 
ATOM   6054 C CD2   . LEU C 1 250 ? -33.792 4.275   10.592  1.00 55.16  ? 222 LEU C CD2   1 
ATOM   6055 N N     . GLY C 1 251 ? -29.318 5.950   11.701  1.00 60.33  ? 223 GLY C N     1 
ATOM   6056 C CA    . GLY C 1 251 ? -29.046 6.859   12.786  1.00 63.92  ? 223 GLY C CA    1 
ATOM   6057 C C     . GLY C 1 251 ? -29.344 8.299   12.426  1.00 62.32  ? 223 GLY C C     1 
ATOM   6058 O O     . GLY C 1 251 ? -29.298 8.697   11.258  1.00 59.93  ? 223 GLY C O     1 
ATOM   6059 N N     . PRO C 1 252 ? -29.666 9.110   13.431  1.00 59.10  ? 224 PRO C N     1 
ATOM   6060 C CA    . PRO C 1 252 ? -29.894 10.536  13.182  1.00 56.11  ? 224 PRO C CA    1 
ATOM   6061 C C     . PRO C 1 252 ? -28.579 11.290  13.065  1.00 54.04  ? 224 PRO C C     1 
ATOM   6062 O O     . PRO C 1 252 ? -27.597 10.982  13.746  1.00 54.78  ? 224 PRO C O     1 
ATOM   6063 C CB    . PRO C 1 252 ? -30.686 10.980  14.416  1.00 63.00  ? 224 PRO C CB    1 
ATOM   6064 C CG    . PRO C 1 252 ? -30.167 10.091  15.503  1.00 67.16  ? 224 PRO C CG    1 
ATOM   6065 C CD    . PRO C 1 252 ? -29.856 8.759   14.850  1.00 60.71  ? 224 PRO C CD    1 
ATOM   6066 N N     . GLN C 1 253 ? -28.566 12.285  12.183  1.00 49.90  ? 225 GLN C N     1 
ATOM   6067 C CA    . GLN C 1 253 ? -27.387 13.106  11.958  1.00 52.04  ? 225 GLN C CA    1 
ATOM   6068 C C     . GLN C 1 253 ? -27.771 14.577  12.039  1.00 50.08  ? 225 GLN C C     1 
ATOM   6069 O O     . GLN C 1 253 ? -28.950 14.941  12.020  1.00 51.46  ? 225 GLN C O     1 
ATOM   6070 C CB    . GLN C 1 253 ? -26.732 12.790  10.606  1.00 57.43  ? 225 GLN C CB    1 
ATOM   6071 C CG    . GLN C 1 253 ? -26.480 11.309  10.375  1.00 59.67  ? 225 GLN C CG    1 
ATOM   6072 C CD    . GLN C 1 253 ? -25.084 10.882  10.781  1.00 63.00  ? 225 GLN C CD    1 
ATOM   6073 O OE1   . GLN C 1 253 ? -24.224 11.715  11.065  1.00 66.78  ? 225 GLN C OE1   1 
ATOM   6074 N NE2   . GLN C 1 253 ? -24.851 9.574   10.806  1.00 58.55  ? 225 GLN C NE2   1 
ATOM   6075 N N     . LYS C 1 254 ? -26.751 15.428  12.128  1.00 49.31  ? 226 LYS C N     1 
ATOM   6076 C CA    . LYS C 1 254 ? -26.944 16.856  12.329  1.00 49.16  ? 226 LYS C CA    1 
ATOM   6077 C C     . LYS C 1 254 ? -25.964 17.625  11.457  1.00 50.08  ? 226 LYS C C     1 
ATOM   6078 O O     . LYS C 1 254 ? -24.772 17.308  11.434  1.00 50.18  ? 226 LYS C O     1 
ATOM   6079 C CB    . LYS C 1 254 ? -26.746 17.230  13.802  1.00 54.22  ? 226 LYS C CB    1 
ATOM   6080 C CG    . LYS C 1 254 ? -27.980 17.047  14.666  1.00 54.28  ? 226 LYS C CG    1 
ATOM   6081 C CD    . LYS C 1 254 ? -27.886 17.877  15.935  1.00 62.23  ? 226 LYS C CD    1 
ATOM   6082 C CE    . LYS C 1 254 ? -27.656 17.000  17.154  1.00 61.74  ? 226 LYS C CE    1 
ATOM   6083 N NZ    . LYS C 1 254 ? -27.986 17.715  18.418  1.00 58.97  ? 226 LYS C NZ    1 
ATOM   6084 N N     . VAL C 1 255 ? -26.468 18.630  10.746  1.00 47.73  ? 227 VAL C N     1 
ATOM   6085 C CA    . VAL C 1 255 ? -25.647 19.522  9.935   1.00 48.24  ? 227 VAL C CA    1 
ATOM   6086 C C     . VAL C 1 255 ? -25.617 20.876  10.630  1.00 51.00  ? 227 VAL C C     1 
ATOM   6087 O O     . VAL C 1 255 ? -26.666 21.497  10.839  1.00 52.99  ? 227 VAL C O     1 
ATOM   6088 C CB    . VAL C 1 255 ? -26.183 19.647  8.502   1.00 45.72  ? 227 VAL C CB    1 
ATOM   6089 C CG1   . VAL C 1 255 ? -25.105 20.202  7.583   1.00 48.03  ? 227 VAL C CG1   1 
ATOM   6090 C CG2   . VAL C 1 255 ? -26.679 18.301  8.002   1.00 44.01  ? 227 VAL C CG2   1 
ATOM   6091 N N     . PHE C 1 256 ? -24.420 21.334  10.982  1.00 47.90  ? 228 PHE C N     1 
ATOM   6092 C CA    . PHE C 1 256 ? -24.244 22.540  11.778  1.00 47.83  ? 228 PHE C CA    1 
ATOM   6093 C C     . PHE C 1 256 ? -23.822 23.710  10.897  1.00 47.02  ? 228 PHE C C     1 
ATOM   6094 O O     . PHE C 1 256 ? -23.031 23.546  9.964   1.00 47.44  ? 228 PHE C O     1 
ATOM   6095 C CB    . PHE C 1 256 ? -23.204 22.308  12.876  1.00 49.41  ? 228 PHE C CB    1 
ATOM   6096 C CG    . PHE C 1 256 ? -22.654 23.571  13.470  1.00 47.67  ? 228 PHE C CG    1 
ATOM   6097 C CD1   . PHE C 1 256 ? -23.449 24.383  14.262  1.00 52.26  ? 228 PHE C CD1   1 
ATOM   6098 C CD2   . PHE C 1 256 ? -21.341 23.945  13.241  1.00 44.31  ? 228 PHE C CD2   1 
ATOM   6099 C CE1   . PHE C 1 256 ? -22.945 25.545  14.810  1.00 52.63  ? 228 PHE C CE1   1 
ATOM   6100 C CE2   . PHE C 1 256 ? -20.832 25.106  13.787  1.00 45.79  ? 228 PHE C CE2   1 
ATOM   6101 C CZ    . PHE C 1 256 ? -21.635 25.907  14.573  1.00 50.12  ? 228 PHE C CZ    1 
ATOM   6102 N N     . PHE C 1 257 ? -24.359 24.892  11.200  1.00 49.49  ? 229 PHE C N     1 
ATOM   6103 C CA    . PHE C 1 257 ? -24.008 26.119  10.501  1.00 50.17  ? 229 PHE C CA    1 
ATOM   6104 C C     . PHE C 1 257 ? -23.730 27.204  11.536  1.00 47.05  ? 229 PHE C C     1 
ATOM   6105 O O     . PHE C 1 257 ? -24.569 27.446  12.421  1.00 44.82  ? 229 PHE C O     1 
ATOM   6106 C CB    . PHE C 1 257 ? -25.118 26.563  9.536   1.00 53.08  ? 229 PHE C CB    1 
ATOM   6107 C CG    . PHE C 1 257 ? -25.599 25.472  8.620   1.00 51.44  ? 229 PHE C CG    1 
ATOM   6108 C CD1   . PHE C 1 257 ? -26.543 24.552  9.044   1.00 51.87  ? 229 PHE C CD1   1 
ATOM   6109 C CD2   . PHE C 1 257 ? -25.094 25.362  7.335   1.00 51.01  ? 229 PHE C CD2   1 
ATOM   6110 C CE1   . PHE C 1 257 ? -26.979 23.547  8.201   1.00 48.47  ? 229 PHE C CE1   1 
ATOM   6111 C CE2   . PHE C 1 257 ? -25.526 24.360  6.488   1.00 48.13  ? 229 PHE C CE2   1 
ATOM   6112 C CZ    . PHE C 1 257 ? -26.470 23.452  6.921   1.00 44.62  ? 229 PHE C CZ    1 
ATOM   6113 N N     . PRO C 1 258 ? -22.579 27.878  11.462  1.00 46.45  ? 230 PRO C N     1 
ATOM   6114 C CA    . PRO C 1 258 ? -22.229 28.826  12.533  1.00 49.78  ? 230 PRO C CA    1 
ATOM   6115 C C     . PRO C 1 258 ? -23.073 30.088  12.531  1.00 52.50  ? 230 PRO C C     1 
ATOM   6116 O O     . PRO C 1 258 ? -23.414 30.594  13.608  1.00 59.75  ? 230 PRO C O     1 
ATOM   6117 C CB    . PRO C 1 258 ? -20.749 29.125  12.260  1.00 48.02  ? 230 PRO C CB    1 
ATOM   6118 C CG    . PRO C 1 258 ? -20.574 28.872  10.801  1.00 44.87  ? 230 PRO C CG    1 
ATOM   6119 C CD    . PRO C 1 258 ? -21.521 27.763  10.443  1.00 46.30  ? 230 PRO C CD    1 
ATOM   6120 N N     . THR C 1 259 ? -23.418 30.618  11.363  1.00 47.55  ? 231 THR C N     1 
ATOM   6121 C CA    . THR C 1 259 ? -24.194 31.846  11.278  1.00 51.47  ? 231 THR C CA    1 
ATOM   6122 C C     . THR C 1 259 ? -25.655 31.539  10.971  1.00 52.88  ? 231 THR C C     1 
ATOM   6123 O O     . THR C 1 259 ? -26.042 30.399  10.706  1.00 53.50  ? 231 THR C O     1 
ATOM   6124 C CB    . THR C 1 259 ? -23.621 32.784  10.211  1.00 51.68  ? 231 THR C CB    1 
ATOM   6125 O OG1   . THR C 1 259 ? -23.968 32.296  8.910   1.00 56.19  ? 231 THR C OG1   1 
ATOM   6126 C CG2   . THR C 1 259 ? -22.111 32.862  10.331  1.00 51.10  ? 231 THR C CG2   1 
ATOM   6127 N N     . ALA C 1 260 ? -26.472 32.592  11.008  1.00 57.21  ? 232 ALA C N     1 
ATOM   6128 C CA    . ALA C 1 260 ? -27.894 32.440  10.728  1.00 58.83  ? 232 ALA C CA    1 
ATOM   6129 C C     . ALA C 1 260 ? -28.164 32.309  9.235   1.00 57.86  ? 232 ALA C C     1 
ATOM   6130 O O     . ALA C 1 260 ? -29.003 31.500  8.824   1.00 57.23  ? 232 ALA C O     1 
ATOM   6131 C CB    . ALA C 1 260 ? -28.671 33.624  11.304  1.00 64.70  ? 232 ALA C CB    1 
ATOM   6132 N N     . GLU C 1 261 ? -27.459 33.085  8.409   1.00 57.34  ? 233 GLU C N     1 
ATOM   6133 C CA    . GLU C 1 261 ? -27.796 33.131  6.992   1.00 57.93  ? 233 GLU C CA    1 
ATOM   6134 C C     . GLU C 1 261 ? -27.188 31.970  6.213   1.00 57.52  ? 233 GLU C C     1 
ATOM   6135 O O     . GLU C 1 261 ? -27.782 31.522  5.226   1.00 61.75  ? 233 GLU C O     1 
ATOM   6136 C CB    . GLU C 1 261 ? -27.366 34.472  6.392   1.00 60.58  ? 233 GLU C CB    1 
ATOM   6137 C CG    . GLU C 1 261 ? -27.890 34.699  4.984   1.00 69.68  ? 233 GLU C CG    1 
ATOM   6138 C CD    . GLU C 1 261 ? -27.771 36.139  4.532   1.00 79.43  ? 233 GLU C CD    1 
ATOM   6139 O OE1   . GLU C 1 261 ? -27.418 36.997  5.368   1.00 90.21  ? 233 GLU C OE1   1 
ATOM   6140 O OE2   . GLU C 1 261 ? -28.036 36.414  3.342   1.00 69.35  ? 233 GLU C OE2   1 
ATOM   6141 N N     . THR C 1 262 ? -26.022 31.465  6.627   1.00 54.78  ? 234 THR C N     1 
ATOM   6142 C CA    . THR C 1 262 ? -25.508 30.243  6.013   1.00 51.68  ? 234 THR C CA    1 
ATOM   6143 C C     . THR C 1 262 ? -26.450 29.072  6.249   1.00 53.60  ? 234 THR C C     1 
ATOM   6144 O O     . THR C 1 262 ? -26.582 28.196  5.387   1.00 53.36  ? 234 THR C O     1 
ATOM   6145 C CB    . THR C 1 262 ? -24.115 29.908  6.546   1.00 43.54  ? 234 THR C CB    1 
ATOM   6146 O OG1   . THR C 1 262 ? -24.160 29.781  7.973   1.00 46.12  ? 234 THR C OG1   1 
ATOM   6147 C CG2   . THR C 1 262 ? -23.123 30.984  6.158   1.00 43.28  ? 234 THR C CG2   1 
ATOM   6148 N N     . HIS C 1 263 ? -27.108 29.040  7.409   1.00 55.25  ? 235 HIS C N     1 
ATOM   6149 C CA    . HIS C 1 263 ? -28.170 28.068  7.635   1.00 51.70  ? 235 HIS C CA    1 
ATOM   6150 C C     . HIS C 1 263 ? -29.352 28.315  6.708   1.00 53.85  ? 235 HIS C C     1 
ATOM   6151 O O     . HIS C 1 263 ? -30.016 27.364  6.280   1.00 52.89  ? 235 HIS C O     1 
ATOM   6152 C CB    . HIS C 1 263 ? -28.616 28.124  9.096   1.00 53.84  ? 235 HIS C CB    1 
ATOM   6153 C CG    . HIS C 1 263 ? -29.781 27.240  9.410   1.00 52.44  ? 235 HIS C CG    1 
ATOM   6154 N ND1   . HIS C 1 263 ? -29.740 25.871  9.259   1.00 48.47  ? 235 HIS C ND1   1 
ATOM   6155 C CD2   . HIS C 1 263 ? -31.021 27.530  9.871   1.00 52.65  ? 235 HIS C CD2   1 
ATOM   6156 C CE1   . HIS C 1 263 ? -30.903 25.356  9.613   1.00 53.03  ? 235 HIS C CE1   1 
ATOM   6157 N NE2   . HIS C 1 263 ? -31.699 26.342  9.987   1.00 56.44  ? 235 HIS C NE2   1 
ATOM   6158 N N     . ARG C 1 264 ? -29.621 29.580  6.380   1.00 56.37  ? 236 ARG C N     1 
ATOM   6159 C CA    . ARG C 1 264 ? -30.731 29.915  5.494   1.00 52.55  ? 236 ARG C CA    1 
ATOM   6160 C C     . ARG C 1 264 ? -30.342 29.761  4.028   1.00 52.88  ? 236 ARG C C     1 
ATOM   6161 O O     . ARG C 1 264 ? -31.086 29.166  3.242   1.00 54.83  ? 236 ARG C O     1 
ATOM   6162 C CB    . ARG C 1 264 ? -31.208 31.342  5.773   1.00 56.76  ? 236 ARG C CB    1 
ATOM   6163 C CG    . ARG C 1 264 ? -32.480 31.730  5.039   1.00 58.08  ? 236 ARG C CG    1 
ATOM   6164 C CD    . ARG C 1 264 ? -32.959 33.107  5.466   1.00 60.68  ? 236 ARG C CD    1 
ATOM   6165 N NE    . ARG C 1 264 ? -34.170 33.510  4.761   1.00 67.56  ? 236 ARG C NE    1 
ATOM   6166 C CZ    . ARG C 1 264 ? -34.186 34.037  3.544   1.00 69.05  ? 236 ARG C CZ    1 
ATOM   6167 N NH1   . ARG C 1 264 ? -33.070 34.237  2.861   1.00 69.84  ? 236 ARG C NH1   1 
ATOM   6168 N NH2   . ARG C 1 264 ? -35.352 34.372  2.998   1.00 64.50  ? 236 ARG C NH2   1 
ATOM   6169 N N     . GLU C 1 265 ? -29.179 30.295  3.641   1.00 52.77  ? 237 GLU C N     1 
ATOM   6170 C CA    . GLU C 1 265 ? -28.769 30.237  2.241   1.00 51.30  ? 237 GLU C CA    1 
ATOM   6171 C C     . GLU C 1 265 ? -28.509 28.808  1.785   1.00 50.31  ? 237 GLU C C     1 
ATOM   6172 O O     . GLU C 1 265 ? -28.635 28.510  0.591   1.00 48.98  ? 237 GLU C O     1 
ATOM   6173 C CB    . GLU C 1 265 ? -27.525 31.096  2.014   1.00 49.44  ? 237 GLU C CB    1 
ATOM   6174 C CG    . GLU C 1 265 ? -27.751 32.586  2.186   1.00 56.56  ? 237 GLU C CG    1 
ATOM   6175 C CD    . GLU C 1 265 ? -28.849 33.123  1.289   1.00 66.42  ? 237 GLU C CD    1 
ATOM   6176 O OE1   . GLU C 1 265 ? -28.924 32.698  0.116   1.00 65.73  ? 237 GLU C OE1   1 
ATOM   6177 O OE2   . GLU C 1 265 ? -29.640 33.969  1.758   1.00 70.97  ? 237 GLU C OE2   1 
ATOM   6178 N N     . PHE C 1 266 ? -28.143 27.914  2.706   1.00 49.65  ? 238 PHE C N     1 
ATOM   6179 C CA    . PHE C 1 266 ? -27.968 26.515  2.332   1.00 46.69  ? 238 PHE C CA    1 
ATOM   6180 C C     . PHE C 1 266 ? -29.302 25.868  1.987   1.00 47.60  ? 238 PHE C C     1 
ATOM   6181 O O     . PHE C 1 266 ? -29.402 25.126  1.003   1.00 49.78  ? 238 PHE C O     1 
ATOM   6182 C CB    . PHE C 1 266 ? -27.279 25.744  3.457   1.00 44.65  ? 238 PHE C CB    1 
ATOM   6183 C CG    . PHE C 1 266 ? -27.060 24.291  3.145   1.00 43.98  ? 238 PHE C CG    1 
ATOM   6184 C CD1   . PHE C 1 266 ? -26.002 23.892  2.344   1.00 43.74  ? 238 PHE C CD1   1 
ATOM   6185 C CD2   . PHE C 1 266 ? -27.916 23.324  3.646   1.00 44.37  ? 238 PHE C CD2   1 
ATOM   6186 C CE1   . PHE C 1 266 ? -25.800 22.557  2.053   1.00 42.52  ? 238 PHE C CE1   1 
ATOM   6187 C CE2   . PHE C 1 266 ? -27.719 21.988  3.358   1.00 43.85  ? 238 PHE C CE2   1 
ATOM   6188 C CZ    . PHE C 1 266 ? -26.660 21.604  2.561   1.00 42.92  ? 238 PHE C CZ    1 
ATOM   6189 N N     . LEU C 1 267 ? -30.339 26.139  2.783   1.00 47.82  ? 239 LEU C N     1 
ATOM   6190 C CA    . LEU C 1 267 ? -31.654 25.570  2.515   1.00 49.00  ? 239 LEU C CA    1 
ATOM   6191 C C     . LEU C 1 267 ? -32.254 26.086  1.214   1.00 50.08  ? 239 LEU C C     1 
ATOM   6192 O O     . LEU C 1 267 ? -33.156 25.444  0.666   1.00 50.94  ? 239 LEU C O     1 
ATOM   6193 C CB    . LEU C 1 267 ? -32.596 25.855  3.685   1.00 49.90  ? 239 LEU C CB    1 
ATOM   6194 C CG    . LEU C 1 267 ? -32.364 24.979  4.918   1.00 49.17  ? 239 LEU C CG    1 
ATOM   6195 C CD1   . LEU C 1 267 ? -33.188 25.462  6.100   1.00 50.09  ? 239 LEU C CD1   1 
ATOM   6196 C CD2   . LEU C 1 267 ? -32.678 23.526  4.601   1.00 49.05  ? 239 LEU C CD2   1 
ATOM   6197 N N     . LYS C 1 268 ? -31.778 27.229  0.710   1.00 51.37  ? 240 LYS C N     1 
ATOM   6198 C CA    . LYS C 1 268 ? -32.191 27.680  -0.615  1.00 51.29  ? 240 LYS C CA    1 
ATOM   6199 C C     . LYS C 1 268 ? -31.761 26.689  -1.688  1.00 50.50  ? 240 LYS C C     1 
ATOM   6200 O O     . LYS C 1 268 ? -32.502 26.437  -2.645  1.00 51.47  ? 240 LYS C O     1 
ATOM   6201 C CB    . LYS C 1 268 ? -31.606 29.061  -0.911  1.00 53.61  ? 240 LYS C CB    1 
ATOM   6202 C CG    . LYS C 1 268 ? -32.457 30.230  -0.450  1.00 55.45  ? 240 LYS C CG    1 
ATOM   6203 C CD    . LYS C 1 268 ? -31.876 31.550  -0.932  1.00 59.18  ? 240 LYS C CD    1 
ATOM   6204 C CE    . LYS C 1 268 ? -32.739 32.726  -0.507  1.00 63.95  ? 240 LYS C CE    1 
ATOM   6205 N NZ    . LYS C 1 268 ? -32.157 34.024  -0.946  1.00 66.93  ? 240 LYS C NZ    1 
ATOM   6206 N N     . SER C 1 269 ? -30.566 26.114  -1.543  1.00 49.01  ? 241 SER C N     1 
ATOM   6207 C CA    . SER C 1 269 ? -30.039 25.226  -2.574  1.00 48.48  ? 241 SER C CA    1 
ATOM   6208 C C     . SER C 1 269 ? -30.735 23.870  -2.555  1.00 49.09  ? 241 SER C C     1 
ATOM   6209 O O     . SER C 1 269 ? -31.035 23.307  -3.614  1.00 57.90  ? 241 SER C O     1 
ATOM   6210 C CB    . SER C 1 269 ? -28.531 25.058  -2.396  1.00 47.45  ? 241 SER C CB    1 
ATOM   6211 O OG    . SER C 1 269 ? -28.240 24.154  -1.344  1.00 51.32  ? 241 SER C OG    1 
ATOM   6212 N N     . VAL C 1 270 ? -31.007 23.334  -1.366  1.00 48.52  ? 242 VAL C N     1 
ATOM   6213 C CA    . VAL C 1 270 ? -31.558 21.988  -1.240  1.00 48.69  ? 242 VAL C CA    1 
ATOM   6214 C C     . VAL C 1 270 ? -33.079 22.017  -1.343  1.00 51.42  ? 242 VAL C C     1 
ATOM   6215 O O     . VAL C 1 270 ? -33.754 21.041  -0.994  1.00 54.71  ? 242 VAL C O     1 
ATOM   6216 C CB    . VAL C 1 270 ? -31.104 21.329  0.075   1.00 49.96  ? 242 VAL C CB    1 
ATOM   6217 C CG1   . VAL C 1 270 ? -29.586 21.346  0.175   1.00 46.95  ? 242 VAL C CG1   1 
ATOM   6218 C CG2   . VAL C 1 270 ? -31.724 22.036  1.269   1.00 50.00  ? 242 VAL C CG2   1 
ATOM   6219 N N     . CYS C 1 271 ? -33.630 23.128  -1.827  1.00 54.76  ? 243 CYS C N     1 
ATOM   6220 C CA    . CYS C 1 271 ? -35.062 23.240  -2.084  1.00 58.34  ? 243 CYS C CA    1 
ATOM   6221 C C     . CYS C 1 271 ? -35.315 22.846  -3.535  1.00 64.34  ? 243 CYS C C     1 
ATOM   6222 O O     . CYS C 1 271 ? -34.970 23.592  -4.458  1.00 67.12  ? 243 CYS C O     1 
ATOM   6223 C CB    . CYS C 1 271 ? -35.559 24.653  -1.795  1.00 61.38  ? 243 CYS C CB    1 
ATOM   6224 S SG    . CYS C 1 271 ? -37.349 24.855  -1.946  1.00 76.50  ? 243 CYS C SG    1 
ATOM   6225 N N     . ALA C 1 272 ? -35.922 21.677  -3.737  1.00 68.73  ? 244 ALA C N     1 
ATOM   6226 C CA    . ALA C 1 272 ? -36.024 21.085  -5.065  1.00 65.37  ? 244 ALA C CA    1 
ATOM   6227 C C     . ALA C 1 272 ? -37.155 21.659  -5.910  1.00 67.41  ? 244 ALA C C     1 
ATOM   6228 O O     . ALA C 1 272 ? -37.248 21.316  -7.093  1.00 70.64  ? 244 ALA C O     1 
ATOM   6229 C CB    . ALA C 1 272 ? -36.200 19.569  -4.947  1.00 64.21  ? 244 ALA C CB    1 
ATOM   6230 N N     . PHE C 1 273 ? -38.008 22.515  -5.351  1.00 69.61  ? 245 PHE C N     1 
ATOM   6231 C CA    . PHE C 1 273 ? -39.151 23.052  -6.080  1.00 73.12  ? 245 PHE C CA    1 
ATOM   6232 C C     . PHE C 1 273 ? -38.964 24.495  -6.528  1.00 75.03  ? 245 PHE C C     1 
ATOM   6233 O O     . PHE C 1 273 ? -39.844 25.034  -7.206  1.00 77.70  ? 245 PHE C O     1 
ATOM   6234 C CB    . PHE C 1 273 ? -40.420 22.954  -5.228  1.00 72.25  ? 245 PHE C CB    1 
ATOM   6235 C CG    . PHE C 1 273 ? -41.045 21.590  -5.215  1.00 74.13  ? 245 PHE C CG    1 
ATOM   6236 C CD1   . PHE C 1 273 ? -41.891 21.193  -6.237  1.00 78.00  ? 245 PHE C CD1   1 
ATOM   6237 C CD2   . PHE C 1 273 ? -40.802 20.712  -4.173  1.00 74.33  ? 245 PHE C CD2   1 
ATOM   6238 C CE1   . PHE C 1 273 ? -42.473 19.941  -6.227  1.00 82.85  ? 245 PHE C CE1   1 
ATOM   6239 C CE2   . PHE C 1 273 ? -41.383 19.459  -4.155  1.00 75.91  ? 245 PHE C CE2   1 
ATOM   6240 C CZ    . PHE C 1 273 ? -42.220 19.073  -5.184  1.00 81.09  ? 245 PHE C CZ    1 
ATOM   6241 N N     . LEU C 1 274 ? -37.848 25.136  -6.171  1.00 74.98  ? 246 LEU C N     1 
ATOM   6242 C CA    . LEU C 1 274 ? -37.694 26.555  -6.476  1.00 78.11  ? 246 LEU C CA    1 
ATOM   6243 C C     . LEU C 1 274 ? -37.517 26.807  -7.969  1.00 81.70  ? 246 LEU C C     1 
ATOM   6244 O O     . LEU C 1 274 ? -37.865 27.889  -8.456  1.00 81.40  ? 246 LEU C O     1 
ATOM   6245 C CB    . LEU C 1 274 ? -36.516 27.138  -5.697  1.00 74.18  ? 246 LEU C CB    1 
ATOM   6246 C CG    . LEU C 1 274 ? -36.826 27.553  -4.258  1.00 72.08  ? 246 LEU C CG    1 
ATOM   6247 C CD1   . LEU C 1 274 ? -35.569 28.034  -3.550  1.00 71.83  ? 246 LEU C CD1   1 
ATOM   6248 C CD2   . LEU C 1 274 ? -37.910 28.620  -4.227  1.00 74.52  ? 246 LEU C CD2   1 
ATOM   6249 N N     . TYR C 1 275 ? -36.984 25.832  -8.710  1.00 81.52  ? 247 TYR C N     1 
ATOM   6250 C CA    . TYR C 1 275 ? -36.780 26.024  -10.142 1.00 81.77  ? 247 TYR C CA    1 
ATOM   6251 C C     . TYR C 1 275 ? -38.094 26.086  -10.912 1.00 82.75  ? 247 TYR C C     1 
ATOM   6252 O O     . TYR C 1 275 ? -38.110 26.577  -12.046 1.00 81.24  ? 247 TYR C O     1 
ATOM   6253 C CB    . TYR C 1 275 ? -35.884 24.913  -10.701 1.00 78.80  ? 247 TYR C CB    1 
ATOM   6254 C CG    . TYR C 1 275 ? -36.590 23.604  -10.996 1.00 80.42  ? 247 TYR C CG    1 
ATOM   6255 C CD1   . TYR C 1 275 ? -36.761 22.646  -10.006 1.00 79.40  ? 247 TYR C CD1   1 
ATOM   6256 C CD2   . TYR C 1 275 ? -37.063 23.318  -12.272 1.00 81.81  ? 247 TYR C CD2   1 
ATOM   6257 C CE1   . TYR C 1 275 ? -37.397 21.446  -10.273 1.00 79.84  ? 247 TYR C CE1   1 
ATOM   6258 C CE2   . TYR C 1 275 ? -37.702 22.123  -12.547 1.00 80.67  ? 247 TYR C CE2   1 
ATOM   6259 C CZ    . TYR C 1 275 ? -37.865 21.191  -11.545 1.00 81.39  ? 247 TYR C CZ    1 
ATOM   6260 O OH    . TYR C 1 275 ? -38.499 20.000  -11.816 1.00 82.00  ? 247 TYR C OH    1 
ATOM   6261 N N     . ARG C 1 276 ? -39.191 25.611  -10.322 1.00 82.96  ? 248 ARG C N     1 
ATOM   6262 C CA    . ARG C 1 276 ? -40.491 25.633  -10.979 1.00 83.27  ? 248 ARG C CA    1 
ATOM   6263 C C     . ARG C 1 276 ? -41.288 26.897  -10.691 1.00 88.70  ? 248 ARG C C     1 
ATOM   6264 O O     . ARG C 1 276 ? -42.235 27.195  -11.427 1.00 93.29  ? 248 ARG C O     1 
ATOM   6265 C CB    . ARG C 1 276 ? -41.322 24.421  -10.549 1.00 80.32  ? 248 ARG C CB    1 
ATOM   6266 C CG    . ARG C 1 276 ? -40.774 23.088  -11.013 1.00 77.75  ? 248 ARG C CG    1 
ATOM   6267 C CD    . ARG C 1 276 ? -41.688 21.953  -10.590 1.00 75.98  ? 248 ARG C CD    1 
ATOM   6268 N NE    . ARG C 1 276 ? -41.205 20.661  -11.061 1.00 82.32  ? 248 ARG C NE    1 
ATOM   6269 C CZ    . ARG C 1 276 ? -41.860 19.518  -10.913 1.00 87.72  ? 248 ARG C CZ    1 
ATOM   6270 N NH1   . ARG C 1 276 ? -43.026 19.466  -10.291 1.00 88.85  ? 248 ARG C NH1   1 
ATOM   6271 N NH2   . ARG C 1 276 ? -41.331 18.400  -11.401 1.00 95.53  ? 248 ARG C NH2   1 
ATOM   6272 N N     . ILE C 1 277 ? -40.931 27.641  -9.650  1.00 87.74  ? 249 ILE C N     1 
ATOM   6273 C CA    . ILE C 1 277 ? -41.733 28.774  -9.197  1.00 87.01  ? 249 ILE C CA    1 
ATOM   6274 C C     . ILE C 1 277 ? -41.245 30.056  -9.861  1.00 91.76  ? 249 ILE C C     1 
ATOM   6275 O O     . ILE C 1 277 ? -40.034 30.310  -9.898  1.00 92.65  ? 249 ILE C O     1 
ATOM   6276 C CB    . ILE C 1 277 ? -41.690 28.896  -7.667  1.00 82.49  ? 249 ILE C CB    1 
ATOM   6277 C CG1   . ILE C 1 277 ? -42.049 27.559  -7.016  1.00 82.89  ? 249 ILE C CG1   1 
ATOM   6278 C CG2   . ILE C 1 277 ? -42.634 29.979  -7.196  1.00 87.13  ? 249 ILE C CG2   1 
ATOM   6279 C CD1   . ILE C 1 277 ? -43.410 27.034  -7.414  1.00 87.73  ? 249 ILE C CD1   1 
ATOM   6280 N N     . PRO C 1 278 ? -42.140 30.881  -10.405 1.00 92.11  ? 250 PRO C N     1 
ATOM   6281 C CA    . PRO C 1 278 ? -41.721 32.192  -10.914 1.00 89.41  ? 250 PRO C CA    1 
ATOM   6282 C C     . PRO C 1 278 ? -41.204 33.079  -9.790  1.00 92.81  ? 250 PRO C C     1 
ATOM   6283 O O     . PRO C 1 278 ? -41.425 32.822  -8.604  1.00 92.59  ? 250 PRO C O     1 
ATOM   6284 C CB    . PRO C 1 278 ? -43.001 32.764  -11.535 1.00 86.23  ? 250 PRO C CB    1 
ATOM   6285 C CG    . PRO C 1 278 ? -43.859 31.573  -11.813 1.00 90.13  ? 250 PRO C CG    1 
ATOM   6286 C CD    . PRO C 1 278 ? -43.543 30.579  -10.736 1.00 92.23  ? 250 PRO C CD    1 
ATOM   6287 N N     . GLU C 1 279 ? -40.515 34.153  -10.187 1.00 91.38  ? 251 GLU C N     1 
ATOM   6288 C CA    . GLU C 1 279 ? -39.811 34.992  -9.220  1.00 91.58  ? 251 GLU C CA    1 
ATOM   6289 C C     . GLU C 1 279 ? -40.769 35.645  -8.230  1.00 90.03  ? 251 GLU C C     1 
ATOM   6290 O O     . GLU C 1 279 ? -40.440 35.794  -7.046  1.00 93.43  ? 251 GLU C O     1 
ATOM   6291 C CB    . GLU C 1 279 ? -38.991 36.057  -9.950  1.00 88.45  ? 251 GLU C CB    1 
ATOM   6292 C CG    . GLU C 1 279 ? -38.158 36.938  -9.031  1.00 93.16  ? 251 GLU C CG    1 
ATOM   6293 C CD    . GLU C 1 279 ? -37.152 36.148  -8.214  1.00 97.83  ? 251 GLU C CD    1 
ATOM   6294 O OE1   . GLU C 1 279 ? -36.629 35.137  -8.728  1.00 96.55  ? 251 GLU C OE1   1 
ATOM   6295 O OE2   . GLU C 1 279 ? -36.889 36.535  -7.056  1.00 101.27 ? 251 GLU C OE2   1 
ATOM   6296 N N     . GLU C 1 280 ? -41.957 36.045  -8.693  1.00 87.87  ? 252 GLU C N     1 
ATOM   6297 C CA    . GLU C 1 280 ? -42.912 36.718  -7.819  1.00 91.17  ? 252 GLU C CA    1 
ATOM   6298 C C     . GLU C 1 280 ? -43.348 35.848  -6.646  1.00 97.93  ? 252 GLU C C     1 
ATOM   6299 O O     . GLU C 1 280 ? -43.751 36.384  -5.608  1.00 102.16 ? 252 GLU C O     1 
ATOM   6300 C CB    . GLU C 1 280 ? -44.139 37.156  -8.621  1.00 88.33  ? 252 GLU C CB    1 
ATOM   6301 N N     . GLN C 1 281 ? -43.280 34.525  -6.784  1.00 96.01  ? 253 GLN C N     1 
ATOM   6302 C CA    . GLN C 1 281 ? -43.653 33.611  -5.713  1.00 98.18  ? 253 GLN C CA    1 
ATOM   6303 C C     . GLN C 1 281 ? -42.475 32.814  -5.171  1.00 96.08  ? 253 GLN C C     1 
ATOM   6304 O O     . GLN C 1 281 ? -42.671 31.984  -4.277  1.00 96.49  ? 253 GLN C O     1 
ATOM   6305 C CB    . GLN C 1 281 ? -44.750 32.652  -6.191  1.00 93.95  ? 253 GLN C CB    1 
ATOM   6306 N N     . LYS C 1 282 ? -41.262 33.041  -5.682  1.00 93.40  ? 254 LYS C N     1 
ATOM   6307 C CA    . LYS C 1 282 ? -40.093 32.328  -5.173  1.00 95.24  ? 254 LYS C CA    1 
ATOM   6308 C C     . LYS C 1 282 ? -39.836 32.665  -3.709  1.00 95.24  ? 254 LYS C C     1 
ATOM   6309 O O     . LYS C 1 282 ? -39.737 31.769  -2.862  1.00 97.85  ? 254 LYS C O     1 
ATOM   6310 C CB    . LYS C 1 282 ? -38.860 32.656  -6.017  1.00 90.86  ? 254 LYS C CB    1 
ATOM   6311 C CG    . LYS C 1 282 ? -38.704 31.816  -7.273  1.00 89.68  ? 254 LYS C CG    1 
ATOM   6312 C CD    . LYS C 1 282 ? -37.360 32.083  -7.936  1.00 87.41  ? 254 LYS C CD    1 
ATOM   6313 C CE    . LYS C 1 282 ? -37.118 31.152  -9.113  1.00 84.87  ? 254 LYS C CE    1 
ATOM   6314 N NZ    . LYS C 1 282 ? -35.871 31.493  -9.851  1.00 89.81  ? 254 LYS C NZ    1 
ATOM   6315 N N     . ASP C 1 283 ? -39.719 33.957  -3.394  1.00 94.42  ? 255 ASP C N     1 
ATOM   6316 C CA    . ASP C 1 283 ? -39.442 34.360  -2.019  1.00 93.96  ? 255 ASP C CA    1 
ATOM   6317 C C     . ASP C 1 283 ? -40.591 34.003  -1.085  1.00 92.12  ? 255 ASP C C     1 
ATOM   6318 O O     . ASP C 1 283 ? -40.371 33.790  0.113   1.00 89.63  ? 255 ASP C O     1 
ATOM   6319 C CB    . ASP C 1 283 ? -39.151 35.859  -1.961  1.00 93.17  ? 255 ASP C CB    1 
ATOM   6320 C CG    . ASP C 1 283 ? -37.921 36.242  -2.760  1.00 96.10  ? 255 ASP C CG    1 
ATOM   6321 O OD1   . ASP C 1 283 ? -37.066 35.363  -2.995  1.00 97.89  ? 255 ASP C OD1   1 
ATOM   6322 O OD2   . ASP C 1 283 ? -37.809 37.422  -3.154  1.00 103.52 ? 255 ASP C OD2   1 
ATOM   6323 N N     . ASP C 1 284 ? -41.816 33.933  -1.607  1.00 90.43  ? 256 ASP C N     1 
ATOM   6324 C CA    . ASP C 1 284 ? -42.940 33.481  -0.798  1.00 91.23  ? 256 ASP C CA    1 
ATOM   6325 C C     . ASP C 1 284 ? -42.940 31.967  -0.628  1.00 93.58  ? 256 ASP C C     1 
ATOM   6326 O O     . ASP C 1 284 ? -43.387 31.464  0.409   1.00 92.58  ? 256 ASP C O     1 
ATOM   6327 C CB    . ASP C 1 284 ? -44.256 33.945  -1.424  1.00 88.93  ? 256 ASP C CB    1 
ATOM   6328 N N     . PHE C 1 285 ? -42.444 31.233  -1.627  1.00 91.73  ? 257 PHE C N     1 
ATOM   6329 C CA    . PHE C 1 285 ? -42.340 29.782  -1.504  1.00 93.49  ? 257 PHE C CA    1 
ATOM   6330 C C     . PHE C 1 285 ? -41.302 29.395  -0.457  1.00 92.59  ? 257 PHE C C     1 
ATOM   6331 O O     . PHE C 1 285 ? -41.499 28.432  0.294   1.00 92.37  ? 257 PHE C O     1 
ATOM   6332 C CB    . PHE C 1 285 ? -41.997 29.171  -2.867  1.00 93.19  ? 257 PHE C CB    1 
ATOM   6333 C CG    . PHE C 1 285 ? -42.056 27.665  -2.901  1.00 89.90  ? 257 PHE C CG    1 
ATOM   6334 C CD1   . PHE C 1 285 ? -41.014 26.898  -2.403  1.00 89.63  ? 257 PHE C CD1   1 
ATOM   6335 C CD2   . PHE C 1 285 ? -43.154 27.019  -3.444  1.00 88.14  ? 257 PHE C CD2   1 
ATOM   6336 C CE1   . PHE C 1 285 ? -41.072 25.518  -2.438  1.00 91.27  ? 257 PHE C CE1   1 
ATOM   6337 C CE2   . PHE C 1 285 ? -43.216 25.640  -3.484  1.00 87.07  ? 257 PHE C CE2   1 
ATOM   6338 C CZ    . PHE C 1 285 ? -42.175 24.889  -2.979  1.00 90.61  ? 257 PHE C CZ    1 
ATOM   6339 N N     . PHE C 1 286 ? -40.194 30.136  -0.391  1.00 90.85  ? 258 PHE C N     1 
ATOM   6340 C CA    . PHE C 1 286 ? -39.139 29.814  0.564   1.00 87.84  ? 258 PHE C CA    1 
ATOM   6341 C C     . PHE C 1 286 ? -39.602 30.047  1.998   1.00 84.78  ? 258 PHE C C     1 
ATOM   6342 O O     . PHE C 1 286 ? -39.370 29.210  2.878   1.00 85.80  ? 258 PHE C O     1 
ATOM   6343 C CB    . PHE C 1 286 ? -37.887 30.636  0.260   1.00 83.34  ? 258 PHE C CB    1 
ATOM   6344 C CG    . PHE C 1 286 ? -36.653 30.137  0.954   1.00 72.32  ? 258 PHE C CG    1 
ATOM   6345 C CD1   . PHE C 1 286 ? -36.337 28.789  0.950   1.00 68.23  ? 258 PHE C CD1   1 
ATOM   6346 C CD2   . PHE C 1 286 ? -35.811 31.016  1.615   1.00 66.75  ? 258 PHE C CD2   1 
ATOM   6347 C CE1   . PHE C 1 286 ? -35.204 28.326  1.590   1.00 62.83  ? 258 PHE C CE1   1 
ATOM   6348 C CE2   . PHE C 1 286 ? -34.677 30.559  2.257   1.00 59.67  ? 258 PHE C CE2   1 
ATOM   6349 C CZ    . PHE C 1 286 ? -34.374 29.212  2.246   1.00 58.37  ? 258 PHE C CZ    1 
ATOM   6350 N N     . ASP C 1 287 ? -40.254 31.184  2.253   1.00 81.88  ? 259 ASP C N     1 
ATOM   6351 C CA    . ASP C 1 287 ? -40.747 31.464  3.598   1.00 86.03  ? 259 ASP C CA    1 
ATOM   6352 C C     . ASP C 1 287 ? -41.813 30.459  4.014   1.00 87.84  ? 259 ASP C C     1 
ATOM   6353 O O     . ASP C 1 287 ? -41.848 30.023  5.171   1.00 86.33  ? 259 ASP C O     1 
ATOM   6354 C CB    . ASP C 1 287 ? -41.294 32.890  3.672   1.00 94.47  ? 259 ASP C CB    1 
ATOM   6355 C CG    . ASP C 1 287 ? -40.197 33.936  3.649   1.00 91.52  ? 259 ASP C CG    1 
ATOM   6356 O OD1   . ASP C 1 287 ? -39.334 33.877  2.749   1.00 87.68  ? 259 ASP C OD1   1 
ATOM   6357 O OD2   . ASP C 1 287 ? -40.199 34.818  4.535   1.00 89.56  ? 259 ASP C OD2   1 
ATOM   6358 N N     . ASP C 1 288 ? -42.695 30.085  3.084   1.00 88.70  ? 260 ASP C N     1 
ATOM   6359 C CA    . ASP C 1 288 ? -43.677 29.045  3.373   1.00 91.89  ? 260 ASP C CA    1 
ATOM   6360 C C     . ASP C 1 288 ? -42.992 27.724  3.697   1.00 91.17  ? 260 ASP C C     1 
ATOM   6361 O O     . ASP C 1 288 ? -43.435 26.983  4.582   1.00 90.58  ? 260 ASP C O     1 
ATOM   6362 C CB    . ASP C 1 288 ? -44.630 28.883  2.189   1.00 93.40  ? 260 ASP C CB    1 
ATOM   6363 C CG    . ASP C 1 288 ? -45.931 28.211  2.574   1.00 97.74  ? 260 ASP C CG    1 
ATOM   6364 O OD1   . ASP C 1 288 ? -46.385 28.401  3.722   1.00 102.09 ? 260 ASP C OD1   1 
ATOM   6365 O OD2   . ASP C 1 288 ? -46.501 27.489  1.728   1.00 99.79  ? 260 ASP C OD2   1 
ATOM   6366 N N     . TRP C 1 289 ? -41.902 27.418  2.991   1.00 91.73  ? 261 TRP C N     1 
ATOM   6367 C CA    . TRP C 1 289 ? -41.144 26.204  3.272   1.00 87.98  ? 261 TRP C CA    1 
ATOM   6368 C C     . TRP C 1 289 ? -40.428 26.302  4.613   1.00 84.29  ? 261 TRP C C     1 
ATOM   6369 O O     . TRP C 1 289 ? -40.508 25.385  5.439   1.00 83.37  ? 261 TRP C O     1 
ATOM   6370 C CB    . TRP C 1 289 ? -40.143 25.946  2.144   1.00 82.31  ? 261 TRP C CB    1 
ATOM   6371 C CG    . TRP C 1 289 ? -39.589 24.555  2.120   1.00 77.62  ? 261 TRP C CG    1 
ATOM   6372 C CD1   . TRP C 1 289 ? -40.289 23.389  2.225   1.00 77.92  ? 261 TRP C CD1   1 
ATOM   6373 C CD2   . TRP C 1 289 ? -38.213 24.186  1.978   1.00 76.02  ? 261 TRP C CD2   1 
ATOM   6374 N NE1   . TRP C 1 289 ? -39.434 22.316  2.158   1.00 78.10  ? 261 TRP C NE1   1 
ATOM   6375 C CE2   . TRP C 1 289 ? -38.153 22.779  2.007   1.00 75.82  ? 261 TRP C CE2   1 
ATOM   6376 C CE3   . TRP C 1 289 ? -37.025 24.908  1.832   1.00 74.04  ? 261 TRP C CE3   1 
ATOM   6377 C CZ2   . TRP C 1 289 ? -36.954 22.081  1.892   1.00 73.11  ? 261 TRP C CZ2   1 
ATOM   6378 C CZ3   . TRP C 1 289 ? -35.835 24.213  1.720   1.00 68.10  ? 261 TRP C CZ3   1 
ATOM   6379 C CH2   . TRP C 1 289 ? -35.808 22.814  1.751   1.00 70.60  ? 261 TRP C CH2   1 
ATOM   6380 N N     . LEU C 1 290 ? -39.731 27.417  4.852   1.00 86.18  ? 262 LEU C N     1 
ATOM   6381 C CA    . LEU C 1 290 ? -38.933 27.551  6.067   1.00 80.00  ? 262 LEU C CA    1 
ATOM   6382 C C     . LEU C 1 290 ? -39.807 27.550  7.315   1.00 81.65  ? 262 LEU C C     1 
ATOM   6383 O O     . LEU C 1 290 ? -39.436 26.965  8.339   1.00 83.83  ? 262 LEU C O     1 
ATOM   6384 C CB    . LEU C 1 290 ? -38.094 28.827  6.008   1.00 74.44  ? 262 LEU C CB    1 
ATOM   6385 C CG    . LEU C 1 290 ? -36.887 28.838  5.067   1.00 63.87  ? 262 LEU C CG    1 
ATOM   6386 C CD1   . LEU C 1 290 ? -35.906 29.920  5.489   1.00 56.41  ? 262 LEU C CD1   1 
ATOM   6387 C CD2   . LEU C 1 290 ? -36.209 27.478  5.032   1.00 66.66  ? 262 LEU C CD2   1 
ATOM   6388 N N     . GLN C 1 291 ? -40.968 28.207  7.253   1.00 82.28  ? 263 GLN C N     1 
ATOM   6389 C CA    . GLN C 1 291 ? -41.847 28.258  8.417   1.00 85.78  ? 263 GLN C CA    1 
ATOM   6390 C C     . GLN C 1 291 ? -42.345 26.868  8.791   1.00 90.30  ? 263 GLN C C     1 
ATOM   6391 O O     . GLN C 1 291 ? -42.385 26.511  9.975   1.00 93.17  ? 263 GLN C O     1 
ATOM   6392 C CB    . GLN C 1 291 ? -43.022 29.200  8.148   1.00 86.57  ? 263 GLN C CB    1 
ATOM   6393 C CG    . GLN C 1 291 ? -44.304 28.826  8.875   1.00 93.30  ? 263 GLN C CG    1 
ATOM   6394 C CD    . GLN C 1 291 ? -45.456 29.753  8.542   1.00 98.97  ? 263 GLN C CD    1 
ATOM   6395 O OE1   . GLN C 1 291 ? -45.796 29.944  7.375   1.00 97.60  ? 263 GLN C OE1   1 
ATOM   6396 N NE2   . GLN C 1 291 ? -46.064 30.335  9.570   1.00 99.37  ? 263 GLN C NE2   1 
ATOM   6397 N N     . ARG C 1 292 ? -42.717 26.063  7.794   1.00 89.90  ? 264 ARG C N     1 
ATOM   6398 C CA    . ARG C 1 292 ? -43.186 24.707  8.048   1.00 89.29  ? 264 ARG C CA    1 
ATOM   6399 C C     . ARG C 1 292 ? -42.084 23.785  8.552   1.00 85.88  ? 264 ARG C C     1 
ATOM   6400 O O     . ARG C 1 292 ? -42.393 22.705  9.067   1.00 86.06  ? 264 ARG C O     1 
ATOM   6401 C CB    . ARG C 1 292 ? -43.798 24.120  6.776   1.00 91.89  ? 264 ARG C CB    1 
ATOM   6402 C CG    . ARG C 1 292 ? -45.025 23.258  7.015   1.00 94.73  ? 264 ARG C CG    1 
ATOM   6403 C CD    . ARG C 1 292 ? -45.902 23.214  5.778   1.00 95.98  ? 264 ARG C CD    1 
ATOM   6404 N NE    . ARG C 1 292 ? -46.939 24.238  5.812   1.00 95.37  ? 264 ARG C NE    1 
ATOM   6405 C CZ    . ARG C 1 292 ? -46.863 25.397  5.173   1.00 96.86  ? 264 ARG C CZ    1 
ATOM   6406 N NH1   . ARG C 1 292 ? -45.808 25.713  4.440   1.00 96.43  ? 264 ARG C NH1   1 
ATOM   6407 N NH2   . ARG C 1 292 ? -47.870 26.259  5.271   1.00 102.74 ? 264 ARG C NH2   1 
ATOM   6408 N N     . LEU C 1 293 ? -40.817 24.180  8.421   1.00 85.82  ? 265 LEU C N     1 
ATOM   6409 C CA    . LEU C 1 293 ? -39.724 23.310  8.841   1.00 84.47  ? 265 LEU C CA    1 
ATOM   6410 C C     . LEU C 1 293 ? -39.569 23.295  10.355  1.00 86.73  ? 265 LEU C C     1 
ATOM   6411 O O     . LEU C 1 293 ? -39.394 22.226  10.952  1.00 83.88  ? 265 LEU C O     1 
ATOM   6412 C CB    . LEU C 1 293 ? -38.423 23.745  8.171   1.00 81.11  ? 265 LEU C CB    1 
ATOM   6413 C CG    . LEU C 1 293 ? -38.374 23.399  6.684   1.00 78.60  ? 265 LEU C CG    1 
ATOM   6414 C CD1   . LEU C 1 293 ? -37.089 23.904  6.043   1.00 71.56  ? 265 LEU C CD1   1 
ATOM   6415 C CD2   . LEU C 1 293 ? -38.560 21.903  6.480   1.00 73.35  ? 265 LEU C CD2   1 
ATOM   6416 N N     . GLU C 1 294 ? -39.622 24.466  10.992  1.00 89.67  ? 266 GLU C N     1 
ATOM   6417 C CA    . GLU C 1 294 ? -39.598 24.508  12.448  1.00 88.68  ? 266 GLU C CA    1 
ATOM   6418 C C     . GLU C 1 294 ? -40.904 24.012  13.052  1.00 86.88  ? 266 GLU C C     1 
ATOM   6419 O O     . GLU C 1 294 ? -40.915 23.591  14.213  1.00 87.98  ? 266 GLU C O     1 
ATOM   6420 C CB    . GLU C 1 294 ? -39.288 25.925  12.931  1.00 92.83  ? 266 GLU C CB    1 
ATOM   6421 C CG    . GLU C 1 294 ? -37.826 26.311  12.764  1.00 105.04 ? 266 GLU C CG    1 
ATOM   6422 C CD    . GLU C 1 294 ? -37.541 27.738  13.186  1.00 118.89 ? 266 GLU C CD    1 
ATOM   6423 O OE1   . GLU C 1 294 ? -38.465 28.406  13.696  1.00 120.31 ? 266 GLU C OE1   1 
ATOM   6424 O OE2   . GLU C 1 294 ? -36.390 28.191  13.009  1.00 116.80 ? 266 GLU C OE2   1 
ATOM   6425 N N     . LYS C 1 295 ? -42.001 24.058  12.292  1.00 88.72  ? 267 LYS C N     1 
ATOM   6426 C CA    . LYS C 1 295 ? -43.222 23.371  12.700  1.00 94.44  ? 267 LYS C CA    1 
ATOM   6427 C C     . LYS C 1 295 ? -42.968 21.878  12.867  1.00 94.07  ? 267 LYS C C     1 
ATOM   6428 O O     . LYS C 1 295 ? -43.231 21.299  13.927  1.00 92.78  ? 267 LYS C O     1 
ATOM   6429 C CB    . LYS C 1 295 ? -44.328 23.613  11.672  1.00 94.69  ? 267 LYS C CB    1 
ATOM   6430 C CG    . LYS C 1 295 ? -45.618 22.865  11.971  1.00 94.07  ? 267 LYS C CG    1 
ATOM   6431 C CD    . LYS C 1 295 ? -46.640 23.046  10.861  1.00 96.28  ? 267 LYS C CD    1 
ATOM   6432 C CE    . LYS C 1 295 ? -47.864 22.174  11.097  1.00 102.97 ? 267 LYS C CE    1 
ATOM   6433 N NZ    . LYS C 1 295 ? -48.873 22.315  10.010  1.00 102.54 ? 267 LYS C NZ    1 
ATOM   6434 N N     . LEU C 1 296 ? -42.447 21.241  11.821  1.00 91.08  ? 268 LEU C N     1 
ATOM   6435 C CA    . LEU C 1 296 ? -42.126 19.821  11.845  1.00 81.40  ? 268 LEU C CA    1 
ATOM   6436 C C     . LEU C 1 296 ? -40.828 19.524  12.584  1.00 81.02  ? 268 LEU C C     1 
ATOM   6437 O O     . LEU C 1 296 ? -40.467 18.349  12.718  1.00 77.52  ? 268 LEU C O     1 
ATOM   6438 C CB    . LEU C 1 296 ? -42.051 19.288  10.413  1.00 76.14  ? 268 LEU C CB    1 
ATOM   6439 C CG    . LEU C 1 296 ? -43.371 19.373  9.643   1.00 73.15  ? 268 LEU C CG    1 
ATOM   6440 C CD1   . LEU C 1 296 ? -43.142 19.201  8.153   1.00 75.79  ? 268 LEU C CD1   1 
ATOM   6441 C CD2   . LEU C 1 296 ? -44.366 18.345  10.159  1.00 75.51  ? 268 LEU C CD2   1 
ATOM   6442 N N     . LYS C 1 297 ? -40.125 20.557  13.055  1.00 83.59  ? 269 LYS C N     1 
ATOM   6443 C CA    . LYS C 1 297 ? -38.921 20.407  13.874  1.00 80.22  ? 269 LYS C CA    1 
ATOM   6444 C C     . LYS C 1 297 ? -37.842 19.601  13.152  1.00 75.49  ? 269 LYS C C     1 
ATOM   6445 O O     . LYS C 1 297 ? -37.233 18.687  13.712  1.00 74.72  ? 269 LYS C O     1 
ATOM   6446 C CB    . LYS C 1 297 ? -39.255 19.790  15.234  1.00 82.77  ? 269 LYS C CB    1 
ATOM   6447 C CG    . LYS C 1 297 ? -40.207 20.632  16.068  1.00 82.49  ? 269 LYS C CG    1 
ATOM   6448 C CD    . LYS C 1 297 ? -40.451 20.014  17.433  1.00 80.10  ? 269 LYS C CD    1 
ATOM   6449 C CE    . LYS C 1 297 ? -41.449 20.834  18.233  1.00 82.24  ? 269 LYS C CE    1 
ATOM   6450 N NZ    . LYS C 1 297 ? -41.716 20.236  19.569  1.00 84.94  ? 269 LYS C NZ    1 
ATOM   6451 N N     . GLY C 1 298 ? -37.607 19.951  11.891  1.00 69.80  ? 270 GLY C N     1 
ATOM   6452 C CA    . GLY C 1 298 ? -36.491 19.392  11.154  1.00 68.42  ? 270 GLY C CA    1 
ATOM   6453 C C     . GLY C 1 298 ? -35.260 20.256  11.312  1.00 67.84  ? 270 GLY C C     1 
ATOM   6454 O O     . GLY C 1 298 ? -34.133 19.754  11.369  1.00 69.21  ? 270 GLY C O     1 
ATOM   6455 N N     . THR C 1 299 ? -35.474 21.565  11.385  1.00 70.55  ? 271 THR C N     1 
ATOM   6456 C CA    . THR C 1 299 ? -34.417 22.525  11.661  1.00 70.91  ? 271 THR C CA    1 
ATOM   6457 C C     . THR C 1 299 ? -34.540 23.008  13.100  1.00 70.85  ? 271 THR C C     1 
ATOM   6458 O O     . THR C 1 299 ? -35.647 23.206  13.607  1.00 73.64  ? 271 THR C O     1 
ATOM   6459 C CB    . THR C 1 299 ? -34.491 23.716  10.703  1.00 73.65  ? 271 THR C CB    1 
ATOM   6460 O OG1   . THR C 1 299 ? -35.677 24.476  10.973  1.00 75.47  ? 271 THR C OG1   1 
ATOM   6461 C CG2   . THR C 1 299 ? -34.523 23.236  9.261   1.00 69.37  ? 271 THR C CG2   1 
ATOM   6462 N N     . SER C 1 300 ? -33.397 23.190  13.756  1.00 65.96  ? 272 SER C N     1 
ATOM   6463 C CA    . SER C 1 300 ? -33.360 23.640  15.139  1.00 65.05  ? 272 SER C CA    1 
ATOM   6464 C C     . SER C 1 300 ? -32.271 24.691  15.288  1.00 66.93  ? 272 SER C C     1 
ATOM   6465 O O     . SER C 1 300 ? -31.566 25.029  14.333  1.00 65.39  ? 272 SER C O     1 
ATOM   6466 C CB    . SER C 1 300 ? -33.130 22.467  16.099  1.00 61.04  ? 272 SER C CB    1 
ATOM   6467 O OG    . SER C 1 300 ? -32.406 22.879  17.245  1.00 64.55  ? 272 SER C OG    1 
ATOM   6468 N N     . GLN C 1 301 ? -32.138 25.212  16.506  1.00 71.51  ? 273 GLN C N     1 
ATOM   6469 C CA    . GLN C 1 301 ? -31.126 26.208  16.815  1.00 69.18  ? 273 GLN C CA    1 
ATOM   6470 C C     . GLN C 1 301 ? -30.628 25.971  18.232  1.00 66.25  ? 273 GLN C C     1 
ATOM   6471 O O     . GLN C 1 301 ? -31.414 25.634  19.122  1.00 64.02  ? 273 GLN C O     1 
ATOM   6472 C CB    . GLN C 1 301 ? -31.681 27.630  16.679  1.00 70.66  ? 273 GLN C CB    1 
ATOM   6473 C CG    . GLN C 1 301 ? -30.611 28.700  16.684  1.00 76.19  ? 273 GLN C CG    1 
ATOM   6474 C CD    . GLN C 1 301 ? -30.990 29.903  17.513  1.00 89.58  ? 273 GLN C CD    1 
ATOM   6475 O OE1   . GLN C 1 301 ? -31.853 30.695  17.133  1.00 91.90  ? 273 GLN C OE1   1 
ATOM   6476 N NE2   . GLN C 1 301 ? -30.336 30.050  18.659  1.00 90.58  ? 273 GLN C NE2   1 
ATOM   6477 N N     . GLY C 1 302 ? -29.325 26.146  18.439  1.00 68.44  ? 274 GLY C N     1 
ATOM   6478 C CA    . GLY C 1 302 ? -28.734 25.873  19.735  1.00 69.13  ? 274 GLY C CA    1 
ATOM   6479 C C     . GLY C 1 302 ? -27.862 26.989  20.272  1.00 71.92  ? 274 GLY C C     1 
ATOM   6480 O O     . GLY C 1 302 ? -27.848 28.098  19.727  1.00 72.82  ? 274 GLY C O     1 
ATOM   6481 N N     . VAL C 1 303 ? -27.130 26.704  21.346  1.00 73.01  ? 275 VAL C N     1 
ATOM   6482 C CA    . VAL C 1 303 ? -26.237 27.667  21.977  1.00 70.98  ? 275 VAL C CA    1 
ATOM   6483 C C     . VAL C 1 303 ? -24.838 27.073  22.026  1.00 73.34  ? 275 VAL C C     1 
ATOM   6484 O O     . VAL C 1 303 ? -24.660 25.851  22.055  1.00 75.07  ? 275 VAL C O     1 
ATOM   6485 C CB    . VAL C 1 303 ? -26.715 28.056  23.393  1.00 62.60  ? 275 VAL C CB    1 
ATOM   6486 C CG1   . VAL C 1 303 ? -27.908 28.995  23.310  1.00 60.20  ? 275 VAL C CG1   1 
ATOM   6487 C CG2   . VAL C 1 303 ? -27.059 26.811  24.197  1.00 59.27  ? 275 VAL C CG2   1 
ATOM   6488 N N     . GLY C 1 304 ? -23.838 27.951  22.036  1.00 73.42  ? 276 GLY C N     1 
ATOM   6489 C CA    . GLY C 1 304 ? -22.457 27.515  22.059  1.00 75.86  ? 276 GLY C CA    1 
ATOM   6490 C C     . GLY C 1 304 ? -21.794 27.684  23.410  1.00 82.75  ? 276 GLY C C     1 
ATOM   6491 O O     . GLY C 1 304 ? -22.262 28.464  24.246  1.00 79.88  ? 276 GLY C O     1 
ATOM   6492 N N     . ARG C 1 305 ? -20.702 26.948  23.638  1.00 86.66  ? 277 ARG C N     1 
ATOM   6493 C CA    . ARG C 1 305 ? -19.962 27.091  24.887  1.00 82.02  ? 277 ARG C CA    1 
ATOM   6494 C C     . ARG C 1 305 ? -19.379 28.490  25.030  1.00 82.10  ? 277 ARG C C     1 
ATOM   6495 O O     . ARG C 1 305 ? -19.271 29.007  26.148  1.00 73.22  ? 277 ARG C O     1 
ATOM   6496 C CB    . ARG C 1 305 ? -18.854 26.040  24.966  1.00 79.71  ? 277 ARG C CB    1 
ATOM   6497 N N     . ASN C 1 306 ? -18.998 29.115  23.916  1.00 92.81  ? 278 ASN C N     1 
ATOM   6498 C CA    . ASN C 1 306 ? -18.537 30.496  23.933  1.00 87.63  ? 278 ASN C CA    1 
ATOM   6499 C C     . ASN C 1 306 ? -19.683 31.498  23.978  1.00 86.51  ? 278 ASN C C     1 
ATOM   6500 O O     . ASN C 1 306 ? -19.430 32.696  24.145  1.00 86.19  ? 278 ASN C O     1 
ATOM   6501 C CB    . ASN C 1 306 ? -17.660 30.774  22.708  1.00 79.92  ? 278 ASN C CB    1 
ATOM   6502 N N     . GLY C 1 307 ? -20.926 31.040  23.836  1.00 89.03  ? 279 GLY C N     1 
ATOM   6503 C CA    . GLY C 1 307 ? -22.082 31.910  23.863  1.00 80.67  ? 279 GLY C CA    1 
ATOM   6504 C C     . GLY C 1 307 ? -22.678 32.235  22.511  1.00 74.92  ? 279 GLY C C     1 
ATOM   6505 O O     . GLY C 1 307 ? -23.665 32.978  22.454  1.00 64.84  ? 279 GLY C O     1 
ATOM   6506 N N     . GLU C 1 308 ? -22.119 31.705  21.428  1.00 79.69  ? 280 GLU C N     1 
ATOM   6507 C CA    . GLU C 1 308 ? -22.592 32.004  20.086  1.00 68.11  ? 280 GLU C CA    1 
ATOM   6508 C C     . GLU C 1 308 ? -23.756 31.093  19.704  1.00 65.22  ? 280 GLU C C     1 
ATOM   6509 O O     . GLU C 1 308 ? -23.980 30.040  20.306  1.00 66.49  ? 280 GLU C O     1 
ATOM   6510 C CB    . GLU C 1 308 ? -21.458 31.859  19.070  1.00 61.29  ? 280 GLU C CB    1 
ATOM   6511 N N     . ALA C 1 309 ? -24.496 31.517  18.683  1.00 65.07  ? 281 ALA C N     1 
ATOM   6512 C CA    . ALA C 1 309 ? -25.665 30.777  18.230  1.00 65.88  ? 281 ALA C CA    1 
ATOM   6513 C C     . ALA C 1 309 ? -25.260 29.644  17.296  1.00 62.15  ? 281 ALA C C     1 
ATOM   6514 O O     . ALA C 1 309 ? -24.337 29.783  16.489  1.00 61.27  ? 281 ALA C O     1 
ATOM   6515 C CB    . ALA C 1 309 ? -26.647 31.711  17.523  1.00 71.88  ? 281 ALA C CB    1 
ATOM   6516 N N     . GLU C 1 310 ? -25.964 28.520  17.409  1.00 63.38  ? 282 GLU C N     1 
ATOM   6517 C CA    . GLU C 1 310 ? -25.706 27.332  16.607  1.00 61.61  ? 282 GLU C CA    1 
ATOM   6518 C C     . GLU C 1 310 ? -26.981 26.944  15.873  1.00 62.61  ? 282 GLU C C     1 
ATOM   6519 O O     . GLU C 1 310 ? -28.055 26.892  16.478  1.00 67.69  ? 282 GLU C O     1 
ATOM   6520 C CB    . GLU C 1 310 ? -25.228 26.172  17.486  1.00 62.93  ? 282 GLU C CB    1 
ATOM   6521 C CG    . GLU C 1 310 ? -23.858 26.379  18.111  1.00 64.78  ? 282 GLU C CG    1 
ATOM   6522 C CD    . GLU C 1 310 ? -23.455 25.233  19.018  1.00 63.90  ? 282 GLU C CD    1 
ATOM   6523 O OE1   . GLU C 1 310 ? -24.350 24.485  19.467  1.00 65.54  ? 282 GLU C OE1   1 
ATOM   6524 O OE2   . GLU C 1 310 ? -22.244 25.079  19.283  1.00 60.89  ? 282 GLU C OE2   1 
ATOM   6525 N N     . TYR C 1 311 ? -26.861 26.665  14.577  1.00 58.58  ? 283 TYR C N     1 
ATOM   6526 C CA    . TYR C 1 311 ? -27.999 26.326  13.732  1.00 56.60  ? 283 TYR C CA    1 
ATOM   6527 C C     . TYR C 1 311 ? -27.820 24.920  13.175  1.00 54.06  ? 283 TYR C C     1 
ATOM   6528 O O     . TYR C 1 311 ? -26.715 24.538  12.778  1.00 54.38  ? 283 TYR C O     1 
ATOM   6529 C CB    . TYR C 1 311 ? -28.152 27.338  12.590  1.00 58.31  ? 283 TYR C CB    1 
ATOM   6530 C CG    . TYR C 1 311 ? -28.435 28.749  13.063  1.00 60.45  ? 283 TYR C CG    1 
ATOM   6531 C CD1   . TYR C 1 311 ? -27.409 29.569  13.516  1.00 63.38  ? 283 TYR C CD1   1 
ATOM   6532 C CD2   . TYR C 1 311 ? -29.726 29.258  13.061  1.00 62.95  ? 283 TYR C CD2   1 
ATOM   6533 C CE1   . TYR C 1 311 ? -27.660 30.857  13.952  1.00 65.77  ? 283 TYR C CE1   1 
ATOM   6534 C CE2   . TYR C 1 311 ? -29.988 30.545  13.494  1.00 69.82  ? 283 TYR C CE2   1 
ATOM   6535 C CZ    . TYR C 1 311 ? -28.951 31.340  13.939  1.00 72.33  ? 283 TYR C CZ    1 
ATOM   6536 O OH    . TYR C 1 311 ? -29.207 32.621  14.372  1.00 82.49  ? 283 TYR C OH    1 
ATOM   6537 N N     . TYR C 1 312 ? -28.909 24.151  13.140  1.00 53.09  ? 284 TYR C N     1 
ATOM   6538 C CA    . TYR C 1 312 ? -28.837 22.730  12.835  1.00 52.53  ? 284 TYR C CA    1 
ATOM   6539 C C     . TYR C 1 312 ? -29.910 22.323  11.831  1.00 56.71  ? 284 TYR C C     1 
ATOM   6540 O O     . TYR C 1 312 ? -30.921 23.006  11.649  1.00 52.97  ? 284 TYR C O     1 
ATOM   6541 C CB    . TYR C 1 312 ? -28.986 21.880  14.104  1.00 52.89  ? 284 TYR C CB    1 
ATOM   6542 C CG    . TYR C 1 312 ? -27.812 21.974  15.047  1.00 53.93  ? 284 TYR C CG    1 
ATOM   6543 C CD1   . TYR C 1 312 ? -27.756 22.962  16.021  1.00 60.18  ? 284 TYR C CD1   1 
ATOM   6544 C CD2   . TYR C 1 312 ? -26.754 21.080  14.960  1.00 55.42  ? 284 TYR C CD2   1 
ATOM   6545 C CE1   . TYR C 1 312 ? -26.684 23.052  16.886  1.00 59.18  ? 284 TYR C CE1   1 
ATOM   6546 C CE2   . TYR C 1 312 ? -25.676 21.163  15.820  1.00 57.15  ? 284 TYR C CE2   1 
ATOM   6547 C CZ    . TYR C 1 312 ? -25.645 22.151  16.780  1.00 59.16  ? 284 TYR C CZ    1 
ATOM   6548 O OH    . TYR C 1 312 ? -24.573 22.237  17.638  1.00 60.80  ? 284 TYR C OH    1 
ATOM   6549 N N     . ILE C 1 313 ? -29.662 21.184  11.182  1.00 56.96  ? 285 ILE C N     1 
ATOM   6550 C CA    . ILE C 1 313 ? -30.629 20.502  10.329  1.00 50.98  ? 285 ILE C CA    1 
ATOM   6551 C C     . ILE C 1 313 ? -30.603 19.023  10.692  1.00 54.74  ? 285 ILE C C     1 
ATOM   6552 O O     . ILE C 1 313 ? -29.538 18.396  10.673  1.00 51.37  ? 285 ILE C O     1 
ATOM   6553 C CB    . ILE C 1 313 ? -30.326 20.691  8.830   1.00 45.42  ? 285 ILE C CB    1 
ATOM   6554 C CG1   . ILE C 1 313 ? -30.495 22.154  8.420   1.00 48.73  ? 285 ILE C CG1   1 
ATOM   6555 C CG2   . ILE C 1 313 ? -31.219 19.795  7.987   1.00 46.15  ? 285 ILE C CG2   1 
ATOM   6556 C CD1   . ILE C 1 313 ? -30.080 22.435  6.990   1.00 45.78  ? 285 ILE C CD1   1 
ATOM   6557 N N     . HIS C 1 314 ? -31.768 18.470  11.022  1.00 59.52  ? 286 HIS C N     1 
ATOM   6558 C CA    . HIS C 1 314 ? -31.884 17.093  11.485  1.00 59.82  ? 286 HIS C CA    1 
ATOM   6559 C C     . HIS C 1 314 ? -32.484 16.208  10.401  1.00 58.66  ? 286 HIS C C     1 
ATOM   6560 O O     . HIS C 1 314 ? -33.359 16.640  9.644   1.00 59.61  ? 286 HIS C O     1 
ATOM   6561 C CB    . HIS C 1 314 ? -32.737 17.015  12.753  1.00 59.98  ? 286 HIS C CB    1 
ATOM   6562 C CG    . HIS C 1 314 ? -32.325 17.986  13.813  1.00 62.58  ? 286 HIS C CG    1 
ATOM   6563 N ND1   . HIS C 1 314 ? -31.302 17.728  14.700  1.00 63.88  ? 286 HIS C ND1   1 
ATOM   6564 C CD2   . HIS C 1 314 ? -32.789 19.219  14.121  1.00 64.29  ? 286 HIS C CD2   1 
ATOM   6565 C CE1   . HIS C 1 314 ? -31.158 18.759  15.513  1.00 67.28  ? 286 HIS C CE1   1 
ATOM   6566 N NE2   . HIS C 1 314 ? -32.048 19.677  15.183  1.00 68.35  ? 286 HIS C NE2   1 
ATOM   6567 N N     . LEU C 1 315 ? -32.017 14.962  10.350  1.00 55.20  ? 287 LEU C N     1 
ATOM   6568 C CA    . LEU C 1 315 ? -32.424 14.002  9.332   1.00 54.60  ? 287 LEU C CA    1 
ATOM   6569 C C     . LEU C 1 315 ? -31.834 12.642  9.680   1.00 52.48  ? 287 LEU C C     1 
ATOM   6570 O O     . LEU C 1 315 ? -30.822 12.547  10.381  1.00 48.46  ? 287 LEU C O     1 
ATOM   6571 C CB    . LEU C 1 315 ? -31.986 14.461  7.935   1.00 52.78  ? 287 LEU C CB    1 
ATOM   6572 C CG    . LEU C 1 315 ? -30.488 14.669  7.690   1.00 44.89  ? 287 LEU C CG    1 
ATOM   6573 C CD1   . LEU C 1 315 ? -29.852 13.437  7.084   1.00 47.29  ? 287 LEU C CD1   1 
ATOM   6574 C CD2   . LEU C 1 315 ? -30.240 15.887  6.817   1.00 44.58  ? 287 LEU C CD2   1 
ATOM   6575 N N     . SER C 1 316 ? -32.483 11.590  9.184   1.00 54.42  ? 288 SER C N     1 
ATOM   6576 C CA    . SER C 1 316 ? -32.065 10.215  9.428   1.00 54.77  ? 288 SER C CA    1 
ATOM   6577 C C     . SER C 1 316 ? -31.292 9.684   8.228   1.00 53.61  ? 288 SER C C     1 
ATOM   6578 O O     . SER C 1 316 ? -31.632 9.977   7.079   1.00 55.18  ? 288 SER C O     1 
ATOM   6579 C CB    . SER C 1 316 ? -33.273 9.319   9.710   1.00 58.75  ? 288 SER C CB    1 
ATOM   6580 O OG    . SER C 1 316 ? -33.985 9.767   10.850  1.00 72.28  ? 288 SER C OG    1 
ATOM   6581 N N     . VAL C 1 317 ? -30.252 8.895   8.500   1.00 51.02  ? 289 VAL C N     1 
ATOM   6582 C CA    . VAL C 1 317 ? -29.348 8.395   7.470   1.00 50.25  ? 289 VAL C CA    1 
ATOM   6583 C C     . VAL C 1 317 ? -29.245 6.881   7.574   1.00 51.91  ? 289 VAL C C     1 
ATOM   6584 O O     . VAL C 1 317 ? -29.029 6.341   8.665   1.00 55.58  ? 289 VAL C O     1 
ATOM   6585 C CB    . VAL C 1 317 ? -27.946 9.026   7.581   1.00 51.68  ? 289 VAL C CB    1 
ATOM   6586 C CG1   . VAL C 1 317 ? -26.989 8.371   6.598   1.00 58.21  ? 289 VAL C CG1   1 
ATOM   6587 C CG2   . VAL C 1 317 ? -28.016 10.505  7.309   1.00 49.12  ? 289 VAL C CG2   1 
ATOM   6588 N N     . ILE C 1 318 ? -29.393 6.202   6.440   1.00 47.96  ? 290 ILE C N     1 
ATOM   6589 C CA    . ILE C 1 318 ? -29.047 4.791   6.323   1.00 48.67  ? 290 ILE C CA    1 
ATOM   6590 C C     . ILE C 1 318 ? -27.624 4.693   5.794   1.00 47.88  ? 290 ILE C C     1 
ATOM   6591 O O     . ILE C 1 318 ? -27.290 5.298   4.768   1.00 50.35  ? 290 ILE C O     1 
ATOM   6592 C CB    . ILE C 1 318 ? -30.026 4.053   5.394   1.00 46.42  ? 290 ILE C CB    1 
ATOM   6593 C CG1   . ILE C 1 318 ? -31.473 4.303   5.816   1.00 54.43  ? 290 ILE C CG1   1 
ATOM   6594 C CG2   . ILE C 1 318 ? -29.722 2.563   5.380   1.00 46.53  ? 290 ILE C CG2   1 
ATOM   6595 C CD1   . ILE C 1 318 ? -32.479 3.934   4.747   1.00 59.81  ? 290 ILE C CD1   1 
ATOM   6596 N N     . THR C 1 319 ? -26.782 3.943   6.495   1.00 48.58  ? 291 THR C N     1 
ATOM   6597 C CA    . THR C 1 319 ? -25.416 3.677   6.066   1.00 49.99  ? 291 THR C CA    1 
ATOM   6598 C C     . THR C 1 319 ? -25.299 2.207   5.693   1.00 54.81  ? 291 THR C C     1 
ATOM   6599 O O     . THR C 1 319 ? -25.692 1.335   6.475   1.00 65.98  ? 291 THR C O     1 
ATOM   6600 C CB    . THR C 1 319 ? -24.410 4.031   7.163   1.00 48.02  ? 291 THR C CB    1 
ATOM   6601 O OG1   . THR C 1 319 ? -24.645 5.371   7.614   1.00 50.33  ? 291 THR C OG1   1 
ATOM   6602 C CG2   . THR C 1 319 ? -22.989 3.927   6.633   1.00 52.26  ? 291 THR C CG2   1 
ATOM   6603 N N     . ALA C 1 320 ? -24.768 1.933   4.504   1.00 51.98  ? 292 ALA C N     1 
ATOM   6604 C CA    . ALA C 1 320 ? -24.718 0.574   3.988   1.00 51.86  ? 292 ALA C CA    1 
ATOM   6605 C C     . ALA C 1 320 ? -23.357 0.295   3.370   1.00 55.09  ? 292 ALA C C     1 
ATOM   6606 O O     . ALA C 1 320 ? -22.695 1.193   2.844   1.00 56.90  ? 292 ALA C O     1 
ATOM   6607 C CB    . ALA C 1 320 ? -25.821 0.325   2.951   1.00 50.34  ? 292 ALA C CB    1 
ATOM   6608 N N     . LEU C 1 321 ? -22.949 -0.971  3.443   1.00 56.78  ? 293 LEU C N     1 
ATOM   6609 C CA    . LEU C 1 321 ? -21.720 -1.450  2.817   1.00 55.09  ? 293 LEU C CA    1 
ATOM   6610 C C     . LEU C 1 321 ? -22.043 -2.775  2.143   1.00 62.10  ? 293 LEU C C     1 
ATOM   6611 O O     . LEU C 1 321 ? -22.242 -3.785  2.825   1.00 67.53  ? 293 LEU C O     1 
ATOM   6612 C CB    . LEU C 1 321 ? -20.596 -1.612  3.842   1.00 51.10  ? 293 LEU C CB    1 
ATOM   6613 C CG    . LEU C 1 321 ? -19.344 -2.354  3.369   1.00 54.43  ? 293 LEU C CG    1 
ATOM   6614 C CD1   . LEU C 1 321 ? -18.689 -1.621  2.210   1.00 54.64  ? 293 LEU C CD1   1 
ATOM   6615 C CD2   . LEU C 1 321 ? -18.362 -2.540  4.516   1.00 65.95  ? 293 LEU C CD2   1 
ATOM   6616 N N     . ALA C 1 322 ? -22.105 -2.773  0.817   1.00 58.37  ? 294 ALA C N     1 
ATOM   6617 C CA    . ALA C 1 322 ? -22.504 -3.938  0.042   1.00 61.71  ? 294 ALA C CA    1 
ATOM   6618 C C     . ALA C 1 322 ? -21.318 -4.474  -0.753  1.00 63.30  ? 294 ALA C C     1 
ATOM   6619 O O     . ALA C 1 322 ? -20.206 -3.941  -0.699  1.00 63.05  ? 294 ALA C O     1 
ATOM   6620 C CB    . ALA C 1 322 ? -23.676 -3.592  -0.878  1.00 60.96  ? 294 ALA C CB    1 
ATOM   6621 N N     . ARG C 1 323 ? -21.567 -5.550  -1.498  1.00 68.99  ? 295 ARG C N     1 
ATOM   6622 C CA    . ARG C 1 323 ? -20.545 -6.157  -2.341  1.00 71.31  ? 295 ARG C CA    1 
ATOM   6623 C C     . ARG C 1 323 ? -21.210 -6.894  -3.492  1.00 73.08  ? 295 ARG C C     1 
ATOM   6624 O O     . ARG C 1 323 ? -22.178 -7.631  -3.284  1.00 73.10  ? 295 ARG C O     1 
ATOM   6625 C CB    . ARG C 1 323 ? -19.659 -7.119  -1.542  1.00 72.20  ? 295 ARG C CB    1 
ATOM   6626 C CG    . ARG C 1 323 ? -18.556 -7.759  -2.374  1.00 76.55  ? 295 ARG C CG    1 
ATOM   6627 C CD    . ARG C 1 323 ? -17.733 -8.743  -1.562  1.00 79.57  ? 295 ARG C CD    1 
ATOM   6628 N NE    . ARG C 1 323 ? -16.989 -8.082  -0.497  1.00 82.49  ? 295 ARG C NE    1 
ATOM   6629 C CZ    . ARG C 1 323 ? -16.506 -8.699  0.573   1.00 82.28  ? 295 ARG C CZ    1 
ATOM   6630 N NH1   . ARG C 1 323 ? -16.668 -9.999  0.753   1.00 86.31  ? 295 ARG C NH1   1 
ATOM   6631 N NH2   . ARG C 1 323 ? -15.842 -7.993  1.484   1.00 79.33  ? 295 ARG C NH2   1 
ATOM   6632 N N     . LYS C 1 324 ? -20.684 -6.695  -4.698  1.00 74.35  ? 296 LYS C N     1 
ATOM   6633 C CA    . LYS C 1 324 ? -21.187 -7.386  -5.877  1.00 78.59  ? 296 LYS C CA    1 
ATOM   6634 C C     . LYS C 1 324 ? -20.673 -8.820  -5.910  1.00 85.10  ? 296 LYS C C     1 
ATOM   6635 O O     . LYS C 1 324 ? -19.533 -9.096  -5.525  1.00 83.73  ? 296 LYS C O     1 
ATOM   6636 C CB    . LYS C 1 324 ? -20.763 -6.645  -7.147  1.00 72.64  ? 296 LYS C CB    1 
ATOM   6637 C CG    . LYS C 1 324 ? -21.204 -7.307  -8.444  1.00 68.57  ? 296 LYS C CG    1 
ATOM   6638 C CD    . LYS C 1 324 ? -20.740 -6.516  -9.655  1.00 63.32  ? 296 LYS C CD    1 
ATOM   6639 C CE    . LYS C 1 324 ? -21.140 -7.206  -10.949 1.00 62.87  ? 296 LYS C CE    1 
ATOM   6640 N NZ    . LYS C 1 324 ? -20.801 -6.389  -12.146 1.00 59.91  ? 296 LYS C NZ    1 
ATOM   6641 N N     . PHE C 1 325 ? -21.523 -9.733  -6.370  1.00 84.82  ? 297 PHE C N     1 
ATOM   6642 C CA    . PHE C 1 325 ? -21.147 -11.137 -6.490  1.00 90.11  ? 297 PHE C CA    1 
ATOM   6643 C C     . PHE C 1 325 ? -20.476 -11.418 -7.832  1.00 87.62  ? 297 PHE C C     1 
ATOM   6644 O O     . PHE C 1 325 ? -20.714 -10.716 -8.816  1.00 83.19  ? 297 PHE C O     1 
ATOM   6645 C CB    . PHE C 1 325 ? -22.371 -12.038 -6.315  1.00 92.12  ? 297 PHE C CB    1 
ATOM   6646 C CG    . PHE C 1 325 ? -22.630 -12.436 -4.892  1.00 93.12  ? 297 PHE C CG    1 
ATOM   6647 C CD1   . PHE C 1 325 ? -21.924 -13.477 -4.312  1.00 97.16  ? 297 PHE C CD1   1 
ATOM   6648 C CD2   . PHE C 1 325 ? -23.580 -11.772 -4.134  1.00 90.52  ? 297 PHE C CD2   1 
ATOM   6649 C CE1   . PHE C 1 325 ? -22.160 -13.847 -3.001  1.00 98.27  ? 297 PHE C CE1   1 
ATOM   6650 C CE2   . PHE C 1 325 ? -23.820 -12.138 -2.823  1.00 90.21  ? 297 PHE C CE2   1 
ATOM   6651 C CZ    . PHE C 1 325 ? -23.109 -13.177 -2.256  1.00 92.66  ? 297 PHE C CZ    1 
ATOM   6652 N N     . GLU D 1 42  ? 11.941  -36.169 24.474  1.00 77.68  ? 14  GLU D N     1 
ATOM   6653 C CA    . GLU D 1 42  ? 10.614  -36.482 24.982  1.00 78.24  ? 14  GLU D CA    1 
ATOM   6654 C C     . GLU D 1 42  ? 10.750  -37.271 26.288  1.00 85.65  ? 14  GLU D C     1 
ATOM   6655 O O     . GLU D 1 42  ? 11.867  -37.563 26.717  1.00 84.08  ? 14  GLU D O     1 
ATOM   6656 C CB    . GLU D 1 42  ? 9.816   -37.262 23.931  1.00 81.81  ? 14  GLU D CB    1 
ATOM   6657 C CG    . GLU D 1 42  ? 8.311   -37.269 24.146  1.00 81.24  ? 14  GLU D CG    1 
ATOM   6658 C CD    . GLU D 1 42  ? 7.675   -38.599 23.796  1.00 79.17  ? 14  GLU D CD    1 
ATOM   6659 O OE1   . GLU D 1 42  ? 8.418   -39.541 23.463  1.00 85.42  ? 14  GLU D OE1   1 
ATOM   6660 O OE2   . GLU D 1 42  ? 6.432   -38.698 23.855  1.00 74.02  ? 14  GLU D OE2   1 
ATOM   6661 N N     . ALA D 1 43  ? 9.616   -37.602 26.913  1.00 95.03  ? 15  ALA D N     1 
ATOM   6662 C CA    . ALA D 1 43  ? 9.578   -38.298 28.196  1.00 91.72  ? 15  ALA D CA    1 
ATOM   6663 C C     . ALA D 1 43  ? 10.335  -37.506 29.255  1.00 87.84  ? 15  ALA D C     1 
ATOM   6664 O O     . ALA D 1 43  ? 9.893   -36.420 29.644  1.00 83.57  ? 15  ALA D O     1 
ATOM   6665 C CB    . ALA D 1 43  ? 10.134  -39.717 28.066  1.00 85.48  ? 15  ALA D CB    1 
ATOM   6666 N N     . TYR D 1 44  ? 11.467  -38.024 29.731  1.00 85.84  ? 16  TYR D N     1 
ATOM   6667 C CA    . TYR D 1 44  ? 12.249  -37.290 30.725  1.00 86.45  ? 16  TYR D CA    1 
ATOM   6668 C C     . TYR D 1 44  ? 12.890  -36.096 30.032  1.00 83.58  ? 16  TYR D C     1 
ATOM   6669 O O     . TYR D 1 44  ? 13.885  -36.242 29.320  1.00 87.96  ? 16  TYR D O     1 
ATOM   6670 C CB    . TYR D 1 44  ? 13.326  -38.155 31.375  1.00 80.82  ? 16  TYR D CB    1 
ATOM   6671 C CG    . TYR D 1 44  ? 12.938  -39.550 31.816  1.00 77.54  ? 16  TYR D CG    1 
ATOM   6672 C CD1   . TYR D 1 44  ? 11.633  -39.872 32.160  1.00 76.84  ? 16  TYR D CD1   1 
ATOM   6673 C CD2   . TYR D 1 44  ? 13.910  -40.532 31.958  1.00 79.75  ? 16  TYR D CD2   1 
ATOM   6674 C CE1   . TYR D 1 44  ? 11.303  -41.151 32.577  1.00 80.93  ? 16  TYR D CE1   1 
ATOM   6675 C CE2   . TYR D 1 44  ? 13.593  -41.807 32.369  1.00 75.36  ? 16  TYR D CE2   1 
ATOM   6676 C CZ    . TYR D 1 44  ? 12.292  -42.113 32.682  1.00 77.95  ? 16  TYR D CZ    1 
ATOM   6677 O OH    . TYR D 1 44  ? 11.987  -43.389 33.099  1.00 76.47  ? 16  TYR D OH    1 
ATOM   6678 N N     . ARG D 1 45  ? 12.308  -34.912 30.230  1.00 72.88  ? 17  ARG D N     1 
ATOM   6679 C CA    . ARG D 1 45  ? 12.867  -33.653 29.745  1.00 66.31  ? 17  ARG D CA    1 
ATOM   6680 C C     . ARG D 1 45  ? 13.064  -33.658 28.233  1.00 69.00  ? 17  ARG D C     1 
ATOM   6681 O O     . ARG D 1 45  ? 14.150  -33.991 27.749  1.00 69.32  ? 17  ARG D O     1 
ATOM   6682 C CB    . ARG D 1 45  ? 14.192  -33.347 30.450  1.00 67.64  ? 17  ARG D CB    1 
ATOM   6683 C CG    . ARG D 1 45  ? 14.151  -33.502 31.965  1.00 69.76  ? 17  ARG D CG    1 
ATOM   6684 C CD    . ARG D 1 45  ? 12.934  -32.813 32.565  1.00 71.07  ? 17  ARG D CD    1 
ATOM   6685 N NE    . ARG D 1 45  ? 13.211  -32.254 33.882  1.00 65.89  ? 17  ARG D NE    1 
ATOM   6686 C CZ    . ARG D 1 45  ? 12.715  -31.109 34.330  1.00 67.28  ? 17  ARG D CZ    1 
ATOM   6687 N NH1   . ARG D 1 45  ? 11.914  -30.364 33.585  1.00 62.86  ? 17  ARG D NH1   1 
ATOM   6688 N NH2   . ARG D 1 45  ? 13.034  -30.698 35.554  1.00 64.30  ? 17  ARG D NH2   1 
ATOM   6689 N N     . GLY D 1 46  ? 12.015  -33.274 27.500  1.00 68.30  ? 18  GLY D N     1 
ATOM   6690 C CA    . GLY D 1 46  ? 11.964  -33.194 26.047  1.00 66.28  ? 18  GLY D CA    1 
ATOM   6691 C C     . GLY D 1 46  ? 13.226  -33.466 25.252  1.00 65.59  ? 18  GLY D C     1 
ATOM   6692 O O     . GLY D 1 46  ? 13.607  -34.624 25.063  1.00 69.94  ? 18  GLY D O     1 
ATOM   6693 N N     . ILE D 1 47  ? 13.879  -32.410 24.775  1.00 57.28  ? 19  ILE D N     1 
ATOM   6694 C CA    . ILE D 1 47  ? 15.063  -32.529 23.931  1.00 58.20  ? 19  ILE D CA    1 
ATOM   6695 C C     . ILE D 1 47  ? 16.241  -31.930 24.686  1.00 55.96  ? 19  ILE D C     1 
ATOM   6696 O O     . ILE D 1 47  ? 16.331  -30.705 24.839  1.00 62.29  ? 19  ILE D O     1 
ATOM   6697 C CB    . ILE D 1 47  ? 14.877  -31.839 22.573  1.00 54.52  ? 19  ILE D CB    1 
ATOM   6698 C CG1   . ILE D 1 47  ? 13.733  -32.489 21.794  1.00 57.93  ? 19  ILE D CG1   1 
ATOM   6699 C CG2   . ILE D 1 47  ? 16.168  -31.889 21.767  1.00 51.66  ? 19  ILE D CG2   1 
ATOM   6700 C CD1   . ILE D 1 47  ? 14.086  -33.828 21.186  1.00 59.64  ? 19  ILE D CD1   1 
ATOM   6701 N N     . ASP D 1 48  ? 17.144  -32.787 25.155  1.00 53.35  ? 20  ASP D N     1 
ATOM   6702 C CA    . ASP D 1 48  ? 18.394  -32.325 25.733  1.00 53.44  ? 20  ASP D CA    1 
ATOM   6703 C C     . ASP D 1 48  ? 19.391  -32.007 24.619  1.00 63.84  ? 20  ASP D C     1 
ATOM   6704 O O     . ASP D 1 48  ? 19.105  -32.168 23.429  1.00 70.99  ? 20  ASP D O     1 
ATOM   6705 C CB    . ASP D 1 48  ? 18.951  -33.365 26.703  1.00 55.95  ? 20  ASP D CB    1 
ATOM   6706 C CG    . ASP D 1 48  ? 18.814  -34.782 26.184  1.00 66.74  ? 20  ASP D CG    1 
ATOM   6707 O OD1   . ASP D 1 48  ? 18.571  -34.956 24.971  1.00 65.33  ? 20  ASP D OD1   1 
ATOM   6708 O OD2   . ASP D 1 48  ? 18.951  -35.725 26.993  1.00 74.86  ? 20  ASP D OD2   1 
ATOM   6709 N N     . LYS D 1 49  ? 20.582  -31.550 25.014  1.00 61.22  ? 21  LYS D N     1 
ATOM   6710 C CA    . LYS D 1 49  ? 21.638  -31.152 24.088  1.00 64.92  ? 21  LYS D CA    1 
ATOM   6711 C C     . LYS D 1 49  ? 21.118  -30.104 23.109  1.00 59.55  ? 21  LYS D C     1 
ATOM   6712 O O     . LYS D 1 49  ? 20.946  -30.388 21.917  1.00 54.13  ? 21  LYS D O     1 
ATOM   6713 C CB    . LYS D 1 49  ? 22.191  -32.367 23.339  1.00 57.32  ? 21  LYS D CB    1 
ATOM   6714 N N     . PRO D 1 50  ? 20.854  -28.883 23.575  1.00 51.85  ? 22  PRO D N     1 
ATOM   6715 C CA    . PRO D 1 50  ? 20.285  -27.874 22.673  1.00 49.30  ? 22  PRO D CA    1 
ATOM   6716 C C     . PRO D 1 50  ? 21.272  -27.359 21.645  1.00 60.76  ? 22  PRO D C     1 
ATOM   6717 O O     . PRO D 1 50  ? 20.846  -26.892 20.582  1.00 57.63  ? 22  PRO D O     1 
ATOM   6718 C CB    . PRO D 1 50  ? 19.846  -26.767 23.638  1.00 48.28  ? 22  PRO D CB    1 
ATOM   6719 C CG    . PRO D 1 50  ? 20.836  -26.874 24.761  1.00 55.61  ? 22  PRO D CG    1 
ATOM   6720 C CD    . PRO D 1 50  ? 21.035  -28.357 24.941  1.00 60.94  ? 22  PRO D CD    1 
ATOM   6721 N N     . HIS D 1 51  ? 22.574  -27.429 21.938  1.00 63.14  ? 23  HIS D N     1 
ATOM   6722 C CA    . HIS D 1 51  ? 23.590  -26.934 21.014  1.00 63.40  ? 23  HIS D CA    1 
ATOM   6723 C C     . HIS D 1 51  ? 23.428  -27.543 19.629  1.00 60.12  ? 23  HIS D C     1 
ATOM   6724 O O     . HIS D 1 51  ? 23.590  -26.856 18.614  1.00 63.40  ? 23  HIS D O     1 
ATOM   6725 C CB    . HIS D 1 51  ? 24.984  -27.238 21.569  1.00 63.29  ? 23  HIS D CB    1 
ATOM   6726 C CG    . HIS D 1 51  ? 25.540  -26.156 22.442  1.00 71.97  ? 23  HIS D CG    1 
ATOM   6727 N ND1   . HIS D 1 51  ? 24.792  -25.517 23.407  1.00 73.71  ? 23  HIS D ND1   1 
ATOM   6728 C CD2   . HIS D 1 51  ? 26.772  -25.596 22.490  1.00 72.95  ? 23  HIS D CD2   1 
ATOM   6729 C CE1   . HIS D 1 51  ? 25.539  -24.612 24.014  1.00 70.50  ? 23  HIS D CE1   1 
ATOM   6730 N NE2   . HIS D 1 51  ? 26.745  -24.639 23.476  1.00 73.56  ? 23  HIS D NE2   1 
ATOM   6731 N N     . LEU D 1 52  ? 23.091  -28.831 19.565  1.00 58.58  ? 24  LEU D N     1 
ATOM   6732 C CA    . LEU D 1 52  ? 22.951  -29.513 18.285  1.00 51.68  ? 24  LEU D CA    1 
ATOM   6733 C C     . LEU D 1 52  ? 21.616  -29.230 17.610  1.00 53.54  ? 24  LEU D C     1 
ATOM   6734 O O     . LEU D 1 52  ? 21.516  -29.369 16.387  1.00 56.01  ? 24  LEU D O     1 
ATOM   6735 C CB    . LEU D 1 52  ? 23.125  -31.021 18.479  1.00 53.30  ? 24  LEU D CB    1 
ATOM   6736 C CG    . LEU D 1 52  ? 24.370  -31.459 19.261  1.00 54.52  ? 24  LEU D CG    1 
ATOM   6737 C CD1   . LEU D 1 52  ? 24.640  -32.939 19.063  1.00 56.22  ? 24  LEU D CD1   1 
ATOM   6738 C CD2   . LEU D 1 52  ? 25.597  -30.639 18.870  1.00 58.40  ? 24  LEU D CD2   1 
ATOM   6739 N N     . TYR D 1 53  ? 20.590  -28.838 18.371  1.00 55.22  ? 25  TYR D N     1 
ATOM   6740 C CA    . TYR D 1 53  ? 19.307  -28.528 17.749  1.00 48.90  ? 25  TYR D CA    1 
ATOM   6741 C C     . TYR D 1 53  ? 19.358  -27.211 16.986  1.00 49.77  ? 25  TYR D C     1 
ATOM   6742 O O     . TYR D 1 53  ? 18.697  -27.073 15.951  1.00 48.19  ? 25  TYR D O     1 
ATOM   6743 C CB    . TYR D 1 53  ? 18.194  -28.487 18.797  1.00 48.46  ? 25  TYR D CB    1 
ATOM   6744 C CG    . TYR D 1 53  ? 16.807  -28.453 18.190  1.00 47.85  ? 25  TYR D CG    1 
ATOM   6745 C CD1   . TYR D 1 53  ? 16.138  -29.628 17.875  1.00 48.75  ? 25  TYR D CD1   1 
ATOM   6746 C CD2   . TYR D 1 53  ? 16.173  -27.247 17.919  1.00 46.47  ? 25  TYR D CD2   1 
ATOM   6747 C CE1   . TYR D 1 53  ? 14.874  -29.603 17.314  1.00 48.30  ? 25  TYR D CE1   1 
ATOM   6748 C CE2   . TYR D 1 53  ? 14.909  -27.211 17.358  1.00 46.00  ? 25  TYR D CE2   1 
ATOM   6749 C CZ    . TYR D 1 53  ? 14.265  -28.393 17.058  1.00 46.92  ? 25  TYR D CZ    1 
ATOM   6750 O OH    . TYR D 1 53  ? 13.009  -28.368 16.499  1.00 46.55  ? 25  TYR D OH    1 
ATOM   6751 N N     . THR D 1 54  ? 20.132  -26.238 17.475  1.00 49.75  ? 26  THR D N     1 
ATOM   6752 C CA    . THR D 1 54  ? 20.300  -24.972 16.770  1.00 46.14  ? 26  THR D CA    1 
ATOM   6753 C C     . THR D 1 54  ? 20.999  -25.134 15.428  1.00 47.31  ? 26  THR D C     1 
ATOM   6754 O O     . THR D 1 54  ? 21.082  -24.160 14.672  1.00 55.19  ? 26  THR D O     1 
ATOM   6755 C CB    . THR D 1 54  ? 21.082  -23.976 17.633  1.00 47.09  ? 26  THR D CB    1 
ATOM   6756 O OG1   . THR D 1 54  ? 22.229  -24.625 18.196  1.00 56.65  ? 26  THR D OG1   1 
ATOM   6757 C CG2   . THR D 1 54  ? 20.211  -23.428 18.746  1.00 53.13  ? 26  THR D CG2   1 
ATOM   6758 N N     . LEU D 1 55  ? 21.513  -26.326 15.118  1.00 47.80  ? 27  LEU D N     1 
ATOM   6759 C CA    . LEU D 1 55  ? 22.025  -26.592 13.781  1.00 48.33  ? 27  LEU D CA    1 
ATOM   6760 C C     . LEU D 1 55  ? 20.917  -26.573 12.738  1.00 47.81  ? 27  LEU D C     1 
ATOM   6761 O O     . LEU D 1 55  ? 21.201  -26.387 11.550  1.00 47.86  ? 27  LEU D O     1 
ATOM   6762 C CB    . LEU D 1 55  ? 22.750  -27.935 13.753  1.00 49.98  ? 27  LEU D CB    1 
ATOM   6763 C CG    . LEU D 1 55  ? 24.066  -27.977 14.531  1.00 50.72  ? 27  LEU D CG    1 
ATOM   6764 C CD1   . LEU D 1 55  ? 24.612  -29.393 14.590  1.00 52.42  ? 27  LEU D CD1   1 
ATOM   6765 C CD2   . LEU D 1 55  ? 25.086  -27.025 13.925  1.00 50.44  ? 27  LEU D CD2   1 
ATOM   6766 N N     . GLY D 1 56  ? 19.669  -26.766 13.152  1.00 47.39  ? 28  GLY D N     1 
ATOM   6767 C CA    . GLY D 1 56  ? 18.521  -26.591 12.291  1.00 46.80  ? 28  GLY D CA    1 
ATOM   6768 C C     . GLY D 1 56  ? 17.881  -25.223 12.364  1.00 49.29  ? 28  GLY D C     1 
ATOM   6769 O O     . GLY D 1 56  ? 16.772  -25.050 11.844  1.00 49.98  ? 28  GLY D O     1 
ATOM   6770 N N     . CYS D 1 57  ? 18.538  -24.245 12.995  1.00 50.77  ? 29  CYS D N     1 
ATOM   6771 C CA    . CYS D 1 57  ? 17.986  -22.895 13.083  1.00 53.09  ? 29  CYS D CA    1 
ATOM   6772 C C     . CYS D 1 57  ? 17.691  -22.324 11.704  1.00 60.58  ? 29  CYS D C     1 
ATOM   6773 O O     . CYS D 1 57  ? 16.600  -21.798 11.461  1.00 63.58  ? 29  CYS D O     1 
ATOM   6774 C CB    . CYS D 1 57  ? 18.955  -21.982 13.834  1.00 57.95  ? 29  CYS D CB    1 
ATOM   6775 S SG    . CYS D 1 57  ? 18.259  -20.405 14.368  1.00 64.43  ? 29  CYS D SG    1 
ATOM   6776 N N     . CYS D 1 58  ? 18.656  -22.425 10.786  1.00 66.58  ? 30  CYS D N     1 
ATOM   6777 C CA    . CYS D 1 58  ? 18.532  -21.792 9.476   1.00 67.80  ? 30  CYS D CA    1 
ATOM   6778 C C     . CYS D 1 58  ? 17.235  -22.189 8.782   1.00 66.94  ? 30  CYS D C     1 
ATOM   6779 O O     . CYS D 1 58  ? 16.496  -21.334 8.281   1.00 66.68  ? 30  CYS D O     1 
ATOM   6780 C CB    . CYS D 1 58  ? 19.736  -22.160 8.609   1.00 74.58  ? 30  CYS D CB    1 
ATOM   6781 S SG    . CYS D 1 58  ? 21.274  -22.393 9.530   1.00 107.92 ? 30  CYS D SG    1 
ATOM   6782 N N     . SER D 1 59  ? 16.934  -23.488 8.757   1.00 67.08  ? 31  SER D N     1 
ATOM   6783 C CA    . SER D 1 59  ? 15.762  -23.964 8.032   1.00 59.19  ? 31  SER D CA    1 
ATOM   6784 C C     . SER D 1 59  ? 14.490  -23.842 8.862   1.00 54.01  ? 31  SER D C     1 
ATOM   6785 O O     . SER D 1 59  ? 13.447  -23.428 8.343   1.00 53.24  ? 31  SER D O     1 
ATOM   6786 C CB    . SER D 1 59  ? 15.975  -25.413 7.592   1.00 49.84  ? 31  SER D CB    1 
ATOM   6787 O OG    . SER D 1 59  ? 17.043  -25.510 6.666   1.00 48.38  ? 31  SER D OG    1 
ATOM   6788 N N     . LEU D 1 60  ? 14.553  -24.194 10.149  1.00 54.81  ? 32  LEU D N     1 
ATOM   6789 C CA    . LEU D 1 60  ? 13.347  -24.187 10.974  1.00 53.90  ? 32  LEU D CA    1 
ATOM   6790 C C     . LEU D 1 60  ? 12.836  -22.770 11.207  1.00 62.70  ? 32  LEU D C     1 
ATOM   6791 O O     . LEU D 1 60  ? 11.623  -22.531 11.174  1.00 61.14  ? 32  LEU D O     1 
ATOM   6792 C CB    . LEU D 1 60  ? 13.616  -24.888 12.304  1.00 49.22  ? 32  LEU D CB    1 
ATOM   6793 C CG    . LEU D 1 60  ? 13.867  -26.395 12.222  1.00 45.05  ? 32  LEU D CG    1 
ATOM   6794 C CD1   . LEU D 1 60  ? 14.200  -26.965 13.592  1.00 45.58  ? 32  LEU D CD1   1 
ATOM   6795 C CD2   . LEU D 1 60  ? 12.666  -27.104 11.618  1.00 47.31  ? 32  LEU D CD2   1 
ATOM   6796 N N     . THR D 1 61  ? 13.742  -21.820 11.453  1.00 65.08  ? 33  THR D N     1 
ATOM   6797 C CA    . THR D 1 61  ? 13.333  -20.426 11.612  1.00 62.87  ? 33  THR D CA    1 
ATOM   6798 C C     . THR D 1 61  ? 12.616  -19.923 10.366  1.00 61.34  ? 33  THR D C     1 
ATOM   6799 O O     . THR D 1 61  ? 11.539  -19.322 10.454  1.00 58.30  ? 33  THR D O     1 
ATOM   6800 C CB    . THR D 1 61  ? 14.550  -19.552 11.923  1.00 65.54  ? 33  THR D CB    1 
ATOM   6801 O OG1   . THR D 1 61  ? 15.103  -19.927 13.192  1.00 66.95  ? 33  THR D OG1   1 
ATOM   6802 C CG2   . THR D 1 61  ? 14.177  -18.080 11.941  1.00 64.44  ? 33  THR D CG2   1 
ATOM   6803 N N     . ALA D 1 62  ? 13.196  -20.174 9.191   1.00 60.78  ? 34  ALA D N     1 
ATOM   6804 C CA    . ALA D 1 62  ? 12.566  -19.741 7.949   1.00 63.10  ? 34  ALA D CA    1 
ATOM   6805 C C     . ALA D 1 62  ? 11.269  -20.492 7.680   1.00 60.88  ? 34  ALA D C     1 
ATOM   6806 O O     . ALA D 1 62  ? 10.354  -19.940 7.059   1.00 65.28  ? 34  ALA D O     1 
ATOM   6807 C CB    . ALA D 1 62  ? 13.534  -19.918 6.779   1.00 67.68  ? 34  ALA D CB    1 
ATOM   6808 N N     . MET D 1 63  ? 11.165  -21.742 8.138   1.00 56.10  ? 35  MET D N     1 
ATOM   6809 C CA    . MET D 1 63  ? 9.963   -22.526 7.872   1.00 59.15  ? 35  MET D CA    1 
ATOM   6810 C C     . MET D 1 63  ? 8.777   -22.005 8.673   1.00 59.44  ? 35  MET D C     1 
ATOM   6811 O O     . MET D 1 63  ? 7.695   -21.774 8.120   1.00 58.26  ? 35  MET D O     1 
ATOM   6812 C CB    . MET D 1 63  ? 10.214  -24.002 8.177   1.00 60.49  ? 35  MET D CB    1 
ATOM   6813 C CG    . MET D 1 63  ? 8.995   -24.883 7.963   1.00 63.30  ? 35  MET D CG    1 
ATOM   6814 S SD    . MET D 1 63  ? 9.204   -26.540 8.635   1.00 72.52  ? 35  MET D SD    1 
ATOM   6815 C CE    . MET D 1 63  ? 10.760  -27.004 7.880   1.00 55.96  ? 35  MET D CE    1 
ATOM   6816 N N     . ALA D 1 64  ? 8.956   -21.822 9.983   1.00 58.85  ? 36  ALA D N     1 
ATOM   6817 C CA    . ALA D 1 64  ? 7.891   -21.241 10.791  1.00 54.98  ? 36  ALA D CA    1 
ATOM   6818 C C     . ALA D 1 64  ? 7.610   -19.801 10.388  1.00 55.47  ? 36  ALA D C     1 
ATOM   6819 O O     . ALA D 1 64  ? 6.471   -19.336 10.508  1.00 57.17  ? 36  ALA D O     1 
ATOM   6820 C CB    . ALA D 1 64  ? 8.248   -21.318 12.274  1.00 56.64  ? 36  ALA D CB    1 
ATOM   6821 N N     . SER D 1 65  ? 8.630   -19.083 9.912   1.00 56.29  ? 37  SER D N     1 
ATOM   6822 C CA    . SER D 1 65  ? 8.410   -17.738 9.395   1.00 55.89  ? 37  SER D CA    1 
ATOM   6823 C C     . SER D 1 65  ? 7.489   -17.753 8.183   1.00 56.04  ? 37  SER D C     1 
ATOM   6824 O O     . SER D 1 65  ? 6.707   -16.816 7.986   1.00 56.44  ? 37  SER D O     1 
ATOM   6825 C CB    . SER D 1 65  ? 9.747   -17.087 9.040   1.00 58.27  ? 37  SER D CB    1 
ATOM   6826 O OG    . SER D 1 65  ? 9.576   -15.730 8.672   1.00 62.40  ? 37  SER D OG    1 
ATOM   6827 N N     . ALA D 1 66  ? 7.563   -18.805 7.366   1.00 63.15  ? 38  ALA D N     1 
ATOM   6828 C CA    . ALA D 1 66  ? 6.687   -18.912 6.206   1.00 60.35  ? 38  ALA D CA    1 
ATOM   6829 C C     . ALA D 1 66  ? 5.280   -19.338 6.606   1.00 58.79  ? 38  ALA D C     1 
ATOM   6830 O O     . ALA D 1 66  ? 4.297   -18.844 6.042   1.00 58.66  ? 38  ALA D O     1 
ATOM   6831 C CB    . ALA D 1 66  ? 7.274   -19.896 5.193   1.00 59.97  ? 38  ALA D CB    1 
ATOM   6832 N N     . GLN D 1 67  ? 5.164   -20.253 7.572   1.00 66.07  ? 39  GLN D N     1 
ATOM   6833 C CA    . GLN D 1 67  ? 3.847   -20.698 8.017   1.00 66.41  ? 39  GLN D CA    1 
ATOM   6834 C C     . GLN D 1 67  ? 3.062   -19.554 8.645   1.00 61.50  ? 39  GLN D C     1 
ATOM   6835 O O     . GLN D 1 67  ? 1.852   -19.426 8.423   1.00 61.71  ? 39  GLN D O     1 
ATOM   6836 C CB    . GLN D 1 67  ? 3.987   -21.851 9.012   1.00 66.35  ? 39  GLN D CB    1 
ATOM   6837 C CG    . GLN D 1 67  ? 4.429   -23.167 8.399   1.00 72.08  ? 39  GLN D CG    1 
ATOM   6838 C CD    . GLN D 1 67  ? 4.749   -24.214 9.449   1.00 75.34  ? 39  GLN D CD    1 
ATOM   6839 O OE1   . GLN D 1 67  ? 5.064   -23.885 10.593  1.00 73.04  ? 39  GLN D OE1   1 
ATOM   6840 N NE2   . GLN D 1 67  ? 4.668   -25.483 9.065   1.00 77.39  ? 39  GLN D NE2   1 
ATOM   6841 N N     . LEU D 1 68  ? 3.734   -18.712 9.432   1.00 63.68  ? 40  LEU D N     1 
ATOM   6842 C CA    . LEU D 1 68  ? 3.042   -17.618 10.103  1.00 67.68  ? 40  LEU D CA    1 
ATOM   6843 C C     . LEU D 1 68  ? 2.615   -16.533 9.123   1.00 68.77  ? 40  LEU D C     1 
ATOM   6844 O O     . LEU D 1 68  ? 1.570   -15.902 9.319   1.00 69.80  ? 40  LEU D O     1 
ATOM   6845 C CB    . LEU D 1 68  ? 3.931   -17.028 11.197  1.00 67.63  ? 40  LEU D CB    1 
ATOM   6846 C CG    . LEU D 1 68  ? 4.081   -17.890 12.451  1.00 63.77  ? 40  LEU D CG    1 
ATOM   6847 C CD1   . LEU D 1 68  ? 5.011   -17.227 13.451  1.00 61.89  ? 40  LEU D CD1   1 
ATOM   6848 C CD2   . LEU D 1 68  ? 2.724   -18.170 13.077  1.00 66.41  ? 40  LEU D CD2   1 
ATOM   6849 N N     . ASP D 1 69  ? 3.402   -16.302 8.068   1.00 66.71  ? 41  ASP D N     1 
ATOM   6850 C CA    . ASP D 1 69  ? 3.032   -15.303 7.072   1.00 67.86  ? 41  ASP D CA    1 
ATOM   6851 C C     . ASP D 1 69  ? 1.756   -15.675 6.330   1.00 67.90  ? 41  ASP D C     1 
ATOM   6852 O O     . ASP D 1 69  ? 1.073   -14.786 5.809   1.00 70.94  ? 41  ASP D O     1 
ATOM   6853 C CB    . ASP D 1 69  ? 4.176   -15.100 6.077   1.00 67.29  ? 41  ASP D CB    1 
ATOM   6854 C CG    . ASP D 1 69  ? 5.326   -14.305 6.666   1.00 69.48  ? 41  ASP D CG    1 
ATOM   6855 O OD1   . ASP D 1 69  ? 5.141   -13.699 7.743   1.00 67.13  ? 41  ASP D OD1   1 
ATOM   6856 O OD2   . ASP D 1 69  ? 6.413   -14.285 6.051   1.00 69.07  ? 41  ASP D OD2   1 
ATOM   6857 N N     . ALA D 1 70  ? 1.419   -16.964 6.271   1.00 68.35  ? 42  ALA D N     1 
ATOM   6858 C CA    . ALA D 1 70  ? 0.177   -17.403 5.650   1.00 70.82  ? 42  ALA D CA    1 
ATOM   6859 C C     . ALA D 1 70  ? -1.027  -17.266 6.572   1.00 73.13  ? 42  ALA D C     1 
ATOM   6860 O O     . ALA D 1 70  ? -2.164  -17.339 6.092   1.00 77.60  ? 42  ALA D O     1 
ATOM   6861 C CB    . ALA D 1 70  ? 0.304   -18.857 5.187   1.00 67.81  ? 42  ALA D CB    1 
ATOM   6862 N N     . LEU D 1 71  ? -0.810  -17.069 7.874   1.00 75.07  ? 43  LEU D N     1 
ATOM   6863 C CA    . LEU D 1 71  ? -1.894  -16.936 8.834   1.00 72.77  ? 43  LEU D CA    1 
ATOM   6864 C C     . LEU D 1 71  ? -1.941  -15.582 9.525   1.00 74.48  ? 43  LEU D C     1 
ATOM   6865 O O     . LEU D 1 71  ? -2.943  -15.285 10.187  1.00 77.79  ? 43  LEU D O     1 
ATOM   6866 C CB    . LEU D 1 71  ? -1.796  -18.025 9.915   1.00 65.41  ? 43  LEU D CB    1 
ATOM   6867 C CG    . LEU D 1 71  ? -1.869  -19.483 9.464   1.00 72.42  ? 43  LEU D CG    1 
ATOM   6868 C CD1   . LEU D 1 71  ? -1.757  -20.414 10.661  1.00 67.51  ? 43  LEU D CD1   1 
ATOM   6869 C CD2   . LEU D 1 71  ? -3.149  -19.743 8.699   1.00 81.90  ? 43  LEU D CD2   1 
ATOM   6870 N N     . TRP D 1 72  ? -0.901  -14.756 9.392   1.00 76.38  ? 44  TRP D N     1 
ATOM   6871 C CA    . TRP D 1 72  ? -0.802  -13.543 10.197  1.00 78.06  ? 44  TRP D CA    1 
ATOM   6872 C C     . TRP D 1 72  ? -1.881  -12.522 9.862   1.00 77.45  ? 44  TRP D C     1 
ATOM   6873 O O     . TRP D 1 72  ? -2.199  -11.680 10.708  1.00 73.45  ? 44  TRP D O     1 
ATOM   6874 C CB    . TRP D 1 72  ? 0.580   -12.911 10.032  1.00 75.57  ? 44  TRP D CB    1 
ATOM   6875 C CG    . TRP D 1 72  ? 0.989   -12.114 11.225  1.00 72.97  ? 44  TRP D CG    1 
ATOM   6876 C CD1   . TRP D 1 72  ? 0.916   -10.761 11.375  1.00 73.32  ? 44  TRP D CD1   1 
ATOM   6877 C CD2   . TRP D 1 72  ? 1.515   -12.628 12.453  1.00 75.79  ? 44  TRP D CD2   1 
ATOM   6878 N NE1   . TRP D 1 72  ? 1.375   -10.399 12.618  1.00 74.66  ? 44  TRP D NE1   1 
ATOM   6879 C CE2   . TRP D 1 72  ? 1.749   -11.527 13.300  1.00 73.54  ? 44  TRP D CE2   1 
ATOM   6880 C CE3   . TRP D 1 72  ? 1.819   -13.912 12.916  1.00 77.06  ? 44  TRP D CE3   1 
ATOM   6881 C CZ2   . TRP D 1 72  ? 2.269   -11.672 14.584  1.00 75.63  ? 44  TRP D CZ2   1 
ATOM   6882 C CZ3   . TRP D 1 72  ? 2.334   -14.053 14.190  1.00 78.36  ? 44  TRP D CZ3   1 
ATOM   6883 C CH2   . TRP D 1 72  ? 2.555   -12.940 15.010  1.00 76.60  ? 44  TRP D CH2   1 
ATOM   6884 N N     . SER D 1 73  ? -2.449  -12.575 8.656   1.00 81.72  ? 45  SER D N     1 
ATOM   6885 C CA    . SER D 1 73  ? -3.524  -11.651 8.315   1.00 79.78  ? 45  SER D CA    1 
ATOM   6886 C C     . SER D 1 73  ? -4.820  -12.011 9.029   1.00 76.96  ? 45  SER D C     1 
ATOM   6887 O O     . SER D 1 73  ? -5.621  -11.123 9.344   1.00 75.02  ? 45  SER D O     1 
ATOM   6888 C CB    . SER D 1 73  ? -3.743  -11.630 6.802   1.00 75.64  ? 45  SER D CB    1 
ATOM   6889 O OG    . SER D 1 73  ? -4.154  -12.901 6.331   1.00 75.64  ? 45  SER D OG    1 
ATOM   6890 N N     . GLN D 1 74  ? -5.041  -13.296 9.297   1.00 74.04  ? 46  GLN D N     1 
ATOM   6891 C CA    . GLN D 1 74  ? -6.258  -13.764 9.946   1.00 74.15  ? 46  GLN D CA    1 
ATOM   6892 C C     . GLN D 1 74  ? -6.204  -13.664 11.466  1.00 79.97  ? 46  GLN D C     1 
ATOM   6893 O O     . GLN D 1 74  ? -7.073  -14.230 12.137  1.00 83.44  ? 46  GLN D O     1 
ATOM   6894 C CB    . GLN D 1 74  ? -6.546  -15.211 9.535   1.00 65.97  ? 46  GLN D CB    1 
ATOM   6895 N N     . LEU D 1 75  ? -5.218  -12.963 12.024  1.00 81.67  ? 47  LEU D N     1 
ATOM   6896 C CA    . LEU D 1 75  ? -5.041  -12.866 13.469  1.00 83.90  ? 47  LEU D CA    1 
ATOM   6897 C C     . LEU D 1 75  ? -5.513  -11.496 13.943  1.00 81.55  ? 47  LEU D C     1 
ATOM   6898 O O     . LEU D 1 75  ? -4.898  -10.474 13.623  1.00 81.89  ? 47  LEU D O     1 
ATOM   6899 C CB    . LEU D 1 75  ? -3.583  -13.101 13.856  1.00 84.93  ? 47  LEU D CB    1 
ATOM   6900 C CG    . LEU D 1 75  ? -3.022  -14.505 13.627  1.00 85.31  ? 47  LEU D CG    1 
ATOM   6901 C CD1   . LEU D 1 75  ? -1.511  -14.501 13.765  1.00 83.77  ? 47  LEU D CD1   1 
ATOM   6902 C CD2   . LEU D 1 75  ? -3.644  -15.498 14.594  1.00 77.05  ? 47  LEU D CD2   1 
ATOM   6903 N N     . SER D 1 76  ? -6.600  -11.480 14.708  1.00 82.58  ? 48  SER D N     1 
ATOM   6904 C CA    . SER D 1 76  ? -7.066  -10.255 15.336  1.00 85.96  ? 48  SER D CA    1 
ATOM   6905 C C     . SER D 1 76  ? -6.338  -10.034 16.657  1.00 85.61  ? 48  SER D C     1 
ATOM   6906 O O     . SER D 1 76  ? -5.897  -10.981 17.313  1.00 89.76  ? 48  SER D O     1 
ATOM   6907 C CB    . SER D 1 76  ? -8.575  -10.311 15.570  1.00 90.08  ? 48  SER D CB    1 
ATOM   6908 O OG    . SER D 1 76  ? -8.905  -11.342 16.483  1.00 92.66  ? 48  SER D OG    1 
ATOM   6909 N N     . TRP D 1 77  ? -6.216  -8.769  17.044  1.00 85.67  ? 49  TRP D N     1 
ATOM   6910 C CA    . TRP D 1 77  ? -5.457  -8.409  18.229  1.00 86.64  ? 49  TRP D CA    1 
ATOM   6911 C C     . TRP D 1 77  ? -6.251  -7.455  19.107  1.00 86.55  ? 49  TRP D C     1 
ATOM   6912 O O     . TRP D 1 77  ? -7.017  -6.628  18.603  1.00 91.24  ? 49  TRP D O     1 
ATOM   6913 C CB    . TRP D 1 77  ? -4.119  -7.759  17.844  1.00 82.74  ? 49  TRP D CB    1 
ATOM   6914 C CG    . TRP D 1 77  ? -3.222  -8.683  17.088  1.00 78.23  ? 49  TRP D CG    1 
ATOM   6915 C CD1   . TRP D 1 77  ? -3.123  -8.803  15.734  1.00 72.29  ? 49  TRP D CD1   1 
ATOM   6916 C CD2   . TRP D 1 77  ? -2.299  -9.626  17.645  1.00 82.20  ? 49  TRP D CD2   1 
ATOM   6917 N NE1   . TRP D 1 77  ? -2.193  -9.762  15.411  1.00 79.07  ? 49  TRP D NE1   1 
ATOM   6918 C CE2   . TRP D 1 77  ? -1.673  -10.282 16.567  1.00 82.24  ? 49  TRP D CE2   1 
ATOM   6919 C CE3   . TRP D 1 77  ? -1.941  -9.979  18.949  1.00 81.40  ? 49  TRP D CE3   1 
ATOM   6920 C CZ2   . TRP D 1 77  ? -0.708  -11.270 16.753  1.00 82.87  ? 49  TRP D CZ2   1 
ATOM   6921 C CZ3   . TRP D 1 77  ? -0.983  -10.958 19.132  1.00 79.24  ? 49  TRP D CZ3   1 
ATOM   6922 C CH2   . TRP D 1 77  ? -0.378  -11.593 18.041  1.00 79.01  ? 49  TRP D CH2   1 
ATOM   6923 N N     . PRO D 1 78  ? -6.091  -7.552  20.423  1.00 87.57  ? 50  PRO D N     1 
ATOM   6924 C CA    . PRO D 1 78  ? -6.766  -6.614  21.323  1.00 94.71  ? 50  PRO D CA    1 
ATOM   6925 C C     . PRO D 1 78  ? -6.095  -5.249  21.314  1.00 103.16 ? 50  PRO D C     1 
ATOM   6926 O O     . PRO D 1 78  ? -4.952  -5.084  20.883  1.00 102.11 ? 50  PRO D O     1 
ATOM   6927 C CB    . PRO D 1 78  ? -6.635  -7.284  22.695  1.00 93.89  ? 50  PRO D CB    1 
ATOM   6928 C CG    . PRO D 1 78  ? -5.388  -8.094  22.590  1.00 94.16  ? 50  PRO D CG    1 
ATOM   6929 C CD    . PRO D 1 78  ? -5.290  -8.549  21.156  1.00 92.81  ? 50  PRO D CD    1 
ATOM   6930 N N     . GLN D 1 79  ? -6.841  -4.256  21.804  1.00 105.68 ? 51  GLN D N     1 
ATOM   6931 C CA    . GLN D 1 79  ? -6.330  -2.889  21.836  1.00 106.68 ? 51  GLN D CA    1 
ATOM   6932 C C     . GLN D 1 79  ? -5.165  -2.767  22.811  1.00 103.03 ? 51  GLN D C     1 
ATOM   6933 O O     . GLN D 1 79  ? -4.067  -2.337  22.439  1.00 99.97  ? 51  GLN D O     1 
ATOM   6934 C CB    . GLN D 1 79  ? -7.453  -1.917  22.200  1.00 108.31 ? 51  GLN D CB    1 
ATOM   6935 C CG    . GLN D 1 79  ? -8.332  -1.526  21.022  1.00 115.22 ? 51  GLN D CG    1 
ATOM   6936 C CD    . GLN D 1 79  ? -7.585  -0.720  19.977  1.00 118.94 ? 51  GLN D CD    1 
ATOM   6937 O OE1   . GLN D 1 79  ? -6.629  -0.010  20.289  1.00 122.12 ? 51  GLN D OE1   1 
ATOM   6938 N NE2   . GLN D 1 79  ? -8.018  -0.829  18.726  1.00 115.64 ? 51  GLN D NE2   1 
ATOM   6939 N N     . THR D 1 80  ? -5.387  -3.137  24.066  1.00 100.03 ? 52  THR D N     1 
ATOM   6940 C CA    . THR D 1 80  ? -4.297  -3.217  25.029  1.00 96.63  ? 52  THR D CA    1 
ATOM   6941 C C     . THR D 1 80  ? -3.608  -4.569  24.889  1.00 96.11  ? 52  THR D C     1 
ATOM   6942 O O     . THR D 1 80  ? -4.280  -5.604  24.966  1.00 94.37  ? 52  THR D O     1 
ATOM   6943 C CB    . THR D 1 80  ? -4.812  -3.030  26.450  1.00 92.82  ? 52  THR D CB    1 
ATOM   6944 O OG1   . THR D 1 80  ? -5.474  -1.764  26.556  1.00 97.22  ? 52  THR D OG1   1 
ATOM   6945 C CG2   . THR D 1 80  ? -3.658  -3.074  27.443  1.00 88.43  ? 52  THR D CG2   1 
ATOM   6946 N N     . PRO D 1 81  ? -2.294  -4.608  24.670  1.00 90.28  ? 53  PRO D N     1 
ATOM   6947 C CA    . PRO D 1 81  ? -1.629  -5.888  24.393  1.00 82.60  ? 53  PRO D CA    1 
ATOM   6948 C C     . PRO D 1 81  ? -1.756  -6.865  25.553  1.00 76.22  ? 53  PRO D C     1 
ATOM   6949 O O     . PRO D 1 81  ? -1.687  -6.487  26.724  1.00 74.67  ? 53  PRO D O     1 
ATOM   6950 C CB    . PRO D 1 81  ? -0.168  -5.488  24.160  1.00 78.38  ? 53  PRO D CB    1 
ATOM   6951 C CG    . PRO D 1 81  ? -0.211  -4.048  23.787  1.00 78.54  ? 53  PRO D CG    1 
ATOM   6952 C CD    . PRO D 1 81  ? -1.394  -3.456  24.492  1.00 87.62  ? 53  PRO D CD    1 
ATOM   6953 N N     . LEU D 1 82  ? -1.949  -8.137  25.208  1.00 74.49  ? 54  LEU D N     1 
ATOM   6954 C CA    . LEU D 1 82  ? -1.962  -9.253  26.136  1.00 69.78  ? 54  LEU D CA    1 
ATOM   6955 C C     . LEU D 1 82  ? -0.730  -10.126 25.917  1.00 64.96  ? 54  LEU D C     1 
ATOM   6956 O O     . LEU D 1 82  ? -0.188  -10.171 24.808  1.00 61.36  ? 54  LEU D O     1 
ATOM   6957 C CB    . LEU D 1 82  ? -3.226  -10.105 25.967  1.00 71.53  ? 54  LEU D CB    1 
ATOM   6958 C CG    . LEU D 1 82  ? -4.556  -9.428  26.300  1.00 72.98  ? 54  LEU D CG    1 
ATOM   6959 C CD1   . LEU D 1 82  ? -5.720  -10.369 26.027  1.00 66.67  ? 54  LEU D CD1   1 
ATOM   6960 C CD2   . LEU D 1 82  ? -4.570  -8.956  27.746  1.00 71.08  ? 54  LEU D CD2   1 
ATOM   6961 N N     . PRO D 1 83  ? -0.254  -10.822 26.950  1.00 61.15  ? 55  PRO D N     1 
ATOM   6962 C CA    . PRO D 1 83  ? 0.936   -11.663 26.777  1.00 54.95  ? 55  PRO D CA    1 
ATOM   6963 C C     . PRO D 1 83  ? 0.686   -12.795 25.790  1.00 56.30  ? 55  PRO D C     1 
ATOM   6964 O O     . PRO D 1 83  ? -0.428  -13.308 25.663  1.00 57.15  ? 55  PRO D O     1 
ATOM   6965 C CB    . PRO D 1 83  ? 1.210   -12.199 28.188  1.00 55.40  ? 55  PRO D CB    1 
ATOM   6966 C CG    . PRO D 1 83  ? 0.433   -11.324 29.113  1.00 58.61  ? 55  PRO D CG    1 
ATOM   6967 C CD    . PRO D 1 83  ? -0.731  -10.797 28.343  1.00 61.65  ? 55  PRO D CD    1 
ATOM   6968 N N     . VAL D 1 84  ? 1.747   -13.175 25.080  1.00 52.30  ? 56  VAL D N     1 
ATOM   6969 C CA    . VAL D 1 84  ? 1.706   -14.233 24.078  1.00 49.69  ? 56  VAL D CA    1 
ATOM   6970 C C     . VAL D 1 84  ? 2.593   -15.377 24.549  1.00 51.85  ? 56  VAL D C     1 
ATOM   6971 O O     . VAL D 1 84  ? 3.694   -15.149 25.064  1.00 52.88  ? 56  VAL D O     1 
ATOM   6972 C CB    . VAL D 1 84  ? 2.152   -13.714 22.694  1.00 47.31  ? 56  VAL D CB    1 
ATOM   6973 C CG1   . VAL D 1 84  ? 2.434   -14.865 21.746  1.00 50.65  ? 56  VAL D CG1   1 
ATOM   6974 C CG2   . VAL D 1 84  ? 1.090   -12.799 22.111  1.00 54.19  ? 56  VAL D CG2   1 
ATOM   6975 N N     . LEU D 1 85  ? 2.111   -16.606 24.377  1.00 49.99  ? 57  LEU D N     1 
ATOM   6976 C CA    . LEU D 1 85  ? 2.788   -17.796 24.873  1.00 52.72  ? 57  LEU D CA    1 
ATOM   6977 C C     . LEU D 1 85  ? 3.220   -18.681 23.712  1.00 54.88  ? 57  LEU D C     1 
ATOM   6978 O O     . LEU D 1 85  ? 2.413   -18.999 22.832  1.00 53.58  ? 57  LEU D O     1 
ATOM   6979 C CB    . LEU D 1 85  ? 1.882   -18.582 25.823  1.00 52.73  ? 57  LEU D CB    1 
ATOM   6980 C CG    . LEU D 1 85  ? 2.458   -19.883 26.382  1.00 47.94  ? 57  LEU D CG    1 
ATOM   6981 C CD1   . LEU D 1 85  ? 3.665   -19.600 27.262  1.00 47.81  ? 57  LEU D CD1   1 
ATOM   6982 C CD2   . LEU D 1 85  ? 1.397   -20.644 27.153  1.00 40.54  ? 57  LEU D CD2   1 
ATOM   6983 N N     . ASP D 1 86  ? 4.492   -19.079 23.718  1.00 52.79  ? 58  ASP D N     1 
ATOM   6984 C CA    . ASP D 1 86  ? 5.036   -20.058 22.784  1.00 52.66  ? 58  ASP D CA    1 
ATOM   6985 C C     . ASP D 1 86  ? 5.365   -21.316 23.576  1.00 53.41  ? 58  ASP D C     1 
ATOM   6986 O O     . ASP D 1 86  ? 6.252   -21.298 24.437  1.00 55.61  ? 58  ASP D O     1 
ATOM   6987 C CB    . ASP D 1 86  ? 6.276   -19.514 22.074  1.00 53.65  ? 58  ASP D CB    1 
ATOM   6988 C CG    . ASP D 1 86  ? 6.828   -20.480 21.037  1.00 64.21  ? 58  ASP D CG    1 
ATOM   6989 O OD1   . ASP D 1 86  ? 6.090   -21.394 20.613  1.00 66.27  ? 58  ASP D OD1   1 
ATOM   6990 O OD2   . ASP D 1 86  ? 8.005   -20.326 20.645  1.00 63.88  ? 58  ASP D OD2   1 
ATOM   6991 N N     . ILE D 1 87  ? 4.656   -22.405 23.291  1.00 53.85  ? 59  ILE D N     1 
ATOM   6992 C CA    . ILE D 1 87  ? 4.811   -23.658 24.019  1.00 47.24  ? 59  ILE D CA    1 
ATOM   6993 C C     . ILE D 1 87  ? 5.735   -24.564 23.219  1.00 52.88  ? 59  ILE D C     1 
ATOM   6994 O O     . ILE D 1 87  ? 5.576   -24.702 21.999  1.00 56.25  ? 59  ILE D O     1 
ATOM   6995 C CB    . ILE D 1 87  ? 3.452   -24.332 24.267  1.00 44.59  ? 59  ILE D CB    1 
ATOM   6996 C CG1   . ILE D 1 87  ? 2.535   -23.395 25.051  1.00 50.59  ? 59  ILE D CG1   1 
ATOM   6997 C CG2   . ILE D 1 87  ? 3.635   -25.603 25.072  1.00 46.58  ? 59  ILE D CG2   1 
ATOM   6998 C CD1   . ILE D 1 87  ? 1.146   -23.947 25.275  1.00 51.50  ? 59  ILE D CD1   1 
ATOM   6999 N N     . GLY D 1 88  ? 6.702   -25.177 23.899  1.00 52.96  ? 60  GLY D N     1 
ATOM   7000 C CA    . GLY D 1 88  ? 7.688   -26.000 23.229  1.00 46.70  ? 60  GLY D CA    1 
ATOM   7001 C C     . GLY D 1 88  ? 8.554   -25.190 22.288  1.00 48.83  ? 60  GLY D C     1 
ATOM   7002 O O     . GLY D 1 88  ? 8.696   -25.531 21.110  1.00 57.78  ? 60  GLY D O     1 
ATOM   7003 N N     . CYS D 1 89  ? 9.139   -24.108 22.805  1.00 48.98  ? 61  CYS D N     1 
ATOM   7004 C CA    . CYS D 1 89  ? 9.892   -23.182 21.969  1.00 52.10  ? 61  CYS D CA    1 
ATOM   7005 C C     . CYS D 1 89  ? 11.240  -23.740 21.534  1.00 53.81  ? 61  CYS D C     1 
ATOM   7006 O O     . CYS D 1 89  ? 11.833  -23.217 20.584  1.00 49.82  ? 61  CYS D O     1 
ATOM   7007 C CB    . CYS D 1 89  ? 10.106  -21.864 22.713  1.00 50.18  ? 61  CYS D CB    1 
ATOM   7008 S SG    . CYS D 1 89  ? 11.128  -22.024 24.195  1.00 49.18  ? 61  CYS D SG    1 
ATOM   7009 N N     . GLY D 1 90  ? 11.737  -24.777 22.203  1.00 54.35  ? 62  GLY D N     1 
ATOM   7010 C CA    . GLY D 1 90  ? 13.043  -25.311 21.908  1.00 51.47  ? 62  GLY D CA    1 
ATOM   7011 C C     . GLY D 1 90  ? 14.144  -24.387 22.390  1.00 49.72  ? 62  GLY D C     1 
ATOM   7012 O O     . GLY D 1 90  ? 14.101  -23.863 23.507  1.00 50.58  ? 62  GLY D O     1 
ATOM   7013 N N     . PRO D 1 91  ? 15.159  -24.169 21.551  1.00 48.39  ? 63  PRO D N     1 
ATOM   7014 C CA    . PRO D 1 91  ? 16.254  -23.265 21.923  1.00 43.50  ? 63  PRO D CA    1 
ATOM   7015 C C     . PRO D 1 91  ? 15.904  -21.789 21.833  1.00 45.26  ? 63  PRO D C     1 
ATOM   7016 O O     . PRO D 1 91  ? 16.785  -20.951 22.050  1.00 46.43  ? 63  PRO D O     1 
ATOM   7017 C CB    . PRO D 1 91  ? 17.353  -23.628 20.917  1.00 44.05  ? 63  PRO D CB    1 
ATOM   7018 C CG    . PRO D 1 91  ? 16.617  -24.134 19.731  1.00 47.97  ? 63  PRO D CG    1 
ATOM   7019 C CD    . PRO D 1 91  ? 15.394  -24.827 20.255  1.00 50.08  ? 63  PRO D CD    1 
ATOM   7020 N N     . GLY D 1 92  ? 14.655  -21.445 21.525  1.00 45.58  ? 64  GLY D N     1 
ATOM   7021 C CA    . GLY D 1 92  ? 14.235  -20.059 21.542  1.00 43.69  ? 64  GLY D CA    1 
ATOM   7022 C C     . GLY D 1 92  ? 14.515  -19.278 20.282  1.00 45.46  ? 64  GLY D C     1 
ATOM   7023 O O     . GLY D 1 92  ? 14.560  -18.045 20.329  1.00 46.90  ? 64  GLY D O     1 
ATOM   7024 N N     . ASP D 1 93  ? 14.700  -19.952 19.148  1.00 45.84  ? 65  ASP D N     1 
ATOM   7025 C CA    . ASP D 1 93  ? 14.962  -19.234 17.908  1.00 43.28  ? 65  ASP D CA    1 
ATOM   7026 C C     . ASP D 1 93  ? 13.668  -18.792 17.237  1.00 45.73  ? 65  ASP D C     1 
ATOM   7027 O O     . ASP D 1 93  ? 13.599  -17.688 16.685  1.00 48.90  ? 65  ASP D O     1 
ATOM   7028 C CB    . ASP D 1 93  ? 15.795  -20.100 16.967  1.00 47.00  ? 65  ASP D CB    1 
ATOM   7029 C CG    . ASP D 1 93  ? 17.181  -20.377 17.515  1.00 54.04  ? 65  ASP D CG    1 
ATOM   7030 O OD1   . ASP D 1 93  ? 18.038  -19.472 17.453  1.00 60.07  ? 65  ASP D OD1   1 
ATOM   7031 O OD2   . ASP D 1 93  ? 17.413  -21.503 18.001  1.00 51.51  ? 65  ASP D OD2   1 
ATOM   7032 N N     . ILE D 1 94  ? 12.636  -19.636 17.270  1.00 45.16  ? 66  ILE D N     1 
ATOM   7033 C CA    . ILE D 1 94  ? 11.324  -19.211 16.795  1.00 44.61  ? 66  ILE D CA    1 
ATOM   7034 C C     . ILE D 1 94  ? 10.765  -18.119 17.700  1.00 44.73  ? 66  ILE D C     1 
ATOM   7035 O O     . ILE D 1 94  ? 10.138  -17.162 17.230  1.00 43.99  ? 66  ILE D O     1 
ATOM   7036 C CB    . ILE D 1 94  ? 10.375  -20.420 16.697  1.00 49.86  ? 66  ILE D CB    1 
ATOM   7037 C CG1   . ILE D 1 94  ? 10.632  -21.194 15.403  1.00 46.96  ? 66  ILE D CG1   1 
ATOM   7038 C CG2   . ILE D 1 94  ? 8.916   -19.985 16.787  1.00 51.65  ? 66  ILE D CG2   1 
ATOM   7039 C CD1   . ILE D 1 94  ? 9.822   -22.461 15.285  1.00 48.37  ? 66  ILE D CD1   1 
ATOM   7040 N N     . ALA D 1 95  ? 11.003  -18.232 19.008  1.00 44.91  ? 67  ALA D N     1 
ATOM   7041 C CA    . ALA D 1 95  ? 10.505  -17.229 19.942  1.00 43.35  ? 67  ALA D CA    1 
ATOM   7042 C C     . ALA D 1 95  ? 11.189  -15.884 19.734  1.00 39.88  ? 67  ALA D C     1 
ATOM   7043 O O     . ALA D 1 95  ? 10.532  -14.837 19.763  1.00 46.29  ? 67  ALA D O     1 
ATOM   7044 C CB    . ALA D 1 95  ? 10.697  -17.712 21.379  1.00 46.73  ? 67  ALA D CB    1 
ATOM   7045 N N     . ARG D 1 96  ? 12.504  -15.888 19.514  1.00 36.70  ? 68  ARG D N     1 
ATOM   7046 C CA    . ARG D 1 96  ? 13.229  -14.628 19.385  1.00 40.60  ? 68  ARG D CA    1 
ATOM   7047 C C     . ARG D 1 96  ? 13.160  -14.076 17.966  1.00 44.77  ? 68  ARG D C     1 
ATOM   7048 O O     . ARG D 1 96  ? 12.809  -12.908 17.765  1.00 45.76  ? 68  ARG D O     1 
ATOM   7049 C CB    . ARG D 1 96  ? 14.687  -14.809 19.813  1.00 44.34  ? 68  ARG D CB    1 
ATOM   7050 C CG    . ARG D 1 96  ? 15.608  -13.723 19.274  1.00 49.13  ? 68  ARG D CG    1 
ATOM   7051 C CD    . ARG D 1 96  ? 15.332  -12.382 19.935  1.00 53.75  ? 68  ARG D CD    1 
ATOM   7052 N NE    . ARG D 1 96  ? 15.929  -11.279 19.191  1.00 59.63  ? 68  ARG D NE    1 
ATOM   7053 C CZ    . ARG D 1 96  ? 16.534  -10.238 19.746  1.00 64.99  ? 68  ARG D CZ    1 
ATOM   7054 N NH1   . ARG D 1 96  ? 16.670  -10.136 21.057  1.00 68.57  ? 68  ARG D NH1   1 
ATOM   7055 N NH2   . ARG D 1 96  ? 17.013  -9.274  18.964  1.00 61.85  ? 68  ARG D NH2   1 
ATOM   7056 N N     . LYS D 1 97  ? 13.494  -14.895 16.970  1.00 45.66  ? 69  LYS D N     1 
ATOM   7057 C CA    . LYS D 1 97  ? 13.711  -14.394 15.619  1.00 43.26  ? 69  LYS D CA    1 
ATOM   7058 C C     . LYS D 1 97  ? 12.455  -14.374 14.756  1.00 41.65  ? 69  LYS D C     1 
ATOM   7059 O O     . LYS D 1 97  ? 12.454  -13.711 13.713  1.00 44.85  ? 69  LYS D O     1 
ATOM   7060 C CB    . LYS D 1 97  ? 14.787  -15.230 14.918  1.00 47.84  ? 69  LYS D CB    1 
ATOM   7061 C CG    . LYS D 1 97  ? 16.148  -15.174 15.594  1.00 48.55  ? 69  LYS D CG    1 
ATOM   7062 C CD    . LYS D 1 97  ? 17.141  -16.102 14.916  1.00 47.88  ? 69  LYS D CD    1 
ATOM   7063 C CE    . LYS D 1 97  ? 18.458  -16.142 15.671  1.00 57.58  ? 69  LYS D CE    1 
ATOM   7064 N NZ    . LYS D 1 97  ? 19.392  -17.153 15.102  1.00 78.02  ? 69  LYS D NZ    1 
ATOM   7065 N N     . VAL D 1 98  ? 11.396  -15.073 15.151  1.00 41.26  ? 70  VAL D N     1 
ATOM   7066 C CA    . VAL D 1 98  ? 10.181  -15.180 14.353  1.00 38.26  ? 70  VAL D CA    1 
ATOM   7067 C C     . VAL D 1 98  ? 9.003   -14.487 15.028  1.00 45.32  ? 70  VAL D C     1 
ATOM   7068 O O     . VAL D 1 98  ? 8.352   -13.629 14.432  1.00 52.16  ? 70  VAL D O     1 
ATOM   7069 C CB    . VAL D 1 98  ? 9.848   -16.658 14.045  1.00 42.44  ? 70  VAL D CB    1 
ATOM   7070 C CG1   . VAL D 1 98  ? 8.607   -16.750 13.173  1.00 45.40  ? 70  VAL D CG1   1 
ATOM   7071 C CG2   . VAL D 1 98  ? 11.024  -17.337 13.376  1.00 52.45  ? 70  VAL D CG2   1 
ATOM   7072 N N     . LEU D 1 99  ? 8.715   -14.849 16.279  1.00 37.96  ? 71  LEU D N     1 
ATOM   7073 C CA    . LEU D 1 99  ? 7.526   -14.329 16.946  1.00 45.66  ? 71  LEU D CA    1 
ATOM   7074 C C     . LEU D 1 99  ? 7.728   -12.896 17.429  1.00 50.31  ? 71  LEU D C     1 
ATOM   7075 O O     . LEU D 1 99  ? 6.856   -12.043 17.235  1.00 53.64  ? 71  LEU D O     1 
ATOM   7076 C CB    . LEU D 1 99  ? 7.141   -15.237 18.115  1.00 45.47  ? 71  LEU D CB    1 
ATOM   7077 C CG    . LEU D 1 99  ? 6.487   -16.571 17.750  1.00 47.61  ? 71  LEU D CG    1 
ATOM   7078 C CD1   . LEU D 1 99  ? 6.283   -17.428 18.989  1.00 53.55  ? 71  LEU D CD1   1 
ATOM   7079 C CD2   . LEU D 1 99  ? 5.165   -16.339 17.036  1.00 49.93  ? 71  LEU D CD2   1 
ATOM   7080 N N     . ALA D 1 100 ? 8.873   -12.616 18.054  1.00 48.03  ? 72  ALA D N     1 
ATOM   7081 C CA    . ALA D 1 100 ? 9.073   -11.316 18.695  1.00 43.62  ? 72  ALA D CA    1 
ATOM   7082 C C     . ALA D 1 100 ? 8.990   -10.141 17.728  1.00 46.15  ? 72  ALA D C     1 
ATOM   7083 O O     . ALA D 1 100 ? 8.284   -9.167  18.042  1.00 55.60  ? 72  ALA D O     1 
ATOM   7084 C CB    . ALA D 1 100 ? 10.400  -11.320 19.462  1.00 42.44  ? 72  ALA D CB    1 
ATOM   7085 N N     . PRO D 1 101 ? 9.660   -10.142 16.568  1.00 41.73  ? 73  PRO D N     1 
ATOM   7086 C CA    . PRO D 1 101 ? 9.542   -8.973  15.680  1.00 49.53  ? 73  PRO D CA    1 
ATOM   7087 C C     . PRO D 1 101 ? 8.145   -8.778  15.115  1.00 56.46  ? 73  PRO D C     1 
ATOM   7088 O O     . PRO D 1 101 ? 7.762   -7.638  14.826  1.00 59.03  ? 73  PRO D O     1 
ATOM   7089 C CB    . PRO D 1 101 ? 10.557  -9.267  14.566  1.00 49.25  ? 73  PRO D CB    1 
ATOM   7090 C CG    . PRO D 1 101 ? 11.497  -10.255 15.152  1.00 48.46  ? 73  PRO D CG    1 
ATOM   7091 C CD    . PRO D 1 101 ? 10.662  -11.097 16.062  1.00 45.01  ? 73  PRO D CD    1 
ATOM   7092 N N     . ARG D 1 102 ? 7.373   -9.850  14.954  1.00 58.32  ? 74  ARG D N     1 
ATOM   7093 C CA    . ARG D 1 102 ? 6.065   -9.767  14.320  1.00 62.78  ? 74  ARG D CA    1 
ATOM   7094 C C     . ARG D 1 102 ? 4.946   -9.391  15.283  1.00 66.15  ? 74  ARG D C     1 
ATOM   7095 O O     . ARG D 1 102 ? 3.856   -9.029  14.826  1.00 69.76  ? 74  ARG D O     1 
ATOM   7096 C CB    . ARG D 1 102 ? 5.734   -11.099 13.635  1.00 61.24  ? 74  ARG D CB    1 
ATOM   7097 C CG    . ARG D 1 102 ? 6.533   -11.337 12.362  1.00 61.46  ? 74  ARG D CG    1 
ATOM   7098 C CD    . ARG D 1 102 ? 6.448   -12.779 11.891  1.00 60.54  ? 74  ARG D CD    1 
ATOM   7099 N NE    . ARG D 1 102 ? 7.071   -12.953 10.584  1.00 64.12  ? 74  ARG D NE    1 
ATOM   7100 C CZ    . ARG D 1 102 ? 8.377   -13.072 10.385  1.00 60.55  ? 74  ARG D CZ    1 
ATOM   7101 N NH1   . ARG D 1 102 ? 9.235   -13.046 11.391  1.00 55.32  ? 74  ARG D NH1   1 
ATOM   7102 N NH2   . ARG D 1 102 ? 8.833   -13.220 9.144   1.00 61.31  ? 74  ARG D NH2   1 
ATOM   7103 N N     . LEU D 1 103 ? 5.182   -9.458  16.592  1.00 65.86  ? 75  LEU D N     1 
ATOM   7104 C CA    . LEU D 1 103 ? 4.152   -9.114  17.558  1.00 65.60  ? 75  LEU D CA    1 
ATOM   7105 C C     . LEU D 1 103 ? 3.911   -7.606  17.583  1.00 68.09  ? 75  LEU D C     1 
ATOM   7106 O O     . LEU D 1 103 ? 4.785   -6.818  17.215  1.00 62.28  ? 75  LEU D O     1 
ATOM   7107 C CB    . LEU D 1 103 ? 4.544   -9.594  18.954  1.00 56.74  ? 75  LEU D CB    1 
ATOM   7108 C CG    . LEU D 1 103 ? 4.562   -11.101 19.208  1.00 57.23  ? 75  LEU D CG    1 
ATOM   7109 C CD1   . LEU D 1 103 ? 5.192   -11.403 20.558  1.00 55.19  ? 75  LEU D CD1   1 
ATOM   7110 C CD2   . LEU D 1 103 ? 3.154   -11.669 19.130  1.00 62.72  ? 75  LEU D CD2   1 
ATOM   7111 N N     . PRO D 1 104 ? 2.719   -7.182  18.007  1.00 70.16  ? 76  PRO D N     1 
ATOM   7112 C CA    . PRO D 1 104 ? 2.479   -5.751  18.214  1.00 68.80  ? 76  PRO D CA    1 
ATOM   7113 C C     . PRO D 1 104 ? 3.388   -5.196  19.301  1.00 65.86  ? 76  PRO D C     1 
ATOM   7114 O O     . PRO D 1 104 ? 3.868   -5.917  20.179  1.00 65.42  ? 76  PRO D O     1 
ATOM   7115 C CB    . PRO D 1 104 ? 1.005   -5.690  18.634  1.00 68.66  ? 76  PRO D CB    1 
ATOM   7116 C CG    . PRO D 1 104 ? 0.407   -6.959  18.123  1.00 69.77  ? 76  PRO D CG    1 
ATOM   7117 C CD    . PRO D 1 104 ? 1.497   -7.983  18.196  1.00 68.39  ? 76  PRO D CD    1 
ATOM   7118 N N     . ALA D 1 105 ? 3.626   -3.888  19.229  1.00 66.60  ? 77  ALA D N     1 
ATOM   7119 C CA    . ALA D 1 105 ? 4.485   -3.234  20.206  1.00 64.17  ? 77  ALA D CA    1 
ATOM   7120 C C     . ALA D 1 105 ? 3.856   -3.290  21.592  1.00 63.46  ? 77  ALA D C     1 
ATOM   7121 O O     . ALA D 1 105 ? 2.641   -3.136  21.750  1.00 61.87  ? 77  ALA D O     1 
ATOM   7122 C CB    . ALA D 1 105 ? 4.743   -1.782  19.799  1.00 64.59  ? 77  ALA D CB    1 
ATOM   7123 N N     . GLY D 1 106 ? 4.694   -3.516  22.603  1.00 60.60  ? 78  GLY D N     1 
ATOM   7124 C CA    . GLY D 1 106 ? 4.233   -3.654  23.966  1.00 61.13  ? 78  GLY D CA    1 
ATOM   7125 C C     . GLY D 1 106 ? 3.760   -5.038  24.348  1.00 59.87  ? 78  GLY D C     1 
ATOM   7126 O O     . GLY D 1 106 ? 3.559   -5.297  25.541  1.00 57.70  ? 78  GLY D O     1 
ATOM   7127 N N     . THR D 1 107 ? 3.574   -5.935  23.383  1.00 63.76  ? 79  THR D N     1 
ATOM   7128 C CA    . THR D 1 107 ? 3.128   -7.292  23.669  1.00 61.74  ? 79  THR D CA    1 
ATOM   7129 C C     . THR D 1 107 ? 4.289   -8.110  24.222  1.00 62.68  ? 79  THR D C     1 
ATOM   7130 O O     . THR D 1 107 ? 5.334   -8.233  23.574  1.00 61.72  ? 79  THR D O     1 
ATOM   7131 C CB    . THR D 1 107 ? 2.568   -7.948  22.408  1.00 60.39  ? 79  THR D CB    1 
ATOM   7132 O OG1   . THR D 1 107 ? 1.466   -7.175  21.912  1.00 64.24  ? 79  THR D OG1   1 
ATOM   7133 C CG2   . THR D 1 107 ? 2.100   -9.359  22.706  1.00 60.03  ? 79  THR D CG2   1 
ATOM   7134 N N     . ARG D 1 108 ? 4.105   -8.668  25.415  1.00 60.49  ? 80  ARG D N     1 
ATOM   7135 C CA    . ARG D 1 108 ? 5.124   -9.487  26.050  1.00 52.78  ? 80  ARG D CA    1 
ATOM   7136 C C     . ARG D 1 108 ? 5.013   -10.929 25.573  1.00 52.99  ? 80  ARG D C     1 
ATOM   7137 O O     . ARG D 1 108 ? 3.933   -11.402 25.206  1.00 51.44  ? 80  ARG D O     1 
ATOM   7138 C CB    . ARG D 1 108 ? 4.993   -9.426  27.573  1.00 53.94  ? 80  ARG D CB    1 
ATOM   7139 C CG    . ARG D 1 108 ? 5.507   -8.129  28.176  1.00 56.54  ? 80  ARG D CG    1 
ATOM   7140 C CD    . ARG D 1 108 ? 5.606   -8.210  29.689  1.00 62.01  ? 80  ARG D CD    1 
ATOM   7141 N NE    . ARG D 1 108 ? 5.612   -6.884  30.295  1.00 79.11  ? 80  ARG D NE    1 
ATOM   7142 C CZ    . ARG D 1 108 ? 4.521   -6.235  30.679  1.00 81.65  ? 80  ARG D CZ    1 
ATOM   7143 N NH1   . ARG D 1 108 ? 3.315   -6.760  30.528  1.00 81.37  ? 80  ARG D NH1   1 
ATOM   7144 N NH2   . ARG D 1 108 ? 4.640   -5.025  31.220  1.00 80.38  ? 80  ARG D NH2   1 
ATOM   7145 N N     . LEU D 1 109 ? 6.144   -11.628 25.581  1.00 50.72  ? 81  LEU D N     1 
ATOM   7146 C CA    . LEU D 1 109 ? 6.232   -12.992 25.080  1.00 47.36  ? 81  LEU D CA    1 
ATOM   7147 C C     . LEU D 1 109 ? 6.755   -13.917 26.169  1.00 42.64  ? 81  LEU D C     1 
ATOM   7148 O O     . LEU D 1 109 ? 7.690   -13.572 26.897  1.00 39.87  ? 81  LEU D O     1 
ATOM   7149 C CB    . LEU D 1 109 ? 7.139   -13.066 23.845  1.00 46.04  ? 81  LEU D CB    1 
ATOM   7150 C CG    . LEU D 1 109 ? 7.373   -14.451 23.235  1.00 43.58  ? 81  LEU D CG    1 
ATOM   7151 C CD1   . LEU D 1 109 ? 6.058   -15.075 22.806  1.00 48.61  ? 81  LEU D CD1   1 
ATOM   7152 C CD2   . LEU D 1 109 ? 8.329   -14.357 22.058  1.00 40.58  ? 81  LEU D CD2   1 
ATOM   7153 N N     . VAL D 1 110 ? 6.138   -15.092 26.277  1.00 40.47  ? 82  VAL D N     1 
ATOM   7154 C CA    . VAL D 1 110 ? 6.554   -16.133 27.208  1.00 38.98  ? 82  VAL D CA    1 
ATOM   7155 C C     . VAL D 1 110 ? 6.783   -17.410 26.412  1.00 46.09  ? 82  VAL D C     1 
ATOM   7156 O O     . VAL D 1 110 ? 5.940   -17.794 25.594  1.00 53.28  ? 82  VAL D O     1 
ATOM   7157 C CB    . VAL D 1 110 ? 5.510   -16.364 28.318  1.00 39.13  ? 82  VAL D CB    1 
ATOM   7158 C CG1   . VAL D 1 110 ? 6.000   -17.416 29.301  1.00 39.05  ? 82  VAL D CG1   1 
ATOM   7159 C CG2   . VAL D 1 110 ? 5.204   -15.060 29.037  1.00 43.89  ? 82  VAL D CG2   1 
ATOM   7160 N N     . ALA D 1 111 ? 7.920   -18.060 26.644  1.00 42.98  ? 83  ALA D N     1 
ATOM   7161 C CA    . ALA D 1 111 ? 8.291   -19.269 25.921  1.00 43.67  ? 83  ALA D CA    1 
ATOM   7162 C C     . ALA D 1 111 ? 8.679   -20.350 26.918  1.00 40.53  ? 83  ALA D C     1 
ATOM   7163 O O     . ALA D 1 111 ? 9.515   -20.117 27.796  1.00 40.77  ? 83  ALA D O     1 
ATOM   7164 C CB    . ALA D 1 111 ? 9.442   -18.997 24.948  1.00 39.22  ? 83  ALA D CB    1 
ATOM   7165 N N     . CYS D 1 112 ? 8.075   -21.526 26.781  1.00 41.27  ? 84  CYS D N     1 
ATOM   7166 C CA    . CYS D 1 112 ? 8.277   -22.623 27.714  1.00 42.41  ? 84  CYS D CA    1 
ATOM   7167 C C     . CYS D 1 112 ? 8.757   -23.869 26.980  1.00 43.25  ? 84  CYS D C     1 
ATOM   7168 O O     . CYS D 1 112 ? 8.729   -23.951 25.749  1.00 47.55  ? 84  CYS D O     1 
ATOM   7169 C CB    . CYS D 1 112 ? 6.989   -22.930 28.488  1.00 42.75  ? 84  CYS D CB    1 
ATOM   7170 S SG    . CYS D 1 112 ? 5.502   -22.940 27.469  1.00 53.97  ? 84  CYS D SG    1 
ATOM   7171 N N     . ASP D 1 113 ? 9.187   -24.852 27.773  1.00 44.36  ? 85  ASP D N     1 
ATOM   7172 C CA    . ASP D 1 113 ? 9.739   -26.108 27.280  1.00 45.37  ? 85  ASP D CA    1 
ATOM   7173 C C     . ASP D 1 113 ? 10.018  -27.015 28.472  1.00 46.57  ? 85  ASP D C     1 
ATOM   7174 O O     . ASP D 1 113 ? 10.429  -26.525 29.529  1.00 46.56  ? 85  ASP D O     1 
ATOM   7175 C CB    . ASP D 1 113 ? 11.021  -25.854 26.482  1.00 45.18  ? 85  ASP D CB    1 
ATOM   7176 C CG    . ASP D 1 113 ? 11.403  -27.021 25.596  1.00 53.23  ? 85  ASP D CG    1 
ATOM   7177 O OD1   . ASP D 1 113 ? 11.811  -28.073 26.132  1.00 56.67  ? 85  ASP D OD1   1 
ATOM   7178 O OD2   . ASP D 1 113 ? 11.306  -26.878 24.358  1.00 53.22  ? 85  ASP D OD2   1 
ATOM   7179 N N     . ILE D 1 114 ? 9.796   -28.327 28.336  1.00 47.68  ? 86  ILE D N     1 
ATOM   7180 C CA    . ILE D 1 114 ? 10.088  -29.228 29.451  1.00 48.92  ? 86  ILE D CA    1 
ATOM   7181 C C     . ILE D 1 114 ? 11.580  -29.239 29.749  1.00 52.19  ? 86  ILE D C     1 
ATOM   7182 O O     . ILE D 1 114 ? 11.999  -29.121 30.906  1.00 53.59  ? 86  ILE D O     1 
ATOM   7183 C CB    . ILE D 1 114 ? 9.579   -30.654 29.174  1.00 51.13  ? 86  ILE D CB    1 
ATOM   7184 C CG1   . ILE D 1 114 ? 8.067   -30.701 29.021  1.00 51.08  ? 86  ILE D CG1   1 
ATOM   7185 C CG2   . ILE D 1 114 ? 9.989   -31.585 30.300  1.00 60.04  ? 86  ILE D CG2   1 
ATOM   7186 C CD1   . ILE D 1 114 ? 7.581   -32.087 28.670  1.00 53.22  ? 86  ILE D CD1   1 
ATOM   7187 N N     . SER D 1 115 ? 12.400  -29.396 28.711  1.00 49.34  ? 87  SER D N     1 
ATOM   7188 C CA    . SER D 1 115 ? 13.843  -29.549 28.846  1.00 50.17  ? 87  SER D CA    1 
ATOM   7189 C C     . SER D 1 115 ? 14.468  -28.348 29.544  1.00 49.22  ? 87  SER D C     1 
ATOM   7190 O O     . SER D 1 115 ? 14.442  -27.233 29.007  1.00 49.15  ? 87  SER D O     1 
ATOM   7191 C CB    . SER D 1 115 ? 14.486  -29.751 27.473  1.00 54.19  ? 87  SER D CB    1 
ATOM   7192 O OG    . SER D 1 115 ? 15.846  -29.353 27.482  1.00 57.77  ? 87  SER D OG    1 
ATOM   7193 N N     . PRO D 1 116 ? 15.027  -28.529 30.743  1.00 49.99  ? 88  PRO D N     1 
ATOM   7194 C CA    . PRO D 1 116 ? 15.784  -27.433 31.366  1.00 49.50  ? 88  PRO D CA    1 
ATOM   7195 C C     . PRO D 1 116 ? 17.029  -27.068 30.587  1.00 49.35  ? 88  PRO D C     1 
ATOM   7196 O O     . PRO D 1 116 ? 17.521  -25.941 30.721  1.00 48.64  ? 88  PRO D O     1 
ATOM   7197 C CB    . PRO D 1 116 ? 16.133  -27.987 32.755  1.00 50.68  ? 88  PRO D CB    1 
ATOM   7198 C CG    . PRO D 1 116 ? 15.193  -29.135 32.970  1.00 51.48  ? 88  PRO D CG    1 
ATOM   7199 C CD    . PRO D 1 116 ? 14.953  -29.713 31.613  1.00 51.39  ? 88  PRO D CD    1 
ATOM   7200 N N     . GLU D 1 117 ? 17.555  -27.992 29.779  1.00 50.53  ? 89  GLU D N     1 
ATOM   7201 C CA    . GLU D 1 117 ? 18.676  -27.669 28.904  1.00 50.42  ? 89  GLU D CA    1 
ATOM   7202 C C     . GLU D 1 117 ? 18.280  -26.612 27.881  1.00 48.99  ? 89  GLU D C     1 
ATOM   7203 O O     . GLU D 1 117 ? 19.072  -25.718 27.561  1.00 48.47  ? 89  GLU D O     1 
ATOM   7204 C CB    . GLU D 1 117 ? 19.179  -28.932 28.200  1.00 51.57  ? 89  GLU D CB    1 
ATOM   7205 C CG    . GLU D 1 117 ? 19.479  -30.118 29.116  1.00 53.11  ? 89  GLU D CG    1 
ATOM   7206 C CD    . GLU D 1 117 ? 18.230  -30.865 29.558  1.00 59.57  ? 89  GLU D CD    1 
ATOM   7207 O OE1   . GLU D 1 117 ? 17.483  -31.351 28.684  1.00 64.63  ? 89  GLU D OE1   1 
ATOM   7208 O OE2   . GLU D 1 117 ? 18.001  -30.973 30.781  1.00 66.03  ? 89  GLU D OE2   1 
ATOM   7209 N N     . MET D 1 118 ? 17.055  -26.698 27.357  1.00 48.30  ? 90  MET D N     1 
ATOM   7210 C CA    . MET D 1 118 ? 16.563  -25.679 26.435  1.00 46.63  ? 90  MET D CA    1 
ATOM   7211 C C     . MET D 1 118 ? 16.402  -24.335 27.135  1.00 45.65  ? 90  MET D C     1 
ATOM   7212 O O     . MET D 1 118 ? 16.850  -23.301 26.625  1.00 44.85  ? 90  MET D O     1 
ATOM   7213 C CB    . MET D 1 118 ? 15.235  -26.123 25.819  1.00 46.38  ? 90  MET D CB    1 
ATOM   7214 C CG    . MET D 1 118 ? 15.346  -27.286 24.850  1.00 47.21  ? 90  MET D CG    1 
ATOM   7215 S SD    . MET D 1 118 ? 16.303  -26.841 23.391  1.00 46.84  ? 90  MET D SD    1 
ATOM   7216 C CE    . MET D 1 118 ? 16.082  -28.300 22.379  1.00 52.34  ? 90  MET D CE    1 
ATOM   7217 N N     . VAL D 1 119 ? 15.765  -24.332 28.308  1.00 45.79  ? 91  VAL D N     1 
ATOM   7218 C CA    . VAL D 1 119 ? 15.497  -23.080 29.013  1.00 44.94  ? 91  VAL D CA    1 
ATOM   7219 C C     . VAL D 1 119 ? 16.801  -22.380 29.376  1.00 45.02  ? 91  VAL D C     1 
ATOM   7220 O O     . VAL D 1 119 ? 16.895  -21.147 29.329  1.00 44.14  ? 91  VAL D O     1 
ATOM   7221 C CB    . VAL D 1 119 ? 14.627  -23.349 30.254  1.00 45.30  ? 91  VAL D CB    1 
ATOM   7222 C CG1   . VAL D 1 119 ? 14.416  -22.073 31.052  1.00 44.58  ? 91  VAL D CG1   1 
ATOM   7223 C CG2   . VAL D 1 119 ? 13.294  -23.952 29.840  1.00 45.22  ? 91  VAL D CG2   1 
ATOM   7224 N N     . ASP D 1 120 ? 17.830  -23.152 29.732  1.00 46.15  ? 92  ASP D N     1 
ATOM   7225 C CA    . ASP D 1 120 ? 19.128  -22.554 30.026  1.00 46.39  ? 92  ASP D CA    1 
ATOM   7226 C C     . ASP D 1 120 ? 19.777  -21.997 28.765  1.00 45.81  ? 92  ASP D C     1 
ATOM   7227 O O     . ASP D 1 120 ? 20.421  -20.942 28.805  1.00 50.51  ? 92  ASP D O     1 
ATOM   7228 C CB    . ASP D 1 120 ? 20.042  -23.581 30.692  1.00 47.86  ? 92  ASP D CB    1 
ATOM   7229 C CG    . ASP D 1 120 ? 19.680  -23.829 32.142  1.00 50.37  ? 92  ASP D CG    1 
ATOM   7230 O OD1   . ASP D 1 120 ? 18.933  -23.009 32.716  1.00 47.75  ? 92  ASP D OD1   1 
ATOM   7231 O OD2   . ASP D 1 120 ? 20.143  -24.842 32.708  1.00 51.78  ? 92  ASP D OD2   1 
ATOM   7232 N N     . PHE D 1 121 ? 19.619  -22.693 27.637  1.00 45.88  ? 93  PHE D N     1 
ATOM   7233 C CA    . PHE D 1 121 ? 20.180  -22.207 26.381  1.00 45.39  ? 93  PHE D CA    1 
ATOM   7234 C C     . PHE D 1 121 ? 19.483  -20.931 25.924  1.00 43.98  ? 93  PHE D C     1 
ATOM   7235 O O     . PHE D 1 121 ? 20.120  -20.042 25.345  1.00 49.43  ? 93  PHE D O     1 
ATOM   7236 C CB    . PHE D 1 121 ? 20.074  -23.295 25.310  1.00 45.87  ? 93  PHE D CB    1 
ATOM   7237 C CG    . PHE D 1 121 ? 20.787  -22.963 24.029  1.00 45.64  ? 93  PHE D CG    1 
ATOM   7238 C CD1   . PHE D 1 121 ? 20.162  -22.219 23.041  1.00 44.54  ? 93  PHE D CD1   1 
ATOM   7239 C CD2   . PHE D 1 121 ? 22.082  -23.401 23.810  1.00 53.74  ? 93  PHE D CD2   1 
ATOM   7240 C CE1   . PHE D 1 121 ? 20.817  -21.914 21.864  1.00 47.61  ? 93  PHE D CE1   1 
ATOM   7241 C CE2   . PHE D 1 121 ? 22.742  -23.100 22.634  1.00 56.33  ? 93  PHE D CE2   1 
ATOM   7242 C CZ    . PHE D 1 121 ? 22.109  -22.356 21.659  1.00 51.66  ? 93  PHE D CZ    1 
ATOM   7243 N N     . CYS D 1 122 ? 18.179  -20.821 26.182  1.00 46.30  ? 94  CYS D N     1 
ATOM   7244 C CA    . CYS D 1 122 ? 17.420  -19.660 25.728  1.00 44.32  ? 94  CYS D CA    1 
ATOM   7245 C C     . CYS D 1 122 ? 17.866  -18.390 26.441  1.00 48.68  ? 94  CYS D C     1 
ATOM   7246 O O     . CYS D 1 122 ? 18.088  -17.353 25.804  1.00 55.67  ? 94  CYS D O     1 
ATOM   7247 C CB    . CYS D 1 122 ? 15.926  -19.891 25.951  1.00 41.81  ? 94  CYS D CB    1 
ATOM   7248 S SG    . CYS D 1 122 ? 15.189  -21.211 24.973  1.00 42.20  ? 94  CYS D SG    1 
ATOM   7249 N N     . ARG D 1 123 ? 18.005  -18.453 27.767  1.00 42.20  ? 95  ARG D N     1 
ATOM   7250 C CA    . ARG D 1 123 ? 18.270  -17.262 28.564  1.00 43.76  ? 95  ARG D CA    1 
ATOM   7251 C C     . ARG D 1 123 ? 19.643  -16.655 28.306  1.00 56.11  ? 95  ARG D C     1 
ATOM   7252 O O     . ARG D 1 123 ? 19.936  -15.584 28.849  1.00 61.78  ? 95  ARG D O     1 
ATOM   7253 C CB    . ARG D 1 123 ? 18.120  -17.589 30.050  1.00 45.63  ? 95  ARG D CB    1 
ATOM   7254 C CG    . ARG D 1 123 ? 16.685  -17.859 30.474  1.00 42.74  ? 95  ARG D CG    1 
ATOM   7255 C CD    . ARG D 1 123 ? 16.589  -18.144 31.963  1.00 46.56  ? 95  ARG D CD    1 
ATOM   7256 N NE    . ARG D 1 123 ? 15.220  -18.426 32.377  1.00 42.92  ? 95  ARG D NE    1 
ATOM   7257 C CZ    . ARG D 1 123 ? 14.879  -19.368 33.246  1.00 43.81  ? 95  ARG D CZ    1 
ATOM   7258 N NH1   . ARG D 1 123 ? 15.787  -20.147 33.812  1.00 44.92  ? 95  ARG D NH1   1 
ATOM   7259 N NH2   . ARG D 1 123 ? 13.596  -19.533 33.553  1.00 43.65  ? 95  ARG D NH2   1 
ATOM   7260 N N     . GLN D 1 124 ? 20.485  -17.297 27.498  1.00 57.25  ? 96  GLN D N     1 
ATOM   7261 C CA    . GLN D 1 124 ? 21.794  -16.762 27.148  1.00 57.71  ? 96  GLN D CA    1 
ATOM   7262 C C     . GLN D 1 124 ? 21.872  -16.281 25.707  1.00 58.12  ? 96  GLN D C     1 
ATOM   7263 O O     . GLN D 1 124 ? 22.264  -15.137 25.457  1.00 62.36  ? 96  GLN D O     1 
ATOM   7264 C CB    . GLN D 1 124 ? 22.883  -17.816 27.396  1.00 57.93  ? 96  GLN D CB    1 
ATOM   7265 C CG    . GLN D 1 124 ? 23.243  -18.013 28.857  1.00 67.09  ? 96  GLN D CG    1 
ATOM   7266 C CD    . GLN D 1 124 ? 24.245  -19.132 29.062  1.00 76.85  ? 96  GLN D CD    1 
ATOM   7267 O OE1   . GLN D 1 124 ? 24.951  -19.527 28.133  1.00 75.11  ? 96  GLN D OE1   1 
ATOM   7268 N NE2   . GLN D 1 124 ? 24.316  -19.647 30.284  1.00 72.43  ? 96  GLN D NE2   1 
ATOM   7269 N N     . HIS D 1 125 ? 21.501  -17.126 24.746  1.00 52.03  ? 97  HIS D N     1 
ATOM   7270 C CA    . HIS D 1 125 ? 21.726  -16.822 23.340  1.00 52.96  ? 97  HIS D CA    1 
ATOM   7271 C C     . HIS D 1 125 ? 20.549  -16.126 22.669  1.00 57.06  ? 97  HIS D C     1 
ATOM   7272 O O     . HIS D 1 125 ? 20.750  -15.443 21.658  1.00 66.42  ? 97  HIS D O     1 
ATOM   7273 C CB    . HIS D 1 125 ? 22.069  -18.108 22.581  1.00 51.18  ? 97  HIS D CB    1 
ATOM   7274 C CG    . HIS D 1 125 ? 23.315  -18.778 23.073  1.00 52.08  ? 97  HIS D CG    1 
ATOM   7275 N ND1   . HIS D 1 125 ? 23.329  -19.607 24.174  1.00 56.05  ? 97  HIS D ND1   1 
ATOM   7276 C CD2   . HIS D 1 125 ? 24.590  -18.731 22.621  1.00 54.72  ? 97  HIS D CD2   1 
ATOM   7277 C CE1   . HIS D 1 125 ? 24.558  -20.049 24.375  1.00 54.64  ? 97  HIS D CE1   1 
ATOM   7278 N NE2   . HIS D 1 125 ? 25.343  -19.532 23.447  1.00 52.23  ? 97  HIS D NE2   1 
ATOM   7279 N N     . ASN D 1 126 ? 19.336  -16.275 23.198  1.00 51.75  ? 98  ASN D N     1 
ATOM   7280 C CA    . ASN D 1 126 ? 18.185  -15.570 22.645  1.00 52.61  ? 98  ASN D CA    1 
ATOM   7281 C C     . ASN D 1 126 ? 17.573  -14.645 23.688  1.00 52.47  ? 98  ASN D C     1 
ATOM   7282 O O     . ASN D 1 126 ? 16.356  -14.651 23.898  1.00 52.86  ? 98  ASN D O     1 
ATOM   7283 C CB    . ASN D 1 126 ? 17.140  -16.561 22.127  1.00 49.97  ? 98  ASN D CB    1 
ATOM   7284 C CG    . ASN D 1 126 ? 17.610  -17.311 20.897  1.00 48.17  ? 98  ASN D CG    1 
ATOM   7285 O OD1   . ASN D 1 126 ? 17.622  -18.541 20.872  1.00 43.76  ? 98  ASN D OD1   1 
ATOM   7286 N ND2   . ASN D 1 126 ? 18.001  -16.571 19.866  1.00 51.66  ? 98  ASN D ND2   1 
ATOM   7287 N N     . ALA D 1 127 ? 18.411  -13.842 24.339  1.00 53.02  ? 99  ALA D N     1 
ATOM   7288 C CA    . ALA D 1 127 ? 17.955  -12.954 25.401  1.00 53.50  ? 99  ALA D CA    1 
ATOM   7289 C C     . ALA D 1 127 ? 17.403  -11.667 24.801  1.00 61.87  ? 99  ALA D C     1 
ATOM   7290 O O     . ALA D 1 127 ? 18.099  -10.972 24.053  1.00 69.06  ? 99  ALA D O     1 
ATOM   7291 C CB    . ALA D 1 127 ? 19.098  -12.653 26.367  1.00 56.11  ? 99  ALA D CB    1 
ATOM   7292 N N     . LEU D 1 128 ? 16.151  -11.353 25.129  1.00 60.19  ? 100 LEU D N     1 
ATOM   7293 C CA    . LEU D 1 128 ? 15.507  -10.098 24.745  1.00 63.34  ? 100 LEU D CA    1 
ATOM   7294 C C     . LEU D 1 128 ? 14.824  -9.542  25.986  1.00 63.75  ? 100 LEU D C     1 
ATOM   7295 O O     . LEU D 1 128 ? 13.624  -9.763  26.203  1.00 63.35  ? 100 LEU D O     1 
ATOM   7296 C CB    . LEU D 1 128 ? 14.518  -10.303 23.596  1.00 63.81  ? 100 LEU D CB    1 
ATOM   7297 C CG    . LEU D 1 128 ? 13.829  -9.052  23.042  1.00 61.65  ? 100 LEU D CG    1 
ATOM   7298 C CD1   . LEU D 1 128 ? 14.844  -7.964  22.719  1.00 63.14  ? 100 LEU D CD1   1 
ATOM   7299 C CD2   . LEU D 1 128 ? 12.999  -9.395  21.814  1.00 61.95  ? 100 LEU D CD2   1 
ATOM   7300 N N     . PRO D 1 129 ? 15.565  -8.827  26.834  1.00 66.28  ? 101 PRO D N     1 
ATOM   7301 C CA    . PRO D 1 129 ? 14.989  -8.341  28.094  1.00 63.81  ? 101 PRO D CA    1 
ATOM   7302 C C     . PRO D 1 129 ? 13.808  -7.412  27.860  1.00 60.21  ? 101 PRO D C     1 
ATOM   7303 O O     . PRO D 1 129 ? 13.732  -6.703  26.854  1.00 65.13  ? 101 PRO D O     1 
ATOM   7304 C CB    . PRO D 1 129 ? 16.157  -7.601  28.756  1.00 59.38  ? 101 PRO D CB    1 
ATOM   7305 C CG    . PRO D 1 129 ? 17.380  -8.212  28.155  1.00 57.51  ? 101 PRO D CG    1 
ATOM   7306 C CD    . PRO D 1 129 ? 17.009  -8.552  26.741  1.00 63.75  ? 101 PRO D CD    1 
ATOM   7307 N N     . GLY D 1 130 ? 12.876  -7.429  28.810  1.00 57.06  ? 102 GLY D N     1 
ATOM   7308 C CA    . GLY D 1 130 ? 11.678  -6.624  28.722  1.00 57.59  ? 102 GLY D CA    1 
ATOM   7309 C C     . GLY D 1 130 ? 10.658  -7.089  27.708  1.00 60.76  ? 102 GLY D C     1 
ATOM   7310 O O     . GLY D 1 130 ? 9.630   -6.422  27.543  1.00 67.36  ? 102 GLY D O     1 
ATOM   7311 N N     . THR D 1 131 ? 10.898  -8.209  27.027  1.00 60.56  ? 103 THR D N     1 
ATOM   7312 C CA    . THR D 1 131 ? 9.977   -8.686  26.003  1.00 56.32  ? 103 THR D CA    1 
ATOM   7313 C C     . THR D 1 131 ? 9.751   -10.189 26.113  1.00 53.11  ? 103 THR D C     1 
ATOM   7314 O O     . THR D 1 131 ? 8.606   -10.645 26.200  1.00 51.29  ? 103 THR D O     1 
ATOM   7315 C CB    . THR D 1 131 ? 10.500  -8.336  24.608  1.00 58.15  ? 103 THR D CB    1 
ATOM   7316 O OG1   . THR D 1 131 ? 10.589  -6.912  24.471  1.00 57.94  ? 103 THR D OG1   1 
ATOM   7317 C CG2   . THR D 1 131 ? 9.570   -8.886  23.537  1.00 59.55  ? 103 THR D CG2   1 
ATOM   7318 N N     . ILE D 1 132 ? 10.831  -10.968 26.111  1.00 52.56  ? 104 ILE D N     1 
ATOM   7319 C CA    . ILE D 1 132 ? 10.759  -12.425 26.119  1.00 49.28  ? 104 ILE D CA    1 
ATOM   7320 C C     . ILE D 1 132 ? 11.210  -12.934 27.480  1.00 48.06  ? 104 ILE D C     1 
ATOM   7321 O O     . ILE D 1 132 ? 12.252  -12.512 27.997  1.00 48.32  ? 104 ILE D O     1 
ATOM   7322 C CB    . ILE D 1 132 ? 11.614  -13.040 24.997  1.00 45.91  ? 104 ILE D CB    1 
ATOM   7323 C CG1   . ILE D 1 132 ? 11.205  -12.474 23.637  1.00 48.32  ? 104 ILE D CG1   1 
ATOM   7324 C CG2   . ILE D 1 132 ? 11.478  -14.552 24.997  1.00 41.21  ? 104 ILE D CG2   1 
ATOM   7325 C CD1   . ILE D 1 132 ? 12.055  -12.976 22.492  1.00 44.68  ? 104 ILE D CD1   1 
ATOM   7326 N N     . THR D 1 133 ? 10.423  -13.839 28.059  1.00 45.43  ? 105 THR D N     1 
ATOM   7327 C CA    . THR D 1 133 ? 10.779  -14.541 29.285  1.00 39.51  ? 105 THR D CA    1 
ATOM   7328 C C     . THR D 1 133 ? 10.642  -16.035 29.036  1.00 38.78  ? 105 THR D C     1 
ATOM   7329 O O     . THR D 1 133 ? 9.628   -16.483 28.491  1.00 38.65  ? 105 THR D O     1 
ATOM   7330 C CB    . THR D 1 133 ? 9.891   -14.115 30.461  1.00 39.50  ? 105 THR D CB    1 
ATOM   7331 O OG1   . THR D 1 133 ? 8.551   -14.572 30.240  1.00 46.12  ? 105 THR D OG1   1 
ATOM   7332 C CG2   . THR D 1 133 ? 9.885   -12.601 30.612  1.00 41.81  ? 105 THR D CG2   1 
ATOM   7333 N N     . TYR D 1 134 ? 11.658  -16.800 29.424  1.00 39.62  ? 106 TYR D N     1 
ATOM   7334 C CA    . TYR D 1 134 ? 11.690  -18.238 29.197  1.00 40.44  ? 106 TYR D CA    1 
ATOM   7335 C C     . TYR D 1 134 ? 11.404  -18.977 30.497  1.00 41.35  ? 106 TYR D C     1 
ATOM   7336 O O     . TYR D 1 134 ? 11.954  -18.637 31.549  1.00 41.70  ? 106 TYR D O     1 
ATOM   7337 C CB    . TYR D 1 134 ? 13.041  -18.674 28.629  1.00 40.88  ? 106 TYR D CB    1 
ATOM   7338 C CG    . TYR D 1 134 ? 13.360  -18.054 27.289  1.00 40.11  ? 106 TYR D CG    1 
ATOM   7339 C CD1   . TYR D 1 134 ? 12.750  -18.511 26.130  1.00 39.88  ? 106 TYR D CD1   1 
ATOM   7340 C CD2   . TYR D 1 134 ? 14.277  -17.018 27.182  1.00 39.70  ? 106 TYR D CD2   1 
ATOM   7341 C CE1   . TYR D 1 134 ? 13.039  -17.948 24.901  1.00 39.24  ? 106 TYR D CE1   1 
ATOM   7342 C CE2   . TYR D 1 134 ? 14.574  -16.449 25.958  1.00 40.35  ? 106 TYR D CE2   1 
ATOM   7343 C CZ    . TYR D 1 134 ? 13.953  -16.919 24.821  1.00 40.14  ? 106 TYR D CZ    1 
ATOM   7344 O OH    . TYR D 1 134 ? 14.244  -16.354 23.600  1.00 46.10  ? 106 TYR D OH    1 
ATOM   7345 N N     . GLU D 1 135 ? 10.544  -19.992 30.419  1.00 41.82  ? 107 GLU D N     1 
ATOM   7346 C CA    . GLU D 1 135 ? 10.060  -20.698 31.595  1.00 42.68  ? 107 GLU D CA    1 
ATOM   7347 C C     . GLU D 1 135 ? 10.121  -22.202 31.371  1.00 43.69  ? 107 GLU D C     1 
ATOM   7348 O O     . GLU D 1 135 ? 10.294  -22.685 30.249  1.00 43.66  ? 107 GLU D O     1 
ATOM   7349 C CB    . GLU D 1 135 ? 8.620   -20.286 31.940  1.00 42.29  ? 107 GLU D CB    1 
ATOM   7350 C CG    . GLU D 1 135 ? 8.361   -18.786 31.915  1.00 41.23  ? 107 GLU D CG    1 
ATOM   7351 C CD    . GLU D 1 135 ? 9.119   -18.030 32.988  1.00 41.34  ? 107 GLU D CD    1 
ATOM   7352 O OE1   . GLU D 1 135 ? 9.681   -18.673 33.901  1.00 42.28  ? 107 GLU D OE1   1 
ATOM   7353 O OE2   . GLU D 1 135 ? 9.159   -16.783 32.917  1.00 41.30  ? 107 GLU D OE2   1 
ATOM   7354 N N     . LEU D 1 136 ? 9.974   -22.941 32.467  1.00 44.67  ? 108 LEU D N     1 
ATOM   7355 C CA    . LEU D 1 136 ? 9.818   -24.389 32.439  1.00 45.76  ? 108 LEU D CA    1 
ATOM   7356 C C     . LEU D 1 136 ? 8.336   -24.727 32.518  1.00 45.83  ? 108 LEU D C     1 
ATOM   7357 O O     . LEU D 1 136 ? 7.614   -24.167 33.351  1.00 45.64  ? 108 LEU D O     1 
ATOM   7358 C CB    . LEU D 1 136 ? 10.560  -25.046 33.604  1.00 46.94  ? 108 LEU D CB    1 
ATOM   7359 C CG    . LEU D 1 136 ? 12.063  -25.277 33.473  1.00 47.42  ? 108 LEU D CG    1 
ATOM   7360 C CD1   . LEU D 1 136 ? 12.651  -25.670 34.817  1.00 48.51  ? 108 LEU D CD1   1 
ATOM   7361 C CD2   . LEU D 1 136 ? 12.337  -26.348 32.439  1.00 47.94  ? 108 LEU D CD2   1 
ATOM   7362 N N     . LEU D 1 137 ? 7.885   -25.641 31.662  1.00 46.18  ? 109 LEU D N     1 
ATOM   7363 C CA    . LEU D 1 137 ? 6.488   -26.051 31.685  1.00 46.39  ? 109 LEU D CA    1 
ATOM   7364 C C     . LEU D 1 137 ? 6.306   -27.289 30.823  1.00 47.13  ? 109 LEU D C     1 
ATOM   7365 O O     . LEU D 1 137 ? 6.850   -27.366 29.719  1.00 46.86  ? 109 LEU D O     1 
ATOM   7366 C CB    . LEU D 1 137 ? 5.568   -24.927 31.186  1.00 45.19  ? 109 LEU D CB    1 
ATOM   7367 C CG    . LEU D 1 137 ? 4.102   -25.318 31.011  1.00 45.40  ? 109 LEU D CG    1 
ATOM   7368 C CD1   . LEU D 1 137 ? 3.371   -25.110 32.318  1.00 45.73  ? 109 LEU D CD1   1 
ATOM   7369 C CD2   . LEU D 1 137 ? 3.448   -24.520 29.897  1.00 44.34  ? 109 LEU D CD2   1 
ATOM   7370 N N     . ASP D 1 138 ? 5.541   -28.249 31.336  1.00 48.14  ? 110 ASP D N     1 
ATOM   7371 C CA    . ASP D 1 138 ? 5.095   -29.401 30.565  1.00 48.92  ? 110 ASP D CA    1 
ATOM   7372 C C     . ASP D 1 138 ? 3.640   -29.174 30.176  1.00 48.56  ? 110 ASP D C     1 
ATOM   7373 O O     . ASP D 1 138 ? 2.798   -28.910 31.040  1.00 48.62  ? 110 ASP D O     1 
ATOM   7374 C CB    . ASP D 1 138 ? 5.247   -30.693 31.371  1.00 51.75  ? 110 ASP D CB    1 
ATOM   7375 C CG    . ASP D 1 138 ? 4.665   -31.906 30.659  1.00 54.09  ? 110 ASP D CG    1 
ATOM   7376 O OD1   . ASP D 1 138 ? 4.461   -31.847 29.428  1.00 55.20  ? 110 ASP D OD1   1 
ATOM   7377 O OD2   . ASP D 1 138 ? 4.415   -32.926 31.337  1.00 52.68  ? 110 ASP D OD2   1 
ATOM   7378 N N     . VAL D 1 139 ? 3.351   -29.281 28.876  1.00 48.26  ? 111 VAL D N     1 
ATOM   7379 C CA    . VAL D 1 139 ? 2.033   -28.925 28.361  1.00 47.82  ? 111 VAL D CA    1 
ATOM   7380 C C     . VAL D 1 139 ? 0.927   -29.787 28.956  1.00 48.91  ? 111 VAL D C     1 
ATOM   7381 O O     . VAL D 1 139 ? -0.242  -29.386 28.942  1.00 50.56  ? 111 VAL D O     1 
ATOM   7382 C CB    . VAL D 1 139 ? 2.034   -29.009 26.818  1.00 47.49  ? 111 VAL D CB    1 
ATOM   7383 C CG1   . VAL D 1 139 ? 1.933   -30.455 26.358  1.00 53.82  ? 111 VAL D CG1   1 
ATOM   7384 C CG2   . VAL D 1 139 ? 0.906   -28.168 26.231  1.00 46.65  ? 111 VAL D CG2   1 
ATOM   7385 N N     . VAL D 1 140 ? 1.263   -30.958 29.493  1.00 50.20  ? 112 VAL D N     1 
ATOM   7386 C CA    . VAL D 1 140 ? 0.259   -31.848 30.066  1.00 52.01  ? 112 VAL D CA    1 
ATOM   7387 C C     . VAL D 1 140 ? 0.484   -31.982 31.566  1.00 52.20  ? 112 VAL D C     1 
ATOM   7388 O O     . VAL D 1 140 ? 0.198   -33.030 32.157  1.00 53.30  ? 112 VAL D O     1 
ATOM   7389 C CB    . VAL D 1 140 ? 0.277   -33.225 29.381  1.00 52.61  ? 112 VAL D CB    1 
ATOM   7390 C CG1   . VAL D 1 140 ? -0.422  -33.152 28.032  1.00 52.53  ? 112 VAL D CG1   1 
ATOM   7391 C CG2   . VAL D 1 140 ? 1.706   -33.721 29.223  1.00 52.95  ? 112 VAL D CG2   1 
ATOM   7392 N N     . GLU D 1 141 ? 0.998   -30.928 32.188  1.00 51.09  ? 113 GLU D N     1 
ATOM   7393 C CA    . GLU D 1 141 ? 1.164   -30.927 33.637  1.00 51.64  ? 113 GLU D CA    1 
ATOM   7394 C C     . GLU D 1 141 ? -0.201  -30.877 34.312  1.00 52.05  ? 113 GLU D C     1 
ATOM   7395 O O     . GLU D 1 141 ? -1.020  -30.013 33.979  1.00 51.45  ? 113 GLU D O     1 
ATOM   7396 C CB    . GLU D 1 141 ? 2.016   -29.738 34.081  1.00 50.61  ? 113 GLU D CB    1 
ATOM   7397 C CG    . GLU D 1 141 ? 2.499   -29.755 35.544  1.00 51.25  ? 113 GLU D CG    1 
ATOM   7398 C CD    . GLU D 1 141 ? 3.157   -31.059 35.999  1.00 63.14  ? 113 GLU D CD    1 
ATOM   7399 O OE1   . GLU D 1 141 ? 3.492   -31.923 35.162  1.00 67.93  ? 113 GLU D OE1   1 
ATOM   7400 O OE2   . GLU D 1 141 ? 3.327   -31.219 37.226  1.00 63.31  ? 113 GLU D OE2   1 
ATOM   7401 N N     . PRO D 1 142 ? -0.488  -31.781 35.253  1.00 53.34  ? 114 PRO D N     1 
ATOM   7402 C CA    . PRO D 1 142 ? -1.772  -31.687 35.971  1.00 53.75  ? 114 PRO D CA    1 
ATOM   7403 C C     . PRO D 1 142 ? -1.882  -30.423 36.806  1.00 52.92  ? 114 PRO D C     1 
ATOM   7404 O O     . PRO D 1 142 ? -2.883  -29.700 36.712  1.00 58.86  ? 114 PRO D O     1 
ATOM   7405 C CB    . PRO D 1 142 ? -1.781  -32.958 36.836  1.00 55.44  ? 114 PRO D CB    1 
ATOM   7406 C CG    . PRO D 1 142 ? -0.732  -33.855 36.243  1.00 55.94  ? 114 PRO D CG    1 
ATOM   7407 C CD    . PRO D 1 142 ? 0.305   -32.943 35.682  1.00 54.62  ? 114 PRO D CD    1 
ATOM   7408 N N     . ARG D 1 143 ? -0.868  -30.131 37.620  1.00 53.31  ? 115 ARG D N     1 
ATOM   7409 C CA    . ARG D 1 143 ? -0.858  -28.935 38.459  1.00 52.21  ? 115 ARG D CA    1 
ATOM   7410 C C     . ARG D 1 143 ? -0.374  -27.725 37.656  1.00 50.65  ? 115 ARG D C     1 
ATOM   7411 O O     . ARG D 1 143 ? 0.650   -27.107 37.947  1.00 51.80  ? 115 ARG D O     1 
ATOM   7412 C CB    . ARG D 1 143 ? 0.006   -29.167 39.691  1.00 53.00  ? 115 ARG D CB    1 
ATOM   7413 C CG    . ARG D 1 143 ? -0.069  -30.582 40.240  1.00 54.63  ? 115 ARG D CG    1 
ATOM   7414 C CD    . ARG D 1 143 ? -1.192  -30.714 41.252  1.00 55.48  ? 115 ARG D CD    1 
ATOM   7415 N NE    . ARG D 1 143 ? -1.018  -29.802 42.375  1.00 55.28  ? 115 ARG D NE    1 
ATOM   7416 C CZ    . ARG D 1 143 ? -2.006  -29.135 42.956  1.00 55.18  ? 115 ARG D CZ    1 
ATOM   7417 N NH1   . ARG D 1 143 ? -3.257  -29.257 42.545  1.00 57.98  ? 115 ARG D NH1   1 
ATOM   7418 N NH2   . ARG D 1 143 ? -1.731  -28.321 43.971  1.00 55.09  ? 115 ARG D NH2   1 
ATOM   7419 N N     . LEU D 1 144 ? -1.143  -27.398 36.615  1.00 49.94  ? 116 LEU D N     1 
ATOM   7420 C CA    . LEU D 1 144 ? -0.803  -26.260 35.767  1.00 52.78  ? 116 LEU D CA    1 
ATOM   7421 C C     . LEU D 1 144 ? -0.868  -24.953 36.547  1.00 53.53  ? 116 LEU D C     1 
ATOM   7422 O O     . LEU D 1 144 ? -0.024  -24.068 36.364  1.00 52.47  ? 116 LEU D O     1 
ATOM   7423 C CB    . LEU D 1 144 ? -1.740  -26.207 34.560  1.00 57.16  ? 116 LEU D CB    1 
ATOM   7424 C CG    . LEU D 1 144 ? -1.521  -25.082 33.544  1.00 48.42  ? 116 LEU D CG    1 
ATOM   7425 C CD1   . LEU D 1 144 ? -0.045  -24.891 33.242  1.00 47.78  ? 116 LEU D CD1   1 
ATOM   7426 C CD2   . LEU D 1 144 ? -2.302  -25.342 32.266  1.00 46.44  ? 116 LEU D CD2   1 
ATOM   7427 N N     . GLU D 1 145 ? -1.858  -24.819 37.430  1.00 55.16  ? 117 GLU D N     1 
ATOM   7428 C CA    . GLU D 1 145 ? -2.064  -23.580 38.168  1.00 55.51  ? 117 GLU D CA    1 
ATOM   7429 C C     . GLU D 1 145 ? -0.932  -23.269 39.138  1.00 53.69  ? 117 GLU D C     1 
ATOM   7430 O O     . GLU D 1 145 ? -0.874  -22.149 39.655  1.00 52.69  ? 117 GLU D O     1 
ATOM   7431 C CB    . GLU D 1 145 ? -3.393  -23.653 38.920  1.00 58.30  ? 117 GLU D CB    1 
ATOM   7432 C CG    . GLU D 1 145 ? -4.595  -23.304 38.060  1.00 59.23  ? 117 GLU D CG    1 
ATOM   7433 C CD    . GLU D 1 145 ? -5.148  -24.512 37.327  1.00 60.13  ? 117 GLU D CD    1 
ATOM   7434 O OE1   . GLU D 1 145 ? -5.105  -25.625 37.896  1.00 61.74  ? 117 GLU D OE1   1 
ATOM   7435 O OE2   . GLU D 1 145 ? -5.617  -24.353 36.180  1.00 55.98  ? 117 GLU D OE2   1 
ATOM   7436 N N     . ASP D 1 146 ? -0.038  -24.223 39.392  1.00 49.75  ? 118 ASP D N     1 
ATOM   7437 C CA    . ASP D 1 146 ? 1.095   -24.028 40.284  1.00 50.03  ? 118 ASP D CA    1 
ATOM   7438 C C     . ASP D 1 146 ? 2.382   -23.710 39.534  1.00 49.29  ? 118 ASP D C     1 
ATOM   7439 O O     . ASP D 1 146 ? 3.463   -23.760 40.129  1.00 50.43  ? 118 ASP D O     1 
ATOM   7440 C CB    . ASP D 1 146 ? 1.292   -25.268 41.158  1.00 51.52  ? 118 ASP D CB    1 
ATOM   7441 C CG    . ASP D 1 146 ? 0.099   -25.546 42.049  1.00 52.39  ? 118 ASP D CG    1 
ATOM   7442 O OD1   . ASP D 1 146 ? -1.025  -25.667 41.518  1.00 52.28  ? 118 ASP D OD1   1 
ATOM   7443 O OD2   . ASP D 1 146 ? 0.283   -25.648 43.280  1.00 53.26  ? 118 ASP D OD2   1 
ATOM   7444 N N     . THR D 1 147 ? 2.293   -23.388 38.249  1.00 47.22  ? 119 THR D N     1 
ATOM   7445 C CA    . THR D 1 147 ? 3.456   -23.084 37.431  1.00 46.53  ? 119 THR D CA    1 
ATOM   7446 C C     . THR D 1 147 ? 3.566   -21.583 37.192  1.00 45.30  ? 119 THR D C     1 
ATOM   7447 O O     . THR D 1 147 ? 2.589   -20.837 37.293  1.00 47.53  ? 119 THR D O     1 
ATOM   7448 C CB    . THR D 1 147 ? 3.386   -23.821 36.090  1.00 48.43  ? 119 THR D CB    1 
ATOM   7449 O OG1   . THR D 1 147 ? 2.292   -23.309 35.317  1.00 48.42  ? 119 THR D OG1   1 
ATOM   7450 C CG2   . THR D 1 147 ? 3.188   -25.313 36.312  1.00 50.73  ? 119 THR D CG2   1 
ATOM   7451 N N     . VAL D 1 148 ? 4.787   -21.145 36.872  1.00 44.86  ? 120 VAL D N     1 
ATOM   7452 C CA    . VAL D 1 148 ? 5.024   -19.730 36.607  1.00 43.76  ? 120 VAL D CA    1 
ATOM   7453 C C     . VAL D 1 148 ? 4.281   -19.282 35.354  1.00 42.78  ? 120 VAL D C     1 
ATOM   7454 O O     . VAL D 1 148 ? 3.788   -18.149 35.286  1.00 43.93  ? 120 VAL D O     1 
ATOM   7455 C CB    . VAL D 1 148 ? 6.538   -19.463 36.498  1.00 43.65  ? 120 VAL D CB    1 
ATOM   7456 C CG1   . VAL D 1 148 ? 6.807   -18.077 35.937  1.00 42.49  ? 120 VAL D CG1   1 
ATOM   7457 C CG2   . VAL D 1 148 ? 7.211   -19.635 37.854  1.00 44.58  ? 120 VAL D CG2   1 
ATOM   7458 N N     . VAL D 1 149 ? 4.168   -20.163 34.357  1.00 42.89  ? 121 VAL D N     1 
ATOM   7459 C CA    . VAL D 1 149 ? 3.525   -19.796 33.097  1.00 46.65  ? 121 VAL D CA    1 
ATOM   7460 C C     . VAL D 1 149 ? 2.057   -19.456 33.319  1.00 50.47  ? 121 VAL D C     1 
ATOM   7461 O O     . VAL D 1 149 ? 1.536   -18.487 32.751  1.00 51.82  ? 121 VAL D O     1 
ATOM   7462 C CB    . VAL D 1 149 ? 3.689   -20.928 32.064  1.00 43.63  ? 121 VAL D CB    1 
ATOM   7463 C CG1   . VAL D 1 149 ? 2.854   -20.651 30.819  1.00 41.71  ? 121 VAL D CG1   1 
ATOM   7464 C CG2   . VAL D 1 149 ? 5.151   -21.109 31.700  1.00 46.99  ? 121 VAL D CG2   1 
ATOM   7465 N N     . TRP D 1 150 ? 1.367   -20.244 34.147  1.00 50.89  ? 122 TRP D N     1 
ATOM   7466 C CA    . TRP D 1 150 ? -0.063  -20.034 34.354  1.00 50.37  ? 122 TRP D CA    1 
ATOM   7467 C C     . TRP D 1 150 ? -0.346  -18.661 34.947  1.00 49.29  ? 122 TRP D C     1 
ATOM   7468 O O     . TRP D 1 150 ? -1.356  -18.029 34.616  1.00 51.80  ? 122 TRP D O     1 
ATOM   7469 C CB    . TRP D 1 150 ? -0.631  -21.127 35.258  1.00 51.94  ? 122 TRP D CB    1 
ATOM   7470 C CG    . TRP D 1 150 ? -2.006  -20.816 35.766  1.00 56.08  ? 122 TRP D CG    1 
ATOM   7471 C CD1   . TRP D 1 150 ? -2.336  -20.337 37.001  1.00 55.75  ? 122 TRP D CD1   1 
ATOM   7472 C CD2   . TRP D 1 150 ? -3.237  -20.957 35.048  1.00 59.39  ? 122 TRP D CD2   1 
ATOM   7473 N NE1   . TRP D 1 150 ? -3.697  -20.173 37.097  1.00 56.74  ? 122 TRP D NE1   1 
ATOM   7474 C CE2   . TRP D 1 150 ? -4.273  -20.547 35.911  1.00 59.90  ? 122 TRP D CE2   1 
ATOM   7475 C CE3   . TRP D 1 150 ? -3.565  -21.392 33.760  1.00 58.95  ? 122 TRP D CE3   1 
ATOM   7476 C CZ2   . TRP D 1 150 ? -5.612  -20.559 35.528  1.00 67.31  ? 122 TRP D CZ2   1 
ATOM   7477 C CZ3   . TRP D 1 150 ? -4.895  -21.403 33.381  1.00 58.16  ? 122 TRP D CZ3   1 
ATOM   7478 C CH2   . TRP D 1 150 ? -5.902  -20.989 34.262  1.00 61.98  ? 122 TRP D CH2   1 
ATOM   7479 N N     . ARG D 1 151 ? 0.533   -18.181 35.822  1.00 45.23  ? 123 ARG D N     1 
ATOM   7480 C CA    . ARG D 1 151 ? 0.301   -16.923 36.515  1.00 42.09  ? 123 ARG D CA    1 
ATOM   7481 C C     . ARG D 1 151 ? 0.834   -15.716 35.758  1.00 47.19  ? 123 ARG D C     1 
ATOM   7482 O O     . ARG D 1 151 ? 0.517   -14.582 36.131  1.00 52.00  ? 123 ARG D O     1 
ATOM   7483 C CB    . ARG D 1 151 ? 0.904   -16.990 37.918  1.00 42.78  ? 123 ARG D CB    1 
ATOM   7484 C CG    . ARG D 1 151 ? 0.243   -18.072 38.747  1.00 43.96  ? 123 ARG D CG    1 
ATOM   7485 C CD    . ARG D 1 151 ? 0.641   -18.039 40.199  1.00 44.79  ? 123 ARG D CD    1 
ATOM   7486 N NE    . ARG D 1 151 ? 0.066   -19.178 40.904  1.00 45.98  ? 123 ARG D NE    1 
ATOM   7487 C CZ    . ARG D 1 151 ? 0.305   -19.470 42.173  1.00 46.98  ? 123 ARG D CZ    1 
ATOM   7488 N NH1   . ARG D 1 151 ? 1.084   -18.707 42.921  1.00 52.30  ? 123 ARG D NH1   1 
ATOM   7489 N NH2   . ARG D 1 151 ? -0.260  -20.549 42.708  1.00 48.09  ? 123 ARG D NH2   1 
ATOM   7490 N N     . ASN D 1 152 ? 1.630   -15.929 34.709  1.00 48.96  ? 124 ASN D N     1 
ATOM   7491 C CA    . ASN D 1 152 ? 1.865   -14.869 33.739  1.00 52.16  ? 124 ASN D CA    1 
ATOM   7492 C C     . ASN D 1 152 ? 0.656   -14.641 32.846  1.00 52.06  ? 124 ASN D C     1 
ATOM   7493 O O     . ASN D 1 152 ? 0.600   -13.619 32.153  1.00 53.46  ? 124 ASN D O     1 
ATOM   7494 C CB    . ASN D 1 152 ? 3.085   -15.192 32.874  1.00 55.28  ? 124 ASN D CB    1 
ATOM   7495 C CG    . ASN D 1 152 ? 4.392   -15.014 33.618  1.00 59.74  ? 124 ASN D CG    1 
ATOM   7496 O OD1   . ASN D 1 152 ? 4.870   -13.893 33.796  1.00 66.28  ? 124 ASN D OD1   1 
ATOM   7497 N ND2   . ASN D 1 152 ? 4.980   -16.121 34.052  1.00 55.71  ? 124 ASN D ND2   1 
ATOM   7498 N N     . GLY D 1 153 ? -0.305  -15.561 32.851  1.00 52.69  ? 125 GLY D N     1 
ATOM   7499 C CA    . GLY D 1 153 ? -1.481  -15.452 32.027  1.00 57.46  ? 125 GLY D CA    1 
ATOM   7500 C C     . GLY D 1 153 ? -2.568  -14.614 32.668  1.00 60.32  ? 125 GLY D C     1 
ATOM   7501 O O     . GLY D 1 153 ? -2.365  -13.977 33.706  1.00 60.87  ? 125 GLY D O     1 
ATOM   7502 N N     . PRO D 1 154 ? -3.757  -14.600 32.052  1.00 65.87  ? 126 PRO D N     1 
ATOM   7503 C CA    . PRO D 1 154 ? -4.142  -15.335 30.839  1.00 61.96  ? 126 PRO D CA    1 
ATOM   7504 C C     . PRO D 1 154 ? -3.530  -14.728 29.579  1.00 62.95  ? 126 PRO D C     1 
ATOM   7505 O O     . PRO D 1 154 ? -3.207  -13.544 29.541  1.00 62.69  ? 126 PRO D O     1 
ATOM   7506 C CB    . PRO D 1 154 ? -5.670  -15.234 30.857  1.00 61.64  ? 126 PRO D CB    1 
ATOM   7507 C CG    . PRO D 1 154 ? -5.938  -13.899 31.492  1.00 71.50  ? 126 PRO D CG    1 
ATOM   7508 C CD    . PRO D 1 154 ? -4.827  -13.689 32.501  1.00 76.49  ? 126 PRO D CD    1 
ATOM   7509 N N     . PHE D 1 155 ? -3.350  -15.531 28.536  1.00 63.96  ? 127 PHE D N     1 
ATOM   7510 C CA    . PHE D 1 155 ? -2.659  -15.111 27.328  1.00 59.63  ? 127 PHE D CA    1 
ATOM   7511 C C     . PHE D 1 155 ? -3.656  -14.870 26.202  1.00 62.66  ? 127 PHE D C     1 
ATOM   7512 O O     . PHE D 1 155 ? -4.725  -15.485 26.152  1.00 66.11  ? 127 PHE D O     1 
ATOM   7513 C CB    . PHE D 1 155 ? -1.630  -16.161 26.896  1.00 58.24  ? 127 PHE D CB    1 
ATOM   7514 C CG    . PHE D 1 155 ? -0.537  -16.386 27.902  1.00 52.81  ? 127 PHE D CG    1 
ATOM   7515 C CD1   . PHE D 1 155 ? 0.620   -15.628 27.869  1.00 52.11  ? 127 PHE D CD1   1 
ATOM   7516 C CD2   . PHE D 1 155 ? -0.669  -17.357 28.881  1.00 52.23  ? 127 PHE D CD2   1 
ATOM   7517 C CE1   . PHE D 1 155 ? 1.626   -15.833 28.794  1.00 51.41  ? 127 PHE D CE1   1 
ATOM   7518 C CE2   . PHE D 1 155 ? 0.333   -17.567 29.809  1.00 52.06  ? 127 PHE D CE2   1 
ATOM   7519 C CZ    . PHE D 1 155 ? 1.482   -16.804 29.765  1.00 52.41  ? 127 PHE D CZ    1 
ATOM   7520 N N     . GLY D 1 156 ? -3.292  -13.965 25.299  1.00 60.23  ? 128 GLY D N     1 
ATOM   7521 C CA    . GLY D 1 156 ? -4.127  -13.667 24.154  1.00 62.21  ? 128 GLY D CA    1 
ATOM   7522 C C     . GLY D 1 156 ? -3.871  -14.598 22.987  1.00 64.62  ? 128 GLY D C     1 
ATOM   7523 O O     . GLY D 1 156 ? -4.766  -14.847 22.174  1.00 67.86  ? 128 GLY D O     1 
ATOM   7524 N N     . LYS D 1 157 ? -2.647  -15.115 22.891  1.00 59.34  ? 129 LYS D N     1 
ATOM   7525 C CA    . LYS D 1 157 ? -2.262  -16.008 21.809  1.00 58.73  ? 129 LYS D CA    1 
ATOM   7526 C C     . LYS D 1 157 ? -1.389  -17.122 22.361  1.00 56.97  ? 129 LYS D C     1 
ATOM   7527 O O     . LYS D 1 157 ? -0.523  -16.879 23.207  1.00 55.34  ? 129 LYS D O     1 
ATOM   7528 C CB    . LYS D 1 157 ? -1.502  -15.262 20.705  1.00 59.27  ? 129 LYS D CB    1 
ATOM   7529 C CG    . LYS D 1 157 ? -2.212  -14.030 20.183  1.00 65.21  ? 129 LYS D CG    1 
ATOM   7530 C CD    . LYS D 1 157 ? -3.188  -14.362 19.075  1.00 72.27  ? 129 LYS D CD    1 
ATOM   7531 C CE    . LYS D 1 157 ? -3.887  -13.104 18.598  1.00 76.25  ? 129 LYS D CE    1 
ATOM   7532 N NZ    . LYS D 1 157 ? -4.395  -12.294 19.741  1.00 73.68  ? 129 LYS D NZ    1 
ATOM   7533 N N     . VAL D 1 158 ? -1.616  -18.340 21.879  1.00 57.97  ? 130 VAL D N     1 
ATOM   7534 C CA    . VAL D 1 158 ? -0.791  -19.493 22.218  1.00 58.07  ? 130 VAL D CA    1 
ATOM   7535 C C     . VAL D 1 158 ? -0.220  -20.045 20.920  1.00 59.19  ? 130 VAL D C     1 
ATOM   7536 O O     . VAL D 1 158 ? -0.975  -20.414 20.011  1.00 59.22  ? 130 VAL D O     1 
ATOM   7537 C CB    . VAL D 1 158 ? -1.582  -20.570 22.976  1.00 55.94  ? 130 VAL D CB    1 
ATOM   7538 C CG1   . VAL D 1 158 ? -0.912  -21.930 22.825  1.00 54.82  ? 130 VAL D CG1   1 
ATOM   7539 C CG2   . VAL D 1 158 ? -1.710  -20.196 24.444  1.00 56.85  ? 130 VAL D CG2   1 
ATOM   7540 N N     . PHE D 1 159 ? 1.104   -20.090 20.829  1.00 55.65  ? 131 PHE D N     1 
ATOM   7541 C CA    . PHE D 1 159 ? 1.802   -20.580 19.644  1.00 52.39  ? 131 PHE D CA    1 
ATOM   7542 C C     . PHE D 1 159 ? 2.384   -21.949 19.978  1.00 55.95  ? 131 PHE D C     1 
ATOM   7543 O O     . PHE D 1 159 ? 3.403   -22.051 20.666  1.00 62.57  ? 131 PHE D O     1 
ATOM   7544 C CB    . PHE D 1 159 ? 2.883   -19.599 19.202  1.00 53.00  ? 131 PHE D CB    1 
ATOM   7545 C CG    . PHE D 1 159 ? 2.349   -18.405 18.469  1.00 52.21  ? 131 PHE D CG    1 
ATOM   7546 C CD1   . PHE D 1 159 ? 2.060   -18.477 17.116  1.00 57.30  ? 131 PHE D CD1   1 
ATOM   7547 C CD2   . PHE D 1 159 ? 2.127   -17.211 19.133  1.00 57.16  ? 131 PHE D CD2   1 
ATOM   7548 C CE1   . PHE D 1 159 ? 1.565   -17.378 16.439  1.00 61.33  ? 131 PHE D CE1   1 
ATOM   7549 C CE2   . PHE D 1 159 ? 1.632   -16.109 18.462  1.00 64.77  ? 131 PHE D CE2   1 
ATOM   7550 C CZ    . PHE D 1 159 ? 1.351   -16.192 17.113  1.00 64.22  ? 131 PHE D CZ    1 
ATOM   7551 N N     . CYS D 1 160 ? 1.729   -22.996 19.495  1.00 53.58  ? 132 CYS D N     1 
ATOM   7552 C CA    . CYS D 1 160 ? 2.167   -24.373 19.697  1.00 54.75  ? 132 CYS D CA    1 
ATOM   7553 C C     . CYS D 1 160 ? 2.711   -24.886 18.368  1.00 61.60  ? 132 CYS D C     1 
ATOM   7554 O O     . CYS D 1 160 ? 1.946   -25.277 17.482  1.00 64.71  ? 132 CYS D O     1 
ATOM   7555 C CB    . CYS D 1 160 ? 1.020   -25.238 20.205  1.00 53.59  ? 132 CYS D CB    1 
ATOM   7556 S SG    . CYS D 1 160 ? 1.315   -26.999 20.034  1.00 66.78  ? 132 CYS D SG    1 
ATOM   7557 N N     . MET D 1 161 ? 4.035   -24.882 18.232  1.00 58.87  ? 133 MET D N     1 
ATOM   7558 C CA    . MET D 1 161 ? 4.660   -25.283 16.978  1.00 60.75  ? 133 MET D CA    1 
ATOM   7559 C C     . MET D 1 161 ? 4.808   -26.798 16.895  1.00 61.62  ? 133 MET D C     1 
ATOM   7560 O O     . MET D 1 161 ? 3.874   -27.538 17.223  1.00 62.22  ? 133 MET D O     1 
ATOM   7561 C CB    . MET D 1 161 ? 6.019   -24.598 16.821  1.00 59.51  ? 133 MET D CB    1 
ATOM   7562 C CG    . MET D 1 161 ? 5.930   -23.124 16.457  1.00 66.68  ? 133 MET D CG    1 
ATOM   7563 S SD    . MET D 1 161 ? 4.599   -22.772 15.291  1.00 76.23  ? 133 MET D SD    1 
ATOM   7564 C CE    . MET D 1 161 ? 4.277   -21.047 15.650  1.00 60.22  ? 133 MET D CE    1 
ATOM   7565 N N     . LEU D 1 162 ? 5.978   -27.267 16.462  1.00 53.58  ? 134 LEU D N     1 
ATOM   7566 C CA    . LEU D 1 162 ? 6.214   -28.689 16.213  1.00 54.05  ? 134 LEU D CA    1 
ATOM   7567 C C     . LEU D 1 162 ? 6.549   -29.379 17.532  1.00 58.11  ? 134 LEU D C     1 
ATOM   7568 O O     . LEU D 1 162 ? 7.709   -29.620 17.872  1.00 63.55  ? 134 LEU D O     1 
ATOM   7569 C CB    . LEU D 1 162 ? 7.335   -28.868 15.196  1.00 55.13  ? 134 LEU D CB    1 
ATOM   7570 C CG    . LEU D 1 162 ? 7.231   -28.061 13.901  1.00 55.06  ? 134 LEU D CG    1 
ATOM   7571 C CD1   . LEU D 1 162 ? 8.608   -27.861 13.290  1.00 49.21  ? 134 LEU D CD1   1 
ATOM   7572 C CD2   . LEU D 1 162 ? 6.302   -28.740 12.912  1.00 58.72  ? 134 LEU D CD2   1 
ATOM   7573 N N     . MET D 1 163 ? 5.506   -29.720 18.289  1.00 56.09  ? 135 MET D N     1 
ATOM   7574 C CA    . MET D 1 163 ? 5.739   -30.315 19.599  1.00 57.70  ? 135 MET D CA    1 
ATOM   7575 C C     . MET D 1 163 ? 4.636   -31.286 20.010  1.00 60.74  ? 135 MET D C     1 
ATOM   7576 O O     . MET D 1 163 ? 4.915   -32.289 20.676  1.00 62.38  ? 135 MET D O     1 
ATOM   7577 C CB    . MET D 1 163 ? 5.908   -29.212 20.647  1.00 58.26  ? 135 MET D CB    1 
ATOM   7578 C CG    . MET D 1 163 ? 5.729   -29.659 22.089  1.00 62.76  ? 135 MET D CG    1 
ATOM   7579 S SD    . MET D 1 163 ? 4.059   -29.340 22.676  1.00 70.28  ? 135 MET D SD    1 
ATOM   7580 C CE    . MET D 1 163 ? 3.915   -27.616 22.230  1.00 60.13  ? 135 MET D CE    1 
ATOM   7581 N N     . LEU D 1 164 ? 3.388   -31.016 19.615  1.00 60.72  ? 136 LEU D N     1 
ATOM   7582 C CA    . LEU D 1 164 ? 2.284   -31.887 20.014  1.00 58.49  ? 136 LEU D CA    1 
ATOM   7583 C C     . LEU D 1 164 ? 2.452   -33.325 19.538  1.00 57.65  ? 136 LEU D C     1 
ATOM   7584 O O     . LEU D 1 164 ? 1.725   -34.203 20.016  1.00 57.36  ? 136 LEU D O     1 
ATOM   7585 C CB    . LEU D 1 164 ? 0.947   -31.346 19.503  1.00 54.14  ? 136 LEU D CB    1 
ATOM   7586 C CG    . LEU D 1 164 ? 0.261   -30.288 20.369  1.00 47.90  ? 136 LEU D CG    1 
ATOM   7587 C CD1   . LEU D 1 164 ? -0.928  -29.674 19.641  1.00 50.42  ? 136 LEU D CD1   1 
ATOM   7588 C CD2   . LEU D 1 164 ? -0.157  -30.852 21.716  1.00 52.17  ? 136 LEU D CD2   1 
ATOM   7589 N N     . HIS D 1 165 ? 3.375   -33.587 18.614  1.00 60.80  ? 137 HIS D N     1 
ATOM   7590 C CA    . HIS D 1 165 ? 3.667   -34.960 18.226  1.00 61.75  ? 137 HIS D CA    1 
ATOM   7591 C C     . HIS D 1 165 ? 4.563   -35.657 19.245  1.00 60.96  ? 137 HIS D C     1 
ATOM   7592 O O     . HIS D 1 165 ? 4.537   -36.888 19.345  1.00 66.79  ? 137 HIS D O     1 
ATOM   7593 C CB    . HIS D 1 165 ? 4.289   -34.975 16.827  1.00 66.35  ? 137 HIS D CB    1 
ATOM   7594 C CG    . HIS D 1 165 ? 5.706   -34.500 16.786  1.00 63.23  ? 137 HIS D CG    1 
ATOM   7595 N ND1   . HIS D 1 165 ? 6.053   -33.235 16.362  1.00 60.72  ? 137 HIS D ND1   1 
ATOM   7596 C CD2   . HIS D 1 165 ? 6.868   -35.133 17.071  1.00 59.07  ? 137 HIS D CD2   1 
ATOM   7597 C CE1   . HIS D 1 165 ? 7.366   -33.098 16.419  1.00 62.04  ? 137 HIS D CE1   1 
ATOM   7598 N NE2   . HIS D 1 165 ? 7.885   -34.237 16.842  1.00 58.80  ? 137 HIS D NE2   1 
ATOM   7599 N N     . LEU D 1 166 ? 5.354   -34.895 20.003  1.00 62.56  ? 138 LEU D N     1 
ATOM   7600 C CA    . LEU D 1 166 ? 6.048   -35.401 21.183  1.00 64.85  ? 138 LEU D CA    1 
ATOM   7601 C C     . LEU D 1 166 ? 5.142   -35.501 22.405  1.00 66.20  ? 138 LEU D C     1 
ATOM   7602 O O     . LEU D 1 166 ? 5.627   -35.820 23.495  1.00 62.78  ? 138 LEU D O     1 
ATOM   7603 C CB    . LEU D 1 166 ? 7.254   -34.516 21.518  1.00 66.16  ? 138 LEU D CB    1 
ATOM   7604 C CG    . LEU D 1 166 ? 8.672   -34.997 21.182  1.00 66.33  ? 138 LEU D CG    1 
ATOM   7605 C CD1   . LEU D 1 166 ? 8.802   -35.450 19.742  1.00 67.03  ? 138 LEU D CD1   1 
ATOM   7606 C CD2   . LEU D 1 166 ? 9.687   -33.904 21.490  1.00 66.28  ? 138 LEU D CD2   1 
ATOM   7607 N N     . VAL D 1 167 ? 3.849   -35.232 22.255  1.00 66.55  ? 139 VAL D N     1 
ATOM   7608 C CA    . VAL D 1 167 ? 2.917   -35.256 23.377  1.00 59.69  ? 139 VAL D CA    1 
ATOM   7609 C C     . VAL D 1 167 ? 1.901   -36.365 23.139  1.00 62.23  ? 139 VAL D C     1 
ATOM   7610 O O     . VAL D 1 167 ? 1.033   -36.225 22.265  1.00 66.66  ? 139 VAL D O     1 
ATOM   7611 C CB    . VAL D 1 167 ? 2.223   -33.897 23.552  1.00 55.44  ? 139 VAL D CB    1 
ATOM   7612 C CG1   . VAL D 1 167 ? 1.201   -33.963 24.676  1.00 59.64  ? 139 VAL D CG1   1 
ATOM   7613 C CG2   . VAL D 1 167 ? 3.248   -32.804 23.793  1.00 56.54  ? 139 VAL D CG2   1 
ATOM   7614 N N     . PRO D 1 168 ? 1.978   -37.485 23.867  1.00 59.11  ? 140 PRO D N     1 
ATOM   7615 C CA    . PRO D 1 168 ? 0.988   -38.556 23.688  1.00 57.85  ? 140 PRO D CA    1 
ATOM   7616 C C     . PRO D 1 168 ? -0.437  -38.077 23.912  1.00 58.62  ? 140 PRO D C     1 
ATOM   7617 O O     . PRO D 1 168 ? -1.254  -38.074 22.986  1.00 61.01  ? 140 PRO D O     1 
ATOM   7618 C CB    . PRO D 1 168 ? 1.403   -39.590 24.741  1.00 58.86  ? 140 PRO D CB    1 
ATOM   7619 C CG    . PRO D 1 168 ? 2.872   -39.381 24.891  1.00 60.15  ? 140 PRO D CG    1 
ATOM   7620 C CD    . PRO D 1 168 ? 3.072   -37.892 24.766  1.00 62.06  ? 140 PRO D CD    1 
ATOM   7621 N N     . ASP D 1 169 ? -0.742  -37.664 25.141  1.00 61.99  ? 141 ASP D N     1 
ATOM   7622 C CA    . ASP D 1 169 ? -2.077  -37.191 25.482  1.00 62.49  ? 141 ASP D CA    1 
ATOM   7623 C C     . ASP D 1 169 ? -2.331  -35.822 24.863  1.00 62.32  ? 141 ASP D C     1 
ATOM   7624 O O     . ASP D 1 169 ? -2.104  -34.791 25.504  1.00 65.76  ? 141 ASP D O     1 
ATOM   7625 C CB    . ASP D 1 169 ? -2.249  -37.135 27.003  1.00 69.46  ? 141 ASP D CB    1 
ATOM   7626 C CG    . ASP D 1 169 ? -3.705  -37.121 27.430  1.00 75.28  ? 141 ASP D CG    1 
ATOM   7627 O OD1   . ASP D 1 169 ? -4.559  -36.651 26.647  1.00 72.14  ? 141 ASP D OD1   1 
ATOM   7628 O OD2   . ASP D 1 169 ? -3.996  -37.577 28.556  1.00 75.44  ? 141 ASP D OD2   1 
ATOM   7629 N N     . ASN D 1 170 ? -2.809  -35.804 23.616  1.00 60.83  ? 142 ASN D N     1 
ATOM   7630 C CA    . ASN D 1 170 ? -3.032  -34.537 22.927  1.00 64.84  ? 142 ASN D CA    1 
ATOM   7631 C C     . ASN D 1 170 ? -4.267  -33.809 23.440  1.00 67.42  ? 142 ASN D C     1 
ATOM   7632 O O     . ASN D 1 170 ? -4.288  -32.573 23.455  1.00 69.41  ? 142 ASN D O     1 
ATOM   7633 C CB    . ASN D 1 170 ? -3.146  -34.774 21.421  1.00 65.92  ? 142 ASN D CB    1 
ATOM   7634 C CG    . ASN D 1 170 ? -1.811  -34.683 20.719  1.00 66.52  ? 142 ASN D CG    1 
ATOM   7635 O OD1   . ASN D 1 170 ? -1.125  -35.685 20.531  1.00 73.65  ? 142 ASN D OD1   1 
ATOM   7636 N ND2   . ASN D 1 170 ? -1.441  -33.479 20.311  1.00 60.10  ? 142 ASN D ND2   1 
ATOM   7637 N N     . ARG D 1 171 ? -5.301  -34.543 23.857  1.00 65.92  ? 143 ARG D N     1 
ATOM   7638 C CA    . ARG D 1 171 ? -6.509  -33.887 24.347  1.00 67.09  ? 143 ARG D CA    1 
ATOM   7639 C C     . ARG D 1 171 ? -6.248  -33.161 25.662  1.00 73.83  ? 143 ARG D C     1 
ATOM   7640 O O     . ARG D 1 171 ? -6.798  -32.079 25.901  1.00 73.51  ? 143 ARG D O     1 
ATOM   7641 C CB    . ARG D 1 171 ? -7.637  -34.907 24.501  1.00 66.80  ? 143 ARG D CB    1 
ATOM   7642 C CG    . ARG D 1 171 ? -8.941  -34.320 25.019  1.00 70.39  ? 143 ARG D CG    1 
ATOM   7643 C CD    . ARG D 1 171 ? -10.143 -35.078 24.478  1.00 65.96  ? 143 ARG D CD    1 
ATOM   7644 N NE    . ARG D 1 171 ? -9.794  -36.431 24.064  1.00 59.85  ? 143 ARG D NE    1 
ATOM   7645 C CZ    . ARG D 1 171 ? -10.315 -37.050 23.013  1.00 61.87  ? 143 ARG D CZ    1 
ATOM   7646 N NH1   . ARG D 1 171 ? -11.213 -36.461 22.240  1.00 69.30  ? 143 ARG D NH1   1 
ATOM   7647 N NH2   . ARG D 1 171 ? -9.921  -38.287 22.727  1.00 60.08  ? 143 ARG D NH2   1 
ATOM   7648 N N     . LEU D 1 172 ? -5.407  -33.737 26.525  1.00 74.86  ? 144 LEU D N     1 
ATOM   7649 C CA    . LEU D 1 172 ? -5.033  -33.052 27.759  1.00 70.43  ? 144 LEU D CA    1 
ATOM   7650 C C     . LEU D 1 172 ? -4.228  -31.793 27.463  1.00 64.92  ? 144 LEU D C     1 
ATOM   7651 O O     . LEU D 1 172 ? -4.389  -30.771 28.141  1.00 64.38  ? 144 LEU D O     1 
ATOM   7652 C CB    . LEU D 1 172 ? -4.244  -33.996 28.665  1.00 64.77  ? 144 LEU D CB    1 
ATOM   7653 C CG    . LEU D 1 172 ? -3.668  -33.426 29.964  1.00 60.58  ? 144 LEU D CG    1 
ATOM   7654 C CD1   . LEU D 1 172 ? -4.742  -32.717 30.778  1.00 61.65  ? 144 LEU D CD1   1 
ATOM   7655 C CD2   . LEU D 1 172 ? -3.004  -34.523 30.782  1.00 61.15  ? 144 LEU D CD2   1 
ATOM   7656 N N     . ALA D 1 173 ? -3.359  -31.846 26.451  1.00 61.77  ? 145 ALA D N     1 
ATOM   7657 C CA    . ALA D 1 173 ? -2.594  -30.664 26.073  1.00 58.06  ? 145 ALA D CA    1 
ATOM   7658 C C     . ALA D 1 173 ? -3.486  -29.589 25.468  1.00 61.71  ? 145 ALA D C     1 
ATOM   7659 O O     . ALA D 1 173 ? -3.229  -28.395 25.655  1.00 59.29  ? 145 ALA D O     1 
ATOM   7660 C CB    . ALA D 1 173 ? -1.484  -31.047 25.097  1.00 59.00  ? 145 ALA D CB    1 
ATOM   7661 N N     . VAL D 1 174 ? -4.533  -29.988 24.742  1.00 66.36  ? 146 VAL D N     1 
ATOM   7662 C CA    . VAL D 1 174 ? -5.468  -29.011 24.195  1.00 68.32  ? 146 VAL D CA    1 
ATOM   7663 C C     . VAL D 1 174 ? -6.313  -28.406 25.309  1.00 70.01  ? 146 VAL D C     1 
ATOM   7664 O O     . VAL D 1 174 ? -6.639  -27.212 25.283  1.00 70.62  ? 146 VAL D O     1 
ATOM   7665 C CB    . VAL D 1 174 ? -6.338  -29.662 23.102  1.00 71.50  ? 146 VAL D CB    1 
ATOM   7666 C CG1   . VAL D 1 174 ? -7.478  -28.740 22.697  1.00 78.20  ? 146 VAL D CG1   1 
ATOM   7667 C CG2   . VAL D 1 174 ? -5.487  -30.016 21.893  1.00 68.04  ? 146 VAL D CG2   1 
ATOM   7668 N N     . LYS D 1 175 ? -6.670  -29.213 26.312  1.00 70.67  ? 147 LYS D N     1 
ATOM   7669 C CA    . LYS D 1 175 ? -7.432  -28.694 27.443  1.00 67.13  ? 147 LYS D CA    1 
ATOM   7670 C C     . LYS D 1 175 ? -6.626  -27.665 28.225  1.00 69.64  ? 147 LYS D C     1 
ATOM   7671 O O     . LYS D 1 175 ? -7.166  -26.641 28.660  1.00 71.87  ? 147 LYS D O     1 
ATOM   7672 C CB    . LYS D 1 175 ? -7.866  -29.842 28.354  1.00 66.08  ? 147 LYS D CB    1 
ATOM   7673 N N     . ASN D 1 176 ? -5.327  -27.916 28.411  1.00 68.67  ? 148 ASN D N     1 
ATOM   7674 C CA    . ASN D 1 176 ? -4.491  -26.973 29.147  1.00 61.16  ? 148 ASN D CA    1 
ATOM   7675 C C     . ASN D 1 176 ? -4.228  -25.705 28.345  1.00 64.37  ? 148 ASN D C     1 
ATOM   7676 O O     . ASN D 1 176 ? -4.057  -24.629 28.930  1.00 65.17  ? 148 ASN D O     1 
ATOM   7677 C CB    . ASN D 1 176 ? -3.172  -27.637 29.544  1.00 53.92  ? 148 ASN D CB    1 
ATOM   7678 C CG    . ASN D 1 176 ? -3.301  -28.480 30.797  1.00 57.33  ? 148 ASN D CG    1 
ATOM   7679 O OD1   . ASN D 1 176 ? -4.296  -28.396 31.516  1.00 65.64  ? 148 ASN D OD1   1 
ATOM   7680 N ND2   . ASN D 1 176 ? -2.290  -29.297 31.067  1.00 57.06  ? 148 ASN D ND2   1 
ATOM   7681 N N     . ILE D 1 177 ? -4.186  -25.806 27.015  1.00 64.54  ? 149 ILE D N     1 
ATOM   7682 C CA    . ILE D 1 177 ? -4.069  -24.610 26.188  1.00 64.11  ? 149 ILE D CA    1 
ATOM   7683 C C     . ILE D 1 177 ? -5.360  -23.802 26.241  1.00 69.07  ? 149 ILE D C     1 
ATOM   7684 O O     . ILE D 1 177 ? -5.338  -22.564 26.233  1.00 68.42  ? 149 ILE D O     1 
ATOM   7685 C CB    . ILE D 1 177 ? -3.689  -24.995 24.745  1.00 62.02  ? 149 ILE D CB    1 
ATOM   7686 C CG1   . ILE D 1 177 ? -2.247  -25.507 24.694  1.00 58.52  ? 149 ILE D CG1   1 
ATOM   7687 C CG2   . ILE D 1 177 ? -3.870  -23.817 23.799  1.00 57.57  ? 149 ILE D CG2   1 
ATOM   7688 C CD1   . ILE D 1 177 ? -1.869  -26.132 23.371  1.00 55.71  ? 149 ILE D CD1   1 
ATOM   7689 N N     . HIS D 1 178 ? -6.505  -24.486 26.313  1.00 73.27  ? 150 HIS D N     1 
ATOM   7690 C CA    . HIS D 1 178 ? -7.782  -23.792 26.433  1.00 75.42  ? 150 HIS D CA    1 
ATOM   7691 C C     . HIS D 1 178 ? -7.888  -23.033 27.751  1.00 74.84  ? 150 HIS D C     1 
ATOM   7692 O O     . HIS D 1 178 ? -8.511  -21.967 27.802  1.00 76.27  ? 150 HIS D O     1 
ATOM   7693 C CB    . HIS D 1 178 ? -8.932  -24.791 26.296  1.00 78.42  ? 150 HIS D CB    1 
ATOM   7694 C CG    . HIS D 1 178 ? -10.289 -24.159 26.302  1.00 79.48  ? 150 HIS D CG    1 
ATOM   7695 N ND1   . HIS D 1 178 ? -11.010 -23.956 27.459  1.00 79.27  ? 150 HIS D ND1   1 
ATOM   7696 C CD2   . HIS D 1 178 ? -11.057 -23.687 25.292  1.00 82.95  ? 150 HIS D CD2   1 
ATOM   7697 C CE1   . HIS D 1 178 ? -12.164 -23.384 27.161  1.00 80.71  ? 150 HIS D CE1   1 
ATOM   7698 N NE2   . HIS D 1 178 ? -12.217 -23.210 25.853  1.00 81.04  ? 150 HIS D NE2   1 
ATOM   7699 N N     . LYS D 1 179 ? -7.288  -23.563 28.821  1.00 70.98  ? 151 LYS D N     1 
ATOM   7700 C CA    . LYS D 1 179 ? -7.283  -22.855 30.097  1.00 65.58  ? 151 LYS D CA    1 
ATOM   7701 C C     . LYS D 1 179 ? -6.498  -21.553 30.001  1.00 65.50  ? 151 LYS D C     1 
ATOM   7702 O O     . LYS D 1 179 ? -6.899  -20.530 30.568  1.00 65.97  ? 151 LYS D O     1 
ATOM   7703 C CB    . LYS D 1 179 ? -6.688  -23.742 31.190  1.00 62.51  ? 151 LYS D CB    1 
ATOM   7704 C CG    . LYS D 1 179 ? -7.546  -24.922 31.615  1.00 62.24  ? 151 LYS D CG    1 
ATOM   7705 C CD    . LYS D 1 179 ? -6.846  -25.709 32.717  1.00 64.00  ? 151 LYS D CD    1 
ATOM   7706 C CE    . LYS D 1 179 ? -7.655  -26.914 33.164  1.00 64.03  ? 151 LYS D CE    1 
ATOM   7707 N NZ    . LYS D 1 179 ? -6.933  -27.694 34.210  1.00 60.59  ? 151 LYS D NZ    1 
ATOM   7708 N N     . LEU D 1 180 ? -5.372  -21.574 29.285  1.00 62.95  ? 152 LEU D N     1 
ATOM   7709 C CA    . LEU D 1 180 ? -4.473  -20.428 29.255  1.00 58.44  ? 152 LEU D CA    1 
ATOM   7710 C C     . LEU D 1 180 ? -4.997  -19.290 28.391  1.00 59.82  ? 152 LEU D C     1 
ATOM   7711 O O     . LEU D 1 180 ? -4.589  -18.141 28.589  1.00 63.30  ? 152 LEU D O     1 
ATOM   7712 C CB    . LEU D 1 180 ? -3.096  -20.868 28.757  1.00 55.31  ? 152 LEU D CB    1 
ATOM   7713 C CG    . LEU D 1 180 ? -2.253  -21.672 29.748  1.00 54.10  ? 152 LEU D CG    1 
ATOM   7714 C CD1   . LEU D 1 180 ? -1.146  -22.416 29.026  1.00 48.15  ? 152 LEU D CD1   1 
ATOM   7715 C CD2   . LEU D 1 180 ? -1.671  -20.753 30.806  1.00 56.78  ? 152 LEU D CD2   1 
ATOM   7716 N N     . LEU D 1 181 ? -5.888  -19.576 27.447  1.00 62.79  ? 153 LEU D N     1 
ATOM   7717 C CA    . LEU D 1 181 ? -6.367  -18.569 26.513  1.00 69.02  ? 153 LEU D CA    1 
ATOM   7718 C C     . LEU D 1 181 ? -7.525  -17.780 27.106  1.00 74.48  ? 153 LEU D C     1 
ATOM   7719 O O     . LEU D 1 181 ? -8.356  -18.323 27.839  1.00 73.94  ? 153 LEU D O     1 
ATOM   7720 C CB    . LEU D 1 181 ? -6.803  -19.218 25.199  1.00 70.04  ? 153 LEU D CB    1 
ATOM   7721 C CG    . LEU D 1 181 ? -5.684  -19.697 24.275  1.00 66.02  ? 153 LEU D CG    1 
ATOM   7722 C CD1   . LEU D 1 181 ? -6.235  -20.620 23.202  1.00 71.59  ? 153 LEU D CD1   1 
ATOM   7723 C CD2   . LEU D 1 181 ? -4.969  -18.510 23.650  1.00 63.72  ? 153 LEU D CD2   1 
ATOM   7724 N N     . VAL D 1 182 ? -7.568  -16.491 26.786  1.00 72.00  ? 154 VAL D N     1 
ATOM   7725 C CA    . VAL D 1 182 ? -8.709  -15.646 27.125  1.00 73.15  ? 154 VAL D CA    1 
ATOM   7726 C C     . VAL D 1 182 ? -9.853  -16.032 26.196  1.00 84.11  ? 154 VAL D C     1 
ATOM   7727 O O     . VAL D 1 182 ? -9.603  -16.534 25.089  1.00 90.07  ? 154 VAL D O     1 
ATOM   7728 C CB    . VAL D 1 182 ? -8.364  -14.153 27.002  1.00 67.67  ? 154 VAL D CB    1 
ATOM   7729 C CG1   . VAL D 1 182 ? -7.234  -13.787 27.947  1.00 67.59  ? 154 VAL D CG1   1 
ATOM   7730 C CG2   . VAL D 1 182 ? -7.994  -13.806 25.567  1.00 71.89  ? 154 VAL D CG2   1 
ATOM   7731 N N     . PRO D 1 183 ? -11.110 -15.853 26.602  1.00 88.59  ? 155 PRO D N     1 
ATOM   7732 C CA    . PRO D 1 183 ? -12.225 -16.086 25.672  1.00 93.69  ? 155 PRO D CA    1 
ATOM   7733 C C     . PRO D 1 183 ? -12.095 -15.197 24.445  1.00 92.98  ? 155 PRO D C     1 
ATOM   7734 O O     . PRO D 1 183 ? -12.108 -13.968 24.541  1.00 89.87  ? 155 PRO D O     1 
ATOM   7735 C CB    . PRO D 1 183 ? -13.458 -15.732 26.509  1.00 92.18  ? 155 PRO D CB    1 
ATOM   7736 C CG    . PRO D 1 183 ? -13.035 -15.998 27.913  1.00 89.75  ? 155 PRO D CG    1 
ATOM   7737 C CD    . PRO D 1 183 ? -11.579 -15.614 27.977  1.00 87.07  ? 155 PRO D CD    1 
ATOM   7738 N N     . GLY D 1 184 ? -11.959 -15.832 23.284  1.00 92.71  ? 156 GLY D N     1 
ATOM   7739 C CA    . GLY D 1 184 ? -11.697 -15.132 22.047  1.00 90.63  ? 156 GLY D CA    1 
ATOM   7740 C C     . GLY D 1 184 ? -10.256 -15.188 21.588  1.00 92.86  ? 156 GLY D C     1 
ATOM   7741 O O     . GLY D 1 184 ? -9.975  -14.827 20.438  1.00 97.48  ? 156 GLY D O     1 
ATOM   7742 N N     . GLY D 1 185 ? -9.338  -15.622 22.450  1.00 90.75  ? 157 GLY D N     1 
ATOM   7743 C CA    . GLY D 1 185 ? -7.959  -15.779 22.042  1.00 83.63  ? 157 GLY D CA    1 
ATOM   7744 C C     . GLY D 1 185 ? -7.794  -16.859 20.991  1.00 84.19  ? 157 GLY D C     1 
ATOM   7745 O O     . GLY D 1 185 ? -8.664  -17.703 20.778  1.00 83.37  ? 157 GLY D O     1 
ATOM   7746 N N     . GLU D 1 186 ? -6.645  -16.829 20.322  1.00 81.77  ? 158 GLU D N     1 
ATOM   7747 C CA    . GLU D 1 186 ? -6.382  -17.703 19.190  1.00 81.48  ? 158 GLU D CA    1 
ATOM   7748 C C     . GLU D 1 186 ? -5.157  -18.567 19.457  1.00 78.52  ? 158 GLU D C     1 
ATOM   7749 O O     . GLU D 1 186 ? -4.230  -18.161 20.165  1.00 75.26  ? 158 GLU D O     1 
ATOM   7750 C CB    . GLU D 1 186 ? -6.184  -16.885 17.909  1.00 80.49  ? 158 GLU D CB    1 
ATOM   7751 C CG    . GLU D 1 186 ? -7.369  -15.990 17.579  1.00 87.46  ? 158 GLU D CG    1 
ATOM   7752 C CD    . GLU D 1 186 ? -7.044  -14.943 16.532  1.00 92.90  ? 158 GLU D CD    1 
ATOM   7753 O OE1   . GLU D 1 186 ? -5.929  -14.386 16.574  1.00 91.45  ? 158 GLU D OE1   1 
ATOM   7754 O OE2   . GLU D 1 186 ? -7.907  -14.673 15.671  1.00 97.31  ? 158 GLU D OE2   1 
ATOM   7755 N N     . ALA D 1 187 ? -5.165  -19.768 18.881  1.00 75.88  ? 159 ALA D N     1 
ATOM   7756 C CA    . ALA D 1 187 ? -4.087  -20.736 19.051  1.00 65.59  ? 159 ALA D CA    1 
ATOM   7757 C C     . ALA D 1 187 ? -3.606  -21.183 17.680  1.00 66.32  ? 159 ALA D C     1 
ATOM   7758 O O     . ALA D 1 187 ? -4.397  -21.690 16.878  1.00 70.83  ? 159 ALA D O     1 
ATOM   7759 C CB    . ALA D 1 187 ? -4.550  -21.938 19.880  1.00 64.85  ? 159 ALA D CB    1 
ATOM   7760 N N     . VAL D 1 188 ? -2.316  -21.000 17.416  1.00 65.07  ? 160 VAL D N     1 
ATOM   7761 C CA    . VAL D 1 188 ? -1.706  -21.363 16.141  1.00 63.89  ? 160 VAL D CA    1 
ATOM   7762 C C     . VAL D 1 188 ? -0.937  -22.662 16.332  1.00 66.52  ? 160 VAL D C     1 
ATOM   7763 O O     . VAL D 1 188 ? 0.035   -22.713 17.096  1.00 68.60  ? 160 VAL D O     1 
ATOM   7764 C CB    . VAL D 1 188 ? -0.786  -20.248 15.621  1.00 59.23  ? 160 VAL D CB    1 
ATOM   7765 C CG1   . VAL D 1 188 ? -0.035  -20.714 14.384  1.00 58.55  ? 160 VAL D CG1   1 
ATOM   7766 C CG2   . VAL D 1 188 ? -1.592  -18.993 15.323  1.00 58.69  ? 160 VAL D CG2   1 
ATOM   7767 N N     . PHE D 1 189 ? -1.364  -23.710 15.636  1.00 64.86  ? 161 PHE D N     1 
ATOM   7768 C CA    . PHE D 1 189 ? -0.749  -25.024 15.746  1.00 63.37  ? 161 PHE D CA    1 
ATOM   7769 C C     . PHE D 1 189 ? 0.134   -25.317 14.539  1.00 60.25  ? 161 PHE D C     1 
ATOM   7770 O O     . PHE D 1 189 ? -0.036  -24.751 13.456  1.00 59.37  ? 161 PHE D O     1 
ATOM   7771 C CB    . PHE D 1 189 ? -1.814  -26.114 15.887  1.00 65.79  ? 161 PHE D CB    1 
ATOM   7772 C CG    . PHE D 1 189 ? -2.628  -26.008 17.144  1.00 68.75  ? 161 PHE D CG    1 
ATOM   7773 C CD1   . PHE D 1 189 ? -2.217  -26.644 18.304  1.00 66.25  ? 161 PHE D CD1   1 
ATOM   7774 C CD2   . PHE D 1 189 ? -3.803  -25.277 17.167  1.00 69.66  ? 161 PHE D CD2   1 
ATOM   7775 C CE1   . PHE D 1 189 ? -2.962  -26.552 19.464  1.00 61.22  ? 161 PHE D CE1   1 
ATOM   7776 C CE2   . PHE D 1 189 ? -4.553  -25.181 18.324  1.00 71.73  ? 161 PHE D CE2   1 
ATOM   7777 C CZ    . PHE D 1 189 ? -4.131  -25.819 19.474  1.00 67.18  ? 161 PHE D CZ    1 
ATOM   7778 N N     . SER D 1 190 ? 1.093   -26.222 14.749  1.00 60.51  ? 162 SER D N     1 
ATOM   7779 C CA    . SER D 1 190 ? 1.994   -26.723 13.718  1.00 61.26  ? 162 SER D CA    1 
ATOM   7780 C C     . SER D 1 190 ? 2.348   -28.161 14.104  1.00 58.88  ? 162 SER D C     1 
ATOM   7781 O O     . SER D 1 190 ? 3.478   -28.496 14.454  1.00 62.02  ? 162 SER D O     1 
ATOM   7782 C CB    . SER D 1 190 ? 3.241   -25.849 13.569  1.00 64.84  ? 162 SER D CB    1 
ATOM   7783 O OG    . SER D 1 190 ? 4.042   -26.282 12.483  1.00 62.19  ? 162 SER D OG    1 
ATOM   7784 N N     . VAL D 1 191 ? 1.351   -29.033 14.048  1.00 59.72  ? 163 VAL D N     1 
ATOM   7785 C CA    . VAL D 1 191 ? 1.491   -30.417 14.484  1.00 62.40  ? 163 VAL D CA    1 
ATOM   7786 C C     . VAL D 1 191 ? 1.979   -31.264 13.319  1.00 69.01  ? 163 VAL D C     1 
ATOM   7787 O O     . VAL D 1 191 ? 1.510   -31.118 12.184  1.00 72.61  ? 163 VAL D O     1 
ATOM   7788 C CB    . VAL D 1 191 ? 0.155   -30.950 15.035  1.00 61.73  ? 163 VAL D CB    1 
ATOM   7789 C CG1   . VAL D 1 191 ? 0.331   -32.347 15.612  1.00 63.75  ? 163 VAL D CG1   1 
ATOM   7790 C CG2   . VAL D 1 191 ? -0.402  -29.996 16.076  1.00 63.72  ? 163 VAL D CG2   1 
ATOM   7791 N N     . ILE D 1 192 ? 2.928   -32.152 13.598  1.00 65.62  ? 164 ILE D N     1 
ATOM   7792 C CA    . ILE D 1 192 ? 3.412   -33.091 12.593  1.00 69.48  ? 164 ILE D CA    1 
ATOM   7793 C C     . ILE D 1 192 ? 2.463   -34.282 12.541  1.00 76.20  ? 164 ILE D C     1 
ATOM   7794 O O     . ILE D 1 192 ? 2.295   -35.000 13.532  1.00 79.20  ? 164 ILE D O     1 
ATOM   7795 C CB    . ILE D 1 192 ? 4.848   -33.540 12.894  1.00 65.78  ? 164 ILE D CB    1 
ATOM   7796 C CG1   . ILE D 1 192 ? 5.823   -32.379 12.692  1.00 64.87  ? 164 ILE D CG1   1 
ATOM   7797 C CG2   . ILE D 1 192 ? 5.224   -34.724 12.021  1.00 73.03  ? 164 ILE D CG2   1 
ATOM   7798 C CD1   . ILE D 1 192 ? 7.253   -32.707 13.061  1.00 62.12  ? 164 ILE D CD1   1 
ATOM   7799 N N     . ALA D 1 193 ? 1.837   -34.488 11.383  1.00 82.68  ? 165 ALA D N     1 
ATOM   7800 C CA    . ALA D 1 193 ? 0.922   -35.607 11.197  1.00 84.11  ? 165 ALA D CA    1 
ATOM   7801 C C     . ALA D 1 193 ? 1.680   -36.927 11.217  1.00 82.20  ? 165 ALA D C     1 
ATOM   7802 O O     . ALA D 1 193 ? 1.551   -37.711 12.162  1.00 86.21  ? 165 ALA D O     1 
ATOM   7803 C CB    . ALA D 1 193 ? 0.149   -35.459 9.886   1.00 86.62  ? 165 ALA D CB    1 
ATOM   7804 N N     . ASN D 1 194 ? 2.476   -37.177 10.180  1.00 81.61  ? 166 ASN D N     1 
ATOM   7805 C CA    . ASN D 1 194 ? 3.254   -38.401 10.080  1.00 85.50  ? 166 ASN D CA    1 
ATOM   7806 C C     . ASN D 1 194 ? 4.635   -38.080 9.530   1.00 82.57  ? 166 ASN D C     1 
ATOM   7807 O O     . ASN D 1 194 ? 4.814   -37.117 8.779   1.00 78.55  ? 166 ASN D O     1 
ATOM   7808 C CB    . ASN D 1 194 ? 2.555   -39.442 9.191   1.00 91.52  ? 166 ASN D CB    1 
ATOM   7809 C CG    . ASN D 1 194 ? 2.487   -39.019 7.734   1.00 96.23  ? 166 ASN D CG    1 
ATOM   7810 O OD1   . ASN D 1 194 ? 3.457   -39.153 6.989   1.00 96.42  ? 166 ASN D OD1   1 
ATOM   7811 N ND2   . ASN D 1 194 ? 1.334   -38.502 7.323   1.00 97.42  ? 166 ASN D ND2   1 
ATOM   7812 N N     . MET D 1 195 ? 5.612   -38.897 9.915   1.00 78.73  ? 167 MET D N     1 
ATOM   7813 C CA    . MET D 1 195 ? 6.974   -38.741 9.429   1.00 79.44  ? 167 MET D CA    1 
ATOM   7814 C C     . MET D 1 195 ? 7.684   -40.079 9.554   1.00 84.88  ? 167 MET D C     1 
ATOM   7815 O O     . MET D 1 195 ? 7.281   -40.944 10.336  1.00 87.27  ? 167 MET D O     1 
ATOM   7816 C CB    . MET D 1 195 ? 7.728   -37.651 10.198  1.00 78.39  ? 167 MET D CB    1 
ATOM   7817 C CG    . MET D 1 195 ? 7.561   -37.718 11.707  1.00 90.93  ? 167 MET D CG    1 
ATOM   7818 S SD    . MET D 1 195 ? 8.302   -36.297 12.535  1.00 91.82  ? 167 MET D SD    1 
ATOM   7819 C CE    . MET D 1 195 ? 9.785   -36.076 11.560  1.00 82.64  ? 167 MET D CE    1 
ATOM   7820 N N     . ALA D 1 196 ? 8.755   -40.236 8.774   1.00 86.54  ? 168 ALA D N     1 
ATOM   7821 C CA    . ALA D 1 196 ? 9.486   -41.497 8.759   1.00 90.24  ? 168 ALA D CA    1 
ATOM   7822 C C     . ALA D 1 196 ? 10.320  -41.718 10.014  1.00 88.61  ? 168 ALA D C     1 
ATOM   7823 O O     . ALA D 1 196 ? 10.795  -42.839 10.226  1.00 84.62  ? 168 ALA D O     1 
ATOM   7824 C CB    . ALA D 1 196 ? 10.383  -41.569 7.524   1.00 92.11  ? 168 ALA D CB    1 
ATOM   7825 N N     . LEU D 1 197 ? 10.517  -40.689 10.842  1.00 88.10  ? 169 LEU D N     1 
ATOM   7826 C CA    . LEU D 1 197 ? 11.201  -40.904 12.112  1.00 92.84  ? 169 LEU D CA    1 
ATOM   7827 C C     . LEU D 1 197 ? 10.378  -41.789 13.038  1.00 96.12  ? 169 LEU D C     1 
ATOM   7828 O O     . LEU D 1 197 ? 10.943  -42.527 13.855  1.00 90.50  ? 169 LEU D O     1 
ATOM   7829 C CB    . LEU D 1 197 ? 11.500  -39.569 12.801  1.00 93.05  ? 169 LEU D CB    1 
ATOM   7830 C CG    . LEU D 1 197 ? 12.430  -38.544 12.142  1.00 86.31  ? 169 LEU D CG    1 
ATOM   7831 C CD1   . LEU D 1 197 ? 12.697  -37.386 13.097  1.00 74.85  ? 169 LEU D CD1   1 
ATOM   7832 C CD2   . LEU D 1 197 ? 13.732  -39.157 11.676  1.00 84.02  ? 169 LEU D CD2   1 
ATOM   7833 N N     . CYS D 1 198 ? 9.049   -41.731 12.923  1.00 100.42 ? 170 CYS D N     1 
ATOM   7834 C CA    . CYS D 1 198 ? 8.180   -42.536 13.774  1.00 94.15  ? 170 CYS D CA    1 
ATOM   7835 C C     . CYS D 1 198 ? 8.130   -43.987 13.313  1.00 95.56  ? 170 CYS D C     1 
ATOM   7836 O O     . CYS D 1 198 ? 8.173   -44.904 14.141  1.00 93.03  ? 170 CYS D O     1 
ATOM   7837 C CB    . CYS D 1 198 ? 6.773   -41.939 13.799  1.00 90.15  ? 170 CYS D CB    1 
ATOM   7838 S SG    . CYS D 1 198 ? 6.627   -40.400 14.736  1.00 98.73  ? 170 CYS D SG    1 
ATOM   7839 N N     . ASP D 1 199 ? 8.026   -44.216 12.000  1.00 98.64  ? 171 ASP D N     1 
ATOM   7840 C CA    . ASP D 1 199 ? 8.032   -45.584 11.489  1.00 96.49  ? 171 ASP D CA    1 
ATOM   7841 C C     . ASP D 1 199 ? 9.361   -46.269 11.775  1.00 99.43  ? 171 ASP D C     1 
ATOM   7842 O O     . ASP D 1 199 ? 9.401   -47.475 12.050  1.00 101.07 ? 171 ASP D O     1 
ATOM   7843 C CB    . ASP D 1 199 ? 7.736   -45.589 9.990   1.00 89.16  ? 171 ASP D CB    1 
ATOM   7844 C CG    . ASP D 1 199 ? 6.339   -45.101 9.669   1.00 91.35  ? 171 ASP D CG    1 
ATOM   7845 O OD1   . ASP D 1 199 ? 5.411   -45.398 10.450  1.00 95.72  ? 171 ASP D OD1   1 
ATOM   7846 O OD2   . ASP D 1 199 ? 6.168   -44.424 8.633   1.00 88.99  ? 171 ASP D OD2   1 
ATOM   7847 N N     . ALA D 1 200 ? 10.464  -45.517 11.714  1.00 101.94 ? 172 ALA D N     1 
ATOM   7848 C CA    . ALA D 1 200 ? 11.757  -46.076 12.091  1.00 98.46  ? 172 ALA D CA    1 
ATOM   7849 C C     . ALA D 1 200 ? 11.790  -46.448 13.567  1.00 98.87  ? 172 ALA D C     1 
ATOM   7850 O O     . ALA D 1 200 ? 12.511  -47.372 13.958  1.00 93.61  ? 172 ALA D O     1 
ATOM   7851 C CB    . ALA D 1 200 ? 12.876  -45.088 11.762  1.00 93.92  ? 172 ALA D CB    1 
ATOM   7852 N N     . TYR D 1 201 ? 11.019  -45.743 14.398  1.00 99.98  ? 173 TYR D N     1 
ATOM   7853 C CA    . TYR D 1 201 ? 10.913  -46.114 15.805  1.00 101.48 ? 173 TYR D CA    1 
ATOM   7854 C C     . TYR D 1 201 ? 10.138  -47.416 15.973  1.00 101.44 ? 173 TYR D C     1 
ATOM   7855 O O     . TYR D 1 201 ? 10.544  -48.292 16.745  1.00 98.51  ? 173 TYR D O     1 
ATOM   7856 C CB    . TYR D 1 201 ? 10.240  -44.991 16.594  1.00 98.34  ? 173 TYR D CB    1 
ATOM   7857 C CG    . TYR D 1 201 ? 11.170  -43.887 17.042  1.00 97.29  ? 173 TYR D CG    1 
ATOM   7858 C CD1   . TYR D 1 201 ? 12.534  -44.112 17.187  1.00 91.46  ? 173 TYR D CD1   1 
ATOM   7859 C CD2   . TYR D 1 201 ? 10.682  -42.617 17.318  1.00 95.63  ? 173 TYR D CD2   1 
ATOM   7860 C CE1   . TYR D 1 201 ? 13.383  -43.100 17.598  1.00 87.29  ? 173 TYR D CE1   1 
ATOM   7861 C CE2   . TYR D 1 201 ? 11.521  -41.602 17.727  1.00 90.25  ? 173 TYR D CE2   1 
ATOM   7862 C CZ    . TYR D 1 201 ? 12.870  -41.848 17.866  1.00 87.10  ? 173 TYR D CZ    1 
ATOM   7863 O OH    . TYR D 1 201 ? 13.705  -40.835 18.275  1.00 82.27  ? 173 TYR D OH    1 
ATOM   7864 N N     . GLU D 1 202 ? 9.019   -47.557 15.257  1.00 100.96 ? 174 GLU D N     1 
ATOM   7865 C CA    . GLU D 1 202 ? 8.197   -48.756 15.383  1.00 101.32 ? 174 GLU D CA    1 
ATOM   7866 C C     . GLU D 1 202 ? 8.919   -49.994 14.869  1.00 101.04 ? 174 GLU D C     1 
ATOM   7867 O O     . GLU D 1 202 ? 8.666   -51.103 15.354  1.00 100.89 ? 174 GLU D O     1 
ATOM   7868 C CB    . GLU D 1 202 ? 6.876   -48.569 14.636  1.00 103.31 ? 174 GLU D CB    1 
ATOM   7869 C CG    . GLU D 1 202 ? 5.932   -47.565 15.277  1.00 109.72 ? 174 GLU D CG    1 
ATOM   7870 C CD    . GLU D 1 202 ? 4.761   -47.208 14.381  1.00 110.14 ? 174 GLU D CD    1 
ATOM   7871 O OE1   . GLU D 1 202 ? 4.949   -47.161 13.146  1.00 104.08 ? 174 GLU D OE1   1 
ATOM   7872 O OE2   . GLU D 1 202 ? 3.655   -46.973 14.910  1.00 109.82 ? 174 GLU D OE2   1 
ATOM   7873 N N     . GLU D 1 203 ? 9.813   -49.831 13.892  1.00 103.74 ? 175 GLU D N     1 
ATOM   7874 C CA    . GLU D 1 203 ? 10.555  -50.972 13.369  1.00 102.37 ? 175 GLU D CA    1 
ATOM   7875 C C     . GLU D 1 203 ? 11.698  -51.380 14.289  1.00 103.73 ? 175 GLU D C     1 
ATOM   7876 O O     . GLU D 1 203 ? 12.005  -52.572 14.395  1.00 107.27 ? 175 GLU D O     1 
ATOM   7877 C CB    . GLU D 1 203 ? 11.090  -50.655 11.972  1.00 97.95  ? 175 GLU D CB    1 
ATOM   7878 N N     . MET D 1 204 ? 12.337  -50.416 14.958  1.00 103.17 ? 176 MET D N     1 
ATOM   7879 C CA    . MET D 1 204 ? 13.406  -50.754 15.891  1.00 102.96 ? 176 MET D CA    1 
ATOM   7880 C C     . MET D 1 204 ? 12.870  -51.468 17.125  1.00 104.59 ? 176 MET D C     1 
ATOM   7881 O O     . MET D 1 204 ? 13.569  -52.306 17.705  1.00 99.77  ? 176 MET D O     1 
ATOM   7882 C CB    . MET D 1 204 ? 14.169  -49.496 16.304  1.00 103.15 ? 176 MET D CB    1 
ATOM   7883 C CG    . MET D 1 204 ? 15.009  -48.876 15.200  1.00 103.53 ? 176 MET D CG    1 
ATOM   7884 S SD    . MET D 1 204 ? 15.847  -47.373 15.739  1.00 95.38  ? 176 MET D SD    1 
ATOM   7885 C CE    . MET D 1 204 ? 17.062  -48.052 16.864  1.00 87.45  ? 176 MET D CE    1 
ATOM   7886 N N     . ALA D 1 205 ? 11.636  -51.158 17.534  1.00 105.36 ? 177 ALA D N     1 
ATOM   7887 C CA    . ALA D 1 205 ? 11.088  -51.741 18.755  1.00 107.26 ? 177 ALA D CA    1 
ATOM   7888 C C     . ALA D 1 205 ? 10.915  -53.250 18.637  1.00 110.00 ? 177 ALA D C     1 
ATOM   7889 O O     . ALA D 1 205 ? 10.931  -53.955 19.653  1.00 109.21 ? 177 ALA D O     1 
ATOM   7890 C CB    . ALA D 1 205 ? 9.753   -51.078 19.098  1.00 104.40 ? 177 ALA D CB    1 
ATOM   7891 N N     . LYS D 1 206 ? 10.749  -53.763 17.416  1.00 108.24 ? 178 LYS D N     1 
ATOM   7892 C CA    . LYS D 1 206 ? 10.604  -55.200 17.217  1.00 100.21 ? 178 LYS D CA    1 
ATOM   7893 C C     . LYS D 1 206 ? 11.918  -55.954 17.371  1.00 104.07 ? 178 LYS D C     1 
ATOM   7894 O O     . LYS D 1 206 ? 11.895  -57.174 17.566  1.00 108.13 ? 178 LYS D O     1 
ATOM   7895 C CB    . LYS D 1 206 ? 10.007  -55.486 15.837  1.00 92.39  ? 178 LYS D CB    1 
ATOM   7896 C CG    . LYS D 1 206 ? 8.586   -54.980 15.660  1.00 89.16  ? 178 LYS D CG    1 
ATOM   7897 C CD    . LYS D 1 206 ? 8.092   -55.198 14.241  1.00 83.47  ? 178 LYS D CD    1 
ATOM   7898 C CE    . LYS D 1 206 ? 6.701   -54.615 14.048  1.00 82.13  ? 178 LYS D CE    1 
ATOM   7899 N NZ    . LYS D 1 206 ? 6.250   -54.722 12.633  1.00 85.55  ? 178 LYS D NZ    1 
ATOM   7900 N N     . GLU D 1 207 ? 13.050  -55.266 17.291  1.00 103.04 ? 179 GLU D N     1 
ATOM   7901 C CA    . GLU D 1 207 ? 14.338  -55.934 17.432  1.00 102.09 ? 179 GLU D CA    1 
ATOM   7902 C C     . GLU D 1 207 ? 14.537  -56.381 18.876  1.00 98.99  ? 179 GLU D C     1 
ATOM   7903 O O     . GLU D 1 207 ? 14.341  -55.581 19.798  1.00 102.48 ? 179 GLU D O     1 
ATOM   7904 C CB    . GLU D 1 207 ? 15.472  -55.005 17.006  1.00 103.51 ? 179 GLU D CB    1 
ATOM   7905 N N     . PRO D 1 208 ? 14.917  -57.640 19.115  1.00 100.52 ? 180 PRO D N     1 
ATOM   7906 C CA    . PRO D 1 208 ? 15.167  -58.086 20.497  1.00 106.90 ? 180 PRO D CA    1 
ATOM   7907 C C     . PRO D 1 208 ? 16.246  -57.291 21.210  1.00 106.93 ? 180 PRO D C     1 
ATOM   7908 O O     . PRO D 1 208 ? 16.319  -57.343 22.444  1.00 113.45 ? 180 PRO D O     1 
ATOM   7909 C CB    . PRO D 1 208 ? 15.578  -59.553 20.321  1.00 107.70 ? 180 PRO D CB    1 
ATOM   7910 C CG    . PRO D 1 208 ? 14.922  -59.973 19.047  1.00 109.83 ? 180 PRO D CG    1 
ATOM   7911 C CD    . PRO D 1 208 ? 14.936  -58.759 18.156  1.00 103.04 ? 180 PRO D CD    1 
ATOM   7912 N N     . ARG D 1 209 ? 17.091  -56.566 20.476  1.00 99.20  ? 181 ARG D N     1 
ATOM   7913 C CA    . ARG D 1 209 ? 18.085  -55.695 21.089  1.00 101.21 ? 181 ARG D CA    1 
ATOM   7914 C C     . ARG D 1 209 ? 17.488  -54.392 21.603  1.00 102.23 ? 181 ARG D C     1 
ATOM   7915 O O     . ARG D 1 209 ? 18.104  -53.738 22.450  1.00 89.48  ? 181 ARG D O     1 
ATOM   7916 C CB    . ARG D 1 209 ? 19.199  -55.397 20.082  1.00 101.46 ? 181 ARG D CB    1 
ATOM   7917 C CG    . ARG D 1 209 ? 18.806  -54.416 18.987  1.00 103.02 ? 181 ARG D CG    1 
ATOM   7918 C CD    . ARG D 1 209 ? 19.983  -54.057 18.086  1.00 97.16  ? 181 ARG D CD    1 
ATOM   7919 N NE    . ARG D 1 209 ? 21.184  -53.695 18.830  1.00 99.07  ? 181 ARG D NE    1 
ATOM   7920 C CZ    . ARG D 1 209 ? 22.244  -53.105 18.294  1.00 87.85  ? 181 ARG D CZ    1 
ATOM   7921 N NH1   . ARG D 1 209 ? 22.282  -52.785 17.011  1.00 82.28  ? 181 ARG D NH1   1 
ATOM   7922 N NH2   . ARG D 1 209 ? 23.293  -52.830 19.064  1.00 82.08  ? 181 ARG D NH2   1 
ATOM   7923 N N     . TRP D 1 210 ? 16.300  -54.013 21.125  1.00 105.46 ? 182 TRP D N     1 
ATOM   7924 C CA    . TRP D 1 210 ? 15.702  -52.727 21.454  1.00 107.60 ? 182 TRP D CA    1 
ATOM   7925 C C     . TRP D 1 210 ? 14.380  -52.827 22.199  1.00 103.30 ? 182 TRP D C     1 
ATOM   7926 O O     . TRP D 1 210 ? 13.954  -51.827 22.788  1.00 102.48 ? 182 TRP D O     1 
ATOM   7927 C CB    . TRP D 1 210 ? 15.462  -51.906 20.176  1.00 102.05 ? 182 TRP D CB    1 
ATOM   7928 C CG    . TRP D 1 210 ? 16.692  -51.551 19.377  1.00 98.37  ? 182 TRP D CG    1 
ATOM   7929 C CD1   . TRP D 1 210 ? 16.787  -51.520 18.015  1.00 94.83  ? 182 TRP D CD1   1 
ATOM   7930 C CD2   . TRP D 1 210 ? 17.982  -51.152 19.874  1.00 100.02 ? 182 TRP D CD2   1 
ATOM   7931 N NE1   . TRP D 1 210 ? 18.051  -51.148 17.633  1.00 98.47  ? 182 TRP D NE1   1 
ATOM   7932 C CE2   . TRP D 1 210 ? 18.803  -50.913 18.754  1.00 100.04 ? 182 TRP D CE2   1 
ATOM   7933 C CE3   . TRP D 1 210 ? 18.523  -50.978 21.153  1.00 98.62  ? 182 TRP D CE3   1 
ATOM   7934 C CZ2   . TRP D 1 210 ? 20.132  -50.513 18.873  1.00 99.58  ? 182 TRP D CZ2   1 
ATOM   7935 C CZ3   . TRP D 1 210 ? 19.844  -50.583 21.268  1.00 95.61  ? 182 TRP D CZ3   1 
ATOM   7936 C CH2   . TRP D 1 210 ? 20.632  -50.355 20.135  1.00 95.98  ? 182 TRP D CH2   1 
ATOM   7937 N N     . ALA D 1 211 ? 13.724  -53.992 22.193  1.00 102.00 ? 183 ALA D N     1 
ATOM   7938 C CA    . ALA D 1 211 ? 12.360  -54.090 22.709  1.00 96.22  ? 183 ALA D CA    1 
ATOM   7939 C C     . ALA D 1 211 ? 12.275  -53.730 24.186  1.00 98.46  ? 183 ALA D C     1 
ATOM   7940 O O     . ALA D 1 211 ? 11.222  -53.278 24.651  1.00 100.12 ? 183 ALA D O     1 
ATOM   7941 C CB    . ALA D 1 211 ? 11.811  -55.497 22.476  1.00 97.03  ? 183 ALA D CB    1 
ATOM   7942 N N     . LEU D 1 212 ? 13.360  -53.922 24.938  1.00 101.45 ? 184 LEU D N     1 
ATOM   7943 C CA    . LEU D 1 212 ? 13.349  -53.564 26.353  1.00 97.31  ? 184 LEU D CA    1 
ATOM   7944 C C     . LEU D 1 212 ? 13.222  -52.056 26.534  1.00 98.35  ? 184 LEU D C     1 
ATOM   7945 O O     . LEU D 1 212 ? 12.364  -51.580 27.286  1.00 92.93  ? 184 LEU D O     1 
ATOM   7946 C CB    . LEU D 1 212 ? 14.613  -54.088 27.036  1.00 84.11  ? 184 LEU D CB    1 
ATOM   7947 N N     . TYR D 1 213 ? 14.065  -51.286 25.843  1.00 99.31  ? 185 TYR D N     1 
ATOM   7948 C CA    . TYR D 1 213 ? 14.021  -49.832 25.928  1.00 91.75  ? 185 TYR D CA    1 
ATOM   7949 C C     . TYR D 1 213 ? 12.861  -49.219 25.155  1.00 92.77  ? 185 TYR D C     1 
ATOM   7950 O O     . TYR D 1 213 ? 12.620  -48.015 25.292  1.00 93.36  ? 185 TYR D O     1 
ATOM   7951 C CB    . TYR D 1 213 ? 15.332  -49.228 25.414  1.00 90.02  ? 185 TYR D CB    1 
ATOM   7952 C CG    . TYR D 1 213 ? 16.578  -49.715 26.120  1.00 91.62  ? 185 TYR D CG    1 
ATOM   7953 C CD1   . TYR D 1 213 ? 17.006  -49.122 27.301  1.00 89.20  ? 185 TYR D CD1   1 
ATOM   7954 C CD2   . TYR D 1 213 ? 17.335  -50.755 25.598  1.00 99.36  ? 185 TYR D CD2   1 
ATOM   7955 C CE1   . TYR D 1 213 ? 18.148  -49.558 27.948  1.00 89.40  ? 185 TYR D CE1   1 
ATOM   7956 C CE2   . TYR D 1 213 ? 18.479  -51.198 26.238  1.00 104.61 ? 185 TYR D CE2   1 
ATOM   7957 C CZ    . TYR D 1 213 ? 18.880  -50.596 27.412  1.00 95.79  ? 185 TYR D CZ    1 
ATOM   7958 O OH    . TYR D 1 213 ? 20.017  -51.034 28.052  1.00 89.78  ? 185 TYR D OH    1 
ATOM   7959 N N     . MET D 1 214 ? 12.142  -50.004 24.350  1.00 95.63  ? 186 MET D N     1 
ATOM   7960 C CA    . MET D 1 214 ? 11.110  -49.466 23.470  1.00 95.33  ? 186 MET D CA    1 
ATOM   7961 C C     . MET D 1 214 ? 9.774   -50.175 23.663  1.00 100.12 ? 186 MET D C     1 
ATOM   7962 O O     . MET D 1 214 ? 9.005   -50.329 22.710  1.00 99.52  ? 186 MET D O     1 
ATOM   7963 C CB    . MET D 1 214 ? 11.547  -49.548 22.008  1.00 93.06  ? 186 MET D CB    1 
ATOM   7964 N N     . GLN D 1 215 ? 9.479   -50.611 24.891  1.00 98.29  ? 187 GLN D N     1 
ATOM   7965 C CA    . GLN D 1 215 ? 8.179   -51.220 25.157  1.00 96.21  ? 187 GLN D CA    1 
ATOM   7966 C C     . GLN D 1 215 ? 7.051   -50.205 25.018  1.00 99.89  ? 187 GLN D C     1 
ATOM   7967 O O     . GLN D 1 215 ? 5.928   -50.573 24.655  1.00 99.83  ? 187 GLN D O     1 
ATOM   7968 C CB    . GLN D 1 215 ? 8.165   -51.845 26.552  1.00 89.41  ? 187 GLN D CB    1 
ATOM   7969 N N     . ASP D 1 216 ? 7.332   -48.937 25.292  1.00 96.71  ? 188 ASP D N     1 
ATOM   7970 C CA    . ASP D 1 216 ? 6.361   -47.849 25.165  1.00 95.22  ? 188 ASP D CA    1 
ATOM   7971 C C     . ASP D 1 216 ? 6.557   -47.088 23.861  1.00 92.00  ? 188 ASP D C     1 
ATOM   7972 O O     . ASP D 1 216 ? 6.569   -45.857 23.837  1.00 89.28  ? 188 ASP D O     1 
ATOM   7973 C CB    . ASP D 1 216 ? 6.470   -46.912 26.361  1.00 95.02  ? 188 ASP D CB    1 
ATOM   7974 C CG    . ASP D 1 216 ? 7.905   -46.525 26.665  1.00 93.00  ? 188 ASP D CG    1 
ATOM   7975 O OD1   . ASP D 1 216 ? 8.824   -47.193 26.144  1.00 91.37  ? 188 ASP D OD1   1 
ATOM   7976 O OD2   . ASP D 1 216 ? 8.117   -45.555 27.423  1.00 99.53  ? 188 ASP D OD2   1 
ATOM   7977 N N     . VAL D 1 217 ? 6.712   -47.822 22.756  1.00 91.83  ? 189 VAL D N     1 
ATOM   7978 C CA    . VAL D 1 217 ? 7.025   -47.185 21.481  1.00 89.86  ? 189 VAL D CA    1 
ATOM   7979 C C     . VAL D 1 217 ? 5.855   -46.344 20.982  1.00 88.23  ? 189 VAL D C     1 
ATOM   7980 O O     . VAL D 1 217 ? 6.061   -45.295 20.361  1.00 90.36  ? 189 VAL D O     1 
ATOM   7981 C CB    . VAL D 1 217 ? 7.451   -48.248 20.449  1.00 95.22  ? 189 VAL D CB    1 
ATOM   7982 C CG1   . VAL D 1 217 ? 6.319   -49.232 20.183  1.00 99.63  ? 189 VAL D CG1   1 
ATOM   7983 C CG2   . VAL D 1 217 ? 7.914   -47.588 19.155  1.00 101.57 ? 189 VAL D CG2   1 
ATOM   7984 N N     . GLU D 1 218 ? 4.617   -46.764 21.260  1.00 88.20  ? 190 GLU D N     1 
ATOM   7985 C CA    . GLU D 1 218 ? 3.457   -46.021 20.779  1.00 87.58  ? 190 GLU D CA    1 
ATOM   7986 C C     . GLU D 1 218 ? 3.304   -44.668 21.463  1.00 88.10  ? 190 GLU D C     1 
ATOM   7987 O O     . GLU D 1 218 ? 2.564   -43.815 20.960  1.00 84.47  ? 190 GLU D O     1 
ATOM   7988 C CB    . GLU D 1 218 ? 2.182   -46.850 20.959  1.00 88.02  ? 190 GLU D CB    1 
ATOM   7989 C CG    . GLU D 1 218 ? 1.793   -47.124 22.405  1.00 98.74  ? 190 GLU D CG    1 
ATOM   7990 C CD    . GLU D 1 218 ? 2.566   -48.281 23.019  1.00 93.76  ? 190 GLU D CD    1 
ATOM   7991 O OE1   . GLU D 1 218 ? 3.514   -48.782 22.378  1.00 87.23  ? 190 GLU D OE1   1 
ATOM   7992 O OE2   . GLU D 1 218 ? 2.221   -48.692 24.147  1.00 93.64  ? 190 GLU D OE2   1 
ATOM   7993 N N     . LYS D 1 219 ? 3.980   -44.452 22.592  1.00 86.92  ? 191 LYS D N     1 
ATOM   7994 C CA    . LYS D 1 219 ? 3.987   -43.148 23.240  1.00 86.00  ? 191 LYS D CA    1 
ATOM   7995 C C     . LYS D 1 219 ? 5.062   -42.222 22.688  1.00 86.33  ? 191 LYS D C     1 
ATOM   7996 O O     . LYS D 1 219 ? 4.974   -41.004 22.883  1.00 85.60  ? 191 LYS D O     1 
ATOM   7997 C CB    . LYS D 1 219 ? 4.178   -43.308 24.752  1.00 79.41  ? 191 LYS D CB    1 
ATOM   7998 N N     . PHE D 1 220 ? 6.071   -42.770 22.013  1.00 83.33  ? 192 PHE D N     1 
ATOM   7999 C CA    . PHE D 1 220 ? 7.100   -41.985 21.345  1.00 76.42  ? 192 PHE D CA    1 
ATOM   8000 C C     . PHE D 1 220 ? 6.742   -41.663 19.900  1.00 71.83  ? 192 PHE D C     1 
ATOM   8001 O O     . PHE D 1 220 ? 7.586   -41.141 19.164  1.00 74.52  ? 192 PHE D O     1 
ATOM   8002 C CB    . PHE D 1 220 ? 8.440   -42.727 21.389  1.00 75.77  ? 192 PHE D CB    1 
ATOM   8003 C CG    . PHE D 1 220 ? 9.128   -42.666 22.723  1.00 76.22  ? 192 PHE D CG    1 
ATOM   8004 C CD1   . PHE D 1 220 ? 8.654   -43.399 23.799  1.00 82.60  ? 192 PHE D CD1   1 
ATOM   8005 C CD2   . PHE D 1 220 ? 10.267  -41.896 22.894  1.00 78.52  ? 192 PHE D CD2   1 
ATOM   8006 C CE1   . PHE D 1 220 ? 9.292   -43.348 25.024  1.00 87.00  ? 192 PHE D CE1   1 
ATOM   8007 C CE2   . PHE D 1 220 ? 10.909  -41.841 24.116  1.00 79.91  ? 192 PHE D CE2   1 
ATOM   8008 C CZ    . PHE D 1 220 ? 10.422  -42.569 25.182  1.00 84.03  ? 192 PHE D CZ    1 
ATOM   8009 N N     . VAL D 1 221 ? 5.515   -41.962 19.481  1.00 72.35  ? 193 VAL D N     1 
ATOM   8010 C CA    . VAL D 1 221 ? 5.065   -41.766 18.110  1.00 75.32  ? 193 VAL D CA    1 
ATOM   8011 C C     . VAL D 1 221 ? 3.928   -40.756 18.113  1.00 79.22  ? 193 VAL D C     1 
ATOM   8012 O O     . VAL D 1 221 ? 3.113   -40.731 19.043  1.00 84.38  ? 193 VAL D O     1 
ATOM   8013 C CB    . VAL D 1 221 ? 4.618   -43.100 17.473  1.00 78.63  ? 193 VAL D CB    1 
ATOM   8014 C CG1   . VAL D 1 221 ? 4.080   -42.885 16.069  1.00 83.08  ? 193 VAL D CG1   1 
ATOM   8015 C CG2   . VAL D 1 221 ? 5.772   -44.087 17.449  1.00 86.48  ? 193 VAL D CG2   1 
ATOM   8016 N N     . SER D 1 222 ? 3.889   -39.912 17.087  1.00 67.99  ? 194 SER D N     1 
ATOM   8017 C CA    . SER D 1 222 ? 2.768   -39.002 16.921  1.00 77.00  ? 194 SER D CA    1 
ATOM   8018 C C     . SER D 1 222 ? 1.467   -39.797 16.832  1.00 90.24  ? 194 SER D C     1 
ATOM   8019 O O     . SER D 1 222 ? 1.422   -40.840 16.168  1.00 88.32  ? 194 SER D O     1 
ATOM   8020 C CB    . SER D 1 222 ? 2.949   -38.150 15.664  1.00 73.57  ? 194 SER D CB    1 
ATOM   8021 O OG    . SER D 1 222 ? 1.741   -37.501 15.307  1.00 79.22  ? 194 SER D OG    1 
ATOM   8022 N N     . PRO D 1 223 ? 0.398   -39.349 17.494  1.00 93.59  ? 195 PRO D N     1 
ATOM   8023 C CA    . PRO D 1 223 ? -0.864  -40.100 17.416  1.00 93.60  ? 195 PRO D CA    1 
ATOM   8024 C C     . PRO D 1 223 ? -1.490  -40.059 16.037  1.00 93.69  ? 195 PRO D C     1 
ATOM   8025 O O     . PRO D 1 223 ? -2.224  -40.987 15.673  1.00 97.33  ? 195 PRO D O     1 
ATOM   8026 C CB    . PRO D 1 223 ? -1.753  -39.410 18.459  1.00 91.72  ? 195 PRO D CB    1 
ATOM   8027 C CG    . PRO D 1 223 ? -1.196  -38.043 18.587  1.00 87.36  ? 195 PRO D CG    1 
ATOM   8028 C CD    . PRO D 1 223 ? 0.274   -38.118 18.292  1.00 86.54  ? 195 PRO D CD    1 
ATOM   8029 N N     . TYR D 1 224 ? -1.221  -39.014 15.259  1.00 90.80  ? 196 TYR D N     1 
ATOM   8030 C CA    . TYR D 1 224 ? -1.715  -38.896 13.896  1.00 92.41  ? 196 TYR D CA    1 
ATOM   8031 C C     . TYR D 1 224 ? -0.804  -39.581 12.887  1.00 92.86  ? 196 TYR D C     1 
ATOM   8032 O O     . TYR D 1 224 ? -0.938  -39.337 11.683  1.00 96.30  ? 196 TYR D O     1 
ATOM   8033 C CB    . TYR D 1 224 ? -1.887  -37.420 13.532  1.00 90.21  ? 196 TYR D CB    1 
ATOM   8034 C CG    . TYR D 1 224 ? -2.602  -36.622 14.598  1.00 90.67  ? 196 TYR D CG    1 
ATOM   8035 C CD1   . TYR D 1 224 ? -3.980  -36.699 14.746  1.00 95.57  ? 196 TYR D CD1   1 
ATOM   8036 C CD2   . TYR D 1 224 ? -1.895  -35.800 15.466  1.00 90.20  ? 196 TYR D CD2   1 
ATOM   8037 C CE1   . TYR D 1 224 ? -4.635  -35.974 15.723  1.00 94.94  ? 196 TYR D CE1   1 
ATOM   8038 C CE2   . TYR D 1 224 ? -2.541  -35.072 16.445  1.00 89.17  ? 196 TYR D CE2   1 
ATOM   8039 C CZ    . TYR D 1 224 ? -3.910  -35.163 16.569  1.00 90.79  ? 196 TYR D CZ    1 
ATOM   8040 O OH    . TYR D 1 224 ? -4.557  -34.439 17.544  1.00 93.95  ? 196 TYR D OH    1 
ATOM   8041 N N     . GLN D 1 225 ? 0.120   -40.425 13.353  1.00 91.85  ? 197 GLN D N     1 
ATOM   8042 C CA    . GLN D 1 225 ? 1.012   -41.139 12.445  1.00 92.74  ? 197 GLN D CA    1 
ATOM   8043 C C     . GLN D 1 225 ? 0.228   -42.063 11.524  1.00 98.27  ? 197 GLN D C     1 
ATOM   8044 O O     . GLN D 1 225 ? 0.347   -41.986 10.296  1.00 100.52 ? 197 GLN D O     1 
ATOM   8045 C CB    . GLN D 1 225 ? 2.043   -41.933 13.248  1.00 89.74  ? 197 GLN D CB    1 
ATOM   8046 C CG    . GLN D 1 225 ? 3.032   -42.718 12.403  1.00 87.08  ? 197 GLN D CG    1 
ATOM   8047 C CD    . GLN D 1 225 ? 3.989   -41.822 11.644  1.00 91.31  ? 197 GLN D CD    1 
ATOM   8048 O OE1   . GLN D 1 225 ? 4.276   -40.702 12.067  1.00 91.31  ? 197 GLN D OE1   1 
ATOM   8049 N NE2   . GLN D 1 225 ? 4.487   -42.310 10.515  1.00 97.12  ? 197 GLN D NE2   1 
ATOM   8050 N N     . HIS D 1 226 ? -0.584  -42.947 12.103  1.00 100.18 ? 198 HIS D N     1 
ATOM   8051 C CA    . HIS D 1 226 ? -1.369  -43.909 11.346  1.00 99.98  ? 198 HIS D CA    1 
ATOM   8052 C C     . HIS D 1 226 ? -2.777  -43.408 11.048  1.00 102.20 ? 198 HIS D C     1 
ATOM   8053 O O     . HIS D 1 226 ? -3.648  -44.208 10.688  1.00 107.20 ? 198 HIS D O     1 
ATOM   8054 C CB    . HIS D 1 226 ? -1.428  -45.240 12.099  1.00 95.40  ? 198 HIS D CB    1 
ATOM   8055 C CG    . HIS D 1 226 ? -0.085  -45.753 12.515  1.00 100.03 ? 198 HIS D CG    1 
ATOM   8056 N ND1   . HIS D 1 226 ? 0.908   -46.059 11.610  1.00 101.90 ? 198 HIS D ND1   1 
ATOM   8057 C CD2   . HIS D 1 226 ? 0.432   -46.006 13.741  1.00 102.62 ? 198 HIS D CD2   1 
ATOM   8058 C CE1   . HIS D 1 226 ? 1.978   -46.482 12.260  1.00 103.95 ? 198 HIS D CE1   1 
ATOM   8059 N NE2   . HIS D 1 226 ? 1.715   -46.459 13.554  1.00 105.17 ? 198 HIS D NE2   1 
ATOM   8060 N N     . SER D 1 227 ? -3.017  -42.107 11.186  1.00 105.68 ? 199 SER D N     1 
ATOM   8061 C CA    . SER D 1 227 ? -4.337  -41.552 10.921  1.00 106.96 ? 199 SER D CA    1 
ATOM   8062 C C     . SER D 1 227 ? -4.598  -41.497 9.422   1.00 109.24 ? 199 SER D C     1 
ATOM   8063 O O     . SER D 1 227 ? -3.772  -40.995 8.653   1.00 111.82 ? 199 SER D O     1 
ATOM   8064 C CB    . SER D 1 227 ? -4.457  -40.156 11.530  1.00 106.60 ? 199 SER D CB    1 
ATOM   8065 O OG    . SER D 1 227 ? -5.663  -39.528 11.133  1.00 107.24 ? 199 SER D OG    1 
ATOM   8066 N N     . GLU D 1 228 ? -5.752  -42.019 9.004   1.00 110.15 ? 200 GLU D N     1 
ATOM   8067 C CA    . GLU D 1 228 ? -6.153  -41.930 7.606   1.00 110.86 ? 200 GLU D CA    1 
ATOM   8068 C C     . GLU D 1 228 ? -6.636  -40.536 7.227   1.00 110.12 ? 200 GLU D C     1 
ATOM   8069 O O     . GLU D 1 228 ? -6.771  -40.248 6.033   1.00 111.62 ? 200 GLU D O     1 
ATOM   8070 C CB    . GLU D 1 228 ? -7.245  -42.958 7.304   1.00 112.98 ? 200 GLU D CB    1 
ATOM   8071 N N     . ASP D 1 229 ? -6.897  -39.675 8.208   1.00 108.19 ? 201 ASP D N     1 
ATOM   8072 C CA    . ASP D 1 229 ? -7.295  -38.289 7.952   1.00 107.64 ? 201 ASP D CA    1 
ATOM   8073 C C     . ASP D 1 229 ? -6.855  -37.438 9.131   1.00 103.57 ? 201 ASP D C     1 
ATOM   8074 O O     . ASP D 1 229 ? -7.633  -37.167 10.054  1.00 102.11 ? 201 ASP D O     1 
ATOM   8075 C CB    . ASP D 1 229 ? -8.803  -38.175 7.725   1.00 107.69 ? 201 ASP D CB    1 
ATOM   8076 C CG    . ASP D 1 229 ? -9.242  -36.754 7.425   1.00 107.22 ? 201 ASP D CG    1 
ATOM   8077 O OD1   . ASP D 1 229 ? -8.399  -35.951 6.970   1.00 105.55 ? 201 ASP D OD1   1 
ATOM   8078 O OD2   . ASP D 1 229 ? -10.430 -36.439 7.645   1.00 108.99 ? 201 ASP D OD2   1 
ATOM   8079 N N     . PRO D 1 230 ? -5.590  -37.005 9.142   1.00 101.20 ? 202 PRO D N     1 
ATOM   8080 C CA    . PRO D 1 230 ? -5.106  -36.209 10.283  1.00 94.10  ? 202 PRO D CA    1 
ATOM   8081 C C     . PRO D 1 230 ? -5.818  -34.876 10.438  1.00 88.53  ? 202 PRO D C     1 
ATOM   8082 O O     . PRO D 1 230 ? -6.039  -34.427 11.570  1.00 92.44  ? 202 PRO D O     1 
ATOM   8083 C CB    . PRO D 1 230 ? -3.613  -36.025 9.974   1.00 97.58  ? 202 PRO D CB    1 
ATOM   8084 C CG    . PRO D 1 230 ? -3.274  -37.101 8.995   1.00 100.91 ? 202 PRO D CG    1 
ATOM   8085 C CD    . PRO D 1 230 ? -4.514  -37.346 8.197   1.00 106.32 ? 202 PRO D CD    1 
ATOM   8086 N N     . VAL D 1 231 ? -6.181  -34.227 9.330   1.00 83.19  ? 203 VAL D N     1 
ATOM   8087 C CA    . VAL D 1 231 ? -6.879  -32.948 9.413   1.00 84.52  ? 203 VAL D CA    1 
ATOM   8088 C C     . VAL D 1 231 ? -8.256  -33.132 10.038  1.00 88.44  ? 203 VAL D C     1 
ATOM   8089 O O     . VAL D 1 231 ? -8.732  -32.274 10.793  1.00 88.99  ? 203 VAL D O     1 
ATOM   8090 C CB    . VAL D 1 231 ? -6.965  -32.297 8.020   1.00 86.49  ? 203 VAL D CB    1 
ATOM   8091 C CG1   . VAL D 1 231 ? -7.885  -31.084 8.041   1.00 75.13  ? 203 VAL D CG1   1 
ATOM   8092 C CG2   . VAL D 1 231 ? -5.581  -31.902 7.541   1.00 89.33  ? 203 VAL D CG2   1 
ATOM   8093 N N     . GLY D 1 232 ? -8.913  -34.256 9.749   1.00 92.75  ? 204 GLY D N     1 
ATOM   8094 C CA    . GLY D 1 232 ? -10.223 -34.501 10.330  1.00 96.17  ? 204 GLY D CA    1 
ATOM   8095 C C     . GLY D 1 232 ? -10.160 -34.746 11.827  1.00 99.55  ? 204 GLY D C     1 
ATOM   8096 O O     . GLY D 1 232 ? -10.951 -34.187 12.593  1.00 98.20  ? 204 GLY D O     1 
ATOM   8097 N N     . GLU D 1 233 ? -9.216  -35.583 12.264  1.00 97.78  ? 205 GLU D N     1 
ATOM   8098 C CA    . GLU D 1 233 ? -9.098  -35.886 13.687  1.00 93.74  ? 205 GLU D CA    1 
ATOM   8099 C C     . GLU D 1 233 ? -8.674  -34.660 14.485  1.00 92.04  ? 205 GLU D C     1 
ATOM   8100 O O     . GLU D 1 233 ? -9.147  -34.451 15.609  1.00 90.94  ? 205 GLU D O     1 
ATOM   8101 C CB    . GLU D 1 233 ? -8.109  -37.031 13.906  1.00 91.82  ? 205 GLU D CB    1 
ATOM   8102 C CG    . GLU D 1 233 ? -8.629  -38.397 13.495  1.00 102.63 ? 205 GLU D CG    1 
ATOM   8103 C CD    . GLU D 1 233 ? -7.700  -39.521 13.913  1.00 109.50 ? 205 GLU D CD    1 
ATOM   8104 O OE1   . GLU D 1 233 ? -6.853  -39.293 14.804  1.00 107.98 ? 205 GLU D OE1   1 
ATOM   8105 O OE2   . GLU D 1 233 ? -7.816  -40.632 13.354  1.00 107.07 ? 205 GLU D OE2   1 
ATOM   8106 N N     . PHE D 1 234 ? -7.785  -33.837 13.926  1.00 91.84  ? 206 PHE D N     1 
ATOM   8107 C CA    . PHE D 1 234 ? -7.320  -32.663 14.656  1.00 88.57  ? 206 PHE D CA    1 
ATOM   8108 C C     . PHE D 1 234 ? -8.380  -31.571 14.700  1.00 88.53  ? 206 PHE D C     1 
ATOM   8109 O O     . PHE D 1 234 ? -8.477  -30.846 15.697  1.00 93.42  ? 206 PHE D O     1 
ATOM   8110 C CB    . PHE D 1 234 ? -6.033  -32.125 14.034  1.00 86.54  ? 206 PHE D CB    1 
ATOM   8111 C CG    . PHE D 1 234 ? -5.279  -31.188 14.931  1.00 87.15  ? 206 PHE D CG    1 
ATOM   8112 C CD1   . PHE D 1 234 ? -4.852  -31.602 16.181  1.00 82.87  ? 206 PHE D CD1   1 
ATOM   8113 C CD2   . PHE D 1 234 ? -5.006  -29.890 14.530  1.00 86.81  ? 206 PHE D CD2   1 
ATOM   8114 C CE1   . PHE D 1 234 ? -4.161  -30.744 17.013  1.00 80.49  ? 206 PHE D CE1   1 
ATOM   8115 C CE2   . PHE D 1 234 ? -4.315  -29.026 15.359  1.00 78.71  ? 206 PHE D CE2   1 
ATOM   8116 C CZ    . PHE D 1 234 ? -3.893  -29.454 16.602  1.00 77.48  ? 206 PHE D CZ    1 
ATOM   8117 N N     . ARG D 1 235 ? -9.175  -31.430 13.637  1.00 88.32  ? 207 ARG D N     1 
ATOM   8118 C CA    . ARG D 1 235 ? -10.248 -30.442 13.649  1.00 91.53  ? 207 ARG D CA    1 
ATOM   8119 C C     . ARG D 1 235 ? -11.340 -30.830 14.639  1.00 96.56  ? 207 ARG D C     1 
ATOM   8120 O O     . ARG D 1 235 ? -11.935 -29.962 15.288  1.00 96.08  ? 207 ARG D O     1 
ATOM   8121 C CB    . ARG D 1 235 ? -10.830 -30.277 12.245  1.00 87.13  ? 207 ARG D CB    1 
ATOM   8122 N N     . LEU D 1 236 ? -11.613 -32.130 14.769  1.00 95.22  ? 208 LEU D N     1 
ATOM   8123 C CA    . LEU D 1 236 ? -12.616 -32.582 15.727  1.00 94.39  ? 208 LEU D CA    1 
ATOM   8124 C C     . LEU D 1 236 ? -12.103 -32.472 17.157  1.00 94.74  ? 208 LEU D C     1 
ATOM   8125 O O     . LEU D 1 236 ? -12.864 -32.129 18.069  1.00 93.24  ? 208 LEU D O     1 
ATOM   8126 C CB    . LEU D 1 236 ? -13.029 -34.020 15.414  1.00 94.62  ? 208 LEU D CB    1 
ATOM   8127 N N     . LEU D 1 237 ? -10.816 -32.758 17.372  1.00 93.55  ? 209 LEU D N     1 
ATOM   8128 C CA    . LEU D 1 237 ? -10.258 -32.699 18.720  1.00 87.13  ? 209 LEU D CA    1 
ATOM   8129 C C     . LEU D 1 237 ? -10.282 -31.278 19.267  1.00 85.25  ? 209 LEU D C     1 
ATOM   8130 O O     . LEU D 1 237 ? -10.546 -31.067 20.457  1.00 87.66  ? 209 LEU D O     1 
ATOM   8131 C CB    . LEU D 1 237 ? -8.833  -33.251 18.723  1.00 82.60  ? 209 LEU D CB    1 
ATOM   8132 C CG    . LEU D 1 237 ? -8.088  -33.178 20.057  1.00 77.97  ? 209 LEU D CG    1 
ATOM   8133 C CD1   . LEU D 1 237 ? -8.799  -34.015 21.108  1.00 79.26  ? 209 LEU D CD1   1 
ATOM   8134 C CD2   . LEU D 1 237 ? -6.644  -33.625 19.898  1.00 76.01  ? 209 LEU D CD2   1 
ATOM   8135 N N     . LEU D 1 238 ? -10.009 -30.289 18.415  1.00 82.14  ? 210 LEU D N     1 
ATOM   8136 C CA    . LEU D 1 238 ? -10.033 -28.900 18.863  1.00 87.22  ? 210 LEU D CA    1 
ATOM   8137 C C     . LEU D 1 238 ? -11.455 -28.447 19.168  1.00 91.68  ? 210 LEU D C     1 
ATOM   8138 O O     . LEU D 1 238 ? -11.717 -27.854 20.221  1.00 94.08  ? 210 LEU D O     1 
ATOM   8139 C CB    . LEU D 1 238 ? -9.389  -27.999 17.809  1.00 85.00  ? 210 LEU D CB    1 
ATOM   8140 C CG    . LEU D 1 238 ? -7.882  -28.168 17.604  1.00 79.81  ? 210 LEU D CG    1 
ATOM   8141 C CD1   . LEU D 1 238 ? -7.373  -27.214 16.536  1.00 73.00  ? 210 LEU D CD1   1 
ATOM   8142 C CD2   . LEU D 1 238 ? -7.135  -27.963 18.912  1.00 81.12  ? 210 LEU D CD2   1 
ATOM   8143 N N     . GLU D 1 239 ? -12.393 -28.727 18.258  1.00 90.20  ? 211 GLU D N     1 
ATOM   8144 C CA    . GLU D 1 239 ? -13.780 -28.326 18.473  1.00 88.19  ? 211 GLU D CA    1 
ATOM   8145 C C     . GLU D 1 239 ? -14.396 -29.041 19.669  1.00 92.76  ? 211 GLU D C     1 
ATOM   8146 O O     . GLU D 1 239 ? -15.244 -28.466 20.361  1.00 90.43  ? 211 GLU D O     1 
ATOM   8147 C CB    . GLU D 1 239 ? -14.605 -28.592 17.214  1.00 80.17  ? 211 GLU D CB    1 
ATOM   8148 N N     . SER D 1 240 ? -13.985 -30.283 19.932  1.00 94.91  ? 212 SER D N     1 
ATOM   8149 C CA    . SER D 1 240 ? -14.471 -31.011 21.099  1.00 94.32  ? 212 SER D CA    1 
ATOM   8150 C C     . SER D 1 240 ? -13.960 -30.434 22.411  1.00 93.82  ? 212 SER D C     1 
ATOM   8151 O O     . SER D 1 240 ? -14.344 -30.930 23.476  1.00 96.57  ? 212 SER D O     1 
ATOM   8152 C CB    . SER D 1 240 ? -14.082 -32.487 20.998  1.00 89.93  ? 212 SER D CB    1 
ATOM   8153 O OG    . SER D 1 240 ? -12.690 -32.664 21.200  1.00 86.28  ? 212 SER D OG    1 
ATOM   8154 N N     . GLU D 1 241 ? -13.106 -29.410 22.363  1.00 91.94  ? 213 GLU D N     1 
ATOM   8155 C CA    . GLU D 1 241 ? -12.615 -28.734 23.558  1.00 91.83  ? 213 GLU D CA    1 
ATOM   8156 C C     . GLU D 1 241 ? -13.021 -27.265 23.583  1.00 92.34  ? 213 GLU D C     1 
ATOM   8157 O O     . GLU D 1 241 ? -12.382 -26.458 24.265  1.00 93.34  ? 213 GLU D O     1 
ATOM   8158 C CB    . GLU D 1 241 ? -11.094 -28.870 23.661  1.00 88.24  ? 213 GLU D CB    1 
ATOM   8159 C CG    . GLU D 1 241 ? -10.612 -30.295 23.889  1.00 86.51  ? 213 GLU D CG    1 
ATOM   8160 C CD    . GLU D 1 241 ? -11.163 -30.904 25.164  1.00 92.29  ? 213 GLU D CD    1 
ATOM   8161 O OE1   . GLU D 1 241 ? -11.215 -30.194 26.191  1.00 92.68  ? 213 GLU D OE1   1 
ATOM   8162 O OE2   . GLU D 1 241 ? -11.544 -32.094 25.139  1.00 96.28  ? 213 GLU D OE2   1 
ATOM   8163 N N     . GLY D 1 242 ? -14.069 -26.901 22.846  1.00 91.86  ? 214 GLY D N     1 
ATOM   8164 C CA    . GLY D 1 242 ? -14.557 -25.537 22.852  1.00 93.91  ? 214 GLY D CA    1 
ATOM   8165 C C     . GLY D 1 242 ? -13.833 -24.583 21.932  1.00 95.88  ? 214 GLY D C     1 
ATOM   8166 O O     . GLY D 1 242 ? -13.866 -23.372 22.168  1.00 95.91  ? 214 GLY D O     1 
ATOM   8167 N N     . PHE D 1 243 ? -13.183 -25.085 20.888  1.00 95.96  ? 215 PHE D N     1 
ATOM   8168 C CA    . PHE D 1 243 ? -12.453 -24.247 19.950  1.00 96.44  ? 215 PHE D CA    1 
ATOM   8169 C C     . PHE D 1 243 ? -13.228 -24.086 18.648  1.00 91.29  ? 215 PHE D C     1 
ATOM   8170 O O     . PHE D 1 243 ? -14.060 -24.920 18.280  1.00 88.87  ? 215 PHE D O     1 
ATOM   8171 C CB    . PHE D 1 243 ? -11.068 -24.829 19.656  1.00 96.34  ? 215 PHE D CB    1 
ATOM   8172 C CG    . PHE D 1 243 ? -10.041 -24.515 20.705  1.00 97.16  ? 215 PHE D CG    1 
ATOM   8173 C CD1   . PHE D 1 243 ? -9.357  -23.311 20.683  1.00 93.30  ? 215 PHE D CD1   1 
ATOM   8174 C CD2   . PHE D 1 243 ? -9.752  -25.427 21.706  1.00 95.11  ? 215 PHE D CD2   1 
ATOM   8175 C CE1   . PHE D 1 243 ? -8.408  -23.019 21.645  1.00 90.59  ? 215 PHE D CE1   1 
ATOM   8176 C CE2   . PHE D 1 243 ? -8.805  -25.142 22.670  1.00 93.39  ? 215 PHE D CE2   1 
ATOM   8177 C CZ    . PHE D 1 243 ? -8.132  -23.936 22.639  1.00 90.36  ? 215 PHE D CZ    1 
ATOM   8178 N N     . GLN D 1 244 ? -12.937 -22.993 17.950  1.00 92.24  ? 216 GLN D N     1 
ATOM   8179 C CA    . GLN D 1 244 ? -13.495 -22.708 16.631  1.00 97.04  ? 216 GLN D CA    1 
ATOM   8180 C C     . GLN D 1 244 ? -12.354 -22.798 15.624  1.00 90.38  ? 216 GLN D C     1 
ATOM   8181 O O     . GLN D 1 244 ? -11.561 -21.862 15.486  1.00 89.74  ? 216 GLN D O     1 
ATOM   8182 C CB    . GLN D 1 244 ? -14.162 -21.336 16.600  1.00 100.79 ? 216 GLN D CB    1 
ATOM   8183 C CG    . GLN D 1 244 ? -14.739 -20.961 15.244  1.00 101.79 ? 216 GLN D CG    1 
ATOM   8184 C CD    . GLN D 1 244 ? -15.172 -19.510 15.177  1.00 103.41 ? 216 GLN D CD    1 
ATOM   8185 O OE1   . GLN D 1 244 ? -14.710 -18.676 15.955  1.00 103.14 ? 216 GLN D OE1   1 
ATOM   8186 N NE2   . GLN D 1 244 ? -16.061 -19.200 14.240  1.00 109.40 ? 216 GLN D NE2   1 
ATOM   8187 N N     . VAL D 1 245 ? -12.270 -23.930 14.926  1.00 89.51  ? 217 VAL D N     1 
ATOM   8188 C CA    . VAL D 1 245 ? -11.205 -24.161 13.956  1.00 90.79  ? 217 VAL D CA    1 
ATOM   8189 C C     . VAL D 1 245 ? -11.407 -23.241 12.760  1.00 90.68  ? 217 VAL D C     1 
ATOM   8190 O O     . VAL D 1 245 ? -12.272 -23.486 11.912  1.00 93.76  ? 217 VAL D O     1 
ATOM   8191 C CB    . VAL D 1 245 ? -11.158 -25.637 13.521  1.00 88.42  ? 217 VAL D CB    1 
ATOM   8192 C CG1   . VAL D 1 245 ? -10.080 -25.846 12.467  1.00 89.37  ? 217 VAL D CG1   1 
ATOM   8193 C CG2   . VAL D 1 245 ? -10.921 -26.537 14.723  1.00 84.83  ? 217 VAL D CG2   1 
ATOM   8194 N N     . LEU D 1 246 ? -10.609 -22.174 12.687  1.00 91.86  ? 218 LEU D N     1 
ATOM   8195 C CA    . LEU D 1 246 ? -10.741 -21.207 11.605  1.00 90.54  ? 218 LEU D CA    1 
ATOM   8196 C C     . LEU D 1 246 ? -10.059 -21.659 10.321  1.00 88.66  ? 218 LEU D C     1 
ATOM   8197 O O     . LEU D 1 246 ? -10.431 -21.186 9.242   1.00 100.22 ? 218 LEU D O     1 
ATOM   8198 C CB    . LEU D 1 246 ? -10.168 -19.853 12.033  1.00 90.77  ? 218 LEU D CB    1 
ATOM   8199 C CG    . LEU D 1 246 ? -10.775 -19.200 13.277  1.00 90.53  ? 218 LEU D CG    1 
ATOM   8200 C CD1   . LEU D 1 246 ? -10.087 -17.875 13.574  1.00 84.37  ? 218 LEU D CD1   1 
ATOM   8201 C CD2   . LEU D 1 246 ? -12.273 -19.003 13.109  1.00 92.79  ? 218 LEU D CD2   1 
ATOM   8202 N N     . ARG D 1 247 ? -9.082  -22.560 10.410  1.00 85.73  ? 219 ARG D N     1 
ATOM   8203 C CA    . ARG D 1 247 ? -8.314  -22.981 9.248   1.00 88.15  ? 219 ARG D CA    1 
ATOM   8204 C C     . ARG D 1 247 ? -7.479  -24.192 9.634   1.00 82.66  ? 219 ARG D C     1 
ATOM   8205 O O     . ARG D 1 247 ? -6.876  -24.211 10.709  1.00 82.43  ? 219 ARG D O     1 
ATOM   8206 C CB    . ARG D 1 247 ? -7.417  -21.841 8.747   1.00 86.31  ? 219 ARG D CB    1 
ATOM   8207 C CG    . ARG D 1 247 ? -6.717  -22.095 7.427   1.00 85.65  ? 219 ARG D CG    1 
ATOM   8208 C CD    . ARG D 1 247 ? -6.034  -20.821 6.962   1.00 87.17  ? 219 ARG D CD    1 
ATOM   8209 N NE    . ARG D 1 247 ? -5.211  -21.013 5.775   1.00 97.17  ? 219 ARG D NE    1 
ATOM   8210 C CZ    . ARG D 1 247 ? -5.053  -20.101 4.825   1.00 101.41 ? 219 ARG D CZ    1 
ATOM   8211 N NH1   . ARG D 1 247 ? -5.647  -18.921 4.894   1.00 101.97 ? 219 ARG D NH1   1 
ATOM   8212 N NH2   . ARG D 1 247 ? -4.278  -20.380 3.780   1.00 101.62 ? 219 ARG D NH2   1 
ATOM   8213 N N     . CYS D 1 248 ? -7.453  -25.197 8.761   1.00 79.55  ? 220 CYS D N     1 
ATOM   8214 C CA    . CYS D 1 248 ? -6.732  -26.434 9.045   1.00 82.52  ? 220 CYS D CA    1 
ATOM   8215 C C     . CYS D 1 248 ? -6.325  -27.085 7.733   1.00 87.93  ? 220 CYS D C     1 
ATOM   8216 O O     . CYS D 1 248 ? -7.187  -27.438 6.923   1.00 89.88  ? 220 CYS D O     1 
ATOM   8217 C CB    . CYS D 1 248 ? -7.588  -27.390 9.879   1.00 81.66  ? 220 CYS D CB    1 
ATOM   8218 S SG    . CYS D 1 248 ? -6.673  -28.769 10.605  1.00 93.86  ? 220 CYS D SG    1 
ATOM   8219 N N     . ASP D 1 249 ? -5.018  -27.251 7.530   1.00 86.33  ? 221 ASP D N     1 
ATOM   8220 C CA    . ASP D 1 249 ? -4.489  -27.821 6.300   1.00 83.79  ? 221 ASP D CA    1 
ATOM   8221 C C     . ASP D 1 249 ? -3.341  -28.765 6.627   1.00 79.45  ? 221 ASP D C     1 
ATOM   8222 O O     . ASP D 1 249 ? -2.755  -28.716 7.711   1.00 79.48  ? 221 ASP D O     1 
ATOM   8223 C CB    . ASP D 1 249 ? -4.010  -26.730 5.331   1.00 87.97  ? 221 ASP D CB    1 
ATOM   8224 C CG    . ASP D 1 249 ? -5.047  -25.646 5.114   1.00 92.57  ? 221 ASP D CG    1 
ATOM   8225 O OD1   . ASP D 1 249 ? -6.114  -25.947 4.539   1.00 92.78  ? 221 ASP D OD1   1 
ATOM   8226 O OD2   . ASP D 1 249 ? -4.796  -24.492 5.522   1.00 91.70  ? 221 ASP D OD2   1 
ATOM   8227 N N     . LEU D 1 250 ? -3.025  -29.631 5.664   1.00 79.45  ? 222 LEU D N     1 
ATOM   8228 C CA    . LEU D 1 250 ? -1.915  -30.567 5.766   1.00 79.77  ? 222 LEU D CA    1 
ATOM   8229 C C     . LEU D 1 250 ? -1.031  -30.425 4.537   1.00 82.50  ? 222 LEU D C     1 
ATOM   8230 O O     . LEU D 1 250 ? -1.530  -30.270 3.418   1.00 84.00  ? 222 LEU D O     1 
ATOM   8231 C CB    . LEU D 1 250 ? -2.414  -32.015 5.893   1.00 75.20  ? 222 LEU D CB    1 
ATOM   8232 C CG    . LEU D 1 250 ? -1.376  -33.140 5.887   1.00 81.06  ? 222 LEU D CG    1 
ATOM   8233 C CD1   . LEU D 1 250 ? -0.474  -33.058 7.107   1.00 84.37  ? 222 LEU D CD1   1 
ATOM   8234 C CD2   . LEU D 1 250 ? -2.060  -34.497 5.817   1.00 80.70  ? 222 LEU D CD2   1 
ATOM   8235 N N     . GLY D 1 251 ? 0.282   -30.474 4.748   1.00 83.72  ? 223 GLY D N     1 
ATOM   8236 C CA    . GLY D 1 251 ? 1.229   -30.346 3.667   1.00 83.07  ? 223 GLY D CA    1 
ATOM   8237 C C     . GLY D 1 251 ? 2.600   -30.878 4.027   1.00 85.72  ? 223 GLY D C     1 
ATOM   8238 O O     . GLY D 1 251 ? 2.967   -30.977 5.203   1.00 88.71  ? 223 GLY D O     1 
ATOM   8239 N N     . PRO D 1 252 ? 3.385   -31.238 3.016   1.00 79.76  ? 224 PRO D N     1 
ATOM   8240 C CA    . PRO D 1 252 ? 4.741   -31.729 3.270   1.00 76.64  ? 224 PRO D CA    1 
ATOM   8241 C C     . PRO D 1 252 ? 5.729   -30.591 3.468   1.00 75.74  ? 224 PRO D C     1 
ATOM   8242 O O     . PRO D 1 252 ? 5.542   -29.475 2.977   1.00 75.61  ? 224 PRO D O     1 
ATOM   8243 C CB    . PRO D 1 252 ? 5.063   -32.524 2.001   1.00 72.43  ? 224 PRO D CB    1 
ATOM   8244 C CG    . PRO D 1 252 ? 4.305   -31.802 0.934   1.00 77.24  ? 224 PRO D CG    1 
ATOM   8245 C CD    . PRO D 1 252 ? 3.038   -31.288 1.585   1.00 73.56  ? 224 PRO D CD    1 
ATOM   8246 N N     . GLN D 1 253 ? 6.797   -30.893 4.204   1.00 73.37  ? 225 GLN D N     1 
ATOM   8247 C CA    . GLN D 1 253 ? 7.827   -29.913 4.517   1.00 71.27  ? 225 GLN D CA    1 
ATOM   8248 C C     . GLN D 1 253 ? 9.203   -30.550 4.400   1.00 71.32  ? 225 GLN D C     1 
ATOM   8249 O O     . GLN D 1 253 ? 9.395   -31.710 4.776   1.00 69.73  ? 225 GLN D O     1 
ATOM   8250 C CB    . GLN D 1 253 ? 7.647   -29.337 5.929   1.00 72.42  ? 225 GLN D CB    1 
ATOM   8251 C CG    . GLN D 1 253 ? 6.364   -28.549 6.138   1.00 76.86  ? 225 GLN D CG    1 
ATOM   8252 C CD    . GLN D 1 253 ? 6.374   -27.210 5.426   1.00 80.79  ? 225 GLN D CD    1 
ATOM   8253 O OE1   . GLN D 1 253 ? 7.434   -26.644 5.157   1.00 80.91  ? 225 GLN D OE1   1 
ATOM   8254 N NE2   . GLN D 1 253 ? 5.189   -26.693 5.122   1.00 81.39  ? 225 GLN D NE2   1 
ATOM   8255 N N     . LYS D 1 254 ? 10.154  -29.782 3.875   1.00 67.50  ? 226 LYS D N     1 
ATOM   8256 C CA    . LYS D 1 254 ? 11.555  -30.174 3.818   1.00 63.73  ? 226 LYS D CA    1 
ATOM   8257 C C     . LYS D 1 254 ? 12.366  -29.324 4.788   1.00 54.97  ? 226 LYS D C     1 
ATOM   8258 O O     . LYS D 1 254 ? 12.078  -28.140 4.990   1.00 53.83  ? 226 LYS D O     1 
ATOM   8259 C CB    . LYS D 1 254 ? 12.123  -30.022 2.403   1.00 66.48  ? 226 LYS D CB    1 
ATOM   8260 C CG    . LYS D 1 254 ? 11.560  -30.990 1.375   1.00 61.44  ? 226 LYS D CG    1 
ATOM   8261 C CD    . LYS D 1 254 ? 12.268  -30.823 0.037   1.00 61.36  ? 226 LYS D CD    1 
ATOM   8262 C CE    . LYS D 1 254 ? 11.712  -31.760 -1.022  1.00 66.77  ? 226 LYS D CE    1 
ATOM   8263 N NZ    . LYS D 1 254 ? 12.439  -31.620 -2.315  1.00 54.20  ? 226 LYS D NZ    1 
ATOM   8264 N N     . VAL D 1 255 ? 13.382  -29.935 5.389   1.00 53.25  ? 227 VAL D N     1 
ATOM   8265 C CA    . VAL D 1 255 ? 14.275  -29.250 6.316   1.00 53.16  ? 227 VAL D CA    1 
ATOM   8266 C C     . VAL D 1 255 ? 15.670  -29.310 5.707   1.00 53.12  ? 227 VAL D C     1 
ATOM   8267 O O     . VAL D 1 255 ? 16.325  -30.360 5.730   1.00 54.34  ? 227 VAL D O     1 
ATOM   8268 C CB    . VAL D 1 255 ? 14.250  -29.872 7.718   1.00 50.55  ? 227 VAL D CB    1 
ATOM   8269 C CG1   . VAL D 1 255 ? 15.116  -29.062 8.668   1.00 48.49  ? 227 VAL D CG1   1 
ATOM   8270 C CG2   . VAL D 1 255 ? 12.822  -29.964 8.234   1.00 51.66  ? 227 VAL D CG2   1 
ATOM   8271 N N     . PHE D 1 256 ? 16.130  -28.187 5.165   1.00 49.00  ? 228 PHE D N     1 
ATOM   8272 C CA    . PHE D 1 256 ? 17.412  -28.138 4.478   1.00 49.26  ? 228 PHE D CA    1 
ATOM   8273 C C     . PHE D 1 256 ? 18.569  -28.082 5.469   1.00 49.38  ? 228 PHE D C     1 
ATOM   8274 O O     . PHE D 1 256 ? 18.458  -27.510 6.557   1.00 52.57  ? 228 PHE D O     1 
ATOM   8275 C CB    . PHE D 1 256 ? 17.466  -26.927 3.545   1.00 52.63  ? 228 PHE D CB    1 
ATOM   8276 C CG    . PHE D 1 256 ? 18.819  -26.684 2.941   1.00 53.04  ? 228 PHE D CG    1 
ATOM   8277 C CD1   . PHE D 1 256 ? 19.249  -27.422 1.853   1.00 55.02  ? 228 PHE D CD1   1 
ATOM   8278 C CD2   . PHE D 1 256 ? 19.661  -25.713 3.460   1.00 54.76  ? 228 PHE D CD2   1 
ATOM   8279 C CE1   . PHE D 1 256 ? 20.493  -27.201 1.297   1.00 56.81  ? 228 PHE D CE1   1 
ATOM   8280 C CE2   . PHE D 1 256 ? 20.906  -25.488 2.908   1.00 53.53  ? 228 PHE D CE2   1 
ATOM   8281 C CZ    . PHE D 1 256 ? 21.322  -26.232 1.824   1.00 54.61  ? 228 PHE D CZ    1 
ATOM   8282 N N     . PHE D 1 257 ? 19.691  -28.692 5.077   1.00 50.56  ? 229 PHE D N     1 
ATOM   8283 C CA    . PHE D 1 257 ? 20.937  -28.623 5.829   1.00 50.85  ? 229 PHE D CA    1 
ATOM   8284 C C     . PHE D 1 257 ? 22.066  -28.451 4.818   1.00 51.48  ? 229 PHE D C     1 
ATOM   8285 O O     . PHE D 1 257 ? 22.141  -29.217 3.840   1.00 53.76  ? 229 PHE D O     1 
ATOM   8286 C CB    . PHE D 1 257 ? 21.174  -29.865 6.692   1.00 52.04  ? 229 PHE D CB    1 
ATOM   8287 C CG    . PHE D 1 257 ? 20.163  -30.044 7.786   1.00 51.54  ? 229 PHE D CG    1 
ATOM   8288 C CD1   . PHE D 1 257 ? 18.996  -30.753 7.561   1.00 51.84  ? 229 PHE D CD1   1 
ATOM   8289 C CD2   . PHE D 1 257 ? 20.376  -29.494 9.039   1.00 50.83  ? 229 PHE D CD2   1 
ATOM   8290 C CE1   . PHE D 1 257 ? 18.065  -30.917 8.566   1.00 51.44  ? 229 PHE D CE1   1 
ATOM   8291 C CE2   . PHE D 1 257 ? 19.447  -29.653 10.049  1.00 50.43  ? 229 PHE D CE2   1 
ATOM   8292 C CZ    . PHE D 1 257 ? 18.290  -30.366 9.811   1.00 50.73  ? 229 PHE D CZ    1 
ATOM   8293 N N     . PRO D 1 258 ? 22.954  -27.472 5.016   1.00 50.90  ? 230 PRO D N     1 
ATOM   8294 C CA    . PRO D 1 258 ? 23.995  -27.231 4.003   1.00 52.86  ? 230 PRO D CA    1 
ATOM   8295 C C     . PRO D 1 258 ? 25.075  -28.297 3.978   1.00 55.66  ? 230 PRO D C     1 
ATOM   8296 O O     . PRO D 1 258 ? 25.500  -28.711 2.892   1.00 62.20  ? 230 PRO D O     1 
ATOM   8297 C CB    . PRO D 1 258 ? 24.553  -25.858 4.400   1.00 52.61  ? 230 PRO D CB    1 
ATOM   8298 C CG    . PRO D 1 258 ? 24.296  -25.759 5.866   1.00 50.48  ? 230 PRO D CG    1 
ATOM   8299 C CD    . PRO D 1 258 ? 23.018  -26.509 6.129   1.00 52.35  ? 230 PRO D CD    1 
ATOM   8300 N N     . THR D 1 259 ? 25.535  -28.754 5.137   1.00 53.61  ? 231 THR D N     1 
ATOM   8301 C CA    . THR D 1 259 ? 26.618  -29.722 5.216   1.00 57.20  ? 231 THR D CA    1 
ATOM   8302 C C     . THR D 1 259 ? 26.079  -31.114 5.532   1.00 62.10  ? 231 THR D C     1 
ATOM   8303 O O     . THR D 1 259 ? 24.927  -31.292 5.936   1.00 58.00  ? 231 THR D O     1 
ATOM   8304 C CB    . THR D 1 259 ? 27.643  -29.300 6.273   1.00 55.23  ? 231 THR D CB    1 
ATOM   8305 O OG1   . THR D 1 259 ? 27.094  -29.499 7.581   1.00 57.93  ? 231 THR D OG1   1 
ATOM   8306 C CG2   . THR D 1 259 ? 28.012  -27.836 6.100   1.00 54.05  ? 231 THR D CG2   1 
ATOM   8307 N N     . ALA D 1 260 ? 26.942  -32.115 5.336   1.00 65.35  ? 232 ALA D N     1 
ATOM   8308 C CA    . ALA D 1 260 ? 26.569  -33.487 5.659   1.00 59.21  ? 232 ALA D CA    1 
ATOM   8309 C C     . ALA D 1 260 ? 26.492  -33.705 7.163   1.00 61.61  ? 232 ALA D C     1 
ATOM   8310 O O     . ALA D 1 260 ? 25.673  -34.505 7.631   1.00 62.61  ? 232 ALA D O     1 
ATOM   8311 C CB    . ALA D 1 260 ? 27.563  -34.465 5.033   1.00 61.14  ? 232 ALA D CB    1 
ATOM   8312 N N     . GLU D 1 261 ? 27.330  -33.008 7.933   1.00 63.86  ? 233 GLU D N     1 
ATOM   8313 C CA    . GLU D 1 261 ? 27.313  -33.167 9.383   1.00 64.57  ? 233 GLU D CA    1 
ATOM   8314 C C     . GLU D 1 261 ? 26.038  -32.601 9.992   1.00 64.12  ? 233 GLU D C     1 
ATOM   8315 O O     . GLU D 1 261 ? 25.353  -33.283 10.763  1.00 65.70  ? 233 GLU D O     1 
ATOM   8316 C CB    . GLU D 1 261 ? 28.526  -32.485 10.008  1.00 64.75  ? 233 GLU D CB    1 
ATOM   8317 C CG    . GLU D 1 261 ? 28.567  -32.665 11.510  1.00 71.35  ? 233 GLU D CG    1 
ATOM   8318 C CD    . GLU D 1 261 ? 29.828  -32.131 12.138  1.00 80.11  ? 233 GLU D CD    1 
ATOM   8319 O OE1   . GLU D 1 261 ? 30.740  -31.734 11.388  1.00 81.70  ? 233 GLU D OE1   1 
ATOM   8320 O OE2   . GLU D 1 261 ? 29.899  -32.098 13.385  1.00 83.48  ? 233 GLU D OE2   1 
ATOM   8321 N N     . THR D 1 262 ? 25.716  -31.344 9.671   1.00 61.93  ? 234 THR D N     1 
ATOM   8322 C CA    . THR D 1 262 ? 24.568  -30.683 10.285  1.00 57.59  ? 234 THR D CA    1 
ATOM   8323 C C     . THR D 1 262 ? 23.285  -31.474 10.083  1.00 54.19  ? 234 THR D C     1 
ATOM   8324 O O     . THR D 1 262 ? 22.356  -31.370 10.892  1.00 55.70  ? 234 THR D O     1 
ATOM   8325 C CB    . THR D 1 262 ? 24.410  -29.270 9.722   1.00 52.57  ? 234 THR D CB    1 
ATOM   8326 O OG1   . THR D 1 262 ? 24.564  -29.303 8.298   1.00 55.40  ? 234 THR D OG1   1 
ATOM   8327 C CG2   . THR D 1 262 ? 25.456  -28.343 10.319  1.00 52.19  ? 234 THR D CG2   1 
ATOM   8328 N N     . HIS D 1 263 ? 23.216  -32.274 9.019   1.00 55.19  ? 235 HIS D N     1 
ATOM   8329 C CA    . HIS D 1 263 ? 22.072  -33.152 8.819   1.00 55.60  ? 235 HIS D CA    1 
ATOM   8330 C C     . HIS D 1 263 ? 22.057  -34.305 9.815   1.00 57.53  ? 235 HIS D C     1 
ATOM   8331 O O     . HIS D 1 263 ? 21.005  -34.921 10.017  1.00 63.25  ? 235 HIS D O     1 
ATOM   8332 C CB    . HIS D 1 263 ? 22.079  -33.681 7.383   1.00 56.50  ? 235 HIS D CB    1 
ATOM   8333 C CG    . HIS D 1 263 ? 20.993  -34.670 7.094   1.00 57.19  ? 235 HIS D CG    1 
ATOM   8334 N ND1   . HIS D 1 263 ? 19.658  -34.329 7.099   1.00 56.20  ? 235 HIS D ND1   1 
ATOM   8335 C CD2   . HIS D 1 263 ? 21.045  -35.988 6.789   1.00 58.86  ? 235 HIS D CD2   1 
ATOM   8336 C CE1   . HIS D 1 263 ? 18.934  -35.396 6.811   1.00 57.24  ? 235 HIS D CE1   1 
ATOM   8337 N NE2   . HIS D 1 263 ? 19.751  -36.416 6.619   1.00 58.85  ? 235 HIS D NE2   1 
ATOM   8338 N N     . ARG D 1 264 ? 23.190  -34.597 10.458  1.00 59.82  ? 236 ARG D N     1 
ATOM   8339 C CA    . ARG D 1 264 ? 23.304  -35.726 11.376  1.00 60.94  ? 236 ARG D CA    1 
ATOM   8340 C C     . ARG D 1 264 ? 23.242  -35.292 12.838  1.00 59.39  ? 236 ARG D C     1 
ATOM   8341 O O     . ARG D 1 264 ? 22.415  -35.801 13.601  1.00 61.71  ? 236 ARG D O     1 
ATOM   8342 C CB    . ARG D 1 264 ? 24.607  -36.490 11.110  1.00 66.76  ? 236 ARG D CB    1 
ATOM   8343 C CG    . ARG D 1 264 ? 25.132  -37.261 12.313  1.00 68.63  ? 236 ARG D CG    1 
ATOM   8344 C CD    . ARG D 1 264 ? 25.961  -38.458 11.877  1.00 66.59  ? 236 ARG D CD    1 
ATOM   8345 N NE    . ARG D 1 264 ? 26.992  -38.096 10.908  1.00 75.65  ? 236 ARG D NE    1 
ATOM   8346 C CZ    . ARG D 1 264 ? 27.990  -37.251 11.136  1.00 70.87  ? 236 ARG D CZ    1 
ATOM   8347 N NH1   . ARG D 1 264 ? 28.169  -36.689 12.321  1.00 66.03  ? 236 ARG D NH1   1 
ATOM   8348 N NH2   . ARG D 1 264 ? 28.839  -36.972 10.151  1.00 65.45  ? 236 ARG D NH2   1 
ATOM   8349 N N     . GLU D 1 265 ? 24.115  -34.362 13.246  1.00 58.71  ? 237 GLU D N     1 
ATOM   8350 C CA    . GLU D 1 265 ? 24.133  -33.926 14.640  1.00 59.36  ? 237 GLU D CA    1 
ATOM   8351 C C     . GLU D 1 265 ? 22.787  -33.356 15.064  1.00 60.46  ? 237 GLU D C     1 
ATOM   8352 O O     . GLU D 1 265 ? 22.445  -33.391 16.252  1.00 63.03  ? 237 GLU D O     1 
ATOM   8353 C CB    . GLU D 1 265 ? 25.238  -32.892 14.860  1.00 59.01  ? 237 GLU D CB    1 
ATOM   8354 C CG    . GLU D 1 265 ? 26.591  -33.283 14.293  1.00 68.85  ? 237 GLU D CG    1 
ATOM   8355 C CD    . GLU D 1 265 ? 27.416  -34.119 15.253  1.00 71.67  ? 237 GLU D CD    1 
ATOM   8356 O OE1   . GLU D 1 265 ? 27.414  -33.814 16.464  1.00 71.41  ? 237 GLU D OE1   1 
ATOM   8357 O OE2   . GLU D 1 265 ? 28.073  -35.079 14.795  1.00 67.78  ? 237 GLU D OE2   1 
ATOM   8358 N N     . PHE D 1 266 ? 22.016  -32.824 14.114  1.00 54.59  ? 238 PHE D N     1 
ATOM   8359 C CA    . PHE D 1 266 ? 20.629  -32.474 14.397  1.00 53.52  ? 238 PHE D CA    1 
ATOM   8360 C C     . PHE D 1 266 ? 19.803  -33.718 14.695  1.00 54.50  ? 238 PHE D C     1 
ATOM   8361 O O     . PHE D 1 266 ? 19.119  -33.792 15.723  1.00 57.53  ? 238 PHE D O     1 
ATOM   8362 C CB    . PHE D 1 266 ? 20.027  -31.707 13.223  1.00 52.49  ? 238 PHE D CB    1 
ATOM   8363 C CG    . PHE D 1 266 ? 18.638  -31.208 13.483  1.00 51.35  ? 238 PHE D CG    1 
ATOM   8364 C CD1   . PHE D 1 266 ? 18.415  -30.147 14.342  1.00 50.11  ? 238 PHE D CD1   1 
ATOM   8365 C CD2   . PHE D 1 266 ? 17.549  -31.820 12.884  1.00 51.63  ? 238 PHE D CD2   1 
ATOM   8366 C CE1   . PHE D 1 266 ? 17.133  -29.695 14.586  1.00 49.15  ? 238 PHE D CE1   1 
ATOM   8367 C CE2   . PHE D 1 266 ? 16.266  -31.374 13.124  1.00 50.68  ? 238 PHE D CE2   1 
ATOM   8368 C CZ    . PHE D 1 266 ? 16.057  -30.309 13.977  1.00 49.43  ? 238 PHE D CZ    1 
ATOM   8369 N N     . LEU D 1 267 ? 19.852  -34.708 13.798  1.00 55.69  ? 239 LEU D N     1 
ATOM   8370 C CA    . LEU D 1 267 ? 19.110  -35.947 14.006  1.00 56.80  ? 239 LEU D CA    1 
ATOM   8371 C C     . LEU D 1 267 ? 19.517  -36.651 15.293  1.00 58.79  ? 239 LEU D C     1 
ATOM   8372 O O     . LEU D 1 267 ? 18.727  -37.432 15.835  1.00 60.86  ? 239 LEU D O     1 
ATOM   8373 C CB    . LEU D 1 267 ? 19.302  -36.879 12.808  1.00 58.10  ? 239 LEU D CB    1 
ATOM   8374 C CG    . LEU D 1 267 ? 18.493  -36.531 11.556  1.00 57.51  ? 239 LEU D CG    1 
ATOM   8375 C CD1   . LEU D 1 267 ? 18.914  -37.395 10.378  1.00 58.91  ? 239 LEU D CD1   1 
ATOM   8376 C CD2   . LEU D 1 267 ? 17.003  -36.673 11.821  1.00 57.10  ? 239 LEU D CD2   1 
ATOM   8377 N N     . LYS D 1 268 ? 20.729  -36.394 15.792  1.00 59.86  ? 240 LYS D N     1 
ATOM   8378 C CA    . LYS D 1 268 ? 21.106  -36.891 17.110  1.00 58.70  ? 240 LYS D CA    1 
ATOM   8379 C C     . LYS D 1 268 ? 20.204  -36.313 18.194  1.00 59.74  ? 240 LYS D C     1 
ATOM   8380 O O     . LYS D 1 268 ? 19.827  -37.016 19.139  1.00 66.63  ? 240 LYS D O     1 
ATOM   8381 C CB    . LYS D 1 268 ? 22.567  -36.547 17.402  1.00 59.03  ? 240 LYS D CB    1 
ATOM   8382 C CG    . LYS D 1 268 ? 23.572  -37.573 16.918  1.00 64.55  ? 240 LYS D CG    1 
ATOM   8383 C CD    . LYS D 1 268 ? 24.975  -37.232 17.395  1.00 70.66  ? 240 LYS D CD    1 
ATOM   8384 C CE    . LYS D 1 268 ? 25.982  -38.282 16.955  1.00 74.22  ? 240 LYS D CE    1 
ATOM   8385 N NZ    . LYS D 1 268 ? 27.362  -37.935 17.393  1.00 78.93  ? 240 LYS D NZ    1 
ATOM   8386 N N     . SER D 1 269 ? 19.839  -35.034 18.067  1.00 56.85  ? 241 SER D N     1 
ATOM   8387 C CA    . SER D 1 269 ? 19.080  -34.358 19.115  1.00 54.94  ? 241 SER D CA    1 
ATOM   8388 C C     . SER D 1 269 ? 17.616  -34.784 19.129  1.00 54.83  ? 241 SER D C     1 
ATOM   8389 O O     . SER D 1 269 ? 17.050  -35.022 20.202  1.00 64.35  ? 241 SER D O     1 
ATOM   8390 C CB    . SER D 1 269 ? 19.188  -32.843 18.941  1.00 53.32  ? 241 SER D CB    1 
ATOM   8391 O OG    . SER D 1 269 ? 18.313  -32.384 17.926  1.00 52.41  ? 241 SER D OG    1 
ATOM   8392 N N     . VAL D 1 270 ? 16.988  -34.889 17.958  1.00 54.67  ? 242 VAL D N     1 
ATOM   8393 C CA    . VAL D 1 270 ? 15.560  -35.185 17.877  1.00 54.94  ? 242 VAL D CA    1 
ATOM   8394 C C     . VAL D 1 270 ? 15.312  -36.677 18.058  1.00 61.74  ? 242 VAL D C     1 
ATOM   8395 O O     . VAL D 1 270 ? 14.178  -37.150 17.912  1.00 60.12  ? 242 VAL D O     1 
ATOM   8396 C CB    . VAL D 1 270 ? 14.963  -34.688 16.548  1.00 53.76  ? 242 VAL D CB    1 
ATOM   8397 C CG1   . VAL D 1 270 ? 15.254  -33.209 16.358  1.00 52.19  ? 242 VAL D CG1   1 
ATOM   8398 C CG2   . VAL D 1 270 ? 15.510  -35.498 15.383  1.00 54.89  ? 242 VAL D CG2   1 
ATOM   8399 N N     . CYS D 1 271 ? 16.363  -37.428 18.376  1.00 66.51  ? 243 CYS D N     1 
ATOM   8400 C CA    . CYS D 1 271 ? 16.223  -38.846 18.689  1.00 71.82  ? 243 CYS D CA    1 
ATOM   8401 C C     . CYS D 1 271 ? 15.819  -38.974 20.152  1.00 73.82  ? 243 CYS D C     1 
ATOM   8402 O O     . CYS D 1 271 ? 16.621  -38.706 21.053  1.00 70.79  ? 243 CYS D O     1 
ATOM   8403 C CB    . CYS D 1 271 ? 17.521  -39.593 18.398  1.00 74.51  ? 243 CYS D CB    1 
ATOM   8404 S SG    . CYS D 1 271 ? 17.399  -41.386 18.593  1.00 89.42  ? 243 CYS D SG    1 
ATOM   8405 N N     . ALA D 1 272 ? 14.574  -39.387 20.391  1.00 78.02  ? 244 ALA D N     1 
ATOM   8406 C CA    . ALA D 1 272 ? 13.999  -39.358 21.729  1.00 72.06  ? 244 ALA D CA    1 
ATOM   8407 C C     . ALA D 1 272 ? 14.411  -40.539 22.600  1.00 79.52  ? 244 ALA D C     1 
ATOM   8408 O O     . ALA D 1 272 ? 14.200  -40.483 23.814  1.00 83.56  ? 244 ALA D O     1 
ATOM   8409 C CB    . ALA D 1 272 ? 12.472  -39.305 21.640  1.00 72.63  ? 244 ALA D CB    1 
ATOM   8410 N N     . PHE D 1 273 ? 14.984  -41.597 22.028  1.00 84.39  ? 245 PHE D N     1 
ATOM   8411 C CA    . PHE D 1 273 ? 15.330  -42.784 22.802  1.00 81.32  ? 245 PHE D CA    1 
ATOM   8412 C C     . PHE D 1 273 ? 16.778  -42.807 23.275  1.00 79.36  ? 245 PHE D C     1 
ATOM   8413 O O     . PHE D 1 273 ? 17.143  -43.704 24.042  1.00 76.56  ? 245 PHE D O     1 
ATOM   8414 C CB    . PHE D 1 273 ? 15.066  -44.051 21.983  1.00 77.14  ? 245 PHE D CB    1 
ATOM   8415 C CG    . PHE D 1 273 ? 13.624  -44.465 21.940  1.00 80.02  ? 245 PHE D CG    1 
ATOM   8416 C CD1   . PHE D 1 273 ? 13.079  -45.225 22.962  1.00 81.15  ? 245 PHE D CD1   1 
ATOM   8417 C CD2   . PHE D 1 273 ? 12.819  -44.112 20.870  1.00 80.68  ? 245 PHE D CD2   1 
ATOM   8418 C CE1   . PHE D 1 273 ? 11.754  -45.616 22.923  1.00 84.69  ? 245 PHE D CE1   1 
ATOM   8419 C CE2   . PHE D 1 273 ? 11.494  -44.500 20.825  1.00 82.15  ? 245 PHE D CE2   1 
ATOM   8420 C CZ    . PHE D 1 273 ? 10.961  -45.254 21.853  1.00 86.16  ? 245 PHE D CZ    1 
ATOM   8421 N N     . LEU D 1 274 ? 17.608  -41.854 22.844  1.00 81.53  ? 246 LEU D N     1 
ATOM   8422 C CA    . LEU D 1 274 ? 19.036  -41.930 23.136  1.00 81.80  ? 246 LEU D CA    1 
ATOM   8423 C C     . LEU D 1 274 ? 19.353  -41.730 24.612  1.00 83.40  ? 246 LEU D C     1 
ATOM   8424 O O     . LEU D 1 274 ? 20.412  -42.175 25.067  1.00 87.74  ? 246 LEU D O     1 
ATOM   8425 C CB    . LEU D 1 274 ? 19.801  -40.907 22.298  1.00 79.17  ? 246 LEU D CB    1 
ATOM   8426 C CG    . LEU D 1 274 ? 20.137  -41.368 20.879  1.00 79.23  ? 246 LEU D CG    1 
ATOM   8427 C CD1   . LEU D 1 274 ? 20.820  -40.261 20.092  1.00 76.52  ? 246 LEU D CD1   1 
ATOM   8428 C CD2   . LEU D 1 274 ? 20.997  -42.623 20.912  1.00 90.91  ? 246 LEU D CD2   1 
ATOM   8429 N N     . TYR D 1 275 ? 18.472  -41.076 25.370  1.00 82.25  ? 247 TYR D N     1 
ATOM   8430 C CA    . TYR D 1 275 ? 18.721  -40.903 26.796  1.00 84.38  ? 247 TYR D CA    1 
ATOM   8431 C C     . TYR D 1 275 ? 18.586  -42.209 27.572  1.00 85.56  ? 247 TYR D C     1 
ATOM   8432 O O     . TYR D 1 275 ? 19.127  -42.314 28.678  1.00 80.50  ? 247 TYR D O     1 
ATOM   8433 C CB    . TYR D 1 275 ? 17.782  -39.836 27.369  1.00 79.88  ? 247 TYR D CB    1 
ATOM   8434 C CG    . TYR D 1 275 ? 16.367  -40.315 27.602  1.00 78.87  ? 247 TYR D CG    1 
ATOM   8435 C CD1   . TYR D 1 275 ? 15.406  -40.208 26.608  1.00 78.58  ? 247 TYR D CD1   1 
ATOM   8436 C CD2   . TYR D 1 275 ? 15.995  -40.880 28.811  1.00 84.35  ? 247 TYR D CD2   1 
ATOM   8437 C CE1   . TYR D 1 275 ? 14.112  -40.649 26.817  1.00 77.76  ? 247 TYR D CE1   1 
ATOM   8438 C CE2   . TYR D 1 275 ? 14.714  -41.328 29.020  1.00 86.81  ? 247 TYR D CE2   1 
ATOM   8439 C CZ    . TYR D 1 275 ? 13.775  -41.208 28.027  1.00 83.46  ? 247 TYR D CZ    1 
ATOM   8440 O OH    . TYR D 1 275 ? 12.498  -41.658 28.256  1.00 88.12  ? 247 TYR D OH    1 
ATOM   8441 N N     . ARG D 1 276 ? 17.881  -43.199 27.023  1.00 86.42  ? 248 ARG D N     1 
ATOM   8442 C CA    . ARG D 1 276 ? 17.729  -44.492 27.680  1.00 88.82  ? 248 ARG D CA    1 
ATOM   8443 C C     . ARG D 1 276 ? 18.874  -45.451 27.393  1.00 97.04  ? 248 ARG D C     1 
ATOM   8444 O O     . ARG D 1 276 ? 19.116  -46.362 28.194  1.00 102.59 ? 248 ARG D O     1 
ATOM   8445 C CB    . ARG D 1 276 ? 16.416  -45.159 27.255  1.00 89.48  ? 248 ARG D CB    1 
ATOM   8446 C CG    . ARG D 1 276 ? 15.165  -44.438 27.709  1.00 87.00  ? 248 ARG D CG    1 
ATOM   8447 C CD    . ARG D 1 276 ? 13.909  -45.180 27.282  1.00 84.16  ? 248 ARG D CD    1 
ATOM   8448 N NE    . ARG D 1 276 ? 12.700  -44.498 27.726  1.00 85.85  ? 248 ARG D NE    1 
ATOM   8449 C CZ    . ARG D 1 276 ? 11.471  -44.972 27.569  1.00 90.08  ? 248 ARG D CZ    1 
ATOM   8450 N NH1   . ARG D 1 276 ? 11.249  -46.130 26.970  1.00 97.81  ? 248 ARG D NH1   1 
ATOM   8451 N NH2   . ARG D 1 276 ? 10.441  -44.267 28.027  1.00 89.62  ? 248 ARG D NH2   1 
ATOM   8452 N N     . ILE D 1 277 ? 19.579  -45.271 26.281  1.00 94.43  ? 249 ILE D N     1 
ATOM   8453 C CA    . ILE D 1 277 ? 20.586  -46.231 25.838  1.00 94.81  ? 249 ILE D CA    1 
ATOM   8454 C C     . ILE D 1 277 ? 21.918  -45.941 26.518  1.00 95.59  ? 249 ILE D C     1 
ATOM   8455 O O     . ILE D 1 277 ? 22.380  -44.790 26.509  1.00 88.44  ? 249 ILE D O     1 
ATOM   8456 C CB    . ILE D 1 277 ? 20.736  -46.205 24.310  1.00 92.13  ? 249 ILE D CB    1 
ATOM   8457 C CG1   . ILE D 1 277 ? 19.370  -46.344 23.636  1.00 90.03  ? 249 ILE D CG1   1 
ATOM   8458 C CG2   . ILE D 1 277 ? 21.665  -47.312 23.852  1.00 103.44 ? 249 ILE D CG2   1 
ATOM   8459 C CD1   . ILE D 1 277 ? 18.639  -47.619 23.994  1.00 99.48  ? 249 ILE D CD1   1 
ATOM   8460 N N     . PRO D 1 278 ? 22.564  -46.938 27.121  1.00 100.28 ? 250 PRO D N     1 
ATOM   8461 C CA    . PRO D 1 278 ? 23.932  -46.743 27.617  1.00 95.01  ? 250 PRO D CA    1 
ATOM   8462 C C     . PRO D 1 278 ? 24.888  -46.426 26.475  1.00 103.42 ? 250 PRO D C     1 
ATOM   8463 O O     . PRO D 1 278 ? 24.543  -46.484 25.293  1.00 108.11 ? 250 PRO D O     1 
ATOM   8464 C CB    . PRO D 1 278 ? 24.269  -48.080 28.287  1.00 95.97  ? 250 PRO D CB    1 
ATOM   8465 C CG    . PRO D 1 278 ? 22.941  -48.701 28.592  1.00 94.23  ? 250 PRO D CG    1 
ATOM   8466 C CD    . PRO D 1 278 ? 22.016  -48.251 27.501  1.00 100.08 ? 250 PRO D CD    1 
ATOM   8467 N N     . GLU D 1 279 ? 26.125  -46.094 26.850  1.00 103.22 ? 251 GLU D N     1 
ATOM   8468 C CA    . GLU D 1 279 ? 27.065  -45.540 25.879  1.00 104.50 ? 251 GLU D CA    1 
ATOM   8469 C C     . GLU D 1 279 ? 27.471  -46.566 24.826  1.00 101.88 ? 251 GLU D C     1 
ATOM   8470 O O     . GLU D 1 279 ? 27.610  -46.224 23.645  1.00 105.49 ? 251 GLU D O     1 
ATOM   8471 C CB    . GLU D 1 279 ? 28.300  -44.995 26.597  1.00 100.21 ? 251 GLU D CB    1 
ATOM   8472 C CG    . GLU D 1 279 ? 29.310  -44.350 25.663  1.00 109.67 ? 251 GLU D CG    1 
ATOM   8473 C CD    . GLU D 1 279 ? 28.712  -43.215 24.852  1.00 119.24 ? 251 GLU D CD    1 
ATOM   8474 O OE1   . GLU D 1 279 ? 27.830  -42.502 25.378  1.00 116.37 ? 251 GLU D OE1   1 
ATOM   8475 O OE2   . GLU D 1 279 ? 29.117  -43.043 23.682  1.00 121.35 ? 251 GLU D OE2   1 
ATOM   8476 N N     . GLU D 1 280 ? 27.663  -47.825 25.229  1.00 100.15 ? 252 GLU D N     1 
ATOM   8477 C CA    . GLU D 1 280 ? 28.189  -48.827 24.305  1.00 108.05 ? 252 GLU D CA    1 
ATOM   8478 C C     . GLU D 1 280 ? 27.241  -49.087 23.141  1.00 112.40 ? 252 GLU D C     1 
ATOM   8479 O O     . GLU D 1 280 ? 27.691  -49.437 22.043  1.00 117.97 ? 252 GLU D O     1 
ATOM   8480 C CB    . GLU D 1 280 ? 28.477  -50.129 25.052  1.00 109.04 ? 252 GLU D CB    1 
ATOM   8481 N N     . GLN D 1 281 ? 25.937  -48.924 23.353  1.00 105.36 ? 253 GLN D N     1 
ATOM   8482 C CA    . GLN D 1 281 ? 24.948  -49.153 22.309  1.00 109.35 ? 253 GLN D CA    1 
ATOM   8483 C C     . GLN D 1 281 ? 24.374  -47.864 21.739  1.00 113.39 ? 253 GLN D C     1 
ATOM   8484 O O     . GLN D 1 281 ? 23.546  -47.925 20.823  1.00 111.21 ? 253 GLN D O     1 
ATOM   8485 C CB    . GLN D 1 281 ? 23.812  -50.034 22.842  1.00 95.26  ? 253 GLN D CB    1 
ATOM   8486 N N     . LYS D 1 282 ? 24.788  -46.702 22.250  1.00 113.51 ? 254 LYS D N     1 
ATOM   8487 C CA    . LYS D 1 282 ? 24.264  -45.439 21.740  1.00 104.42 ? 254 LYS D CA    1 
ATOM   8488 C C     . LYS D 1 282 ? 24.687  -45.217 20.293  1.00 104.16 ? 254 LYS D C     1 
ATOM   8489 O O     . LYS D 1 282 ? 23.862  -44.875 19.437  1.00 104.87 ? 254 LYS D O     1 
ATOM   8490 C CB    . LYS D 1 282 ? 24.733  -44.282 22.624  1.00 97.33  ? 254 LYS D CB    1 
ATOM   8491 N N     . ASP D 1 283 ? 25.975  -45.417 20.000  1.00 107.99 ? 255 ASP D N     1 
ATOM   8492 C CA    . ASP D 1 283 ? 26.463  -45.225 18.639  1.00 108.36 ? 255 ASP D CA    1 
ATOM   8493 C C     . ASP D 1 283 ? 25.865  -46.244 17.678  1.00 102.47 ? 255 ASP D C     1 
ATOM   8494 O O     . ASP D 1 283 ? 25.639  -45.929 16.504  1.00 98.35  ? 255 ASP D O     1 
ATOM   8495 C CB    . ASP D 1 283 ? 27.989  -45.302 18.616  1.00 109.67 ? 255 ASP D CB    1 
ATOM   8496 C CG    . ASP D 1 283 ? 28.634  -44.305 19.557  1.00 115.49 ? 255 ASP D CG    1 
ATOM   8497 O OD1   . ASP D 1 283 ? 27.962  -43.318 19.925  1.00 119.13 ? 255 ASP D OD1   1 
ATOM   8498 O OD2   . ASP D 1 283 ? 29.809  -44.507 19.928  1.00 116.23 ? 255 ASP D OD2   1 
ATOM   8499 N N     . ASP D 1 284 ? 25.607  -47.465 18.151  1.00 103.90 ? 256 ASP D N     1 
ATOM   8500 C CA    . ASP D 1 284 ? 24.933  -48.456 17.322  1.00 104.98 ? 256 ASP D CA    1 
ATOM   8501 C C     . ASP D 1 284 ? 23.444  -48.166 17.195  1.00 101.92 ? 256 ASP D C     1 
ATOM   8502 O O     . ASP D 1 284 ? 22.839  -48.492 16.168  1.00 96.77  ? 256 ASP D O     1 
ATOM   8503 C CB    . ASP D 1 284 ? 25.148  -49.858 17.893  1.00 99.98  ? 256 ASP D CB    1 
ATOM   8504 N N     . PHE D 1 285 ? 22.841  -47.563 18.224  1.00 101.10 ? 257 PHE D N     1 
ATOM   8505 C CA    . PHE D 1 285 ? 21.436  -47.180 18.141  1.00 101.10 ? 257 PHE D CA    1 
ATOM   8506 C C     . PHE D 1 285 ? 21.224  -46.122 17.065  1.00 102.77 ? 257 PHE D C     1 
ATOM   8507 O O     . PHE D 1 285 ? 20.234  -46.166 16.325  1.00 98.18  ? 257 PHE D O     1 
ATOM   8508 C CB    . PHE D 1 285 ? 20.955  -46.673 19.505  1.00 98.23  ? 257 PHE D CB    1 
ATOM   8509 C CG    . PHE D 1 285 ? 19.469  -46.446 19.590  1.00 97.84  ? 257 PHE D CG    1 
ATOM   8510 C CD1   . PHE D 1 285 ? 18.888  -45.307 19.055  1.00 99.75  ? 257 PHE D CD1   1 
ATOM   8511 C CD2   . PHE D 1 285 ? 18.654  -47.374 20.217  1.00 99.20  ? 257 PHE D CD2   1 
ATOM   8512 C CE1   . PHE D 1 285 ? 17.525  -45.103 19.138  1.00 101.38 ? 257 PHE D CE1   1 
ATOM   8513 C CE2   . PHE D 1 285 ? 17.290  -47.174 20.303  1.00 97.94  ? 257 PHE D CE2   1 
ATOM   8514 C CZ    . PHE D 1 285 ? 16.726  -46.039 19.762  1.00 100.31 ? 257 PHE D CZ    1 
ATOM   8515 N N     . PHE D 1 286 ? 22.150  -45.167 16.960  1.00 103.32 ? 258 PHE D N     1 
ATOM   8516 C CA    . PHE D 1 286 ? 21.996  -44.083 15.996  1.00 96.24  ? 258 PHE D CA    1 
ATOM   8517 C C     . PHE D 1 286 ? 22.153  -44.585 14.566  1.00 95.60  ? 258 PHE D C     1 
ATOM   8518 O O     . PHE D 1 286 ? 21.332  -44.272 13.696  1.00 92.26  ? 258 PHE D O     1 
ATOM   8519 C CB    . PHE D 1 286 ? 23.005  -42.974 16.291  1.00 86.95  ? 258 PHE D CB    1 
ATOM   8520 C CG    . PHE D 1 286 ? 22.712  -41.689 15.576  1.00 85.87  ? 258 PHE D CG    1 
ATOM   8521 C CD1   . PHE D 1 286 ? 21.425  -41.180 15.538  1.00 82.98  ? 258 PHE D CD1   1 
ATOM   8522 C CD2   . PHE D 1 286 ? 23.722  -40.994 14.933  1.00 86.97  ? 258 PHE D CD2   1 
ATOM   8523 C CE1   . PHE D 1 286 ? 21.151  -39.997 14.878  1.00 78.28  ? 258 PHE D CE1   1 
ATOM   8524 C CE2   . PHE D 1 286 ? 23.456  -39.813 14.270  1.00 82.76  ? 258 PHE D CE2   1 
ATOM   8525 C CZ    . PHE D 1 286 ? 22.168  -39.313 14.241  1.00 77.38  ? 258 PHE D CZ    1 
ATOM   8526 N N     . ASP D 1 287 ? 23.207  -45.362 14.302  1.00 100.54 ? 259 ASP D N     1 
ATOM   8527 C CA    . ASP D 1 287 ? 23.418  -45.885 12.956  1.00 102.42 ? 259 ASP D CA    1 
ATOM   8528 C C     . ASP D 1 287 ? 22.282  -46.809 12.540  1.00 102.09 ? 259 ASP D C     1 
ATOM   8529 O O     . ASP D 1 287 ? 21.857  -46.800 11.378  1.00 99.09  ? 259 ASP D O     1 
ATOM   8530 C CB    . ASP D 1 287 ? 24.761  -46.610 12.877  1.00 104.98 ? 259 ASP D CB    1 
ATOM   8531 C CG    . ASP D 1 287 ? 25.941  -45.660 12.937  1.00 104.57 ? 259 ASP D CG    1 
ATOM   8532 O OD1   . ASP D 1 287 ? 26.004  -44.846 13.882  1.00 105.20 ? 259 ASP D OD1   1 
ATOM   8533 O OD2   . ASP D 1 287 ? 26.805  -45.724 12.037  1.00 102.59 ? 259 ASP D OD2   1 
ATOM   8534 N N     . ASP D 1 288 ? 21.776  -47.616 13.476  1.00 102.34 ? 260 ASP D N     1 
ATOM   8535 C CA    . ASP D 1 288 ? 20.602  -48.433 13.189  1.00 103.53 ? 260 ASP D CA    1 
ATOM   8536 C C     . ASP D 1 288 ? 19.390  -47.558 12.898  1.00 100.79 ? 260 ASP D C     1 
ATOM   8537 O O     . ASP D 1 288 ? 18.566  -47.888 12.037  1.00 99.77  ? 260 ASP D O     1 
ATOM   8538 C CB    . ASP D 1 288 ? 20.320  -49.374 14.361  1.00 104.24 ? 260 ASP D CB    1 
ATOM   8539 C CG    . ASP D 1 288 ? 19.450  -50.550 13.968  1.00 107.92 ? 260 ASP D CG    1 
ATOM   8540 O OD1   . ASP D 1 288 ? 19.548  -51.004 12.808  1.00 108.64 ? 260 ASP D OD1   1 
ATOM   8541 O OD2   . ASP D 1 288 ? 18.667  -51.021 14.819  1.00 107.46 ? 260 ASP D OD2   1 
ATOM   8542 N N     . TRP D 1 289 ? 19.269  -46.433 13.606  1.00 97.32  ? 261 TRP D N     1 
ATOM   8543 C CA    . TRP D 1 289 ? 18.200  -45.483 13.321  1.00 96.33  ? 261 TRP D CA    1 
ATOM   8544 C C     . TRP D 1 289 ? 18.427  -44.790 11.983  1.00 98.53  ? 261 TRP D C     1 
ATOM   8545 O O     . TRP D 1 289 ? 17.505  -44.675 11.167  1.00 100.71 ? 261 TRP D O     1 
ATOM   8546 C CB    . TRP D 1 289 ? 18.100  -44.456 14.449  1.00 95.23  ? 261 TRP D CB    1 
ATOM   8547 C CG    . TRP D 1 289 ? 16.827  -43.665 14.443  1.00 93.23  ? 261 TRP D CG    1 
ATOM   8548 C CD1   . TRP D 1 289 ? 15.558  -44.150 14.323  1.00 94.07  ? 261 TRP D CD1   1 
ATOM   8549 C CD2   . TRP D 1 289 ? 16.704  -42.243 14.560  1.00 86.37  ? 261 TRP D CD2   1 
ATOM   8550 N NE1   . TRP D 1 289 ? 14.651  -43.117 14.360  1.00 90.56  ? 261 TRP D NE1   1 
ATOM   8551 C CE2   . TRP D 1 289 ? 15.331  -41.936 14.504  1.00 86.56  ? 261 TRP D CE2   1 
ATOM   8552 C CE3   . TRP D 1 289 ? 17.623  -41.199 14.707  1.00 81.03  ? 261 TRP D CE3   1 
ATOM   8553 C CZ2   . TRP D 1 289 ? 14.854  -40.631 14.592  1.00 84.41  ? 261 TRP D CZ2   1 
ATOM   8554 C CZ3   . TRP D 1 289 ? 17.148  -39.905 14.791  1.00 77.61  ? 261 TRP D CZ3   1 
ATOM   8555 C CH2   . TRP D 1 289 ? 15.776  -39.631 14.733  1.00 80.82  ? 261 TRP D CH2   1 
ATOM   8556 N N     . LEU D 1 290 ? 19.655  -44.325 11.739  1.00 99.10  ? 262 LEU D N     1 
ATOM   8557 C CA    . LEU D 1 290 ? 19.943  -43.592 10.509  1.00 93.03  ? 262 LEU D CA    1 
ATOM   8558 C C     . LEU D 1 290 ? 19.767  -44.474 9.279   1.00 96.76  ? 262 LEU D C     1 
ATOM   8559 O O     . LEU D 1 290 ? 19.270  -44.014 8.244   1.00 99.54  ? 262 LEU D O     1 
ATOM   8560 C CB    . LEU D 1 290 ? 21.361  -43.022 10.557  1.00 86.53  ? 262 LEU D CB    1 
ATOM   8561 C CG    . LEU D 1 290 ? 21.606  -41.820 11.470  1.00 76.04  ? 262 LEU D CG    1 
ATOM   8562 C CD1   . LEU D 1 290 ? 22.857  -41.075 11.034  1.00 65.32  ? 262 LEU D CD1   1 
ATOM   8563 C CD2   . LEU D 1 290 ? 20.401  -40.892 11.477  1.00 79.31  ? 262 LEU D CD2   1 
ATOM   8564 N N     . GLN D 1 291 ? 20.173  -45.743 9.370   1.00 94.84  ? 263 GLN D N     1 
ATOM   8565 C CA    . GLN D 1 291 ? 20.055  -46.639 8.224   1.00 99.80  ? 263 GLN D CA    1 
ATOM   8566 C C     . GLN D 1 291 ? 18.595  -46.874 7.856   1.00 103.88 ? 263 GLN D C     1 
ATOM   8567 O O     . GLN D 1 291 ? 18.239  -46.883 6.671   1.00 107.50 ? 263 GLN D O     1 
ATOM   8568 C CB    . GLN D 1 291 ? 20.754  -47.965 8.520   1.00 99.10  ? 263 GLN D CB    1 
ATOM   8569 N N     . ARG D 1 292 ? 17.734  -47.059 8.858   1.00 99.66  ? 264 ARG D N     1 
ATOM   8570 C CA    . ARG D 1 292 ? 16.320  -47.296 8.596   1.00 100.62 ? 264 ARG D CA    1 
ATOM   8571 C C     . ARG D 1 292 ? 15.617  -46.064 8.041   1.00 98.04  ? 264 ARG D C     1 
ATOM   8572 O O     . ARG D 1 292 ? 14.524  -46.190 7.479   1.00 95.79  ? 264 ARG D O     1 
ATOM   8573 C CB    . ARG D 1 292 ? 15.620  -47.754 9.876   1.00 99.49  ? 264 ARG D CB    1 
ATOM   8574 C CG    . ARG D 1 292 ? 14.574  -48.835 9.665   1.00 98.19  ? 264 ARG D CG    1 
ATOM   8575 C CD    . ARG D 1 292 ? 14.367  -49.650 10.932  1.00 96.71  ? 264 ARG D CD    1 
ATOM   8576 N NE    . ARG D 1 292 ? 15.198  -50.847 10.963  1.00 96.36  ? 264 ARG D NE    1 
ATOM   8577 C CZ    . ARG D 1 292 ? 16.338  -50.948 11.632  1.00 102.81 ? 264 ARG D CZ    1 
ATOM   8578 N NH1   . ARG D 1 292 ? 16.817  -49.936 12.337  1.00 100.25 ? 264 ARG D NH1   1 
ATOM   8579 N NH2   . ARG D 1 292 ? 17.014  -52.092 11.594  1.00 113.16 ? 264 ARG D NH2   1 
ATOM   8580 N N     . LEU D 1 293 ? 16.217  -44.880 8.181   1.00 93.13  ? 265 LEU D N     1 
ATOM   8581 C CA    . LEU D 1 293 ? 15.552  -43.660 7.737   1.00 93.31  ? 265 LEU D CA    1 
ATOM   8582 C C     . LEU D 1 293 ? 15.585  -43.535 6.220   1.00 95.81  ? 265 LEU D C     1 
ATOM   8583 O O     . LEU D 1 293 ? 14.556  -43.270 5.587   1.00 94.72  ? 265 LEU D O     1 
ATOM   8584 C CB    . LEU D 1 293 ? 16.197  -42.442 8.396   1.00 89.75  ? 265 LEU D CB    1 
ATOM   8585 C CG    . LEU D 1 293 ? 15.839  -42.303 9.875   1.00 86.74  ? 265 LEU D CG    1 
ATOM   8586 C CD1   . LEU D 1 293 ? 16.562  -41.126 10.513  1.00 82.57  ? 265 LEU D CD1   1 
ATOM   8587 C CD2   . LEU D 1 293 ? 14.333  -42.192 10.037  1.00 83.12  ? 265 LEU D CD2   1 
ATOM   8588 N N     . GLU D 1 294 ? 16.760  -43.717 5.616   1.00 100.38 ? 266 GLU D N     1 
ATOM   8589 C CA    . GLU D 1 294 ? 16.839  -43.712 4.161   1.00 107.34 ? 266 GLU D CA    1 
ATOM   8590 C C     . GLU D 1 294 ? 16.141  -44.918 3.549   1.00 105.40 ? 266 GLU D C     1 
ATOM   8591 O O     . GLU D 1 294 ? 15.767  -44.871 2.372   1.00 108.13 ? 266 GLU D O     1 
ATOM   8592 C CB    . GLU D 1 294 ? 18.298  -43.652 3.707   1.00 114.92 ? 266 GLU D CB    1 
ATOM   8593 C CG    . GLU D 1 294 ? 18.924  -42.274 3.864   1.00 118.81 ? 266 GLU D CG    1 
ATOM   8594 C CD    . GLU D 1 294 ? 20.384  -42.238 3.458   1.00 128.87 ? 266 GLU D CD    1 
ATOM   8595 O OE1   . GLU D 1 294 ? 20.894  -43.268 2.972   1.00 129.17 ? 266 GLU D OE1   1 
ATOM   8596 O OE2   . GLU D 1 294 ? 21.019  -41.174 3.622   1.00 128.29 ? 266 GLU D OE2   1 
ATOM   8597 N N     . LYS D 1 295 ? 15.957  -45.993 4.319   1.00 101.99 ? 267 LYS D N     1 
ATOM   8598 C CA    . LYS D 1 295 ? 15.115  -47.092 3.861   1.00 102.61 ? 267 LYS D CA    1 
ATOM   8599 C C     . LYS D 1 295 ? 13.668  -46.637 3.718   1.00 105.51 ? 267 LYS D C     1 
ATOM   8600 O O     . LYS D 1 295 ? 13.035  -46.852 2.678   1.00 110.96 ? 267 LYS D O     1 
ATOM   8601 C CB    . LYS D 1 295 ? 15.219  -48.272 4.829   1.00 101.58 ? 267 LYS D CB    1 
ATOM   8602 N N     . LEU D 1 296 ? 13.133  -45.991 4.754   1.00 101.01 ? 268 LEU D N     1 
ATOM   8603 C CA    . LEU D 1 296 ? 11.785  -45.440 4.715   1.00 94.79  ? 268 LEU D CA    1 
ATOM   8604 C C     . LEU D 1 296 ? 11.707  -44.116 3.964   1.00 96.06  ? 268 LEU D C     1 
ATOM   8605 O O     . LEU D 1 296 ? 10.607  -43.569 3.824   1.00 89.18  ? 268 LEU D O     1 
ATOM   8606 C CB    . LEU D 1 296 ? 11.256  -45.263 6.140   1.00 87.00  ? 268 LEU D CB    1 
ATOM   8607 C CG    . LEU D 1 296 ? 11.095  -46.563 6.929   1.00 88.12  ? 268 LEU D CG    1 
ATOM   8608 C CD1   . LEU D 1 296 ? 10.935  -46.280 8.413   1.00 97.14  ? 268 LEU D CD1   1 
ATOM   8609 C CD2   . LEU D 1 296 ? 9.914   -47.363 6.402   1.00 86.25  ? 268 LEU D CD2   1 
ATOM   8610 N N     . LYS D 1 297 ? 12.841  -43.595 3.491   1.00 95.91  ? 269 LYS D N     1 
ATOM   8611 C CA    . LYS D 1 297 ? 12.888  -42.387 2.664   1.00 90.98  ? 269 LYS D CA    1 
ATOM   8612 C C     . LYS D 1 297 ? 12.300  -41.180 3.395   1.00 83.89  ? 269 LYS D C     1 
ATOM   8613 O O     . LYS D 1 297 ? 11.422  -40.480 2.886   1.00 82.19  ? 269 LYS D O     1 
ATOM   8614 C CB    . LYS D 1 297 ? 12.186  -42.614 1.322   1.00 95.32  ? 269 LYS D CB    1 
ATOM   8615 N N     . GLY D 1 298 ? 12.797  -40.938 4.604   1.00 75.76  ? 270 GLY D N     1 
ATOM   8616 C CA    . GLY D 1 298 ? 12.441  -39.737 5.333   1.00 72.22  ? 270 GLY D CA    1 
ATOM   8617 C C     . GLY D 1 298 ? 13.477  -38.653 5.135   1.00 77.79  ? 270 GLY D C     1 
ATOM   8618 O O     . GLY D 1 298 ? 13.150  -37.465 5.057   1.00 76.32  ? 270 GLY D O     1 
ATOM   8619 N N     . THR D 1 299 ? 14.738  -39.062 5.053   1.00 78.23  ? 271 THR D N     1 
ATOM   8620 C CA    . THR D 1 299 ? 15.845  -38.170 4.753   1.00 76.39  ? 271 THR D CA    1 
ATOM   8621 C C     . THR D 1 299 ? 16.306  -38.388 3.318   1.00 78.46  ? 271 THR D C     1 
ATOM   8622 O O     . THR D 1 299 ? 16.229  -39.497 2.782   1.00 81.76  ? 271 THR D O     1 
ATOM   8623 C CB    . THR D 1 299 ? 17.011  -38.400 5.717   1.00 74.78  ? 271 THR D CB    1 
ATOM   8624 O OG1   . THR D 1 299 ? 17.577  -39.696 5.485   1.00 83.08  ? 271 THR D OG1   1 
ATOM   8625 C CG2   . THR D 1 299 ? 16.533  -38.315 7.158   1.00 68.36  ? 271 THR D CG2   1 
ATOM   8626 N N     . SER D 1 300 ? 16.786  -37.314 2.695   1.00 72.19  ? 272 SER D N     1 
ATOM   8627 C CA    . SER D 1 300 ? 17.222  -37.360 1.308   1.00 72.59  ? 272 SER D CA    1 
ATOM   8628 C C     . SER D 1 300 ? 18.454  -36.485 1.133   1.00 76.70  ? 272 SER D C     1 
ATOM   8629 O O     . SER D 1 300 ? 18.845  -35.732 2.029   1.00 75.68  ? 272 SER D O     1 
ATOM   8630 C CB    . SER D 1 300 ? 16.108  -36.911 0.354   1.00 71.01  ? 272 SER D CB    1 
ATOM   8631 O OG    . SER D 1 300 ? 16.644  -36.293 -0.802  1.00 75.45  ? 272 SER D OG    1 
ATOM   8632 N N     . GLN D 1 301 ? 19.066  -36.596 -0.044  1.00 77.41  ? 273 GLN D N     1 
ATOM   8633 C CA    . GLN D 1 301 ? 20.230  -35.800 -0.400  1.00 71.70  ? 273 GLN D CA    1 
ATOM   8634 C C     . GLN D 1 301 ? 20.063  -35.300 -1.826  1.00 77.87  ? 273 GLN D C     1 
ATOM   8635 O O     . GLN D 1 301 ? 19.583  -36.035 -2.694  1.00 81.52  ? 273 GLN D O     1 
ATOM   8636 C CB    . GLN D 1 301 ? 21.527  -36.610 -0.262  1.00 62.23  ? 273 GLN D CB    1 
ATOM   8637 C CG    . GLN D 1 301 ? 22.793  -35.784 -0.414  1.00 68.83  ? 273 GLN D CG    1 
ATOM   8638 C CD    . GLN D 1 301 ? 23.933  -36.567 -1.032  1.00 76.65  ? 273 GLN D CD    1 
ATOM   8639 O OE1   . GLN D 1 301 ? 24.492  -37.470 -0.408  1.00 72.11  ? 273 GLN D OE1   1 
ATOM   8640 N NE2   . GLN D 1 301 ? 24.290  -36.221 -2.264  1.00 79.46  ? 273 GLN D NE2   1 
ATOM   8641 N N     . GLY D 1 302 ? 20.451  -34.049 -2.062  1.00 81.12  ? 274 GLY D N     1 
ATOM   8642 C CA    . GLY D 1 302 ? 20.276  -33.449 -3.370  1.00 81.64  ? 274 GLY D CA    1 
ATOM   8643 C C     . GLY D 1 302 ? 21.479  -32.676 -3.868  1.00 83.49  ? 274 GLY D C     1 
ATOM   8644 O O     . GLY D 1 302 ? 22.579  -32.795 -3.319  1.00 82.22  ? 274 GLY D O     1 
ATOM   8645 N N     . VAL D 1 303 ? 21.279  -31.880 -4.917  1.00 85.56  ? 275 VAL D N     1 
ATOM   8646 C CA    . VAL D 1 303 ? 22.333  -31.066 -5.508  1.00 83.45  ? 275 VAL D CA    1 
ATOM   8647 C C     . VAL D 1 303 ? 21.846  -29.628 -5.598  1.00 84.08  ? 275 VAL D C     1 
ATOM   8648 O O     . VAL D 1 303 ? 20.643  -29.363 -5.690  1.00 83.36  ? 275 VAL D O     1 
ATOM   8649 C CB    . VAL D 1 303 ? 22.752  -31.586 -6.901  1.00 79.06  ? 275 VAL D CB    1 
ATOM   8650 C CG1   . VAL D 1 303 ? 23.599  -32.842 -6.766  1.00 73.36  ? 275 VAL D CG1   1 
ATOM   8651 C CG2   . VAL D 1 303 ? 21.524  -31.851 -7.760  1.00 77.67  ? 275 VAL D CG2   1 
ATOM   8652 N N     . GLY D 1 304 ? 22.795  -28.692 -5.571  1.00 85.17  ? 276 GLY D N     1 
ATOM   8653 C CA    . GLY D 1 304 ? 22.498  -27.280 -5.614  1.00 88.49  ? 276 GLY D CA    1 
ATOM   8654 C C     . GLY D 1 304 ? 22.870  -26.650 -6.949  1.00 95.83  ? 276 GLY D C     1 
ATOM   8655 O O     . GLY D 1 304 ? 23.511  -27.257 -7.805  1.00 94.76  ? 276 GLY D O     1 
ATOM   8656 N N     . ARG D 1 305 ? 22.441  -25.395 -7.110  1.00 100.25 ? 277 ARG D N     1 
ATOM   8657 C CA    . ARG D 1 305 ? 22.762  -24.654 -8.326  1.00 101.44 ? 277 ARG D CA    1 
ATOM   8658 C C     . ARG D 1 305 ? 24.258  -24.397 -8.447  1.00 101.13 ? 277 ARG D C     1 
ATOM   8659 O O     . ARG D 1 305 ? 24.797  -24.392 -9.560  1.00 90.81  ? 277 ARG D O     1 
ATOM   8660 C CB    . ARG D 1 305 ? 21.991  -23.334 -8.358  1.00 94.94  ? 277 ARG D CB    1 
ATOM   8661 N N     . ASN D 1 306 ? 24.941  -24.180 -7.323  1.00 108.66 ? 278 ASN D N     1 
ATOM   8662 C CA    . ASN D 1 306 ? 26.389  -24.028 -7.328  1.00 100.41 ? 278 ASN D CA    1 
ATOM   8663 C C     . ASN D 1 306 ? 27.119  -25.361 -7.416  1.00 87.32  ? 278 ASN D C     1 
ATOM   8664 O O     . ASN D 1 306 ? 28.343  -25.368 -7.585  1.00 72.49  ? 278 ASN D O     1 
ATOM   8665 C CB    . ASN D 1 306 ? 26.843  -23.274 -6.075  1.00 91.38  ? 278 ASN D CB    1 
ATOM   8666 N N     . GLY D 1 307 ? 26.405  -26.481 -7.307  1.00 89.06  ? 279 GLY D N     1 
ATOM   8667 C CA    . GLY D 1 307 ? 26.997  -27.798 -7.385  1.00 86.56  ? 279 GLY D CA    1 
ATOM   8668 C C     . GLY D 1 307 ? 27.189  -28.492 -6.054  1.00 88.22  ? 279 GLY D C     1 
ATOM   8669 O O     . GLY D 1 307 ? 27.547  -29.677 -6.040  1.00 78.79  ? 279 GLY D O     1 
ATOM   8670 N N     . GLU D 1 308 ? 26.958  -27.799 -4.941  1.00 90.80  ? 280 GLU D N     1 
ATOM   8671 C CA    . GLU D 1 308 ? 27.177  -28.383 -3.628  1.00 79.54  ? 280 GLU D CA    1 
ATOM   8672 C C     . GLU D 1 308 ? 26.095  -29.414 -3.309  1.00 81.09  ? 280 GLU D C     1 
ATOM   8673 O O     . GLU D 1 308 ? 25.067  -29.516 -3.984  1.00 82.89  ? 280 GLU D O     1 
ATOM   8674 C CB    . GLU D 1 308 ? 27.207  -27.293 -2.557  1.00 70.59  ? 280 GLU D CB    1 
ATOM   8675 N N     . ALA D 1 309 ? 26.343  -30.188 -2.255  1.00 79.64  ? 281 ALA D N     1 
ATOM   8676 C CA    . ALA D 1 309 ? 25.424  -31.231 -1.824  1.00 77.95  ? 281 ALA D CA    1 
ATOM   8677 C C     . ALA D 1 309 ? 24.402  -30.670 -0.844  1.00 75.59  ? 281 ALA D C     1 
ATOM   8678 O O     . ALA D 1 309 ? 24.740  -29.883 0.045   1.00 71.10  ? 281 ALA D O     1 
ATOM   8679 C CB    . ALA D 1 309 ? 26.187  -32.389 -1.179  1.00 70.14  ? 281 ALA D CB    1 
ATOM   8680 N N     . GLU D 1 310 ? 23.149  -31.085 -1.012  1.00 73.52  ? 282 GLU D N     1 
ATOM   8681 C CA    . GLU D 1 310 ? 22.044  -30.628 -0.186  1.00 67.39  ? 282 GLU D CA    1 
ATOM   8682 C C     . GLU D 1 310 ? 21.461  -31.806 0.584   1.00 68.05  ? 282 GLU D C     1 
ATOM   8683 O O     . GLU D 1 310 ? 21.423  -32.932 0.084   1.00 74.25  ? 282 GLU D O     1 
ATOM   8684 C CB    . GLU D 1 310 ? 20.956  -29.969 -1.041  1.00 67.75  ? 282 GLU D CB    1 
ATOM   8685 C CG    . GLU D 1 310 ? 21.388  -28.664 -1.691  1.00 72.90  ? 282 GLU D CG    1 
ATOM   8686 C CD    . GLU D 1 310 ? 20.309  -28.064 -2.571  1.00 77.15  ? 282 GLU D CD    1 
ATOM   8687 O OE1   . GLU D 1 310 ? 19.396  -28.810 -2.986  1.00 80.01  ? 282 GLU D OE1   1 
ATOM   8688 O OE2   . GLU D 1 310 ? 20.375  -26.848 -2.849  1.00 75.74  ? 282 GLU D OE2   1 
ATOM   8689 N N     . TYR D 1 311 ? 21.007  -31.540 1.808   1.00 60.61  ? 283 TYR D N     1 
ATOM   8690 C CA    . TYR D 1 311 ? 20.495  -32.576 2.694   1.00 55.81  ? 283 TYR D CA    1 
ATOM   8691 C C     . TYR D 1 311 ? 19.146  -32.146 3.252   1.00 54.57  ? 283 TYR D C     1 
ATOM   8692 O O     . TYR D 1 311 ? 18.956  -30.976 3.600   1.00 55.77  ? 283 TYR D O     1 
ATOM   8693 C CB    . TYR D 1 311 ? 21.484  -32.866 3.831   1.00 56.22  ? 283 TYR D CB    1 
ATOM   8694 C CG    . TYR D 1 311 ? 22.832  -33.351 3.340   1.00 58.13  ? 283 TYR D CG    1 
ATOM   8695 C CD1   . TYR D 1 311 ? 23.799  -32.453 2.905   1.00 64.55  ? 283 TYR D CD1   1 
ATOM   8696 C CD2   . TYR D 1 311 ? 23.131  -34.706 3.292   1.00 61.95  ? 283 TYR D CD2   1 
ATOM   8697 C CE1   . TYR D 1 311 ? 25.027  -32.889 2.446   1.00 70.13  ? 283 TYR D CE1   1 
ATOM   8698 C CE2   . TYR D 1 311 ? 24.358  -35.152 2.834   1.00 68.20  ? 283 TYR D CE2   1 
ATOM   8699 C CZ    . TYR D 1 311 ? 25.302  -34.239 2.412   1.00 67.94  ? 283 TYR D CZ    1 
ATOM   8700 O OH    . TYR D 1 311 ? 26.524  -34.676 1.956   1.00 67.69  ? 283 TYR D OH    1 
ATOM   8701 N N     . TYR D 1 312 ? 18.212  -33.093 3.340   1.00 55.26  ? 284 TYR D N     1 
ATOM   8702 C CA    . TYR D 1 312 ? 16.823  -32.769 3.632   1.00 55.38  ? 284 TYR D CA    1 
ATOM   8703 C C     . TYR D 1 312 ? 16.236  -33.750 4.637   1.00 60.01  ? 284 TYR D C     1 
ATOM   8704 O O     . TYR D 1 312 ? 16.733  -34.864 4.819   1.00 62.40  ? 284 TYR D O     1 
ATOM   8705 C CB    . TYR D 1 312 ? 15.968  -32.781 2.358   1.00 57.89  ? 284 TYR D CB    1 
ATOM   8706 C CG    . TYR D 1 312 ? 16.289  -31.669 1.390   1.00 53.66  ? 284 TYR D CG    1 
ATOM   8707 C CD1   . TYR D 1 312 ? 17.279  -31.824 0.430   1.00 59.88  ? 284 TYR D CD1   1 
ATOM   8708 C CD2   . TYR D 1 312 ? 15.602  -30.464 1.436   1.00 52.10  ? 284 TYR D CD2   1 
ATOM   8709 C CE1   . TYR D 1 312 ? 17.576  -30.810 -0.458  1.00 66.56  ? 284 TYR D CE1   1 
ATOM   8710 C CE2   . TYR D 1 312 ? 15.892  -29.443 0.553   1.00 56.96  ? 284 TYR D CE2   1 
ATOM   8711 C CZ    . TYR D 1 312 ? 16.880  -29.621 -0.392  1.00 66.21  ? 284 TYR D CZ    1 
ATOM   8712 O OH    . TYR D 1 312 ? 17.174  -28.608 -1.275  1.00 68.70  ? 284 TYR D OH    1 
ATOM   8713 N N     . ILE D 1 313 ? 15.156  -33.313 5.283   1.00 57.38  ? 285 ILE D N     1 
ATOM   8714 C CA    . ILE D 1 313 ? 14.322  -34.154 6.135   1.00 54.70  ? 285 ILE D CA    1 
ATOM   8715 C C     . ILE D 1 313 ? 12.873  -33.914 5.733   1.00 63.51  ? 285 ILE D C     1 
ATOM   8716 O O     . ILE D 1 313 ? 12.395  -32.774 5.778   1.00 61.74  ? 285 ILE D O     1 
ATOM   8717 C CB    . ILE D 1 313 ? 14.521  -33.858 7.632   1.00 53.76  ? 285 ILE D CB    1 
ATOM   8718 C CG1   . ILE D 1 313 ? 15.938  -34.228 8.073   1.00 54.50  ? 285 ILE D CG1   1 
ATOM   8719 C CG2   . ILE D 1 313 ? 13.489  -34.603 8.464   1.00 54.18  ? 285 ILE D CG2   1 
ATOM   8720 C CD1   . ILE D 1 313 ? 16.250  -33.841 9.503   1.00 53.87  ? 285 ILE D CD1   1 
ATOM   8721 N N     . HIS D 1 314 ? 12.178  -34.978 5.340   1.00 69.78  ? 286 HIS D N     1 
ATOM   8722 C CA    . HIS D 1 314 ? 10.802  -34.887 4.873   1.00 70.64  ? 286 HIS D CA    1 
ATOM   8723 C C     . HIS D 1 314 ? 9.839   -35.311 5.974   1.00 68.19  ? 286 HIS D C     1 
ATOM   8724 O O     . HIS D 1 314 ? 10.102  -36.266 6.710   1.00 68.03  ? 286 HIS D O     1 
ATOM   8725 C CB    . HIS D 1 314 ? 10.590  -35.754 3.632   1.00 69.09  ? 286 HIS D CB    1 
ATOM   8726 C CG    . HIS D 1 314 ? 11.617  -35.539 2.566   1.00 71.02  ? 286 HIS D CG    1 
ATOM   8727 N ND1   . HIS D 1 314 ? 11.528  -34.520 1.642   1.00 72.80  ? 286 HIS D ND1   1 
ATOM   8728 C CD2   . HIS D 1 314 ? 12.756  -36.211 2.277   1.00 72.04  ? 286 HIS D CD2   1 
ATOM   8729 C CE1   . HIS D 1 314 ? 12.568  -34.574 0.829   1.00 75.48  ? 286 HIS D CE1   1 
ATOM   8730 N NE2   . HIS D 1 314 ? 13.328  -35.591 1.193   1.00 73.92  ? 286 HIS D NE2   1 
ATOM   8731 N N     . LEU D 1 315 ? 8.716   -34.601 6.069   1.00 63.54  ? 287 LEU D N     1 
ATOM   8732 C CA    . LEU D 1 315 ? 7.739   -34.824 7.125   1.00 71.06  ? 287 LEU D CA    1 
ATOM   8733 C C     . LEU D 1 315 ? 6.489   -34.004 6.831   1.00 76.64  ? 287 LEU D C     1 
ATOM   8734 O O     . LEU D 1 315 ? 6.567   -32.931 6.225   1.00 75.47  ? 287 LEU D O     1 
ATOM   8735 C CB    . LEU D 1 315 ? 8.325   -34.466 8.500   1.00 68.63  ? 287 LEU D CB    1 
ATOM   8736 C CG    . LEU D 1 315 ? 8.824   -33.035 8.718   1.00 54.24  ? 287 LEU D CG    1 
ATOM   8737 C CD1   . LEU D 1 315 ? 7.761   -32.166 9.356   1.00 59.95  ? 287 LEU D CD1   1 
ATOM   8738 C CD2   . LEU D 1 315 ? 10.099  -33.023 9.549   1.00 51.50  ? 287 LEU D CD2   1 
ATOM   8739 N N     . SER D 1 316 ? 5.341   -34.527 7.261   1.00 78.90  ? 288 SER D N     1 
ATOM   8740 C CA    . SER D 1 316 ? 4.056   -33.875 7.044   1.00 80.12  ? 288 SER D CA    1 
ATOM   8741 C C     . SER D 1 316 ? 3.698   -33.000 8.238   1.00 77.20  ? 288 SER D C     1 
ATOM   8742 O O     . SER D 1 316 ? 3.951   -33.368 9.388   1.00 80.00  ? 288 SER D O     1 
ATOM   8743 C CB    . SER D 1 316 ? 2.958   -34.914 6.809   1.00 80.33  ? 288 SER D CB    1 
ATOM   8744 O OG    . SER D 1 316 ? 3.248   -35.717 5.678   1.00 94.39  ? 288 SER D OG    1 
ATOM   8745 N N     . VAL D 1 317 ? 3.102   -31.842 7.959   1.00 74.47  ? 289 VAL D N     1 
ATOM   8746 C CA    . VAL D 1 317 ? 2.759   -30.863 8.985   1.00 69.41  ? 289 VAL D CA    1 
ATOM   8747 C C     . VAL D 1 317 ? 1.294   -30.482 8.846   1.00 71.32  ? 289 VAL D C     1 
ATOM   8748 O O     . VAL D 1 317 ? 0.832   -30.161 7.746   1.00 75.08  ? 289 VAL D O     1 
ATOM   8749 C CB    . VAL D 1 317 ? 3.642   -29.603 8.898   1.00 71.37  ? 289 VAL D CB    1 
ATOM   8750 C CG1   . VAL D 1 317 ? 3.169   -28.553 9.892   1.00 75.19  ? 289 VAL D CG1   1 
ATOM   8751 C CG2   . VAL D 1 317 ? 5.084   -29.952 9.166   1.00 69.55  ? 289 VAL D CG2   1 
ATOM   8752 N N     . ILE D 1 318 ? 0.570   -30.511 9.960   1.00 73.90  ? 290 ILE D N     1 
ATOM   8753 C CA    . ILE D 1 318 ? -0.773  -29.950 10.036  1.00 72.51  ? 290 ILE D CA    1 
ATOM   8754 C C     . ILE D 1 318 ? -0.664  -28.525 10.556  1.00 66.91  ? 290 ILE D C     1 
ATOM   8755 O O     . ILE D 1 318 ? -0.042  -28.280 11.597  1.00 70.56  ? 290 ILE D O     1 
ATOM   8756 C CB    . ILE D 1 318 ? -1.677  -30.796 10.948  1.00 73.18  ? 290 ILE D CB    1 
ATOM   8757 C CG1   . ILE D 1 318 ? -1.627  -32.270 10.548  1.00 73.20  ? 290 ILE D CG1   1 
ATOM   8758 C CG2   . ILE D 1 318 ? -3.108  -30.278 10.906  1.00 73.83  ? 290 ILE D CG2   1 
ATOM   8759 C CD1   . ILE D 1 318 ? -2.152  -33.196 11.620  1.00 80.16  ? 290 ILE D CD1   1 
ATOM   8760 N N     . THR D 1 319 ? -1.257  -27.582 9.832   1.00 65.91  ? 291 THR D N     1 
ATOM   8761 C CA    . THR D 1 319 ? -1.322  -26.189 10.253  1.00 72.57  ? 291 THR D CA    1 
ATOM   8762 C C     . THR D 1 319 ? -2.752  -25.871 10.663  1.00 74.74  ? 291 THR D C     1 
ATOM   8763 O O     . THR D 1 319 ? -3.696  -26.206 9.940   1.00 83.84  ? 291 THR D O     1 
ATOM   8764 C CB    . THR D 1 319 ? -0.866  -25.249 9.135   1.00 73.66  ? 291 THR D CB    1 
ATOM   8765 O OG1   . THR D 1 319 ? 0.421   -25.661 8.658   1.00 75.19  ? 291 THR D OG1   1 
ATOM   8766 C CG2   . THR D 1 319 ? -0.774  -23.819 9.646   1.00 66.75  ? 291 THR D CG2   1 
ATOM   8767 N N     . ALA D 1 320 ? -2.911  -25.234 11.821  1.00 74.04  ? 292 ALA D N     1 
ATOM   8768 C CA    . ALA D 1 320 ? -4.234  -24.969 12.366  1.00 74.70  ? 292 ALA D CA    1 
ATOM   8769 C C     . ALA D 1 320 ? -4.288  -23.570 12.961  1.00 76.04  ? 292 ALA D C     1 
ATOM   8770 O O     . ALA D 1 320 ? -3.282  -23.037 13.438  1.00 77.11  ? 292 ALA D O     1 
ATOM   8771 C CB    . ALA D 1 320 ? -4.620  -26.003 13.432  1.00 71.31  ? 292 ALA D CB    1 
ATOM   8772 N N     . LEU D 1 321 ? -5.483  -22.984 12.924  1.00 73.16  ? 293 LEU D N     1 
ATOM   8773 C CA    . LEU D 1 321 ? -5.758  -21.692 13.547  1.00 74.15  ? 293 LEU D CA    1 
ATOM   8774 C C     . LEU D 1 321 ? -7.112  -21.803 14.233  1.00 82.64  ? 293 LEU D C     1 
ATOM   8775 O O     . LEU D 1 321 ? -8.137  -21.955 13.561  1.00 90.14  ? 293 LEU D O     1 
ATOM   8776 C CB    . LEU D 1 321 ? -5.751  -20.560 12.520  1.00 71.71  ? 293 LEU D CB    1 
ATOM   8777 C CG    . LEU D 1 321 ? -6.278  -19.207 13.002  1.00 75.85  ? 293 LEU D CG    1 
ATOM   8778 C CD1   . LEU D 1 321 ? -5.432  -18.679 14.149  1.00 74.63  ? 293 LEU D CD1   1 
ATOM   8779 C CD2   . LEU D 1 321 ? -6.323  -18.205 11.858  1.00 81.61  ? 293 LEU D CD2   1 
ATOM   8780 N N     . ALA D 1 322 ? -7.119  -21.734 15.559  1.00 76.52  ? 294 ALA D N     1 
ATOM   8781 C CA    . ALA D 1 322 ? -8.320  -21.946 16.355  1.00 73.85  ? 294 ALA D CA    1 
ATOM   8782 C C     . ALA D 1 322 ? -8.648  -20.689 17.155  1.00 76.11  ? 294 ALA D C     1 
ATOM   8783 O O     . ALA D 1 322 ? -7.979  -19.659 17.047  1.00 73.84  ? 294 ALA D O     1 
ATOM   8784 C CB    . ALA D 1 322 ? -8.150  -23.154 17.280  1.00 76.14  ? 294 ALA D CB    1 
ATOM   8785 N N     . ARG D 1 323 ? -9.699  -20.788 17.967  1.00 83.60  ? 295 ARG D N     1 
ATOM   8786 C CA    . ARG D 1 323 ? -10.132 -19.682 18.807  1.00 86.06  ? 295 ARG D CA    1 
ATOM   8787 C C     . ARG D 1 323 ? -10.994 -20.223 19.937  1.00 89.93  ? 295 ARG D C     1 
ATOM   8788 O O     . ARG D 1 323 ? -11.859 -21.073 19.712  1.00 88.38  ? 295 ARG D O     1 
ATOM   8789 C CB    . ARG D 1 323 ? -10.912 -18.636 18.002  1.00 85.23  ? 295 ARG D CB    1 
ATOM   8790 C CG    . ARG D 1 323 ? -11.363 -17.439 18.824  1.00 86.98  ? 295 ARG D CG    1 
ATOM   8791 C CD    . ARG D 1 323 ? -12.179 -16.476 17.984  1.00 91.07  ? 295 ARG D CD    1 
ATOM   8792 N NE    . ARG D 1 323 ? -11.383 -15.894 16.910  1.00 97.72  ? 295 ARG D NE    1 
ATOM   8793 C CZ    . ARG D 1 323 ? -11.889 -15.356 15.810  1.00 97.77  ? 295 ARG D CZ    1 
ATOM   8794 N NH1   . ARG D 1 323 ? -13.194 -15.310 15.599  1.00 99.80  ? 295 ARG D NH1   1 
ATOM   8795 N NH2   . ARG D 1 323 ? -11.064 -14.851 14.897  1.00 93.79  ? 295 ARG D NH2   1 
ATOM   8796 N N     . LYS D 1 324 ? -10.754 -19.723 21.146  1.00 93.46  ? 296 LYS D N     1 
ATOM   8797 C CA    . LYS D 1 324 ? -11.529 -20.137 22.305  1.00 97.84  ? 296 LYS D CA    1 
ATOM   8798 C C     . LYS D 1 324 ? -12.851 -19.382 22.361  1.00 99.90  ? 296 LYS D C     1 
ATOM   8799 O O     . LYS D 1 324 ? -12.939 -18.210 21.984  1.00 93.89  ? 296 LYS D O     1 
ATOM   8800 C CB    . LYS D 1 324 ? -10.738 -19.900 23.592  1.00 95.53  ? 296 LYS D CB    1 
ATOM   8801 N N     . PHE D 1 325 ? -13.885 -20.068 22.837  1.00 101.69 ? 297 PHE D N     1 
ATOM   8802 C CA    . PHE D 1 325 ? -15.209 -19.468 22.969  1.00 102.37 ? 297 PHE D CA    1 
ATOM   8803 C C     . PHE D 1 325 ? -15.367 -18.779 24.322  1.00 104.56 ? 297 PHE D C     1 
ATOM   8804 O O     . PHE D 1 325 ? -14.765 -19.192 25.314  1.00 103.91 ? 297 PHE D O     1 
ATOM   8805 C CB    . PHE D 1 325 ? -16.298 -20.526 22.787  1.00 100.72 ? 297 PHE D CB    1 
ATOM   8806 C CG    . PHE D 1 325 ? -16.714 -20.728 21.358  1.00 104.92 ? 297 PHE D CG    1 
ATOM   8807 C CD1   . PHE D 1 325 ? -17.610 -19.863 20.755  1.00 109.43 ? 297 PHE D CD1   1 
ATOM   8808 C CD2   . PHE D 1 325 ? -16.206 -21.783 20.616  1.00 104.00 ? 297 PHE D CD2   1 
ATOM   8809 C CE1   . PHE D 1 325 ? -17.995 -20.044 19.440  1.00 114.85 ? 297 PHE D CE1   1 
ATOM   8810 C CE2   . PHE D 1 325 ? -16.587 -21.970 19.299  1.00 103.28 ? 297 PHE D CE2   1 
ATOM   8811 C CZ    . PHE D 1 325 ? -17.483 -21.099 18.711  1.00 108.56 ? 297 PHE D CZ    1 
HETATM 8812 N N     . SAM E 2 .   ? -3.668  28.036  10.671  1.00 53.92  ? 301 SAM A N     1 
HETATM 8813 C CA    . SAM E 2 .   ? -5.019  27.811  11.144  1.00 51.91  ? 301 SAM A CA    1 
HETATM 8814 C C     . SAM E 2 .   ? -5.965  27.641  9.964   1.00 56.93  ? 301 SAM A C     1 
HETATM 8815 O O     . SAM E 2 .   ? -5.649  28.096  8.836   1.00 54.04  ? 301 SAM A O     1 
HETATM 8816 O OXT   . SAM E 2 .   ? -7.084  27.035  10.122  1.00 59.37  ? 301 SAM A OXT   1 
HETATM 8817 C CB    . SAM E 2 .   ? -5.479  28.989  12.035  1.00 44.34  ? 301 SAM A CB    1 
HETATM 8818 C CG    . SAM E 2 .   ? -5.063  30.350  11.416  1.00 46.64  ? 301 SAM A CG    1 
HETATM 8819 S SD    . SAM E 2 .   ? -5.539  31.729  12.545  1.00 54.08  ? 301 SAM A SD    1 
HETATM 8820 C CE    . SAM E 2 .   ? -5.749  33.248  11.591  1.00 57.02  ? 301 SAM A CE    1 
HETATM 8821 C "C5'" . SAM E 2 .   ? -4.226  31.961  13.761  1.00 43.81  ? 301 SAM A "C5'" 1 
HETATM 8822 C "C4'" . SAM E 2 .   ? -4.505  31.075  15.000  1.00 40.69  ? 301 SAM A "C4'" 1 
HETATM 8823 O "O4'" . SAM E 2 .   ? -3.443  31.033  15.765  1.00 42.51  ? 301 SAM A "O4'" 1 
HETATM 8824 C "C3'" . SAM E 2 .   ? -5.658  31.720  15.861  1.00 37.69  ? 301 SAM A "C3'" 1 
HETATM 8825 O "O3'" . SAM E 2 .   ? -6.534  30.759  16.276  1.00 37.39  ? 301 SAM A "O3'" 1 
HETATM 8826 C "C2'" . SAM E 2 .   ? -4.954  32.328  17.049  1.00 37.70  ? 301 SAM A "C2'" 1 
HETATM 8827 O "O2'" . SAM E 2 .   ? -5.838  32.270  18.257  1.00 38.18  ? 301 SAM A "O2'" 1 
HETATM 8828 C "C1'" . SAM E 2 .   ? -3.868  31.550  17.224  1.00 37.67  ? 301 SAM A "C1'" 1 
HETATM 8829 N N9    . SAM E 2 .   ? -2.787  32.322  17.812  1.00 41.04  ? 301 SAM A N9    1 
HETATM 8830 C C8    . SAM E 2 .   ? -2.574  33.620  17.619  1.00 46.01  ? 301 SAM A C8    1 
HETATM 8831 N N7    . SAM E 2 .   ? -1.497  33.999  18.309  1.00 48.93  ? 301 SAM A N7    1 
HETATM 8832 C C5    . SAM E 2 .   ? -1.011  32.922  18.956  1.00 45.02  ? 301 SAM A C5    1 
HETATM 8833 C C6    . SAM E 2 .   ? 0.084   32.719  19.818  1.00 41.63  ? 301 SAM A C6    1 
HETATM 8834 N N6    . SAM E 2 .   ? 0.997   33.858  20.182  1.00 39.01  ? 301 SAM A N6    1 
HETATM 8835 N N1    . SAM E 2 .   ? 0.282   31.503  20.291  1.00 43.19  ? 301 SAM A N1    1 
HETATM 8836 C C2    . SAM E 2 .   ? -0.528  30.478  19.971  1.00 40.52  ? 301 SAM A C2    1 
HETATM 8837 N N3    . SAM E 2 .   ? -1.561  30.638  19.168  1.00 39.11  ? 301 SAM A N3    1 
HETATM 8838 C C4    . SAM E 2 .   ? -1.833  31.842  18.641  1.00 41.39  ? 301 SAM A C4    1 
HETATM 8839 N N     . SAM F 2 .   ? 26.747  -9.005  5.948   1.00 49.70  ? 301 SAM B N     1 
HETATM 8840 C CA    . SAM F 2 .   ? 26.412  -10.316 5.431   1.00 51.53  ? 301 SAM B CA    1 
HETATM 8841 C C     . SAM F 2 .   ? 26.150  -11.277 6.581   1.00 54.66  ? 301 SAM B C     1 
HETATM 8842 O O     . SAM F 2 .   ? 26.673  -11.070 7.704   1.00 49.69  ? 301 SAM B O     1 
HETATM 8843 O OXT   . SAM F 2 .   ? 25.390  -12.295 6.405   1.00 54.74  ? 301 SAM B OXT   1 
HETATM 8844 C CB    . SAM F 2 .   ? 27.553  -10.854 4.532   1.00 45.34  ? 301 SAM B CB    1 
HETATM 8845 C CG    . SAM F 2 .   ? 28.936  -10.769 5.233   1.00 46.46  ? 301 SAM B CG    1 
HETATM 8846 S SD    . SAM F 2 .   ? 30.231  -11.532 4.160   1.00 67.29  ? 301 SAM B SD    1 
HETATM 8847 C CE    . SAM F 2 .   ? 31.672  -11.965 5.159   1.00 58.40  ? 301 SAM B CE    1 
HETATM 8848 C "C5'" . SAM F 2 .   ? 30.731  -10.348 2.893   1.00 54.63  ? 301 SAM B "C5'" 1 
HETATM 8849 C "C4'" . SAM F 2 .   ? 29.863  -10.522 1.623   1.00 49.56  ? 301 SAM B "C4'" 1 
HETATM 8850 O "O4'" . SAM F 2 .   ? 30.024  -9.487  0.839   1.00 51.28  ? 301 SAM B "O4'" 1 
HETATM 8851 C "C3'" . SAM F 2 .   ? 30.347  -11.786 0.813   1.00 47.00  ? 301 SAM B "C3'" 1 
HETATM 8852 O "O3'" . SAM F 2 .   ? 29.277  -12.535 0.415   1.00 46.51  ? 301 SAM B "O3'" 1 
HETATM 8853 C "C2'" . SAM F 2 .   ? 31.068  -11.226 -0.389  1.00 47.53  ? 301 SAM B "C2'" 1 
HETATM 8854 O "O2'" . SAM F 2 .   ? 30.849  -12.115 -1.575  1.00 52.66  ? 301 SAM B "O2'" 1 
HETATM 8855 C "C1'" . SAM F 2 .   ? 30.499  -10.022 -0.598  1.00 47.59  ? 301 SAM B "C1'" 1 
HETATM 8856 N N9    . SAM F 2 .   ? 31.460  -9.100  -1.178  1.00 47.40  ? 301 SAM B N9    1 
HETATM 8857 C C8    . SAM F 2 .   ? 32.769  -9.107  -0.946  1.00 52.80  ? 301 SAM B C8    1 
HETATM 8858 N N7    . SAM F 2 .   ? 33.344  -8.124  -1.642  1.00 50.17  ? 301 SAM B N7    1 
HETATM 8859 C C5    . SAM F 2 .   ? 32.386  -7.476  -2.330  1.00 44.93  ? 301 SAM B C5    1 
HETATM 8860 C C6    . SAM F 2 .   ? 32.396  -6.380  -3.213  1.00 44.75  ? 301 SAM B C6    1 
HETATM 8861 N N6    . SAM F 2 .   ? 33.683  -5.679  -3.557  1.00 45.65  ? 301 SAM B N6    1 
HETATM 8862 N N1    . SAM F 2 .   ? 31.245  -5.988  -3.728  1.00 44.90  ? 301 SAM B N1    1 
HETATM 8863 C C2    . SAM F 2 .   ? 30.090  -6.607  -3.428  1.00 43.11  ? 301 SAM B C2    1 
HETATM 8864 N N3    . SAM F 2 .   ? 30.049  -7.634  -2.605  1.00 43.26  ? 301 SAM B N3    1 
HETATM 8865 C C4    . SAM F 2 .   ? 31.173  -8.095  -2.036  1.00 44.84  ? 301 SAM B C4    1 
HETATM 8866 N N     . SAM G 2 .   ? -22.857 13.510  -0.929  1.00 60.02  ? 301 SAM C N     1 
HETATM 8867 C CA    . SAM G 2 .   ? -22.371 14.789  -1.398  1.00 59.31  ? 301 SAM C CA    1 
HETATM 8868 C C     . SAM G 2 .   ? -22.169 15.737  -0.227  1.00 59.89  ? 301 SAM C C     1 
HETATM 8869 O O     . SAM G 2 .   ? -22.686 15.476  0.886   1.00 54.01  ? 301 SAM C O     1 
HETATM 8870 O OXT   . SAM G 2 .   ? -21.476 16.805  -0.382  1.00 61.11  ? 301 SAM C OXT   1 
HETATM 8871 C CB    . SAM G 2 .   ? -23.368 15.399  -2.407  1.00 53.51  ? 301 SAM C CB    1 
HETATM 8872 C CG    . SAM G 2 .   ? -24.789 15.462  -1.793  1.00 54.13  ? 301 SAM C CG    1 
HETATM 8873 S SD    . SAM G 2 .   ? -25.884 16.372  -2.961  1.00 58.00  ? 301 SAM C SD    1 
HETATM 8874 C CE    . SAM G 2 .   ? -27.156 17.226  -2.025  1.00 56.48  ? 301 SAM C CE    1 
HETATM 8875 C "C5'" . SAM G 2 .   ? -26.693 15.204  -4.063  1.00 53.89  ? 301 SAM C "C5'" 1 
HETATM 8876 C "C4'" . SAM G 2 .   ? -26.126 15.443  -5.478  1.00 52.50  ? 301 SAM C "C4'" 1 
HETATM 8877 O "O4'" . SAM G 2 .   ? -26.499 14.467  -6.254  1.00 53.83  ? 301 SAM C "O4'" 1 
HETATM 8878 C "C3'" . SAM G 2 .   ? -26.729 16.775  -6.072  1.00 49.73  ? 301 SAM C "C3'" 1 
HETATM 8879 O "O3'" . SAM G 2 .   ? -25.722 17.621  -6.442  1.00 49.25  ? 301 SAM C "O3'" 1 
HETATM 8880 C "C2'" . SAM G 2 .   ? -27.525 16.356  -7.285  1.00 49.91  ? 301 SAM C "C2'" 1 
HETATM 8881 O "O2'" . SAM G 2 .   ? -27.228 17.293  -8.417  1.00 50.03  ? 301 SAM C "O2'" 1 
HETATM 8882 C "C1'" . SAM G 2 .   ? -27.085 15.119  -7.594  1.00 48.80  ? 301 SAM C "C1'" 1 
HETATM 8883 N N9    . SAM G 2 .   ? -28.160 14.273  -8.075  1.00 49.35  ? 301 SAM C N9    1 
HETATM 8884 C C8    . SAM G 2 .   ? -29.455 14.414  -7.811  1.00 53.56  ? 301 SAM C C8    1 
HETATM 8885 N N7    . SAM G 2 .   ? -30.130 13.441  -8.426  1.00 54.55  ? 301 SAM C N7    1 
HETATM 8886 C C5    . SAM G 2 .   ? -29.250 12.665  -9.089  1.00 51.45  ? 301 SAM C C5    1 
HETATM 8887 C C6    . SAM G 2 .   ? -29.369 11.519  -9.897  1.00 52.46  ? 301 SAM C C6    1 
HETATM 8888 N N6    . SAM G 2 .   ? -30.715 10.904  -10.173 1.00 57.21  ? 301 SAM C N6    1 
HETATM 8889 N N1    . SAM G 2 .   ? -28.266 11.000  -10.403 1.00 50.25  ? 301 SAM C N1    1 
HETATM 8890 C C2    . SAM G 2 .   ? -27.056 11.534  -10.167 1.00 50.49  ? 301 SAM C C2    1 
HETATM 8891 N N3    . SAM G 2 .   ? -26.913 12.605  -9.417  1.00 49.22  ? 301 SAM C N3    1 
HETATM 8892 C C4    . SAM G 2 .   ? -27.984 13.193  -8.862  1.00 48.88  ? 301 SAM C C4    1 
HETATM 8893 C C2    . 4VP H 3 .   ? -33.278 18.451  -2.820  1.00 58.75  ? 302 4VP C C2    1 
HETATM 8894 C C3    . 4VP H 3 .   ? -33.472 17.875  -1.651  1.00 60.59  ? 302 4VP C C3    1 
HETATM 8895 C "C1'" . 4VP H 3 .   ? -32.276 17.568  -0.751  1.00 66.15  ? 302 4VP C "C1'" 1 
HETATM 8896 C "C6'" . 4VP H 3 .   ? -31.010 17.969  -1.140  1.00 65.67  ? 302 4VP C "C6'" 1 
HETATM 8897 C "C5'" . 4VP H 3 .   ? -29.924 17.701  -0.327  1.00 61.45  ? 302 4VP C "C5'" 1 
HETATM 8898 C "C4'" . 4VP H 3 .   ? -30.084 17.028  0.869   1.00 63.27  ? 302 4VP C "C4'" 1 
HETATM 8899 O "O4'" . 4VP H 3 .   ? -28.966 16.765  1.671   1.00 59.66  ? 302 4VP C "O4'" 1 
HETATM 8900 C "C3'" . 4VP H 3 .   ? -31.350 16.627  1.264   1.00 67.31  ? 302 4VP C "C3'" 1 
HETATM 8901 C "C2'" . 4VP H 3 .   ? -32.443 16.895  0.452   1.00 68.14  ? 302 4VP C "C2'" 1 
HETATM 8902 N N     . SAM I 2 .   ? 8.829   -25.896 17.613  1.00 53.39  ? 301 SAM D N     1 
HETATM 8903 C CA    . SAM I 2 .   ? 10.138  -25.525 18.108  1.00 57.07  ? 301 SAM D CA    1 
HETATM 8904 C C     . SAM I 2 .   ? 11.038  -25.127 16.948  1.00 62.22  ? 301 SAM D C     1 
HETATM 8905 O O     . SAM I 2 .   ? 10.824  -25.592 15.801  1.00 59.21  ? 301 SAM D O     1 
HETATM 8906 O OXT   . SAM I 2 .   ? 12.011  -24.314 17.140  1.00 61.61  ? 301 SAM D OXT   1 
HETATM 8907 C CB    . SAM I 2 .   ? 10.762  -26.699 18.897  1.00 52.88  ? 301 SAM D CB    1 
HETATM 8908 C CG    . SAM I 2 .   ? 10.421  -28.054 18.222  1.00 57.03  ? 301 SAM D CG    1 
HETATM 8909 S SD    . SAM I 2 .   ? 11.176  -29.444 19.169  1.00 66.17  ? 301 SAM D SD    1 
HETATM 8910 C CE    . SAM I 2 .   ? 11.442  -30.856 18.075  1.00 66.78  ? 301 SAM D CE    1 
HETATM 8911 C "C5'" . SAM I 2 .   ? 10.045  -29.913 20.493  1.00 55.90  ? 301 SAM D "C5'" 1 
HETATM 8912 C "C4'" . SAM I 2 .   ? 10.325  -29.017 21.724  1.00 52.25  ? 301 SAM D "C4'" 1 
HETATM 8913 O "O4'" . SAM I 2 .   ? 9.290   -29.025 22.522  1.00 60.18  ? 301 SAM D "O4'" 1 
HETATM 8914 C "C3'" . SAM I 2 .   ? 11.536  -29.614 22.536  1.00 50.84  ? 301 SAM D "C3'" 1 
HETATM 8915 O "O3'" . SAM I 2 .   ? 12.353  -28.610 22.972  1.00 48.15  ? 301 SAM D "O3'" 1 
HETATM 8916 C "C2'" . SAM I 2 .   ? 10.898  -30.322 23.707  1.00 54.18  ? 301 SAM D "C2'" 1 
HETATM 8917 O "O2'" . SAM I 2 .   ? 11.793  -30.221 24.905  1.00 62.19  ? 301 SAM D "O2'" 1 
HETATM 8918 C "C1'" . SAM I 2 .   ? 9.750   -29.652 23.928  1.00 55.54  ? 301 SAM D "C1'" 1 
HETATM 8919 N N9    . SAM I 2 .   ? 8.710   -30.535 24.427  1.00 53.86  ? 301 SAM D N9    1 
HETATM 8920 C C8    . SAM I 2 .   ? 8.630   -31.847 24.222  1.00 58.16  ? 301 SAM D C8    1 
HETATM 8921 N N7    . SAM I 2 .   ? 7.538   -32.316 24.830  1.00 57.19  ? 301 SAM D N7    1 
HETATM 8922 C C5    . SAM I 2 .   ? 6.909   -31.286 25.429  1.00 52.69  ? 301 SAM D C5    1 
HETATM 8923 C C6    . SAM I 2 .   ? 5.733   -31.170 26.196  1.00 55.65  ? 301 SAM D C6    1 
HETATM 8924 N N6    . SAM I 2 .   ? 4.894   -32.379 26.512  1.00 58.54  ? 301 SAM D N6    1 
HETATM 8925 N N1    . SAM I 2 .   ? 5.400   -29.976 26.649  1.00 56.62  ? 301 SAM D N1    1 
HETATM 8926 C C2    . SAM I 2 .   ? 6.143   -28.888 26.383  1.00 55.70  ? 301 SAM D C2    1 
HETATM 8927 N N3    . SAM I 2 .   ? 7.243   -28.964 25.665  1.00 54.08  ? 301 SAM D N3    1 
HETATM 8928 C C4    . SAM I 2 .   ? 7.657   -30.142 25.174  1.00 52.83  ? 301 SAM D C4    1 
HETATM 8929 O O     . HOH J 4 .   ? 15.507  19.195  22.711  1.00 33.58  ? 401 HOH A O     1 
HETATM 8930 O O     . HOH J 4 .   ? -9.112  38.327  22.253  1.00 43.50  ? 402 HOH A O     1 
HETATM 8931 O O     . HOH J 4 .   ? 17.990  35.377  11.733  1.00 45.97  ? 403 HOH A O     1 
HETATM 8932 O O     . HOH J 4 .   ? 10.069  26.771  33.272  1.00 40.77  ? 404 HOH A O     1 
HETATM 8933 O O     . HOH J 4 .   ? -9.173  17.092  24.382  1.00 34.59  ? 405 HOH A O     1 
HETATM 8934 O O     . HOH J 4 .   ? -6.142  46.725  26.268  1.00 52.59  ? 406 HOH A O     1 
HETATM 8935 O O     . HOH J 4 .   ? -16.303 14.748  13.462  1.00 33.49  ? 407 HOH A O     1 
HETATM 8936 O O     . HOH J 4 .   ? 0.832   28.153  32.427  1.00 39.88  ? 408 HOH A O     1 
HETATM 8937 O O     . HOH J 4 .   ? -1.313  30.181  27.669  1.00 38.51  ? 409 HOH A O     1 
HETATM 8938 O O     . HOH J 4 .   ? 8.373   14.738  28.938  1.00 32.91  ? 410 HOH A O     1 
HETATM 8939 O O     . HOH J 4 .   ? 6.235   4.823   8.041   1.00 27.54  ? 411 HOH A O     1 
HETATM 8940 O O     . HOH J 4 .   ? -10.691 17.809  28.724  1.00 35.41  ? 412 HOH A O     1 
HETATM 8941 O O     . HOH J 4 .   ? 9.917   20.325  34.653  1.00 38.42  ? 413 HOH A O     1 
HETATM 8942 O O     . HOH J 4 .   ? -0.022  15.244  31.565  1.00 33.85  ? 414 HOH A O     1 
HETATM 8943 O O     . HOH K 4 .   ? 27.366  -10.115 19.543  1.00 40.76  ? 401 HOH B O     1 
HETATM 8944 O O     . HOH K 4 .   ? 39.084  -4.860  20.601  1.00 49.47  ? 402 HOH B O     1 
HETATM 8945 O O     . HOH K 4 .   ? 12.087  -19.209 2.770   1.00 40.22  ? 403 HOH B O     1 
HETATM 8946 O O     . HOH K 4 .   ? 15.216  -12.326 -8.130  1.00 40.55  ? 404 HOH B O     1 
HETATM 8947 O O     . HOH K 4 .   ? 40.758  -9.104  17.362  1.00 52.07  ? 405 HOH B O     1 
HETATM 8948 O O     . HOH K 4 .   ? 28.285  -6.903  22.416  1.00 40.83  ? 406 HOH B O     1 
HETATM 8949 O O     . HOH K 4 .   ? 4.679   -4.051  -2.865  1.00 32.28  ? 407 HOH B O     1 
HETATM 8950 O O     . HOH K 4 .   ? 13.286  -14.493 -5.385  1.00 40.11  ? 408 HOH B O     1 
HETATM 8951 O O     . HOH K 4 .   ? 15.931  -14.566 -12.408 1.00 44.79  ? 409 HOH B O     1 
HETATM 8952 O O     . HOH K 4 .   ? 31.376  -9.735  23.635  1.00 44.70  ? 410 HOH B O     1 
HETATM 8953 O O     . HOH L 4 .   ? -44.041 21.035  -14.680 1.00 70.41  ? 401 HOH C O     1 
HETATM 8954 O O     . HOH M 4 .   ? 28.413  -37.979 7.920   1.00 65.24  ? 401 HOH D O     1 
HETATM 8955 O O     . HOH M 4 .   ? 27.260  -36.482 19.606  1.00 69.66  ? 402 HOH D O     1 
HETATM 8956 O O     . HOH M 4 .   ? 5.999   -12.114 4.353   1.00 34.16  ? 403 HOH D O     1 
HETATM 8957 O O     . HOH M 4 .   ? 16.741  -35.808 29.083  1.00 57.41  ? 404 HOH D O     1 
HETATM 8958 O O     . HOH M 4 .   ? 4.623   -11.316 31.847  1.00 40.39  ? 405 HOH D O     1 
HETATM 8959 O O     . HOH M 4 .   ? 7.144   -28.839 34.551  1.00 50.11  ? 406 HOH D O     1 
HETATM 8960 O O     . HOH M 4 .   ? -9.230  -10.381 9.394   1.00 35.07  ? 407 HOH D O     1 
HETATM 8961 O O     . HOH M 4 .   ? 4.856   -27.672 39.448  1.00 51.39  ? 408 HOH D O     1 
HETATM 8962 O O     . HOH M 4 .   ? -11.284 -17.609 30.961  1.00 42.94  ? 409 HOH D O     1 
HETATM 8963 O O     . HOH M 4 .   ? -5.644  -16.196 36.004  1.00 49.17  ? 410 HOH D O     1 
HETATM 8964 O O     . HOH M 4 .   ? -3.889  -16.294 40.754  1.00 44.72  ? 411 HOH D O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N     . GLU A 42  ? 0.8733 0.4414 0.6051 0.2254  -0.1254 -0.0451 14  GLU A N     
2    C CA    . GLU A 42  ? 0.9103 0.4601 0.6370 0.2135  -0.1353 -0.0392 14  GLU A CA    
3    C C     . GLU A 42  ? 0.9919 0.5140 0.6992 0.2122  -0.1393 -0.0468 14  GLU A C     
4    O O     . GLU A 42  ? 1.0252 0.5432 0.7236 0.2208  -0.1337 -0.0562 14  GLU A O     
5    C CB    . GLU A 42  ? 0.9856 0.5361 0.7253 0.2088  -0.1422 -0.0272 14  GLU A CB    
6    C CG    . GLU A 42  ? 0.9677 0.5117 0.7100 0.1953  -0.1506 -0.0181 14  GLU A CG    
7    C CD    . GLU A 42  ? 0.9474 0.4808 0.6959 0.1896  -0.1587 -0.0092 14  GLU A CD    
8    O OE1   . GLU A 42  ? 0.9688 0.5089 0.7258 0.1956  -0.1566 -0.0061 14  GLU A OE1   
9    O OE2   . GLU A 42  ? 0.9054 0.4240 0.6503 0.1791  -0.1671 -0.0051 14  GLU A OE2   
10   N N     . ALA A 43  ? 1.0720 0.5764 0.7730 0.2013  -0.1491 -0.0426 15  ALA A N     
11   C CA    . ALA A 43  ? 1.1000 0.5768 0.7814 0.1982  -0.1548 -0.0492 15  ALA A CA    
12   C C     . ALA A 43  ? 1.0883 0.5637 0.7542 0.2028  -0.1473 -0.0608 15  ALA A C     
13   O O     . ALA A 43  ? 1.0839 0.5655 0.7474 0.1986  -0.1456 -0.0612 15  ALA A O     
14   C CB    . ALA A 43  ? 1.0840 0.5455 0.7621 0.2028  -0.1573 -0.0508 15  ALA A CB    
15   N N     . TYR A 44  ? 1.0308 0.4988 0.6865 0.2114  -0.1422 -0.0699 16  TYR A N     
16   C CA    . TYR A 44  ? 1.1156 0.5852 0.7579 0.2161  -0.1334 -0.0805 16  TYR A CA    
17   C C     . TYR A 44  ? 1.1328 0.6317 0.7882 0.2219  -0.1221 -0.0813 16  TYR A C     
18   O O     . TYR A 44  ? 1.1365 0.6508 0.8032 0.2310  -0.1158 -0.0818 16  TYR A O     
19   C CB    . TYR A 44  ? 1.0995 0.5560 0.7298 0.2241  -0.1301 -0.0887 16  TYR A CB    
20   C CG    . TYR A 44  ? 1.1209 0.5474 0.7379 0.2189  -0.1410 -0.0886 16  TYR A CG    
21   C CD1   . TYR A 44  ? 1.0669 0.4791 0.6803 0.2065  -0.1530 -0.0828 16  TYR A CD1   
22   C CD2   . TYR A 44  ? 1.1915 0.6040 0.7997 0.2261  -0.1392 -0.0941 16  TYR A CD2   
23   C CE1   . TYR A 44  ? 1.1263 0.5115 0.7279 0.2009  -0.1633 -0.0830 16  TYR A CE1   
24   C CE2   . TYR A 44  ? 1.2265 0.6109 0.8221 0.2212  -0.1490 -0.0944 16  TYR A CE2   
25   C CZ    . TYR A 44  ? 1.2405 0.6113 0.8327 0.2083  -0.1613 -0.0890 16  TYR A CZ    
26   O OH    . TYR A 44  ? 1.2646 0.6076 0.8444 0.2025  -0.1714 -0.0896 16  TYR A OH    
27   N N     . ARG A 45  ? 1.0120 0.5185 0.6659 0.2166  -0.1200 -0.0811 17  ARG A N     
28   C CA    . ARG A 45  ? 0.9288 0.4623 0.5960 0.2196  -0.1108 -0.0804 17  ARG A CA    
29   C C     . ARG A 45  ? 0.9633 0.5111 0.6509 0.2201  -0.1138 -0.0706 17  ARG A C     
30   O O     . ARG A 45  ? 1.0226 0.5593 0.7137 0.2152  -0.1237 -0.0628 17  ARG A O     
31   C CB    . ARG A 45  ? 0.9711 0.5194 0.6379 0.2294  -0.0979 -0.0896 17  ARG A CB    
32   C CG    . ARG A 45  ? 1.0856 0.6255 0.7339 0.2284  -0.0925 -0.0983 17  ARG A CG    
33   C CD    . ARG A 45  ? 1.0120 0.5420 0.6503 0.2181  -0.0974 -0.0962 17  ARG A CD    
34   N NE    . ARG A 45  ? 0.9545 0.4824 0.5772 0.2174  -0.0901 -0.1038 17  ARG A NE    
35   C CZ    . ARG A 45  ? 1.0101 0.5309 0.6218 0.2097  -0.0922 -0.1034 17  ARG A CZ    
36   N NH1   . ARG A 45  ? 1.0125 0.5290 0.6283 0.2017  -0.1011 -0.0956 17  ARG A NH1   
37   N NH2   . ARG A 45  ? 1.0302 0.5501 0.6277 0.2097  -0.0849 -0.1099 17  ARG A NH2   
38   N N     . GLY A 46  ? 0.9377 0.5131 0.6395 0.2242  -0.1051 -0.0702 18  GLY A N     
39   C CA    . GLY A 46  ? 0.7970 0.3902 0.5182 0.2234  -0.1070 -0.0606 18  GLY A CA    
40   C C     . GLY A 46  ? 0.7427 0.3486 0.4729 0.2357  -0.1021 -0.0629 18  GLY A C     
41   O O     . GLY A 46  ? 0.8378 0.4313 0.5634 0.2414  -0.1041 -0.0653 18  GLY A O     
42   N N     . ILE A 47  ? 0.6994 0.3353 0.4446 0.2366  -0.0949 -0.0615 19  ILE A N     
43   C CA    . ILE A 47  ? 0.7165 0.3696 0.4722 0.2477  -0.0901 -0.0633 19  ILE A CA    
44   C C     . ILE A 47  ? 0.7321 0.3962 0.4841 0.2537  -0.0792 -0.0745 19  ILE A C     
45   O O     . ILE A 47  ? 0.7378 0.4240 0.4963 0.2495  -0.0716 -0.0764 19  ILE A O     
46   C CB    . ILE A 47  ? 0.6698 0.3495 0.4438 0.2450  -0.0894 -0.0552 19  ILE A CB    
47   C CG1   . ILE A 47  ? 0.7307 0.3999 0.5078 0.2373  -0.0992 -0.0435 19  ILE A CG1   
48   C CG2   . ILE A 47  ? 0.6677 0.3638 0.4521 0.2567  -0.0863 -0.0563 19  ILE A CG2   
49   C CD1   . ILE A 47  ? 0.8136 0.4602 0.5869 0.2430  -0.1077 -0.0397 19  ILE A CD1   
50   N N     . ASP A 48  ? 0.7925 0.4425 0.5347 0.2623  -0.0777 -0.0813 20  ASP A N     
51   C CA    . ASP A 48  ? 0.7649 0.4291 0.5066 0.2688  -0.0666 -0.0907 20  ASP A CA    
52   C C     . ASP A 48  ? 0.8253 0.5176 0.5851 0.2776  -0.0620 -0.0899 20  ASP A C     
53   O O     . ASP A 48  ? 0.8530 0.5526 0.6240 0.2787  -0.0675 -0.0823 20  ASP A O     
54   C CB    . ASP A 48  ? 0.7948 0.4398 0.5225 0.2725  -0.0657 -0.0965 20  ASP A CB    
55   C CG    . ASP A 48  ? 0.8814 0.5091 0.6083 0.2758  -0.0742 -0.0917 20  ASP A CG    
56   O OD1   . ASP A 48  ? 0.9199 0.5556 0.6595 0.2771  -0.0790 -0.0840 20  ASP A OD1   
57   O OD2   . ASP A 48  ? 0.9817 0.5876 0.6946 0.2768  -0.0758 -0.0955 20  ASP A OD2   
58   N N     . LYS A 49  ? 0.8144 0.5235 0.5772 0.2836  -0.0518 -0.0976 21  LYS A N     
59   C CA    . LYS A 49  ? 0.8625 0.6018 0.6430 0.2914  -0.0466 -0.0980 21  LYS A CA    
60   C C     . LYS A 49  ? 0.7619 0.5231 0.5553 0.2832  -0.0472 -0.0925 21  LYS A C     
61   O O     . LYS A 49  ? 0.6690 0.4386 0.4730 0.2840  -0.0530 -0.0850 21  LYS A O     
62   C CB    . LYS A 49  ? 0.7951 0.5329 0.5821 0.3004  -0.0515 -0.0937 21  LYS A CB    
63   N N     . PRO A 50  ? 0.7076 0.4790 0.5003 0.2734  -0.0411 -0.0953 22  PRO A N     
64   C CA    . PRO A 50  ? 0.6240 0.4166 0.4288 0.2638  -0.0410 -0.0899 22  PRO A CA    
65   C C     . PRO A 50  ? 0.6312 0.4561 0.4535 0.2684  -0.0367 -0.0907 22  PRO A C     
66   O O     . PRO A 50  ? 0.6027 0.4438 0.4352 0.2624  -0.0385 -0.0853 22  PRO A O     
67   C CB    . PRO A 50  ? 0.6184 0.4104 0.4158 0.2537  -0.0345 -0.0939 22  PRO A CB    
68   C CG    . PRO A 50  ? 0.7392 0.5239 0.5268 0.2605  -0.0275 -0.1032 22  PRO A CG    
69   C CD    . PRO A 50  ? 0.7696 0.5321 0.5493 0.2708  -0.0339 -0.1031 22  PRO A CD    
70   N N     . HIS A 51  ? 0.7030 0.5381 0.5292 0.2789  -0.0310 -0.0972 23  HIS A N     
71   C CA    . HIS A 51  ? 0.6730 0.5404 0.5168 0.2835  -0.0276 -0.0979 23  HIS A CA    
72   C C     . HIS A 51  ? 0.6638 0.5357 0.5162 0.2876  -0.0366 -0.0894 23  HIS A C     
73   O O     . HIS A 51  ? 0.6712 0.5672 0.5361 0.2843  -0.0370 -0.0863 23  HIS A O     
74   C CB    . HIS A 51  ? 0.6960 0.5718 0.5425 0.2954  -0.0205 -0.1055 23  HIS A CB    
75   C CG    . HIS A 51  ? 0.7733 0.6639 0.6211 0.2907  -0.0092 -0.1133 23  HIS A CG    
76   N ND1   . HIS A 51  ? 0.7971 0.6721 0.6313 0.2818  -0.0053 -0.1163 23  HIS A ND1   
77   C CD2   . HIS A 51  ? 0.7927 0.7126 0.6541 0.2936  -0.0010 -0.1183 23  HIS A CD2   
78   C CE1   . HIS A 51  ? 0.7968 0.6899 0.6356 0.2794  0.0052  -0.1227 23  HIS A CE1   
79   N NE2   . HIS A 51  ? 0.8233 0.7440 0.6790 0.2861  0.0080  -0.1241 23  HIS A NE2   
80   N N     . LEU A 52  ? 0.6740 0.5218 0.5188 0.2947  -0.0438 -0.0855 24  LEU A N     
81   C CA    . LEU A 52  ? 0.6175 0.4673 0.4694 0.2992  -0.0522 -0.0767 24  LEU A CA    
82   C C     . LEU A 52  ? 0.6041 0.4526 0.4567 0.2875  -0.0577 -0.0683 24  LEU A C     
83   O O     . LEU A 52  ? 0.6790 0.5377 0.5399 0.2893  -0.0629 -0.0609 24  LEU A O     
84   C CB    . LEU A 52  ? 0.6416 0.4631 0.4842 0.3092  -0.0581 -0.0747 24  LEU A CB    
85   C CG    . LEU A 52  ? 0.6572 0.4804 0.5002 0.3221  -0.0530 -0.0813 24  LEU A CG    
86   C CD1   . LEU A 52  ? 0.7547 0.5508 0.5890 0.3254  -0.0587 -0.0773 24  LEU A CD1   
87   C CD2   . LEU A 52  ? 0.6792 0.5365 0.5401 0.3304  -0.0501 -0.0814 24  LEU A CD2   
88   N N     . TYR A 53  ? 0.5998 0.4367 0.4439 0.2761  -0.0565 -0.0689 25  TYR A N     
89   C CA    . TYR A 53  ? 0.5885 0.4231 0.4333 0.2657  -0.0615 -0.0604 25  TYR A CA    
90   C C     . TYR A 53  ? 0.5937 0.4567 0.4491 0.2587  -0.0568 -0.0604 25  TYR A C     
91   O O     . TYR A 53  ? 0.6075 0.4769 0.4678 0.2546  -0.0610 -0.0527 25  TYR A O     
92   C CB    . TYR A 53  ? 0.5961 0.4059 0.4278 0.2567  -0.0629 -0.0600 25  TYR A CB    
93   C CG    . TYR A 53  ? 0.5969 0.3996 0.4292 0.2480  -0.0696 -0.0498 25  TYR A CG    
94   C CD1   . TYR A 53  ? 0.6239 0.4065 0.4529 0.2501  -0.0786 -0.0421 25  TYR A CD1   
95   C CD2   . TYR A 53  ? 0.6121 0.4280 0.4484 0.2379  -0.0664 -0.0475 25  TYR A CD2   
96   C CE1   . TYR A 53  ? 0.6359 0.4134 0.4666 0.2422  -0.0841 -0.0321 25  TYR A CE1   
97   C CE2   . TYR A 53  ? 0.6414 0.4519 0.4789 0.2307  -0.0717 -0.0379 25  TYR A CE2   
98   C CZ    . TYR A 53  ? 0.6296 0.4217 0.4647 0.2328  -0.0805 -0.0300 25  TYR A CZ    
99   O OH    . TYR A 53  ? 0.6359 0.4240 0.4733 0.2256  -0.0852 -0.0198 25  TYR A OH    
100  N N     . THR A 54  ? 0.5672 0.4471 0.4258 0.2572  -0.0481 -0.0689 26  THR A N     
101  C CA    . THR A 54  ? 0.5413 0.4477 0.4097 0.2504  -0.0438 -0.0697 26  THR A CA    
102  C C     . THR A 54  ? 0.5587 0.4877 0.4395 0.2567  -0.0468 -0.0668 26  THR A C     
103  O O     . THR A 54  ? 0.6885 0.6389 0.5767 0.2511  -0.0448 -0.0667 26  THR A O     
104  C CB    . THR A 54  ? 0.5370 0.4559 0.4065 0.2473  -0.0337 -0.0795 26  THR A CB    
105  O OG1   . THR A 54  ? 0.5945 0.5149 0.4649 0.2579  -0.0307 -0.0856 26  THR A OG1   
106  C CG2   . THR A 54  ? 0.5549 0.4558 0.4127 0.2380  -0.0304 -0.0810 26  THR A CG2   
107  N N     . LEU A 55  ? 0.5481 0.4725 0.4304 0.2684  -0.0517 -0.0644 27  LEU A N     
108  C CA    . LEU A 55  ? 0.5575 0.5013 0.4505 0.2749  -0.0560 -0.0598 27  LEU A CA    
109  C C     . LEU A 55  ? 0.5954 0.5377 0.4881 0.2688  -0.0619 -0.0501 27  LEU A C     
110  O O     . LEU A 55  ? 0.6750 0.6380 0.5759 0.2703  -0.0641 -0.0469 27  LEU A O     
111  C CB    . LEU A 55  ? 0.5645 0.4990 0.4576 0.2892  -0.0602 -0.0582 27  LEU A CB    
112  C CG    . LEU A 55  ? 0.5695 0.5108 0.4653 0.2978  -0.0539 -0.0673 27  LEU A CG    
113  C CD1   . LEU A 55  ? 0.5971 0.5231 0.4906 0.3121  -0.0581 -0.0652 27  LEU A CD1   
114  C CD2   . LEU A 55  ? 0.5568 0.5344 0.4673 0.2985  -0.0492 -0.0719 27  LEU A CD2   
115  N N     . GLY A 56  ? 0.5695 0.4884 0.4529 0.2620  -0.0645 -0.0453 28  GLY A N     
116  C CA    . GLY A 56  ? 0.5627 0.4797 0.4457 0.2552  -0.0687 -0.0361 28  GLY A CA    
117  C C     . GLY A 56  ? 0.6048 0.5285 0.4867 0.2429  -0.0635 -0.0378 28  GLY A C     
118  O O     . GLY A 56  ? 0.6245 0.5463 0.5057 0.2371  -0.0660 -0.0303 28  GLY A O     
119  N N     . CYS A 57  ? 0.5730 0.5039 0.4547 0.2390  -0.0559 -0.0472 29  CYS A N     
120  C CA    . CYS A 57  ? 0.6264 0.5644 0.5074 0.2278  -0.0503 -0.0493 29  CYS A CA    
121  C C     . CYS A 57  ? 0.7088 0.6679 0.5964 0.2248  -0.0506 -0.0463 29  CYS A C     
122  O O     . CYS A 57  ? 0.6954 0.6506 0.5805 0.2182  -0.0514 -0.0403 29  CYS A O     
123  C CB    . CYS A 57  ? 0.7460 0.6917 0.6272 0.2253  -0.0417 -0.0601 29  CYS A CB    
124  S SG    . CYS A 57  ? 0.8393 0.7918 0.7189 0.2118  -0.0339 -0.0632 29  CYS A SG    
125  N N     . CYS A 58  ? 0.8159 0.7978 0.7119 0.2300  -0.0501 -0.0503 30  CYS A N     
126  C CA    . CYS A 58  ? 0.7963 0.7998 0.6977 0.2271  -0.0506 -0.0488 30  CYS A CA    
127  C C     . CYS A 58  ? 0.7395 0.7366 0.6383 0.2277  -0.0571 -0.0376 30  CYS A C     
128  O O     . CYS A 58  ? 0.7331 0.7439 0.6331 0.2239  -0.0570 -0.0356 30  CYS A O     
129  C CB    . CYS A 58  ? 0.8632 0.8914 0.7744 0.2343  -0.0512 -0.0536 30  CYS A CB    
130  S SG    . CYS A 58  ? 1.3104 1.3504 1.2276 0.2357  -0.0435 -0.0661 30  CYS A SG    
131  N N     . SER A 59  ? 0.8057 0.7816 0.7003 0.2321  -0.0624 -0.0303 31  SER A N     
132  C CA    . SER A 59  ? 0.6636 0.6310 0.5557 0.2320  -0.0681 -0.0188 31  SER A CA    
133  C C     . SER A 59  ? 0.5275 0.4731 0.4131 0.2246  -0.0678 -0.0137 31  SER A C     
134  O O     . SER A 59  ? 0.4860 0.4324 0.3704 0.2189  -0.0675 -0.0075 31  SER A O     
135  C CB    . SER A 59  ? 0.5972 0.5581 0.4909 0.2430  -0.0755 -0.0127 31  SER A CB    
136  O OG    . SER A 59  ? 0.6061 0.5895 0.5065 0.2502  -0.0768 -0.0149 31  SER A OG    
137  N N     . LEU A 60  ? 0.6385 0.5648 0.5198 0.2248  -0.0680 -0.0161 32  LEU A N     
138  C CA    . LEU A 60  ? 0.5217 0.4279 0.3972 0.2176  -0.0685 -0.0113 32  LEU A CA    
139  C C     . LEU A 60  ? 0.5844 0.4970 0.4587 0.2080  -0.0615 -0.0146 32  LEU A C     
140  O O     . LEU A 60  ? 0.5233 0.4259 0.3950 0.2017  -0.0617 -0.0082 32  LEU A O     
141  C CB    . LEU A 60  ? 0.5365 0.4213 0.4063 0.2198  -0.0704 -0.0145 32  LEU A CB    
142  C CG    . LEU A 60  ? 0.5255 0.3960 0.3942 0.2284  -0.0780 -0.0100 32  LEU A CG    
143  C CD1   . LEU A 60  ? 0.5380 0.3874 0.3991 0.2299  -0.0787 -0.0154 32  LEU A CD1   
144  C CD2   . LEU A 60  ? 0.5284 0.3888 0.3975 0.2263  -0.0844 0.0028  32  LEU A CD2   
145  N N     . THR A 61  ? 0.5996 0.5284 0.4760 0.2066  -0.0550 -0.0243 33  THR A N     
146  C CA    . THR A 61  ? 0.5923 0.5271 0.4673 0.1976  -0.0479 -0.0276 33  THR A CA    
147  C C     . THR A 61  ? 0.6029 0.5461 0.4792 0.1943  -0.0481 -0.0207 33  THR A C     
148  O O     . THR A 61  ? 0.6097 0.5458 0.4831 0.1878  -0.0455 -0.0167 33  THR A O     
149  C CB    . THR A 61  ? 0.5963 0.5481 0.4743 0.1967  -0.0412 -0.0391 33  THR A CB    
150  O OG1   . THR A 61  ? 0.6848 0.6280 0.5606 0.1997  -0.0398 -0.0452 33  THR A OG1   
151  C CG2   . THR A 61  ? 0.6172 0.5740 0.4933 0.1872  -0.0337 -0.0425 33  THR A CG2   
152  N N     . ALA A 62  ? 0.6098 0.5681 0.4903 0.1993  -0.0512 -0.0189 34  ALA A N     
153  C CA    . ALA A 62  ? 0.5661 0.5328 0.4464 0.1969  -0.0512 -0.0126 34  ALA A CA    
154  C C     . ALA A 62  ? 0.5980 0.5491 0.4764 0.1967  -0.0556 -0.0001 34  ALA A C     
155  O O     . ALA A 62  ? 0.6262 0.5787 0.5030 0.1923  -0.0533 0.0054  34  ALA A O     
156  C CB    . ALA A 62  ? 0.5736 0.5599 0.4579 0.2028  -0.0544 -0.0133 34  ALA A CB    
157  N N     . MET A 63  ? 0.5782 0.5141 0.4567 0.2012  -0.0617 0.0045  35  MET A N     
158  C CA    . MET A 63  ? 0.5507 0.4721 0.4285 0.2005  -0.0665 0.0168  35  MET A CA    
159  C C     . MET A 63  ? 0.5991 0.5090 0.4745 0.1923  -0.0632 0.0193  35  MET A C     
160  O O     . MET A 63  ? 0.6985 0.6088 0.5745 0.1887  -0.0621 0.0275  35  MET A O     
161  C CB    . MET A 63  ? 0.5578 0.4641 0.4358 0.2067  -0.0739 0.0201  35  MET A CB    
162  C CG    . MET A 63  ? 0.6003 0.4902 0.4781 0.2048  -0.0793 0.0327  35  MET A CG    
163  S SD    . MET A 63  ? 0.6447 0.5110 0.5205 0.2097  -0.0875 0.0344  35  MET A SD    
164  C CE    . MET A 63  ? 0.6567 0.5353 0.5347 0.2212  -0.0894 0.0299  35  MET A CE    
165  N N     . ALA A 64  ? 0.6057 0.5055 0.4784 0.1898  -0.0614 0.0126  36  ALA A N     
166  C CA    . ALA A 64  ? 0.5737 0.4633 0.4441 0.1824  -0.0585 0.0149  36  ALA A CA    
167  C C     . ALA A 64  ? 0.6094 0.5115 0.4794 0.1773  -0.0501 0.0119  36  ALA A C     
168  O O     . ALA A 64  ? 0.6274 0.5248 0.4970 0.1722  -0.0477 0.0175  36  ALA A O     
169  C CB    . ALA A 64  ? 0.6365 0.5126 0.5024 0.1812  -0.0585 0.0080  36  ALA A CB    
170  N N     . SER A 65  ? 0.6437 0.5619 0.5141 0.1785  -0.0458 0.0030  37  SER A N     
171  C CA    . SER A 65  ? 0.6661 0.5955 0.5353 0.1735  -0.0381 -0.0003 37  SER A CA    
172  C C     . SER A 65  ? 0.6914 0.6260 0.5614 0.1735  -0.0385 0.0090  37  SER A C     
173  O O     . SER A 65  ? 0.7582 0.6957 0.6260 0.1689  -0.0323 0.0095  37  SER A O     
174  C CB    . SER A 65  ? 0.6578 0.6038 0.5278 0.1745  -0.0345 -0.0117 37  SER A CB    
175  O OG    . SER A 65  ? 0.7067 0.6610 0.5745 0.1686  -0.0268 -0.0163 37  SER A OG    
176  N N     . ALA A 66  ? 0.6740 0.6091 0.5464 0.1788  -0.0452 0.0167  38  ALA A N     
177  C CA    . ALA A 66  ? 0.6396 0.5789 0.5123 0.1790  -0.0454 0.0267  38  ALA A CA    
178  C C     . ALA A 66  ? 0.6485 0.5733 0.5228 0.1762  -0.0469 0.0379  38  ALA A C     
179  O O     . ALA A 66  ? 0.7153 0.6424 0.5895 0.1737  -0.0431 0.0446  38  ALA A O     
180  C CB    . ALA A 66  ? 0.6271 0.5743 0.5013 0.1859  -0.0514 0.0306  38  ALA A CB    
181  N N     . GLN A 67  ? 0.6302 0.5403 0.5061 0.1765  -0.0525 0.0400  39  GLN A N     
182  C CA    . GLN A 67  ? 0.6451 0.5419 0.5235 0.1728  -0.0549 0.0502  39  GLN A CA    
183  C C     . GLN A 67  ? 0.6705 0.5657 0.5476 0.1668  -0.0479 0.0485  39  GLN A C     
184  O O     . GLN A 67  ? 0.7140 0.6083 0.5937 0.1641  -0.0459 0.0577  39  GLN A O     
185  C CB    . GLN A 67  ? 0.6691 0.5495 0.5478 0.1738  -0.0626 0.0509  39  GLN A CB    
186  C CG    . GLN A 67  ? 0.7339 0.6109 0.6146 0.1793  -0.0703 0.0566  39  GLN A CG    
187  C CD    . GLN A 67  ? 0.7163 0.5756 0.5955 0.1805  -0.0773 0.0549  39  GLN A CD    
188  O OE1   . GLN A 67  ? 0.7510 0.6006 0.6318 0.1830  -0.0843 0.0622  39  GLN A OE1   
189  N NE2   . GLN A 67  ? 0.6707 0.5246 0.5457 0.1787  -0.0751 0.0451  39  GLN A NE2   
190  N N     . LEU A 68  ? 0.6845 0.5794 0.5578 0.1650  -0.0438 0.0373  40  LEU A N     
191  C CA    . LEU A 68  ? 0.7146 0.6061 0.5860 0.1596  -0.0373 0.0357  40  LEU A CA    
192  C C     . LEU A 68  ? 0.8070 0.7097 0.6776 0.1581  -0.0293 0.0364  40  LEU A C     
193  O O     . LEU A 68  ? 0.8300 0.7291 0.7008 0.1547  -0.0246 0.0408  40  LEU A O     
194  C CB    . LEU A 68  ? 0.6570 0.5457 0.5238 0.1582  -0.0344 0.0235  40  LEU A CB    
195  C CG    . LEU A 68  ? 0.5997 0.4735 0.4649 0.1586  -0.0407 0.0228  40  LEU A CG    
196  C CD1   . LEU A 68  ? 0.6033 0.4759 0.4633 0.1577  -0.0365 0.0106  40  LEU A CD1   
197  C CD2   . LEU A 68  ? 0.6099 0.4712 0.4766 0.1547  -0.0437 0.0324  40  LEU A CD2   
198  N N     . ASP A 69  ? 0.7563 0.6722 0.6254 0.1609  -0.0276 0.0323  41  ASP A N     
199  C CA    . ASP A 69  ? 0.7723 0.6978 0.6388 0.1596  -0.0202 0.0323  41  ASP A CA    
200  C C     . ASP A 69  ? 0.7946 0.7189 0.6640 0.1602  -0.0202 0.0458  41  ASP A C     
201  O O     . ASP A 69  ? 0.8326 0.7596 0.7000 0.1584  -0.0129 0.0477  41  ASP A O     
202  C CB    . ASP A 69  ? 0.8219 0.7622 0.6858 0.1623  -0.0199 0.0251  41  ASP A CB    
203  C CG    . ASP A 69  ? 0.8798 0.8247 0.7411 0.1602  -0.0167 0.0112  41  ASP A CG    
204  O OD1   . ASP A 69  ? 0.8712 0.8079 0.7314 0.1562  -0.0128 0.0070  41  ASP A OD1   
205  O OD2   . ASP A 69  ? 0.8653 0.8227 0.7262 0.1625  -0.0182 0.0048  41  ASP A OD2   
206  N N     . ALA A 70  ? 0.7521 0.6719 0.6263 0.1627  -0.0280 0.0554  42  ALA A N     
207  C CA    . ALA A 70  ? 0.7300 0.6493 0.6085 0.1630  -0.0280 0.0692  42  ALA A CA    
208  C C     . ALA A 70  ? 0.7847 0.6943 0.6674 0.1589  -0.0265 0.0755  42  ALA A C     
209  O O     . ALA A 70  ? 0.8503 0.7619 0.7364 0.1583  -0.0230 0.0854  42  ALA A O     
210  C CB    . ALA A 70  ? 0.6922 0.6094 0.5747 0.1664  -0.0368 0.0777  42  ALA A CB    
211  N N     . LEU A 71  ? 0.7985 0.6982 0.6810 0.1563  -0.0290 0.0703  43  LEU A N     
212  C CA    . LEU A 71  ? 0.7072 0.5978 0.5936 0.1524  -0.0290 0.0763  43  LEU A CA    
213  C C     . LEU A 71  ? 0.7050 0.5944 0.5869 0.1497  -0.0209 0.0689  43  LEU A C     
214  O O     . LEU A 71  ? 0.7481 0.6320 0.6331 0.1471  -0.0193 0.0748  43  LEU A O     
215  C CB    . LEU A 71  ? 0.6771 0.5551 0.5655 0.1511  -0.0387 0.0773  43  LEU A CB    
216  C CG    . LEU A 71  ? 0.7372 0.6120 0.6303 0.1531  -0.0477 0.0855  43  LEU A CG    
217  C CD1   . LEU A 71  ? 0.6687 0.5285 0.5616 0.1513  -0.0566 0.0846  43  LEU A CD1   
218  C CD2   . LEU A 71  ? 0.7913 0.6698 0.6922 0.1522  -0.0474 0.1002  43  LEU A CD2   
219  N N     . TRP A 72  ? 0.7357 0.6302 0.6107 0.1500  -0.0157 0.0566  44  TRP A N     
220  C CA    . TRP A 72  ? 0.7170 0.6078 0.5873 0.1469  -0.0087 0.0487  44  TRP A CA    
221  C C     . TRP A 72  ? 0.7667 0.6587 0.6373 0.1458  -0.0002 0.0540  44  TRP A C     
222  O O     . TRP A 72  ? 0.7605 0.6458 0.6295 0.1432  0.0041  0.0526  44  TRP A O     
223  C CB    . TRP A 72  ? 0.6785 0.5758 0.5426 0.1469  -0.0049 0.0348  44  TRP A CB    
224  C CG    . TRP A 72  ? 0.6415 0.5319 0.5013 0.1436  -0.0013 0.0261  44  TRP A CG    
225  C CD1   . TRP A 72  ? 0.6390 0.5284 0.4944 0.1405  0.0078  0.0210  44  TRP A CD1   
226  C CD2   . TRP A 72  ? 0.6552 0.5376 0.5139 0.1432  -0.0066 0.0220  44  TRP A CD2   
227  N NE1   . TRP A 72  ? 0.6441 0.5259 0.4960 0.1380  0.0087  0.0143  44  TRP A NE1   
228  C CE2   . TRP A 72  ? 0.6916 0.5694 0.5453 0.1397  0.0000  0.0146  44  TRP A CE2   
229  C CE3   . TRP A 72  ? 0.6553 0.5330 0.5160 0.1456  -0.0159 0.0236  44  TRP A CE3   
230  C CZ2   . TRP A 72  ? 0.7360 0.6055 0.5862 0.1387  -0.0022 0.0092  44  TRP A CZ2   
231  C CZ3   . TRP A 72  ? 0.6791 0.5480 0.5361 0.1447  -0.0181 0.0175  44  TRP A CZ3   
232  C CH2   . TRP A 72  ? 0.7047 0.5701 0.5564 0.1414  -0.0112 0.0105  44  TRP A CH2   
233  N N     . SER A 73  ? 0.7801 0.6801 0.6523 0.1481  0.0025  0.0603  45  SER A N     
234  C CA    . SER A 73  ? 0.7768 0.6776 0.6494 0.1481  0.0111  0.0660  45  SER A CA    
235  C C     . SER A 73  ? 0.7845 0.6791 0.6655 0.1472  0.0083  0.0784  45  SER A C     
236  O O     . SER A 73  ? 0.8179 0.7098 0.6994 0.1466  0.0150  0.0815  45  SER A O     
237  C CB    . SER A 73  ? 0.7639 0.6747 0.6351 0.1513  0.0147  0.0698  45  SER A CB    
238  O OG    . SER A 73  ? 0.8514 0.7652 0.7295 0.1534  0.0073  0.0805  45  SER A OG    
239  N N     . GLN A 74  ? 0.7397 0.6319 0.6275 0.1471  -0.0016 0.0857  46  GLN A N     
240  C CA    . GLN A 74  ? 0.7112 0.5985 0.6081 0.1454  -0.0059 0.0978  46  GLN A CA    
241  C C     . GLN A 74  ? 0.7142 0.5909 0.6097 0.1421  -0.0092 0.0942  46  GLN A C     
242  O O     . GLN A 74  ? 0.7119 0.5843 0.6146 0.1401  -0.0139 0.1036  46  GLN A O     
243  C CB    . GLN A 74  ? 0.7180 0.6059 0.6224 0.1457  -0.0156 0.1072  46  GLN A CB    
244  C CG    . GLN A 74  ? 0.7972 0.6953 0.7036 0.1490  -0.0128 0.1136  46  GLN A CG    
245  C CD    . GLN A 74  ? 0.8511 0.7483 0.7639 0.1491  -0.0226 0.1222  46  GLN A CD    
246  O OE1   . GLN A 74  ? 0.8346 0.7357 0.7440 0.1519  -0.0246 0.1198  46  GLN A OE1   
247  N NE2   . GLN A 74  ? 0.8288 0.7205 0.7510 0.1459  -0.0289 0.1324  46  GLN A NE2   
248  N N     . LEU A 75  ? 0.6435 0.5163 0.5301 0.1413  -0.0069 0.0811  47  LEU A N     
249  C CA    . LEU A 75  ? 0.7162 0.5785 0.5995 0.1384  -0.0096 0.0771  47  LEU A CA    
250  C C     . LEU A 75  ? 0.6819 0.5422 0.5622 0.1376  -0.0001 0.0760  47  LEU A C     
251  O O     . LEU A 75  ? 0.6737 0.5377 0.5482 0.1383  0.0091  0.0686  47  LEU A O     
252  C CB    . LEU A 75  ? 0.6550 0.5141 0.5305 0.1382  -0.0121 0.0640  47  LEU A CB    
253  C CG    . LEU A 75  ? 0.5557 0.4140 0.4331 0.1397  -0.0219 0.0642  47  LEU A CG    
254  C CD1   . LEU A 75  ? 0.5974 0.4562 0.4675 0.1408  -0.0215 0.0508  47  LEU A CD1   
255  C CD2   . LEU A 75  ? 0.5540 0.4017 0.4349 0.1375  -0.0318 0.0714  47  LEU A CD2   
256  N N     . SER A 76  ? 0.6620 0.5163 0.5462 0.1359  -0.0025 0.0836  48  SER A N     
257  C CA    . SER A 76  ? 0.6492 0.5000 0.5307 0.1356  0.0056  0.0838  48  SER A CA    
258  C C     . SER A 76  ? 0.6349 0.4752 0.5082 0.1330  0.0040  0.0759  48  SER A C     
259  O O     . SER A 76  ? 0.6282 0.4628 0.5009 0.1312  -0.0056 0.0754  48  SER A O     
260  C CB    . SER A 76  ? 0.7532 0.6058 0.6451 0.1362  0.0046  0.0986  48  SER A CB    
261  O OG    . SER A 76  ? 0.8924 0.7401 0.7893 0.1335  -0.0069 0.1049  48  SER A OG    
262  N N     . TRP A 77  ? 0.6759 0.5130 0.5422 0.1327  0.0136  0.0697  49  TRP A N     
263  C CA    . TRP A 77  ? 0.6555 0.4833 0.5124 0.1303  0.0141  0.0609  49  TRP A CA    
264  C C     . TRP A 77  ? 0.6254 0.4464 0.4800 0.1300  0.0200  0.0649  49  TRP A C     
265  O O     . TRP A 77  ? 0.6898 0.5136 0.5472 0.1320  0.0280  0.0695  49  TRP A O     
266  C CB    . TRP A 77  ? 0.6426 0.4728 0.4917 0.1296  0.0206  0.0470  49  TRP A CB    
267  C CG    . TRP A 77  ? 0.6079 0.4452 0.4589 0.1306  0.0149  0.0427  49  TRP A CG    
268  C CD1   . TRP A 77  ? 0.6046 0.4520 0.4595 0.1327  0.0163  0.0436  49  TRP A CD1   
269  C CD2   . TRP A 77  ? 0.6048 0.4393 0.4532 0.1302  0.0072  0.0370  49  TRP A CD2   
270  N NE1   . TRP A 77  ? 0.6317 0.4832 0.4872 0.1336  0.0095  0.0393  49  TRP A NE1   
271  C CE2   . TRP A 77  ? 0.6177 0.4611 0.4695 0.1323  0.0040  0.0351  49  TRP A CE2   
272  C CE3   . TRP A 77  ? 0.6201 0.4449 0.4628 0.1286  0.0028  0.0334  49  TRP A CE3   
273  C CZ2   . TRP A 77  ? 0.6345 0.4774 0.4851 0.1333  -0.0031 0.0299  49  TRP A CZ2   
274  C CZ3   . TRP A 77  ? 0.6372 0.4611 0.4780 0.1295  -0.0040 0.0277  49  TRP A CZ3   
275  C CH2   . TRP A 77  ? 0.6480 0.4808 0.4932 0.1320  -0.0068 0.0262  49  TRP A CH2   
276  N N     . PRO A 78  ? 0.6013 0.4128 0.4500 0.1280  0.0164  0.0632  50  PRO A N     
277  C CA    . PRO A 78  ? 0.6490 0.4535 0.4946 0.1279  0.0218  0.0671  50  PRO A CA    
278  C C     . PRO A 78  ? 0.6926 0.4934 0.5291 0.1274  0.0343  0.0574  50  PRO A C     
279  O O     . PRO A 78  ? 0.7303 0.5333 0.5619 0.1259  0.0374  0.0462  50  PRO A O     
280  C CB    . PRO A 78  ? 0.6451 0.4405 0.4855 0.1257  0.0127  0.0675  50  PRO A CB    
281  C CG    . PRO A 78  ? 0.6622 0.4576 0.4981 0.1244  0.0078  0.0575  50  PRO A CG    
282  C CD    . PRO A 78  ? 0.6417 0.4479 0.4857 0.1260  0.0072  0.0580  50  PRO A CD    
283  N N     . GLN A 79  ? 0.6658 0.4613 0.5008 0.1285  0.0414  0.0623  51  GLN A N     
284  C CA    . GLN A 79  ? 0.6831 0.4724 0.5091 0.1274  0.0535  0.0542  51  GLN A CA    
285  C C     . GLN A 79  ? 0.7212 0.5038 0.5370 0.1238  0.0530  0.0438  51  GLN A C     
286  O O     . GLN A 79  ? 0.7234 0.5091 0.5354 0.1216  0.0564  0.0327  51  GLN A O     
287  C CB    . GLN A 79  ? 0.7800 0.5623 0.6058 0.1299  0.0598  0.0628  51  GLN A CB    
288  C CG    . GLN A 79  ? 0.7205 0.5079 0.5529 0.1338  0.0671  0.0688  51  GLN A CG    
289  C CD    . GLN A 79  ? 0.7222 0.5089 0.5481 0.1328  0.0784  0.0581  51  GLN A CD    
290  O OE1   . GLN A 79  ? 0.7585 0.5517 0.5884 0.1352  0.0825  0.0594  51  GLN A OE1   
291  N NE2   . GLN A 79  ? 0.7066 0.4856 0.5223 0.1289  0.0834  0.0475  51  GLN A NE2   
292  N N     . THR A 80  ? 0.7284 0.5024 0.5395 0.1232  0.0488  0.0474  52  THR A N     
293  C CA    . THR A 80  ? 0.7239 0.4916 0.5249 0.1202  0.0473  0.0386  52  THR A CA    
294  C C     . THR A 80  ? 0.7573 0.5305 0.5610 0.1198  0.0367  0.0353  52  THR A C     
295  O O     . THR A 80  ? 0.7709 0.5451 0.5802 0.1210  0.0264  0.0434  52  THR A O     
296  C CB    . THR A 80  ? 0.7431 0.4998 0.5372 0.1200  0.0452  0.0441  52  THR A CB    
297  O OG1   . THR A 80  ? 0.7934 0.5443 0.5851 0.1211  0.0555  0.0477  52  THR A OG1   
298  C CG2   . THR A 80  ? 0.8190 0.5689 0.6014 0.1173  0.0446  0.0349  52  THR A CG2   
299  N N     . PRO A 81  ? 0.7310 0.5078 0.5313 0.1183  0.0388  0.0238  53  PRO A N     
300  C CA    . PRO A 81  ? 0.7101 0.4921 0.5135 0.1190  0.0293  0.0209  53  PRO A CA    
301  C C     . PRO A 81  ? 0.6887 0.4619 0.4867 0.1188  0.0195  0.0233  53  PRO A C     
302  O O     . PRO A 81  ? 0.7202 0.4839 0.5092 0.1176  0.0213  0.0230  53  PRO A O     
303  C CB    . PRO A 81  ? 0.6993 0.4864 0.4991 0.1175  0.0353  0.0079  53  PRO A CB    
304  C CG    . PRO A 81  ? 0.6840 0.4718 0.4824 0.1157  0.0475  0.0050  53  PRO A CG    
305  C CD    . PRO A 81  ? 0.7081 0.4858 0.5035 0.1159  0.0502  0.0136  53  PRO A CD    
306  N N     . LEU A 82  ? 0.5913 0.3672 0.3944 0.1200  0.0090  0.0257  54  LEU A N     
307  C CA    . LEU A 82  ? 0.5962 0.3633 0.3938 0.1198  -0.0015 0.0266  54  LEU A CA    
308  C C     . LEU A 82  ? 0.6027 0.3716 0.3979 0.1209  -0.0047 0.0171  54  LEU A C     
309  O O     . LEU A 82  ? 0.6187 0.3978 0.4201 0.1222  -0.0017 0.0130  54  LEU A O     
310  C CB    . LEU A 82  ? 0.5821 0.3489 0.3880 0.1199  -0.0123 0.0387  54  LEU A CB    
311  C CG    . LEU A 82  ? 0.5894 0.3549 0.3988 0.1194  -0.0110 0.0497  54  LEU A CG    
312  C CD1   . LEU A 82  ? 0.5703 0.3380 0.3901 0.1190  -0.0221 0.0616  54  LEU A CD1   
313  C CD2   . LEU A 82  ? 0.6559 0.4102 0.4529 0.1181  -0.0095 0.0484  54  LEU A CD2   
314  N N     . PRO A 83  ? 0.5099 0.2690 0.2956 0.1209  -0.0105 0.0133  55  PRO A N     
315  C CA    . PRO A 83  ? 0.5892 0.3493 0.3728 0.1230  -0.0134 0.0046  55  PRO A CA    
316  C C     . PRO A 83  ? 0.5740 0.3389 0.3675 0.1248  -0.0221 0.0093  55  PRO A C     
317  O O     . PRO A 83  ? 0.6545 0.4164 0.4531 0.1238  -0.0300 0.0191  55  PRO A O     
318  C CB    . PRO A 83  ? 0.6664 0.4124 0.4365 0.1228  -0.0185 0.0015  55  PRO A CB    
319  C CG    . PRO A 83  ? 0.6715 0.4108 0.4353 0.1202  -0.0153 0.0063  55  PRO A CG    
320  C CD    . PRO A 83  ? 0.6397 0.3861 0.4150 0.1193  -0.0139 0.0162  55  PRO A CD    
321  N N     . VAL A 84  ? 0.5376 0.3105 0.3345 0.1275  -0.0206 0.0025  56  VAL A N     
322  C CA    . VAL A 84  ? 0.4962 0.2738 0.3018 0.1298  -0.0279 0.0061  56  VAL A CA    
323  C C     . VAL A 84  ? 0.6915 0.4621 0.4913 0.1327  -0.0341 -0.0004 56  VAL A C     
324  O O     . VAL A 84  ? 0.6054 0.3761 0.3983 0.1344  -0.0289 -0.0103 56  VAL A O     
325  C CB    . VAL A 84  ? 0.4844 0.2778 0.2990 0.1312  -0.0214 0.0046  56  VAL A CB    
326  C CG1   . VAL A 84  ? 0.5391 0.3371 0.3605 0.1345  -0.0285 0.0066  56  VAL A CG1   
327  C CG2   . VAL A 84  ? 0.5274 0.3258 0.3478 0.1290  -0.0166 0.0125  56  VAL A CG2   
328  N N     . LEU A 85  ? 0.5695 0.3336 0.3720 0.1334  -0.0448 0.0054  57  LEU A N     
329  C CA    . LEU A 85  ? 0.5212 0.2748 0.3169 0.1363  -0.0518 0.0003  57  LEU A CA    
330  C C     . LEU A 85  ? 0.8120 0.5724 0.6160 0.1404  -0.0552 0.0006  57  LEU A C     
331  O O     . LEU A 85  ? 0.6175 0.3846 0.4317 0.1397  -0.0577 0.0090  57  LEU A O     
332  C CB    . LEU A 85  ? 0.5336 0.2709 0.3237 0.1334  -0.0626 0.0063  57  LEU A CB    
333  C CG    . LEU A 85  ? 0.5694 0.2921 0.3508 0.1360  -0.0709 0.0015  57  LEU A CG    
334  C CD1   . LEU A 85  ? 0.6436 0.3614 0.4119 0.1389  -0.0648 -0.0104 57  LEU A CD1   
335  C CD2   . LEU A 85  ? 0.5609 0.2686 0.3386 0.1317  -0.0826 0.0087  57  LEU A CD2   
336  N N     . ASP A 86  ? 0.6373 0.3960 0.4365 0.1452  -0.0548 -0.0083 58  ASP A N     
337  C CA    . ASP A 86  ? 0.6612 0.4240 0.4665 0.1501  -0.0589 -0.0084 58  ASP A CA    
338  C C     . ASP A 86  ? 0.6782 0.4236 0.4749 0.1531  -0.0671 -0.0113 58  ASP A C     
339  O O     . ASP A 86  ? 0.6600 0.3991 0.4466 0.1556  -0.0642 -0.0204 58  ASP A O     
340  C CB    . ASP A 86  ? 0.6978 0.4771 0.5070 0.1543  -0.0504 -0.0165 58  ASP A CB    
341  C CG    . ASP A 86  ? 0.8344 0.6197 0.6506 0.1599  -0.0546 -0.0155 58  ASP A CG    
342  O OD1   . ASP A 86  ? 0.8377 0.6166 0.6577 0.1597  -0.0628 -0.0070 58  ASP A OD1   
343  O OD2   . ASP A 86  ? 0.8436 0.6402 0.6618 0.1644  -0.0498 -0.0229 58  ASP A OD2   
344  N N     . ILE A 87  ? 0.7656 0.5025 0.5659 0.1526  -0.0769 -0.0036 59  ILE A N     
345  C CA    . ILE A 87  ? 0.5636 0.2810 0.3553 0.1546  -0.0858 -0.0054 59  ILE A CA    
346  C C     . ILE A 87  ? 0.6374 0.3573 0.4328 0.1619  -0.0872 -0.0081 59  ILE A C     
347  O O     . ILE A 87  ? 0.6948 0.4263 0.5015 0.1631  -0.0875 -0.0021 59  ILE A O     
348  C CB    . ILE A 87  ? 0.5701 0.2752 0.3633 0.1485  -0.0965 0.0050  59  ILE A CB    
349  C CG1   . ILE A 87  ? 0.5696 0.2717 0.3582 0.1421  -0.0957 0.0074  59  ILE A CG1   
350  C CG2   . ILE A 87  ? 0.6507 0.3347 0.4354 0.1502  -0.1064 0.0032  59  ILE A CG2   
351  C CD1   . ILE A 87  ? 0.5765 0.2693 0.3682 0.1356  -0.1062 0.0182  59  ILE A CD1   
352  N N     . GLY A 88  ? 0.6703 0.3790 0.4557 0.1673  -0.0878 -0.0169 60  GLY A N     
353  C CA    . GLY A 88  ? 0.6348 0.3459 0.4232 0.1756  -0.0883 -0.0202 60  GLY A CA    
354  C C     . GLY A 88  ? 0.6381 0.3733 0.4357 0.1794  -0.0790 -0.0238 60  GLY A C     
355  O O     . GLY A 88  ? 0.6812 0.4273 0.4887 0.1827  -0.0801 -0.0197 60  GLY A O     
356  N N     . CYS A 89  ? 0.6260 0.3698 0.4200 0.1787  -0.0699 -0.0315 61  CYS A N     
357  C CA    . CYS A 89  ? 0.6273 0.3947 0.4302 0.1802  -0.0609 -0.0351 61  CYS A CA    
358  C C     . CYS A 89  ? 0.6461 0.4222 0.4523 0.1892  -0.0589 -0.0414 61  CYS A C     
359  O O     . CYS A 89  ? 0.6370 0.4340 0.4523 0.1907  -0.0534 -0.0433 61  CYS A O     
360  C CB    . CYS A 89  ? 0.6451 0.4174 0.4430 0.1758  -0.0518 -0.0410 61  CYS A CB    
361  S SG    . CYS A 89  ? 0.6202 0.3799 0.4036 0.1797  -0.0482 -0.0521 61  CYS A SG    
362  N N     . GLY A 90  ? 0.6357 0.3966 0.4348 0.1954  -0.0634 -0.0447 62  GLY A N     
363  C CA    . GLY A 90  ? 0.6328 0.4014 0.4351 0.2051  -0.0613 -0.0506 62  GLY A CA    
364  C C     . GLY A 90  ? 0.6073 0.3902 0.4093 0.2069  -0.0508 -0.0606 62  GLY A C     
365  O O     . GLY A 90  ? 0.6382 0.4140 0.4309 0.2033  -0.0462 -0.0653 62  GLY A O     
366  N N     . PRO A 91  ? 0.6042 0.4084 0.4168 0.2124  -0.0467 -0.0636 63  PRO A N     
367  C CA    . PRO A 91  ? 0.5556 0.3764 0.3704 0.2135  -0.0364 -0.0727 63  PRO A CA    
368  C C     . PRO A 91  ? 0.5923 0.4276 0.4113 0.2041  -0.0298 -0.0727 63  PRO A C     
369  O O     . PRO A 91  ? 0.5498 0.4028 0.3739 0.2037  -0.0215 -0.0792 63  PRO A O     
370  C CB    . PRO A 91  ? 0.5533 0.3923 0.3794 0.2225  -0.0363 -0.0744 63  PRO A CB    
371  C CG    . PRO A 91  ? 0.5488 0.3877 0.3809 0.2226  -0.0446 -0.0649 63  PRO A CG    
372  C CD    . PRO A 91  ? 0.5640 0.3770 0.3864 0.2185  -0.0518 -0.0587 63  PRO A CD    
373  N N     . GLY A 92  ? 0.5972 0.4251 0.4146 0.1966  -0.0332 -0.0654 64  GLY A N     
374  C CA    . GLY A 92  ? 0.5522 0.3894 0.3714 0.1879  -0.0267 -0.0653 64  GLY A CA    
375  C C     . GLY A 92  ? 0.5334 0.3943 0.3647 0.1864  -0.0233 -0.0650 64  GLY A C     
376  O O     . GLY A 92  ? 0.5543 0.4268 0.3876 0.1811  -0.0153 -0.0692 64  GLY A O     
377  N N     . ASP A 93  ? 0.5448 0.4125 0.3836 0.1906  -0.0293 -0.0600 65  ASP A N     
378  C CA    . ASP A 93  ? 0.5431 0.4330 0.3919 0.1893  -0.0269 -0.0597 65  ASP A CA    
379  C C     . ASP A 93  ? 0.5450 0.4337 0.3948 0.1829  -0.0287 -0.0514 65  ASP A C     
380  O O     . ASP A 93  ? 0.5529 0.4551 0.4063 0.1777  -0.0232 -0.0529 65  ASP A O     
381  C CB    . ASP A 93  ? 0.5458 0.4463 0.4020 0.1982  -0.0318 -0.0591 65  ASP A CB    
382  C CG    . ASP A 93  ? 0.6456 0.5518 0.5030 0.2052  -0.0287 -0.0676 65  ASP A CG    
383  O OD1   . ASP A 93  ? 0.7200 0.6445 0.5828 0.2036  -0.0215 -0.0746 65  ASP A OD1   
384  O OD2   . ASP A 93  ? 0.6606 0.5528 0.5137 0.2124  -0.0332 -0.0671 65  ASP A OD2   
385  N N     . ILE A 94  ? 0.5355 0.4084 0.3825 0.1831  -0.0361 -0.0427 66  ILE A N     
386  C CA    . ILE A 94  ? 0.5161 0.3866 0.3639 0.1770  -0.0369 -0.0344 66  ILE A CA    
387  C C     . ILE A 94  ? 0.5500 0.4151 0.3924 0.1696  -0.0304 -0.0365 66  ILE A C     
388  O O     . ILE A 94  ? 0.5636 0.4349 0.4079 0.1644  -0.0263 -0.0339 66  ILE A O     
389  C CB    . ILE A 94  ? 0.5528 0.4072 0.3993 0.1784  -0.0463 -0.0244 66  ILE A CB    
390  C CG1   . ILE A 94  ? 0.5847 0.4474 0.4379 0.1842  -0.0516 -0.0195 66  ILE A CG1   
391  C CG2   . ILE A 94  ? 0.5819 0.4293 0.4277 0.1714  -0.0466 -0.0162 66  ILE A CG2   
392  C CD1   . ILE A 94  ? 0.6240 0.4704 0.4765 0.1859  -0.0608 -0.0100 66  ILE A CD1   
393  N N     . ALA A 95  ? 0.6086 0.4618 0.4434 0.1695  -0.0291 -0.0414 67  ALA A N     
394  C CA    . ALA A 95  ? 0.5048 0.3520 0.3335 0.1631  -0.0230 -0.0432 67  ALA A CA    
395  C C     . ALA A 95  ? 0.4787 0.3420 0.3103 0.1597  -0.0130 -0.0502 67  ALA A C     
396  O O     . ALA A 95  ? 0.5121 0.3759 0.3428 0.1536  -0.0079 -0.0486 67  ALA A O     
397  C CB    . ALA A 95  ? 0.5294 0.3602 0.3478 0.1643  -0.0240 -0.0472 67  ALA A CB    
398  N N     . ARG A 96  ? 0.4784 0.3552 0.3142 0.1634  -0.0101 -0.0580 68  ARG A N     
399  C CA    . ARG A 96  ? 0.4727 0.3650 0.3117 0.1594  -0.0008 -0.0654 68  ARG A CA    
400  C C     . ARG A 96  ? 0.5838 0.4931 0.4309 0.1576  -0.0001 -0.0642 68  ARG A C     
401  O O     . ARG A 96  ? 0.5927 0.5066 0.4396 0.1512  0.0062  -0.0655 68  ARG A O     
402  C CB    . ARG A 96  ? 0.4914 0.3920 0.3320 0.1638  0.0025  -0.0744 68  ARG A CB    
403  C CG    . ARG A 96  ? 0.5302 0.4524 0.3784 0.1606  0.0100  -0.0816 68  ARG A CG    
404  C CD    . ARG A 96  ? 0.6148 0.5345 0.4586 0.1519  0.0191  -0.0846 68  ARG A CD    
405  N NE    . ARG A 96  ? 0.7108 0.6501 0.5621 0.1471  0.0252  -0.0903 68  ARG A NE    
406  C CZ    . ARG A 96  ? 0.8424 0.7869 0.6935 0.1415  0.0344  -0.0970 68  ARG A CZ    
407  N NH1   . ARG A 96  ? 0.8802 0.8126 0.7236 0.1404  0.0392  -0.0989 68  ARG A NH1   
408  N NH2   . ARG A 96  ? 0.8797 0.8418 0.7380 0.1364  0.0387  -0.1018 68  ARG A NH2   
409  N N     . LYS A 97  ? 0.5876 0.5056 0.4408 0.1634  -0.0064 -0.0618 69  LYS A N     
410  C CA    . LYS A 97  ? 0.5229 0.4591 0.3829 0.1625  -0.0060 -0.0619 69  LYS A CA    
411  C C     . LYS A 97  ? 0.5001 0.4323 0.3595 0.1605  -0.0091 -0.0527 69  LYS A C     
412  O O     . LYS A 97  ? 0.5610 0.5063 0.4235 0.1584  -0.0074 -0.0530 69  LYS A O     
413  C CB    . LYS A 97  ? 0.5073 0.4569 0.3742 0.1703  -0.0109 -0.0638 69  LYS A CB    
414  C CG    . LYS A 97  ? 0.4911 0.4494 0.3608 0.1729  -0.0069 -0.0732 69  LYS A CG    
415  C CD    . LYS A 97  ? 0.5664 0.5374 0.4435 0.1820  -0.0123 -0.0739 69  LYS A CD    
416  C CE    . LYS A 97  ? 0.8062 0.7851 0.6865 0.1856  -0.0079 -0.0825 69  LYS A CE    
417  N NZ    . LYS A 97  ? 1.0325 1.0219 0.9200 0.1959  -0.0133 -0.0825 69  LYS A NZ    
418  N N     . VAL A 98  ? 0.5834 0.4982 0.4388 0.1609  -0.0135 -0.0446 70  VAL A N     
419  C CA    . VAL A 98  ? 0.4508 0.3627 0.3070 0.1595  -0.0165 -0.0348 70  VAL A CA    
420  C C     . VAL A 98  ? 0.5050 0.4039 0.3564 0.1537  -0.0129 -0.0308 70  VAL A C     
421  O O     . VAL A 98  ? 0.6197 0.5225 0.4710 0.1495  -0.0077 -0.0292 70  VAL A O     
422  C CB    . VAL A 98  ? 0.4550 0.3602 0.3132 0.1654  -0.0261 -0.0266 70  VAL A CB    
423  C CG1   . VAL A 98  ? 0.5169 0.4207 0.3768 0.1639  -0.0283 -0.0159 70  VAL A CG1   
424  C CG2   . VAL A 98  ? 0.4842 0.4017 0.3470 0.1721  -0.0296 -0.0301 70  VAL A CG2   
425  N N     . LEU A 99  ? 0.4910 0.3740 0.3379 0.1538  -0.0157 -0.0290 71  LEU A N     
426  C CA    . LEU A 99  ? 0.4567 0.3273 0.2995 0.1489  -0.0137 -0.0239 71  LEU A CA    
427  C C     . LEU A 99  ? 0.6174 0.4906 0.4567 0.1437  -0.0037 -0.0303 71  LEU A C     
428  O O     . LEU A 99  ? 0.5368 0.4098 0.3759 0.1399  0.0009  -0.0266 71  LEU A O     
429  C CB    . LEU A 99  ? 0.5044 0.3577 0.3421 0.1500  -0.0198 -0.0214 71  LEU A CB    
430  C CG    . LEU A 99  ? 0.4820 0.3276 0.3225 0.1531  -0.0301 -0.0126 71  LEU A CG    
431  C CD1   . LEU A 99  ? 0.5487 0.3766 0.3824 0.1536  -0.0359 -0.0126 71  LEU A CD1   
432  C CD2   . LEU A 99  ? 0.5343 0.3799 0.3791 0.1502  -0.0312 -0.0016 71  LEU A CD2   
433  N N     . ALA A 100 ? 0.5310 0.4063 0.3675 0.1436  0.0004  -0.0398 72  ALA A N     
434  C CA    . ALA A 100 ? 0.4577 0.3336 0.2904 0.1382  0.0101  -0.0457 72  ALA A CA    
435  C C     . ALA A 100 ? 0.5915 0.4795 0.4275 0.1344  0.0165  -0.0477 72  ALA A C     
436  O O     . ALA A 100 ? 0.6279 0.5104 0.4603 0.1296  0.0229  -0.0467 72  ALA A O     
437  C CB    . ALA A 100 ? 0.4622 0.3409 0.2927 0.1391  0.0135  -0.0555 72  ALA A CB    
438  N N     . PRO A 101 ? 0.5749 0.4785 0.4167 0.1363  0.0152  -0.0506 73  PRO A N     
439  C CA    . PRO A 101 ? 0.6051 0.5187 0.4482 0.1321  0.0211  -0.0530 73  PRO A CA    
440  C C     . PRO A 101 ? 0.6021 0.5096 0.4439 0.1313  0.0211  -0.0439 73  PRO A C     
441  O O     . PRO A 101 ? 0.6205 0.5313 0.4605 0.1273  0.0275  -0.0458 73  PRO A O     
442  C CB    . PRO A 101 ? 0.6312 0.5626 0.4804 0.1353  0.0174  -0.0570 73  PRO A CB    
443  C CG    . PRO A 101 ? 0.6304 0.5622 0.4817 0.1404  0.0128  -0.0598 73  PRO A CG    
444  C CD    . PRO A 101 ? 0.5977 0.5108 0.4445 0.1422  0.0089  -0.0528 73  PRO A CD    
445  N N     . ARG A 102 ? 0.6064 0.5052 0.4491 0.1348  0.0142  -0.0342 74  ARG A N     
446  C CA    . ARG A 102 ? 0.5543 0.4496 0.3976 0.1348  0.0139  -0.0245 74  ARG A CA    
447  C C     . ARG A 102 ? 0.5621 0.4428 0.4021 0.1323  0.0163  -0.0185 74  ARG A C     
448  O O     . ARG A 102 ? 0.6204 0.4988 0.4613 0.1319  0.0181  -0.0108 74  ARG A O     
449  C CB    . ARG A 102 ? 0.5575 0.4546 0.4056 0.1399  0.0047  -0.0163 74  ARG A CB    
450  C CG    . ARG A 102 ? 0.5991 0.5116 0.4502 0.1428  0.0027  -0.0195 74  ARG A CG    
451  C CD    . ARG A 102 ? 0.6285 0.5411 0.4838 0.1483  -0.0069 -0.0121 74  ARG A CD    
452  N NE    . ARG A 102 ? 0.6888 0.6163 0.5465 0.1515  -0.0087 -0.0136 74  ARG A NE    
453  C CZ    . ARG A 102 ? 0.7095 0.6479 0.5689 0.1537  -0.0101 -0.0217 74  ARG A CZ    
454  N NH1   . ARG A 102 ? 0.6366 0.5727 0.4958 0.1534  -0.0091 -0.0293 74  ARG A NH1   
455  N NH2   . ARG A 102 ? 0.7719 0.7242 0.6333 0.1566  -0.0124 -0.0220 74  ARG A NH2   
456  N N     . LEU A 103 ? 0.5809 0.4522 0.4170 0.1310  0.0166  -0.0215 75  LEU A N     
457  C CA    . LEU A 103 ? 0.5547 0.4126 0.3872 0.1288  0.0183  -0.0158 75  LEU A CA    
458  C C     . LEU A 103 ? 0.5947 0.4517 0.4235 0.1247  0.0290  -0.0188 75  LEU A C     
459  O O     . LEU A 103 ? 0.5581 0.4227 0.3856 0.1223  0.0352  -0.0278 75  LEU A O     
460  C CB    . LEU A 103 ? 0.5313 0.3792 0.3588 0.1288  0.0153  -0.0186 75  LEU A CB    
461  C CG    . LEU A 103 ? 0.4963 0.3399 0.3253 0.1328  0.0045  -0.0152 75  LEU A CG    
462  C CD1   . LEU A 103 ? 0.5325 0.3668 0.3543 0.1329  0.0033  -0.0209 75  LEU A CD1   
463  C CD2   . LEU A 103 ? 0.5242 0.3608 0.3565 0.1332  -0.0021 -0.0029 75  LEU A CD2   
464  N N     . PRO A 104 ? 0.5648 0.4124 0.3921 0.1237  0.0313  -0.0111 76  PRO A N     
465  C CA    . PRO A 104 ? 0.5100 0.3537 0.3327 0.1202  0.0418  -0.0137 76  PRO A CA    
466  C C     . PRO A 104 ? 0.5726 0.4117 0.3890 0.1167  0.0468  -0.0227 76  PRO A C     
467  O O     . PRO A 104 ? 0.6589 0.4951 0.4735 0.1176  0.0421  -0.0249 76  PRO A O     
468  C CB    . PRO A 104 ? 0.5210 0.3550 0.3443 0.1212  0.0413  -0.0022 76  PRO A CB    
469  C CG    . PRO A 104 ? 0.5570 0.3941 0.3872 0.1247  0.0313  0.0067  76  PRO A CG    
470  C CD    . PRO A 104 ? 0.6217 0.4628 0.4524 0.1259  0.0243  0.0009  76  PRO A CD    
471  N N     . ALA A 105 ? 0.5316 0.3695 0.3441 0.1128  0.0569  -0.0278 77  ALA A N     
472  C CA    . ALA A 105 ? 0.5265 0.3604 0.3333 0.1088  0.0631  -0.0360 77  ALA A CA    
473  C C     . ALA A 105 ? 0.5593 0.3791 0.3605 0.1093  0.0619  -0.0307 77  ALA A C     
474  O O     . ALA A 105 ? 0.5288 0.3404 0.3295 0.1108  0.0609  -0.0213 77  ALA A O     
475  C CB    . ALA A 105 ? 0.6083 0.4416 0.4120 0.1040  0.0742  -0.0415 77  ALA A CB    
476  N N     . GLY A 106 ? 0.5823 0.4001 0.3792 0.1081  0.0620  -0.0366 78  GLY A N     
477  C CA    . GLY A 106 ? 0.6476 0.4521 0.4372 0.1085  0.0605  -0.0326 78  GLY A CA    
478  C C     . GLY A 106 ? 0.6687 0.4694 0.4593 0.1127  0.0487  -0.0258 78  GLY A C     
479  O O     . GLY A 106 ? 0.6496 0.4389 0.4335 0.1130  0.0462  -0.0219 78  GLY A O     
480  N N     . THR A 107 ? 0.6376 0.4469 0.4358 0.1157  0.0413  -0.0242 79  THR A N     
481  C CA    . THR A 107 ? 0.6098 0.4148 0.4092 0.1191  0.0299  -0.0180 79  THR A CA    
482  C C     . THR A 107 ? 0.6563 0.4605 0.4516 0.1207  0.0262  -0.0253 79  THR A C     
483  O O     . THR A 107 ? 0.6659 0.4807 0.4651 0.1220  0.0270  -0.0324 79  THR A O     
484  C CB    . THR A 107 ? 0.5944 0.4078 0.4035 0.1217  0.0241  -0.0123 79  THR A CB    
485  O OG1   . THR A 107 ? 0.6232 0.4373 0.4356 0.1207  0.0285  -0.0055 79  THR A OG1   
486  C CG2   . THR A 107 ? 0.6098 0.4175 0.4205 0.1243  0.0122  -0.0054 79  THR A CG2   
487  N N     . ARG A 108 ? 0.6607 0.4524 0.4478 0.1210  0.0222  -0.0236 80  ARG A N     
488  C CA    . ARG A 108 ? 0.6486 0.4374 0.4299 0.1232  0.0190  -0.0304 80  ARG A CA    
489  C C     . ARG A 108 ? 0.6610 0.4490 0.4463 0.1271  0.0074  -0.0271 80  ARG A C     
490  O O     . ARG A 108 ? 0.6378 0.4211 0.4262 0.1271  0.0001  -0.0178 80  ARG A O     
491  C CB    . ARG A 108 ? 0.6547 0.4293 0.4233 0.1219  0.0199  -0.0305 80  ARG A CB    
492  C CG    . ARG A 108 ? 0.8134 0.5854 0.5741 0.1240  0.0208  -0.0395 80  ARG A CG    
493  C CD    . ARG A 108 ? 0.9833 0.7405 0.7295 0.1228  0.0216  -0.0391 80  ARG A CD    
494  N NE    . ARG A 108 ? 0.9675 0.7126 0.7098 0.1230  0.0112  -0.0302 80  ARG A NE    
495  C CZ    . ARG A 108 ? 0.8290 0.5611 0.5595 0.1243  0.0047  -0.0306 80  ARG A CZ    
496  N NH1   . ARG A 108 ? 0.7540 0.4825 0.4747 0.1263  0.0081  -0.0393 80  ARG A NH1   
497  N NH2   . ARG A 108 ? 0.7205 0.4431 0.4489 0.1235  -0.0055 -0.0221 80  ARG A NH2   
498  N N     . LEU A 109 ? 0.6983 0.4909 0.4841 0.1305  0.0059  -0.0344 81  LEU A N     
499  C CA    . LEU A 109 ? 0.6751 0.4668 0.4646 0.1347  -0.0042 -0.0322 81  LEU A CA    
500  C C     . LEU A 109 ? 0.6942 0.4734 0.4734 0.1374  -0.0089 -0.0364 81  LEU A C     
501  O O     . LEU A 109 ? 0.6926 0.4713 0.4649 0.1379  -0.0026 -0.0445 81  LEU A O     
502  C CB    . LEU A 109 ? 0.6211 0.4289 0.4201 0.1376  -0.0027 -0.0366 81  LEU A CB    
503  C CG    . LEU A 109 ? 0.5854 0.3932 0.3887 0.1427  -0.0122 -0.0347 81  LEU A CG    
504  C CD1   . LEU A 109 ? 0.6070 0.4086 0.4142 0.1418  -0.0206 -0.0233 81  LEU A CD1   
505  C CD2   . LEU A 109 ? 0.5477 0.3729 0.3598 0.1457  -0.0097 -0.0393 81  LEU A CD2   
506  N N     . VAL A 110 ? 0.7701 0.5388 0.5480 0.1389  -0.0198 -0.0308 82  VAL A N     
507  C CA    . VAL A 110 ? 0.5361 0.2907 0.3034 0.1417  -0.0257 -0.0346 82  VAL A CA    
508  C C     . VAL A 110 ? 0.5369 0.2917 0.3100 0.1463  -0.0340 -0.0335 82  VAL A C     
509  O O     . VAL A 110 ? 0.8680 0.6225 0.6485 0.1451  -0.0411 -0.0249 82  VAL A O     
510  C CB    . VAL A 110 ? 0.5470 0.2848 0.3044 0.1383  -0.0320 -0.0288 82  VAL A CB    
511  C CG1   . VAL A 110 ? 0.5689 0.2909 0.3134 0.1412  -0.0384 -0.0337 82  VAL A CG1   
512  C CG2   . VAL A 110 ? 0.5832 0.3208 0.3349 0.1343  -0.0237 -0.0289 82  VAL A CG2   
513  N N     . ALA A 111 ? 0.5532 0.3084 0.3232 0.1517  -0.0328 -0.0419 83  ALA A N     
514  C CA    . ALA A 111 ? 0.5757 0.3305 0.3505 0.1571  -0.0397 -0.0416 83  ALA A CA    
515  C C     . ALA A 111 ? 0.6293 0.3656 0.3913 0.1607  -0.0454 -0.0459 83  ALA A C     
516  O O     . ALA A 111 ? 0.6431 0.3759 0.3954 0.1627  -0.0396 -0.0541 83  ALA A O     
517  C CB    . ALA A 111 ? 0.5366 0.3103 0.3207 0.1616  -0.0334 -0.0474 83  ALA A CB    
518  N N     . CYS A 112 ? 0.6412 0.3651 0.4029 0.1615  -0.0563 -0.0405 84  CYS A N     
519  C CA    . CYS A 112 ? 0.6103 0.3136 0.3588 0.1645  -0.0628 -0.0443 84  CYS A CA    
520  C C     . CYS A 112 ? 0.6273 0.3276 0.3805 0.1707  -0.0689 -0.0441 84  CYS A C     
521  O O     . CYS A 112 ? 0.6579 0.3693 0.4243 0.1712  -0.0708 -0.0382 84  CYS A O     
522  C CB    . CYS A 112 ? 0.6205 0.3063 0.3608 0.1581  -0.0718 -0.0380 84  CYS A CB    
523  S SG    . CYS A 112 ? 0.6994 0.3910 0.4544 0.1516  -0.0788 -0.0237 84  CYS A SG    
524  N N     . ASP A 113 ? 0.6406 0.3248 0.3818 0.1759  -0.0717 -0.0507 85  ASP A N     
525  C CA    . ASP A 113 ? 0.6276 0.3049 0.3706 0.1828  -0.0774 -0.0513 85  ASP A CA    
526  C C     . ASP A 113 ? 0.6535 0.3057 0.3785 0.1857  -0.0820 -0.0574 85  ASP A C     
527  O O     . ASP A 113 ? 0.6617 0.3102 0.3748 0.1872  -0.0758 -0.0654 85  ASP A O     
528  C CB    . ASP A 113 ? 0.6184 0.3150 0.3710 0.1907  -0.0695 -0.0564 85  ASP A CB    
529  C CG    . ASP A 113 ? 0.6521 0.3461 0.4111 0.1973  -0.0757 -0.0536 85  ASP A CG    
530  O OD1   . ASP A 113 ? 0.6775 0.3539 0.4270 0.2033  -0.0796 -0.0579 85  ASP A OD1   
531  O OD2   . ASP A 113 ? 0.6644 0.3733 0.4372 0.1968  -0.0766 -0.0471 85  ASP A OD2   
532  N N     . ILE A 114 ? 0.6676 0.3019 0.3899 0.1865  -0.0926 -0.0538 86  ILE A N     
533  C CA    . ILE A 114 ? 0.6949 0.3027 0.3986 0.1887  -0.0979 -0.0598 86  ILE A CA    
534  C C     . ILE A 114 ? 0.7057 0.3129 0.4029 0.1998  -0.0905 -0.0706 86  ILE A C     
535  O O     . ILE A 114 ? 0.7365 0.3265 0.4159 0.2024  -0.0897 -0.0785 86  ILE A O     
536  C CB    . ILE A 114 ? 0.7088 0.2968 0.4118 0.1863  -0.1112 -0.0532 86  ILE A CB    
537  C CG1   . ILE A 114 ? 0.7641 0.3229 0.4459 0.1845  -0.1183 -0.0583 86  ILE A CG1   
538  C CG2   . ILE A 114 ? 0.7114 0.3005 0.4222 0.1951  -0.1120 -0.0531 86  ILE A CG2   
539  C CD1   . ILE A 114 ? 0.9245 0.4607 0.6035 0.1832  -0.1310 -0.0541 86  ILE A CD1   
540  N N     . SER A 115 ? 0.6928 0.3192 0.4038 0.2066  -0.0848 -0.0712 87  SER A N     
541  C CA    . SER A 115 ? 0.7043 0.3331 0.4119 0.2178  -0.0775 -0.0806 87  SER A CA    
542  C C     . SER A 115 ? 0.6937 0.3383 0.3994 0.2178  -0.0652 -0.0876 87  SER A C     
543  O O     . SER A 115 ? 0.6713 0.3383 0.3894 0.2132  -0.0597 -0.0846 87  SER A O     
544  C CB    . SER A 115 ? 0.7203 0.3650 0.4443 0.2252  -0.0768 -0.0778 87  SER A CB    
545  O OG    . SER A 115 ? 0.6950 0.3502 0.4199 0.2356  -0.0678 -0.0864 87  SER A OG    
546  N N     . PRO A 116 ? 0.7123 0.3451 0.4022 0.2226  -0.0603 -0.0968 88  PRO A N     
547  C CA    . PRO A 116 ? 0.7054 0.3539 0.3941 0.2229  -0.0476 -0.1031 88  PRO A CA    
548  C C     . PRO A 116 ? 0.7243 0.4014 0.4311 0.2287  -0.0389 -0.1051 88  PRO A C     
549  O O     . PRO A 116 ? 0.7469 0.4456 0.4645 0.2234  -0.0325 -0.1036 88  PRO A O     
550  C CB    . PRO A 116 ? 0.7322 0.3615 0.4008 0.2281  -0.0450 -0.1118 88  PRO A CB    
551  C CG    . PRO A 116 ? 0.7519 0.3528 0.4080 0.2256  -0.0579 -0.1088 88  PRO A CG    
552  C CD    . PRO A 116 ? 0.8011 0.4037 0.4716 0.2266  -0.0664 -0.1014 88  PRO A CD    
553  N N     . GLU A 117 ? 0.6971 0.3739 0.4071 0.2397  -0.0391 -0.1082 89  GLU A N     
554  C CA    . GLU A 117 ? 0.6837 0.3877 0.4108 0.2466  -0.0317 -0.1103 89  GLU A CA    
555  C C     . GLU A 117 ? 0.6586 0.3873 0.4040 0.2395  -0.0314 -0.1037 89  GLU A C     
556  O O     . GLU A 117 ? 0.6419 0.3960 0.3990 0.2401  -0.0227 -0.1066 89  GLU A O     
557  C CB    . GLU A 117 ? 0.7717 0.4696 0.5019 0.2581  -0.0363 -0.1105 89  GLU A CB    
558  C CG    . GLU A 117 ? 0.7507 0.4280 0.4660 0.2609  -0.0370 -0.1145 89  GLU A CG    
559  C CD    . GLU A 117 ? 0.7771 0.4244 0.4798 0.2567  -0.0493 -0.1101 89  GLU A CD    
560  O OE1   . GLU A 117 ? 0.8659 0.5100 0.5749 0.2535  -0.0577 -0.1028 89  GLU A OE1   
561  O OE2   . GLU A 117 ? 0.7626 0.3900 0.4495 0.2562  -0.0505 -0.1137 89  GLU A OE2   
562  N N     . MET A 118 ? 0.6627 0.3842 0.4105 0.2325  -0.0406 -0.0950 90  MET A N     
563  C CA    . MET A 118 ? 0.6254 0.3680 0.3880 0.2252  -0.0399 -0.0887 90  MET A CA    
564  C C     . MET A 118 ? 0.6152 0.3662 0.3757 0.2165  -0.0320 -0.0907 90  MET A C     
565  O O     . MET A 118 ? 0.6863 0.4607 0.4582 0.2144  -0.0248 -0.0919 90  MET A O     
566  C CB    . MET A 118 ? 0.6227 0.3546 0.3877 0.2201  -0.0509 -0.0785 90  MET A CB    
567  C CG    . MET A 118 ? 0.6314 0.3564 0.4003 0.2280  -0.0585 -0.0751 90  MET A CG    
568  S SD    . MET A 118 ? 0.6455 0.4015 0.4349 0.2327  -0.0558 -0.0722 90  MET A SD    
569  C CE    . MET A 118 ? 0.6860 0.4310 0.4799 0.2320  -0.0680 -0.0603 90  MET A CE    
570  N N     . VAL A 119 ? 0.6262 0.3577 0.3714 0.2114  -0.0335 -0.0910 91  VAL A N     
571  C CA    . VAL A 119 ? 0.6170 0.3549 0.3600 0.2028  -0.0267 -0.0913 91  VAL A CA    
572  C C     . VAL A 119 ? 0.6181 0.3702 0.3612 0.2057  -0.0141 -0.1000 91  VAL A C     
573  O O     . VAL A 119 ? 0.7016 0.4685 0.4501 0.1996  -0.0066 -0.1004 91  VAL A O     
574  C CB    . VAL A 119 ? 0.6298 0.3440 0.3563 0.1968  -0.0320 -0.0889 91  VAL A CB    
575  C CG1   . VAL A 119 ? 0.6324 0.3325 0.3597 0.1943  -0.0450 -0.0803 91  VAL A CG1   
576  C CG2   . VAL A 119 ? 0.6527 0.3498 0.3609 0.2016  -0.0293 -0.0969 91  VAL A CG2   
577  N N     . ASP A 120 ? 0.6314 0.3797 0.3693 0.2151  -0.0113 -0.1071 92  ASP A N     
578  C CA    . ASP A 120 ? 0.6301 0.3953 0.3712 0.2183  0.0011  -0.1148 92  ASP A CA    
579  C C     . ASP A 120 ? 0.6117 0.4061 0.3738 0.2201  0.0048  -0.1147 92  ASP A C     
580  O O     . ASP A 120 ? 0.6025 0.4162 0.3718 0.2173  0.0146  -0.1184 92  ASP A O     
581  C CB    . ASP A 120 ? 0.7097 0.4627 0.4389 0.2285  0.0039  -0.1222 92  ASP A CB    
582  C CG    . ASP A 120 ? 0.7982 0.5208 0.5047 0.2270  -0.0008 -0.1230 92  ASP A CG    
583  O OD1   . ASP A 120 ? 0.8206 0.5244 0.5216 0.2269  -0.0122 -0.1186 92  ASP A OD1   
584  O OD2   . ASP A 120 ? 0.8509 0.5717 0.5479 0.2231  0.0065  -0.1261 92  ASP A OD2   
585  N N     . PHE A 121 ? 0.6073 0.4050 0.3790 0.2246  -0.0032 -0.1103 93  PHE A N     
586  C CA    . PHE A 121 ? 0.5900 0.4153 0.3809 0.2256  -0.0011 -0.1093 93  PHE A CA    
587  C C     . PHE A 121 ? 0.5713 0.4091 0.3690 0.2142  0.0010  -0.1055 93  PHE A C     
588  O O     . PHE A 121 ? 0.5926 0.4542 0.4025 0.2120  0.0076  -0.1081 93  PHE A O     
589  C CB    . PHE A 121 ? 0.5910 0.4145 0.3886 0.2324  -0.0108 -0.1042 93  PHE A CB    
590  C CG    . PHE A 121 ? 0.5765 0.4283 0.3926 0.2354  -0.0096 -0.1036 93  PHE A CG    
591  C CD1   . PHE A 121 ? 0.5580 0.4255 0.3840 0.2273  -0.0101 -0.0991 93  PHE A CD1   
592  C CD2   . PHE A 121 ? 0.5826 0.4452 0.4057 0.2467  -0.0080 -0.1074 93  PHE A CD2   
593  C CE1   . PHE A 121 ? 0.5465 0.4396 0.3880 0.2298  -0.0096 -0.0989 93  PHE A CE1   
594  C CE2   . PHE A 121 ? 0.5775 0.4670 0.4176 0.2495  -0.0076 -0.1066 93  PHE A CE2   
595  C CZ    . PHE A 121 ? 0.5524 0.4570 0.4012 0.2407  -0.0087 -0.1025 93  PHE A CZ    
596  N N     . CYS A 122 ? 0.5705 0.3921 0.3605 0.2070  -0.0044 -0.0995 94  CYS A N     
597  C CA    . CYS A 122 ? 0.5550 0.3855 0.3500 0.1969  -0.0020 -0.0956 94  CYS A CA    
598  C C     . CYS A 122 ? 0.5532 0.3914 0.3456 0.1917  0.0095  -0.1014 94  CYS A C     
599  O O     . CYS A 122 ? 0.6899 0.5487 0.4932 0.1877  0.0158  -0.1032 94  CYS A O     
600  C CB    . CYS A 122 ? 0.5569 0.3675 0.3437 0.1912  -0.0097 -0.0877 94  CYS A CB    
601  S SG    . CYS A 122 ? 0.5607 0.3595 0.3497 0.1955  -0.0233 -0.0796 94  CYS A SG    
602  N N     . ARG A 123 ? 0.5672 0.3884 0.3447 0.1914  0.0123  -0.1042 95  ARG A N     
603  C CA    . ARG A 123 ? 0.5679 0.3932 0.3407 0.1861  0.0232  -0.1087 95  ARG A CA    
604  C C     . ARG A 123 ? 0.5649 0.4125 0.3478 0.1892  0.0330  -0.1161 95  ARG A C     
605  O O     . ARG A 123 ? 0.5646 0.4183 0.3459 0.1841  0.0429  -0.1197 95  ARG A O     
606  C CB    . ARG A 123 ? 0.5866 0.3882 0.3397 0.1868  0.0233  -0.1103 95  ARG A CB    
607  C CG    . ARG A 123 ? 0.5920 0.3715 0.3354 0.1842  0.0123  -0.1032 95  ARG A CG    
608  C CD    . ARG A 123 ? 0.6035 0.3652 0.3297 0.1792  0.0139  -0.1026 95  ARG A CD    
609  N NE    . ARG A 123 ? 0.6407 0.3829 0.3501 0.1851  0.0114  -0.1068 95  ARG A NE    
610  C CZ    . ARG A 123 ? 0.6786 0.3980 0.3721 0.1829  0.0042  -0.1039 95  ARG A CZ    
611  N NH1   . ARG A 123 ? 0.6795 0.3934 0.3728 0.1753  -0.0012 -0.0961 95  ARG A NH1   
612  N NH2   . ARG A 123 ? 0.6696 0.3714 0.3470 0.1887  0.0024  -0.1089 95  ARG A NH2   
613  N N     . GLN A 124 ? 0.5732 0.4334 0.3668 0.1972  0.0305  -0.1180 96  GLN A N     
614  C CA    . GLN A 124 ? 0.5762 0.4598 0.3813 0.2008  0.0391  -0.1246 96  GLN A CA    
615  C C     . GLN A 124 ? 0.5898 0.4990 0.4137 0.1987  0.0381  -0.1235 96  GLN A C     
616  O O     . GLN A 124 ? 0.6136 0.5440 0.4476 0.1955  0.0464  -0.1280 96  GLN A O     
617  C CB    . GLN A 124 ? 0.6163 0.4961 0.4188 0.2132  0.0384  -0.1287 96  GLN A CB    
618  C CG    . GLN A 124 ? 0.6742 0.5727 0.4833 0.2170  0.0499  -0.1361 96  GLN A CG    
619  C CD    . GLN A 124 ? 0.7772 0.6902 0.5982 0.2288  0.0482  -0.1384 96  GLN A CD    
620  O OE1   . GLN A 124 ? 0.7396 0.6677 0.5746 0.2300  0.0425  -0.1353 96  GLN A OE1   
621  N NE2   . GLN A 124 ? 0.8354 0.7435 0.6502 0.2382  0.0534  -0.1436 96  GLN A NE2   
622  N N     . HIS A 125 ? 0.5930 0.5010 0.4216 0.2000  0.0282  -0.1175 97  HIS A N     
623  C CA    . HIS A 125 ? 0.5462 0.4774 0.3906 0.1978  0.0267  -0.1161 97  HIS A CA    
624  C C     . HIS A 125 ? 0.5759 0.5045 0.4196 0.1875  0.0250  -0.1109 97  HIS A C     
625  O O     . HIS A 125 ? 0.5913 0.5326 0.4398 0.1795  0.0318  -0.1135 97  HIS A O     
626  C CB    . HIS A 125 ? 0.5228 0.4577 0.3739 0.2074  0.0176  -0.1129 97  HIS A CB    
627  C CG    . HIS A 125 ? 0.5391 0.4741 0.3903 0.2191  0.0187  -0.1172 97  HIS A CG    
628  N ND1   . HIS A 125 ? 0.6669 0.5770 0.5043 0.2251  0.0159  -0.1172 97  HIS A ND1   
629  C CD2   . HIS A 125 ? 0.5761 0.5331 0.4396 0.2260  0.0224  -0.1218 97  HIS A CD2   
630  C CE1   . HIS A 125 ? 0.7008 0.6163 0.5410 0.2358  0.0184  -0.1218 97  HIS A CE1   
631  N NE2   . HIS A 125 ? 0.6469 0.5915 0.5037 0.2368  0.0224  -0.1243 97  HIS A NE2   
632  N N     . ASN A 126 ? 0.6060 0.5182 0.4441 0.1877  0.0162  -0.1036 98  ASN A N     
633  C CA    . ASN A 126 ? 0.5644 0.4741 0.4023 0.1792  0.0145  -0.0978 98  ASN A CA    
634  C C     . ASN A 126 ? 0.5646 0.4588 0.3911 0.1718  0.0194  -0.0974 98  ASN A C     
635  O O     . ASN A 126 ? 0.6100 0.4930 0.4322 0.1671  0.0159  -0.0908 98  ASN A O     
636  C CB    . ASN A 126 ? 0.5228 0.4221 0.3601 0.1822  0.0036  -0.0893 98  ASN A CB    
637  C CG    . ASN A 126 ? 0.5766 0.4853 0.4219 0.1916  -0.0022 -0.0890 98  ASN A CG    
638  O OD1   . ASN A 126 ? 0.6557 0.5623 0.4997 0.1993  -0.0020 -0.0931 98  ASN A OD1   
639  N ND2   . ASN A 126 ? 0.6008 0.5195 0.4539 0.1914  -0.0072 -0.0838 98  ASN A ND2   
640  N N     . ALA A 127 ? 0.5163 0.4104 0.3381 0.1711  0.0277  -0.1037 99  ALA A N     
641  C CA    . ALA A 127 ? 0.5673 0.4469 0.3775 0.1645  0.0329  -0.1033 99  ALA A CA    
642  C C     . ALA A 127 ? 0.6330 0.5221 0.4481 0.1551  0.0388  -0.1026 99  ALA A C     
643  O O     . ALA A 127 ? 0.5454 0.4528 0.3692 0.1522  0.0460  -0.1081 99  ALA A O     
644  C CB    . ALA A 127 ? 0.7363 0.6136 0.5396 0.1669  0.0408  -0.1102 99  ALA A CB    
645  N N     . LEU A 128 ? 0.6820 0.5584 0.4918 0.1503  0.0359  -0.0959 100 LEU A N     
646  C CA    . LEU A 128 ? 0.6984 0.5799 0.5109 0.1418  0.0416  -0.0947 100 LEU A CA    
647  C C     . LEU A 128 ? 0.6887 0.5540 0.4891 0.1369  0.0471  -0.0934 100 LEU A C     
648  O O     . LEU A 128 ? 0.7315 0.5798 0.5237 0.1370  0.0416  -0.0867 100 LEU A O     
649  C CB    . LEU A 128 ? 0.6614 0.5430 0.4784 0.1408  0.0348  -0.0874 100 LEU A CB    
650  C CG    . LEU A 128 ? 0.6026 0.4846 0.4201 0.1331  0.0396  -0.0846 100 LEU A CG    
651  C CD1   . LEU A 128 ? 0.6246 0.5200 0.4462 0.1272  0.0499  -0.0922 100 LEU A CD1   
652  C CD2   . LEU A 128 ? 0.6643 0.5517 0.4885 0.1339  0.0333  -0.0788 100 LEU A CD2   
653  N N     . PRO A 129 ? 0.6402 0.5101 0.4390 0.1324  0.0575  -0.0990 101 PRO A N     
654  C CA    . PRO A 129 ? 0.6517 0.5054 0.4378 0.1283  0.0629  -0.0974 101 PRO A CA    
655  C C     . PRO A 129 ? 0.6920 0.5383 0.4765 0.1224  0.0633  -0.0909 101 PRO A C     
656  O O     . PRO A 129 ? 0.7421 0.5985 0.5354 0.1193  0.0637  -0.0902 101 PRO A O     
657  C CB    . PRO A 129 ? 0.6350 0.4990 0.4226 0.1248  0.0746  -0.1051 101 PRO A CB    
658  C CG    . PRO A 129 ? 0.6468 0.5309 0.4469 0.1292  0.0737  -0.1110 101 PRO A CG    
659  C CD    . PRO A 129 ? 0.6023 0.4926 0.4109 0.1312  0.0646  -0.1070 101 PRO A CD    
660  N N     . GLY A 130 ? 0.7113 0.5394 0.4836 0.1211  0.0633  -0.0861 102 GLY A N     
661  C CA    . GLY A 130 ? 0.7318 0.5516 0.5017 0.1163  0.0645  -0.0794 102 GLY A CA    
662  C C     . GLY A 130 ? 0.6966 0.5153 0.4720 0.1181  0.0553  -0.0718 102 GLY A C     
663  O O     . GLY A 130 ? 0.7055 0.5190 0.4804 0.1148  0.0567  -0.0660 102 GLY A O     
664  N N     . THR A 131 ? 0.6655 0.4887 0.4460 0.1235  0.0464  -0.0714 103 THR A N     
665  C CA    . THR A 131 ? 0.6822 0.5051 0.4685 0.1252  0.0379  -0.0637 103 THR A CA    
666  C C     . THR A 131 ? 0.7259 0.5405 0.5097 0.1308  0.0269  -0.0605 103 THR A C     
667  O O     . THR A 131 ? 0.7939 0.5960 0.5735 0.1307  0.0203  -0.0528 103 THR A O     
668  C CB    . THR A 131 ? 0.6480 0.4886 0.4462 0.1250  0.0388  -0.0661 103 THR A CB    
669  O OG1   . THR A 131 ? 0.5551 0.4028 0.3549 0.1191  0.0492  -0.0706 103 THR A OG1   
670  C CG2   . THR A 131 ? 0.6446 0.4845 0.4478 0.1261  0.0318  -0.0573 103 THR A CG2   
671  N N     . ILE A 132 ? 0.6135 0.4350 0.4001 0.1356  0.0247  -0.0662 104 ILE A N     
672  C CA    . ILE A 132 ? 0.6625 0.4758 0.4470 0.1414  0.0145  -0.0640 104 ILE A CA    
673  C C     . ILE A 132 ? 0.6172 0.4180 0.3892 0.1436  0.0152  -0.0686 104 ILE A C     
674  O O     . ILE A 132 ? 0.5843 0.3912 0.3544 0.1441  0.0233  -0.0764 104 ILE A O     
675  C CB    . ILE A 132 ? 0.5756 0.4029 0.3705 0.1465  0.0112  -0.0668 104 ILE A CB    
676  C CG1   . ILE A 132 ? 0.5914 0.4343 0.3972 0.1436  0.0137  -0.0650 104 ILE A CG1   
677  C CG2   . ILE A 132 ? 0.6886 0.5058 0.4826 0.1516  -0.0003 -0.0618 104 ILE A CG2   
678  C CD1   . ILE A 132 ? 0.5996 0.4559 0.4152 0.1487  0.0090  -0.0657 104 ILE A CD1   
679  N N     . THR A 133 ? 0.6139 0.3973 0.3771 0.1447  0.0069  -0.0637 105 THR A N     
680  C CA    . THR A 133 ? 0.6319 0.4007 0.3809 0.1473  0.0058  -0.0678 105 THR A CA    
681  C C     . THR A 133 ? 0.6864 0.4466 0.4343 0.1529  -0.0051 -0.0667 105 THR A C     
682  O O     . THR A 133 ? 0.7203 0.4699 0.4673 0.1515  -0.0146 -0.0592 105 THR A O     
683  C CB    . THR A 133 ? 0.6772 0.4310 0.4142 0.1427  0.0055  -0.0633 105 THR A CB    
684  O OG1   . THR A 133 ? 0.7818 0.5258 0.5192 0.1415  -0.0056 -0.0542 105 THR A OG1   
685  C CG2   . THR A 133 ? 0.6706 0.4321 0.4106 0.1370  0.0154  -0.0621 105 THR A CG2   
686  N N     . TYR A 134 ? 0.6655 0.4302 0.4141 0.1592  -0.0036 -0.0739 106 TYR A N     
687  C CA    . TYR A 134 ? 0.5886 0.3446 0.3363 0.1653  -0.0131 -0.0735 106 TYR A CA    
688  C C     . TYR A 134 ? 0.5917 0.3251 0.3216 0.1668  -0.0176 -0.0754 106 TYR A C     
689  O O     . TYR A 134 ? 0.6309 0.3606 0.3502 0.1682  -0.0106 -0.0821 106 TYR A O     
690  C CB    . TYR A 134 ? 0.5690 0.3391 0.3248 0.1724  -0.0095 -0.0802 106 TYR A CB    
691  C CG    . TYR A 134 ? 0.5505 0.3432 0.3231 0.1712  -0.0063 -0.0788 106 TYR A CG    
692  C CD1   . TYR A 134 ? 0.6165 0.4123 0.3983 0.1715  -0.0140 -0.0717 106 TYR A CD1   
693  C CD2   . TYR A 134 ? 0.5427 0.3532 0.3213 0.1694  0.0043  -0.0845 106 TYR A CD2   
694  C CE1   . TYR A 134 ? 0.6136 0.4296 0.4089 0.1705  -0.0113 -0.0706 106 TYR A CE1   
695  C CE2   . TYR A 134 ? 0.5277 0.3582 0.3203 0.1678  0.0066  -0.0838 106 TYR A CE2   
696  C CZ    . TYR A 134 ? 0.5811 0.4142 0.3814 0.1686  -0.0013 -0.0770 106 TYR A CZ    
697  O OH    . TYR A 134 ? 0.6211 0.4736 0.4336 0.1671  0.0009  -0.0766 106 TYR A OH    
698  N N     . GLU A 135 ? 0.5987 0.3168 0.3250 0.1662  -0.0292 -0.0694 107 GLU A N     
699  C CA    . GLU A 135 ? 0.6196 0.3148 0.3281 0.1663  -0.0352 -0.0706 107 GLU A CA    
700  C C     . GLU A 135 ? 0.6308 0.3127 0.3378 0.1705  -0.0463 -0.0694 107 GLU A C     
701  O O     . GLU A 135 ? 0.6216 0.3120 0.3417 0.1731  -0.0495 -0.0664 107 GLU A O     
702  C CB    . GLU A 135 ? 0.6224 0.3088 0.3252 0.1585  -0.0391 -0.0634 107 GLU A CB    
703  C CG    . GLU A 135 ? 0.6945 0.3938 0.4008 0.1539  -0.0286 -0.0627 107 GLU A CG    
704  C CD    . GLU A 135 ? 0.7724 0.4618 0.4616 0.1529  -0.0229 -0.0673 107 GLU A CD    
705  O OE1   . GLU A 135 ? 0.7981 0.4726 0.4727 0.1566  -0.0260 -0.0725 107 GLU A OE1   
706  O OE2   . GLU A 135 ? 0.7950 0.4909 0.4846 0.1486  -0.0150 -0.0659 107 GLU A OE2   
707  N N     . LEU A 136 ? 0.6524 0.3121 0.3422 0.1711  -0.0523 -0.0718 108 LEU A N     
708  C CA    . LEU A 136 ? 0.6677 0.3101 0.3529 0.1743  -0.0633 -0.0713 108 LEU A CA    
709  C C     . LEU A 136 ? 0.6722 0.3011 0.3547 0.1666  -0.0753 -0.0624 108 LEU A C     
710  O O     . LEU A 136 ? 0.6760 0.2992 0.3497 0.1609  -0.0758 -0.0604 108 LEU A O     
711  C CB    . LEU A 136 ? 0.6922 0.3178 0.3587 0.1808  -0.0617 -0.0813 108 LEU A CB    
712  C CG    . LEU A 136 ? 0.7131 0.3171 0.3714 0.1851  -0.0720 -0.0829 108 LEU A CG    
713  C CD1   . LEU A 136 ? 0.7277 0.3278 0.3779 0.1958  -0.0654 -0.0935 108 LEU A CD1   
714  C CD2   . LEU A 136 ? 0.7332 0.3126 0.3740 0.1791  -0.0824 -0.0810 108 LEU A CD2   
715  N N     . LEU A 137 ? 0.6723 0.2965 0.3630 0.1665  -0.0849 -0.0566 109 LEU A N     
716  C CA    . LEU A 137 ? 0.6772 0.2894 0.3674 0.1590  -0.0970 -0.0476 109 LEU A CA    
717  C C     . LEU A 137 ? 0.6826 0.2868 0.3795 0.1607  -0.1066 -0.0435 109 LEU A C     
718  O O     . LEU A 137 ? 0.6716 0.2882 0.3810 0.1658  -0.1032 -0.0430 109 LEU A O     
719  C CB    . LEU A 137 ? 0.6560 0.2846 0.3595 0.1520  -0.0952 -0.0380 109 LEU A CB    
720  C CG    . LEU A 137 ? 0.6582 0.2789 0.3651 0.1440  -0.1071 -0.0272 109 LEU A CG    
721  C CD1   . LEU A 137 ? 0.6778 0.2802 0.3666 0.1398  -0.1130 -0.0289 109 LEU A CD1   
722  C CD2   . LEU A 137 ? 0.6352 0.2753 0.3587 0.1395  -0.1036 -0.0177 109 LEU A CD2   
723  N N     . ASP A 138 ? 0.7006 0.2840 0.3889 0.1562  -0.1187 -0.0405 110 ASP A N     
724  C CA    . ASP A 138 ? 0.7065 0.2806 0.4019 0.1552  -0.1291 -0.0343 110 ASP A CA    
725  C C     . ASP A 138 ? 0.6942 0.2753 0.4024 0.1457  -0.1358 -0.0214 110 ASP A C     
726  O O     . ASP A 138 ? 0.7657 0.3408 0.4674 0.1388  -0.1404 -0.0186 110 ASP A O     
727  C CB    . ASP A 138 ? 0.7373 0.2822 0.4144 0.1561  -0.1384 -0.0399 110 ASP A CB    
728  C CG    . ASP A 138 ? 0.7461 0.2794 0.4297 0.1557  -0.1485 -0.0343 110 ASP A CG    
729  O OD1   . ASP A 138 ? 0.7337 0.2820 0.4361 0.1543  -0.1489 -0.0252 110 ASP A OD1   
730  O OD2   . ASP A 138 ? 0.7726 0.2807 0.4417 0.1568  -0.1560 -0.0392 110 ASP A OD2   
731  N N     . VAL A 139 ? 0.6785 0.2730 0.4048 0.1458  -0.1361 -0.0133 111 VAL A N     
732  C CA    . VAL A 139 ? 0.6642 0.2694 0.4049 0.1379  -0.1400 -0.0006 111 VAL A CA    
733  C C     . VAL A 139 ? 0.6809 0.2679 0.4179 0.1299  -0.1540 0.0057  111 VAL A C     
734  O O     . VAL A 139 ? 0.7164 0.3104 0.4623 0.1224  -0.1579 0.0156  111 VAL A O     
735  C CB    . VAL A 139 ? 0.6607 0.2830 0.4200 0.1405  -0.1370 0.0063  111 VAL A CB    
736  C CG1   . VAL A 139 ? 0.7629 0.3712 0.5237 0.1423  -0.1458 0.0090  111 VAL A CG1   
737  C CG2   . VAL A 139 ? 0.6281 0.2666 0.4024 0.1340  -0.1366 0.0182  111 VAL A CG2   
738  N N     . VAL A 140 ? 0.7052 0.2689 0.4293 0.1311  -0.1618 0.0003  112 VAL A N     
739  C CA    . VAL A 140 ? 0.7244 0.2688 0.4431 0.1227  -0.1759 0.0050  112 VAL A CA    
740  C C     . VAL A 140 ? 0.7471 0.2720 0.4424 0.1221  -0.1789 -0.0049 112 VAL A C     
741  O O     . VAL A 140 ? 0.7729 0.2735 0.4552 0.1203  -0.1886 -0.0086 112 VAL A O     
742  C CB    . VAL A 140 ? 0.7375 0.2678 0.4600 0.1231  -0.1843 0.0081  112 VAL A CB    
743  C CG1   . VAL A 140 ? 0.7175 0.2658 0.4630 0.1205  -0.1842 0.0212  112 VAL A CG1   
744  C CG2   . VAL A 140 ? 0.7473 0.2691 0.4606 0.1343  -0.1786 -0.0028 112 VAL A CG2   
745  N N     . GLU A 141 ? 0.7798 0.3146 0.4690 0.1233  -0.1703 -0.0092 113 GLU A N     
746  C CA    . GLU A 141 ? 0.8129 0.3307 0.4786 0.1236  -0.1714 -0.0188 113 GLU A CA    
747  C C     . GLU A 141 ? 0.8126 0.3169 0.4717 0.1133  -0.1852 -0.0132 113 GLU A C     
748  O O     . GLU A 141 ? 0.7879 0.3058 0.4611 0.1063  -0.1884 -0.0022 113 GLU A O     
749  C CB    . GLU A 141 ? 0.8024 0.3353 0.4645 0.1271  -0.1582 -0.0234 113 GLU A CB    
750  C CG    . GLU A 141 ? 0.8056 0.3317 0.4519 0.1363  -0.1490 -0.0370 113 GLU A CG    
751  C CD    . GLU A 141 ? 0.9476 0.4505 0.5679 0.1352  -0.1539 -0.0448 113 GLU A CD    
752  O OE1   . GLU A 141 ? 0.9555 0.4501 0.5703 0.1268  -0.1640 -0.0396 113 GLU A OE1   
753  O OE2   . GLU A 141 ? 1.1045 0.5977 0.7097 0.1429  -0.1478 -0.0561 113 GLU A OE2   
754  N N     . PRO A 142 ? 0.8305 0.3086 0.4686 0.1121  -0.1939 -0.0205 114 PRO A N     
755  C CA    . PRO A 142 ? 0.8533 0.3193 0.4838 0.1017  -0.2076 -0.0158 114 PRO A CA    
756  C C     . PRO A 142 ? 0.8783 0.3567 0.5060 0.0985  -0.2041 -0.0130 114 PRO A C     
757  O O     . PRO A 142 ? 0.8883 0.3762 0.5278 0.0903  -0.2109 -0.0019 114 PRO A O     
758  C CB    . PRO A 142 ? 0.8757 0.3106 0.4799 0.1033  -0.2144 -0.0275 114 PRO A CB    
759  C CG    . PRO A 142 ? 0.8951 0.3251 0.5013 0.1126  -0.2083 -0.0336 114 PRO A CG    
760  C CD    . PRO A 142 ? 0.8518 0.3096 0.4738 0.1198  -0.1928 -0.0323 114 PRO A CD    
761  N N     . ARG A 143 ? 0.8573 0.3362 0.4701 0.1050  -0.1932 -0.0224 115 ARG A N     
762  C CA    . ARG A 143 ? 0.8380 0.3279 0.4468 0.1031  -0.1881 -0.0203 115 ARG A CA    
763  C C     . ARG A 143 ? 0.8325 0.3472 0.4565 0.1088  -0.1720 -0.0191 115 ARG A C     
764  O O     . ARG A 143 ? 0.8338 0.3506 0.4484 0.1158  -0.1600 -0.0281 115 ARG A O     
765  C CB    . ARG A 143 ? 0.9076 0.3789 0.4871 0.1052  -0.1877 -0.0312 115 ARG A CB    
766  C CG    . ARG A 143 ? 0.9404 0.3828 0.5006 0.1031  -0.2006 -0.0376 115 ARG A CG    
767  C CD    . ARG A 143 ? 0.9445 0.3698 0.4745 0.1050  -0.1997 -0.0477 115 ARG A CD    
768  N NE    . ARG A 143 ? 0.9557 0.3895 0.4832 0.0992  -0.2017 -0.0410 115 ARG A NE    
769  C CZ    . ARG A 143 ? 0.9854 0.4093 0.5054 0.0902  -0.2166 -0.0360 115 ARG A CZ    
770  N NH1   . ARG A 143 ? 1.0299 0.4337 0.5432 0.0849  -0.2314 -0.0374 115 ARG A NH1   
771  N NH2   . ARG A 143 ? 0.9804 0.4146 0.4997 0.0862  -0.2171 -0.0293 115 ARG A NH2   
772  N N     . LEU A 144 ? 0.8221 0.3558 0.4699 0.1056  -0.1718 -0.0077 116 LEU A N     
773  C CA    . LEU A 144 ? 0.8400 0.3970 0.5024 0.1100  -0.1575 -0.0059 116 LEU A CA    
774  C C     . LEU A 144 ? 0.8448 0.4080 0.4986 0.1099  -0.1494 -0.0070 116 LEU A C     
775  O O     . LEU A 144 ? 0.8151 0.3884 0.4685 0.1154  -0.1358 -0.0126 116 LEU A O     
776  C CB    . LEU A 144 ? 0.8416 0.4157 0.5293 0.1061  -0.1597 0.0070  116 LEU A CB    
777  C CG    . LEU A 144 ? 0.7436 0.3391 0.4494 0.1109  -0.1477 0.0089  116 LEU A CG    
778  C CD1   . LEU A 144 ? 0.7403 0.3490 0.4678 0.1060  -0.1522 0.0226  116 LEU A CD1   
779  C CD2   . LEU A 144 ? 0.6987 0.3075 0.4027 0.1145  -0.1334 0.0049  116 LEU A CD2   
780  N N     . GLU A 145 ? 0.8466 0.4038 0.4936 0.1036  -0.1581 -0.0015 117 GLU A N     
781  C CA    . GLU A 145 ? 0.8696 0.4332 0.5102 0.1029  -0.1515 0.0001  117 GLU A CA    
782  C C     . GLU A 145 ? 0.8561 0.4096 0.4737 0.1081  -0.1430 -0.0121 117 GLU A C     
783  O O     . GLU A 145 ? 0.8531 0.4117 0.4646 0.1084  -0.1355 -0.0116 117 GLU A O     
784  C CB    . GLU A 145 ? 0.9211 0.4797 0.5590 0.0952  -0.1646 0.0092  117 GLU A CB    
785  C CG    . GLU A 145 ? 0.9393 0.5160 0.6021 0.0908  -0.1672 0.0235  117 GLU A CG    
786  C CD    . GLU A 145 ? 1.0472 0.6222 0.7240 0.0867  -0.1786 0.0292  117 GLU A CD    
787  O OE1   . GLU A 145 ? 1.0331 0.5892 0.6978 0.0838  -0.1901 0.0249  117 GLU A OE1   
788  O OE2   . GLU A 145 ? 1.0468 0.6384 0.7460 0.0862  -0.1758 0.0379  117 GLU A OE2   
789  N N     . ASP A 146 ? 0.8293 0.3685 0.4343 0.1125  -0.1434 -0.0227 118 ASP A N     
790  C CA    . ASP A 146 ? 0.8235 0.3532 0.4068 0.1181  -0.1348 -0.0345 118 ASP A CA    
791  C C     . ASP A 146 ? 0.8293 0.3711 0.4200 0.1258  -0.1199 -0.0416 118 ASP A C     
792  O O     . ASP A 146 ? 0.8715 0.4063 0.4462 0.1314  -0.1120 -0.0519 118 ASP A O     
793  C CB    . ASP A 146 ? 0.9161 0.4199 0.4773 0.1184  -0.1451 -0.0422 118 ASP A CB    
794  C CG    . ASP A 146 ? 0.9887 0.4796 0.5392 0.1102  -0.1601 -0.0365 118 ASP A CG    
795  O OD1   . ASP A 146 ? 0.9877 0.4857 0.5550 0.1037  -0.1696 -0.0256 118 ASP A OD1   
796  O OD2   . ASP A 146 ? 1.0108 0.4852 0.5361 0.1104  -0.1624 -0.0428 118 ASP A OD2   
797  N N     . THR A 147 ? 0.8403 0.4004 0.4544 0.1264  -0.1158 -0.0364 119 THR A N     
798  C CA    . THR A 147 ? 0.7694 0.3430 0.3925 0.1331  -0.1029 -0.0425 119 THR A CA    
799  C C     . THR A 147 ? 0.7034 0.2958 0.3348 0.1326  -0.0900 -0.0402 119 THR A C     
800  O O     . THR A 147 ? 0.7209 0.3183 0.3563 0.1275  -0.0914 -0.0318 119 THR A O     
801  C CB    . THR A 147 ? 0.7097 0.2908 0.3519 0.1344  -0.1067 -0.0389 119 THR A CB    
802  O OG1   . THR A 147 ? 0.6900 0.2854 0.3509 0.1291  -0.1090 -0.0271 119 THR A OG1   
803  C CG2   . THR A 147 ? 0.8383 0.3990 0.4726 0.1341  -0.1199 -0.0402 119 THR A CG2   
804  N N     . VAL A 148 ? 0.6953 0.2983 0.3297 0.1382  -0.0774 -0.0477 120 VAL A N     
805  C CA    . VAL A 148 ? 0.6781 0.2983 0.3204 0.1376  -0.0645 -0.0467 120 VAL A CA    
806  C C     . VAL A 148 ? 0.6545 0.2913 0.3192 0.1346  -0.0649 -0.0374 120 VAL A C     
807  O O     . VAL A 148 ? 0.7035 0.3496 0.3738 0.1312  -0.0594 -0.0321 120 VAL A O     
808  C CB    . VAL A 148 ? 0.6765 0.3045 0.3175 0.1438  -0.0517 -0.0572 120 VAL A CB    
809  C CG1   . VAL A 148 ? 0.6565 0.3043 0.3099 0.1424  -0.0390 -0.0561 120 VAL A CG1   
810  C CG2   . VAL A 148 ? 0.6999 0.3130 0.3178 0.1466  -0.0486 -0.0656 120 VAL A CG2   
811  N N     . VAL A 149 ? 0.6481 0.2878 0.3250 0.1359  -0.0712 -0.0352 121 VAL A N     
812  C CA    . VAL A 149 ? 0.6326 0.2885 0.3301 0.1339  -0.0707 -0.0269 121 VAL A CA    
813  C C     . VAL A 149 ? 0.7313 0.3858 0.4329 0.1276  -0.0779 -0.0154 121 VAL A C     
814  O O     . VAL A 149 ? 0.6769 0.3450 0.3911 0.1255  -0.0730 -0.0088 121 VAL A O     
815  C CB    . VAL A 149 ? 0.6230 0.2809 0.3309 0.1372  -0.0762 -0.0268 121 VAL A CB    
816  C CG1   . VAL A 149 ? 0.6037 0.2762 0.3312 0.1346  -0.0773 -0.0169 121 VAL A CG1   
817  C CG2   . VAL A 149 ? 0.6219 0.2861 0.3293 0.1441  -0.0676 -0.0372 121 VAL A CG2   
818  N N     . TRP A 150 ? 0.6463 0.2845 0.3374 0.1245  -0.0895 -0.0128 122 TRP A N     
819  C CA    . TRP A 150 ? 0.6791 0.3171 0.3750 0.1185  -0.0971 -0.0014 122 TRP A CA    
820  C C     . TRP A 150 ? 0.7044 0.3476 0.3963 0.1170  -0.0889 0.0008  122 TRP A C     
821  O O     . TRP A 150 ? 0.7527 0.4057 0.4565 0.1141  -0.0884 0.0105  122 TRP A O     
822  C CB    . TRP A 150 ? 0.7459 0.3649 0.4296 0.1151  -0.1118 -0.0002 122 TRP A CB    
823  C CG    . TRP A 150 ? 0.8150 0.4335 0.5005 0.1089  -0.1195 0.0105  122 TRP A CG    
824  C CD1   . TRP A 150 ? 0.8399 0.4506 0.5104 0.1067  -0.1207 0.0108  122 TRP A CD1   
825  C CD2   . TRP A 150 ? 0.8220 0.4491 0.5257 0.1043  -0.1270 0.0232  122 TRP A CD2   
826  N NE1   . TRP A 150 ? 0.8165 0.4309 0.4954 0.1013  -0.1290 0.0228  122 TRP A NE1   
827  C CE2   . TRP A 150 ? 0.8307 0.4556 0.5304 0.0997  -0.1327 0.0305  122 TRP A CE2   
828  C CE3   . TRP A 150 ? 0.8529 0.4899 0.5759 0.1039  -0.1292 0.0293  122 TRP A CE3   
829  C CZ2   . TRP A 150 ? 0.8952 0.5284 0.6109 0.0949  -0.1404 0.0438  122 TRP A CZ2   
830  C CZ3   . TRP A 150 ? 0.8585 0.5031 0.5966 0.0989  -0.1364 0.0425  122 TRP A CZ3   
831  C CH2   . TRP A 150 ? 0.8822 0.5254 0.6172 0.0945  -0.1418 0.0495  122 TRP A CH2   
832  N N     . ARG A 151 ? 0.7032 0.3398 0.3785 0.1193  -0.0817 -0.0078 123 ARG A N     
833  C CA    . ARG A 151 ? 0.6741 0.3130 0.3433 0.1178  -0.0740 -0.0057 123 ARG A CA    
834  C C     . ARG A 151 ? 0.7091 0.3642 0.3894 0.1195  -0.0594 -0.0070 123 ARG A C     
835  O O     . ARG A 151 ? 0.7548 0.4129 0.4332 0.1179  -0.0524 -0.0037 123 ARG A O     
836  C CB    . ARG A 151 ? 0.6690 0.2929 0.3144 0.1191  -0.0726 -0.0137 123 ARG A CB    
837  C CG    . ARG A 151 ? 0.6899 0.2964 0.3222 0.1165  -0.0877 -0.0121 123 ARG A CG    
838  C CD    . ARG A 151 ? 0.7135 0.3045 0.3202 0.1175  -0.0868 -0.0189 123 ARG A CD    
839  N NE    . ARG A 151 ? 0.7872 0.3607 0.3809 0.1148  -0.1022 -0.0185 123 ARG A NE    
840  C CZ    . ARG A 151 ? 0.9061 0.4625 0.4752 0.1155  -0.1049 -0.0248 123 ARG A CZ    
841  N NH1   . ARG A 151 ? 0.9764 0.5311 0.5310 0.1187  -0.0931 -0.0311 123 ARG A NH1   
842  N NH2   . ARG A 151 ? 0.9409 0.4811 0.4991 0.1124  -0.1199 -0.0246 123 ARG A NH2   
843  N N     . ASN A 152 ? 0.6824 0.3476 0.3738 0.1224  -0.0548 -0.0116 124 ASN A N     
844  C CA    . ASN A 152 ? 0.7103 0.3921 0.4150 0.1229  -0.0433 -0.0113 124 ASN A CA    
845  C C     . ASN A 152 ? 0.7236 0.4145 0.4445 0.1203  -0.0466 0.0001  124 ASN A C     
846  O O     . ASN A 152 ? 0.7246 0.4270 0.4545 0.1200  -0.0372 0.0019  124 ASN A O     
847  C CB    . ASN A 152 ? 0.6990 0.3897 0.4101 0.1269  -0.0384 -0.0197 124 ASN A CB    
848  C CG    . ASN A 152 ? 0.7816 0.4688 0.4799 0.1299  -0.0304 -0.0310 124 ASN A CG    
849  O OD1   . ASN A 152 ? 0.9167 0.6101 0.6135 0.1292  -0.0189 -0.0344 124 ASN A OD1   
850  N ND2   . ASN A 152 ? 0.8049 0.4819 0.4942 0.1332  -0.0362 -0.0367 124 ASN A ND2   
851  N N     . GLY A 153 ? 0.7098 0.3956 0.4345 0.1184  -0.0593 0.0076  125 GLY A N     
852  C CA    . GLY A 153 ? 0.6861 0.3811 0.4271 0.1163  -0.0626 0.0190  125 GLY A CA    
853  C C     . GLY A 153 ? 0.6995 0.3949 0.4403 0.1137  -0.0612 0.0275  125 GLY A C     
854  O O     . GLY A 153 ? 0.7633 0.4525 0.4914 0.1136  -0.0560 0.0244  125 GLY A O     
855  N N     . PRO A 154 ? 0.6392 0.3420 0.3944 0.1119  -0.0654 0.0390  126 PRO A N     
856  C CA    . PRO A 154 ? 0.6043 0.3147 0.3750 0.1118  -0.0713 0.0444  126 PRO A CA    
857  C C     . PRO A 154 ? 0.6700 0.3938 0.4507 0.1147  -0.0607 0.0411  126 PRO A C     
858  O O     . PRO A 154 ? 0.7296 0.4582 0.5082 0.1160  -0.0490 0.0371  126 PRO A O     
859  C CB    . PRO A 154 ? 0.5562 0.2705 0.3372 0.1088  -0.0773 0.0584  126 PRO A CB    
860  C CG    . PRO A 154 ? 0.6194 0.3354 0.3960 0.1095  -0.0678 0.0599  126 PRO A CG    
861  C CD    . PRO A 154 ? 0.6594 0.3648 0.4171 0.1105  -0.0629 0.0481  126 PRO A CD    
862  N N     . PHE A 155 ? 0.6466 0.3759 0.4374 0.1157  -0.0646 0.0425  127 PHE A N     
863  C CA    . PHE A 155 ? 0.6077 0.3491 0.4060 0.1187  -0.0559 0.0383  127 PHE A CA    
864  C C     . PHE A 155 ? 0.6514 0.4049 0.4655 0.1184  -0.0546 0.0488  127 PHE A C     
865  O O     . PHE A 155 ? 0.5122 0.2653 0.3343 0.1163  -0.0635 0.0590  127 PHE A O     
866  C CB    . PHE A 155 ? 0.5907 0.3299 0.3877 0.1212  -0.0602 0.0313  127 PHE A CB    
867  C CG    . PHE A 155 ? 0.5920 0.3210 0.3739 0.1228  -0.0593 0.0199  127 PHE A CG    
868  C CD1   . PHE A 155 ? 0.5665 0.3013 0.3442 0.1253  -0.0483 0.0099  127 PHE A CD1   
869  C CD2   . PHE A 155 ? 0.6334 0.3471 0.4052 0.1217  -0.0693 0.0190  127 PHE A CD2   
870  C CE1   . PHE A 155 ? 0.6071 0.3335 0.3716 0.1271  -0.0467 -0.0001 127 PHE A CE1   
871  C CE2   . PHE A 155 ? 0.6525 0.3564 0.4094 0.1237  -0.0678 0.0084  127 PHE A CE2   
872  C CZ    . PHE A 155 ? 0.6692 0.3799 0.4228 0.1267  -0.0561 -0.0009 127 PHE A CZ    
873  N N     . GLY A 156 ? 0.6068 0.3710 0.4251 0.1203  -0.0434 0.0463  128 GLY A N     
874  C CA    . GLY A 156 ? 0.5218 0.2977 0.3534 0.1209  -0.0404 0.0550  128 GLY A CA    
875  C C     . GLY A 156 ? 0.5932 0.3748 0.4330 0.1224  -0.0455 0.0567  128 GLY A C     
876  O O     . GLY A 156 ? 0.6522 0.4375 0.5025 0.1215  -0.0510 0.0674  128 GLY A O     
877  N N     . LYS A 157 ? 0.6687 0.4515 0.5042 0.1248  -0.0437 0.0466  129 LYS A N     
878  C CA    . LYS A 157 ? 0.6477 0.4353 0.4895 0.1269  -0.0484 0.0475  129 LYS A CA    
879  C C     . LYS A 157 ? 0.5657 0.3438 0.3997 0.1284  -0.0548 0.0395  129 LYS A C     
880  O O     . LYS A 157 ? 0.4967 0.2694 0.3203 0.1289  -0.0515 0.0300  129 LYS A O     
881  C CB    . LYS A 157 ? 0.5981 0.3996 0.4441 0.1297  -0.0392 0.0437  129 LYS A CB    
882  C CG    . LYS A 157 ? 0.5936 0.4029 0.4445 0.1289  -0.0307 0.0492  129 LYS A CG    
883  C CD    . LYS A 157 ? 0.6807 0.4920 0.5421 0.1279  -0.0358 0.0633  129 LYS A CD    
884  C CE    . LYS A 157 ? 0.7366 0.5527 0.6015 0.1275  -0.0276 0.0693  129 LYS A CE    
885  N NZ    . LYS A 157 ? 0.6635 0.4735 0.5315 0.1250  -0.0331 0.0789  129 LYS A NZ    
886  N N     . VAL A 158 ? 0.6289 0.4045 0.4677 0.1292  -0.0635 0.0438  130 VAL A N     
887  C CA    . VAL A 158 ? 0.5571 0.3225 0.3890 0.1314  -0.0701 0.0371  130 VAL A CA    
888  C C     . VAL A 158 ? 0.5078 0.2802 0.3467 0.1351  -0.0717 0.0381  130 VAL A C     
889  O O     . VAL A 158 ? 0.4996 0.2740 0.3477 0.1340  -0.0768 0.0483  130 VAL A O     
890  C CB    . VAL A 158 ? 0.5299 0.2792 0.3578 0.1279  -0.0817 0.0418  130 VAL A CB    
891  C CG1   . VAL A 158 ? 0.5299 0.2680 0.3519 0.1307  -0.0888 0.0361  130 VAL A CG1   
892  C CG2   . VAL A 158 ? 0.5447 0.2859 0.3624 0.1251  -0.0805 0.0388  130 VAL A CG2   
893  N N     . PHE A 159 ? 0.5448 0.3218 0.3801 0.1397  -0.0672 0.0281  131 PHE A N     
894  C CA    . PHE A 159 ? 0.4981 0.2820 0.3389 0.1442  -0.0687 0.0282  131 PHE A CA    
895  C C     . PHE A 159 ? 0.6595 0.4294 0.4947 0.1472  -0.0771 0.0248  131 PHE A C     
896  O O     . PHE A 159 ? 0.7524 0.5163 0.5785 0.1496  -0.0755 0.0149  131 PHE A O     
897  C CB    . PHE A 159 ? 0.5715 0.3705 0.4127 0.1477  -0.0592 0.0197  131 PHE A CB    
898  C CG    . PHE A 159 ? 0.4826 0.2938 0.3278 0.1450  -0.0506 0.0219  131 PHE A CG    
899  C CD1   . PHE A 159 ? 0.5573 0.3790 0.4109 0.1453  -0.0496 0.0296  131 PHE A CD1   
900  C CD2   . PHE A 159 ? 0.4764 0.2876 0.3162 0.1423  -0.0431 0.0164  131 PHE A CD2   
901  C CE1   . PHE A 159 ? 0.5332 0.3648 0.3893 0.1433  -0.0412 0.0311  131 PHE A CE1   
902  C CE2   . PHE A 159 ? 0.5168 0.3372 0.3595 0.1400  -0.0348 0.0182  131 PHE A CE2   
903  C CZ    . PHE A 159 ? 0.5286 0.3590 0.3792 0.1407  -0.0339 0.0253  131 PHE A CZ    
904  N N     . CYS A 160 ? 0.5924 0.3567 0.4329 0.1471  -0.0856 0.0333  132 CYS A N     
905  C CA    . CYS A 160 ? 0.5927 0.3425 0.4285 0.1502  -0.0937 0.0310  132 CYS A CA    
906  C C     . CYS A 160 ? 0.6775 0.4360 0.5204 0.1556  -0.0941 0.0335  132 CYS A C     
907  O O     . CYS A 160 ? 0.6676 0.4287 0.5189 0.1539  -0.0978 0.0442  132 CYS A O     
908  C CB    . CYS A 160 ? 0.5907 0.3237 0.4256 0.1448  -0.1043 0.0389  132 CYS A CB    
909  S SG    . CYS A 160 ? 0.7464 0.4620 0.5794 0.1477  -0.1153 0.0406  132 CYS A SG    
910  N N     . MET A 161 ? 0.6689 0.4328 0.5086 0.1622  -0.0900 0.0241  133 MET A N     
911  C CA    . MET A 161 ? 0.7166 0.4911 0.5626 0.1680  -0.0899 0.0259  133 MET A CA    
912  C C     . MET A 161 ? 0.7177 0.4770 0.5619 0.1722  -0.0987 0.0280  133 MET A C     
913  O O     . MET A 161 ? 0.7492 0.4915 0.5914 0.1681  -0.1065 0.0337  133 MET A O     
914  C CB    . MET A 161 ? 0.7211 0.5112 0.5664 0.1731  -0.0815 0.0154  133 MET A CB    
915  C CG    . MET A 161 ? 0.7525 0.5574 0.5996 0.1688  -0.0724 0.0131  133 MET A CG    
916  S SD    . MET A 161 ? 0.7344 0.5496 0.5906 0.1645  -0.0714 0.0256  133 MET A SD    
917  C CE    . MET A 161 ? 0.6585 0.4912 0.5146 0.1622  -0.0594 0.0185  133 MET A CE    
918  N N     . LEU A 162 ? 0.7210 0.4859 0.5657 0.1802  -0.0977 0.0236  134 LEU A N     
919  C CA    . LEU A 162 ? 0.6266 0.3778 0.4702 0.1853  -0.1054 0.0263  134 LEU A CA    
920  C C     . LEU A 162 ? 0.6255 0.3546 0.4580 0.1865  -0.1096 0.0193  134 LEU A C     
921  O O     . LEU A 162 ? 0.6432 0.3687 0.4712 0.1945  -0.1089 0.0116  134 LEU A O     
922  C CB    . LEU A 162 ? 0.5563 0.3214 0.4039 0.1944  -0.1027 0.0237  134 LEU A CB    
923  C CG    . LEU A 162 ? 0.5519 0.3400 0.4082 0.1939  -0.0980 0.0287  134 LEU A CG    
924  C CD1   . LEU A 162 ? 0.5488 0.3546 0.4070 0.2017  -0.0931 0.0212  134 LEU A CD1   
925  C CD2   . LEU A 162 ? 0.5428 0.3283 0.4050 0.1928  -0.1036 0.0422  134 LEU A CD2   
926  N N     . MET A 163 ? 0.6347 0.3491 0.4626 0.1789  -0.1140 0.0218  135 MET A N     
927  C CA    . MET A 163 ? 0.6232 0.3148 0.4386 0.1791  -0.1188 0.0153  135 MET A CA    
928  C C     . MET A 163 ? 0.6507 0.3219 0.4639 0.1719  -0.1292 0.0232  135 MET A C     
929  O O     . MET A 163 ? 0.7008 0.3501 0.5030 0.1726  -0.1349 0.0184  135 MET A O     
930  C CB    . MET A 163 ? 0.6888 0.3829 0.4959 0.1773  -0.1122 0.0056  135 MET A CB    
931  C CG    . MET A 163 ? 0.7574 0.4554 0.5664 0.1679  -0.1113 0.0106  135 MET A CG    
932  S SD    . MET A 163 ? 0.7344 0.4076 0.5350 0.1596  -0.1222 0.0148  135 MET A SD    
933  C CE    . MET A 163 ? 0.6920 0.3472 0.4739 0.1645  -0.1215 0.0005  135 MET A CE    
934  N N     . LEU A 164 ? 0.6531 0.3305 0.4764 0.1649  -0.1319 0.0349  136 LEU A N     
935  C CA    . LEU A 164 ? 0.6271 0.2890 0.4510 0.1560  -0.1413 0.0426  136 LEU A CA    
936  C C     . LEU A 164 ? 0.6321 0.2826 0.4581 0.1556  -0.1470 0.0454  136 LEU A C     
937  O O     . LEU A 164 ? 0.6496 0.2853 0.4745 0.1478  -0.1548 0.0491  136 LEU A O     
938  C CB    . LEU A 164 ? 0.6010 0.2783 0.4384 0.1478  -0.1402 0.0545  136 LEU A CB    
939  C CG    . LEU A 164 ? 0.6055 0.2743 0.4421 0.1377  -0.1461 0.0588  136 LEU A CG    
940  C CD1   . LEU A 164 ? 0.6086 0.2700 0.4312 0.1393  -0.1444 0.0489  136 LEU A CD1   
941  C CD2   . LEU A 164 ? 0.5891 0.2759 0.4409 0.1310  -0.1435 0.0709  136 LEU A CD2   
942  N N     . HIS A 165 ? 0.6316 0.2885 0.4605 0.1638  -0.1437 0.0438  137 HIS A N     
943  C CA    . HIS A 165 ? 0.6549 0.2992 0.4841 0.1648  -0.1485 0.0456  137 HIS A CA    
944  C C     . HIS A 165 ? 0.7153 0.3374 0.5289 0.1698  -0.1514 0.0342  137 HIS A C     
945  O O     . HIS A 165 ? 0.7391 0.3443 0.5498 0.1688  -0.1569 0.0351  137 HIS A O     
946  C CB    . HIS A 165 ? 0.6408 0.3008 0.4788 0.1721  -0.1438 0.0490  137 HIS A CB    
947  C CG    . HIS A 165 ? 0.6354 0.3047 0.4684 0.1837  -0.1374 0.0390  137 HIS A CG    
948  N ND1   . HIS A 165 ? 0.6215 0.3099 0.4569 0.1864  -0.1309 0.0369  137 HIS A ND1   
949  C CD2   . HIS A 165 ? 0.6470 0.3102 0.4735 0.1934  -0.1362 0.0306  137 HIS A CD2   
950  C CE1   . HIS A 165 ? 0.6714 0.3654 0.5024 0.1970  -0.1263 0.0276  137 HIS A CE1   
951  N NE2   . HIS A 165 ? 0.6343 0.3140 0.4603 0.2016  -0.1292 0.0238  137 HIS A NE2   
952  N N     . LEU A 166 ? 0.6897 0.3110 0.4926 0.1755  -0.1472 0.0236  138 LEU A N     
953  C CA    . LEU A 166 ? 0.6952 0.2953 0.4816 0.1797  -0.1490 0.0123  138 LEU A CA    
954  C C     . LEU A 166 ? 0.7630 0.3442 0.5394 0.1704  -0.1561 0.0116  138 LEU A C     
955  O O     . LEU A 166 ? 0.8411 0.4036 0.6015 0.1731  -0.1576 0.0018  138 LEU A O     
956  C CB    . LEU A 166 ? 0.6956 0.3045 0.4756 0.1900  -0.1403 0.0012  138 LEU A CB    
957  C CG    . LEU A 166 ? 0.7498 0.3619 0.5290 0.2021  -0.1356 -0.0055 138 LEU A CG    
958  C CD1   . LEU A 166 ? 0.8056 0.4317 0.5993 0.2041  -0.1356 0.0033  138 LEU A CD1   
959  C CD2   . LEU A 166 ? 0.7388 0.3658 0.5155 0.2101  -0.1260 -0.0152 138 LEU A CD2   
960  N N     . VAL A 167 ? 0.7221 0.3083 0.5073 0.1598  -0.1603 0.0217  139 VAL A N     
961  C CA    . VAL A 167 ? 0.7504 0.3210 0.5276 0.1503  -0.1680 0.0223  139 VAL A CA    
962  C C     . VAL A 167 ? 0.8216 0.3825 0.6057 0.1409  -0.1773 0.0314  139 VAL A C     
963  O O     . VAL A 167 ? 0.8426 0.4189 0.6433 0.1352  -0.1771 0.0430  139 VAL A O     
964  C CB    . VAL A 167 ? 0.7353 0.3207 0.5171 0.1455  -0.1652 0.0263  139 VAL A CB    
965  C CG1   . VAL A 167 ? 0.8381 0.4078 0.6114 0.1361  -0.1738 0.0273  139 VAL A CG1   
966  C CG2   . VAL A 167 ? 0.6924 0.2894 0.4686 0.1539  -0.1546 0.0170  139 VAL A CG2   
967  N N     . PRO A 168 ? 0.8312 0.3664 0.6028 0.1392  -0.1850 0.0266  140 PRO A N     
968  C CA    . PRO A 168 ? 0.8611 0.3861 0.6395 0.1297  -0.1942 0.0353  140 PRO A CA    
969  C C     . PRO A 168 ? 0.9659 0.4960 0.7524 0.1171  -0.2003 0.0446  140 PRO A C     
970  O O     . PRO A 168 ? 0.9978 0.5350 0.7995 0.1097  -0.2034 0.0560  140 PRO A O     
971  C CB    . PRO A 168 ? 0.8754 0.3697 0.6347 0.1311  -0.2008 0.0256  140 PRO A CB    
972  C CG    . PRO A 168 ? 0.8405 0.3344 0.5882 0.1443  -0.1923 0.0135  140 PRO A CG    
973  C CD    . PRO A 168 ? 0.8681 0.3835 0.6198 0.1469  -0.1846 0.0130  140 PRO A CD    
974  N N     . ASP A 169 ? 0.9441 0.4716 0.7212 0.1147  -0.2018 0.0405  141 ASP A N     
975  C CA    . ASP A 169 ? 0.9468 0.4798 0.7312 0.1033  -0.2079 0.0490  141 ASP A CA    
976  C C     . ASP A 169 ? 0.9303 0.4922 0.7284 0.1048  -0.1983 0.0549  141 ASP A C     
977  O O     . ASP A 169 ? 0.9516 0.5175 0.7418 0.1082  -0.1939 0.0496  141 ASP A O     
978  C CB    . ASP A 169 ? 1.0053 0.5171 0.7703 0.0998  -0.2159 0.0416  141 ASP A CB    
979  C CG    . ASP A 169 ? 1.0286 0.5419 0.8006 0.0868  -0.2255 0.0510  141 ASP A CG    
980  O OD1   . ASP A 169 ? 0.9851 0.5209 0.7780 0.0817  -0.2230 0.0629  141 ASP A OD1   
981  O OD2   . ASP A 169 ? 1.0374 0.5297 0.7938 0.0818  -0.2354 0.0465  141 ASP A OD2   
982  N N     . ASN A 170 ? 0.8902 0.4714 0.7081 0.1023  -0.1947 0.0659  142 ASN A N     
983  C CA    . ASN A 170 ? 0.8619 0.4699 0.6923 0.1041  -0.1850 0.0714  142 ASN A CA    
984  C C     . ASN A 170 ? 0.8539 0.4696 0.6891 0.0960  -0.1876 0.0774  142 ASN A C     
985  O O     . ASN A 170 ? 0.8329 0.4611 0.6674 0.0990  -0.1806 0.0759  142 ASN A O     
986  C CB    . ASN A 170 ? 0.8327 0.4581 0.6812 0.1043  -0.1803 0.0815  142 ASN A CB    
987  C CG    . ASN A 170 ? 0.8119 0.4416 0.6580 0.1154  -0.1728 0.0760  142 ASN A CG    
988  O OD1   . ASN A 170 ? 0.8749 0.4880 0.7086 0.1211  -0.1748 0.0669  142 ASN A OD1   
989  N ND2   . ASN A 170 ? 0.7081 0.3605 0.5659 0.1187  -0.1642 0.0815  142 ASN A ND2   
990  N N     . ARG A 171 ? 0.8440 0.4526 0.6842 0.0855  -0.1976 0.0844  143 ARG A N     
991  C CA    . ARG A 171 ? 0.8803 0.4989 0.7276 0.0777  -0.2002 0.0915  143 ARG A CA    
992  C C     . ARG A 171 ? 0.8818 0.4899 0.7114 0.0794  -0.2020 0.0827  143 ARG A C     
993  O O     . ARG A 171 ? 0.8919 0.5138 0.7256 0.0783  -0.1981 0.0861  143 ARG A O     
994  C CB    . ARG A 171 ? 0.9155 0.5281 0.7719 0.0660  -0.2117 0.1006  143 ARG A CB    
995  C CG    . ARG A 171 ? 0.8839 0.5076 0.7489 0.0578  -0.2155 0.1086  143 ARG A CG    
996  C CD    . ARG A 171 ? 0.8206 0.4538 0.7057 0.0480  -0.2207 0.1221  143 ARG A CD    
997  N NE    . ARG A 171 ? 0.9562 0.5757 0.8420 0.0459  -0.2259 0.1228  143 ARG A NE    
998  C CZ    . ARG A 171 ? 1.0590 0.6904 0.9625 0.0427  -0.2237 0.1334  143 ARG A CZ    
999  N NH1   . ARG A 171 ? 1.0071 0.6642 0.9288 0.0413  -0.2163 0.1441  143 ARG A NH1   
1000 N NH2   . ARG A 171 ? 1.1188 0.7351 1.0208 0.0412  -0.2286 0.1334  143 ARG A NH2   
1001 N N     . LEU A 172 ? 0.8660 0.4491 0.6750 0.0827  -0.2074 0.0714  144 LEU A N     
1002 C CA    . LEU A 172 ? 0.8700 0.4419 0.6597 0.0856  -0.2080 0.0625  144 LEU A CA    
1003 C C     . LEU A 172 ? 0.7955 0.3819 0.5835 0.0953  -0.1945 0.0578  144 LEU A C     
1004 O O     . LEU A 172 ? 0.7541 0.3462 0.5363 0.0951  -0.1906 0.0551  144 LEU A O     
1005 C CB    . LEU A 172 ? 0.8991 0.4403 0.6661 0.0883  -0.2153 0.0509  144 LEU A CB    
1006 C CG    . LEU A 172 ? 0.8366 0.3669 0.5817 0.0916  -0.2134 0.0392  144 LEU A CG    
1007 C CD1   . LEU A 172 ? 0.7379 0.2746 0.4836 0.0834  -0.2179 0.0446  144 LEU A CD1   
1008 C CD2   . LEU A 172 ? 0.8924 0.3928 0.6161 0.0931  -0.2206 0.0282  144 LEU A CD2   
1009 N N     . ALA A 173 ? 0.8053 0.4013 0.5998 0.1027  -0.1860 0.0561  145 ALA A N     
1010 C CA    . ALA A 173 ? 0.7545 0.3670 0.5491 0.1107  -0.1727 0.0510  145 ALA A CA    
1011 C C     . ALA A 173 ? 0.8134 0.4491 0.6239 0.1077  -0.1670 0.0611  145 ALA A C     
1012 O O     . ALA A 173 ? 0.7576 0.4052 0.5660 0.1100  -0.1577 0.0572  145 ALA A O     
1013 C CB    . ALA A 173 ? 0.7449 0.3602 0.5413 0.1197  -0.1669 0.0466  145 ALA A CB    
1014 N N     . VAL A 174 ? 0.7846 0.4309 0.6128 0.1014  -0.1700 0.0732  146 VAL A N     
1015 C CA    . VAL A 174 ? 0.6795 0.3481 0.5232 0.0983  -0.1641 0.0831  146 VAL A CA    
1016 C C     . VAL A 174 ? 0.7119 0.3785 0.5518 0.0928  -0.1680 0.0853  146 VAL A C     
1017 O O     . VAL A 174 ? 0.7023 0.3827 0.5465 0.0940  -0.1608 0.0883  146 VAL A O     
1018 C CB    . VAL A 174 ? 0.6762 0.3575 0.5400 0.0929  -0.1652 0.0954  146 VAL A CB    
1019 C CG1   . VAL A 174 ? 0.7115 0.4159 0.5909 0.0913  -0.1577 0.1054  146 VAL A CG1   
1020 C CG2   . VAL A 174 ? 0.7501 0.4323 0.6162 0.0988  -0.1617 0.0935  146 VAL A CG2   
1021 N N     . LYS A 175 ? 0.7294 0.3781 0.5605 0.0869  -0.1797 0.0839  147 LYS A N     
1022 C CA    . LYS A 175 ? 0.6921 0.3373 0.5170 0.0820  -0.1847 0.0853  147 LYS A CA    
1023 C C     . LYS A 175 ? 0.7461 0.3901 0.5557 0.0884  -0.1762 0.0754  147 LYS A C     
1024 O O     . LYS A 175 ? 0.7759 0.4324 0.5891 0.0879  -0.1706 0.0790  147 LYS A O     
1025 C CB    . LYS A 175 ? 0.6824 0.3054 0.4966 0.0751  -0.1995 0.0834  147 LYS A CB    
1026 C CG    . LYS A 175 ? 0.7265 0.3534 0.5575 0.0654  -0.2083 0.0941  147 LYS A CG    
1027 C CD    . LYS A 175 ? 0.7280 0.3421 0.5523 0.0563  -0.2224 0.0962  147 LYS A CD    
1028 C CE    . LYS A 175 ? 0.7533 0.3589 0.5859 0.0472  -0.2343 0.1020  147 LYS A CE    
1029 N NZ    . LYS A 175 ? 0.8208 0.4510 0.6808 0.0425  -0.2306 0.1157  147 LYS A NZ    
1030 N N     . ASN A 176 ? 0.7334 0.3646 0.5269 0.0940  -0.1736 0.0623  148 ASN A N     
1031 C CA    . ASN A 176 ? 0.7265 0.3584 0.5062 0.0989  -0.1641 0.0517  148 ASN A CA    
1032 C C     . ASN A 176 ? 0.6781 0.3318 0.4679 0.1036  -0.1499 0.0527  148 ASN A C     
1033 O O     . ASN A 176 ? 0.7011 0.3602 0.4851 0.1047  -0.1424 0.0493  148 ASN A O     
1034 C CB    . ASN A 176 ? 0.7372 0.3527 0.5000 0.1046  -0.1634 0.0381  148 ASN A CB    
1035 C CG    . ASN A 176 ? 0.7448 0.3360 0.4912 0.1004  -0.1758 0.0341  148 ASN A CG    
1036 O OD1   . ASN A 176 ? 0.7676 0.3551 0.5135 0.0929  -0.1845 0.0404  148 ASN A OD1   
1037 N ND2   . ASN A 176 ? 0.7711 0.3458 0.5037 0.1053  -0.1766 0.0236  148 ASN A ND2   
1038 N N     . ILE A 177 ? 0.6247 0.2903 0.4286 0.1062  -0.1460 0.0572  149 ILE A N     
1039 C CA    . ILE A 177 ? 0.6502 0.3363 0.4641 0.1095  -0.1336 0.0593  149 ILE A CA    
1040 C C     . ILE A 177 ? 0.7274 0.4243 0.5519 0.1046  -0.1335 0.0706  149 ILE A C     
1041 O O     . ILE A 177 ? 0.8026 0.5110 0.6285 0.1065  -0.1234 0.0702  149 ILE A O     
1042 C CB    . ILE A 177 ? 0.6097 0.3051 0.4349 0.1135  -0.1306 0.0617  149 ILE A CB    
1043 C CG1   . ILE A 177 ? 0.5783 0.2664 0.3934 0.1201  -0.1281 0.0497  149 ILE A CG1   
1044 C CG2   . ILE A 177 ? 0.5770 0.2934 0.4135 0.1156  -0.1194 0.0659  149 ILE A CG2   
1045 C CD1   . ILE A 177 ? 0.5964 0.2906 0.4209 0.1241  -0.1277 0.0525  149 ILE A CD1   
1046 N N     . HIS A 178 ? 0.7420 0.4352 0.5742 0.0983  -0.1446 0.0811  150 HIS A N     
1047 C CA    . HIS A 178 ? 0.7297 0.4336 0.5730 0.0939  -0.1453 0.0926  150 HIS A CA    
1048 C C     . HIS A 178 ? 0.7574 0.4561 0.5887 0.0925  -0.1452 0.0890  150 HIS A C     
1049 O O     . HIS A 178 ? 0.7671 0.4772 0.6046 0.0923  -0.1397 0.0951  150 HIS A O     
1050 C CB    . HIS A 178 ? 0.7114 0.4162 0.5682 0.0862  -0.1563 0.1038  150 HIS A CB    
1051 C CG    . HIS A 178 ? 0.7343 0.4558 0.6069 0.0813  -0.1553 0.1158  150 HIS A CG    
1052 N ND1   . HIS A 178 ? 0.7656 0.4834 0.6346 0.0763  -0.1621 0.1185  150 HIS A ND1   
1053 C CD2   . HIS A 178 ? 0.7343 0.4764 0.6258 0.0815  -0.1479 0.1260  150 HIS A CD2   
1054 C CE1   . HIS A 178 ? 0.8008 0.5370 0.6871 0.0737  -0.1589 0.1298  150 HIS A CE1   
1055 N NE2   . HIS A 178 ? 0.7938 0.5446 0.6936 0.0770  -0.1499 0.1344  150 HIS A NE2   
1056 N N     . LYS A 179 ? 0.7582 0.4390 0.5714 0.0919  -0.1509 0.0794  151 LYS A N     
1057 C CA    . LYS A 179 ? 0.7440 0.4191 0.5433 0.0913  -0.1499 0.0752  151 LYS A CA    
1058 C C     . LYS A 179 ? 0.7266 0.4099 0.5208 0.0972  -0.1345 0.0680  151 LYS A C     
1059 O O     . LYS A 179 ? 0.7468 0.4334 0.5374 0.0969  -0.1302 0.0696  151 LYS A O     
1060 C CB    . LYS A 179 ? 0.7559 0.4091 0.5354 0.0898  -0.1589 0.0659  151 LYS A CB    
1061 C CG    . LYS A 179 ? 0.7732 0.4152 0.5537 0.0822  -0.1755 0.0723  151 LYS A CG    
1062 C CD    . LYS A 179 ? 0.8572 0.4759 0.6147 0.0815  -0.1830 0.0613  151 LYS A CD    
1063 C CE    . LYS A 179 ? 1.0200 0.6254 0.7767 0.0730  -0.2003 0.0666  151 LYS A CE    
1064 N NZ    . LYS A 179 ? 1.1055 0.6864 0.8377 0.0727  -0.2073 0.0549  151 LYS A NZ    
1065 N N     . LEU A 180 ? 0.7248 0.4116 0.5190 0.1026  -0.1264 0.0602  152 LEU A N     
1066 C CA    . LEU A 180 ? 0.5917 0.2850 0.3800 0.1075  -0.1125 0.0517  152 LEU A CA    
1067 C C     . LEU A 180 ? 0.6807 0.3920 0.4826 0.1086  -0.1024 0.0582  152 LEU A C     
1068 O O     . LEU A 180 ? 0.6651 0.3812 0.4622 0.1112  -0.0912 0.0528  152 LEU A O     
1069 C CB    . LEU A 180 ? 0.6013 0.2925 0.3850 0.1127  -0.1084 0.0409  152 LEU A CB    
1070 C CG    . LEU A 180 ? 0.6153 0.2881 0.3815 0.1139  -0.1138 0.0309  152 LEU A CG    
1071 C CD1   . LEU A 180 ? 0.6064 0.2782 0.3729 0.1192  -0.1123 0.0237  152 LEU A CD1   
1072 C CD2   . LEU A 180 ? 0.6953 0.3639 0.4460 0.1153  -0.1065 0.0227  152 LEU A CD2   
1073 N N     . LEU A 181 ? 0.6391 0.3598 0.4573 0.1067  -0.1056 0.0696  153 LEU A N     
1074 C CA    . LEU A 181 ? 0.6861 0.4233 0.5169 0.1085  -0.0957 0.0756  153 LEU A CA    
1075 C C     . LEU A 181 ? 0.6841 0.4248 0.5185 0.1059  -0.0954 0.0847  153 LEU A C     
1076 O O     . LEU A 181 ? 0.6642 0.3992 0.4994 0.1016  -0.1062 0.0916  153 LEU A O     
1077 C CB    . LEU A 181 ? 0.6669 0.4135 0.5133 0.1086  -0.0980 0.0837  153 LEU A CB    
1078 C CG    . LEU A 181 ? 0.6312 0.3792 0.4768 0.1126  -0.0952 0.0762  153 LEU A CG    
1079 C CD1   . LEU A 181 ? 0.6745 0.4280 0.5339 0.1117  -0.1007 0.0857  153 LEU A CD1   
1080 C CD2   . LEU A 181 ? 0.6869 0.4457 0.5314 0.1169  -0.0813 0.0694  153 LEU A CD2   
1081 N N     . VAL A 182 ? 0.7194 0.4692 0.5557 0.1087  -0.0832 0.0846  154 VAL A N     
1082 C CA    . VAL A 182 ? 0.6891 0.4444 0.5316 0.1077  -0.0811 0.0946  154 VAL A CA    
1083 C C     . VAL A 182 ? 0.6996 0.4665 0.5610 0.1066  -0.0847 0.1078  154 VAL A C     
1084 O O     . VAL A 182 ? 0.6951 0.4681 0.5638 0.1080  -0.0831 0.1078  154 VAL A O     
1085 C CB    . VAL A 182 ? 0.5941 0.3542 0.4329 0.1113  -0.0663 0.0904  154 VAL A CB    
1086 C CG1   . VAL A 182 ? 0.6058 0.3550 0.4265 0.1117  -0.0626 0.0783  154 VAL A CG1   
1087 C CG2   . VAL A 182 ? 0.5764 0.3475 0.4227 0.1145  -0.0569 0.0878  154 VAL A CG2   
1088 N N     . PRO A 183 ? 0.6314 0.4020 0.5013 0.1042  -0.0896 0.1197  155 PRO A N     
1089 C CA    . PRO A 183 ? 0.6254 0.4092 0.5148 0.1036  -0.0911 0.1331  155 PRO A CA    
1090 C C     . PRO A 183 ? 0.6600 0.4556 0.5558 0.1088  -0.0769 0.1332  155 PRO A C     
1091 O O     . PRO A 183 ? 0.7408 0.5385 0.6328 0.1121  -0.0663 0.1312  155 PRO A O     
1092 C CB    . PRO A 183 ? 0.6503 0.4369 0.5458 0.1014  -0.0961 0.1444  155 PRO A CB    
1093 C CG    . PRO A 183 ? 0.7304 0.5020 0.6095 0.0984  -0.1042 0.1375  155 PRO A CG    
1094 C CD    . PRO A 183 ? 0.6971 0.4600 0.5593 0.1017  -0.0957 0.1220  155 PRO A CD    
1095 N N     . GLY A 184 ? 0.6922 0.4944 0.5968 0.1094  -0.0770 0.1354  156 GLY A N     
1096 C CA    . GLY A 184 ? 0.6668 0.4789 0.5749 0.1141  -0.0646 0.1338  156 GLY A CA    
1097 C C     . GLY A 184 ? 0.7320 0.5401 0.6291 0.1162  -0.0602 0.1199  156 GLY A C     
1098 O O     . GLY A 184 ? 0.7927 0.6091 0.6923 0.1196  -0.0514 0.1180  156 GLY A O     
1099 N N     . GLY A 185 ? 0.7250 0.5210 0.6099 0.1146  -0.0659 0.1102  157 GLY A N     
1100 C CA    . GLY A 185 ? 0.7059 0.4992 0.5817 0.1170  -0.0624 0.0976  157 GLY A CA    
1101 C C     . GLY A 185 ? 0.6314 0.4277 0.5138 0.1175  -0.0677 0.0997  157 GLY A C     
1102 O O     . GLY A 185 ? 0.6911 0.4864 0.5820 0.1146  -0.0772 0.1091  157 GLY A O     
1103 N N     . GLU A 186 ? 0.6846 0.4847 0.5632 0.1210  -0.0618 0.0911  158 GLU A N     
1104 C CA    . GLU A 186 ? 0.7158 0.5201 0.6002 0.1226  -0.0651 0.0931  158 GLU A CA    
1105 C C     . GLU A 186 ? 0.6800 0.4747 0.5555 0.1236  -0.0708 0.0832  158 GLU A C     
1106 O O     . GLU A 186 ? 0.6517 0.4401 0.5160 0.1245  -0.0683 0.0724  158 GLU A O     
1107 C CB    . GLU A 186 ? 0.7301 0.5478 0.6177 0.1264  -0.0544 0.0919  158 GLU A CB    
1108 C CG    . GLU A 186 ? 0.7577 0.5847 0.6535 0.1265  -0.0474 0.1013  158 GLU A CG    
1109 C CD    . GLU A 186 ? 0.8203 0.6578 0.7150 0.1301  -0.0356 0.0972  158 GLU A CD    
1110 O OE1   . GLU A 186 ? 0.8358 0.6723 0.7210 0.1314  -0.0305 0.0849  158 GLU A OE1   
1111 O OE2   . GLU A 186 ? 0.8342 0.6810 0.7372 0.1315  -0.0314 0.1061  158 GLU A OE2   
1112 N N     . ALA A 187 ? 0.6425 0.4357 0.5231 0.1239  -0.0781 0.0875  159 ALA A N     
1113 C CA    . ALA A 187 ? 0.5629 0.3470 0.4363 0.1260  -0.0835 0.0794  159 ALA A CA    
1114 C C     . ALA A 187 ? 0.5773 0.3703 0.4560 0.1301  -0.0816 0.0806  159 ALA A C     
1115 O O     . ALA A 187 ? 0.5927 0.3931 0.4817 0.1294  -0.0822 0.0914  159 ALA A O     
1116 C CB    . ALA A 187 ? 0.5560 0.3248 0.4282 0.1221  -0.0964 0.0833  159 ALA A CB    
1117 N N     . VAL A 188 ? 0.5449 0.3381 0.4167 0.1346  -0.0792 0.0698  160 VAL A N     
1118 C CA    . VAL A 188 ? 0.4841 0.2864 0.3595 0.1392  -0.0774 0.0697  160 VAL A CA    
1119 C C     . VAL A 188 ? 0.6071 0.3978 0.4785 0.1418  -0.0857 0.0663  160 VAL A C     
1120 O O     . VAL A 188 ? 0.6138 0.3975 0.4761 0.1440  -0.0857 0.0555  160 VAL A O     
1121 C CB    . VAL A 188 ? 0.4754 0.2904 0.3473 0.1427  -0.0669 0.0602  160 VAL A CB    
1122 C CG1   . VAL A 188 ? 0.5011 0.3253 0.3756 0.1477  -0.0665 0.0597  160 VAL A CG1   
1123 C CG2   . VAL A 188 ? 0.4664 0.2909 0.3415 0.1403  -0.0584 0.0638  160 VAL A CG2   
1124 N N     . PHE A 189 ? 0.5822 0.3705 0.4602 0.1418  -0.0923 0.0756  161 PHE A N     
1125 C CA    . PHE A 189 ? 0.5955 0.3709 0.4701 0.1445  -0.1005 0.0739  161 PHE A CA    
1126 C C     . PHE A 189 ? 0.6268 0.4117 0.5036 0.1510  -0.0982 0.0730  161 PHE A C     
1127 O O     . PHE A 189 ? 0.6512 0.4499 0.5349 0.1517  -0.0940 0.0797  161 PHE A O     
1128 C CB    . PHE A 189 ? 0.5698 0.3331 0.4497 0.1393  -0.1106 0.0852  161 PHE A CB    
1129 C CG    . PHE A 189 ? 0.5834 0.3362 0.4607 0.1327  -0.1151 0.0861  161 PHE A CG    
1130 C CD1   . PHE A 189 ? 0.6041 0.3655 0.4890 0.1278  -0.1126 0.0943  161 PHE A CD1   
1131 C CD2   . PHE A 189 ? 0.5876 0.3222 0.4545 0.1319  -0.1219 0.0789  161 PHE A CD2   
1132 C CE1   . PHE A 189 ? 0.6433 0.3962 0.5260 0.1221  -0.1174 0.0957  161 PHE A CE1   
1133 C CE2   . PHE A 189 ? 0.6282 0.3533 0.4915 0.1258  -0.1267 0.0798  161 PHE A CE2   
1134 C CZ    . PHE A 189 ? 0.6658 0.4005 0.5374 0.1208  -0.1247 0.0884  161 PHE A CZ    
1135 N N     . SER A 190 ? 0.6192 0.3966 0.4896 0.1563  -0.1009 0.0649  162 SER A N     
1136 C CA    . SER A 190 ? 0.5519 0.3360 0.4239 0.1633  -0.1007 0.0645  162 SER A CA    
1137 C C     . SER A 190 ? 0.5519 0.3173 0.4207 0.1658  -0.1100 0.0651  162 SER A C     
1138 O O     . SER A 190 ? 0.6026 0.3635 0.4653 0.1720  -0.1103 0.0561  162 SER A O     
1139 C CB    . SER A 190 ? 0.6342 0.4316 0.5025 0.1686  -0.0930 0.0525  162 SER A CB    
1140 O OG    . SER A 190 ? 0.6258 0.4323 0.4966 0.1753  -0.0930 0.0531  162 SER A OG    
1141 N N     . VAL A 191 ? 0.5439 0.2997 0.4179 0.1600  -0.1166 0.0757  163 VAL A N     
1142 C CA    . VAL A 191 ? 0.5602 0.2995 0.4331 0.1581  -0.1238 0.0759  163 VAL A CA    
1143 C C     . VAL A 191 ? 0.5637 0.3080 0.4414 0.1630  -0.1238 0.0795  163 VAL A C     
1144 O O     . VAL A 191 ? 0.5886 0.3477 0.4750 0.1626  -0.1207 0.0880  163 VAL A O     
1145 C CB    . VAL A 191 ? 0.5650 0.2964 0.4443 0.1471  -0.1292 0.0852  163 VAL A CB    
1146 C CG1   . VAL A 191 ? 0.5846 0.2962 0.4604 0.1450  -0.1370 0.0843  163 VAL A CG1   
1147 C CG2   . VAL A 191 ? 0.5814 0.3105 0.4567 0.1424  -0.1289 0.0828  163 VAL A CG2   
1148 N N     . ILE A 192 ? 0.5777 0.3095 0.4492 0.1680  -0.1272 0.0731  164 ILE A N     
1149 C CA    . ILE A 192 ? 0.5844 0.3180 0.4601 0.1726  -0.1281 0.0769  164 ILE A CA    
1150 C C     . ILE A 192 ? 0.5965 0.3177 0.4779 0.1647  -0.1338 0.0867  164 ILE A C     
1151 O O     . ILE A 192 ? 0.6116 0.3131 0.4870 0.1616  -0.1395 0.0833  164 ILE A O     
1152 C CB    . ILE A 192 ? 0.5949 0.3212 0.4618 0.1825  -0.1283 0.0658  164 ILE A CB    
1153 C CG1   . ILE A 192 ? 0.5822 0.3248 0.4459 0.1908  -0.1220 0.0573  164 ILE A CG1   
1154 C CG2   . ILE A 192 ? 0.6056 0.3299 0.4767 0.1864  -0.1304 0.0708  164 ILE A CG2   
1155 C CD1   . ILE A 192 ? 0.5913 0.3294 0.4476 0.2011  -0.1213 0.0461  164 ILE A CD1   
1156 N N     . ALA A 193 ? 0.6332 0.3657 0.5254 0.1617  -0.1324 0.0988  165 ALA A N     
1157 C CA    . ALA A 193 ? 0.6224 0.3453 0.5212 0.1545  -0.1369 0.1094  165 ALA A CA    
1158 C C     . ALA A 193 ? 0.7063 0.4127 0.6006 0.1586  -0.1412 0.1070  165 ALA A C     
1159 O O     . ALA A 193 ? 0.8026 0.4885 0.6915 0.1547  -0.1472 0.1041  165 ALA A O     
1160 C CB    . ALA A 193 ? 0.6718 0.4118 0.5825 0.1521  -0.1329 0.1229  165 ALA A CB    
1161 N N     . ASN A 194 ? 0.7278 0.4426 0.6238 0.1666  -0.1384 0.1082  166 ASN A N     
1162 C CA    . ASN A 194 ? 0.7024 0.4030 0.5948 0.1718  -0.1416 0.1067  166 ASN A CA    
1163 C C     . ASN A 194 ? 0.6820 0.3938 0.5716 0.1835  -0.1379 0.1002  166 ASN A C     
1164 O O     . ASN A 194 ? 0.6943 0.4266 0.5868 0.1866  -0.1331 0.1001  166 ASN A O     
1165 C CB    . ASN A 194 ? 0.7372 0.4349 0.6381 0.1678  -0.1432 0.1205  166 ASN A CB    
1166 C CG    . ASN A 194 ? 0.8046 0.5246 0.7142 0.1706  -0.1380 0.1299  166 ASN A CG    
1167 O OD1   . ASN A 194 ? 0.8083 0.5356 0.7173 0.1792  -0.1362 0.1286  166 ASN A OD1   
1168 N ND2   . ASN A 194 ? 0.8316 0.5628 0.7489 0.1637  -0.1355 0.1395  166 ASN A ND2   
1169 N N     . MET A 195 ? 0.7658 0.4638 0.6495 0.1902  -0.1403 0.0946  167 MET A N     
1170 C CA    . MET A 195 ? 0.8126 0.5209 0.6946 0.2019  -0.1373 0.0892  167 MET A CA    
1171 C C     . MET A 195 ? 0.8131 0.5032 0.6914 0.2073  -0.1406 0.0880  167 MET A C     
1172 O O     . MET A 195 ? 0.8201 0.4876 0.6938 0.2026  -0.1451 0.0876  167 MET A O     
1173 C CB    . MET A 195 ? 0.6797 0.3954 0.5548 0.2075  -0.1341 0.0759  167 MET A CB    
1174 C CG    . MET A 195 ? 0.7204 0.4168 0.5857 0.2046  -0.1366 0.0668  167 MET A CG    
1175 S SD    . MET A 195 ? 0.7833 0.4910 0.6416 0.2105  -0.1314 0.0531  167 MET A SD    
1176 C CE    . MET A 195 ? 0.6854 0.4140 0.5478 0.2235  -0.1271 0.0505  167 MET A CE    
1177 N N     . ALA A 196 ? 0.7291 0.4291 0.6090 0.2174  -0.1384 0.0873  168 ALA A N     
1178 C CA    . ALA A 196 ? 0.7859 0.4701 0.6630 0.2239  -0.1408 0.0869  168 ALA A CA    
1179 C C     . ALA A 196 ? 0.8208 0.4881 0.6869 0.2290  -0.1417 0.0736  168 ALA A C     
1180 O O     . ALA A 196 ? 0.8671 0.5146 0.7287 0.2324  -0.1443 0.0727  168 ALA A O     
1181 C CB    . ALA A 196 ? 0.8013 0.5027 0.6839 0.2336  -0.1384 0.0902  168 ALA A CB    
1182 N N     . LEU A 197 ? 0.7641 0.4379 0.6251 0.2299  -0.1392 0.0634  169 LEU A N     
1183 C CA    . LEU A 197 ? 0.7887 0.4459 0.6383 0.2343  -0.1395 0.0510  169 LEU A CA    
1184 C C     . LEU A 197 ? 0.8768 0.5058 0.7192 0.2257  -0.1452 0.0515  169 LEU A C     
1185 O O     . LEU A 197 ? 0.8938 0.5024 0.7265 0.2298  -0.1470 0.0445  169 LEU A O     
1186 C CB    . LEU A 197 ? 0.7868 0.4562 0.6324 0.2357  -0.1355 0.0412  169 LEU A CB    
1187 C CG    . LEU A 197 ? 0.7042 0.4008 0.5548 0.2444  -0.1297 0.0372  169 LEU A CG    
1188 C CD1   . LEU A 197 ? 0.7233 0.4253 0.5679 0.2450  -0.1260 0.0265  169 LEU A CD1   
1189 C CD2   . LEU A 197 ? 0.7268 0.4271 0.5785 0.2567  -0.1281 0.0343  169 LEU A CD2   
1190 N N     . CYS A 198 ? 0.8853 0.5133 0.7321 0.2138  -0.1482 0.0597  170 CYS A N     
1191 C CA    . CYS A 198 ? 0.9020 0.5049 0.7427 0.2045  -0.1545 0.0605  170 CYS A CA    
1192 C C     . CYS A 198 ? 0.9216 0.5063 0.7627 0.2049  -0.1583 0.0666  170 CYS A C     
1193 O O     . CYS A 198 ? 0.9301 0.4893 0.7611 0.2036  -0.1628 0.0615  170 CYS A O     
1194 C CB    . CYS A 198 ? 0.9162 0.5262 0.7636 0.1920  -0.1562 0.0684  170 CYS A CB    
1195 S SG    . CYS A 198 ? 0.9744 0.5967 0.8180 0.1895  -0.1532 0.0604  170 CYS A SG    
1196 N N     . ASP A 199 ? 0.9372 0.5341 0.7892 0.2065  -0.1566 0.0775  171 ASP A N     
1197 C CA    . ASP A 199 ? 0.9187 0.4987 0.7716 0.2074  -0.1596 0.0842  171 ASP A CA    
1198 C C     . ASP A 199 ? 0.9333 0.5014 0.7780 0.2196  -0.1586 0.0756  171 ASP A C     
1199 O O     . ASP A 199 ? 0.9476 0.4909 0.7861 0.2197  -0.1623 0.0753  171 ASP A O     
1200 C CB    . ASP A 199 ? 0.9117 0.5090 0.7777 0.2070  -0.1573 0.0983  171 ASP A CB    
1201 C CG    . ASP A 199 ? 1.0122 0.6191 0.8865 0.1950  -0.1579 0.1080  171 ASP A CG    
1202 O OD1   . ASP A 199 ? 0.9993 0.5908 0.8703 0.1851  -0.1625 0.1077  171 ASP A OD1   
1203 O OD2   . ASP A 199 ? 1.0454 0.6755 0.9292 0.1954  -0.1538 0.1160  171 ASP A OD2   
1204 N N     . ALA A 200 ? 0.8836 0.4694 0.7283 0.2300  -0.1535 0.0686  172 ALA A N     
1205 C CA    . ALA A 200 ? 0.8635 0.4400 0.7008 0.2422  -0.1517 0.0597  172 ALA A CA    
1206 C C     . ALA A 200 ? 0.8841 0.4351 0.7066 0.2408  -0.1543 0.0485  172 ALA A C     
1207 O O     . ALA A 200 ? 0.9019 0.4347 0.7166 0.2480  -0.1546 0.0434  172 ALA A O     
1208 C CB    . ALA A 200 ? 0.8342 0.4370 0.6752 0.2527  -0.1457 0.0540  172 ALA A CB    
1209 N N     . TYR A 201 ? 0.9293 0.4784 0.7473 0.2318  -0.1561 0.0446  173 TYR A N     
1210 C CA    . TYR A 201 ? 0.9252 0.4489 0.7280 0.2289  -0.1597 0.0348  173 TYR A CA    
1211 C C     . TYR A 201 ? 0.9436 0.4397 0.7425 0.2213  -0.1668 0.0400  173 TYR A C     
1212 O O     . TYR A 201 ? 0.9847 0.4563 0.7712 0.2245  -0.1689 0.0329  173 TYR A O     
1213 C CB    . TYR A 201 ? 0.8977 0.4274 0.6974 0.2207  -0.1603 0.0308  173 TYR A CB    
1214 C CG    . TYR A 201 ? 0.8598 0.4057 0.6561 0.2288  -0.1537 0.0205  173 TYR A CG    
1215 C CD1   . TYR A 201 ? 0.8513 0.3991 0.6437 0.2421  -0.1486 0.0127  173 TYR A CD1   
1216 C CD2   . TYR A 201 ? 0.8397 0.3992 0.6371 0.2232  -0.1523 0.0190  173 TYR A CD2   
1217 C CE1   . TYR A 201 ? 0.8166 0.3803 0.6069 0.2492  -0.1422 0.0035  173 TYR A CE1   
1218 C CE2   . TYR A 201 ? 0.8422 0.4161 0.6367 0.2303  -0.1460 0.0098  173 TYR A CE2   
1219 C CZ    . TYR A 201 ? 0.8489 0.4251 0.6400 0.2431  -0.1409 0.0020  173 TYR A CZ    
1220 O OH    . TYR A 201 ? 0.8788 0.4704 0.6681 0.2500  -0.1342 -0.0069 173 TYR A OH    
1221 N N     . GLU A 202 ? 0.8866 0.3864 0.6958 0.2112  -0.1702 0.0523  174 GLU A N     
1222 C CA    . GLU A 202 ? 0.9144 0.3889 0.7209 0.2026  -0.1772 0.0577  174 GLU A CA    
1223 C C     . GLU A 202 ? 0.9792 0.4403 0.7852 0.2107  -0.1767 0.0606  174 GLU A C     
1224 O O     . GLU A 202 ? 1.0218 0.4549 0.8194 0.2073  -0.1819 0.0595  174 GLU A O     
1225 C CB    . GLU A 202 ? 0.9111 0.3960 0.7303 0.1902  -0.1799 0.0709  174 GLU A CB    
1226 C CG    . GLU A 202 ? 0.9532 0.4441 0.7717 0.1799  -0.1825 0.0689  174 GLU A CG    
1227 C CD    . GLU A 202 ? 1.0402 0.5482 0.8736 0.1699  -0.1828 0.0824  174 GLU A CD    
1228 O OE1   . GLU A 202 ? 1.0579 0.5848 0.9029 0.1738  -0.1778 0.0913  174 GLU A OE1   
1229 O OE2   . GLU A 202 ? 1.0762 0.5791 0.9097 0.1582  -0.1881 0.0843  174 GLU A OE2   
1230 N N     . GLU A 203 ? 0.9705 0.4507 0.7852 0.2212  -0.1707 0.0643  175 GLU A N     
1231 C CA    . GLU A 203 ? 0.9932 0.4614 0.8077 0.2301  -0.1699 0.0671  175 GLU A CA    
1232 C C     . GLU A 203 ? 1.0142 0.4655 0.8148 0.2404  -0.1684 0.0538  175 GLU A C     
1233 O O     . GLU A 203 ? 1.0914 0.5180 0.8853 0.2433  -0.1705 0.0531  175 GLU A O     
1234 C CB    . GLU A 203 ? 0.9765 0.4714 0.8045 0.2381  -0.1646 0.0756  175 GLU A CB    
1235 C CG    . GLU A 203 ? 1.0003 0.5088 0.8414 0.2292  -0.1654 0.0905  175 GLU A CG    
1236 C CD    . GLU A 203 ? 1.0666 0.5968 0.9191 0.2376  -0.1610 0.0995  175 GLU A CD    
1237 O OE1   . GLU A 203 ? 1.1070 0.6416 0.9578 0.2503  -0.1580 0.0942  175 GLU A OE1   
1238 O OE2   . GLU A 203 ? 1.1094 0.6527 0.9722 0.2317  -0.1607 0.1119  175 GLU A OE2   
1239 N N     . MET A 204 ? 0.9518 0.4158 0.7478 0.2461  -0.1643 0.0431  176 MET A N     
1240 C CA    . MET A 204 ? 0.9684 0.4180 0.7511 0.2560  -0.1618 0.0303  176 MET A CA    
1241 C C     . MET A 204 ? 1.0377 0.4557 0.8041 0.2483  -0.1676 0.0231  176 MET A C     
1242 O O     . MET A 204 ? 1.0777 0.4751 0.8319 0.2552  -0.1669 0.0149  176 MET A O     
1243 C CB    . MET A 204 ? 0.9217 0.3945 0.7043 0.2635  -0.1554 0.0213  176 MET A CB    
1244 C CG    . MET A 204 ? 0.9209 0.4231 0.7171 0.2736  -0.1497 0.0258  176 MET A CG    
1245 S SD    . MET A 204 ? 0.8775 0.4076 0.6745 0.2808  -0.1425 0.0153  176 MET A SD    
1246 C CE    . MET A 204 ? 0.9050 0.4159 0.6870 0.2921  -0.1388 0.0014  176 MET A CE    
1247 N N     . ALA A 205 ? 1.0398 0.4541 0.8059 0.2340  -0.1734 0.0262  177 ALA A N     
1248 C CA    . ALA A 205 ? 1.0549 0.4403 0.8056 0.2255  -0.1801 0.0197  177 ALA A CA    
1249 C C     . ALA A 205 ? 1.1022 0.4582 0.8478 0.2235  -0.1851 0.0230  177 ALA A C     
1250 O O     . ALA A 205 ? 1.1552 0.4838 0.8851 0.2195  -0.1901 0.0155  177 ALA A O     
1251 C CB    . ALA A 205 ? 1.0226 0.4133 0.7765 0.2104  -0.1857 0.0238  177 ALA A CB    
1252 N N     . LYS A 206 ? 1.0849 0.4455 0.8427 0.2260  -0.1840 0.0342  178 LYS A N     
1253 C CA    . LYS A 206 ? 1.1379 0.4710 0.8919 0.2247  -0.1881 0.0382  178 LYS A CA    
1254 C C     . LYS A 206 ? 1.2400 0.5601 0.9859 0.2396  -0.1834 0.0313  178 LYS A C     
1255 O O     . LYS A 206 ? 1.2511 0.5439 0.9904 0.2395  -0.1865 0.0323  178 LYS A O     
1256 C CB    . LYS A 206 ? 1.0869 0.4300 0.8577 0.2202  -0.1888 0.0544  178 LYS A CB    
1257 C CG    . LYS A 206 ? 1.0986 0.4500 0.8774 0.2043  -0.1939 0.0627  178 LYS A CG    
1258 C CD    . LYS A 206 ? 1.1260 0.4898 0.9214 0.2012  -0.1929 0.0790  178 LYS A CD    
1259 C CE    . LYS A 206 ? 0.9998 0.3748 0.8045 0.1862  -0.1969 0.0874  178 LYS A CE    
1260 N NZ    . LYS A 206 ? 1.1027 0.4926 0.9233 0.1840  -0.1945 0.1035  178 LYS A NZ    
1261 N N     . GLU A 207 ? 1.2153 0.5540 0.9618 0.2523  -0.1759 0.0247  179 GLU A N     
1262 C CA    . GLU A 207 ? 1.2359 0.5645 0.9755 0.2672  -0.1708 0.0180  179 GLU A CA    
1263 C C     . GLU A 207 ? 1.2516 0.5521 0.9702 0.2668  -0.1727 0.0046  179 GLU A C     
1264 O O     . GLU A 207 ? 1.2833 0.5894 0.9942 0.2642  -0.1721 -0.0043 179 GLU A O     
1265 C CB    . GLU A 207 ? 1.2111 0.5706 0.9588 0.2803  -0.1624 0.0150  179 GLU A CB    
1266 C CG    . GLU A 207 ? 1.2322 0.6201 0.9993 0.2826  -0.1602 0.0275  179 GLU A CG    
1267 C CD    . GLU A 207 ? 1.2002 0.6174 0.9746 0.2958  -0.1526 0.0240  179 GLU A CD    
1268 O OE1   . GLU A 207 ? 1.1691 0.5818 0.9350 0.3061  -0.1481 0.0133  179 GLU A OE1   
1269 O OE2   . GLU A 207 ? 1.1664 0.6116 0.9551 0.2957  -0.1510 0.0319  179 GLU A OE2   
1270 N N     . PRO A 208 ? 1.2678 0.5376 0.9763 0.2691  -0.1748 0.0027  180 PRO A N     
1271 C CA    . PRO A 208 ? 1.2616 0.5056 0.9490 0.2706  -0.1755 -0.0110 180 PRO A CA    
1272 C C     . PRO A 208 ? 1.2373 0.4958 0.9198 0.2841  -0.1666 -0.0218 180 PRO A C     
1273 O O     . PRO A 208 ? 1.2517 0.4989 0.9180 0.2832  -0.1663 -0.0333 180 PRO A O     
1274 C CB    . PRO A 208 ? 1.3383 0.5515 1.0194 0.2741  -0.1773 -0.0093 180 PRO A CB    
1275 C CG    . PRO A 208 ? 1.2915 0.5082 0.9881 0.2669  -0.1814 0.0059  180 PRO A CG    
1276 C CD    . PRO A 208 ? 1.2389 0.4949 0.9540 0.2694  -0.1770 0.0132  180 PRO A CD    
1277 N N     . ARG A 209 ? 1.2314 0.5152 0.9280 0.2964  -0.1593 -0.0180 181 ARG A N     
1278 C CA    . ARG A 209 ? 1.1489 0.4535 0.8453 0.3085  -0.1506 -0.0265 181 ARG A CA    
1279 C C     . ARG A 209 ? 1.1371 0.4551 0.8291 0.3010  -0.1507 -0.0329 181 ARG A C     
1280 O O     . ARG A 209 ? 1.1214 0.4394 0.8024 0.3065  -0.1456 -0.0440 181 ARG A O     
1281 C CB    . ARG A 209 ? 1.1536 0.4887 0.8696 0.3188  -0.1452 -0.0185 181 ARG A CB    
1282 C CG    . ARG A 209 ? 1.1018 0.4633 0.8219 0.3313  -0.1363 -0.0254 181 ARG A CG    
1283 C CD    . ARG A 209 ? 1.0818 0.4728 0.8221 0.3381  -0.1336 -0.0153 181 ARG A CD    
1284 N NE    . ARG A 209 ? 1.0923 0.5152 0.8407 0.3475  -0.1262 -0.0197 181 ARG A NE    
1285 C CZ    . ARG A 209 ? 1.1315 0.5846 0.8972 0.3523  -0.1242 -0.0122 181 ARG A CZ    
1286 N NH1   . ARG A 209 ? 1.0830 0.5389 0.8592 0.3489  -0.1285 0.0003  181 ARG A NH1   
1287 N NH2   . ARG A 209 ? 1.1826 0.6639 0.9548 0.3603  -0.1177 -0.0172 181 ARG A NH2   
1288 N N     . TRP A 210 ? 1.1861 0.5158 0.8866 0.2885  -0.1559 -0.0255 182 TRP A N     
1289 C CA    . TRP A 210 ? 1.1566 0.4999 0.8544 0.2812  -0.1561 -0.0302 182 TRP A CA    
1290 C C     . TRP A 210 ? 1.1691 0.4876 0.8537 0.2663  -0.1652 -0.0321 182 TRP A C     
1291 O O     . TRP A 210 ? 1.2025 0.5030 0.8691 0.2661  -0.1654 -0.0428 182 TRP A O     
1292 C CB    . TRP A 210 ? 1.1074 0.4838 0.8243 0.2784  -0.1549 -0.0211 182 TRP A CB    
1293 C CG    . TRP A 210 ? 1.0281 0.4300 0.7578 0.2925  -0.1470 -0.0194 182 TRP A CG    
1294 C CD1   . TRP A 210 ? 1.0329 0.4505 0.7788 0.2956  -0.1466 -0.0083 182 TRP A CD1   
1295 C CD2   . TRP A 210 ? 1.0137 0.4289 0.7410 0.3053  -0.1384 -0.0288 182 TRP A CD2   
1296 N NE1   . TRP A 210 ? 1.0749 0.5148 0.8286 0.3094  -0.1391 -0.0104 182 TRP A NE1   
1297 C CE2   . TRP A 210 ? 1.0006 0.4399 0.7438 0.3155  -0.1339 -0.0229 182 TRP A CE2   
1298 C CE3   . TRP A 210 ? 1.0216 0.4315 0.7352 0.3088  -0.1340 -0.0414 182 TRP A CE3   
1299 C CZ2   . TRP A 210 ? 0.9975 0.4562 0.7443 0.3289  -0.1255 -0.0291 182 TRP A CZ2   
1300 C CZ3   . TRP A 210 ? 1.0156 0.4448 0.7329 0.3221  -0.1248 -0.0473 182 TRP A CZ3   
1301 C CH2   . TRP A 210 ? 1.0022 0.4557 0.7364 0.3319  -0.1208 -0.0412 182 TRP A CH2   
1302 N N     . ALA A 211 ? 1.1721 0.4904 0.8657 0.2538  -0.1725 -0.0216 183 ALA A N     
1303 C CA    . ALA A 211 ? 1.1832 0.4778 0.8676 0.2387  -0.1826 -0.0207 183 ALA A CA    
1304 C C     . ALA A 211 ? 1.2172 0.5003 0.8832 0.2341  -0.1847 -0.0323 183 ALA A C     
1305 O O     . ALA A 211 ? 1.2578 0.5464 0.9243 0.2226  -0.1898 -0.0307 183 ALA A O     
1306 C CB    . ALA A 211 ? 1.2310 0.4951 0.9092 0.2381  -0.1871 -0.0185 183 ALA A CB    
1307 N N     . LEU A 212 ? 1.2668 0.5336 0.9163 0.2430  -0.1808 -0.0436 184 LEU A N     
1308 C CA    . LEU A 212 ? 1.2499 0.5034 0.8796 0.2392  -0.1825 -0.0548 184 LEU A CA    
1309 C C     . LEU A 212 ? 1.2406 0.5198 0.8741 0.2371  -0.1791 -0.0568 184 LEU A C     
1310 O O     . LEU A 212 ? 1.2824 0.5553 0.9067 0.2266  -0.1849 -0.0595 184 LEU A O     
1311 C CB    . LEU A 212 ? 1.2336 0.4723 0.8477 0.2519  -0.1757 -0.0660 184 LEU A CB    
1312 N N     . TYR A 213 ? 1.1646 0.4729 0.8119 0.2470  -0.1700 -0.0553 185 TYR A N     
1313 C CA    . TYR A 213 ? 1.1124 0.4459 0.7647 0.2453  -0.1663 -0.0567 185 TYR A CA    
1314 C C     . TYR A 213 ? 1.0965 0.4448 0.7640 0.2338  -0.1719 -0.0456 185 TYR A C     
1315 O O     . TYR A 213 ? 1.1408 0.5051 0.8105 0.2295  -0.1708 -0.0464 185 TYR A O     
1316 C CB    . TYR A 213 ? 1.0453 0.4055 0.7071 0.2597  -0.1545 -0.0594 185 TYR A CB    
1317 C CG    . TYR A 213 ? 1.0835 0.4345 0.7357 0.2732  -0.1473 -0.0681 185 TYR A CG    
1318 C CD1   . TYR A 213 ? 1.1206 0.4597 0.7754 0.2804  -0.1473 -0.0651 185 TYR A CD1   
1319 C CD2   . TYR A 213 ? 1.1044 0.4594 0.7456 0.2791  -0.1399 -0.0789 185 TYR A CD2   
1320 C CE1   . TYR A 213 ? 1.1120 0.4432 0.7589 0.2932  -0.1403 -0.0727 185 TYR A CE1   
1321 C CE2   . TYR A 213 ? 1.1293 0.4774 0.7627 0.2916  -0.1326 -0.0864 185 TYR A CE2   
1322 C CZ    . TYR A 213 ? 1.0999 0.4360 0.7363 0.2988  -0.1329 -0.0833 185 TYR A CZ    
1323 O OH    . TYR A 213 ? 1.1174 0.4466 0.7466 0.3117  -0.1253 -0.0905 185 TYR A OH    
1324 N N     . MET A 214 ? 1.0624 0.4062 0.7407 0.2288  -0.1774 -0.0350 186 MET A N     
1325 C CA    . MET A 214 ? 1.0382 0.3997 0.7336 0.2193  -0.1811 -0.0232 186 MET A CA    
1326 C C     . MET A 214 ? 1.0701 0.4115 0.7630 0.2041  -0.1925 -0.0173 186 MET A C     
1327 O O     . MET A 214 ? 1.0248 0.3738 0.7327 0.1971  -0.1959 -0.0053 186 MET A O     
1328 C CB    . MET A 214 ? 1.0205 0.4007 0.7342 0.2264  -0.1765 -0.0138 186 MET A CB    
1329 C CG    . MET A 214 ? 0.9634 0.3665 0.6818 0.2408  -0.1660 -0.0187 186 MET A CG    
1330 S SD    . MET A 214 ? 0.9789 0.4058 0.7184 0.2487  -0.1617 -0.0073 186 MET A SD    
1331 C CE    . MET A 214 ? 0.9466 0.4009 0.7013 0.2383  -0.1628 0.0020  186 MET A CE    
1332 N N     . GLN A 215 ? 1.1390 0.4556 0.8133 0.1986  -0.1983 -0.0254 187 GLN A N     
1333 C CA    . GLN A 215 ? 1.2000 0.4979 0.8713 0.1833  -0.2101 -0.0205 187 GLN A CA    
1334 C C     . GLN A 215 ? 1.1971 0.5135 0.8800 0.1718  -0.2140 -0.0129 187 GLN A C     
1335 O O     . GLN A 215 ? 1.2008 0.5107 0.8901 0.1591  -0.2229 -0.0043 187 GLN A O     
1336 C CB    . GLN A 215 ? 1.2210 0.4895 0.8680 0.1803  -0.2155 -0.0319 187 GLN A CB    
1337 C CG    . GLN A 215 ? 1.2987 0.5455 0.9331 0.1905  -0.2124 -0.0392 187 GLN A CG    
1338 C CD    . GLN A 215 ? 1.4461 0.6685 1.0552 0.1900  -0.2150 -0.0519 187 GLN A CD    
1339 O OE1   . GLN A 215 ? 1.5478 0.7667 1.1481 0.1804  -0.2210 -0.0547 187 GLN A OE1   
1340 N NE2   . GLN A 215 ? 1.4637 0.6694 1.0607 0.2005  -0.2102 -0.0596 187 GLN A NE2   
1341 N N     . ASP A 216 ? 1.1934 0.5330 0.8798 0.1761  -0.2074 -0.0155 188 ASP A N     
1342 C CA    . ASP A 216 ? 1.1239 0.4821 0.8212 0.1665  -0.2098 -0.0086 188 ASP A CA    
1343 C C     . ASP A 216 ? 1.1091 0.4989 0.8271 0.1714  -0.2019 -0.0001 188 ASP A C     
1344 O O     . ASP A 216 ? 1.0584 0.4695 0.7815 0.1725  -0.1970 -0.0005 188 ASP A O     
1345 C CB    . ASP A 216 ? 1.0878 0.4464 0.7714 0.1662  -0.2088 -0.0181 188 ASP A CB    
1346 C CG    . ASP A 216 ? 1.0721 0.4372 0.7472 0.1808  -0.1979 -0.0291 188 ASP A CG    
1347 O OD1   . ASP A 216 ? 1.0764 0.4404 0.7532 0.1911  -0.1926 -0.0306 188 ASP A OD1   
1348 O OD2   . ASP A 216 ? 1.0708 0.4426 0.7380 0.1821  -0.1943 -0.0357 188 ASP A OD2   
1349 N N     . VAL A 217 ? 1.0910 0.4835 0.8205 0.1744  -0.2006 0.0078  189 VAL A N     
1350 C CA    . VAL A 217 ? 1.0029 0.4246 0.7503 0.1804  -0.1929 0.0152  189 VAL A CA    
1351 C C     . VAL A 217 ? 1.0361 0.4781 0.7982 0.1701  -0.1944 0.0256  189 VAL A C     
1352 O O     . VAL A 217 ? 1.0297 0.4981 0.8018 0.1741  -0.1875 0.0279  189 VAL A O     
1353 C CB    . VAL A 217 ? 1.0167 0.4346 0.7715 0.1858  -0.1916 0.0217  189 VAL A CB    
1354 C CG1   . VAL A 217 ? 1.1029 0.5053 0.8623 0.1738  -0.2002 0.0316  189 VAL A CG1   
1355 C CG2   . VAL A 217 ? 0.9992 0.4474 0.7705 0.1932  -0.1836 0.0285  189 VAL A CG2   
1356 N N     . GLU A 218 ? 1.0903 0.5212 0.8541 0.1566  -0.2033 0.0320  190 GLU A N     
1357 C CA    . GLU A 218 ? 1.0482 0.4991 0.8271 0.1468  -0.2043 0.0426  190 GLU A CA    
1358 C C     . GLU A 218 ? 1.0057 0.4699 0.7814 0.1461  -0.2017 0.0375  190 GLU A C     
1359 O O     . GLU A 218 ? 0.9722 0.4597 0.7615 0.1424  -0.1986 0.0452  190 GLU A O     
1360 C CB    . GLU A 218 ? 1.0883 0.5239 0.8699 0.1324  -0.2149 0.0503  190 GLU A CB    
1361 C CG    . GLU A 218 ? 1.1337 0.5456 0.8985 0.1252  -0.2241 0.0421  190 GLU A CG    
1362 C CD    . GLU A 218 ? 1.2110 0.5926 0.9575 0.1300  -0.2274 0.0322  190 GLU A CD    
1363 O OE1   . GLU A 218 ? 1.1913 0.5716 0.9383 0.1404  -0.2215 0.0309  190 GLU A OE1   
1364 O OE2   . GLU A 218 ? 1.2539 0.6131 0.9853 0.1235  -0.2358 0.0257  190 GLU A OE2   
1365 N N     . LYS A 219 ? 0.9839 0.4336 0.7415 0.1498  -0.2024 0.0248  191 LYS A N     
1366 C CA    . LYS A 219 ? 0.9552 0.4168 0.7087 0.1505  -0.1989 0.0195  191 LYS A CA    
1367 C C     . LYS A 219 ? 0.9467 0.4289 0.7030 0.1632  -0.1874 0.0147  191 LYS A C     
1368 O O     . LYS A 219 ? 0.9695 0.4645 0.7244 0.1642  -0.1832 0.0111  191 LYS A O     
1369 C CB    . LYS A 219 ? 0.9449 0.3823 0.6768 0.1485  -0.2043 0.0084  191 LYS A CB    
1370 C CG    . LYS A 219 ? 0.9042 0.3266 0.6339 0.1339  -0.2164 0.0133  191 LYS A CG    
1371 C CD    . LYS A 219 ? 0.8933 0.2939 0.6005 0.1320  -0.2216 0.0022  191 LYS A CD    
1372 C CE    . LYS A 219 ? 0.9339 0.3220 0.6400 0.1169  -0.2347 0.0078  191 LYS A CE    
1373 N NZ    . LYS A 219 ? 0.9997 0.3652 0.6822 0.1146  -0.2408 -0.0029 191 LYS A NZ    
1374 N N     . PHE A 220 ? 0.9095 0.3955 0.6701 0.1727  -0.1826 0.0147  192 PHE A N     
1375 C CA    . PHE A 220 ? 0.8636 0.3726 0.6304 0.1839  -0.1727 0.0121  192 PHE A CA    
1376 C C     . PHE A 220 ? 0.8052 0.3377 0.5914 0.1830  -0.1697 0.0242  192 PHE A C     
1377 O O     . PHE A 220 ? 0.7826 0.3341 0.5751 0.1922  -0.1625 0.0234  192 PHE A O     
1378 C CB    . PHE A 220 ? 0.8998 0.3997 0.6580 0.1965  -0.1686 0.0033  192 PHE A CB    
1379 C CG    . PHE A 220 ? 0.8805 0.3650 0.6200 0.2005  -0.1675 -0.0101 192 PHE A CG    
1380 C CD1   . PHE A 220 ? 0.9009 0.3571 0.6253 0.1945  -0.1750 -0.0142 192 PHE A CD1   
1381 C CD2   . PHE A 220 ? 0.9133 0.4120 0.6498 0.2101  -0.1586 -0.0187 192 PHE A CD2   
1382 C CE1   . PHE A 220 ? 0.9421 0.3845 0.6481 0.1983  -0.1734 -0.0265 192 PHE A CE1   
1383 C CE2   . PHE A 220 ? 0.9286 0.4143 0.6479 0.2138  -0.1564 -0.0306 192 PHE A CE2   
1384 C CZ    . PHE A 220 ? 0.9430 0.4006 0.6465 0.2080  -0.1636 -0.0345 192 PHE A CZ    
1385 N N     . VAL A 221 ? 0.8046 0.3367 0.6002 0.1720  -0.1751 0.0355  193 VAL A N     
1386 C CA    . VAL A 221 ? 0.8010 0.3544 0.6143 0.1702  -0.1723 0.0478  193 VAL A CA    
1387 C C     . VAL A 221 ? 0.8334 0.4017 0.6549 0.1605  -0.1725 0.0544  193 VAL A C     
1388 O O     . VAL A 221 ? 0.8714 0.4280 0.6881 0.1515  -0.1785 0.0539  193 VAL A O     
1389 C CB    . VAL A 221 ? 0.8078 0.3487 0.6264 0.1664  -0.1771 0.0569  193 VAL A CB    
1390 C CG1   . VAL A 221 ? 0.8441 0.4070 0.6801 0.1642  -0.1736 0.0703  193 VAL A CG1   
1391 C CG2   . VAL A 221 ? 0.8868 0.4132 0.6974 0.1769  -0.1762 0.0507  193 VAL A CG2   
1392 N N     . SER A 222 ? 0.8386 0.4329 0.6724 0.1626  -0.1660 0.0604  194 SER A N     
1393 C CA    . SER A 222 ? 0.7824 0.3926 0.6253 0.1543  -0.1649 0.0675  194 SER A CA    
1394 C C     . SER A 222 ? 0.8029 0.4052 0.6530 0.1423  -0.1716 0.0782  194 SER A C     
1395 O O     . SER A 222 ? 0.8745 0.4708 0.7296 0.1414  -0.1738 0.0850  194 SER A O     
1396 C CB    . SER A 222 ? 0.7376 0.3751 0.5920 0.1587  -0.1569 0.0732  194 SER A CB    
1397 O OG    . SER A 222 ? 0.7184 0.3704 0.5834 0.1503  -0.1558 0.0826  194 SER A OG    
1398 N N     . PRO A 223 ? 0.8133 0.4153 0.6642 0.1330  -0.1752 0.0802  195 PRO A N     
1399 C CA    . PRO A 223 ? 0.8680 0.4640 0.7269 0.1213  -0.1820 0.0906  195 PRO A CA    
1400 C C     . PRO A 223 ? 0.8338 0.4495 0.7100 0.1189  -0.1774 0.1044  195 PRO A C     
1401 O O     . PRO A 223 ? 0.8587 0.4683 0.7420 0.1112  -0.1823 0.1136  195 PRO A O     
1402 C CB    . PRO A 223 ? 0.8447 0.4408 0.7012 0.1135  -0.1856 0.0892  195 PRO A CB    
1403 C CG    . PRO A 223 ? 0.8201 0.4307 0.6728 0.1209  -0.1776 0.0822  195 PRO A CG    
1404 C CD    . PRO A 223 ? 0.7792 0.3876 0.6244 0.1330  -0.1728 0.0737  195 PRO A CD    
1405 N N     . TYR A 224 ? 0.7871 0.4256 0.6694 0.1253  -0.1684 0.1061  196 TYR A N     
1406 C CA    . TYR A 224 ? 0.8403 0.4976 0.7367 0.1246  -0.1632 0.1187  196 TYR A CA    
1407 C C     . TYR A 224 ? 0.8854 0.5429 0.7822 0.1329  -0.1604 0.1202  196 TYR A C     
1408 O O     . TYR A 224 ? 0.8646 0.5401 0.7703 0.1356  -0.1545 0.1285  196 TYR A O     
1409 C CB    . TYR A 224 ? 0.7928 0.4744 0.6949 0.1264  -0.1554 0.1202  196 TYR A CB    
1410 C CG    . TYR A 224 ? 0.8510 0.5327 0.7513 0.1200  -0.1573 0.1174  196 TYR A CG    
1411 C CD1   . TYR A 224 ? 0.8726 0.5554 0.7815 0.1097  -0.1609 0.1265  196 TYR A CD1   
1412 C CD2   . TYR A 224 ? 0.8575 0.5381 0.7474 0.1246  -0.1556 0.1059  196 TYR A CD2   
1413 C CE1   . TYR A 224 ? 0.7985 0.4820 0.7062 0.1042  -0.1630 0.1245  196 TYR A CE1   
1414 C CE2   . TYR A 224 ? 0.8095 0.4895 0.6970 0.1192  -0.1572 0.1038  196 TYR A CE2   
1415 C CZ    . TYR A 224 ? 0.7838 0.4655 0.6805 0.1090  -0.1612 0.1133  196 TYR A CZ    
1416 O OH    . TYR A 224 ? 0.8247 0.5066 0.7194 0.1039  -0.1631 0.1118  196 TYR A OH    
1417 N N     . GLN A 225 ? 0.8971 0.5345 0.7838 0.1374  -0.1646 0.1126  197 GLN A N     
1418 C CA    . GLN A 225 ? 0.8383 0.4750 0.7253 0.1459  -0.1623 0.1140  197 GLN A CA    
1419 C C     . GLN A 225 ? 0.8623 0.4973 0.7588 0.1409  -0.1636 0.1277  197 GLN A C     
1420 O O     . GLN A 225 ? 0.9108 0.5614 0.8149 0.1451  -0.1582 0.1358  197 GLN A O     
1421 C CB    . GLN A 225 ? 0.8097 0.4238 0.6833 0.1519  -0.1662 0.1026  197 GLN A CB    
1422 C CG    . GLN A 225 ? 0.8407 0.4531 0.7144 0.1615  -0.1640 0.1037  197 GLN A CG    
1423 C CD    . GLN A 225 ? 0.8946 0.5298 0.7710 0.1716  -0.1566 0.1010  197 GLN A CD    
1424 O OE1   . GLN A 225 ? 0.8588 0.5045 0.7319 0.1737  -0.1536 0.0934  197 GLN A OE1   
1425 N NE2   . GLN A 225 ? 0.9423 0.5850 0.8242 0.1777  -0.1540 0.1074  197 GLN A NE2   
1426 N N     . HIS A 226 ? 0.8811 0.4969 0.7766 0.1319  -0.1710 0.1304  198 HIS A N     
1427 C CA    . HIS A 226 ? 0.9411 0.5524 0.8447 0.1263  -0.1729 0.1430  198 HIS A CA    
1428 C C     . HIS A 226 ? 0.9863 0.6123 0.9016 0.1166  -0.1718 0.1538  198 HIS A C     
1429 O O     . HIS A 226 ? 1.0973 0.7184 1.0194 0.1099  -0.1744 0.1641  198 HIS A O     
1430 C CB    . HIS A 226 ? 0.9538 0.5347 0.8498 0.1214  -0.1821 0.1400  198 HIS A CB    
1431 C CG    . HIS A 226 ? 0.9781 0.5423 0.8612 0.1311  -0.1831 0.1286  198 HIS A CG    
1432 N ND1   . HIS A 226 ? 1.0446 0.6135 0.9280 0.1421  -0.1779 0.1295  198 HIS A ND1   
1433 C CD2   . HIS A 226 ? 0.9897 0.5331 0.8590 0.1319  -0.1885 0.1162  198 HIS A CD2   
1434 C CE1   . HIS A 226 ? 1.0115 0.5637 0.8828 0.1494  -0.1797 0.1182  198 HIS A CE1   
1435 N NE2   . HIS A 226 ? 1.0081 0.5442 0.8701 0.1436  -0.1858 0.1097  198 HIS A NE2   
1436 N N     . SER A 227 ? 0.9401 0.5839 0.8581 0.1160  -0.1679 0.1518  199 SER A N     
1437 C CA    . SER A 227 ? 0.9792 0.6380 0.9084 0.1078  -0.1661 0.1618  199 SER A CA    
1438 C C     . SER A 227 ? 0.9918 0.6685 0.9295 0.1115  -0.1582 0.1733  199 SER A C     
1439 O O     . SER A 227 ? 0.9435 0.6322 0.8793 0.1213  -0.1516 0.1718  199 SER A O     
1440 C CB    . SER A 227 ? 0.9988 0.6709 0.9275 0.1074  -0.1633 0.1562  199 SER A CB    
1441 O OG    . SER A 227 ? 0.9993 0.6881 0.9391 0.1013  -0.1601 0.1660  199 SER A OG    
1442 N N     . GLU A 228 ? 1.0404 0.7184 0.9870 0.1035  -0.1594 0.1849  200 GLU A N     
1443 C CA    . GLU A 228 ? 1.0042 0.6978 0.9569 0.1066  -0.1520 0.1961  200 GLU A CA    
1444 C C     . GLU A 228 ? 0.9195 0.6372 0.8761 0.1087  -0.1440 0.1981  200 GLU A C     
1445 O O     . GLU A 228 ? 0.8782 0.6095 0.8356 0.1142  -0.1369 0.2045  200 GLU A O     
1446 C CB    . GLU A 228 ? 0.9968 0.6830 0.9575 0.0969  -0.1561 0.2075  200 GLU A CB    
1447 N N     . ASP A 229 ? 0.9211 0.6430 0.8786 0.1047  -0.1453 0.1925  201 ASP A N     
1448 C CA    . ASP A 229 ? 0.8984 0.6412 0.8587 0.1069  -0.1378 0.1935  201 ASP A CA    
1449 C C     . ASP A 229 ? 0.9108 0.6529 0.8662 0.1076  -0.1391 0.1822  201 ASP A C     
1450 O O     . ASP A 229 ? 0.9049 0.6446 0.8633 0.1000  -0.1432 0.1813  201 ASP A O     
1451 C CB    . ASP A 229 ? 0.8732 0.6249 0.8442 0.0982  -0.1371 0.2038  201 ASP A CB    
1452 C CG    . ASP A 229 ? 0.8936 0.6654 0.8665 0.1011  -0.1291 0.2046  201 ASP A CG    
1453 O OD1   . ASP A 229 ? 0.9005 0.6803 0.8660 0.1106  -0.1230 0.1997  201 ASP A OD1   
1454 O OD2   . ASP A 229 ? 0.9227 0.7021 0.9049 0.0938  -0.1292 0.2103  201 ASP A OD2   
1455 N N     . PRO A 230 ? 0.8522 0.5966 0.8001 0.1165  -0.1362 0.1734  202 PRO A N     
1456 C CA    . PRO A 230 ? 0.8507 0.5921 0.7923 0.1172  -0.1379 0.1617  202 PRO A CA    
1457 C C     . PRO A 230 ? 0.8214 0.5782 0.7667 0.1153  -0.1329 0.1628  202 PRO A C     
1458 O O     . PRO A 230 ? 0.8660 0.6174 0.8090 0.1110  -0.1364 0.1574  202 PRO A O     
1459 C CB    . PRO A 230 ? 0.8501 0.5926 0.7841 0.1275  -0.1354 0.1531  202 PRO A CB    
1460 C CG    . PRO A 230 ? 0.8360 0.5757 0.7719 0.1309  -0.1353 0.1596  202 PRO A CG    
1461 C CD    . PRO A 230 ? 0.8629 0.6100 0.8075 0.1257  -0.1329 0.1733  202 PRO A CD    
1462 N N     . VAL A 231 ? 0.7314 0.5063 0.6814 0.1190  -0.1249 0.1696  203 VAL A N     
1463 C CA    . VAL A 231 ? 0.7112 0.4999 0.6640 0.1183  -0.1195 0.1707  203 VAL A CA    
1464 C C     . VAL A 231 ? 0.8170 0.6039 0.7770 0.1086  -0.1228 0.1766  203 VAL A C     
1465 O O     . VAL A 231 ? 0.8464 0.6366 0.8071 0.1059  -0.1224 0.1740  203 VAL A O     
1466 C CB    . VAL A 231 ? 0.7464 0.5519 0.7001 0.1247  -0.1108 0.1766  203 VAL A CB    
1467 C CG1   . VAL A 231 ? 0.8047 0.6215 0.7602 0.1235  -0.1055 0.1784  203 VAL A CG1   
1468 C CG2   . VAL A 231 ? 0.6753 0.4859 0.6246 0.1329  -0.1086 0.1703  203 VAL A CG2   
1469 N N     . GLY A 232 ? 0.7894 0.5712 0.7555 0.1029  -0.1267 0.1849  204 GLY A N     
1470 C CA    . GLY A 232 ? 0.8363 0.6179 0.8119 0.0927  -0.1311 0.1913  204 GLY A CA    
1471 C C     . GLY A 232 ? 0.8432 0.6103 0.8160 0.0867  -0.1403 0.1845  204 GLY A C     
1472 O O     . GLY A 232 ? 0.8101 0.5811 0.7870 0.0814  -0.1421 0.1852  204 GLY A O     
1473 N N     . GLU A 233 ? 0.8683 0.6174 0.8326 0.0877  -0.1466 0.1776  205 GLU A N     
1474 C CA    . GLU A 233 ? 0.8907 0.6225 0.8489 0.0823  -0.1564 0.1701  205 GLU A CA    
1475 C C     . GLU A 233 ? 0.8490 0.5836 0.7992 0.0861  -0.1539 0.1605  205 GLU A C     
1476 O O     . GLU A 233 ? 0.8578 0.5862 0.8062 0.0803  -0.1598 0.1578  205 GLU A O     
1477 C CB    . GLU A 233 ? 0.8847 0.5951 0.8338 0.0838  -0.1629 0.1641  205 GLU A CB    
1478 C CG    . GLU A 233 ? 0.9358 0.6374 0.8918 0.0774  -0.1685 0.1731  205 GLU A CG    
1479 C CD    . GLU A 233 ? 1.0567 0.7334 1.0023 0.0782  -0.1762 0.1663  205 GLU A CD    
1480 O OE1   . GLU A 233 ? 1.1004 0.7648 1.0333 0.0815  -0.1793 0.1544  205 GLU A OE1   
1481 O OE2   . GLU A 233 ? 1.1812 0.8499 1.1304 0.0757  -0.1788 0.1728  205 GLU A OE2   
1482 N N     . PHE A 234 ? 0.8176 0.5612 0.7628 0.0955  -0.1457 0.1554  206 PHE A N     
1483 C CA    . PHE A 234 ? 0.7729 0.5188 0.7105 0.0989  -0.1430 0.1464  206 PHE A CA    
1484 C C     . PHE A 234 ? 0.8180 0.5802 0.7637 0.0963  -0.1378 0.1527  206 PHE A C     
1485 O O     . PHE A 234 ? 0.8362 0.5964 0.7776 0.0947  -0.1390 0.1478  206 PHE A O     
1486 C CB    . PHE A 234 ? 0.7189 0.4690 0.6489 0.1092  -0.1368 0.1387  206 PHE A CB    
1487 C CG    . PHE A 234 ? 0.6598 0.4063 0.5786 0.1129  -0.1357 0.1269  206 PHE A CG    
1488 C CD1   . PHE A 234 ? 0.6175 0.3456 0.5257 0.1106  -0.1430 0.1183  206 PHE A CD1   
1489 C CD2   . PHE A 234 ? 0.6420 0.4022 0.5594 0.1188  -0.1275 0.1241  206 PHE A CD2   
1490 C CE1   . PHE A 234 ? 0.5659 0.2900 0.4623 0.1145  -0.1413 0.1076  206 PHE A CE1   
1491 C CE2   . PHE A 234 ? 0.5879 0.3437 0.4939 0.1223  -0.1261 0.1131  206 PHE A CE2   
1492 C CZ    . PHE A 234 ? 0.5578 0.2960 0.4535 0.1203  -0.1326 0.1051  206 PHE A CZ    
1493 N N     . ARG A 235 ? 0.8003 0.5777 0.7567 0.0962  -0.1318 0.1633  207 ARG A N     
1494 C CA    . ARG A 235 ? 0.8397 0.6314 0.8041 0.0937  -0.1271 0.1698  207 ARG A CA    
1495 C C     . ARG A 235 ? 0.8307 0.6174 0.8017 0.0836  -0.1354 0.1740  207 ARG A C     
1496 O O     . ARG A 235 ? 0.8503 0.6427 0.8236 0.0814  -0.1346 0.1745  207 ARG A O     
1497 C CB    . ARG A 235 ? 0.8064 0.6131 0.7784 0.0962  -0.1194 0.1793  207 ARG A CB    
1498 C CG    . ARG A 235 ? 0.8119 0.6328 0.7921 0.0939  -0.1143 0.1857  207 ARG A CG    
1499 C CD    . ARG A 235 ? 0.8281 0.6622 0.8143 0.0961  -0.1072 0.1937  207 ARG A CD    
1500 N NE    . ARG A 235 ? 0.8856 0.7262 0.8637 0.1048  -0.0992 0.1892  207 ARG A NE    
1501 C CZ    . ARG A 235 ? 0.9064 0.7494 0.8804 0.1100  -0.0962 0.1896  207 ARG A CZ    
1502 N NH1   . ARG A 235 ? 0.8850 0.7242 0.8616 0.1082  -0.0993 0.1947  207 ARG A NH1   
1503 N NH2   . ARG A 235 ? 0.8696 0.7190 0.8375 0.1164  -0.0906 0.1851  207 ARG A NH2   
1504 N N     . LEU A 236 ? 0.8038 0.5793 0.7779 0.0774  -0.1439 0.1772  208 LEU A N     
1505 C CA    . LEU A 236 ? 0.7393 0.5090 0.7198 0.0669  -0.1537 0.1812  208 LEU A CA    
1506 C C     . LEU A 236 ? 0.7411 0.4959 0.7096 0.0655  -0.1610 0.1709  208 LEU A C     
1507 O O     . LEU A 236 ? 0.7433 0.4994 0.7151 0.0595  -0.1659 0.1729  208 LEU A O     
1508 C CB    . LEU A 236 ? 0.6741 0.4338 0.6604 0.0603  -0.1616 0.1871  208 LEU A CB    
1509 N N     . LEU A 237 ? 0.7579 0.4987 0.7119 0.0712  -0.1620 0.1599  209 LEU A N     
1510 C CA    . LEU A 237 ? 0.6807 0.4053 0.6207 0.0705  -0.1687 0.1492  209 LEU A CA    
1511 C C     . LEU A 237 ? 0.7349 0.4697 0.6721 0.0736  -0.1627 0.1463  209 LEU A C     
1512 O O     . LEU A 237 ? 0.8132 0.5413 0.7456 0.0692  -0.1688 0.1439  209 LEU A O     
1513 C CB    . LEU A 237 ? 0.6592 0.3674 0.5844 0.0772  -0.1697 0.1379  209 LEU A CB    
1514 C CG    . LEU A 237 ? 0.6583 0.3483 0.5658 0.0783  -0.1755 0.1256  209 LEU A CG    
1515 C CD1   . LEU A 237 ? 0.7362 0.4095 0.6412 0.0684  -0.1888 0.1268  209 LEU A CD1   
1516 C CD2   . LEU A 237 ? 0.7084 0.3854 0.6020 0.0869  -0.1741 0.1144  209 LEU A CD2   
1517 N N     . LEU A 238 ? 0.7513 0.5012 0.6906 0.0811  -0.1512 0.1465  210 LEU A N     
1518 C CA    . LEU A 238 ? 0.7493 0.5077 0.6856 0.0843  -0.1450 0.1438  210 LEU A CA    
1519 C C     . LEU A 238 ? 0.7719 0.5419 0.7202 0.0782  -0.1453 0.1537  210 LEU A C     
1520 O O     . LEU A 238 ? 0.7504 0.5182 0.6944 0.0763  -0.1475 0.1513  210 LEU A O     
1521 C CB    . LEU A 238 ? 0.6583 0.4294 0.5946 0.0931  -0.1334 0.1427  210 LEU A CB    
1522 C CG    . LEU A 238 ? 0.5783 0.3405 0.5021 0.1004  -0.1323 0.1316  210 LEU A CG    
1523 C CD1   . LEU A 238 ? 0.5195 0.2955 0.4441 0.1081  -0.1220 0.1312  210 LEU A CD1   
1524 C CD2   . LEU A 238 ? 0.6494 0.3957 0.5571 0.1016  -0.1364 0.1194  210 LEU A CD2   
1525 N N     . GLU A 239 ? 0.7630 0.5455 0.7261 0.0753  -0.1432 0.1648  211 GLU A N     
1526 C CA    . GLU A 239 ? 0.7435 0.5385 0.7193 0.0699  -0.1433 0.1744  211 GLU A CA    
1527 C C     . GLU A 239 ? 0.7494 0.5339 0.7265 0.0603  -0.1566 0.1757  211 GLU A C     
1528 O O     . GLU A 239 ? 0.7989 0.5911 0.7828 0.0563  -0.1584 0.1807  211 GLU A O     
1529 C CB    . GLU A 239 ? 0.7207 0.5304 0.7112 0.0691  -0.1381 0.1854  211 GLU A CB    
1530 C CG    . GLU A 239 ? 0.7643 0.5859 0.7533 0.0783  -0.1252 0.1854  211 GLU A CG    
1531 C CD    . GLU A 239 ? 0.8447 0.6761 0.8439 0.0779  -0.1213 0.1942  211 GLU A CD    
1532 O OE1   . GLU A 239 ? 0.8879 0.7154 0.8947 0.0711  -0.1285 0.1998  211 GLU A OE1   
1533 O OE2   . GLU A 239 ? 0.8745 0.7166 0.8735 0.0842  -0.1115 0.1956  211 GLU A OE2   
1534 N N     . SER A 240 ? 0.7174 0.4837 0.6876 0.0566  -0.1664 0.1712  212 SER A N     
1535 C CA    . SER A 240 ? 0.6871 0.4397 0.6552 0.0473  -0.1806 0.1709  212 SER A CA    
1536 C C     . SER A 240 ? 0.7363 0.4772 0.6882 0.0489  -0.1842 0.1611  212 SER A C     
1537 O O     . SER A 240 ? 0.7508 0.4779 0.6972 0.0418  -0.1967 0.1595  212 SER A O     
1538 C CB    . SER A 240 ? 0.7254 0.4595 0.6897 0.0432  -0.1900 0.1690  212 SER A CB    
1539 O OG    . SER A 240 ? 0.7599 0.4776 0.7062 0.0501  -0.1892 0.1566  212 SER A OG    
1540 N N     . GLU A 241 ? 0.7669 0.5121 0.7102 0.0577  -0.1741 0.1545  213 GLU A N     
1541 C CA    . GLU A 241 ? 0.7571 0.4918 0.6843 0.0597  -0.1761 0.1454  213 GLU A CA    
1542 C C     . GLU A 241 ? 0.7779 0.5289 0.7091 0.0636  -0.1665 0.1483  213 GLU A C     
1543 O O     . GLU A 241 ? 0.7648 0.5091 0.6822 0.0675  -0.1645 0.1405  213 GLU A O     
1544 C CB    . GLU A 241 ? 0.7619 0.4805 0.6708 0.0669  -0.1744 0.1322  213 GLU A CB    
1545 C CG    . GLU A 241 ? 0.7935 0.4908 0.6938 0.0636  -0.1853 0.1273  213 GLU A CG    
1546 C CD    . GLU A 241 ? 0.8533 0.5349 0.7459 0.0556  -0.1990 0.1263  213 GLU A CD    
1547 O OE1   . GLU A 241 ? 0.8104 0.4894 0.6931 0.0563  -0.1996 0.1225  213 GLU A OE1   
1548 O OE2   . GLU A 241 ? 0.9304 0.6016 0.8262 0.0483  -0.2095 0.1296  213 GLU A OE2   
1549 N N     . GLY A 242 ? 0.7968 0.5679 0.7456 0.0629  -0.1601 0.1594  214 GLY A N     
1550 C CA    . GLY A 242 ? 0.7798 0.5655 0.7328 0.0669  -0.1509 0.1629  214 GLY A CA    
1551 C C     . GLY A 242 ? 0.7640 0.5568 0.7140 0.0762  -0.1375 0.1597  214 GLY A C     
1552 O O     . GLY A 242 ? 0.7645 0.5612 0.7102 0.0805  -0.1307 0.1580  214 GLY A O     
1553 N N     . PHE A 243 ? 0.7215 0.5155 0.6732 0.0793  -0.1339 0.1590  215 PHE A N     
1554 C CA    . PHE A 243 ? 0.7262 0.5262 0.6745 0.0878  -0.1227 0.1557  215 PHE A CA    
1555 C C     . PHE A 243 ? 0.6950 0.5119 0.6569 0.0895  -0.1150 0.1657  215 PHE A C     
1556 O O     . PHE A 243 ? 0.7104 0.5314 0.6829 0.0846  -0.1188 0.1731  215 PHE A O     
1557 C CB    . PHE A 243 ? 0.7114 0.4991 0.6482 0.0915  -0.1245 0.1457  215 PHE A CB    
1558 C CG    . PHE A 243 ? 0.6727 0.4446 0.5915 0.0937  -0.1274 0.1332  215 PHE A CG    
1559 C CD1   . PHE A 243 ? 0.6757 0.4483 0.5849 0.1005  -0.1193 0.1262  215 PHE A CD1   
1560 C CD2   . PHE A 243 ? 0.6889 0.4439 0.5988 0.0894  -0.1381 0.1279  215 PHE A CD2   
1561 C CE1   . PHE A 243 ? 0.6913 0.4490 0.5825 0.1033  -0.1209 0.1145  215 PHE A CE1   
1562 C CE2   . PHE A 243 ? 0.7025 0.4421 0.5938 0.0923  -0.1401 0.1162  215 PHE A CE2   
1563 C CZ    . PHE A 243 ? 0.6801 0.4216 0.5623 0.0994  -0.1311 0.1096  215 PHE A CZ    
1564 N N     . GLN A 244 ? 0.6780 0.5031 0.6384 0.0965  -0.1044 0.1653  216 GLN A N     
1565 C CA    . GLN A 244 ? 0.6631 0.5016 0.6318 0.0994  -0.0965 0.1722  216 GLN A CA    
1566 C C     . GLN A 244 ? 0.6860 0.5223 0.6482 0.1054  -0.0932 0.1674  216 GLN A C     
1567 O O     . GLN A 244 ? 0.7408 0.5756 0.6949 0.1113  -0.0882 0.1613  216 GLN A O     
1568 C CB    . GLN A 244 ? 0.7084 0.5566 0.6797 0.1024  -0.0878 0.1748  216 GLN A CB    
1569 C CG    . GLN A 244 ? 0.7557 0.6180 0.7358 0.1043  -0.0795 0.1806  216 GLN A CG    
1570 C CD    . GLN A 244 ? 0.8155 0.6871 0.7977 0.1077  -0.0691 0.1814  216 GLN A CD    
1571 O OE1   . GLN A 244 ? 0.8686 0.7345 0.8427 0.1103  -0.0669 0.1759  216 GLN A OE1   
1572 N NE2   . GLN A 244 ? 0.8045 0.6905 0.7975 0.1080  -0.0617 0.1885  216 GLN A NE2   
1573 N N     . VAL A 245 ? 0.6417 0.4779 0.6079 0.1036  -0.0965 0.1704  217 VAL A N     
1574 C CA    . VAL A 245 ? 0.6555 0.4904 0.6161 0.1093  -0.0942 0.1668  217 VAL A CA    
1575 C C     . VAL A 245 ? 0.7001 0.5471 0.6627 0.1138  -0.0853 0.1697  217 VAL A C     
1576 O O     . VAL A 245 ? 0.7445 0.6012 0.7165 0.1111  -0.0828 0.1776  217 VAL A O     
1577 C CB    . VAL A 245 ? 0.7296 0.5598 0.6938 0.1058  -0.1004 0.1698  217 VAL A CB    
1578 C CG1   . VAL A 245 ? 0.8172 0.6477 0.7761 0.1125  -0.0977 0.1669  217 VAL A CG1   
1579 C CG2   . VAL A 245 ? 0.6790 0.4948 0.6403 0.1001  -0.1107 0.1651  217 VAL A CG2   
1580 N N     . LEU A 246 ? 0.7301 0.5794 0.6866 0.1193  -0.0793 0.1636  218 LEU A N     
1581 C CA    . LEU A 246 ? 0.7116 0.5756 0.6701 0.1234  -0.0673 0.1649  218 LEU A CA    
1582 C C     . LEU A 246 ? 0.7652 0.6336 0.7216 0.1272  -0.0656 0.1645  218 LEU A C     
1583 O O     . LEU A 246 ? 0.9180 0.7985 0.8784 0.1287  -0.0581 0.1693  218 LEU A O     
1584 C CB    . LEU A 246 ? 0.6842 0.5486 0.6322 0.1292  -0.0581 0.1563  218 LEU A CB    
1585 C CG    . LEU A 246 ? 0.6987 0.5599 0.6477 0.1263  -0.0578 0.1563  218 LEU A CG    
1586 C CD1   . LEU A 246 ? 0.6798 0.5410 0.6173 0.1294  -0.0482 0.1439  218 LEU A CD1   
1587 C CD2   . LEU A 246 ? 0.7780 0.6497 0.7410 0.1219  -0.0556 0.1672  218 LEU A CD2   
1588 N N     . ARG A 247 ? 0.7522 0.6108 0.7017 0.1292  -0.0722 0.1590  219 ARG A N     
1589 C CA    . ARG A 247 ? 0.7861 0.6487 0.7321 0.1338  -0.0708 0.1576  219 ARG A CA    
1590 C C     . ARG A 247 ? 0.7940 0.6433 0.7360 0.1337  -0.0808 0.1533  219 ARG A C     
1591 O O     . ARG A 247 ? 0.7602 0.5981 0.6938 0.1341  -0.0845 0.1441  219 ARG A O     
1592 C CB    . ARG A 247 ? 0.7789 0.6491 0.7139 0.1410  -0.0606 0.1481  219 ARG A CB    
1593 C CG    . ARG A 247 ? 0.8519 0.7295 0.7832 0.1462  -0.0582 0.1475  219 ARG A CG    
1594 C CD    . ARG A 247 ? 0.8712 0.7586 0.7938 0.1501  -0.0481 0.1372  219 ARG A CD    
1595 N NE    . ARG A 247 ? 1.0256 0.9202 0.9429 0.1551  -0.0468 0.1347  219 ARG A NE    
1596 C CZ    . ARG A 247 ? 0.9833 0.8895 0.8955 0.1582  -0.0381 0.1323  219 ARG A CZ    
1597 N NH1   . ARG A 247 ? 0.9343 0.8454 0.8461 0.1573  -0.0292 0.1318  219 ARG A NH1   
1598 N NH2   . ARG A 247 ? 0.9647 0.8772 0.8718 0.1626  -0.0385 0.1302  219 ARG A NH2   
1599 N N     . CYS A 248 ? 0.8275 0.6773 0.7746 0.1326  -0.0849 0.1592  220 CYS A N     
1600 C CA    . CYS A 248 ? 0.8153 0.6542 0.7615 0.1322  -0.0925 0.1572  220 CYS A CA    
1601 C C     . CYS A 248 ? 0.8376 0.6808 0.7857 0.1348  -0.0931 0.1614  220 CYS A C     
1602 O O     . CYS A 248 ? 0.8616 0.7033 0.8123 0.1315  -0.0961 0.1695  220 CYS A O     
1603 C CB    . CYS A 248 ? 0.7876 0.6180 0.7387 0.1259  -0.0970 0.1627  220 CYS A CB    
1604 S SG    . CYS A 248 ? 0.9089 0.7207 0.8546 0.1235  -0.1069 0.1549  220 CYS A SG    
1605 N N     . ASP A 249 ? 0.8064 0.6483 0.7443 0.1417  -0.0925 0.1516  221 ASP A N     
1606 C CA    . ASP A 249 ? 0.7715 0.6186 0.7096 0.1453  -0.0925 0.1547  221 ASP A CA    
1607 C C     . ASP A 249 ? 0.7028 0.5397 0.6354 0.1490  -0.0978 0.1473  221 ASP A C     
1608 O O     . ASP A 249 ? 0.7053 0.5324 0.6307 0.1501  -0.1002 0.1368  221 ASP A O     
1609 C CB    . ASP A 249 ? 0.8603 0.7222 0.7912 0.1521  -0.0837 0.1511  221 ASP A CB    
1610 C CG    . ASP A 249 ? 0.9406 0.8125 0.8750 0.1497  -0.0761 0.1563  221 ASP A CG    
1611 O OD1   . ASP A 249 ? 0.9560 0.8310 0.8990 0.1446  -0.0761 0.1670  221 ASP A OD1   
1612 O OD2   . ASP A 249 ? 0.9211 0.7970 0.8487 0.1531  -0.0698 0.1492  221 ASP A OD2   
1613 N N     . LEU A 250 ? 0.6851 0.5238 0.6203 0.1510  -0.0997 0.1525  222 LEU A N     
1614 C CA    . LEU A 250 ? 0.6373 0.4669 0.5681 0.1552  -0.1042 0.1468  222 LEU A CA    
1615 C C     . LEU A 250 ? 0.5790 0.4192 0.5057 0.1626  -0.1020 0.1456  222 LEU A C     
1616 O O     . LEU A 250 ? 0.5595 0.4091 0.4905 0.1617  -0.0998 0.1548  222 LEU A O     
1617 C CB    . LEU A 250 ? 0.6203 0.4382 0.5585 0.1502  -0.1092 0.1557  222 LEU A CB    
1618 C CG    . LEU A 250 ? 0.6403 0.4471 0.5743 0.1545  -0.1137 0.1518  222 LEU A CG    
1619 C CD1   . LEU A 250 ? 0.6955 0.4905 0.6195 0.1576  -0.1167 0.1369  222 LEU A CD1   
1620 C CD2   . LEU A 250 ? 0.6582 0.4538 0.5978 0.1499  -0.1168 0.1619  222 LEU A CD2   
1621 N N     . GLY A 251 ? 0.5979 0.4368 0.5160 0.1699  -0.1026 0.1342  223 GLY A N     
1622 C CA    . GLY A 251 ? 0.6225 0.4726 0.5366 0.1776  -0.1009 0.1323  223 GLY A CA    
1623 C C     . GLY A 251 ? 0.6288 0.4728 0.5377 0.1844  -0.1045 0.1227  223 GLY A C     
1624 O O     . GLY A 251 ? 0.6808 0.5127 0.5864 0.1843  -0.1069 0.1148  223 GLY A O     
1625 N N     . PRO A 252 ? 0.5950 0.4473 0.5026 0.1908  -0.1048 0.1235  224 PRO A N     
1626 C CA    . PRO A 252 ? 0.5934 0.4422 0.4969 0.1985  -0.1076 0.1148  224 PRO A CA    
1627 C C     . PRO A 252 ? 0.5951 0.4556 0.4912 0.2056  -0.1043 0.1021  224 PRO A C     
1628 O O     . PRO A 252 ? 0.5890 0.4636 0.4824 0.2064  -0.0996 0.1010  224 PRO A O     
1629 C CB    . PRO A 252 ? 0.6378 0.4925 0.5443 0.2019  -0.1093 0.1227  224 PRO A CB    
1630 C CG    . PRO A 252 ? 0.6336 0.5029 0.5406 0.1997  -0.1051 0.1300  224 PRO A CG    
1631 C CD    . PRO A 252 ? 0.5979 0.4625 0.5079 0.1912  -0.1028 0.1332  224 PRO A CD    
1632 N N     . GLN A 253 ? 0.6342 0.4888 0.5272 0.2113  -0.1066 0.0925  225 GLN A N     
1633 C CA    . GLN A 253 ? 0.5732 0.4386 0.4607 0.2186  -0.1039 0.0801  225 GLN A CA    
1634 C C     . GLN A 253 ? 0.5800 0.4479 0.4674 0.2276  -0.1065 0.0747  225 GLN A C     
1635 O O     . GLN A 253 ? 0.6164 0.4703 0.5058 0.2279  -0.1103 0.0776  225 GLN A O     
1636 C CB    . GLN A 253 ? 0.6040 0.4589 0.4874 0.2161  -0.1028 0.0718  225 GLN A CB    
1637 C CG    . GLN A 253 ? 0.6247 0.4799 0.5087 0.2072  -0.0991 0.0755  225 GLN A CG    
1638 C CD    . GLN A 253 ? 0.6841 0.5613 0.5682 0.2055  -0.0915 0.0717  225 GLN A CD    
1639 O OE1   . GLN A 253 ? 0.6874 0.5787 0.5703 0.2098  -0.0888 0.0626  225 GLN A OE1   
1640 N NE2   . GLN A 253 ? 0.7344 0.6145 0.6201 0.1992  -0.0879 0.0785  225 GLN A NE2   
1641 N N     . LYS A 254 ? 0.6122 0.4985 0.4976 0.2352  -0.1043 0.0670  226 LYS A N     
1642 C CA    . LYS A 254 ? 0.6503 0.5427 0.5366 0.2446  -0.1060 0.0605  226 LYS A CA    
1643 C C     . LYS A 254 ? 0.6151 0.5138 0.5001 0.2464  -0.1022 0.0466  226 LYS A C     
1644 O O     . LYS A 254 ? 0.5956 0.5049 0.4805 0.2391  -0.0964 0.0414  226 LYS A O     
1645 C CB    . LYS A 254 ? 0.6589 0.5726 0.5473 0.2499  -0.1064 0.0638  226 LYS A CB    
1646 C CG    . LYS A 254 ? 0.6851 0.5945 0.5763 0.2469  -0.1088 0.0769  226 LYS A CG    
1647 C CD    . LYS A 254 ? 0.7761 0.7067 0.6680 0.2531  -0.1095 0.0790  226 LYS A CD    
1648 C CE    . LYS A 254 ? 0.8690 0.7954 0.7630 0.2505  -0.1117 0.0923  226 LYS A CE    
1649 N NZ    . LYS A 254 ? 0.6773 0.6236 0.5709 0.2568  -0.1129 0.0942  226 LYS A NZ    
1650 N N     . VAL A 255 ? 0.6231 0.5159 0.5082 0.2538  -0.1040 0.0402  227 VAL A N     
1651 C CA    . VAL A 255 ? 0.5933 0.4940 0.4789 0.2542  -0.0990 0.0267  227 VAL A CA    
1652 C C     . VAL A 255 ? 0.6361 0.5571 0.5267 0.2641  -0.0993 0.0225  227 VAL A C     
1653 O O     . VAL A 255 ? 0.6647 0.5791 0.5561 0.2741  -0.1038 0.0250  227 VAL A O     
1654 C CB    . VAL A 255 ? 0.5962 0.4733 0.4772 0.2547  -0.0999 0.0219  227 VAL A CB    
1655 C CG1   . VAL A 255 ? 0.5901 0.4763 0.4712 0.2544  -0.0935 0.0085  227 VAL A CG1   
1656 C CG2   . VAL A 255 ? 0.6424 0.4991 0.5190 0.2453  -0.1015 0.0278  227 VAL A CG2   
1657 N N     . PHE A 256 ? 0.6201 0.5659 0.5142 0.2614  -0.0946 0.0162  228 PHE A N     
1658 C CA    . PHE A 256 ? 0.6145 0.5837 0.5145 0.2696  -0.0955 0.0130  228 PHE A CA    
1659 C C     . PHE A 256 ? 0.6111 0.5851 0.5149 0.2749  -0.0925 0.0019  228 PHE A C     
1660 O O     . PHE A 256 ? 0.6302 0.6001 0.5324 0.2689  -0.0870 -0.0063 228 PHE A O     
1661 C CB    . PHE A 256 ? 0.5990 0.5929 0.5008 0.2635  -0.0923 0.0109  228 PHE A CB    
1662 C CG    . PHE A 256 ? 0.6379 0.6585 0.5465 0.2702  -0.0933 0.0062  228 PHE A CG    
1663 C CD1   . PHE A 256 ? 0.6856 0.7147 0.5958 0.2789  -0.0995 0.0141  228 PHE A CD1   
1664 C CD2   . PHE A 256 ? 0.6504 0.6882 0.5640 0.2677  -0.0881 -0.0057 228 PHE A CD2   
1665 C CE1   . PHE A 256 ? 0.7228 0.7779 0.6398 0.2851  -0.1011 0.0101  228 PHE A CE1   
1666 C CE2   . PHE A 256 ? 0.6326 0.6967 0.5538 0.2733  -0.0895 -0.0098 228 PHE A CE2   
1667 C CZ    . PHE A 256 ? 0.7103 0.7835 0.6333 0.2822  -0.0963 -0.0020 228 PHE A CZ    
1668 N N     . PHE A 257 ? 0.6061 0.5890 0.5149 0.2866  -0.0959 0.0022  229 PHE A N     
1669 C CA    . PHE A 257 ? 0.6163 0.6092 0.5307 0.2932  -0.0927 -0.0077 229 PHE A CA    
1670 C C     . PHE A 257 ? 0.6143 0.6367 0.5379 0.3008  -0.0948 -0.0081 229 PHE A C     
1671 O O     . PHE A 257 ? 0.6363 0.6597 0.5605 0.3087  -0.1011 0.0008  229 PHE A O     
1672 C CB    . PHE A 257 ? 0.6425 0.6110 0.5535 0.3021  -0.0946 -0.0075 229 PHE A CB    
1673 C CG    . PHE A 257 ? 0.6268 0.5674 0.5286 0.2947  -0.0929 -0.0086 229 PHE A CG    
1674 C CD1   . PHE A 257 ? 0.5988 0.5373 0.4988 0.2906  -0.0865 -0.0191 229 PHE A CD1   
1675 C CD2   . PHE A 257 ? 0.6132 0.5303 0.5083 0.2914  -0.0979 0.0010  229 PHE A CD2   
1676 C CE1   . PHE A 257 ? 0.5644 0.4777 0.4552 0.2838  -0.0855 -0.0200 229 PHE A CE1   
1677 C CE2   . PHE A 257 ? 0.5713 0.4640 0.4586 0.2841  -0.0972 0.0000  229 PHE A CE2   
1678 C CZ    . PHE A 257 ? 0.5680 0.4588 0.4527 0.2805  -0.0912 -0.0106 229 PHE A CZ    
1679 N N     . PRO A 258 ? 0.5907 0.6376 0.5215 0.2985  -0.0900 -0.0177 230 PRO A N     
1680 C CA    . PRO A 258 ? 0.6954 0.7727 0.6355 0.3044  -0.0929 -0.0179 230 PRO A CA    
1681 C C     . PRO A 258 ? 0.7090 0.7902 0.6559 0.3199  -0.0961 -0.0168 230 PRO A C     
1682 O O     . PRO A 258 ? 0.7587 0.8549 0.7101 0.3279  -0.1019 -0.0109 230 PRO A O     
1683 C CB    . PRO A 258 ? 0.7411 0.8408 0.6870 0.2955  -0.0863 -0.0292 230 PRO A CB    
1684 C CG    . PRO A 258 ? 0.6305 0.7115 0.5724 0.2911  -0.0796 -0.0359 230 PRO A CG    
1685 C CD    . PRO A 258 ? 0.6123 0.6607 0.5431 0.2896  -0.0821 -0.0283 230 PRO A CD    
1686 N N     . THR A 259 ? 0.6496 0.7174 0.5966 0.3249  -0.0924 -0.0223 231 THR A N     
1687 C CA    . THR A 259 ? 0.6807 0.7515 0.6342 0.3404  -0.0941 -0.0221 231 THR A CA    
1688 C C     . THR A 259 ? 0.7122 0.7486 0.6565 0.3445  -0.0970 -0.0149 231 THR A C     
1689 O O     . THR A 259 ? 0.7340 0.7453 0.6680 0.3372  -0.0980 -0.0109 231 THR A O     
1690 C CB    . THR A 259 ? 0.7221 0.8025 0.6822 0.3422  -0.0864 -0.0337 231 THR A CB    
1691 O OG1   . THR A 259 ? 0.8105 0.8611 0.7603 0.3388  -0.0821 -0.0374 231 THR A OG1   
1692 C CG2   . THR A 259 ? 0.7196 0.8285 0.6869 0.3311  -0.0817 -0.0414 231 THR A CG2   
1693 N N     . ALA A 260 ? 0.6996 0.7351 0.6482 0.3533  -0.0975 -0.0132 232 ALA A N     
1694 C CA    . ALA A 260 ? 0.7061 0.7096 0.6468 0.3547  -0.0994 -0.0068 232 ALA A CA    
1695 C C     . ALA A 260 ? 0.7374 0.7155 0.6704 0.3545  -0.0948 -0.0138 232 ALA A C     
1696 O O     . ALA A 260 ? 0.6665 0.6142 0.5890 0.3492  -0.0965 -0.0100 232 ALA A O     
1697 C CB    . ALA A 260 ? 0.7424 0.7536 0.6903 0.3648  -0.1015 -0.0021 232 ALA A CB    
1698 N N     . GLU A 261 ? 0.7777 0.7681 0.7156 0.3595  -0.0888 -0.0240 233 GLU A N     
1699 C CA    . GLU A 261 ? 0.8285 0.7947 0.7580 0.3603  -0.0839 -0.0309 233 GLU A CA    
1700 C C     . GLU A 261 ? 0.8015 0.7536 0.7216 0.3502  -0.0820 -0.0350 233 GLU A C     
1701 O O     . GLU A 261 ? 0.8535 0.7757 0.7619 0.3472  -0.0814 -0.0363 233 GLU A O     
1702 C CB    . GLU A 261 ? 0.8788 0.8632 0.8169 0.3691  -0.0771 -0.0399 233 GLU A CB    
1703 C CG    . GLU A 261 ? 0.9474 0.9065 0.8758 0.3711  -0.0717 -0.0465 233 GLU A CG    
1704 C CD    . GLU A 261 ? 1.0314 1.0066 0.9685 0.3812  -0.0650 -0.0531 233 GLU A CD    
1705 O OE1   . GLU A 261 ? 1.0806 1.0859 1.0323 0.3872  -0.0656 -0.0515 233 GLU A OE1   
1706 O OE2   . GLU A 261 ? 1.0565 1.0149 0.9859 0.3828  -0.0592 -0.0598 233 GLU A OE2   
1707 N N     . THR A 262 ? 0.7733 0.7459 0.6978 0.3449  -0.0812 -0.0372 234 THR A N     
1708 C CA    . THR A 262 ? 0.7208 0.6795 0.6363 0.3314  -0.0789 -0.0395 234 THR A CA    
1709 C C     . THR A 262 ? 0.7380 0.6702 0.6438 0.3264  -0.0856 -0.0298 234 THR A C     
1710 O O     . THR A 262 ? 0.7115 0.6231 0.6078 0.3171  -0.0845 -0.0310 234 THR A O     
1711 C CB    . THR A 262 ? 0.6147 0.6010 0.5370 0.3201  -0.0750 -0.0430 234 THR A CB    
1712 O OG1   . THR A 262 ? 0.7354 0.7394 0.6638 0.3203  -0.0806 -0.0354 234 THR A OG1   
1713 C CG2   . THR A 262 ? 0.5675 0.5783 0.4994 0.3227  -0.0676 -0.0531 234 THR A CG2   
1714 N N     . HIS A 263 ? 0.7478 0.6814 0.6563 0.3290  -0.0916 -0.0199 235 HIS A N     
1715 C CA    . HIS A 263 ? 0.6793 0.5865 0.5798 0.3223  -0.0967 -0.0103 235 HIS A CA    
1716 C C     . HIS A 263 ? 0.7152 0.5926 0.6078 0.3242  -0.0968 -0.0117 235 HIS A C     
1717 O O     . HIS A 263 ? 0.7008 0.5524 0.5843 0.3165  -0.0991 -0.0088 235 HIS A O     
1718 C CB    . HIS A 263 ? 0.6580 0.5753 0.5639 0.3234  -0.1017 0.0005  235 HIS A CB    
1719 C CG    . HIS A 263 ? 0.6224 0.5143 0.5224 0.3171  -0.1062 0.0108  235 HIS A CG    
1720 N ND1   . HIS A 263 ? 0.6214 0.4996 0.5156 0.3062  -0.1075 0.0148  235 HIS A ND1   
1721 C CD2   . HIS A 263 ? 0.6395 0.5181 0.5396 0.3200  -0.1096 0.0183  235 HIS A CD2   
1722 C CE1   . HIS A 263 ? 0.6285 0.4871 0.5202 0.3022  -0.1114 0.0242  235 HIS A CE1   
1723 N NE2   . HIS A 263 ? 0.6430 0.5009 0.5379 0.3105  -0.1127 0.0264  235 HIS A NE2   
1724 N N     . ARG A 264 ? 0.7226 0.6036 0.6185 0.3344  -0.0942 -0.0162 236 ARG A N     
1725 C CA    . ARG A 264 ? 0.7090 0.5623 0.5966 0.3374  -0.0938 -0.0184 236 ARG A CA    
1726 C C     . ARG A 264 ? 0.7336 0.5744 0.6123 0.3348  -0.0889 -0.0288 236 ARG A C     
1727 O O     . ARG A 264 ? 0.7485 0.5602 0.6157 0.3297  -0.0906 -0.0289 236 ARG A O     
1728 C CB    . ARG A 264 ? 0.7844 0.6467 0.6787 0.3499  -0.0922 -0.0193 236 ARG A CB    
1729 C CG    . ARG A 264 ? 0.7529 0.5860 0.6388 0.3541  -0.0922 -0.0201 236 ARG A CG    
1730 C CD    . ARG A 264 ? 0.7155 0.5596 0.6095 0.3669  -0.0909 -0.0192 236 ARG A CD    
1731 N NE    . ARG A 264 ? 0.8169 0.6327 0.7025 0.3718  -0.0905 -0.0201 236 ARG A NE    
1732 C CZ    . ARG A 264 ? 0.9166 0.7219 0.7957 0.3760  -0.0850 -0.0296 236 ARG A CZ    
1733 N NH1   . ARG A 264 ? 0.9147 0.7354 0.7951 0.3758  -0.0790 -0.0387 236 ARG A NH1   
1734 N NH2   . ARG A 264 ? 0.8445 0.6230 0.7152 0.3805  -0.0853 -0.0299 236 ARG A NH2   
1735 N N     . GLU A 265 ? 0.7740 0.6371 0.6581 0.3377  -0.0827 -0.0374 237 GLU A N     
1736 C CA    . GLU A 265 ? 0.7517 0.6047 0.6276 0.3355  -0.0768 -0.0474 237 GLU A CA    
1737 C C     . GLU A 265 ? 0.7255 0.5618 0.5918 0.3237  -0.0789 -0.0463 237 GLU A C     
1738 O O     . GLU A 265 ? 0.7399 0.5546 0.5945 0.3200  -0.0770 -0.0515 237 GLU A O     
1739 C CB    . GLU A 265 ? 0.7225 0.6058 0.6081 0.3400  -0.0690 -0.0562 237 GLU A CB    
1740 C CG    . GLU A 265 ? 0.7992 0.6990 0.6943 0.3518  -0.0656 -0.0587 237 GLU A CG    
1741 C CD    . GLU A 265 ? 0.9669 0.8417 0.8524 0.3569  -0.0634 -0.0618 237 GLU A CD    
1742 O OE1   . GLU A 265 ? 0.9437 0.7978 0.8166 0.3520  -0.0604 -0.0674 237 GLU A OE1   
1743 O OE2   . GLU A 265 ? 1.0361 0.9116 0.9261 0.3657  -0.0647 -0.0585 237 GLU A OE2   
1744 N N     . PHE A 266 ? 0.6735 0.5196 0.5443 0.3176  -0.0828 -0.0395 238 PHE A N     
1745 C CA    . PHE A 266 ? 0.6240 0.4551 0.4869 0.3054  -0.0847 -0.0369 238 PHE A CA    
1746 C C     . PHE A 266 ? 0.6468 0.4452 0.4997 0.3013  -0.0910 -0.0310 238 PHE A C     
1747 O O     . PHE A 266 ? 0.6631 0.4412 0.5058 0.2940  -0.0917 -0.0329 238 PHE A O     
1748 C CB    . PHE A 266 ? 0.6043 0.4556 0.4751 0.2970  -0.0861 -0.0301 238 PHE A CB    
1749 C CG    . PHE A 266 ? 0.5967 0.4359 0.4615 0.2831  -0.0872 -0.0265 238 PHE A CG    
1750 C CD1   . PHE A 266 ? 0.5853 0.4301 0.4479 0.2740  -0.0808 -0.0333 238 PHE A CD1   
1751 C CD2   . PHE A 266 ? 0.6018 0.4241 0.4636 0.2795  -0.0945 -0.0159 238 PHE A CD2   
1752 C CE1   . PHE A 266 ? 0.5789 0.4132 0.4366 0.2621  -0.0818 -0.0295 238 PHE A CE1   
1753 C CE2   . PHE A 266 ? 0.5949 0.4078 0.4527 0.2672  -0.0954 -0.0121 238 PHE A CE2   
1754 C CZ    . PHE A 266 ? 0.5834 0.4025 0.4391 0.2589  -0.0892 -0.0189 238 PHE A CZ    
1755 N N     . LEU A 267 ? 0.6826 0.4762 0.5386 0.3046  -0.0955 -0.0237 239 LEU A N     
1756 C CA    . LEU A 267 ? 0.6706 0.4346 0.5186 0.2995  -0.1010 -0.0180 239 LEU A CA    
1757 C C     . LEU A 267 ? 0.7039 0.4448 0.5405 0.3023  -0.0993 -0.0262 239 LEU A C     
1758 O O     . LEU A 267 ? 0.7350 0.4491 0.5622 0.2960  -0.1038 -0.0240 239 LEU A O     
1759 C CB    . LEU A 267 ? 0.6787 0.4441 0.5333 0.3028  -0.1052 -0.0083 239 LEU A CB    
1760 C CG    . LEU A 267 ? 0.6635 0.4427 0.5257 0.2965  -0.1085 0.0022  239 LEU A CG    
1761 C CD1   . LEU A 267 ? 0.6718 0.4557 0.5409 0.3013  -0.1114 0.0111  239 LEU A CD1   
1762 C CD2   . LEU A 267 ? 0.6617 0.4231 0.5186 0.2837  -0.1122 0.0078  239 LEU A CD2   
1763 N N     . LYS A 268 ? 0.6934 0.4448 0.5306 0.3114  -0.0928 -0.0356 240 LYS A N     
1764 C CA    . LYS A 268 ? 0.7121 0.4430 0.5371 0.3136  -0.0898 -0.0443 240 LYS A CA    
1765 C C     . LYS A 268 ? 0.7089 0.4256 0.5228 0.3037  -0.0897 -0.0484 240 LYS A C     
1766 O O     . LYS A 268 ? 0.7273 0.4171 0.5279 0.3002  -0.0919 -0.0510 240 LYS A O     
1767 C CB    . LYS A 268 ? 0.7125 0.4620 0.5423 0.3245  -0.0814 -0.0531 240 LYS A CB    
1768 C CG    . LYS A 268 ? 0.7565 0.5075 0.5912 0.3356  -0.0812 -0.0515 240 LYS A CG    
1769 C CD    . LYS A 268 ? 0.8644 0.6331 0.7037 0.3455  -0.0723 -0.0605 240 LYS A CD    
1770 C CE    . LYS A 268 ? 0.9977 0.7674 0.8421 0.3572  -0.0718 -0.0585 240 LYS A CE    
1771 N NZ    . LYS A 268 ? 1.0571 0.8467 0.9080 0.3669  -0.0629 -0.0664 240 LYS A NZ    
1772 N N     . SER A 269 ? 0.6869 0.4209 0.5055 0.2990  -0.0873 -0.0489 241 SER A N     
1773 C CA    . SER A 269 ? 0.6835 0.4063 0.4920 0.2904  -0.0861 -0.0533 241 SER A CA    
1774 C C     . SER A 269 ? 0.6876 0.3886 0.4901 0.2795  -0.0945 -0.0452 241 SER A C     
1775 O O     . SER A 269 ? 0.7173 0.3964 0.5070 0.2736  -0.0963 -0.0483 241 SER A O     
1776 C CB    . SER A 269 ? 0.6953 0.4443 0.5117 0.2879  -0.0801 -0.0560 241 SER A CB    
1777 O OG    . SER A 269 ? 0.6426 0.4026 0.4673 0.2798  -0.0842 -0.0466 241 SER A OG    
1778 N N     . VAL A 270 ? 0.6792 0.3867 0.4908 0.2764  -0.0997 -0.0346 242 VAL A N     
1779 C CA    . VAL A 270 ? 0.6797 0.3717 0.4888 0.2649  -0.1069 -0.0258 242 VAL A CA    
1780 C C     . VAL A 270 ? 0.7327 0.3997 0.5361 0.2636  -0.1131 -0.0223 242 VAL A C     
1781 O O     . VAL A 270 ? 0.7962 0.4507 0.5995 0.2543  -0.1196 -0.0140 242 VAL A O     
1782 C CB    . VAL A 270 ? 0.6603 0.3717 0.4818 0.2612  -0.1086 -0.0157 242 VAL A CB    
1783 C CG1   . VAL A 270 ? 0.6388 0.3750 0.4656 0.2626  -0.1022 -0.0200 242 VAL A CG1   
1784 C CG2   . VAL A 270 ? 0.6787 0.3986 0.5090 0.2674  -0.1103 -0.0095 242 VAL A CG2   
1785 N N     . CYS A 271 ? 0.7206 0.3804 0.5196 0.2728  -0.1109 -0.0283 243 CYS A N     
1786 C CA    . CYS A 271 ? 0.7462 0.3798 0.5378 0.2724  -0.1160 -0.0266 243 CYS A CA    
1787 C C     . CYS A 271 ? 0.8555 0.4646 0.6307 0.2670  -0.1176 -0.0338 243 CYS A C     
1788 O O     . CYS A 271 ? 0.8396 0.4467 0.6064 0.2728  -0.1120 -0.0441 243 CYS A O     
1789 C CB    . CYS A 271 ? 0.7596 0.3962 0.5535 0.2851  -0.1126 -0.0296 243 CYS A CB    
1790 S SG    . CYS A 271 ? 0.8140 0.4184 0.5997 0.2856  -0.1186 -0.0267 243 CYS A SG    
1791 N N     . ALA A 272 ? 0.9135 0.5051 0.6845 0.2556  -0.1251 -0.0281 244 ALA A N     
1792 C CA    . ALA A 272 ? 0.9157 0.4868 0.6717 0.2486  -0.1277 -0.0339 244 ALA A CA    
1793 C C     . ALA A 272 ? 0.8666 0.4110 0.6079 0.2516  -0.1297 -0.0404 244 ALA A C     
1794 O O     . ALA A 272 ? 0.9153 0.4440 0.6419 0.2481  -0.1304 -0.0475 244 ALA A O     
1795 C CB    . ALA A 272 ? 0.9675 0.5315 0.7257 0.2349  -0.1356 -0.0249 244 ALA A CB    
1796 N N     . PHE A 273 ? 0.8428 0.3812 0.5870 0.2582  -0.1305 -0.0381 245 PHE A N     
1797 C CA    . PHE A 273 ? 0.8559 0.3671 0.5861 0.2608  -0.1327 -0.0435 245 PHE A CA    
1798 C C     . PHE A 273 ? 0.8662 0.3811 0.5911 0.2740  -0.1240 -0.0536 245 PHE A C     
1799 O O     . PHE A 273 ? 0.8936 0.3861 0.6047 0.2767  -0.1245 -0.0596 245 PHE A O     
1800 C CB    . PHE A 273 ? 0.8704 0.3690 0.6056 0.2599  -0.1387 -0.0349 245 PHE A CB    
1801 C CG    . PHE A 273 ? 0.8735 0.3572 0.6083 0.2458  -0.1482 -0.0270 245 PHE A CG    
1802 C CD1   . PHE A 273 ? 0.8992 0.3535 0.6185 0.2392  -0.1547 -0.0308 245 PHE A CD1   
1803 C CD2   . PHE A 273 ? 0.8516 0.3515 0.6016 0.2391  -0.1507 -0.0157 245 PHE A CD2   
1804 C CE1   . PHE A 273 ? 0.9024 0.3445 0.6226 0.2258  -0.1639 -0.0233 245 PHE A CE1   
1805 C CE2   . PHE A 273 ? 0.8543 0.3426 0.6056 0.2260  -0.1589 -0.0078 245 PHE A CE2   
1806 C CZ    . PHE A 273 ? 0.8795 0.3391 0.6165 0.2192  -0.1658 -0.0116 245 PHE A CZ    
1807 N N     . LEU A 274 ? 0.8459 0.3889 0.5816 0.2819  -0.1161 -0.0554 246 LEU A N     
1808 C CA    . LEU A 274 ? 0.8550 0.4049 0.5891 0.2947  -0.1076 -0.0635 246 LEU A CA    
1809 C C     . LEU A 274 ? 0.8687 0.4067 0.5861 0.2948  -0.1031 -0.0746 246 LEU A C     
1810 O O     . LEU A 274 ? 0.8861 0.4202 0.5981 0.3042  -0.0974 -0.0812 246 LEU A O     
1811 C CB    . LEU A 274 ? 0.8290 0.4139 0.5796 0.3018  -0.1006 -0.0627 246 LEU A CB    
1812 C CG    . LEU A 274 ? 0.8240 0.4222 0.5898 0.3079  -0.1022 -0.0541 246 LEU A CG    
1813 C CD1   . LEU A 274 ? 0.7979 0.4316 0.5791 0.3136  -0.0963 -0.0538 246 LEU A CD1   
1814 C CD2   . LEU A 274 ? 0.8509 0.4352 0.6131 0.3178  -0.1012 -0.0557 246 LEU A CD2   
1815 N N     . TYR A 275 ? 0.8849 0.4174 0.5940 0.2846  -0.1054 -0.0764 247 TYR A N     
1816 C CA    . TYR A 275 ? 0.9149 0.4361 0.6070 0.2840  -0.1012 -0.0864 247 TYR A CA    
1817 C C     . TYR A 275 ? 0.9817 0.4701 0.6562 0.2827  -0.1064 -0.0897 247 TYR A C     
1818 O O     . TYR A 275 ? 1.0363 0.5146 0.6958 0.2844  -0.1021 -0.0984 247 TYR A O     
1819 C CB    . TYR A 275 ? 0.9029 0.4274 0.5910 0.2734  -0.1026 -0.0867 247 TYR A CB    
1820 C CG    . TYR A 275 ? 0.9244 0.4253 0.6035 0.2611  -0.1140 -0.0821 247 TYR A CG    
1821 C CD1   . TYR A 275 ? 0.8851 0.3893 0.5761 0.2540  -0.1216 -0.0716 247 TYR A CD1   
1822 C CD2   . TYR A 275 ? 1.0131 0.4894 0.6721 0.2561  -0.1173 -0.0880 247 TYR A CD2   
1823 C CE1   . TYR A 275 ? 0.9072 0.3916 0.5918 0.2423  -0.1320 -0.0668 247 TYR A CE1   
1824 C CE2   . TYR A 275 ? 1.0283 0.4841 0.6799 0.2445  -0.1285 -0.0838 247 TYR A CE2   
1825 C CZ    . TYR A 275 ? 1.0095 0.4697 0.6746 0.2375  -0.1358 -0.0731 247 TYR A CZ    
1826 O OH    . TYR A 275 ? 1.1133 0.5547 0.7726 0.2255  -0.1469 -0.0684 247 TYR A OH    
1827 N N     . ARG A 276 ? 0.9523 0.4240 0.6281 0.2795  -0.1151 -0.0830 248 ARG A N     
1828 C CA    . ARG A 276 ? 0.9803 0.4199 0.6398 0.2780  -0.1205 -0.0860 248 ARG A CA    
1829 C C     . ARG A 276 ? 1.0883 0.5224 0.7484 0.2904  -0.1162 -0.0881 248 ARG A C     
1830 O O     . ARG A 276 ? 1.1237 0.5326 0.7681 0.2919  -0.1175 -0.0935 248 ARG A O     
1831 C CB    . ARG A 276 ? 0.9616 0.3839 0.6216 0.2662  -0.1328 -0.0775 248 ARG A CB    
1832 C CG    . ARG A 276 ? 0.9768 0.3987 0.6339 0.2529  -0.1387 -0.0753 248 ARG A CG    
1833 C CD    . ARG A 276 ? 0.9984 0.4031 0.6570 0.2414  -0.1508 -0.0666 248 ARG A CD    
1834 N NE    . ARG A 276 ? 1.0329 0.4372 0.6895 0.2286  -0.1570 -0.0637 248 ARG A NE    
1835 C CZ    . ARG A 276 ? 1.0285 0.4188 0.6857 0.2166  -0.1679 -0.0566 248 ARG A CZ    
1836 N NH1   . ARG A 276 ? 1.0216 0.3964 0.6809 0.2150  -0.1737 -0.0517 248 ARG A NH1   
1837 N NH2   . ARG A 276 ? 1.0644 0.4569 0.7207 0.2059  -0.1729 -0.0541 248 ARG A NH2   
1838 N N     . ILE A 277 ? 1.0524 0.5095 0.7299 0.2995  -0.1112 -0.0839 249 ILE A N     
1839 C CA    . ILE A 277 ? 1.0664 0.5193 0.7473 0.3113  -0.1082 -0.0837 249 ILE A CA    
1840 C C     . ILE A 277 ? 1.1282 0.5912 0.8059 0.3233  -0.0969 -0.0929 249 ILE A C     
1841 O O     . ILE A 277 ? 1.1090 0.5981 0.7945 0.3256  -0.0899 -0.0955 249 ILE A O     
1842 C CB    . ILE A 277 ? 0.9962 0.4689 0.6978 0.3149  -0.1093 -0.0735 249 ILE A CB    
1843 C CG1   . ILE A 277 ? 0.9541 0.4186 0.6598 0.3023  -0.1196 -0.0636 249 ILE A CG1   
1844 C CG2   . ILE A 277 ? 1.1322 0.5990 0.8369 0.3271  -0.1068 -0.0724 249 ILE A CG2   
1845 C CD1   . ILE A 277 ? 0.9849 0.4144 0.6774 0.2962  -0.1276 -0.0627 249 ILE A CD1   
1846 N N     . PRO A 278 ? 1.1117 0.5553 0.7787 0.3309  -0.0945 -0.0980 250 PRO A N     
1847 C CA    . PRO A 278 ? 1.1747 0.6301 0.8414 0.3435  -0.0831 -0.1056 250 PRO A CA    
1848 C C     . PRO A 278 ? 1.1985 0.6844 0.8869 0.3543  -0.0775 -0.1010 250 PRO A C     
1849 O O     . PRO A 278 ? 1.2666 0.7609 0.9686 0.3534  -0.0827 -0.0920 250 PRO A O     
1850 C CB    . PRO A 278 ? 1.2768 0.7011 0.9277 0.3487  -0.0835 -0.1102 250 PRO A CB    
1851 C CG    . PRO A 278 ? 1.2405 0.6353 0.8780 0.3358  -0.0950 -0.1080 250 PRO A CG    
1852 C CD    . PRO A 278 ? 1.1105 0.5186 0.7630 0.3272  -0.1021 -0.0979 250 PRO A CD    
1853 N N     . GLU A 279 ? 1.2056 0.7087 0.8974 0.3646  -0.0668 -0.1072 251 GLU A N     
1854 C CA    . GLU A 279 ? 1.3246 0.8617 1.0378 0.3740  -0.0611 -0.1038 251 GLU A CA    
1855 C C     . GLU A 279 ? 1.3647 0.8994 1.0876 0.3832  -0.0637 -0.0971 251 GLU A C     
1856 O O     . GLU A 279 ? 1.3373 0.8947 1.0779 0.3854  -0.0653 -0.0897 251 GLU A O     
1857 C CB    . GLU A 279 ? 1.3094 0.8646 1.0243 0.3825  -0.0489 -0.1120 251 GLU A CB    
1858 C CG    . GLU A 279 ? 1.3969 0.9892 1.1346 0.3919  -0.0430 -0.1090 251 GLU A CG    
1859 C CD    . GLU A 279 ? 1.4666 1.0830 1.2180 0.3843  -0.0467 -0.1034 251 GLU A CD    
1860 O OE1   . GLU A 279 ? 1.4983 1.1111 1.2424 0.3728  -0.0489 -0.1050 251 GLU A OE1   
1861 O OE2   . GLU A 279 ? 1.3871 1.0261 1.1564 0.3899  -0.0475 -0.0972 251 GLU A OE2   
1862 N N     . GLU A 280 ? 1.3490 0.8563 1.0601 0.3886  -0.0641 -0.0995 252 GLU A N     
1863 C CA    . GLU A 280 ? 1.3399 0.8442 1.0598 0.3983  -0.0656 -0.0932 252 GLU A CA    
1864 C C     . GLU A 280 ? 1.3282 0.8285 1.0554 0.3907  -0.0758 -0.0824 252 GLU A C     
1865 O O     . GLU A 280 ? 1.3856 0.8911 1.1243 0.3980  -0.0771 -0.0752 252 GLU A O     
1866 C CB    . GLU A 280 ? 1.4385 0.9106 1.1425 0.4046  -0.0643 -0.0982 252 GLU A CB    
1867 C CG    . GLU A 280 ? 1.4357 0.8708 1.1206 0.3929  -0.0731 -0.0990 252 GLU A CG    
1868 C CD    . GLU A 280 ? 1.3984 0.8206 1.0644 0.3863  -0.0709 -0.1089 252 GLU A CD    
1869 O OE1   . GLU A 280 ? 1.4059 0.8512 1.0756 0.3863  -0.0644 -0.1131 252 GLU A OE1   
1870 O OE2   . GLU A 280 ? 1.3453 0.7344 0.9925 0.3810  -0.0758 -0.1123 252 GLU A OE2   
1871 N N     . GLN A 281 ? 1.2601 0.7518 0.9812 0.3762  -0.0827 -0.0806 253 GLN A N     
1872 C CA    . GLN A 281 ? 1.1980 0.6875 0.9266 0.3679  -0.0918 -0.0699 253 GLN A CA    
1873 C C     . GLN A 281 ? 1.1314 0.6457 0.8702 0.3589  -0.0936 -0.0662 253 GLN A C     
1874 O O     . GLN A 281 ? 1.0899 0.6055 0.8360 0.3515  -0.1006 -0.0568 253 GLN A O     
1875 C CB    . GLN A 281 ? 1.1639 0.6159 0.8765 0.3578  -0.1002 -0.0693 253 GLN A CB    
1876 C CG    . GLN A 281 ? 1.2163 0.6412 0.9195 0.3660  -0.0997 -0.0713 253 GLN A CG    
1877 C CD    . GLN A 281 ? 1.2252 0.6141 0.9142 0.3553  -0.1088 -0.0699 253 GLN A CD    
1878 O OE1   . GLN A 281 ? 1.2429 0.6288 0.9381 0.3460  -0.1165 -0.0608 253 GLN A OE1   
1879 N NE2   . GLN A 281 ? 1.1756 0.5375 0.8455 0.3563  -0.1078 -0.0788 253 GLN A NE2   
1880 N N     . LYS A 282 ? 1.1721 0.7057 0.9115 0.3593  -0.0872 -0.0730 254 LYS A N     
1881 C CA    . LYS A 282 ? 1.0925 0.6511 0.8423 0.3519  -0.0880 -0.0698 254 LYS A CA    
1882 C C     . LYS A 282 ? 1.0216 0.6064 0.7912 0.3568  -0.0887 -0.0609 254 LYS A C     
1883 O O     . LYS A 282 ? 1.0352 0.6249 0.8116 0.3488  -0.0948 -0.0525 254 LYS A O     
1884 C CB    . LYS A 282 ? 1.1286 0.7048 0.8769 0.3534  -0.0795 -0.0789 254 LYS A CB    
1885 C CG    . LYS A 282 ? 1.1124 0.6701 0.8432 0.3435  -0.0803 -0.0856 254 LYS A CG    
1886 C CD    . LYS A 282 ? 1.0773 0.6571 0.8098 0.3444  -0.0714 -0.0928 254 LYS A CD    
1887 C CE    . LYS A 282 ? 0.9844 0.5479 0.7000 0.3339  -0.0723 -0.0984 254 LYS A CE    
1888 N NZ    . LYS A 282 ? 1.1006 0.6842 0.8170 0.3353  -0.0624 -0.1057 254 LYS A NZ    
1889 N N     . ASP A 283 ? 1.0393 0.6424 0.8186 0.3700  -0.0823 -0.0623 255 ASP A N     
1890 C CA    . ASP A 283 ? 0.9839 0.6134 0.7817 0.3754  -0.0831 -0.0542 255 ASP A CA    
1891 C C     . ASP A 283 ? 0.9869 0.6012 0.7868 0.3740  -0.0906 -0.0437 255 ASP A C     
1892 O O     . ASP A 283 ? 0.9754 0.6090 0.7890 0.3749  -0.0932 -0.0350 255 ASP A O     
1893 C CB    . ASP A 283 ? 1.0660 0.7164 0.8732 0.3901  -0.0751 -0.0580 255 ASP A CB    
1894 C CG    . ASP A 283 ? 1.1779 0.8461 0.9851 0.3913  -0.0667 -0.0678 255 ASP A CG    
1895 O OD1   . ASP A 283 ? 1.2576 0.9320 1.0627 0.3813  -0.0673 -0.0697 255 ASP A OD1   
1896 O OD2   . ASP A 283 ? 1.1853 0.8613 0.9948 0.4021  -0.0591 -0.0733 255 ASP A OD2   
1897 N N     . ASP A 284 ? 0.9861 0.5661 0.7724 0.3717  -0.0942 -0.0442 256 ASP A N     
1898 C CA    . ASP A 284 ? 1.0210 0.5835 0.8085 0.3689  -0.1012 -0.0344 256 ASP A CA    
1899 C C     . ASP A 284 ? 0.9493 0.5035 0.7347 0.3533  -0.1087 -0.0283 256 ASP A C     
1900 O O     . ASP A 284 ? 0.9254 0.4825 0.7196 0.3497  -0.1136 -0.0174 256 ASP A O     
1901 C CB    . ASP A 284 ? 1.1223 0.6514 0.8964 0.3736  -0.1015 -0.0379 256 ASP A CB    
1902 C CG    . ASP A 284 ? 1.1496 0.6863 0.9268 0.3897  -0.0939 -0.0427 256 ASP A CG    
1903 O OD1   . ASP A 284 ? 1.0474 0.6157 0.8396 0.3975  -0.0898 -0.0408 256 ASP A OD1   
1904 O OD2   . ASP A 284 ? 1.2177 0.7290 0.9823 0.3945  -0.0920 -0.0484 256 ASP A OD2   
1905 N N     . PHE A 285 ? 0.9443 0.4884 0.7184 0.3439  -0.1096 -0.0347 257 PHE A N     
1906 C CA    . PHE A 285 ? 0.9122 0.4526 0.6861 0.3292  -0.1162 -0.0290 257 PHE A CA    
1907 C C     . PHE A 285 ? 0.8791 0.4522 0.6689 0.3272  -0.1156 -0.0225 257 PHE A C     
1908 O O     . PHE A 285 ? 0.8685 0.4427 0.6639 0.3180  -0.1210 -0.0131 257 PHE A O     
1909 C CB    . PHE A 285 ? 0.9139 0.4403 0.6731 0.3208  -0.1166 -0.0377 257 PHE A CB    
1910 C CG    . PHE A 285 ? 0.9063 0.4222 0.6632 0.3054  -0.1244 -0.0320 257 PHE A CG    
1911 C CD1   . PHE A 285 ? 0.8760 0.4141 0.6430 0.2985  -0.1251 -0.0270 257 PHE A CD1   
1912 C CD2   . PHE A 285 ? 0.9306 0.4145 0.6753 0.2978  -0.1310 -0.0316 257 PHE A CD2   
1913 C CE1   . PHE A 285 ? 0.8694 0.3989 0.6354 0.2847  -0.1318 -0.0212 257 PHE A CE1   
1914 C CE2   . PHE A 285 ? 0.9239 0.3997 0.6679 0.2834  -0.1383 -0.0260 257 PHE A CE2   
1915 C CZ    . PHE A 285 ? 0.8930 0.3920 0.6480 0.2771  -0.1385 -0.0205 257 PHE A CZ    
1916 N N     . PHE A 286 ? 0.8700 0.4703 0.6673 0.3357  -0.1089 -0.0272 258 PHE A N     
1917 C CA    . PHE A 286 ? 0.8334 0.4653 0.6448 0.3341  -0.1082 -0.0222 258 PHE A CA    
1918 C C     . PHE A 286 ? 0.8637 0.5063 0.6875 0.3381  -0.1109 -0.0111 258 PHE A C     
1919 O O     . PHE A 286 ? 0.8613 0.5130 0.6921 0.3305  -0.1148 -0.0021 258 PHE A O     
1920 C CB    . PHE A 286 ? 0.8192 0.4770 0.6353 0.3419  -0.1003 -0.0308 258 PHE A CB    
1921 C CG    . PHE A 286 ? 0.7882 0.4756 0.6153 0.3379  -0.0995 -0.0283 258 PHE A CG    
1922 C CD1   . PHE A 286 ? 0.7737 0.4577 0.5984 0.3253  -0.1033 -0.0250 258 PHE A CD1   
1923 C CD2   . PHE A 286 ? 0.7746 0.4933 0.6145 0.3466  -0.0951 -0.0291 258 PHE A CD2   
1924 C CE1   . PHE A 286 ? 0.7468 0.4571 0.5808 0.3219  -0.1023 -0.0229 258 PHE A CE1   
1925 C CE2   . PHE A 286 ? 0.7599 0.5053 0.6090 0.3427  -0.0946 -0.0273 258 PHE A CE2   
1926 C CZ    . PHE A 286 ? 0.7342 0.4747 0.5799 0.3306  -0.0980 -0.0243 258 PHE A CZ    
1927 N N     . ASP A 287 ? 0.8654 0.5074 0.6920 0.3501  -0.1086 -0.0111 259 ASP A N     
1928 C CA    . ASP A 287 ? 0.8818 0.5338 0.7198 0.3546  -0.1112 -0.0004 259 ASP A CA    
1929 C C     . ASP A 287 ? 0.8856 0.5142 0.7205 0.3457  -0.1180 0.0095  259 ASP A C     
1930 O O     . ASP A 287 ? 0.8774 0.5173 0.7217 0.3427  -0.1211 0.0202  259 ASP A O     
1931 C CB    . ASP A 287 ? 0.9704 0.6242 0.8113 0.3697  -0.1073 -0.0027 259 ASP A CB    
1932 C CG    . ASP A 287 ? 1.0652 0.7503 0.9146 0.3788  -0.1009 -0.0093 259 ASP A CG    
1933 O OD1   . ASP A 287 ? 1.0759 0.7664 0.9209 0.3762  -0.0969 -0.0184 259 ASP A OD1   
1934 O OD2   . ASP A 287 ? 1.1387 0.8437 0.9998 0.3884  -0.0998 -0.0050 259 ASP A OD2   
1935 N N     . ASP A 288 ? 0.8906 0.4870 0.7125 0.3413  -0.1202 0.0060  260 ASP A N     
1936 C CA    . ASP A 288 ? 0.9232 0.4975 0.7424 0.3308  -0.1268 0.0148  260 ASP A CA    
1937 C C     . ASP A 288 ? 0.8806 0.4669 0.7046 0.3177  -0.1299 0.0205  260 ASP A C     
1938 O O     . ASP A 288 ? 0.8667 0.4525 0.6971 0.3112  -0.1339 0.0319  260 ASP A O     
1939 C CB    . ASP A 288 ? 0.9249 0.4638 0.7280 0.3273  -0.1289 0.0082  260 ASP A CB    
1940 C CG    . ASP A 288 ? 1.0083 0.5218 0.8093 0.3201  -0.1353 0.0172  260 ASP A CG    
1941 O OD1   . ASP A 288 ? 1.1309 0.6497 0.9416 0.3235  -0.1363 0.0275  260 ASP A OD1   
1942 O OD2   . ASP A 288 ? 0.9910 0.4796 0.7806 0.3107  -0.1394 0.0142  260 ASP A OD2   
1943 N N     . TRP A 289 ? 0.9049 0.5024 0.7260 0.3141  -0.1275 0.0129  261 TRP A N     
1944 C CA    . TRP A 289 ? 0.8261 0.4359 0.6516 0.3024  -0.1296 0.0175  261 TRP A CA    
1945 C C     . TRP A 289 ? 0.8041 0.4450 0.6440 0.3048  -0.1282 0.0252  261 TRP A C     
1946 O O     . TRP A 289 ? 0.8012 0.4465 0.6475 0.2969  -0.1314 0.0357  261 TRP A O     
1947 C CB    . TRP A 289 ? 0.8184 0.4311 0.6366 0.2991  -0.1269 0.0069  261 TRP A CB    
1948 C CG    . TRP A 289 ? 0.8185 0.4350 0.6376 0.2860  -0.1297 0.0105  261 TRP A CG    
1949 C CD1   . TRP A 289 ? 0.8079 0.4086 0.6259 0.2741  -0.1356 0.0181  261 TRP A CD1   
1950 C CD2   . TRP A 289 ? 0.7700 0.4079 0.5920 0.2835  -0.1264 0.0067  261 TRP A CD2   
1951 N NE1   . TRP A 289 ? 0.7780 0.3896 0.5984 0.2647  -0.1361 0.0197  261 TRP A NE1   
1952 C CE2   . TRP A 289 ? 0.7600 0.3936 0.5823 0.2703  -0.1304 0.0126  261 TRP A CE2   
1953 C CE3   . TRP A 289 ? 0.7554 0.4160 0.5804 0.2911  -0.1201 -0.0009 261 TRP A CE3   
1954 C CZ2   . TRP A 289 ? 0.8224 0.4723 0.6470 0.2650  -0.1283 0.0111  261 TRP A CZ2   
1955 C CZ3   . TRP A 289 ? 0.7325 0.4089 0.5596 0.2855  -0.1182 -0.0027 261 TRP A CZ3   
1956 C CH2   . TRP A 289 ? 0.8106 0.4811 0.6371 0.2728  -0.1222 0.0033  261 TRP A CH2   
1957 N N     . LEU A 290 ? 0.7961 0.4595 0.6412 0.3157  -0.1233 0.0201  262 LEU A N     
1958 C CA    . LEU A 290 ? 0.7755 0.4699 0.6329 0.3180  -0.1222 0.0259  262 LEU A CA    
1959 C C     . LEU A 290 ? 0.7960 0.4898 0.6605 0.3192  -0.1257 0.0385  262 LEU A C     
1960 O O     . LEU A 290 ? 0.7691 0.4795 0.6412 0.3145  -0.1271 0.0471  262 LEU A O     
1961 C CB    . LEU A 290 ? 0.7689 0.4865 0.6309 0.3299  -0.1168 0.0178  262 LEU A CB    
1962 C CG    . LEU A 290 ? 0.7536 0.4818 0.6123 0.3289  -0.1122 0.0066  262 LEU A CG    
1963 C CD1   . LEU A 290 ? 0.7406 0.5010 0.6091 0.3386  -0.1076 0.0023  262 LEU A CD1   
1964 C CD2   . LEU A 290 ? 0.7348 0.4646 0.5920 0.3161  -0.1142 0.0088  262 LEU A CD2   
1965 N N     . GLN A 291 ? 0.8899 0.5646 0.7516 0.3257  -0.1266 0.0398  263 GLN A N     
1966 C CA    . GLN A 291 ? 0.8818 0.5534 0.7496 0.3270  -0.1298 0.0521  263 GLN A CA    
1967 C C     . GLN A 291 ? 0.8562 0.5159 0.7241 0.3135  -0.1341 0.0620  263 GLN A C     
1968 O O     . GLN A 291 ? 0.8527 0.5248 0.7287 0.3107  -0.1357 0.0730  263 GLN A O     
1969 C CB    . GLN A 291 ? 0.8751 0.5248 0.7386 0.3363  -0.1297 0.0508  263 GLN A CB    
1970 C CG    . GLN A 291 ? 0.8939 0.5244 0.7586 0.3331  -0.1340 0.0628  263 GLN A CG    
1971 C CD    . GLN A 291 ? 1.0197 0.6263 0.8790 0.3424  -0.1337 0.0608  263 GLN A CD    
1972 O OE1   . GLN A 291 ? 0.9863 0.5720 0.8348 0.3432  -0.1327 0.0512  263 GLN A OE1   
1973 N NE2   . GLN A 291 ? 1.1337 0.7427 1.0000 0.3496  -0.1345 0.0700  263 GLN A NE2   
1974 N N     . ARG A 292 ? 0.8259 0.4623 0.6848 0.3048  -0.1360 0.0583  264 ARG A N     
1975 C CA    . ARG A 292 ? 0.8240 0.4496 0.6836 0.2913  -0.1401 0.0673  264 ARG A CA    
1976 C C     . ARG A 292 ? 0.8161 0.4650 0.6820 0.2832  -0.1394 0.0709  264 ARG A C     
1977 O O     . ARG A 292 ? 0.8375 0.4820 0.7061 0.2723  -0.1420 0.0797  264 ARG A O     
1978 C CB    . ARG A 292 ? 0.8814 0.4773 0.7294 0.2841  -0.1429 0.0614  264 ARG A CB    
1979 C CG    . ARG A 292 ? 0.9560 0.5295 0.8037 0.2750  -0.1478 0.0714  264 ARG A CG    
1980 C CD    . ARG A 292 ? 0.9459 0.4864 0.7804 0.2723  -0.1509 0.0640  264 ARG A CD    
1981 N NE    . ARG A 292 ? 0.9101 0.4325 0.7407 0.2819  -0.1508 0.0634  264 ARG A NE    
1982 C CZ    . ARG A 292 ? 1.0146 0.5324 0.8382 0.2933  -0.1475 0.0527  264 ARG A CZ    
1983 N NH1   . ARG A 292 ? 0.9538 0.4843 0.7736 0.2965  -0.1439 0.0419  264 ARG A NH1   
1984 N NH2   . ARG A 292 ? 1.1863 0.6867 1.0069 0.3018  -0.1474 0.0533  264 ARG A NH2   
1985 N N     . LEU A 293 ? 0.7913 0.4649 0.6597 0.2882  -0.1356 0.0644  265 LEU A N     
1986 C CA    . LEU A 293 ? 0.7557 0.4510 0.6291 0.2811  -0.1345 0.0669  265 LEU A CA    
1987 C C     . LEU A 293 ? 0.8300 0.5465 0.7133 0.2824  -0.1346 0.0778  265 LEU A C     
1988 O O     . LEU A 293 ? 0.8784 0.5999 0.7658 0.2733  -0.1357 0.0868  265 LEU A O     
1989 C CB    . LEU A 293 ? 0.7492 0.4604 0.6201 0.2852  -0.1305 0.0547  265 LEU A CB    
1990 C CG    . LEU A 293 ? 0.7374 0.4297 0.5981 0.2805  -0.1305 0.0452  265 LEU A CG    
1991 C CD1   . LEU A 293 ? 0.7225 0.4309 0.5811 0.2849  -0.1258 0.0337  265 LEU A CD1   
1992 C CD2   . LEU A 293 ? 0.7327 0.4139 0.5923 0.2665  -0.1339 0.0515  265 LEU A CD2   
1993 N N     . GLU A 294 ? 0.8069 0.5366 0.6940 0.2938  -0.1333 0.0773  266 GLU A N     
1994 C CA    . GLU A 294 ? 0.8159 0.5640 0.7110 0.2954  -0.1341 0.0878  266 GLU A CA    
1995 C C     . GLU A 294 ? 0.8637 0.5946 0.7610 0.2915  -0.1374 0.1007  266 GLU A C     
1996 O O     . GLU A 294 ? 0.9217 0.6648 0.8249 0.2888  -0.1384 0.1114  266 GLU A O     
1997 C CB    . GLU A 294 ? 0.8766 0.6432 0.7754 0.3086  -0.1325 0.0840  266 GLU A CB    
1998 C CG    . GLU A 294 ? 0.9159 0.7081 0.8157 0.3113  -0.1293 0.0745  266 GLU A CG    
1999 C CD    . GLU A 294 ? 1.0749 0.8870 0.9797 0.3242  -0.1279 0.0708  266 GLU A CD    
2000 O OE1   . GLU A 294 ? 1.1224 0.9294 1.0300 0.3311  -0.1297 0.0765  266 GLU A OE1   
2001 O OE2   . GLU A 294 ? 1.0866 0.9201 0.9932 0.3273  -0.1251 0.0624  266 GLU A OE2   
2002 N N     . LYS A 295 ? 0.8703 0.5731 0.7626 0.2913  -0.1391 0.0998  267 LYS A N     
2003 C CA    . LYS A 295 ? 0.8827 0.5669 0.7767 0.2848  -0.1422 0.1118  267 LYS A CA    
2004 C C     . LYS A 295 ? 0.8498 0.5368 0.7462 0.2712  -0.1428 0.1184  267 LYS A C     
2005 O O     . LYS A 295 ? 0.8061 0.4996 0.7090 0.2669  -0.1435 0.1310  267 LYS A O     
2006 C CB    . LYS A 295 ? 0.9264 0.5784 0.8126 0.2858  -0.1439 0.1076  267 LYS A CB    
2007 C CG    . LYS A 295 ? 1.0347 0.6656 0.9221 0.2783  -0.1471 0.1194  267 LYS A CG    
2008 C CD    . LYS A 295 ? 1.0690 0.6666 0.9469 0.2781  -0.1492 0.1137  267 LYS A CD    
2009 C CE    . LYS A 295 ? 1.1454 0.7223 1.0244 0.2691  -0.1525 0.1252  267 LYS A CE    
2010 N NZ    . LYS A 295 ? 1.1800 0.7230 1.0485 0.2680  -0.1553 0.1192  267 LYS A NZ    
2011 N N     . LEU A 296 ? 0.8438 0.5263 0.7352 0.2647  -0.1423 0.1102  268 LEU A N     
2012 C CA    . LEU A 296 ? 0.8259 0.5122 0.7198 0.2522  -0.1426 0.1155  268 LEU A CA    
2013 C C     . LEU A 296 ? 0.8234 0.5393 0.7221 0.2515  -0.1396 0.1161  268 LEU A C     
2014 O O     . LEU A 296 ? 0.7850 0.5067 0.6865 0.2420  -0.1391 0.1211  268 LEU A O     
2015 C CB    . LEU A 296 ? 0.8166 0.4857 0.7027 0.2456  -0.1438 0.1065  268 LEU A CB    
2016 C CG    . LEU A 296 ? 0.8336 0.4709 0.7132 0.2439  -0.1476 0.1057  268 LEU A CG    
2017 C CD1   . LEU A 296 ? 0.9496 0.5718 0.8191 0.2402  -0.1489 0.0936  268 LEU A CD1   
2018 C CD2   . LEU A 296 ? 0.8618 0.4887 0.7465 0.2345  -0.1502 0.1195  268 LEU A CD2   
2019 N N     . LYS A 297 ? 0.8289 0.5632 0.7283 0.2615  -0.1377 0.1111  269 LYS A N     
2020 C CA    . LYS A 297 ? 0.7996 0.5621 0.7027 0.2618  -0.1353 0.1117  269 LYS A CA    
2021 C C     . LYS A 297 ? 0.7417 0.5106 0.6421 0.2551  -0.1330 0.1047  269 LYS A C     
2022 O O     . LYS A 297 ? 0.6928 0.4758 0.5961 0.2491  -0.1317 0.1097  269 LYS A O     
2023 C CB    . LYS A 297 ? 0.8285 0.5996 0.7378 0.2578  -0.1362 0.1262  269 LYS A CB    
2024 C CG    . LYS A 297 ? 0.8842 0.6512 0.7964 0.2651  -0.1384 0.1336  269 LYS A CG    
2025 C CD    . LYS A 297 ? 0.9048 0.6811 0.8225 0.2611  -0.1393 0.1480  269 LYS A CD    
2026 C CE    . LYS A 297 ? 0.9667 0.7369 0.8869 0.2684  -0.1418 0.1559  269 LYS A CE    
2027 N NZ    . LYS A 297 ? 1.0406 0.8188 0.9654 0.2646  -0.1430 0.1702  269 LYS A NZ    
2028 N N     . GLY A 298 ? 0.7321 0.4901 0.6262 0.2565  -0.1325 0.0932  270 GLY A N     
2029 C CA    . GLY A 298 ? 0.7215 0.4858 0.6124 0.2518  -0.1302 0.0855  270 GLY A CA    
2030 C C     . GLY A 298 ? 0.7398 0.5269 0.6304 0.2599  -0.1268 0.0764  270 GLY A C     
2031 O O     . GLY A 298 ? 0.7424 0.5434 0.6327 0.2565  -0.1242 0.0731  270 GLY A O     
2032 N N     . THR A 299 ? 0.7203 0.5115 0.6114 0.2707  -0.1266 0.0723  271 THR A N     
2033 C CA    . THR A 299 ? 0.7502 0.5659 0.6433 0.2794  -0.1237 0.0651  271 THR A CA    
2034 C C     . THR A 299 ? 0.8189 0.6518 0.7180 0.2839  -0.1249 0.0734  271 THR A C     
2035 O O     . THR A 299 ? 0.8136 0.6361 0.7148 0.2834  -0.1277 0.0832  271 THR A O     
2036 C CB    . THR A 299 ? 0.6764 0.4871 0.5667 0.2890  -0.1222 0.0541  271 THR A CB    
2037 O OG1   . THR A 299 ? 0.7437 0.5427 0.6352 0.2954  -0.1245 0.0584  271 THR A OG1   
2038 C CG2   . THR A 299 ? 0.6638 0.4545 0.5464 0.2844  -0.1215 0.0463  271 THR A CG2   
2039 N N     . SER A 300 ? 0.7909 0.6502 0.6925 0.2883  -0.1230 0.0695  272 SER A N     
2040 C CA    . SER A 300 ? 0.8283 0.7061 0.7344 0.2926  -0.1245 0.0765  272 SER A CA    
2041 C C     . SER A 300 ? 0.8239 0.7289 0.7327 0.3005  -0.1226 0.0678  272 SER A C     
2042 O O     . SER A 300 ? 0.8269 0.7377 0.7344 0.3012  -0.1198 0.0573  272 SER A O     
2043 C CB    . SER A 300 ? 0.8443 0.7270 0.7505 0.2838  -0.1250 0.0866  272 SER A CB    
2044 O OG    . SER A 300 ? 0.8808 0.7888 0.7889 0.2876  -0.1252 0.0886  272 SER A OG    
2045 N N     . GLN A 301 ? 0.8687 0.7908 0.7815 0.3064  -0.1246 0.0725  273 GLN A N     
2046 C CA    . GLN A 301 ? 0.8256 0.7764 0.7424 0.3137  -0.1239 0.0658  273 GLN A CA    
2047 C C     . GLN A 301 ? 0.8476 0.8183 0.7648 0.3120  -0.1258 0.0729  273 GLN A C     
2048 O O     . GLN A 301 ? 0.8774 0.8413 0.7942 0.3110  -0.1284 0.0839  273 GLN A O     
2049 C CB    . GLN A 301 ? 0.7984 0.7515 0.7202 0.3251  -0.1246 0.0629  273 GLN A CB    
2050 C CG    . GLN A 301 ? 0.8070 0.7912 0.7350 0.3326  -0.1239 0.0553  273 GLN A CG    
2051 C CD    . GLN A 301 ? 0.9055 0.8986 0.8398 0.3430  -0.1264 0.0588  273 GLN A CD    
2052 O OE1   . GLN A 301 ? 0.9290 0.9095 0.8652 0.3499  -0.1255 0.0567  273 GLN A OE1   
2053 N NE2   . GLN A 301 ? 0.9335 0.9480 0.8705 0.3444  -0.1294 0.0642  273 GLN A NE2   
2054 N N     . GLY A 302 ? 0.8798 0.8746 0.7972 0.3116  -0.1245 0.0666  274 GLY A N     
2055 C CA    . GLY A 302 ? 0.9087 0.9227 0.8244 0.3097  -0.1262 0.0721  274 GLY A CA    
2056 C C     . GLY A 302 ? 0.8887 0.9339 0.8089 0.3165  -0.1275 0.0659  274 GLY A C     
2057 O O     . GLY A 302 ? 0.8764 0.9290 0.8032 0.3242  -0.1277 0.0595  274 GLY A O     
2058 N N     . VAL A 303 ? 0.9039 0.9683 0.8208 0.3136  -0.1286 0.0677  275 VAL A N     
2059 C CA    . VAL A 303 ? 0.8707 0.9668 0.7914 0.3184  -0.1308 0.0620  275 VAL A CA    
2060 C C     . VAL A 303 ? 0.9156 1.0269 0.8318 0.3125  -0.1289 0.0555  275 VAL A C     
2061 O O     . VAL A 303 ? 0.9932 1.0924 0.9017 0.3052  -0.1266 0.0591  275 VAL A O     
2062 C CB    . VAL A 303 ? 0.8076 0.9142 0.7276 0.3219  -0.1353 0.0712  275 VAL A CB    
2063 C CG1   . VAL A 303 ? 0.7441 0.8420 0.6707 0.3301  -0.1375 0.0754  275 VAL A CG1   
2064 C CG2   . VAL A 303 ? 0.8063 0.9002 0.7172 0.3150  -0.1352 0.0820  275 VAL A CG2   
2065 N N     . GLY A 304 ? 0.9302 1.0690 0.8519 0.3156  -0.1300 0.0459  276 GLY A N     
2066 C CA    . GLY A 304 ? 0.9961 1.1511 0.9142 0.3104  -0.1286 0.0384  276 GLY A CA    
2067 C C     . GLY A 304 ? 1.0439 1.2254 0.9587 0.3097  -0.1326 0.0389  276 GLY A C     
2068 O O     . GLY A 304 ? 0.9818 1.1738 0.8994 0.3143  -0.1368 0.0436  276 GLY A O     
2069 N N     . ARG A 305 ? 1.1102 1.2996 1.0189 0.2998  -0.1294 0.0333  277 ARG A N     
2070 C CA    . ARG A 305 ? 1.0690 1.2830 0.9729 0.2972  -0.1328 0.0319  277 ARG A CA    
2071 C C     . ARG A 305 ? 0.9920 1.2356 0.9073 0.3013  -0.1369 0.0237  277 ARG A C     
2072 O O     . ARG A 305 ? 0.9204 1.1853 0.8342 0.3056  -0.1436 0.0265  277 ARG A O     
2073 C CB    . ARG A 305 ? 0.9966 1.2092 0.8922 0.2829  -0.1261 0.0252  277 ARG A CB    
2074 N N     . ASN A 306 ? 1.0364 1.2825 0.9632 0.3002  -0.1330 0.0139  278 ASN A N     
2075 C CA    . ASN A 306 ? 0.9454 1.2195 0.8857 0.3051  -0.1364 0.0069  278 ASN A CA    
2076 C C     . ASN A 306 ? 0.9228 1.1979 0.8711 0.3216  -0.1423 0.0148  278 ASN A C     
2077 O O     . ASN A 306 ? 0.8704 1.1686 0.8310 0.3266  -0.1450 0.0105  278 ASN A O     
2078 C CB    . ASN A 306 ? 0.8662 1.1428 0.8157 0.2974  -0.1290 -0.0063 278 ASN A CB    
2079 N N     . GLY A 307 ? 0.9403 1.1855 0.8821 0.3237  -0.1409 0.0253  279 GLY A N     
2080 C CA    . GLY A 307 ? 0.9022 1.1384 0.8499 0.3317  -0.1424 0.0321  279 GLY A CA    
2081 C C     . GLY A 307 ? 0.9110 1.1289 0.8655 0.3362  -0.1380 0.0291  279 GLY A C     
2082 O O     . GLY A 307 ? 0.8463 1.0517 0.8040 0.3428  -0.1387 0.0351  279 GLY A O     
2083 N N     . GLU A 308 ? 0.9062 1.1212 0.8622 0.3330  -0.1335 0.0198  280 GLU A N     
2084 C CA    . GLU A 308 ? 0.8550 1.0533 0.8163 0.3373  -0.1290 0.0157  280 GLU A CA    
2085 C C     . GLU A 308 ? 0.9054 1.0654 0.8572 0.3352  -0.1270 0.0237  280 GLU A C     
2086 O O     . GLU A 308 ? 0.9154 1.0626 0.8573 0.3290  -0.1278 0.0309  280 GLU A O     
2087 C CB    . GLU A 308 ? 0.9585 1.1655 0.9242 0.3327  -0.1239 0.0031  280 GLU A CB    
2088 N N     . ALA A 309 ? 0.8902 1.0325 0.8452 0.3403  -0.1243 0.0222  281 ALA A N     
2089 C CA    . ALA A 309 ? 0.8075 0.9139 0.7547 0.3382  -0.1231 0.0289  281 ALA A CA    
2090 C C     . ALA A 309 ? 0.8182 0.9073 0.7588 0.3307  -0.1191 0.0244  281 ALA A C     
2091 O O     . ALA A 309 ? 0.7226 0.8194 0.6666 0.3310  -0.1155 0.0140  281 ALA A O     
2092 C CB    . ALA A 309 ? 0.6645 0.7580 0.6166 0.3468  -0.1221 0.0287  281 ALA A CB    
2093 N N     . GLU A 310 ? 0.8613 0.9275 0.7929 0.3238  -0.1195 0.0326  282 GLU A N     
2094 C CA    . GLU A 310 ? 0.8007 0.8487 0.7256 0.3159  -0.1163 0.0304  282 GLU A CA    
2095 C C     . GLU A 310 ? 0.7668 0.7813 0.6878 0.3145  -0.1159 0.0349  282 GLU A C     
2096 O O     . GLU A 310 ? 0.7927 0.7957 0.7133 0.3157  -0.1187 0.0441  282 GLU A O     
2097 C CB    . GLU A 310 ? 0.8228 0.8741 0.7411 0.3078  -0.1169 0.0362  282 GLU A CB    
2098 C CG    . GLU A 310 ? 0.8663 0.9488 0.7863 0.3078  -0.1173 0.0303  282 GLU A CG    
2099 C CD    . GLU A 310 ? 0.8937 0.9776 0.8056 0.2993  -0.1170 0.0362  282 GLU A CD    
2100 O OE1   . GLU A 310 ? 0.9311 0.9975 0.8379 0.2969  -0.1182 0.0472  282 GLU A OE1   
2101 O OE2   . GLU A 310 ? 0.8589 0.9602 0.7703 0.2910  -0.1135 0.0291  282 GLU A OE2   
2102 N N     . TYR A 311 ? 0.7226 0.7216 0.6406 0.3117  -0.1126 0.0284  283 TYR A N     
2103 C CA    . TYR A 311 ? 0.6825 0.6499 0.5960 0.3097  -0.1125 0.0309  283 TYR A CA    
2104 C C     . TYR A 311 ? 0.6336 0.5842 0.5402 0.2994  -0.1111 0.0320  283 TYR A C     
2105 O O     . TYR A 311 ? 0.6541 0.6146 0.5596 0.2965  -0.1083 0.0257  283 TYR A O     
2106 C CB    . TYR A 311 ? 0.6705 0.6328 0.5860 0.3171  -0.1100 0.0215  283 TYR A CB    
2107 C CG    . TYR A 311 ? 0.6865 0.6645 0.6098 0.3278  -0.1110 0.0210  283 TYR A CG    
2108 C CD1   . TYR A 311 ? 0.7441 0.7546 0.6756 0.3328  -0.1103 0.0156  283 TYR A CD1   
2109 C CD2   . TYR A 311 ? 0.7060 0.6668 0.6291 0.3328  -0.1129 0.0262  283 TYR A CD2   
2110 C CE1   . TYR A 311 ? 0.7760 0.8023 0.7157 0.3423  -0.1115 0.0158  283 TYR A CE1   
2111 C CE2   . TYR A 311 ? 0.7701 0.7452 0.7007 0.3431  -0.1138 0.0264  283 TYR A CE2   
2112 C CZ    . TYR A 311 ? 0.7684 0.7766 0.7074 0.3477  -0.1131 0.0214  283 TYR A CZ    
2113 O OH    . TYR A 311 ? 0.6884 0.7121 0.6358 0.3578  -0.1141 0.0220  283 TYR A OH    
2114 N N     . TYR A 312 ? 0.6038 0.5295 0.5066 0.2938  -0.1131 0.0403  284 TYR A N     
2115 C CA    . TYR A 312 ? 0.6210 0.5329 0.5189 0.2832  -0.1125 0.0440  284 TYR A CA    
2116 C C     . TYR A 312 ? 0.6711 0.5528 0.5650 0.2793  -0.1137 0.0450  284 TYR A C     
2117 O O     . TYR A 312 ? 0.6601 0.5296 0.5544 0.2843  -0.1154 0.0453  284 TYR A O     
2118 C CB    . TYR A 312 ? 0.6691 0.5859 0.5675 0.2776  -0.1142 0.0558  284 TYR A CB    
2119 C CG    . TYR A 312 ? 0.6732 0.6180 0.5727 0.2794  -0.1131 0.0547  284 TYR A CG    
2120 C CD1   . TYR A 312 ? 0.7232 0.6866 0.6265 0.2866  -0.1151 0.0560  284 TYR A CD1   
2121 C CD2   . TYR A 312 ? 0.7095 0.6620 0.6057 0.2740  -0.1102 0.0522  284 TYR A CD2   
2122 C CE1   . TYR A 312 ? 0.7709 0.7602 0.6743 0.2879  -0.1148 0.0546  284 TYR A CE1   
2123 C CE2   . TYR A 312 ? 0.7403 0.7178 0.6363 0.2757  -0.1094 0.0506  284 TYR A CE2   
2124 C CZ    . TYR A 312 ? 0.7826 0.7787 0.6820 0.2823  -0.1120 0.0516  284 TYR A CZ    
2125 O OH    . TYR A 312 ? 0.8483 0.8697 0.7468 0.2835  -0.1120 0.0496  284 TYR A OH    
2126 N N     . ILE A 313 ? 0.6757 0.5457 0.5655 0.2702  -0.1128 0.0455  285 ILE A N     
2127 C CA    . ILE A 313 ? 0.6039 0.4462 0.4899 0.2639  -0.1148 0.0481  285 ILE A CA    
2128 C C     . ILE A 313 ? 0.6165 0.4550 0.5030 0.2528  -0.1154 0.0575  285 ILE A C     
2129 O O     . ILE A 313 ? 0.6124 0.4613 0.4979 0.2490  -0.1126 0.0557  285 ILE A O     
2130 C CB    . ILE A 313 ? 0.5987 0.4292 0.4787 0.2644  -0.1129 0.0369  285 ILE A CB    
2131 C CG1   . ILE A 313 ? 0.6078 0.4408 0.4879 0.2756  -0.1117 0.0281  285 ILE A CG1   
2132 C CG2   . ILE A 313 ? 0.6088 0.4117 0.4839 0.2560  -0.1158 0.0401  285 ILE A CG2   
2133 C CD1   . ILE A 313 ? 0.6087 0.4329 0.4826 0.2771  -0.1086 0.0165  285 ILE A CD1   
2134 N N     . HIS A 314 ? 0.6478 0.4719 0.5364 0.2479  -0.1187 0.0677  286 HIS A N     
2135 C CA    . HIS A 314 ? 0.6902 0.5129 0.5815 0.2380  -0.1191 0.0783  286 HIS A CA    
2136 C C     . HIS A 314 ? 0.6833 0.4837 0.5726 0.2292  -0.1211 0.0797  286 HIS A C     
2137 O O     . HIS A 314 ? 0.6879 0.4694 0.5744 0.2303  -0.1240 0.0770  286 HIS A O     
2138 C CB    . HIS A 314 ? 0.7357 0.5612 0.6323 0.2381  -0.1212 0.0905  286 HIS A CB    
2139 C CG    . HIS A 314 ? 0.7330 0.5787 0.6310 0.2472  -0.1204 0.0894  286 HIS A CG    
2140 N ND1   . HIS A 314 ? 0.7296 0.5972 0.6277 0.2475  -0.1178 0.0902  286 HIS A ND1   
2141 C CD2   . HIS A 314 ? 0.7427 0.5903 0.6417 0.2565  -0.1220 0.0874  286 HIS A CD2   
2142 C CE1   . HIS A 314 ? 0.7482 0.6311 0.6474 0.2560  -0.1184 0.0888  286 HIS A CE1   
2143 N NE2   . HIS A 314 ? 0.7648 0.6364 0.6652 0.2617  -0.1209 0.0873  286 HIS A NE2   
2144 N N     . LEU A 315 ? 0.6042 0.4072 0.4949 0.2205  -0.1197 0.0840  287 LEU A N     
2145 C CA    . LEU A 315 ? 0.6177 0.4030 0.5073 0.2114  -0.1217 0.0854  287 LEU A CA    
2146 C C     . LEU A 315 ? 0.6072 0.4009 0.5009 0.2028  -0.1194 0.0927  287 LEU A C     
2147 O O     . LEU A 315 ? 0.5898 0.4019 0.4839 0.2048  -0.1153 0.0924  287 LEU A O     
2148 C CB    . LEU A 315 ? 0.5983 0.3739 0.4798 0.2139  -0.1215 0.0723  287 LEU A CB    
2149 C CG    . LEU A 315 ? 0.5795 0.3712 0.4576 0.2180  -0.1167 0.0632  287 LEU A CG    
2150 C CD1   . LEU A 315 ? 0.5694 0.3592 0.4461 0.2097  -0.1151 0.0637  287 LEU A CD1   
2151 C CD2   . LEU A 315 ? 0.5852 0.3735 0.4571 0.2268  -0.1158 0.0504  287 LEU A CD2   
2152 N N     . SER A 316 ? 0.6395 0.4203 0.5363 0.1936  -0.1220 0.0995  288 SER A N     
2153 C CA    . SER A 316 ? 0.6689 0.4575 0.5711 0.1855  -0.1197 0.1075  288 SER A CA    
2154 C C     . SER A 316 ? 0.6591 0.4429 0.5567 0.1814  -0.1188 0.1004  288 SER A C     
2155 O O     . SER A 316 ? 0.6603 0.4278 0.5525 0.1804  -0.1223 0.0937  288 SER A O     
2156 C CB    . SER A 316 ? 0.6782 0.4588 0.5886 0.1778  -0.1225 0.1210  288 SER A CB    
2157 O OG    . SER A 316 ? 0.7072 0.4921 0.6216 0.1817  -0.1230 0.1284  288 SER A OG    
2158 N N     . VAL A 317 ? 0.6337 0.4312 0.5327 0.1793  -0.1142 0.1018  289 VAL A N     
2159 C CA    . VAL A 317 ? 0.5432 0.3380 0.4376 0.1763  -0.1125 0.0954  289 VAL A CA    
2160 C C     . VAL A 317 ? 0.5550 0.3539 0.4568 0.1676  -0.1110 0.1058  289 VAL A C     
2161 O O     . VAL A 317 ? 0.6695 0.4823 0.5766 0.1674  -0.1072 0.1137  289 VAL A O     
2162 C CB    . VAL A 317 ? 0.5505 0.3582 0.4380 0.1838  -0.1070 0.0853  289 VAL A CB    
2163 C CG1   . VAL A 317 ? 0.6681 0.4728 0.5513 0.1803  -0.1045 0.0804  289 VAL A CG1   
2164 C CG2   . VAL A 317 ? 0.5400 0.3451 0.4216 0.1928  -0.1083 0.0750  289 VAL A CG2   
2165 N N     . ILE A 318 ? 0.5513 0.3384 0.4533 0.1606  -0.1139 0.1058  290 ILE A N     
2166 C CA    . ILE A 318 ? 0.5802 0.3725 0.4889 0.1532  -0.1120 0.1140  290 ILE A CA    
2167 C C     . ILE A 318 ? 0.6062 0.4034 0.5080 0.1552  -0.1072 0.1059  290 ILE A C     
2168 O O     . ILE A 318 ? 0.6696 0.4569 0.5626 0.1569  -0.1087 0.0956  290 ILE A O     
2169 C CB    . ILE A 318 ? 0.5860 0.3641 0.4988 0.1444  -0.1181 0.1190  290 ILE A CB    
2170 C CG1   . ILE A 318 ? 0.5762 0.3462 0.4933 0.1433  -0.1227 0.1253  290 ILE A CG1   
2171 C CG2   . ILE A 318 ? 0.6462 0.4327 0.5682 0.1373  -0.1158 0.1289  290 ILE A CG2   
2172 C CD1   . ILE A 318 ? 0.6168 0.3684 0.5333 0.1360  -0.1300 0.1260  290 ILE A CD1   
2173 N N     . THR A 319 ? 0.5576 0.3692 0.4625 0.1555  -0.1009 0.1107  291 THR A N     
2174 C CA    . THR A 319 ? 0.6098 0.4277 0.5099 0.1559  -0.0944 0.1042  291 THR A CA    
2175 C C     . THR A 319 ? 0.6783 0.4960 0.5851 0.1489  -0.0940 0.1134  291 THR A C     
2176 O O     . THR A 319 ? 0.7578 0.5821 0.6744 0.1457  -0.0935 0.1254  291 THR A O     
2177 C CB    . THR A 319 ? 0.6070 0.4438 0.5060 0.1604  -0.0855 0.1008  291 THR A CB    
2178 O OG1   . THR A 319 ? 0.7052 0.5439 0.5998 0.1672  -0.0870 0.0944  291 THR A OG1   
2179 C CG2   . THR A 319 ? 0.5946 0.4383 0.4896 0.1587  -0.0775 0.0914  291 THR A CG2   
2180 N N     . ALA A 320 ? 0.6631 0.4757 0.5666 0.1452  -0.0932 0.1075  292 ALA A N     
2181 C CA    . ALA A 320 ? 0.6153 0.4266 0.5254 0.1387  -0.0943 0.1160  292 ALA A CA    
2182 C C     . ALA A 320 ? 0.6202 0.4379 0.5267 0.1378  -0.0861 0.1095  292 ALA A C     
2183 O O     . ALA A 320 ? 0.6455 0.4634 0.5433 0.1405  -0.0820 0.0970  292 ALA A O     
2184 C CB    . ALA A 320 ? 0.6003 0.3960 0.5118 0.1325  -0.1041 0.1178  292 ALA A CB    
2185 N N     . LEU A 321 ? 0.6127 0.4357 0.5268 0.1339  -0.0837 0.1186  293 LEU A N     
2186 C CA    . LEU A 321 ? 0.5769 0.4044 0.4887 0.1326  -0.0763 0.1148  293 LEU A CA    
2187 C C     . LEU A 321 ? 0.5876 0.4118 0.5076 0.1269  -0.0809 0.1253  293 LEU A C     
2188 O O     . LEU A 321 ? 0.6672 0.4990 0.5983 0.1255  -0.0806 0.1380  293 LEU A O     
2189 C CB    . LEU A 321 ? 0.5921 0.4351 0.5050 0.1360  -0.0648 0.1146  293 LEU A CB    
2190 C CG    . LEU A 321 ? 0.5619 0.4093 0.4742 0.1348  -0.0564 0.1135  293 LEU A CG    
2191 C CD1   . LEU A 321 ? 0.6273 0.4671 0.5291 0.1343  -0.0551 0.1005  293 LEU A CD1   
2192 C CD2   . LEU A 321 ? 0.6359 0.4969 0.5487 0.1382  -0.0454 0.1141  293 LEU A CD2   
2193 N N     . ALA A 322 ? 0.4776 0.2913 0.3921 0.1238  -0.0851 0.1206  294 ALA A N     
2194 C CA    . ALA A 322 ? 0.5183 0.3280 0.4396 0.1181  -0.0914 0.1298  294 ALA A CA    
2195 C C     . ALA A 322 ? 0.8547 0.6671 0.7727 0.1177  -0.0849 0.1270  294 ALA A C     
2196 O O     . ALA A 322 ? 0.7923 0.6085 0.7027 0.1213  -0.0755 0.1176  294 ALA A O     
2197 C CB    . ALA A 322 ? 0.6095 0.4029 0.5267 0.1138  -0.1038 0.1278  294 ALA A CB    
2198 N N     . ARG A 323 ? 0.7480 0.5586 0.6723 0.1130  -0.0902 0.1355  295 ARG A N     
2199 C CA    . ARG A 323 ? 0.7452 0.5573 0.6668 0.1126  -0.0852 0.1345  295 ARG A CA    
2200 C C     . ARG A 323 ? 0.7550 0.5599 0.6801 0.1066  -0.0962 0.1413  295 ARG A C     
2201 O O     . ARG A 323 ? 0.7417 0.5539 0.6806 0.1018  -0.1005 0.1513  295 ARG A O     
2202 C CB    . ARG A 323 ? 0.7467 0.5740 0.6772 0.1155  -0.0740 0.1416  295 ARG A CB    
2203 C CG    . ARG A 323 ? 0.7981 0.6263 0.7259 0.1160  -0.0680 0.1410  295 ARG A CG    
2204 C CD    . ARG A 323 ? 0.7974 0.6392 0.7342 0.1194  -0.0569 0.1488  295 ARG A CD    
2205 N NE    . ARG A 323 ? 0.8895 0.7366 0.8208 0.1241  -0.0463 0.1413  295 ARG A NE    
2206 C CZ    . ARG A 323 ? 0.9631 0.8217 0.9009 0.1275  -0.0372 0.1471  295 ARG A CZ    
2207 N NH1   . ARG A 323 ? 0.9393 0.8065 0.8906 0.1269  -0.0366 0.1604  295 ARG A NH1   
2208 N NH2   . ARG A 323 ? 0.9106 0.7728 0.8412 0.1312  -0.0287 0.1387  295 ARG A NH2   
2209 N N     . LYS A 324 ? 0.7638 0.5595 0.6776 0.1057  -0.0975 0.1341  296 LYS A N     
2210 C CA    . LYS A 324 ? 0.7162 0.5063 0.6315 0.0996  -0.1074 0.1388  296 LYS A CA    
2211 C C     . LYS A 324 ? 0.7134 0.5173 0.6417 0.0985  -0.1031 0.1503  296 LYS A C     
2212 O O     . LYS A 324 ? 0.6612 0.4707 0.5893 0.1038  -0.0933 0.1516  296 LYS A O     
2213 C CB    . LYS A 324 ? 0.6960 0.4704 0.5924 0.0999  -0.1101 0.1273  296 LYS A CB    
2214 C CG    . LYS A 324 ? 0.7154 0.4834 0.6105 0.0937  -0.1204 0.1311  296 LYS A CG    
2215 C CD    . LYS A 324 ? 0.6804 0.4324 0.5547 0.0948  -0.1220 0.1194  296 LYS A CD    
2216 C CE    . LYS A 324 ? 0.6961 0.4411 0.5674 0.0889  -0.1330 0.1237  296 LYS A CE    
2217 N NZ    . LYS A 324 ? 0.6929 0.4218 0.5425 0.0897  -0.1346 0.1121  296 LYS A NZ    
2218 N N     . PHE A 325 ? 0.7836 0.5921 0.7220 0.0921  -0.1105 0.1579  297 PHE A N     
2219 C CA    . PHE A 325 ? 0.7806 0.6021 0.7305 0.0913  -0.1073 0.1680  297 PHE A CA    
2220 C C     . PHE A 325 ? 0.7759 0.5911 0.7171 0.0908  -0.1095 0.1661  297 PHE A C     
2221 O O     . PHE A 325 ? 0.7838 0.5870 0.7157 0.0863  -0.1195 0.1612  297 PHE A O     
2222 C CB    . PHE A 325 ? 0.7215 0.5511 0.6861 0.0843  -0.1148 0.1766  297 PHE A CB    
2223 C CG    . PHE A 325 ? 0.7041 0.5462 0.6811 0.0857  -0.1088 0.1827  297 PHE A CG    
2224 C CD1   . PHE A 325 ? 0.7182 0.5744 0.7048 0.0886  -0.0999 0.1892  297 PHE A CD1   
2225 C CD2   . PHE A 325 ? 0.7311 0.5700 0.7095 0.0839  -0.1121 0.1815  297 PHE A CD2   
2226 C CE1   . PHE A 325 ? 0.7595 0.6268 0.7569 0.0893  -0.0946 0.1944  297 PHE A CE1   
2227 C CE2   . PHE A 325 ? 0.7858 0.6358 0.7746 0.0850  -0.1066 0.1873  297 PHE A CE2   
2228 C CZ    . PHE A 325 ? 0.8054 0.6697 0.8035 0.0875  -0.0980 0.1936  297 PHE A CZ    
2229 N N     . GLU B 42  ? 0.8477 0.7834 0.8635 0.3099  0.2930  0.2925  14  GLU B N     
2230 C CA    . GLU B 42  ? 0.9179 0.8827 0.9579 0.3073  0.2862  0.3035  14  GLU B CA    
2231 C C     . GLU B 42  ? 0.9924 0.9642 1.0328 0.3172  0.3020  0.3132  14  GLU B C     
2232 O O     . GLU B 42  ? 1.0238 0.9787 1.0476 0.3264  0.3174  0.3127  14  GLU B O     
2233 C CB    . GLU B 42  ? 0.9905 0.9778 1.0580 0.3031  0.2740  0.3141  14  GLU B CB    
2234 C CG    . GLU B 42  ? 0.9689 0.9825 1.0600 0.2949  0.2601  0.3216  14  GLU B CG    
2235 C CD    . GLU B 42  ? 0.9669 1.0060 1.0867 0.2947  0.2547  0.3368  14  GLU B CD    
2236 O OE1   . GLU B 42  ? 0.9912 1.0281 1.1149 0.2935  0.2486  0.3373  14  GLU B OE1   
2237 O OE2   . GLU B 42  ? 0.8866 0.9479 1.0247 0.2959  0.2569  0.3487  14  GLU B OE2   
2238 N N     . ALA B 43  ? 1.0486 1.0444 1.1074 0.3149  0.2978  0.3222  15  ALA B N     
2239 C CA    . ALA B 43  ? 1.0517 1.0578 1.1139 0.3236  0.3116  0.3335  15  ALA B CA    
2240 C C     . ALA B 43  ? 1.0553 1.0350 1.0856 0.3302  0.3253  0.3248  15  ALA B C     
2241 O O     . ALA B 43  ? 1.1008 1.0725 1.1182 0.3261  0.3213  0.3156  15  ALA B O     
2242 C CB    . ALA B 43  ? 1.0063 1.0241 1.0834 0.3315  0.3203  0.3475  15  ALA B CB    
2243 N N     . TYR B 44  ? 1.0288 0.9936 1.0455 0.3403  0.3403  0.3275  16  TYR B N     
2244 C CA    . TYR B 44  ? 1.0448 0.9800 1.0291 0.3460  0.3512  0.3183  16  TYR B CA    
2245 C C     . TYR B 44  ? 0.9805 0.8885 0.9427 0.3401  0.3462  0.3000  16  TYR B C     
2246 O O     . TYR B 44  ? 1.0280 0.9225 0.9848 0.3409  0.3481  0.2962  16  TYR B O     
2247 C CB    . TYR B 44  ? 1.0378 0.9625 1.0143 0.3577  0.3664  0.3254  16  TYR B CB    
2248 C CG    . TYR B 44  ? 1.0037 0.9528 0.9998 0.3647  0.3731  0.3439  16  TYR B CG    
2249 C CD1   . TYR B 44  ? 0.9430 0.9230 0.9640 0.3597  0.3655  0.3539  16  TYR B CD1   
2250 C CD2   . TYR B 44  ? 1.0452 0.9861 1.0353 0.3762  0.3868  0.3513  16  TYR B CD2   
2251 C CE1   . TYR B 44  ? 1.0251 1.0275 1.0645 0.3656  0.3718  0.3714  16  TYR B CE1   
2252 C CE2   . TYR B 44  ? 1.0866 1.0494 1.0945 0.3829  0.3931  0.3686  16  TYR B CE2   
2253 C CZ    . TYR B 44  ? 1.1391 1.1328 1.1717 0.3774  0.3857  0.3790  16  TYR B CZ    
2254 O OH    . TYR B 44  ? 1.1809 1.1965 1.2318 0.3835  0.3919  0.3969  16  TYR B OH    
2255 N N     . ARG B 45  ? 0.8513 0.7518 0.8013 0.3343  0.3399  0.2893  17  ARG B N     
2256 C CA    . ARG B 45  ? 0.8098 0.6888 0.7424 0.3268  0.3328  0.2724  17  ARG B CA    
2257 C C     . ARG B 45  ? 0.8631 0.7552 0.8154 0.3197  0.3206  0.2737  17  ARG B C     
2258 O O     . ARG B 45  ? 0.9287 0.8488 0.9085 0.3178  0.3134  0.2853  17  ARG B O     
2259 C CB    . ARG B 45  ? 0.8216 0.6670 0.7258 0.3307  0.3429  0.2615  17  ARG B CB    
2260 C CG    . ARG B 45  ? 0.8428 0.6739 0.7269 0.3351  0.3502  0.2556  17  ARG B CG    
2261 C CD    . ARG B 45  ? 0.8362 0.6800 0.7229 0.3308  0.3423  0.2533  17  ARG B CD    
2262 N NE    . ARG B 45  ? 0.8189 0.6452 0.6823 0.3317  0.3462  0.2408  17  ARG B NE    
2263 C CZ    . ARG B 45  ? 0.7954 0.6198 0.6493 0.3252  0.3388  0.2290  17  ARG B CZ    
2264 N NH1   . ARG B 45  ? 0.7274 0.5645 0.5924 0.3183  0.3278  0.2290  17  ARG B NH1   
2265 N NH2   . ARG B 45  ? 0.7814 0.5911 0.6138 0.3249  0.3424  0.2161  17  ARG B NH2   
2266 N N     . GLY B 46  ? 0.7727 0.6446 0.7114 0.3148  0.3165  0.2615  18  GLY B N     
2267 C CA    . GLY B 46  ? 0.7249 0.6060 0.6793 0.3078  0.3034  0.2617  18  GLY B CA    
2268 C C     . GLY B 46  ? 0.7467 0.6144 0.6965 0.3109  0.3087  0.2614  18  GLY B C     
2269 O O     . GLY B 46  ? 0.8568 0.7318 0.8154 0.3187  0.3173  0.2721  18  GLY B O     
2270 N N     . ILE B 47  ? 0.7345 0.5822 0.6700 0.3053  0.3041  0.2495  19  ILE B N     
2271 C CA    . ILE B 47  ? 0.7893 0.6224 0.7189 0.3075  0.3085  0.2483  19  ILE B CA    
2272 C C     . ILE B 47  ? 0.8143 0.6150 0.7139 0.3107  0.3220  0.2377  19  ILE B C     
2273 O O     . ILE B 47  ? 0.8551 0.6358 0.7360 0.3043  0.3195  0.2240  19  ILE B O     
2274 C CB    . ILE B 47  ? 0.7357 0.5677 0.6695 0.2987  0.2943  0.2430  19  ILE B CB    
2275 C CG1   . ILE B 47  ? 0.7413 0.6037 0.7036 0.2938  0.2786  0.2527  19  ILE B CG1   
2276 C CG2   . ILE B 47  ? 0.7087 0.5252 0.6357 0.3016  0.2995  0.2423  19  ILE B CG2   
2277 C CD1   . ILE B 47  ? 0.7805 0.6656 0.7653 0.3007  0.2820  0.2686  19  ILE B CD1   
2278 N N     . ASP B 48  ? 0.8572 0.6522 0.7522 0.3200  0.3356  0.2440  20  ASP B N     
2279 C CA    . ASP B 48  ? 0.8889 0.6516 0.7563 0.3223  0.3470  0.2340  20  ASP B CA    
2280 C C     . ASP B 48  ? 0.9319 0.6767 0.7915 0.3200  0.3474  0.2288  20  ASP B C     
2281 O O     . ASP B 48  ? 0.9380 0.6957 0.8133 0.3174  0.3389  0.2332  20  ASP B O     
2282 C CB    . ASP B 48  ? 0.9535 0.7146 0.8182 0.3331  0.3605  0.2424  20  ASP B CB    
2283 C CG    . ASP B 48  ? 1.0095 0.7948 0.8988 0.3407  0.3630  0.2596  20  ASP B CG    
2284 O OD1   . ASP B 48  ? 0.9953 0.7930 0.9006 0.3376  0.3548  0.2633  20  ASP B OD1   
2285 O OD2   . ASP B 48  ? 1.0300 0.8218 0.9229 0.3495  0.3724  0.2692  20  ASP B OD2   
2286 N N     . LYS B 49  ? 0.9378 0.6522 0.7730 0.3204  0.3566  0.2191  21  LYS B N     
2287 C CA    . LYS B 49  ? 0.8449 0.5379 0.6687 0.3171  0.3580  0.2123  21  LYS B CA    
2288 C C     . LYS B 49  ? 0.8103 0.5049 0.6358 0.3064  0.3449  0.2044  21  LYS B C     
2289 O O     . LYS B 49  ? 0.7977 0.5044 0.6378 0.3054  0.3379  0.2100  21  LYS B O     
2290 C CB    . LYS B 49  ? 0.8403 0.5410 0.6771 0.3253  0.3629  0.2248  21  LYS B CB    
2291 N N     . PRO B 50  ? 0.8058 0.4892 0.6174 0.2982  0.3407  0.1913  22  PRO B N     
2292 C CA    . PRO B 50  ? 0.7871 0.4704 0.5991 0.2882  0.3289  0.1835  22  PRO B CA    
2293 C C     . PRO B 50  ? 0.7993 0.4620 0.6005 0.2842  0.3304  0.1777  22  PRO B C     
2294 O O     . PRO B 50  ? 0.8082 0.4747 0.6144 0.2779  0.3206  0.1753  22  PRO B O     
2295 C CB    . PRO B 50  ? 0.7849 0.4591 0.5825 0.2815  0.3263  0.1703  22  PRO B CB    
2296 C CG    . PRO B 50  ? 0.8967 0.5543 0.6787 0.2858  0.3380  0.1665  22  PRO B CG    
2297 C CD    . PRO B 50  ? 0.9181 0.5890 0.7133 0.2975  0.3456  0.1824  22  PRO B CD    
2298 N N     . HIS B 51  ? 0.8553 0.4960 0.6417 0.2876  0.3422  0.1753  23  HIS B N     
2299 C CA    . HIS B 51  ? 0.8692 0.4896 0.6451 0.2841  0.3447  0.1705  23  HIS B CA    
2300 C C     . HIS B 51  ? 0.8583 0.4949 0.6524 0.2877  0.3396  0.1817  23  HIS B C     
2301 O O     . HIS B 51  ? 0.8547 0.4844 0.6463 0.2818  0.3341  0.1778  23  HIS B O     
2302 C CB    . HIS B 51  ? 0.9298 0.5256 0.6888 0.2885  0.3586  0.1679  23  HIS B CB    
2303 C CG    . HIS B 51  ? 1.0459 0.6174 0.7828 0.2801  0.3612  0.1516  23  HIS B CG    
2304 N ND1   . HIS B 51  ? 1.1304 0.6742 0.8496 0.2750  0.3671  0.1423  23  HIS B ND1   
2305 C CD2   . HIS B 51  ? 1.0513 0.6234 0.7820 0.2755  0.3581  0.1425  23  HIS B CD2   
2306 C CE1   . HIS B 51  ? 1.1455 0.6748 0.8495 0.2669  0.3670  0.1279  23  HIS B CE1   
2307 N NE2   . HIS B 51  ? 1.1125 0.6589 0.8230 0.2672  0.3614  0.1274  23  HIS B NE2   
2308 N N     . LEU B 52  ? 0.8255 0.4843 0.6385 0.2970  0.3405  0.1957  24  LEU B N     
2309 C CA    . LEU B 52  ? 0.8162 0.4925 0.6485 0.3003  0.3343  0.2065  24  LEU B CA    
2310 C C     . LEU B 52  ? 0.7855 0.4838 0.6346 0.2936  0.3173  0.2079  24  LEU B C     
2311 O O     . LEU B 52  ? 0.7772 0.4885 0.6411 0.2939  0.3090  0.2152  24  LEU B O     
2312 C CB    . LEU B 52  ? 0.8224 0.5160 0.6704 0.3119  0.3408  0.2209  24  LEU B CB    
2313 C CG    . LEU B 52  ? 0.8551 0.5281 0.6888 0.3202  0.3573  0.2221  24  LEU B CG    
2314 C CD1   . LEU B 52  ? 0.8593 0.5525 0.7112 0.3318  0.3627  0.2376  24  LEU B CD1   
2315 C CD2   . LEU B 52  ? 0.8729 0.5229 0.6937 0.3186  0.3607  0.2175  24  LEU B CD2   
2316 N N     . TYR B 53  ? 0.7697 0.4721 0.6167 0.2873  0.3111  0.2012  25  TYR B N     
2317 C CA    . TYR B 53  ? 0.7419 0.4641 0.6041 0.2806  0.2946  0.2025  25  TYR B CA    
2318 C C     . TYR B 53  ? 0.7375 0.4441 0.5870 0.2707  0.2874  0.1911  25  TYR B C     
2319 O O     . TYR B 53  ? 0.7229 0.4413 0.5836 0.2659  0.2740  0.1936  25  TYR B O     
2320 C CB    . TYR B 53  ? 0.7259 0.4644 0.5956 0.2798  0.2908  0.2032  25  TYR B CB    
2321 C CG    . TYR B 53  ? 0.6984 0.4617 0.5885 0.2742  0.2735  0.2082  25  TYR B CG    
2322 C CD1   . TYR B 53  ? 0.6881 0.4780 0.6028 0.2778  0.2674  0.2218  25  TYR B CD1   
2323 C CD2   . TYR B 53  ? 0.6842 0.4436 0.5687 0.2649  0.2627  0.1991  25  TYR B CD2   
2324 C CE1   . TYR B 53  ? 0.6651 0.4760 0.5974 0.2712  0.2505  0.2259  25  TYR B CE1   
2325 C CE2   . TYR B 53  ? 0.6875 0.4676 0.5891 0.2591  0.2463  0.2035  25  TYR B CE2   
2326 C CZ    . TYR B 53  ? 0.6765 0.4817 0.6016 0.2618  0.2399  0.2166  25  TYR B CZ    
2327 O OH    . TYR B 53  ? 0.6927 0.5167 0.6335 0.2547  0.2227  0.2205  25  TYR B OH    
2328 N N     . THR B 54  ? 0.7527 0.4331 0.5791 0.2670  0.2957  0.1788  26  THR B N     
2329 C CA    . THR B 54  ? 0.7511 0.4157 0.5651 0.2576  0.2905  0.1682  26  THR B CA    
2330 C C     . THR B 54  ? 0.7595 0.4173 0.5737 0.2577  0.2897  0.1716  26  THR B C     
2331 O O     . THR B 54  ? 0.7587 0.4044 0.5636 0.2501  0.2853  0.1642  26  THR B O     
2332 C CB    . THR B 54  ? 0.7678 0.4060 0.5579 0.2526  0.2996  0.1542  26  THR B CB    
2333 O OG1   . THR B 54  ? 0.8098 0.4334 0.5903 0.2587  0.3135  0.1554  26  THR B OG1   
2334 C CG2   . THR B 54  ? 0.7555 0.4004 0.5445 0.2495  0.2960  0.1482  26  THR B CG2   
2335 N N     . LEU B 55  ? 0.7685 0.4337 0.5928 0.2663  0.2940  0.1826  27  LEU B N     
2336 C CA    . LEU B 55  ? 0.7743 0.4372 0.6018 0.2671  0.2909  0.1874  27  LEU B CA    
2337 C C     . LEU B 55  ? 0.7512 0.4331 0.5936 0.2619  0.2732  0.1914  27  LEU B C     
2338 O O     . LEU B 55  ? 0.8278 0.5039 0.6680 0.2591  0.2683  0.1918  27  LEU B O     
2339 C CB    . LEU B 55  ? 0.7887 0.4576 0.6254 0.2781  0.2989  0.1990  27  LEU B CB    
2340 C CG    . LEU B 55  ? 0.8172 0.4625 0.6360 0.2832  0.3167  0.1952  27  LEU B CG    
2341 C CD1   . LEU B 55  ? 0.8302 0.4843 0.6599 0.2950  0.3244  0.2077  27  LEU B CD1   
2342 C CD2   . LEU B 55  ? 0.8356 0.4521 0.6338 0.2779  0.3220  0.1859  27  LEU B CD2   
2343 N N     . GLY B 56  ? 0.7295 0.4332 0.5865 0.2601  0.2634  0.1946  28  GLY B N     
2344 C CA    . GLY B 56  ? 0.7465 0.4671 0.6164 0.2539  0.2458  0.1977  28  GLY B CA    
2345 C C     . GLY B 56  ? 0.7532 0.4667 0.6127 0.2445  0.2393  0.1866  28  GLY B C     
2346 O O     . GLY B 56  ? 0.7179 0.4464 0.5876 0.2389  0.2248  0.1883  28  GLY B O     
2347 N N     . CYS B 57  ? 0.7548 0.4450 0.5939 0.2423  0.2500  0.1752  29  CYS B N     
2348 C CA    . CYS B 57  ? 0.7922 0.4738 0.6202 0.2334  0.2451  0.1639  29  CYS B CA    
2349 C C     . CYS B 57  ? 0.8825 0.5632 0.7101 0.2267  0.2336  0.1631  29  CYS B C     
2350 O O     . CYS B 57  ? 0.8546 0.5467 0.6883 0.2212  0.2208  0.1625  29  CYS B O     
2351 C CB    . CYS B 57  ? 0.9321 0.5871 0.7378 0.2313  0.2588  0.1517  29  CYS B CB    
2352 S SG    . CYS B 57  ? 0.8547 0.5014 0.6484 0.2217  0.2548  0.1375  29  CYS B SG    
2353 N N     . CYS B 58  ? 0.9858 0.6526 0.8055 0.2272  0.2381  0.1635  30  CYS B N     
2354 C CA    . CYS B 58  ? 0.9734 0.6349 0.7881 0.2207  0.2294  0.1615  30  CYS B CA    
2355 C C     . CYS B 58  ? 0.9296 0.6142 0.7613 0.2188  0.2119  0.1697  30  CYS B C     
2356 O O     . CYS B 58  ? 0.9458 0.6300 0.7738 0.2117  0.2019  0.1659  30  CYS B O     
2357 C CB    . CYS B 58  ? 1.0320 0.6783 0.8387 0.2235  0.2369  0.1637  30  CYS B CB    
2358 S SG    . CYS B 58  ? 1.2670 0.8921 1.0603 0.2292  0.2576  0.1596  30  CYS B SG    
2359 N N     . SER B 59  ? 0.8948 0.5992 0.7448 0.2247  0.2080  0.1810  31  SER B N     
2360 C CA    . SER B 59  ? 0.8163 0.5424 0.6830 0.2222  0.1910  0.1894  31  SER B CA    
2361 C C     . SER B 59  ? 0.7529 0.4952 0.6297 0.2188  0.1827  0.1888  31  SER B C     
2362 O O     . SER B 59  ? 0.7452 0.4941 0.6243 0.2120  0.1691  0.1878  31  SER B O     
2363 C CB    . SER B 59  ? 0.8191 0.5590 0.7014 0.2294  0.1902  0.2022  31  SER B CB    
2364 O OG    . SER B 59  ? 0.8524 0.5784 0.7261 0.2321  0.1951  0.2038  31  SER B OG    
2365 N N     . LEU B 60  ? 0.7842 0.5325 0.6662 0.2237  0.1909  0.1897  32  LEU B N     
2366 C CA    . LEU B 60  ? 0.7216 0.4860 0.6138 0.2210  0.1836  0.1902  32  LEU B CA    
2367 C C     . LEU B 60  ? 0.7259 0.4795 0.6046 0.2140  0.1808  0.1787  32  LEU B C     
2368 O O     . LEU B 60  ? 0.7012 0.4673 0.5875 0.2091  0.1691  0.1790  32  LEU B O     
2369 C CB    . LEU B 60  ? 0.7484 0.5195 0.6467 0.2284  0.1948  0.1935  32  LEU B CB    
2370 C CG    . LEU B 60  ? 0.6839 0.4707 0.5993 0.2358  0.1967  0.2063  32  LEU B CG    
2371 C CD1   . LEU B 60  ? 0.6779 0.4685 0.5959 0.2434  0.2099  0.2086  32  LEU B CD1   
2372 C CD2   . LEU B 60  ? 0.6396 0.4501 0.5754 0.2318  0.1796  0.2157  32  LEU B CD2   
2373 N N     . THR B 61  ? 0.8259 0.5561 0.6848 0.2131  0.1915  0.1685  33  THR B N     
2374 C CA    . THR B 61  ? 0.7449 0.4640 0.5906 0.2063  0.1892  0.1574  33  THR B CA    
2375 C C     . THR B 61  ? 0.7670 0.4901 0.6141 0.1995  0.1744  0.1579  33  THR B C     
2376 O O     . THR B 61  ? 0.7806 0.5112 0.6303 0.1948  0.1645  0.1556  33  THR B O     
2377 C CB    . THR B 61  ? 0.8303 0.5227 0.6549 0.2057  0.2033  0.1467  33  THR B CB    
2378 O OG1   . THR B 61  ? 0.8898 0.5772 0.7111 0.2114  0.2165  0.1451  33  THR B OG1   
2379 C CG2   . THR B 61  ? 0.8879 0.5689 0.6995 0.1982  0.2007  0.1351  33  THR B CG2   
2380 N N     . ALA B 62  ? 0.7925 0.5102 0.6372 0.1992  0.1727  0.1611  34  ALA B N     
2381 C CA    . ALA B 62  ? 0.8320 0.5511 0.6752 0.1930  0.1594  0.1615  34  ALA B CA    
2382 C C     . ALA B 62  ? 0.7998 0.5422 0.6615 0.1915  0.1434  0.1704  34  ALA B C     
2383 O O     . ALA B 62  ? 0.8117 0.5568 0.6722 0.1855  0.1313  0.1687  34  ALA B O     
2384 C CB    . ALA B 62  ? 0.8819 0.5896 0.7175 0.1938  0.1620  0.1637  34  ALA B CB    
2385 N N     . MET B 63  ? 0.7664 0.5250 0.6449 0.1965  0.1433  0.1797  35  MET B N     
2386 C CA    . MET B 63  ? 0.7464 0.5268 0.6432 0.1942  0.1282  0.1884  35  MET B CA    
2387 C C     . MET B 63  ? 0.7536 0.5417 0.6537 0.1898  0.1220  0.1846  35  MET B C     
2388 O O     . MET B 63  ? 0.7643 0.5589 0.6677 0.1838  0.1077  0.1852  35  MET B O     
2389 C CB    . MET B 63  ? 0.7040 0.4996 0.6179 0.2008  0.1312  0.1993  35  MET B CB    
2390 C CG    . MET B 63  ? 0.6881 0.5064 0.6219 0.1979  0.1164  0.2086  35  MET B CG    
2391 S SD    . MET B 63  ? 0.6168 0.4541 0.5712 0.2060  0.1228  0.2204  35  MET B SD    
2392 C CE    . MET B 63  ? 0.7166 0.5424 0.6648 0.2133  0.1331  0.2238  35  MET B CE    
2393 N N     . ALA B 64  ? 0.7280 0.5150 0.6265 0.1932  0.1325  0.1807  36  ALA B N     
2394 C CA    . ALA B 64  ? 0.6479 0.4408 0.5479 0.1896  0.1276  0.1766  36  ALA B CA    
2395 C C     . ALA B 64  ? 0.7047 0.4827 0.5881 0.1840  0.1244  0.1661  36  ALA B C     
2396 O O     . ALA B 64  ? 0.7443 0.5285 0.6301 0.1792  0.1140  0.1644  36  ALA B O     
2397 C CB    . ALA B 64  ? 0.6803 0.4731 0.5796 0.1951  0.1405  0.1747  36  ALA B CB    
2398 N N     . SER B 65  ? 0.7667 0.5246 0.6332 0.1844  0.1337  0.1592  37  SER B N     
2399 C CA    . SER B 65  ? 0.8056 0.5490 0.6562 0.1791  0.1314  0.1496  37  SER B CA    
2400 C C     . SER B 65  ? 0.7911 0.5398 0.6443 0.1740  0.1161  0.1529  37  SER B C     
2401 O O     . SER B 65  ? 0.7897 0.5329 0.6343 0.1694  0.1101  0.1467  37  SER B O     
2402 C CB    . SER B 65  ? 0.8444 0.5651 0.6772 0.1800  0.1449  0.1423  37  SER B CB    
2403 O OG    . SER B 65  ? 0.9475 0.6535 0.7647 0.1750  0.1447  0.1323  37  SER B OG    
2404 N N     . ALA B 66  ? 0.7596 0.5183 0.6239 0.1749  0.1096  0.1626  38  ALA B N     
2405 C CA    . ALA B 66  ? 0.7877 0.5510 0.6540 0.1700  0.0942  0.1662  38  ALA B CA    
2406 C C     . ALA B 66  ? 0.7282 0.5097 0.6099 0.1669  0.0807  0.1712  38  ALA B C     
2407 O O     . ALA B 66  ? 0.7468 0.5281 0.6254 0.1617  0.0688  0.1694  38  ALA B O     
2408 C CB    . ALA B 66  ? 0.8612 0.6257 0.7311 0.1721  0.0923  0.1744  38  ALA B CB    
2409 N N     . GLN B 67  ? 0.6868 0.4832 0.5845 0.1700  0.0827  0.1773  39  GLN B N     
2410 C CA    . GLN B 67  ? 0.6832 0.4964 0.5959 0.1666  0.0709  0.1820  39  GLN B CA    
2411 C C     . GLN B 67  ? 0.7004 0.5096 0.6057 0.1635  0.0692  0.1736  39  GLN B C     
2412 O O     . GLN B 67  ? 0.7085 0.5233 0.6178 0.1583  0.0560  0.1744  39  GLN B O     
2413 C CB    . GLN B 67  ? 0.7364 0.5653 0.6661 0.1712  0.0760  0.1899  39  GLN B CB    
2414 C CG    . GLN B 67  ? 0.7515 0.5896 0.6932 0.1739  0.0739  0.2003  39  GLN B CG    
2415 C CD    . GLN B 67  ? 0.7235 0.5754 0.6801 0.1798  0.0824  0.2073  39  GLN B CD    
2416 O OE1   . GLN B 67  ? 0.6406 0.4903 0.5940 0.1836  0.0940  0.2033  39  GLN B OE1   
2417 N NE2   . GLN B 67  ? 0.7539 0.6200 0.7264 0.1810  0.0768  0.2181  39  GLN B NE2   
2418 N N     . LEU B 68  ? 0.6931 0.4916 0.5871 0.1667  0.0823  0.1656  40  LEU B N     
2419 C CA    . LEU B 68  ? 0.6799 0.4744 0.5665 0.1646  0.0814  0.1577  40  LEU B CA    
2420 C C     . LEU B 68  ? 0.7944 0.5766 0.6669 0.1601  0.0744  0.1508  40  LEU B C     
2421 O O     . LEU B 68  ? 0.8131 0.5973 0.6846 0.1570  0.0663  0.1475  40  LEU B O     
2422 C CB    . LEU B 68  ? 0.6211 0.4055 0.4976 0.1693  0.0972  0.1507  40  LEU B CB    
2423 C CG    . LEU B 68  ? 0.5658 0.3621 0.4538 0.1742  0.1042  0.1559  40  LEU B CG    
2424 C CD1   . LEU B 68  ? 0.6174 0.3999 0.4917 0.1787  0.1197  0.1479  40  LEU B CD1   
2425 C CD2   . LEU B 68  ? 0.5876 0.4010 0.4891 0.1716  0.0938  0.1602  40  LEU B CD2   
2426 N N     . ASP B 69  ? 0.8048 0.5741 0.6659 0.1600  0.0776  0.1488  41  ASP B N     
2427 C CA    . ASP B 69  ? 0.7636 0.5201 0.6095 0.1563  0.0722  0.1423  41  ASP B CA    
2428 C C     . ASP B 69  ? 0.7541 0.5197 0.6070 0.1518  0.0548  0.1471  41  ASP B C     
2429 O O     . ASP B 69  ? 0.7421 0.5002 0.5844 0.1489  0.0485  0.1412  41  ASP B O     
2430 C CB    . ASP B 69  ? 0.8315 0.5731 0.6645 0.1570  0.0792  0.1407  41  ASP B CB    
2431 C CG    . ASP B 69  ? 0.9165 0.6426 0.7368 0.1596  0.0959  0.1326  41  ASP B CG    
2432 O OD1   . ASP B 69  ? 0.9358 0.6664 0.7572 0.1575  0.0998  0.1239  41  ASP B OD1   
2433 O OD2   . ASP B 69  ? 0.9283 0.6430 0.7404 0.1606  0.1038  0.1324  41  ASP B OD2   
2434 N N     . ALA B 70  ? 0.7442 0.5250 0.6143 0.1512  0.0470  0.1576  42  ALA B N     
2435 C CA    . ALA B 70  ? 0.7370 0.5254 0.6141 0.1463  0.0301  0.1625  42  ALA B CA    
2436 C C     . ALA B 70  ? 0.7618 0.5588 0.6466 0.1441  0.0237  0.1613  42  ALA B C     
2437 O O     . ALA B 70  ? 0.7882 0.5852 0.6723 0.1397  0.0108  0.1613  42  ALA B O     
2438 C CB    . ALA B 70  ? 0.7148 0.5157 0.6074 0.1461  0.0235  0.1742  42  ALA B CB    
2439 N N     . LEU B 71  ? 0.7694 0.5728 0.6608 0.1471  0.0326  0.1604  43  LEU B N     
2440 C CA    . LEU B 71  ? 0.7439 0.5562 0.6432 0.1453  0.0275  0.1601  43  LEU B CA    
2441 C C     . LEU B 71  ? 0.7242 0.5262 0.6094 0.1469  0.0335  0.1492  43  LEU B C     
2442 O O     . LEU B 71  ? 0.7223 0.5290 0.6106 0.1447  0.0267  0.1474  43  LEU B O     
2443 C CB    . LEU B 71  ? 0.6880 0.5161 0.6045 0.1478  0.0324  0.1673  43  LEU B CB    
2444 C CG    . LEU B 71  ? 0.7510 0.5926 0.6846 0.1468  0.0266  0.1787  43  LEU B CG    
2445 C CD1   . LEU B 71  ? 0.6496 0.5052 0.5973 0.1504  0.0343  0.1843  43  LEU B CD1   
2446 C CD2   . LEU B 71  ? 0.8196 0.6662 0.7601 0.1402  0.0089  0.1832  43  LEU B CD2   
2447 N N     . TRP B 72  ? 0.7077 0.4976 0.5788 0.1488  0.0454  0.1404  44  TRP B N     
2448 C CA    . TRP B 72  ? 0.6914 0.4793 0.5545 0.1466  0.0518  0.1265  44  TRP B CA    
2449 C C     . TRP B 72  ? 0.8024 0.5896 0.6601 0.1408  0.0418  0.1174  44  TRP B C     
2450 O O     . TRP B 72  ? 0.8063 0.5969 0.6624 0.1392  0.0436  0.1085  44  TRP B O     
2451 C CB    . TRP B 72  ? 0.6965 0.4722 0.5465 0.1474  0.0652  0.1179  44  TRP B CB    
2452 C CG    . TRP B 72  ? 0.6716 0.4483 0.5178 0.1471  0.0749  0.1076  44  TRP B CG    
2453 C CD1   . TRP B 72  ? 0.6595 0.4336 0.4964 0.1424  0.0763  0.0935  44  TRP B CD1   
2454 C CD2   . TRP B 72  ? 0.6762 0.4577 0.5278 0.1518  0.0843  0.1108  44  TRP B CD2   
2455 N NE1   . TRP B 72  ? 0.6795 0.4565 0.5155 0.1434  0.0853  0.0876  44  TRP B NE1   
2456 C CE2   . TRP B 72  ? 0.7243 0.5051 0.5683 0.1492  0.0905  0.0977  44  TRP B CE2   
2457 C CE3   . TRP B 72  ? 0.6270 0.4136 0.4889 0.1582  0.0884  0.1235  44  TRP B CE3   
2458 C CZ2   . TRP B 72  ? 0.6944 0.4782 0.5392 0.1524  0.1001  0.0964  44  TRP B CZ2   
2459 C CZ3   . TRP B 72  ? 0.6274 0.4169 0.4904 0.1620  0.0988  0.1223  44  TRP B CZ3   
2460 C CH2   . TRP B 72  ? 0.6488 0.4362 0.5024 0.1590  0.1044  0.1087  44  TRP B CH2   
2461 N N     . SER B 73  ? 0.8375 0.6201 0.6919 0.1380  0.0313  0.1193  45  SER B N     
2462 C CA    . SER B 73  ? 0.8080 0.5890 0.6571 0.1333  0.0218  0.1111  45  SER B CA    
2463 C C     . SER B 73  ? 0.7518 0.5436 0.6134 0.1324  0.0121  0.1162  45  SER B C     
2464 O O     . SER B 73  ? 0.7438 0.5364 0.6027 0.1300  0.0082  0.1081  45  SER B O     
2465 C CB    . SER B 73  ? 0.8168 0.5885 0.6571 0.1308  0.0135  0.1117  45  SER B CB    
2466 O OG    . SER B 73  ? 0.8397 0.6155 0.6896 0.1315  0.0042  0.1254  45  SER B OG    
2467 N N     . GLN B 74  ? 0.7441 0.5443 0.6197 0.1345  0.0085  0.1301  46  GLN B N     
2468 C CA    . GLN B 74  ? 0.7229 0.5332 0.6114 0.1332  -0.0007 0.1367  46  GLN B CA    
2469 C C     . GLN B 74  ? 0.6722 0.4914 0.5667 0.1356  0.0069  0.1352  46  GLN B C     
2470 O O     . GLN B 74  ? 0.6785 0.5065 0.5839 0.1349  0.0006  0.1413  46  GLN B O     
2471 C CB    . GLN B 74  ? 0.6775 0.4950 0.5802 0.1339  -0.0076 0.1528  46  GLN B CB    
2472 C CG    . GLN B 74  ? 0.7353 0.5461 0.6335 0.1303  -0.0180 0.1552  46  GLN B CG    
2473 C CD    . GLN B 74  ? 0.7978 0.6212 0.7136 0.1271  -0.0250 0.1672  46  GLN B CD    
2474 O OE1   . GLN B 74  ? 0.8595 0.6812 0.7740 0.1276  -0.0242 0.1707  46  GLN B OE1   
2475 N NE2   . GLN B 74  ? 0.7198 0.5551 0.6511 0.1240  -0.0320 0.1734  46  GLN B NE2   
2476 N N     . LEU B 75  ? 0.5786 0.3953 0.4656 0.1382  0.0200  0.1273  47  LEU B N     
2477 C CA    . LEU B 75  ? 0.5753 0.3999 0.4658 0.1407  0.0276  0.1253  47  LEU B CA    
2478 C C     . LEU B 75  ? 0.7838 0.6071 0.6661 0.1378  0.0260  0.1121  47  LEU B C     
2479 O O     . LEU B 75  ? 0.7448 0.5598 0.6150 0.1358  0.0287  0.1007  47  LEU B O     
2480 C CB    . LEU B 75  ? 0.5511 0.3732 0.4376 0.1450  0.0426  0.1240  47  LEU B CB    
2481 C CG    . LEU B 75  ? 0.4754 0.3005 0.3714 0.1497  0.0464  0.1379  47  LEU B CG    
2482 C CD1   . LEU B 75  ? 0.5243 0.3419 0.4123 0.1537  0.0613  0.1341  47  LEU B CD1   
2483 C CD2   . LEU B 75  ? 0.4844 0.3234 0.3959 0.1524  0.0446  0.1495  47  LEU B CD2   
2484 N N     . SER B 76  ? 0.6349 0.4671 0.5244 0.1379  0.0218  0.1142  48  SER B N     
2485 C CA    . SER B 76  ? 0.6452 0.4783 0.5288 0.1362  0.0200  0.1033  48  SER B CA    
2486 C C     . SER B 76  ? 0.6109 0.4507 0.4934 0.1390  0.0302  0.0995  48  SER B C     
2487 O O     . SER B 76  ? 0.7213 0.5683 0.6118 0.1422  0.0341  0.1087  48  SER B O     
2488 C CB    . SER B 76  ? 0.7248 0.5616 0.6157 0.1342  0.0071  0.1080  48  SER B CB    
2489 O OG    . SER B 76  ? 0.8500 0.6969 0.7536 0.1362  0.0065  0.1200  48  SER B OG    
2490 N N     . TRP B 77  ? 0.6133 0.4510 0.4856 0.1377  0.0345  0.0861  49  TRP B N     
2491 C CA    . TRP B 77  ? 0.6249 0.4674 0.4934 0.1396  0.0444  0.0805  49  TRP B CA    
2492 C C     . TRP B 77  ? 0.5608 0.4102 0.4280 0.1389  0.0400  0.0737  49  TRP B C     
2493 O O     . TRP B 77  ? 0.6705 0.5180 0.5356 0.1365  0.0323  0.0682  49  TRP B O     
2494 C CB    . TRP B 77  ? 0.6370 0.4714 0.4944 0.1384  0.0547  0.0701  49  TRP B CB    
2495 C CG    . TRP B 77  ? 0.6114 0.4381 0.4689 0.1399  0.0602  0.0767  49  TRP B CG    
2496 C CD1   . TRP B 77  ? 0.6259 0.4440 0.4812 0.1382  0.0569  0.0781  49  TRP B CD1   
2497 C CD2   . TRP B 77  ? 0.6410 0.4677 0.5005 0.1441  0.0701  0.0830  49  TRP B CD2   
2498 N NE1   . TRP B 77  ? 0.6195 0.4327 0.4759 0.1411  0.0638  0.0854  49  TRP B NE1   
2499 C CE2   . TRP B 77  ? 0.6134 0.4316 0.4727 0.1450  0.0722  0.0884  49  TRP B CE2   
2500 C CE3   . TRP B 77  ? 0.6035 0.4361 0.4642 0.1476  0.0776  0.0846  49  TRP B CE3   
2501 C CZ2   . TRP B 77  ? 0.5925 0.4082 0.4537 0.1497  0.0817  0.0956  49  TRP B CZ2   
2502 C CZ3   . TRP B 77  ? 0.6023 0.4319 0.4641 0.1522  0.0874  0.0913  49  TRP B CZ3   
2503 C CH2   . TRP B 77  ? 0.6375 0.4587 0.5001 0.1533  0.0894  0.0968  49  TRP B CH2   
2504 N N     . PRO B 78  ? 0.5303 0.3877 0.3982 0.1413  0.0448  0.0741  50  PRO B N     
2505 C CA    . PRO B 78  ? 0.6071 0.4716 0.4728 0.1410  0.0411  0.0675  50  PRO B CA    
2506 C C     . PRO B 78  ? 0.6270 0.4898 0.4823 0.1384  0.0456  0.0522  50  PRO B C     
2507 O O     . PRO B 78  ? 0.6237 0.4800 0.4726 0.1370  0.0540  0.0466  50  PRO B O     
2508 C CB    . PRO B 78  ? 0.5755 0.4486 0.4440 0.1447  0.0459  0.0738  50  PRO B CB    
2509 C CG    . PRO B 78  ? 0.6026 0.4714 0.4695 0.1465  0.0566  0.0770  50  PRO B CG    
2510 C CD    . PRO B 78  ? 0.6436 0.5040 0.5138 0.1450  0.0540  0.0812  50  PRO B CD    
2511 N N     . GLN B 79  ? 0.6543 0.5230 0.5085 0.1378  0.0399  0.0457  51  GLN B N     
2512 C CA    . GLN B 79  ? 0.6565 0.5267 0.5028 0.1353  0.0432  0.0315  51  GLN B CA    
2513 C C     . GLN B 79  ? 0.6491 0.5216 0.4891 0.1350  0.0537  0.0262  51  GLN B C     
2514 O O     . GLN B 79  ? 0.6523 0.5181 0.4861 0.1323  0.0615  0.0196  51  GLN B O     
2515 C CB    . GLN B 79  ? 0.7093 0.5878 0.5573 0.1360  0.0350  0.0275  51  GLN B CB    
2516 C CG    . GLN B 79  ? 0.7102 0.5840 0.5599 0.1351  0.0266  0.0257  51  GLN B CG    
2517 C CD    . GLN B 79  ? 0.7259 0.5945 0.5692 0.1316  0.0308  0.0147  51  GLN B CD    
2518 O OE1   . GLN B 79  ? 0.6960 0.5679 0.5344 0.1294  0.0382  0.0057  51  GLN B OE1   
2519 N NE2   . GLN B 79  ? 0.7368 0.5970 0.5798 0.1307  0.0261  0.0152  51  GLN B NE2   
2520 N N     . THR B 80  ? 0.6348 0.5160 0.4753 0.1377  0.0541  0.0290  52  THR B N     
2521 C CA    . THR B 80  ? 0.6246 0.5069 0.4579 0.1380  0.0640  0.0251  52  THR B CA    
2522 C C     . THR B 80  ? 0.6715 0.5469 0.5065 0.1407  0.0710  0.0348  52  THR B C     
2523 O O     . THR B 80  ? 0.6825 0.5606 0.5258 0.1442  0.0674  0.0474  52  THR B O     
2524 C CB    . THR B 80  ? 0.6060 0.4998 0.4380 0.1405  0.0619  0.0252  52  THR B CB    
2525 O OG1   . THR B 80  ? 0.6288 0.5299 0.4604 0.1386  0.0550  0.0167  52  THR B OG1   
2526 C CG2   . THR B 80  ? 0.6362 0.5300 0.4586 0.1405  0.0721  0.0200  52  THR B CG2   
2527 N N     . PRO B 81  ? 0.6229 0.4896 0.4510 0.1393  0.0810  0.0300  53  PRO B N     
2528 C CA    . PRO B 81  ? 0.5779 0.4374 0.4084 0.1427  0.0876  0.0397  53  PRO B CA    
2529 C C     . PRO B 81  ? 0.5812 0.4469 0.4136 0.1479  0.0913  0.0484  53  PRO B C     
2530 O O     . PRO B 81  ? 0.6350 0.5071 0.4616 0.1485  0.0931  0.0436  53  PRO B O     
2531 C CB    . PRO B 81  ? 0.6151 0.4634 0.4354 0.1400  0.0982  0.0303  53  PRO B CB    
2532 C CG    . PRO B 81  ? 0.6533 0.5023 0.4690 0.1340  0.0950  0.0172  53  PRO B CG    
2533 C CD    . PRO B 81  ? 0.6693 0.5315 0.4881 0.1343  0.0861  0.0157  53  PRO B CD    
2534 N N     . LEU B 82  ? 0.5470 0.4116 0.3880 0.1519  0.0923  0.0617  54  LEU B N     
2535 C CA    . LEU B 82  ? 0.5323 0.4018 0.3761 0.1575  0.0979  0.0716  54  LEU B CA    
2536 C C     . LEU B 82  ? 0.5520 0.4121 0.3927 0.1608  0.1098  0.0740  54  LEU B C     
2537 O O     . LEU B 82  ? 0.5837 0.4342 0.4239 0.1590  0.1114  0.0723  54  LEU B O     
2538 C CB    . LEU B 82  ? 0.5220 0.3998 0.3805 0.1598  0.0895  0.0867  54  LEU B CB    
2539 C CG    . LEU B 82  ? 0.5021 0.3887 0.3644 0.1579  0.0781  0.0868  54  LEU B CG    
2540 C CD1   . LEU B 82  ? 0.4820 0.3745 0.3591 0.1595  0.0706  0.1023  54  LEU B CD1   
2541 C CD2   . LEU B 82  ? 0.5252 0.4188 0.3791 0.1594  0.0812  0.0813  54  LEU B CD2   
2542 N N     . PRO B 83  ? 0.4957 0.3578 0.3334 0.1659  0.1188  0.0780  55  PRO B N     
2543 C CA    . PRO B 83  ? 0.5061 0.3586 0.3411 0.1703  0.1308  0.0812  55  PRO B CA    
2544 C C     . PRO B 83  ? 0.5267 0.3797 0.3762 0.1733  0.1283  0.0956  55  PRO B C     
2545 O O     . PRO B 83  ? 0.5060 0.3695 0.3686 0.1740  0.1198  0.1067  55  PRO B O     
2546 C CB    . PRO B 83  ? 0.5219 0.3787 0.3516 0.1759  0.1396  0.0836  55  PRO B CB    
2547 C CG    . PRO B 83  ? 0.5737 0.4399 0.3986 0.1730  0.1332  0.0773  55  PRO B CG    
2548 C CD    . PRO B 83  ? 0.4997 0.3718 0.3344 0.1683  0.1193  0.0786  55  PRO B CD    
2549 N N     . VAL B 84  ? 0.5082 0.3497 0.3552 0.1748  0.1356  0.0955  56  VAL B N     
2550 C CA    . VAL B 84  ? 0.5054 0.3464 0.3648 0.1777  0.1338  0.1085  56  VAL B CA    
2551 C C     . VAL B 84  ? 0.5165 0.3544 0.3766 0.1859  0.1468  0.1162  56  VAL B C     
2552 O O     . VAL B 84  ? 0.5891 0.4163 0.4360 0.1877  0.1583  0.1076  56  VAL B O     
2553 C CB    . VAL B 84  ? 0.5050 0.3349 0.3611 0.1730  0.1303  0.1029  56  VAL B CB    
2554 C CG1   . VAL B 84  ? 0.5152 0.3429 0.3814 0.1770  0.1306  0.1158  56  VAL B CG1   
2555 C CG2   . VAL B 84  ? 0.5148 0.3493 0.3729 0.1661  0.1168  0.0980  56  VAL B CG2   
2556 N N     . LEU B 85  ? 0.5124 0.3597 0.3883 0.1908  0.1450  0.1324  57  LEU B N     
2557 C CA    . LEU B 85  ? 0.5221 0.3698 0.4017 0.1998  0.1571  0.1419  57  LEU B CA    
2558 C C     . LEU B 85  ? 0.5239 0.3673 0.4126 0.2032  0.1579  0.1517  57  LEU B C     
2559 O O     . LEU B 85  ? 0.5140 0.3629 0.4142 0.1999  0.1464  0.1587  57  LEU B O     
2560 C CB    . LEU B 85  ? 0.5172 0.3819 0.4091 0.2039  0.1559  0.1544  57  LEU B CB    
2561 C CG    . LEU B 85  ? 0.5265 0.3950 0.4248 0.2140  0.1683  0.1662  57  LEU B CG    
2562 C CD1   . LEU B 85  ? 0.5432 0.3998 0.4228 0.2184  0.1833  0.1556  57  LEU B CD1   
2563 C CD2   . LEU B 85  ? 0.5195 0.4069 0.4328 0.2165  0.1649  0.1798  57  LEU B CD2   
2564 N N     . ASP B 86  ? 0.5379 0.3711 0.4207 0.2099  0.1715  0.1520  58  ASP B N     
2565 C CA    . ASP B 86  ? 0.5422 0.3720 0.4338 0.2153  0.1743  0.1629  58  ASP B CA    
2566 C C     . ASP B 86  ? 0.5494 0.3871 0.4498 0.2255  0.1851  0.1750  58  ASP B C     
2567 O O     . ASP B 86  ? 0.5640 0.3919 0.4524 0.2315  0.1992  0.1700  58  ASP B O     
2568 C CB    . ASP B 86  ? 0.6022 0.4112 0.4790 0.2144  0.1814  0.1527  58  ASP B CB    
2569 C CG    . ASP B 86  ? 0.7468 0.5544 0.6327 0.2180  0.1824  0.1628  58  ASP B CG    
2570 O OD1   . ASP B 86  ? 0.7327 0.5602 0.6380 0.2154  0.1727  0.1733  58  ASP B OD1   
2571 O OD2   . ASP B 86  ? 0.7216 0.5121 0.5963 0.2200  0.1915  0.1576  58  ASP B OD2   
2572 N N     . ILE B 87  ? 0.5383 0.3982 0.4605 0.2231  0.1772  0.1870  59  ILE B N     
2573 C CA    . ILE B 87  ? 0.5427 0.4164 0.4769 0.2299  0.1858  0.1977  59  ILE B CA    
2574 C C     . ILE B 87  ? 0.5959 0.4682 0.5359 0.2328  0.1911  0.2020  59  ILE B C     
2575 O O     . ILE B 87  ? 0.6290 0.5045 0.5775 0.2269  0.1808  0.2036  59  ILE B O     
2576 C CB    . ILE B 87  ? 0.5279 0.4266 0.4838 0.2254  0.1748  0.2083  59  ILE B CB    
2577 C CG1   . ILE B 87  ? 0.5223 0.4221 0.4714 0.2233  0.1706  0.2046  59  ILE B CG1   
2578 C CG2   . ILE B 87  ? 0.5327 0.4468 0.5029 0.2323  0.1840  0.2202  59  ILE B CG2   
2579 C CD1   . ILE B 87  ? 0.5089 0.4311 0.4780 0.2177  0.1595  0.2140  59  ILE B CD1   
2580 N N     . GLY B 88  ? 0.6095 0.4762 0.5438 0.2422  0.2071  0.2040  60  GLY B N     
2581 C CA    . GLY B 88  ? 0.6112 0.4745 0.5488 0.2461  0.2137  0.2078  60  GLY B CA    
2582 C C     . GLY B 88  ? 0.6068 0.4483 0.5289 0.2428  0.2134  0.1975  60  GLY B C     
2583 O O     . GLY B 88  ? 0.6386 0.4829 0.5688 0.2391  0.2060  0.2003  60  GLY B O     
2584 N N     . CYS B 89  ? 0.6512 0.4707 0.5507 0.2440  0.2214  0.1853  61  CYS B N     
2585 C CA    . CYS B 89  ? 0.7061 0.5039 0.5901 0.2398  0.2214  0.1744  61  CYS B CA    
2586 C C     . CYS B 89  ? 0.7351 0.5208 0.6138 0.2443  0.2324  0.1753  61  CYS B C     
2587 O O     . CYS B 89  ? 0.7306 0.5017 0.6007 0.2404  0.2312  0.1694  61  CYS B O     
2588 C CB    . CYS B 89  ? 0.6799 0.4589 0.5426 0.2388  0.2263  0.1598  61  CYS B CB    
2589 S SG    . CYS B 89  ? 0.6296 0.3961 0.4759 0.2468  0.2453  0.1538  61  CYS B SG    
2590 N N     . GLY B 90  ? 0.6999 0.4909 0.5830 0.2525  0.2432  0.1830  62  GLY B N     
2591 C CA    . GLY B 90  ? 0.7107 0.4889 0.5872 0.2575  0.2546  0.1840  62  GLY B CA    
2592 C C     . GLY B 90  ? 0.6987 0.4479 0.5488 0.2568  0.2654  0.1700  62  GLY B C     
2593 O O     . GLY B 90  ? 0.6942 0.4365 0.5321 0.2564  0.2693  0.1617  62  GLY B O     
2594 N N     . PRO B 91  ? 0.6862 0.4183 0.5272 0.2556  0.2697  0.1665  63  PRO B N     
2595 C CA    . PRO B 91  ? 0.7008 0.4049 0.5175 0.2525  0.2788  0.1526  63  PRO B CA    
2596 C C     . PRO B 91  ? 0.6935 0.3879 0.4989 0.2429  0.2720  0.1384  63  PRO B C     
2597 O O     . PRO B 91  ? 0.7200 0.3933 0.5070 0.2375  0.2774  0.1255  63  PRO B O     
2598 C CB    . PRO B 91  ? 0.7150 0.4070 0.5289 0.2537  0.2837  0.1553  63  PRO B CB    
2599 C CG    . PRO B 91  ? 0.6965 0.4081 0.5306 0.2533  0.2721  0.1654  63  PRO B CG    
2600 C CD    . PRO B 91  ? 0.6782 0.4167 0.5315 0.2561  0.2653  0.1748  63  PRO B CD    
2601 N N     . GLY B 92  ? 0.7162 0.4260 0.5329 0.2397  0.2596  0.1402  64  GLY B N     
2602 C CA    . GLY B 92  ? 0.7280 0.4306 0.5348 0.2316  0.2535  0.1268  64  GLY B CA    
2603 C C     . GLY B 92  ? 0.7058 0.3965 0.5074 0.2245  0.2485  0.1213  64  GLY B C     
2604 O O     . GLY B 92  ? 0.7259 0.4056 0.5150 0.2169  0.2474  0.1073  64  GLY B O     
2605 N N     . ASP B 93  ? 0.7023 0.3968 0.5134 0.2259  0.2452  0.1313  65  ASP B N     
2606 C CA    . ASP B 93  ? 0.7274 0.4110 0.5331 0.2194  0.2405  0.1270  65  ASP B CA    
2607 C C     . ASP B 93  ? 0.7025 0.3990 0.5177 0.2143  0.2248  0.1289  65  ASP B C     
2608 O O     . ASP B 93  ? 0.7313 0.4169 0.5371 0.2075  0.2211  0.1199  65  ASP B O     
2609 C CB    . ASP B 93  ? 0.7600 0.4412 0.5697 0.2228  0.2439  0.1356  65  ASP B CB    
2610 C CG    . ASP B 93  ? 0.7972 0.4608 0.5942 0.2267  0.2594  0.1326  65  ASP B CG    
2611 O OD1   . ASP B 93  ? 0.8930 0.5348 0.6726 0.2211  0.2653  0.1213  65  ASP B OD1   
2612 O OD2   . ASP B 93  ? 0.7476 0.4193 0.5520 0.2348  0.2654  0.1416  65  ASP B OD2   
2613 N N     . ILE B 94  ? 0.6574 0.3774 0.4913 0.2166  0.2154  0.1404  66  ILE B N     
2614 C CA    . ILE B 94  ? 0.6062 0.3388 0.4484 0.2107  0.1998  0.1417  66  ILE B CA    
2615 C C     . ILE B 94  ? 0.6032 0.3309 0.4363 0.2083  0.1992  0.1315  66  ILE B C     
2616 O O     . ILE B 94  ? 0.6360 0.3653 0.4663 0.1997  0.1894  0.1244  66  ILE B O     
2617 C CB    . ILE B 94  ? 0.6420 0.4014 0.5070 0.2124  0.1899  0.1554  66  ILE B CB    
2618 C CG1   . ILE B 94  ? 0.7029 0.4680 0.5775 0.2120  0.1847  0.1634  66  ILE B CG1   
2619 C CG2   . ILE B 94  ? 0.6510 0.4237 0.5234 0.2068  0.1756  0.1557  66  ILE B CG2   
2620 C CD1   . ILE B 94  ? 0.7191 0.5099 0.6168 0.2133  0.1759  0.1764  66  ILE B CD1   
2621 N N     . ALA B 95  ? 0.6537 0.3815 0.4828 0.2123  0.2083  0.1279  67  ALA B N     
2622 C CA    . ALA B 95  ? 0.6215 0.3544 0.4436 0.2052  0.2054  0.1151  67  ALA B CA    
2623 C C     . ALA B 95  ? 0.6083 0.3252 0.4131 0.1963  0.2080  0.0979  67  ALA B C     
2624 O O     . ALA B 95  ? 0.5975 0.3205 0.4001 0.1875  0.1992  0.0888  67  ALA B O     
2625 C CB    . ALA B 95  ? 0.6078 0.3443 0.4279 0.2116  0.2150  0.1153  67  ALA B CB    
2626 N N     . ARG B 96  ? 0.6274 0.3238 0.4205 0.1983  0.2201  0.0937  68  ARG B N     
2627 C CA    . ARG B 96  ? 0.6368 0.3174 0.4136 0.1894  0.2239  0.0774  68  ARG B CA    
2628 C C     . ARG B 96  ? 0.6331 0.3082 0.4094 0.1832  0.2174  0.0766  68  ARG B C     
2629 O O     . ARG B 96  ? 0.6556 0.3308 0.4260 0.1734  0.2124  0.0650  68  ARG B O     
2630 C CB    . ARG B 96  ? 0.6613 0.3207 0.4244 0.1932  0.2401  0.0724  68  ARG B CB    
2631 C CG    . ARG B 96  ? 0.7000 0.3421 0.4493 0.1826  0.2430  0.0599  68  ARG B CG    
2632 C CD    . ARG B 96  ? 0.7742 0.4198 0.5156 0.1718  0.2391  0.0436  68  ARG B CD    
2633 N NE    . ARG B 96  ? 0.9200 0.5534 0.6526 0.1610  0.2392  0.0333  68  ARG B NE    
2634 C CZ    . ARG B 96  ? 1.0360 0.6644 0.7591 0.1501  0.2405  0.0192  68  ARG B CZ    
2635 N NH1   . ARG B 96  ? 1.0609 0.6941 0.7804 0.1484  0.2415  0.0128  68  ARG B NH1   
2636 N NH2   . ARG B 96  ? 0.9639 0.5828 0.6814 0.1405  0.2406  0.0115  68  ARG B NH2   
2637 N N     . LYS B 97  ? 0.6622 0.3332 0.4445 0.1890  0.2174  0.0891  69  LYS B N     
2638 C CA    . LYS B 97  ? 0.6382 0.3000 0.4167 0.1841  0.2138  0.0884  69  LYS B CA    
2639 C C     . LYS B 97  ? 0.6196 0.2972 0.4091 0.1810  0.1980  0.0950  69  LYS B C     
2640 O O     . LYS B 97  ? 0.6543 0.3265 0.4386 0.1747  0.1934  0.0908  69  LYS B O     
2641 C CB    . LYS B 97  ? 0.6859 0.3328 0.4624 0.1914  0.2227  0.0977  69  LYS B CB    
2642 C CG    . LYS B 97  ? 0.7383 0.3695 0.5024 0.1913  0.2373  0.0902  69  LYS B CG    
2643 C CD    . LYS B 97  ? 0.7883 0.4129 0.5530 0.1961  0.2437  0.0998  69  LYS B CD    
2644 C CE    . LYS B 97  ? 0.9828 0.5913 0.7351 0.1962  0.2574  0.0935  69  LYS B CE    
2645 N NZ    . LYS B 97  ? 1.1301 0.7333 0.8838 0.2026  0.2643  0.1035  69  LYS B NZ    
2646 N N     . VAL B 98  ? 0.6058 0.3022 0.4099 0.1852  0.1899  0.1049  70  VAL B N     
2647 C CA    . VAL B 98  ? 0.5901 0.3005 0.4049 0.1825  0.1746  0.1119  70  VAL B CA    
2648 C C     . VAL B 98  ? 0.5741 0.2997 0.3927 0.1767  0.1653  0.1052  70  VAL B C     
2649 O O     . VAL B 98  ? 0.6824 0.4104 0.4986 0.1694  0.1563  0.0988  70  VAL B O     
2650 C CB    . VAL B 98  ? 0.5870 0.3086 0.4175 0.1905  0.1705  0.1297  70  VAL B CB    
2651 C CG1   . VAL B 98  ? 0.6185 0.3548 0.4595 0.1857  0.1536  0.1352  70  VAL B CG1   
2652 C CG2   . VAL B 98  ? 0.6779 0.3921 0.5068 0.1931  0.1778  0.1336  70  VAL B CG2   
2653 N N     . LEU B 99  ? 0.5702 0.3059 0.3945 0.1804  0.1676  0.1070  71  LEU B N     
2654 C CA    . LEU B 99  ? 0.5556 0.3064 0.3846 0.1759  0.1584  0.1029  71  LEU B CA    
2655 C C     . LEU B 99  ? 0.5569 0.3025 0.3729 0.1682  0.1606  0.0855  71  LEU B C     
2656 O O     . LEU B 99  ? 0.6289 0.3806 0.4449 0.1616  0.1509  0.0793  71  LEU B O     
2657 C CB    . LEU B 99  ? 0.5526 0.3157 0.3910 0.1825  0.1609  0.1110  71  LEU B CB    
2658 C CG    . LEU B 99  ? 0.5465 0.3217 0.4023 0.1886  0.1551  0.1290  71  LEU B CG    
2659 C CD1   . LEU B 99  ? 0.5457 0.3323 0.4099 0.1953  0.1602  0.1365  71  LEU B CD1   
2660 C CD2   . LEU B 99  ? 0.5321 0.3179 0.3966 0.1829  0.1387  0.1323  71  LEU B CD2   
2661 N N     . ALA B 100 ? 0.5703 0.3048 0.3752 0.1690  0.1732  0.0773  72  ALA B N     
2662 C CA    . ALA B 100 ? 0.5723 0.3039 0.3658 0.1615  0.1751  0.0609  72  ALA B CA    
2663 C C     . ALA B 100 ? 0.6379 0.3645 0.4259 0.1529  0.1702  0.0519  72  ALA B C     
2664 O O     . ALA B 100 ? 0.6715 0.4063 0.4582 0.1466  0.1641  0.0424  72  ALA B O     
2665 C CB    . ALA B 100 ? 0.5907 0.3080 0.3720 0.1633  0.1899  0.0539  72  ALA B CB    
2666 N N     . PRO B 101 ? 0.6337 0.3477 0.4183 0.1524  0.1726  0.0543  73  PRO B N     
2667 C CA    . PRO B 101 ? 0.6651 0.3758 0.4445 0.1443  0.1680  0.0460  73  PRO B CA    
2668 C C     . PRO B 101 ? 0.6512 0.3760 0.4394 0.1423  0.1534  0.0495  73  PRO B C     
2669 O O     . PRO B 101 ? 0.6795 0.4074 0.4644 0.1355  0.1486  0.0399  73  PRO B O     
2670 C CB    . PRO B 101 ? 0.7425 0.4361 0.5162 0.1458  0.1746  0.0505  73  PRO B CB    
2671 C CG    . PRO B 101 ? 0.7214 0.4060 0.4935 0.1533  0.1859  0.0559  73  PRO B CG    
2672 C CD    . PRO B 101 ? 0.6480 0.3486 0.4311 0.1591  0.1816  0.0632  73  PRO B CD    
2673 N N     . ARG B 102 ? 0.6226 0.3560 0.4221 0.1480  0.1463  0.0630  74  ARG B N     
2674 C CA    . ARG B 102 ? 0.6028 0.3468 0.4098 0.1460  0.1322  0.0670  74  ARG B CA    
2675 C C     . ARG B 102 ? 0.6363 0.3954 0.4492 0.1443  0.1246  0.0636  74  ARG B C     
2676 O O     . ARG B 102 ? 0.6930 0.4595 0.5105 0.1418  0.1131  0.0645  74  ARG B O     
2677 C CB    . ARG B 102 ? 0.5427 0.2894 0.3597 0.1519  0.1270  0.0831  74  ARG B CB    
2678 C CG    . ARG B 102 ? 0.6400 0.3733 0.4513 0.1528  0.1300  0.0872  74  ARG B CG    
2679 C CD    . ARG B 102 ? 0.6898 0.4265 0.5116 0.1598  0.1270  0.1038  74  ARG B CD    
2680 N NE    . ARG B 102 ? 0.8134 0.5384 0.6294 0.1604  0.1276  0.1082  74  ARG B NE    
2681 C CZ    . ARG B 102 ? 0.8255 0.5357 0.6333 0.1631  0.1394  0.1080  74  ARG B CZ    
2682 N NH1   . ARG B 102 ? 0.7643 0.4684 0.5681 0.1653  0.1519  0.1030  74  ARG B NH1   
2683 N NH2   . ARG B 102 ? 0.8762 0.5765 0.6787 0.1637  0.1387  0.1129  74  ARG B NH2   
2684 N N     . LEU B 103 ? 0.6278 0.3910 0.4398 0.1457  0.1306  0.0596  75  LEU B N     
2685 C CA    . LEU B 103 ? 0.6702 0.4476 0.4872 0.1447  0.1237  0.0573  75  LEU B CA    
2686 C C     . LEU B 103 ? 0.6153 0.3948 0.4263 0.1375  0.1197  0.0436  75  LEU B C     
2687 O O     . LEU B 103 ? 0.6698 0.4396 0.4715 0.1331  0.1254  0.0342  75  LEU B O     
2688 C CB    . LEU B 103 ? 0.5525 0.3331 0.3685 0.1485  0.1318  0.0570  75  LEU B CB    
2689 C CG    . LEU B 103 ? 0.5227 0.3051 0.3466 0.1566  0.1358  0.0713  75  LEU B CG    
2690 C CD1   . LEU B 103 ? 0.5479 0.3299 0.3666 0.1603  0.1464  0.0683  75  LEU B CD1   
2691 C CD2   . LEU B 103 ? 0.5513 0.3479 0.3898 0.1587  0.1242  0.0832  75  LEU B CD2   
2692 N N     . PRO B 104 ? 0.6126 0.4046 0.4291 0.1364  0.1101  0.0427  76  PRO B N     
2693 C CA    . PRO B 104 ? 0.6092 0.4053 0.4208 0.1308  0.1072  0.0296  76  PRO B CA    
2694 C C     . PRO B 104 ? 0.6828 0.4778 0.4862 0.1286  0.1165  0.0190  76  PRO B C     
2695 O O     . PRO B 104 ? 0.7309 0.5238 0.5326 0.1322  0.1239  0.0218  76  PRO B O     
2696 C CB    . PRO B 104 ? 0.6085 0.4182 0.4288 0.1320  0.0957  0.0335  76  PRO B CB    
2697 C CG    . PRO B 104 ? 0.6275 0.4380 0.4571 0.1364  0.0906  0.0483  76  PRO B CG    
2698 C CD    . PRO B 104 ? 0.6219 0.4249 0.4502 0.1402  0.1010  0.0542  76  PRO B CD    
2699 N N     . ALA B 105 ? 0.6405 0.4372 0.4388 0.1226  0.1159  0.0065  77  ALA B N     
2700 C CA    . ALA B 105 ? 0.6397 0.4360 0.4301 0.1191  0.1235  -0.0048 77  ALA B CA    
2701 C C     . ALA B 105 ? 0.6541 0.4620 0.4465 0.1221  0.1214  -0.0039 77  ALA B C     
2702 O O     . ALA B 105 ? 0.6596 0.4790 0.4596 0.1245  0.1119  0.0011  77  ALA B O     
2703 C CB    . ALA B 105 ? 0.6877 0.4866 0.4747 0.1118  0.1220  -0.0176 77  ALA B CB    
2704 N N     . GLY B 106 ? 0.7055 0.5093 0.4900 0.1220  0.1303  -0.0088 78  GLY B N     
2705 C CA    . GLY B 106 ? 0.7152 0.5289 0.4992 0.1250  0.1295  -0.0084 78  GLY B CA    
2706 C C     . GLY B 106 ? 0.7016 0.5182 0.4922 0.1329  0.1288  0.0060  78  GLY B C     
2707 O O     . GLY B 106 ? 0.7254 0.5510 0.5159 0.1360  0.1278  0.0079  78  GLY B O     
2708 N N     . THR B 107 ? 0.7126 0.5227 0.5092 0.1364  0.1294  0.0165  79  THR B N     
2709 C CA    . THR B 107 ? 0.6410 0.4552 0.4462 0.1437  0.1288  0.0312  79  THR B CA    
2710 C C     . THR B 107 ? 0.6266 0.4317 0.4252 0.1482  0.1417  0.0330  79  THR B C     
2711 O O     . THR B 107 ? 0.6434 0.4348 0.4376 0.1483  0.1494  0.0323  79  THR B O     
2712 C CB    . THR B 107 ? 0.6223 0.4345 0.4372 0.1451  0.1227  0.0418  79  THR B CB    
2713 O OG1   . THR B 107 ? 0.6511 0.4698 0.4702 0.1410  0.1112  0.0391  79  THR B OG1   
2714 C CG2   . THR B 107 ? 0.5851 0.4037 0.4108 0.1519  0.1214  0.0574  79  THR B CG2   
2715 N N     . ARG B 108 ? 0.6422 0.4542 0.4395 0.1523  0.1444  0.0355  80  ARG B N     
2716 C CA    . ARG B 108 ? 0.6267 0.4304 0.4175 0.1578  0.1570  0.0376  80  ARG B CA    
2717 C C     . ARG B 108 ? 0.5931 0.3973 0.3953 0.1653  0.1588  0.0541  80  ARG B C     
2718 O O     . ARG B 108 ? 0.5359 0.3510 0.3515 0.1668  0.1496  0.0647  80  ARG B O     
2719 C CB    . ARG B 108 ? 0.6350 0.4462 0.4190 0.1597  0.1595  0.0342  80  ARG B CB    
2720 C CG    . ARG B 108 ? 0.7074 0.5156 0.4773 0.1529  0.1610  0.0172  80  ARG B CG    
2721 C CD    . ARG B 108 ? 0.8048 0.6229 0.5685 0.1547  0.1608  0.0147  80  ARG B CD    
2722 N NE    . ARG B 108 ? 0.9663 0.8013 0.7411 0.1560  0.1494  0.0225  80  ARG B NE    
2723 C CZ    . ARG B 108 ? 1.0589 0.9053 0.8300 0.1547  0.1440  0.0182  80  ARG B CZ    
2724 N NH1   . ARG B 108 ? 1.0014 0.8456 0.7579 0.1517  0.1482  0.0057  80  ARG B NH1   
2725 N NH2   . ARG B 108 ? 1.0238 0.8837 0.8057 0.1564  0.1339  0.0266  80  ARG B NH2   
2726 N N     . LEU B 109 ? 0.6724 0.4644 0.4695 0.1702  0.1709  0.0561  81  LEU B N     
2727 C CA    . LEU B 109 ? 0.6058 0.3976 0.4136 0.1779  0.1742  0.0715  81  LEU B CA    
2728 C C     . LEU B 109 ? 0.5675 0.3590 0.3721 0.1861  0.1856  0.0762  81  LEU B C     
2729 O O     . LEU B 109 ? 0.5826 0.3638 0.3720 0.1861  0.1953  0.0659  81  LEU B O     
2730 C CB    . LEU B 109 ? 0.5624 0.3390 0.3683 0.1776  0.1786  0.0717  81  LEU B CB    
2731 C CG    . LEU B 109 ? 0.5650 0.3404 0.3815 0.1860  0.1826  0.0874  81  LEU B CG    
2732 C CD1   . LEU B 109 ? 0.5484 0.3406 0.3830 0.1872  0.1704  0.1011  81  LEU B CD1   
2733 C CD2   . LEU B 109 ? 0.5741 0.3328 0.3858 0.1854  0.1873  0.0861  81  LEU B CD2   
2734 N N     . VAL B 110 ? 0.5617 0.3645 0.3804 0.1930  0.1844  0.0919  82  VAL B N     
2735 C CA    . VAL B 110 ? 0.5727 0.3768 0.3908 0.2022  0.1957  0.0990  82  VAL B CA    
2736 C C     . VAL B 110 ? 0.5736 0.3773 0.4049 0.2096  0.1994  0.1142  82  VAL B C     
2737 O O     . VAL B 110 ? 0.5597 0.3747 0.4076 0.2091  0.1895  0.1257  82  VAL B O     
2738 C CB    . VAL B 110 ? 0.5655 0.3871 0.3892 0.2040  0.1916  0.1047  82  VAL B CB    
2739 C CG1   . VAL B 110 ? 0.5787 0.4012 0.4005 0.2139  0.2046  0.1119  82  VAL B CG1   
2740 C CG2   . VAL B 110 ? 0.5642 0.3874 0.3755 0.1968  0.1864  0.0904  82  VAL B CG2   
2741 N N     . ALA B 111 ? 0.5909 0.3814 0.4148 0.2164  0.2135  0.1142  83  ALA B N     
2742 C CA    . ALA B 111 ? 0.5944 0.3841 0.4302 0.2249  0.2186  0.1286  83  ALA B CA    
2743 C C     . ALA B 111 ? 0.6069 0.3991 0.4427 0.2357  0.2317  0.1358  83  ALA B C     
2744 O O     . ALA B 111 ? 0.6226 0.4043 0.4413 0.2374  0.2422  0.1255  83  ALA B O     
2745 C CB    . ALA B 111 ? 0.6057 0.3752 0.4331 0.2243  0.2241  0.1233  83  ALA B CB    
2746 N N     . CYS B 112 ? 0.6009 0.4073 0.4558 0.2430  0.2312  0.1535  84  CYS B N     
2747 C CA    . CYS B 112 ? 0.6116 0.4234 0.4693 0.2540  0.2436  0.1624  84  CYS B CA    
2748 C C     . CYS B 112 ? 0.6960 0.5124 0.5689 0.2605  0.2474  0.1773  84  CYS B C     
2749 O O     . CYS B 112 ? 0.7434 0.5654 0.6286 0.2552  0.2375  0.1823  84  CYS B O     
2750 C CB    . CYS B 112 ? 0.6003 0.4333 0.4678 0.2537  0.2380  0.1697  84  CYS B CB    
2751 S SG    . CYS B 112 ? 0.5741 0.4273 0.4647 0.2459  0.2176  0.1807  84  CYS B SG    
2752 N N     . ASP B 113 ? 0.6735 0.4911 0.5448 0.2683  0.2603  0.1827  85  ASP B N     
2753 C CA    . ASP B 113 ? 0.6776 0.5038 0.5629 0.2726  0.2646  0.1957  85  ASP B CA    
2754 C C     . ASP B 113 ? 0.7165 0.5501 0.6024 0.2815  0.2767  0.2036  85  ASP B C     
2755 O O     . ASP B 113 ? 0.7477 0.5680 0.6142 0.2838  0.2850  0.1947  85  ASP B O     
2756 C CB    . ASP B 113 ? 0.6927 0.4983 0.5665 0.2721  0.2705  0.1896  85  ASP B CB    
2757 C CG    . ASP B 113 ? 0.7305 0.5486 0.6235 0.2728  0.2672  0.2013  85  ASP B CG    
2758 O OD1   . ASP B 113 ? 0.7325 0.5577 0.6363 0.2656  0.2538  0.2019  85  ASP B OD1   
2759 O OD2   . ASP B 113 ? 0.7643 0.5852 0.6613 0.2801  0.2774  0.2096  85  ASP B OD2   
2760 N N     . ILE B 114 ? 0.7407 0.5963 0.6489 0.2850  0.2767  0.2194  86  ILE B N     
2761 C CA    . ILE B 114 ? 0.6513 0.5146 0.5611 0.2938  0.2887  0.2287  86  ILE B CA    
2762 C C     . ILE B 114 ? 0.6787 0.5203 0.5707 0.3000  0.3027  0.2252  86  ILE B C     
2763 O O     . ILE B 114 ? 0.6956 0.5335 0.5790 0.3066  0.3128  0.2275  86  ILE B O     
2764 C CB    . ILE B 114 ? 0.6378 0.5317 0.5780 0.2950  0.2849  0.2461  86  ILE B CB    
2765 C CG1   . ILE B 114 ? 0.6474 0.5523 0.5900 0.3033  0.2959  0.2563  86  ILE B CG1   
2766 C CG2   . ILE B 114 ? 0.6418 0.5376 0.5928 0.2962  0.2863  0.2519  86  ILE B CG2   
2767 C CD1   . ILE B 114 ? 0.6692 0.6044 0.6423 0.3044  0.2940  0.2736  86  ILE B CD1   
2768 N N     . SER B 115 ? 0.6875 0.5135 0.5732 0.2974  0.3027  0.2194  87  SER B N     
2769 C CA    . SER B 115 ? 0.7116 0.5158 0.5812 0.3023  0.3148  0.2161  87  SER B CA    
2770 C C     . SER B 115 ? 0.7274 0.5043 0.5690 0.2982  0.3173  0.1977  87  SER B C     
2771 O O     . SER B 115 ? 0.7734 0.5402 0.6071 0.2900  0.3100  0.1858  87  SER B O     
2772 C CB    . SER B 115 ? 0.7729 0.5734 0.6488 0.3011  0.3135  0.2184  87  SER B CB    
2773 O OG    . SER B 115 ? 0.8705 0.6449 0.7271 0.3040  0.3240  0.2120  87  SER B OG    
2774 N N     . PRO B 116 ? 0.7494 0.5148 0.5763 0.3026  0.3265  0.1938  88  PRO B N     
2775 C CA    . PRO B 116 ? 0.7655 0.5065 0.5670 0.2964  0.3275  0.1743  88  PRO B CA    
2776 C C     . PRO B 116 ? 0.7957 0.5127 0.5849 0.2927  0.3305  0.1657  88  PRO B C     
2777 O O     . PRO B 116 ? 0.7880 0.4872 0.5594 0.2842  0.3284  0.1489  88  PRO B O     
2778 C CB    . PRO B 116 ? 0.7866 0.5243 0.5785 0.3030  0.3366  0.1744  88  PRO B CB    
2779 C CG    . PRO B 116 ? 0.7756 0.5392 0.5888 0.3115  0.3382  0.1936  88  PRO B CG    
2780 C CD    . PRO B 116 ? 0.7599 0.5362 0.5935 0.3124  0.3351  0.2064  88  PRO B CD    
2781 N N     . GLU B 117 ? 0.8112 0.5284 0.6097 0.2981  0.3353  0.1769  89  GLU B N     
2782 C CA    . GLU B 117 ? 0.8253 0.5202 0.6127 0.2947  0.3381  0.1699  89  GLU B CA    
2783 C C     . GLU B 117 ? 0.8069 0.5006 0.5957 0.2850  0.3276  0.1626  89  GLU B C     
2784 O O     . GLU B 117 ? 0.8175 0.4897 0.5907 0.2778  0.3276  0.1496  89  GLU B O     
2785 C CB    . GLU B 117 ? 0.8502 0.5484 0.6483 0.3035  0.3457  0.1844  89  GLU B CB    
2786 C CG    . GLU B 117 ? 0.9165 0.6172 0.7151 0.3143  0.3568  0.1935  89  GLU B CG    
2787 C CD    . GLU B 117 ? 0.9421 0.6724 0.7607 0.3196  0.3545  0.2075  89  GLU B CD    
2788 O OE1   . GLU B 117 ? 0.9833 0.7363 0.8237 0.3193  0.3481  0.2184  89  GLU B OE1   
2789 O OE2   . GLU B 117 ? 0.9463 0.6778 0.7593 0.3235  0.3588  0.2071  89  GLU B OE2   
2790 N N     . MET B 118 ? 0.7954 0.5121 0.6030 0.2843  0.3184  0.1708  90  MET B N     
2791 C CA    . MET B 118 ? 0.7363 0.4526 0.5451 0.2753  0.3075  0.1635  90  MET B CA    
2792 C C     . MET B 118 ? 0.7365 0.4418 0.5286 0.2667  0.3036  0.1462  90  MET B C     
2793 O O     . MET B 118 ? 0.7391 0.4287 0.5197 0.2583  0.3007  0.1339  90  MET B O     
2794 C CB    . MET B 118 ? 0.7149 0.4592 0.5481 0.2759  0.2971  0.1753  90  MET B CB    
2795 C CG    . MET B 118 ? 0.7201 0.4789 0.5728 0.2806  0.2967  0.1899  90  MET B CG    
2796 S SD    . MET B 118 ? 0.7174 0.4556 0.5613 0.2780  0.2988  0.1853  90  MET B SD    
2797 C CE    . MET B 118 ? 0.7014 0.4670 0.5748 0.2806  0.2906  0.2015  90  MET B CE    
2798 N N     . VAL B 119 ? 0.7340 0.4490 0.5249 0.2683  0.3035  0.1450  91  VAL B N     
2799 C CA    . VAL B 119 ? 0.7325 0.4422 0.5094 0.2596  0.2986  0.1285  91  VAL B CA    
2800 C C     . VAL B 119 ? 0.7566 0.4408 0.5117 0.2535  0.3038  0.1131  91  VAL B C     
2801 O O     . VAL B 119 ? 0.7551 0.4306 0.4996 0.2430  0.2985  0.0983  91  VAL B O     
2802 C CB    . VAL B 119 ? 0.7281 0.4538 0.5075 0.2634  0.2985  0.1314  91  VAL B CB    
2803 C CG1   . VAL B 119 ? 0.7239 0.4483 0.4905 0.2539  0.2919  0.1151  91  VAL B CG1   
2804 C CG2   . VAL B 119 ? 0.7061 0.4573 0.5091 0.2697  0.2942  0.1486  91  VAL B CG2   
2805 N N     . ASP B 120 ? 0.7797 0.4523 0.5287 0.2597  0.3143  0.1164  92  ASP B N     
2806 C CA    . ASP B 120 ? 0.8046 0.4523 0.5337 0.2541  0.3196  0.1025  92  ASP B CA    
2807 C C     . ASP B 120 ? 0.8061 0.4390 0.5324 0.2478  0.3183  0.0983  92  ASP B C     
2808 O O     . ASP B 120 ? 0.8166 0.4332 0.5285 0.2379  0.3174  0.0833  92  ASP B O     
2809 C CB    . ASP B 120 ? 0.8713 0.5097 0.5949 0.2634  0.3315  0.1082  92  ASP B CB    
2810 C CG    . ASP B 120 ? 0.8563 0.5031 0.5757 0.2672  0.3337  0.1070  92  ASP B CG    
2811 O OD1   . ASP B 120 ? 0.8240 0.4797 0.5404 0.2607  0.3262  0.0983  92  ASP B OD1   
2812 O OD2   . ASP B 120 ? 1.0031 0.6478 0.7218 0.2768  0.3430  0.1149  92  ASP B OD2   
2813 N N     . PHE B 121 ? 0.7961 0.4356 0.5364 0.2530  0.3180  0.1117  93  PHE B N     
2814 C CA    . PHE B 121 ? 0.7971 0.4239 0.5352 0.2476  0.3166  0.1090  93  PHE B CA    
2815 C C     . PHE B 121 ? 0.7781 0.4086 0.5160 0.2369  0.3057  0.0989  93  PHE B C     
2816 O O     . PHE B 121 ? 0.7843 0.3993 0.5129 0.2283  0.3048  0.0892  93  PHE B O     
2817 C CB    . PHE B 121 ? 0.7910 0.4273 0.5451 0.2562  0.3184  0.1261  93  PHE B CB    
2818 C CG    . PHE B 121 ? 0.7966 0.4188 0.5472 0.2524  0.3187  0.1248  93  PHE B CG    
2819 C CD1   . PHE B 121 ? 0.7781 0.4049 0.5338 0.2456  0.3092  0.1222  93  PHE B CD1   
2820 C CD2   . PHE B 121 ? 0.8215 0.4257 0.5636 0.2559  0.3289  0.1265  93  PHE B CD2   
2821 C CE1   . PHE B 121 ? 0.7842 0.3983 0.5362 0.2421  0.3097  0.1213  93  PHE B CE1   
2822 C CE2   . PHE B 121 ? 0.8275 0.4191 0.5662 0.2525  0.3296  0.1257  93  PHE B CE2   
2823 C CZ    . PHE B 121 ? 0.8087 0.4055 0.5524 0.2456  0.3200  0.1232  93  PHE B CZ    
2824 N N     . CYS B 122 ? 0.7559 0.4067 0.5040 0.2371  0.2978  0.1012  94  CYS B N     
2825 C CA    . CYS B 122 ? 0.7374 0.3932 0.4863 0.2280  0.2873  0.0927  94  CYS B CA    
2826 C C     . CYS B 122 ? 0.7460 0.3908 0.4782 0.2166  0.2857  0.0737  94  CYS B C     
2827 O O     . CYS B 122 ? 0.7478 0.3844 0.4746 0.2070  0.2815  0.0638  94  CYS B O     
2828 C CB    . CYS B 122 ? 0.7134 0.3937 0.4774 0.2319  0.2798  0.1004  94  CYS B CB    
2829 S SG    . CYS B 122 ? 0.6978 0.3960 0.4858 0.2420  0.2771  0.1220  94  CYS B SG    
2830 N N     . ARG B 123 ? 0.7562 0.4019 0.4806 0.2172  0.2888  0.0684  95  ARG B N     
2831 C CA    . ARG B 123 ? 0.7625 0.4027 0.4729 0.2063  0.2856  0.0507  95  ARG B CA    
2832 C C     . ARG B 123 ? 0.7834 0.4005 0.4802 0.1982  0.2900  0.0395  95  ARG B C     
2833 O O     . ARG B 123 ? 0.8836 0.4967 0.5702 0.1875  0.2865  0.0244  95  ARG B O     
2834 C CB    . ARG B 123 ? 0.7707 0.4173 0.4755 0.2099  0.2882  0.0487  95  ARG B CB    
2835 C CG    . ARG B 123 ? 0.7496 0.4199 0.4658 0.2149  0.2825  0.0566  95  ARG B CG    
2836 C CD    . ARG B 123 ? 0.7597 0.4355 0.4686 0.2181  0.2854  0.0543  95  ARG B CD    
2837 N NE    . ARG B 123 ? 0.7405 0.4389 0.4603 0.2230  0.2806  0.0627  95  ARG B NE    
2838 C CZ    . ARG B 123 ? 0.7444 0.4525 0.4673 0.2320  0.2852  0.0719  95  ARG B CZ    
2839 N NH1   . ARG B 123 ? 0.7670 0.4643 0.4827 0.2376  0.2948  0.0737  95  ARG B NH1   
2840 N NH2   . ARG B 123 ? 0.7262 0.4551 0.4596 0.2355  0.2803  0.0798  95  ARG B NH2   
2841 N N     . GLN B 124 ? 0.8068 0.4096 0.5035 0.2029  0.2975  0.0469  96  GLN B N     
2842 C CA    . GLN B 124 ? 0.8183 0.3984 0.5028 0.1954  0.3021  0.0378  96  GLN B CA    
2843 C C     . GLN B 124 ? 0.8327 0.4085 0.5216 0.1904  0.2987  0.0389  96  GLN B C     
2844 O O     . GLN B 124 ? 0.8846 0.4520 0.5662 0.1788  0.2958  0.0266  96  GLN B O     
2845 C CB    . GLN B 124 ? 0.8717 0.4358 0.5503 0.2038  0.3140  0.0443  96  GLN B CB    
2846 C CG    . GLN B 124 ? 1.0136 0.5736 0.6816 0.2059  0.3191  0.0384  96  GLN B CG    
2847 C CD    . GLN B 124 ? 1.1452 0.6895 0.8079 0.2153  0.3312  0.0459  96  GLN B CD    
2848 O OE1   . GLN B 124 ? 1.1254 0.6571 0.7885 0.2172  0.3361  0.0516  96  GLN B OE1   
2849 N NE2   . GLN B 124 ? 1.2170 0.7620 0.8742 0.2215  0.3363  0.0461  96  GLN B NE2   
2850 N N     . HIS B 125 ? 0.8122 0.3945 0.5132 0.1989  0.2988  0.0537  97  HIS B N     
2851 C CA    . HIS B 125 ? 0.8306 0.4060 0.5342 0.1960  0.2975  0.0565  97  HIS B CA    
2852 C C     . HIS B 125 ? 0.8051 0.3955 0.5178 0.1917  0.2866  0.0558  97  HIS B C     
2853 O O     . HIS B 125 ? 0.8673 0.4504 0.5781 0.1852  0.2842  0.0523  97  HIS B O     
2854 C CB    . HIS B 125 ? 0.8304 0.4039 0.5412 0.2075  0.3039  0.0729  97  HIS B CB    
2855 C CG    . HIS B 125 ? 0.8525 0.4093 0.5537 0.2122  0.3154  0.0741  97  HIS B CG    
2856 N ND1   . HIS B 125 ? 0.8758 0.4370 0.5769 0.2199  0.3203  0.0777  97  HIS B ND1   
2857 C CD2   . HIS B 125 ? 0.8997 0.4347 0.5906 0.2105  0.3233  0.0722  97  HIS B CD2   
2858 C CE1   . HIS B 125 ? 0.9190 0.4616 0.6100 0.2230  0.3307  0.0777  97  HIS B CE1   
2859 N NE2   . HIS B 125 ? 0.9564 0.4828 0.6412 0.2173  0.3326  0.0745  97  HIS B NE2   
2860 N N     . ASN B 126 ? 0.7484 0.3590 0.4705 0.1954  0.2803  0.0591  98  ASN B N     
2861 C CA    . ASN B 126 ? 0.7640 0.3880 0.4935 0.1912  0.2698  0.0571  98  ASN B CA    
2862 C C     . ASN B 126 ? 0.7464 0.3801 0.4715 0.1841  0.2642  0.0448  98  ASN B C     
2863 O O     . ASN B 126 ? 0.7435 0.3951 0.4773 0.1866  0.2573  0.0478  98  ASN B O     
2864 C CB    . ASN B 126 ? 0.7315 0.3723 0.4779 0.2016  0.2658  0.0732  98  ASN B CB    
2865 C CG    . ASN B 126 ? 0.7672 0.4018 0.5193 0.2069  0.2685  0.0849  98  ASN B CG    
2866 O OD1   . ASN B 126 ? 0.7790 0.4208 0.5408 0.2167  0.2718  0.0986  98  ASN B OD1   
2867 N ND2   . ASN B 126 ? 0.7982 0.4209 0.5447 0.2000  0.2670  0.0798  98  ASN B ND2   
2868 N N     . ALA B 127 ? 0.7787 0.4013 0.4908 0.1754  0.2668  0.0312  99  ALA B N     
2869 C CA    . ALA B 127 ? 0.7992 0.4312 0.5064 0.1681  0.2613  0.0187  99  ALA B CA    
2870 C C     . ALA B 127 ? 0.8503 0.4890 0.5594 0.1584  0.2523  0.0104  99  ALA B C     
2871 O O     . ALA B 127 ? 0.8962 0.5233 0.6014 0.1508  0.2529  0.0048  99  ALA B O     
2872 C CB    . ALA B 127 ? 0.8841 0.5021 0.5772 0.1620  0.2668  0.0071  99  ALA B CB    
2873 N N     . LEU B 128 ? 0.8673 0.5245 0.5823 0.1590  0.2445  0.0101  100 LEU B N     
2874 C CA    . LEU B 128 ? 0.8455 0.5112 0.5620 0.1503  0.2357  0.0016  100 LEU B CA    
2875 C C     . LEU B 128 ? 0.8105 0.4910 0.5245 0.1472  0.2302  -0.0064 100 LEU B C     
2876 O O     . LEU B 128 ? 0.8377 0.5338 0.5586 0.1528  0.2251  -0.0007 100 LEU B O     
2877 C CB    . LEU B 128 ? 0.7999 0.4732 0.5276 0.1558  0.2308  0.0118  100 LEU B CB    
2878 C CG    . LEU B 128 ? 0.7610 0.4417 0.4903 0.1479  0.2221  0.0042  100 LEU B CG    
2879 C CD1   . LEU B 128 ? 0.8259 0.4950 0.5470 0.1355  0.2234  -0.0084 100 LEU B CD1   
2880 C CD2   . LEU B 128 ? 0.8107 0.4969 0.5517 0.1521  0.2158  0.0157  100 LEU B CD2   
2881 N N     . PRO B 129 ? 0.7698 0.4455 0.4735 0.1387  0.2312  -0.0195 101 PRO B N     
2882 C CA    . PRO B 129 ? 0.7911 0.4805 0.4909 0.1364  0.2264  -0.0271 101 PRO B CA    
2883 C C     . PRO B 129 ? 0.8217 0.5272 0.5270 0.1326  0.2165  -0.0306 101 PRO B C     
2884 O O     . PRO B 129 ? 0.8404 0.5442 0.5488 0.1265  0.2132  -0.0341 101 PRO B O     
2885 C CB    . PRO B 129 ? 0.8770 0.5559 0.5648 0.1265  0.2292  -0.0414 101 PRO B CB    
2886 C CG    . PRO B 129 ? 0.8740 0.5321 0.5587 0.1278  0.2382  -0.0377 101 PRO B CG    
2887 C CD    . PRO B 129 ? 0.8282 0.4851 0.5228 0.1318  0.2375  -0.0271 101 PRO B CD    
2888 N N     . GLY B 130 ? 0.7978 0.5187 0.5038 0.1366  0.2122  -0.0292 102 GLY B N     
2889 C CA    . GLY B 130 ? 0.8618 0.5984 0.5724 0.1349  0.2030  -0.0314 102 GLY B CA    
2890 C C     . GLY B 130 ? 0.8353 0.5803 0.5600 0.1414  0.1977  -0.0179 102 GLY B C     
2891 O O     . GLY B 130 ? 0.8529 0.6154 0.5863 0.1399  0.1864  -0.0159 102 GLY B O     
2892 N N     . THR B 131 ? 0.7990 0.5341 0.5289 0.1469  0.2028  -0.0077 103 THR B N     
2893 C CA    . THR B 131 ? 0.7550 0.4998 0.5013 0.1508  0.1948  0.0062  103 THR B CA    
2894 C C     . THR B 131 ? 0.7378 0.4851 0.4913 0.1618  0.1990  0.0214  103 THR B C     
2895 O O     . THR B 131 ? 0.7778 0.5414 0.5420 0.1654  0.1917  0.0304  103 THR B O     
2896 C CB    . THR B 131 ? 0.7766 0.5104 0.5249 0.1471  0.1948  0.0062  103 THR B CB    
2897 O OG1   . THR B 131 ? 0.8835 0.6183 0.6276 0.1369  0.1901  -0.0067 103 THR B OG1   
2898 C CG2   . THR B 131 ? 0.6932 0.4358 0.4571 0.1513  0.1864  0.0206  103 THR B CG2   
2899 N N     . ILE B 132 ? 0.7455 0.4772 0.4941 0.1675  0.2109  0.0248  104 ILE B N     
2900 C CA    . ILE B 132 ? 0.6404 0.3747 0.3978 0.1785  0.2156  0.0403  104 ILE B CA    
2901 C C     . ILE B 132 ? 0.6346 0.3665 0.3821 0.1844  0.2258  0.0384  104 ILE B C     
2902 O O     . ILE B 132 ? 0.6512 0.3709 0.3849 0.1792  0.2310  0.0269  104 ILE B O     
2903 C CB    . ILE B 132 ? 0.6278 0.3471 0.3873 0.1826  0.2223  0.0471  104 ILE B CB    
2904 C CG1   . ILE B 132 ? 0.6639 0.3843 0.4305 0.1763  0.2126  0.0478  104 ILE B CG1   
2905 C CG2   . ILE B 132 ? 0.6273 0.3524 0.3987 0.1942  0.2262  0.0642  104 ILE B CG2   
2906 C CD1   . ILE B 132 ? 0.6847 0.3899 0.4517 0.1797  0.2186  0.0540  104 ILE B CD1   
2907 N N     . THR B 133 ? 0.6279 0.3741 0.3853 0.1921  0.2247  0.0507  105 THR B N     
2908 C CA    . THR B 133 ? 0.6426 0.3874 0.3922 0.1999  0.2354  0.0522  105 THR B CA    
2909 C C     . THR B 133 ? 0.6418 0.3911 0.4052 0.2112  0.2405  0.0702  105 THR B C     
2910 O O     . THR B 133 ? 0.6239 0.3876 0.4057 0.2122  0.2313  0.0827  105 THR B O     
2911 C CB    . THR B 133 ? 0.6364 0.3971 0.3837 0.1981  0.2294  0.0493  105 THR B CB    
2912 O OG1   . THR B 133 ? 0.6272 0.4078 0.3934 0.1998  0.2187  0.0629  105 THR B OG1   
2913 C CG2   . THR B 133 ? 0.6353 0.3947 0.3715 0.1868  0.2226  0.0325  105 THR B CG2   
2914 N N     . TYR B 134 ? 0.6605 0.3998 0.4180 0.2158  0.2506  0.0722  106 TYR B N     
2915 C CA    . TYR B 134 ? 0.6628 0.4055 0.4327 0.2270  0.2571  0.0889  106 TYR B CA    
2916 C C     . TYR B 134 ? 0.6686 0.4217 0.4386 0.2337  0.2619  0.0951  106 TYR B C     
2917 O O     . TYR B 134 ? 0.6834 0.4300 0.4382 0.2302  0.2647  0.0847  106 TYR B O     
2918 C CB    . TYR B 134 ? 0.6808 0.4040 0.4452 0.2274  0.2646  0.0886  106 TYR B CB    
2919 C CG    . TYR B 134 ? 0.6760 0.3891 0.4411 0.2217  0.2607  0.0849  106 TYR B CG    
2920 C CD1   . TYR B 134 ? 0.6618 0.3823 0.4432 0.2266  0.2567  0.0974  106 TYR B CD1   
2921 C CD2   . TYR B 134 ? 0.6863 0.3831 0.4365 0.2110  0.2602  0.0693  106 TYR B CD2   
2922 C CE1   . TYR B 134 ? 0.6587 0.3695 0.4399 0.2216  0.2527  0.0942  106 TYR B CE1   
2923 C CE2   . TYR B 134 ? 0.6828 0.3706 0.4334 0.2057  0.2572  0.0664  106 TYR B CE2   
2924 C CZ    . TYR B 134 ? 0.6695 0.3637 0.4346 0.2114  0.2538  0.0788  106 TYR B CZ    
2925 O OH    . TYR B 134 ? 0.6673 0.3521 0.4317 0.2063  0.2505  0.0760  106 TYR B OH    
2926 N N     . GLU B 135 ? 0.6576 0.4273 0.4455 0.2431  0.2626  0.1121  107 GLU B N     
2927 C CA    . GLU B 135 ? 0.6604 0.4433 0.4510 0.2496  0.2666  0.1199  107 GLU B CA    
2928 C C     . GLU B 135 ? 0.6626 0.4526 0.4694 0.2602  0.2732  0.1382  107 GLU B C     
2929 O O     . GLU B 135 ? 0.6595 0.4466 0.4769 0.2623  0.2731  0.1456  107 GLU B O     
2930 C CB    . GLU B 135 ? 0.6408 0.4441 0.4398 0.2477  0.2572  0.1230  107 GLU B CB    
2931 C CG    . GLU B 135 ? 0.6331 0.4340 0.4219 0.2353  0.2460  0.1076  107 GLU B CG    
2932 C CD    . GLU B 135 ? 0.6512 0.4400 0.4158 0.2319  0.2518  0.0907  107 GLU B CD    
2933 O OE1   . GLU B 135 ? 0.6686 0.4525 0.4260 0.2355  0.2592  0.0913  107 GLU B OE1   
2934 O OE2   . GLU B 135 ? 0.6478 0.4329 0.4028 0.2227  0.2450  0.0769  107 GLU B OE2   
2935 N N     . LEU B 136 ? 0.6687 0.4689 0.4773 0.2664  0.2786  0.1459  108 LEU B N     
2936 C CA    . LEU B 136 ? 0.6687 0.4814 0.4952 0.2764  0.2843  0.1649  108 LEU B CA    
2937 C C     . LEU B 136 ? 0.6470 0.4856 0.4943 0.2793  0.2781  0.1782  108 LEU B C     
2938 O O     . LEU B 136 ? 0.6425 0.4892 0.4843 0.2773  0.2755  0.1740  108 LEU B O     
2939 C CB    . LEU B 136 ? 0.6922 0.4984 0.5077 0.2819  0.2949  0.1654  108 LEU B CB    
2940 C CG    . LEU B 136 ? 0.7159 0.4996 0.5189 0.2833  0.3034  0.1603  108 LEU B CG    
2941 C CD1   . LEU B 136 ? 0.7396 0.5162 0.5287 0.2876  0.3121  0.1570  108 LEU B CD1   
2942 C CD2   . LEU B 136 ? 0.7132 0.5020 0.5339 0.2898  0.3068  0.1761  108 LEU B CD2   
2943 N N     . LEU B 137 ? 0.6344 0.4863 0.5057 0.2827  0.2743  0.1943  109 LEU B N     
2944 C CA    . LEU B 137 ? 0.6149 0.4909 0.5087 0.2825  0.2647  0.2085  109 LEU B CA    
2945 C C     . LEU B 137 ? 0.6077 0.5002 0.5259 0.2824  0.2620  0.2248  109 LEU B C     
2946 O O     . LEU B 137 ? 0.6071 0.4937 0.5288 0.2791  0.2593  0.2234  109 LEU B O     
2947 C CB    . LEU B 137 ? 0.5964 0.4752 0.4911 0.2690  0.2463  0.2013  109 LEU B CB    
2948 C CG    . LEU B 137 ? 0.5776 0.4793 0.4937 0.2649  0.2336  0.2148  109 LEU B CG    
2949 C CD1   . LEU B 137 ? 0.5814 0.4936 0.4932 0.2673  0.2380  0.2168  109 LEU B CD1   
2950 C CD2   . LEU B 137 ? 0.5611 0.4624 0.4790 0.2526  0.2157  0.2082  109 LEU B CD2   
2951 N N     . ASP B 138 ? 0.6025 0.5174 0.5379 0.2850  0.2628  0.2387  110 ASP B N     
2952 C CA    . ASP B 138 ? 0.5907 0.5287 0.5545 0.2816  0.2568  0.2523  110 ASP B CA    
2953 C C     . ASP B 138 ? 0.5681 0.5227 0.5487 0.2700  0.2379  0.2548  110 ASP B C     
2954 O O     . ASP B 138 ? 0.5816 0.5425 0.5606 0.2689  0.2351  0.2559  110 ASP B O     
2955 C CB    . ASP B 138 ? 0.6003 0.5533 0.5739 0.2907  0.2699  0.2659  110 ASP B CB    
2956 C CG    . ASP B 138 ? 0.5908 0.5672 0.5941 0.2882  0.2654  0.2794  110 ASP B CG    
2957 O OD1   . ASP B 138 ? 0.5763 0.5579 0.5925 0.2787  0.2507  0.2783  110 ASP B OD1   
2958 O OD2   . ASP B 138 ? 0.5992 0.5886 0.6122 0.2957  0.2765  0.2914  110 ASP B OD2   
2959 N N     . VAL B 139 ? 0.5556 0.5157 0.5504 0.2611  0.2248  0.2553  111 VAL B N     
2960 C CA    . VAL B 139 ? 0.5367 0.5077 0.5439 0.2490  0.2058  0.2555  111 VAL B CA    
2961 C C     . VAL B 139 ? 0.5289 0.5245 0.5573 0.2471  0.2025  0.2683  111 VAL B C     
2962 O O     . VAL B 139 ? 0.5166 0.5194 0.5512 0.2381  0.1891  0.2681  111 VAL B O     
2963 C CB    . VAL B 139 ? 0.5282 0.4990 0.5452 0.2410  0.1934  0.2541  111 VAL B CB    
2964 C CG1   . VAL B 139 ? 0.5275 0.5169 0.5680 0.2423  0.1941  0.2672  111 VAL B CG1   
2965 C CG2   . VAL B 139 ? 0.5126 0.4857 0.5334 0.2287  0.1744  0.2498  111 VAL B CG2   
2966 N N     . VAL B 140 ? 0.5368 0.5451 0.5762 0.2553  0.2147  0.2795  112 VAL B N     
2967 C CA    . VAL B 140 ? 0.5313 0.5633 0.5911 0.2542  0.2136  0.2926  112 VAL B CA    
2968 C C     . VAL B 140 ? 0.5445 0.5755 0.5923 0.2653  0.2301  0.2953  112 VAL B C     
2969 O O     . VAL B 140 ? 0.5795 0.6269 0.6409 0.2716  0.2398  0.3079  112 VAL B O     
2970 C CB    . VAL B 140 ? 0.5293 0.5806 0.6152 0.2542  0.2136  0.3058  112 VAL B CB    
2971 C CG1   . VAL B 140 ? 0.5149 0.5714 0.6151 0.2414  0.1940  0.3051  112 VAL B CG1   
2972 C CG2   . VAL B 140 ? 0.5444 0.5868 0.6232 0.2648  0.2286  0.3061  112 VAL B CG2   
2973 N N     . GLU B 141 ? 0.6212 0.6329 0.6431 0.2681  0.2334  0.2840  113 GLU B N     
2974 C CA    . GLU B 141 ? 0.6389 0.6464 0.6450 0.2792  0.2487  0.2854  113 GLU B CA    
2975 C C     . GLU B 141 ? 0.6300 0.6573 0.6490 0.2761  0.2441  0.2946  113 GLU B C     
2976 O O     . GLU B 141 ? 0.6150 0.6459 0.6384 0.2650  0.2283  0.2916  113 GLU B O     
2977 C CB    . GLU B 141 ? 0.6462 0.6272 0.6205 0.2823  0.2516  0.2705  113 GLU B CB    
2978 C CG    . GLU B 141 ? 0.7182 0.6799 0.6709 0.2955  0.2708  0.2656  113 GLU B CG    
2979 C CD    . GLU B 141 ? 0.8053 0.7701 0.7483 0.3066  0.2853  0.2702  113 GLU B CD    
2980 O OE1   . GLU B 141 ? 0.6981 0.6774 0.6467 0.3029  0.2797  0.2763  113 GLU B OE1   
2981 O OE2   . GLU B 141 ? 1.0490 1.0002 0.9755 0.3121  0.2976  0.2653  113 GLU B OE2   
2982 N N     . PRO B 142 ? 0.6687 0.7088 0.6940 0.2855  0.2578  0.3060  114 PRO B N     
2983 C CA    . PRO B 142 ? 0.5629 0.6211 0.5995 0.2826  0.2541  0.3147  114 PRO B CA    
2984 C C     . PRO B 142 ? 0.5646 0.6106 0.5784 0.2803  0.2493  0.3054  114 PRO B C     
2985 O O     . PRO B 142 ? 0.5516 0.6058 0.5738 0.2694  0.2347  0.3057  114 PRO B O     
2986 C CB    . PRO B 142 ? 0.5780 0.6470 0.6192 0.2965  0.2735  0.3267  114 PRO B CB    
2987 C CG    . PRO B 142 ? 0.5843 0.6501 0.6302 0.3015  0.2820  0.3289  114 PRO B CG    
2988 C CD    . PRO B 142 ? 0.6806 0.7212 0.7062 0.2980  0.2763  0.3130  114 PRO B CD    
2989 N N     . ARG B 143 ? 0.6308 0.6564 0.6145 0.2899  0.2612  0.2970  115 ARG B N     
2990 C CA    . ARG B 143 ? 0.5865 0.6000 0.5444 0.2869  0.2575  0.2875  115 ARG B CA    
2991 C C     . ARG B 143 ? 0.5828 0.5763 0.5250 0.2801  0.2491  0.2694  115 ARG B C     
2992 O O     . ARG B 143 ? 0.5965 0.5727 0.5150 0.2829  0.2572  0.2540  115 ARG B O     
2993 C CB    . ARG B 143 ? 0.6084 0.6171 0.5434 0.2963  0.2745  0.2838  115 ARG B CB    
2994 C CG    . ARG B 143 ? 0.6161 0.6407 0.5689 0.3059  0.2852  0.2977  115 ARG B CG    
2995 C CD    . ARG B 143 ? 0.6389 0.6551 0.5689 0.3121  0.2946  0.2899  115 ARG B CD    
2996 N NE    . ARG B 143 ? 0.6371 0.6544 0.5524 0.3052  0.2874  0.2832  115 ARG B NE    
2997 C CZ    . ARG B 143 ? 0.6532 0.6877 0.5790 0.3039  0.2843  0.2936  115 ARG B CZ    
2998 N NH1   . ARG B 143 ? 0.7142 0.7677 0.6665 0.3083  0.2880  0.3105  115 ARG B NH1   
2999 N NH2   . ARG B 143 ? 0.6333 0.6663 0.5434 0.2977  0.2773  0.2868  115 ARG B NH2   
3000 N N     . LEU B 144 ? 0.6050 0.6013 0.5613 0.2704  0.2323  0.2708  116 LEU B N     
3001 C CA    . LEU B 144 ? 0.5680 0.5476 0.5121 0.2630  0.2231  0.2541  116 LEU B CA    
3002 C C     . LEU B 144 ? 0.5650 0.5346 0.4837 0.2587  0.2212  0.2371  116 LEU B C     
3003 O O     . LEU B 144 ? 0.5718 0.5245 0.4714 0.2573  0.2234  0.2204  116 LEU B O     
3004 C CB    . LEU B 144 ? 0.5489 0.5364 0.5135 0.2517  0.2046  0.2572  116 LEU B CB    
3005 C CG    . LEU B 144 ? 0.5320 0.5062 0.4943 0.2457  0.1957  0.2471  116 LEU B CG    
3006 C CD1   . LEU B 144 ? 0.5156 0.5022 0.4993 0.2325  0.1773  0.2495  116 LEU B CD1   
3007 C CD2   . LEU B 144 ? 0.5367 0.4922 0.4730 0.2429  0.1945  0.2284  116 LEU B CD2   
3008 N N     . GLU B 145 ? 0.5632 0.5435 0.4816 0.2567  0.2172  0.2414  117 GLU B N     
3009 C CA    . GLU B 145 ? 0.5665 0.5402 0.4635 0.2518  0.2124  0.2269  117 GLU B CA    
3010 C C     . GLU B 145 ? 0.5869 0.5481 0.4570 0.2575  0.2262  0.2134  117 GLU B C     
3011 O O     . GLU B 145 ? 0.5908 0.5440 0.4413 0.2529  0.2221  0.1983  117 GLU B O     
3012 C CB    . GLU B 145 ? 0.5623 0.5509 0.4657 0.2499  0.2065  0.2371  117 GLU B CB    
3013 C CG    . GLU B 145 ? 0.5437 0.5383 0.4639 0.2404  0.1884  0.2419  117 GLU B CG    
3014 C CD    . GLU B 145 ? 0.6232 0.6307 0.5721 0.2407  0.1857  0.2610  117 GLU B CD    
3015 O OE1   . GLU B 145 ? 0.6906 0.7103 0.6498 0.2463  0.1961  0.2717  117 GLU B OE1   
3016 O OE2   . GLU B 145 ? 0.6333 0.6424 0.5973 0.2313  0.1718  0.2591  117 GLU B OE2   
3017 N N     . ASP B 146 ? 0.6009 0.5601 0.4694 0.2674  0.2422  0.2183  118 ASP B N     
3018 C CA    . ASP B 146 ? 0.6234 0.5693 0.4655 0.2734  0.2562  0.2061  118 ASP B CA    
3019 C C     . ASP B 146 ? 0.6304 0.5564 0.4615 0.2732  0.2607  0.1923  118 ASP B C     
3020 O O     . ASP B 146 ? 0.6510 0.5632 0.4611 0.2779  0.2724  0.1818  118 ASP B O     
3021 C CB    . ASP B 146 ? 0.6382 0.5920 0.4824 0.2853  0.2727  0.2189  118 ASP B CB    
3022 C CG    . ASP B 146 ? 0.6351 0.6073 0.4865 0.2856  0.2702  0.2317  118 ASP B CG    
3023 O OD1   . ASP B 146 ? 0.6164 0.6021 0.4900 0.2799  0.2579  0.2432  118 ASP B OD1   
3024 O OD2   . ASP B 146 ? 0.6521 0.6231 0.4892 0.2896  0.2761  0.2282  118 ASP B OD2   
3025 N N     . THR B 147 ? 0.6152 0.5383 0.4595 0.2673  0.2508  0.1918  119 THR B N     
3026 C CA    . THR B 147 ? 0.6213 0.5258 0.4569 0.2668  0.2546  0.1803  119 THR B CA    
3027 C C     . THR B 147 ? 0.6186 0.5115 0.4378 0.2565  0.2450  0.1613  119 THR B C     
3028 O O     . THR B 147 ? 0.6062 0.5073 0.4274 0.2490  0.2321  0.1592  119 THR B O     
3029 C CB    . THR B 147 ? 0.6083 0.5159 0.4671 0.2670  0.2503  0.1914  119 THR B CB    
3030 O OG1   . THR B 147 ? 0.5871 0.5031 0.4594 0.2571  0.2324  0.1934  119 THR B OG1   
3031 C CG2   . THR B 147 ? 0.6317 0.5537 0.5096 0.2768  0.2589  0.2113  119 THR B CG2   
3032 N N     . VAL B 148 ? 0.6314 0.5048 0.4347 0.2563  0.2518  0.1476  120 VAL B N     
3033 C CA    . VAL B 148 ? 0.6300 0.4922 0.4188 0.2463  0.2438  0.1294  120 VAL B CA    
3034 C C     . VAL B 148 ? 0.6077 0.4747 0.4129 0.2380  0.2284  0.1315  120 VAL B C     
3035 O O     . VAL B 148 ? 0.5991 0.4671 0.3996 0.2292  0.2172  0.1217  120 VAL B O     
3036 C CB    . VAL B 148 ? 0.6500 0.4896 0.4198 0.2478  0.2554  0.1157  120 VAL B CB    
3037 C CG1   . VAL B 148 ? 0.6466 0.4753 0.4059 0.2367  0.2468  0.0986  120 VAL B CG1   
3038 C CG2   . VAL B 148 ? 0.6727 0.5059 0.4261 0.2496  0.2621  0.1101  120 VAL B CG2   
3039 N N     . VAL B 149 ? 0.5987 0.4694 0.4236 0.2408  0.2275  0.1444  121 VAL B N     
3040 C CA    . VAL B 149 ? 0.5798 0.4536 0.4190 0.2333  0.2132  0.1464  121 VAL B CA    
3041 C C     . VAL B 149 ? 0.5638 0.4538 0.4133 0.2279  0.1994  0.1518  121 VAL B C     
3042 O O     . VAL B 149 ? 0.5738 0.4632 0.4238 0.2195  0.1869  0.1447  121 VAL B O     
3043 C CB    . VAL B 149 ? 0.5758 0.4511 0.4334 0.2382  0.2153  0.1602  121 VAL B CB    
3044 C CG1   . VAL B 149 ? 0.5569 0.4373 0.4297 0.2305  0.1995  0.1640  121 VAL B CG1   
3045 C CG2   . VAL B 149 ? 0.5918 0.4484 0.4383 0.2427  0.2277  0.1536  121 VAL B CG2   
3046 N N     . TRP B 150 ? 0.5637 0.4680 0.4215 0.2330  0.2017  0.1645  122 TRP B N     
3047 C CA    . TRP B 150 ? 0.5500 0.4689 0.4184 0.2282  0.1890  0.1713  122 TRP B CA    
3048 C C     . TRP B 150 ? 0.5502 0.4665 0.4022 0.2220  0.1824  0.1567  122 TRP B C     
3049 O O     . TRP B 150 ? 0.5514 0.4729 0.4096 0.2152  0.1687  0.1560  122 TRP B O     
3050 C CB    . TRP B 150 ? 0.5528 0.4867 0.4314 0.2350  0.1947  0.1874  122 TRP B CB    
3051 C CG    . TRP B 150 ? 0.5437 0.4903 0.4278 0.2305  0.1838  0.1925  122 TRP B CG    
3052 C CD1   . TRP B 150 ? 0.5510 0.5011 0.4215 0.2312  0.1853  0.1886  122 TRP B CD1   
3053 C CD2   . TRP B 150 ? 0.5397 0.4960 0.4436 0.2248  0.1695  0.2025  122 TRP B CD2   
3054 N NE1   . TRP B 150 ? 0.5398 0.5012 0.4209 0.2266  0.1732  0.1961  122 TRP B NE1   
3055 C CE2   . TRP B 150 ? 0.5254 0.4902 0.4270 0.2224  0.1635  0.2044  122 TRP B CE2   
3056 C CE3   . TRP B 150 ? 0.5335 0.4915 0.4561 0.2213  0.1611  0.2100  122 TRP B CE3   
3057 C CZ2   . TRP B 150 ? 0.5179 0.4915 0.4353 0.2168  0.1498  0.2133  122 TRP B CZ2   
3058 C CZ3   . TRP B 150 ? 0.5131 0.4801 0.4508 0.2153  0.1471  0.2183  122 TRP B CZ3   
3059 C CH2   . TRP B 150 ? 0.5254 0.4995 0.4605 0.2131  0.1418  0.2198  122 TRP B CH2   
3060 N N     . ARG B 151 ? 0.5661 0.4741 0.3967 0.2242  0.1917  0.1448  123 ARG B N     
3061 C CA    . ARG B 151 ? 0.5681 0.4754 0.3829 0.2188  0.1859  0.1314  123 ARG B CA    
3062 C C     . ARG B 151 ? 0.5656 0.4610 0.3716 0.2111  0.1804  0.1149  123 ARG B C     
3063 O O     . ARG B 151 ? 0.5649 0.4613 0.3605 0.2057  0.1736  0.1039  123 ARG B O     
3064 C CB    . ARG B 151 ? 0.5879 0.4931 0.3831 0.2243  0.1976  0.1266  123 ARG B CB    
3065 C CG    . ARG B 151 ? 0.5903 0.5089 0.3941 0.2316  0.2027  0.1433  123 ARG B CG    
3066 C CD    . ARG B 151 ? 0.6105 0.5280 0.3938 0.2371  0.2133  0.1391  123 ARG B CD    
3067 N NE    . ARG B 151 ? 0.6135 0.5436 0.4064 0.2449  0.2201  0.1565  123 ARG B NE    
3068 C CZ    . ARG B 151 ? 0.6319 0.5630 0.4101 0.2519  0.2316  0.1574  123 ARG B CZ    
3069 N NH1   . ARG B 151 ? 0.6750 0.5948 0.4271 0.2518  0.2370  0.1416  123 ARG B NH1   
3070 N NH2   . ARG B 151 ? 0.6334 0.5771 0.4231 0.2588  0.2378  0.1747  123 ARG B NH2   
3071 N N     . ASN B 152 ? 0.5649 0.4497 0.3749 0.2106  0.1834  0.1134  124 ASN B N     
3072 C CA    . ASN B 152 ? 0.5587 0.4347 0.3656 0.2026  0.1762  0.1012  124 ASN B CA    
3073 C C     . ASN B 152 ? 0.5553 0.4397 0.3790 0.1975  0.1614  0.1074  124 ASN B C     
3074 O O     . ASN B 152 ? 0.6452 0.5250 0.4666 0.1906  0.1538  0.0973  124 ASN B O     
3075 C CB    . ASN B 152 ? 0.5858 0.4462 0.3897 0.2041  0.1852  0.0977  124 ASN B CB    
3076 C CG    . ASN B 152 ? 0.6768 0.5239 0.4598 0.2066  0.1984  0.0861  124 ASN B CG    
3077 O OD1   . ASN B 152 ? 0.8881 0.7277 0.6562 0.2004  0.1973  0.0704  124 ASN B OD1   
3078 N ND2   . ASN B 152 ? 0.6097 0.4537 0.3915 0.2156  0.2112  0.0937  124 ASN B ND2   
3079 N N     . GLY B 153 ? 0.5583 0.4547 0.3987 0.2006  0.1574  0.1235  125 GLY B N     
3080 C CA    . GLY B 153 ? 0.5472 0.4506 0.4033 0.1958  0.1434  0.1300  125 GLY B CA    
3081 C C     . GLY B 153 ? 0.5833 0.4947 0.4370 0.1917  0.1330  0.1264  125 GLY B C     
3082 O O     . GLY B 153 ? 0.6734 0.5850 0.5124 0.1916  0.1357  0.1170  125 GLY B O     
3083 N N     . PRO B 154 ? 0.5369 0.4549 0.4048 0.1883  0.1206  0.1341  126 PRO B N     
3084 C CA    . PRO B 154 ? 0.4974 0.4163 0.3829 0.1875  0.1153  0.1454  126 PRO B CA    
3085 C C     . PRO B 154 ? 0.5329 0.4402 0.4158 0.1832  0.1127  0.1363  126 PRO B C     
3086 O O     . PRO B 154 ? 0.5785 0.4791 0.4489 0.1793  0.1115  0.1217  126 PRO B O     
3087 C CB    . PRO B 154 ? 0.5154 0.4436 0.4118 0.1842  0.1023  0.1530  126 PRO B CB    
3088 C CG    . PRO B 154 ? 0.5653 0.4925 0.4484 0.1810  0.0977  0.1397  126 PRO B CG    
3089 C CD    . PRO B 154 ? 0.6100 0.5339 0.4761 0.1844  0.1098  0.1302  126 PRO B CD    
3090 N N     . PHE B 155 ? 0.4937 0.3991 0.3883 0.1839  0.1118  0.1450  127 PHE B N     
3091 C CA    . PHE B 155 ? 0.5140 0.4076 0.4050 0.1809  0.1113  0.1377  127 PHE B CA    
3092 C C     . PHE B 155 ? 0.4715 0.3656 0.3719 0.1752  0.0971  0.1400  127 PHE B C     
3093 O O     . PHE B 155 ? 0.5092 0.4120 0.4236 0.1748  0.0891  0.1521  127 PHE B O     
3094 C CB    . PHE B 155 ? 0.5148 0.4042 0.4100 0.1864  0.1214  0.1451  127 PHE B CB    
3095 C CG    . PHE B 155 ? 0.5006 0.3857 0.3841 0.1923  0.1365  0.1411  127 PHE B CG    
3096 C CD1   . PHE B 155 ? 0.5099 0.3812 0.3767 0.1910  0.1439  0.1265  127 PHE B CD1   
3097 C CD2   . PHE B 155 ? 0.5051 0.3995 0.3938 0.1989  0.1436  0.1518  127 PHE B CD2   
3098 C CE1   . PHE B 155 ? 0.5243 0.3899 0.3790 0.1961  0.1576  0.1221  127 PHE B CE1   
3099 C CE2   . PHE B 155 ? 0.5193 0.4087 0.3957 0.2048  0.1579  0.1476  127 PHE B CE2   
3100 C CZ    . PHE B 155 ? 0.5294 0.4036 0.3882 0.2033  0.1647  0.1325  127 PHE B CZ    
3101 N N     . GLY B 156 ? 0.4694 0.3536 0.3614 0.1707  0.0940  0.1282  128 GLY B N     
3102 C CA    . GLY B 156 ? 0.4629 0.3452 0.3607 0.1655  0.0815  0.1286  128 GLY B CA    
3103 C C     . GLY B 156 ? 0.4639 0.3439 0.3721 0.1665  0.0798  0.1392  128 GLY B C     
3104 O O     . GLY B 156 ? 0.5271 0.4125 0.4477 0.1646  0.0697  0.1492  128 GLY B O     
3105 N N     . LYS B 157 ? 0.4790 0.3507 0.3819 0.1691  0.0894  0.1372  129 LYS B N     
3106 C CA    . LYS B 157 ? 0.4762 0.3459 0.3881 0.1710  0.0890  0.1475  129 LYS B CA    
3107 C C     . LYS B 157 ? 0.4963 0.3668 0.4102 0.1786  0.1025  0.1544  129 LYS B C     
3108 O O     . LYS B 157 ? 0.5128 0.3788 0.4153 0.1814  0.1136  0.1466  129 LYS B O     
3109 C CB    . LYS B 157 ? 0.4723 0.3289 0.3756 0.1674  0.0871  0.1391  129 LYS B CB    
3110 C CG    . LYS B 157 ? 0.5370 0.3909 0.4347 0.1606  0.0764  0.1292  129 LYS B CG    
3111 C CD    . LYS B 157 ? 0.6222 0.4842 0.5326 0.1580  0.0625  0.1385  129 LYS B CD    
3112 C CE    . LYS B 157 ? 0.6336 0.4939 0.5381 0.1526  0.0531  0.1286  129 LYS B CE    
3113 N NZ    . LYS B 157 ? 0.5720 0.4426 0.4838 0.1525  0.0473  0.1331  129 LYS B NZ    
3114 N N     . VAL B 158 ? 0.5079 0.3843 0.4363 0.1821  0.1013  0.1692  130 VAL B N     
3115 C CA    . VAL B 158 ? 0.4846 0.3643 0.4180 0.1891  0.1135  0.1768  130 VAL B CA    
3116 C C     . VAL B 158 ? 0.4857 0.3651 0.4268 0.1870  0.1113  0.1801  130 VAL B C     
3117 O O     . VAL B 158 ? 0.4782 0.3687 0.4342 0.1810  0.0994  0.1862  130 VAL B O     
3118 C CB    . VAL B 158 ? 0.4805 0.3792 0.4294 0.1902  0.1134  0.1873  130 VAL B CB    
3119 C CG1   . VAL B 158 ? 0.4871 0.3921 0.4447 0.1960  0.1242  0.1952  130 VAL B CG1   
3120 C CG2   . VAL B 158 ? 0.4829 0.3806 0.4213 0.1943  0.1186  0.1844  130 VAL B CG2   
3121 N N     . PHE B 159 ? 0.4966 0.3622 0.4266 0.1919  0.1226  0.1759  131 PHE B N     
3122 C CA    . PHE B 159 ? 0.4999 0.3645 0.4357 0.1912  0.1221  0.1794  131 PHE B CA    
3123 C C     . PHE B 159 ? 0.5300 0.4053 0.4775 0.1974  0.1314  0.1889  131 PHE B C     
3124 O O     . PHE B 159 ? 0.6022 0.4728 0.5422 0.2048  0.1452  0.1879  131 PHE B O     
3125 C CB    . PHE B 159 ? 0.5102 0.3529 0.4274 0.1926  0.1291  0.1697  131 PHE B CB    
3126 C CG    . PHE B 159 ? 0.5066 0.3384 0.4122 0.1871  0.1211  0.1605  131 PHE B CG    
3127 C CD1   . PHE B 159 ? 0.5358 0.3677 0.4448 0.1809  0.1092  0.1609  131 PHE B CD1   
3128 C CD2   . PHE B 159 ? 0.5090 0.3358 0.4017 0.1843  0.1240  0.1473  131 PHE B CD2   
3129 C CE1   . PHE B 159 ? 0.5643 0.3866 0.4622 0.1761  0.1025  0.1520  131 PHE B CE1   
3130 C CE2   . PHE B 159 ? 0.5031 0.3253 0.3875 0.1765  0.1159  0.1359  131 PHE B CE2   
3131 C CZ    . PHE B 159 ? 0.5559 0.3757 0.4430 0.1726  0.1056  0.1382  131 PHE B CZ    
3132 N N     . CYS B 160 ? 0.5185 0.4077 0.4838 0.1947  0.1238  0.1981  132 CYS B N     
3133 C CA    . CYS B 160 ? 0.5229 0.4247 0.5020 0.2004  0.1313  0.2085  132 CYS B CA    
3134 C C     . CYS B 160 ? 0.5274 0.4284 0.5120 0.1997  0.1283  0.2120  132 CYS B C     
3135 O O     . CYS B 160 ? 0.5664 0.4777 0.5639 0.1936  0.1147  0.2175  132 CYS B O     
3136 C CB    . CYS B 160 ? 0.5136 0.4370 0.5121 0.1978  0.1245  0.2183  132 CYS B CB    
3137 S SG    . CYS B 160 ? 0.6149 0.5577 0.6355 0.2026  0.1294  0.2331  132 CYS B SG    
3138 N N     . MET B 161 ? 0.5358 0.4233 0.5094 0.2060  0.1406  0.2089  133 MET B N     
3139 C CA    . MET B 161 ? 0.5601 0.4431 0.5348 0.2059  0.1387  0.2108  133 MET B CA    
3140 C C     . MET B 161 ? 0.5757 0.4665 0.5602 0.2141  0.1494  0.2199  133 MET B C     
3141 O O     . MET B 161 ? 0.6416 0.5236 0.6168 0.2219  0.1652  0.2178  133 MET B O     
3142 C CB    . MET B 161 ? 0.5785 0.4375 0.5313 0.2058  0.1439  0.1995  133 MET B CB    
3143 C CG    . MET B 161 ? 0.5794 0.4279 0.5185 0.2006  0.1395  0.1890  133 MET B CG    
3144 S SD    . MET B 161 ? 0.6017 0.4528 0.5440 0.1902  0.1194  0.1878  133 MET B SD    
3145 C CE    . MET B 161 ? 0.6595 0.5014 0.5984 0.1908  0.1197  0.1892  133 MET B CE    
3146 N N     . LEU B 162 ? 0.5338 0.4402 0.5364 0.2125  0.1410  0.2301  134 LEU B N     
3147 C CA    . LEU B 162 ? 0.5433 0.4576 0.5565 0.2201  0.1495  0.2396  134 LEU B CA    
3148 C C     . LEU B 162 ? 0.5485 0.4691 0.5649 0.2286  0.1646  0.2437  134 LEU B C     
3149 O O     . LEU B 162 ? 0.5626 0.4718 0.5686 0.2369  0.1802  0.2419  134 LEU B O     
3150 C CB    . LEU B 162 ? 0.5569 0.4531 0.5566 0.2238  0.1563  0.2352  134 LEU B CB    
3151 C CG    . LEU B 162 ? 0.5550 0.4402 0.5460 0.2164  0.1443  0.2295  134 LEU B CG    
3152 C CD1   . LEU B 162 ? 0.5703 0.4354 0.5455 0.2209  0.1544  0.2244  134 LEU B CD1   
3153 C CD2   . LEU B 162 ? 0.5488 0.4500 0.5571 0.2115  0.1285  0.2386  134 LEU B CD2   
3154 N N     . MET B 163 ? 0.5864 0.5247 0.6167 0.2263  0.1600  0.2497  135 MET B N     
3155 C CA    . MET B 163 ? 0.5629 0.5081 0.5958 0.2342  0.1741  0.2542  135 MET B CA    
3156 C C     . MET B 163 ? 0.5398 0.5105 0.5958 0.2320  0.1683  0.2660  135 MET B C     
3157 O O     . MET B 163 ? 0.5707 0.5522 0.6351 0.2396  0.1799  0.2743  135 MET B O     
3158 C CB    . MET B 163 ? 0.5456 0.4746 0.5577 0.2355  0.1814  0.2431  135 MET B CB    
3159 C CG    . MET B 163 ? 0.5323 0.4673 0.5460 0.2277  0.1701  0.2402  135 MET B CG    
3160 S SD    . MET B 163 ? 0.5960 0.5520 0.6242 0.2310  0.1748  0.2503  135 MET B SD    
3161 C CE    . MET B 163 ? 0.5605 0.4999 0.5671 0.2432  0.1969  0.2450  135 MET B CE    
3162 N N     . LEU B 164 ? 0.5205 0.5001 0.5863 0.2217  0.1508  0.2670  136 LEU B N     
3163 C CA    . LEU B 164 ? 0.5124 0.5153 0.6004 0.2186  0.1448  0.2783  136 LEU B CA    
3164 C C     . LEU B 164 ? 0.5513 0.5713 0.6597 0.2221  0.1463  0.2916  136 LEU B C     
3165 O O     . LEU B 164 ? 0.5999 0.6404 0.7276 0.2221  0.1463  0.3027  136 LEU B O     
3166 C CB    . LEU B 164 ? 0.4997 0.5055 0.5918 0.2063  0.1255  0.2758  136 LEU B CB    
3167 C CG    . LEU B 164 ? 0.4937 0.4901 0.5720 0.2028  0.1238  0.2664  136 LEU B CG    
3168 C CD1   . LEU B 164 ? 0.5140 0.5100 0.5941 0.1912  0.1048  0.2632  136 LEU B CD1   
3169 C CD2   . LEU B 164 ? 0.4934 0.5019 0.5783 0.2073  0.1333  0.2724  136 LEU B CD2   
3170 N N     . HIS B 165 ? 0.5697 0.5823 0.6747 0.2253  0.1477  0.2912  137 HIS B N     
3171 C CA    . HIS B 165 ? 0.5560 0.5838 0.6789 0.2305  0.1513  0.3039  137 HIS B CA    
3172 C C     . HIS B 165 ? 0.5705 0.6013 0.6938 0.2429  0.1718  0.3093  137 HIS B C     
3173 O O     . HIS B 165 ? 0.6111 0.6574 0.7512 0.2483  0.1766  0.3215  137 HIS B O     
3174 C CB    . HIS B 165 ? 0.5381 0.5559 0.6557 0.2301  0.1458  0.3017  137 HIS B CB    
3175 C CG    . HIS B 165 ? 0.5493 0.5434 0.6441 0.2365  0.1577  0.2916  137 HIS B CG    
3176 N ND1   . HIS B 165 ? 0.5642 0.5547 0.6574 0.2468  0.1718  0.2956  137 HIS B ND1   
3177 C CD2   . HIS B 165 ? 0.5750 0.5472 0.6475 0.2338  0.1579  0.2780  137 HIS B CD2   
3178 C CE1   . HIS B 165 ? 0.5849 0.5514 0.6553 0.2498  0.1800  0.2846  137 HIS B CE1   
3179 N NE2   . HIS B 165 ? 0.6531 0.6087 0.7110 0.2419  0.1719  0.2739  137 HIS B NE2   
3180 N N     . LEU B 166 ? 0.5482 0.5641 0.6527 0.2478  0.1840  0.3009  138 LEU B N     
3181 C CA    . LEU B 166 ? 0.5993 0.6162 0.7012 0.2595  0.2038  0.3053  138 LEU B CA    
3182 C C     . LEU B 166 ? 0.6264 0.6578 0.7365 0.2598  0.2071  0.3108  138 LEU B C     
3183 O O     . LEU B 166 ? 0.7024 0.7379 0.8127 0.2695  0.2231  0.3169  138 LEU B O     
3184 C CB    . LEU B 166 ? 0.6768 0.6660 0.7504 0.2655  0.2165  0.2928  138 LEU B CB    
3185 C CG    . LEU B 166 ? 0.7286 0.7055 0.7944 0.2740  0.2281  0.2932  138 LEU B CG    
3186 C CD1   . LEU B 166 ? 0.7773 0.7591 0.8541 0.2696  0.2158  0.2967  138 LEU B CD1   
3187 C CD2   . LEU B 166 ? 0.6908 0.6379 0.7272 0.2769  0.2377  0.2791  138 LEU B CD2   
3188 N N     . VAL B 167 ? 0.5703 0.6087 0.6863 0.2495  0.1926  0.3091  139 VAL B N     
3189 C CA    . VAL B 167 ? 0.5928 0.6439 0.7157 0.2489  0.1946  0.3138  139 VAL B CA    
3190 C C     . VAL B 167 ? 0.6040 0.6819 0.7562 0.2437  0.1855  0.3283  139 VAL B C     
3191 O O     . VAL B 167 ? 0.5995 0.6817 0.7601 0.2326  0.1676  0.3276  139 VAL B O     
3192 C CB    . VAL B 167 ? 0.5724 0.6118 0.6808 0.2411  0.1854  0.3021  139 VAL B CB    
3193 C CG1   . VAL B 167 ? 0.6042 0.6562 0.7188 0.2413  0.1882  0.3074  139 VAL B CG1   
3194 C CG2   . VAL B 167 ? 0.5567 0.5693 0.6367 0.2456  0.1936  0.2880  139 VAL B CG2   
3195 N N     . PRO B 168 ? 0.5575 0.6533 0.7252 0.2510  0.1972  0.3417  140 PRO B N     
3196 C CA    . PRO B 168 ? 0.5248 0.6472 0.7218 0.2456  0.1887  0.3563  140 PRO B CA    
3197 C C     . PRO B 168 ? 0.5227 0.6531 0.7270 0.2347  0.1756  0.3565  140 PRO B C     
3198 O O     . PRO B 168 ? 0.5303 0.6728 0.7519 0.2249  0.1601  0.3619  140 PRO B O     
3199 C CB    . PRO B 168 ? 0.5822 0.7192 0.7896 0.2573  0.2075  0.3695  140 PRO B CB    
3200 C CG    . PRO B 168 ? 0.6304 0.7472 0.8162 0.2685  0.2229  0.3624  140 PRO B CG    
3201 C CD    . PRO B 168 ? 0.5824 0.6742 0.7417 0.2650  0.2188  0.3448  140 PRO B CD    
3202 N N     . ASP B 169 ? 0.5577 0.6810 0.7487 0.2362  0.1812  0.3507  141 ASP B N     
3203 C CA    . ASP B 169 ? 0.5466 0.6761 0.7430 0.2264  0.1696  0.3507  141 ASP B CA    
3204 C C     . ASP B 169 ? 0.5398 0.6484 0.7171 0.2181  0.1560  0.3350  141 ASP B C     
3205 O O     . ASP B 169 ? 0.5519 0.6443 0.7078 0.2205  0.1606  0.3242  141 ASP B O     
3206 C CB    . ASP B 169 ? 0.6116 0.7458 0.8042 0.2330  0.1829  0.3540  141 ASP B CB    
3207 C CG    . ASP B 169 ? 0.7186 0.8648 0.9230 0.2236  0.1724  0.3587  141 ASP B CG    
3208 O OD1   . ASP B 169 ? 0.6912 0.8356 0.8999 0.2116  0.1542  0.3551  141 ASP B OD1   
3209 O OD2   . ASP B 169 ? 0.7406 0.8973 0.9492 0.2286  0.1826  0.3661  141 ASP B OD2   
3210 N N     . ASN B 170 ? 0.5865 0.6954 0.7712 0.2084  0.1393  0.3341  142 ASN B N     
3211 C CA    . ASN B 170 ? 0.5514 0.6402 0.7180 0.2011  0.1267  0.3198  142 ASN B CA    
3212 C C     . ASN B 170 ? 0.4785 0.5654 0.6417 0.1925  0.1166  0.3156  142 ASN B C     
3213 O O     . ASN B 170 ? 0.4859 0.5545 0.6292 0.1900  0.1124  0.3028  142 ASN B O     
3214 C CB    . ASN B 170 ? 0.5313 0.6199 0.7049 0.1946  0.1129  0.3204  142 ASN B CB    
3215 C CG    . ASN B 170 ? 0.4960 0.5684 0.6544 0.2004  0.1182  0.3128  142 ASN B CG    
3216 O OD1   . ASN B 170 ? 0.4946 0.5485 0.6354 0.1965  0.1112  0.3008  142 ASN B OD1   
3217 N ND2   . ASN B 170 ? 0.5137 0.5927 0.6785 0.2099  0.1311  0.3201  142 ASN B ND2   
3218 N N     . ARG B 171 ? 0.4892 0.5943 0.6716 0.1880  0.1126  0.3264  143 ARG B N     
3219 C CA    . ARG B 171 ? 0.5074 0.6098 0.6862 0.1802  0.1034  0.3229  143 ARG B CA    
3220 C C     . ARG B 171 ? 0.4896 0.5845 0.6518 0.1870  0.1155  0.3173  143 ARG B C     
3221 O O     . ARG B 171 ? 0.4904 0.5730 0.6381 0.1826  0.1090  0.3079  143 ARG B O     
3222 C CB    . ARG B 171 ? 0.5348 0.6583 0.7389 0.1735  0.0966  0.3367  143 ARG B CB    
3223 C CG    . ARG B 171 ? 0.4991 0.6197 0.7001 0.1655  0.0875  0.3341  143 ARG B CG    
3224 C CD    . ARG B 171 ? 0.4518 0.5850 0.6739 0.1545  0.0730  0.3434  143 ARG B CD    
3225 N NE    . ARG B 171 ? 0.5751 0.7281 0.8211 0.1556  0.0751  0.3573  143 ARG B NE    
3226 C CZ    . ARG B 171 ? 0.7180 0.8779 0.9791 0.1469  0.0613  0.3630  143 ARG B CZ    
3227 N NH1   . ARG B 171 ? 0.7125 0.8601 0.9667 0.1367  0.0446  0.3557  143 ARG B NH1   
3228 N NH2   . ARG B 171 ? 0.7144 0.8939 0.9979 0.1488  0.0645  0.3765  143 ARG B NH2   
3229 N N     . LEU B 172 ? 0.4837 0.5853 0.6469 0.1983  0.1332  0.3231  144 LEU B N     
3230 C CA    . LEU B 172 ? 0.4912 0.5842 0.6361 0.2059  0.1456  0.3177  144 LEU B CA    
3231 C C     . LEU B 172 ? 0.4804 0.5490 0.5988 0.2078  0.1461  0.3018  144 LEU B C     
3232 O O     . LEU B 172 ? 0.5023 0.5601 0.6034 0.2084  0.1473  0.2937  144 LEU B O     
3233 C CB    . LEU B 172 ? 0.5109 0.6146 0.6609 0.2186  0.1652  0.3274  144 LEU B CB    
3234 C CG    . LEU B 172 ? 0.4977 0.5917 0.6270 0.2287  0.1803  0.3226  144 LEU B CG    
3235 C CD1   . LEU B 172 ? 0.5073 0.6021 0.6321 0.2233  0.1738  0.3208  144 LEU B CD1   
3236 C CD2   . LEU B 172 ? 0.5419 0.6479 0.6784 0.2412  0.1994  0.3340  144 LEU B CD2   
3237 N N     . ALA B 173 ? 0.4824 0.5425 0.5975 0.2087  0.1453  0.2976  145 ALA B N     
3238 C CA    . ALA B 173 ? 0.4848 0.5219 0.5760 0.2099  0.1457  0.2831  145 ALA B CA    
3239 C C     . ALA B 173 ? 0.4754 0.5034 0.5599 0.1989  0.1287  0.2742  145 ALA B C     
3240 O O     . ALA B 173 ? 0.4762 0.4881 0.5406 0.1995  0.1293  0.2630  145 ALA B O     
3241 C CB    . ALA B 173 ? 0.4904 0.5210 0.5806 0.2134  0.1491  0.2819  145 ALA B CB    
3242 N N     . VAL B 174 ? 0.4712 0.5089 0.5719 0.1893  0.1136  0.2793  146 VAL B N     
3243 C CA    . VAL B 174 ? 0.4604 0.4893 0.5549 0.1793  0.0976  0.2716  146 VAL B CA    
3244 C C     . VAL B 174 ? 0.4872 0.5171 0.5768 0.1779  0.0974  0.2704  146 VAL B C     
3245 O O     . VAL B 174 ? 0.4900 0.5068 0.5643 0.1748  0.0917  0.2603  146 VAL B O     
3246 C CB    . VAL B 174 ? 0.4558 0.4934 0.5677 0.1698  0.0821  0.2778  146 VAL B CB    
3247 C CG1   . VAL B 174 ? 0.4502 0.4793 0.5562 0.1600  0.0663  0.2712  146 VAL B CG1   
3248 C CG2   . VAL B 174 ? 0.4589 0.4921 0.5712 0.1709  0.0806  0.2769  146 VAL B CG2   
3249 N N     . LYS B 175 ? 0.4838 0.5299 0.5864 0.1807  0.1040  0.2812  147 LYS B N     
3250 C CA    . LYS B 175 ? 0.4866 0.5342 0.5840 0.1804  0.1051  0.2811  147 LYS B CA    
3251 C C     . LYS B 175 ? 0.4808 0.5142 0.5542 0.1885  0.1161  0.2714  147 LYS B C     
3252 O O     . LYS B 175 ? 0.4741 0.4997 0.5349 0.1862  0.1116  0.2646  147 LYS B O     
3253 C CB    . LYS B 175 ? 0.4614 0.5294 0.5772 0.1831  0.1123  0.2956  147 LYS B CB    
3254 C CG    . LYS B 175 ? 0.5371 0.6071 0.6462 0.1848  0.1163  0.2965  147 LYS B CG    
3255 C CD    . LYS B 175 ? 0.6245 0.7148 0.7511 0.1890  0.1259  0.3114  147 LYS B CD    
3256 C CE    . LYS B 175 ? 0.6459 0.7367 0.7622 0.1928  0.1323  0.3119  147 LYS B CE    
3257 N NZ    . LYS B 175 ? 0.5531 0.6637 0.6857 0.1977  0.1429  0.3268  147 LYS B NZ    
3258 N N     . ASN B 176 ? 0.4935 0.5227 0.5597 0.1983  0.1305  0.2706  148 ASN B N     
3259 C CA    . ASN B 176 ? 0.4839 0.4978 0.5259 0.2065  0.1416  0.2614  148 ASN B CA    
3260 C C     . ASN B 176 ? 0.5029 0.4977 0.5279 0.2026  0.1340  0.2477  148 ASN B C     
3261 O O     . ASN B 176 ? 0.5038 0.4869 0.5096 0.2050  0.1364  0.2393  148 ASN B O     
3262 C CB    . ASN B 176 ? 0.4929 0.5055 0.5312 0.2183  0.1595  0.2645  148 ASN B CB    
3263 C CG    . ASN B 176 ? 0.4997 0.5264 0.5448 0.2257  0.1715  0.2754  148 ASN B CG    
3264 O OD1   . ASN B 176 ? 0.4964 0.5317 0.5451 0.2227  0.1677  0.2793  148 ASN B OD1   
3265 N ND2   . ASN B 176 ? 0.5833 0.6120 0.6297 0.2359  0.1867  0.2807  148 ASN B ND2   
3266 N N     . ILE B 177 ? 0.4735 0.4651 0.5046 0.1970  0.1252  0.2456  149 ILE B N     
3267 C CA    . ILE B 177 ? 0.4705 0.4455 0.4872 0.1924  0.1169  0.2336  149 ILE B CA    
3268 C C     . ILE B 177 ? 0.5416 0.5170 0.5576 0.1845  0.1035  0.2306  149 ILE B C     
3269 O O     . ILE B 177 ? 0.5495 0.5120 0.5489 0.1841  0.1011  0.2205  149 ILE B O     
3270 C CB    . ILE B 177 ? 0.4683 0.4407 0.4920 0.1883  0.1101  0.2333  149 ILE B CB    
3271 C CG1   . ILE B 177 ? 0.4780 0.4452 0.4974 0.1970  0.1242  0.2337  149 ILE B CG1   
3272 C CG2   . ILE B 177 ? 0.4642 0.4218 0.4759 0.1821  0.0992  0.2224  149 ILE B CG2   
3273 C CD1   . ILE B 177 ? 0.4772 0.4451 0.5058 0.1940  0.1185  0.2360  149 ILE B CD1   
3274 N N     . HIS B 178 ? 0.5268 0.5167 0.5607 0.1784  0.0949  0.2395  150 HIS B N     
3275 C CA    . HIS B 178 ? 0.5296 0.5193 0.5635 0.1710  0.0823  0.2374  150 HIS B CA    
3276 C C     . HIS B 178 ? 0.5455 0.5329 0.5659 0.1758  0.0888  0.2344  150 HIS B C     
3277 O O     . HIS B 178 ? 0.5339 0.5141 0.5450 0.1722  0.0807  0.2276  150 HIS B O     
3278 C CB    . HIS B 178 ? 0.5455 0.5503 0.6012 0.1640  0.0735  0.2485  150 HIS B CB    
3279 C CG    . HIS B 178 ? 0.5672 0.5701 0.6235 0.1559  0.0599  0.2468  150 HIS B CG    
3280 N ND1   . HIS B 178 ? 0.5793 0.5873 0.6350 0.1563  0.0614  0.2498  150 HIS B ND1   
3281 C CD2   . HIS B 178 ? 0.5958 0.5910 0.6523 0.1476  0.0449  0.2425  150 HIS B CD2   
3282 C CE1   . HIS B 178 ? 0.6125 0.6160 0.6686 0.1485  0.0478  0.2474  150 HIS B CE1   
3283 N NE2   . HIS B 178 ? 0.6346 0.6299 0.6909 0.1433  0.0378  0.2428  150 HIS B NE2   
3284 N N     . LYS B 179 ? 0.5113 0.5047 0.5299 0.1844  0.1032  0.2395  151 LYS B N     
3285 C CA    . LYS B 179 ? 0.4849 0.4754 0.4881 0.1899  0.1100  0.2367  151 LYS B CA    
3286 C C     . LYS B 179 ? 0.5046 0.4767 0.4838 0.1942  0.1133  0.2239  151 LYS B C     
3287 O O     . LYS B 179 ? 0.5260 0.4933 0.4912 0.1955  0.1121  0.2188  151 LYS B O     
3288 C CB    . LYS B 179 ? 0.4782 0.4779 0.4830 0.1991  0.1256  0.2453  151 LYS B CB    
3289 C CG    . LYS B 179 ? 0.4899 0.5088 0.5162 0.1961  0.1241  0.2587  151 LYS B CG    
3290 C CD    . LYS B 179 ? 0.5186 0.5454 0.5437 0.2068  0.1412  0.2666  151 LYS B CD    
3291 C CE    . LYS B 179 ? 0.5822 0.6293 0.6295 0.2044  0.1410  0.2808  151 LYS B CE    
3292 N NZ    . LYS B 179 ? 0.6146 0.6697 0.6604 0.2158  0.1587  0.2888  151 LYS B NZ    
3293 N N     . LEU B 180 ? 0.4742 0.4362 0.4484 0.1965  0.1175  0.2188  152 LEU B N     
3294 C CA    . LEU B 180 ? 0.4808 0.4244 0.4320 0.2008  0.1228  0.2066  152 LEU B CA    
3295 C C     . LEU B 180 ? 0.4730 0.4087 0.4191 0.1925  0.1095  0.1956  152 LEU B C     
3296 O O     . LEU B 180 ? 0.4760 0.4020 0.4050 0.1906  0.1112  0.1800  152 LEU B O     
3297 C CB    . LEU B 180 ? 0.4884 0.4234 0.4360 0.2061  0.1337  0.2047  152 LEU B CB    
3298 C CG    . LEU B 180 ? 0.5004 0.4383 0.4454 0.2156  0.1502  0.2099  152 LEU B CG    
3299 C CD1   . LEU B 180 ? 0.5063 0.4384 0.4546 0.2206  0.1586  0.2124  152 LEU B CD1   
3300 C CD2   . LEU B 180 ? 0.5105 0.4407 0.4329 0.2170  0.1584  0.1956  152 LEU B CD2   
3301 N N     . LEU B 181 ? 0.4636 0.4045 0.4245 0.1853  0.0962  0.2007  153 LEU B N     
3302 C CA    . LEU B 181 ? 0.4680 0.3996 0.4238 0.1794  0.0843  0.1924  153 LEU B CA    
3303 C C     . LEU B 181 ? 0.6372 0.5714 0.5904 0.1761  0.0754  0.1902  153 LEU B C     
3304 O O     . LEU B 181 ? 0.6025 0.5484 0.5655 0.1746  0.0732  0.1982  153 LEU B O     
3305 C CB    . LEU B 181 ? 0.4518 0.3866 0.4230 0.1716  0.0738  0.1959  153 LEU B CB    
3306 C CG    . LEU B 181 ? 0.4552 0.3845 0.4265 0.1736  0.0796  0.1952  153 LEU B CG    
3307 C CD1   . LEU B 181 ? 0.4837 0.4204 0.4724 0.1665  0.0690  0.2018  153 LEU B CD1   
3308 C CD2   . LEU B 181 ? 0.4719 0.3833 0.4247 0.1753  0.0812  0.1835  153 LEU B CD2   
3309 N N     . VAL B 182 ? 0.5763 0.5016 0.5172 0.1719  0.0700  0.1758  154 VAL B N     
3310 C CA    . VAL B 182 ? 0.5704 0.4972 0.5090 0.1681  0.0601  0.1719  154 VAL B CA    
3311 C C     . VAL B 182 ? 0.5860 0.5133 0.5383 0.1632  0.0465  0.1805  154 VAL B C     
3312 O O     . VAL B 182 ? 0.5993 0.5236 0.5581 0.1601  0.0435  0.1819  154 VAL B O     
3313 C CB    . VAL B 182 ? 0.5772 0.4953 0.4994 0.1657  0.0592  0.1538  154 VAL B CB    
3314 C CG1   . VAL B 182 ? 0.5763 0.4937 0.4846 0.1696  0.0719  0.1451  154 VAL B CG1   
3315 C CG2   . VAL B 182 ? 0.5702 0.4781 0.4906 0.1621  0.0555  0.1473  154 VAL B CG2   
3316 N N     . PRO B 183 ? 0.5505 0.4825 0.5078 0.1599  0.0377  0.1838  155 PRO B N     
3317 C CA    . PRO B 183 ? 0.5914 0.5225 0.5601 0.1511  0.0235  0.1860  155 PRO B CA    
3318 C C     . PRO B 183 ? 0.5925 0.5107 0.5529 0.1495  0.0174  0.1768  155 PRO B C     
3319 O O     . PRO B 183 ? 0.6354 0.5468 0.5824 0.1509  0.0171  0.1656  155 PRO B O     
3320 C CB    . PRO B 183 ? 0.5842 0.5188 0.5538 0.1494  0.0171  0.1876  155 PRO B CB    
3321 C CG    . PRO B 183 ? 0.6075 0.5510 0.5742 0.1556  0.0284  0.1920  155 PRO B CG    
3322 C CD    . PRO B 183 ? 0.5509 0.4893 0.5042 0.1633  0.0405  0.1861  155 PRO B CD    
3323 N N     . GLY B 184 ? 0.6037 0.5198 0.5721 0.1446  0.0123  0.1792  156 GLY B N     
3324 C CA    . GLY B 184 ? 0.5983 0.5022 0.5582 0.1438  0.0084  0.1716  156 GLY B CA    
3325 C C     . GLY B 184 ? 0.6597 0.5590 0.6126 0.1484  0.0192  0.1685  156 GLY B C     
3326 O O     . GLY B 184 ? 0.7339 0.6235 0.6805 0.1467  0.0165  0.1625  156 GLY B O     
3327 N N     . GLY B 185 ? 0.5407 0.4460 0.4935 0.1538  0.0316  0.1717  157 GLY B N     
3328 C CA    . GLY B 185 ? 0.5859 0.4861 0.5326 0.1575  0.0422  0.1685  157 GLY B CA    
3329 C C     . GLY B 185 ? 0.6435 0.5462 0.6022 0.1542  0.0390  0.1755  157 GLY B C     
3330 O O     . GLY B 185 ? 0.6343 0.5472 0.6086 0.1492  0.0314  0.1838  157 GLY B O     
3331 N N     . GLU B 186 ? 0.6149 0.5083 0.5658 0.1566  0.0447  0.1714  158 GLU B N     
3332 C CA    . GLU B 186 ? 0.6199 0.5144 0.5796 0.1533  0.0407  0.1760  158 GLU B CA    
3333 C C     . GLU B 186 ? 0.5634 0.4608 0.5255 0.1589  0.0537  0.1801  158 GLU B C     
3334 O O     . GLU B 186 ? 0.5565 0.4475 0.5070 0.1655  0.0664  0.1755  158 GLU B O     
3335 C CB    . GLU B 186 ? 0.6702 0.5505 0.6186 0.1510  0.0352  0.1685  158 GLU B CB    
3336 C CG    . GLU B 186 ? 0.7187 0.5943 0.6632 0.1465  0.0230  0.1640  158 GLU B CG    
3337 C CD    . GLU B 186 ? 0.8012 0.6623 0.7311 0.1450  0.0205  0.1536  158 GLU B CD    
3338 O OE1   . GLU B 186 ? 0.7993 0.6537 0.7178 0.1469  0.0306  0.1443  158 GLU B OE1   
3339 O OE2   . GLU B 186 ? 0.8247 0.6815 0.7545 0.1404  0.0085  0.1530  158 GLU B OE2   
3340 N N     . ALA B 187 ? 0.5549 0.4612 0.5315 0.1565  0.0504  0.1885  159 ALA B N     
3341 C CA    . ALA B 187 ? 0.4678 0.3781 0.4490 0.1620  0.0617  0.1935  159 ALA B CA    
3342 C C     . ALA B 187 ? 0.4740 0.3790 0.4558 0.1601  0.0578  0.1941  159 ALA B C     
3343 O O     . ALA B 187 ? 0.5153 0.4217 0.5029 0.1536  0.0442  0.1961  159 ALA B O     
3344 C CB    . ALA B 187 ? 0.4557 0.3841 0.4551 0.1626  0.0631  0.2049  159 ALA B CB    
3345 N N     . VAL B 188 ? 0.4683 0.3663 0.4431 0.1660  0.0697  0.1923  160 VAL B N     
3346 C CA    . VAL B 188 ? 0.4734 0.3657 0.4472 0.1654  0.0679  0.1930  160 VAL B CA    
3347 C C     . VAL B 188 ? 0.4780 0.3802 0.4636 0.1706  0.0764  0.2019  160 VAL B C     
3348 O O     . VAL B 188 ? 0.5373 0.4363 0.5175 0.1780  0.0911  0.2008  160 VAL B O     
3349 C CB    . VAL B 188 ? 0.4801 0.3526 0.4336 0.1677  0.0747  0.1825  160 VAL B CB    
3350 C CG1   . VAL B 188 ? 0.4869 0.3540 0.4396 0.1678  0.0743  0.1843  160 VAL B CG1   
3351 C CG2   . VAL B 188 ? 0.4762 0.3397 0.4188 0.1630  0.0662  0.1742  160 VAL B CG2   
3352 N N     . PHE B 189 ? 0.4769 0.3904 0.4777 0.1673  0.0673  0.2107  161 PHE B N     
3353 C CA    . PHE B 189 ? 0.4813 0.4064 0.4955 0.1723  0.0741  0.2203  161 PHE B CA    
3354 C C     . PHE B 189 ? 0.4890 0.4073 0.5003 0.1735  0.0736  0.2211  161 PHE B C     
3355 O O     . PHE B 189 ? 0.5044 0.4153 0.5102 0.1680  0.0625  0.2180  161 PHE B O     
3356 C CB    . PHE B 189 ? 0.4759 0.4207 0.5113 0.1684  0.0653  0.2312  161 PHE B CB    
3357 C CG    . PHE B 189 ? 0.4720 0.4252 0.5121 0.1678  0.0669  0.2325  161 PHE B CG    
3358 C CD1   . PHE B 189 ? 0.4719 0.4340 0.5176 0.1750  0.0806  0.2375  161 PHE B CD1   
3359 C CD2   . PHE B 189 ? 0.5459 0.4973 0.5841 0.1605  0.0549  0.2289  161 PHE B CD2   
3360 C CE1   . PHE B 189 ? 0.4674 0.4372 0.5166 0.1747  0.0823  0.2393  161 PHE B CE1   
3361 C CE2   . PHE B 189 ? 0.5388 0.4977 0.5810 0.1600  0.0564  0.2305  161 PHE B CE2   
3362 C CZ    . PHE B 189 ? 0.4778 0.4461 0.5255 0.1670  0.0699  0.2358  161 PHE B CZ    
3363 N N     . SER B 190 ? 0.4967 0.4172 0.5111 0.1813  0.0862  0.2254  162 SER B N     
3364 C CA    . SER B 190 ? 0.5054 0.4222 0.5198 0.1836  0.0869  0.2285  162 SER B CA    
3365 C C     . SER B 190 ? 0.5088 0.4426 0.5413 0.1895  0.0932  0.2404  162 SER B C     
3366 O O     . SER B 190 ? 0.5469 0.4781 0.5769 0.1980  0.1083  0.2414  162 SER B O     
3367 C CB    . SER B 190 ? 0.5409 0.4375 0.5356 0.1882  0.0985  0.2195  162 SER B CB    
3368 O OG    . SER B 190 ? 0.5815 0.4737 0.5755 0.1898  0.0977  0.2225  162 SER B OG    
3369 N N     . VAL B 191 ? 0.5034 0.4545 0.5542 0.1850  0.0820  0.2495  163 VAL B N     
3370 C CA    . VAL B 191 ? 0.5053 0.4757 0.5759 0.1897  0.0872  0.2619  163 VAL B CA    
3371 C C     . VAL B 191 ? 0.5134 0.4873 0.5910 0.1917  0.0842  0.2688  163 VAL B C     
3372 O O     . VAL B 191 ? 0.5135 0.4842 0.5897 0.1855  0.0701  0.2683  163 VAL B O     
3373 C CB    . VAL B 191 ? 0.4959 0.4840 0.5836 0.1835  0.0774  0.2687  163 VAL B CB    
3374 C CG1   . VAL B 191 ? 0.4980 0.5071 0.6068 0.1889  0.0848  0.2820  163 VAL B CG1   
3375 C CG2   . VAL B 191 ? 0.4886 0.4714 0.5674 0.1809  0.0785  0.2613  163 VAL B CG2   
3376 N N     . ILE B 192 ? 0.5215 0.5016 0.6060 0.2009  0.0974  0.2755  164 ILE B N     
3377 C CA    . ILE B 192 ? 0.5301 0.5161 0.6235 0.2040  0.0956  0.2837  164 ILE B CA    
3378 C C     . ILE B 192 ? 0.5258 0.5361 0.6440 0.2009  0.0867  0.2967  164 ILE B C     
3379 O O     . ILE B 192 ? 0.5243 0.5503 0.6570 0.2051  0.0951  0.3046  164 ILE B O     
3380 C CB    . ILE B 192 ? 0.5424 0.5240 0.6324 0.2156  0.1139  0.2857  164 ILE B CB    
3381 C CG1   . ILE B 192 ? 0.5489 0.5048 0.6139 0.2178  0.1217  0.2730  164 ILE B CG1   
3382 C CG2   . ILE B 192 ? 0.5513 0.5429 0.6541 0.2195  0.1120  0.2964  164 ILE B CG2   
3383 C CD1   . ILE B 192 ? 0.5629 0.5109 0.6214 0.2290  0.1408  0.2734  164 ILE B CD1   
3384 N N     . ALA B 193 ? 0.5250 0.5382 0.6477 0.1935  0.0698  0.2992  165 ALA B N     
3385 C CA    . ALA B 193 ? 0.5496 0.5850 0.6954 0.1895  0.0600  0.3115  165 ALA B CA    
3386 C C     . ALA B 193 ? 0.6244 0.6755 0.7869 0.1982  0.0692  0.3240  165 ALA B C     
3387 O O     . ALA B 193 ? 0.7205 0.7883 0.8991 0.2022  0.0783  0.3324  165 ALA B O     
3388 C CB    . ALA B 193 ? 0.5777 0.6099 0.7214 0.1804  0.0402  0.3107  165 ALA B CB    
3389 N N     . ASN B 194 ? 0.6282 0.6738 0.7867 0.2014  0.0673  0.3256  166 ASN B N     
3390 C CA    . ASN B 194 ? 0.6435 0.7025 0.8167 0.2102  0.0757  0.3373  166 ASN B CA    
3391 C C     . ASN B 194 ? 0.6351 0.6759 0.7914 0.2177  0.0842  0.3322  166 ASN B C     
3392 O O     . ASN B 194 ? 0.6198 0.6406 0.7563 0.2140  0.0785  0.3219  166 ASN B O     
3393 C CB    . ASN B 194 ? 0.6608 0.7390 0.8540 0.2056  0.0612  0.3493  166 ASN B CB    
3394 C CG    . ASN B 194 ? 0.7156 0.7812 0.8964 0.2004  0.0460  0.3450  166 ASN B CG    
3395 O OD1   . ASN B 194 ? 0.7185 0.7762 0.8921 0.2062  0.0491  0.3456  166 ASN B OD1   
3396 N ND2   . ASN B 194 ? 0.7688 0.8317 0.9462 0.1896  0.0299  0.3409  166 ASN B ND2   
3397 N N     . MET B 195 ? 0.6935 0.7412 0.8577 0.2283  0.0983  0.3399  167 MET B N     
3398 C CA    . MET B 195 ? 0.7062 0.7379 0.8567 0.2362  0.1071  0.3371  167 MET B CA    
3399 C C     . MET B 195 ? 0.6948 0.7423 0.8624 0.2464  0.1171  0.3506  167 MET B C     
3400 O O     . MET B 195 ? 0.6708 0.7394 0.8582 0.2485  0.1212  0.3605  167 MET B O     
3401 C CB    . MET B 195 ? 0.6545 0.6637 0.7827 0.2401  0.1214  0.3245  167 MET B CB    
3402 C CG    . MET B 195 ? 0.6954 0.7106 0.8275 0.2442  0.1351  0.3246  167 MET B CG    
3403 S SD    . MET B 195 ? 0.6563 0.6432 0.7597 0.2469  0.1490  0.3084  167 MET B SD    
3404 C CE    . MET B 195 ? 0.6506 0.6170 0.7381 0.2521  0.1534  0.3049  167 MET B CE    
3405 N N     . ALA B 196 ? 0.6961 0.7331 0.8557 0.2530  0.1214  0.3513  168 ALA B N     
3406 C CA    . ALA B 196 ? 0.7236 0.7739 0.8981 0.2634  0.1306  0.3641  168 ALA B CA    
3407 C C     . ALA B 196 ? 0.7240 0.7724 0.8971 0.2742  0.1527  0.3649  168 ALA B C     
3408 O O     . ALA B 196 ? 0.7252 0.7884 0.9136 0.2830  0.1617  0.3769  168 ALA B O     
3409 C CB    . ALA B 196 ? 0.7175 0.7558 0.8828 0.2673  0.1282  0.3647  168 ALA B CB    
3410 N N     . LEU B 197 ? 0.7021 0.7324 0.8564 0.2739  0.1618  0.3527  169 LEU B N     
3411 C CA    . LEU B 197 ? 0.6942 0.7220 0.8455 0.2838  0.1824  0.3532  169 LEU B CA    
3412 C C     . LEU B 197 ? 0.7859 0.8394 0.9595 0.2845  0.1848  0.3640  169 LEU B C     
3413 O O     . LEU B 197 ? 0.8462 0.9062 1.0257 0.2946  0.2009  0.3713  169 LEU B O     
3414 C CB    . LEU B 197 ? 0.7207 0.7243 0.8472 0.2822  0.1899  0.3377  169 LEU B CB    
3415 C CG    . LEU B 197 ? 0.6683 0.6432 0.7697 0.2820  0.1917  0.3256  169 LEU B CG    
3416 C CD1   . LEU B 197 ? 0.7760 0.7311 0.8563 0.2814  0.2016  0.3122  169 LEU B CD1   
3417 C CD2   . LEU B 197 ? 0.7077 0.6745 0.8055 0.2922  0.2023  0.3303  169 LEU B CD2   
3418 N N     . CYS B 198 ? 0.7899 0.8576 0.9754 0.2737  0.1694  0.3654  170 CYS B N     
3419 C CA    . CYS B 198 ? 0.7590 0.8515 0.9662 0.2730  0.1709  0.3759  170 CYS B CA    
3420 C C     . CYS B 198 ? 0.8270 0.9443 1.0600 0.2769  0.1691  0.3930  170 CYS B C     
3421 O O     . CYS B 198 ? 0.8185 0.9522 1.0662 0.2838  0.1811  0.4039  170 CYS B O     
3422 C CB    . CYS B 198 ? 0.6899 0.7876 0.9005 0.2598  0.1547  0.3716  170 CYS B CB    
3423 S SG    . CYS B 198 ? 0.6785 0.7541 0.8644 0.2562  0.1592  0.3546  170 CYS B SG    
3424 N N     . ASP B 199 ? 0.8480 0.9683 1.0863 0.2725  0.1543  0.3961  171 ASP B N     
3425 C CA    . ASP B 199 ? 0.7868 0.9304 1.0491 0.2764  0.1521  0.4124  171 ASP B CA    
3426 C C     . ASP B 199 ? 0.7656 0.9059 1.0262 0.2911  0.1706  0.4181  171 ASP B C     
3427 O O     . ASP B 199 ? 0.7856 0.9475 1.0673 0.2974  0.1766  0.4329  171 ASP B O     
3428 C CB    . ASP B 199 ? 0.8075 0.9524 1.0724 0.2688  0.1319  0.4134  171 ASP B CB    
3429 C CG    . ASP B 199 ? 0.8583 1.0088 1.1276 0.2544  0.1132  0.4102  171 ASP B CG    
3430 O OD1   . ASP B 199 ? 0.8054 0.9728 1.0901 0.2505  0.1136  0.4156  171 ASP B OD1   
3431 O OD2   . ASP B 199 ? 0.8703 1.0078 1.1269 0.2470  0.0984  0.4025  171 ASP B OD2   
3432 N N     . ALA B 200 ? 0.7205 0.8339 0.9562 0.2967  0.1801  0.4068  172 ALA B N     
3433 C CA    . ALA B 200 ? 0.7995 0.9064 1.0306 0.3109  0.1995  0.4110  172 ALA B CA    
3434 C C     . ALA B 200 ? 0.8591 0.9738 1.0950 0.3178  0.2170  0.4155  172 ALA B C     
3435 O O     . ALA B 200 ? 0.8707 0.9922 1.1139 0.3294  0.2314  0.4256  172 ALA B O     
3436 C CB    . ALA B 200 ? 0.7853 0.8598 0.9873 0.3140  0.2057  0.3971  172 ALA B CB    
3437 N N     . TYR B 201 ? 0.8668 0.9803 1.0982 0.3113  0.2162  0.4086  173 TYR B N     
3438 C CA    . TYR B 201 ? 0.9061 1.0283 1.1422 0.3173  0.2316  0.4137  173 TYR B CA    
3439 C C     . TYR B 201 ? 0.8716 1.0272 1.1392 0.3171  0.2290  0.4317  173 TYR B C     
3440 O O     . TYR B 201 ? 0.8400 1.0059 1.1161 0.3273  0.2447  0.4424  173 TYR B O     
3441 C CB    . TYR B 201 ? 0.8771 0.9894 1.0999 0.3100  0.2301  0.4018  173 TYR B CB    
3442 C CG    . TYR B 201 ? 0.8486 0.9293 1.0403 0.3137  0.2409  0.3862  173 TYR B CG    
3443 C CD1   . TYR B 201 ? 0.8610 0.9251 1.0389 0.3252  0.2565  0.3853  173 TYR B CD1   
3444 C CD2   . TYR B 201 ? 0.7993 0.8664 0.9754 0.3056  0.2354  0.3727  173 TYR B CD2   
3445 C CE1   . TYR B 201 ? 0.8532 0.8875 1.0023 0.3278  0.2662  0.3712  173 TYR B CE1   
3446 C CE2   . TYR B 201 ? 0.8511 0.8898 0.9992 0.3085  0.2451  0.3589  173 TYR B CE2   
3447 C CZ    . TYR B 201 ? 0.8771 0.8993 1.0118 0.3193  0.2603  0.3581  173 TYR B CZ    
3448 O OH    . TYR B 201 ? 0.8660 0.8590 0.9725 0.3214  0.2697  0.3443  173 TYR B OH    
3449 N N     . GLU B 202 ? 0.8478 1.0200 1.1323 0.3056  0.2095  0.4356  174 GLU B N     
3450 C CA    . GLU B 202 ? 0.8522 1.0566 1.1675 0.3036  0.2057  0.4527  174 GLU B CA    
3451 C C     . GLU B 202 ? 0.9374 1.1557 1.2684 0.3130  0.2107  0.4670  174 GLU B C     
3452 O O     . GLU B 202 ? 0.9606 1.2031 1.3141 0.3170  0.2172  0.4826  174 GLU B O     
3453 C CB    . GLU B 202 ? 0.7965 1.0123 1.1239 0.2883  0.1826  0.4525  174 GLU B CB    
3454 C CG    . GLU B 202 ? 0.7542 0.9635 1.0729 0.2790  0.1780  0.4425  174 GLU B CG    
3455 C CD    . GLU B 202 ? 0.7359 0.9494 1.0604 0.2640  0.1546  0.4395  174 GLU B CD    
3456 O OE1   . GLU B 202 ? 0.7642 0.9713 1.0848 0.2607  0.1420  0.4369  174 GLU B OE1   
3457 O OE2   . GLU B 202 ? 0.7239 0.9461 1.0559 0.2556  0.1489  0.4399  174 GLU B OE2   
3458 N N     . GLU B 203 ? 0.9270 1.1306 1.2467 0.3166  0.2080  0.4627  175 GLU B N     
3459 C CA    . GLU B 203 ? 0.9399 1.1555 1.2735 0.3262  0.2127  0.4761  175 GLU B CA    
3460 C C     . GLU B 203 ? 0.9567 1.1656 1.2832 0.3416  0.2370  0.4799  175 GLU B C     
3461 O O     . GLU B 203 ? 0.9328 1.1611 1.2781 0.3499  0.2451  0.4955  175 GLU B O     
3462 C CB    . GLU B 203 ? 0.9473 1.1489 1.2704 0.3252  0.2014  0.4707  175 GLU B CB    
3463 C CG    . GLU B 203 ? 0.9930 1.2036 1.3251 0.3112  0.1768  0.4701  175 GLU B CG    
3464 C CD    . GLU B 203 ? 1.0417 1.2421 1.3661 0.3118  0.1664  0.4684  175 GLU B CD    
3465 O OE1   . GLU B 203 ? 1.0511 1.2386 1.3651 0.3231  0.1784  0.4683  175 GLU B OE1   
3466 O OE2   . GLU B 203 ? 1.0471 1.2513 1.3748 0.3009  0.1463  0.4672  175 GLU B OE2   
3467 N N     . MET B 204 ? 0.9687 1.1498 1.2676 0.3456  0.2489  0.4660  176 MET B N     
3468 C CA    . MET B 204 ? 0.9708 1.1420 1.2594 0.3599  0.2722  0.4685  176 MET B CA    
3469 C C     . MET B 204 ? 0.9971 1.1869 1.2990 0.3627  0.2830  0.4786  176 MET B C     
3470 O O     . MET B 204 ? 0.9992 1.1910 1.3022 0.3752  0.3006  0.4875  176 MET B O     
3471 C CB    . MET B 204 ? 0.9681 1.1040 1.2228 0.3621  0.2811  0.4506  176 MET B CB    
3472 C CG    . MET B 204 ? 0.9651 1.0795 1.2040 0.3626  0.2759  0.4420  176 MET B CG    
3473 S SD    . MET B 204 ? 1.0016 1.0750 1.2016 0.3637  0.2864  0.4214  176 MET B SD    
3474 C CE    . MET B 204 ? 0.8465 0.9104 1.0370 0.3805  0.3135  0.4271  176 MET B CE    
3475 N N     . ALA B 205 ? 0.9930 1.1955 1.3043 0.3515  0.2728  0.4777  177 ALA B N     
3476 C CA    . ALA B 205 ? 0.9534 1.1734 1.2771 0.3535  0.2826  0.4876  177 ALA B CA    
3477 C C     . ALA B 205 ? 0.9880 1.2390 1.3423 0.3580  0.2843  0.5087  177 ALA B C     
3478 O O     . ALA B 205 ? 0.9945 1.2571 1.3566 0.3650  0.2986  0.5196  177 ALA B O     
3479 C CB    . ALA B 205 ? 0.9319 1.1582 1.2592 0.3398  0.2700  0.4820  177 ALA B CB    
3480 N N     . LYS B 206 ? 0.9725 1.2369 1.3438 0.3540  0.2699  0.5151  178 LYS B N     
3481 C CA    . LYS B 206 ? 0.9193 1.2136 1.3204 0.3581  0.2705  0.5354  178 LYS B CA    
3482 C C     . LYS B 206 ? 0.8932 1.1825 1.2904 0.3749  0.2886  0.5429  178 LYS B C     
3483 O O     . LYS B 206 ? 0.8646 1.1781 1.2851 0.3807  0.2935  0.5607  178 LYS B O     
3484 C CB    . LYS B 206 ? 0.8427 1.1521 1.2619 0.3479  0.2479  0.5395  178 LYS B CB    
3485 C CG    . LYS B 206 ? 0.8507 1.1694 1.2785 0.3311  0.2292  0.5357  178 LYS B CG    
3486 C CD    . LYS B 206 ? 0.8851 1.2145 1.3265 0.3214  0.2068  0.5385  178 LYS B CD    
3487 C CE    . LYS B 206 ? 0.8514 1.1863 1.2982 0.3045  0.1880  0.5336  178 LYS B CE    
3488 N NZ    . LYS B 206 ? 0.8351 1.1762 1.2905 0.2949  0.1655  0.5347  178 LYS B NZ    
3489 N N     . GLU B 207 ? 0.9445 1.2033 1.3134 0.3825  0.2984  0.5302  179 GLU B N     
3490 C CA    . GLU B 207 ? 0.9398 1.1906 1.3026 0.3986  0.3160  0.5365  179 GLU B CA    
3491 C C     . GLU B 207 ? 0.9641 1.2161 1.3237 0.4082  0.3367  0.5432  179 GLU B C     
3492 O O     . GLU B 207 ? 0.9769 1.2123 1.3169 0.4064  0.3431  0.5324  179 GLU B O     
3493 C CB    . GLU B 207 ? 0.9672 1.1828 1.2994 0.4029  0.3200  0.5205  179 GLU B CB    
3494 C CG    . GLU B 207 ? 1.0218 1.2336 1.3545 0.3955  0.3013  0.5148  179 GLU B CG    
3495 C CD    . GLU B 207 ? 1.1108 1.2876 1.4134 0.4003  0.3067  0.5003  179 GLU B CD    
3496 O OE1   . GLU B 207 ? 1.1259 1.2842 1.4111 0.4118  0.3261  0.4981  179 GLU B OE1   
3497 O OE2   . GLU B 207 ? 1.0689 1.2359 1.3644 0.3922  0.2916  0.4912  179 GLU B OE2   
3498 N N     . PRO B 208 ? 0.9838 1.2547 1.3615 0.4186  0.3471  0.5610  180 PRO B N     
3499 C CA    . PRO B 208 ? 1.0016 1.2686 1.3714 0.4299  0.3684  0.5669  180 PRO B CA    
3500 C C     . PRO B 208 ? 0.9735 1.2024 1.3070 0.4394  0.3840  0.5530  180 PRO B C     
3501 O O     . PRO B 208 ? 0.9630 1.1805 1.2812 0.4454  0.3989  0.5518  180 PRO B O     
3502 C CB    . PRO B 208 ? 0.9480 1.2396 1.3429 0.4402  0.3751  0.5879  180 PRO B CB    
3503 C CG    . PRO B 208 ? 0.8705 1.1888 1.2940 0.4297  0.3542  0.5953  180 PRO B CG    
3504 C CD    . PRO B 208 ? 0.8570 1.1553 1.2640 0.4200  0.3390  0.5772  180 PRO B CD    
3505 N N     . ARG B 209 ? 0.9543 1.1627 1.2732 0.4407  0.3804  0.5426  181 ARG B N     
3506 C CA    . ARG B 209 ? 0.9970 1.1672 1.2805 0.4475  0.3930  0.5278  181 ARG B CA    
3507 C C     . ARG B 209 ? 1.0240 1.1755 1.2852 0.4394  0.3926  0.5121  181 ARG B C     
3508 O O     . ARG B 209 ? 0.9579 1.0806 1.1906 0.4460  0.4067  0.5028  181 ARG B O     
3509 C CB    . ARG B 209 ? 1.0173 1.1725 1.2931 0.4470  0.3849  0.5201  181 ARG B CB    
3510 C CG    . ARG B 209 ? 1.0355 1.1510 1.2766 0.4533  0.3962  0.5054  181 ARG B CG    
3511 C CD    . ARG B 209 ? 0.9794 1.0864 1.2185 0.4505  0.3847  0.5000  181 ARG B CD    
3512 N NE    . ARG B 209 ? 1.0674 1.1360 1.2737 0.4532  0.3921  0.4844  181 ARG B NE    
3513 C CZ    . ARG B 209 ? 1.0484 1.1031 1.2466 0.4496  0.3827  0.4765  181 ARG B CZ    
3514 N NH1   . ARG B 209 ? 0.9216 0.9963 1.1403 0.4432  0.3650  0.4820  181 ARG B NH1   
3515 N NH2   . ARG B 209 ? 1.1169 1.1363 1.2851 0.4521  0.3910  0.4630  181 ARG B NH2   
3516 N N     . TRP B 210 ? 1.0553 1.2219 1.3285 0.4253  0.3765  0.5090  182 TRP B N     
3517 C CA    . TRP B 210 ? 1.0695 1.2183 1.3219 0.4169  0.3740  0.4932  182 TRP B CA    
3518 C C     . TRP B 210 ? 1.0401 1.2104 1.3070 0.4100  0.3706  0.4993  182 TRP B C     
3519 O O     . TRP B 210 ? 1.0302 1.1860 1.2785 0.4075  0.3748  0.4896  182 TRP B O     
3520 C CB    . TRP B 210 ? 1.0434 1.1817 1.2891 0.4051  0.3562  0.4788  182 TRP B CB    
3521 C CG    . TRP B 210 ? 1.0146 1.1315 1.2460 0.4102  0.3574  0.4723  182 TRP B CG    
3522 C CD1   . TRP B 210 ? 0.9739 1.0974 1.2167 0.4062  0.3432  0.4737  182 TRP B CD1   
3523 C CD2   . TRP B 210 ? 1.0567 1.1404 1.2584 0.4196  0.3731  0.4631  182 TRP B CD2   
3524 N NE1   . TRP B 210 ? 1.0240 1.1215 1.2467 0.4130  0.3498  0.4666  182 TRP B NE1   
3525 C CE2   . TRP B 210 ? 1.0471 1.1197 1.2448 0.4210  0.3681  0.4599  182 TRP B CE2   
3526 C CE3   . TRP B 210 ? 1.0555 1.1168 1.2327 0.4268  0.3905  0.4575  182 TRP B CE3   
3527 C CZ2   . TRP B 210 ? 1.0299 1.0704 1.2011 0.4291  0.3804  0.4515  182 TRP B CZ2   
3528 C CZ3   . TRP B 210 ? 1.0421 1.0708 1.1925 0.4344  0.4020  0.4487  182 TRP B CZ3   
3529 C CH2   . TRP B 210 ? 1.0310 1.0499 1.1791 0.4354  0.3972  0.4459  182 TRP B CH2   
3530 N N     . ALA B 211 ? 1.0187 1.2230 1.3184 0.4068  0.3630  0.5155  183 ALA B N     
3531 C CA    . ALA B 211 ? 0.9591 1.1870 1.2775 0.3969  0.3548  0.5217  183 ALA B CA    
3532 C C     . ALA B 211 ? 0.9756 1.1940 1.2779 0.3997  0.3676  0.5191  183 ALA B C     
3533 O O     . ALA B 211 ? 0.9741 1.2008 1.2811 0.3896  0.3593  0.5164  183 ALA B O     
3534 C CB    . ALA B 211 ? 0.9511 1.2148 1.3050 0.3979  0.3522  0.5433  183 ALA B CB    
3535 N N     . LEU B 212 ? 0.9882 1.1882 1.2707 0.4135  0.3871  0.5198  184 LEU B N     
3536 C CA    . LEU B 212 ? 1.0181 1.2060 1.2820 0.4171  0.3990  0.5171  184 LEU B CA    
3537 C C     . LEU B 212 ? 1.0844 1.2484 1.3231 0.4086  0.3929  0.4969  184 LEU B C     
3538 O O     . LEU B 212 ? 1.0487 1.2163 1.2853 0.4029  0.3908  0.4949  184 LEU B O     
3539 C CB    . LEU B 212 ? 0.8336 1.0020 1.0782 0.4336  0.4197  0.5204  184 LEU B CB    
3540 N N     . TYR B 213 ? 1.0485 1.1879 1.2680 0.4080  0.3901  0.4821  185 TYR B N     
3541 C CA    . TYR B 213 ? 1.0297 1.1452 1.2246 0.4003  0.3846  0.4627  185 TYR B CA    
3542 C C     . TYR B 213 ? 1.0154 1.1467 1.2262 0.3848  0.3639  0.4580  185 TYR B C     
3543 O O     . TYR B 213 ? 1.0261 1.1436 1.2209 0.3776  0.3586  0.4442  185 TYR B O     
3544 C CB    . TYR B 213 ? 1.0230 1.1066 1.1924 0.4042  0.3883  0.4491  185 TYR B CB    
3545 C CG    . TYR B 213 ? 1.0552 1.1183 1.2058 0.4190  0.4078  0.4516  185 TYR B CG    
3546 C CD1   . TYR B 213 ? 1.0903 1.1262 1.2108 0.4237  0.4196  0.4427  185 TYR B CD1   
3547 C CD2   . TYR B 213 ? 1.0910 1.1607 1.2531 0.4281  0.4137  0.4626  185 TYR B CD2   
3548 C CE1   . TYR B 213 ? 1.1203 1.1351 1.2225 0.4369  0.4363  0.4442  185 TYR B CE1   
3549 C CE2   . TYR B 213 ? 1.1324 1.1821 1.2770 0.4419  0.4313  0.4646  185 TYR B CE2   
3550 C CZ    . TYR B 213 ? 1.1384 1.1602 1.2529 0.4460  0.4424  0.4552  185 TYR B CZ    
3551 O OH    . TYR B 213 ? 1.1689 1.1691 1.2652 0.4594  0.4591  0.4565  185 TYR B OH    
3552 N N     . MET B 214 ? 0.9825 1.1412 1.2236 0.3795  0.3517  0.4689  186 MET B N     
3553 C CA    . MET B 214 ? 0.9809 1.1506 1.2352 0.3648  0.3301  0.4635  186 MET B CA    
3554 C C     . MET B 214 ? 0.9396 1.1424 1.2241 0.3574  0.3216  0.4773  186 MET B C     
3555 O O     . MET B 214 ? 0.8745 1.0954 1.1807 0.3479  0.3045  0.4815  186 MET B O     
3556 C CB    . MET B 214 ? 0.9567 1.1247 1.2167 0.3629  0.3192  0.4618  186 MET B CB    
3557 C CG    . MET B 214 ? 0.9259 1.0607 1.1566 0.3690  0.3266  0.4482  186 MET B CG    
3558 S SD    . MET B 214 ? 0.9465 1.0788 1.1827 0.3667  0.3132  0.4465  186 MET B SD    
3559 C CE    . MET B 214 ? 0.9292 1.0575 1.1622 0.3493  0.2902  0.4325  186 MET B CE    
3560 N N     . GLN B 215 ? 0.9314 1.1413 1.2166 0.3615  0.3332  0.4847  187 GLN B N     
3561 C CA    . GLN B 215 ? 0.9775 1.2177 1.2904 0.3538  0.3258  0.4977  187 GLN B CA    
3562 C C     . GLN B 215 ? 0.9879 1.2282 1.3011 0.3391  0.3085  0.4868  187 GLN B C     
3563 O O     . GLN B 215 ? 0.9808 1.2444 1.3194 0.3285  0.2941  0.4947  187 GLN B O     
3564 C CB    . GLN B 215 ? 1.0017 1.2473 1.3128 0.3626  0.3434  0.5088  187 GLN B CB    
3565 C CG    . GLN B 215 ? 0.9571 1.2048 1.2703 0.3772  0.3599  0.5220  187 GLN B CG    
3566 C CD    . GLN B 215 ? 1.1004 1.3437 1.4022 0.3873  0.3779  0.5293  187 GLN B CD    
3567 O OE1   . GLN B 215 ? 1.1909 1.4343 1.4873 0.3828  0.3774  0.5271  187 GLN B OE1   
3568 N NE2   . GLN B 215 ? 1.0759 1.3143 1.3730 0.4014  0.3934  0.5382  187 GLN B NE2   
3569 N N     . ASP B 216 ? 0.9641 1.1779 1.2491 0.3379  0.3093  0.4691  188 ASP B N     
3570 C CA    . ASP B 216 ? 0.9520 1.1623 1.2337 0.3249  0.2934  0.4572  188 ASP B CA    
3571 C C     . ASP B 216 ? 0.9453 1.1401 1.2180 0.3180  0.2784  0.4437  188 ASP B C     
3572 O O     . ASP B 216 ? 0.9688 1.1413 1.2190 0.3143  0.2745  0.4273  188 ASP B O     
3573 C CB    . ASP B 216 ? 0.9787 1.1708 1.2354 0.3277  0.3032  0.4471  188 ASP B CB    
3574 C CG    . ASP B 216 ? 1.0331 1.1953 1.2586 0.3390  0.3187  0.4372  188 ASP B CG    
3575 O OD1   . ASP B 216 ? 1.0279 1.1859 1.2533 0.3466  0.3251  0.4411  188 ASP B OD1   
3576 O OD2   . ASP B 216 ? 1.0633 1.2053 1.2640 0.3402  0.3242  0.4256  188 ASP B OD2   
3577 N N     . VAL B 217 ? 0.9265 1.1329 1.2164 0.3165  0.2698  0.4510  189 VAL B N     
3578 C CA    . VAL B 217 ? 0.8945 1.0856 1.1748 0.3112  0.2565  0.4395  189 VAL B CA    
3579 C C     . VAL B 217 ? 0.8577 1.0485 1.1392 0.2961  0.2359  0.4307  189 VAL B C     
3580 O O     . VAL B 217 ? 0.8447 1.0138 1.1067 0.2916  0.2280  0.4158  189 VAL B O     
3581 C CB    . VAL B 217 ? 0.9017 1.1061 1.2000 0.3141  0.2526  0.4508  189 VAL B CB    
3582 C CG1   . VAL B 217 ? 0.9597 1.1965 1.2910 0.3065  0.2411  0.4665  189 VAL B CG1   
3583 C CG2   . VAL B 217 ? 0.8481 1.0344 1.1335 0.3100  0.2404  0.4392  189 VAL B CG2   
3584 N N     . GLU B 218 ? 0.8235 1.0370 1.1267 0.2880  0.2274  0.4399  190 GLU B N     
3585 C CA    . GLU B 218 ? 0.7563 0.9691 1.0607 0.2734  0.2074  0.4324  190 GLU B CA    
3586 C C     . GLU B 218 ? 0.7801 0.9708 1.0592 0.2712  0.2090  0.4162  190 GLU B C     
3587 O O     . GLU B 218 ? 0.7985 0.9791 1.0697 0.2607  0.1932  0.4055  190 GLU B O     
3588 C CB    . GLU B 218 ? 0.8675 1.1088 1.2007 0.2654  0.1994  0.4466  190 GLU B CB    
3589 C CG    . GLU B 218 ? 1.0815 1.3326 1.4186 0.2694  0.2130  0.4531  190 GLU B CG    
3590 C CD    . GLU B 218 ? 1.1037 1.3674 1.4502 0.2828  0.2329  0.4676  190 GLU B CD    
3591 O OE1   . GLU B 218 ? 0.9933 1.2555 1.3407 0.2899  0.2372  0.4710  190 GLU B OE1   
3592 O OE2   . GLU B 218 ? 1.1083 1.3830 1.4606 0.2864  0.2443  0.4760  190 GLU B OE2   
3593 N N     . LYS B 219 ? 0.8028 0.9852 1.0681 0.2811  0.2275  0.4144  191 LYS B N     
3594 C CA    . LYS B 219 ? 0.8094 0.9699 1.0491 0.2801  0.2299  0.3990  191 LYS B CA    
3595 C C     . LYS B 219 ? 0.8819 1.0135 1.0951 0.2833  0.2321  0.3840  191 LYS B C     
3596 O O     . LYS B 219 ? 0.8799 0.9922 1.0719 0.2803  0.2304  0.3700  191 LYS B O     
3597 C CB    . LYS B 219 ? 0.7668 0.9291 1.0007 0.2892  0.2485  0.4032  191 LYS B CB    
3598 C CG    . LYS B 219 ? 0.7538 0.9401 1.0087 0.2838  0.2449  0.4143  191 LYS B CG    
3599 C CD    . LYS B 219 ? 0.8149 1.0002 1.0601 0.2929  0.2631  0.4173  191 LYS B CD    
3600 C CE    . LYS B 219 ? 0.9019 1.1107 1.1678 0.2869  0.2589  0.4282  191 LYS B CE    
3601 N NZ    . LYS B 219 ? 0.9257 1.1348 1.1823 0.2964  0.2770  0.4328  191 LYS B NZ    
3602 N N     . PHE B 220 ? 0.8222 0.9506 1.0361 0.2893  0.2359  0.3870  192 PHE B N     
3603 C CA    . PHE B 220 ? 0.7935 0.8956 0.9847 0.2912  0.2364  0.3741  192 PHE B CA    
3604 C C     . PHE B 220 ? 0.7104 0.8117 0.9064 0.2812  0.2165  0.3704  192 PHE B C     
3605 O O     . PHE B 220 ? 0.7329 0.8149 0.9131 0.2825  0.2159  0.3619  192 PHE B O     
3606 C CB    . PHE B 220 ? 0.7806 0.8761 0.9665 0.3045  0.2536  0.3789  192 PHE B CB    
3607 C CG    . PHE B 220 ? 0.7960 0.8804 0.9654 0.3149  0.2742  0.3776  192 PHE B CG    
3608 C CD1   . PHE B 220 ? 0.8511 0.9539 1.0335 0.3199  0.2839  0.3901  192 PHE B CD1   
3609 C CD2   . PHE B 220 ? 0.8652 0.9195 1.0049 0.3195  0.2837  0.3641  192 PHE B CD2   
3610 C CE1   . PHE B 220 ? 0.9149 1.0055 1.0794 0.3297  0.3026  0.3891  192 PHE B CE1   
3611 C CE2   . PHE B 220 ? 0.8680 0.9096 0.9900 0.3288  0.3019  0.3626  192 PHE B CE2   
3612 C CZ    . PHE B 220 ? 0.8925 0.9517 1.0261 0.3341  0.3112  0.3751  192 PHE B CZ    
3613 N N     . VAL B 221 ? 0.6554 0.7761 0.8716 0.2711  0.2005  0.3769  193 VAL B N     
3614 C CA    . VAL B 221 ? 0.5767 0.6973 0.7974 0.2613  0.1808  0.3747  193 VAL B CA    
3615 C C     . VAL B 221 ? 0.6305 0.7458 0.8450 0.2490  0.1661  0.3653  193 VAL B C     
3616 O O     . VAL B 221 ? 0.6970 0.8216 0.9175 0.2464  0.1674  0.3676  193 VAL B O     
3617 C CB    . VAL B 221 ? 0.5658 0.7128 0.8152 0.2596  0.1733  0.3911  193 VAL B CB    
3618 C CG1   . VAL B 221 ? 0.5597 0.7057 0.8119 0.2491  0.1521  0.3886  193 VAL B CG1   
3619 C CG2   . VAL B 221 ? 0.6799 0.8317 0.9348 0.2724  0.1880  0.4004  193 VAL B CG2   
3620 N N     . SER B 222 ? 0.6146 0.7142 0.8162 0.2420  0.1529  0.3551  194 SER B N     
3621 C CA    . SER B 222 ? 0.5679 0.6614 0.7630 0.2303  0.1380  0.3464  194 SER B CA    
3622 C C     . SER B 222 ? 0.5731 0.6900 0.7924 0.2218  0.1255  0.3573  194 SER B C     
3623 O O     . SER B 222 ? 0.6005 0.7340 0.8389 0.2213  0.1202  0.3688  194 SER B O     
3624 C CB    . SER B 222 ? 0.5700 0.6448 0.7493 0.2246  0.1255  0.3360  194 SER B CB    
3625 O OG    . SER B 222 ? 0.6233 0.6955 0.8002 0.2127  0.1089  0.3304  194 SER B OG    
3626 N N     . PRO B 223 ? 0.5750 0.6938 0.7943 0.2151  0.1207  0.3543  195 PRO B N     
3627 C CA    . PRO B 223 ? 0.6031 0.7434 0.8456 0.2065  0.1093  0.3651  195 PRO B CA    
3628 C C     . PRO B 223 ? 0.5910 0.7311 0.8377 0.1962  0.0889  0.3648  195 PRO B C     
3629 O O     . PRO B 223 ? 0.6360 0.7959 0.9051 0.1906  0.0800  0.3766  195 PRO B O     
3630 C CB    . PRO B 223 ? 0.5590 0.6957 0.7949 0.2022  0.1093  0.3594  195 PRO B CB    
3631 C CG    . PRO B 223 ? 0.5453 0.6557 0.7525 0.2044  0.1131  0.3430  195 PRO B CG    
3632 C CD    . PRO B 223 ? 0.5254 0.6264 0.7235 0.2146  0.1250  0.3413  195 PRO B CD    
3633 N N     . TYR B 224 ? 0.5583 0.6765 0.7839 0.1935  0.0814  0.3521  196 TYR B N     
3634 C CA    . TYR B 224 ? 0.5894 0.7046 0.8151 0.1848  0.0627  0.3510  196 TYR B CA    
3635 C C     . TYR B 224 ? 0.7268 0.8441 0.9561 0.1899  0.0626  0.3564  196 TYR B C     
3636 O O     . TYR B 224 ? 0.7626 0.8717 0.9851 0.1847  0.0489  0.3530  196 TYR B O     
3637 C CB    . TYR B 224 ? 0.5735 0.6639 0.7739 0.1790  0.0544  0.3350  196 TYR B CB    
3638 C CG    . TYR B 224 ? 0.5782 0.6641 0.7721 0.1757  0.0565  0.3286  196 TYR B CG    
3639 C CD1   . TYR B 224 ? 0.6692 0.7652 0.8747 0.1665  0.0454  0.3326  196 TYR B CD1   
3640 C CD2   . TYR B 224 ? 0.5590 0.6306 0.7351 0.1818  0.0697  0.3190  196 TYR B CD2   
3641 C CE1   . TYR B 224 ? 0.6100 0.7018 0.8094 0.1639  0.0473  0.3272  196 TYR B CE1   
3642 C CE2   . TYR B 224 ? 0.5684 0.6365 0.7383 0.1792  0.0713  0.3136  196 TYR B CE2   
3643 C CZ    . TYR B 224 ? 0.5632 0.6415 0.7448 0.1704  0.0601  0.3178  196 TYR B CZ    
3644 O OH    . TYR B 224 ? 0.5552 0.6297 0.7304 0.1681  0.0617  0.3128  196 TYR B OH    
3645 N N     . GLN B 225 ? 0.7110 0.8388 0.9501 0.2004  0.0778  0.3649  197 GLN B N     
3646 C CA    . GLN B 225 ? 0.7199 0.8507 0.9635 0.2063  0.0787  0.3711  197 GLN B CA    
3647 C C     . GLN B 225 ? 0.7706 0.9203 1.0352 0.1993  0.0629  0.3826  197 GLN B C     
3648 O O     . GLN B 225 ? 0.8082 0.9508 1.0666 0.1957  0.0504  0.3805  197 GLN B O     
3649 C CB    . GLN B 225 ? 0.6743 0.8137 0.9255 0.2193  0.0990  0.3789  197 GLN B CB    
3650 C CG    . GLN B 225 ? 0.6890 0.8312 0.9446 0.2268  0.1019  0.3858  197 GLN B CG    
3651 C CD    . GLN B 225 ? 0.7417 0.8575 0.9718 0.2297  0.1028  0.3735  197 GLN B CD    
3652 O OE1   . GLN B 225 ? 0.7288 0.8246 0.9379 0.2303  0.1089  0.3608  197 GLN B OE1   
3653 N NE2   . GLN B 225 ? 0.7815 0.8973 1.0133 0.2314  0.0966  0.3777  197 GLN B NE2   
3654 N N     . HIS B 226 ? 0.7386 0.9127 1.0280 0.1972  0.0635  0.3954  198 HIS B N     
3655 C CA    . HIS B 226 ? 0.7200 0.9147 1.0322 0.1900  0.0492  0.4078  198 HIS B CA    
3656 C C     . HIS B 226 ? 0.7364 0.9291 1.0484 0.1760  0.0313  0.4038  198 HIS B C     
3657 O O     . HIS B 226 ? 0.7769 0.9884 1.1100 0.1685  0.0199  0.4148  198 HIS B O     
3658 C CB    . HIS B 226 ? 0.6747 0.8979 1.0156 0.1945  0.0593  0.4250  198 HIS B CB    
3659 C CG    . HIS B 226 ? 0.7057 0.9308 1.0468 0.2089  0.0784  0.4295  198 HIS B CG    
3660 N ND1   . HIS B 226 ? 0.7458 0.9665 1.0828 0.2155  0.0790  0.4307  198 HIS B ND1   
3661 C CD2   . HIS B 226 ? 0.6986 0.9287 1.0424 0.2185  0.0980  0.4331  198 HIS B CD2   
3662 C CE1   . HIS B 226 ? 0.7509 0.9732 1.0884 0.2283  0.0981  0.4348  198 HIS B CE1   
3663 N NE2   . HIS B 226 ? 0.7258 0.9536 1.0668 0.2304  0.1100  0.4362  198 HIS B NE2   
3664 N N     . SER B 227 ? 0.7581 0.9283 1.0467 0.1724  0.0286  0.3888  199 SER B N     
3665 C CA    . SER B 227 ? 0.7828 0.9484 1.0687 0.1598  0.0121  0.3841  199 SER B CA    
3666 C C     . SER B 227 ? 0.8371 0.9959 1.1171 0.1535  -0.0056 0.3823  199 SER B C     
3667 O O     . SER B 227 ? 0.8430 0.9853 1.1046 0.1579  -0.0055 0.3748  199 SER B O     
3668 C CB    . SER B 227 ? 0.7763 0.9199 1.0385 0.1587  0.0155  0.3687  199 SER B CB    
3669 O OG    . SER B 227 ? 0.7780 0.9139 1.0345 0.1472  -0.0007 0.3631  199 SER B OG    
3670 N N     . GLU B 228 ? 0.8457 1.0173 1.1414 0.1430  -0.0209 0.3897  200 GLU B N     
3671 C CA    . GLU B 228 ? 0.8340 0.9989 1.1232 0.1361  -0.0389 0.3878  200 GLU B CA    
3672 C C     . GLU B 228 ? 0.8652 1.0037 1.1272 0.1304  -0.0478 0.3720  200 GLU B C     
3673 O O     . GLU B 228 ? 0.8620 0.9885 1.1105 0.1273  -0.0598 0.3673  200 GLU B O     
3674 C CB    . GLU B 228 ? 0.7296 0.9172 1.0451 0.1263  -0.0524 0.4015  200 GLU B CB    
3675 N N     . ASP B 229 ? 0.7722 0.9018 1.0258 0.1292  -0.0420 0.3641  201 ASP B N     
3676 C CA    . ASP B 229 ? 0.7419 0.8467 0.9698 0.1246  -0.0487 0.3491  201 ASP B CA    
3677 C C     . ASP B 229 ? 0.7336 0.8275 0.9489 0.1304  -0.0338 0.3400  201 ASP B C     
3678 O O     . ASP B 229 ? 0.7430 0.8393 0.9621 0.1266  -0.0324 0.3390  201 ASP B O     
3679 C CB    . ASP B 229 ? 0.7520 0.8589 0.9857 0.1123  -0.0647 0.3501  201 ASP B CB    
3680 C CG    . ASP B 229 ? 0.8155 0.8968 1.0227 0.1081  -0.0716 0.3351  201 ASP B CG    
3681 O OD1   . ASP B 229 ? 0.8301 0.8927 1.0147 0.1134  -0.0681 0.3250  201 ASP B OD1   
3682 O OD2   . ASP B 229 ? 0.8562 0.9363 1.0656 0.0995  -0.0802 0.3340  201 ASP B OD2   
3683 N N     . PRO B 230 ? 0.6884 0.7703 0.8886 0.1395  -0.0222 0.3336  202 PRO B N     
3684 C CA    . PRO B 230 ? 0.6589 0.7309 0.8472 0.1450  -0.0077 0.3252  202 PRO B CA    
3685 C C     . PRO B 230 ? 0.6366 0.6902 0.8060 0.1391  -0.0137 0.3125  202 PRO B C     
3686 O O     . PRO B 230 ? 0.6465 0.6994 0.8143 0.1398  -0.0061 0.3091  202 PRO B O     
3687 C CB    . PRO B 230 ? 0.7066 0.7678 0.8820 0.1545  0.0033  0.3211  202 PRO B CB    
3688 C CG    . PRO B 230 ? 0.7015 0.7744 0.8896 0.1561  -0.0019 0.3315  202 PRO B CG    
3689 C CD    . PRO B 230 ? 0.7434 0.8221 0.9390 0.1455  -0.0209 0.3353  202 PRO B CD    
3690 N N     . VAL B 231 ? 0.6655 0.7040 0.8200 0.1337  -0.0269 0.3056  203 VAL B N     
3691 C CA    . VAL B 231 ? 0.6686 0.6894 0.8049 0.1285  -0.0327 0.2938  203 VAL B CA    
3692 C C     . VAL B 231 ? 0.6481 0.6786 0.7970 0.1210  -0.0394 0.2976  203 VAL B C     
3693 O O     . VAL B 231 ? 0.6767 0.6995 0.8174 0.1197  -0.0366 0.2907  203 VAL B O     
3694 C CB    . VAL B 231 ? 0.7221 0.7257 0.8403 0.1248  -0.0453 0.2871  203 VAL B CB    
3695 C CG1   . VAL B 231 ? 0.6892 0.6768 0.7915 0.1188  -0.0529 0.2767  203 VAL B CG1   
3696 C CG2   . VAL B 231 ? 0.6857 0.6767 0.7888 0.1321  -0.0371 0.2820  203 VAL B CG2   
3697 N N     . GLY B 232 ? 0.6793 0.7270 0.8488 0.1157  -0.0483 0.3092  204 GLY B N     
3698 C CA    . GLY B 232 ? 0.6757 0.7332 0.8590 0.1079  -0.0547 0.3141  204 GLY B CA    
3699 C C     . GLY B 232 ? 0.6542 0.7242 0.8496 0.1119  -0.0409 0.3187  204 GLY B C     
3700 O O     . GLY B 232 ? 0.6356 0.7026 0.8291 0.1083  -0.0415 0.3157  204 GLY B O     
3701 N N     . GLU B 233 ? 0.6647 0.7483 0.8717 0.1200  -0.0281 0.3263  205 GLU B N     
3702 C CA    . GLU B 233 ? 0.6558 0.7518 0.8737 0.1249  -0.0138 0.3314  205 GLU B CA    
3703 C C     . GLU B 233 ? 0.6328 0.7116 0.8291 0.1296  -0.0040 0.3187  205 GLU B C     
3704 O O     . GLU B 233 ? 0.6108 0.6932 0.8097 0.1293  0.0012  0.3191  205 GLU B O     
3705 C CB    . GLU B 233 ? 0.6066 0.7198 0.8402 0.1335  -0.0016 0.3422  205 GLU B CB    
3706 C CG    . GLU B 233 ? 0.6855 0.8219 0.9465 0.1290  -0.0089 0.3580  205 GLU B CG    
3707 C CD    . GLU B 233 ? 0.7857 0.9412 1.0642 0.1383  0.0053  0.3698  205 GLU B CD    
3708 O OE1   . GLU B 233 ? 0.8193 0.9722 1.0911 0.1476  0.0218  0.3670  205 GLU B OE1   
3709 O OE2   . GLU B 233 ? 0.7762 0.9493 1.0748 0.1366  0.0001  0.3820  205 GLU B OE2   
3710 N N     . PHE B 234 ? 0.5946 0.6550 0.7698 0.1339  -0.0015 0.3079  206 PHE B N     
3711 C CA    . PHE B 234 ? 0.5762 0.6210 0.7317 0.1382  0.0078  0.2962  206 PHE B CA    
3712 C C     . PHE B 234 ? 0.6331 0.6651 0.7766 0.1307  -0.0025 0.2875  206 PHE B C     
3713 O O     . PHE B 234 ? 0.6770 0.7047 0.8133 0.1322  0.0039  0.2824  206 PHE B O     
3714 C CB    . PHE B 234 ? 0.5760 0.6054 0.7138 0.1444  0.0138  0.2880  206 PHE B CB    
3715 C CG    . PHE B 234 ? 0.5705 0.5881 0.6922 0.1505  0.0271  0.2787  206 PHE B CG    
3716 C CD1   . PHE B 234 ? 0.5556 0.5832 0.6842 0.1572  0.0419  0.2831  206 PHE B CD1   
3717 C CD2   . PHE B 234 ? 0.5429 0.5397 0.6424 0.1497  0.0252  0.2659  206 PHE B CD2   
3718 C CE1   . PHE B 234 ? 0.4889 0.5054 0.6017 0.1630  0.0540  0.2746  206 PHE B CE1   
3719 C CE2   . PHE B 234 ? 0.4863 0.4731 0.5717 0.1550  0.0374  0.2577  206 PHE B CE2   
3720 C CZ    . PHE B 234 ? 0.4701 0.4663 0.5617 0.1616  0.0516  0.2619  206 PHE B CZ    
3721 N N     . ARG B 235 ? 0.6453 0.6709 0.7859 0.1230  -0.0184 0.2858  207 ARG B N     
3722 C CA    . ARG B 235 ? 0.6715 0.6852 0.8018 0.1161  -0.0284 0.2785  207 ARG B CA    
3723 C C     . ARG B 235 ? 0.6584 0.6854 0.8044 0.1119  -0.0291 0.2857  207 ARG B C     
3724 O O     . ARG B 235 ? 0.6527 0.6719 0.7900 0.1103  -0.0291 0.2796  207 ARG B O     
3725 C CB    . ARG B 235 ? 0.6779 0.6826 0.8023 0.1092  -0.0447 0.2763  207 ARG B CB    
3726 C CG    . ARG B 235 ? 0.6906 0.6824 0.8044 0.1025  -0.0552 0.2691  207 ARG B CG    
3727 C CD    . ARG B 235 ? 0.7494 0.7311 0.8555 0.0964  -0.0705 0.2667  207 ARG B CD    
3728 N NE    . ARG B 235 ? 0.8501 0.8123 0.9329 0.1000  -0.0700 0.2558  207 ARG B NE    
3729 C CZ    . ARG B 235 ? 0.8900 0.8476 0.9667 0.1010  -0.0742 0.2558  207 ARG B CZ    
3730 N NH1   . ARG B 235 ? 0.9069 0.8778 0.9986 0.0988  -0.0799 0.2659  207 ARG B NH1   
3731 N NH2   . ARG B 235 ? 0.8245 0.7640 0.8796 0.1042  -0.0728 0.2461  207 ARG B NH2   
3732 N N     . LEU B 236 ? 0.6371 0.6846 0.8068 0.1101  -0.0297 0.2992  208 LEU B N     
3733 C CA    . LEU B 236 ? 0.6020 0.6635 0.7884 0.1061  -0.0294 0.3077  208 LEU B CA    
3734 C C     . LEU B 236 ? 0.5926 0.6585 0.7778 0.1138  -0.0130 0.3075  208 LEU B C     
3735 O O     . LEU B 236 ? 0.6013 0.6673 0.7863 0.1115  -0.0124 0.3071  208 LEU B O     
3736 C CB    . LEU B 236 ? 0.5422 0.6261 0.7558 0.1023  -0.0335 0.3234  208 LEU B CB    
3737 C CG    . LEU B 236 ? 0.5537 0.6544 0.7878 0.0978  -0.0327 0.3345  208 LEU B CG    
3738 C CD1   . LEU B 236 ? 0.5640 0.6529 0.7912 0.0887  -0.0450 0.3293  208 LEU B CD1   
3739 C CD2   . LEU B 236 ? 0.5809 0.7055 0.8438 0.0944  -0.0358 0.3510  208 LEU B CD2   
3740 N N     . LEU B 237 ? 0.5804 0.6495 0.7640 0.1231  0.0004  0.3080  209 LEU B N     
3741 C CA    . LEU B 237 ? 0.5478 0.6212 0.7297 0.1312  0.0168  0.3083  209 LEU B CA    
3742 C C     . LEU B 237 ? 0.5608 0.6159 0.7201 0.1320  0.0184  0.2950  209 LEU B C     
3743 O O     . LEU B 237 ? 0.6040 0.6624 0.7630 0.1338  0.0251  0.2957  209 LEU B O     
3744 C CB    . LEU B 237 ? 0.5491 0.6267 0.7316 0.1413  0.0306  0.3106  209 LEU B CB    
3745 C CG    . LEU B 237 ? 0.4949 0.5749 0.6729 0.1509  0.0487  0.3103  209 LEU B CG    
3746 C CD1   . LEU B 237 ? 0.5399 0.6402 0.7378 0.1507  0.0535  0.3230  209 LEU B CD1   
3747 C CD2   . LEU B 237 ? 0.4782 0.5577 0.6532 0.1610  0.0619  0.3108  209 LEU B CD2   
3748 N N     . LEU B 238 ? 0.5662 0.6023 0.7066 0.1309  0.0124  0.2833  210 LEU B N     
3749 C CA    . LEU B 238 ? 0.5898 0.6094 0.7098 0.1314  0.0133  0.2710  210 LEU B CA    
3750 C C     . LEU B 238 ? 0.6460 0.6637 0.7670 0.1237  0.0026  0.2704  210 LEU B C     
3751 O O     . LEU B 238 ? 0.6926 0.7078 0.8070 0.1253  0.0073  0.2670  210 LEU B O     
3752 C CB    . LEU B 238 ? 0.5980 0.5989 0.6992 0.1317  0.0093  0.2599  210 LEU B CB    
3753 C CG    . LEU B 238 ? 0.5416 0.5396 0.6369 0.1400  0.0213  0.2580  210 LEU B CG    
3754 C CD1   . LEU B 238 ? 0.4569 0.4358 0.5335 0.1392  0.0166  0.2472  210 LEU B CD1   
3755 C CD2   . LEU B 238 ? 0.5275 0.5273 0.6181 0.1482  0.0379  0.2567  210 LEU B CD2   
3756 N N     . GLU B 239 ? 0.6607 0.6793 0.7895 0.1155  -0.0117 0.2739  211 GLU B N     
3757 C CA    . GLU B 239 ? 0.6455 0.6606 0.7749 0.1080  -0.0222 0.2734  211 GLU B CA    
3758 C C     . GLU B 239 ? 0.5907 0.6224 0.7370 0.1073  -0.0171 0.2840  211 GLU B C     
3759 O O     . GLU B 239 ? 0.5803 0.6079 0.7233 0.1041  -0.0204 0.2823  211 GLU B O     
3760 C CB    . GLU B 239 ? 0.6654 0.6772 0.7991 0.0997  -0.0382 0.2752  211 GLU B CB    
3761 C CG    . GLU B 239 ? 0.7302 0.7228 0.8442 0.0997  -0.0448 0.2639  211 GLU B CG    
3762 C CD    . GLU B 239 ? 0.8431 0.8350 0.9622 0.0930  -0.0586 0.2674  211 GLU B CD    
3763 O OE1   . GLU B 239 ? 0.8173 0.8256 0.9572 0.0889  -0.0621 0.2792  211 GLU B OE1   
3764 O OE2   . GLU B 239 ? 0.8487 0.8244 0.9514 0.0919  -0.0659 0.2588  211 GLU B OE2   
3765 N N     . SER B 240 ? 0.5710 0.6214 0.7354 0.1107  -0.0087 0.2954  212 SER B N     
3766 C CA    . SER B 240 ? 0.5702 0.6377 0.7513 0.1108  -0.0023 0.3066  212 SER B CA    
3767 C C     . SER B 240 ? 0.5847 0.6501 0.7547 0.1184  0.0112  0.3025  212 SER B C     
3768 O O     . SER B 240 ? 0.6690 0.7458 0.8491 0.1187  0.0163  0.3105  212 SER B O     
3769 C CB    . SER B 240 ? 0.5935 0.6827 0.7979 0.1130  0.0035  0.3207  212 SER B CB    
3770 O OG    . SER B 240 ? 0.6213 0.7124 0.8207 0.1235  0.0179  0.3194  212 SER B OG    
3771 N N     . GLU B 241 ? 0.6068 0.6580 0.7565 0.1245  0.0170  0.2908  213 GLU B N     
3772 C CA    . GLU B 241 ? 0.6223 0.6703 0.7595 0.1318  0.0294  0.2862  213 GLU B CA    
3773 C C     . GLU B 241 ? 0.6455 0.6751 0.7622 0.1298  0.0233  0.2734  213 GLU B C     
3774 O O     . GLU B 241 ? 0.6253 0.6493 0.7280 0.1361  0.0326  0.2673  213 GLU B O     
3775 C CB    . GLU B 241 ? 0.6188 0.6668 0.7500 0.1418  0.0437  0.2843  213 GLU B CB    
3776 C CG    . GLU B 241 ? 0.6376 0.7051 0.7883 0.1466  0.0537  0.2977  213 GLU B CG    
3777 C CD    . GLU B 241 ? 0.7867 0.8688 0.9480 0.1485  0.0613  0.3073  213 GLU B CD    
3778 O OE1   . GLU B 241 ? 0.7862 0.8620 0.9338 0.1522  0.0674  0.3021  213 GLU B OE1   
3779 O OE2   . GLU B 241 ? 0.8363 0.9366 1.0199 0.1464  0.0612  0.3207  213 GLU B OE2   
3780 N N     . GLY B 242 ? 0.6949 0.7151 0.8094 0.1216  0.0082  0.2696  214 GLY B N     
3781 C CA    . GLY B 242 ? 0.7242 0.7281 0.8210 0.1197  0.0020  0.2585  214 GLY B CA    
3782 C C     . GLY B 242 ? 0.7250 0.7130 0.8042 0.1221  0.0009  0.2466  214 GLY B C     
3783 O O     . GLY B 242 ? 0.7318 0.7097 0.7952 0.1254  0.0040  0.2375  214 GLY B O     
3784 N N     . PHE B 243 ? 0.6754 0.6616 0.7573 0.1205  -0.0033 0.2469  215 PHE B N     
3785 C CA    . PHE B 243 ? 0.6256 0.5970 0.6917 0.1224  -0.0045 0.2367  215 PHE B CA    
3786 C C     . PHE B 243 ? 0.6172 0.5795 0.6815 0.1152  -0.0199 0.2344  215 PHE B C     
3787 O O     . PHE B 243 ? 0.6379 0.6078 0.7159 0.1098  -0.0279 0.2424  215 PHE B O     
3788 C CB    . PHE B 243 ? 0.5817 0.5571 0.6492 0.1287  0.0063  0.2384  215 PHE B CB    
3789 C CG    . PHE B 243 ? 0.5586 0.5355 0.6193 0.1373  0.0223  0.2362  215 PHE B CG    
3790 C CD1   . PHE B 243 ? 0.5567 0.5197 0.5986 0.1413  0.0273  0.2253  215 PHE B CD1   
3791 C CD2   . PHE B 243 ? 0.6051 0.5972 0.6778 0.1418  0.0330  0.2454  215 PHE B CD2   
3792 C CE1   . PHE B 243 ? 0.5358 0.4989 0.5698 0.1494  0.0420  0.2231  215 PHE B CE1   
3793 C CE2   . PHE B 243 ? 0.5977 0.5895 0.6620 0.1504  0.0480  0.2433  215 PHE B CE2   
3794 C CZ    . PHE B 243 ? 0.5169 0.4937 0.5613 0.1541  0.0523  0.2319  215 PHE B CZ    
3795 N N     . GLN B 244 ? 0.6273 0.5731 0.6744 0.1155  -0.0236 0.2238  216 GLN B N     
3796 C CA    . GLN B 244 ? 0.6535 0.5881 0.6949 0.1102  -0.0369 0.2205  216 GLN B CA    
3797 C C     . GLN B 244 ? 0.6379 0.5681 0.6739 0.1131  -0.0342 0.2184  216 GLN B C     
3798 O O     . GLN B 244 ? 0.6285 0.5492 0.6509 0.1176  -0.0277 0.2105  216 GLN B O     
3799 C CB    . GLN B 244 ? 0.7093 0.6286 0.7354 0.1090  -0.0430 0.2108  216 GLN B CB    
3800 C CG    . GLN B 244 ? 0.7806 0.6868 0.7986 0.1045  -0.0560 0.2070  216 GLN B CG    
3801 C CD    . GLN B 244 ? 0.7969 0.6876 0.7988 0.1052  -0.0598 0.1970  216 GLN B CD    
3802 O OE1   . GLN B 244 ? 0.8317 0.7206 0.8266 0.1099  -0.0516 0.1916  216 GLN B OE1   
3803 N NE2   . GLN B 244 ? 0.7660 0.6459 0.7621 0.1009  -0.0717 0.1947  216 GLN B NE2   
3804 N N     . VAL B 245 ? 0.6105 0.5481 0.6575 0.1106  -0.0390 0.2260  217 VAL B N     
3805 C CA    . VAL B 245 ? 0.6156 0.5500 0.6585 0.1134  -0.0368 0.2254  217 VAL B CA    
3806 C C     . VAL B 245 ? 0.6420 0.5583 0.6678 0.1110  -0.0462 0.2171  217 VAL B C     
3807 O O     . VAL B 245 ? 0.6785 0.5915 0.7049 0.1054  -0.0589 0.2187  217 VAL B O     
3808 C CB    . VAL B 245 ? 0.6402 0.5889 0.7006 0.1117  -0.0397 0.2367  217 VAL B CB    
3809 C CG1   . VAL B 245 ? 0.6511 0.5952 0.7058 0.1148  -0.0385 0.2360  217 VAL B CG1   
3810 C CG2   . VAL B 245 ? 0.6147 0.5818 0.6921 0.1151  -0.0289 0.2455  217 VAL B CG2   
3811 N N     . LEU B 246 ? 0.6871 0.5919 0.6977 0.1153  -0.0393 0.2085  218 LEU B N     
3812 C CA    . LEU B 246 ? 0.6078 0.4956 0.6019 0.1138  -0.0466 0.2010  218 LEU B CA    
3813 C C     . LEU B 246 ? 0.6026 0.4869 0.5936 0.1141  -0.0495 0.2032  218 LEU B C     
3814 O O     . LEU B 246 ? 0.7133 0.5865 0.6943 0.1111  -0.0597 0.2006  218 LEU B O     
3815 C CB    . LEU B 246 ? 0.5646 0.4427 0.5447 0.1183  -0.0375 0.1913  218 LEU B CB    
3816 C CG    . LEU B 246 ? 0.6506 0.5306 0.6308 0.1190  -0.0346 0.1880  218 LEU B CG    
3817 C CD1   . LEU B 246 ? 0.6963 0.5672 0.6615 0.1243  -0.0245 0.1782  218 LEU B CD1   
3818 C CD2   . LEU B 246 ? 0.7188 0.5941 0.6988 0.1133  -0.0485 0.1877  218 LEU B CD2   
3819 N N     . ARG B 247 ? 0.6275 0.5207 0.6261 0.1181  -0.0404 0.2081  219 ARG B N     
3820 C CA    . ARG B 247 ? 0.6287 0.5186 0.6240 0.1192  -0.0419 0.2105  219 ARG B CA    
3821 C C     . ARG B 247 ? 0.6416 0.5469 0.6523 0.1231  -0.0335 0.2191  219 ARG B C     
3822 O O     . ARG B 247 ? 0.5808 0.4931 0.5969 0.1275  -0.0210 0.2195  219 ARG B O     
3823 C CB    . ARG B 247 ? 0.6736 0.5480 0.6507 0.1225  -0.0356 0.2018  219 ARG B CB    
3824 C CG    . ARG B 247 ? 0.8309 0.6990 0.8015 0.1231  -0.0386 0.2036  219 ARG B CG    
3825 C CD    . ARG B 247 ? 0.9179 0.7696 0.8695 0.1253  -0.0328 0.1945  219 ARG B CD    
3826 N NE    . ARG B 247 ? 1.0154 0.8608 0.9599 0.1265  -0.0335 0.1964  219 ARG B NE    
3827 C CZ    . ARG B 247 ? 0.9929 0.8235 0.9204 0.1258  -0.0360 0.1910  219 ARG B CZ    
3828 N NH1   . ARG B 247 ? 1.0136 0.8341 0.9293 0.1244  -0.0378 0.1830  219 ARG B NH1   
3829 N NH2   . ARG B 247 ? 0.9407 0.7667 0.8626 0.1271  -0.0362 0.1939  219 ARG B NH2   
3830 N N     . CYS B 248 ? 0.6721 0.5827 0.6895 0.1219  -0.0400 0.2262  220 CYS B N     
3831 C CA    . CYS B 248 ? 0.6598 0.5868 0.6942 0.1257  -0.0332 0.2359  220 CYS B CA    
3832 C C     . CYS B 248 ? 0.7169 0.6436 0.7512 0.1256  -0.0399 0.2408  220 CYS B C     
3833 O O     . CYS B 248 ? 0.7551 0.6839 0.7927 0.1202  -0.0535 0.2445  220 CYS B O     
3834 C CB    . CYS B 248 ? 0.6188 0.5635 0.6730 0.1226  -0.0358 0.2441  220 CYS B CB    
3835 S SG    . CYS B 248 ? 0.7330 0.6996 0.8093 0.1286  -0.0236 0.2560  220 CYS B SG    
3836 N N     . ASP B 249 ? 0.7083 0.6324 0.7390 0.1318  -0.0302 0.2410  221 ASP B N     
3837 C CA    . ASP B 249 ? 0.6794 0.6027 0.7090 0.1328  -0.0353 0.2458  221 ASP B CA    
3838 C C     . ASP B 249 ? 0.6233 0.5579 0.6647 0.1401  -0.0230 0.2529  221 ASP B C     
3839 O O     . ASP B 249 ? 0.6473 0.5862 0.6931 0.1450  -0.0093 0.2521  221 ASP B O     
3840 C CB    . ASP B 249 ? 0.7589 0.6614 0.7658 0.1327  -0.0373 0.2375  221 ASP B CB    
3841 C CG    . ASP B 249 ? 0.8190 0.7089 0.8126 0.1269  -0.0468 0.2296  221 ASP B CG    
3842 O OD1   . ASP B 249 ? 0.8500 0.7420 0.8458 0.1216  -0.0606 0.2324  221 ASP B OD1   
3843 O OD2   . ASP B 249 ? 0.8038 0.6821 0.7849 0.1280  -0.0400 0.2207  221 ASP B OD2   
3844 N N     . LEU B 250 ? 0.5631 0.5021 0.6089 0.1413  -0.0280 0.2599  222 LEU B N     
3845 C CA    . LEU B 250 ? 0.5283 0.4772 0.5848 0.1489  -0.0173 0.2674  222 LEU B CA    
3846 C C     . LEU B 250 ? 0.5452 0.4820 0.5887 0.1516  -0.0185 0.2665  222 LEU B C     
3847 O O     . LEU B 250 ? 0.5969 0.5287 0.6338 0.1472  -0.0322 0.2672  222 LEU B O     
3848 C CB    . LEU B 250 ? 0.5281 0.5003 0.6093 0.1482  -0.0218 0.2803  222 LEU B CB    
3849 C CG    . LEU B 250 ? 0.5340 0.5185 0.6283 0.1562  -0.0123 0.2899  222 LEU B CG    
3850 C CD1   . LEU B 250 ? 0.5382 0.5233 0.6336 0.1640  0.0068  0.2880  222 LEU B CD1   
3851 C CD2   . LEU B 250 ? 0.5344 0.5426 0.6535 0.1541  -0.0194 0.3032  222 LEU B CD2   
3852 N N     . GLY B 251 ? 0.5790 0.5105 0.6179 0.1591  -0.0039 0.2650  223 GLY B N     
3853 C CA    . GLY B 251 ? 0.5816 0.5014 0.6084 0.1623  -0.0030 0.2646  223 GLY B CA    
3854 C C     . GLY B 251 ? 0.5894 0.5114 0.6204 0.1717  0.0134  0.2679  223 GLY B C     
3855 O O     . GLY B 251 ? 0.6207 0.5478 0.6579 0.1761  0.0265  0.2672  223 GLY B O     
3856 N N     . PRO B 252 ? 0.5734 0.4909 0.6002 0.1754  0.0131  0.2719  224 PRO B N     
3857 C CA    . PRO B 252 ? 0.5883 0.5060 0.6178 0.1849  0.0289  0.2752  224 PRO B CA    
3858 C C     . PRO B 252 ? 0.6227 0.5200 0.6328 0.1877  0.0422  0.2646  224 PRO B C     
3859 O O     . PRO B 252 ? 0.6268 0.5089 0.6202 0.1826  0.0381  0.2557  224 PRO B O     
3860 C CB    . PRO B 252 ? 0.6461 0.5659 0.6775 0.1869  0.0213  0.2835  224 PRO B CB    
3861 C CG    . PRO B 252 ? 0.6393 0.5479 0.6562 0.1789  0.0055  0.2790  224 PRO B CG    
3862 C CD    . PRO B 252 ? 0.5834 0.4954 0.6024 0.1714  -0.0019 0.2741  224 PRO B CD    
3863 N N     . GLN B 253 ? 0.6246 0.5216 0.6372 0.1963  0.0589  0.2659  225 GLN B N     
3864 C CA    . GLN B 253 ? 0.6065 0.4843 0.6015 0.1998  0.0735  0.2564  225 GLN B CA    
3865 C C     . GLN B 253 ? 0.6120 0.4862 0.6071 0.2093  0.0863  0.2612  225 GLN B C     
3866 O O     . GLN B 253 ? 0.6172 0.5066 0.6287 0.2151  0.0899  0.2708  225 GLN B O     
3867 C CB    . GLN B 253 ? 0.6235 0.5008 0.6175 0.2002  0.0835  0.2495  225 GLN B CB    
3868 C CG    . GLN B 253 ? 0.6032 0.4813 0.5947 0.1914  0.0726  0.2435  225 GLN B CG    
3869 C CD    . GLN B 253 ? 0.7133 0.5719 0.6841 0.1864  0.0692  0.2334  225 GLN B CD    
3870 O OE1   . GLN B 253 ? 0.7723 0.6150 0.7288 0.1897  0.0791  0.2285  225 GLN B OE1   
3871 N NE2   . GLN B 253 ? 0.6798 0.5392 0.6486 0.1785  0.0557  0.2303  225 GLN B NE2   
3872 N N     . LYS B 254 ? 0.6671 0.5210 0.6438 0.2108  0.0936  0.2547  226 LYS B N     
3873 C CA    . LYS B 254 ? 0.6647 0.5104 0.6376 0.2198  0.1078  0.2572  226 LYS B CA    
3874 C C     . LYS B 254 ? 0.6548 0.4839 0.6135 0.2228  0.1249  0.2469  226 LYS B C     
3875 O O     . LYS B 254 ? 0.7276 0.5453 0.6731 0.2170  0.1245  0.2366  226 LYS B O     
3876 C CB    . LYS B 254 ? 0.7687 0.6027 0.7307 0.2195  0.1029  0.2587  226 LYS B CB    
3877 C CG    . LYS B 254 ? 0.7839 0.6323 0.7580 0.2179  0.0869  0.2696  226 LYS B CG    
3878 C CD    . LYS B 254 ? 0.8396 0.6747 0.8009 0.2187  0.0840  0.2712  226 LYS B CD    
3879 C CE    . LYS B 254 ? 0.8695 0.7177 0.8407 0.2169  0.0671  0.2817  226 LYS B CE    
3880 N NZ    . LYS B 254 ? 0.7899 0.6251 0.7479 0.2183  0.0646  0.2840  226 LYS B NZ    
3881 N N     . VAL B 255 ? 0.6467 0.4741 0.6076 0.2319  0.1402  0.2499  227 VAL B N     
3882 C CA    . VAL B 255 ? 0.6648 0.4746 0.6110 0.2355  0.1575  0.2407  227 VAL B CA    
3883 C C     . VAL B 255 ? 0.7716 0.5639 0.7059 0.2411  0.1676  0.2408  227 VAL B C     
3884 O O     . VAL B 255 ? 0.7663 0.5641 0.7092 0.2492  0.1734  0.2496  227 VAL B O     
3885 C CB    . VAL B 255 ? 0.6509 0.4708 0.6069 0.2416  0.1683  0.2432  227 VAL B CB    
3886 C CG1   . VAL B 255 ? 0.6740 0.4734 0.6119 0.2441  0.1849  0.2326  227 VAL B CG1   
3887 C CG2   . VAL B 255 ? 0.6313 0.4709 0.6016 0.2362  0.1572  0.2454  227 VAL B CG2   
3888 N N     . PHE B 256 ? 0.7854 0.5564 0.6999 0.2369  0.1702  0.2312  228 PHE B N     
3889 C CA    . PHE B 256 ? 0.7621 0.5151 0.6640 0.2407  0.1784  0.2310  228 PHE B CA    
3890 C C     . PHE B 256 ? 0.8025 0.5405 0.6953 0.2477  0.1982  0.2269  228 PHE B C     
3891 O O     . PHE B 256 ? 0.8098 0.5417 0.6960 0.2465  0.2060  0.2188  228 PHE B O     
3892 C CB    . PHE B 256 ? 0.7145 0.4506 0.5987 0.2328  0.1737  0.2226  228 PHE B CB    
3893 C CG    . PHE B 256 ? 0.7837 0.4986 0.6527 0.2358  0.1836  0.2209  228 PHE B CG    
3894 C CD1   . PHE B 256 ? 0.8507 0.5677 0.7230 0.2390  0.1785  0.2300  228 PHE B CD1   
3895 C CD2   . PHE B 256 ? 0.7896 0.4819 0.6405 0.2350  0.1979  0.2103  228 PHE B CD2   
3896 C CE1   . PHE B 256 ? 0.9268 0.6239 0.7848 0.2417  0.1877  0.2289  228 PHE B CE1   
3897 C CE2   . PHE B 256 ? 0.8263 0.4984 0.6631 0.2371  0.2072  0.2088  228 PHE B CE2   
3898 C CZ    . PHE B 256 ? 0.9404 0.6149 0.7808 0.2407  0.2023  0.2182  228 PHE B CZ    
3899 N N     . PHE B 257 ? 0.7989 0.5300 0.6904 0.2552  0.2063  0.2327  229 PHE B N     
3900 C CA    . PHE B 257 ? 0.7806 0.4935 0.6604 0.2617  0.2253  0.2289  229 PHE B CA    
3901 C C     . PHE B 257 ? 0.7841 0.4783 0.6514 0.2637  0.2301  0.2294  229 PHE B C     
3902 O O     . PHE B 257 ? 0.7904 0.4934 0.6663 0.2662  0.2221  0.2390  229 PHE B O     
3903 C CB    . PHE B 257 ? 0.7608 0.4867 0.6545 0.2716  0.2336  0.2375  229 PHE B CB    
3904 C CG    . PHE B 257 ? 0.7754 0.5178 0.6799 0.2704  0.2315  0.2370  229 PHE B CG    
3905 C CD1   . PHE B 257 ? 0.7346 0.5034 0.6598 0.2684  0.2172  0.2453  229 PHE B CD1   
3906 C CD2   . PHE B 257 ? 0.8051 0.5359 0.6983 0.2708  0.2437  0.2282  229 PHE B CD2   
3907 C CE1   . PHE B 257 ? 0.7067 0.4905 0.6419 0.2671  0.2157  0.2452  229 PHE B CE1   
3908 C CE2   . PHE B 257 ? 0.7278 0.4734 0.6302 0.2700  0.2420  0.2282  229 PHE B CE2   
3909 C CZ    . PHE B 257 ? 0.7093 0.4817 0.6330 0.2682  0.2281  0.2369  229 PHE B CZ    
3910 N N     . PRO B 258 ? 0.7897 0.4581 0.6367 0.2623  0.2428  0.2196  230 PRO B N     
3911 C CA    . PRO B 258 ? 0.8902 0.5396 0.7244 0.2632  0.2474  0.2196  230 PRO B CA    
3912 C C     . PRO B 258 ? 0.9347 0.5807 0.7721 0.2742  0.2579  0.2283  230 PRO B C     
3913 O O     . PRO B 258 ? 0.9760 0.6220 0.8156 0.2774  0.2541  0.2360  230 PRO B O     
3914 C CB    . PRO B 258 ? 0.9455 0.5691 0.7578 0.2568  0.2577  0.2056  230 PRO B CB    
3915 C CG    . PRO B 258 ? 0.8147 0.4408 0.6278 0.2573  0.2645  0.2002  230 PRO B CG    
3916 C CD    . PRO B 258 ? 0.7882 0.4435 0.6225 0.2583  0.2521  0.2075  230 PRO B CD    
3917 N N     . THR B 259 ? 0.8786 0.5211 0.7155 0.2803  0.2712  0.2272  231 THR B N     
3918 C CA    . THR B 259 ? 0.8813 0.5183 0.7194 0.2913  0.2831  0.2347  231 THR B CA    
3919 C C     . THR B 259 ? 0.8805 0.5452 0.7422 0.2991  0.2784  0.2475  231 THR B C     
3920 O O     . THR B 259 ? 0.8507 0.5380 0.7273 0.2955  0.2661  0.2503  231 THR B O     
3921 C CB    . THR B 259 ? 0.9255 0.5398 0.7469 0.2934  0.3015  0.2263  231 THR B CB    
3922 O OG1   . THR B 259 ? 0.9725 0.5992 0.8014 0.2951  0.3040  0.2256  231 THR B OG1   
3923 C CG2   . THR B 259 ? 0.9508 0.5408 0.7507 0.2832  0.3046  0.2124  231 THR B CG2   
3924 N N     . ALA B 260 ? 0.9817 0.6443 0.8466 0.3100  0.2887  0.2557  232 ALA B N     
3925 C CA    . ALA B 260 ? 0.9216 0.6096 0.8088 0.3184  0.2863  0.2687  232 ALA B CA    
3926 C C     . ALA B 260 ? 0.8671 0.5601 0.7573 0.3225  0.2969  0.2674  232 ALA B C     
3927 O O     . ALA B 260 ? 0.8515 0.5701 0.7612 0.3245  0.2909  0.2748  232 ALA B O     
3928 C CB    . ALA B 260 ? 0.9982 0.6830 0.8885 0.3288  0.2921  0.2793  232 ALA B CB    
3929 N N     . GLU B 261 ? 0.9317 0.6001 0.8023 0.3235  0.3125  0.2582  233 GLU B N     
3930 C CA    . GLU B 261 ? 0.9338 0.6046 0.8048 0.3281  0.3234  0.2575  233 GLU B CA    
3931 C C     . GLU B 261 ? 0.9111 0.5881 0.7810 0.3193  0.3176  0.2488  233 GLU B C     
3932 O O     . GLU B 261 ? 0.9791 0.6716 0.8590 0.3223  0.3194  0.2522  233 GLU B O     
3933 C CB    . GLU B 261 ? 0.9673 0.6084 0.8168 0.3330  0.3423  0.2520  233 GLU B CB    
3934 C CG    . GLU B 261 ? 1.0068 0.6489 0.8554 0.3394  0.3545  0.2529  233 GLU B CG    
3935 C CD    . GLU B 261 ? 1.1341 0.7487 0.9642 0.3463  0.3726  0.2509  233 GLU B CD    
3936 O OE1   . GLU B 261 ? 1.1820 0.7790 1.0027 0.3475  0.3761  0.2506  233 GLU B OE1   
3937 O OE2   . GLU B 261 ? 1.0838 0.6937 0.9080 0.3505  0.3832  0.2498  233 GLU B OE2   
3938 N N     . THR B 262 ? 0.9182 0.5839 0.7762 0.3085  0.3107  0.2380  234 THR B N     
3939 C CA    . THR B 262 ? 0.8727 0.5464 0.7315 0.3003  0.3034  0.2307  234 THR B CA    
3940 C C     . THR B 262 ? 0.8057 0.5118 0.6893 0.2992  0.2877  0.2397  234 THR B C     
3941 O O     . THR B 262 ? 0.7884 0.5072 0.6783 0.2960  0.2838  0.2378  234 THR B O     
3942 C CB    . THR B 262 ? 0.8277 0.4833 0.6696 0.2892  0.2989  0.2181  234 THR B CB    
3943 O OG1   . THR B 262 ? 0.8777 0.5364 0.7238 0.2863  0.2878  0.2219  234 THR B OG1   
3944 C CG2   . THR B 262 ? 0.8530 0.4764 0.6702 0.2885  0.3144  0.2081  234 THR B CG2   
3945 N N     . HIS B 263 ? 0.8042 0.5234 0.7014 0.3013  0.2784  0.2497  235 HIS B N     
3946 C CA    . HIS B 263 ? 0.7844 0.5347 0.7064 0.3011  0.2648  0.2602  235 HIS B CA    
3947 C C     . HIS B 263 ? 0.7879 0.5536 0.7237 0.3106  0.2737  0.2693  235 HIS B C     
3948 O O     . HIS B 263 ? 0.7699 0.5576 0.7214 0.3089  0.2672  0.2733  235 HIS B O     
3949 C CB    . HIS B 263 ? 0.7860 0.5443 0.7173 0.3013  0.2531  0.2688  235 HIS B CB    
3950 C CG    . HIS B 263 ? 0.7697 0.5588 0.7262 0.3011  0.2392  0.2804  235 HIS B CG    
3951 N ND1   . HIS B 263 ? 0.7459 0.5506 0.7113 0.2923  0.2253  0.2786  235 HIS B ND1   
3952 C CD2   . HIS B 263 ? 0.7751 0.5820 0.7496 0.3082  0.2370  0.2941  235 HIS B CD2   
3953 C CE1   . HIS B 263 ? 0.7376 0.5678 0.7252 0.2935  0.2150  0.2905  235 HIS B CE1   
3954 N NE2   . HIS B 263 ? 0.7547 0.5873 0.7486 0.3031  0.2218  0.3001  235 HIS B NE2   
3955 N N     . ARG B 264 ? 0.8121 0.5661 0.7419 0.3205  0.2890  0.2728  236 ARG B N     
3956 C CA    . ARG B 264 ? 0.8188 0.5856 0.7599 0.3304  0.2993  0.2818  236 ARG B CA    
3957 C C     . ARG B 264 ? 0.8180 0.5772 0.7484 0.3298  0.3094  0.2739  236 ARG B C     
3958 O O     . ARG B 264 ? 0.8064 0.5856 0.7506 0.3315  0.3087  0.2793  236 ARG B O     
3959 C CB    . ARG B 264 ? 0.8472 0.6021 0.7839 0.3415  0.3124  0.2881  236 ARG B CB    
3960 C CG    . ARG B 264 ? 0.8563 0.6260 0.8064 0.3528  0.3228  0.2996  236 ARG B CG    
3961 C CD    . ARG B 264 ? 0.8845 0.6431 0.8313 0.3637  0.3338  0.3066  236 ARG B CD    
3962 N NE    . ARG B 264 ? 0.9552 0.7270 0.9140 0.3752  0.3447  0.3181  236 ARG B NE    
3963 C CZ    . ARG B 264 ? 0.9810 0.7389 0.9271 0.3813  0.3613  0.3155  236 ARG B CZ    
3964 N NH1   . ARG B 264 ? 0.9286 0.6589 0.8494 0.3766  0.3688  0.3016  236 ARG B NH1   
3965 N NH2   . ARG B 264 ? 0.9274 0.6991 0.8858 0.3920  0.3704  0.3272  236 ARG B NH2   
3966 N N     . GLU B 265 ? 0.8317 0.5616 0.7368 0.3270  0.3188  0.2614  237 GLU B N     
3967 C CA    . GLU B 265 ? 0.8350 0.5545 0.7269 0.3264  0.3286  0.2536  237 GLU B CA    
3968 C C     . GLU B 265 ? 0.8073 0.5436 0.7075 0.3185  0.3172  0.2502  237 GLU B C     
3969 O O     . GLU B 265 ? 0.8051 0.5463 0.7052 0.3204  0.3228  0.2499  237 GLU B O     
3970 C CB    . GLU B 265 ? 0.8545 0.5390 0.7177 0.3226  0.3381  0.2400  237 GLU B CB    
3971 C CG    . GLU B 265 ? 0.8864 0.5500 0.7378 0.3307  0.3523  0.2422  237 GLU B CG    
3972 C CD    . GLU B 265 ? 0.9474 0.6151 0.8023 0.3420  0.3651  0.2504  237 GLU B CD    
3973 O OE1   . GLU B 265 ? 0.8980 0.5688 0.7503 0.3417  0.3687  0.2479  237 GLU B OE1   
3974 O OE2   . GLU B 265 ? 1.0840 0.7514 0.9438 0.3513  0.3719  0.2596  237 GLU B OE2   
3975 N N     . PHE B 266 ? 0.7874 0.5318 0.6940 0.3096  0.3012  0.2478  238 PHE B N     
3976 C CA    . PHE B 266 ? 0.7615 0.5230 0.6775 0.3023  0.2894  0.2457  238 PHE B CA    
3977 C C     . PHE B 266 ? 0.7491 0.5417 0.6909 0.3066  0.2847  0.2590  238 PHE B C     
3978 O O     . PHE B 266 ? 0.7368 0.5411 0.6842 0.3051  0.2839  0.2589  238 PHE B O     
3979 C CB    . PHE B 266 ? 0.7455 0.5076 0.6618 0.2919  0.2731  0.2408  238 PHE B CB    
3980 C CG    . PHE B 266 ? 0.7201 0.4985 0.6456 0.2840  0.2601  0.2387  238 PHE B CG    
3981 C CD1   . PHE B 266 ? 0.7153 0.4823 0.6265 0.2789  0.2626  0.2273  238 PHE B CD1   
3982 C CD2   . PHE B 266 ? 0.7023 0.5072 0.6506 0.2815  0.2452  0.2482  238 PHE B CD2   
3983 C CE1   . PHE B 266 ? 0.6930 0.4747 0.6126 0.2721  0.2508  0.2257  238 PHE B CE1   
3984 C CE2   . PHE B 266 ? 0.6806 0.4994 0.6367 0.2739  0.2333  0.2464  238 PHE B CE2   
3985 C CZ    . PHE B 266 ? 0.6758 0.4830 0.6177 0.2696  0.2362  0.2353  238 PHE B CZ    
3986 N N     . LEU B 267 ? 0.7528 0.5593 0.7108 0.3117  0.2816  0.2708  239 LEU B N     
3987 C CA    . LEU B 267 ? 0.7428 0.5793 0.7264 0.3155  0.2774  0.2843  239 LEU B CA    
3988 C C     . LEU B 267 ? 0.7553 0.5936 0.7387 0.3250  0.2941  0.2888  239 LEU B C     
3989 O O     . LEU B 267 ? 0.7451 0.6077 0.7477 0.3270  0.2921  0.2983  239 LEU B O     
3990 C CB    . LEU B 267 ? 0.7468 0.5961 0.7463 0.3189  0.2706  0.2958  239 LEU B CB    
3991 C CG    . LEU B 267 ? 0.7305 0.5875 0.7369 0.3089  0.2502  0.2953  239 LEU B CG    
3992 C CD1   . LEU B 267 ? 0.7395 0.6045 0.7573 0.3131  0.2449  0.3061  239 LEU B CD1   
3993 C CD2   . LEU B 267 ? 0.7059 0.5862 0.7290 0.3012  0.2366  0.2978  239 LEU B CD2   
3994 N N     . LYS B 268 ? 0.7785 0.5910 0.7402 0.3306  0.3103  0.2826  240 LYS B N     
3995 C CA    . LYS B 268 ? 0.7924 0.6024 0.7491 0.3388  0.3260  0.2853  240 LYS B CA    
3996 C C     . LYS B 268 ? 0.7773 0.5923 0.7314 0.3335  0.3239  0.2797  240 LYS B C     
3997 O O     . LYS B 268 ? 0.7770 0.6062 0.7399 0.3386  0.3298  0.2870  240 LYS B O     
3998 C CB    . LYS B 268 ? 0.8224 0.5996 0.7529 0.3441  0.3422  0.2782  240 LYS B CB    
3999 C CG    . LYS B 268 ? 0.8448 0.6195 0.7791 0.3546  0.3513  0.2878  240 LYS B CG    
4000 C CD    . LYS B 268 ? 0.8763 0.6168 0.7832 0.3592  0.3678  0.2803  240 LYS B CD    
4001 C CE    . LYS B 268 ? 0.9320 0.6691 0.8423 0.3705  0.3774  0.2901  240 LYS B CE    
4002 N NZ    . LYS B 268 ? 0.9405 0.6425 0.8235 0.3742  0.3928  0.2824  240 LYS B NZ    
4003 N N     . SER B 269 ? 0.7654 0.5692 0.7076 0.3236  0.3157  0.2672  241 SER B N     
4004 C CA    . SER B 269 ? 0.7538 0.5586 0.6902 0.3188  0.3145  0.2607  241 SER B CA    
4005 C C     . SER B 269 ? 0.7275 0.5641 0.6891 0.3149  0.3012  0.2687  241 SER B C     
4006 O O     . SER B 269 ? 0.7222 0.5687 0.6872 0.3162  0.3043  0.2708  241 SER B O     
4007 C CB    . SER B 269 ? 0.7511 0.5332 0.6665 0.3096  0.3102  0.2449  241 SER B CB    
4008 O OG    . SER B 269 ? 0.7291 0.5224 0.6554 0.3008  0.2929  0.2437  241 SER B OG    
4009 N N     . VAL B 270 ? 0.7124 0.5643 0.6910 0.3097  0.2861  0.2733  242 VAL B N     
4010 C CA    . VAL B 270 ? 0.7034 0.5830 0.7046 0.3037  0.2713  0.2799  242 VAL B CA    
4011 C C     . VAL B 270 ? 0.7510 0.6562 0.7762 0.3106  0.2739  0.2961  242 VAL B C     
4012 O O     . VAL B 270 ? 0.7998 0.7299 0.8469 0.3059  0.2616  0.3039  242 VAL B O     
4013 C CB    . VAL B 270 ? 0.6733 0.5559 0.6798 0.2937  0.2525  0.2771  242 VAL B CB    
4014 C CG1   . VAL B 270 ? 0.6852 0.5423 0.6678 0.2872  0.2512  0.2616  242 VAL B CG1   
4015 C CG2   . VAL B 270 ? 0.6823 0.5685 0.6977 0.2972  0.2499  0.2852  242 VAL B CG2   
4016 N N     . CYS B 271 ? 0.7601 0.6588 0.7810 0.3216  0.2900  0.3013  243 CYS B N     
4017 C CA    . CYS B 271 ? 0.7748 0.6966 0.8169 0.3295  0.2954  0.3170  243 CYS B CA    
4018 C C     . CYS B 271 ? 0.8229 0.7502 0.8636 0.3330  0.3053  0.3190  243 CYS B C     
4019 O O     . CYS B 271 ? 0.8092 0.7166 0.8295 0.3395  0.3209  0.3142  243 CYS B O     
4020 C CB    . CYS B 271 ? 0.7815 0.6933 0.8193 0.3401  0.3079  0.3225  243 CYS B CB    
4021 S SG    . CYS B 271 ? 0.7946 0.7358 0.8603 0.3502  0.3137  0.3430  243 CYS B SG    
4022 N N     . ALA B 272 ? 0.8587 0.8121 0.9203 0.3283  0.2961  0.3261  244 ALA B N     
4023 C CA    . ALA B 272 ? 0.8589 0.8183 0.9191 0.3298  0.3030  0.3273  244 ALA B CA    
4024 C C     . ALA B 272 ? 0.7965 0.7668 0.8647 0.3412  0.3184  0.3406  244 ALA B C     
4025 O O     . ALA B 272 ? 0.8491 0.8221 0.9135 0.3438  0.3261  0.3422  244 ALA B O     
4026 C CB    . ALA B 272 ? 0.9019 0.8840 0.9808 0.3195  0.2866  0.3296  244 ALA B CB    
4027 N N     . PHE B 273 ? 0.7417 0.7180 0.8204 0.3482  0.3230  0.3505  245 PHE B N     
4028 C CA    . PHE B 273 ? 0.8107 0.7987 0.8986 0.3593  0.3372  0.3644  245 PHE B CA    
4029 C C     . PHE B 273 ? 0.9263 0.8875 0.9905 0.3704  0.3556  0.3616  245 PHE B C     
4030 O O     . PHE B 273 ? 0.9698 0.9365 1.0375 0.3804  0.3687  0.3724  245 PHE B O     
4031 C CB    . PHE B 273 ? 0.7592 0.7753 0.8777 0.3604  0.3302  0.3799  245 PHE B CB    
4032 C CG    . PHE B 273 ? 0.7683 0.8152 0.9136 0.3520  0.3167  0.3882  245 PHE B CG    
4033 C CD1   . PHE B 273 ? 0.8297 0.8965 0.9889 0.3558  0.3241  0.4003  245 PHE B CD1   
4034 C CD2   . PHE B 273 ? 0.8111 0.8660 0.9667 0.3400  0.2964  0.3843  245 PHE B CD2   
4035 C CE1   . PHE B 273 ? 0.8694 0.9640 1.0536 0.3474  0.3117  0.4083  245 PHE B CE1   
4036 C CE2   . PHE B 273 ? 0.8219 0.9032 1.0012 0.3315  0.2835  0.3918  245 PHE B CE2   
4037 C CZ    . PHE B 273 ? 0.8614 0.9629 1.0556 0.3351  0.2912  0.4038  245 PHE B CZ    
4038 N N     . LEU B 274 ? 0.9454 0.8771 0.9854 0.3687  0.3568  0.3477  246 LEU B N     
4039 C CA    . LEU B 274 ? 0.9253 0.8302 0.9433 0.3785  0.3730  0.3452  246 LEU B CA    
4040 C C     . LEU B 274 ? 0.9650 0.8538 0.9624 0.3837  0.3867  0.3420  246 LEU B C     
4041 O O     . LEU B 274 ? 0.9088 0.7829 0.8945 0.3940  0.4013  0.3452  246 LEU B O     
4042 C CB    . LEU B 274 ? 0.8784 0.7558 0.8764 0.3740  0.3700  0.3312  246 LEU B CB    
4043 C CG    . LEU B 274 ? 0.8217 0.7053 0.8328 0.3744  0.3630  0.3361  246 LEU B CG    
4044 C CD1   . LEU B 274 ? 0.9154 0.7714 0.9056 0.3688  0.3596  0.3219  246 LEU B CD1   
4045 C CD2   . LEU B 274 ? 0.8417 0.7285 0.8593 0.3872  0.3757  0.3487  246 LEU B CD2   
4046 N N     . TYR B 275 ? 1.0022 0.8926 0.9944 0.3771  0.3818  0.3356  247 TYR B N     
4047 C CA    . TYR B 275 ? 1.0029 0.8771 0.9745 0.3817  0.3930  0.3322  247 TYR B CA    
4048 C C     . TYR B 275 ? 0.9800 0.8724 0.9651 0.3915  0.4026  0.3482  247 TYR B C     
4049 O O     . TYR B 275 ? 0.9511 0.8280 0.9183 0.3977  0.4132  0.3466  247 TYR B O     
4050 C CB    . TYR B 275 ? 0.9276 0.8004 0.8915 0.3722  0.3841  0.3219  247 TYR B CB    
4051 C CG    . TYR B 275 ? 0.9374 0.8433 0.9259 0.3692  0.3769  0.3323  247 TYR B CG    
4052 C CD1   . TYR B 275 ? 0.9325 0.8633 0.9460 0.3607  0.3616  0.3356  247 TYR B CD1   
4053 C CD2   . TYR B 275 ? 1.0137 0.9246 0.9999 0.3743  0.3844  0.3384  247 TYR B CD2   
4054 C CE1   . TYR B 275 ? 0.9537 0.9137 0.9901 0.3569  0.3544  0.3448  247 TYR B CE1   
4055 C CE2   . TYR B 275 ? 1.0213 0.9621 1.0301 0.3711  0.3782  0.3483  247 TYR B CE2   
4056 C CZ    . TYR B 275 ? 0.9963 0.9618 1.0305 0.3621  0.3634  0.3514  247 TYR B CZ    
4057 O OH    . TYR B 275 ? 1.0101 1.0046 1.0673 0.3580  0.3567  0.3611  247 TYR B OH    
4058 N N     . ARG B 276 ? 0.9705 0.8948 0.9864 0.3928  0.3984  0.3632  248 ARG B N     
4059 C CA    . ARG B 276 ? 1.0105 0.9541 1.0416 0.4019  0.4076  0.3799  248 ARG B CA    
4060 C C     . ARG B 276 ? 1.0607 0.9997 1.0935 0.4135  0.4191  0.3887  248 ARG B C     
4061 O O     . ARG B 276 ? 1.0435 0.9883 1.0797 0.4235  0.4306  0.4000  248 ARG B O     
4062 C CB    . ARG B 276 ? 0.9715 0.9546 1.0375 0.3960  0.3961  0.3925  248 ARG B CB    
4063 C CG    . ARG B 276 ? 1.0533 1.0451 1.1212 0.3859  0.3861  0.3871  248 ARG B CG    
4064 C CD    . ARG B 276 ? 1.0580 1.0884 1.1614 0.3802  0.3753  0.4006  248 ARG B CD    
4065 N NE    . ARG B 276 ? 1.0871 1.1262 1.1932 0.3708  0.3658  0.3961  248 ARG B NE    
4066 C CZ    . ARG B 276 ? 1.0002 1.0701 1.1342 0.3643  0.3561  0.4062  248 ARG B CZ    
4067 N NH1   . ARG B 276 ? 0.9566 1.0525 1.1191 0.3655  0.3537  0.4216  248 ARG B NH1   
4068 N NH2   . ARG B 276 ? 0.9953 1.0698 1.1289 0.3562  0.3482  0.4010  248 ARG B NH2   
4069 N N     . ILE B 277 ? 1.0508 0.9795 1.0813 0.4129  0.4164  0.3840  249 ILE B N     
4070 C CA    . ILE B 277 ? 1.0823 1.0100 1.1180 0.4236  0.4257  0.3934  249 ILE B CA    
4071 C C     . ILE B 277 ? 1.1961 1.0863 1.1996 0.4318  0.4406  0.3849  249 ILE B C     
4072 O O     . ILE B 277 ? 1.1997 1.0618 1.1783 0.4262  0.4392  0.3687  249 ILE B O     
4073 C CB    . ILE B 277 ? 1.0249 0.9607 1.0749 0.4192  0.4144  0.3935  249 ILE B CB    
4074 C CG1   . ILE B 277 ? 0.9356 0.9057 1.0157 0.4093  0.3972  0.3998  249 ILE B CG1   
4075 C CG2   . ILE B 277 ? 1.1310 1.0690 1.1891 0.4308  0.4235  0.4050  249 ILE B CG2   
4076 C CD1   . ILE B 277 ? 0.9287 0.9315 1.0362 0.4137  0.3994  0.4182  249 ILE B CD1   
4077 N N     . PRO B 278 ? 1.2262 1.1142 1.2291 0.4447  0.4548  0.3950  250 PRO B N     
4078 C CA    . PRO B 278 ? 1.2262 1.0774 1.1994 0.4527  0.4685  0.3868  250 PRO B CA    
4079 C C     . PRO B 278 ? 1.2877 1.1212 1.2531 0.4518  0.4673  0.3802  250 PRO B C     
4080 O O     . PRO B 278 ? 1.2799 1.1312 1.2646 0.4474  0.4570  0.3841  250 PRO B O     
4081 C CB    . PRO B 278 ? 1.1406 1.0006 1.1220 0.4671  0.4824  0.4021  250 PRO B CB    
4082 C CG    . PRO B 278 ? 1.0997 0.9968 1.1086 0.4652  0.4767  0.4156  250 PRO B CG    
4083 C CD    . PRO B 278 ? 1.1064 1.0247 1.1346 0.4523  0.4592  0.4141  250 PRO B CD    
4084 N N     . GLU B 279 ? 1.3181 1.1153 1.2545 0.4561  0.4778  0.3699  251 GLU B N     
4085 C CA    . GLU B 279 ? 1.3982 1.1729 1.3220 0.4538  0.4770  0.3610  251 GLU B CA    
4086 C C     . GLU B 279 ? 1.4127 1.2012 1.3554 0.4621  0.4794  0.3741  251 GLU B C     
4087 O O     . GLU B 279 ? 1.3855 1.1733 1.3326 0.4575  0.4715  0.3713  251 GLU B O     
4088 C CB    . GLU B 279 ? 1.4177 1.1506 1.3070 0.4565  0.4884  0.3477  251 GLU B CB    
4089 C CG    . GLU B 279 ? 1.5216 1.2282 1.3956 0.4537  0.4886  0.3381  251 GLU B CG    
4090 C CD    . GLU B 279 ? 1.5411 1.2499 1.4165 0.4394  0.4734  0.3282  251 GLU B CD    
4091 O OE1   . GLU B 279 ? 1.5228 1.2377 1.3970 0.4303  0.4650  0.3215  251 GLU B OE1   
4092 O OE2   . GLU B 279 ? 1.3836 1.0879 1.2612 0.4377  0.4698  0.3272  251 GLU B OE2   
4093 N N     . GLU B 280 ? 1.3646 1.1655 1.3187 0.4747  0.4900  0.3886  252 GLU B N     
4094 C CA    . GLU B 280 ? 1.3507 1.1637 1.3221 0.4837  0.4931  0.4014  252 GLU B CA    
4095 C C     . GLU B 280 ? 1.3015 1.1498 1.3047 0.4773  0.4774  0.4099  252 GLU B C     
4096 O O     . GLU B 280 ? 1.2669 1.1226 1.2827 0.4817  0.4757  0.4172  252 GLU B O     
4097 C CB    . GLU B 280 ? 1.4151 1.2363 1.3936 0.4986  0.5076  0.4158  252 GLU B CB    
4098 C CG    . GLU B 280 ? 1.4398 1.2967 1.4434 0.4986  0.5042  0.4288  252 GLU B CG    
4099 C CD    . GLU B 280 ? 1.4152 1.2614 1.4020 0.4973  0.5090  0.4227  252 GLU B CD    
4100 O OE1   . GLU B 280 ? 1.4998 1.3165 1.4593 0.4910  0.5085  0.4058  252 GLU B OE1   
4101 O OE2   . GLU B 280 ? 1.4033 1.2709 1.4046 0.5026  0.5130  0.4349  252 GLU B OE2   
4102 N N     . GLN B 281 ? 1.2812 1.1507 1.2972 0.4670  0.4653  0.4091  253 GLN B N     
4103 C CA    . GLN B 281 ? 1.2240 1.1257 1.2693 0.4593  0.4486  0.4157  253 GLN B CA    
4104 C C     . GLN B 281 ? 1.1789 1.0759 1.2182 0.4443  0.4332  0.4014  253 GLN B C     
4105 O O     . GLN B 281 ? 1.1274 1.0489 1.1890 0.4364  0.4175  0.4052  253 GLN B O     
4106 C CB    . GLN B 281 ? 1.2185 1.1567 1.2917 0.4607  0.4466  0.4311  253 GLN B CB    
4107 C CG    . GLN B 281 ? 1.2633 1.2125 1.3487 0.4755  0.4598  0.4478  253 GLN B CG    
4108 C CD    . GLN B 281 ? 1.3062 1.2937 1.4220 0.4759  0.4567  0.4642  253 GLN B CD    
4109 O OE1   . GLN B 281 ? 1.3165 1.3322 1.4579 0.4674  0.4415  0.4696  253 GLN B OE1   
4110 N NE2   . GLN B 281 ? 1.3171 1.3051 1.4299 0.4855  0.4709  0.4721  253 GLN B NE2   
4111 N N     . LYS B 282 ? 1.2510 1.1167 1.2606 0.4398  0.4367  0.3853  254 LYS B N     
4112 C CA    . LYS B 282 ? 1.1802 1.0387 1.1823 0.4261  0.4229  0.3713  254 LYS B CA    
4113 C C     . LYS B 282 ? 1.1329 0.9888 1.1396 0.4231  0.4139  0.3695  254 LYS B C     
4114 O O     . LYS B 282 ? 1.0841 0.9579 1.1067 0.4140  0.3974  0.3693  254 LYS B O     
4115 C CB    . LYS B 282 ? 1.2482 1.0715 1.2165 0.4228  0.4298  0.3549  254 LYS B CB    
4116 C CG    . LYS B 282 ? 1.1835 1.0105 1.1468 0.4198  0.4307  0.3521  254 LYS B CG    
4117 C CD    . LYS B 282 ? 1.2069 0.9986 1.1372 0.4146  0.4341  0.3342  254 LYS B CD    
4118 C CE    . LYS B 282 ? 1.1591 0.9545 1.0842 0.4106  0.4326  0.3305  254 LYS B CE    
4119 N NZ    . LYS B 282 ? 1.1902 0.9505 1.0830 0.4062  0.4361  0.3133  254 LYS B NZ    
4120 N N     . ASP B 283 ? 1.1470 0.9796 1.1390 0.4308  0.4241  0.3682  255 ASP B N     
4121 C CA    . ASP B 283 ? 1.0094 0.8371 1.0036 0.4290  0.4166  0.3669  255 ASP B CA    
4122 C C     . ASP B 283 ? 0.9414 0.8025 0.9677 0.4318  0.4072  0.3826  255 ASP B C     
4123 O O     . ASP B 283 ? 0.9339 0.7974 0.9663 0.4277  0.3958  0.3821  255 ASP B O     
4124 C CB    . ASP B 283 ? 1.0408 0.8359 1.0122 0.4374  0.4311  0.3632  255 ASP B CB    
4125 C CG    . ASP B 283 ? 1.2021 0.9617 1.1407 0.4329  0.4387  0.3468  255 ASP B CG    
4126 O OD1   . ASP B 283 ? 1.3110 1.0694 1.2437 0.4217  0.4300  0.3364  255 ASP B OD1   
4127 O OD2   . ASP B 283 ? 1.2331 0.9658 1.1519 0.4405  0.4531  0.3443  255 ASP B OD2   
4128 N N     . ASP B 284 ? 0.9747 0.8613 1.0213 0.4385  0.4113  0.3966  256 ASP B N     
4129 C CA    . ASP B 284 ? 0.9751 0.8958 1.0539 0.4399  0.4013  0.4120  256 ASP B CA    
4130 C C     . ASP B 284 ? 0.8988 0.8473 0.9979 0.4280  0.3842  0.4133  256 ASP B C     
4131 O O     . ASP B 284 ? 0.8794 0.8516 1.0018 0.4243  0.3700  0.4215  256 ASP B O     
4132 C CB    . ASP B 284 ? 1.1100 1.0446 1.2017 0.4537  0.4150  0.4279  256 ASP B CB    
4133 C CG    . ASP B 284 ? 1.2245 1.1342 1.2998 0.4663  0.4304  0.4288  256 ASP B CG    
4134 O OD1   . ASP B 284 ? 1.1791 1.0673 1.2400 0.4642  0.4277  0.4203  256 ASP B OD1   
4135 O OD2   . ASP B 284 ? 1.2568 1.1679 1.3333 0.4782  0.4453  0.4382  256 ASP B OD2   
4136 N N     . PHE B 285 ? 0.9752 0.9205 1.0654 0.4219  0.3849  0.4055  257 PHE B N     
4137 C CA    . PHE B 285 ? 0.9309 0.8987 1.0374 0.4097  0.3683  0.4047  257 PHE B CA    
4138 C C     . PHE B 285 ? 0.8802 0.8376 0.9793 0.3981  0.3523  0.3925  257 PHE B C     
4139 O O     . PHE B 285 ? 0.8485 0.8267 0.9665 0.3893  0.3347  0.3956  257 PHE B O     
4140 C CB    . PHE B 285 ? 0.9586 0.9243 1.0561 0.4073  0.3746  0.4000  257 PHE B CB    
4141 C CG    . PHE B 285 ? 0.9341 0.9246 1.0501 0.3959  0.3592  0.4011  257 PHE B CG    
4142 C CD1   . PHE B 285 ? 0.8929 0.8763 1.0018 0.3834  0.3446  0.3883  257 PHE B CD1   
4143 C CD2   . PHE B 285 ? 0.9602 0.9804 1.1001 0.3977  0.3596  0.4153  257 PHE B CD2   
4144 C CE1   . PHE B 285 ? 0.8917 0.8966 1.0169 0.3731  0.3304  0.3893  257 PHE B CE1   
4145 C CE2   . PHE B 285 ? 0.8577 0.8997 1.0144 0.3868  0.3456  0.4165  257 PHE B CE2   
4146 C CZ    . PHE B 285 ? 0.8357 0.8696 0.9847 0.3746  0.3308  0.4033  257 PHE B CZ    
4147 N N     . PHE B 286 ? 0.8625 0.7868 0.9335 0.3976  0.3580  0.3787  258 PHE B N     
4148 C CA    . PHE B 286 ? 0.8337 0.7458 0.8955 0.3870  0.3442  0.3670  258 PHE B CA    
4149 C C     . PHE B 286 ? 0.8391 0.7604 0.9146 0.3876  0.3336  0.3743  258 PHE B C     
4150 O O     . PHE B 286 ? 0.8146 0.7462 0.8993 0.3777  0.3156  0.3727  258 PHE B O     
4151 C CB    . PHE B 286 ? 0.8508 0.7251 0.8796 0.3871  0.3546  0.3518  258 PHE B CB    
4152 C CG    . PHE B 286 ? 0.8365 0.6972 0.8533 0.3751  0.3418  0.3384  258 PHE B CG    
4153 C CD1   . PHE B 286 ? 0.8084 0.6836 0.8339 0.3640  0.3270  0.3345  258 PHE B CD1   
4154 C CD2   . PHE B 286 ? 0.8523 0.6855 0.8492 0.3750  0.3449  0.3300  258 PHE B CD2   
4155 C CE1   . PHE B 286 ? 0.8249 0.6872 0.8389 0.3534  0.3156  0.3224  258 PHE B CE1   
4156 C CE2   . PHE B 286 ? 0.8401 0.6610 0.8260 0.3641  0.3338  0.3183  258 PHE B CE2   
4157 C CZ    . PHE B 286 ? 0.8123 0.6478 0.8066 0.3535  0.3191  0.3145  258 PHE B CZ    
4158 N N     . ASP B 287 ? 0.9140 0.8308 0.9900 0.3992  0.3445  0.3826  259 ASP B N     
4159 C CA    . ASP B 287 ? 0.8625 0.7871 0.9505 0.4009  0.3352  0.3903  259 ASP B CA    
4160 C C     . ASP B 287 ? 0.8437 0.8052 0.9635 0.3975  0.3205  0.4036  259 ASP B C     
4161 O O     . ASP B 287 ? 0.8565 0.8264 0.9853 0.3913  0.3039  0.4054  259 ASP B O     
4162 C CB    . ASP B 287 ? 0.8941 0.8068 0.9765 0.4151  0.3513  0.3972  259 ASP B CB    
4163 C CG    . ASP B 287 ? 0.9627 0.8368 1.0137 0.4167  0.3620  0.3841  259 ASP B CG    
4164 O OD1   . ASP B 287 ? 0.9128 0.7687 0.9444 0.4121  0.3677  0.3717  259 ASP B OD1   
4165 O OD2   . ASP B 287 ? 1.1379 0.9998 1.1837 0.4226  0.3648  0.3866  259 ASP B OD2   
4166 N N     . ASP B 288 ? 0.8583 0.8415 0.9946 0.4014  0.3263  0.4134  260 ASP B N     
4167 C CA    . ASP B 288 ? 0.8776 0.8960 1.0442 0.3965  0.3123  0.4256  260 ASP B CA    
4168 C C     . ASP B 288 ? 0.8634 0.8868 1.0316 0.3810  0.2932  0.4169  260 ASP B C     
4169 O O     . ASP B 288 ? 0.8766 0.9196 1.0631 0.3741  0.2757  0.4231  260 ASP B O     
4170 C CB    . ASP B 288 ? 0.9447 0.9828 1.1260 0.4028  0.3236  0.4365  260 ASP B CB    
4171 C CG    . ASP B 288 ? 0.9962 1.0712 1.2112 0.4016  0.3132  0.4533  260 ASP B CG    
4172 O OD1   . ASP B 288 ? 1.0340 1.1175 1.2603 0.4020  0.3032  0.4600  260 ASP B OD1   
4173 O OD2   . ASP B 288 ? 1.0086 1.1039 1.2384 0.3999  0.3147  0.4600  260 ASP B OD2   
4174 N N     . TRP B 289 ? 0.8731 0.8779 1.0213 0.3753  0.2961  0.4026  261 TRP B N     
4175 C CA    . TRP B 289 ? 0.8639 0.8706 1.0111 0.3611  0.2790  0.3935  261 TRP B CA    
4176 C C     . TRP B 289 ? 0.8527 0.8457 0.9903 0.3548  0.2655  0.3865  261 TRP B C     
4177 O O     . TRP B 289 ? 0.8488 0.8555 0.9983 0.3454  0.2467  0.3883  261 TRP B O     
4178 C CB    . TRP B 289 ? 0.8860 0.8753 1.0133 0.3580  0.2870  0.3803  261 TRP B CB    
4179 C CG    . TRP B 289 ? 0.8246 0.8209 0.9546 0.3446  0.2716  0.3733  261 TRP B CG    
4180 C CD1   . TRP B 289 ? 0.7986 0.8224 0.9520 0.3376  0.2582  0.3812  261 TRP B CD1   
4181 C CD2   . TRP B 289 ? 0.7370 0.7115 0.8451 0.3365  0.2681  0.3569  261 TRP B CD2   
4182 N NE1   . TRP B 289 ? 0.7863 0.8060 0.9331 0.3259  0.2466  0.3706  261 TRP B NE1   
4183 C CE2   . TRP B 289 ? 0.7768 0.7670 0.8962 0.3253  0.2524  0.3558  261 TRP B CE2   
4184 C CE3   . TRP B 289 ? 0.7345 0.6776 0.8146 0.3375  0.2767  0.3434  261 TRP B CE3   
4185 C CZ2   . TRP B 289 ? 0.8398 0.8158 0.9436 0.3158  0.2453  0.3419  261 TRP B CZ2   
4186 C CZ3   . TRP B 289 ? 0.7215 0.6513 0.7867 0.3277  0.2697  0.3297  261 TRP B CZ3   
4187 C CH2   . TRP B 289 ? 0.7983 0.7448 0.8755 0.3173  0.2542  0.3291  261 TRP B CH2   
4188 N N     . LEU B 290 ? 0.8354 0.8004 0.9505 0.3597  0.2751  0.3786  262 LEU B N     
4189 C CA    . LEU B 290 ? 0.8299 0.7790 0.9328 0.3537  0.2639  0.3713  262 LEU B CA    
4190 C C     . LEU B 290 ? 0.9119 0.8779 1.0326 0.3547  0.2515  0.3833  262 LEU B C     
4191 O O     . LEU B 290 ? 0.8896 0.8551 1.0093 0.3459  0.2346  0.3804  262 LEU B O     
4192 C CB    . LEU B 290 ? 0.8002 0.7163 0.8764 0.3595  0.2785  0.3619  262 LEU B CB    
4193 C CG    . LEU B 290 ? 0.7990 0.6922 0.8520 0.3559  0.2877  0.3469  262 LEU B CG    
4194 C CD1   . LEU B 290 ? 0.8178 0.6778 0.8446 0.3573  0.2955  0.3367  262 LEU B CD1   
4195 C CD2   . LEU B 290 ? 0.7724 0.6724 0.8269 0.3428  0.2731  0.3391  262 LEU B CD2   
4196 N N     . GLN B 291 ? 0.9759 0.9564 1.1120 0.3656  0.2596  0.3972  263 GLN B N     
4197 C CA    . GLN B 291 ? 0.9710 0.9691 1.1251 0.3673  0.2480  0.4097  263 GLN B CA    
4198 C C     . GLN B 291 ? 0.9409 0.9654 1.1157 0.3564  0.2281  0.4148  263 GLN B C     
4199 O O     . GLN B 291 ? 0.8848 0.9139 1.0637 0.3505  0.2112  0.4169  263 GLN B O     
4200 C CB    . GLN B 291 ? 0.9736 0.9836 1.1414 0.3815  0.2619  0.4241  263 GLN B CB    
4201 C CG    . GLN B 291 ? 1.1041 1.1455 1.3007 0.3822  0.2499  0.4405  263 GLN B CG    
4202 C CD    . GLN B 291 ? 1.1895 1.2432 1.3999 0.3968  0.2646  0.4550  263 GLN B CD    
4203 O OE1   . GLN B 291 ? 1.1385 1.1957 1.3511 0.4029  0.2799  0.4574  263 GLN B OE1   
4204 N NE2   . GLN B 291 ? 1.1966 1.2565 1.4157 0.4028  0.2602  0.4651  263 GLN B NE2   
4205 N N     . ARG B 292 ? 0.9492 0.9902 1.1360 0.3533  0.2298  0.4167  264 ARG B N     
4206 C CA    . ARG B 292 ? 0.9337 0.9988 1.1399 0.3424  0.2118  0.4213  264 ARG B CA    
4207 C C     . ARG B 292 ? 0.9324 0.9849 1.1247 0.3288  0.1959  0.4081  264 ARG B C     
4208 O O     . ARG B 292 ? 0.9231 0.9919 1.1285 0.3190  0.1783  0.4112  264 ARG B O     
4209 C CB    . ARG B 292 ? 0.9130 0.9968 1.1338 0.3429  0.2195  0.4265  264 ARG B CB    
4210 C CG    . ARG B 292 ? 0.8655 0.9834 1.1171 0.3392  0.2083  0.4414  264 ARG B CG    
4211 C CD    . ARG B 292 ? 0.9064 1.0422 1.1731 0.3454  0.2226  0.4507  264 ARG B CD    
4212 N NE    . ARG B 292 ? 0.9347 1.0803 1.2128 0.3589  0.2355  0.4644  264 ARG B NE    
4213 C CZ    . ARG B 292 ? 0.9737 1.1032 1.2379 0.3713  0.2559  0.4630  264 ARG B CZ    
4214 N NH1   . ARG B 292 ? 0.9558 1.0582 1.1939 0.3717  0.2658  0.4484  264 ARG B NH1   
4215 N NH2   . ARG B 292 ? 1.0246 1.1648 1.3009 0.3835  0.2665  0.4765  264 ARG B NH2   
4216 N N     . LEU B 293 ? 0.9413 0.9649 1.1072 0.3279  0.2019  0.3937  265 LEU B N     
4217 C CA    . LEU B 293 ? 0.9001 0.9111 1.0520 0.3153  0.1882  0.3810  265 LEU B CA    
4218 C C     . LEU B 293 ? 0.8596 0.8659 1.0077 0.3107  0.1722  0.3815  265 LEU B C     
4219 O O     . LEU B 293 ? 0.8247 0.8388 0.9774 0.3001  0.1540  0.3807  265 LEU B O     
4220 C CB    . LEU B 293 ? 0.8944 0.8770 1.0200 0.3158  0.2006  0.3659  265 LEU B CB    
4221 C CG    . LEU B 293 ? 0.8321 0.8184 0.9585 0.3169  0.2120  0.3629  265 LEU B CG    
4222 C CD1   . LEU B 293 ? 0.7533 0.7106 0.8527 0.3175  0.2241  0.3480  265 LEU B CD1   
4223 C CD2   . LEU B 293 ? 0.8085 0.8141 0.9492 0.3062  0.1976  0.3639  265 LEU B CD2   
4224 N N     . GLU B 294 ? 0.8880 0.8802 1.0264 0.3187  0.1790  0.3830  266 GLU B N     
4225 C CA    . GLU B 294 ? 0.8978 0.8869 1.0333 0.3157  0.1645  0.3855  266 GLU B CA    
4226 C C     . GLU B 294 ? 0.8767 0.8944 1.0376 0.3153  0.1514  0.4004  266 GLU B C     
4227 O O     . GLU B 294 ? 0.8448 0.8644 1.0054 0.3090  0.1342  0.4021  266 GLU B O     
4228 C CB    . GLU B 294 ? 1.0155 0.9838 1.1360 0.3253  0.1760  0.3850  266 GLU B CB    
4229 C CG    . GLU B 294 ? 1.0991 1.0362 1.1918 0.3228  0.1841  0.3695  266 GLU B CG    
4230 C CD    . GLU B 294 ? 1.2848 1.2009 1.3630 0.3323  0.1965  0.3695  266 GLU B CD    
4231 O OE1   . GLU B 294 ? 1.2013 1.1269 1.2907 0.3408  0.1976  0.3816  266 GLU B OE1   
4232 O OE2   . GLU B 294 ? 1.3963 1.2864 1.4521 0.3311  0.2052  0.3576  266 GLU B OE2   
4233 N N     . LYS B 295 ? 0.8926 0.9325 1.0749 0.3217  0.1594  0.4115  267 LYS B N     
4234 C CA    . LYS B 295 ? 0.8487 0.9185 1.0574 0.3196  0.1465  0.4256  267 LYS B CA    
4235 C C     . LYS B 295 ? 0.8519 0.9309 1.0653 0.3051  0.1285  0.4216  267 LYS B C     
4236 O O     . LYS B 295 ? 0.7612 0.8499 0.9815 0.2986  0.1103  0.4262  267 LYS B O     
4237 C CB    . LYS B 295 ? 0.8796 0.9709 1.1098 0.3289  0.1605  0.4378  267 LYS B CB    
4238 N N     . LEU B 296 ? 0.8744 0.9495 1.0830 0.3002  0.1332  0.4128  268 LEU B N     
4239 C CA    . LEU B 296 ? 0.8265 0.9072 1.0371 0.2866  0.1174  0.4077  268 LEU B CA    
4240 C C     . LEU B 296 ? 0.8267 0.8826 1.0123 0.2783  0.1073  0.3936  268 LEU B C     
4241 O O     . LEU B 296 ? 0.7283 0.7856 0.9125 0.2670  0.0936  0.3883  268 LEU B O     
4242 C CB    . LEU B 296 ? 0.7619 0.8493 0.9781 0.2852  0.1269  0.4049  268 LEU B CB    
4243 C CG    . LEU B 296 ? 0.7662 0.8808 1.0087 0.2918  0.1359  0.4196  268 LEU B CG    
4244 C CD1   . LEU B 296 ? 0.8851 0.9998 1.1267 0.2933  0.1500  0.4156  268 LEU B CD1   
4245 C CD2   . LEU B 296 ? 0.8074 0.9489 1.0742 0.2840  0.1185  0.4310  268 LEU B CD2   
4246 N N     . LYS B 297 ? 0.8530 0.8860 1.0188 0.2836  0.1141  0.3877  269 LYS B N     
4247 C CA    . LYS B 297 ? 0.7833 0.7927 0.9253 0.2765  0.1054  0.3758  269 LYS B CA    
4248 C C     . LYS B 297 ? 0.7729 0.7708 0.9023 0.2684  0.1059  0.3623  269 LYS B C     
4249 O O     . LYS B 297 ? 0.7055 0.6998 0.8284 0.2577  0.0910  0.3563  269 LYS B O     
4250 C CB    . LYS B 297 ? 0.6954 0.7115 0.8406 0.2693  0.0839  0.3805  269 LYS B CB    
4251 N N     . GLY B 298 ? 0.8329 0.8246 0.9582 0.2738  0.1235  0.3575  270 GLY B N     
4252 C CA    . GLY B 298 ? 0.7593 0.7379 0.8705 0.2676  0.1262  0.3443  270 GLY B CA    
4253 C C     . GLY B 298 ? 0.7235 0.6731 0.8089 0.2697  0.1359  0.3327  270 GLY B C     
4254 O O     . GLY B 298 ? 0.7070 0.6416 0.7764 0.2623  0.1324  0.3208  270 GLY B O     
4255 N N     . THR B 299 ? 0.7689 0.7103 0.8504 0.2799  0.1485  0.3363  271 THR B N     
4256 C CA    . THR B 299 ? 0.7552 0.6690 0.8131 0.2824  0.1578  0.3271  271 THR B CA    
4257 C C     . THR B 299 ? 0.7622 0.6704 0.8159 0.2829  0.1489  0.3316  271 THR B C     
4258 O O     . THR B 299 ? 0.7686 0.6943 0.8385 0.2854  0.1406  0.3436  271 THR B O     
4259 C CB    . THR B 299 ? 0.7286 0.6333 0.7818 0.2939  0.1799  0.3271  271 THR B CB    
4260 O OG1   . THR B 299 ? 0.8295 0.7468 0.8974 0.3037  0.1839  0.3405  271 THR B OG1   
4261 C CG2   . THR B 299 ? 0.7451 0.6570 0.8031 0.2942  0.1886  0.3242  271 THR B CG2   
4262 N N     . SER B 300 ? 0.7545 0.6383 0.7861 0.2805  0.1507  0.3223  272 SER B N     
4263 C CA    . SER B 300 ? 0.8046 0.6805 0.8291 0.2806  0.1427  0.3258  272 SER B CA    
4264 C C     . SER B 300 ? 0.8437 0.6907 0.8444 0.2826  0.1545  0.3167  272 SER B C     
4265 O O     . SER B 300 ? 0.8184 0.6512 0.8068 0.2814  0.1656  0.3060  272 SER B O     
4266 C CB    . SER B 300 ? 0.8071 0.6886 0.8315 0.2695  0.1212  0.3252  272 SER B CB    
4267 O OG    . SER B 300 ? 0.9551 0.8184 0.9617 0.2672  0.1165  0.3221  272 SER B OG    
4268 N N     . GLN B 301 ? 0.8994 0.7380 0.8936 0.2855  0.1518  0.3212  273 GLN B N     
4269 C CA    . GLN B 301 ? 0.8970 0.7083 0.8691 0.2871  0.1618  0.3141  273 GLN B CA    
4270 C C     . GLN B 301 ? 0.9547 0.7584 0.9159 0.2802  0.1474  0.3136  273 GLN B C     
4271 O O     . GLN B 301 ? 0.9478 0.7656 0.9191 0.2797  0.1332  0.3233  273 GLN B O     
4272 C CB    . GLN B 301 ? 0.8844 0.6896 0.8572 0.2997  0.1767  0.3211  273 GLN B CB    
4273 C CG    . GLN B 301 ? 0.9433 0.7189 0.8931 0.3017  0.1895  0.3135  273 GLN B CG    
4274 C CD    . GLN B 301 ? 1.0767 0.8468 1.0265 0.3120  0.1956  0.3231  273 GLN B CD    
4275 O OE1   . GLN B 301 ? 1.0971 0.8718 1.0556 0.3223  0.2074  0.3294  273 GLN B OE1   
4276 N NE2   . GLN B 301 ? 1.0790 0.8389 1.0184 0.3095  0.1879  0.3246  273 GLN B NE2   
4277 N N     . GLY B 302 ? 1.0205 0.8018 0.9605 0.2748  0.1511  0.3025  274 GLY B N     
4278 C CA    . GLY B 302 ? 1.0107 0.7829 0.9378 0.2679  0.1390  0.3010  274 GLY B CA    
4279 C C     . GLY B 302 ? 1.0163 0.7618 0.9221 0.2696  0.1506  0.2955  274 GLY B C     
4280 O O     . GLY B 302 ? 1.0118 0.7445 0.9120 0.2756  0.1679  0.2918  274 GLY B O     
4281 N N     . VAL B 303 ? 1.0444 0.7811 0.9378 0.2641  0.1408  0.2950  275 VAL B N     
4282 C CA    . VAL B 303 ? 1.0437 0.7553 0.9161 0.2642  0.1499  0.2902  275 VAL B CA    
4283 C C     . VAL B 303 ? 1.0631 0.7627 0.9197 0.2537  0.1477  0.2779  275 VAL B C     
4284 O O     . VAL B 303 ? 1.0381 0.7490 0.8989 0.2462  0.1346  0.2758  275 VAL B O     
4285 C CB    . VAL B 303 ? 1.0020 0.7117 0.8710 0.2673  0.1422  0.3004  275 VAL B CB    
4286 C CG1   . VAL B 303 ? 0.9230 0.6381 0.8034 0.2793  0.1497  0.3111  275 VAL B CG1   
4287 C CG2   . VAL B 303 ? 1.0702 0.7962 0.9457 0.2610  0.1206  0.3060  275 VAL B CG2   
4288 N N     . GLY B 304 ? 1.0553 0.7312 0.8934 0.2531  0.1609  0.2699  276 GLY B N     
4289 C CA    . GLY B 304 ? 1.0567 0.7193 0.8788 0.2439  0.1616  0.2579  276 GLY B CA    
4290 C C     . GLY B 304 ? 1.1094 0.7569 0.9141 0.2404  0.1586  0.2581  276 GLY B C     
4291 O O     . GLY B 304 ? 1.1183 0.7621 0.9211 0.2457  0.1583  0.2667  276 GLY B O     
4292 N N     . ARG B 305 ? 1.1482 0.7867 0.9394 0.2316  0.1567  0.2484  277 ARG B N     
4293 C CA    . ARG B 305 ? 1.1321 0.7551 0.9049 0.2277  0.1554  0.2474  277 ARG B CA    
4294 C C     . ARG B 305 ? 1.1097 0.7098 0.8690 0.2314  0.1726  0.2450  277 ARG B C     
4295 O O     . ARG B 305 ? 1.0945 0.6831 0.8416 0.2315  0.1725  0.2485  277 ARG B O     
4296 C CB    . ARG B 305 ? 1.0923 0.7111 0.8541 0.2179  0.1511  0.2372  277 ARG B CB    
4297 N N     . ASN B 306 ? 1.1739 0.7665 0.9344 0.2343  0.1873  0.2390  278 ASN B N     
4298 C CA    . ASN B 306 ? 1.1643 0.7347 0.9130 0.2382  0.2041  0.2369  278 ASN B CA    
4299 C C     . ASN B 306 ? 1.1319 0.7060 0.8905 0.2492  0.2079  0.2480  278 ASN B C     
4300 O O     . ASN B 306 ? 1.0229 0.5785 0.7724 0.2535  0.2217  0.2476  278 ASN B O     
4301 C CB    . ASN B 306 ? 1.1060 0.6640 0.8488 0.2354  0.2185  0.2244  278 ASN B CB    
4302 N N     . GLY B 307 ? 1.1239 0.7210 0.9009 0.2537  0.1963  0.2579  279 GLY B N     
4303 C CA    . GLY B 307 ? 1.1095 0.7125 0.8974 0.2645  0.1990  0.2693  279 GLY B CA    
4304 C C     . GLY B 307 ? 1.1840 0.7938 0.9845 0.2711  0.2089  0.2689  279 GLY B C     
4305 O O     . GLY B 307 ? 1.2057 0.8219 1.0165 0.2808  0.2117  0.2787  279 GLY B O     
4306 N N     . GLU B 308 ? 1.1359 0.7444 0.9353 0.2665  0.2144  0.2583  280 GLU B N     
4307 C CA    . GLU B 308 ? 1.0647 0.6779 0.8736 0.2726  0.2250  0.2573  280 GLU B CA    
4308 C C     . GLU B 308 ? 1.0860 0.7282 0.9173 0.2747  0.2132  0.2647  280 GLU B C     
4309 O O     . GLU B 308 ? 1.0646 0.7221 0.9027 0.2690  0.1968  0.2673  280 GLU B O     
4310 C CB    . GLU B 308 ? 1.0608 0.6599 0.8582 0.2666  0.2357  0.2430  280 GLU B CB    
4311 N N     . ALA B 309 ? 1.0718 0.7211 0.9142 0.2828  0.2222  0.2681  281 ALA B N     
4312 C CA    . ALA B 309 ? 0.8957 0.5725 0.7603 0.2855  0.2135  0.2756  281 ALA B CA    
4313 C C     . ALA B 309 ? 0.9282 0.6127 0.7955 0.2782  0.2106  0.2667  281 ALA B C     
4314 O O     . ALA B 309 ? 0.8852 0.5544 0.7404 0.2757  0.2221  0.2558  281 ALA B O     
4315 C CB    . ALA B 309 ? 0.8755 0.5570 0.7504 0.2976  0.2254  0.2833  281 ALA B CB    
4316 N N     . GLU B 310 ? 0.9638 0.6718 0.8469 0.2746  0.1951  0.2715  282 GLU B N     
4317 C CA    . GLU B 310 ? 0.9244 0.6423 0.8121 0.2676  0.1901  0.2646  282 GLU B CA    
4318 C C     . GLU B 310 ? 0.9124 0.6554 0.8227 0.2724  0.1871  0.2730  282 GLU B C     
4319 O O     . GLU B 310 ? 0.9764 0.7358 0.9012 0.2758  0.1779  0.2847  282 GLU B O     
4320 C CB    . GLU B 310 ? 0.9379 0.6590 0.8216 0.2571  0.1733  0.2616  282 GLU B CB    
4321 C CG    . GLU B 310 ? 0.9988 0.6960 0.8599 0.2512  0.1769  0.2521  282 GLU B CG    
4322 C CD    . GLU B 310 ? 1.0219 0.7228 0.8788 0.2418  0.1604  0.2502  282 GLU B CD    
4323 O OE1   . GLU B 310 ? 1.0276 0.7473 0.8978 0.2406  0.1451  0.2585  282 GLU B OE1   
4324 O OE2   . GLU B 310 ? 1.0224 0.7070 0.8623 0.2354  0.1629  0.2406  282 GLU B OE2   
4325 N N     . TYR B 311 ? 0.8505 0.5963 0.7634 0.2724  0.1948  0.2674  283 TYR B N     
4326 C CA    . TYR B 311 ? 0.8127 0.5813 0.7461 0.2771  0.1946  0.2749  283 TYR B CA    
4327 C C     . TYR B 311 ? 0.7414 0.5232 0.6815 0.2686  0.1843  0.2704  283 TYR B C     
4328 O O     . TYR B 311 ? 0.7548 0.5242 0.6814 0.2622  0.1862  0.2589  283 TYR B O     
4329 C CB    . TYR B 311 ? 0.7991 0.5598 0.7300 0.2863  0.2145  0.2739  283 TYR B CB    
4330 C CG    . TYR B 311 ? 0.8532 0.6011 0.7784 0.2955  0.2252  0.2793  283 TYR B CG    
4331 C CD1   . TYR B 311 ? 0.8906 0.6113 0.7944 0.2945  0.2334  0.2717  283 TYR B CD1   
4332 C CD2   . TYR B 311 ? 0.8974 0.6605 0.8391 0.3052  0.2272  0.2923  283 TYR B CD2   
4333 C CE1   . TYR B 311 ? 0.9265 0.6347 0.8249 0.3029  0.2431  0.2769  283 TYR B CE1   
4334 C CE2   . TYR B 311 ? 0.9724 0.7236 0.9089 0.3142  0.2370  0.2976  283 TYR B CE2   
4335 C CZ    . TYR B 311 ? 0.9271 0.6504 0.8417 0.3130  0.2448  0.2898  283 TYR B CZ    
4336 O OH    . TYR B 311 ? 0.8804 0.5910 0.7896 0.3219  0.2547  0.2952  283 TYR B OH    
4337 N N     . TYR B 312 ? 0.7290 0.5360 0.6899 0.2685  0.1735  0.2797  284 TYR B N     
4338 C CA    . TYR B 312 ? 0.7069 0.5278 0.6756 0.2598  0.1607  0.2771  284 TYR B CA    
4339 C C     . TYR B 312 ? 0.6989 0.5421 0.6879 0.2635  0.1625  0.2840  284 TYR B C     
4340 O O     . TYR B 312 ? 0.7117 0.5641 0.7122 0.2726  0.1702  0.2934  284 TYR B O     
4341 C CB    . TYR B 312 ? 0.7236 0.5525 0.6960 0.2526  0.1405  0.2813  284 TYR B CB    
4342 C CG    . TYR B 312 ? 0.7726 0.5806 0.7242 0.2470  0.1370  0.2737  284 TYR B CG    
4343 C CD1   . TYR B 312 ? 0.8403 0.6369 0.7837 0.2512  0.1395  0.2774  284 TYR B CD1   
4344 C CD2   . TYR B 312 ? 0.8026 0.6028 0.7431 0.2378  0.1316  0.2633  284 TYR B CD2   
4345 C CE1   . TYR B 312 ? 0.9081 0.6859 0.8324 0.2461  0.1370  0.2710  284 TYR B CE1   
4346 C CE2   . TYR B 312 ? 0.8161 0.5979 0.7377 0.2330  0.1293  0.2567  284 TYR B CE2   
4347 C CZ    . TYR B 312 ? 0.8866 0.6573 0.8001 0.2370  0.1322  0.2607  284 TYR B CZ    
4348 O OH    . TYR B 312 ? 0.8858 0.6385 0.7805 0.2321  0.1306  0.2547  284 TYR B OH    
4349 N N     . ILE B 313 ? 0.6788 0.5307 0.6720 0.2564  0.1557  0.2797  285 ILE B N     
4350 C CA    . ILE B 313 ? 0.6671 0.5420 0.6804 0.2575  0.1542  0.2864  285 ILE B CA    
4351 C C     . ILE B 313 ? 0.6496 0.5370 0.6704 0.2469  0.1350  0.2863  285 ILE B C     
4352 O O     . ILE B 313 ? 0.6403 0.5175 0.6489 0.2393  0.1305  0.2762  285 ILE B O     
4353 C CB    . ILE B 313 ? 0.6645 0.5349 0.6734 0.2610  0.1695  0.2803  285 ILE B CB    
4354 C CG1   . ILE B 313 ? 0.6846 0.5421 0.6856 0.2720  0.1889  0.2810  285 ILE B CG1   
4355 C CG2   . ILE B 313 ? 0.6511 0.5457 0.6802 0.2607  0.1665  0.2872  285 ILE B CG2   
4356 C CD1   . ILE B 313 ? 0.6860 0.5346 0.6779 0.2753  0.2045  0.2739  285 ILE B CD1   
4357 N N     . HIS B 314 ? 0.6464 0.5551 0.6867 0.2463  0.1238  0.2977  286 HIS B N     
4358 C CA    . HIS B 314 ? 0.6331 0.5530 0.6805 0.2362  0.1047  0.2987  286 HIS B CA    
4359 C C     . HIS B 314 ? 0.6187 0.5580 0.6831 0.2341  0.1037  0.3020  286 HIS B C     
4360 O O     . HIS B 314 ? 0.6209 0.5736 0.6996 0.2414  0.1138  0.3097  286 HIS B O     
4361 C CB    . HIS B 314 ? 0.6405 0.5703 0.6971 0.2355  0.0911  0.3089  286 HIS B CB    
4362 C CG    . HIS B 314 ? 0.6782 0.5909 0.7199 0.2389  0.0930  0.3079  286 HIS B CG    
4363 N ND1   . HIS B 314 ? 0.7303 0.6257 0.7533 0.2322  0.0847  0.3001  286 HIS B ND1   
4364 C CD2   . HIS B 314 ? 0.7604 0.6704 0.8030 0.2485  0.1026  0.3142  286 HIS B CD2   
4365 C CE1   . HIS B 314 ? 0.8490 0.7320 0.8621 0.2372  0.0891  0.3017  286 HIS B CE1   
4366 N NE2   . HIS B 314 ? 0.8129 0.7041 0.8375 0.2471  0.0998  0.3101  286 HIS B NE2   
4367 N N     . LEU B 315 ? 0.6052 0.5455 0.6676 0.2243  0.0915  0.2966  287 LEU B N     
4368 C CA    . LEU B 315 ? 0.5912 0.5471 0.6671 0.2210  0.0899  0.2983  287 LEU B CA    
4369 C C     . LEU B 315 ? 0.5798 0.5327 0.6500 0.2095  0.0737  0.2919  287 LEU B C     
4370 O O     . LEU B 315 ? 0.5821 0.5177 0.6347 0.2051  0.0679  0.2838  287 LEU B O     
4371 C CB    . LEU B 315 ? 0.5895 0.5400 0.6601 0.2267  0.1079  0.2929  287 LEU B CB    
4372 C CG    . LEU B 315 ? 0.5905 0.5163 0.6368 0.2254  0.1148  0.2786  287 LEU B CG    
4373 C CD1   . LEU B 315 ? 0.5758 0.5005 0.6178 0.2175  0.1087  0.2708  287 LEU B CD1   
4374 C CD2   . LEU B 315 ? 0.6015 0.5168 0.6396 0.2354  0.1355  0.2761  287 LEU B CD2   
4375 N N     . SER B 316 ? 0.5685 0.5382 0.6538 0.2048  0.0670  0.2960  288 SER B N     
4376 C CA    . SER B 316 ? 0.5585 0.5268 0.6405 0.1942  0.0516  0.2911  288 SER B CA    
4377 C C     . SER B 316 ? 0.5472 0.5125 0.6249 0.1923  0.0579  0.2834  288 SER B C     
4378 O O     . SER B 316 ? 0.5555 0.5311 0.6433 0.1973  0.0694  0.2871  288 SER B O     
4379 C CB    . SER B 316 ? 0.5558 0.5448 0.6580 0.1892  0.0374  0.3018  288 SER B CB    
4380 O OG    . SER B 316 ? 0.6277 0.6197 0.7332 0.1909  0.0305  0.3091  288 SER B OG    
4381 N N     . VAL B 317 ? 0.5419 0.4931 0.6041 0.1853  0.0505  0.2731  289 VAL B N     
4382 C CA    . VAL B 317 ? 0.5323 0.4781 0.5875 0.1834  0.0558  0.2647  289 VAL B CA    
4383 C C     . VAL B 317 ? 0.5232 0.4718 0.5800 0.1735  0.0399  0.2627  289 VAL B C     
4384 O O     . VAL B 317 ? 0.5668 0.5081 0.6163 0.1678  0.0266  0.2607  289 VAL B O     
4385 C CB    . VAL B 317 ? 0.5496 0.4730 0.5821 0.1856  0.0652  0.2527  289 VAL B CB    
4386 C CG1   . VAL B 317 ? 0.6197 0.5380 0.6447 0.1832  0.0690  0.2441  289 VAL B CG1   
4387 C CG2   . VAL B 317 ? 0.5467 0.4654 0.5764 0.1954  0.0819  0.2542  289 VAL B CG2   
4388 N N     . ILE B 318 ? 0.5138 0.4719 0.5790 0.1719  0.0416  0.2632  290 ILE B N     
4389 C CA    . ILE B 318 ? 0.5083 0.4655 0.5719 0.1632  0.0290  0.2593  290 ILE B CA    
4390 C C     . ILE B 318 ? 0.5260 0.4667 0.5710 0.1629  0.0348  0.2469  290 ILE B C     
4391 O O     . ILE B 318 ? 0.5692 0.5089 0.6116 0.1686  0.0491  0.2442  290 ILE B O     
4392 C CB    . ILE B 318 ? 0.4986 0.4758 0.5823 0.1611  0.0272  0.2677  290 ILE B CB    
4393 C CG1   . ILE B 318 ? 0.5089 0.5046 0.6131 0.1626  0.0243  0.2811  290 ILE B CG1   
4394 C CG2   . ILE B 318 ? 0.4923 0.4675 0.5743 0.1518  0.0132  0.2642  290 ILE B CG2   
4395 C CD1   . ILE B 318 ? 0.6013 0.6182 0.7269 0.1630  0.0281  0.2908  290 ILE B CD1   
4396 N N     . THR B 319 ? 0.5008 0.4286 0.5326 0.1567  0.0241  0.2396  291 THR B N     
4397 C CA    . THR B 319 ? 0.5028 0.4164 0.5183 0.1555  0.0276  0.2282  291 THR B CA    
4398 C C     . THR B 319 ? 0.5324 0.4503 0.5518 0.1488  0.0170  0.2271  291 THR B C     
4399 O O     . THR B 319 ? 0.6624 0.5833 0.6865 0.1427  0.0024  0.2306  291 THR B O     
4400 C CB    . THR B 319 ? 0.5526 0.4477 0.5493 0.1542  0.0250  0.2206  291 THR B CB    
4401 O OG1   . THR B 319 ? 0.6311 0.5226 0.6254 0.1600  0.0336  0.2230  291 THR B OG1   
4402 C CG2   . THR B 319 ? 0.5496 0.4310 0.5301 0.1544  0.0317  0.2092  291 THR B CG2   
4403 N N     . ALA B 320 ? 0.4900 0.4075 0.5065 0.1501  0.0243  0.2224  292 ALA B N     
4404 C CA    . ALA B 320 ? 0.4909 0.4136 0.5124 0.1446  0.0157  0.2223  292 ALA B CA    
4405 C C     . ALA B 320 ? 0.5216 0.4331 0.5286 0.1451  0.0203  0.2119  292 ALA B C     
4406 O O     . ALA B 320 ? 0.5326 0.4373 0.5298 0.1509  0.0336  0.2067  292 ALA B O     
4407 C CB    . ALA B 320 ? 0.5192 0.4610 0.5599 0.1459  0.0193  0.2319  292 ALA B CB    
4408 N N     . LEU B 321 ? 0.5087 0.4178 0.5138 0.1391  0.0091  0.2091  293 LEU B N     
4409 C CA    . LEU B 321 ? 0.5079 0.4083 0.5010 0.1392  0.0116  0.2001  293 LEU B CA    
4410 C C     . LEU B 321 ? 0.5570 0.4660 0.5596 0.1347  0.0034  0.2033  293 LEU B C     
4411 O O     . LEU B 321 ? 0.6697 0.5767 0.6741 0.1284  -0.0105 0.2043  293 LEU B O     
4412 C CB    . LEU B 321 ? 0.5414 0.4249 0.5176 0.1371  0.0061  0.1913  293 LEU B CB    
4413 C CG    . LEU B 321 ? 0.5394 0.4146 0.5041 0.1367  0.0059  0.1824  293 LEU B CG    
4414 C CD1   . LEU B 321 ? 0.5869 0.4607 0.5448 0.1433  0.0214  0.1776  293 LEU B CD1   
4415 C CD2   . LEU B 321 ? 0.6078 0.4672 0.5569 0.1349  0.0000  0.1749  293 LEU B CD2   
4416 N N     . ALA B 322 ? 0.4995 0.4168 0.5069 0.1380  0.0122  0.2050  294 ALA B N     
4417 C CA    . ALA B 322 ? 0.5071 0.4330 0.5236 0.1342  0.0064  0.2087  294 ALA B CA    
4418 C C     . ALA B 322 ? 0.5756 0.4942 0.5801 0.1357  0.0091  0.2005  294 ALA B C     
4419 O O     . ALA B 322 ? 0.6562 0.5644 0.6461 0.1401  0.0167  0.1923  294 ALA B O     
4420 C CB    . ALA B 322 ? 0.5436 0.4868 0.5764 0.1370  0.0140  0.2188  294 ALA B CB    
4421 N N     . ARG B 323 ? 0.5976 0.5217 0.6081 0.1321  0.0029  0.2030  295 ARG B N     
4422 C CA    . ARG B 323 ? 0.6022 0.5213 0.6029 0.1336  0.0046  0.1965  295 ARG B CA    
4423 C C     . ARG B 323 ? 0.6389 0.5700 0.6506 0.1323  0.0042  0.2033  295 ARG B C     
4424 O O     . ARG B 323 ? 0.6405 0.5772 0.6640 0.1264  -0.0054 0.2099  295 ARG B O     
4425 C CB    . ARG B 323 ? 0.5983 0.5043 0.5888 0.1295  -0.0070 0.1891  295 ARG B CB    
4426 C CG    . ARG B 323 ? 0.6807 0.5821 0.6612 0.1318  -0.0057 0.1823  295 ARG B CG    
4427 C CD    . ARG B 323 ? 0.7536 0.6425 0.7251 0.1285  -0.0169 0.1756  295 ARG B CD    
4428 N NE    . ARG B 323 ? 0.7956 0.6728 0.7548 0.1305  -0.0150 0.1687  295 ARG B NE    
4429 C CZ    . ARG B 323 ? 0.8218 0.6875 0.7735 0.1277  -0.0245 0.1644  295 ARG B CZ    
4430 N NH1   . ARG B 323 ? 0.8915 0.7549 0.8469 0.1227  -0.0371 0.1661  295 ARG B NH1   
4431 N NH2   . ARG B 323 ? 0.7973 0.6525 0.7365 0.1301  -0.0209 0.1582  295 ARG B NH2   
4432 N N     . LYS B 324 ? 0.6151 0.5495 0.6220 0.1381  0.0150  0.2020  296 LYS B N     
4433 C CA    . LYS B 324 ? 0.6122 0.5572 0.6274 0.1375  0.0156  0.2083  296 LYS B CA    
4434 C C     . LYS B 324 ? 0.6405 0.5795 0.6522 0.1325  0.0039  0.2048  296 LYS B C     
4435 O O     . LYS B 324 ? 0.6090 0.5362 0.6075 0.1330  0.0005  0.1956  296 LYS B O     
4436 C CB    . LYS B 324 ? 0.5863 0.5348 0.5942 0.1458  0.0304  0.2074  296 LYS B CB    
4437 C CG    . LYS B 324 ? 0.5651 0.5242 0.5793 0.1460  0.0320  0.2139  296 LYS B CG    
4438 C CD    . LYS B 324 ? 0.5303 0.4914 0.5345 0.1550  0.0467  0.2127  296 LYS B CD    
4439 C CE    . LYS B 324 ? 0.5944 0.5657 0.6035 0.1553  0.0478  0.2194  296 LYS B CE    
4440 N NZ    . LYS B 324 ? 0.5470 0.5205 0.5453 0.1646  0.0624  0.2193  296 LYS B NZ    
4441 N N     . PHE B 325 ? 0.7211 0.6682 0.7447 0.1280  -0.0018 0.2125  297 PHE B N     
4442 C CA    . PHE B 325 ? 0.7606 0.7014 0.7816 0.1234  -0.0127 0.2103  297 PHE B CA    
4443 C C     . PHE B 325 ? 0.7833 0.7259 0.7969 0.1279  -0.0069 0.2081  297 PHE B C     
4444 O O     . PHE B 325 ? 0.7601 0.7132 0.7771 0.1322  0.0036  0.2132  297 PHE B O     
4445 C CB    . PHE B 325 ? 0.7277 0.6748 0.7640 0.1163  -0.0214 0.2197  297 PHE B CB    
4446 C CG    . PHE B 325 ? 0.6902 0.6301 0.7287 0.1104  -0.0330 0.2191  297 PHE B CG    
4447 C CD1   . PHE B 325 ? 0.7672 0.6926 0.7962 0.1070  -0.0442 0.2124  297 PHE B CD1   
4448 C CD2   . PHE B 325 ? 0.6737 0.6214 0.7233 0.1089  -0.0324 0.2255  297 PHE B CD2   
4449 C CE1   . PHE B 325 ? 0.8332 0.7514 0.8625 0.1021  -0.0545 0.2120  297 PHE B CE1   
4450 C CE2   . PHE B 325 ? 0.7293 0.6707 0.7800 0.1038  -0.0432 0.2253  297 PHE B CE2   
4451 C CZ    . PHE B 325 ? 0.7659 0.6922 0.8057 0.1003  -0.0542 0.2184  297 PHE B CZ    
4452 N N     . ALA C 43  ? 0.5091 1.2228 0.6194 0.2118  -0.1725 -0.1167 15  ALA C N     
4453 C CA    . ALA C 43  ? 0.5329 1.2357 0.6464 0.1966  -0.1603 -0.1274 15  ALA C CA    
4454 C C     . ALA C 43  ? 0.7230 1.3840 0.8252 0.2008  -0.1480 -0.1243 15  ALA C C     
4455 O O     . ALA C 43  ? 0.8768 1.5214 0.9741 0.2166  -0.1486 -0.1142 15  ALA C O     
4456 C CB    . ALA C 43  ? 0.5344 1.2370 0.6344 0.1765  -0.1616 -0.1373 15  ALA C CB    
4457 N N     . TYR C 44  ? 0.6506 1.2942 0.7484 0.1864  -0.1370 -0.1330 16  TYR C N     
4458 C CA    . TYR C 44  ? 0.6094 1.2150 0.6975 0.1888  -0.1252 -0.1310 16  TYR C CA    
4459 C C     . TYR C 44  ? 0.6056 1.1789 0.6665 0.1845  -0.1245 -0.1285 16  TYR C C     
4460 O O     . TYR C 44  ? 0.6067 1.1693 0.6565 0.1691  -0.1200 -0.1362 16  TYR C O     
4461 C CB    . TYR C 44  ? 0.5756 1.1790 0.6732 0.1766  -0.1133 -0.1407 16  TYR C CB    
4462 C CG    . TYR C 44  ? 0.5846 1.1538 0.6762 0.1816  -0.1018 -0.1380 16  TYR C CG    
4463 C CD1   . TYR C 44  ? 0.6825 1.2477 0.7820 0.1989  -0.1009 -0.1305 16  TYR C CD1   
4464 C CD2   . TYR C 44  ? 0.5060 1.0463 0.5832 0.1694  -0.0921 -0.1429 16  TYR C CD2   
4465 C CE1   . TYR C 44  ? 0.6966 1.2303 0.7894 0.2031  -0.0911 -0.1284 16  TYR C CE1   
4466 C CE2   . TYR C 44  ? 0.5240 1.0340 0.5954 0.1740  -0.0824 -0.1402 16  TYR C CE2   
4467 C CZ    . TYR C 44  ? 0.5804 1.0872 0.6593 0.1905  -0.0822 -0.1332 16  TYR C CZ    
4468 O OH    . TYR C 44  ? 0.5102 0.9866 0.5823 0.1947  -0.0733 -0.1309 16  TYR C OH    
4469 N N     . ARG C 45  ? 0.6246 1.1822 0.6751 0.1985  -0.1286 -0.1175 17  ARG C N     
4470 C CA    . ARG C 45  ? 0.6235 1.1470 0.6498 0.1967  -0.1259 -0.1133 17  ARG C CA    
4471 C C     . ARG C 45  ? 0.6512 1.1421 0.6745 0.1998  -0.1149 -0.1110 17  ARG C C     
4472 O O     . ARG C 45  ? 0.6800 1.1491 0.6951 0.2109  -0.1150 -0.1015 17  ARG C O     
4473 C CB    . ARG C 45  ? 0.6810 1.2043 0.6970 0.2090  -0.1361 -0.1021 17  ARG C CB    
4474 C CG    . ARG C 45  ? 0.7783 1.3300 0.7922 0.2050  -0.1474 -0.1041 17  ARG C CG    
4475 C CD    . ARG C 45  ? 0.8087 1.3474 0.8015 0.1904  -0.1457 -0.1099 17  ARG C CD    
4476 N NE    . ARG C 45  ? 0.8072 1.3164 0.7780 0.1948  -0.1444 -0.1015 17  ARG C NE    
4477 C CZ    . ARG C 45  ? 0.8144 1.3217 0.7781 0.2080  -0.1517 -0.0897 17  ARG C CZ    
4478 N NH1   . ARG C 45  ? 0.8353 1.3683 0.8112 0.2192  -0.1616 -0.0844 17  ARG C NH1   
4479 N NH2   . ARG C 45  ? 0.7273 1.2068 0.6714 0.2100  -0.1489 -0.0827 17  ARG C NH2   
4480 N N     . GLY C 46  ? 0.6386 1.1271 0.6687 0.1893  -0.1054 -0.1200 18  GLY C N     
4481 C CA    . GLY C 46  ? 0.5691 1.0288 0.5964 0.1898  -0.0945 -0.1197 18  GLY C CA    
4482 C C     . GLY C 46  ? 0.5661 1.0208 0.6020 0.2066  -0.0947 -0.1120 18  GLY C C     
4483 O O     . GLY C 46  ? 0.5876 1.0669 0.6385 0.2167  -0.1007 -0.1096 18  GLY C O     
4484 N N     . ILE C 47  ? 0.5698 0.9917 0.5959 0.2097  -0.0881 -0.1080 19  ILE C N     
4485 C CA    . ILE C 47  ? 0.5711 0.9814 0.6018 0.2248  -0.0874 -0.1011 19  ILE C CA    
4486 C C     . ILE C 47  ? 0.5403 0.9361 0.5593 0.2354  -0.0948 -0.0896 19  ILE C C     
4487 O O     . ILE C 47  ? 0.5611 0.9330 0.5634 0.2309  -0.0935 -0.0862 19  ILE C O     
4488 C CB    . ILE C 47  ? 0.4837 0.8665 0.5104 0.2218  -0.0764 -0.1037 19  ILE C CB    
4489 C CG1   . ILE C 47  ? 0.5632 0.9578 0.5985 0.2087  -0.0682 -0.1149 19  ILE C CG1   
4490 C CG2   . ILE C 47  ? 0.4875 0.8606 0.5198 0.2371  -0.0757 -0.0982 19  ILE C CG2   
4491 C CD1   . ILE C 47  ? 0.4836 0.8609 0.5211 0.2098  -0.0580 -0.1175 19  ILE C CD1   
4492 N N     . ASP C 48  ? 0.5289 0.9392 0.5567 0.2497  -0.1023 -0.0832 20  ASP C N     
4493 C CA    . ASP C 48  ? 0.4818 0.8761 0.5000 0.2617  -0.1084 -0.0713 20  ASP C CA    
4494 C C     . ASP C 48  ? 0.5976 0.9636 0.6143 0.2702  -0.1031 -0.0673 20  ASP C C     
4495 O O     . ASP C 48  ? 0.6639 1.0202 0.6835 0.2653  -0.0943 -0.0738 20  ASP C O     
4496 C CB    . ASP C 48  ? 0.4895 0.9110 0.5170 0.2735  -0.1190 -0.0658 20  ASP C CB    
4497 C CG    . ASP C 48  ? 0.6142 1.0618 0.6632 0.2799  -0.1184 -0.0703 20  ASP C CG    
4498 O OD1   . ASP C 48  ? 0.6727 1.1166 0.7287 0.2751  -0.1094 -0.0778 20  ASP C OD1   
4499 O OD2   . ASP C 48  ? 0.6582 1.1303 0.7172 0.2903  -0.1268 -0.0659 20  ASP C OD2   
4500 N N     . LYS C 49  ? 0.5825 0.9349 0.5943 0.2830  -0.1084 -0.0566 21  LYS C N     
4501 C CA    . LYS C 49  ? 0.6140 0.9377 0.6228 0.2917  -0.1048 -0.0521 21  LYS C CA    
4502 C C     . LYS C 49  ? 0.6656 0.9613 0.6638 0.2806  -0.0960 -0.0560 21  LYS C C     
4503 O O     . LYS C 49  ? 0.6021 0.8901 0.6048 0.2798  -0.0889 -0.0618 21  LYS C O     
4504 C CB    . LYS C 49  ? 0.4952 0.8311 0.5197 0.3024  -0.1029 -0.0550 21  LYS C CB    
4505 N N     . PRO C 50  ? 0.6076 0.8885 0.5918 0.2721  -0.0962 -0.0528 22  PRO C N     
4506 C CA    . PRO C 50  ? 0.5323 0.7880 0.5071 0.2617  -0.0881 -0.0560 22  PRO C CA    
4507 C C     . PRO C 50  ? 0.6744 0.9005 0.6451 0.2684  -0.0857 -0.0514 22  PRO C C     
4508 O O     . PRO C 50  ? 0.6643 0.8721 0.6302 0.2612  -0.0787 -0.0554 22  PRO C O     
4509 C CB    . PRO C 50  ? 0.4783 0.7269 0.4398 0.2540  -0.0900 -0.0516 22  PRO C CB    
4510 C CG    . PRO C 50  ? 0.5678 0.8255 0.5284 0.2643  -0.0995 -0.0421 22  PRO C CG    
4511 C CD    . PRO C 50  ? 0.6225 0.9084 0.5982 0.2723  -0.1035 -0.0455 22  PRO C CD    
4512 N N     . HIS C 51  ? 0.6899 0.9103 0.6620 0.2820  -0.0916 -0.0432 23  HIS C N     
4513 C CA    . HIS C 51  ? 0.6954 0.8867 0.6632 0.2884  -0.0899 -0.0393 23  HIS C CA    
4514 C C     . HIS C 51  ? 0.6707 0.8616 0.6455 0.2894  -0.0830 -0.0483 23  HIS C C     
4515 O O     . HIS C 51  ? 0.6997 0.8653 0.6679 0.2873  -0.0783 -0.0494 23  HIS C O     
4516 C CB    . HIS C 51  ? 0.7159 0.9026 0.6843 0.3032  -0.0976 -0.0291 23  HIS C CB    
4517 C CG    . HIS C 51  ? 0.8677 1.0372 0.8246 0.3026  -0.1024 -0.0180 23  HIS C CG    
4518 N ND1   . HIS C 51  ? 0.9539 1.1336 0.9054 0.2948  -0.1044 -0.0156 23  HIS C ND1   
4519 C CD2   . HIS C 51  ? 0.9023 1.0449 0.8521 0.3085  -0.1054 -0.0086 23  HIS C CD2   
4520 C CE1   . HIS C 51  ? 0.9229 1.0838 0.8648 0.2964  -0.1079 -0.0048 23  HIS C CE1   
4521 N NE2   . HIS C 51  ? 0.9441 1.0825 0.8854 0.3042  -0.1087 -0.0002 23  HIS C NE2   
4522 N N     . LEU C 52  ? 0.6465 0.8658 0.6348 0.2924  -0.0822 -0.0546 24  LEU C N     
4523 C CA    . LEU C 52  ? 0.5847 0.8060 0.5805 0.2942  -0.0749 -0.0628 24  LEU C CA    
4524 C C     . LEU C 52  ? 0.5948 0.8144 0.5881 0.2792  -0.0663 -0.0717 24  LEU C C     
4525 O O     . LEU C 52  ? 0.5767 0.7859 0.5701 0.2788  -0.0592 -0.0771 24  LEU C O     
4526 C CB    . LEU C 52  ? 0.5004 0.7545 0.5132 0.3028  -0.0766 -0.0659 24  LEU C CB    
4527 C CG    . LEU C 52  ? 0.5073 0.7628 0.5243 0.3201  -0.0838 -0.0577 24  LEU C CG    
4528 C CD1   . LEU C 52  ? 0.5160 0.8063 0.5515 0.3284  -0.0846 -0.0611 24  LEU C CD1   
4529 C CD2   . LEU C 52  ? 0.5628 0.7851 0.5718 0.3289  -0.0816 -0.0547 24  LEU C CD2   
4530 N N     . TYR C 53  ? 0.5851 0.8137 0.5752 0.2671  -0.0666 -0.0733 25  TYR C N     
4531 C CA    . TYR C 53  ? 0.5273 0.7550 0.5154 0.2530  -0.0582 -0.0817 25  TYR C CA    
4532 C C     . TYR C 53  ? 0.5449 0.7389 0.5189 0.2476  -0.0539 -0.0798 25  TYR C C     
4533 O O     . TYR C 53  ? 0.5056 0.6920 0.4782 0.2408  -0.0459 -0.0862 25  TYR C O     
4534 C CB    . TYR C 53  ? 0.5208 0.7682 0.5094 0.2419  -0.0597 -0.0848 25  TYR C CB    
4535 C CG    . TYR C 53  ? 0.4853 0.7363 0.4748 0.2281  -0.0509 -0.0945 25  TYR C CG    
4536 C CD1   . TYR C 53  ? 0.4526 0.7287 0.4561 0.2258  -0.0472 -0.1026 25  TYR C CD1   
4537 C CD2   . TYR C 53  ? 0.4918 0.7212 0.4687 0.2176  -0.0461 -0.0950 25  TYR C CD2   
4538 C CE1   . TYR C 53  ? 0.4528 0.7311 0.4571 0.2128  -0.0388 -0.1111 25  TYR C CE1   
4539 C CE2   . TYR C 53  ? 0.4654 0.6965 0.4425 0.2053  -0.0378 -0.1033 25  TYR C CE2   
4540 C CZ    . TYR C 53  ? 0.4751 0.7300 0.4656 0.2026  -0.0342 -0.1114 25  TYR C CZ    
4541 O OH    . TYR C 53  ? 0.5768 0.8322 0.5672 0.1900  -0.0256 -0.1192 25  TYR C OH    
4542 N N     . THR C 54  ? 0.5356 0.7097 0.4994 0.2503  -0.0590 -0.0707 26  THR C N     
4543 C CA    . THR C 54  ? 0.4850 0.6284 0.4367 0.2453  -0.0558 -0.0681 26  THR C CA    
4544 C C     . THR C 54  ? 0.5811 0.7062 0.5315 0.2511  -0.0524 -0.0700 26  THR C C     
4545 O O     . THR C 54  ? 0.7169 0.8176 0.6577 0.2463  -0.0493 -0.0691 26  THR C O     
4546 C CB    . THR C 54  ? 0.5037 0.6313 0.4465 0.2475  -0.0623 -0.0572 26  THR C CB    
4547 O OG1   . THR C 54  ? 0.6287 0.7598 0.5755 0.2606  -0.0696 -0.0508 26  THR C OG1   
4548 C CG2   . THR C 54  ? 0.5589 0.6980 0.4984 0.2390  -0.0633 -0.0561 26  THR C CG2   
4549 N N     . LEU C 55  ? 0.5890 0.7253 0.5485 0.2617  -0.0528 -0.0724 27  LEU C N     
4550 C CA    . LEU C 55  ? 0.5345 0.6551 0.4923 0.2670  -0.0483 -0.0759 27  LEU C CA    
4551 C C     . LEU C 55  ? 0.5405 0.6618 0.4976 0.2570  -0.0386 -0.0849 27  LEU C C     
4552 O O     . LEU C 55  ? 0.5889 0.6906 0.5395 0.2583  -0.0342 -0.0873 27  LEU C O     
4553 C CB    . LEU C 55  ? 0.5092 0.6443 0.4778 0.2811  -0.0500 -0.0767 27  LEU C CB    
4554 C CG    . LEU C 55  ? 0.5210 0.6489 0.4885 0.2933  -0.0591 -0.0673 27  LEU C CG    
4555 C CD1   . LEU C 55  ? 0.5142 0.6613 0.4943 0.3073  -0.0604 -0.0683 27  LEU C CD1   
4556 C CD2   . LEU C 55  ? 0.6006 0.6917 0.5548 0.2960  -0.0607 -0.0623 27  LEU C CD2   
4557 N N     . GLY C 56  ? 0.5095 0.6517 0.4722 0.2470  -0.0353 -0.0898 28  GLY C N     
4558 C CA    . GLY C 56  ? 0.4925 0.6345 0.4538 0.2361  -0.0261 -0.0975 28  GLY C CA    
4559 C C     . GLY C 56  ? 0.6378 0.7630 0.5877 0.2240  -0.0243 -0.0958 28  GLY C C     
4560 O O     . GLY C 56  ? 0.6863 0.8083 0.6336 0.2148  -0.0165 -0.1015 28  GLY C O     
4561 N N     . CYS C 57  ? 0.6270 0.7416 0.5702 0.2242  -0.0309 -0.0879 29  CYS C N     
4562 C CA    . CYS C 57  ? 0.6889 0.7868 0.6215 0.2141  -0.0290 -0.0853 29  CYS C CA    
4563 C C     . CYS C 57  ? 0.8782 0.9506 0.8018 0.2115  -0.0241 -0.0860 29  CYS C C     
4564 O O     . CYS C 57  ? 0.8238 0.8918 0.7433 0.2017  -0.0173 -0.0901 29  CYS C O     
4565 C CB    . CYS C 57  ? 0.7008 0.7905 0.6282 0.2168  -0.0369 -0.0754 29  CYS C CB    
4566 S SG    . CYS C 57  ? 0.7451 0.8149 0.6606 0.2058  -0.0344 -0.0710 29  CYS C SG    
4567 N N     . CYS C 58  ? 1.0155 1.0702 0.9351 0.2203  -0.0276 -0.0822 30  CYS C N     
4568 C CA    . CYS C 58  ? 0.9873 1.0167 0.8969 0.2183  -0.0242 -0.0827 30  CYS C CA    
4569 C C     . CYS C 58  ? 0.9112 0.9450 0.8214 0.2132  -0.0146 -0.0918 30  CYS C C     
4570 O O     . CYS C 58  ? 0.9178 0.9320 0.8185 0.2093  -0.0109 -0.0924 30  CYS C O     
4571 C CB    . CYS C 58  ? 1.0183 1.0304 0.9242 0.2293  -0.0294 -0.0790 30  CYS C CB    
4572 S SG    . CYS C 58  ? 1.3925 1.3986 1.2987 0.2375  -0.0407 -0.0678 30  CYS C SG    
4573 N N     . SER C 59  ? 0.9425 1.0019 0.8636 0.2127  -0.0105 -0.0983 31  SER C N     
4574 C CA    . SER C 59  ? 0.7075 0.7737 0.6305 0.2067  -0.0007 -0.1066 31  SER C CA    
4575 C C     . SER C 59  ? 0.6277 0.7113 0.5556 0.1951  0.0036  -0.1106 31  SER C C     
4576 O O     . SER C 59  ? 0.5694 0.6469 0.4927 0.1861  0.0112  -0.1144 31  SER C O     
4577 C CB    . SER C 59  ? 0.6026 0.6843 0.5352 0.2157  0.0019  -0.1118 31  SER C CB    
4578 O OG    . SER C 59  ? 0.6691 0.7312 0.5949 0.2258  -0.0001 -0.1098 31  SER C OG    
4579 N N     . LEU C 60  ? 0.7615 0.8659 0.6978 0.1951  -0.0012 -0.1098 32  LEU C N     
4580 C CA    . LEU C 60  ? 0.6778 0.7975 0.6175 0.1837  0.0022  -0.1140 32  LEU C CA    
4581 C C     . LEU C 60  ? 0.6959 0.7968 0.6238 0.1751  0.0031  -0.1103 32  LEU C C     
4582 O O     . LEU C 60  ? 0.6691 0.7733 0.5958 0.1644  0.0091  -0.1148 32  LEU C O     
4583 C CB    . LEU C 60  ? 0.5603 0.7060 0.5102 0.1861  -0.0042 -0.1138 32  LEU C CB    
4584 C CG    . LEU C 60  ? 0.5121 0.6840 0.4771 0.1926  -0.0044 -0.1183 32  LEU C CG    
4585 C CD1   . LEU C 60  ? 0.4620 0.6577 0.4353 0.1953  -0.0125 -0.1166 32  LEU C CD1   
4586 C CD2   . LEU C 60  ? 0.5437 0.7282 0.5154 0.1840  0.0051  -0.1271 32  LEU C CD2   
4587 N N     . THR C 61  ? 0.7757 0.8571 0.6953 0.1796  -0.0025 -0.1021 33  THR C N     
4588 C CA    . THR C 61  ? 0.7902 0.8538 0.6994 0.1724  -0.0014 -0.0978 33  THR C CA    
4589 C C     . THR C 61  ? 0.7680 0.8162 0.6705 0.1657  0.0070  -0.1012 33  THR C C     
4590 O O     . THR C 61  ? 0.7409 0.7856 0.6391 0.1564  0.0121  -0.1026 33  THR C O     
4591 C CB    . THR C 61  ? 0.8319 0.8782 0.7351 0.1789  -0.0090 -0.0879 33  THR C CB    
4592 O OG1   . THR C 61  ? 0.8810 0.9414 0.7895 0.1846  -0.0164 -0.0841 33  THR C OG1   
4593 C CG2   . THR C 61  ? 0.7795 0.8081 0.6733 0.1720  -0.0074 -0.0828 33  THR C CG2   
4594 N N     . ALA C 62  ? 0.7826 0.8209 0.6832 0.1707  0.0086  -0.1024 34  ALA C N     
4595 C CA    . ALA C 62  ? 0.8119 0.8356 0.7051 0.1650  0.0164  -0.1053 34  ALA C CA    
4596 C C     . ALA C 62  ? 0.7668 0.8060 0.6654 0.1571  0.0254  -0.1137 34  ALA C C     
4597 O O     . ALA C 62  ? 0.7875 0.8165 0.6797 0.1490  0.0324  -0.1154 34  ALA C O     
4598 C CB    . ALA C 62  ? 0.8845 0.8941 0.7731 0.1728  0.0157  -0.1050 34  ALA C CB    
4599 N N     . MET C 63  ? 0.6996 0.7635 0.6103 0.1591  0.0253  -0.1188 35  MET C N     
4600 C CA    . MET C 63  ? 0.7432 0.8233 0.6606 0.1510  0.0337  -0.1268 35  MET C CA    
4601 C C     . MET C 63  ? 0.7578 0.8413 0.6738 0.1397  0.0360  -0.1282 35  MET C C     
4602 O O     . MET C 63  ? 0.8185 0.8958 0.7304 0.1305  0.0442  -0.1316 35  MET C O     
4603 C CB    . MET C 63  ? 0.7523 0.8599 0.6847 0.1563  0.0323  -0.1312 35  MET C CB    
4604 C CG    . MET C 63  ? 0.8302 0.9574 0.7718 0.1473  0.0404  -0.1393 35  MET C CG    
4605 S SD    . MET C 63  ? 0.8668 1.0312 0.8283 0.1521  0.0367  -0.1435 35  MET C SD    
4606 C CE    . MET C 63  ? 0.7260 0.8849 0.6886 0.1691  0.0334  -0.1400 35  MET C CE    
4607 N N     . ALA C 64  ? 0.7471 0.8397 0.6654 0.1405  0.0290  -0.1255 36  ALA C N     
4608 C CA    . ALA C 64  ? 0.7183 0.8127 0.6335 0.1304  0.0309  -0.1271 36  ALA C CA    
4609 C C     . ALA C 64  ? 0.7085 0.7767 0.6104 0.1264  0.0340  -0.1223 36  ALA C C     
4610 O O     . ALA C 64  ? 0.6841 0.7485 0.5817 0.1169  0.0397  -0.1250 36  ALA C O     
4611 C CB    . ALA C 64  ? 0.7522 0.8614 0.6712 0.1331  0.0225  -0.1249 36  ALA C CB    
4612 N N     . SER C 65  ? 0.7969 0.8469 0.6924 0.1335  0.0301  -0.1150 37  SER C N     
4613 C CA    . SER C 65  ? 0.8297 0.8558 0.7140 0.1302  0.0329  -0.1100 37  SER C CA    
4614 C C     . SER C 65  ? 0.8416 0.8588 0.7219 0.1238  0.0425  -0.1145 37  SER C C     
4615 O O     . SER C 65  ? 0.8701 0.8738 0.7428 0.1173  0.0476  -0.1132 37  SER C O     
4616 C CB    . SER C 65  ? 0.8421 0.8520 0.7216 0.1387  0.0261  -0.1016 37  SER C CB    
4617 O OG    . SER C 65  ? 0.8925 0.8817 0.7625 0.1355  0.0277  -0.0958 37  SER C OG    
4618 N N     . ALA C 66  ? 0.8051 0.8298 0.6903 0.1260  0.0456  -0.1195 38  ALA C N     
4619 C CA    . ALA C 66  ? 0.8047 0.8218 0.6859 0.1202  0.0552  -0.1236 38  ALA C CA    
4620 C C     . ALA C 66  ? 0.7913 0.8204 0.6767 0.1093  0.0626  -0.1303 38  ALA C C     
4621 O O     . ALA C 66  ? 0.8019 0.8190 0.6806 0.1018  0.0705  -0.1314 38  ALA C O     
4622 C CB    . ALA C 66  ? 0.8241 0.8458 0.7088 0.1265  0.0568  -0.1267 38  ALA C CB    
4623 N N     . GLN C 67  ? 0.8485 0.9009 0.7446 0.1080  0.0599  -0.1347 39  GLN C N     
4624 C CA    . GLN C 67  ? 0.8517 0.9159 0.7521 0.0967  0.0661  -0.1416 39  GLN C CA    
4625 C C     . GLN C 67  ? 0.8710 0.9210 0.7618 0.0898  0.0677  -0.1395 39  GLN C C     
4626 O O     . GLN C 67  ? 0.8519 0.8959 0.7391 0.0801  0.0760  -0.1433 39  GLN C O     
4627 C CB    . GLN C 67  ? 0.8147 0.9075 0.7285 0.0972  0.0611  -0.1463 39  GLN C CB    
4628 C CG    . GLN C 67  ? 0.9132 1.0242 0.8390 0.1020  0.0621  -0.1500 39  GLN C CG    
4629 C CD    . GLN C 67  ? 0.9004 1.0399 0.8398 0.1048  0.0551  -0.1527 39  GLN C CD    
4630 O OE1   . GLN C 67  ? 0.8636 1.0062 0.8016 0.1070  0.0472  -0.1498 39  GLN C OE1   
4631 N NE2   . GLN C 67  ? 0.8686 1.0295 0.8213 0.1049  0.0580  -0.1578 39  GLN C NE2   
4632 N N     . LEU C 68  ? 0.9172 0.9613 0.8036 0.0949  0.0604  -0.1334 40  LEU C N     
4633 C CA    . LEU C 68  ? 0.8377 0.8693 0.7151 0.0895  0.0623  -0.1311 40  LEU C CA    
4634 C C     . LEU C 68  ? 0.8790 0.8857 0.7460 0.0873  0.0688  -0.1271 40  LEU C C     
4635 O O     . LEU C 68  ? 0.8816 0.8785 0.7423 0.0798  0.0750  -0.1283 40  LEU C O     
4636 C CB    . LEU C 68  ? 0.8091 0.8407 0.6846 0.0963  0.0533  -0.1245 40  LEU C CB    
4637 C CG    . LEU C 68  ? 0.7710 0.8256 0.6538 0.0968  0.0471  -0.1280 40  LEU C CG    
4638 C CD1   . LEU C 68  ? 0.7078 0.7598 0.5871 0.1040  0.0390  -0.1201 40  LEU C CD1   
4639 C CD2   . LEU C 68  ? 0.7048 0.7669 0.5869 0.0856  0.0523  -0.1359 40  LEU C CD2   
4640 N N     . ASP C 69  ? 0.9071 0.9030 0.7717 0.0938  0.0674  -0.1224 41  ASP C N     
4641 C CA    . ASP C 69  ? 0.9353 0.9086 0.7898 0.0920  0.0728  -0.1183 41  ASP C CA    
4642 C C     . ASP C 69  ? 0.8814 0.8529 0.7345 0.0830  0.0836  -0.1246 41  ASP C C     
4643 O O     . ASP C 69  ? 0.9206 0.8746 0.7650 0.0787  0.0896  -0.1222 41  ASP C O     
4644 C CB    . ASP C 69  ? 0.9348 0.8981 0.7866 0.1003  0.0685  -0.1132 41  ASP C CB    
4645 C CG    . ASP C 69  ? 0.9851 0.9427 0.8355 0.1079  0.0588  -0.1049 41  ASP C CG    
4646 O OD1   . ASP C 69  ? 0.9691 0.9276 0.8191 0.1066  0.0568  -0.1020 41  ASP C OD1   
4647 O OD2   . ASP C 69  ? 0.9571 0.9087 0.8065 0.1150  0.0536  -0.1013 41  ASP C OD2   
4648 N N     . ALA C 70  ? 0.8117 0.8011 0.6737 0.0800  0.0862  -0.1322 42  ALA C N     
4649 C CA    . ALA C 70  ? 0.7435 0.7327 0.6054 0.0705  0.0968  -0.1381 42  ALA C CA    
4650 C C     . ALA C 70  ? 0.7835 0.7743 0.6447 0.0605  0.1009  -0.1424 42  ALA C C     
4651 O O     . ALA C 70  ? 0.8421 0.8262 0.7003 0.0517  0.1102  -0.1459 42  ALA C O     
4652 C CB    . ALA C 70  ? 0.7640 0.7735 0.6371 0.0707  0.0985  -0.1444 42  ALA C CB    
4653 N N     . LEU C 71  ? 0.9004 0.8988 0.7633 0.0615  0.0945  -0.1421 43  LEU C N     
4654 C CA    . LEU C 71  ? 0.8744 0.8741 0.7352 0.0524  0.0977  -0.1469 43  LEU C CA    
4655 C C     . LEU C 71  ? 0.8642 0.8472 0.7147 0.0541  0.0963  -0.1411 43  LEU C C     
4656 O O     . LEU C 71  ? 0.8679 0.8460 0.7134 0.0466  0.1009  -0.1447 43  LEU C O     
4657 C CB    . LEU C 71  ? 0.7747 0.8006 0.6462 0.0504  0.0920  -0.1533 43  LEU C CB    
4658 C CG    . LEU C 71  ? 0.8865 0.9342 0.7711 0.0476  0.0933  -0.1599 43  LEU C CG    
4659 C CD1   . LEU C 71  ? 0.7915 0.8651 0.6862 0.0463  0.0863  -0.1651 43  LEU C CD1   
4660 C CD2   . LEU C 71  ? 0.9420 0.9844 0.8260 0.0364  0.1045  -0.1653 43  LEU C CD2   
4661 N N     . TRP C 72  ? 0.9072 0.8813 0.7543 0.0637  0.0905  -0.1323 44  TRP C N     
4662 C CA    . TRP C 72  ? 0.9032 0.8656 0.7427 0.0663  0.0884  -0.1262 44  TRP C CA    
4663 C C     . TRP C 72  ? 0.9427 0.8837 0.7721 0.0612  0.0974  -0.1245 44  TRP C C     
4664 O O     . TRP C 72  ? 0.9192 0.8521 0.7425 0.0613  0.0981  -0.1217 44  TRP C O     
4665 C CB    . TRP C 72  ? 0.8956 0.8535 0.7351 0.0771  0.0803  -0.1166 44  TRP C CB    
4666 C CG    . TRP C 72  ? 0.9072 0.8646 0.7439 0.0810  0.0752  -0.1113 44  TRP C CG    
4667 C CD1   . TRP C 72  ? 0.9183 0.8596 0.7475 0.0826  0.0770  -0.1041 44  TRP C CD1   
4668 C CD2   . TRP C 72  ? 0.8938 0.8685 0.7353 0.0840  0.0678  -0.1125 44  TRP C CD2   
4669 N NE1   . TRP C 72  ? 0.9555 0.9027 0.7844 0.0863  0.0717  -0.1007 44  TRP C NE1   
4670 C CE2   . TRP C 72  ? 0.8677 0.8350 0.7035 0.0872  0.0658  -0.1058 44  TRP C CE2   
4671 C CE3   . TRP C 72  ? 0.8762 0.8725 0.7265 0.0846  0.0626  -0.1181 44  TRP C CE3   
4672 C CZ2   . TRP C 72  ? 0.8369 0.8166 0.6741 0.0908  0.0591  -0.1045 44  TRP C CZ2   
4673 C CZ3   . TRP C 72  ? 0.8902 0.8990 0.7422 0.0884  0.0553  -0.1168 44  TRP C CZ3   
4674 C CH2   . TRP C 72  ? 0.8396 0.8397 0.6845 0.0913  0.0537  -0.1101 44  TRP C CH2   
4675 N N     . SER C 73  ? 1.0375 0.9690 0.8648 0.0573  0.1047  -0.1257 45  SER C N     
4676 C CA    . SER C 73  ? 1.0724 0.9832 0.8901 0.0527  0.1136  -0.1239 45  SER C CA    
4677 C C     . SER C 73  ? 1.0101 0.9219 0.8257 0.0425  0.1203  -0.1323 45  SER C C     
4678 O O     . SER C 73  ? 0.9973 0.8924 0.8042 0.0397  0.1265  -0.1308 45  SER C O     
4679 C CB    . SER C 73  ? 1.1080 1.0078 0.9230 0.0519  0.1192  -0.1221 45  SER C CB    
4680 O OG    . SER C 73  ? 1.0803 0.9924 0.9014 0.0457  0.1230  -0.1303 45  SER C OG    
4681 N N     . GLN C 74  ? 0.9831 0.9143 0.8068 0.0369  0.1192  -0.1411 46  GLN C N     
4682 C CA    . GLN C 74  ? 0.9911 0.9248 0.8136 0.0258  0.1247  -0.1502 46  GLN C CA    
4683 C C     . GLN C 74  ? 1.0196 0.9606 0.8401 0.0259  0.1195  -0.1527 46  GLN C C     
4684 O O     . GLN C 74  ? 0.9879 0.9325 0.8070 0.0166  0.1225  -0.1611 46  GLN C O     
4685 C CB    . GLN C 74  ? 0.9951 0.9476 0.8283 0.0187  0.1261  -0.1586 46  GLN C CB    
4686 C CG    . GLN C 74  ? 1.0526 0.9981 0.8867 0.0172  0.1330  -0.1572 46  GLN C CG    
4687 C CD    . GLN C 74  ? 1.1211 1.0883 0.9676 0.0117  0.1339  -0.1646 46  GLN C CD    
4688 O OE1   . GLN C 74  ? 1.1107 1.0855 0.9630 0.0172  0.1325  -0.1625 46  GLN C OE1   
4689 N NE2   . GLN C 74  ? 1.0366 1.0139 0.8872 0.0007  0.1365  -0.1733 46  GLN C NE2   
4690 N N     . LEU C 75  ? 1.0325 0.9752 0.8523 0.0358  0.1118  -0.1456 47  LEU C N     
4691 C CA    . LEU C 75  ? 1.0073 0.9582 0.8248 0.0371  0.1063  -0.1470 47  LEU C CA    
4692 C C     . LEU C 75  ? 0.9736 0.9036 0.7785 0.0384  0.1113  -0.1426 47  LEU C C     
4693 O O     . LEU C 75  ? 0.9855 0.9029 0.7874 0.0461  0.1111  -0.1328 47  LEU C O     
4694 C CB    . LEU C 75  ? 0.9760 0.9417 0.8001 0.0473  0.0953  -0.1414 47  LEU C CB    
4695 C CG    . LEU C 75  ? 0.8852 0.8739 0.7220 0.0479  0.0894  -0.1455 47  LEU C CG    
4696 C CD1   . LEU C 75  ? 0.7634 0.7600 0.6050 0.0595  0.0796  -0.1378 47  LEU C CD1   
4697 C CD2   . LEU C 75  ? 0.8812 0.8886 0.7220 0.0399  0.0877  -0.1557 47  LEU C CD2   
4698 N N     . SER C 76  ? 0.9013 0.8279 0.6992 0.0309  0.1156  -0.1498 48  SER C N     
4699 C CA    . SER C 76  ? 1.0025 0.9110 0.7882 0.0327  0.1203  -0.1467 48  SER C CA    
4700 C C     . SER C 76  ? 1.0249 0.9434 0.8086 0.0394  0.1126  -0.1437 48  SER C C     
4701 O O     . SER C 76  ? 1.0711 1.0104 0.8608 0.0390  0.1048  -0.1479 48  SER C O     
4702 C CB    . SER C 76  ? 1.0159 0.9134 0.7929 0.0215  0.1291  -0.1563 48  SER C CB    
4703 O OG    . SER C 76  ? 0.9779 0.8928 0.7568 0.0144  0.1247  -0.1666 48  SER C OG    
4704 N N     . TRP C 77  ? 1.0480 0.9522 0.8237 0.0459  0.1151  -0.1360 49  TRP C N     
4705 C CA    . TRP C 77  ? 1.0819 0.9938 0.8549 0.0529  0.1089  -0.1316 49  TRP C CA    
4706 C C     . TRP C 77  ? 1.1475 1.0440 0.9067 0.0526  0.1160  -0.1322 49  TRP C C     
4707 O O     . TRP C 77  ? 1.1495 1.0259 0.9028 0.0519  0.1251  -0.1300 49  TRP C O     
4708 C CB    . TRP C 77  ? 1.0376 0.9507 0.8170 0.0638  0.1031  -0.1187 49  TRP C CB    
4709 C CG    . TRP C 77  ? 1.0071 0.9345 0.7987 0.0655  0.0957  -0.1180 49  TRP C CG    
4710 C CD1   . TRP C 77  ? 1.0066 0.9285 0.8037 0.0656  0.0973  -0.1156 49  TRP C CD1   
4711 C CD2   . TRP C 77  ? 1.0477 0.9968 0.8468 0.0679  0.0860  -0.1199 49  TRP C CD2   
4712 N NE1   . TRP C 77  ? 1.0182 0.9564 0.8254 0.0680  0.0894  -0.1161 49  TRP C NE1   
4713 C CE2   . TRP C 77  ? 1.0526 1.0077 0.8617 0.0696  0.0824  -0.1186 49  TRP C CE2   
4714 C CE3   . TRP C 77  ? 1.0357 0.9994 0.8332 0.0691  0.0799  -0.1223 49  TRP C CE3   
4715 C CZ2   . TRP C 77  ? 1.0048 0.9798 0.8232 0.0730  0.0734  -0.1196 49  TRP C CZ2   
4716 C CZ3   . TRP C 77  ? 0.9699 0.9539 0.7769 0.0722  0.0705  -0.1228 49  TRP C CZ3   
4717 C CH2   . TRP C 77  ? 0.9145 0.9038 0.7321 0.0744  0.0675  -0.1214 49  TRP C CH2   
4718 N N     . PRO C 78  ? 1.1930 1.0981 0.9463 0.0535  0.1124  -0.1350 50  PRO C N     
4719 C CA    . PRO C 78  ? 1.2203 1.1105 0.9589 0.0541  0.1194  -0.1358 50  PRO C CA    
4720 C C     . PRO C 78  ? 1.2460 1.1267 0.9833 0.0652  0.1213  -0.1222 50  PRO C C     
4721 O O     . PRO C 78  ? 1.1856 1.0738 0.9326 0.0724  0.1150  -0.1124 50  PRO C O     
4722 C CB    . PRO C 78  ? 1.1769 1.0827 0.9102 0.0519  0.1133  -0.1430 50  PRO C CB    
4723 C CG    . PRO C 78  ? 1.1730 1.1013 0.9193 0.0563  0.1017  -0.1391 50  PRO C CG    
4724 C CD    . PRO C 78  ? 1.1871 1.1160 0.9460 0.0545  0.1016  -0.1377 50  PRO C CD    
4725 N N     . GLN C 79  ? 1.3177 1.1811 1.0426 0.0664  0.1303  -0.1218 51  GLN C N     
4726 C CA    . GLN C 79  ? 1.2588 1.1132 0.9826 0.0768  0.1334  -0.1089 51  GLN C CA    
4727 C C     . GLN C 79  ? 1.1708 1.0406 0.8961 0.0841  0.1255  -0.1024 51  GLN C C     
4728 O O     . GLN C 79  ? 1.1077 0.9825 0.8425 0.0917  0.1208  -0.0906 51  GLN C O     
4729 C CB    . GLN C 79  ? 1.2374 1.0705 0.9471 0.0768  0.1455  -0.1107 51  GLN C CB    
4730 C CG    . GLN C 79  ? 1.2623 1.0763 0.9722 0.0740  0.1542  -0.1102 51  GLN C CG    
4731 C CD    . GLN C 79  ? 1.3424 1.1536 1.0630 0.0818  0.1533  -0.0961 51  GLN C CD    
4732 O OE1   . GLN C 79  ? 1.4308 1.2480 1.1556 0.0906  0.1498  -0.0854 51  GLN C OE1   
4733 N NE2   . GLN C 79  ? 1.2456 1.0479 0.9705 0.0783  0.1562  -0.0959 51  GLN C NE2   
4734 N N     . THR C 80  ? 1.1487 1.0258 0.8644 0.0818  0.1238  -0.1100 52  THR C N     
4735 C CA    . THR C 80  ? 1.1071 1.0004 0.8236 0.0880  0.1156  -0.1047 52  THR C CA    
4736 C C     . THR C 80  ? 1.0832 0.9973 0.8097 0.0846  0.1043  -0.1092 52  THR C C     
4737 O O     . THR C 80  ? 1.0505 0.9698 0.7749 0.0757  0.1032  -0.1215 52  THR C O     
4738 C CB    . THR C 80  ? 1.1097 1.0007 0.8094 0.0879  0.1192  -0.1102 52  THR C CB    
4739 O OG1   . THR C 80  ? 1.1311 1.0020 0.8215 0.0919  0.1307  -0.1061 52  THR C OG1   
4740 C CG2   . THR C 80  ? 1.1371 1.0445 0.8369 0.0949  0.1110  -0.1036 52  THR C CG2   
4741 N N     . PRO C 81  ? 1.0474 0.9734 0.7852 0.0912  0.0959  -0.0996 53  PRO C N     
4742 C CA    . PRO C 81  ? 1.0323 0.9770 0.7808 0.0890  0.0858  -0.1033 53  PRO C CA    
4743 C C     . PRO C 81  ? 0.9624 0.9226 0.7045 0.0855  0.0803  -0.1123 53  PRO C C     
4744 O O     . PRO C 81  ? 0.9303 0.8914 0.6616 0.0887  0.0805  -0.1109 53  PRO C O     
4745 C CB    . PRO C 81  ? 1.0122 0.9630 0.7710 0.0983  0.0788  -0.0899 53  PRO C CB    
4746 C CG    . PRO C 81  ? 0.9548 0.8886 0.7123 0.1032  0.0859  -0.0797 53  PRO C CG    
4747 C CD    . PRO C 81  ? 1.0197 0.9411 0.7626 0.1007  0.0959  -0.0846 53  PRO C CD    
4748 N N     . LEU C 82  ? 0.8705 0.8436 0.6195 0.0788  0.0754  -0.1214 54  LEU C N     
4749 C CA    . LEU C 82  ? 0.7634 0.7552 0.5101 0.0752  0.0680  -0.1297 54  LEU C CA    
4750 C C     . LEU C 82  ? 0.7554 0.7674 0.5162 0.0801  0.0569  -0.1253 54  LEU C C     
4751 O O     . LEU C 82  ? 0.7886 0.7993 0.5614 0.0830  0.0559  -0.1200 54  LEU C O     
4752 C CB    . LEU C 82  ? 0.7391 0.7315 0.4835 0.0628  0.0712  -0.1443 54  LEU C CB    
4753 C CG    . LEU C 82  ? 0.7725 0.7448 0.5012 0.0566  0.0818  -0.1510 54  LEU C CG    
4754 C CD1   . LEU C 82  ? 0.6527 0.6266 0.3814 0.0435  0.0838  -0.1652 54  LEU C CD1   
4755 C CD2   . LEU C 82  ? 0.8352 0.8064 0.5479 0.0601  0.0815  -0.1509 54  LEU C CD2   
4756 N N     . PRO C 83  ? 0.7482 0.7784 0.5073 0.0816  0.0485  -0.1273 55  PRO C N     
4757 C CA    . PRO C 83  ? 0.7016 0.7507 0.4741 0.0870  0.0380  -0.1230 55  PRO C CA    
4758 C C     . PRO C 83  ? 0.6606 0.7186 0.4464 0.0811  0.0367  -0.1303 55  PRO C C     
4759 O O     . PRO C 83  ? 0.6768 0.7351 0.4610 0.0711  0.0407  -0.1414 55  PRO C O     
4760 C CB    . PRO C 83  ? 0.7262 0.7925 0.4918 0.0880  0.0303  -0.1257 55  PRO C CB    
4761 C CG    . PRO C 83  ? 0.7798 0.8333 0.5271 0.0860  0.0368  -0.1278 55  PRO C CG    
4762 C CD    . PRO C 83  ? 0.7633 0.7967 0.5072 0.0792  0.0480  -0.1328 55  PRO C CD    
4763 N N     . VAL C 84  ? 0.6112 0.6760 0.4102 0.0875  0.0315  -0.1238 56  VAL C N     
4764 C CA    . VAL C 84  ? 0.6217 0.6962 0.4343 0.0840  0.0301  -0.1292 56  VAL C CA    
4765 C C     . VAL C 84  ? 0.6576 0.7563 0.4797 0.0890  0.0192  -0.1287 56  VAL C C     
4766 O O     . VAL C 84  ? 0.7217 0.8237 0.5439 0.0984  0.0129  -0.1195 56  VAL C O     
4767 C CB    . VAL C 84  ? 0.5950 0.6547 0.4142 0.0876  0.0342  -0.1226 56  VAL C CB    
4768 C CG1   . VAL C 84  ? 0.5848 0.6566 0.4180 0.0867  0.0316  -0.1265 56  VAL C CG1   
4769 C CG2   . VAL C 84  ? 0.6672 0.7051 0.4783 0.0816  0.0452  -0.1245 56  VAL C CG2   
4770 N N     . LEU C 85  ? 0.6295 0.7454 0.4601 0.0827  0.0170  -0.1383 57  LEU C N     
4771 C CA    . LEU C 85  ? 0.5952 0.7366 0.4350 0.0865  0.0068  -0.1392 57  LEU C CA    
4772 C C     . LEU C 85  ? 0.6488 0.7995 0.5053 0.0888  0.0056  -0.1396 57  LEU C C     
4773 O O     . LEU C 85  ? 0.6442 0.7911 0.5054 0.0814  0.0122  -0.1459 57  LEU C O     
4774 C CB    . LEU C 85  ? 0.5426 0.7005 0.3791 0.0774  0.0041  -0.1501 57  LEU C CB    
4775 C CG    . LEU C 85  ? 0.5039 0.6912 0.3501 0.0803  -0.0070 -0.1519 57  LEU C CG    
4776 C CD1   . LEU C 85  ? 0.5041 0.6951 0.3450 0.0917  -0.0149 -0.1418 57  LEU C CD1   
4777 C CD2   . LEU C 85  ? 0.5162 0.7179 0.3593 0.0686  -0.0087 -0.1640 57  LEU C CD2   
4778 N N     . ASP C 86  ? 0.5878 0.7500 0.4524 0.0992  -0.0025 -0.1328 58  ASP C N     
4779 C CA    . ASP C 86  ? 0.5808 0.7541 0.4609 0.1030  -0.0046 -0.1333 58  ASP C CA    
4780 C C     . ASP C 86  ? 0.5815 0.7837 0.4705 0.1060  -0.0141 -0.1357 58  ASP C C     
4781 O O     . ASP C 86  ? 0.5862 0.7944 0.4740 0.1153  -0.0220 -0.1284 58  ASP C O     
4782 C CB    . ASP C 86  ? 0.6143 0.7732 0.4962 0.1137  -0.0054 -0.1227 58  ASP C CB    
4783 C CG    . ASP C 86  ? 0.7931 0.9602 0.6891 0.1179  -0.0061 -0.1238 58  ASP C CG    
4784 O OD1   . ASP C 86  ? 0.8065 0.9863 0.7106 0.1111  -0.0031 -0.1326 58  ASP C OD1   
4785 O OD2   . ASP C 86  ? 0.7744 0.9347 0.6730 0.1279  -0.0095 -0.1158 58  ASP C OD2   
4786 N N     . ILE C 87  ? 0.5627 0.7830 0.4611 0.0980  -0.0135 -0.1455 59  ILE C N     
4787 C CA    . ILE C 87  ? 0.4866 0.7370 0.3949 0.0995  -0.0226 -0.1487 59  ILE C CA    
4788 C C     . ILE C 87  ? 0.5339 0.7967 0.4587 0.1086  -0.0254 -0.1456 59  ILE C C     
4789 O O     . ILE C 87  ? 0.5879 0.8431 0.5193 0.1074  -0.0185 -0.1472 59  ILE C O     
4790 C CB    . ILE C 87  ? 0.4799 0.7450 0.3906 0.0853  -0.0209 -0.1610 59  ILE C CB    
4791 C CG1   . ILE C 87  ? 0.4908 0.7406 0.3830 0.0768  -0.0176 -0.1645 59  ILE C CG1   
4792 C CG2   . ILE C 87  ? 0.4827 0.7806 0.4041 0.0866  -0.0312 -0.1639 59  ILE C CG2   
4793 C CD1   . ILE C 87  ? 0.5005 0.7603 0.3929 0.0616  -0.0154 -0.1770 59  ILE C CD1   
4794 N N     . GLY C 88  ? 0.5066 0.7881 0.4376 0.1181  -0.0352 -0.1411 60  GLY C N     
4795 C CA    . GLY C 88  ? 0.4797 0.7718 0.4254 0.1288  -0.0382 -0.1373 60  GLY C CA    
4796 C C     . GLY C 88  ? 0.5555 0.8218 0.4974 0.1368  -0.0341 -0.1295 60  GLY C C     
4797 O O     . GLY C 88  ? 0.6473 0.9094 0.5971 0.1378  -0.0287 -0.1311 60  GLY C O     
4798 N N     . CYS C 89  ? 0.5204 0.7692 0.4499 0.1422  -0.0366 -0.1209 61  CYS C N     
4799 C CA    . CYS C 89  ? 0.5849 0.8069 0.5090 0.1475  -0.0327 -0.1135 61  CYS C CA    
4800 C C     . CYS C 89  ? 0.5870 0.8097 0.5194 0.1607  -0.0374 -0.1069 61  CYS C C     
4801 O O     . CYS C 89  ? 0.6238 0.8258 0.5540 0.1644  -0.0339 -0.1026 61  CYS C O     
4802 C CB    . CYS C 89  ? 0.5921 0.7963 0.5009 0.1479  -0.0334 -0.1063 61  CYS C CB    
4803 S SG    . CYS C 89  ? 0.5636 0.7803 0.4692 0.1577  -0.0448 -0.0979 61  CYS C SG    
4804 N N     . GLY C 90  ? 0.5535 0.7989 0.4950 0.1679  -0.0453 -0.1059 62  GLY C N     
4805 C CA    . GLY C 90  ? 0.5734 0.8186 0.5219 0.1813  -0.0499 -0.0993 62  GLY C CA    
4806 C C     . GLY C 90  ? 0.5300 0.7568 0.4685 0.1893  -0.0545 -0.0877 62  GLY C C     
4807 O O     . GLY C 90  ? 0.5108 0.7380 0.4404 0.1877  -0.0580 -0.0840 62  GLY C O     
4808 N N     . PRO C 91  ? 0.5561 0.7661 0.4956 0.1978  -0.0545 -0.0819 63  PRO C N     
4809 C CA    . PRO C 91  ? 0.5197 0.7112 0.4507 0.2048  -0.0589 -0.0704 63  PRO C CA    
4810 C C     . PRO C 91  ? 0.5729 0.7395 0.4920 0.1977  -0.0535 -0.0675 63  PRO C C     
4811 O O     . PRO C 91  ? 0.5614 0.7073 0.4758 0.2024  -0.0547 -0.0591 63  PRO C O     
4812 C CB    . PRO C 91  ? 0.5354 0.7191 0.4728 0.2160  -0.0610 -0.0667 63  PRO C CB    
4813 C CG    . PRO C 91  ? 0.5767 0.7630 0.5210 0.2119  -0.0539 -0.0761 63  PRO C CG    
4814 C CD    . PRO C 91  ? 0.5969 0.8072 0.5463 0.2027  -0.0516 -0.0853 63  PRO C CD    
4815 N N     . GLY C 92  ? 0.6105 0.7789 0.5252 0.1864  -0.0476 -0.0742 64  GLY C N     
4816 C CA    . GLY C 92  ? 0.6245 0.7716 0.5280 0.1800  -0.0424 -0.0711 64  GLY C CA    
4817 C C     . GLY C 92  ? 0.5940 0.7183 0.4965 0.1797  -0.0375 -0.0694 64  GLY C C     
4818 O O     . GLY C 92  ? 0.6072 0.7122 0.5017 0.1781  -0.0356 -0.0630 64  GLY C O     
4819 N N     . ASP C 93  ? 0.5920 0.7185 0.5022 0.1813  -0.0354 -0.0748 65  ASP C N     
4820 C CA    . ASP C 93  ? 0.5776 0.6824 0.4856 0.1815  -0.0313 -0.0735 65  ASP C CA    
4821 C C     . ASP C 93  ? 0.5933 0.6906 0.4976 0.1708  -0.0221 -0.0802 65  ASP C C     
4822 O O     . ASP C 93  ? 0.6266 0.7028 0.5244 0.1685  -0.0188 -0.0766 65  ASP C O     
4823 C CB    . ASP C 93  ? 0.6346 0.7431 0.5509 0.1897  -0.0332 -0.0755 65  ASP C CB    
4824 C CG    . ASP C 93  ? 0.6543 0.7614 0.5723 0.2014  -0.0418 -0.0670 65  ASP C CG    
4825 O OD1   . ASP C 93  ? 0.6563 0.7454 0.5674 0.2033  -0.0447 -0.0581 65  ASP C OD1   
4826 O OD2   . ASP C 93  ? 0.6386 0.7622 0.5653 0.2087  -0.0454 -0.0689 65  ASP C OD2   
4827 N N     . ILE C 94  ? 0.6196 0.7340 0.5282 0.1640  -0.0182 -0.0896 66  ILE C N     
4828 C CA    . ILE C 94  ? 0.6130 0.7205 0.5179 0.1533  -0.0091 -0.0960 66  ILE C CA    
4829 C C     . ILE C 94  ? 0.6125 0.7163 0.5085 0.1465  -0.0074 -0.0949 66  ILE C C     
4830 O O     . ILE C 94  ? 0.6375 0.7443 0.5313 0.1370  -0.0013 -0.1021 66  ILE C O     
4831 C CB    . ILE C 94  ? 0.6816 0.8083 0.5958 0.1485  -0.0051 -0.1066 66  ILE C CB    
4832 C CG1   . ILE C 94  ? 0.7015 0.8373 0.6258 0.1577  -0.0081 -0.1070 66  ILE C CG1   
4833 C CG2   . ILE C 94  ? 0.7336 0.8489 0.6443 0.1390  0.0048  -0.1121 66  ILE C CG2   
4834 C CD1   . ILE C 94  ? 0.7323 0.8461 0.6527 0.1628  -0.0062 -0.1031 66  ILE C CD1   
4835 N N     . ALA C 95  ? 0.5872 0.6841 0.4777 0.1515  -0.0124 -0.0859 67  ALA C N     
4836 C CA    . ALA C 95  ? 0.5469 0.6389 0.4280 0.1466  -0.0105 -0.0837 67  ALA C CA    
4837 C C     . ALA C 95  ? 0.5796 0.6509 0.4544 0.1504  -0.0112 -0.0727 67  ALA C C     
4838 O O     . ALA C 95  ? 0.6981 0.7553 0.5659 0.1453  -0.0053 -0.0712 67  ALA C O     
4839 C CB    . ALA C 95  ? 0.5132 0.6246 0.3942 0.1483  -0.0165 -0.0842 67  ALA C CB    
4840 N N     . ARG C 96  ? 0.5211 0.5904 0.3989 0.1595  -0.0183 -0.0646 68  ARG C N     
4841 C CA    . ARG C 96  ? 0.5254 0.5758 0.3987 0.1627  -0.0197 -0.0536 68  ARG C CA    
4842 C C     . ARG C 96  ? 0.5950 0.6273 0.4685 0.1613  -0.0162 -0.0532 68  ARG C C     
4843 O O     . ARG C 96  ? 0.7081 0.7243 0.5768 0.1590  -0.0136 -0.0472 68  ARG C O     
4844 C CB    . ARG C 96  ? 0.5413 0.5946 0.4174 0.1722  -0.0286 -0.0450 68  ARG C CB    
4845 C CG    . ARG C 96  ? 0.5909 0.6244 0.4659 0.1763  -0.0315 -0.0343 68  ARG C CG    
4846 C CD    . ARG C 96  ? 0.6146 0.6364 0.4830 0.1723  -0.0279 -0.0272 68  ARG C CD    
4847 N NE    . ARG C 96  ? 0.7043 0.7101 0.5731 0.1760  -0.0318 -0.0160 68  ARG C NE    
4848 C CZ    . ARG C 96  ? 0.7488 0.7401 0.6147 0.1725  -0.0285 -0.0099 68  ARG C CZ    
4849 N NH1   . ARG C 96  ? 0.7478 0.7372 0.6096 0.1659  -0.0208 -0.0137 68  ARG C NH1   
4850 N NH2   . ARG C 96  ? 0.7504 0.7287 0.6179 0.1755  -0.0332 0.0004  68  ARG C NH2   
4851 N N     . LYS C 97  ? 0.5429 0.5781 0.4218 0.1626  -0.0159 -0.0594 69  LYS C N     
4852 C CA    . LYS C 97  ? 0.5798 0.5979 0.4578 0.1624  -0.0137 -0.0588 69  LYS C CA    
4853 C C     . LYS C 97  ? 0.5895 0.6052 0.4658 0.1545  -0.0049 -0.0672 69  LYS C C     
4854 O O     . LYS C 97  ? 0.5927 0.5918 0.4654 0.1528  -0.0020 -0.0657 69  LYS C O     
4855 C CB    . LYS C 97  ? 0.5734 0.5924 0.4567 0.1705  -0.0190 -0.0590 69  LYS C CB    
4856 C CG    . LYS C 97  ? 0.5463 0.5698 0.4321 0.1788  -0.0276 -0.0515 69  LYS C CG    
4857 C CD    . LYS C 97  ? 0.4671 0.4780 0.3541 0.1865  -0.0328 -0.0474 69  LYS C CD    
4858 C CE    . LYS C 97  ? 0.5393 0.5618 0.4317 0.1958  -0.0400 -0.0448 69  LYS C CE    
4859 N NZ    . LYS C 97  ? 0.7315 0.7489 0.6270 0.2032  -0.0423 -0.0471 69  LYS C NZ    
4860 N N     . VAL C 98  ? 0.6043 0.6358 0.4828 0.1492  -0.0008 -0.0758 70  VAL C N     
4861 C CA    . VAL C 98  ? 0.5843 0.6142 0.4616 0.1411  0.0079  -0.0840 70  VAL C CA    
4862 C C     . VAL C 98  ? 0.6087 0.6362 0.4797 0.1330  0.0136  -0.0855 70  VAL C C     
4863 O O     . VAL C 98  ? 0.6432 0.6550 0.5083 0.1286  0.0195  -0.0843 70  VAL C O     
4864 C CB    . VAL C 98  ? 0.6305 0.6796 0.5164 0.1404  0.0090  -0.0935 70  VAL C CB    
4865 C CG1   . VAL C 98  ? 0.5987 0.6470 0.4833 0.1308  0.0185  -0.1017 70  VAL C CG1   
4866 C CG2   . VAL C 98  ? 0.7012 0.7493 0.5920 0.1488  0.0053  -0.0924 70  VAL C CG2   
4867 N N     . LEU C 99  ? 0.5561 0.5988 0.4276 0.1314  0.0118  -0.0882 71  LEU C N     
4868 C CA    . LEU C 99  ? 0.6210 0.6619 0.4856 0.1235  0.0176  -0.0915 71  LEU C CA    
4869 C C     . LEU C 99  ? 0.6613 0.6861 0.5178 0.1249  0.0185  -0.0823 71  LEU C C     
4870 O O     . LEU C 99  ? 0.7100 0.7197 0.5611 0.1204  0.0254  -0.0817 71  LEU C O     
4871 C CB    . LEU C 99  ? 0.6139 0.6756 0.4801 0.1216  0.0144  -0.0971 71  LEU C CB    
4872 C CG    . LEU C 99  ? 0.6003 0.6799 0.4743 0.1166  0.0158  -0.1080 71  LEU C CG    
4873 C CD1   . LEU C 99  ? 0.5965 0.6974 0.4721 0.1154  0.0106  -0.1121 71  LEU C CD1   
4874 C CD2   . LEU C 99  ? 0.5934 0.6644 0.4644 0.1064  0.0257  -0.1151 71  LEU C CD2   
4875 N N     . ALA C 100 ? 0.6412 0.6695 0.4972 0.1312  0.0119  -0.0748 72  ALA C N     
4876 C CA    . ALA C 100 ? 0.6541 0.6703 0.5032 0.1326  0.0130  -0.0658 72  ALA C CA    
4877 C C     . ALA C 100 ? 0.7045 0.7007 0.5524 0.1330  0.0158  -0.0589 72  ALA C C     
4878 O O     . ALA C 100 ? 0.7541 0.7399 0.5961 0.1306  0.0211  -0.0552 72  ALA C O     
4879 C CB    . ALA C 100 ? 0.6357 0.6592 0.4858 0.1401  0.0048  -0.0577 72  ALA C CB    
4880 N N     . PRO C 101 ? 0.6967 0.6867 0.5493 0.1362  0.0126  -0.0568 73  PRO C N     
4881 C CA    . PRO C 101 ? 0.6890 0.6602 0.5395 0.1359  0.0148  -0.0503 73  PRO C CA    
4882 C C     . PRO C 101 ? 0.6861 0.6482 0.5316 0.1289  0.0243  -0.0546 73  PRO C C     
4883 O O     . PRO C 101 ? 0.7044 0.6537 0.5464 0.1283  0.0273  -0.0478 73  PRO C O     
4884 C CB    . PRO C 101 ? 0.7194 0.6877 0.5745 0.1397  0.0100  -0.0508 73  PRO C CB    
4885 C CG    . PRO C 101 ? 0.7176 0.7003 0.5777 0.1453  0.0028  -0.0512 73  PRO C CG    
4886 C CD    . PRO C 101 ? 0.6920 0.6909 0.5515 0.1417  0.0057  -0.0582 73  PRO C CD    
4887 N N     . ARG C 102 ? 0.6428 0.6112 0.4883 0.1236  0.0292  -0.0653 74  ARG C N     
4888 C CA    . ARG C 102 ? 0.7150 0.6736 0.5555 0.1167  0.0386  -0.0696 74  ARG C CA    
4889 C C     . ARG C 102 ? 0.7537 0.7156 0.5888 0.1117  0.0443  -0.0738 74  ARG C C     
4890 O O     . ARG C 102 ? 0.7896 0.7456 0.6206 0.1051  0.0524  -0.0798 74  ARG C O     
4891 C CB    . ARG C 102 ? 0.7372 0.6987 0.5803 0.1130  0.0418  -0.0785 74  ARG C CB    
4892 C CG    . ARG C 102 ? 0.7358 0.7176 0.5852 0.1126  0.0389  -0.0867 74  ARG C CG    
4893 C CD    . ARG C 102 ? 0.7591 0.7442 0.6139 0.1136  0.0386  -0.0912 74  ARG C CD    
4894 N NE    . ARG C 102 ? 0.7535 0.7340 0.6107 0.1219  0.0313  -0.0845 74  ARG C NE    
4895 C CZ    . ARG C 102 ? 0.7786 0.7543 0.6371 0.1242  0.0312  -0.0858 74  ARG C CZ    
4896 N NH1   . ARG C 102 ? 0.8014 0.7769 0.6596 0.1191  0.0383  -0.0928 74  ARG C NH1   
4897 N NH2   . ARG C 102 ? 0.7178 0.6882 0.5775 0.1317  0.0240  -0.0799 74  ARG C NH2   
4898 N N     . LEU C 103 ? 0.7080 0.6781 0.5420 0.1146  0.0405  -0.0710 75  LEU C N     
4899 C CA    . LEU C 103 ? 0.7396 0.7120 0.5667 0.1095  0.0462  -0.0764 75  LEU C CA    
4900 C C     . LEU C 103 ? 0.7470 0.7036 0.5670 0.1098  0.0522  -0.0696 75  LEU C C     
4901 O O     . LEU C 103 ? 0.7041 0.6535 0.5257 0.1153  0.0495  -0.0588 75  LEU C O     
4902 C CB    . LEU C 103 ? 0.7471 0.7360 0.5741 0.1119  0.0402  -0.0776 75  LEU C CB    
4903 C CG    . LEU C 103 ? 0.7042 0.7118 0.5365 0.1091  0.0366  -0.0876 75  LEU C CG    
4904 C CD1   . LEU C 103 ? 0.6410 0.6630 0.4698 0.1097  0.0325  -0.0898 75  LEU C CD1   
4905 C CD2   . LEU C 103 ? 0.7780 0.7839 0.6100 0.1001  0.0440  -0.0981 75  LEU C CD2   
4906 N N     . PRO C 104 ? 0.8300 0.7809 0.6424 0.1038  0.0607  -0.0757 76  PRO C N     
4907 C CA    . PRO C 104 ? 0.8471 0.7841 0.6523 0.1050  0.0671  -0.0694 76  PRO C CA    
4908 C C     . PRO C 104 ? 0.8015 0.7430 0.6057 0.1117  0.0627  -0.0605 76  PRO C C     
4909 O O     . PRO C 104 ? 0.8696 0.8239 0.6717 0.1122  0.0590  -0.0638 76  PRO C O     
4910 C CB    . PRO C 104 ? 0.8315 0.7657 0.6280 0.0976  0.0753  -0.0800 76  PRO C CB    
4911 C CG    . PRO C 104 ? 0.8976 0.8377 0.6984 0.0911  0.0754  -0.0900 76  PRO C CG    
4912 C CD    . PRO C 104 ? 0.8615 0.8159 0.6724 0.0954  0.0656  -0.0882 76  PRO C CD    
4913 N N     . ALA C 105 ? 0.7939 0.7259 0.6001 0.1167  0.0629  -0.0487 77  ALA C N     
4914 C CA    . ALA C 105 ? 0.8186 0.7549 0.6252 0.1231  0.0590  -0.0387 77  ALA C CA    
4915 C C     . ALA C 105 ? 0.8804 0.8190 0.6767 0.1224  0.0643  -0.0420 77  ALA C C     
4916 O O     . ALA C 105 ? 0.8573 0.7860 0.6461 0.1192  0.0734  -0.0459 77  ALA C O     
4917 C CB    . ALA C 105 ? 0.8361 0.7611 0.6467 0.1272  0.0599  -0.0259 77  ALA C CB    
4918 N N     . GLY C 106 ? 0.8488 0.7999 0.6440 0.1258  0.0585  -0.0404 78  GLY C N     
4919 C CA    . GLY C 106 ? 0.8308 0.7864 0.6150 0.1251  0.0619  -0.0448 78  GLY C CA    
4920 C C     . GLY C 106 ? 0.8840 0.8526 0.6649 0.1202  0.0583  -0.0574 78  GLY C C     
4921 O O     . GLY C 106 ? 0.9422 0.9185 0.7147 0.1207  0.0575  -0.0601 78  GLY C O     
4922 N N     . THR C 107 ? 0.8864 0.8584 0.6740 0.1156  0.0560  -0.0649 79  THR C N     
4923 C CA    . THR C 107 ? 0.8632 0.8501 0.6507 0.1109  0.0519  -0.0763 79  THR C CA    
4924 C C     . THR C 107 ? 0.8556 0.8591 0.6485 0.1168  0.0411  -0.0721 79  THR C C     
4925 O O     . THR C 107 ? 0.8314 0.8342 0.6323 0.1229  0.0361  -0.0625 79  THR C O     
4926 C CB    . THR C 107 ? 0.8440 0.8303 0.6384 0.1048  0.0532  -0.0844 79  THR C CB    
4927 O OG1   . THR C 107 ? 0.8608 0.8296 0.6504 0.1003  0.0632  -0.0863 79  THR C OG1   
4928 C CG2   . THR C 107 ? 0.8468 0.8488 0.6414 0.0986  0.0504  -0.0969 79  THR C CG2   
4929 N N     . ARG C 108 ? 0.8054 0.8233 0.5936 0.1148  0.0374  -0.0791 80  ARG C N     
4930 C CA    . ARG C 108 ? 0.7558 0.7907 0.5483 0.1203  0.0271  -0.0758 80  ARG C CA    
4931 C C     . ARG C 108 ? 0.7297 0.7808 0.5300 0.1163  0.0220  -0.0859 80  ARG C C     
4932 O O     . ARG C 108 ? 0.7074 0.7615 0.5043 0.1080  0.0255  -0.0974 80  ARG C O     
4933 C CB    . ARG C 108 ? 0.7438 0.7843 0.5242 0.1226  0.0260  -0.0742 80  ARG C CB    
4934 C CG    . ARG C 108 ? 0.8362 0.8970 0.6186 0.1262  0.0157  -0.0745 80  ARG C CG    
4935 C CD    . ARG C 108 ? 0.9070 0.9708 0.6763 0.1298  0.0149  -0.0702 80  ARG C CD    
4936 N NE    . ARG C 108 ? 1.0703 1.1396 0.8274 0.1230  0.0168  -0.0820 80  ARG C NE    
4937 C CZ    . ARG C 108 ? 0.9414 1.0294 0.6979 0.1209  0.0091  -0.0892 80  ARG C CZ    
4938 N NH1   . ARG C 108 ? 0.9009 1.0044 0.6686 0.1260  -0.0005 -0.0856 80  ARG C NH1   
4939 N NH2   . ARG C 108 ? 0.8907 0.9819 0.6352 0.1137  0.0110  -0.1003 80  ARG C NH2   
4940 N N     . LEU C 109 ? 0.6720 0.7331 0.4829 0.1221  0.0138  -0.0815 81  LEU C N     
4941 C CA    . LEU C 109 ? 0.5696 0.6472 0.3902 0.1200  0.0088  -0.0895 81  LEU C CA    
4942 C C     . LEU C 109 ? 0.5912 0.6894 0.4113 0.1234  -0.0001 -0.0902 81  LEU C C     
4943 O O     . LEU C 109 ? 0.6760 0.7753 0.4929 0.1309  -0.0048 -0.0808 81  LEU C O     
4944 C CB    . LEU C 109 ? 0.4995 0.5742 0.3322 0.1249  0.0061  -0.0849 81  LEU C CB    
4945 C CG    . LEU C 109 ? 0.4980 0.5885 0.3422 0.1238  0.0023  -0.0924 81  LEU C CG    
4946 C CD1   . LEU C 109 ? 0.5487 0.6403 0.3931 0.1132  0.0093  -0.1043 81  LEU C CD1   
4947 C CD2   . LEU C 109 ? 0.5099 0.5943 0.3633 0.1302  -0.0001 -0.0865 81  LEU C CD2   
4948 N N     . VAL C 110 ? 0.5568 0.6717 0.3804 0.1176  -0.0023 -0.1011 82  VAL C N     
4949 C CA    . VAL C 110 ? 0.4911 0.6285 0.3164 0.1205  -0.0117 -0.1026 82  VAL C CA    
4950 C C     . VAL C 110 ? 0.5683 0.7220 0.4094 0.1207  -0.0160 -0.1076 82  VAL C C     
4951 O O     . VAL C 110 ? 0.6612 0.8181 0.5069 0.1122  -0.0117 -0.1174 82  VAL C O     
4952 C CB    . VAL C 110 ? 0.5363 0.6813 0.3499 0.1129  -0.0112 -0.1115 82  VAL C CB    
4953 C CG1   . VAL C 110 ? 0.5409 0.7107 0.3565 0.1161  -0.0220 -0.1126 82  VAL C CG1   
4954 C CG2   . VAL C 110 ? 0.6677 0.7955 0.4649 0.1134  -0.0056 -0.1068 82  VAL C CG2   
4955 N N     . ALA C 111 ? 0.5287 0.6919 0.3779 0.1305  -0.0239 -0.1005 83  ALA C N     
4956 C CA    . ALA C 111 ? 0.5532 0.7325 0.4178 0.1328  -0.0281 -0.1039 83  ALA C CA    
4957 C C     . ALA C 111 ? 0.5419 0.7466 0.4098 0.1366  -0.0380 -0.1048 83  ALA C C     
4958 O O     . ALA C 111 ? 0.5461 0.7522 0.4074 0.1436  -0.0437 -0.0968 83  ALA C O     
4959 C CB    . ALA C 111 ? 0.5042 0.6723 0.3761 0.1419  -0.0290 -0.0952 83  ALA C CB    
4960 N N     . CYS C 112 ? 0.4997 0.7250 0.3779 0.1319  -0.0400 -0.1140 84  CYS C N     
4961 C CA    . CYS C 112 ? 0.4833 0.7353 0.3657 0.1345  -0.0497 -0.1157 84  CYS C CA    
4962 C C     . CYS C 112 ? 0.4838 0.7559 0.3850 0.1374  -0.0530 -0.1191 84  CYS C C     
4963 O O     . CYS C 112 ? 0.5400 0.8127 0.4495 0.1305  -0.0469 -0.1265 84  CYS C O     
4964 C CB    . CYS C 112 ? 0.4941 0.7559 0.3674 0.1234  -0.0500 -0.1252 84  CYS C CB    
4965 S SG    . CYS C 112 ? 0.4942 0.7518 0.3702 0.1075  -0.0401 -0.1390 84  CYS C SG    
4966 N N     . ASP C 113 ? 0.4779 0.7663 0.3859 0.1480  -0.0623 -0.1132 85  ASP C N     
4967 C CA    . ASP C 113 ? 0.4744 0.7867 0.4005 0.1521  -0.0667 -0.1159 85  ASP C CA    
4968 C C     . ASP C 113 ? 0.4824 0.8233 0.4105 0.1523  -0.0767 -0.1181 85  ASP C C     
4969 O O     . ASP C 113 ? 0.4911 0.8311 0.4052 0.1510  -0.0806 -0.1161 85  ASP C O     
4970 C CB    . ASP C 113 ? 0.4953 0.8009 0.4288 0.1663  -0.0690 -0.1064 85  ASP C CB    
4971 C CG    . ASP C 113 ? 0.5059 0.8256 0.4577 0.1689  -0.0676 -0.1108 85  ASP C CG    
4972 O OD1   . ASP C 113 ? 0.5438 0.8520 0.4984 0.1631  -0.0588 -0.1157 85  ASP C OD1   
4973 O OD2   . ASP C 113 ? 0.5052 0.8476 0.4685 0.1770  -0.0750 -0.1090 85  ASP C OD2   
4974 N N     . ILE C 114 ? 0.4804 0.8476 0.4259 0.1540  -0.0808 -0.1221 86  ILE C N     
4975 C CA    . ILE C 114 ? 0.4880 0.8851 0.4376 0.1550  -0.0915 -0.1236 86  ILE C CA    
4976 C C     . ILE C 114 ? 0.4900 0.8946 0.4425 0.1713  -0.1006 -0.1121 86  ILE C C     
4977 O O     . ILE C 114 ? 0.5277 0.9498 0.4763 0.1739  -0.1100 -0.1100 86  ILE C O     
4978 C CB    . ILE C 114 ? 0.4859 0.9111 0.4542 0.1480  -0.0919 -0.1335 86  ILE C CB    
4979 C CG1   . ILE C 114 ? 0.4950 0.9523 0.4668 0.1467  -0.1034 -0.1361 86  ILE C CG1   
4980 C CG2   . ILE C 114 ? 0.4771 0.9080 0.4637 0.1578  -0.0899 -0.1305 86  ILE C CG2   
4981 C CD1   . ILE C 114 ? 0.4938 0.9807 0.4847 0.1381  -0.1043 -0.1459 86  ILE C CD1   
4982 N N     . SER C 115 ? 0.4837 0.8740 0.4415 0.1823  -0.0981 -0.1046 87  SER C N     
4983 C CA    . SER C 115 ? 0.5040 0.8997 0.4655 0.1982  -0.1062 -0.0937 87  SER C CA    
4984 C C     . SER C 115 ? 0.4906 0.8607 0.4349 0.2037  -0.1067 -0.0830 87  SER C C     
4985 O O     . SER C 115 ? 0.4860 0.8286 0.4226 0.2006  -0.0987 -0.0817 87  SER C O     
4986 C CB    . SER C 115 ? 0.5299 0.9247 0.5072 0.2077  -0.1036 -0.0918 87  SER C CB    
4987 O OG    . SER C 115 ? 0.5594 0.9219 0.5293 0.2112  -0.0972 -0.0862 87  SER C OG    
4988 N N     . PRO C 116 ? 0.4996 0.8784 0.4378 0.2116  -0.1157 -0.0751 88  PRO C N     
4989 C CA    . PRO C 116 ? 0.5039 0.8589 0.4272 0.2177  -0.1160 -0.0636 88  PRO C CA    
4990 C C     . PRO C 116 ? 0.5119 0.8441 0.4394 0.2268  -0.1125 -0.0558 88  PRO C C     
4991 O O     . PRO C 116 ? 0.5392 0.8450 0.4558 0.2257  -0.1077 -0.0503 88  PRO C O     
4992 C CB    . PRO C 116 ? 0.5273 0.9013 0.4475 0.2264  -0.1273 -0.0564 88  PRO C CB    
4993 C CG    . PRO C 116 ? 0.5967 0.9997 0.5211 0.2179  -0.1314 -0.0670 88  PRO C CG    
4994 C CD    . PRO C 116 ? 0.5079 0.9178 0.4487 0.2114  -0.1254 -0.0776 88  PRO C CD    
4995 N N     . GLU C 117 ? 0.5026 0.8446 0.4456 0.2358  -0.1148 -0.0552 89  GLU C N     
4996 C CA    . GLU C 117 ? 0.5004 0.8207 0.4466 0.2453  -0.1124 -0.0481 89  GLU C CA    
4997 C C     . GLU C 117 ? 0.5117 0.8055 0.4531 0.2371  -0.1023 -0.0516 89  GLU C C     
4998 O O     . GLU C 117 ? 0.5360 0.8040 0.4703 0.2407  -0.1003 -0.0437 89  GLU C O     
4999 C CB    . GLU C 117 ? 0.5074 0.8440 0.4714 0.2549  -0.1149 -0.0497 89  GLU C CB    
5000 C CG    . GLU C 117 ? 0.5073 0.8741 0.4784 0.2628  -0.1251 -0.0471 89  GLU C CG    
5001 C CD    . GLU C 117 ? 0.5524 0.9502 0.5325 0.2534  -0.1261 -0.0584 89  GLU C CD    
5002 O OE1   . GLU C 117 ? 0.6390 1.0391 0.6278 0.2458  -0.1190 -0.0680 89  GLU C OE1   
5003 O OE2   . GLU C 117 ? 0.5115 0.9312 0.4898 0.2534  -0.1343 -0.0575 89  GLU C OE2   
5004 N N     . MET C 118 ? 0.5201 0.8200 0.4655 0.2259  -0.0959 -0.0631 90  MET C N     
5005 C CA    . MET C 118 ? 0.4830 0.7585 0.4225 0.2174  -0.0863 -0.0663 90  MET C CA    
5006 C C     . MET C 118 ? 0.4752 0.7345 0.3982 0.2110  -0.0843 -0.0625 90  MET C C     
5007 O O     . MET C 118 ? 0.5077 0.7414 0.4236 0.2117  -0.0806 -0.0564 90  MET C O     
5008 C CB    . MET C 118 ? 0.4670 0.7537 0.4145 0.2068  -0.0799 -0.0791 90  MET C CB    
5009 C CG    . MET C 118 ? 0.5197 0.8217 0.4841 0.2128  -0.0800 -0.0830 90  MET C CG    
5010 S SD    . MET C 118 ? 0.4593 0.7349 0.4256 0.2154  -0.0714 -0.0830 90  MET C SD    
5011 C CE    . MET C 118 ? 0.5820 0.8762 0.5658 0.2292  -0.0751 -0.0826 90  MET C CE    
5012 N N     . VAL C 119 ? 0.4800 0.7541 0.3966 0.2049  -0.0869 -0.0660 91  VAL C N     
5013 C CA    . VAL C 119 ? 0.4841 0.7444 0.3842 0.1997  -0.0848 -0.0625 91  VAL C CA    
5014 C C     . VAL C 119 ? 0.4887 0.7344 0.3819 0.2097  -0.0886 -0.0484 91  VAL C C     
5015 O O     . VAL C 119 ? 0.4898 0.7163 0.3714 0.2069  -0.0845 -0.0432 91  VAL C O     
5016 C CB    . VAL C 119 ? 0.4915 0.7723 0.3853 0.1929  -0.0882 -0.0688 91  VAL C CB    
5017 C CG1   . VAL C 119 ? 0.4981 0.7647 0.3734 0.1888  -0.0857 -0.0650 91  VAL C CG1   
5018 C CG2   . VAL C 119 ? 0.4877 0.7805 0.3884 0.1813  -0.0838 -0.0828 91  VAL C CG2   
5019 N N     . ASP C 120 ? 0.4922 0.7459 0.3926 0.2215  -0.0960 -0.0416 92  ASP C N     
5020 C CA    . ASP C 120 ? 0.4974 0.7357 0.3926 0.2311  -0.0995 -0.0279 92  ASP C CA    
5021 C C     . ASP C 120 ? 0.4921 0.7058 0.3913 0.2342  -0.0953 -0.0239 92  ASP C C     
5022 O O     . ASP C 120 ? 0.4944 0.6875 0.3862 0.2361  -0.0945 -0.0142 92  ASP C O     
5023 C CB    . ASP C 120 ? 0.5200 0.7760 0.4203 0.2430  -0.1094 -0.0217 92  ASP C CB    
5024 C CG    . ASP C 120 ? 0.5714 0.8484 0.4640 0.2411  -0.1149 -0.0224 92  ASP C CG    
5025 O OD1   . ASP C 120 ? 0.6048 0.8774 0.4852 0.2318  -0.1109 -0.0255 92  ASP C OD1   
5026 O OD2   . ASP C 120 ? 0.5204 0.8177 0.4184 0.2492  -0.1233 -0.0200 92  ASP C OD2   
5027 N N     . PHE C 121 ? 0.4861 0.7019 0.3966 0.2344  -0.0928 -0.0311 93  PHE C N     
5028 C CA    . PHE C 121 ? 0.4825 0.6746 0.3953 0.2366  -0.0888 -0.0285 93  PHE C CA    
5029 C C     . PHE C 121 ? 0.5059 0.6773 0.4099 0.2266  -0.0812 -0.0292 93  PHE C C     
5030 O O     . PHE C 121 ? 0.5926 0.7410 0.4931 0.2284  -0.0799 -0.0219 93  PHE C O     
5031 C CB    . PHE C 121 ? 0.4782 0.6783 0.4036 0.2383  -0.0867 -0.0372 93  PHE C CB    
5032 C CG    . PHE C 121 ? 0.4816 0.6592 0.4092 0.2439  -0.0848 -0.0339 93  PHE C CG    
5033 C CD1   . PHE C 121 ? 0.5085 0.6660 0.4323 0.2365  -0.0776 -0.0370 93  PHE C CD1   
5034 C CD2   . PHE C 121 ? 0.5595 0.7357 0.4925 0.2567  -0.0905 -0.0279 93  PHE C CD2   
5035 C CE1   . PHE C 121 ? 0.5587 0.6952 0.4831 0.2412  -0.0765 -0.0344 93  PHE C CE1   
5036 C CE2   . PHE C 121 ? 0.6310 0.7849 0.5645 0.2615  -0.0889 -0.0256 93  PHE C CE2   
5037 C CZ    . PHE C 121 ? 0.5904 0.7246 0.5193 0.2535  -0.0822 -0.0291 93  PHE C CZ    
5038 N N     . CYS C 122 ? 0.5181 0.6972 0.4187 0.2159  -0.0762 -0.0378 94  CYS C N     
5039 C CA    . CYS C 122 ? 0.5053 0.6657 0.3978 0.2067  -0.0684 -0.0388 94  CYS C CA    
5040 C C     . CYS C 122 ? 0.5256 0.6726 0.4074 0.2081  -0.0693 -0.0277 94  CYS C C     
5041 O O     . CYS C 122 ? 0.5962 0.7218 0.4754 0.2079  -0.0665 -0.0213 94  CYS C O     
5042 C CB    . CYS C 122 ? 0.5071 0.6790 0.3974 0.1956  -0.0631 -0.0503 94  CYS C CB    
5043 S SG    . CYS C 122 ? 0.5694 0.7611 0.4730 0.1924  -0.0616 -0.0635 94  CYS C SG    
5044 N N     . ARG C 123 ? 0.4804 0.6407 0.3560 0.2093  -0.0733 -0.0250 95  ARG C N     
5045 C CA    . ARG C 123 ? 0.4858 0.6356 0.3504 0.2102  -0.0732 -0.0146 95  ARG C CA    
5046 C C     . ARG C 123 ? 0.5048 0.6385 0.3711 0.2185  -0.0767 -0.0016 95  ARG C C     
5047 O O     . ARG C 123 ? 0.5306 0.6512 0.3897 0.2181  -0.0750 0.0077  95  ARG C O     
5048 C CB    . ARG C 123 ? 0.4948 0.6635 0.3522 0.2117  -0.0780 -0.0141 95  ARG C CB    
5049 C CG    . ARG C 123 ? 0.4948 0.6799 0.3499 0.2029  -0.0756 -0.0273 95  ARG C CG    
5050 C CD    . ARG C 123 ? 0.5055 0.7096 0.3527 0.2047  -0.0817 -0.0268 95  ARG C CD    
5051 N NE    . ARG C 123 ? 0.5278 0.7334 0.3628 0.1952  -0.0767 -0.0339 95  ARG C NE    
5052 C CZ    . ARG C 123 ? 0.5193 0.7434 0.3474 0.1928  -0.0809 -0.0392 95  ARG C CZ    
5053 N NH1   . ARG C 123 ? 0.5242 0.7689 0.3571 0.1993  -0.0905 -0.0378 95  ARG C NH1   
5054 N NH2   . ARG C 123 ? 0.5582 0.7799 0.3739 0.1838  -0.0755 -0.0461 95  ARG C NH2   
5055 N N     . GLN C 124 ? 0.5148 0.6490 0.3905 0.2259  -0.0814 -0.0007 96  GLN C N     
5056 C CA    . GLN C 124 ? 0.5869 0.7037 0.4643 0.2333  -0.0850 0.0108  96  GLN C CA    
5057 C C     . GLN C 124 ? 0.6337 0.7291 0.5142 0.2297  -0.0803 0.0096  96  GLN C C     
5058 O O     . GLN C 124 ? 0.6749 0.7522 0.5513 0.2274  -0.0783 0.0175  96  GLN C O     
5059 C CB    . GLN C 124 ? 0.6081 0.7351 0.4928 0.2443  -0.0927 0.0129  96  GLN C CB    
5060 C CG    . GLN C 124 ? 0.6622 0.7698 0.5488 0.2523  -0.0965 0.0237  96  GLN C CG    
5061 C CD    . GLN C 124 ? 0.8362 0.9540 0.7270 0.2643  -0.1045 0.0287  96  GLN C CD    
5062 O OE1   . GLN C 124 ? 1.0207 1.1310 0.9078 0.2704  -0.1090 0.0407  96  GLN C OE1   
5063 N NE2   . GLN C 124 ? 0.8093 0.9449 0.7085 0.2678  -0.1062 0.0198  96  GLN C NE2   
5064 N N     . HIS C 125 ? 0.5842 0.6823 0.4720 0.2291  -0.0786 -0.0001 97  HIS C N     
5065 C CA    . HIS C 125 ? 0.5378 0.6159 0.4277 0.2267  -0.0750 -0.0016 97  HIS C CA    
5066 C C     . HIS C 125 ? 0.5912 0.6630 0.4770 0.2157  -0.0669 -0.0071 97  HIS C C     
5067 O O     . HIS C 125 ? 0.7379 0.7942 0.6186 0.2121  -0.0646 -0.0002 97  HIS C O     
5068 C CB    . HIS C 125 ? 0.5523 0.6352 0.4507 0.2316  -0.0760 -0.0092 97  HIS C CB    
5069 C CG    . HIS C 125 ? 0.6048 0.6951 0.5079 0.2433  -0.0835 -0.0044 97  HIS C CG    
5070 N ND1   . HIS C 125 ? 0.6525 0.7672 0.5589 0.2473  -0.0875 -0.0061 97  HIS C ND1   
5071 C CD2   . HIS C 125 ? 0.6221 0.6979 0.5270 0.2520  -0.0881 0.0024  97  HIS C CD2   
5072 C CE1   . HIS C 125 ? 0.6504 0.7660 0.5608 0.2587  -0.0938 -0.0003 97  HIS C CE1   
5073 N NE2   . HIS C 125 ? 0.6057 0.6971 0.5150 0.2617  -0.0941 0.0048  97  HIS C NE2   
5074 N N     . ASN C 126 ? 0.5318 0.6154 0.4201 0.2102  -0.0623 -0.0190 98  ASN C N     
5075 C CA    . ASN C 126 ? 0.5479 0.6241 0.4323 0.2001  -0.0542 -0.0245 98  ASN C CA    
5076 C C     . ASN C 126 ? 0.5834 0.6643 0.4597 0.1945  -0.0513 -0.0233 98  ASN C C     
5077 O O     . ASN C 126 ? 0.5994 0.6864 0.4733 0.1868  -0.0455 -0.0320 98  ASN C O     
5078 C CB    . ASN C 126 ? 0.5185 0.6049 0.4082 0.1958  -0.0499 -0.0374 98  ASN C CB    
5079 C CG    . ASN C 126 ? 0.6518 0.7380 0.5495 0.2027  -0.0526 -0.0396 98  ASN C CG    
5080 O OD1   . ASN C 126 ? 0.7407 0.8365 0.6430 0.2114  -0.0590 -0.0367 98  ASN C OD1   
5081 N ND2   . ASN C 126 ? 0.6474 0.7221 0.5460 0.1994  -0.0475 -0.0445 98  ASN C ND2   
5082 N N     . ALA C 127 ? 0.5780 0.6552 0.4495 0.1983  -0.0547 -0.0125 99  ALA C N     
5083 C CA    . ALA C 127 ? 0.5646 0.6453 0.4271 0.1942  -0.0516 -0.0104 99  ALA C CA    
5084 C C     . ALA C 127 ? 0.6196 0.6816 0.4779 0.1887  -0.0449 -0.0064 99  ALA C C     
5085 O O     . ALA C 127 ? 0.6254 0.6725 0.4852 0.1914  -0.0465 0.0035  99  ALA C O     
5086 C CB    . ALA C 127 ? 0.6304 0.7168 0.4893 0.2012  -0.0578 -0.0001 99  ALA C CB    
5087 N N     . LEU C 128 ? 0.6584 0.7213 0.5117 0.1809  -0.0376 -0.0138 100 LEU C N     
5088 C CA    . LEU C 128 ? 0.6864 0.7333 0.5357 0.1759  -0.0305 -0.0104 100 LEU C CA    
5089 C C     . LEU C 128 ? 0.6922 0.7430 0.5316 0.1737  -0.0264 -0.0086 100 LEU C C     
5090 O O     . LEU C 128 ? 0.7148 0.7730 0.5489 0.1682  -0.0220 -0.0185 100 LEU C O     
5091 C CB    . LEU C 128 ? 0.7329 0.7743 0.5842 0.1691  -0.0242 -0.0203 100 LEU C CB    
5092 C CG    . LEU C 128 ? 0.7201 0.7465 0.5669 0.1634  -0.0160 -0.0188 100 LEU C CG    
5093 C CD1   . LEU C 128 ? 0.7087 0.7215 0.5563 0.1668  -0.0174 -0.0051 100 LEU C CD1   
5094 C CD2   . LEU C 128 ? 0.7292 0.7488 0.5792 0.1584  -0.0115 -0.0270 100 LEU C CD2   
5095 N N     . PRO C 129 ? 0.7154 0.7611 0.5515 0.1776  -0.0275 0.0035  101 PRO C N     
5096 C CA    . PRO C 129 ? 0.6838 0.7336 0.5092 0.1765  -0.0234 0.0055  101 PRO C CA    
5097 C C     . PRO C 129 ? 0.6727 0.7125 0.4931 0.1700  -0.0134 0.0019  101 PRO C C     
5098 O O     . PRO C 129 ? 0.7170 0.7443 0.5424 0.1673  -0.0099 0.0023  101 PRO C O     
5099 C CB    . PRO C 129 ? 0.5496 0.5946 0.3748 0.1826  -0.0267 0.0209  101 PRO C CB    
5100 C CG    . PRO C 129 ? 0.6410 0.6832 0.4763 0.1875  -0.0347 0.0252  101 PRO C CG    
5101 C CD    . PRO C 129 ? 0.7001 0.7369 0.5418 0.1834  -0.0330 0.0159  101 PRO C CD    
5102 N N     . GLY C 130 ? 0.6000 0.6449 0.4093 0.1678  -0.0087 -0.0015 102 GLY C N     
5103 C CA    . GLY C 130 ? 0.5946 0.6302 0.3973 0.1624  0.0014  -0.0054 102 GLY C CA    
5104 C C     . GLY C 130 ? 0.6412 0.6747 0.4458 0.1553  0.0054  -0.0185 102 GLY C C     
5105 O O     . GLY C 130 ? 0.7642 0.7882 0.5633 0.1508  0.0140  -0.0220 102 GLY C O     
5106 N N     . THR C 131 ? 0.5729 0.6146 0.3849 0.1546  -0.0002 -0.0255 103 THR C N     
5107 C CA    . THR C 131 ? 0.5849 0.6253 0.3996 0.1477  0.0038  -0.0374 103 THR C CA    
5108 C C     . THR C 131 ? 0.6364 0.6949 0.4534 0.1459  -0.0014 -0.0478 103 THR C C     
5109 O O     . THR C 131 ? 0.6782 0.7432 0.4885 0.1401  0.0016  -0.0576 103 THR C O     
5110 C CB    . THR C 131 ? 0.6682 0.6973 0.4926 0.1482  0.0037  -0.0343 103 THR C CB    
5111 O OG1   . THR C 131 ? 0.7013 0.7157 0.5251 0.1504  0.0067  -0.0232 103 THR C OG1   
5112 C CG2   . THR C 131 ? 0.6894 0.7146 0.5148 0.1408  0.0097  -0.0454 103 THR C CG2   
5113 N N     . ILE C 132 ? 0.6356 0.7021 0.4621 0.1510  -0.0092 -0.0457 104 ILE C N     
5114 C CA    . ILE C 132 ? 0.6304 0.7155 0.4621 0.1501  -0.0144 -0.0548 104 ILE C CA    
5115 C C     . ILE C 132 ? 0.5917 0.6922 0.4192 0.1550  -0.0215 -0.0518 104 ILE C C     
5116 O O     . ILE C 132 ? 0.5811 0.6795 0.4087 0.1626  -0.0263 -0.0407 104 ILE C O     
5117 C CB    . ILE C 132 ? 0.5975 0.6831 0.4416 0.1538  -0.0184 -0.0546 104 ILE C CB    
5118 C CG1   . ILE C 132 ? 0.6261 0.6927 0.4723 0.1509  -0.0121 -0.0535 104 ILE C CG1   
5119 C CG2   . ILE C 132 ? 0.5692 0.6735 0.4201 0.1511  -0.0208 -0.0658 104 ILE C CG2   
5120 C CD1   . ILE C 132 ? 0.6185 0.6844 0.4747 0.1535  -0.0147 -0.0552 104 ILE C CD1   
5121 N N     . THR C 133 ? 0.5875 0.7031 0.4111 0.1503  -0.0225 -0.0616 105 THR C N     
5122 C CA    . THR C 133 ? 0.5500 0.6832 0.3695 0.1542  -0.0301 -0.0605 105 THR C CA    
5123 C C     . THR C 133 ? 0.5433 0.6970 0.3735 0.1537  -0.0363 -0.0687 105 THR C C     
5124 O O     . THR C 133 ? 0.5523 0.7112 0.3854 0.1454  -0.0329 -0.0802 105 THR C O     
5125 C CB    . THR C 133 ? 0.6173 0.7516 0.4213 0.1490  -0.0266 -0.0649 105 THR C CB    
5126 O OG1   . THR C 133 ? 0.7574 0.8991 0.5610 0.1393  -0.0238 -0.0791 105 THR C OG1   
5127 C CG2   . THR C 133 ? 0.6060 0.7191 0.4010 0.1483  -0.0178 -0.0588 105 THR C CG2   
5128 N N     . TYR C 134 ? 0.5171 0.6823 0.3536 0.1626  -0.0452 -0.0625 106 TYR C N     
5129 C CA    . TYR C 134 ? 0.4866 0.6727 0.3351 0.1642  -0.0515 -0.0686 106 TYR C CA    
5130 C C     . TYR C 134 ? 0.4968 0.7044 0.3399 0.1645  -0.0586 -0.0712 106 TYR C C     
5131 O O     . TYR C 134 ? 0.5318 0.7423 0.3693 0.1722  -0.0644 -0.0620 106 TYR C O     
5132 C CB    . TYR C 134 ? 0.4808 0.6653 0.3404 0.1746  -0.0566 -0.0603 106 TYR C CB    
5133 C CG    . TYR C 134 ? 0.4722 0.6360 0.3366 0.1744  -0.0507 -0.0581 106 TYR C CG    
5134 C CD1   . TYR C 134 ? 0.4739 0.6378 0.3462 0.1689  -0.0460 -0.0673 106 TYR C CD1   
5135 C CD2   . TYR C 134 ? 0.5485 0.6929 0.4093 0.1794  -0.0502 -0.0466 106 TYR C CD2   
5136 C CE1   . TYR C 134 ? 0.5212 0.6661 0.3964 0.1689  -0.0411 -0.0652 106 TYR C CE1   
5137 C CE2   . TYR C 134 ? 0.5307 0.6566 0.3954 0.1788  -0.0458 -0.0447 106 TYR C CE2   
5138 C CZ    . TYR C 134 ? 0.5465 0.6725 0.4177 0.1738  -0.0414 -0.0541 106 TYR C CZ    
5139 O OH    . TYR C 134 ? 0.6966 0.8041 0.5702 0.1734  -0.0373 -0.0522 106 TYR C OH    
5140 N N     . GLU C 135 ? 0.4997 0.7221 0.3441 0.1558  -0.0583 -0.0835 107 GLU C N     
5141 C CA    . GLU C 135 ? 0.5101 0.7550 0.3502 0.1546  -0.0658 -0.0877 107 GLU C CA    
5142 C C     . GLU C 135 ? 0.5064 0.7755 0.3629 0.1540  -0.0714 -0.0949 107 GLU C C     
5143 O O     . GLU C 135 ? 0.4963 0.7639 0.3665 0.1549  -0.0687 -0.0965 107 GLU C O     
5144 C CB    . GLU C 135 ? 0.5205 0.7619 0.3455 0.1437  -0.0610 -0.0964 107 GLU C CB    
5145 C CG    . GLU C 135 ? 0.5293 0.7554 0.3361 0.1465  -0.0584 -0.0886 107 GLU C CG    
5146 C CD    . GLU C 135 ? 0.6598 0.8591 0.4615 0.1434  -0.0472 -0.0865 107 GLU C CD    
5147 O OE1   . GLU C 135 ? 0.7746 0.9631 0.5870 0.1463  -0.0443 -0.0822 107 GLU C OE1   
5148 O OE2   . GLU C 135 ? 0.7139 0.9028 0.5004 0.1382  -0.0413 -0.0893 107 GLU C OE2   
5149 N N     . LEU C 136 ? 0.5155 0.8079 0.3705 0.1527  -0.0793 -0.0990 108 LEU C N     
5150 C CA    . LEU C 136 ? 0.5135 0.8331 0.3846 0.1522  -0.0856 -0.1054 108 LEU C CA    
5151 C C     . LEU C 136 ? 0.5195 0.8506 0.3887 0.1378  -0.0839 -0.1194 108 LEU C C     
5152 O O     . LEU C 136 ? 0.5314 0.8601 0.3843 0.1316  -0.0842 -0.1229 108 LEU C O     
5153 C CB    . LEU C 136 ? 0.5199 0.8601 0.3929 0.1629  -0.0976 -0.0981 108 LEU C CB    
5154 C CG    . LEU C 136 ? 0.5221 0.8960 0.4091 0.1629  -0.1066 -0.1038 108 LEU C CG    
5155 C CD1   . LEU C 136 ? 0.5229 0.9087 0.4171 0.1783  -0.1159 -0.0926 108 LEU C CD1   
5156 C CD2   . LEU C 136 ? 0.5355 0.9255 0.4119 0.1533  -0.1115 -0.1122 108 LEU C CD2   
5157 N N     . LEU C 137 ? 0.5126 0.8555 0.3980 0.1322  -0.0819 -0.1275 109 LEU C N     
5158 C CA    . LEU C 137 ? 0.5184 0.8713 0.4039 0.1173  -0.0798 -0.1409 109 LEU C CA    
5159 C C     . LEU C 137 ? 0.5109 0.8862 0.4189 0.1148  -0.0810 -0.1470 109 LEU C C     
5160 O O     . LEU C 137 ? 0.4995 0.8696 0.4198 0.1207  -0.0769 -0.1434 109 LEU C O     
5161 C CB    . LEU C 137 ? 0.5190 0.8443 0.3930 0.1073  -0.0678 -0.1459 109 LEU C CB    
5162 C CG    . LEU C 137 ? 0.5264 0.8574 0.3996 0.0910  -0.0642 -0.1600 109 LEU C CG    
5163 C CD1   . LEU C 137 ? 0.5433 0.8847 0.4019 0.0853  -0.0709 -0.1651 109 LEU C CD1   
5164 C CD2   . LEU C 137 ? 0.5247 0.8271 0.3904 0.0832  -0.0512 -0.1635 109 LEU C CD2   
5165 N N     . ASP C 138 ? 0.5185 0.9188 0.4313 0.1060  -0.0866 -0.1561 110 ASP C N     
5166 C CA    . ASP C 138 ? 0.5133 0.9360 0.4472 0.1002  -0.0864 -0.1636 110 ASP C CA    
5167 C C     . ASP C 138 ? 0.5170 0.9295 0.4469 0.0830  -0.0774 -0.1753 110 ASP C C     
5168 O O     . ASP C 138 ? 0.5299 0.9400 0.4454 0.0729  -0.0787 -0.1819 110 ASP C O     
5169 C CB    . ASP C 138 ? 0.5197 0.9792 0.4638 0.1011  -0.0992 -0.1656 110 ASP C CB    
5170 C CG    . ASP C 138 ? 0.5134 0.9995 0.4825 0.0970  -0.0994 -0.1717 110 ASP C CG    
5171 O OD1   . ASP C 138 ? 0.5053 0.9808 0.4824 0.0921  -0.0891 -0.1753 110 ASP C OD1   
5172 O OD2   . ASP C 138 ? 0.5172 1.0356 0.4981 0.0990  -0.1099 -0.1724 110 ASP C OD2   
5173 N N     . VAL C 139 ? 0.5073 0.9126 0.4489 0.0798  -0.0682 -0.1778 111 VAL C N     
5174 C CA    . VAL C 139 ? 0.5109 0.9015 0.4478 0.0645  -0.0581 -0.1874 111 VAL C CA    
5175 C C     . VAL C 139 ? 0.5218 0.9353 0.4633 0.0498  -0.0623 -0.1991 111 VAL C C     
5176 O O     . VAL C 139 ? 0.5306 0.9309 0.4624 0.0359  -0.0561 -0.2077 111 VAL C O     
5177 C CB    . VAL C 139 ? 0.4989 0.8795 0.4482 0.0650  -0.0479 -0.1868 111 VAL C CB    
5178 C CG1   . VAL C 139 ? 0.5019 0.9137 0.4756 0.0648  -0.0508 -0.1901 111 VAL C CG1   
5179 C CG2   . VAL C 139 ? 0.5030 0.8592 0.4426 0.0518  -0.0362 -0.1937 111 VAL C CG2   
5180 N N     . VAL C 140 ? 0.5223 0.9700 0.4786 0.0525  -0.0730 -0.1996 112 VAL C N     
5181 C CA    . VAL C 140 ? 0.5336 1.0061 0.4950 0.0385  -0.0790 -0.2103 112 VAL C CA    
5182 C C     . VAL C 140 ? 0.5458 1.0310 0.4949 0.0415  -0.0917 -0.2089 112 VAL C C     
5183 O O     . VAL C 140 ? 0.5504 1.0685 0.5111 0.0399  -0.1025 -0.2116 112 VAL C O     
5184 C CB    . VAL C 140 ? 0.5261 1.0314 0.5160 0.0372  -0.0812 -0.2128 112 VAL C CB    
5185 C CG1   . VAL C 140 ? 0.5200 1.0136 0.5188 0.0280  -0.0681 -0.2179 112 VAL C CG1   
5186 C CG2   . VAL C 140 ? 0.5147 1.0341 0.5180 0.0561  -0.0867 -0.2018 112 VAL C CG2   
5187 N N     . GLU C 141 ? 0.5518 1.0116 0.4774 0.0460  -0.0904 -0.2045 113 GLU C N     
5188 C CA    . GLU C 141 ? 0.5647 1.0336 0.4757 0.0497  -0.1016 -0.2024 113 GLU C CA    
5189 C C     . GLU C 141 ? 0.5831 1.0608 0.4849 0.0328  -0.1055 -0.2153 113 GLU C C     
5190 O O     . GLU C 141 ? 0.5898 1.0463 0.4813 0.0202  -0.0963 -0.2236 113 GLU C O     
5191 C CB    . GLU C 141 ? 0.5666 1.0050 0.4551 0.0588  -0.0977 -0.1939 113 GLU C CB    
5192 C CG    . GLU C 141 ? 0.5617 1.0072 0.4511 0.0768  -0.1055 -0.1805 113 GLU C CG    
5193 C CD    . GLU C 141 ? 0.6741 1.1392 0.5532 0.0785  -0.1185 -0.1801 113 GLU C CD    
5194 O OE1   . GLU C 141 ? 0.6571 1.1263 0.5248 0.0656  -0.1209 -0.1904 113 GLU C OE1   
5195 O OE2   . GLU C 141 ? 0.8495 1.3252 0.7311 0.0928  -0.1263 -0.1694 113 GLU C OE2   
5196 N N     . PRO C 142 ? 0.5928 1.1009 0.4978 0.0318  -0.1190 -0.2175 114 PRO C N     
5197 C CA    . PRO C 142 ? 0.6129 1.1282 0.5068 0.0150  -0.1237 -0.2303 114 PRO C CA    
5198 C C     . PRO C 142 ? 0.6288 1.1127 0.4910 0.0112  -0.1191 -0.2331 114 PRO C C     
5199 O O     . PRO C 142 ? 0.6424 1.1140 0.4939 -0.0045 -0.1144 -0.2447 114 PRO C O     
5200 C CB    . PRO C 142 ? 0.6195 1.1725 0.5210 0.0192  -0.1404 -0.2286 114 PRO C CB    
5201 C CG    . PRO C 142 ? 0.6000 1.1717 0.5268 0.0337  -0.1424 -0.2184 114 PRO C CG    
5202 C CD    . PRO C 142 ? 0.5865 1.1254 0.5075 0.0450  -0.1307 -0.2091 114 PRO C CD    
5203 N N     . ARG C 143 ? 0.6285 1.0985 0.4754 0.0253  -0.1199 -0.2224 115 ARG C N     
5204 C CA    . ARG C 143 ? 0.6438 1.0851 0.4605 0.0242  -0.1153 -0.2233 115 ARG C CA    
5205 C C     . ARG C 143 ? 0.6304 1.0396 0.4426 0.0335  -0.1025 -0.2141 115 ARG C C     
5206 O O     . ARG C 143 ? 0.6258 1.0277 0.4314 0.0478  -0.1036 -0.2021 115 ARG C O     
5207 C CB    . ARG C 143 ? 0.6574 1.1109 0.4586 0.0321  -0.1272 -0.2184 115 ARG C CB    
5208 C CG    . ARG C 143 ? 0.6632 1.1566 0.4774 0.0294  -0.1427 -0.2219 115 ARG C CG    
5209 C CD    . ARG C 143 ? 0.6814 1.1823 0.4745 0.0353  -0.1537 -0.2184 115 ARG C CD    
5210 N NE    . ARG C 143 ? 0.7015 1.1752 0.4642 0.0275  -0.1478 -0.2254 115 ARG C NE    
5211 C CZ    . ARG C 143 ? 0.7227 1.1990 0.4729 0.0116  -0.1510 -0.2395 115 ARG C CZ    
5212 N NH1   . ARG C 143 ? 0.7266 1.2330 0.4926 0.0009  -0.1608 -0.2483 115 ARG C NH1   
5213 N NH2   . ARG C 143 ? 0.7412 1.1891 0.4627 0.0062  -0.1441 -0.2451 115 ARG C NH2   
5214 N N     . LEU C 144 ? 0.6251 1.0150 0.4410 0.0248  -0.0904 -0.2197 116 LEU C N     
5215 C CA    . LEU C 144 ? 0.6132 0.9727 0.4253 0.0323  -0.0783 -0.2116 116 LEU C CA    
5216 C C     . LEU C 144 ? 0.6261 0.9601 0.4106 0.0359  -0.0742 -0.2085 116 LEU C C     
5217 O O     . LEU C 144 ? 0.6174 0.9356 0.3977 0.0481  -0.0702 -0.1968 116 LEU C O     
5218 C CB    . LEU C 144 ? 0.6078 0.9527 0.4281 0.0212  -0.0665 -0.2190 116 LEU C CB    
5219 C CG    . LEU C 144 ? 0.5892 0.9142 0.4186 0.0281  -0.0557 -0.2112 116 LEU C CG    
5220 C CD1   . LEU C 144 ? 0.5894 0.9026 0.4243 0.0146  -0.0453 -0.2205 116 LEU C CD1   
5221 C CD2   . LEU C 144 ? 0.5883 0.8848 0.4006 0.0381  -0.0496 -0.2016 116 LEU C CD2   
5222 N N     . GLU C 145 ? 0.6481 0.9781 0.4136 0.0252  -0.0753 -0.2188 117 GLU C N     
5223 C CA    . GLU C 145 ? 0.6628 0.9666 0.4009 0.0274  -0.0694 -0.2174 117 GLU C CA    
5224 C C     . GLU C 145 ? 0.6650 0.9739 0.3927 0.0419  -0.0764 -0.2055 117 GLU C C     
5225 O O     . GLU C 145 ? 0.6730 0.9597 0.3808 0.0470  -0.0702 -0.2008 117 GLU C O     
5226 C CB    . GLU C 145 ? 0.6886 0.9879 0.4081 0.0123  -0.0697 -0.2323 117 GLU C CB    
5227 C CG    . GLU C 145 ? 0.6919 0.9690 0.4107 -0.0005 -0.0574 -0.2421 117 GLU C CG    
5228 C CD    . GLU C 145 ? 0.7126 1.0095 0.4536 -0.0128 -0.0604 -0.2511 117 GLU C CD    
5229 O OE1   . GLU C 145 ? 0.7540 1.0808 0.5026 -0.0169 -0.0729 -0.2555 117 GLU C OE1   
5230 O OE2   . GLU C 145 ? 0.6774 0.9607 0.4286 -0.0183 -0.0502 -0.2533 117 GLU C OE2   
5231 N N     . ASP C 146 ? 0.6589 0.9965 0.3996 0.0488  -0.0887 -0.2003 118 ASP C N     
5232 C CA    . ASP C 146 ? 0.6614 1.0051 0.3934 0.0628  -0.0959 -0.1882 118 ASP C CA    
5233 C C     . ASP C 146 ? 0.6399 0.9787 0.3861 0.0775  -0.0934 -0.1732 118 ASP C C     
5234 O O     . ASP C 146 ? 0.6395 0.9869 0.3839 0.0897  -0.1005 -0.1621 118 ASP C O     
5235 C CB    . ASP C 146 ? 0.6705 1.0482 0.4062 0.0626  -0.1117 -0.1906 118 ASP C CB    
5236 C CG    . ASP C 146 ? 0.6956 1.0776 0.4132 0.0488  -0.1158 -0.2047 118 ASP C CG    
5237 O OD1   . ASP C 146 ? 0.6995 1.0747 0.4190 0.0345  -0.1103 -0.2172 118 ASP C OD1   
5238 O OD2   . ASP C 146 ? 0.7127 1.1043 0.4135 0.0521  -0.1248 -0.2034 118 ASP C OD2   
5239 N N     . THR C 147 ? 0.6234 0.9479 0.3830 0.0763  -0.0838 -0.1726 119 THR C N     
5240 C CA    . THR C 147 ? 0.6041 0.9220 0.3770 0.0889  -0.0812 -0.1595 119 THR C CA    
5241 C C     . THR C 147 ? 0.6024 0.8882 0.3623 0.0928  -0.0698 -0.1526 119 THR C C     
5242 O O     . THR C 147 ? 0.6122 0.8792 0.3577 0.0845  -0.0612 -0.1595 119 THR C O     
5243 C CB    . THR C 147 ? 0.5868 0.9123 0.3844 0.0861  -0.0790 -0.1625 119 THR C CB    
5244 O OG1   . THR C 147 ? 0.5864 0.8923 0.3819 0.0749  -0.0674 -0.1710 119 THR C OG1   
5245 C CG2   . THR C 147 ? 0.5887 0.9477 0.4010 0.0816  -0.0896 -0.1695 119 THR C CG2   
5246 N N     . VAL C 148 ? 0.5907 0.8703 0.3561 0.1057  -0.0698 -0.1387 120 VAL C N     
5247 C CA    . VAL C 148 ? 0.5875 0.8390 0.3437 0.1101  -0.0597 -0.1306 120 VAL C CA    
5248 C C     . VAL C 148 ? 0.5776 0.8113 0.3412 0.1030  -0.0486 -0.1357 120 VAL C C     
5249 O O     . VAL C 148 ? 0.5820 0.7927 0.3335 0.1001  -0.0387 -0.1361 120 VAL C O     
5250 C CB    . VAL C 148 ? 0.5774 0.8279 0.3400 0.1246  -0.0632 -0.1146 120 VAL C CB    
5251 C CG1   . VAL C 148 ? 0.5704 0.7935 0.3295 0.1282  -0.0528 -0.1063 120 VAL C CG1   
5252 C CG2   . VAL C 148 ? 0.5905 0.8530 0.3408 0.1319  -0.0720 -0.1081 120 VAL C CG2   
5253 N N     . VAL C 149 ? 0.5650 0.8094 0.3483 0.1005  -0.0500 -0.1396 121 VAL C N     
5254 C CA    . VAL C 149 ? 0.5557 0.7842 0.3466 0.0942  -0.0398 -0.1438 121 VAL C CA    
5255 C C     . VAL C 149 ? 0.5691 0.7867 0.3473 0.0809  -0.0326 -0.1560 121 VAL C C     
5256 O O     . VAL C 149 ? 0.5679 0.7622 0.3413 0.0775  -0.0218 -0.1566 121 VAL C O     
5257 C CB    . VAL C 149 ? 0.5425 0.7876 0.3560 0.0936  -0.0430 -0.1465 121 VAL C CB    
5258 C CG1   . VAL C 149 ? 0.5360 0.7664 0.3557 0.0853  -0.0326 -0.1526 121 VAL C CG1   
5259 C CG2   . VAL C 149 ? 0.5301 0.7794 0.3548 0.1075  -0.0481 -0.1340 121 VAL C CG2   
5260 N N     . TRP C 150 ? 0.5833 0.8170 0.3555 0.0731  -0.0386 -0.1658 122 TRP C N     
5261 C CA    . TRP C 150 ? 0.5985 0.8216 0.3582 0.0596  -0.0323 -0.1785 122 TRP C CA    
5262 C C     . TRP C 150 ? 0.6102 0.8068 0.3477 0.0612  -0.0239 -0.1759 122 TRP C C     
5263 O O     . TRP C 150 ? 0.6388 0.8163 0.3678 0.0526  -0.0142 -0.1832 122 TRP C O     
5264 C CB    . TRP C 150 ? 0.6134 0.8597 0.3697 0.0513  -0.0419 -0.1890 122 TRP C CB    
5265 C CG    . TRP C 150 ? 0.6342 0.8673 0.3724 0.0383  -0.0367 -0.2016 122 TRP C CG    
5266 C CD1   . TRP C 150 ? 0.6549 0.8807 0.3692 0.0374  -0.0375 -0.2043 122 TRP C CD1   
5267 C CD2   . TRP C 150 ? 0.6380 0.8622 0.3796 0.0244  -0.0293 -0.2131 122 TRP C CD2   
5268 N NE1   . TRP C 150 ? 0.6720 0.8841 0.3742 0.0239  -0.0313 -0.2173 122 TRP C NE1   
5269 C CE2   . TRP C 150 ? 0.6620 0.8727 0.3809 0.0155  -0.0262 -0.2227 122 TRP C CE2   
5270 C CE3   . TRP C 150 ? 0.6249 0.8505 0.3857 0.0187  -0.0246 -0.2161 122 TRP C CE3   
5271 C CZ2   . TRP C 150 ? 0.6999 0.8978 0.4153 0.0009  -0.0189 -0.2351 122 TRP C CZ2   
5272 C CZ3   . TRP C 150 ? 0.6355 0.8494 0.3931 0.0042  -0.0172 -0.2278 122 TRP C CZ3   
5273 C CH2   . TRP C 150 ? 0.6885 0.8883 0.4238 -0.0047 -0.0145 -0.2372 122 TRP C CH2   
5274 N N     . ARG C 151 ? 0.6120 0.8070 0.3401 0.0723  -0.0268 -0.1652 123 ARG C N     
5275 C CA    . ARG C 151 ? 0.6255 0.7989 0.3318 0.0743  -0.0193 -0.1627 123 ARG C CA    
5276 C C     . ARG C 151 ? 0.6694 0.8217 0.3782 0.0828  -0.0105 -0.1505 123 ARG C C     
5277 O O     . ARG C 151 ? 0.7195 0.8529 0.4122 0.0849  -0.0026 -0.1476 123 ARG C O     
5278 C CB    . ARG C 151 ? 0.6397 0.8247 0.3310 0.0799  -0.0275 -0.1593 123 ARG C CB    
5279 C CG    . ARG C 151 ? 0.6540 0.8590 0.3415 0.0704  -0.0363 -0.1721 123 ARG C CG    
5280 C CD    . ARG C 151 ? 0.6722 0.8861 0.3407 0.0745  -0.0436 -0.1705 123 ARG C CD    
5281 N NE    . ARG C 151 ? 0.6847 0.9212 0.3522 0.0655  -0.0541 -0.1822 123 ARG C NE    
5282 C CZ    . ARG C 151 ? 0.7017 0.9517 0.3543 0.0675  -0.0633 -0.1827 123 ARG C CZ    
5283 N NH1   . ARG C 151 ? 0.7097 0.9516 0.3456 0.0777  -0.0622 -0.1727 123 ARG C NH1   
5284 N NH2   . ARG C 151 ? 0.7119 0.9844 0.3661 0.0588  -0.0737 -0.1932 123 ARG C NH2   
5285 N N     . ASN C 152 ? 0.6659 0.8214 0.3941 0.0879  -0.0117 -0.1433 124 ASN C N     
5286 C CA    . ASN C 152 ? 0.6946 0.8288 0.4272 0.0922  -0.0026 -0.1351 124 ASN C CA    
5287 C C     . ASN C 152 ? 0.6848 0.8040 0.4192 0.0822  0.0072  -0.1441 124 ASN C C     
5288 O O     . ASN C 152 ? 0.7467 0.8461 0.4818 0.0845  0.0158  -0.1385 124 ASN C O     
5289 C CB    . ASN C 152 ? 0.7496 0.8910 0.5009 0.1010  -0.0077 -0.1247 124 ASN C CB    
5290 C CG    . ASN C 152 ? 0.7756 0.9239 0.5240 0.1124  -0.0147 -0.1123 124 ASN C CG    
5291 O OD1   . ASN C 152 ? 0.8440 0.9778 0.5851 0.1186  -0.0101 -0.1024 124 ASN C OD1   
5292 N ND2   . ASN C 152 ? 0.7440 0.9151 0.4989 0.1155  -0.0257 -0.1124 124 ASN C ND2   
5293 N N     . GLY C 153 ? 0.6252 0.7535 0.3603 0.0711  0.0058  -0.1575 125 GLY C N     
5294 C CA    . GLY C 153 ? 0.6282 0.7425 0.3643 0.0607  0.0149  -0.1665 125 GLY C CA    
5295 C C     . GLY C 153 ? 0.6693 0.7639 0.3844 0.0550  0.0234  -0.1729 125 GLY C C     
5296 O O     . GLY C 153 ? 0.7588 0.8481 0.4582 0.0604  0.0237  -0.1688 125 GLY C O     
5297 N N     . PRO C 154 ? 0.6692 0.7516 0.3829 0.0440  0.0311  -0.1829 126 PRO C N     
5298 C CA    . PRO C 154 ? 0.6569 0.7446 0.3875 0.0362  0.0321  -0.1885 126 PRO C CA    
5299 C C     . PRO C 154 ? 0.6483 0.7252 0.3915 0.0430  0.0373  -0.1784 126 PRO C C     
5300 O O     . PRO C 154 ? 0.6624 0.7208 0.3989 0.0500  0.0436  -0.1698 126 PRO C O     
5301 C CB    . PRO C 154 ? 0.6736 0.7458 0.3925 0.0230  0.0402  -0.2014 126 PRO C CB    
5302 C CG    . PRO C 154 ? 0.6878 0.7357 0.3868 0.0278  0.0485  -0.1977 126 PRO C CG    
5303 C CD    . PRO C 154 ? 0.7301 0.7885 0.4238 0.0394  0.0412  -0.1883 126 PRO C CD    
5304 N N     . PHE C 155 ? 0.6449 0.7339 0.4063 0.0411  0.0347  -0.1792 127 PHE C N     
5305 C CA    . PHE C 155 ? 0.6611 0.7429 0.4346 0.0483  0.0375  -0.1696 127 PHE C CA    
5306 C C     . PHE C 155 ? 0.7043 0.7678 0.4792 0.0407  0.0483  -0.1737 127 PHE C C     
5307 O O     . PHE C 155 ? 0.7190 0.7851 0.4948 0.0291  0.0509  -0.1847 127 PHE C O     
5308 C CB    . PHE C 155 ? 0.6703 0.7756 0.4621 0.0526  0.0284  -0.1671 127 PHE C CB    
5309 C CG    . PHE C 155 ? 0.6212 0.7430 0.4129 0.0619  0.0178  -0.1606 127 PHE C CG    
5310 C CD1   . PHE C 155 ? 0.6475 0.7631 0.4400 0.0740  0.0161  -0.1475 127 PHE C CD1   
5311 C CD2   . PHE C 155 ? 0.5689 0.7122 0.3593 0.0584  0.0095  -0.1673 127 PHE C CD2   
5312 C CE1   . PHE C 155 ? 0.6189 0.7485 0.4109 0.0826  0.0067  -0.1410 127 PHE C CE1   
5313 C CE2   . PHE C 155 ? 0.5971 0.7553 0.3866 0.0674  -0.0002 -0.1608 127 PHE C CE2   
5314 C CZ    . PHE C 155 ? 0.6170 0.7678 0.4072 0.0797  -0.0013 -0.1475 127 PHE C CZ    
5315 N N     . GLY C 156 ? 0.6278 0.6729 0.4029 0.0472  0.0544  -0.1644 128 GLY C N     
5316 C CA    . GLY C 156 ? 0.6980 0.7256 0.4747 0.0414  0.0643  -0.1667 128 GLY C CA    
5317 C C     . GLY C 156 ? 0.7551 0.7950 0.5483 0.0381  0.0626  -0.1694 128 GLY C C     
5318 O O     . GLY C 156 ? 0.7720 0.8102 0.5674 0.0276  0.0677  -0.1782 128 GLY C O     
5319 N N     . LYS C 157 ? 0.7500 0.8019 0.5548 0.0470  0.0557  -0.1618 129 LYS C N     
5320 C CA    . LYS C 157 ? 0.7672 0.8319 0.5877 0.0458  0.0538  -0.1637 129 LYS C CA    
5321 C C     . LYS C 157 ? 0.7356 0.8268 0.5662 0.0513  0.0424  -0.1629 129 LYS C C     
5322 O O     . LYS C 157 ? 0.7557 0.8514 0.5821 0.0591  0.0359  -0.1568 129 LYS C O     
5323 C CB    . LYS C 157 ? 0.7764 0.8266 0.6013 0.0523  0.0577  -0.1549 129 LYS C CB    
5324 C CG    . LYS C 157 ? 0.8555 0.8786 0.6698 0.0498  0.0681  -0.1527 129 LYS C CG    
5325 C CD    . LYS C 157 ? 0.8903 0.9073 0.7020 0.0371  0.0764  -0.1631 129 LYS C CD    
5326 C CE    . LYS C 157 ? 0.9303 0.9202 0.7288 0.0350  0.0864  -0.1614 129 LYS C CE    
5327 N NZ    . LYS C 157 ? 0.9064 0.8917 0.6935 0.0261  0.0902  -0.1707 129 LYS C NZ    
5328 N N     . VAL C 158 ? 0.7111 0.8203 0.5553 0.0472  0.0403  -0.1686 130 VAL C N     
5329 C CA    . VAL C 158 ? 0.6426 0.7785 0.4987 0.0526  0.0299  -0.1681 130 VAL C CA    
5330 C C     . VAL C 158 ? 0.6543 0.7968 0.5255 0.0559  0.0307  -0.1665 130 VAL C C     
5331 O O     . VAL C 158 ? 0.6479 0.7918 0.5252 0.0474  0.0368  -0.1731 130 VAL C O     
5332 C CB    . VAL C 158 ? 0.5499 0.7074 0.4080 0.0435  0.0252  -0.1784 130 VAL C CB    
5333 C CG1   . VAL C 158 ? 0.5000 0.6868 0.3738 0.0489  0.0155  -0.1779 130 VAL C CG1   
5334 C CG2   . VAL C 158 ? 0.6228 0.7756 0.4646 0.0428  0.0225  -0.1791 130 VAL C CG2   
5335 N N     . PHE C 159 ? 0.6366 0.7825 0.5132 0.0681  0.0249  -0.1578 131 PHE C N     
5336 C CA    . PHE C 159 ? 0.5538 0.7057 0.4435 0.0730  0.0250  -0.1560 131 PHE C CA    
5337 C C     . PHE C 159 ? 0.5628 0.7447 0.4663 0.0764  0.0165  -0.1585 131 PHE C C     
5338 O O     . PHE C 159 ? 0.6080 0.8020 0.5101 0.0812  0.0079  -0.1561 131 PHE C O     
5339 C CB    . PHE C 159 ? 0.6118 0.7467 0.4987 0.0843  0.0241  -0.1450 131 PHE C CB    
5340 C CG    . PHE C 159 ? 0.5940 0.7010 0.4698 0.0818  0.0323  -0.1417 131 PHE C CG    
5341 C CD1   . PHE C 159 ? 0.6478 0.7433 0.5255 0.0786  0.0400  -0.1430 131 PHE C CD1   
5342 C CD2   . PHE C 159 ? 0.6083 0.7013 0.4717 0.0829  0.0326  -0.1368 131 PHE C CD2   
5343 C CE1   . PHE C 159 ? 0.6250 0.6956 0.4928 0.0767  0.0471  -0.1394 131 PHE C CE1   
5344 C CE2   . PHE C 159 ? 0.6363 0.7050 0.4907 0.0812  0.0402  -0.1332 131 PHE C CE2   
5345 C CZ    . PHE C 159 ? 0.6096 0.6673 0.4664 0.0782  0.0471  -0.1344 131 PHE C CZ    
5346 N N     . CYS C 160 ? 0.5794 0.7734 0.4961 0.0744  0.0191  -0.1629 132 CYS C N     
5347 C CA    . CYS C 160 ? 0.5592 0.7835 0.4915 0.0773  0.0122  -0.1657 132 CYS C CA    
5348 C C     . CYS C 160 ? 0.5916 0.8178 0.5354 0.0833  0.0155  -0.1640 132 CYS C C     
5349 O O     . CYS C 160 ? 0.6247 0.8501 0.5734 0.0758  0.0237  -0.1694 132 CYS C O     
5350 C CB    . CYS C 160 ? 0.4955 0.7391 0.4332 0.0642  0.0125  -0.1762 132 CYS C CB    
5351 S SG    . CYS C 160 ? 0.6054 0.8861 0.5666 0.0650  0.0081  -0.1808 132 CYS C SG    
5352 N N     . MET C 161 ? 0.5783 0.8064 0.5258 0.0968  0.0095  -0.1565 133 MET C N     
5353 C CA    . MET C 161 ? 0.5727 0.7984 0.5280 0.1044  0.0124  -0.1542 133 MET C CA    
5354 C C     . MET C 161 ? 0.6082 0.8612 0.5789 0.1132  0.0053  -0.1539 133 MET C C     
5355 O O     . MET C 161 ? 0.6572 0.9157 0.6273 0.1225  -0.0037 -0.1482 133 MET C O     
5356 C CB    . MET C 161 ? 0.6349 0.8333 0.5794 0.1132  0.0125  -0.1452 133 MET C CB    
5357 C CG    . MET C 161 ? 0.7209 0.8959 0.6496 0.1081  0.0151  -0.1423 133 MET C CG    
5358 S SD    . MET C 161 ? 0.7707 0.9278 0.6931 0.0954  0.0279  -0.1479 133 MET C SD    
5359 C CE    . MET C 161 ? 0.6870 0.8330 0.6129 0.1025  0.0322  -0.1449 133 MET C CE    
5360 N N     . LEU C 162 ? 0.5801 0.8501 0.5647 0.1107  0.0097  -0.1596 134 LEU C N     
5361 C CA    . LEU C 162 ? 0.5442 0.8390 0.5450 0.1203  0.0050  -0.1590 134 LEU C CA    
5362 C C     . LEU C 162 ? 0.5338 0.8518 0.5397 0.1238  -0.0064 -0.1578 134 LEU C C     
5363 O O     . LEU C 162 ? 0.5860 0.9050 0.5917 0.1364  -0.0140 -0.1508 134 LEU C O     
5364 C CB    . LEU C 162 ? 0.5349 0.8142 0.5337 0.1345  0.0049  -0.1521 134 LEU C CB    
5365 C CG    . LEU C 162 ? 0.5059 0.7572 0.4951 0.1326  0.0143  -0.1515 134 LEU C CG    
5366 C CD1   . LEU C 162 ? 0.5339 0.7675 0.5179 0.1466  0.0116  -0.1440 134 LEU C CD1   
5367 C CD2   . LEU C 162 ? 0.4377 0.6992 0.4367 0.1261  0.0239  -0.1585 134 LEU C CD2   
5368 N N     . MET C 163 ? 0.4980 0.8344 0.5081 0.1119  -0.0075 -0.1648 135 MET C N     
5369 C CA    . MET C 163 ? 0.4947 0.8535 0.5081 0.1138  -0.0185 -0.1642 135 MET C CA    
5370 C C     . MET C 163 ? 0.5087 0.8954 0.5335 0.1010  -0.0193 -0.1735 135 MET C C     
5371 O O     . MET C 163 ? 0.5489 0.9647 0.5852 0.1041  -0.0281 -0.1740 135 MET C O     
5372 C CB    . MET C 163 ? 0.5160 0.8552 0.5102 0.1138  -0.0227 -0.1598 135 MET C CB    
5373 C CG    . MET C 163 ? 0.5677 0.9254 0.5596 0.1091  -0.0315 -0.1623 135 MET C CG    
5374 S SD    . MET C 163 ? 0.5433 0.8977 0.5270 0.0887  -0.0259 -0.1732 135 MET C SD    
5375 C CE    . MET C 163 ? 0.5516 0.8648 0.5119 0.0886  -0.0197 -0.1682 135 MET C CE    
5376 N N     . LEU C 164 ? 0.4519 0.8303 0.4739 0.0865  -0.0104 -0.1807 136 LEU C N     
5377 C CA    . LEU C 164 ? 0.4569 0.8599 0.4896 0.0725  -0.0106 -0.1900 136 LEU C CA    
5378 C C     . LEU C 164 ? 0.4536 0.8891 0.5106 0.0754  -0.0112 -0.1919 136 LEU C C     
5379 O O     . LEU C 164 ? 0.4575 0.9199 0.5267 0.0653  -0.0140 -0.1986 136 LEU C O     
5380 C CB    . LEU C 164 ? 0.4613 0.8454 0.4859 0.0568  0.0003  -0.1967 136 LEU C CB    
5381 C CG    . LEU C 164 ? 0.4711 0.8489 0.4822 0.0436  -0.0018 -0.2024 136 LEU C CG    
5382 C CD1   . LEU C 164 ? 0.4727 0.8306 0.4645 0.0509  -0.0071 -0.1963 136 LEU C CD1   
5383 C CD2   . LEU C 164 ? 0.4765 0.8349 0.4812 0.0290  0.0100  -0.2087 136 LEU C CD2   
5384 N N     . HIS C 165 ? 0.4475 0.8817 0.5119 0.0888  -0.0087 -0.1864 137 HIS C N     
5385 C CA    . HIS C 165 ? 0.4450 0.9113 0.5327 0.0944  -0.0097 -0.1872 137 HIS C CA    
5386 C C     . HIS C 165 ? 0.4452 0.9368 0.5414 0.1055  -0.0229 -0.1829 137 HIS C C     
5387 O O     . HIS C 165 ? 0.4442 0.9676 0.5613 0.1095  -0.0254 -0.1837 137 HIS C O     
5388 C CB    . HIS C 165 ? 0.4408 0.8941 0.5314 0.1050  -0.0012 -0.1834 137 HIS C CB    
5389 C CG    . HIS C 165 ? 0.4574 0.8855 0.5343 0.1199  -0.0043 -0.1748 137 HIS C CG    
5390 N ND1   . HIS C 165 ? 0.5224 0.9148 0.5784 0.1180  -0.0009 -0.1721 137 HIS C ND1   
5391 C CD2   . HIS C 165 ? 0.4729 0.9059 0.5546 0.1370  -0.0100 -0.1681 137 HIS C CD2   
5392 C CE1   . HIS C 165 ? 0.6159 0.9933 0.6649 0.1324  -0.0051 -0.1642 137 HIS C CE1   
5393 N NE2   . HIS C 165 ? 0.5838 0.9841 0.6474 0.1441  -0.0105 -0.1617 137 HIS C NE2   
5394 N N     . LEU C 166 ? 0.4471 0.9257 0.5278 0.1108  -0.0310 -0.1778 138 LEU C N     
5395 C CA    . LEU C 166 ? 0.4495 0.9506 0.5348 0.1194  -0.0442 -0.1738 138 LEU C CA    
5396 C C     . LEU C 166 ? 0.4564 0.9742 0.5391 0.1063  -0.0514 -0.1797 138 LEU C C     
5397 O O     . LEU C 166 ? 0.4597 1.0001 0.5471 0.1119  -0.0629 -0.1771 138 LEU C O     
5398 C CB    . LEU C 166 ? 0.4889 0.9666 0.5585 0.1333  -0.0491 -0.1640 138 LEU C CB    
5399 C CG    . LEU C 166 ? 0.5408 1.0146 0.6163 0.1519  -0.0497 -0.1558 138 LEU C CG    
5400 C CD1   . LEU C 166 ? 0.5399 1.0085 0.6245 0.1528  -0.0385 -0.1584 138 LEU C CD1   
5401 C CD2   . LEU C 166 ? 0.5719 1.0131 0.6278 0.1602  -0.0515 -0.1474 138 LEU C CD2   
5402 N N     . VAL C 167 ? 0.4600 0.9670 0.5348 0.0894  -0.0452 -0.1875 139 VAL C N     
5403 C CA    . VAL C 167 ? 0.4691 0.9878 0.5387 0.0757  -0.0514 -0.1942 139 VAL C CA    
5404 C C     . VAL C 167 ? 0.4710 1.0184 0.5607 0.0624  -0.0492 -0.2031 139 VAL C C     
5405 O O     . VAL C 167 ? 0.4707 1.0061 0.5611 0.0515  -0.0380 -0.2085 139 VAL C O     
5406 C CB    . VAL C 167 ? 0.4744 0.9591 0.5197 0.0659  -0.0461 -0.1969 139 VAL C CB    
5407 C CG1   . VAL C 167 ? 0.4858 0.9794 0.5209 0.0567  -0.0549 -0.2017 139 VAL C CG1   
5408 C CG2   . VAL C 167 ? 0.4697 0.9227 0.4990 0.0787  -0.0439 -0.1875 139 VAL C CG2   
5409 N N     . PRO C 168 ? 0.4735 1.0588 0.5800 0.0629  -0.0593 -0.2045 140 PRO C N     
5410 C CA    . PRO C 168 ? 0.4757 1.0901 0.6029 0.0492  -0.0574 -0.2128 140 PRO C CA    
5411 C C     . PRO C 168 ? 0.4852 1.0886 0.6019 0.0278  -0.0534 -0.2228 140 PRO C C     
5412 O O     . PRO C 168 ? 0.4849 1.0838 0.6083 0.0166  -0.0427 -0.2282 140 PRO C O     
5413 C CB    . PRO C 168 ? 0.4782 1.1334 0.6214 0.0547  -0.0717 -0.2111 140 PRO C CB    
5414 C CG    . PRO C 168 ? 0.4730 1.1213 0.6115 0.0763  -0.0767 -0.2001 140 PRO C CG    
5415 C CD    . PRO C 168 ? 0.4738 1.0789 0.5841 0.0774  -0.0724 -0.1974 140 PRO C CD    
5416 N N     . ASP C 169 ? 0.4952 1.0929 0.5945 0.0219  -0.0615 -0.2255 141 ASP C N     
5417 C CA    . ASP C 169 ? 0.5071 1.0914 0.5935 0.0021  -0.0583 -0.2354 141 ASP C CA    
5418 C C     . ASP C 169 ? 0.5060 1.0453 0.5710 0.0016  -0.0463 -0.2341 141 ASP C C     
5419 O O     . ASP C 169 ? 0.5090 1.0242 0.5521 0.0068  -0.0482 -0.2306 141 ASP C O     
5420 C CB    . ASP C 169 ? 0.5200 1.1138 0.5941 -0.0028 -0.0712 -0.2388 141 ASP C CB    
5421 N N     . ASN C 170 ? 0.5021 1.0308 0.5740 -0.0047 -0.0335 -0.2365 142 ASN C N     
5422 C CA    . ASN C 170 ? 0.5008 0.9884 0.5544 -0.0049 -0.0218 -0.2347 142 ASN C CA    
5423 C C     . ASN C 170 ? 0.5147 0.9805 0.5496 -0.0213 -0.0182 -0.2427 142 ASN C C     
5424 O O     . ASN C 170 ? 0.5742 1.0063 0.5878 -0.0187 -0.0135 -0.2401 142 ASN C O     
5425 C CB    . ASN C 170 ? 0.4928 0.9769 0.5596 -0.0046 -0.0096 -0.2338 142 ASN C CB    
5426 C CG    . ASN C 170 ? 0.5168 0.9983 0.5884 0.0150  -0.0089 -0.2239 142 ASN C CG    
5427 O OD1   . ASN C 170 ? 0.6264 1.1364 0.7175 0.0235  -0.0133 -0.2212 142 ASN C OD1   
5428 N ND2   . ASN C 170 ? 0.4767 0.9236 0.5309 0.0222  -0.0032 -0.2184 142 ASN C ND2   
5429 N N     . ARG C 171 ? 0.5353 1.0192 0.5778 -0.0382 -0.0203 -0.2525 143 ARG C N     
5430 C CA    . ARG C 171 ? 0.5512 1.0133 0.5750 -0.0541 -0.0170 -0.2609 143 ARG C CA    
5431 C C     . ARG C 171 ? 0.5600 1.0128 0.5622 -0.0504 -0.0262 -0.2604 143 ARG C C     
5432 O O     . ARG C 171 ? 0.5703 0.9923 0.5502 -0.0558 -0.0212 -0.2632 143 ARG C O     
5433 C CB    . ARG C 171 ? 0.5622 1.0469 0.6002 -0.0737 -0.0178 -0.2716 143 ARG C CB    
5434 C CG    . ARG C 171 ? 0.5908 1.0533 0.6096 -0.0913 -0.0148 -0.2814 143 ARG C CG    
5435 C CD    . ARG C 171 ? 0.5898 1.0598 0.6223 -0.1107 -0.0077 -0.2901 143 ARG C CD    
5436 N NE    . ARG C 171 ? 0.6143 1.1232 0.6773 -0.1100 -0.0103 -0.2887 143 ARG C NE    
5437 C CZ    . ARG C 171 ? 0.6953 1.2093 0.7751 -0.1179 0.0000  -0.2901 143 ARG C CZ    
5438 N NH1   . ARG C 171 ? 0.7079 1.1903 0.7769 -0.1272 0.0133  -0.2927 143 ARG C NH1   
5439 N NH2   . ARG C 171 ? 0.6134 1.1653 0.7214 -0.1159 -0.0028 -0.2884 143 ARG C NH2   
5440 N N     . LEU C 172 ? 0.5494 1.0280 0.5575 -0.0404 -0.0392 -0.2564 144 LEU C N     
5441 C CA    . LEU C 172 ? 0.5555 1.0252 0.5423 -0.0349 -0.0477 -0.2545 144 LEU C CA    
5442 C C     . LEU C 172 ? 0.5478 0.9846 0.5178 -0.0208 -0.0419 -0.2449 144 LEU C C     
5443 O O     . LEU C 172 ? 0.5574 0.9701 0.5041 -0.0215 -0.0411 -0.2453 144 LEU C O     
5444 C CB    . LEU C 172 ? 0.5541 1.0600 0.5522 -0.0267 -0.0629 -0.2513 144 LEU C CB    
5445 C CG    . LEU C 172 ? 0.5619 1.0623 0.5394 -0.0183 -0.0726 -0.2474 144 LEU C CG    
5446 C CD1   . LEU C 172 ? 0.5817 1.0625 0.5352 -0.0323 -0.0718 -0.2566 144 LEU C CD1   
5447 C CD2   . LEU C 172 ? 0.5620 1.1012 0.5527 -0.0116 -0.0878 -0.2447 144 LEU C CD2   
5448 N N     . ALA C 173 ? 0.5315 0.9668 0.5130 -0.0079 -0.0376 -0.2363 145 ALA C N     
5449 C CA    . ALA C 173 ? 0.5241 0.9291 0.4913 0.0050  -0.0325 -0.2270 145 ALA C CA    
5450 C C     . ALA C 173 ? 0.5284 0.8980 0.4809 -0.0033 -0.0195 -0.2299 145 ALA C C     
5451 O O     . ALA C 173 ? 0.5297 0.8721 0.4635 0.0023  -0.0166 -0.2250 145 ALA C O     
5452 C CB    . ALA C 173 ? 0.5078 0.9198 0.4907 0.0199  -0.0316 -0.2180 145 ALA C CB    
5453 N N     . VAL C 174 ? 0.5312 0.9008 0.4922 -0.0165 -0.0114 -0.2372 146 VAL C N     
5454 C CA    . VAL C 174 ? 0.5374 0.8735 0.4844 -0.0250 0.0010  -0.2402 146 VAL C CA    
5455 C C     . VAL C 174 ? 0.5553 0.8771 0.4814 -0.0347 -0.0004 -0.2469 146 VAL C C     
5456 O O     . VAL C 174 ? 0.5602 0.8502 0.4673 -0.0339 0.0066  -0.2451 146 VAL C O     
5457 C CB    . VAL C 174 ? 0.5373 0.8781 0.4991 -0.0369 0.0100  -0.2460 146 VAL C CB    
5458 C CG1   . VAL C 174 ? 0.5479 0.8552 0.4941 -0.0479 0.0220  -0.2503 146 VAL C CG1   
5459 C CG2   . VAL C 174 ? 0.5209 0.8684 0.4988 -0.0257 0.0138  -0.2387 146 VAL C CG2   
5460 N N     . LYS C 175 ? 0.5664 0.9116 0.4953 -0.0438 -0.0096 -0.2547 147 LYS C N     
5461 C CA    . LYS C 175 ? 0.5860 0.9181 0.4935 -0.0530 -0.0116 -0.2619 147 LYS C CA    
5462 C C     . LYS C 175 ? 0.5864 0.9042 0.4748 -0.0396 -0.0156 -0.2543 147 LYS C C     
5463 O O     . LYS C 175 ? 0.5993 0.8908 0.4656 -0.0427 -0.0111 -0.2567 147 LYS C O     
5464 C CB    . LYS C 175 ? 0.5981 0.9609 0.5133 -0.0648 -0.0223 -0.2715 147 LYS C CB    
5465 N N     . ASN C 176 ? 0.5734 0.9079 0.4698 -0.0244 -0.0237 -0.2450 148 ASN C N     
5466 C CA    . ASN C 176 ? 0.5731 0.8943 0.4527 -0.0113 -0.0271 -0.2364 148 ASN C CA    
5467 C C     . ASN C 176 ? 0.5657 0.8531 0.4358 -0.0042 -0.0157 -0.2290 148 ASN C C     
5468 O O     . ASN C 176 ? 0.5724 0.8382 0.4228 -0.0002 -0.0136 -0.2258 148 ASN C O     
5469 C CB    . ASN C 176 ? 0.5620 0.9093 0.4537 0.0029  -0.0384 -0.2279 148 ASN C CB    
5470 C CG    . ASN C 176 ? 0.5736 0.9491 0.4653 -0.0008 -0.0516 -0.2329 148 ASN C CG    
5471 O OD1   . ASN C 176 ? 0.5913 0.9636 0.4696 -0.0130 -0.0529 -0.2423 148 ASN C OD1   
5472 N ND2   . ASN C 176 ? 0.5650 0.9678 0.4710 0.0098  -0.0617 -0.2267 148 ASN C ND2   
5473 N N     . ILE C 177 ? 0.5525 0.8356 0.4363 -0.0025 -0.0084 -0.2260 149 ILE C N     
5474 C CA    . ILE C 177 ? 0.5466 0.7980 0.4219 0.0026  0.0023  -0.2197 149 ILE C CA    
5475 C C     . ILE C 177 ? 0.5617 0.7872 0.4207 -0.0095 0.0118  -0.2270 149 ILE C C     
5476 O O     . ILE C 177 ? 0.5660 0.7640 0.4097 -0.0050 0.0181  -0.2221 149 ILE C O     
5477 C CB    . ILE C 177 ? 0.5313 0.7851 0.4243 0.0064  0.0075  -0.2158 149 ILE C CB    
5478 C CG1   . ILE C 177 ? 0.5175 0.7893 0.4226 0.0216  -0.0008 -0.2067 149 ILE C CG1   
5479 C CG2   . ILE C 177 ? 0.5283 0.7492 0.4123 0.0080  0.0192  -0.2114 149 ILE C CG2   
5480 C CD1   . ILE C 177 ? 0.5048 0.7838 0.4281 0.0253  0.0031  -0.2043 149 ILE C CD1   
5481 N N     . HIS C 178 ? 0.5886 0.8222 0.4506 -0.0250 0.0129  -0.2385 150 HIS C N     
5482 C CA    . HIS C 178 ? 0.6286 0.8369 0.4743 -0.0372 0.0216  -0.2462 150 HIS C CA    
5483 C C     . HIS C 178 ? 0.6311 0.8277 0.4542 -0.0356 0.0184  -0.2474 150 HIS C C     
5484 O O     . HIS C 178 ? 0.6507 0.8178 0.4563 -0.0373 0.0272  -0.2481 150 HIS C O     
5485 C CB    . HIS C 178 ? 0.6677 0.8894 0.5228 -0.0548 0.0223  -0.2584 150 HIS C CB    
5486 C CG    . HIS C 178 ? 0.7463 0.9407 0.5856 -0.0681 0.0319  -0.2668 150 HIS C CG    
5487 N ND1   . HIS C 178 ? 0.8283 1.0161 0.6498 -0.0763 0.0290  -0.2753 150 HIS C ND1   
5488 C CD2   . HIS C 178 ? 0.7696 0.9408 0.6077 -0.0745 0.0446  -0.2681 150 HIS C CD2   
5489 C CE1   . HIS C 178 ? 0.8343 0.9953 0.6444 -0.0870 0.0397  -0.2816 150 HIS C CE1   
5490 N NE2   . HIS C 178 ? 0.8527 1.0034 0.6729 -0.0861 0.0492  -0.2770 150 HIS C NE2   
5491 N N     . LYS C 179 ? 0.6083 0.8275 0.4309 -0.0318 0.0062  -0.2475 151 LYS C N     
5492 C CA    . LYS C 179 ? 0.6228 0.8321 0.4231 -0.0290 0.0029  -0.2478 151 LYS C CA    
5493 C C     . LYS C 179 ? 0.6146 0.8020 0.4045 -0.0143 0.0078  -0.2355 151 LYS C C     
5494 O O     . LYS C 179 ? 0.6848 0.8492 0.4542 -0.0138 0.0130  -0.2358 151 LYS C O     
5495 C CB    . LYS C 179 ? 0.6260 0.8659 0.4289 -0.0265 -0.0118 -0.2488 151 LYS C CB    
5496 C CG    . LYS C 179 ? 0.6392 0.9010 0.4482 -0.0421 -0.0183 -0.2617 151 LYS C CG    
5497 C CD    . LYS C 179 ? 0.6418 0.9341 0.4528 -0.0375 -0.0336 -0.2608 151 LYS C CD    
5498 C CE    . LYS C 179 ? 0.6660 0.9830 0.4844 -0.0531 -0.0414 -0.2733 151 LYS C CE    
5499 N NZ    . LYS C 179 ? 0.7070 1.0551 0.5279 -0.0479 -0.0570 -0.2717 151 LYS C NZ    
5500 N N     . LEU C 180 ? 0.5940 0.7883 0.3981 -0.0022 0.0062  -0.2247 152 LEU C N     
5501 C CA    . LEU C 180 ? 0.5854 0.7632 0.3821 0.0120  0.0086  -0.2123 152 LEU C CA    
5502 C C     . LEU C 180 ? 0.6336 0.7798 0.4235 0.0115  0.0218  -0.2095 152 LEU C C     
5503 O O     . LEU C 180 ? 0.6480 0.7772 0.4284 0.0211  0.0250  -0.2004 152 LEU C O     
5504 C CB    . LEU C 180 ? 0.5656 0.7605 0.3797 0.0243  0.0020  -0.2022 152 LEU C CB    
5505 C CG    . LEU C 180 ? 0.5659 0.7887 0.3840 0.0300  -0.0115 -0.2004 152 LEU C CG    
5506 C CD1   . LEU C 180 ? 0.5479 0.7893 0.3870 0.0393  -0.0168 -0.1934 152 LEU C CD1   
5507 C CD2   . LEU C 180 ? 0.5727 0.7869 0.3731 0.0389  -0.0145 -0.1933 152 LEU C CD2   
5508 N N     . LEU C 181 ? 0.6852 0.8239 0.4804 0.0007  0.0295  -0.2167 153 LEU C N     
5509 C CA    . LEU C 181 ? 0.7218 0.8316 0.5119 0.0005  0.0418  -0.2137 153 LEU C CA    
5510 C C     . LEU C 181 ? 0.7894 0.8758 0.5590 -0.0073 0.0494  -0.2205 153 LEU C C     
5511 O O     . LEU C 181 ? 0.7581 0.8503 0.5208 -0.0180 0.0470  -0.2314 153 LEU C O     
5512 C CB    . LEU C 181 ? 0.6815 0.7935 0.4872 -0.0063 0.0471  -0.2167 153 LEU C CB    
5513 C CG    . LEU C 181 ? 0.6120 0.7378 0.4359 0.0032  0.0435  -0.2085 153 LEU C CG    
5514 C CD1   . LEU C 181 ? 0.7020 0.8359 0.5410 -0.0055 0.0477  -0.2140 153 LEU C CD1   
5515 C CD2   . LEU C 181 ? 0.7311 0.8357 0.5504 0.0148  0.0482  -0.1967 153 LEU C CD2   
5516 N N     . VAL C 182 ? 0.8188 0.8786 0.5788 -0.0017 0.0586  -0.2139 154 VAL C N     
5517 C CA    . VAL C 182 ? 0.8320 0.8656 0.5734 -0.0080 0.0682  -0.2194 154 VAL C CA    
5518 C C     . VAL C 182 ? 0.9140 0.9380 0.6603 -0.0206 0.0762  -0.2274 154 VAL C C     
5519 O O     . VAL C 182 ? 0.9525 0.9832 0.7150 -0.0206 0.0772  -0.2243 154 VAL C O     
5520 C CB    . VAL C 182 ? 0.7592 0.7693 0.4905 0.0033  0.0753  -0.2085 154 VAL C CB    
5521 C CG1   . VAL C 182 ? 0.7273 0.7471 0.4537 0.0151  0.0678  -0.2003 154 VAL C CG1   
5522 C CG2   . VAL C 182 ? 0.7843 0.7867 0.5284 0.0085  0.0801  -0.1995 154 VAL C CG2   
5523 N N     . PRO C 183 ? 0.9625 0.9708 0.6949 -0.0318 0.0822  -0.2377 155 PRO C N     
5524 C CA    . PRO C 183 ? 1.0141 1.0094 0.7501 -0.0436 0.0913  -0.2441 155 PRO C CA    
5525 C C     . PRO C 183 ? 1.0501 1.0243 0.7883 -0.0365 0.1011  -0.2342 155 PRO C C     
5526 O O     . PRO C 183 ? 1.0510 1.0025 0.7761 -0.0294 0.1076  -0.2286 155 PRO C O     
5527 C CB    . PRO C 183 ? 1.0780 1.0546 0.7939 -0.0539 0.0962  -0.2552 155 PRO C CB    
5528 C CG    . PRO C 183 ? 1.0810 1.0743 0.7888 -0.0520 0.0856  -0.2586 155 PRO C CG    
5529 C CD    . PRO C 183 ? 0.9957 1.0001 0.7091 -0.0353 0.0799  -0.2451 155 PRO C CD    
5530 N N     . GLY C 184 ? 1.0831 1.0655 0.8382 -0.0382 0.1020  -0.2319 156 GLY C N     
5531 C CA    . GLY C 184 ? 1.0430 1.0100 0.8021 -0.0308 0.1092  -0.2219 156 GLY C CA    
5532 C C     . GLY C 184 ? 0.9789 0.9614 0.7508 -0.0180 0.1022  -0.2110 156 GLY C C     
5533 O O     . GLY C 184 ? 1.0068 0.9794 0.7838 -0.0125 0.1068  -0.2031 156 GLY C O     
5534 N N     . GLY C 185 ? 0.9316 0.9373 0.7081 -0.0131 0.0911  -0.2103 157 GLY C N     
5535 C CA    . GLY C 185 ? 0.8908 0.9116 0.6799 -0.0015 0.0840  -0.2007 157 GLY C CA    
5536 C C     . GLY C 185 ? 0.9282 0.9645 0.7351 -0.0048 0.0831  -0.2023 157 GLY C C     
5537 O O     . GLY C 185 ? 0.9379 0.9797 0.7497 -0.0169 0.0860  -0.2114 157 GLY C O     
5538 N N     . GLU C 186 ? 0.9015 0.9449 0.7183 0.0060  0.0791  -0.1932 158 GLU C N     
5539 C CA    . GLU C 186 ? 0.8895 0.9449 0.7221 0.0053  0.0793  -0.1931 158 GLU C CA    
5540 C C     . GLU C 186 ? 0.8332 0.9152 0.6785 0.0135  0.0681  -0.1901 158 GLU C C     
5541 O O     . GLU C 186 ? 0.7833 0.8675 0.6252 0.0236  0.0614  -0.1833 158 GLU C O     
5542 C CB    . GLU C 186 ? 0.8994 0.9344 0.7311 0.0107  0.0865  -0.1850 158 GLU C CB    
5543 C CG    . GLU C 186 ? 0.9427 0.9505 0.7622 0.0038  0.0978  -0.1868 158 GLU C CG    
5544 C CD    . GLU C 186 ? 1.0752 1.0621 0.8914 0.0114  0.1033  -0.1769 158 GLU C CD    
5545 O OE1   . GLU C 186 ? 1.0768 1.0634 0.8933 0.0229  0.0980  -0.1676 158 GLU C OE1   
5546 O OE2   . GLU C 186 ? 1.1360 1.1067 0.9493 0.0056  0.1126  -0.1781 158 GLU C OE2   
5547 N N     . ALA C 187 ? 0.8338 0.9360 0.6942 0.0092  0.0666  -0.1949 159 ALA C N     
5548 C CA    . ALA C 187 ? 0.7074 0.8360 0.5816 0.0168  0.0569  -0.1927 159 ALA C CA    
5549 C C     . ALA C 187 ? 0.7021 0.8331 0.5884 0.0212  0.0600  -0.1892 159 ALA C C     
5550 O O     . ALA C 187 ? 0.6792 0.8086 0.5704 0.0126  0.0677  -0.1941 159 ALA C O     
5551 C CB    . ALA C 187 ? 0.6536 0.8093 0.5360 0.0082  0.0509  -0.2021 159 ALA C CB    
5552 N N     . VAL C 188 ? 0.6734 0.8072 0.5635 0.0344  0.0545  -0.1807 160 VAL C N     
5553 C CA    . VAL C 188 ? 0.5801 0.7144 0.4795 0.0404  0.0568  -0.1769 160 VAL C CA    
5554 C C     . VAL C 188 ? 0.5611 0.7250 0.4763 0.0455  0.0488  -0.1782 160 VAL C C     
5555 O O     . VAL C 188 ? 0.6452 0.8177 0.5615 0.0554  0.0398  -0.1731 160 VAL C O     
5556 C CB    . VAL C 188 ? 0.5411 0.6540 0.4326 0.0515  0.0566  -0.1664 160 VAL C CB    
5557 C CG1   . VAL C 188 ? 0.5887 0.7032 0.4888 0.0584  0.0576  -0.1631 160 VAL C CG1   
5558 C CG2   . VAL C 188 ? 0.5521 0.6370 0.4295 0.0468  0.0650  -0.1647 160 VAL C CG2   
5559 N N     . PHE C 189 ? 0.5667 0.7466 0.4947 0.0392  0.0525  -0.1844 161 PHE C N     
5560 C CA    . PHE C 189 ? 0.5647 0.7747 0.5097 0.0437  0.0460  -0.1859 161 PHE C CA    
5561 C C     . PHE C 189 ? 0.5758 0.7845 0.5280 0.0538  0.0482  -0.1810 161 PHE C C     
5562 O O     . PHE C 189 ? 0.5609 0.7495 0.5075 0.0531  0.0566  -0.1793 161 PHE C O     
5563 C CB    . PHE C 189 ? 0.5603 0.7922 0.5169 0.0306  0.0483  -0.1958 161 PHE C CB    
5564 C CG    . PHE C 189 ? 0.5572 0.7940 0.5076 0.0206  0.0443  -0.2018 161 PHE C CG    
5565 C CD1   . PHE C 189 ? 0.6174 0.8331 0.5548 0.0091  0.0516  -0.2060 161 PHE C CD1   
5566 C CD2   . PHE C 189 ? 0.5356 0.7974 0.4922 0.0230  0.0333  -0.2031 161 PHE C CD2   
5567 C CE1   . PHE C 189 ? 0.6256 0.8442 0.5556 0.0000  0.0482  -0.2122 161 PHE C CE1   
5568 C CE2   . PHE C 189 ? 0.5326 0.7984 0.4817 0.0137  0.0293  -0.2091 161 PHE C CE2   
5569 C CZ    . PHE C 189 ? 0.5675 0.8112 0.5029 0.0021  0.0369  -0.2140 161 PHE C CZ    
5570 N N     . SER C 190 ? 0.5810 0.8110 0.5450 0.0637  0.0406  -0.1788 162 SER C N     
5571 C CA    . SER C 190 ? 0.5395 0.7723 0.5118 0.0740  0.0420  -0.1753 162 SER C CA    
5572 C C     . SER C 190 ? 0.5237 0.7912 0.5146 0.0777  0.0359  -0.1781 162 SER C C     
5573 O O     . SER C 190 ? 0.5633 0.8405 0.5583 0.0896  0.0274  -0.1733 162 SER C O     
5574 C CB    . SER C 190 ? 0.5880 0.8007 0.5505 0.0872  0.0380  -0.1660 162 SER C CB    
5575 O OG    . SER C 190 ? 0.6307 0.8429 0.5991 0.0965  0.0400  -0.1636 162 SER C OG    
5576 N N     . VAL C 191 ? 0.4694 0.7559 0.4722 0.0671  0.0405  -0.1856 163 VAL C N     
5577 C CA    . VAL C 191 ? 0.4496 0.7720 0.4719 0.0684  0.0352  -0.1889 163 VAL C CA    
5578 C C     . VAL C 191 ? 0.4651 0.7965 0.5001 0.0762  0.0405  -0.1878 163 VAL C C     
5579 O O     . VAL C 191 ? 0.4832 0.8001 0.5153 0.0727  0.0510  -0.1888 163 VAL C O     
5580 C CB    . VAL C 191 ? 0.4551 0.7950 0.4844 0.0515  0.0368  -0.1977 163 VAL C CB    
5581 C CG1   . VAL C 191 ? 0.4539 0.8334 0.5043 0.0527  0.0297  -0.2006 163 VAL C CG1   
5582 C CG2   . VAL C 191 ? 0.4607 0.7863 0.4739 0.0436  0.0332  -0.1994 163 VAL C CG2   
5583 N N     . ILE C 192 ? 0.4622 0.8174 0.5109 0.0875  0.0334  -0.1855 164 ILE C N     
5584 C CA    . ILE C 192 ? 0.4751 0.8429 0.5375 0.0959  0.0382  -0.1849 164 ILE C CA    
5585 C C     . ILE C 192 ? 0.5042 0.9041 0.5865 0.0855  0.0418  -0.1920 164 ILE C C     
5586 O O     . ILE C 192 ? 0.5302 0.9587 0.6252 0.0837  0.0336  -0.1941 164 ILE C O     
5587 C CB    . ILE C 192 ? 0.4386 0.8157 0.5065 0.1139  0.0294  -0.1788 164 ILE C CB    
5588 C CG1   . ILE C 192 ? 0.4500 0.7936 0.4989 0.1237  0.0271  -0.1716 164 ILE C CG1   
5589 C CG2   . ILE C 192 ? 0.4824 0.8776 0.5669 0.1223  0.0344  -0.1793 164 ILE C CG2   
5590 C CD1   . ILE C 192 ? 0.4616 0.8104 0.5137 0.1408  0.0180  -0.1651 164 ILE C CD1   
5591 N N     . ALA C 193 ? 0.5198 0.9151 0.6049 0.0783  0.0538  -0.1953 165 ALA C N     
5592 C CA    . ALA C 193 ? 0.5524 0.9772 0.6569 0.0672  0.0586  -0.2016 165 ALA C CA    
5593 C C     . ALA C 193 ? 0.5895 1.0486 0.7163 0.0783  0.0551  -0.2004 165 ALA C C     
5594 O O     . ALA C 193 ? 0.6563 1.1472 0.7990 0.0751  0.0476  -0.2029 165 ALA C O     
5595 C CB    . ALA C 193 ? 0.6549 1.0648 0.7561 0.0581  0.0731  -0.2043 165 ALA C CB    
5596 N N     . ASN C 194 ? 0.6410 1.0939 0.7690 0.0919  0.0604  -0.1966 166 ASN C N     
5597 C CA    . ASN C 194 ? 0.6239 1.1068 0.7722 0.1044  0.0586  -0.1950 166 ASN C CA    
5598 C C     . ASN C 194 ? 0.6182 1.0815 0.7569 0.1237  0.0580  -0.1888 166 ASN C C     
5599 O O     . ASN C 194 ? 0.6042 1.0335 0.7240 0.1253  0.0635  -0.1869 166 ASN C O     
5600 C CB    . ASN C 194 ? 0.5971 1.1021 0.7638 0.0977  0.0701  -0.1993 166 ASN C CB    
5601 C CG    . ASN C 194 ? 0.6676 1.1459 0.8225 0.0988  0.0838  -0.1988 166 ASN C CG    
5602 O OD1   . ASN C 194 ? 0.7598 1.2302 0.9123 0.1139  0.0869  -0.1952 166 ASN C OD1   
5603 N ND2   . ASN C 194 ? 0.6615 1.1251 0.8083 0.0827  0.0919  -0.2024 166 ASN C ND2   
5604 N N     . MET C 195 ? 0.5671 1.0520 0.7190 0.1382  0.0511  -0.1856 167 MET C N     
5605 C CA    . MET C 195 ? 0.6025 1.0709 0.7471 0.1571  0.0503  -0.1800 167 MET C CA    
5606 C C     . MET C 195 ? 0.5958 1.0978 0.7628 0.1705  0.0476  -0.1785 167 MET C C     
5607 O O     . MET C 195 ? 0.6281 1.1651 0.8142 0.1662  0.0424  -0.1803 167 MET C O     
5608 C CB    . MET C 195 ? 0.6098 1.0527 0.7357 0.1631  0.0399  -0.1746 167 MET C CB    
5609 C CG    . MET C 195 ? 0.6635 1.1246 0.7940 0.1591  0.0275  -0.1740 167 MET C CG    
5610 S SD    . MET C 195 ? 0.7266 1.1547 0.8331 0.1641  0.0176  -0.1674 167 MET C SD    
5611 C CE    . MET C 195 ? 0.6029 1.0061 0.7011 0.1831  0.0202  -0.1615 167 MET C CE    
5612 N N     . ALA C 196 ? 0.5731 1.0637 0.7371 0.1870  0.0512  -0.1752 168 ALA C N     
5613 C CA    . ALA C 196 ? 0.5965 1.1166 0.7811 0.2017  0.0503  -0.1735 168 ALA C CA    
5614 C C     . ALA C 196 ? 0.6028 1.1356 0.7924 0.2126  0.0358  -0.1683 168 ALA C C     
5615 O O     . ALA C 196 ? 0.6075 1.1709 0.8172 0.2234  0.0333  -0.1667 168 ALA C O     
5616 C CB    . ALA C 196 ? 0.7248 1.2263 0.9029 0.2163  0.0593  -0.1720 168 ALA C CB    
5617 N N     . LEU C 197 ? 0.6530 1.1637 0.8251 0.2106  0.0265  -0.1652 169 LEU C N     
5618 C CA    . LEU C 197 ? 0.6967 1.2214 0.8734 0.2190  0.0127  -0.1602 169 LEU C CA    
5619 C C     . LEU C 197 ? 0.6598 1.2262 0.8571 0.2097  0.0071  -0.1632 169 LEU C C     
5620 O O     . LEU C 197 ? 0.5694 1.1605 0.7792 0.2192  -0.0026 -0.1595 169 LEU C O     
5621 C CB    . LEU C 197 ? 0.7412 1.2347 0.8948 0.2165  0.0049  -0.1563 169 LEU C CB    
5622 C CG    . LEU C 197 ? 0.6533 1.1047 0.7852 0.2254  0.0067  -0.1519 169 LEU C CG    
5623 C CD1   . LEU C 197 ? 0.6424 1.0726 0.7567 0.2223  -0.0026 -0.1474 169 LEU C CD1   
5624 C CD2   . LEU C 197 ? 0.6709 1.1212 0.8074 0.2458  0.0061  -0.1474 169 LEU C CD2   
5625 N N     . CYS C 198 ? 0.7308 1.3052 0.9317 0.1910  0.0128  -0.1699 170 CYS C N     
5626 C CA    . CYS C 198 ? 0.6720 1.2844 0.8914 0.1797  0.0073  -0.1736 170 CYS C CA    
5627 C C     . CYS C 198 ? 0.6972 1.3481 0.9448 0.1837  0.0124  -0.1754 170 CYS C C     
5628 O O     . CYS C 198 ? 0.7179 1.4059 0.9851 0.1849  0.0040  -0.1749 170 CYS C O     
5629 C CB    . CYS C 198 ? 0.6831 1.2860 0.8937 0.1574  0.0111  -0.1802 170 CYS C CB    
5630 S SG    . CYS C 198 ? 0.6636 1.2324 0.8456 0.1510  0.0028  -0.1784 170 CYS C SG    
5631 N N     . ASP C 199 ? 0.7352 1.3786 0.9853 0.1858  0.0261  -0.1772 171 ASP C N     
5632 C CA    . ASP C 199 ? 0.6559 1.3352 0.9329 0.1914  0.0323  -0.1781 171 ASP C CA    
5633 C C     . ASP C 199 ? 0.6226 1.3167 0.9101 0.2140  0.0257  -0.1717 171 ASP C C     
5634 O O     . ASP C 199 ? 0.6250 1.3599 0.9387 0.2188  0.0237  -0.1711 171 ASP C O     
5635 C CB    . ASP C 199 ? 0.5898 1.2543 0.8639 0.1900  0.0491  -0.1809 171 ASP C CB    
5636 C CG    . ASP C 199 ? 0.6304 1.2872 0.8992 0.1674  0.0567  -0.1871 171 ASP C CG    
5637 O OD1   . ASP C 199 ? 0.7262 1.4075 1.0071 0.1524  0.0516  -0.1906 171 ASP C OD1   
5638 O OD2   . ASP C 199 ? 0.5693 1.1953 0.8217 0.1646  0.0675  -0.1884 171 ASP C OD2   
5639 N N     . ALA C 200 ? 0.6862 1.3477 0.9540 0.2281  0.0224  -0.1666 172 ALA C N     
5640 C CA    . ALA C 200 ? 0.6908 1.3627 0.9663 0.2496  0.0152  -0.1600 172 ALA C CA    
5641 C C     . ALA C 200 ? 0.6777 1.3782 0.9641 0.2491  -0.0001 -0.1572 172 ALA C C     
5642 O O     . ALA C 200 ? 0.6606 1.3890 0.9651 0.2635  -0.0055 -0.1529 172 ALA C O     
5643 C CB    . ALA C 200 ? 0.7564 1.3841 1.0067 0.2626  0.0144  -0.1554 172 ALA C CB    
5644 N N     . TYR C 201 ? 0.7136 1.4076 0.9888 0.2332  -0.0072 -0.1593 173 TYR C N     
5645 C CA    . TYR C 201 ? 0.6843 1.4067 0.9688 0.2305  -0.0216 -0.1576 173 TYR C CA    
5646 C C     . TYR C 201 ? 0.6859 1.4578 1.0009 0.2242  -0.0216 -0.1612 173 TYR C C     
5647 O O     . TYR C 201 ? 0.7156 1.5207 1.0489 0.2342  -0.0306 -0.1572 173 TYR C O     
5648 C CB    . TYR C 201 ? 0.6895 1.3927 0.9540 0.2135  -0.0273 -0.1604 173 TYR C CB    
5649 C CG    . TYR C 201 ? 0.6324 1.2986 0.8711 0.2214  -0.0335 -0.1545 173 TYR C CG    
5650 C CD1   . TYR C 201 ? 0.5849 1.2454 0.8224 0.2422  -0.0387 -0.1465 173 TYR C CD1   
5651 C CD2   . TYR C 201 ? 0.6518 1.2888 0.8680 0.2080  -0.0338 -0.1567 173 TYR C CD2   
5652 C CE1   . TYR C 201 ? 0.6228 1.2497 0.8376 0.2486  -0.0442 -0.1407 173 TYR C CE1   
5653 C CE2   . TYR C 201 ? 0.6552 1.2598 0.8492 0.2148  -0.0391 -0.1509 173 TYR C CE2   
5654 C CZ    . TYR C 201 ? 0.6292 1.2292 0.8228 0.2347  -0.0444 -0.1428 173 TYR C CZ    
5655 O OH    . TYR C 201 ? 0.6071 1.1752 0.7794 0.2407  -0.0495 -0.1366 173 TYR C OH    
5656 N N     . GLU C 202 ? 0.6902 1.4681 1.0117 0.2074  -0.0114 -0.1684 174 GLU C N     
5657 C CA    . GLU C 202 ? 0.7076 1.5324 1.0584 0.1982  -0.0112 -0.1721 174 GLU C CA    
5658 C C     . GLU C 202 ? 0.6948 1.5489 1.0708 0.2156  -0.0065 -0.1684 174 GLU C C     
5659 O O     . GLU C 202 ? 0.6522 1.5516 1.0556 0.2146  -0.0113 -0.1684 174 GLU C O     
5660 C CB    . GLU C 202 ? 0.7242 1.5443 1.0745 0.1763  -0.0001 -0.1802 174 GLU C CB    
5661 C CG    . GLU C 202 ? 0.7063 1.5068 1.0369 0.1570  -0.0056 -0.1847 174 GLU C CG    
5662 C CD    . GLU C 202 ? 0.7390 1.5248 1.0643 0.1376  0.0071  -0.1918 174 GLU C CD    
5663 O OE1   . GLU C 202 ? 0.6967 1.4661 1.0194 0.1418  0.0207  -0.1918 174 GLU C OE1   
5664 O OE2   . GLU C 202 ? 0.7721 1.5617 1.0948 0.1183  0.0035  -0.1974 174 GLU C OE2   
5665 N N     . GLU C 203 ? 0.6961 1.5254 1.0636 0.2317  0.0028  -0.1654 175 GLU C N     
5666 C CA    . GLU C 203 ? 0.6821 1.5363 1.0715 0.2504  0.0077  -0.1616 175 GLU C CA    
5667 C C     . GLU C 203 ? 0.6868 1.5546 1.0820 0.2696  -0.0056 -0.1539 175 GLU C C     
5668 O O     . GLU C 203 ? 0.7394 1.6461 1.1612 0.2806  -0.0073 -0.1508 175 GLU C O     
5669 C CB    . GLU C 203 ? 0.7440 1.5655 1.1204 0.2609  0.0226  -0.1617 175 GLU C CB    
5670 C CG    . GLU C 203 ? 0.7404 1.5553 1.1160 0.2447  0.0377  -0.1684 175 GLU C CG    
5671 C CD    . GLU C 203 ? 0.8315 1.6220 1.1983 0.2572  0.0525  -0.1682 175 GLU C CD    
5672 O OE1   . GLU C 203 ? 0.8622 1.6415 1.2244 0.2785  0.0512  -0.1633 175 GLU C OE1   
5673 O OE2   . GLU C 203 ? 0.8391 1.6206 1.2026 0.2457  0.0656  -0.1730 175 GLU C OE2   
5674 N N     . MET C 204 ? 0.7111 1.5479 1.0822 0.2739  -0.0151 -0.1501 176 MET C N     
5675 C CA    . MET C 204 ? 0.7470 1.5946 1.1215 0.2912  -0.0284 -0.1422 176 MET C CA    
5676 C C     . MET C 204 ? 0.7286 1.6177 1.1202 0.2827  -0.0422 -0.1419 176 MET C C     
5677 O O     . MET C 204 ? 0.6930 1.6017 1.0950 0.2962  -0.0520 -0.1348 176 MET C O     
5678 C CB    . MET C 204 ? 0.7787 1.5805 1.1222 0.2972  -0.0340 -0.1379 176 MET C CB    
5679 C CG    . MET C 204 ? 0.7880 1.5501 1.1152 0.3104  -0.0235 -0.1363 176 MET C CG    
5680 S SD    . MET C 204 ? 0.7679 1.4783 1.0605 0.3154  -0.0311 -0.1309 176 MET C SD    
5681 C CE    . MET C 204 ? 0.7369 1.4685 1.0396 0.3355  -0.0460 -0.1209 176 MET C CE    
5682 N N     . ALA C 205 ? 0.7463 1.6438 1.1377 0.2593  -0.0432 -0.1489 177 ALA C N     
5683 C CA    . ALA C 205 ? 0.7413 1.6778 1.1477 0.2497  -0.0567 -0.1496 177 ALA C CA    
5684 C C     . ALA C 205 ? 0.8308 1.8202 1.2741 0.2540  -0.0561 -0.1490 177 ALA C C     
5685 O O     . ALA C 205 ? 0.8299 1.8485 1.2851 0.2528  -0.0688 -0.1456 177 ALA C O     
5686 C CB    . ALA C 205 ? 0.6840 1.6131 1.0796 0.2230  -0.0571 -0.1580 177 ALA C CB    
5687 N N     . LYS C 206 ? 0.7984 1.7923 1.2551 0.2568  -0.0410 -0.1511 178 LYS C N     
5688 C CA    . LYS C 206 ? 0.7535 1.7822 1.2378 0.2577  -0.0381 -0.1481 178 LYS C CA    
5689 C C     . LYS C 206 ? 0.8433 1.8698 1.3306 0.2798  -0.0421 -0.1369 178 LYS C C     
5690 O O     . LYS C 206 ? 0.9785 2.0371 1.4893 0.2818  -0.0437 -0.1329 178 LYS C O     
5691 C CB    . LYS C 206 ? 0.6653 1.6952 1.1602 0.2528  -0.0195 -0.1532 178 LYS C CB    
5692 C CG    . LYS C 206 ? 0.6162 1.6542 1.1136 0.2286  -0.0142 -0.1640 178 LYS C CG    
5693 C CD    . LYS C 206 ? 0.5945 1.6289 1.0992 0.2251  0.0052  -0.1677 178 LYS C CD    
5694 C CE    . LYS C 206 ? 0.6613 1.6849 1.1584 0.1978  0.0112  -0.1760 178 LYS C CE    
5695 N NZ    . LYS C 206 ? 0.6120 1.6275 1.1127 0.1947  0.0307  -0.1790 178 LYS C NZ    
5696 N N     . GLU C 207 ? 0.8548 1.8442 1.3194 0.2958  -0.0436 -0.1317 179 GLU C N     
5697 C CA    . GLU C 207 ? 0.8957 1.8794 1.3614 0.3164  -0.0471 -0.1211 179 GLU C CA    
5698 C C     . GLU C 207 ? 0.8897 1.8960 1.3610 0.3163  -0.0645 -0.1153 179 GLU C C     
5699 O O     . GLU C 207 ? 0.8943 1.8913 1.3493 0.3099  -0.0753 -0.1162 179 GLU C O     
5700 C CB    . GLU C 207 ? 0.9072 1.8422 1.3456 0.3315  -0.0442 -0.1175 179 GLU C CB    
5701 C CG    . GLU C 207 ? 0.9155 1.8242 1.3459 0.3340  -0.0272 -0.1222 179 GLU C CG    
5702 C CD    . GLU C 207 ? 0.8937 1.7536 1.2968 0.3486  -0.0256 -0.1183 179 GLU C CD    
5703 O OE1   . GLU C 207 ? 0.9048 1.7538 1.2998 0.3603  -0.0356 -0.1102 179 GLU C OE1   
5704 O OE2   . GLU C 207 ? 0.8600 1.6917 1.2492 0.3478  -0.0143 -0.1232 179 GLU C OE2   
5705 N N     . PRO C 208 ? 0.9154 1.9513 1.4087 0.3229  -0.0676 -0.1092 180 PRO C N     
5706 C CA    . PRO C 208 ? 0.9430 1.9953 1.4385 0.3257  -0.0842 -0.1022 180 PRO C CA    
5707 C C     . PRO C 208 ? 0.9326 1.9488 1.4026 0.3403  -0.0910 -0.0947 180 PRO C C     
5708 O O     . PRO C 208 ? 0.8917 1.9127 1.3547 0.3391  -0.1052 -0.0905 180 PRO C O     
5709 C CB    . PRO C 208 ? 0.8996 1.9835 1.4231 0.3346  -0.0825 -0.0961 180 PRO C CB    
5710 C CG    . PRO C 208 ? 0.8477 1.9452 1.3884 0.3271  -0.0673 -0.1028 180 PRO C CG    
5711 C CD    . PRO C 208 ? 0.8454 1.9032 1.3636 0.3268  -0.0561 -0.1086 180 PRO C CD    
5712 N N     . ARG C 209 ? 0.9407 1.9200 1.3962 0.3536  -0.0812 -0.0929 181 ARG C N     
5713 C CA    . ARG C 209 ? 0.8891 1.8292 1.3188 0.3660  -0.0861 -0.0864 181 ARG C CA    
5714 C C     . ARG C 209 ? 0.8547 1.7804 1.2632 0.3545  -0.0951 -0.0897 181 ARG C C     
5715 O O     . ARG C 209 ? 0.7455 1.6529 1.1373 0.3611  -0.1047 -0.0828 181 ARG C O     
5716 C CB    . ARG C 209 ? 0.8385 1.7415 1.2564 0.3778  -0.0724 -0.0868 181 ARG C CB    
5717 C CG    . ARG C 209 ? 0.7800 1.6386 1.1719 0.3909  -0.0751 -0.0803 181 ARG C CG    
5718 C CD    . ARG C 209 ? 0.7815 1.6074 1.1638 0.3989  -0.0605 -0.0830 181 ARG C CD    
5719 N NE    . ARG C 209 ? 0.8388 1.6179 1.1943 0.4085  -0.0616 -0.0787 181 ARG C NE    
5720 C CZ    . ARG C 209 ? 0.8542 1.5981 1.1953 0.4138  -0.0508 -0.0813 181 ARG C CZ    
5721 N NH1   . ARG C 209 ? 0.8301 1.5787 1.1796 0.4111  -0.0376 -0.0881 181 ARG C NH1   
5722 N NH2   . ARG C 209 ? 0.8610 1.5634 1.1782 0.4213  -0.0534 -0.0769 181 ARG C NH2   
5723 N N     . TRP C 210 ? 0.8892 1.8228 1.2983 0.3372  -0.0917 -0.0999 182 TRP C N     
5724 C CA    . TRP C 210 ? 0.8308 1.7494 1.2197 0.3260  -0.0984 -0.1041 182 TRP C CA    
5725 C C     . TRP C 210 ? 0.8046 1.7574 1.2034 0.3061  -0.1065 -0.1108 182 TRP C C     
5726 O O     . TRP C 210 ? 0.7571 1.7007 1.1390 0.2978  -0.1151 -0.1127 182 TRP C O     
5727 C CB    . TRP C 210 ? 0.8386 1.7261 1.2129 0.3228  -0.0866 -0.1111 182 TRP C CB    
5728 C CG    . TRP C 210 ? 0.8282 1.6781 1.1901 0.3401  -0.0778 -0.1062 182 TRP C CG    
5729 C CD1   . TRP C 210 ? 0.8014 1.6387 1.1658 0.3434  -0.0629 -0.1101 182 TRP C CD1   
5730 C CD2   . TRP C 210 ? 0.8277 1.6460 1.1713 0.3551  -0.0832 -0.0966 182 TRP C CD2   
5731 N NE1   . TRP C 210 ? 0.7958 1.5956 1.1443 0.3596  -0.0593 -0.1041 182 TRP C NE1   
5732 C CE2   . TRP C 210 ? 0.7954 1.5831 1.1316 0.3667  -0.0715 -0.0958 182 TRP C CE2   
5733 C CE3   . TRP C 210 ? 0.8206 1.6327 1.1528 0.3593  -0.0965 -0.0886 182 TRP C CE3   
5734 C CZ2   . TRP C 210 ? 0.7894 1.5410 1.1080 0.3816  -0.0731 -0.0876 182 TRP C CZ2   
5735 C CZ3   . TRP C 210 ? 0.7836 1.5601 1.0989 0.3743  -0.0974 -0.0800 182 TRP C CZ3   
5736 C CH2   . TRP C 210 ? 0.7789 1.5257 1.0880 0.3850  -0.0860 -0.0797 182 TRP C CH2   
5737 N N     . ALA C 211 ? 0.8171 1.8080 1.2421 0.2980  -0.1043 -0.1142 183 ALA C N     
5738 C CA    . ALA C 211 ? 0.7870 1.8071 1.2218 0.2758  -0.1085 -0.1234 183 ALA C CA    
5739 C C     . ALA C 211 ? 0.7811 1.8058 1.2030 0.2681  -0.1250 -0.1223 183 ALA C C     
5740 O O     . ALA C 211 ? 0.7881 1.8208 1.2060 0.2495  -0.1286 -0.1310 183 ALA C O     
5741 C CB    . ALA C 211 ? 0.7894 1.8510 1.2556 0.2701  -0.1057 -0.1245 183 ALA C CB    
5742 N N     . LEU C 212 ? 0.7641 1.7825 1.1783 0.2818  -0.1347 -0.1118 184 LEU C N     
5743 C CA    . LEU C 212 ? 0.6905 1.7118 1.0906 0.2753  -0.1499 -0.1100 184 LEU C CA    
5744 C C     . LEU C 212 ? 0.7397 1.7287 1.1120 0.2696  -0.1507 -0.1141 184 LEU C C     
5745 O O     . LEU C 212 ? 0.7052 1.7006 1.0678 0.2550  -0.1595 -0.1192 184 LEU C O     
5746 C CB    . LEU C 212 ? 0.5222 1.5406 0.9192 0.2922  -0.1586 -0.0972 184 LEU C CB    
5747 N N     . TYR C 213 ? 0.7579 1.7114 1.1168 0.2807  -0.1416 -0.1122 185 TYR C N     
5748 C CA    . TYR C 213 ? 0.7563 1.6778 1.0895 0.2769  -0.1419 -0.1150 185 TYR C CA    
5749 C C     . TYR C 213 ? 0.7273 1.6414 1.0583 0.2585  -0.1319 -0.1269 185 TYR C C     
5750 O O     . TYR C 213 ? 0.7438 1.6251 1.0491 0.2475  -0.1313 -0.1296 185 TYR C O     
5751 C CB    . TYR C 213 ? 0.7524 1.6332 1.0694 0.2953  -0.1364 -0.1070 185 TYR C CB    
5752 C CG    . TYR C 213 ? 0.7572 1.6318 1.0709 0.3116  -0.1432 -0.0942 185 TYR C CG    
5753 C CD1   . TYR C 213 ? 0.8220 1.6832 1.1162 0.3134  -0.1543 -0.0875 185 TYR C CD1   
5754 C CD2   . TYR C 213 ? 0.7344 1.6156 1.0641 0.3251  -0.1381 -0.0887 185 TYR C CD2   
5755 C CE1   . TYR C 213 ? 0.8524 1.7074 1.1439 0.3278  -0.1600 -0.0756 185 TYR C CE1   
5756 C CE2   . TYR C 213 ? 0.7680 1.6431 1.0952 0.3399  -0.1441 -0.0771 185 TYR C CE2   
5757 C CZ    . TYR C 213 ? 0.8219 1.6840 1.1302 0.3410  -0.1551 -0.0706 185 TYR C CZ    
5758 O OH    . TYR C 213 ? 0.8228 1.6785 1.1289 0.3552  -0.1606 -0.0589 185 TYR C OH    
5759 N N     . MET C 214 ? 0.6786 1.6131 1.0315 0.2527  -0.1223 -0.1327 186 MET C N     
5760 C CA    . MET C 214 ? 0.6193 1.5348 0.9662 0.2346  -0.1092 -0.1421 186 MET C CA    
5761 C C     . MET C 214 ? 0.6660 1.6184 1.0323 0.2145  -0.1105 -0.1507 186 MET C C     
5762 O O     . MET C 214 ? 0.6921 1.6484 1.0695 0.2045  -0.0984 -0.1570 186 MET C O     
5763 C CB    . MET C 214 ? 0.6699 1.5684 1.0215 0.2451  -0.0937 -0.1415 186 MET C CB    
5764 C CG    . MET C 214 ? 0.7176 1.5762 1.0489 0.2634  -0.0920 -0.1339 186 MET C CG    
5765 S SD    . MET C 214 ? 0.8398 1.6748 1.1728 0.2746  -0.0739 -0.1343 186 MET C SD    
5766 C CE    . MET C 214 ? 0.7519 1.5496 1.0628 0.2523  -0.0629 -0.1431 186 MET C CE    
5767 N N     . GLN C 215 ? 0.7098 1.6895 1.0797 0.2078  -0.1253 -0.1510 187 GLN C N     
5768 C CA    . GLN C 215 ? 0.6798 1.6933 1.0663 0.1869  -0.1281 -0.1596 187 GLN C CA    
5769 C C     . GLN C 215 ? 0.7210 1.7060 1.0871 0.1637  -0.1222 -0.1692 187 GLN C C     
5770 O O     . GLN C 215 ? 0.7719 1.7763 1.1513 0.1450  -0.1191 -0.1775 187 GLN C O     
5771 C CB    . GLN C 215 ? 0.6261 1.6765 1.0209 0.1869  -0.1468 -0.1571 187 GLN C CB    
5772 N N     . ASP C 216 ? 0.7208 1.6605 1.0555 0.1646  -0.1205 -0.1680 188 ASP C N     
5773 C CA    . ASP C 216 ? 0.7192 1.6284 1.0329 0.1445  -0.1141 -0.1764 188 ASP C CA    
5774 C C     . ASP C 216 ? 0.6765 1.5458 0.9785 0.1479  -0.0979 -0.1762 188 ASP C C     
5775 O O     . ASP C 216 ? 0.7007 1.5296 0.9756 0.1448  -0.0947 -0.1765 188 ASP C O     
5776 C CB    . ASP C 216 ? 0.7341 1.6231 1.0202 0.1410  -0.1247 -0.1756 188 ASP C CB    
5777 C CG    . ASP C 216 ? 0.7139 1.5820 0.9853 0.1625  -0.1291 -0.1647 188 ASP C CG    
5778 O OD1   . ASP C 216 ? 0.6768 1.5529 0.9621 0.1808  -0.1270 -0.1577 188 ASP C OD1   
5779 O OD2   . ASP C 216 ? 0.7874 1.6305 1.0332 0.1610  -0.1344 -0.1631 188 ASP C OD2   
5780 N N     . VAL C 217 ? 0.6010 1.4820 0.9231 0.1546  -0.0875 -0.1756 189 VAL C N     
5781 C CA    . VAL C 217 ? 0.5689 1.4133 0.8798 0.1604  -0.0728 -0.1746 189 VAL C CA    
5782 C C     . VAL C 217 ? 0.6689 1.4866 0.9651 0.1400  -0.0629 -0.1829 189 VAL C C     
5783 O O     . VAL C 217 ? 0.7337 1.5104 1.0088 0.1420  -0.0546 -0.1819 189 VAL C O     
5784 C CB    . VAL C 217 ? 0.4938 1.3592 0.8298 0.1727  -0.0640 -0.1723 189 VAL C CB    
5785 C CG1   . VAL C 217 ? 0.5555 1.4570 0.9171 0.1571  -0.0593 -0.1794 189 VAL C CG1   
5786 C CG2   . VAL C 217 ? 0.5625 1.3887 0.8845 0.1812  -0.0501 -0.1707 189 VAL C CG2   
5787 N N     . GLU C 218 ? 0.6907 1.5302 0.9970 0.1200  -0.0638 -0.1909 190 GLU C N     
5788 C CA    . GLU C 218 ? 0.6878 1.5021 0.9806 0.1004  -0.0540 -0.1987 190 GLU C CA    
5789 C C     . GLU C 218 ? 0.6655 1.4429 0.9267 0.0949  -0.0581 -0.1994 190 GLU C C     
5790 O O     . GLU C 218 ? 0.6567 1.4039 0.9020 0.0828  -0.0489 -0.2041 190 GLU C O     
5791 C CB    . GLU C 218 ? 0.6823 1.5292 0.9943 0.0799  -0.0545 -0.2071 190 GLU C CB    
5792 C CG    . GLU C 218 ? 0.7286 1.5977 1.0404 0.0704  -0.0704 -0.2101 190 GLU C CG    
5793 C CD    . GLU C 218 ? 0.7299 1.6425 1.0643 0.0834  -0.0829 -0.2046 190 GLU C CD    
5794 O OE1   . GLU C 218 ? 0.6632 1.5853 1.0116 0.1019  -0.0793 -0.1978 190 GLU C OE1   
5795 O OE2   . GLU C 218 ? 0.7532 1.6904 1.0912 0.0754  -0.0964 -0.2072 190 GLU C OE2   
5796 N N     . LYS C 219 ? 0.6618 1.4411 0.9135 0.1038  -0.0714 -0.1946 191 LYS C N     
5797 C CA    . LYS C 219 ? 0.6478 1.3925 0.8696 0.1011  -0.0750 -0.1939 191 LYS C CA    
5798 C C     . LYS C 219 ? 0.6588 1.3682 0.8638 0.1183  -0.0711 -0.1855 191 LYS C C     
5799 O O     . LYS C 219 ? 0.7017 1.3800 0.8821 0.1172  -0.0725 -0.1840 191 LYS C O     
5800 C CB    . LYS C 219 ? 0.5451 1.3098 0.7634 0.1001  -0.0913 -0.1932 191 LYS C CB    
5801 C CG    . LYS C 219 ? 0.4724 1.2611 0.6981 0.0788  -0.0957 -0.2031 191 LYS C CG    
5802 C CD    . LYS C 219 ? 0.4818 1.2864 0.6997 0.0775  -0.1121 -0.2028 191 LYS C CD    
5803 C CE    . LYS C 219 ? 0.5026 1.3281 0.7258 0.0549  -0.1165 -0.2137 191 LYS C CE    
5804 N NZ    . LYS C 219 ? 0.5224 1.3658 0.7380 0.0533  -0.1332 -0.2139 191 LYS C NZ    
5805 N N     . PHE C 220 ? 0.5975 1.3111 0.8153 0.1340  -0.0662 -0.1802 192 PHE C N     
5806 C CA    . PHE C 220 ? 0.5752 1.2540 0.7783 0.1488  -0.0609 -0.1733 192 PHE C CA    
5807 C C     . PHE C 220 ? 0.5366 1.1948 0.7391 0.1455  -0.0452 -0.1764 192 PHE C C     
5808 O O     . PHE C 220 ? 0.5613 1.1966 0.7571 0.1589  -0.0399 -0.1712 192 PHE C O     
5809 C CB    . PHE C 220 ? 0.5467 1.2402 0.7608 0.1708  -0.0673 -0.1646 192 PHE C CB    
5810 C CG    . PHE C 220 ? 0.5684 1.2700 0.7757 0.1776  -0.0822 -0.1589 192 PHE C CG    
5811 C CD1   . PHE C 220 ? 0.6457 1.3855 0.8666 0.1723  -0.0930 -0.1610 192 PHE C CD1   
5812 C CD2   . PHE C 220 ? 0.6272 1.2984 0.8142 0.1892  -0.0855 -0.1512 192 PHE C CD2   
5813 C CE1   . PHE C 220 ? 0.7094 1.4565 0.9226 0.1789  -0.1068 -0.1555 192 PHE C CE1   
5814 C CE2   . PHE C 220 ? 0.6487 1.3270 0.8288 0.1956  -0.0986 -0.1453 192 PHE C CE2   
5815 C CZ    . PHE C 220 ? 0.7111 1.4270 0.9036 0.1908  -0.1092 -0.1475 192 PHE C CZ    
5816 N N     . VAL C 221 ? 0.4804 1.1458 0.6892 0.1278  -0.0380 -0.1846 193 VAL C N     
5817 C CA    . VAL C 221 ? 0.4497 1.0980 0.6584 0.1230  -0.0228 -0.1878 193 VAL C CA    
5818 C C     . VAL C 221 ? 0.5012 1.1248 0.6924 0.1039  -0.0177 -0.1940 193 VAL C C     
5819 O O     . VAL C 221 ? 0.6346 1.2695 0.8246 0.0903  -0.0239 -0.1990 193 VAL C O     
5820 C CB    . VAL C 221 ? 0.5248 1.2090 0.7620 0.1206  -0.0169 -0.1912 193 VAL C CB    
5821 C CG1   . VAL C 221 ? 0.6392 1.3054 0.8747 0.1144  -0.0007 -0.1945 193 VAL C CG1   
5822 C CG2   . VAL C 221 ? 0.6183 1.3260 0.8727 0.1411  -0.0213 -0.1846 193 VAL C CG2   
5823 N N     . SER C 222 ? 0.4485 1.0375 0.6251 0.1034  -0.0065 -0.1937 194 SER C N     
5824 C CA    . SER C 222 ? 0.4606 1.0250 0.6212 0.0863  -0.0002 -0.1991 194 SER C CA    
5825 C C     . SER C 222 ? 0.5419 1.1308 0.7184 0.0681  0.0040  -0.2074 194 SER C C     
5826 O O     . SER C 222 ? 0.5613 1.1757 0.7595 0.0693  0.0089  -0.2085 194 SER C O     
5827 C CB    . SER C 222 ? 0.4649 0.9927 0.6111 0.0895  0.0118  -0.1970 194 SER C CB    
5828 O OG    . SER C 222 ? 0.5087 1.0173 0.6440 0.0725  0.0200  -0.2025 194 SER C OG    
5829 N N     . PRO C 223 ? 0.5453 1.1276 0.7120 0.0511  0.0023  -0.2134 195 PRO C N     
5830 C CA    . PRO C 223 ? 0.5622 1.1669 0.7439 0.0326  0.0059  -0.2216 195 PRO C CA    
5831 C C     . PRO C 223 ? 0.6416 1.2340 0.8263 0.0256  0.0217  -0.2240 195 PRO C C     
5832 O O     . PRO C 223 ? 0.6884 1.3063 0.8931 0.0152  0.0263  -0.2285 195 PRO C O     
5833 C CB    . PRO C 223 ? 0.5203 1.1121 0.6849 0.0177  0.0005  -0.2271 195 PRO C CB    
5834 C CG    . PRO C 223 ? 0.5148 1.0674 0.6531 0.0263  0.0007  -0.2221 195 PRO C CG    
5835 C CD    . PRO C 223 ? 0.4723 1.0249 0.6133 0.0479  -0.0020 -0.2130 195 PRO C CD    
5836 N N     . TYR C 224 ? 0.6084 1.1630 0.7741 0.0307  0.0300  -0.2206 196 TYR C N     
5837 C CA    . TYR C 224 ? 0.6385 1.1783 0.8042 0.0258  0.0451  -0.2218 196 TYR C CA    
5838 C C     . TYR C 224 ? 0.6653 1.2163 0.8444 0.0410  0.0506  -0.2172 196 TYR C C     
5839 O O     . TYR C 224 ? 0.7120 1.2462 0.8873 0.0409  0.0631  -0.2167 196 TYR C O     
5840 C CB    . TYR C 224 ? 0.6460 1.1399 0.7841 0.0243  0.0510  -0.2202 196 TYR C CB    
5841 C CG    . TYR C 224 ? 0.6483 1.1281 0.7703 0.0135  0.0447  -0.2236 196 TYR C CG    
5842 C CD1   . TYR C 224 ? 0.6719 1.1542 0.7948 -0.0064 0.0480  -0.2314 196 TYR C CD1   
5843 C CD2   . TYR C 224 ? 0.6503 1.1139 0.7559 0.0231  0.0358  -0.2191 196 TYR C CD2   
5844 C CE1   . TYR C 224 ? 0.7282 1.1962 0.8348 -0.0157 0.0427  -0.2350 196 TYR C CE1   
5845 C CE2   . TYR C 224 ? 0.6549 1.1055 0.7449 0.0140  0.0308  -0.2221 196 TYR C CE2   
5846 C CZ    . TYR C 224 ? 0.6591 1.1116 0.7492 -0.0051 0.0343  -0.2303 196 TYR C CZ    
5847 O OH    . TYR C 224 ? 0.6511 1.0894 0.7244 -0.0138 0.0297  -0.2339 196 TYR C OH    
5848 N N     . GLN C 225 ? 0.6296 1.2079 0.8235 0.0545  0.0417  -0.2137 197 GLN C N     
5849 C CA    . GLN C 225 ? 0.6219 1.2120 0.8291 0.0701  0.0469  -0.2095 197 GLN C CA    
5850 C C     . GLN C 225 ? 0.6607 1.2722 0.8877 0.0610  0.0586  -0.2135 197 GLN C C     
5851 O O     . GLN C 225 ? 0.7261 1.3243 0.9508 0.0656  0.0707  -0.2121 197 GLN C O     
5852 C CB    . GLN C 225 ? 0.5839 1.2028 0.8054 0.0849  0.0346  -0.2054 197 GLN C CB    
5853 C CG    . GLN C 225 ? 0.5611 1.1909 0.7952 0.1034  0.0391  -0.2006 197 GLN C CG    
5854 C CD    . GLN C 225 ? 0.6088 1.2003 0.8214 0.1180  0.0420  -0.1953 197 GLN C CD    
5855 O OE1   . GLN C 225 ? 0.6283 1.1922 0.8200 0.1189  0.0361  -0.1930 197 GLN C OE1   
5856 N NE2   . GLN C 225 ? 0.6720 1.2616 0.8897 0.1294  0.0514  -0.1933 197 GLN C NE2   
5857 N N     . HIS C 226 ? 0.6448 1.2899 0.8911 0.0476  0.0551  -0.2184 198 HIS C N     
5858 C CA    . HIS C 226 ? 0.6833 1.3531 0.9512 0.0373  0.0654  -0.2220 198 HIS C CA    
5859 C C     . HIS C 226 ? 0.7003 1.3525 0.9593 0.0154  0.0739  -0.2279 198 HIS C C     
5860 O O     . HIS C 226 ? 0.7399 1.4155 1.0177 0.0019  0.0802  -0.2320 198 HIS C O     
5861 C CB    . HIS C 226 ? 0.6538 1.3737 0.9511 0.0353  0.0566  -0.2235 198 HIS C CB    
5862 C CG    . HIS C 226 ? 0.6700 1.4088 0.9770 0.0569  0.0476  -0.2174 198 HIS C CG    
5863 N ND1   . HIS C 226 ? 0.6667 1.4048 0.9787 0.0752  0.0549  -0.2123 198 HIS C ND1   
5864 C CD2   . HIS C 226 ? 0.6532 1.4108 0.9647 0.0634  0.0321  -0.2154 198 HIS C CD2   
5865 C CE1   . HIS C 226 ? 0.6738 1.4291 0.9936 0.0921  0.0443  -0.2074 198 HIS C CE1   
5866 N NE2   . HIS C 226 ? 0.7056 1.4734 1.0254 0.0854  0.0303  -0.2088 198 HIS C NE2   
5867 N N     . SER C 227 ? 0.6998 1.3117 0.9313 0.0116  0.0745  -0.2282 199 SER C N     
5868 C CA    . SER C 227 ? 0.7616 1.3530 0.9825 -0.0081 0.0827  -0.2334 199 SER C CA    
5869 C C     . SER C 227 ? 0.8350 1.4098 1.0532 -0.0081 0.0994  -0.2319 199 SER C C     
5870 O O     . SER C 227 ? 0.9116 1.4627 1.1162 0.0064  0.1036  -0.2268 199 SER C O     
5871 C CB    . SER C 227 ? 0.7865 1.3411 0.9791 -0.0107 0.0775  -0.2337 199 SER C CB    
5872 O OG    . SER C 227 ? 0.8001 1.3302 0.9804 -0.0275 0.0869  -0.2378 199 SER C OG    
5873 N N     . GLU C 228 ? 0.8195 1.4064 1.0502 -0.0247 0.1087  -0.2363 200 GLU C N     
5874 C CA    . GLU C 228 ? 0.8677 1.4383 1.0947 -0.0266 0.1252  -0.2349 200 GLU C CA    
5875 C C     . GLU C 228 ? 0.9133 1.4366 1.1108 -0.0318 0.1310  -0.2346 200 GLU C C     
5876 O O     . GLU C 228 ? 0.9278 1.4304 1.1160 -0.0290 0.1433  -0.2318 200 GLU C O     
5877 C CB    . GLU C 228 ? 0.9084 1.5069 1.1584 -0.0436 0.1337  -0.2391 200 GLU C CB    
5878 N N     . ASP C 229 ? 0.8742 1.3806 1.0567 -0.0389 0.1225  -0.2371 201 ASP C N     
5879 C CA    . ASP C 229 ? 0.8754 1.3375 1.0300 -0.0427 0.1270  -0.2364 201 ASP C CA    
5880 C C     . ASP C 229 ? 0.8396 1.2881 0.9788 -0.0379 0.1137  -0.2359 201 ASP C C     
5881 O O     . ASP C 229 ? 0.8145 1.2607 0.9489 -0.0508 0.1086  -0.2409 201 ASP C O     
5882 C CB    . ASP C 229 ? 0.9001 1.3528 1.0529 -0.0644 0.1361  -0.2417 201 ASP C CB    
5883 C CG    . ASP C 229 ? 0.9129 1.3199 1.0376 -0.0676 0.1415  -0.2404 201 ASP C CG    
5884 O OD1   . ASP C 229 ? 0.9864 1.3696 1.0950 -0.0531 0.1417  -0.2346 201 ASP C OD1   
5885 O OD2   . ASP C 229 ? 0.8341 1.2291 0.9531 -0.0848 0.1453  -0.2451 201 ASP C OD2   
5886 N N     . PRO C 230 ? 0.8293 1.2680 0.9597 -0.0192 0.1081  -0.2299 202 PRO C N     
5887 C CA    . PRO C 230 ? 0.7578 1.1852 0.8743 -0.0139 0.0956  -0.2286 202 PRO C CA    
5888 C C     . PRO C 230 ? 0.7749 1.1650 0.8671 -0.0223 0.0982  -0.2295 202 PRO C C     
5889 O O     . PRO C 230 ? 0.8087 1.1956 0.8929 -0.0270 0.0896  -0.2320 202 PRO C O     
5890 C CB    . PRO C 230 ? 0.7695 1.1917 0.8822 0.0077  0.0917  -0.2213 202 PRO C CB    
5891 C CG    . PRO C 230 ? 0.7889 1.2319 0.9197 0.0138  0.0991  -0.2202 202 PRO C CG    
5892 C CD    . PRO C 230 ? 0.8336 1.2747 0.9682 -0.0022 0.1121  -0.2243 202 PRO C CD    
5893 N N     . VAL C 231 ? 0.7713 1.1333 0.8511 -0.0239 0.1099  -0.2274 203 VAL C N     
5894 C CA    . VAL C 231 ? 0.7647 1.0908 0.8219 -0.0310 0.1131  -0.2276 203 VAL C CA    
5895 C C     . VAL C 231 ? 0.7764 1.1062 0.8354 -0.0508 0.1144  -0.2354 203 VAL C C     
5896 O O     . VAL C 231 ? 0.7838 1.0952 0.8275 -0.0561 0.1107  -0.2373 203 VAL C O     
5897 C CB    . VAL C 231 ? 0.8421 1.1394 0.8870 -0.0282 0.1254  -0.2233 203 VAL C CB    
5898 C CG1   . VAL C 231 ? 0.7908 1.0535 0.8149 -0.0374 0.1302  -0.2237 203 VAL C CG1   
5899 C CG2   . VAL C 231 ? 0.8581 1.1461 0.8967 -0.0089 0.1223  -0.2159 203 VAL C CG2   
5900 N N     . GLY C 232 ? 0.8134 1.1670 0.8910 -0.0622 0.1197  -0.2401 204 GLY C N     
5901 C CA    . GLY C 232 ? 0.8541 1.2114 0.9342 -0.0823 0.1208  -0.2479 204 GLY C CA    
5902 C C     . GLY C 232 ? 0.8060 1.1822 0.8896 -0.0854 0.1067  -0.2525 204 GLY C C     
5903 O O     . GLY C 232 ? 0.8124 1.1733 0.8828 -0.0960 0.1043  -0.2573 204 GLY C O     
5904 N N     . GLU C 233 ? 0.7698 1.1791 0.8704 -0.0758 0.0972  -0.2511 205 GLU C N     
5905 C CA    . GLU C 233 ? 0.6765 1.1066 0.7811 -0.0780 0.0831  -0.2550 205 GLU C CA    
5906 C C     . GLU C 233 ? 0.7157 1.1194 0.7964 -0.0706 0.0760  -0.2527 205 GLU C C     
5907 O O     . GLU C 233 ? 0.7475 1.1503 0.8203 -0.0794 0.0689  -0.2579 205 GLU C O     
5908 C CB    . GLU C 233 ? 0.6486 1.1181 0.7757 -0.0666 0.0747  -0.2523 205 GLU C CB    
5909 C CG    . GLU C 233 ? 0.7275 1.2314 0.8818 -0.0758 0.0793  -0.2557 205 GLU C CG    
5910 C CD    . GLU C 233 ? 0.8271 1.3720 1.0041 -0.0645 0.0697  -0.2533 205 GLU C CD    
5911 O OE1   . GLU C 233 ? 0.8268 1.3758 0.9984 -0.0536 0.0574  -0.2508 205 GLU C OE1   
5912 O OE2   . GLU C 233 ? 0.8405 1.4136 1.0411 -0.0662 0.0747  -0.2535 205 GLU C OE2   
5913 N N     . PHE C 234 ? 0.7373 1.1192 0.8059 -0.0547 0.0779  -0.2448 206 PHE C N     
5914 C CA    . PHE C 234 ? 0.6573 1.0152 0.7046 -0.0470 0.0716  -0.2415 206 PHE C CA    
5915 C C     . PHE C 234 ? 0.6831 1.0077 0.7101 -0.0588 0.0783  -0.2449 206 PHE C C     
5916 O O     . PHE C 234 ? 0.7013 1.0157 0.7144 -0.0612 0.0721  -0.2470 206 PHE C O     
5917 C CB    . PHE C 234 ? 0.6074 0.9511 0.6483 -0.0279 0.0719  -0.2321 206 PHE C CB    
5918 C CG    . PHE C 234 ? 0.5819 0.9117 0.6070 -0.0176 0.0627  -0.2275 206 PHE C CG    
5919 C CD1   . PHE C 234 ? 0.5459 0.8981 0.5759 -0.0143 0.0500  -0.2284 206 PHE C CD1   
5920 C CD2   . PHE C 234 ? 0.6167 0.9117 0.6223 -0.0113 0.0668  -0.2220 206 PHE C CD2   
5921 C CE1   . PHE C 234 ? 0.5134 0.8529 0.5287 -0.0049 0.0422  -0.2237 206 PHE C CE1   
5922 C CE2   . PHE C 234 ? 0.5210 0.8042 0.5132 -0.0022 0.0589  -0.2173 206 PHE C CE2   
5923 C CZ    . PHE C 234 ? 0.4855 0.7906 0.4823 0.0010  0.0469  -0.2181 206 PHE C CZ    
5924 N N     . ARG C 235 ? 0.7561 1.0628 0.7806 -0.0658 0.0912  -0.2452 207 ARG C N     
5925 C CA    . ARG C 235 ? 0.7880 1.0630 0.7942 -0.0774 0.0984  -0.2485 207 ARG C CA    
5926 C C     . ARG C 235 ? 0.7659 1.0519 0.7745 -0.0950 0.0951  -0.2584 207 ARG C C     
5927 O O     . ARG C 235 ? 0.8184 1.0827 0.8093 -0.1010 0.0944  -0.2617 207 ARG C O     
5928 C CB    . ARG C 235 ? 0.8290 1.0854 0.8336 -0.0817 0.1130  -0.2466 207 ARG C CB    
5929 C CG    . ARG C 235 ? 0.8536 1.0763 0.8398 -0.0933 0.1213  -0.2494 207 ARG C CG    
5930 C CD    . ARG C 235 ? 0.8750 1.0795 0.8593 -0.0969 0.1356  -0.2466 207 ARG C CD    
5931 N NE    . ARG C 235 ? 0.8671 1.0465 0.8377 -0.0825 0.1389  -0.2376 207 ARG C NE    
5932 C CZ    . ARG C 235 ? 0.8859 1.0661 0.8613 -0.0741 0.1444  -0.2320 207 ARG C CZ    
5933 N NH1   . ARG C 235 ? 0.7932 0.9981 0.7871 -0.0776 0.1481  -0.2339 207 ARG C NH1   
5934 N NH2   . ARG C 235 ? 0.9668 1.1228 0.9281 -0.0619 0.1461  -0.2243 207 ARG C NH2   
5935 N N     . LEU C 236 ? 0.7514 1.0709 0.7818 -0.1035 0.0929  -0.2633 208 LEU C N     
5936 C CA    . LEU C 236 ? 0.8056 1.1385 0.8396 -0.1207 0.0880  -0.2731 208 LEU C CA    
5937 C C     . LEU C 236 ? 0.8084 1.1518 0.8362 -0.1157 0.0734  -0.2746 208 LEU C C     
5938 O O     . LEU C 236 ? 0.8229 1.1588 0.8395 -0.1272 0.0697  -0.2818 208 LEU C O     
5939 C CB    . LEU C 236 ? 0.8256 1.1946 0.8868 -0.1307 0.0889  -0.2771 208 LEU C CB    
5940 C CG    . LEU C 236 ? 0.8794 1.2672 0.9479 -0.1498 0.0827  -0.2874 208 LEU C CG    
5941 C CD1   . LEU C 236 ? 0.8910 1.2457 0.9414 -0.1662 0.0908  -0.2937 208 LEU C CD1   
5942 C CD2   . LEU C 236 ? 0.9872 1.4141 1.0855 -0.1579 0.0834  -0.2898 208 LEU C CD2   
5943 N N     . LEU C 237 ? 0.7891 1.1488 0.8230 -0.0985 0.0651  -0.2680 209 LEU C N     
5944 C CA    . LEU C 237 ? 0.7703 1.1404 0.7979 -0.0926 0.0512  -0.2683 209 LEU C CA    
5945 C C     . LEU C 237 ? 0.7507 1.0848 0.7506 -0.0892 0.0517  -0.2668 209 LEU C C     
5946 O O     . LEU C 237 ? 0.7874 1.1209 0.7762 -0.0942 0.0442  -0.2717 209 LEU C O     
5947 C CB    . LEU C 237 ? 0.6859 1.0793 0.7262 -0.0742 0.0432  -0.2606 209 LEU C CB    
5948 C CG    . LEU C 237 ? 0.6245 1.0287 0.6582 -0.0660 0.0288  -0.2592 209 LEU C CG    
5949 C CD1   . LEU C 237 ? 0.6343 1.0664 0.6766 -0.0798 0.0197  -0.2682 209 LEU C CD1   
5950 C CD2   . LEU C 237 ? 0.6224 1.0432 0.6664 -0.0464 0.0226  -0.2502 209 LEU C CD2   
5951 N N     . LEU C 238 ? 0.7145 1.0189 0.7029 -0.0805 0.0606  -0.2600 210 LEU C N     
5952 C CA    . LEU C 238 ? 0.6930 0.9638 0.6566 -0.0767 0.0620  -0.2576 210 LEU C CA    
5953 C C     . LEU C 238 ? 0.7852 1.0354 0.7354 -0.0937 0.0681  -0.2662 210 LEU C C     
5954 O O     . LEU C 238 ? 0.8508 1.0889 0.7842 -0.0955 0.0639  -0.2693 210 LEU C O     
5955 C CB    . LEU C 238 ? 0.7008 0.9465 0.6571 -0.0641 0.0698  -0.2481 210 LEU C CB    
5956 C CG    . LEU C 238 ? 0.6162 0.8742 0.5801 -0.0456 0.0635  -0.2390 210 LEU C CG    
5957 C CD1   . LEU C 238 ? 0.5190 0.7494 0.4738 -0.0354 0.0713  -0.2305 210 LEU C CD1   
5958 C CD2   . LEU C 238 ? 0.6203 0.8860 0.5773 -0.0374 0.0512  -0.2370 210 LEU C CD2   
5959 N N     . GLU C 239 ? 0.8210 1.0665 0.7778 -0.1061 0.0783  -0.2702 211 GLU C N     
5960 C CA    . GLU C 239 ? 0.8630 1.0865 0.8071 -0.1226 0.0850  -0.2783 211 GLU C CA    
5961 C C     . GLU C 239 ? 0.8574 1.1006 0.8045 -0.1367 0.0763  -0.2890 211 GLU C C     
5962 O O     . GLU C 239 ? 0.9167 1.1393 0.8473 -0.1476 0.0784  -0.2960 211 GLU C O     
5963 C CB    . GLU C 239 ? 0.9313 1.1451 0.8824 -0.1323 0.0984  -0.2790 211 GLU C CB    
5964 C CG    . GLU C 239 ? 0.9964 1.1818 0.9379 -0.1211 0.1083  -0.2696 211 GLU C CG    
5965 C CD    . GLU C 239 ? 1.0225 1.2060 0.9746 -0.1275 0.1201  -0.2686 211 GLU C CD    
5966 O OE1   . GLU C 239 ? 1.0170 1.2263 0.9876 -0.1383 0.1201  -0.2738 211 GLU C OE1   
5967 O OE2   . GLU C 239 ? 0.9942 1.1511 0.9362 -0.1217 0.1294  -0.2622 211 GLU C OE2   
5968 N N     . SER C 240 ? 0.8378 1.1200 0.8050 -0.1366 0.0664  -0.2905 212 SER C N     
5969 C CA    . SER C 240 ? 0.8089 1.1123 0.7788 -0.1488 0.0560  -0.3001 212 SER C CA    
5970 C C     . SER C 240 ? 0.7652 1.0636 0.7169 -0.1410 0.0456  -0.3000 212 SER C C     
5971 O O     . SER C 240 ? 0.7490 1.0625 0.6990 -0.1505 0.0361  -0.3081 212 SER C O     
5972 C CB    . SER C 240 ? 0.8180 1.1668 0.8166 -0.1501 0.0483  -0.3007 212 SER C CB    
5973 O OG    . SER C 240 ? 0.7686 1.1360 0.7734 -0.1314 0.0393  -0.2926 212 SER C OG    
5974 N N     . GLU C 241 ? 0.8094 1.0875 0.7474 -0.1244 0.0470  -0.2911 213 GLU C N     
5975 C CA    . GLU C 241 ? 0.7742 1.0456 0.6941 -0.1158 0.0385  -0.2897 213 GLU C CA    
5976 C C     . GLU C 241 ? 0.7901 1.0193 0.6842 -0.1139 0.0474  -0.2883 213 GLU C C     
5977 O O     . GLU C 241 ? 0.7527 0.9716 0.6312 -0.1032 0.0431  -0.2841 213 GLU C O     
5978 C CB    . GLU C 241 ? 0.7379 1.0272 0.6658 -0.0965 0.0303  -0.2793 213 GLU C CB    
5979 C CG    . GLU C 241 ? 0.6982 1.0308 0.6498 -0.0963 0.0197  -0.2804 213 GLU C CG    
5980 C CD    . GLU C 241 ? 0.7794 1.1311 0.7285 -0.1076 0.0086  -0.2898 213 GLU C CD    
5981 O OE1   . GLU C 241 ? 0.7923 1.1299 0.7202 -0.1058 0.0041  -0.2913 213 GLU C OE1   
5982 O OE2   . GLU C 241 ? 0.8432 1.2245 0.8116 -0.1183 0.0043  -0.2957 213 GLU C OE2   
5983 N N     . GLY C 242 ? 0.8472 1.0520 0.7369 -0.1237 0.0599  -0.2913 214 GLY C N     
5984 C CA    . GLY C 242 ? 0.9034 1.0683 0.7695 -0.1224 0.0690  -0.2902 214 GLY C CA    
5985 C C     . GLY C 242 ? 0.8926 1.0373 0.7555 -0.1075 0.0766  -0.2783 214 GLY C C     
5986 O O     . GLY C 242 ? 0.9297 1.0449 0.7733 -0.1023 0.0818  -0.2753 214 GLY C O     
5987 N N     . PHE C 243 ? 0.8860 1.0456 0.7668 -0.1004 0.0774  -0.2717 215 PHE C N     
5988 C CA    . PHE C 243 ? 0.9162 1.0581 0.7944 -0.0866 0.0835  -0.2606 215 PHE C CA    
5989 C C     . PHE C 243 ? 0.9874 1.1108 0.8674 -0.0936 0.0968  -0.2604 215 PHE C C     
5990 O O     . PHE C 243 ? 0.9769 1.1095 0.8671 -0.1075 0.1006  -0.2673 215 PHE C O     
5991 C CB    . PHE C 243 ? 0.8780 1.0450 0.7723 -0.0727 0.0760  -0.2528 215 PHE C CB    
5992 C CG    . PHE C 243 ? 0.8406 1.0160 0.7291 -0.0605 0.0650  -0.2483 215 PHE C CG    
5993 C CD1   . PHE C 243 ? 0.8276 0.9816 0.7029 -0.0475 0.0662  -0.2393 215 PHE C CD1   
5994 C CD2   . PHE C 243 ? 0.8096 1.0149 0.7062 -0.0621 0.0533  -0.2527 215 PHE C CD2   
5995 C CE1   . PHE C 243 ? 0.7742 0.9356 0.6443 -0.0365 0.0565  -0.2346 215 PHE C CE1   
5996 C CE2   . PHE C 243 ? 0.7311 0.9436 0.6216 -0.0507 0.0433  -0.2479 215 PHE C CE2   
5997 C CZ    . PHE C 243 ? 0.7153 0.9054 0.5923 -0.0380 0.0452  -0.2388 215 PHE C CZ    
5998 N N     . GLN C 244 ? 1.0039 1.1012 0.8739 -0.0840 0.1039  -0.2519 216 GLN C N     
5999 C CA    . GLN C 244 ? 1.0598 1.1378 0.9299 -0.0875 0.1163  -0.2494 216 GLN C CA    
6000 C C     . GLN C 244 ? 1.0182 1.1040 0.8988 -0.0741 0.1159  -0.2397 216 GLN C C     
6001 O O     . GLN C 244 ? 1.0238 1.0956 0.8962 -0.0609 0.1152  -0.2310 216 GLN C O     
6002 C CB    . GLN C 244 ? 1.1062 1.1464 0.9554 -0.0874 0.1249  -0.2474 216 GLN C CB    
6003 C CG    . GLN C 244 ? 1.1696 1.1879 1.0171 -0.0902 0.1377  -0.2438 216 GLN C CG    
6004 C CD    . GLN C 244 ? 1.1833 1.1654 1.0109 -0.0863 0.1453  -0.2395 216 GLN C CD    
6005 O OE1   . GLN C 244 ? 1.1944 1.1687 1.0111 -0.0775 0.1410  -0.2362 216 GLN C OE1   
6006 N NE2   . GLN C 244 ? 1.2126 1.1728 1.0357 -0.0927 0.1570  -0.2389 216 GLN C NE2   
6007 N N     . VAL C 245 ? 0.9361 1.0446 0.8350 -0.0777 0.1164  -0.2414 217 VAL C N     
6008 C CA    . VAL C 245 ? 0.9301 1.0475 0.8392 -0.0655 0.1162  -0.2335 217 VAL C CA    
6009 C C     . VAL C 245 ? 0.9246 1.0121 0.8234 -0.0622 0.1271  -0.2270 217 VAL C C     
6010 O O     . VAL C 245 ? 0.9859 1.0656 0.8865 -0.0719 0.1370  -0.2294 217 VAL C O     
6011 C CB    . VAL C 245 ? 0.8874 1.0362 0.8183 -0.0706 0.1156  -0.2373 217 VAL C CB    
6012 C CG1   . VAL C 245 ? 0.8393 0.9941 0.7787 -0.0575 0.1166  -0.2294 217 VAL C CG1   
6013 C CG2   . VAL C 245 ? 0.8234 1.0034 0.7651 -0.0730 0.1038  -0.2429 217 VAL C CG2   
6014 N N     . LEU C 246 ? 0.9213 0.9924 0.8096 -0.0488 0.1250  -0.2185 218 LEU C N     
6015 C CA    . LEU C 246 ? 0.9439 0.9868 0.8217 -0.0448 0.1340  -0.2116 218 LEU C CA    
6016 C C     . LEU C 246 ? 0.9711 1.0204 0.8580 -0.0381 0.1366  -0.2065 218 LEU C C     
6017 O O     . LEU C 246 ? 1.0699 1.0996 0.9506 -0.0388 0.1457  -0.2028 218 LEU C O     
6018 C CB    . LEU C 246 ? 0.8891 0.9125 0.7526 -0.0336 0.1305  -0.2042 218 LEU C CB    
6019 C CG    . LEU C 246 ? 0.9316 0.9444 0.7829 -0.0378 0.1290  -0.2080 218 LEU C CG    
6020 C CD1   . LEU C 246 ? 0.8904 0.8859 0.7297 -0.0254 0.1264  -0.1990 218 LEU C CD1   
6021 C CD2   . LEU C 246 ? 1.0208 1.0144 0.8638 -0.0515 0.1395  -0.2140 218 LEU C CD2   
6022 N N     . ARG C 247 ? 0.9542 1.0300 0.8550 -0.0314 0.1289  -0.2062 219 ARG C N     
6023 C CA    . ARG C 247 ? 0.9703 1.0519 0.8785 -0.0231 0.1308  -0.2014 219 ARG C CA    
6024 C C     . ARG C 247 ? 0.8991 1.0139 0.8245 -0.0182 0.1222  -0.2035 219 ARG C C     
6025 O O     . ARG C 247 ? 0.8714 0.9976 0.7981 -0.0133 0.1121  -0.2036 219 ARG C O     
6026 C CB    . ARG C 247 ? 0.9287 0.9886 0.8250 -0.0099 0.1293  -0.1917 219 ARG C CB    
6027 C CG    . ARG C 247 ? 0.9709 1.0302 0.8704 -0.0017 0.1322  -0.1868 219 ARG C CG    
6028 C CD    . ARG C 247 ? 1.0417 1.0761 0.9274 0.0087  0.1310  -0.1777 219 ARG C CD    
6029 N NE    . ARG C 247 ? 1.2067 1.2398 1.0936 0.0177  0.1318  -0.1730 219 ARG C NE    
6030 C CZ    . ARG C 247 ? 1.2011 1.2107 1.0761 0.0223  0.1355  -0.1665 219 ARG C CZ    
6031 N NH1   . ARG C 247 ? 1.1486 1.1348 1.0109 0.0193  0.1391  -0.1632 219 ARG C NH1   
6032 N NH2   . ARG C 247 ? 1.2081 1.2178 1.0838 0.0303  0.1356  -0.1633 219 ARG C NH2   
6033 N N     . CYS C 248 ? 0.8414 0.9717 0.7796 -0.0192 0.1267  -0.2049 220 CYS C N     
6034 C CA    . CYS C 248 ? 0.8423 1.0056 0.7985 -0.0144 0.1197  -0.2068 220 CYS C CA    
6035 C C     . CYS C 248 ? 0.8971 1.0667 0.8616 -0.0091 0.1260  -0.2045 220 CYS C C     
6036 O O     . CYS C 248 ? 0.9727 1.1390 0.9392 -0.0181 0.1366  -0.2068 220 CYS C O     
6037 C CB    . CYS C 248 ? 0.8098 0.9976 0.7786 -0.0276 0.1178  -0.2156 220 CYS C CB    
6038 S SG    . CYS C 248 ? 0.8451 1.0749 0.8354 -0.0209 0.1063  -0.2175 220 CYS C SG    
6039 N N     . ASP C 249 ? 0.8893 1.0671 0.8578 0.0055  0.1199  -0.1999 221 ASP C N     
6040 C CA    . ASP C 249 ? 0.8954 1.0778 0.8698 0.0127  0.1253  -0.1976 221 ASP C CA    
6041 C C     . ASP C 249 ? 0.8175 1.0276 0.8070 0.0238  0.1170  -0.1972 221 ASP C C     
6042 O O     . ASP C 249 ? 0.8059 1.0255 0.7975 0.0286  0.1062  -0.1966 221 ASP C O     
6043 C CB    . ASP C 249 ? 0.9538 1.1056 0.9111 0.0216  0.1284  -0.1905 221 ASP C CB    
6044 C CG    . ASP C 249 ? 1.0528 1.1758 0.9941 0.0127  0.1353  -0.1895 221 ASP C CG    
6045 O OD1   . ASP C 249 ? 1.0981 1.2184 1.0404 0.0018  0.1456  -0.1926 221 ASP C OD1   
6046 O OD2   . ASP C 249 ? 1.0668 1.1700 0.9949 0.0167  0.1306  -0.1852 221 ASP C OD2   
6047 N N     . LEU C 250 ? 0.8101 1.0327 0.8097 0.0283  0.1226  -0.1973 222 LEU C N     
6048 C CA    . LEU C 250 ? 0.7105 0.9580 0.7245 0.0404  0.1165  -0.1965 222 LEU C CA    
6049 C C     . LEU C 250 ? 0.6773 0.9112 0.6847 0.0532  0.1207  -0.1918 222 LEU C C     
6050 O O     . LEU C 250 ? 0.6965 0.9201 0.6997 0.0495  0.1317  -0.1921 222 LEU C O     
6051 C CB    . LEU C 250 ? 0.6390 0.9219 0.6757 0.0332  0.1192  -0.2022 222 LEU C CB    
6052 C CG    . LEU C 250 ? 0.6174 0.9292 0.6716 0.0457  0.1145  -0.2015 222 LEU C CG    
6053 C CD1   . LEU C 250 ? 0.6194 0.9401 0.6751 0.0543  0.1002  -0.1994 222 LEU C CD1   
6054 C CD2   . LEU C 250 ? 0.5576 0.9034 0.6346 0.0370  0.1196  -0.2068 222 LEU C CD2   
6055 N N     . GLY C 251 ? 0.6845 0.9176 0.6903 0.0679  0.1120  -0.1876 223 GLY C N     
6056 C CA    . GLY C 251 ? 0.7370 0.9562 0.7354 0.0806  0.1145  -0.1837 223 GLY C CA    
6057 C C     . GLY C 251 ? 0.7099 0.9423 0.7158 0.0960  0.1055  -0.1812 223 GLY C C     
6058 O O     . GLY C 251 ? 0.6742 0.9176 0.6853 0.0985  0.0951  -0.1803 223 GLY C O     
6059 N N     . PRO C 252 ? 0.6696 0.9003 0.6757 0.1068  0.1095  -0.1800 224 PRO C N     
6060 C CA    . PRO C 252 ? 0.6270 0.8663 0.6386 0.1228  0.1015  -0.1774 224 PRO C CA    
6061 C C     . PRO C 252 ? 0.6162 0.8268 0.6101 0.1310  0.0934  -0.1715 224 PRO C C     
6062 O O     . PRO C 252 ? 0.6409 0.8229 0.6175 0.1286  0.0966  -0.1692 224 PRO C O     
6063 C CB    . PRO C 252 ? 0.7110 0.9558 0.7270 0.1302  0.1108  -0.1789 224 PRO C CB    
6064 C CG    . PRO C 252 ? 0.7764 0.9978 0.7776 0.1219  0.1214  -0.1793 224 PRO C CG    
6065 C CD    . PRO C 252 ? 0.6953 0.9157 0.6958 0.1054  0.1221  -0.1811 224 PRO C CD    
6066 N N     . GLN C 253 ? 0.5594 0.7783 0.5583 0.1407  0.0825  -0.1686 225 GLN C N     
6067 C CA    . GLN C 253 ? 0.5995 0.7939 0.5840 0.1488  0.0740  -0.1626 225 GLN C CA    
6068 C C     . GLN C 253 ? 0.5714 0.7708 0.5606 0.1653  0.0687  -0.1602 225 GLN C C     
6069 O O     . GLN C 253 ? 0.5750 0.8001 0.5802 0.1707  0.0702  -0.1629 225 GLN C O     
6070 C CB    . GLN C 253 ? 0.6682 0.8629 0.6509 0.1433  0.0652  -0.1602 225 GLN C CB    
6071 C CG    . GLN C 253 ? 0.6985 0.8906 0.6779 0.1272  0.0704  -0.1634 225 GLN C CG    
6072 C CD    . GLN C 253 ? 0.7581 0.9172 0.7182 0.1234  0.0720  -0.1595 225 GLN C CD    
6073 O OE1   . GLN C 253 ? 0.8163 0.9553 0.7658 0.1321  0.0675  -0.1541 225 GLN C OE1   
6074 N NE2   . GLN C 253 ? 0.7052 0.8584 0.6610 0.1102  0.0783  -0.1622 225 GLN C NE2   
6075 N N     . LYS C 254 ? 0.5746 0.7490 0.5500 0.1734  0.0624  -0.1547 226 LYS C N     
6076 C CA    . LYS C 254 ? 0.5734 0.7452 0.5495 0.1891  0.0576  -0.1521 226 LYS C CA    
6077 C C     . LYS C 254 ? 0.5921 0.7499 0.5609 0.1944  0.0458  -0.1455 226 LYS C C     
6078 O O     . LYS C 254 ? 0.6055 0.7405 0.5607 0.1888  0.0437  -0.1420 226 LYS C O     
6079 C CB    . LYS C 254 ? 0.6490 0.7987 0.6127 0.1946  0.0645  -0.1529 226 LYS C CB    
6080 C CG    . LYS C 254 ? 0.6406 0.8077 0.6140 0.1964  0.0753  -0.1586 226 LYS C CG    
6081 C CD    . LYS C 254 ? 0.7521 0.8989 0.7134 0.2071  0.0795  -0.1588 226 LYS C CD    
6082 C CE    . LYS C 254 ? 0.7551 0.8867 0.7043 0.1990  0.0905  -0.1615 226 LYS C CE    
6083 N NZ    . LYS C 254 ? 0.7264 0.8467 0.6673 0.2095  0.0969  -0.1636 226 LYS C NZ    
6084 N N     . VAL C 255 ? 0.5543 0.7265 0.5328 0.2052  0.0384  -0.1432 227 VAL C N     
6085 C CA    . VAL C 255 ? 0.5668 0.7267 0.5394 0.2118  0.0273  -0.1362 227 VAL C CA    
6086 C C     . VAL C 255 ? 0.6087 0.7530 0.5760 0.2264  0.0254  -0.1338 227 VAL C C     
6087 O O     . VAL C 255 ? 0.6251 0.7852 0.6030 0.2362  0.0271  -0.1361 227 VAL C O     
6088 C CB    . VAL C 255 ? 0.5215 0.7080 0.5075 0.2130  0.0196  -0.1346 227 VAL C CB    
6089 C CG1   . VAL C 255 ? 0.5588 0.7302 0.5360 0.2155  0.0094  -0.1270 227 VAL C CG1   
6090 C CG2   . VAL C 255 ? 0.4899 0.6980 0.4844 0.1992  0.0235  -0.1397 227 VAL C CG2   
6091 N N     . PHE C 256 ? 0.5852 0.6984 0.5363 0.2278  0.0218  -0.1293 228 PHE C N     
6092 C CA    . PHE C 256 ? 0.5941 0.6867 0.5366 0.2398  0.0202  -0.1277 228 PHE C CA    
6093 C C     . PHE C 256 ? 0.5861 0.6722 0.5283 0.2491  0.0090  -0.1206 228 PHE C C     
6094 O O     . PHE C 256 ? 0.5932 0.6762 0.5332 0.2440  0.0024  -0.1153 228 PHE C O     
6095 C CB    . PHE C 256 ? 0.6308 0.6919 0.5548 0.2348  0.0234  -0.1275 228 PHE C CB    
6096 C CG    . PHE C 256 ? 0.6217 0.6559 0.5335 0.2452  0.0187  -0.1245 228 PHE C CG    
6097 C CD1   . PHE C 256 ? 0.6803 0.7133 0.5922 0.2567  0.0223  -0.1282 228 PHE C CD1   
6098 C CD2   . PHE C 256 ? 0.5911 0.6011 0.4914 0.2432  0.0107  -0.1180 228 PHE C CD2   
6099 C CE1   . PHE C 256 ? 0.6980 0.7042 0.5973 0.2659  0.0179  -0.1261 228 PHE C CE1   
6100 C CE2   . PHE C 256 ? 0.6220 0.6066 0.5111 0.2516  0.0059  -0.1154 228 PHE C CE2   
6101 C CZ    . PHE C 256 ? 0.6783 0.6600 0.5662 0.2629  0.0093  -0.1198 228 PHE C CZ    
6102 N N     . PHE C 257 ? 0.6176 0.7013 0.5615 0.2631  0.0074  -0.1204 229 PHE C N     
6103 C CA    . PHE C 257 ? 0.6296 0.7042 0.5723 0.2733  -0.0026 -0.1135 229 PHE C CA    
6104 C C     . PHE C 257 ? 0.6037 0.6500 0.5340 0.2832  -0.0027 -0.1134 229 PHE C C     
6105 O O     . PHE C 257 ? 0.5739 0.6232 0.5057 0.2904  0.0043  -0.1191 229 PHE C O     
6106 C CB    . PHE C 257 ? 0.6506 0.7553 0.6108 0.2821  -0.0061 -0.1125 229 PHE C CB    
6107 C CG    . PHE C 257 ? 0.6154 0.7506 0.5884 0.2723  -0.0055 -0.1143 229 PHE C CG    
6108 C CD1   . PHE C 257 ? 0.6102 0.7676 0.5932 0.2667  0.0034  -0.1217 229 PHE C CD1   
6109 C CD2   . PHE C 257 ? 0.6077 0.7486 0.5819 0.2683  -0.0136 -0.1087 229 PHE C CD2   
6110 C CE1   . PHE C 257 ? 0.5544 0.7385 0.5486 0.2568  0.0034  -0.1237 229 PHE C CE1   
6111 C CE2   . PHE C 257 ? 0.5591 0.7264 0.5431 0.2591  -0.0134 -0.1109 229 PHE C CE2   
6112 C CZ    . PHE C 257 ? 0.5042 0.6928 0.4983 0.2531  -0.0052 -0.1187 229 PHE C CZ    
6113 N N     . PRO C 258 ? 0.6096 0.6281 0.5273 0.2839  -0.0101 -0.1074 230 PRO C N     
6114 C CA    . PRO C 258 ? 0.6664 0.6549 0.5700 0.2914  -0.0103 -0.1082 230 PRO C CA    
6115 C C     . PRO C 258 ? 0.6989 0.6889 0.6072 0.3080  -0.0119 -0.1083 230 PRO C C     
6116 O O     . PRO C 258 ? 0.7977 0.7741 0.6984 0.3154  -0.0070 -0.1131 230 PRO C O     
6117 C CB    . PRO C 258 ? 0.6570 0.6190 0.5486 0.2858  -0.0188 -0.1008 230 PRO C CB    
6118 C CG    . PRO C 258 ? 0.6076 0.5876 0.5096 0.2822  -0.0247 -0.0945 230 PRO C CG    
6119 C CD    . PRO C 258 ? 0.6104 0.6232 0.5258 0.2770  -0.0183 -0.0997 230 PRO C CD    
6120 N N     . THR C 259 ? 0.6271 0.6327 0.5469 0.3145  -0.0184 -0.1030 231 THR C N     
6121 C CA    . THR C 259 ? 0.6747 0.6815 0.5993 0.3312  -0.0204 -0.1021 231 THR C CA    
6122 C C     . THR C 259 ? 0.6737 0.7180 0.6175 0.3370  -0.0151 -0.1060 231 THR C C     
6123 O O     . THR C 259 ? 0.6700 0.7394 0.6236 0.3273  -0.0109 -0.1091 231 THR C O     
6124 C CB    . THR C 259 ? 0.6805 0.6783 0.6049 0.3363  -0.0316 -0.0925 231 THR C CB    
6125 O OG1   . THR C 259 ? 0.7228 0.7507 0.6616 0.3332  -0.0351 -0.0887 231 THR C OG1   
6126 C CG2   . THR C 259 ? 0.6888 0.6553 0.5975 0.3272  -0.0371 -0.0876 231 THR C CG2   
6127 N N     . ALA C 260 ? 0.7255 0.7731 0.6750 0.3532  -0.0154 -0.1058 232 ALA C N     
6128 C CA    . ALA C 260 ? 0.7274 0.8114 0.6964 0.3605  -0.0109 -0.1088 232 ALA C CA    
6129 C C     . ALA C 260 ? 0.7009 0.8126 0.6849 0.3597  -0.0187 -0.1028 232 ALA C C     
6130 O O     . ALA C 260 ? 0.6762 0.8222 0.6761 0.3554  -0.0157 -0.1057 232 ALA C O     
6131 C CB    . ALA C 260 ? 0.8040 0.8807 0.7735 0.3738  -0.0082 -0.1087 232 ALA C CB    
6132 N N     . GLU C 261 ? 0.7009 0.7982 0.6797 0.3633  -0.0287 -0.0944 233 GLU C N     
6133 C CA    . GLU C 261 ? 0.6955 0.8184 0.6872 0.3652  -0.0364 -0.0883 233 GLU C CA    
6134 C C     . GLU C 261 ? 0.6866 0.8205 0.6785 0.3483  -0.0390 -0.0871 233 GLU C C     
6135 O O     . GLU C 261 ? 0.7254 0.8903 0.7306 0.3463  -0.0420 -0.0859 233 GLU C O     
6136 C CB    . GLU C 261 ? 0.7373 0.8412 0.7234 0.3763  -0.0455 -0.0790 233 GLU C CB    
6137 C CG    . GLU C 261 ? 0.8392 0.9699 0.8385 0.3804  -0.0531 -0.0721 233 GLU C CG    
6138 C CD    . GLU C 261 ? 0.9704 1.0826 0.9649 0.3878  -0.0595 -0.0625 233 GLU C CD    
6139 O OE1   . GLU C 261 ? 1.1215 1.2020 1.1042 0.3907  -0.0575 -0.0622 233 GLU C OE1   
6140 O OE2   . GLU C 261 ? 0.8346 0.9637 0.8367 0.3904  -0.0663 -0.0554 233 GLU C OE2   
6141 N N     . THR C 262 ? 0.6649 0.7742 0.6422 0.3362  -0.0381 -0.0874 234 THR C N     
6142 C CA    . THR C 262 ? 0.6220 0.7420 0.5995 0.3203  -0.0385 -0.0875 234 THR C CA    
6143 C C     . THR C 262 ? 0.6328 0.7819 0.6220 0.3129  -0.0306 -0.0958 234 THR C C     
6144 O O     . THR C 262 ? 0.6200 0.7911 0.6164 0.3036  -0.0322 -0.0961 234 THR C O     
6145 C CB    . THR C 262 ? 0.5352 0.6236 0.4956 0.3096  -0.0380 -0.0863 234 THR C CB    
6146 O OG1   . THR C 262 ? 0.5755 0.6483 0.5285 0.3090  -0.0299 -0.0931 234 THR C OG1   
6147 C CG2   . THR C 262 ? 0.5441 0.6060 0.4943 0.3147  -0.0466 -0.0773 234 THR C CG2   
6148 N N     . HIS C 263 ? 0.6530 0.8023 0.6441 0.3165  -0.0219 -0.1027 235 HIS C N     
6149 C CA    . HIS C 263 ? 0.5933 0.7729 0.5983 0.3112  -0.0140 -0.1100 235 HIS C CA    
6150 C C     . HIS C 263 ? 0.6018 0.8175 0.6265 0.3190  -0.0178 -0.1088 235 HIS C C     
6151 O O     . HIS C 263 ? 0.5755 0.8209 0.6130 0.3106  -0.0158 -0.1125 235 HIS C O     
6152 C CB    . HIS C 263 ? 0.6244 0.7951 0.6263 0.3152  -0.0036 -0.1167 235 HIS C CB    
6153 C CG    . HIS C 263 ? 0.5911 0.7931 0.6084 0.3110  0.0053  -0.1237 235 HIS C CG    
6154 N ND1   . HIS C 263 ? 0.5353 0.7506 0.5558 0.2947  0.0091  -0.1274 235 HIS C ND1   
6155 C CD2   . HIS C 263 ? 0.5824 0.8050 0.6132 0.3208  0.0115  -0.1275 235 HIS C CD2   
6156 C CE1   . HIS C 263 ? 0.5790 0.8217 0.6145 0.2939  0.0169  -0.1331 235 HIS C CE1   
6157 N NE2   . HIS C 263 ? 0.6177 0.8664 0.6603 0.3097  0.0187  -0.1331 235 HIS C NE2   
6158 N N     . ARG C 264 ? 0.6337 0.8472 0.6610 0.3348  -0.0236 -0.1034 236 ARG C N     
6159 C CA    . ARG C 264 ? 0.5676 0.8152 0.6137 0.3439  -0.0280 -0.1012 236 ARG C CA    
6160 C C     . ARG C 264 ? 0.5679 0.8262 0.6152 0.3390  -0.0384 -0.0948 236 ARG C C     
6161 O O     . ARG C 264 ? 0.5765 0.8685 0.6381 0.3349  -0.0407 -0.0961 236 ARG C O     
6162 C CB    . ARG C 264 ? 0.6228 0.8628 0.6709 0.3640  -0.0293 -0.0978 236 ARG C CB    
6163 C CG    . ARG C 264 ? 0.6203 0.8970 0.6894 0.3755  -0.0326 -0.0957 236 ARG C CG    
6164 C CD    . ARG C 264 ? 0.6574 0.9217 0.7264 0.3924  -0.0320 -0.0922 236 ARG C CD    
6165 N NE    . ARG C 264 ? 0.7276 1.0240 0.8154 0.4000  -0.0351 -0.0885 236 ARG C NE    
6166 C CZ    . ARG C 264 ? 0.7427 1.0473 0.8337 0.4035  -0.0454 -0.0801 236 ARG C CZ    
6167 N NH1   . ARG C 264 ? 0.7642 1.0479 0.8415 0.4000  -0.0534 -0.0742 236 ARG C NH1   
6168 N NH2   . ARG C 264 ? 0.6693 1.0037 0.7777 0.4102  -0.0476 -0.0771 236 ARG C NH2   
6169 N N     . GLU C 265 ? 0.5809 0.8110 0.6132 0.3391  -0.0450 -0.0879 237 GLU C N     
6170 C CA    . GLU C 265 ? 0.5596 0.7982 0.5914 0.3356  -0.0546 -0.0810 237 GLU C CA    
6171 C C     . GLU C 265 ? 0.5426 0.7944 0.5743 0.3177  -0.0532 -0.0851 237 GLU C C     
6172 O O     . GLU C 265 ? 0.5177 0.7893 0.5540 0.3143  -0.0597 -0.0822 237 GLU C O     
6173 C CB    . GLU C 265 ? 0.5529 0.7570 0.5685 0.3389  -0.0607 -0.0725 237 GLU C CB    
6174 C CG    . GLU C 265 ? 0.6478 0.8384 0.6630 0.3569  -0.0641 -0.0671 237 GLU C CG    
6175 C CD    . GLU C 265 ? 0.7574 0.9782 0.7881 0.3692  -0.0696 -0.0633 237 GLU C CD    
6176 O OE1   . GLU C 265 ? 0.7399 0.9821 0.7754 0.3643  -0.0757 -0.0599 237 GLU C OE1   
6177 O OE2   . GLU C 265 ? 0.8122 1.0350 0.8495 0.3832  -0.0676 -0.0635 237 GLU C OE2   
6178 N N     . PHE C 266 ? 0.5402 0.7807 0.5658 0.3062  -0.0448 -0.0917 238 PHE C N     
6179 C CA    . PHE C 266 ? 0.4986 0.7511 0.5243 0.2894  -0.0425 -0.0962 238 PHE C CA    
6180 C C     . PHE C 266 ? 0.4906 0.7828 0.5350 0.2869  -0.0409 -0.1019 238 PHE C C     
6181 O O     . PHE C 266 ? 0.5108 0.8219 0.5588 0.2779  -0.0448 -0.1025 238 PHE C O     
6182 C CB    . PHE C 266 ? 0.4839 0.7139 0.4986 0.2787  -0.0336 -0.1013 238 PHE C CB    
6183 C CG    . PHE C 266 ? 0.4728 0.7117 0.4866 0.2617  -0.0303 -0.1059 238 PHE C CG    
6184 C CD1   . PHE C 266 ? 0.4771 0.7045 0.4801 0.2536  -0.0348 -0.1017 238 PHE C CD1   
6185 C CD2   . PHE C 266 ? 0.4679 0.7265 0.4916 0.2540  -0.0224 -0.1143 238 PHE C CD2   
6186 C CE1   . PHE C 266 ? 0.4601 0.6942 0.4614 0.2386  -0.0315 -0.1062 238 PHE C CE1   
6187 C CE2   . PHE C 266 ? 0.4596 0.7246 0.4818 0.2382  -0.0193 -0.1187 238 PHE C CE2   
6188 C CZ    . PHE C 266 ? 0.4560 0.7081 0.4666 0.2308  -0.0239 -0.1148 238 PHE C CZ    
6189 N N     . LEU C 267 ? 0.4851 0.7906 0.5415 0.2945  -0.0351 -0.1062 239 LEU C N     
6190 C CA    . LEU C 267 ? 0.4801 0.8253 0.5565 0.2923  -0.0334 -0.1113 239 LEU C CA    
6191 C C     . LEU C 267 ? 0.4812 0.8528 0.5687 0.2999  -0.0441 -0.1060 239 LEU C C     
6192 O O     . LEU C 267 ? 0.4757 0.8815 0.5782 0.2944  -0.0455 -0.1096 239 LEU C O     
6193 C CB    . LEU C 267 ? 0.4855 0.8383 0.5723 0.3005  -0.0244 -0.1160 239 LEU C CB    
6194 C CG    . LEU C 267 ? 0.4830 0.8218 0.5633 0.2898  -0.0126 -0.1232 239 LEU C CG    
6195 C CD1   . LEU C 267 ? 0.4913 0.8331 0.5788 0.3004  -0.0036 -0.1267 239 LEU C CD1   
6196 C CD2   . LEU C 267 ? 0.4720 0.8324 0.5595 0.2722  -0.0095 -0.1291 239 LEU C CD2   
6197 N N     . LYS C 268 ? 0.5048 0.8616 0.5853 0.3121  -0.0519 -0.0974 240 LYS C N     
6198 C CA    . LYS C 268 ? 0.4938 0.8731 0.5819 0.3185  -0.0627 -0.0913 240 LYS C CA    
6199 C C     . LYS C 268 ? 0.4824 0.8708 0.5655 0.3036  -0.0677 -0.0918 240 LYS C C     
6200 O O     . LYS C 268 ? 0.4805 0.9005 0.5748 0.3025  -0.0740 -0.0918 240 LYS C O     
6201 C CB    . LYS C 268 ? 0.5340 0.8903 0.6127 0.3333  -0.0694 -0.0814 240 LYS C CB    
6202 C CG    . LYS C 268 ? 0.5521 0.9136 0.6413 0.3523  -0.0689 -0.0790 240 LYS C CG    
6203 C CD    . LYS C 268 ? 0.6098 0.9492 0.6894 0.3659  -0.0766 -0.0686 240 LYS C CD    
6204 C CE    . LYS C 268 ? 0.6660 1.0087 0.7552 0.3849  -0.0758 -0.0660 240 LYS C CE    
6205 N NZ    . LYS C 268 ? 0.7180 1.0310 0.7942 0.3913  -0.0816 -0.0551 240 LYS C NZ    
6206 N N     . SER C 269 ? 0.4783 0.8395 0.5444 0.2923  -0.0651 -0.0923 241 SER C N     
6207 C CA    . SER C 269 ? 0.4725 0.8381 0.5313 0.2792  -0.0693 -0.0924 241 SER C CA    
6208 C C     . SER C 269 ? 0.4689 0.8593 0.5371 0.2647  -0.0648 -0.1021 241 SER C C     
6209 O O     . SER C 269 ? 0.5722 0.9843 0.6435 0.2579  -0.0706 -0.1033 241 SER C O     
6210 C CB    . SER C 269 ? 0.4785 0.8074 0.5171 0.2726  -0.0673 -0.0894 241 SER C CB    
6211 O OG    . SER C 269 ? 0.5330 0.8491 0.5677 0.2617  -0.0573 -0.0967 241 SER C OG    
6212 N N     . VAL C 270 ? 0.4613 0.8484 0.5336 0.2595  -0.0545 -0.1093 242 VAL C N     
6213 C CA    . VAL C 270 ? 0.4547 0.8608 0.5346 0.2442  -0.0489 -0.1184 242 VAL C CA    
6214 C C     . VAL C 270 ? 0.4683 0.9142 0.5713 0.2479  -0.0499 -0.1219 242 VAL C C     
6215 O O     . VAL C 270 ? 0.5006 0.9645 0.6138 0.2369  -0.0440 -0.1297 242 VAL C O     
6216 C CB    . VAL C 270 ? 0.4807 0.8642 0.5534 0.2360  -0.0370 -0.1238 242 VAL C CB    
6217 C CG1   . VAL C 270 ? 0.4624 0.8079 0.5135 0.2330  -0.0367 -0.1196 242 VAL C CG1   
6218 C CG2   . VAL C 270 ? 0.4787 0.8614 0.5597 0.2473  -0.0305 -0.1249 242 VAL C CG2   
6219 N N     . CYS C 271 ? 0.5028 0.9631 0.6146 0.2634  -0.0575 -0.1158 243 CYS C N     
6220 C CA    . CYS C 271 ? 0.5269 1.0279 0.6618 0.2683  -0.0601 -0.1177 243 CYS C CA    
6221 C C     . CYS C 271 ? 0.5937 1.1195 0.7316 0.2621  -0.0711 -0.1168 243 CYS C C     
6222 O O     . CYS C 271 ? 0.6321 1.1548 0.7633 0.2707  -0.0808 -0.1090 243 CYS C O     
6223 C CB    . CYS C 271 ? 0.5618 1.0653 0.7051 0.2893  -0.0620 -0.1114 243 CYS C CB    
6224 S SG    . CYS C 271 ? 0.7261 1.2804 0.9001 0.2974  -0.0639 -0.1131 243 CYS C SG    
6225 N N     . ALA C 272 ? 0.6382 1.1879 0.7853 0.2470  -0.0696 -0.1246 244 ALA C N     
6226 C CA    . ALA C 272 ? 0.5898 1.1585 0.7355 0.2376  -0.0793 -0.1256 244 ALA C CA    
6227 C C     . ALA C 272 ? 0.5965 1.2044 0.7605 0.2469  -0.0898 -0.1222 244 ALA C C     
6228 O O     . ALA C 272 ? 0.6328 1.2568 0.7945 0.2409  -0.0995 -0.1221 244 ALA C O     
6229 C CB    . ALA C 272 ? 0.5719 1.1487 0.7192 0.2166  -0.0738 -0.1358 244 ALA C CB    
6230 N N     . PHE C 273 ? 0.6134 1.2368 0.7948 0.2615  -0.0883 -0.1195 245 PHE C N     
6231 C CA    . PHE C 273 ? 0.6381 1.3010 0.8392 0.2711  -0.0978 -0.1160 245 PHE C CA    
6232 C C     . PHE C 273 ? 0.6660 1.3214 0.8633 0.2918  -0.1055 -0.1048 245 PHE C C     
6233 O O     . PHE C 273 ? 0.6844 1.3711 0.8967 0.3016  -0.1144 -0.1005 245 PHE C O     
6234 C CB    . PHE C 273 ? 0.6084 1.3010 0.8357 0.2734  -0.0909 -0.1206 245 PHE C CB    
6235 C CG    . PHE C 273 ? 0.6202 1.3374 0.8589 0.2536  -0.0879 -0.1304 245 PHE C CG    
6236 C CD1   . PHE C 273 ? 0.6516 1.4079 0.9043 0.2474  -0.0983 -0.1319 245 PHE C CD1   
6237 C CD2   . PHE C 273 ? 0.6290 1.3305 0.8645 0.2410  -0.0750 -0.1379 245 PHE C CD2   
6238 C CE1   . PHE C 273 ? 0.7022 1.4804 0.9655 0.2282  -0.0958 -0.1412 245 PHE C CE1   
6239 C CE2   . PHE C 273 ? 0.6385 1.3614 0.8845 0.2223  -0.0720 -0.1467 245 PHE C CE2   
6240 C CZ    . PHE C 273 ? 0.6866 1.4477 0.9468 0.2156  -0.0824 -0.1485 245 PHE C CZ    
6241 N N     . LEU C 274 ? 0.6853 1.3002 0.8634 0.2987  -0.1026 -0.0997 246 LEU C N     
6242 C CA    . LEU C 274 ? 0.7292 1.3345 0.9042 0.3187  -0.1088 -0.0890 246 LEU C CA    
6243 C C     . LEU C 274 ? 0.7736 1.3888 0.9417 0.3206  -0.1224 -0.0820 246 LEU C C     
6244 O O     . LEU C 274 ? 0.7653 1.3891 0.9384 0.3372  -0.1299 -0.0733 246 LEU C O     
6245 C CB    . LEU C 274 ? 0.7014 1.2600 0.8573 0.3238  -0.1024 -0.0857 246 LEU C CB    
6246 C CG    . LEU C 274 ? 0.6759 1.2238 0.8389 0.3319  -0.0913 -0.0886 246 LEU C CG    
6247 C CD1   . LEU C 274 ? 0.6955 1.1962 0.8374 0.3345  -0.0862 -0.0858 246 LEU C CD1   
6248 C CD2   . LEU C 274 ? 0.6931 1.2637 0.8746 0.3515  -0.0941 -0.0837 246 LEU C CD2   
6249 N N     . TYR C 275 ? 0.7758 1.3897 0.9318 0.3043  -0.1256 -0.0856 247 TYR C N     
6250 C CA    . TYR C 275 ? 0.7792 1.4015 0.9262 0.3056  -0.1381 -0.0793 247 TYR C CA    
6251 C C     . TYR C 275 ? 0.7695 1.4383 0.9364 0.3096  -0.1480 -0.0788 247 TYR C C     
6252 O O     . TYR C 275 ? 0.7486 1.4273 0.9108 0.3162  -0.1594 -0.0713 247 TYR C O     
6253 C CB    . TYR C 275 ? 0.7525 1.3608 0.8806 0.2871  -0.1380 -0.0841 247 TYR C CB    
6254 C CG    . TYR C 275 ? 0.7605 1.3977 0.8975 0.2697  -0.1388 -0.0947 247 TYR C CG    
6255 C CD1   . TYR C 275 ? 0.7461 1.3815 0.8893 0.2569  -0.1279 -0.1048 247 TYR C CD1   
6256 C CD2   . TYR C 275 ? 0.7686 1.4335 0.9064 0.2657  -0.1504 -0.0945 247 TYR C CD2   
6257 C CE1   . TYR C 275 ? 0.7407 1.4010 0.8920 0.2402  -0.1285 -0.1144 247 TYR C CE1   
6258 C CE2   . TYR C 275 ? 0.7432 1.4333 0.8885 0.2489  -0.1516 -0.1046 247 TYR C CE2   
6259 C CZ    . TYR C 275 ? 0.7509 1.4383 0.9033 0.2361  -0.1405 -0.1145 247 TYR C CZ    
6260 O OH    . TYR C 275 ? 0.7481 1.4594 0.9080 0.2187  -0.1416 -0.1245 247 TYR C OH    
6261 N N     . ARG C 276 ? 0.7550 1.4529 0.9442 0.3058  -0.1439 -0.0860 248 ARG C N     
6262 C CA    . ARG C 276 ? 0.7360 1.4809 0.9469 0.3089  -0.1531 -0.0858 248 ARG C CA    
6263 C C     . ARG C 276 ? 0.8005 1.5465 1.0231 0.3254  -0.1516 -0.0771 248 ARG C C     
6264 O O     . ARG C 276 ? 0.8469 1.6176 1.0801 0.3275  -0.1587 -0.0729 248 ARG C O     
6265 C CB    . ARG C 276 ? 0.6838 1.4560 0.9118 0.2923  -0.1481 -0.0975 248 ARG C CB    
6266 C CG    . ARG C 276 ? 0.6585 1.4237 0.8719 0.2697  -0.1482 -0.1059 248 ARG C CG    
6267 C CD    . ARG C 276 ? 0.6205 1.4138 0.8525 0.2537  -0.1437 -0.1169 248 ARG C CD    
6268 N NE    . ARG C 276 ? 0.7080 1.4941 0.9257 0.2321  -0.1439 -0.1253 248 ARG C NE    
6269 C CZ    . ARG C 276 ? 0.7654 1.5728 0.9949 0.2146  -0.1414 -0.1354 248 ARG C CZ    
6270 N NH1   . ARG C 276 ? 0.7601 1.5990 1.0170 0.2154  -0.1380 -0.1383 248 ARG C NH1   
6271 N NH2   . ARG C 276 ? 0.8733 1.6697 1.0868 0.1959  -0.1419 -0.1426 248 ARG C NH2   
6272 N N     . ILE C 277 ? 0.7985 1.5169 1.0184 0.3365  -0.1424 -0.0745 249 ILE C N     
6273 C CA    . ILE C 277 ? 0.7857 1.5035 1.0169 0.3512  -0.1389 -0.0679 249 ILE C CA    
6274 C C     . ILE C 277 ? 0.8601 1.5508 1.0755 0.3631  -0.1444 -0.0552 249 ILE C C     
6275 O O     . ILE C 277 ? 0.8899 1.5462 1.0844 0.3639  -0.1440 -0.0521 249 ILE C O     
6276 C CB    . ILE C 277 ? 0.7319 1.4341 0.9682 0.3563  -0.1254 -0.0726 249 ILE C CB    
6277 C CG1   . ILE C 277 ? 0.7239 1.4509 0.9746 0.3430  -0.1191 -0.0852 249 ILE C CG1   
6278 C CG2   . ILE C 277 ? 0.7854 1.4905 1.0346 0.3707  -0.1216 -0.0668 249 ILE C CG2   
6279 C CD1   . ILE C 277 ? 0.7618 1.5352 1.0365 0.3366  -0.1228 -0.0883 249 ILE C CD1   
6280 N N     . PRO C 278 ? 0.8565 1.5615 1.0816 0.3721  -0.1495 -0.0474 250 PRO C N     
6281 C CA    . PRO C 278 ? 0.8359 1.5137 1.0476 0.3842  -0.1532 -0.0353 250 PRO C CA    
6282 C C     . PRO C 278 ? 0.8935 1.5345 1.0982 0.3949  -0.1437 -0.0330 250 PRO C C     
6283 O O     . PRO C 278 ? 0.8880 1.5286 1.1013 0.3955  -0.1341 -0.0400 250 PRO C O     
6284 C CB    . PRO C 278 ? 0.7804 1.4871 1.0090 0.3915  -0.1592 -0.0292 250 PRO C CB    
6285 C CG    . PRO C 278 ? 0.8097 1.5594 1.0553 0.3793  -0.1626 -0.0375 250 PRO C CG    
6286 C CD    . PRO C 278 ? 0.8358 1.5843 1.0843 0.3701  -0.1533 -0.0492 250 PRO C CD    
6287 N N     . GLU C 279 ? 0.8912 1.5009 1.0800 0.4029  -0.1464 -0.0230 251 GLU C N     
6288 C CA    . GLU C 279 ? 0.9106 1.4803 1.0887 0.4110  -0.1385 -0.0208 251 GLU C CA    
6289 C C     . GLU C 279 ? 0.8845 1.4583 1.0780 0.4223  -0.1311 -0.0216 251 GLU C C     
6290 O O     . GLU C 279 ? 0.9360 1.4876 1.1261 0.4251  -0.1217 -0.0259 251 GLU C O     
6291 C CB    . GLU C 279 ? 0.8874 1.4258 1.0474 0.4166  -0.1436 -0.0093 251 GLU C CB    
6292 C CG    . GLU C 279 ? 0.9659 1.4607 1.1131 0.4232  -0.1367 -0.0068 251 GLU C CG    
6293 C CD    . GLU C 279 ? 1.0352 1.5106 1.1715 0.4144  -0.1306 -0.0147 251 GLU C CD    
6294 O OE1   . GLU C 279 ? 1.0180 1.5020 1.1485 0.4030  -0.1340 -0.0183 251 GLU C OE1   
6295 O OE2   . GLU C 279 ? 1.0878 1.5389 1.2210 0.4188  -0.1225 -0.0175 251 GLU C OE2   
6296 N N     . GLU C 280 ? 0.8421 1.4440 1.0525 0.4291  -0.1349 -0.0175 252 GLU C N     
6297 C CA    . GLU C 280 ? 0.8771 1.4840 1.1028 0.4408  -0.1278 -0.0174 252 GLU C CA    
6298 C C     . GLU C 280 ? 0.9538 1.5752 1.1921 0.4360  -0.1179 -0.0286 252 GLU C C     
6299 O O     . GLU C 280 ? 1.0084 1.6207 1.2526 0.4450  -0.1089 -0.0300 252 GLU C O     
6300 C CB    . GLU C 280 ? 0.8246 1.4637 1.0679 0.4477  -0.1346 -0.0111 252 GLU C CB    
6301 N N     . GLN C 281 ? 0.9208 1.5641 1.1630 0.4219  -0.1189 -0.0368 253 GLN C N     
6302 C CA    . GLN C 281 ? 0.9395 1.5973 1.1938 0.4156  -0.1092 -0.0476 253 GLN C CA    
6303 C C     . GLN C 281 ? 0.9256 1.5608 1.1642 0.4055  -0.1046 -0.0549 253 GLN C C     
6304 O O     . GLN C 281 ? 0.9248 1.5698 1.1715 0.3992  -0.0961 -0.0642 253 GLN C O     
6305 C CB    . GLN C 281 ? 0.8619 1.5693 1.1387 0.4067  -0.1130 -0.0521 253 GLN C CB    
6306 N N     . LYS C 282 ? 0.9090 1.5142 1.1255 0.4037  -0.1096 -0.0508 254 LYS C N     
6307 C CA    . LYS C 282 ? 0.9450 1.5272 1.1464 0.3949  -0.1054 -0.0570 254 LYS C CA    
6308 C C     . LYS C 282 ? 0.9556 1.5104 1.1527 0.4004  -0.0934 -0.0609 254 LYS C C     
6309 O O     . LYS C 282 ? 0.9865 1.5447 1.1866 0.3932  -0.0855 -0.0703 254 LYS C O     
6310 C CB    . LYS C 282 ? 0.9064 1.4603 1.0854 0.3932  -0.1130 -0.0501 254 LYS C CB    
6311 C CG    . LYS C 282 ? 0.8847 1.4606 1.0619 0.3823  -0.1227 -0.0504 254 LYS C CG    
6312 C CD    . LYS C 282 ? 0.8745 1.4187 1.0281 0.3802  -0.1278 -0.0440 254 LYS C CD    
6313 C CE    . LYS C 282 ? 0.8373 1.4010 0.9865 0.3686  -0.1364 -0.0454 254 LYS C CE    
6314 N NZ    . LYS C 282 ? 0.9172 1.4512 1.0437 0.3674  -0.1411 -0.0377 254 LYS C NZ    
6315 N N     . ASP C 283 ? 0.9572 1.4838 1.1465 0.4129  -0.0918 -0.0539 255 ASP C N     
6316 C CA    . ASP C 283 ? 0.9634 1.4609 1.1459 0.4182  -0.0810 -0.0574 255 ASP C CA    
6317 C C     . ASP C 283 ? 0.9255 1.4475 1.1273 0.4201  -0.0713 -0.0644 255 ASP C C     
6318 O O     . ASP C 283 ? 0.9007 1.4065 1.0981 0.4193  -0.0610 -0.0709 255 ASP C O     
6319 C CB    . ASP C 283 ? 0.9685 1.4323 1.1394 0.4307  -0.0821 -0.0485 255 ASP C CB    
6320 C CG    . ASP C 283 ? 1.0215 1.4572 1.1725 0.4280  -0.0901 -0.0414 255 ASP C CG    
6321 O OD1   . ASP C 283 ? 1.0484 1.4806 1.1904 0.4171  -0.0921 -0.0447 255 ASP C OD1   
6322 O OD2   . ASP C 283 ? 1.1238 1.5410 1.2684 0.4367  -0.0940 -0.0324 255 ASP C OD2   
6323 N N     . ASP C 284 ? 0.8841 1.4449 1.1070 0.4222  -0.0743 -0.0629 256 ASP C N     
6324 C CA    . ASP C 284 ? 0.8782 1.4666 1.1216 0.4223  -0.0652 -0.0692 256 ASP C CA    
6325 C C     . ASP C 284 ? 0.8974 1.5096 1.1487 0.4068  -0.0621 -0.0792 256 ASP C C     
6326 O O     . ASP C 284 ? 0.8791 1.4992 1.1394 0.4043  -0.0511 -0.0864 256 ASP C O     
6327 C CB    . ASP C 284 ? 0.8308 1.4530 1.0953 0.4297  -0.0697 -0.0636 256 ASP C CB    
6328 N N     . PHE C 285 ? 0.8716 1.4946 1.1190 0.3961  -0.0713 -0.0798 257 PHE C N     
6329 C CA    . PHE C 285 ? 0.8851 1.5283 1.1386 0.3805  -0.0686 -0.0897 257 PHE C CA    
6330 C C     . PHE C 285 ? 0.8901 1.5006 1.1274 0.3765  -0.0592 -0.0960 257 PHE C C     
6331 O O     . PHE C 285 ? 0.8807 1.5031 1.1258 0.3677  -0.0502 -0.1051 257 PHE C O     
6332 C CB    . PHE C 285 ? 0.8769 1.5363 1.1276 0.3706  -0.0812 -0.0886 257 PHE C CB    
6333 C CG    . PHE C 285 ? 0.8233 1.5092 1.0832 0.3538  -0.0798 -0.0990 257 PHE C CG    
6334 C CD1   . PHE C 285 ? 0.8364 1.4916 1.0775 0.3396  -0.0734 -0.1046 257 PHE C CD1   
6335 C CD2   . PHE C 285 ? 0.7791 1.5094 1.0605 0.3459  -0.0839 -0.1018 257 PHE C CD2   
6336 C CE1   . PHE C 285 ? 0.8526 1.5195 1.0957 0.3184  -0.0705 -0.1128 257 PHE C CE1   
6337 C CE2   . PHE C 285 ? 0.7587 1.5051 1.0445 0.3257  -0.0818 -0.1109 257 PHE C CE2   
6338 C CZ    . PHE C 285 ? 0.8220 1.5337 1.0871 0.3112  -0.0746 -0.1161 257 PHE C CZ    
6339 N N     . PHE C 286 ? 0.8894 1.4583 1.1042 0.3824  -0.0610 -0.0912 258 PHE C N     
6340 C CA    . PHE C 286 ? 0.8681 1.4037 1.0660 0.3785  -0.0531 -0.0965 258 PHE C CA    
6341 C C     . PHE C 286 ? 0.8317 1.3571 1.0324 0.3837  -0.0397 -0.1008 258 PHE C C     
6342 O O     . PHE C 286 ? 0.8473 1.3674 1.0453 0.3748  -0.0301 -0.1089 258 PHE C O     
6343 C CB    . PHE C 286 ? 0.8328 1.3268 1.0069 0.3833  -0.0589 -0.0892 258 PHE C CB    
6344 C CG    . PHE C 286 ? 0.7123 1.1697 0.8657 0.3727  -0.0533 -0.0932 258 PHE C CG    
6345 C CD1   . PHE C 286 ? 0.6603 1.1217 0.8105 0.3523  -0.0501 -0.0996 258 PHE C CD1   
6346 C CD2   . PHE C 286 ? 0.6612 1.0779 0.7971 0.3813  -0.0511 -0.0902 258 PHE C CD2   
6347 C CE1   . PHE C 286 ? 0.6101 1.0365 0.7406 0.3416  -0.0448 -0.1024 258 PHE C CE1   
6348 C CE2   . PHE C 286 ? 0.5895 0.9719 0.7058 0.3698  -0.0464 -0.0932 258 PHE C CE2   
6349 C CZ    . PHE C 286 ? 0.5720 0.9599 0.6860 0.3503  -0.0431 -0.0991 258 PHE C CZ    
6350 N N     . ASP C 287 ? 0.7955 1.3156 0.9998 0.3968  -0.0383 -0.0952 259 ASP C N     
6351 C CA    . ASP C 287 ? 0.8506 1.3611 1.0569 0.4024  -0.0256 -0.0990 259 ASP C CA    
6352 C C     . ASP C 287 ? 0.8532 1.4025 1.0817 0.3952  -0.0175 -0.1063 259 ASP C C     
6353 O O     . ASP C 287 ? 0.8374 1.3788 1.0639 0.3919  -0.0054 -0.1130 259 ASP C O     
6354 C CB    . ASP C 287 ? 0.9608 1.4607 1.1681 0.4182  -0.0263 -0.0915 259 ASP C CB    
6355 C CG    . ASP C 287 ? 0.9466 1.4008 1.1299 0.4247  -0.0307 -0.0856 259 ASP C CG    
6356 O OD1   . ASP C 287 ? 0.9045 1.3495 1.0775 0.4203  -0.0402 -0.0817 259 ASP C OD1   
6357 O OD2   . ASP C 287 ? 0.9335 1.3610 1.1083 0.4338  -0.0244 -0.0849 259 ASP C OD2   
6358 N N     . ASP C 288 ? 0.8433 1.4344 1.0926 0.3920  -0.0241 -0.1049 260 ASP C N     
6359 C CA    . ASP C 288 ? 0.8632 1.4934 1.1349 0.3827  -0.0175 -0.1117 260 ASP C CA    
6360 C C     . ASP C 288 ? 0.8563 1.4852 1.1224 0.3669  -0.0126 -0.1209 260 ASP C C     
6361 O O     . ASP C 288 ? 0.8422 1.4823 1.1170 0.3599  -0.0011 -0.1279 260 ASP C O     
6362 C CB    . ASP C 288 ? 0.8607 1.5343 1.1539 0.3806  -0.0277 -0.1082 260 ASP C CB    
6363 C CG    . ASP C 288 ? 0.8931 1.6075 1.2131 0.3751  -0.0205 -0.1126 260 ASP C CG    
6364 O OD1   . ASP C 288 ? 0.9489 1.6574 1.2726 0.3800  -0.0079 -0.1147 260 ASP C OD1   
6365 O OD2   . ASP C 288 ? 0.9010 1.6529 1.2377 0.3652  -0.0276 -0.1139 260 ASP C OD2   
6366 N N     . TRP C 289 ? 0.8747 1.4864 1.1244 0.3592  -0.0208 -0.1203 261 TRP C N     
6367 C CA    . TRP C 289 ? 0.8374 1.4320 1.0734 0.3379  -0.0162 -0.1265 261 TRP C CA    
6368 C C     . TRP C 289 ? 0.8099 1.3651 1.0275 0.3388  -0.0046 -0.1296 261 TRP C C     
6369 O O     . TRP C 289 ? 0.7986 1.3530 1.0162 0.3267  0.0060  -0.1363 261 TRP C O     
6370 C CB    . TRP C 289 ? 0.7758 1.3560 0.9957 0.3283  -0.0277 -0.1233 261 TRP C CB    
6371 C CG    . TRP C 289 ? 0.7214 1.2952 0.9325 0.3056  -0.0248 -0.1296 261 TRP C CG    
6372 C CD1   . TRP C 289 ? 0.7115 1.3123 0.9368 0.2904  -0.0200 -0.1365 261 TRP C CD1   
6373 C CD2   . TRP C 289 ? 0.7216 1.2591 0.9079 0.2955  -0.0265 -0.1292 261 TRP C CD2   
6374 N NE1   . TRP C 289 ? 0.7252 1.3072 0.9350 0.2719  -0.0183 -0.1407 261 TRP C NE1   
6375 C CE2   . TRP C 289 ? 0.7170 1.2608 0.9031 0.2750  -0.0222 -0.1362 261 TRP C CE2   
6376 C CE3   . TRP C 289 ? 0.7160 1.2165 0.8807 0.3017  -0.0310 -0.1234 261 TRP C CE3   
6377 C CZ2   . TRP C 289 ? 0.6994 1.2140 0.8645 0.2617  -0.0220 -0.1375 261 TRP C CZ2   
6378 C CZ3   . TRP C 289 ? 0.6564 1.1296 0.8014 0.2880  -0.0310 -0.1244 261 TRP C CZ3   
6379 C CH2   . TRP C 289 ? 0.6856 1.1660 0.8309 0.2687  -0.0264 -0.1314 261 TRP C CH2   
6380 N N     . LEU C 290 ? 0.8504 1.3723 1.0517 0.3528  -0.0065 -0.1247 262 LEU C N     
6381 C CA    . LEU C 290 ? 0.7924 1.2740 0.9733 0.3532  0.0027  -0.1274 262 LEU C CA    
6382 C C     . LEU C 290 ? 0.8068 1.2977 0.9978 0.3592  0.0165  -0.1326 262 LEU C C     
6383 O O     . LEU C 290 ? 0.8444 1.3164 1.0243 0.3507  0.0266  -0.1380 262 LEU C O     
6384 C CB    . LEU C 290 ? 0.7397 1.1858 0.9028 0.3675  -0.0032 -0.1210 262 LEU C CB    
6385 C CG    . LEU C 290 ? 0.6188 1.0429 0.7650 0.3605  -0.0142 -0.1158 262 LEU C CG    
6386 C CD1   . LEU C 290 ? 0.5459 0.9265 0.6711 0.3710  -0.0158 -0.1114 262 LEU C CD1   
6387 C CD2   . LEU C 290 ? 0.6590 1.0774 0.7965 0.3384  -0.0121 -0.1205 262 LEU C CD2   
6388 N N     . GLN C 291 ? 0.7997 1.3166 1.0099 0.3720  0.0171  -0.1300 263 GLN C N     
6389 C CA    . GLN C 291 ? 0.8397 1.3616 1.0577 0.3752  0.0303  -0.1330 263 GLN C CA    
6390 C C     . GLN C 291 ? 0.8828 1.4333 1.1149 0.3607  0.0394  -0.1409 263 GLN C C     
6391 O O     . GLN C 291 ? 0.9252 1.4635 1.1515 0.3572  0.0522  -0.1457 263 GLN C O     
6392 C CB    . GLN C 291 ? 0.8370 1.3796 1.0725 0.3882  0.0283  -0.1268 263 GLN C CB    
6393 C CG    . GLN C 291 ? 0.9056 1.4775 1.1619 0.3875  0.0400  -0.1301 263 GLN C CG    
6394 C CD    . GLN C 291 ? 0.9640 1.5575 1.2387 0.4008  0.0375  -0.1236 263 GLN C CD    
6395 O OE1   . GLN C 291 ? 0.9349 1.5517 1.2218 0.4026  0.0260  -0.1186 263 GLN C OE1   
6396 N NE2   . GLN C 291 ? 0.9714 1.5567 1.2474 0.4101  0.0485  -0.1235 263 GLN C NE2   
6397 N N     . ARG C 292 ? 0.8601 1.4464 1.1094 0.3504  0.0327  -0.1421 264 ARG C N     
6398 C CA    . ARG C 292 ? 0.8411 1.4498 1.1018 0.3315  0.0400  -0.1484 264 ARG C CA    
6399 C C     . ARG C 292 ? 0.8170 1.3917 1.0544 0.3141  0.0447  -0.1526 264 ARG C C     
6400 O O     . ARG C 292 ? 0.8138 1.3990 1.0569 0.2996  0.0538  -0.1581 264 ARG C O     
6401 C CB    . ARG C 292 ? 0.8539 1.5028 1.1348 0.3218  0.0296  -0.1476 264 ARG C CB    
6402 C CG    . ARG C 292 ? 0.8666 1.5581 1.1744 0.3126  0.0371  -0.1522 264 ARG C CG    
6403 C CD    . ARG C 292 ? 0.8594 1.5959 1.1916 0.3119  0.0254  -0.1496 264 ARG C CD    
6404 N NE    . ARG C 292 ? 0.8382 1.5967 1.1888 0.3302  0.0251  -0.1441 264 ARG C NE    
6405 C CZ    . ARG C 292 ? 0.8622 1.6106 1.2074 0.3446  0.0150  -0.1359 264 ARG C CZ    
6406 N NH1   . ARG C 292 ? 0.8707 1.5960 1.1971 0.3467  0.0044  -0.1333 264 ARG C NH1   
6407 N NH2   . ARG C 292 ? 0.9278 1.6891 1.2867 0.3572  0.0159  -0.1299 264 ARG C NH2   
6408 N N     . LEU C 293 ? 0.8380 1.3729 1.0501 0.3152  0.0390  -0.1498 265 LEU C N     
6409 C CA    . LEU C 293 ? 0.8386 1.3419 1.0291 0.2992  0.0426  -0.1531 265 LEU C CA    
6410 C C     . LEU C 293 ? 0.8789 1.3586 1.0578 0.3014  0.0566  -0.1568 265 LEU C C     
6411 O O     . LEU C 293 ? 0.8462 1.3206 1.0202 0.2864  0.0650  -0.1616 265 LEU C O     
6412 C CB    . LEU C 293 ? 0.8139 1.2848 0.9829 0.2997  0.0316  -0.1483 265 LEU C CB    
6413 C CG    . LEU C 293 ? 0.7735 1.2638 0.9491 0.2920  0.0190  -0.1456 265 LEU C CG    
6414 C CD1   . LEU C 293 ? 0.7020 1.1604 0.8565 0.2937  0.0090  -0.1400 265 LEU C CD1   
6415 C CD2   . LEU C 293 ? 0.6993 1.2067 0.8811 0.2707  0.0221  -0.1514 265 LEU C CD2   
6416 N N     . GLU C 294 ? 0.9233 1.3874 1.0964 0.3199  0.0593  -0.1548 266 GLU C N     
6417 C CA    . GLU C 294 ? 0.9211 1.3650 1.0833 0.3234  0.0728  -0.1587 266 GLU C CA    
6418 C C     . GLU C 294 ? 0.8795 1.3580 1.0636 0.3228  0.0850  -0.1629 266 GLU C C     
6419 O O     . GLU C 294 ? 0.8999 1.3667 1.0761 0.3191  0.0977  -0.1670 266 GLU C O     
6420 C CB    . GLU C 294 ? 0.9875 1.4036 1.1361 0.3436  0.0719  -0.1559 266 GLU C CB    
6421 C CG    . GLU C 294 ? 1.1652 1.5385 1.2873 0.3419  0.0634  -0.1528 266 GLU C CG    
6422 C CD    . GLU C 294 ? 1.3556 1.6980 1.4636 0.3580  0.0611  -0.1487 266 GLU C CD    
6423 O OE1   . GLU C 294 ? 1.3688 1.7176 1.4847 0.3675  0.0666  -0.1475 266 GLU C OE1   
6424 O OE2   . GLU C 294 ? 1.3466 1.6563 1.4351 0.3589  0.0536  -0.1459 266 GLU C OE2   
6425 N N     . LYS C 295 ? 0.8794 1.4007 1.0909 0.3261  0.0815  -0.1614 267 LYS C N     
6426 C CA    . LYS C 295 ? 0.9313 1.4903 1.1667 0.3213  0.0921  -0.1651 267 LYS C CA    
6427 C C     . LYS C 295 ? 0.9273 1.4869 1.1600 0.2975  0.0971  -0.1697 267 LYS C C     
6428 O O     . LYS C 295 ? 0.9119 1.4697 1.1435 0.2920  0.1109  -0.1736 267 LYS C O     
6429 C CB    . LYS C 295 ? 0.9095 1.5139 1.1743 0.3261  0.0843  -0.1617 267 LYS C CB    
6430 C CG    . LYS C 295 ? 0.8792 1.5243 1.1709 0.3182  0.0937  -0.1643 267 LYS C CG    
6431 C CD    . LYS C 295 ? 0.8829 1.5722 1.2029 0.3207  0.0839  -0.1605 267 LYS C CD    
6432 C CE    . LYS C 295 ? 0.9445 1.6757 1.2921 0.3101  0.0923  -0.1632 267 LYS C CE    
6433 N NZ    . LYS C 295 ? 0.9152 1.6903 1.2907 0.3113  0.0819  -0.1593 267 LYS C NZ    
6434 N N     . LEU C 296 ? 0.8897 1.4508 1.1203 0.2834  0.0864  -0.1691 268 LEU C N     
6435 C CA    . LEU C 296 ? 0.7691 1.3282 0.9957 0.2607  0.0899  -0.1733 268 LEU C CA    
6436 C C     . LEU C 296 ? 0.7899 1.3021 0.9862 0.2545  0.0940  -0.1744 268 LEU C C     
6437 O O     . LEU C 296 ? 0.7499 1.2555 0.9401 0.2365  0.0980  -0.1777 268 LEU C O     
6438 C CB    . LEU C 296 ? 0.6937 1.2709 0.9282 0.2489  0.0767  -0.1725 268 LEU C CB    
6439 C CG    . LEU C 296 ? 0.6287 1.2561 0.8947 0.2516  0.0720  -0.1719 268 LEU C CG    
6440 C CD1   . LEU C 296 ? 0.6574 1.2965 0.9259 0.2448  0.0562  -0.1699 268 LEU C CD1   
6441 C CD2   . LEU C 296 ? 0.6419 1.2992 0.9280 0.2387  0.0831  -0.1767 268 LEU C CD2   
6442 N N     . LYS C 297 ? 0.8397 1.3193 1.0169 0.2689  0.0929  -0.1718 269 LYS C N     
6443 C CA    . LYS C 297 ? 0.8213 1.2567 0.9699 0.2650  0.0967  -0.1725 269 LYS C CA    
6444 C C     . LYS C 297 ? 0.7714 1.1899 0.9069 0.2489  0.0889  -0.1719 269 LYS C C     
6445 O O     . LYS C 297 ? 0.7726 1.1720 0.8946 0.2359  0.0950  -0.1743 269 LYS C O     
6446 C CB    . LYS C 297 ? 0.8560 1.2873 1.0015 0.2602  0.1129  -0.1769 269 LYS C CB    
6447 C CG    . LYS C 297 ? 0.8456 1.2885 1.0003 0.2774  0.1221  -0.1776 269 LYS C CG    
6448 C CD    . LYS C 297 ? 0.8195 1.2558 0.9682 0.2725  0.1386  -0.1816 269 LYS C CD    
6449 C CE    . LYS C 297 ? 0.8397 1.2875 0.9976 0.2889  0.1481  -0.1816 269 LYS C CE    
6450 N NZ    . LYS C 297 ? 0.8793 1.3179 1.0300 0.2824  0.1640  -0.1839 269 LYS C NZ    
6451 N N     . GLY C 298 ? 0.6958 1.1213 0.8349 0.2506  0.0754  -0.1682 270 GLY C N     
6452 C CA    . GLY C 298 ? 0.6895 1.0961 0.8141 0.2385  0.0674  -0.1668 270 GLY C CA    
6453 C C     . GLY C 298 ? 0.7030 1.0701 0.8044 0.2472  0.0619  -0.1624 270 GLY C C     
6454 O O     . GLY C 298 ? 0.7356 1.0753 0.8187 0.2377  0.0607  -0.1618 270 GLY C O     
6455 N N     . THR C 299 ? 0.7380 1.1022 0.8404 0.2653  0.0585  -0.1590 271 THR C N     
6456 C CA    . THR C 299 ? 0.7621 1.0887 0.8435 0.2749  0.0540  -0.1550 271 THR C CA    
6457 C C     . THR C 299 ? 0.7706 1.0788 0.8427 0.2841  0.0644  -0.1576 271 THR C C     
6458 O O     . THR C 299 ? 0.7942 1.1236 0.8803 0.2918  0.0722  -0.1603 271 THR C O     
6459 C CB    . THR C 299 ? 0.7933 1.1252 0.8799 0.2891  0.0423  -0.1491 271 THR C CB    
6460 O OG1   . THR C 299 ? 0.8037 1.1575 0.9064 0.3042  0.0458  -0.1496 271 THR C OG1   
6461 C CG2   . THR C 299 ? 0.7283 1.0824 0.8249 0.2807  0.0323  -0.1468 271 THR C CG2   
6462 N N     . SER C 300 ? 0.7295 0.9988 0.7778 0.2832  0.0645  -0.1568 272 SER C N     
6463 C CA    . SER C 300 ? 0.7299 0.9769 0.7649 0.2910  0.0736  -0.1595 272 SER C CA    
6464 C C     . SER C 300 ? 0.7732 0.9824 0.7873 0.2997  0.0660  -0.1556 272 SER C C     
6465 O O     . SER C 300 ? 0.7572 0.9588 0.7684 0.2991  0.0546  -0.1504 272 SER C O     
6466 C CB    . SER C 300 ? 0.6850 0.9232 0.7109 0.2772  0.0844  -0.1639 272 SER C CB    
6467 O OG    . SER C 300 ? 0.7491 0.9515 0.7520 0.2814  0.0882  -0.1647 272 SER C OG    
6468 N N     . GLN C 301 ? 0.8442 1.0294 0.8434 0.3074  0.0726  -0.1581 273 GLN C N     
6469 C CA    . GLN C 301 ? 0.8345 0.9816 0.8126 0.3148  0.0662  -0.1552 273 GLN C CA    
6470 C C     . GLN C 301 ? 0.8138 0.9323 0.7711 0.3108  0.0743  -0.1588 273 GLN C C     
6471 O O     . GLN C 301 ? 0.7817 0.9088 0.7421 0.3094  0.0855  -0.1624 273 GLN C O     
6472 C CB    . GLN C 301 ? 0.8520 0.9983 0.8347 0.3322  0.0624  -0.1525 273 GLN C CB    
6473 C CG    . GLN C 301 ? 0.9409 1.0495 0.9046 0.3371  0.0528  -0.1477 273 GLN C CG    
6474 C CD    . GLN C 301 ? 1.1191 1.2092 1.0753 0.3475  0.0552  -0.1469 273 GLN C CD    
6475 O OE1   . GLN C 301 ? 1.1393 1.2440 1.1084 0.3587  0.0541  -0.1447 273 GLN C OE1   
6476 N NE2   . GLN C 301 ? 1.1498 1.2071 1.0846 0.3438  0.0583  -0.1487 273 GLN C NE2   
6477 N N     . GLY C 302 ? 0.8599 0.9443 0.7964 0.3068  0.0681  -0.1564 274 GLY C N     
6478 C CA    . GLY C 302 ? 0.8849 0.9410 0.8009 0.2998  0.0738  -0.1582 274 GLY C CA    
6479 C C     . GLY C 302 ? 0.9396 0.9578 0.8353 0.3045  0.0669  -0.1551 274 GLY C C     
6480 O O     . GLY C 302 ? 0.9520 0.9649 0.8499 0.3145  0.0589  -0.1516 274 GLY C O     
6481 N N     . VAL C 303 ? 0.9687 0.9605 0.8447 0.2970  0.0697  -0.1561 275 VAL C N     
6482 C CA    . VAL C 303 ? 0.9620 0.9174 0.8175 0.2994  0.0632  -0.1539 275 VAL C CA    
6483 C C     . VAL C 303 ? 1.0039 0.9381 0.8446 0.2884  0.0576  -0.1516 275 VAL C C     
6484 O O     . VAL C 303 ? 1.0226 0.9656 0.8643 0.2783  0.0624  -0.1529 275 VAL C O     
6485 C CB    . VAL C 303 ? 0.8640 0.8062 0.7083 0.3020  0.0717  -0.1574 275 VAL C CB    
6486 C CG1   . VAL C 303 ? 0.8249 0.7810 0.6814 0.3153  0.0748  -0.1584 275 VAL C CG1   
6487 C CG2   . VAL C 303 ? 0.8187 0.7709 0.6623 0.2924  0.0836  -0.1612 275 VAL C CG2   
6488 N N     . GLY C 304 ? 1.0190 0.9248 0.8459 0.2903  0.0474  -0.1479 276 GLY C N     
6489 C CA    . GLY C 304 ? 1.0614 0.9464 0.8748 0.2808  0.0410  -0.1449 276 GLY C CA    
6490 C C     . GLY C 304 ? 1.1657 1.0212 0.9573 0.2761  0.0415  -0.1458 276 GLY C C     
6491 O O     . GLY C 304 ? 1.1350 0.9806 0.9196 0.2820  0.0443  -0.1482 276 GLY C O     
6492 N N     . ARG C 305 ? 1.2234 1.0653 1.0040 0.2658  0.0388  -0.1437 277 ARG C N     
6493 C CA    . ARG C 305 ? 1.1809 0.9950 0.9403 0.2610  0.0378  -0.1440 277 ARG C CA    
6494 C C     . ARG C 305 ? 1.1944 0.9825 0.9425 0.2669  0.0274  -0.1418 277 ARG C C     
6495 O O     . ARG C 305 ? 1.0937 0.8622 0.8262 0.2674  0.0280  -0.1440 277 ARG C O     
6496 C CB    . ARG C 305 ? 1.1571 0.9630 0.9085 0.2494  0.0357  -0.1412 277 ARG C CB    
6497 N N     . ASN C 306 ? 1.3279 1.1152 1.0834 0.2711  0.0180  -0.1376 278 ASN C N     
6498 C CA    . ASN C 306 ? 1.2729 1.0367 1.0198 0.2768  0.0084  -0.1352 278 ASN C CA    
6499 C C     . ASN C 306 ? 1.2547 1.0247 1.0077 0.2885  0.0119  -0.1379 278 ASN C C     
6500 O O     . ASN C 306 ? 1.2604 1.0096 1.0049 0.2936  0.0054  -0.1368 278 ASN C O     
6501 C CB    . ASN C 306 ? 1.1745 0.9346 0.9273 0.2764  -0.0029 -0.1287 278 ASN C CB    
6502 N N     . GLY C 307 ? 1.2725 1.0702 1.0400 0.2927  0.0219  -0.1413 279 GLY C N     
6503 C CA    . GLY C 307 ? 1.1611 0.9676 0.9362 0.3043  0.0261  -0.1436 279 GLY C CA    
6504 C C     . GLY C 307 ? 1.0742 0.9030 0.8695 0.3124  0.0232  -0.1406 279 GLY C C     
6505 O O     . GLY C 307 ? 0.9409 0.7786 0.7441 0.3229  0.0263  -0.1418 279 GLY C O     
6506 N N     . GLU C 308 ? 1.1286 0.9670 0.9323 0.3083  0.0173  -0.1365 280 GLU C N     
6507 C CA    . GLU C 308 ? 0.9687 0.8282 0.7908 0.3156  0.0132  -0.1330 280 GLU C CA    
6508 C C     . GLU C 308 ? 0.9133 0.8102 0.7544 0.3167  0.0223  -0.1364 280 GLU C C     
6509 O O     . GLU C 308 ? 0.9265 0.8327 0.7670 0.3094  0.0310  -0.1407 280 GLU C O     
6510 C CB    . GLU C 308 ? 0.8844 0.7377 0.7068 0.3108  0.0027  -0.1268 280 GLU C CB    
6511 N N     . ALA C 309 ? 0.8984 0.8171 0.7567 0.3255  0.0200  -0.1341 281 ALA C N     
6512 C CA    . ALA C 309 ? 0.8893 0.8460 0.7678 0.3273  0.0274  -0.1371 281 ALA C CA    
6513 C C     . ALA C 309 ? 0.8333 0.8079 0.7201 0.3192  0.0252  -0.1363 281 ALA C C     
6514 O O     . ALA C 309 ? 0.8259 0.7914 0.7106 0.3153  0.0155  -0.1303 281 ALA C O     
6515 C CB    . ALA C 309 ? 0.9544 0.9285 0.8483 0.3403  0.0252  -0.1346 281 ALA C CB    
6516 N N     . GLU C 310 ? 0.8368 0.8373 0.7342 0.3132  0.0343  -0.1408 282 GLU C N     
6517 C CA    . GLU C 310 ? 0.8050 0.8242 0.7119 0.2988  0.0331  -0.1387 282 GLU C CA    
6518 C C     . GLU C 310 ? 0.7964 0.8558 0.7267 0.3007  0.0367  -0.1403 282 GLU C C     
6519 O O     . GLU C 310 ? 0.8530 0.9280 0.7909 0.3064  0.0459  -0.1456 282 GLU C O     
6520 C CB    . GLU C 310 ? 0.8283 0.8384 0.7244 0.2856  0.0404  -0.1421 282 GLU C CB    
6521 C CG    . GLU C 310 ? 0.8715 0.8446 0.7454 0.2812  0.0357  -0.1396 282 GLU C CG    
6522 C CD    . GLU C 310 ? 0.8665 0.8317 0.7299 0.2693  0.0432  -0.1426 282 GLU C CD    
6523 O OE1   . GLU C 310 ? 0.8788 0.8625 0.7490 0.2670  0.0539  -0.1478 282 GLU C OE1   
6524 O OE2   . GLU C 310 ? 0.8413 0.7823 0.6901 0.2622  0.0385  -0.1394 282 GLU C OE2   
6525 N N     . TYR C 311 ? 0.7357 0.8123 0.6775 0.2957  0.0294  -0.1358 283 TYR C N     
6526 C CA    . TYR C 311 ? 0.6903 0.8056 0.6545 0.2967  0.0305  -0.1368 283 TYR C CA    
6527 C C     . TYR C 311 ? 0.6509 0.7822 0.6208 0.2799  0.0317  -0.1376 283 TYR C C     
6528 O O     . TYR C 311 ? 0.6635 0.7792 0.6236 0.2707  0.0265  -0.1340 283 TYR C O     
6529 C CB    . TYR C 311 ? 0.7064 0.8298 0.6792 0.3074  0.0200  -0.1308 283 TYR C CB    
6530 C CG    . TYR C 311 ? 0.7398 0.8485 0.7083 0.3250  0.0189  -0.1299 283 TYR C CG    
6531 C CD1   . TYR C 311 ? 0.7960 0.8670 0.7452 0.3286  0.0143  -0.1272 283 TYR C CD1   
6532 C CD2   . TYR C 311 ? 0.7586 0.8909 0.7424 0.3379  0.0226  -0.1319 283 TYR C CD2   
6533 C CE1   . TYR C 311 ? 0.8333 0.8884 0.7772 0.3445  0.0134  -0.1269 283 TYR C CE1   
6534 C CE2   . TYR C 311 ? 0.8521 0.9694 0.8313 0.3546  0.0222  -0.1312 283 TYR C CE2   
6535 C CZ    . TYR C 311 ? 0.9041 0.9814 0.8627 0.3553  0.0174  -0.1281 283 TYR C CZ    
6536 O OH    . TYR C 311 ? 1.0407 1.1000 0.9936 0.3653  0.0165  -0.1257 283 TYR C OH    
6537 N N     . TYR C 312 ? 0.6230 0.7853 0.6090 0.2759  0.0388  -0.1423 284 TYR C N     
6538 C CA    . TYR C 312 ? 0.6100 0.7855 0.6003 0.2593  0.0421  -0.1446 284 TYR C CA    
6539 C C     . TYR C 312 ? 0.6423 0.8574 0.6549 0.2571  0.0407  -0.1459 284 TYR C C     
6540 O O     . TYR C 312 ? 0.5832 0.8194 0.6102 0.2685  0.0402  -0.1461 284 TYR C O     
6541 C CB    . TYR C 312 ? 0.6187 0.7881 0.6028 0.2519  0.0546  -0.1503 284 TYR C CB    
6542 C CG    . TYR C 312 ? 0.6523 0.7835 0.6131 0.2501  0.0556  -0.1492 284 TYR C CG    
6543 C CD1   . TYR C 312 ? 0.7422 0.8527 0.6916 0.2619  0.0574  -0.1499 284 TYR C CD1   
6544 C CD2   . TYR C 312 ? 0.6800 0.7958 0.6300 0.2368  0.0545  -0.1475 284 TYR C CD2   
6545 C CE1   . TYR C 312 ? 0.7482 0.8243 0.6760 0.2596  0.0574  -0.1490 284 TYR C CE1   
6546 C CE2   . TYR C 312 ? 0.7197 0.8023 0.6493 0.2351  0.0547  -0.1460 284 TYR C CE2   
6547 C CZ    . TYR C 312 ? 0.7554 0.8185 0.6740 0.2462  0.0558  -0.1468 284 TYR C CZ    
6548 O OH    . TYR C 312 ? 0.7939 0.8244 0.6918 0.2440  0.0551  -0.1455 284 TYR C OH    
6549 N N     . ILE C 313 ? 0.6415 0.8660 0.6566 0.2423  0.0400  -0.1467 285 ILE C N     
6550 C CA    . ILE C 313 ? 0.5471 0.8082 0.5818 0.2360  0.0396  -0.1493 285 ILE C CA    
6551 C C     . ILE C 313 ? 0.5941 0.8579 0.6278 0.2189  0.0480  -0.1544 285 ILE C C     
6552 O O     . ILE C 313 ? 0.5635 0.8054 0.5827 0.2092  0.0475  -0.1532 285 ILE C O     
6553 C CB    . ILE C 313 ? 0.4725 0.7428 0.5106 0.2355  0.0273  -0.1446 285 ILE C CB    
6554 C CG1   . ILE C 313 ? 0.5133 0.7839 0.5544 0.2528  0.0192  -0.1391 285 ILE C CG1   
6555 C CG2   . ILE C 313 ? 0.4640 0.7699 0.5197 0.2259  0.0268  -0.1482 285 ILE C CG2   
6556 C CD1   . ILE C 313 ? 0.4740 0.7498 0.5156 0.2533  0.0071  -0.1334 285 ILE C CD1   
6557 N N     . HIS C 314 ? 0.6405 0.9309 0.6900 0.2154  0.0560  -0.1595 286 HIS C N     
6558 C CA    . HIS C 314 ? 0.6432 0.9368 0.6929 0.1995  0.0654  -0.1645 286 HIS C CA    
6559 C C     . HIS C 314 ? 0.6133 0.9367 0.6786 0.1878  0.0624  -0.1671 286 HIS C C     
6560 O O     . HIS C 314 ? 0.6099 0.9624 0.6925 0.1933  0.0568  -0.1668 286 HIS C O     
6561 C CB    . HIS C 314 ? 0.6412 0.9415 0.6964 0.2023  0.0781  -0.1686 286 HIS C CB    
6562 C CG    . HIS C 314 ? 0.6878 0.9615 0.7283 0.2153  0.0810  -0.1668 286 HIS C CG    
6563 N ND1   . HIS C 314 ? 0.7228 0.9625 0.7417 0.2114  0.0850  -0.1664 286 HIS C ND1   
6564 C CD2   . HIS C 314 ? 0.7079 0.9833 0.7516 0.2322  0.0801  -0.1656 286 HIS C CD2   
6565 C CE1   . HIS C 314 ? 0.7753 0.9969 0.7842 0.2247  0.0862  -0.1654 286 HIS C CE1   
6566 N NE2   . HIS C 314 ? 0.7774 1.0192 0.8006 0.2376  0.0836  -0.1650 286 HIS C NE2   
6567 N N     . LEU C 315 ? 0.5744 0.8899 0.6329 0.1717  0.0660  -0.1696 287 LEU C N     
6568 C CA    . LEU C 315 ? 0.5556 0.8938 0.6250 0.1585  0.0630  -0.1728 287 LEU C CA    
6569 C C     . LEU C 315 ? 0.5382 0.8595 0.5965 0.1420  0.0704  -0.1759 287 LEU C C     
6570 O O     . LEU C 315 ? 0.5038 0.7934 0.5438 0.1417  0.0740  -0.1737 287 LEU C O     
6571 C CB    . LEU C 315 ? 0.5320 0.8735 0.6000 0.1617  0.0494  -0.1689 287 LEU C CB    
6572 C CG    . LEU C 315 ? 0.4505 0.7579 0.4970 0.1627  0.0442  -0.1638 287 LEU C CG    
6573 C CD1   . LEU C 315 ? 0.4862 0.7860 0.5245 0.1470  0.0442  -0.1658 287 LEU C CD1   
6574 C CD2   . LEU C 315 ? 0.4464 0.7548 0.4926 0.1758  0.0323  -0.1577 287 LEU C CD2   
6575 N N     . SER C 316 ? 0.5517 0.8944 0.6214 0.1282  0.0723  -0.1808 288 SER C N     
6576 C CA    . SER C 316 ? 0.5636 0.8928 0.6247 0.1117  0.0796  -0.1842 288 SER C CA    
6577 C C     . SER C 316 ? 0.5544 0.8758 0.6067 0.1036  0.0715  -0.1838 288 SER C C     
6578 O O     . SER C 316 ? 0.5648 0.9061 0.6257 0.1051  0.0618  -0.1838 288 SER C O     
6579 C CB    . SER C 316 ? 0.5994 0.9549 0.6780 0.1003  0.0880  -0.1903 288 SER C CB    
6580 O OG    . SER C 316 ? 0.7658 1.1285 0.8521 0.1078  0.0968  -0.1904 288 SER C OG    
6581 N N     . VAL C 317 ? 0.5370 0.8295 0.5718 0.0955  0.0758  -0.1833 289 VAL C N     
6582 C CA    . VAL C 317 ? 0.5352 0.8153 0.5587 0.0890  0.0695  -0.1824 289 VAL C CA    
6583 C C     . VAL C 317 ? 0.5603 0.8328 0.5792 0.0718  0.0775  -0.1874 289 VAL C C     
6584 O O     . VAL C 317 ? 0.6145 0.8703 0.6268 0.0677  0.0877  -0.1878 289 VAL C O     
6585 C CB    . VAL C 317 ? 0.5700 0.8186 0.5749 0.0978  0.0656  -0.1754 289 VAL C CB    
6586 C CG1   . VAL C 317 ? 0.6612 0.8963 0.6541 0.0904  0.0613  -0.1745 289 VAL C CG1   
6587 C CG2   . VAL C 317 ? 0.5343 0.7892 0.5430 0.1139  0.0568  -0.1705 289 VAL C CG2   
6588 N N     . ILE C 318 ? 0.5058 0.7894 0.5272 0.0619  0.0728  -0.1911 290 ILE C N     
6589 C CA    . ILE C 318 ? 0.5219 0.7925 0.5349 0.0461  0.0788  -0.1954 290 ILE C CA    
6590 C C     . ILE C 318 ? 0.5278 0.7702 0.5211 0.0477  0.0750  -0.1911 290 ILE C C     
6591 O O     . ILE C 318 ? 0.5585 0.8049 0.5495 0.0538  0.0649  -0.1884 290 ILE C O     
6592 C CB    . ILE C 318 ? 0.4801 0.7777 0.5059 0.0336  0.0760  -0.2026 290 ILE C CB    
6593 C CG1   . ILE C 318 ? 0.5632 0.8934 0.6116 0.0335  0.0784  -0.2059 290 ILE C CG1   
6594 C CG2   . ILE C 318 ? 0.4898 0.7717 0.5065 0.0168  0.0834  -0.2076 290 ILE C CG2   
6595 C CD1   . ILE C 318 ? 0.6155 0.9779 0.6793 0.0244  0.0718  -0.2118 290 ILE C CD1   
6596 N N     . THR C 319 ? 0.5508 0.7651 0.5300 0.0426  0.0833  -0.1900 291 THR C N     
6597 C CA    . THR C 319 ? 0.5837 0.7710 0.5449 0.0428  0.0813  -0.1859 291 THR C CA    
6598 C C     . THR C 319 ? 0.6494 0.8285 0.6045 0.0274  0.0870  -0.1915 291 THR C C     
6599 O O     . THR C 319 ? 0.7916 0.9670 0.7483 0.0180  0.0969  -0.1951 291 THR C O     
6600 C CB    . THR C 319 ? 0.5720 0.7316 0.5209 0.0505  0.0856  -0.1792 291 THR C CB    
6601 O OG1   . THR C 319 ? 0.5969 0.7637 0.5516 0.0640  0.0812  -0.1752 291 THR C OG1   
6602 C CG2   . THR C 319 ? 0.6392 0.7745 0.5720 0.0525  0.0823  -0.1739 291 THR C CG2   
6603 N N     . ALA C 320 ? 0.6174 0.7929 0.5648 0.0248  0.0812  -0.1920 292 ALA C N     
6604 C CA    . ALA C 320 ? 0.6203 0.7888 0.5614 0.0104  0.0856  -0.1982 292 ALA C CA    
6605 C C     . ALA C 320 ? 0.6757 0.8189 0.5987 0.0122  0.0843  -0.1943 292 ALA C C     
6606 O O     . ALA C 320 ? 0.7007 0.8417 0.6193 0.0231  0.0766  -0.1883 292 ALA C O     
6607 C CB    . ALA C 320 ? 0.5876 0.7847 0.5403 0.0022  0.0798  -0.2059 292 ALA C CB    
6608 N N     . LEU C 321 ? 0.7069 0.8310 0.6196 0.0016  0.0923  -0.1975 293 LEU C N     
6609 C CA    . LEU C 321 ? 0.6989 0.7995 0.5947 0.0018  0.0927  -0.1948 293 LEU C CA    
6610 C C     . LEU C 321 ? 0.7900 0.8884 0.6812 -0.0129 0.0966  -0.2037 293 LEU C C     
6611 O O     . LEU C 321 ? 0.8629 0.9503 0.7526 -0.0229 0.1063  -0.2074 293 LEU C O     
6612 C CB    . LEU C 321 ? 0.6618 0.7333 0.5466 0.0064  0.1000  -0.1876 293 LEU C CB    
6613 C CG    . LEU C 321 ? 0.7181 0.7637 0.5862 0.0053  0.1032  -0.1850 293 LEU C CG    
6614 C CD1   . LEU C 321 ? 0.7213 0.7700 0.5846 0.0138  0.0938  -0.1809 293 LEU C CD1   
6615 C CD2   . LEU C 321 ? 0.8755 0.8952 0.7350 0.0093  0.1104  -0.1778 293 LEU C CD2   
6616 N N     . ALA C 322 ? 0.7406 0.8485 0.6287 -0.0145 0.0892  -0.2073 294 ALA C N     
6617 C CA    . ALA C 322 ? 0.7844 0.8923 0.6679 -0.0286 0.0911  -0.2168 294 ALA C CA    
6618 C C     . ALA C 322 ? 0.8192 0.9030 0.6832 -0.0278 0.0923  -0.2155 294 ALA C C     
6619 O O     . ALA C 322 ? 0.8236 0.8926 0.6794 -0.0165 0.0917  -0.2068 294 ALA C O     
6620 C CB    . ALA C 322 ? 0.7601 0.9006 0.6555 -0.0326 0.0814  -0.2233 294 ALA C CB    
6621 N N     . ARG C 323 ? 0.8950 0.9748 0.7516 -0.0401 0.0943  -0.2244 295 ARG C N     
6622 C CA    . ARG C 323 ? 0.9382 0.9957 0.7756 -0.0400 0.0962  -0.2246 295 ARG C CA    
6623 C C     . ARG C 323 ? 0.9592 1.0253 0.7921 -0.0521 0.0927  -0.2359 295 ARG C C     
6624 O O     . ARG C 323 ? 0.9547 1.0283 0.7944 -0.0657 0.0955  -0.2445 295 ARG C O     
6625 C CB    . ARG C 323 ? 0.9642 0.9889 0.7903 -0.0423 0.1087  -0.2222 295 ARG C CB    
6626 C CG    . ARG C 323 ? 1.0337 1.0346 0.8401 -0.0410 0.1117  -0.2219 295 ARG C CG    
6627 C CD    . ARG C 323 ? 1.0860 1.0552 0.8822 -0.0431 0.1243  -0.2192 295 ARG C CD    
6628 N NE    . ARG C 323 ? 1.1245 1.0856 0.9241 -0.0318 0.1264  -0.2078 295 ARG C NE    
6629 C CZ    . ARG C 323 ? 1.1302 1.0699 0.9263 -0.0327 0.1363  -0.2040 295 ARG C CZ    
6630 N NH1   . ARG C 323 ? 1.1891 1.1120 0.9783 -0.0440 0.1456  -0.2102 295 ARG C NH1   
6631 N NH2   . ARG C 323 ? 1.0936 1.0281 0.8926 -0.0221 0.1365  -0.1936 295 ARG C NH2   
6632 N N     . LYS C 324 ? 0.9797 1.0446 0.8007 -0.0476 0.0867  -0.2358 296 LYS C N     
6633 C CA    . LYS C 324 ? 1.0343 1.1047 0.8472 -0.0584 0.0830  -0.2465 296 LYS C CA    
6634 C C     . LYS C 324 ? 1.1324 1.1723 0.9287 -0.0682 0.0937  -0.2525 296 LYS C C     
6635 O O     . LYS C 324 ? 1.1277 1.1408 0.9129 -0.0619 0.1018  -0.2461 296 LYS C O     
6636 C CB    . LYS C 324 ? 0.9590 1.0378 0.7632 -0.0491 0.0732  -0.2438 296 LYS C CB    
6637 C CG    . LYS C 324 ? 0.9096 0.9931 0.7025 -0.0593 0.0685  -0.2547 296 LYS C CG    
6638 C CD    . LYS C 324 ? 0.8437 0.9351 0.6270 -0.0489 0.0593  -0.2508 296 LYS C CD    
6639 C CE    . LYS C 324 ? 0.8416 0.9361 0.6111 -0.0590 0.0546  -0.2620 296 LYS C CE    
6640 N NZ    . LYS C 324 ? 0.8038 0.9087 0.5640 -0.0489 0.0450  -0.2581 296 LYS C NZ    
6641 N N     . PHE C 325 ? 1.1280 1.1721 0.9227 -0.0838 0.0936  -0.2645 297 PHE C N     
6642 C CA    . PHE C 325 ? 1.2103 1.2249 0.9884 -0.0943 0.1034  -0.2716 297 PHE C CA    
6643 C C     . PHE C 325 ? 1.1899 1.1924 0.9467 -0.0923 0.1009  -0.2751 297 PHE C C     
6644 O O     . PHE C 325 ? 1.1274 1.1498 0.8835 -0.0882 0.0900  -0.2759 297 PHE C O     
6645 C CB    . PHE C 325 ? 1.2305 1.2532 1.0165 -0.1132 0.1050  -0.2832 297 PHE C CB    
6646 C CG    . PHE C 325 ? 1.2419 1.2572 1.0391 -0.1180 0.1149  -0.2808 297 PHE C CG    
6647 C CD1   . PHE C 325 ? 1.3085 1.2896 1.0934 -0.1215 0.1278  -0.2803 297 PHE C CD1   
6648 C CD2   . PHE C 325 ? 1.1923 1.2348 1.0121 -0.1185 0.1117  -0.2786 297 PHE C CD2   
6649 C CE1   . PHE C 325 ? 1.3219 1.2958 1.1160 -0.1258 0.1370  -0.2776 297 PHE C CE1   
6650 C CE2   . PHE C 325 ? 1.1877 1.2233 1.0167 -0.1227 0.1214  -0.2762 297 PHE C CE2   
6651 C CZ    . PHE C 325 ? 1.2345 1.2358 1.0504 -0.1266 0.1339  -0.2756 297 PHE C CZ    
6652 N N     . GLU D 42  ? 1.3588 0.6562 0.9366 0.1572  0.3718  0.1098  14  GLU D N     
6653 C CA    . GLU D 42  ? 1.3752 0.6567 0.9410 0.1441  0.3776  0.1019  14  GLU D CA    
6654 C C     . GLU D 42  ? 1.4751 0.7451 1.0342 0.1475  0.3804  0.1100  14  GLU D C     
6655 O O     . GLU D 42  ? 1.4520 0.7267 1.0161 0.1597  0.3776  0.1212  14  GLU D O     
6656 C CB    . GLU D 42  ? 1.4296 0.6922 0.9865 0.1340  0.3897  0.0903  14  GLU D CB    
6657 C CG    . GLU D 42  ? 1.4290 0.6808 0.9771 0.1178  0.3940  0.0796  14  GLU D CG    
6658 C CD    . GLU D 42  ? 1.4153 0.6411 0.9516 0.1094  0.4079  0.0730  14  GLU D CD    
6659 O OE1   . GLU D 42  ? 1.4991 0.7136 1.0327 0.1170  0.4144  0.0772  14  GLU D OE1   
6660 O OE2   . GLU D 42  ? 1.3551 0.5719 0.8852 0.0951  0.4124  0.0635  14  GLU D OE2   
6661 N N     . ALA D 43  ? 1.6021 0.8579 1.1506 0.1365  0.3858  0.1046  15  ALA D N     
6662 C CA    . ALA D 43  ? 1.5666 0.8109 1.1075 0.1381  0.3886  0.1116  15  ALA D CA    
6663 C C     . ALA D 43  ? 1.5087 0.7719 1.0568 0.1472  0.3752  0.1230  15  ALA D C     
6664 O O     . ALA D 43  ? 1.4493 0.7261 0.9998 0.1428  0.3663  0.1211  15  ALA D O     
6665 C CB    . ALA D 43  ? 1.4958 0.7208 1.0311 0.1442  0.3993  0.1160  15  ALA D CB    
6666 N N     . TYR D 44  ? 1.4820 0.7463 1.0332 0.1594  0.3734  0.1348  16  TYR D N     
6667 C CA    . TYR D 44  ? 1.4810 0.7641 1.0395 0.1675  0.3598  0.1460  16  TYR D CA    
6668 C C     . TYR D 44  ? 1.4315 0.7396 1.0046 0.1718  0.3483  0.1464  16  TYR D C     
6669 O O     . TYR D 44  ? 1.4815 0.7966 1.0639 0.1807  0.3479  0.1505  16  TYR D O     
6670 C CB    . TYR D 44  ? 1.4109 0.6899 0.9701 0.1793  0.3604  0.1589  16  TYR D CB    
6671 C CG    . TYR D 44  ? 1.3827 0.6351 0.9286 0.1775  0.3735  0.1597  16  TYR D CG    
6672 C CD1   . TYR D 44  ? 1.3836 0.6191 0.9168 0.1652  0.3813  0.1517  16  TYR D CD1   
6673 C CD2   . TYR D 44  ? 1.4129 0.6576 0.9595 0.1884  0.3778  0.1692  16  TYR D CD2   
6674 C CE1   . TYR D 44  ? 1.4474 0.6585 0.9689 0.1634  0.3931  0.1529  16  TYR D CE1   
6675 C CE2   . TYR D 44  ? 1.3698 0.5896 0.9041 0.1872  0.3896  0.1704  16  TYR D CE2   
6676 C CZ    . TYR D 44  ? 1.4124 0.6152 0.9342 0.1745  0.3971  0.1623  16  TYR D CZ    
6677 O OH    . TYR D 44  ? 1.4059 0.5837 0.9159 0.1731  0.4089  0.1639  16  TYR D OH    
6678 N N     . ARG D 45  ? 1.2911 0.6121 0.8660 0.1655  0.3394  0.1421  17  ARG D N     
6679 C CA    . ARG D 45  ? 1.1952 0.5406 0.7837 0.1690  0.3269  0.1432  17  ARG D CA    
6680 C C     . ARG D 45  ? 1.2264 0.5739 0.8215 0.1698  0.3317  0.1369  17  ARG D C     
6681 O O     . ARG D 45  ? 1.2258 0.5788 0.8294 0.1796  0.3319  0.1432  17  ARG D O     
6682 C CB    . ARG D 45  ? 1.2028 0.5655 0.8017 0.1804  0.3149  0.1570  17  ARG D CB    
6683 C CG    . ARG D 45  ? 1.2335 0.5927 0.8246 0.1809  0.3105  0.1648  17  ARG D CG    
6684 C CD    . ARG D 45  ? 1.2540 0.6110 0.8354 0.1701  0.3082  0.1579  17  ARG D CD    
6685 N NE    . ARG D 45  ? 1.1859 0.5524 0.7652 0.1723  0.2965  0.1665  17  ARG D NE    
6686 C CZ    . ARG D 45  ? 1.2007 0.5776 0.7782 0.1670  0.2872  0.1640  17  ARG D CZ    
6687 N NH1   . ARG D 45  ? 1.1433 0.5233 0.7217 0.1596  0.2879  0.1534  17  ARG D NH1   
6688 N NH2   . ARG D 45  ? 1.1616 0.5457 0.7357 0.1694  0.2768  0.1724  17  ARG D NH2   
6689 N N     . GLY D 46  ? 1.2201 0.5637 0.8113 0.1594  0.3355  0.1248  18  GLY D N     
6690 C CA    . GLY D 46  ? 1.1930 0.5374 0.7880 0.1577  0.3399  0.1171  18  GLY D CA    
6691 C C     . GLY D 46  ? 1.1784 0.5303 0.7834 0.1691  0.3402  0.1233  18  GLY D C     
6692 O O     . GLY D 46  ? 1.2399 0.5772 0.8404 0.1734  0.3501  0.1257  18  GLY D O     
6693 N N     . ILE D 47  ? 1.0613 0.4354 0.6797 0.1740  0.3299  0.1260  19  ILE D N     
6694 C CA    . ILE D 47  ? 1.0661 0.4499 0.6954 0.1844  0.3300  0.1316  19  ILE D CA    
6695 C C     . ILE D 47  ? 1.0258 0.4313 0.6689 0.1943  0.3170  0.1446  19  ILE D C     
6696 O O     . ILE D 47  ? 1.0966 0.5215 0.7487 0.1933  0.3044  0.1458  19  ILE D O     
6697 C CB    . ILE D 47  ? 1.0151 0.4072 0.6493 0.1815  0.3295  0.1238  19  ILE D CB    
6698 C CG1   . ILE D 47  ? 1.0699 0.4406 0.6905 0.1708  0.3418  0.1110  19  ILE D CG1   
6699 C CG2   . ILE D 47  ? 0.9709 0.3748 0.6170 0.1929  0.3293  0.1308  19  ILE D CG2   
6700 C CD1   . ILE D 47  ? 1.0999 0.4524 0.7137 0.1744  0.3549  0.1111  19  ILE D CD1   
6701 N N     . ASP D 48  ? 0.9935 0.3955 0.6383 0.2034  0.3198  0.1544  20  ASP D N     
6702 C CA    . ASP D 48  ? 0.9826 0.4057 0.6421 0.2130  0.3080  0.1672  20  ASP D CA    
6703 C C     . ASP D 48  ? 1.1042 0.5431 0.7782 0.2207  0.3069  0.1703  20  ASP D C     
6704 O O     . ASP D 48  ? 1.1978 0.6304 0.8692 0.2189  0.3154  0.1626  20  ASP D O     
6705 C CB    . ASP D 48  ? 1.0189 0.4323 0.6746 0.2196  0.3112  0.1769  20  ASP D CB    
6706 C CG    . ASP D 48  ? 1.1673 0.5563 0.8123 0.2215  0.3282  0.1739  20  ASP D CG    
6707 O OD1   . ASP D 48  ? 1.1522 0.5350 0.7952 0.2196  0.3366  0.1661  20  ASP D OD1   
6708 O OD2   . ASP D 48  ? 1.2769 0.6524 0.9148 0.2247  0.3329  0.1795  20  ASP D OD2   
6709 N N     . LYS D 49  ? 1.0588 0.5189 0.7483 0.2290  0.2962  0.1820  21  LYS D N     
6710 C CA    . LYS D 49  ? 1.0941 0.5727 0.7998 0.2366  0.2937  0.1868  21  LYS D CA    
6711 C C     . LYS D 49  ? 1.0218 0.5098 0.7309 0.2305  0.2905  0.1780  21  LYS D C     
6712 O O     . LYS D 49  ? 0.9565 0.4374 0.6626 0.2305  0.3004  0.1716  21  LYS D O     
6713 C CB    . LYS D 49  ? 1.0029 0.4687 0.7062 0.2446  0.3084  0.1886  21  LYS D CB    
6714 N N     . PRO D 50  ? 0.9173 0.4207 0.6320 0.2251  0.2767  0.1775  22  PRO D N     
6715 C CA    . PRO D 50  ? 0.8817 0.3929 0.5988 0.2192  0.2736  0.1689  22  PRO D CA    
6716 C C     . PRO D 50  ? 1.0149 0.5453 0.7484 0.2258  0.2711  0.1732  22  PRO D C     
6717 O O     . PRO D 50  ? 0.9750 0.5066 0.7081 0.2225  0.2737  0.1656  22  PRO D O     
6718 C CB    . PRO D 50  ? 0.8649 0.3866 0.5831 0.2127  0.2591  0.1690  22  PRO D CB    
6719 C CG    . PRO D 50  ? 0.9517 0.4835 0.6777 0.2188  0.2503  0.1818  22  PRO D CG    
6720 C CD    . PRO D 50  ? 1.0282 0.5413 0.7458 0.2240  0.2632  0.1846  22  PRO D CD    
6721 N N     . HIS D 51  ? 1.0353 0.5809 0.7830 0.2348  0.2661  0.1855  23  HIS D N     
6722 C CA    . HIS D 51  ? 1.0263 0.5918 0.7909 0.2412  0.2638  0.1908  23  HIS D CA    
6723 C C     . HIS D 51  ? 0.9906 0.5444 0.7491 0.2435  0.2789  0.1844  23  HIS D C     
6724 O O     . HIS D 51  ? 1.0259 0.5913 0.7919 0.2439  0.2779  0.1823  23  HIS D O     
6725 C CB    . HIS D 51  ? 1.0156 0.5947 0.7943 0.2509  0.2594  0.2051  23  HIS D CB    
6726 C CG    . HIS D 51  ? 1.1133 0.7152 0.9060 0.2493  0.2409  0.2130  23  HIS D CG    
6727 N ND1   . HIS D 51  ? 1.1381 0.7387 0.9240 0.2409  0.2304  0.2099  23  HIS D ND1   
6728 C CD2   . HIS D 51  ? 1.1111 0.7371 0.9235 0.2545  0.2310  0.2239  23  HIS D CD2   
6729 C CE1   . HIS D 51  ? 1.0855 0.7075 0.8855 0.2410  0.2145  0.2183  23  HIS D CE1   
6730 N NE2   . HIS D 51  ? 1.1134 0.7514 0.9301 0.2488  0.2143  0.2269  23  HIS D NE2   
6731 N N     . LEU D 52  ? 0.9842 0.5138 0.7279 0.2448  0.2929  0.1810  24  LEU D N     
6732 C CA    . LEU D 52  ? 0.9041 0.4199 0.6397 0.2466  0.3075  0.1749  24  LEU D CA    
6733 C C     . LEU D 52  ? 0.9365 0.4393 0.6586 0.2358  0.3110  0.1608  24  LEU D C     
6734 O O     . LEU D 52  ? 0.9707 0.4684 0.6889 0.2360  0.3190  0.1554  24  LEU D O     
6735 C CB    . LEU D 52  ? 0.9356 0.4295 0.6602 0.2516  0.3208  0.1770  24  LEU D CB    
6736 C CG    . LEU D 52  ? 0.9440 0.4475 0.6800 0.2623  0.3181  0.1910  24  LEU D CG    
6737 C CD1   . LEU D 52  ? 0.9762 0.4581 0.7017 0.2689  0.3336  0.1927  24  LEU D CD1   
6738 C CD2   . LEU D 52  ? 0.9762 0.5086 0.7339 0.2698  0.3100  0.2007  24  LEU D CD2   
6739 N N     . TYR D 53  ? 0.9619 0.4595 0.6767 0.2264  0.3052  0.1548  25  TYR D N     
6740 C CA    . TYR D 53  ? 0.8894 0.3761 0.5926 0.2157  0.3081  0.1415  25  TYR D CA    
6741 C C     . TYR D 53  ? 0.8902 0.3967 0.6042 0.2145  0.2993  0.1396  25  TYR D C     
6742 O O     . TYR D 53  ? 0.8746 0.3746 0.5819 0.2095  0.3040  0.1303  25  TYR D O     
6743 C CB    . TYR D 53  ? 0.8910 0.3667 0.5836 0.2062  0.3052  0.1360  25  TYR D CB    
6744 C CG    . TYR D 53  ? 0.8929 0.3535 0.5719 0.1946  0.3106  0.1219  25  TYR D CG    
6745 C CD1   . TYR D 53  ? 0.9177 0.3534 0.5813 0.1896  0.3240  0.1147  25  TYR D CD1   
6746 C CD2   . TYR D 53  ? 0.8706 0.3422 0.5529 0.1882  0.3021  0.1160  25  TYR D CD2   
6747 C CE1   . TYR D 53  ? 0.9197 0.3430 0.5724 0.1777  0.3280  0.1017  25  TYR D CE1   
6748 C CE2   . TYR D 53  ? 0.8725 0.3316 0.5437 0.1773  0.3065  0.1031  25  TYR D CE2   
6749 C CZ    . TYR D 53  ? 0.8967 0.3324 0.5537 0.1717  0.3191  0.0960  25  TYR D CZ    
6750 O OH    . TYR D 53  ? 0.8986 0.3238 0.5464 0.1596  0.3224  0.0830  25  TYR D OH    
6751 N N     . THR D 54  ? 0.8763 0.4070 0.6069 0.2185  0.2860  0.1485  26  THR D N     
6752 C CA    . THR D 54  ? 0.8200 0.3707 0.5624 0.2181  0.2773  0.1481  26  THR D CA    
6753 C C     . THR D 54  ? 0.8314 0.3870 0.5792 0.2248  0.2847  0.1497  26  THR D C     
6754 O O     . THR D 54  ? 0.9235 0.4937 0.6795 0.2244  0.2794  0.1486  26  THR D O     
6755 C CB    . THR D 54  ? 0.8181 0.3934 0.5777 0.2205  0.2612  0.1583  26  THR D CB    
6756 O OG1   . THR D 54  ? 0.9346 0.5152 0.7025 0.2290  0.2615  0.1697  26  THR D OG1   
6757 C CG2   . THR D 54  ? 0.8976 0.4701 0.6510 0.2122  0.2519  0.1548  26  THR D CG2   
6758 N N     . LEU D 55  ? 0.8433 0.3868 0.5862 0.2312  0.2969  0.1525  27  LEU D N     
6759 C CA    . LEU D 55  ? 0.8496 0.3933 0.5934 0.2368  0.3059  0.1526  27  LEU D CA    
6760 C C     . LEU D 55  ? 0.8529 0.3817 0.5821 0.2288  0.3119  0.1393  27  LEU D C     
6761 O O     . LEU D 55  ? 0.8516 0.3846 0.5824 0.2317  0.3157  0.1382  27  LEU D O     
6762 C CB    . LEU D 55  ? 0.8760 0.4072 0.6156 0.2451  0.3181  0.1582  27  LEU D CB    
6763 C CG    . LEU D 55  ? 0.8740 0.4228 0.6305 0.2549  0.3128  0.1726  27  LEU D CG    
6764 C CD1   . LEU D 55  ? 0.9030 0.4358 0.6528 0.2627  0.3256  0.1771  27  LEU D CD1   
6765 C CD2   . LEU D 55  ? 0.8546 0.4309 0.6310 0.2610  0.3063  0.1805  27  LEU D CD2   
6766 N N     . GLY D 56  ? 0.8578 0.3698 0.5731 0.2184  0.3126  0.1293  28  GLY D N     
6767 C CA    . GLY D 56  ? 0.8578 0.3587 0.5616 0.2088  0.3152  0.1161  28  GLY D CA    
6768 C C     . GLY D 56  ? 0.8826 0.3978 0.5922 0.2025  0.3033  0.1116  28  GLY D C     
6769 O O     . GLY D 56  ? 0.8975 0.4039 0.5978 0.1931  0.3039  0.0997  28  GLY D O     
6770 N N     . CYS D 57  ? 0.8888 0.4260 0.6141 0.2070  0.2916  0.1205  29  CYS D N     
6771 C CA    . CYS D 57  ? 0.9118 0.4625 0.6429 0.2016  0.2797  0.1171  29  CYS D CA    
6772 C C     . CYS D 57  ? 1.0054 0.5603 0.7363 0.2001  0.2807  0.1102  29  CYS D C     
6773 O O     . CYS D 57  ? 1.0466 0.5978 0.7712 0.1916  0.2777  0.0997  29  CYS D O     
6774 C CB    . CYS D 57  ? 0.9592 0.5343 0.7086 0.2070  0.2667  0.1290  29  CYS D CB    
6775 S SG    . CYS D 57  ? 1.0349 0.6236 0.7897 0.1996  0.2506  0.1261  29  CYS D SG    
6776 N N     . CYS D 58  ? 1.0763 0.6394 0.8140 0.2083  0.2849  0.1160  30  CYS D N     
6777 C CA    . CYS D 58  ? 1.0890 0.6591 0.8281 0.2081  0.2847  0.1113  30  CYS D CA    
6778 C C     . CYS D 58  ? 1.0897 0.6415 0.8122 0.1982  0.2899  0.0956  30  CYS D C     
6779 O O     . CYS D 58  ? 1.0843 0.6424 0.8068 0.1925  0.2841  0.0873  30  CYS D O     
6780 C CB    . CYS D 58  ? 1.1705 0.7472 0.9159 0.2184  0.2916  0.1196  30  CYS D CB    
6781 S SG    . CYS D 58  ? 1.5820 1.1740 1.3443 0.2292  0.2897  0.1368  30  CYS D SG    
6782 N N     . SER D 59  ? 1.1031 0.6333 0.8122 0.1953  0.3002  0.0911  31  SER D N     
6783 C CA    . SER D 59  ? 1.0130 0.5276 0.7083 0.1846  0.3042  0.0761  31  SER D CA    
6784 C C     . SER D 59  ? 0.9518 0.4593 0.6411 0.1729  0.3001  0.0669  31  SER D C     
6785 O O     . SER D 59  ? 0.9426 0.4518 0.6286 0.1633  0.2962  0.0545  31  SER D O     
6786 C CB    . SER D 59  ? 0.9052 0.3993 0.5891 0.1858  0.3165  0.0749  31  SER D CB    
6787 O OG    . SER D 59  ? 0.8834 0.3834 0.5715 0.1959  0.3209  0.0817  31  SER D OG    
6788 N N     . LEU D 60  ? 0.9642 0.4655 0.6526 0.1734  0.3006  0.0727  32  LEU D N     
6789 C CA    . LEU D 60  ? 0.9578 0.4507 0.6393 0.1624  0.2983  0.0644  32  LEU D CA    
6790 C C     . LEU D 60  ? 1.0612 0.5709 0.7503 0.1591  0.2866  0.0613  32  LEU D C     
6791 O O     . LEU D 60  ? 1.0437 0.5513 0.7279 0.1482  0.2842  0.0494  32  LEU D O     
6792 C CB    . LEU D 60  ? 0.9031 0.3859 0.5814 0.1649  0.3017  0.0723  32  LEU D CB    
6793 C CG    . LEU D 60  ? 0.8603 0.3228 0.5285 0.1662  0.3142  0.0734  32  LEU D CG    
6794 C CD1   . LEU D 60  ? 0.8698 0.3257 0.5364 0.1697  0.3161  0.0819  32  LEU D CD1   
6795 C CD2   . LEU D 60  ? 0.8991 0.3438 0.5545 0.1537  0.3203  0.0591  32  LEU D CD2   
6796 N N     . THR D 61  ? 1.0810 0.6087 0.7829 0.1681  0.2787  0.0720  33  THR D N     
6797 C CA    . THR D 61  ? 1.0454 0.5887 0.7547 0.1659  0.2672  0.0697  33  THR D CA    
6798 C C     . THR D 61  ? 1.0244 0.5739 0.7326 0.1603  0.2659  0.0575  33  THR D C     
6799 O O     . THR D 61  ? 0.9853 0.5385 0.6915 0.1517  0.2607  0.0472  33  THR D O     
6800 C CB    . THR D 61  ? 1.0676 0.6302 0.7924 0.1760  0.2586  0.0840  33  THR D CB    
6801 O OG1   . THR D 61  ? 1.0852 0.6464 0.8120 0.1791  0.2568  0.0939  33  THR D OG1   
6802 C CG2   . THR D 61  ? 1.0461 0.6241 0.7784 0.1740  0.2465  0.0820  33  THR D CG2   
6803 N N     . ALA D 62  ? 1.0159 0.5680 0.7254 0.1649  0.2703  0.0583  34  ALA D N     
6804 C CA    . ALA D 62  ? 1.0432 0.6028 0.7514 0.1595  0.2683  0.0470  34  ALA D CA    
6805 C C     . ALA D 62  ? 1.0232 0.5702 0.7197 0.1463  0.2719  0.0318  34  ALA D C     
6806 O O     . ALA D 62  ? 1.0759 0.6320 0.7722 0.1383  0.2667  0.0204  34  ALA D O     
6807 C CB    . ALA D 62  ? 1.0989 0.6628 0.8099 0.1679  0.2728  0.0521  34  ALA D CB    
6808 N N     . MET D 63  ? 0.9723 0.4994 0.6598 0.1435  0.2803  0.0318  35  MET D N     
6809 C CA    . MET D 63  ? 1.0184 0.5333 0.6959 0.1305  0.2840  0.0180  35  MET D CA    
6810 C C     . MET D 63  ? 1.0206 0.5397 0.6983 0.1203  0.2781  0.0103  35  MET D C     
6811 O O     . MET D 63  ? 1.0038 0.5292 0.6804 0.1099  0.2745  -0.0026 35  MET D O     
6812 C CB    . MET D 63  ? 1.0464 0.5379 0.7141 0.1309  0.2952  0.0209  35  MET D CB    
6813 C CG    . MET D 63  ? 1.0902 0.5674 0.7476 0.1171  0.2996  0.0074  35  MET D CG    
6814 S SD    . MET D 63  ? 1.2205 0.6690 0.8661 0.1170  0.3127  0.0118  35  MET D SD    
6815 C CE    . MET D 63  ? 1.0115 0.4571 0.6576 0.1321  0.3189  0.0229  35  MET D CE    
6816 N N     . ALA D 64  ? 1.0135 0.5300 0.6926 0.1232  0.2770  0.0180  36  ALA D N     
6817 C CA    . ALA D 64  ? 0.9629 0.4841 0.6421 0.1146  0.2715  0.0114  36  ALA D CA    
6818 C C     . ALA D 64  ? 0.9585 0.5024 0.6466 0.1144  0.2606  0.0074  36  ALA D C     
6819 O O     . ALA D 64  ? 0.9774 0.5290 0.6657 0.1048  0.2560  -0.0028 36  ALA D O     
6820 C CB    . ALA D 64  ? 0.9870 0.5001 0.6648 0.1190  0.2724  0.0214  36  ALA D CB    
6821 N N     . SER D 65  ? 0.9625 0.5179 0.6583 0.1251  0.2568  0.0156  37  SER D N     
6822 C CA    . SER D 65  ? 0.9479 0.5241 0.6515 0.1255  0.2472  0.0121  37  SER D CA    
6823 C C     . SER D 65  ? 0.9481 0.5314 0.6496 0.1163  0.2461  -0.0016 37  SER D C     
6824 O O     . SER D 65  ? 0.9469 0.5454 0.6521 0.1112  0.2384  -0.0091 37  SER D O     
6825 C CB    . SER D 65  ? 0.9719 0.5578 0.6844 0.1389  0.2446  0.0244  37  SER D CB    
6826 O OG    . SER D 65  ? 1.0155 0.6202 0.7353 0.1399  0.2355  0.0223  37  SER D OG    
6827 N N     . ALA D 66  ? 1.0439 0.6163 0.7393 0.1143  0.2533  -0.0050 38  ALA D N     
6828 C CA    . ALA D 66  ? 1.0076 0.5853 0.7000 0.1055  0.2520  -0.0182 38  ALA D CA    
6829 C C     . ALA D 66  ? 0.9908 0.5642 0.6789 0.0916  0.2522  -0.0303 38  ALA D C     
6830 O O     . ALA D 66  ? 0.9841 0.5706 0.6740 0.0836  0.2465  -0.0412 38  ALA D O     
6831 C CB    . ALA D 66  ? 1.0087 0.5751 0.6950 0.1086  0.2597  -0.0179 38  ALA D CB    
6832 N N     . GLN D 67  ? 1.0906 0.6464 0.7732 0.0887  0.2589  -0.0280 39  GLN D N     
6833 C CA    . GLN D 67  ? 1.0978 0.6488 0.7766 0.0754  0.2602  -0.0385 39  GLN D CA    
6834 C C     . GLN D 67  ? 1.0276 0.5960 0.7132 0.0714  0.2516  -0.0420 39  GLN D C     
6835 O O     . GLN D 67  ? 1.0272 0.6037 0.7136 0.0607  0.2488  -0.0536 39  GLN D O     
6836 C CB    . GLN D 67  ? 1.1073 0.6351 0.7785 0.0744  0.2697  -0.0334 39  GLN D CB    
6837 C CG    . GLN D 67  ? 1.1892 0.6976 0.8519 0.0751  0.2793  -0.0329 39  GLN D CG    
6838 C CD    . GLN D 67  ? 1.2405 0.7263 0.8958 0.0765  0.2888  -0.0254 39  GLN D CD    
6839 O OE1   . GLN D 67  ? 1.2110 0.6962 0.8680 0.0813  0.2879  -0.0168 39  GLN D OE1   
6840 N NE2   . GLN D 67  ? 1.2759 0.7425 0.9221 0.0726  0.2979  -0.0286 39  GLN D NE2   
6841 N N     . LEU D 68  ? 1.0517 0.6259 0.7419 0.0802  0.2473  -0.0322 40  LEU D N     
6842 C CA    . LEU D 68  ? 1.0957 0.6848 0.7911 0.0773  0.2395  -0.0350 40  LEU D CA    
6843 C C     . LEU D 68  ? 1.0999 0.7110 0.8021 0.0761  0.2306  -0.0419 40  LEU D C     
6844 O O     . LEU D 68  ? 1.1076 0.7314 0.8131 0.0691  0.2253  -0.0498 40  LEU D O     
6845 C CB    . LEU D 68  ? 1.0951 0.6825 0.7922 0.0875  0.2372  -0.0226 40  LEU D CB    
6846 C CG    . LEU D 68  ? 1.0551 0.6229 0.7449 0.0876  0.2445  -0.0166 40  LEU D CG    
6847 C CD1   . LEU D 68  ? 1.0310 0.5983 0.7224 0.0987  0.2409  -0.0043 40  LEU D CD1   
6848 C CD2   . LEU D 68  ? 1.0904 0.6562 0.7767 0.0752  0.2462  -0.0261 40  LEU D CD2   
6849 N N     . ASP D 69  ? 1.0715 0.6876 0.7756 0.0831  0.2294  -0.0388 41  ASP D N     
6850 C CA    . ASP D 69  ? 1.0777 0.7137 0.7869 0.0826  0.2216  -0.0448 41  ASP D CA    
6851 C C     . ASP D 69  ? 1.0773 0.7182 0.7844 0.0705  0.2213  -0.0593 41  ASP D C     
6852 O O     . ASP D 69  ? 1.1086 0.7672 0.8198 0.0677  0.2141  -0.0661 41  ASP D O     
6853 C CB    . ASP D 69  ? 1.0692 0.7078 0.7797 0.0927  0.2220  -0.0379 41  ASP D CB    
6854 C CG    . ASP D 69  ? 1.0941 0.7356 0.8101 0.1049  0.2194  -0.0244 41  ASP D CG    
6855 O OD1   . ASP D 69  ? 1.0627 0.7066 0.7812 0.1053  0.2153  -0.0218 41  ASP D OD1   
6856 O OD2   . ASP D 69  ? 1.0884 0.7297 0.8061 0.1142  0.2215  -0.0163 41  ASP D OD2   
6857 N N     . ALA D 70  ? 1.0906 0.7157 0.7908 0.0636  0.2290  -0.0640 42  ALA D N     
6858 C CA    . ALA D 70  ? 1.1217 0.7498 0.8194 0.0515  0.2292  -0.0779 42  ALA D CA    
6859 C C     . ALA D 70  ? 1.1485 0.7813 0.8489 0.0419  0.2278  -0.0843 42  ALA D C     
6860 O O     . ALA D 70  ? 1.2023 0.8431 0.9030 0.0319  0.2262  -0.0961 42  ALA D O     
6861 C CB    . ALA D 70  ? 1.0934 0.7011 0.7819 0.0477  0.2384  -0.0807 42  ALA D CB    
6862 N N     . LEU D 71  ? 1.1741 0.8023 0.8760 0.0447  0.2287  -0.0769 43  LEU D N     
6863 C CA    . LEU D 71  ? 1.1430 0.7750 0.8468 0.0365  0.2283  -0.0819 43  LEU D CA    
6864 C C     . LEU D 71  ? 1.1571 0.8050 0.8677 0.0414  0.2202  -0.0783 43  LEU D C     
6865 O O     . LEU D 71  ? 1.1956 0.8510 0.9089 0.0348  0.2188  -0.0837 43  LEU D O     
6866 C CB    . LEU D 71  ? 1.0594 0.6694 0.7566 0.0338  0.2378  -0.0775 43  LEU D CB    
6867 C CG    . LEU D 71  ? 1.1574 0.7477 0.8464 0.0277  0.2472  -0.0812 43  LEU D CG    
6868 C CD1   . LEU D 71  ? 1.1048 0.6734 0.7869 0.0261  0.2565  -0.0755 43  LEU D CD1   
6869 C CD2   . LEU D 71  ? 1.2748 0.8726 0.9645 0.0150  0.2468  -0.0956 43  LEU D CD2   
6870 N N     . TRP D 72  ? 1.1786 0.8315 0.8918 0.0527  0.2153  -0.0695 44  TRP D N     
6871 C CA    . TRP D 72  ? 1.1950 0.8583 0.9127 0.0581  0.2084  -0.0648 44  TRP D CA    
6872 C C     . TRP D 72  ? 1.1780 0.8627 0.9020 0.0536  0.2007  -0.0739 44  TRP D C     
6873 O O     . TRP D 72  ? 1.1240 0.8160 0.8507 0.0548  0.1962  -0.0729 44  TRP D O     
6874 C CB    . TRP D 72  ? 1.1631 0.8262 0.8820 0.0710  0.2052  -0.0534 44  TRP D CB    
6875 C CG    . TRP D 72  ? 1.1278 0.7941 0.8505 0.0762  0.1989  -0.0443 44  TRP D CG    
6876 C CD1   . TRP D 72  ? 1.1232 0.8079 0.8546 0.0787  0.1871  -0.0420 44  TRP D CD1   
6877 C CD2   . TRP D 72  ? 1.1700 0.8214 0.8883 0.0788  0.2027  -0.0357 44  TRP D CD2   
6878 N NE1   . TRP D 72  ? 1.1409 0.8227 0.8731 0.0823  0.1831  -0.0331 44  TRP D NE1   
6879 C CE2   . TRP D 72  ? 1.1360 0.7981 0.8602 0.0825  0.1923  -0.0289 44  TRP D CE2   
6880 C CE3   . TRP D 72  ? 1.1964 0.8258 0.9056 0.0785  0.2138  -0.0330 44  TRP D CE3   
6881 C CZ2   . TRP D 72  ? 1.1668 0.8192 0.8877 0.0857  0.1923  -0.0198 44  TRP D CZ2   
6882 C CZ3   . TRP D 72  ? 1.2169 0.8370 0.9236 0.0821  0.2139  -0.0232 44  TRP D CZ3   
6883 C CH2   . TRP D 72  ? 1.1887 0.8208 0.9010 0.0855  0.2030  -0.0168 44  TRP D CH2   
6884 N N     . SER D 73  ? 1.2283 0.9227 0.9540 0.0488  0.1991  -0.0828 45  SER D N     
6885 C CA    . SER D 73  ? 1.1951 0.9098 0.9265 0.0446  0.1923  -0.0916 45  SER D CA    
6886 C C     . SER D 73  ? 1.1581 0.8752 0.8909 0.0340  0.1951  -0.0999 45  SER D C     
6887 O O     . SER D 73  ? 1.1266 0.8590 0.8648 0.0325  0.1901  -0.1041 45  SER D O     
6888 C CB    . SER D 73  ? 1.1395 0.8636 0.8709 0.0429  0.1900  -0.0987 45  SER D CB    
6889 O OG    . SER D 73  ? 1.1444 0.8586 0.8708 0.0343  0.1966  -0.1056 45  SER D OG    
6890 N N     . GLN D 74  ? 1.1279 0.8296 0.8556 0.0267  0.2037  -0.1020 46  GLN D N     
6891 C CA    . GLN D 74  ? 1.1288 0.8312 0.8574 0.0158  0.2081  -0.1097 46  GLN D CA    
6892 C C     . GLN D 74  ? 1.2052 0.9006 0.9326 0.0175  0.2107  -0.1032 46  GLN D C     
6893 O O     . GLN D 74  ? 1.2506 0.9425 0.9772 0.0088  0.2166  -0.1077 46  GLN D O     
6894 C CB    . GLN D 74  ? 1.0322 0.7194 0.7548 0.0066  0.2168  -0.1152 46  GLN D CB    
6895 N N     . LEU D 75  ? 1.2277 0.9209 0.9544 0.0282  0.2067  -0.0929 47  LEU D N     
6896 C CA    . LEU D 75  ? 1.2600 0.9448 0.9832 0.0308  0.2087  -0.0861 47  LEU D CA    
6897 C C     . LEU D 75  ? 1.2221 0.9250 0.9514 0.0338  0.2002  -0.0870 47  LEU D C     
6898 O O     . LEU D 75  ? 1.2214 0.9345 0.9558 0.0418  0.1906  -0.0820 47  LEU D O     
6899 C CB    . LEU D 75  ? 1.2807 0.9486 0.9977 0.0407  0.2104  -0.0736 47  LEU D CB    
6900 C CG    . LEU D 75  ? 1.2946 0.9420 1.0049 0.0393  0.2196  -0.0706 47  LEU D CG    
6901 C CD1   . LEU D 75  ? 1.2803 0.9159 0.9867 0.0512  0.2196  -0.0582 47  LEU D CD1   
6902 C CD2   . LEU D 75  ? 1.1968 0.8298 0.9009 0.0313  0.2288  -0.0721 47  LEU D CD2   
6903 N N     . SER D 76  ? 1.2328 0.9412 0.9637 0.0271  0.2026  -0.0924 48  SER D N     
6904 C CA    . SER D 76  ? 1.2680 0.9929 1.0053 0.0300  0.1944  -0.0920 48  SER D CA    
6905 C C     . SER D 76  ? 1.2693 0.9831 1.0005 0.0363  0.1935  -0.0817 48  SER D C     
6906 O O     . SER D 76  ? 1.3312 1.0259 1.0535 0.0356  0.2014  -0.0768 48  SER D O     
6907 C CB    . SER D 76  ? 1.3144 1.0516 1.0565 0.0205  0.1979  -0.1022 48  SER D CB    
6908 O OG    . SER D 76  ? 1.3545 1.0767 1.0895 0.0141  0.2088  -0.1022 48  SER D OG    
6909 N N     . TRP D 77  ? 1.2648 0.9900 1.0001 0.0427  0.1836  -0.0784 49  TRP D N     
6910 C CA    . TRP D 77  ? 1.2823 0.9981 1.0115 0.0491  0.1805  -0.0687 49  TRP D CA    
6911 C C     . TRP D 77  ? 1.2770 1.0037 1.0078 0.0494  0.1761  -0.0715 49  TRP D C     
6912 O O     . TRP D 77  ? 1.3276 1.0723 1.0670 0.0488  0.1708  -0.0782 49  TRP D O     
6913 C CB    . TRP D 77  ? 1.2324 0.9476 0.9636 0.0585  0.1713  -0.0594 49  TRP D CB    
6914 C CG    . TRP D 77  ? 1.1800 0.8835 0.9089 0.0598  0.1763  -0.0552 49  TRP D CG    
6915 C CD1   . TRP D 77  ? 1.1013 0.8105 0.8350 0.0594  0.1761  -0.0588 49  TRP D CD1   
6916 C CD2   . TRP D 77  ? 1.2396 0.9233 0.9602 0.0624  0.1825  -0.0466 49  TRP D CD2   
6917 N NE1   . TRP D 77  ? 1.1939 0.8877 0.9226 0.0618  0.1823  -0.0533 49  TRP D NE1   
6918 C CE2   . TRP D 77  ? 1.2418 0.9199 0.9630 0.0638  0.1863  -0.0455 49  TRP D CE2   
6919 C CE3   . TRP D 77  ? 1.2368 0.9070 0.9489 0.0640  0.1852  -0.0394 49  TRP D CE3   
6920 C CZ2   . TRP D 77  ? 1.2581 0.9177 0.9728 0.0673  0.1930  -0.0375 49  TRP D CZ2   
6921 C CZ3   . TRP D 77  ? 1.2176 0.8699 0.9233 0.0672  0.1912  -0.0311 49  TRP D CZ3   
6922 C CH2   . TRP D 77  ? 1.2158 0.8630 0.9233 0.0690  0.1952  -0.0302 49  TRP D CH2   
6923 N N     . PRO D 78  ? 1.2964 1.0123 1.0184 0.0509  0.1783  -0.0664 50  PRO D N     
6924 C CA    . PRO D 78  ? 1.3842 1.1087 1.1057 0.0523  0.1744  -0.0687 50  PRO D CA    
6925 C C     . PRO D 78  ? 1.4881 1.2191 1.2124 0.0608  0.1610  -0.0641 50  PRO D C     
6926 O O     . PRO D 78  ? 1.4760 1.2026 1.2011 0.0660  0.1551  -0.0568 50  PRO D O     
6927 C CB    . PRO D 78  ? 1.3837 1.0914 1.0923 0.0513  0.1815  -0.0637 50  PRO D CB    
6928 C CG    . PRO D 78  ? 1.3946 1.0854 1.0976 0.0541  0.1833  -0.0546 50  PRO D CG    
6929 C CD    . PRO D 78  ? 1.3735 1.0683 1.0846 0.0516  0.1849  -0.0582 50  PRO D CD    
6930 N N     . GLN D 79  ? 1.5159 1.2575 1.2419 0.0623  0.1566  -0.0684 51  GLN D N     
6931 C CA    . GLN D 79  ? 1.5260 1.2732 1.2543 0.0699  0.1440  -0.0649 51  GLN D CA    
6932 C C     . GLN D 79  ? 1.4884 1.2200 1.2061 0.0750  0.1394  -0.0547 51  GLN D C     
6933 O O     . GLN D 79  ? 1.4497 1.1792 1.1697 0.0799  0.1310  -0.0475 51  GLN D O     
6934 C CB    . GLN D 79  ? 1.5412 1.3015 1.2725 0.0706  0.1415  -0.0723 51  GLN D CB    
6935 C CG    . GLN D 79  ? 1.6178 1.3976 1.3626 0.0687  0.1400  -0.0805 51  GLN D CG    
6936 C CD    . GLN D 79  ? 1.6603 1.4462 1.4125 0.0739  0.1292  -0.0771 51  GLN D CD    
6937 O OE1   . GLN D 79  ? 1.7040 1.4831 1.4527 0.0799  0.1208  -0.0699 51  GLN D OE1   
6938 N NE2   . GLN D 79  ? 1.6110 1.4098 1.3730 0.0713  0.1294  -0.0822 51  GLN D NE2   
6939 N N     . THR D 80  ? 1.4578 1.1790 1.1641 0.0738  0.1447  -0.0535 52  THR D N     
6940 C CA    . THR D 80  ? 1.4236 1.1293 1.1186 0.0779  0.1413  -0.0436 52  THR D CA    
6941 C C     . THR D 80  ? 1.4224 1.1153 1.1141 0.0758  0.1490  -0.0375 52  THR D C     
6942 O O     . THR D 80  ? 1.4027 1.0913 1.0918 0.0699  0.1607  -0.0413 52  THR D O     
6943 C CB    . THR D 80  ? 1.3818 1.0811 1.0640 0.0780  0.1436  -0.0446 52  THR D CB    
6944 O OG1   . THR D 80  ? 1.4328 1.1434 1.1178 0.0807  0.1371  -0.0507 52  THR D OG1   
6945 C CG2   . THR D 80  ? 1.3356 1.0193 1.0052 0.0822  0.1387  -0.0341 52  THR D CG2   
6946 N N     . PRO D 81  ? 1.3505 1.0369 1.0426 0.0804  0.1432  -0.0279 53  PRO D N     
6947 C CA    . PRO D 81  ? 1.2577 0.9325 0.9481 0.0795  0.1509  -0.0222 53  PRO D CA    
6948 C C     . PRO D 81  ? 1.1866 0.8457 0.8635 0.0772  0.1601  -0.0191 53  PRO D C     
6949 O O     . PRO D 81  ? 1.1722 0.8259 0.8389 0.0792  0.1568  -0.0159 53  PRO D O     
6950 C CB    . PRO D 81  ? 1.2039 0.8768 0.8975 0.0862  0.1411  -0.0114 53  PRO D CB    
6951 C CG    . PRO D 81  ? 1.1987 0.8854 0.9001 0.0890  0.1291  -0.0138 53  PRO D CG    
6952 C CD    . PRO D 81  ? 1.3138 1.0050 1.0104 0.0865  0.1294  -0.0223 53  PRO D CD    
6953 N N     . LEU D 82  ? 1.1678 0.8187 0.8436 0.0727  0.1718  -0.0202 54  LEU D N     
6954 C CA    . LEU D 82  ? 1.1180 0.7518 0.7815 0.0705  0.1819  -0.0161 54  LEU D CA    
6955 C C     . LEU D 82  ? 1.0621 0.6824 0.7238 0.0746  0.1840  -0.0059 54  LEU D C     
6956 O O     . LEU D 82  ? 1.0120 0.6364 0.6830 0.0766  0.1820  -0.0051 54  LEU D O     
6957 C CB    . LEU D 82  ? 1.1404 0.7736 0.8038 0.0614  0.1949  -0.0255 54  LEU D CB    
6958 C CG    . LEU D 82  ? 1.1537 0.8002 0.8190 0.0570  0.1954  -0.0354 54  LEU D CG    
6959 C CD1   . LEU D 82  ? 1.0730 0.7198 0.7404 0.0473  0.2084  -0.0438 54  LEU D CD1   
6960 C CD2   . LEU D 82  ? 1.1355 0.7768 0.7885 0.0601  0.1930  -0.0313 54  LEU D CD2   
6961 N N     . PRO D 83  ? 1.0232 0.6274 0.6728 0.0764  0.1881  0.0026  55  PRO D N     
6962 C CA    . PRO D 83  ? 0.9494 0.5409 0.5977 0.0814  0.1903  0.0131  55  PRO D CA    
6963 C C     . PRO D 83  ? 0.9675 0.5524 0.6194 0.0772  0.2020  0.0088  55  PRO D C     
6964 O O     . PRO D 83  ? 0.9790 0.5626 0.6296 0.0692  0.2113  -0.0004 55  PRO D O     
6965 C CB    . PRO D 83  ? 0.9654 0.5412 0.5984 0.0831  0.1935  0.0216  55  PRO D CB    
6966 C CG    . PRO D 83  ? 1.0060 0.5884 0.6326 0.0809  0.1891  0.0168  55  PRO D CG    
6967 C CD    . PRO D 83  ? 1.0362 0.6337 0.6724 0.0751  0.1903  0.0036  55  PRO D CD    
6968 N N     . VAL D 84  ? 0.9166 0.4972 0.5732 0.0827  0.2014  0.0156  56  VAL D N     
6969 C CA    . VAL D 84  ? 0.8855 0.4580 0.5446 0.0802  0.2119  0.0123  56  VAL D CA    
6970 C C     . VAL D 84  ? 0.9225 0.4743 0.5732 0.0850  0.2192  0.0233  56  VAL D C     
6971 O O     . VAL D 84  ? 0.9364 0.4864 0.5863 0.0932  0.2125  0.0352  56  VAL D O     
6972 C CB    . VAL D 84  ? 0.8468 0.4322 0.5186 0.0833  0.2062  0.0101  56  VAL D CB    
6973 C CG1   . VAL D 84  ? 0.8931 0.4666 0.5649 0.0832  0.2166  0.0093  56  VAL D CG1   
6974 C CG2   . VAL D 84  ? 0.9253 0.5292 0.6046 0.0776  0.2015  -0.0021 56  VAL D CG2   
6975 N N     . LEU D 85  ? 0.9061 0.4424 0.5510 0.0798  0.2327  0.0195  57  LEU D N     
6976 C CA    . LEU D 85  ? 0.9512 0.4652 0.5867 0.0837  0.2414  0.0293  57  LEU D CA    
6977 C C     . LEU D 85  ? 0.9807 0.4852 0.6194 0.0853  0.2493  0.0283  57  LEU D C     
6978 O O     . LEU D 85  ? 0.9632 0.4683 0.6043 0.0778  0.2554  0.0167  57  LEU D O     
6979 C CB    . LEU D 85  ? 0.9602 0.4599 0.5835 0.0762  0.2518  0.0269  57  LEU D CB    
6980 C CG    . LEU D 85  ? 0.9116 0.3861 0.5238 0.0796  0.2621  0.0367  57  LEU D CG    
6981 C CD1   . LEU D 85  ? 0.9118 0.3844 0.5203 0.0904  0.2541  0.0519  57  LEU D CD1   
6982 C CD2   . LEU D 85  ? 0.8260 0.2872 0.4272 0.0704  0.2734  0.0326  57  LEU D CD2   
6983 N N     . ASP D 86  ? 0.9572 0.4528 0.5956 0.0954  0.2492  0.0405  58  ASP D N     
6984 C CA    . ASP D 86  ? 0.9599 0.4422 0.5988 0.0989  0.2584  0.0416  58  ASP D CA    
6985 C C     . ASP D 86  ? 0.9818 0.4387 0.6087 0.1015  0.2691  0.0502  58  ASP D C     
6986 O O     . ASP D 86  ? 1.0118 0.4651 0.6359 0.1098  0.2651  0.0635  58  ASP D O     
6987 C CB    . ASP D 86  ? 0.9651 0.4585 0.6148 0.1094  0.2505  0.0495  58  ASP D CB    
6988 C CG    . ASP D 86  ? 1.1032 0.5835 0.7531 0.1138  0.2605  0.0500  58  ASP D CG    
6989 O OD1   . ASP D 86  ? 1.1365 0.6022 0.7795 0.1069  0.2720  0.0408  58  ASP D OD1   
6990 O OD2   . ASP D 86  ? 1.0952 0.5799 0.7521 0.1242  0.2570  0.0596  58  ASP D OD2   
6991 N N     . ILE D 87  ? 0.9959 0.4348 0.6154 0.0943  0.2824  0.0428  59  ILE D N     
6992 C CA    . ILE D 87  ? 0.9243 0.3388 0.5319 0.0951  0.2935  0.0497  59  ILE D CA    
6993 C C     . ILE D 87  ? 0.9950 0.4074 0.6066 0.1010  0.2979  0.0536  59  ILE D C     
6994 O O     . ILE D 87  ? 1.0356 0.4500 0.6517 0.0982  0.3008  0.0455  59  ILE D O     
6995 C CB    . ILE D 87  ? 0.8983 0.2991 0.4969 0.0818  0.3045  0.0392  59  ILE D CB    
6996 C CG1   . ILE D 87  ? 0.9684 0.3862 0.5678 0.0747  0.2973  0.0345  59  ILE D CG1   
6997 C CG2   . ILE D 87  ? 0.9333 0.3152 0.5214 0.0821  0.3141  0.0467  59  ILE D CG2   
6998 C CD1   . ILE D 87  ? 0.9842 0.3948 0.5778 0.0609  0.3071  0.0239  59  ILE D CD1   
6999 N N     . GLY D 88  ? 0.9972 0.4073 0.6077 0.1094  0.2980  0.0653  60  GLY D N     
7000 C CA    . GLY D 88  ? 0.9170 0.3257 0.5317 0.1168  0.3021  0.0699  60  GLY D CA    
7001 C C     . GLY D 88  ? 0.9335 0.3605 0.5613 0.1244  0.2936  0.0724  60  GLY D C     
7002 O O     . GLY D 88  ? 1.0463 0.4722 0.6770 0.1245  0.2983  0.0679  60  GLY D O     
7003 N N     . CYS D 89  ? 0.9271 0.3713 0.5628 0.1303  0.2807  0.0798  61  CYS D N     
7004 C CA    . CYS D 89  ? 0.9558 0.4189 0.6048 0.1366  0.2716  0.0823  61  CYS D CA    
7005 C C     . CYS D 89  ? 0.9726 0.4418 0.6302 0.1470  0.2726  0.0912  61  CYS D C     
7006 O O     . CYS D 89  ? 0.9143 0.3965 0.5824 0.1516  0.2687  0.0922  61  CYS D O     
7007 C CB    . CYS D 89  ? 0.9242 0.4036 0.5788 0.1388  0.2571  0.0877  61  CYS D CB    
7008 S SG    . CYS D 89  ? 0.9088 0.3946 0.5652 0.1460  0.2492  0.1021  61  CYS D SG    
7009 N N     . GLY D 90  ? 0.9836 0.4440 0.6375 0.1510  0.2778  0.0978  62  GLY D N     
7010 C CA    . GLY D 90  ? 0.9422 0.4087 0.6049 0.1615  0.2786  0.1069  62  GLY D CA    
7011 C C     . GLY D 90  ? 0.9074 0.3971 0.5846 0.1692  0.2641  0.1179  62  GLY D C     
7012 O O     . GLY D 90  ? 0.9165 0.4119 0.5932 0.1681  0.2550  0.1222  62  GLY D O     
7013 N N     . PRO D 91  ? 0.8815 0.3853 0.5718 0.1766  0.2617  0.1228  63  PRO D N     
7014 C CA    . PRO D 91  ? 0.8063 0.3339 0.5126 0.1829  0.2475  0.1334  63  PRO D CA    
7015 C C     . PRO D 91  ? 0.8218 0.3641 0.5337 0.1787  0.2353  0.1307  63  PRO D C     
7016 O O     . PRO D 91  ? 0.8253 0.3880 0.5510 0.1826  0.2228  0.1388  63  PRO D O     
7017 C CB    . PRO D 91  ? 0.8067 0.3425 0.5243 0.1916  0.2516  0.1385  63  PRO D CB    
7018 C CG    . PRO D 91  ? 0.8646 0.3853 0.5729 0.1880  0.2643  0.1279  63  PRO D CG    
7019 C CD    . PRO D 91  ? 0.9048 0.4027 0.5954 0.1795  0.2724  0.1195  63  PRO D CD    
7020 N N     . GLY D 92  ? 0.8324 0.3652 0.5343 0.1705  0.2384  0.1196  64  GLY D N     
7021 C CA    . GLY D 92  ? 0.8033 0.3480 0.5089 0.1665  0.2271  0.1169  64  GLY D CA    
7022 C C     . GLY D 92  ? 0.8175 0.3757 0.5341 0.1686  0.2240  0.1150  64  GLY D C     
7023 O O     . GLY D 92  ? 0.8284 0.4012 0.5522 0.1676  0.2121  0.1163  64  GLY D O     
7024 N N     . ASP D 93  ? 0.8238 0.3769 0.5409 0.1712  0.2343  0.1121  65  ASP D N     
7025 C CA    . ASP D 93  ? 0.7841 0.3496 0.5108 0.1735  0.2320  0.1105  65  ASP D CA    
7026 C C     . ASP D 93  ? 0.8206 0.3780 0.5389 0.1658  0.2346  0.0972  65  ASP D C     
7027 O O     . ASP D 93  ? 0.8541 0.4244 0.5796 0.1657  0.2269  0.0955  65  ASP D O     
7028 C CB    . ASP D 93  ? 0.8303 0.3948 0.5609 0.1804  0.2415  0.1136  65  ASP D CB    
7029 C CG    . ASP D 93  ? 0.9113 0.4880 0.6539 0.1889  0.2377  0.1270  65  ASP D CG    
7030 O OD1   . ASP D 93  ? 0.9752 0.5736 0.7335 0.1927  0.2269  0.1347  65  ASP D OD1   
7031 O OD2   . ASP D 93  ? 0.8851 0.4500 0.6219 0.1914  0.2453  0.1298  65  ASP D OD2   
7032 N N     . ILE D 94  ? 0.8249 0.3621 0.5289 0.1590  0.2450  0.0874  66  ILE D N     
7033 C CA    . ILE D 94  ? 0.8220 0.3537 0.5194 0.1502  0.2463  0.0733  66  ILE D CA    
7034 C C     . ILE D 94  ? 0.8216 0.3589 0.5189 0.1468  0.2359  0.0727  66  ILE D C     
7035 O O     . ILE D 94  ? 0.8055 0.3583 0.5077 0.1412  0.2287  0.0642  66  ILE D O     
7036 C CB    . ILE D 94  ? 0.8997 0.4110 0.5836 0.1419  0.2591  0.0630  66  ILE D CB    
7037 C CG1   . ILE D 94  ? 0.8645 0.3720 0.5478 0.1429  0.2677  0.0592  66  ILE D CG1   
7038 C CG2   . ILE D 94  ? 0.9251 0.4342 0.6031 0.1308  0.2583  0.0489  66  ILE D CG2   
7039 C CD1   . ILE D 94  ? 0.8930 0.3809 0.5641 0.1341  0.2791  0.0505  66  ILE D CD1   
7040 N N     . ALA D 95  ? 0.8257 0.3607 0.5200 0.1475  0.2322  0.0808  67  ALA D N     
7041 C CA    . ALA D 95  ? 0.8038 0.3463 0.4970 0.1433  0.2215  0.0804  67  ALA D CA    
7042 C C     . ALA D 95  ? 0.7475 0.3132 0.4545 0.1472  0.2069  0.0861  67  ALA D C     
7043 O O     . ALA D 95  ? 0.8231 0.4028 0.5330 0.1412  0.1979  0.0790  67  ALA D O     
7044 C CB    . ALA D 95  ? 0.8524 0.3854 0.5376 0.1442  0.2214  0.0886  67  ALA D CB    
7045 N N     . ARG D 96  ? 0.7007 0.2753 0.4183 0.1560  0.2036  0.0979  68  ARG D N     
7046 C CA    . ARG D 96  ? 0.7383 0.3345 0.4698 0.1592  0.1896  0.1046  68  ARG D CA    
7047 C C     . ARG D 96  ? 0.7856 0.3906 0.5247 0.1600  0.1900  0.0995  68  ARG D C     
7048 O O     . ARG D 96  ? 0.7908 0.4118 0.5360 0.1558  0.1797  0.0949  68  ARG D O     
7049 C CB    . ARG D 96  ? 0.7768 0.3872 0.5209 0.1656  0.1835  0.1177  68  ARG D CB    
7050 C CG    . ARG D 96  ? 0.8237 0.4573 0.5856 0.1690  0.1720  0.1243  68  ARG D CG    
7051 C CD    . ARG D 96  ? 0.8789 0.5214 0.6419 0.1650  0.1574  0.1246  68  ARG D CD    
7052 N NE    . ARG D 96  ? 0.9418 0.6038 0.7200 0.1665  0.1479  0.1282  68  ARG D NE    
7053 C CZ    . ARG D 96  ? 1.0012 0.6787 0.7893 0.1656  0.1328  0.1348  68  ARG D CZ    
7054 N NH1   . ARG D 96  ? 1.0484 0.7246 0.8323 0.1637  0.1250  0.1386  68  ARG D NH1   
7055 N NH2   . ARG D 96  ? 0.9514 0.6455 0.7533 0.1664  0.1254  0.1375  68  ARG D NH2   
7056 N N     . LYS D 97  ? 0.7981 0.3982 0.5384 0.1639  0.2007  0.0986  69  LYS D N     
7057 C CA    . LYS D 97  ? 0.7613 0.3724 0.5101 0.1664  0.2006  0.0963  69  LYS D CA    
7058 C C     . LYS D 97  ? 0.7432 0.3535 0.4856 0.1577  0.2049  0.0793  69  LYS D C     
7059 O O     . LYS D 97  ? 0.7769 0.4008 0.5263 0.1576  0.2017  0.0757  69  LYS D O     
7060 C CB    . LYS D 97  ? 0.8165 0.4297 0.5715 0.1738  0.2083  0.1030  69  LYS D CB    
7061 C CG    . LYS D 97  ? 0.8159 0.4447 0.5842 0.1793  0.2009  0.1173  69  LYS D CG    
7062 C CD    . LYS D 97  ? 0.8052 0.4353 0.5789 0.1866  0.2102  0.1228  69  LYS D CD    
7063 C CE    . LYS D 97  ? 0.9184 0.5636 0.7060 0.1919  0.2032  0.1361  69  LYS D CE    
7064 N NZ    . LYS D 97  ? 1.1760 0.8206 0.9679 0.1996  0.2135  0.1415  69  LYS D NZ    
7065 N N     . VAL D 98  ? 0.7474 0.3431 0.4773 0.1502  0.2119  0.0691  70  VAL D N     
7066 C CA    . VAL D 98  ? 0.7117 0.3063 0.4358 0.1414  0.2165  0.0530  70  VAL D CA    
7067 C C     . VAL D 98  ? 0.7997 0.4012 0.5213 0.1316  0.2093  0.0441  70  VAL D C     
7068 O O     . VAL D 98  ? 0.8799 0.4961 0.6059 0.1269  0.2032  0.0358  70  VAL D O     
7069 C CB    . VAL D 98  ? 0.7764 0.3478 0.4882 0.1399  0.2321  0.0470  70  VAL D CB    
7070 C CG1   . VAL D 98  ? 0.8156 0.3874 0.5221 0.1300  0.2359  0.0301  70  VAL D CG1   
7071 C CG2   . VAL D 98  ? 0.9051 0.4690 0.6188 0.1507  0.2399  0.0557  70  VAL D CG2   
7072 N N     . LEU D 99  ? 0.7123 0.3033 0.4267 0.1291  0.2103  0.0461  71  LEU D N     
7073 C CA    . LEU D 99  ? 0.8095 0.4053 0.5202 0.1199  0.2058  0.0372  71  LEU D CA    
7074 C C     . LEU D 99  ? 0.8596 0.4736 0.5785 0.1212  0.1907  0.0414  71  LEU D C     
7075 O O     . LEU D 99  ? 0.8968 0.5233 0.6182 0.1154  0.1848  0.0324  71  LEU D O     
7076 C CB    . LEU D 99  ? 0.8171 0.3946 0.5161 0.1168  0.2131  0.0380  71  LEU D CB    
7077 C CG    . LEU D 99  ? 0.8537 0.4123 0.5429 0.1115  0.2278  0.0298  71  LEU D CG    
7078 C CD1   . LEU D 99  ? 0.9388 0.4789 0.6168 0.1096  0.2346  0.0335  71  LEU D CD1   
7079 C CD2   . LEU D 99  ? 0.8804 0.4469 0.5697 0.1011  0.2289  0.0138  71  LEU D CD2   
7080 N N     . ALA D 100 ? 0.8287 0.4443 0.5517 0.1287  0.1843  0.0552  72  ALA D N     
7081 C CA    . ALA D 100 ? 0.7662 0.3960 0.4950 0.1291  0.1698  0.0594  72  ALA D CA    
7082 C C     . ALA D 100 ? 0.7884 0.4370 0.5280 0.1284  0.1612  0.0555  72  ALA D C     
7083 O O     . ALA D 100 ? 0.9049 0.5628 0.6451 0.1238  0.1529  0.0495  72  ALA D O     
7084 C CB    . ALA D 100 ? 0.7509 0.3789 0.4827 0.1370  0.1644  0.0754  72  ALA D CB    
7085 N N     . PRO D 101 ? 0.7275 0.3824 0.4755 0.1331  0.1627  0.0586  73  PRO D N     
7086 C CA    . PRO D 101 ? 0.8172 0.4899 0.5748 0.1323  0.1542  0.0552  73  PRO D CA    
7087 C C     . PRO D 101 ? 0.9049 0.5817 0.6588 0.1245  0.1563  0.0398  73  PRO D C     
7088 O O     . PRO D 101 ? 0.9308 0.6217 0.6904 0.1225  0.1471  0.0361  73  PRO D O     
7089 C CB    . PRO D 101 ? 0.8101 0.4859 0.5753 0.1393  0.1584  0.0621  73  PRO D CB    
7090 C CG    . PRO D 101 ? 0.8051 0.4681 0.5681 0.1455  0.1646  0.0730  73  PRO D CG    
7091 C CD    . PRO D 101 ? 0.7713 0.4180 0.5209 0.1404  0.1714  0.0668  73  PRO D CD    
7092 N N     . ARG D 102 ? 0.9355 0.6003 0.6803 0.1200  0.1678  0.0309  74  ARG D N     
7093 C CA    . ARG D 102 ? 0.9912 0.6608 0.7334 0.1123  0.1702  0.0164  74  ARG D CA    
7094 C C     . ARG D 102 ? 1.0348 0.7059 0.7727 0.1054  0.1670  0.0091  74  ARG D C     
7095 O O     . ARG D 102 ? 1.0773 0.7572 0.8160 0.0995  0.1661  -0.0021 74  ARG D O     
7096 C CB    . ARG D 102 ? 0.9787 0.6348 0.7133 0.1097  0.1839  0.0096  74  ARG D CB    
7097 C CG    . ARG D 102 ? 0.9798 0.6373 0.7180 0.1155  0.1875  0.0127  74  ARG D CG    
7098 C CD    . ARG D 102 ? 0.9775 0.6167 0.7061 0.1144  0.2017  0.0082  74  ARG D CD    
7099 N NE    . ARG D 102 ? 1.0216 0.6626 0.7521 0.1196  0.2055  0.0091  74  ARG D NE    
7100 C CZ    . ARG D 102 ? 0.9753 0.6149 0.7104 0.1295  0.2068  0.0213  74  ARG D CZ    
7101 N NH1   . ARG D 102 ? 0.9088 0.5454 0.6476 0.1351  0.2040  0.0339  74  ARG D NH1   
7102 N NH2   . ARG D 102 ? 0.9840 0.6256 0.7198 0.1339  0.2111  0.0210  74  ARG D NH2   
7103 N N     . LEU D 103 ? 1.0352 0.6986 0.7685 0.1064  0.1653  0.0153  75  LEU D N     
7104 C CA    . LEU D 103 ? 1.0334 0.6976 0.7616 0.1005  0.1631  0.0089  75  LEU D CA    
7105 C C     . LEU D 103 ? 1.0570 0.7380 0.7922 0.1008  0.1502  0.0073  75  LEU D C     
7106 O O     . LEU D 103 ? 0.9779 0.6673 0.7211 0.1061  0.1415  0.0146  75  LEU D O     
7107 C CB    . LEU D 103 ? 0.9285 0.5791 0.6483 0.1022  0.1647  0.0168  75  LEU D CB    
7108 C CG    . LEU D 103 ? 0.9442 0.5756 0.6548 0.1010  0.1782  0.0178  75  LEU D CG    
7109 C CD1   . LEU D 103 ? 0.9246 0.5444 0.6278 0.1046  0.1774  0.0284  75  LEU D CD1   
7110 C CD2   . LEU D 103 ? 1.0168 0.6444 0.7216 0.0916  0.1871  0.0047  75  LEU D CD2   
7111 N N     . PRO D 104 ? 1.0824 0.7684 0.8151 0.0952  0.1490  -0.0021 76  PRO D N     
7112 C CA    . PRO D 104 ? 1.0591 0.7584 0.7968 0.0961  0.1370  -0.0033 76  PRO D CA    
7113 C C     . PRO D 104 ? 1.0239 0.7192 0.7594 0.1008  0.1284  0.0073  76  PRO D C     
7114 O O     . PRO D 104 ? 1.0250 0.7074 0.7530 0.1021  0.1322  0.0137  76  PRO D O     
7115 C CB    . PRO D 104 ? 1.0575 0.7600 0.7911 0.0895  0.1403  -0.0149 76  PRO D CB    
7116 C CG    . PRO D 104 ? 1.0749 0.7708 0.8053 0.0840  0.1530  -0.0217 76  PRO D CG    
7117 C CD    . PRO D 104 ? 1.0639 0.7446 0.7900 0.0876  0.1590  -0.0124 76  PRO D CD    
7118 N N     . ALA D 105 ? 1.0276 0.7336 0.7694 0.1034  0.1164  0.0092  77  ALA D N     
7119 C CA    . ALA D 105 ? 0.9983 0.7014 0.7384 0.1071  0.1065  0.0186  77  ALA D CA    
7120 C C     . ALA D 105 ? 0.9962 0.6908 0.7241 0.1045  0.1074  0.0156  77  ALA D C     
7121 O O     . ALA D 105 ? 0.9763 0.6738 0.7008 0.1004  0.1106  0.0053  77  ALA D O     
7122 C CB    . ALA D 105 ? 0.9965 0.7119 0.7455 0.1092  0.0937  0.0200  77  ALA D CB    
7123 N N     . GLY D 106 ? 0.9655 0.6503 0.6869 0.1072  0.1047  0.0251  78  GLY D N     
7124 C CA    . GLY D 106 ? 0.9798 0.6550 0.6878 0.1054  0.1059  0.0237  78  GLY D CA    
7125 C C     . GLY D 106 ? 0.9709 0.6341 0.6698 0.1025  0.1197  0.0218  78  GLY D C     
7126 O O     . GLY D 106 ? 0.9508 0.6043 0.6374 0.1017  0.1215  0.0230  78  GLY D O     
7127 N N     . THR D 107 ? 1.0188 0.6815 0.7224 0.1008  0.1296  0.0188  79  THR D N     
7128 C CA    . THR D 107 ? 1.0003 0.6501 0.6955 0.0974  0.1433  0.0168  79  THR D CA    
7129 C C     . THR D 107 ? 1.0184 0.6548 0.7085 0.1023  0.1452  0.0295  79  THR D C     
7130 O O     . THR D 107 ? 1.0031 0.6410 0.7009 0.1072  0.1431  0.0372  79  THR D O     
7131 C CB    . THR D 107 ? 0.9802 0.6329 0.6815 0.0937  0.1525  0.0089  79  THR D CB    
7132 O OG1   . THR D 107 ? 1.0225 0.6891 0.7291 0.0894  0.1500  -0.0024 79  THR D OG1   
7133 C CG2   . THR D 107 ? 0.9835 0.6213 0.6759 0.0894  0.1666  0.0067  79  THR D CG2   
7134 N N     . ARG D 108 ? 0.9992 0.6230 0.6763 0.1012  0.1497  0.0319  80  ARG D N     
7135 C CA    . ARG D 108 ? 0.9080 0.5184 0.5789 0.1060  0.1518  0.0442  80  ARG D CA    
7136 C C     . ARG D 108 ? 0.9155 0.5135 0.5844 0.1046  0.1665  0.0437  80  ARG D C     
7137 O O     . ARG D 108 ? 0.8971 0.4933 0.5642 0.0980  0.1760  0.0332  80  ARG D O     
7138 C CB    . ARG D 108 ? 0.9305 0.5323 0.5869 0.1058  0.1497  0.0476  80  ARG D CB    
7139 C CG    . ARG D 108 ? 0.9607 0.5705 0.6171 0.1088  0.1340  0.0516  80  ARG D CG    
7140 C CD    . ARG D 108 ? 1.0390 0.6381 0.6792 0.1097  0.1318  0.0570  80  ARG D CD    
7141 N NE    . ARG D 108 ? 1.2541 0.8602 0.8914 0.1102  0.1184  0.0556  80  ARG D NE    
7142 C CZ    . ARG D 108 ? 1.2874 0.8964 0.9185 0.1063  0.1183  0.0453  80  ARG D CZ    
7143 N NH1   . ARG D 108 ? 1.2851 0.8928 0.9137 0.1013  0.1305  0.0357  80  ARG D NH1   
7144 N NH2   . ARG D 108 ? 1.2710 0.8844 0.8987 0.1075  0.1057  0.0446  80  ARG D NH2   
7145 N N     . LEU D 109 ? 0.8895 0.4788 0.5587 0.1108  0.1683  0.0551  81  LEU D N     
7146 C CA    . LEU D 109 ? 0.8522 0.4279 0.5194 0.1110  0.1819  0.0560  81  LEU D CA    
7147 C C     . LEU D 109 ? 0.8021 0.3602 0.4577 0.1146  0.1868  0.0665  81  LEU D C     
7148 O O     . LEU D 109 ? 0.7672 0.3262 0.4216 0.1206  0.1780  0.0778  81  LEU D O     
7149 C CB    . LEU D 109 ? 0.8295 0.4106 0.5090 0.1166  0.1813  0.0600  81  LEU D CB    
7150 C CG    . LEU D 109 ? 0.8042 0.3701 0.4814 0.1182  0.1951  0.0613  81  LEU D CG    
7151 C CD1   . LEU D 109 ? 0.8718 0.4312 0.5438 0.1090  0.2063  0.0474  81  LEU D CD1   
7152 C CD2   . LEU D 109 ? 0.7597 0.3330 0.4490 0.1248  0.1936  0.0658  81  LEU D CD2   
7153 N N     . VAL D 110 ? 0.7829 0.3249 0.4296 0.1105  0.2007  0.0629  82  VAL D N     
7154 C CA    . VAL D 110 ? 0.7745 0.2973 0.4094 0.1137  0.2077  0.0727  82  VAL D CA    
7155 C C     . VAL D 110 ? 0.8692 0.3774 0.5046 0.1151  0.2209  0.0734  82  VAL D C     
7156 O O     . VAL D 110 ? 0.9604 0.4667 0.5973 0.1083  0.2292  0.0620  82  VAL D O     
7157 C CB    . VAL D 110 ? 0.7840 0.2981 0.4047 0.1068  0.2129  0.0682  82  VAL D CB    
7158 C CG1   . VAL D 110 ? 0.7940 0.2879 0.4017 0.1107  0.2197  0.0796  82  VAL D CG1   
7159 C CG2   . VAL D 110 ? 0.8400 0.3682 0.4593 0.1055  0.2006  0.0659  82  VAL D CG2   
7160 N N     . ALA D 111 ? 0.8337 0.3315 0.4677 0.1239  0.2225  0.0866  83  ALA D N     
7161 C CA    . ALA D 111 ? 0.8466 0.3310 0.4815 0.1269  0.2344  0.0881  83  ALA D CA    
7162 C C     . ALA D 111 ? 0.8121 0.2877 0.4403 0.1291  0.2390  0.0952  83  ALA D C     
7163 O O     . ALA D 111 ? 0.8112 0.2961 0.4419 0.1347  0.2294  0.1049  83  ALA D O     
7164 C CB    . ALA D 111 ? 0.7796 0.2800 0.4306 0.1346  0.2283  0.0928  83  ALA D CB    
7165 N N     . CYS D 112 ? 0.8300 0.2879 0.4503 0.1244  0.2532  0.0901  84  CYS D N     
7166 C CA    . CYS D 112 ? 0.8508 0.2975 0.4633 0.1258  0.2591  0.0957  84  CYS D CA    
7167 C C     . CYS D 112 ? 0.8632 0.3014 0.4788 0.1289  0.2693  0.0960  84  CYS D C     
7168 O O     . CYS D 112 ? 0.9157 0.3543 0.5369 0.1282  0.2736  0.0902  84  CYS D O     
7169 C CB    . CYS D 112 ? 0.8655 0.2961 0.4627 0.1163  0.2675  0.0899  84  CYS D CB    
7170 S SG    . CYS D 112 ? 1.0127 0.4320 0.6061 0.1038  0.2788  0.0744  84  CYS D SG    
7171 N N     . ASP D 113 ? 0.8815 0.3114 0.4925 0.1325  0.2733  0.1028  85  ASP D N     
7172 C CA    . ASP D 113 ? 0.8971 0.3175 0.5094 0.1368  0.2829  0.1047  85  ASP D CA    
7173 C C     . ASP D 113 ? 0.9180 0.3286 0.5229 0.1398  0.2858  0.1125  85  ASP D C     
7174 O O     . ASP D 113 ? 0.9149 0.3343 0.5199 0.1433  0.2758  0.1203  85  ASP D O     
7175 C CB    . ASP D 113 ? 0.8842 0.3207 0.5116 0.1465  0.2766  0.1108  85  ASP D CB    
7176 C CG    . ASP D 113 ? 0.9894 0.4154 0.6175 0.1497  0.2882  0.1098  85  ASP D CG    
7177 O OD1   . ASP D 113 ? 1.0378 0.4535 0.6617 0.1538  0.2940  0.1154  85  ASP D OD1   
7178 O OD2   . ASP D 113 ? 0.9875 0.4152 0.6196 0.1484  0.2914  0.1035  85  ASP D OD2   
7179 N N     . ILE D 114 ? 0.9406 0.3327 0.5384 0.1383  0.2990  0.1105  86  ILE D N     
7180 C CA    . ILE D 114 ? 0.9620 0.3440 0.5528 0.1417  0.3020  0.1183  86  ILE D CA    
7181 C C     . ILE D 114 ? 0.9954 0.3909 0.5967 0.1542  0.2931  0.1310  86  ILE D C     
7182 O O     . ILE D 114 ? 1.0122 0.4123 0.6119 0.1579  0.2856  0.1398  86  ILE D O     
7183 C CB    . ILE D 114 ? 1.0009 0.3595 0.5822 0.1376  0.3182  0.1136  86  ILE D CB    
7184 C CG1   . ILE D 114 ? 1.0080 0.3534 0.5793 0.1238  0.3269  0.1015  86  ILE D CG1   
7185 C CG2   . ILE D 114 ? 1.1193 0.4678 0.6941 0.1425  0.3208  0.1228  86  ILE D CG2   
7186 C CD1   . ILE D 114 ? 1.0454 0.3682 0.6083 0.1187  0.3422  0.0965  86  ILE D CD1   
7187 N N     . SER D 115 ? 0.9536 0.3557 0.5656 0.1605  0.2940  0.1324  87  SER D N     
7188 C CA    . SER D 115 ? 0.9561 0.3704 0.5795 0.1722  0.2876  0.1442  87  SER D CA    
7189 C C     . SER D 115 ? 0.9337 0.3702 0.5662 0.1754  0.2704  0.1518  87  SER D C     
7190 O O     . SER D 115 ? 0.9253 0.3766 0.5657 0.1736  0.2623  0.1486  87  SER D O     
7191 C CB    . SER D 115 ? 1.0023 0.4211 0.6357 0.1773  0.2920  0.1429  87  SER D CB    
7192 O OG    . SER D 115 ? 1.0358 0.4746 0.6845 0.1873  0.2819  0.1535  87  SER D OG    
7193 N N     . PRO D 116 ? 0.9432 0.3820 0.5742 0.1797  0.2641  0.1619  88  PRO D N     
7194 C CA    . PRO D 116 ? 0.9267 0.3871 0.5671 0.1830  0.2469  0.1699  88  PRO D CA    
7195 C C     . PRO D 116 ? 0.9120 0.3919 0.5714 0.1907  0.2401  0.1759  88  PRO D C     
7196 O O     . PRO D 116 ? 0.8931 0.3925 0.5625 0.1913  0.2259  0.1796  88  PRO D O     
7197 C CB    . PRO D 116 ? 0.9458 0.4010 0.5789 0.1862  0.2441  0.1796  88  PRO D CB    
7198 C CG    . PRO D 116 ? 0.9695 0.3995 0.5868 0.1820  0.2595  0.1743  88  PRO D CG    
7199 C CD    . PRO D 116 ? 0.9704 0.3917 0.5903 0.1812  0.2720  0.1663  88  PRO D CD    
7200 N N     . GLU D 117 ? 0.9271 0.4016 0.5913 0.1965  0.2500  0.1770  89  GLU D N     
7201 C CA    . GLU D 117 ? 0.9137 0.4062 0.5958 0.2037  0.2456  0.1819  89  GLU D CA    
7202 C C     . GLU D 117 ? 0.8901 0.3930 0.5783 0.1991  0.2423  0.1737  89  GLU D C     
7203 O O     . GLU D 117 ? 0.8714 0.3956 0.5748 0.2022  0.2314  0.1784  89  GLU D O     
7204 C CB    . GLU D 117 ? 0.9316 0.4132 0.6146 0.2106  0.2591  0.1835  89  GLU D CB    
7205 C CG    . GLU D 117 ? 0.9584 0.4260 0.6337 0.2153  0.2647  0.1909  89  GLU D CG    
7206 C CD    . GLU D 117 ? 1.0550 0.4975 0.7109 0.2079  0.2757  0.1833  89  GLU D CD    
7207 O OE1   . GLU D 117 ? 1.1266 0.5540 0.7751 0.2034  0.2881  0.1733  89  GLU D OE1   
7208 O OE2   . GLU D 117 ? 1.1413 0.5788 0.7888 0.2061  0.2719  0.1874  89  GLU D OE2   
7209 N N     . MET D 118 ? 0.8900 0.3784 0.5669 0.1913  0.2515  0.1617  90  MET D N     
7210 C CA    . MET D 118 ? 0.8646 0.3616 0.5456 0.1865  0.2484  0.1536  90  MET D CA    
7211 C C     . MET D 118 ? 0.8464 0.3580 0.5302 0.1827  0.2331  0.1549  90  MET D C     
7212 O O     . MET D 118 ? 0.8259 0.3559 0.5222 0.1838  0.2234  0.1561  90  MET D O     
7213 C CB    . MET D 118 ? 0.8726 0.3496 0.5399 0.1782  0.2614  0.1406  90  MET D CB    
7214 C CG    . MET D 118 ? 0.8887 0.3518 0.5533 0.1808  0.2761  0.1375  90  MET D CG    
7215 S SD    . MET D 118 ? 0.8730 0.3530 0.5536 0.1877  0.2744  0.1390  90  MET D SD    
7216 C CE    . MET D 118 ? 0.9537 0.4107 0.6242 0.1881  0.2934  0.1329  90  MET D CE    
7217 N N     . VAL D 119 ? 0.8550 0.3581 0.5265 0.1781  0.2311  0.1547  91  VAL D N     
7218 C CA    . VAL D 119 ? 0.8410 0.3549 0.5117 0.1740  0.2176  0.1550  91  VAL D CA    
7219 C C     . VAL D 119 ? 0.8296 0.3655 0.5154 0.1800  0.2021  0.1662  91  VAL D C     
7220 O O     . VAL D 119 ? 0.8113 0.3621 0.5036 0.1779  0.1900  0.1662  91  VAL D O     
7221 C CB    . VAL D 119 ? 0.8564 0.3555 0.5095 0.1688  0.2198  0.1536  91  VAL D CB    
7222 C CG1   . VAL D 119 ? 0.8447 0.3541 0.4951 0.1654  0.2059  0.1545  91  VAL D CG1   
7223 C CG2   . VAL D 119 ? 0.8666 0.3451 0.5063 0.1615  0.2348  0.1421  91  VAL D CG2   
7224 N N     . ASP D 120 ? 0.8413 0.3794 0.5329 0.1871  0.2021  0.1761  92  ASP D N     
7225 C CA    . ASP D 120 ? 0.8319 0.3914 0.5392 0.1924  0.1877  0.1872  92  ASP D CA    
7226 C C     . ASP D 120 ? 0.8132 0.3892 0.5382 0.1952  0.1852  0.1872  92  ASP D C     
7227 O O     . ASP D 120 ? 0.8622 0.4575 0.5996 0.1952  0.1712  0.1919  92  ASP D O     
7228 C CB    . ASP D 120 ? 0.8509 0.4078 0.5598 0.1995  0.1892  0.1979  92  ASP D CB    
7229 C CG    . ASP D 120 ? 0.8909 0.4378 0.5851 0.1973  0.1861  0.2013  92  ASP D CG    
7230 O OD1   . ASP D 120 ? 0.8612 0.4072 0.5460 0.1907  0.1797  0.1970  92  ASP D OD1   
7231 O OD2   . ASP D 120 ? 0.9124 0.4516 0.6035 0.2023  0.1904  0.2083  92  ASP D OD2   
7232 N N     . PHE D 121 ? 0.8164 0.3845 0.5422 0.1974  0.1988  0.1819  93  PHE D N     
7233 C CA    . PHE D 121 ? 0.8003 0.3829 0.5413 0.2002  0.1980  0.1815  93  PHE D CA    
7234 C C     . PHE D 121 ? 0.7798 0.3697 0.5215 0.1936  0.1913  0.1740  93  PHE D C     
7235 O O     . PHE D 121 ? 0.8376 0.4463 0.5943 0.1949  0.1827  0.1769  93  PHE D O     
7236 C CB    . PHE D 121 ? 0.8119 0.3813 0.5499 0.2038  0.2150  0.1770  93  PHE D CB    
7237 C CG    . PHE D 121 ? 0.7993 0.3828 0.5521 0.2083  0.2158  0.1780  93  PHE D CG    
7238 C CD1   . PHE D 121 ? 0.7842 0.3705 0.5375 0.2039  0.2165  0.1694  93  PHE D CD1   
7239 C CD2   . PHE D 121 ? 0.8938 0.4879 0.6600 0.2173  0.2163  0.1880  93  PHE D CD2   
7240 C CE1   . PHE D 121 ? 0.8145 0.4137 0.5807 0.2082  0.2176  0.1708  93  PHE D CE1   
7241 C CE2   . PHE D 121 ? 0.9179 0.5252 0.6973 0.2216  0.2179  0.1894  93  PHE D CE2   
7242 C CZ    . PHE D 121 ? 0.8580 0.4677 0.6372 0.2170  0.2186  0.1808  93  PHE D CZ    
7243 N N     . CYS D 122 ? 0.8193 0.3946 0.5452 0.1863  0.1952  0.1644  94  CYS D N     
7244 C CA    . CYS D 122 ? 0.7928 0.3730 0.5180 0.1802  0.1900  0.1567  94  CYS D CA    
7245 C C     . CYS D 122 ? 0.8397 0.4375 0.5724 0.1789  0.1721  0.1624  94  CYS D C     
7246 O O     . CYS D 122 ? 0.9197 0.5322 0.6632 0.1781  0.1641  0.1618  94  CYS D O     
7247 C CB    . CYS D 122 ? 0.7741 0.3341 0.4804 0.1727  0.1987  0.1458  94  CYS D CB    
7248 S SG    . CYS D 122 ? 0.7896 0.3277 0.4861 0.1713  0.2191  0.1366  94  CYS D SG    
7249 N N     . ARG D 123 ? 0.7605 0.3562 0.4867 0.1784  0.1654  0.1679  95  ARG D N     
7250 C CA    . ARG D 123 ? 0.7751 0.3836 0.5041 0.1759  0.1486  0.1722  95  ARG D CA    
7251 C C     . ARG D 123 ? 0.9170 0.5481 0.6668 0.1798  0.1363  0.1818  95  ARG D C     
7252 O O     . ARG D 123 ? 0.9837 0.6263 0.7374 0.1772  0.1214  0.1853  95  ARG D O     
7253 C CB    . ARG D 123 ? 0.8064 0.4056 0.5217 0.1748  0.1454  0.1762  95  ARG D CB    
7254 C CG    . ARG D 123 ? 0.7836 0.3625 0.4778 0.1692  0.1548  0.1667  95  ARG D CG    
7255 C CD    . ARG D 123 ? 0.8393 0.4100 0.5196 0.1685  0.1514  0.1714  95  ARG D CD    
7256 N NE    . ARG D 123 ? 0.8065 0.3578 0.4667 0.1629  0.1613  0.1628  95  ARG D NE    
7257 C CZ    . ARG D 123 ? 0.8273 0.3635 0.4738 0.1627  0.1688  0.1643  95  ARG D CZ    
7258 N NH1   . ARG D 123 ? 0.8399 0.3771 0.4898 0.1682  0.1676  0.1741  95  ARG D NH1   
7259 N NH2   . ARG D 123 ? 0.8364 0.3562 0.4658 0.1568  0.1779  0.1561  95  ARG D NH2   
7260 N N     . GLN D 124 ? 0.9251 0.5623 0.6878 0.1859  0.1422  0.1862  96  GLN D N     
7261 C CA    . GLN D 124 ? 0.9168 0.5758 0.7003 0.1896  0.1320  0.1953  96  GLN D CA    
7262 C C     . GLN D 124 ? 0.9148 0.5836 0.7101 0.1902  0.1352  0.1913  96  GLN D C     
7263 O O     . GLN D 124 ? 0.9590 0.6441 0.7661 0.1880  0.1234  0.1935  96  GLN D O     
7264 C CB    . GLN D 124 ? 0.9164 0.5776 0.7072 0.1971  0.1354  0.2053  96  GLN D CB    
7265 C CG    . GLN D 124 ? 1.0349 0.6943 0.8199 0.1972  0.1268  0.2132  96  GLN D CG    
7266 C CD    . GLN D 124 ? 1.1563 0.8161 0.9475 0.2052  0.1315  0.2228  96  GLN D CD    
7267 O OE1   . GLN D 124 ? 1.1276 0.7946 0.9316 0.2110  0.1378  0.2257  96  GLN D OE1   
7268 N NE2   . GLN D 124 ? 1.1062 0.7581 0.8877 0.2059  0.1287  0.2281  96  GLN D NE2   
7269 N N     . HIS D 125 ? 0.8423 0.5006 0.6340 0.1930  0.1509  0.1856  97  HIS D N     
7270 C CA    . HIS D 125 ? 0.8474 0.5148 0.6501 0.1950  0.1551  0.1833  97  HIS D CA    
7271 C C     . HIS D 125 ? 0.9039 0.5656 0.6986 0.1891  0.1571  0.1719  97  HIS D C     
7272 O O     . HIS D 125 ? 1.0151 0.6885 0.8202 0.1895  0.1553  0.1709  97  HIS D O     
7273 C CB    . HIS D 125 ? 0.8275 0.4868 0.6303 0.2019  0.1709  0.1838  97  HIS D CB    
7274 C CG    . HIS D 125 ? 0.8333 0.4997 0.6458 0.2089  0.1696  0.1955  97  HIS D CG    
7275 N ND1   . HIS D 125 ? 0.8903 0.5455 0.6938 0.2103  0.1710  0.1992  97  HIS D ND1   
7276 C CD2   . HIS D 125 ? 0.8549 0.5386 0.6855 0.2152  0.1671  0.2048  97  HIS D CD2   
7277 C CE1   . HIS D 125 ? 0.8651 0.5302 0.6806 0.2172  0.1691  0.2101  97  HIS D CE1   
7278 N NE2   . HIS D 125 ? 0.8232 0.5059 0.6554 0.2203  0.1669  0.2137  97  HIS D NE2   
7279 N N     . ASN D 126 ? 0.8483 0.4927 0.6251 0.1839  0.1610  0.1637  98  ASN D N     
7280 C CA    . ASN D 126 ? 0.8637 0.5026 0.6327 0.1782  0.1623  0.1531  98  ASN D CA    
7281 C C     . ASN D 126 ? 0.8647 0.5032 0.6258 0.1723  0.1511  0.1513  98  ASN D C     
7282 O O     . ASN D 126 ? 0.8799 0.5033 0.6254 0.1674  0.1561  0.1425  98  ASN D O     
7283 C CB    . ASN D 126 ? 0.8426 0.4597 0.5965 0.1765  0.1790  0.1431  98  ASN D CB    
7284 C CG    . ASN D 126 ? 0.8181 0.4345 0.5778 0.1817  0.1903  0.1429  98  ASN D CG    
7285 O OD1   . ASN D 126 ? 0.7692 0.3716 0.5219 0.1842  0.2022  0.1424  98  ASN D OD1   
7286 N ND2   . ASN D 126 ? 0.8535 0.4843 0.6251 0.1835  0.1869  0.1434  98  ASN D ND2   
7287 N N     . ALA D 127 ? 0.8629 0.5172 0.6342 0.1726  0.1360  0.1596  99  ALA D N     
7288 C CA    . ALA D 127 ? 0.8721 0.5256 0.6349 0.1677  0.1245  0.1588  99  ALA D CA    
7289 C C     . ALA D 127 ? 0.9754 0.6352 0.7402 0.1638  0.1180  0.1528  99  ALA D C     
7290 O O     . ALA D 127 ? 1.0555 0.7318 0.8365 0.1651  0.1114  0.1563  99  ALA D O     
7291 C CB    . ALA D 127 ? 0.8979 0.5641 0.6697 0.1691  0.1106  0.1702  99  ALA D CB    
7292 N N     . LEU D 128 ? 0.9640 0.6104 0.7123 0.1592  0.1202  0.1439  100 LEU D N     
7293 C CA    . LEU D 128 ? 1.0031 0.6531 0.7504 0.1556  0.1135  0.1378  100 LEU D CA    
7294 C C     . LEU D 128 ? 1.0166 0.6577 0.7478 0.1517  0.1068  0.1353  100 LEU D C     
7295 O O     . LEU D 128 ? 1.0227 0.6473 0.7370 0.1487  0.1150  0.1270  100 LEU D O     
7296 C CB    . LEU D 128 ? 1.0137 0.6546 0.7563 0.1546  0.1257  0.1277  100 LEU D CB    
7297 C CG    . LEU D 128 ? 0.9842 0.6308 0.7276 0.1511  0.1194  0.1204  100 LEU D CG    
7298 C CD1   . LEU D 128 ? 0.9910 0.6569 0.7511 0.1532  0.1056  0.1283  100 LEU D CD1   
7299 C CD2   . LEU D 128 ? 0.9877 0.6338 0.7322 0.1482  0.1303  0.1085  100 LEU D CD2   
7300 N N     . PRO D 129 ? 1.0440 0.6951 0.7794 0.1514  0.0920  0.1424  101 PRO D N     
7301 C CA    . PRO D 129 ? 1.0217 0.6632 0.7396 0.1483  0.0856  0.1404  101 PRO D CA    
7302 C C     . PRO D 129 ? 0.9819 0.6168 0.6891 0.1448  0.0849  0.1301  101 PRO D C     
7303 O O     . PRO D 129 ? 1.0362 0.6829 0.7557 0.1433  0.0821  0.1255  101 PRO D O     
7304 C CB    . PRO D 129 ? 0.9573 0.6136 0.6854 0.1485  0.0684  0.1501  101 PRO D CB    
7305 C CG    . PRO D 129 ? 0.9222 0.5922 0.6708 0.1523  0.0693  0.1588  101 PRO D CG    
7306 C CD    . PRO D 129 ? 0.9989 0.6691 0.7542 0.1539  0.0814  0.1531  101 PRO D CD    
7307 N N     . GLY D 130 ? 0.9509 0.5759 0.6411 0.1404  0.0865  0.1229  102 GLY D N     
7308 C CA    . GLY D 130 ? 0.9582 0.5860 0.6439 0.1341  0.0854  0.1087  102 GLY D CA    
7309 C C     . GLY D 130 ? 0.9976 0.6249 0.6861 0.1308  0.0986  0.0971  102 GLY D C     
7310 O O     . GLY D 130 ? 1.0803 0.7119 0.7670 0.1258  0.0979  0.0853  102 GLY D O     
7311 N N     . THR D 131 ? 0.9954 0.6177 0.6881 0.1335  0.1103  0.0999  103 THR D N     
7312 C CA    . THR D 131 ? 0.9410 0.5627 0.6362 0.1299  0.1222  0.0888  103 THR D CA    
7313 C C     . THR D 131 ? 0.9086 0.5139 0.5952 0.1302  0.1376  0.0894  103 THR D C     
7314 O O     . THR D 131 ? 0.8909 0.4890 0.5690 0.1244  0.1469  0.0792  103 THR D O     
7315 C CB    . THR D 131 ? 0.9544 0.5887 0.6663 0.1324  0.1205  0.0896  103 THR D CB    
7316 O OG1   . THR D 131 ? 0.9445 0.5931 0.6640 0.1312  0.1068  0.0882  103 THR D OG1   
7317 C CG2   . THR D 131 ? 0.9721 0.6052 0.6852 0.1286  0.1325  0.0781  103 THR D CG2   
7318 N N     . ILE D 132 ? 0.9028 0.5021 0.5920 0.1370  0.1404  0.1014  104 ILE D N     
7319 C CA    . ILE D 132 ? 0.8694 0.4516 0.5512 0.1384  0.1552  0.1032  104 ILE D CA    
7320 C C     . ILE D 132 ? 0.8620 0.4323 0.5319 0.1417  0.1543  0.1136  104 ILE D C     
7321 O O     . ILE D 132 ? 0.8590 0.4409 0.5362 0.1456  0.1424  0.1229  104 ILE D O     
7322 C CB    . ILE D 132 ? 0.8228 0.4056 0.5159 0.1447  0.1612  0.1088  104 ILE D CB    
7323 C CG1   . ILE D 132 ? 0.8455 0.4409 0.5494 0.1417  0.1612  0.0989  104 ILE D CG1   
7324 C CG2   . ILE D 132 ? 0.7717 0.3369 0.4572 0.1455  0.1765  0.1088  104 ILE D CG2   
7325 C CD1   . ILE D 132 ? 0.7954 0.3924 0.5098 0.1482  0.1668  0.1041  104 ILE D CD1   
7326 N N     . THR D 133 ? 0.8388 0.3927 0.4945 0.1381  0.1655  0.1097  105 THR D N     
7327 C CA    . THR D 133 ? 0.7700 0.3153 0.4160 0.1401  0.1663  0.1175  105 THR D CA    
7328 C C     . THR D 133 ? 0.7659 0.2981 0.4095 0.1401  0.1817  0.1164  105 THR D C     
7329 O O     . THR D 133 ? 0.7709 0.2899 0.4076 0.1351  0.1940  0.1076  105 THR D O     
7330 C CB    . THR D 133 ? 0.7790 0.3153 0.4065 0.1355  0.1645  0.1144  105 THR D CB    
7331 O OG1   . THR D 133 ? 0.8673 0.3965 0.4886 0.1275  0.1767  0.1015  105 THR D OG1   
7332 C CG2   . THR D 133 ? 0.8010 0.3543 0.4333 0.1337  0.1489  0.1110  105 THR D CG2   
7333 N N     . TYR D 134 ? 0.7736 0.3090 0.4228 0.1454  0.1808  0.1253  106 TYR D N     
7334 C CA    . TYR D 134 ? 0.7887 0.3118 0.4361 0.1466  0.1945  0.1253  106 TYR D CA    
7335 C C     . TYR D 134 ? 0.8095 0.3194 0.4424 0.1453  0.1986  0.1284  106 TYR D C     
7336 O O     . TYR D 134 ? 0.8124 0.3286 0.4434 0.1478  0.1882  0.1360  106 TYR D O     
7337 C CB    . TYR D 134 ? 0.7847 0.3196 0.4488 0.1543  0.1923  0.1333  106 TYR D CB    
7338 C CG    . TYR D 134 ? 0.7660 0.3136 0.4444 0.1559  0.1898  0.1308  106 TYR D CG    
7339 C CD1   . TYR D 134 ? 0.7664 0.3050 0.4438 0.1537  0.2019  0.1222  106 TYR D CD1   
7340 C CD2   . TYR D 134 ? 0.7491 0.3174 0.4419 0.1592  0.1753  0.1370  106 TYR D CD2   
7341 C CE1   . TYR D 134 ? 0.7506 0.3005 0.4400 0.1555  0.1998  0.1200  106 TYR D CE1   
7342 C CE2   . TYR D 134 ? 0.7490 0.3292 0.4549 0.1607  0.1734  0.1351  106 TYR D CE2   
7343 C CZ    . TYR D 134 ? 0.7502 0.3212 0.4539 0.1592  0.1857  0.1268  106 TYR D CZ    
7344 O OH    . TYR D 134 ? 0.8177 0.4002 0.5334 0.1610  0.1840  0.1251  106 TYR D OH    
7345 N N     . GLU D 135 ? 0.8250 0.3164 0.4474 0.1410  0.2137  0.1225  107 GLU D N     
7346 C CA    . GLU D 135 ? 0.8458 0.3228 0.4531 0.1385  0.2194  0.1240  107 GLU D CA    
7347 C C     . GLU D 135 ? 0.8638 0.3267 0.4695 0.1396  0.2332  0.1244  107 GLU D C     
7348 O O     . GLU D 135 ? 0.8612 0.3227 0.4748 0.1407  0.2399  0.1211  107 GLU D O     
7349 C CB    . GLU D 135 ? 0.8493 0.3157 0.4417 0.1295  0.2246  0.1152  107 GLU D CB    
7350 C CG    . GLU D 135 ? 0.8320 0.3097 0.4247 0.1279  0.2134  0.1125  107 GLU D CG    
7351 C CD    . GLU D 135 ? 0.8302 0.3190 0.4215 0.1324  0.1981  0.1210  107 GLU D CD    
7352 O OE1   . GLU D 135 ? 0.8442 0.3304 0.4317 0.1358  0.1970  0.1287  107 GLU D OE1   
7353 O OE2   . GLU D 135 ? 0.8254 0.3250 0.4189 0.1324  0.1869  0.1200  107 GLU D OE2   
7354 N N     . LEU D 136 ? 0.8838 0.3354 0.4782 0.1392  0.2373  0.1284  108 LEU D N     
7355 C CA    . LEU D 136 ? 0.9050 0.3395 0.4943 0.1389  0.2512  0.1281  108 LEU D CA    
7356 C C     . LEU D 136 ? 0.9161 0.3333 0.4918 0.1284  0.2637  0.1181  108 LEU D C     
7357 O O     . LEU D 136 ? 0.9177 0.3333 0.4831 0.1236  0.2615  0.1165  108 LEU D O     
7358 C CB    . LEU D 136 ? 0.9220 0.3542 0.5074 0.1449  0.2484  0.1391  108 LEU D CB    
7359 C CG    . LEU D 136 ? 0.9193 0.3638 0.5186 0.1551  0.2411  0.1497  108 LEU D CG    
7360 C CD1   . LEU D 136 ? 0.9355 0.3788 0.5290 0.1597  0.2360  0.1605  108 LEU D CD1   
7361 C CD2   . LEU D 136 ? 0.9266 0.3630 0.5318 0.1579  0.2528  0.1478  108 LEU D CD2   
7362 N N     . LEU D 137 ? 0.9249 0.3291 0.5005 0.1246  0.2770  0.1114  109 LEU D N     
7363 C CA    . LEU D 137 ? 0.9368 0.3247 0.5011 0.1134  0.2894  0.1019  109 LEU D CA    
7364 C C     . LEU D 137 ? 0.9511 0.3241 0.5157 0.1107  0.3031  0.0968  109 LEU D C     
7365 O O     . LEU D 137 ? 0.9430 0.3205 0.5171 0.1143  0.3032  0.0953  109 LEU D O     
7366 C CB    . LEU D 137 ? 0.9195 0.3135 0.4841 0.1058  0.2871  0.0928  109 LEU D CB    
7367 C CG    . LEU D 137 ? 0.9300 0.3092 0.4860 0.0929  0.3004  0.0820  109 LEU D CG    
7368 C CD1   . LEU D 137 ? 0.9395 0.3151 0.4831 0.0882  0.3011  0.0834  109 LEU D CD1   
7369 C CD2   . LEU D 137 ? 0.9129 0.2975 0.4745 0.0866  0.3003  0.0720  109 LEU D CD2   
7370 N N     . ASP D 138 ? 0.9734 0.3285 0.5272 0.1042  0.3146  0.0942  110 ASP D N     
7371 C CA    . ASP D 138 ? 0.9896 0.3280 0.5412 0.0986  0.3286  0.0874  110 ASP D CA    
7372 C C     . ASP D 138 ? 0.9886 0.3206 0.5358 0.0844  0.3361  0.0750  110 ASP D C     
7373 O O     . ASP D 138 ? 0.9928 0.3222 0.5324 0.0777  0.3375  0.0736  110 ASP D O     
7374 C CB    . ASP D 138 ? 1.0335 0.3559 0.5769 0.1004  0.3367  0.0932  110 ASP D CB    
7375 C CG    . ASP D 138 ? 1.0710 0.3740 0.6101 0.0931  0.3516  0.0856  110 ASP D CG    
7376 O OD1   . ASP D 138 ? 1.0832 0.3868 0.6273 0.0892  0.3547  0.0774  110 ASP D OD1   
7377 O OD2   . ASP D 138 ? 1.0614 0.3485 0.5919 0.0911  0.3599  0.0879  110 ASP D OD2   
7378 N N     . VAL D 139 ? 0.9837 0.3139 0.5359 0.0794  0.3409  0.0660  111 VAL D N     
7379 C CA    . VAL D 139 ? 0.9795 0.3070 0.5305 0.0657  0.3461  0.0536  111 VAL D CA    
7380 C C     . VAL D 139 ? 1.0021 0.3129 0.5434 0.0540  0.3584  0.0490  111 VAL D C     
7381 O O     . VAL D 139 ? 1.0235 0.3341 0.5633 0.0421  0.3620  0.0406  111 VAL D O     
7382 C CB    . VAL D 139 ? 0.9724 0.3012 0.5309 0.0630  0.3483  0.0449  111 VAL D CB    
7383 C CG1   . VAL D 139 ? 1.0598 0.3712 0.6139 0.0588  0.3605  0.0417  111 VAL D CG1   
7384 C CG2   . VAL D 139 ? 0.9585 0.2933 0.5206 0.0518  0.3475  0.0325  111 VAL D CG2   
7385 N N     . VAL D 140 ? 1.0249 0.3222 0.5601 0.0571  0.3649  0.0545  112 VAL D N     
7386 C CA    . VAL D 140 ? 1.0563 0.3373 0.5828 0.0462  0.3767  0.0507  112 VAL D CA    
7387 C C     . VAL D 140 ? 1.0618 0.3408 0.5809 0.0516  0.3745  0.0610  112 VAL D C     
7388 O O     . VAL D 140 ? 1.0833 0.3470 0.5950 0.0485  0.3834  0.0627  112 VAL D O     
7389 C CB    . VAL D 140 ? 1.0703 0.3339 0.5946 0.0430  0.3878  0.0470  112 VAL D CB    
7390 C CG1   . VAL D 140 ? 1.0676 0.3314 0.5969 0.0320  0.3918  0.0340  112 VAL D CG1   
7391 C CG2   . VAL D 140 ? 1.0742 0.3373 0.6005 0.0578  0.3844  0.0565  112 VAL D CG2   
7392 N N     . GLU D 141 ? 1.0421 0.3365 0.5626 0.0595  0.3624  0.0678  113 GLU D N     
7393 C CA    . GLU D 141 ? 1.0517 0.3459 0.5643 0.0640  0.3591  0.0771  113 GLU D CA    
7394 C C     . GLU D 141 ? 1.0611 0.3504 0.5662 0.0515  0.3663  0.0717  113 GLU D C     
7395 O O     . GLU D 141 ? 1.0495 0.3479 0.5573 0.0434  0.3655  0.0641  113 GLU D O     
7396 C CB    . GLU D 141 ? 1.0315 0.3443 0.5473 0.0744  0.3435  0.0848  113 GLU D CB    
7397 C CG    . GLU D 141 ? 1.0420 0.3558 0.5497 0.0814  0.3377  0.0960  113 GLU D CG    
7398 C CD    . GLU D 141 ? 1.1981 0.4986 0.7022 0.0874  0.3429  0.1040  113 GLU D CD    
7399 O OE1   . GLU D 141 ? 1.2601 0.5521 0.7687 0.0887  0.3494  0.1023  113 GLU D OE1   
7400 O OE2   . GLU D 141 ? 1.2038 0.5021 0.6995 0.0908  0.3405  0.1121  113 GLU D OE2   
7401 N N     . PRO D 142 ? 1.0847 0.3609 0.5810 0.0494  0.3736  0.0757  114 PRO D N     
7402 C CA    . PRO D 142 ? 1.0927 0.3668 0.5828 0.0378  0.3802  0.0714  114 PRO D CA    
7403 C C     . PRO D 142 ? 1.0779 0.3681 0.5648 0.0404  0.3704  0.0746  114 PRO D C     
7404 O O     . PRO D 142 ? 1.1496 0.4488 0.6379 0.0311  0.3719  0.0670  114 PRO D O     
7405 C CB    . PRO D 142 ? 1.1229 0.3795 0.6042 0.0380  0.3886  0.0774  114 PRO D CB    
7406 C CG    . PRO D 142 ? 1.1315 0.3787 0.6154 0.0466  0.3895  0.0814  114 PRO D CG    
7407 C CD    . PRO D 142 ? 1.1066 0.3698 0.5987 0.0572  0.3768  0.0843  114 PRO D CD    
7408 N N     . ARG D 143 ? 1.0826 0.3777 0.5651 0.0527  0.3602  0.0855  115 ARG D N     
7409 C CA    . ARG D 143 ? 1.0656 0.3750 0.5432 0.0560  0.3500  0.0890  115 ARG D CA    
7410 C C     . ARG D 143 ? 1.0374 0.3634 0.5237 0.0604  0.3386  0.0867  115 ARG D C     
7411 O O     . ARG D 143 ? 1.0486 0.3841 0.5354 0.0709  0.3260  0.0942  115 ARG D O     
7412 C CB    . ARG D 143 ? 1.0793 0.3865 0.5479 0.0663  0.3436  0.1014  115 ARG D CB    
7413 C CG    . ARG D 143 ? 1.1082 0.3971 0.5703 0.0652  0.3542  0.1058  115 ARG D CG    
7414 C CD    . ARG D 143 ? 1.1243 0.4080 0.5757 0.0567  0.3619  0.1045  115 ARG D CD    
7415 N NE    . ARG D 143 ? 1.1215 0.4155 0.5635 0.0618  0.3522  0.1105  115 ARG D NE    
7416 C CZ    . ARG D 143 ? 1.1202 0.4205 0.5561 0.0550  0.3540  0.1062  115 ARG D CZ    
7417 N NH1   . ARG D 143 ? 1.1546 0.4541 0.5944 0.0425  0.3648  0.0964  115 ARG D NH1   
7418 N NH2   . ARG D 143 ? 1.1195 0.4281 0.5453 0.0608  0.3446  0.1118  115 ARG D NH2   
7419 N N     . LEU D 144 ? 1.0247 0.3544 0.5182 0.0514  0.3432  0.0760  116 LEU D N     
7420 C CA    . LEU D 144 ? 1.0530 0.3977 0.5546 0.0544  0.3337  0.0731  116 LEU D CA    
7421 C C     . LEU D 144 ? 1.0594 0.4192 0.5553 0.0572  0.3233  0.0754  116 LEU D C     
7422 O O     . LEU D 144 ? 1.0411 0.4120 0.5406 0.0656  0.3107  0.0794  116 LEU D O     
7423 C CB    . LEU D 144 ? 1.1056 0.4517 0.6147 0.0430  0.3417  0.0609  116 LEU D CB    
7424 C CG    . LEU D 144 ? 0.9855 0.3492 0.5050 0.0449  0.3324  0.0559  116 LEU D CG    
7425 C CD1   . LEU D 144 ? 0.9761 0.3400 0.4992 0.0585  0.3221  0.0654  116 LEU D CD1   
7426 C CD2   . LEU D 144 ? 0.9546 0.3232 0.4868 0.0348  0.3379  0.0417  116 LEU D CD2   
7427 N N     . GLU D 145 ? 1.0826 0.4434 0.5700 0.0505  0.3283  0.0727  117 GLU D N     
7428 C CA    . GLU D 145 ? 1.0844 0.4595 0.5651 0.0524  0.3197  0.0729  117 GLU D CA    
7429 C C     . GLU D 145 ? 1.0640 0.4392 0.5366 0.0644  0.3074  0.0846  117 GLU D C     
7430 O O     . GLU D 145 ? 1.0496 0.4361 0.5162 0.0676  0.2978  0.0853  117 GLU D O     
7431 C CB    . GLU D 145 ? 1.1213 0.4979 0.5959 0.0428  0.3289  0.0671  117 GLU D CB    
7432 C CG    . GLU D 145 ? 1.1254 0.5148 0.6104 0.0315  0.3356  0.0534  117 GLU D CG    
7433 C CD    . GLU D 145 ? 1.1383 0.5157 0.6306 0.0217  0.3487  0.0483  117 GLU D CD    
7434 O OE1   . GLU D 145 ? 1.1666 0.5263 0.6529 0.0207  0.3560  0.0537  117 GLU D OE1   
7435 O OE2   . GLU D 145 ? 1.0790 0.4652 0.5828 0.0151  0.3513  0.0383  117 GLU D OE2   
7436 N N     . ASP D 146 ? 1.0178 0.3823 0.4902 0.0709  0.3070  0.0931  118 ASP D N     
7437 C CA    . ASP D 146 ? 1.0224 0.3894 0.4892 0.0818  0.2950  0.1042  118 ASP D CA    
7438 C C     . ASP D 146 ? 1.0061 0.3817 0.4850 0.0909  0.2834  0.1089  118 ASP D C     
7439 O O     . ASP D 146 ? 1.0197 0.3984 0.4979 0.0998  0.2738  0.1186  118 ASP D O     
7440 C CB    . ASP D 146 ? 1.0485 0.4013 0.5078 0.0837  0.3014  0.1115  118 ASP D CB    
7441 C CG    . ASP D 146 ? 1.0660 0.4114 0.5132 0.0755  0.3118  0.1085  118 ASP D CG    
7442 O OD1   . ASP D 146 ? 1.0639 0.4078 0.5146 0.0651  0.3224  0.0989  118 ASP D OD1   
7443 O OD2   . ASP D 146 ? 1.0821 0.4245 0.5169 0.0791  0.3091  0.1157  118 ASP D OD2   
7444 N N     . THR D 147 ? 0.9741 0.3550 0.4649 0.0886  0.2841  0.1022  119 THR D N     
7445 C CA    . THR D 147 ? 0.9577 0.3482 0.4619 0.0967  0.2740  0.1059  119 THR D CA    
7446 C C     . THR D 147 ? 0.9362 0.3422 0.4429 0.0983  0.2615  0.1041  119 THR D C     
7447 O O     . THR D 147 ? 0.9659 0.3745 0.4657 0.0918  0.2635  0.0973  119 THR D O     
7448 C CB    . THR D 147 ? 0.9798 0.3648 0.4956 0.0940  0.2831  0.1003  119 THR D CB    
7449 O OG1   . THR D 147 ? 0.9788 0.3651 0.4958 0.0845  0.2890  0.0894  119 THR D OG1   
7450 C CG2   . THR D 147 ? 1.0160 0.3839 0.5278 0.0917  0.2961  0.1012  119 THR D CG2   
7451 N N     . VAL D 148 ? 0.9232 0.3406 0.4406 0.1069  0.2487  0.1102  120 VAL D N     
7452 C CA    . VAL D 148 ? 0.9032 0.3352 0.4244 0.1090  0.2357  0.1092  120 VAL D CA    
7453 C C     . VAL D 148 ? 0.8872 0.3225 0.4160 0.1030  0.2405  0.0989  120 VAL D C     
7454 O O     . VAL D 148 ? 0.8944 0.3468 0.4279 0.1000  0.2321  0.0903  120 VAL D O     
7455 C CB    . VAL D 148 ? 0.8932 0.3382 0.4270 0.1187  0.2212  0.1183  120 VAL D CB    
7456 C CG1   . VAL D 148 ? 0.8711 0.3309 0.4125 0.1203  0.2086  0.1164  120 VAL D CG1   
7457 C CG2   . VAL D 148 ? 0.9078 0.3529 0.4332 0.1236  0.2138  0.1280  120 VAL D CG2   
7458 N N     . VAL D 149 ? 0.8884 0.3160 0.4250 0.1007  0.2511  0.0955  121 VAL D N     
7459 C CA    . VAL D 149 ? 0.9268 0.3674 0.4783 0.0946  0.2521  0.0819  121 VAL D CA    
7460 C C     . VAL D 149 ? 0.9737 0.4210 0.5227 0.0840  0.2567  0.0690  121 VAL D C     
7461 O O     . VAL D 149 ? 0.9812 0.4472 0.5405 0.0806  0.2503  0.0589  121 VAL D O     
7462 C CB    . VAL D 149 ? 0.8909 0.3188 0.4482 0.0940  0.2635  0.0809  121 VAL D CB    
7463 C CG1   . VAL D 149 ? 0.8583 0.2982 0.4283 0.0862  0.2657  0.0658  121 VAL D CG1   
7464 C CG2   . VAL D 149 ? 0.9302 0.3596 0.4955 0.1052  0.2570  0.0914  121 VAL D CG2   
7465 N N     . TRP D 150 ? 0.9886 0.4210 0.5241 0.0788  0.2683  0.0698  122 TRP D N     
7466 C CA    . TRP D 150 ? 0.9803 0.4191 0.5143 0.0685  0.2745  0.0582  122 TRP D CA    
7467 C C     . TRP D 150 ? 0.9611 0.4178 0.4939 0.0697  0.2629  0.0547  122 TRP D C     
7468 O O     . TRP D 150 ? 0.9855 0.4572 0.5256 0.0633  0.2628  0.0428  122 TRP D O     
7469 C CB    . TRP D 150 ? 1.0119 0.4308 0.5307 0.0635  0.2889  0.0619  122 TRP D CB    
7470 C CG    . TRP D 150 ? 1.0628 0.4894 0.5783 0.0542  0.2945  0.0525  122 TRP D CG    
7471 C CD1   . TRP D 150 ? 1.0627 0.4908 0.5649 0.0550  0.2928  0.0552  122 TRP D CD1   
7472 C CD2   . TRP D 150 ? 1.0987 0.5333 0.6244 0.0430  0.3027  0.0391  122 TRP D CD2   
7473 N NE1   . TRP D 150 ? 1.0716 0.5085 0.5758 0.0454  0.3002  0.0445  122 TRP D NE1   
7474 C CE2   . TRP D 150 ? 1.1049 0.5467 0.6243 0.0377  0.3060  0.0346  122 TRP D CE2   
7475 C CE3   . TRP D 150 ? 1.0879 0.5247 0.6272 0.0369  0.3073  0.0303  122 TRP D CE3   
7476 C CZ2   . TRP D 150 ? 1.1923 0.6448 0.7204 0.0266  0.3138  0.0224  122 TRP D CZ2   
7477 C CZ3   . TRP D 150 ? 1.0720 0.5188 0.6190 0.0254  0.3143  0.0178  122 TRP D CZ3   
7478 C CH2   . TRP D 150 ? 1.1191 0.5744 0.6613 0.0204  0.3175  0.0142  122 TRP D CH2   
7479 N N     . ARG D 151 ? 0.9132 0.3686 0.4368 0.0780  0.2528  0.0649  123 ARG D N     
7480 C CA    . ARG D 151 ? 0.8705 0.3392 0.3896 0.0793  0.2420  0.0621  123 ARG D CA    
7481 C C     . ARG D 151 ? 0.9241 0.4114 0.4575 0.0834  0.2269  0.0588  123 ARG D C     
7482 O O     . ARG D 151 ? 0.9815 0.4809 0.5134 0.0837  0.2180  0.0540  123 ARG D O     
7483 C CB    . ARG D 151 ? 0.8896 0.3467 0.3893 0.0851  0.2384  0.0740  123 ARG D CB    
7484 C CG    . ARG D 151 ? 0.9155 0.3550 0.3999 0.0806  0.2537  0.0768  123 ARG D CG    
7485 C CD    . ARG D 151 ? 0.9365 0.3658 0.3995 0.0856  0.2505  0.0873  123 ARG D CD    
7486 N NE    . ARG D 151 ? 0.9617 0.3738 0.4117 0.0813  0.2657  0.0906  123 ARG D NE    
7487 C CZ    . ARG D 151 ? 0.9808 0.3862 0.4179 0.0847  0.2636  0.0976  123 ARG D CZ    
7488 N NH1   . ARG D 151 ? 1.0496 0.4594 0.4782 0.0920  0.2494  0.1038  123 ARG D NH1   
7489 N NH2   . ARG D 151 ? 1.0002 0.3943 0.4325 0.0803  0.2759  0.0984  123 ARG D NH2   
7490 N N     . ASN D 152 ? 0.9415 0.4307 0.4880 0.0869  0.2241  0.0615  124 ASN D N     
7491 C CA    . ASN D 152 ? 0.9705 0.4783 0.5330 0.0885  0.2128  0.0560  124 ASN D CA    
7492 C C     . ASN D 152 ? 0.9616 0.4812 0.5350 0.0804  0.2181  0.0413  124 ASN D C     
7493 O O     . ASN D 152 ? 0.9699 0.5063 0.5550 0.0809  0.2089  0.0352  124 ASN D O     
7494 C CB    . ASN D 152 ? 1.0069 0.5136 0.5800 0.0948  0.2092  0.0637  124 ASN D CB    
7495 C CG    . ASN D 152 ? 1.0665 0.5693 0.6340 0.1037  0.1989  0.0780  124 ASN D CG    
7496 O OD1   . ASN D 152 ? 1.1444 0.6592 0.7149 0.1071  0.1848  0.0796  124 ASN D OD1   
7497 N ND2   . ASN D 152 ? 1.0238 0.5097 0.5832 0.1075  0.2058  0.0886  124 ASN D ND2   
7498 N N     . GLY D 153 ? 0.9736 0.4849 0.5435 0.0728  0.2325  0.0358  125 GLY D N     
7499 C CA    . GLY D 153 ? 1.0267 0.5494 0.6070 0.0645  0.2380  0.0222  125 GLY D CA    
7500 C C     . GLY D 153 ? 1.0600 0.5944 0.6373 0.0605  0.2368  0.0143  125 GLY D C     
7501 O O     . GLY D 153 ? 1.0707 0.6048 0.6374 0.0648  0.2304  0.0187  125 GLY D O     
7502 N N     . PRO D 154 ? 1.1237 0.6688 0.7102 0.0524  0.2430  0.0024  126 PRO D N     
7503 C CA    . PRO D 154 ? 1.0702 0.6161 0.6681 0.0459  0.2505  -0.0043 126 PRO D CA    
7504 C C     . PRO D 154 ? 1.0739 0.6318 0.6860 0.0500  0.2405  -0.0065 126 PRO D C     
7505 O O     . PRO D 154 ? 1.0649 0.6359 0.6813 0.0554  0.2281  -0.0064 126 PRO D O     
7506 C CB    . PRO D 154 ? 1.0608 0.6181 0.6630 0.0364  0.2577  -0.0159 126 PRO D CB    
7507 C CG    . PRO D 154 ? 1.1814 0.7531 0.7823 0.0406  0.2483  -0.0180 126 PRO D CG    
7508 C CD    . PRO D 154 ? 1.2532 0.8129 0.8400 0.0494  0.2415  -0.0060 126 PRO D CD    
7509 N N     . PHE D 155 ? 1.0863 0.6389 0.7048 0.0475  0.2459  -0.0083 127 PHE D N     
7510 C CA    . PHE D 155 ? 1.0246 0.5861 0.6548 0.0518  0.2380  -0.0090 127 PHE D CA    
7511 C C     . PHE D 155 ? 1.0537 0.6308 0.6963 0.0446  0.2391  -0.0222 127 PHE D C     
7512 O O     . PHE D 155 ? 1.0978 0.6738 0.7404 0.0352  0.2489  -0.0300 127 PHE D O     
7513 C CB    . PHE D 155 ? 1.0137 0.5577 0.6415 0.0557  0.2429  -0.0012 127 PHE D CB    
7514 C CG    . PHE D 155 ? 0.9530 0.4833 0.5702 0.0640  0.2406  0.0129  127 PHE D CG    
7515 C CD1   . PHE D 155 ? 0.9408 0.4773 0.5618 0.0734  0.2283  0.0212  127 PHE D CD1   
7516 C CD2   . PHE D 155 ? 0.9564 0.4679 0.5602 0.0620  0.2506  0.0182  127 PHE D CD2   
7517 C CE1   . PHE D 155 ? 0.9386 0.4640 0.5506 0.0808  0.2254  0.0344  127 PHE D CE1   
7518 C CE2   . PHE D 155 ? 0.9616 0.4611 0.5554 0.0699  0.2480  0.0316  127 PHE D CE2   
7519 C CZ    . PHE D 155 ? 0.9621 0.4691 0.5602 0.0793  0.2351  0.0396  127 PHE D CZ    
7520 N N     . GLY D 156 ? 1.0144 0.6065 0.6677 0.0488  0.2286  -0.0244 128 GLY D N     
7521 C CA    . GLY D 156 ? 1.0303 0.6383 0.6953 0.0431  0.2281  -0.0360 128 GLY D CA    
7522 C C     . GLY D 156 ? 1.0622 0.6626 0.7304 0.0405  0.2341  -0.0384 128 GLY D C     
7523 O O     . GLY D 156 ? 1.0988 0.7064 0.7730 0.0326  0.2382  -0.0489 128 GLY D O     
7524 N N     . LYS D 157 ? 1.0015 0.5877 0.6656 0.0474  0.2347  -0.0288 129 LYS D N     
7525 C CA    . LYS D 157 ? 0.9966 0.5732 0.6619 0.0467  0.2408  -0.0302 129 LYS D CA    
7526 C C     . LYS D 157 ? 0.9859 0.5381 0.6407 0.0508  0.2488  -0.0199 129 LYS D C     
7527 O O     . LYS D 157 ? 0.9682 0.5158 0.6187 0.0587  0.2442  -0.0086 129 LYS D O     
7528 C CB    . LYS D 157 ? 0.9961 0.5850 0.6708 0.0535  0.2314  -0.0292 129 LYS D CB    
7529 C CG    . LYS D 157 ? 1.0598 0.6729 0.7448 0.0514  0.2219  -0.0374 129 LYS D CG    
7530 C CD    . LYS D 157 ? 1.1454 0.7654 0.8354 0.0427  0.2264  -0.0501 129 LYS D CD    
7531 C CE    . LYS D 157 ? 1.1840 0.8287 0.8844 0.0417  0.2166  -0.0573 129 LYS D CE    
7532 N NZ    . LYS D 157 ? 1.1488 0.8016 0.8490 0.0420  0.2121  -0.0565 129 LYS D NZ    
7533 N N     . VAL D 158 ? 1.0052 0.5415 0.6558 0.0454  0.2604  -0.0237 130 VAL D N     
7534 C CA    . VAL D 158 ? 1.0180 0.5296 0.6590 0.0496  0.2691  -0.0144 130 VAL D CA    
7535 C C     . VAL D 158 ? 1.0335 0.5385 0.6771 0.0522  0.2725  -0.0163 130 VAL D C     
7536 O O     . VAL D 158 ? 1.0329 0.5386 0.6784 0.0439  0.2773  -0.0277 130 VAL D O     
7537 C CB    . VAL D 158 ? 1.0003 0.4939 0.6311 0.0409  0.2818  -0.0164 130 VAL D CB    
7538 C CG1   . VAL D 158 ? 0.9981 0.4647 0.6202 0.0433  0.2928  -0.0107 130 VAL D CG1   
7539 C CG2   . VAL D 158 ? 1.0138 0.5079 0.6382 0.0423  0.2796  -0.0096 130 VAL D CG2   
7540 N N     . PHE D 159 ? 0.9906 0.4897 0.6341 0.0637  0.2699  -0.0051 131 PHE D N     
7541 C CA    . PHE D 159 ? 0.9508 0.4434 0.5962 0.0683  0.2734  -0.0052 131 PHE D CA    
7542 C C     . PHE D 159 ? 1.0088 0.4733 0.6437 0.0716  0.2854  0.0022  131 PHE D C     
7543 O O     . PHE D 159 ? 1.0959 0.5532 0.7284 0.0815  0.2841  0.0156  131 PHE D O     
7544 C CB    . PHE D 159 ? 0.9502 0.4586 0.6051 0.0791  0.2621  0.0023  131 PHE D CB    
7545 C CG    . PHE D 159 ? 0.9283 0.4617 0.5936 0.0760  0.2520  -0.0062 131 PHE D CG    
7546 C CD1   . PHE D 159 ? 0.9899 0.5283 0.6588 0.0729  0.2538  -0.0157 131 PHE D CD1   
7547 C CD2   . PHE D 159 ? 0.9834 0.5344 0.6539 0.0763  0.2408  -0.0048 131 PHE D CD2   
7548 C CE1   . PHE D 159 ? 1.0303 0.5915 0.7083 0.0705  0.2444  -0.0230 131 PHE D CE1   
7549 C CE2   . PHE D 159 ? 1.0695 0.6424 0.7493 0.0740  0.2318  -0.0123 131 PHE D CE2   
7550 C CZ    . PHE D 159 ? 1.0592 0.6377 0.7431 0.0712  0.2335  -0.0210 131 PHE D CZ    
7551 N N     . CYS D 160 ? 0.9832 0.4377 0.6151 0.0617  0.2940  -0.0048 132 CYS D N     
7552 C CA    . CYS D 160 ? 1.0091 0.4392 0.6319 0.0629  0.3051  0.0015  132 CYS D CA    
7553 C C     . CYS D 160 ? 1.0945 0.5248 0.7212 0.0648  0.3063  0.0002  132 CYS D C     
7554 O O     . CYS D 160 ? 1.1331 0.5646 0.7611 0.0547  0.3087  -0.0108 132 CYS D O     
7555 C CB    . CYS D 160 ? 1.0019 0.4175 0.6166 0.0500  0.3151  -0.0053 132 CYS D CB    
7556 S SG    . CYS D 160 ? 1.1816 0.5696 0.7863 0.0480  0.3289  -0.0017 132 CYS D SG    
7557 N N     . MET D 161 ? 1.0595 0.4893 0.6881 0.0779  0.3046  0.0115  133 MET D N     
7558 C CA    . MET D 161 ? 1.0818 0.5126 0.7137 0.0814  0.3059  0.0111  133 MET D CA    
7559 C C     . MET D 161 ? 1.1035 0.5119 0.7259 0.0797  0.3180  0.0128  133 MET D C     
7560 O O     . MET D 161 ? 1.1180 0.5130 0.7332 0.0689  0.3253  0.0064  133 MET D O     
7561 C CB    . MET D 161 ? 1.0597 0.5021 0.6992 0.0961  0.2991  0.0225  133 MET D CB    
7562 C CG    . MET D 161 ? 1.1395 0.6049 0.7892 0.0977  0.2872  0.0192  133 MET D CG    
7563 S SD    . MET D 161 ? 1.2547 0.7333 0.9084 0.0840  0.2841  0.0011  133 MET D SD    
7564 C CE    . MET D 161 ? 1.0410 0.5436 0.7034 0.0853  0.2711  -0.0009 133 MET D CE    
7565 N N     . LEU D 162 ? 1.0027 0.4075 0.6256 0.0903  0.3206  0.0212  134 LEU D N     
7566 C CA    . LEU D 162 ? 1.0183 0.4029 0.6325 0.0899  0.3320  0.0224  134 LEU D CA    
7567 C C     . LEU D 162 ? 1.0767 0.4475 0.6836 0.0943  0.3380  0.0322  134 LEU D C     
7568 O O     . LEU D 162 ? 1.1451 0.5162 0.7534 0.1067  0.3385  0.0439  134 LEU D O     
7569 C CB    . LEU D 162 ? 1.0296 0.4176 0.6475 0.1002  0.3324  0.0271  134 LEU D CB    
7570 C CG    . LEU D 162 ? 1.0205 0.4250 0.6464 0.0987  0.3252  0.0196  134 LEU D CG    
7571 C CD1   . LEU D 162 ? 0.9417 0.3544 0.5736 0.1128  0.3237  0.0291  134 LEU D CD1   
7572 C CD2   . LEU D 162 ? 1.0716 0.4674 0.6920 0.0866  0.3296  0.0058  134 LEU D CD2   
7573 N N     . MET D 163 ? 1.0571 0.4171 0.6568 0.0837  0.3425  0.0271  135 MET D N     
7574 C CA    . MET D 163 ? 1.0840 0.4320 0.6764 0.0875  0.3474  0.0360  135 MET D CA    
7575 C C     . MET D 163 ? 1.1326 0.4610 0.7143 0.0747  0.3578  0.0291  135 MET D C     
7576 O O     . MET D 163 ? 1.1611 0.4740 0.7350 0.0776  0.3657  0.0349  135 MET D O     
7577 C CB    . MET D 163 ? 1.0851 0.4467 0.6819 0.0926  0.3378  0.0426  135 MET D CB    
7578 C CG    . MET D 163 ? 1.1483 0.4993 0.7369 0.0924  0.3414  0.0486  135 MET D CG    
7579 S SD    . MET D 163 ? 1.2475 0.5930 0.8298 0.0764  0.3439  0.0380  135 MET D SD    
7580 C CE    . MET D 163 ? 1.1072 0.4767 0.7008 0.0772  0.3302  0.0338  135 MET D CE    
7581 N N     . LEU D 164 ? 1.1316 0.4617 0.7139 0.0606  0.3578  0.0165  136 LEU D N     
7582 C CA    . LEU D 164 ? 1.1120 0.4250 0.6855 0.0473  0.3676  0.0096  136 LEU D CA    
7583 C C     . LEU D 164 ? 1.1108 0.4034 0.6763 0.0455  0.3784  0.0086  136 LEU D C     
7584 O O     . LEU D 164 ? 1.1155 0.3913 0.6727 0.0363  0.3877  0.0053  136 LEU D O     
7585 C CB    . LEU D 164 ? 1.0522 0.3744 0.6306 0.0323  0.3648  -0.0049 136 LEU D CB    
7586 C CG    . LEU D 164 ? 0.9680 0.3023 0.5497 0.0288  0.3591  -0.0064 136 LEU D CG    
7587 C CD1   . LEU D 164 ? 0.9920 0.3420 0.5819 0.0158  0.3545  -0.0214 136 LEU D CD1   
7588 C CD2   . LEU D 164 ? 1.0310 0.3489 0.6025 0.0254  0.3677  -0.0018 136 LEU D CD2   
7589 N N     . HIS D 165 ? 1.1497 0.4431 0.7173 0.0540  0.3779  0.0112  137 HIS D N     
7590 C CA    . HIS D 165 ? 1.1715 0.4443 0.7304 0.0543  0.3883  0.0114  137 HIS D CA    
7591 C C     . HIS D 165 ? 1.1669 0.4289 0.7202 0.0660  0.3936  0.0243  137 HIS D C     
7592 O O     . HIS D 165 ? 1.2507 0.4922 0.7948 0.0643  0.4038  0.0245  137 HIS D O     
7593 C CB    . HIS D 165 ? 1.2271 0.5043 0.7897 0.0590  0.3861  0.0089  137 HIS D CB    
7594 C CG    . HIS D 165 ? 1.1815 0.4706 0.7504 0.0763  0.3809  0.0208  137 HIS D CG    
7595 N ND1   . HIS D 165 ? 1.1384 0.4502 0.7184 0.0813  0.3698  0.0217  137 HIS D ND1   
7596 C CD2   . HIS D 165 ? 1.1318 0.4141 0.6984 0.0896  0.3853  0.0320  137 HIS D CD2   
7597 C CE1   . HIS D 165 ? 1.1514 0.4699 0.7359 0.0965  0.3678  0.0333  137 HIS D CE1   
7598 N NE2   . HIS D 165 ? 1.1184 0.4201 0.6954 0.1019  0.3769  0.0396  137 HIS D NE2   
7599 N N     . LEU D 166 ? 1.1806 0.4566 0.7398 0.0778  0.3861  0.0349  138 LEU D N     
7600 C CA    . LEU D 166 ? 1.2129 0.4826 0.7685 0.0877  0.3885  0.0465  138 LEU D CA    
7601 C C     . LEU D 166 ? 1.2346 0.4969 0.7838 0.0797  0.3911  0.0457  138 LEU D C     
7602 O O     . LEU D 166 ? 1.1934 0.4521 0.7399 0.0873  0.3914  0.0552  138 LEU D O     
7603 C CB    . LEU D 166 ? 1.2194 0.5092 0.7853 0.1028  0.3779  0.0579  138 LEU D CB    
7604 C CG    . LEU D 166 ? 1.2198 0.5109 0.7895 0.1176  0.3788  0.0674  138 LEU D CG    
7605 C CD1   . LEU D 166 ? 1.2310 0.5161 0.7997 0.1163  0.3842  0.0614  138 LEU D CD1   
7606 C CD2   . LEU D 166 ? 1.2069 0.5220 0.7895 0.1296  0.3663  0.0771  138 LEU D CD2   
7607 N N     . VAL D 167 ? 1.2400 0.5009 0.7875 0.0647  0.3926  0.0347  139 VAL D N     
7608 C CA    . VAL D 167 ? 1.1570 0.4119 0.6989 0.0564  0.3956  0.0334  139 VAL D CA    
7609 C C     . VAL D 167 ? 1.1988 0.4334 0.7324 0.0421  0.4075  0.0242  139 VAL D C     
7610 O O     . VAL D 167 ? 1.2536 0.4898 0.7895 0.0296  0.4084  0.0124  139 VAL D O     
7611 C CB    . VAL D 167 ? 1.0955 0.3676 0.6435 0.0507  0.3870  0.0289  139 VAL D CB    
7612 C CG1   . VAL D 167 ? 1.1532 0.4181 0.6947 0.0413  0.3914  0.0271  139 VAL D CG1   
7613 C CG2   . VAL D 167 ? 1.1003 0.3916 0.6563 0.0645  0.3747  0.0381  139 VAL D CG2   
7614 N N     . PRO D 168 ? 1.1684 0.3846 0.6931 0.0433  0.4162  0.0289  140 PRO D N     
7615 C CA    . PRO D 168 ? 1.1616 0.3579 0.6785 0.0290  0.4277  0.0202  140 PRO D CA    
7616 C C     . PRO D 168 ? 1.1697 0.3698 0.6877 0.0126  0.4285  0.0103  140 PRO D C     
7617 O O     . PRO D 168 ? 1.1989 0.3997 0.7195 -0.0003 0.4300  -0.0016 140 PRO D O     
7618 C CB    . PRO D 168 ? 1.1830 0.3623 0.6913 0.0356  0.4346  0.0295  140 PRO D CB    
7619 C CG    . PRO D 168 ? 1.1952 0.3830 0.7073 0.0543  0.4281  0.0417  140 PRO D CG    
7620 C CD    . PRO D 168 ? 1.2076 0.4204 0.7300 0.0582  0.4157  0.0424  140 PRO D CD    
7621 N N     . ASP D 169 ? 1.2117 0.4152 0.7283 0.0129  0.4272  0.0152  141 ASP D N     
7622 C CA    . ASP D 169 ? 1.2164 0.4239 0.7342 -0.0020 0.4287  0.0069  141 ASP D CA    
7623 C C     . ASP D 169 ? 1.2037 0.4327 0.7315 -0.0042 0.4190  0.0010  141 ASP D C     
7624 O O     . ASP D 169 ? 1.2418 0.4842 0.7725 0.0025  0.4111  0.0065  141 ASP D O     
7625 C CB    . ASP D 169 ? 1.3072 0.5121 0.8199 0.0004  0.4297  0.0148  141 ASP D CB    
7626 C CG    . ASP D 169 ? 1.3820 0.5845 0.8938 -0.0167 0.4359  0.0066  141 ASP D CG    
7627 O OD1   . ASP D 169 ? 1.3375 0.5479 0.8555 -0.0289 0.4356  -0.0048 141 ASP D OD1   
7628 O OD2   . ASP D 169 ? 1.3890 0.5828 0.8946 -0.0178 0.4407  0.0118  141 ASP D OD2   
7629 N N     . ASN D 170 ? 1.1818 0.4145 0.7149 -0.0135 0.4186  -0.0103 142 ASN D N     
7630 C CA    . ASN D 170 ? 1.2217 0.4762 0.7656 -0.0151 0.4083  -0.0167 142 ASN D CA    
7631 C C     . ASN D 170 ? 1.2505 0.5135 0.7979 -0.0272 0.4081  -0.0239 142 ASN D C     
7632 O O     . ASN D 170 ? 1.2670 0.5487 0.8217 -0.0237 0.3986  -0.0250 142 ASN D O     
7633 C CB    . ASN D 170 ? 1.2327 0.4903 0.7818 -0.0208 0.4066  -0.0268 142 ASN D CB    
7634 C CG    . ASN D 170 ? 1.2381 0.5002 0.7893 -0.0057 0.4007  -0.0200 142 ASN D CG    
7635 O OD1   . ASN D 170 ? 1.3356 0.5824 0.8802 -0.0001 0.4067  -0.0152 142 ASN D OD1   
7636 N ND2   . ASN D 170 ? 1.1463 0.4299 0.7072 0.0008  0.3890  -0.0197 142 ASN D ND2   
7637 N N     . ARG D 171 ? 1.2371 0.4877 0.7800 -0.0411 0.4183  -0.0293 143 ARG D N     
7638 C CA    . ARG D 171 ? 1.2478 0.5067 0.7947 -0.0532 0.4193  -0.0364 143 ARG D CA    
7639 C C     . ARG D 171 ? 1.3334 0.5954 0.8764 -0.0446 0.4168  -0.0256 143 ARG D C     
7640 O O     . ARG D 171 ? 1.3218 0.6005 0.8708 -0.0472 0.4113  -0.0294 143 ARG D O     
7641 C CB    . ARG D 171 ? 1.2497 0.4948 0.7934 -0.0706 0.4313  -0.0437 143 ARG D CB    
7642 C CG    . ARG D 171 ? 1.2906 0.5444 0.8395 -0.0846 0.4340  -0.0509 143 ARG D CG    
7643 C CD    . ARG D 171 ? 1.2346 0.4842 0.7873 -0.1046 0.4418  -0.0639 143 ARG D CD    
7644 N NE    . ARG D 171 ? 1.1660 0.3967 0.7115 -0.1054 0.4480  -0.0631 143 ARG D NE    
7645 C CZ    . ARG D 171 ? 1.1913 0.4194 0.7399 -0.1174 0.4499  -0.0747 143 ARG D CZ    
7646 N NH1   . ARG D 171 ? 1.2759 0.5215 0.8358 -0.1297 0.4453  -0.0883 143 ARG D NH1   
7647 N NH2   . ARG D 171 ? 1.1781 0.3864 0.7183 -0.1167 0.4560  -0.0729 143 ARG D NH2   
7648 N N     . LEU D 172 ? 1.3531 0.6040 0.8872 -0.0333 0.4189  -0.0126 144 LEU D N     
7649 C CA    . LEU D 172 ? 1.2963 0.5532 0.8267 -0.0237 0.4139  -0.0015 144 LEU D CA    
7650 C C     . LEU D 172 ? 1.2189 0.4926 0.7551 -0.0117 0.4009  0.0023  144 LEU D C     
7651 O O     . LEU D 172 ? 1.2082 0.4932 0.7447 -0.0098 0.3953  0.0060  144 LEU D O     
7652 C CB    . LEU D 172 ? 1.2319 0.4755 0.7534 -0.0134 0.4169  0.0102  144 LEU D CB    
7653 C CG    . LEU D 172 ? 1.1780 0.4284 0.6954 -0.0017 0.4097  0.0226  144 LEU D CG    
7654 C CD1   . LEU D 172 ? 1.1888 0.4481 0.7057 -0.0109 0.4103  0.0204  144 LEU D CD1   
7655 C CD2   . LEU D 172 ? 1.1927 0.4286 0.7020 0.0065  0.4136  0.0324  144 LEU D CD2   
7656 N N     . ALA D 173 ? 1.1763 0.4533 0.7172 -0.0037 0.3960  0.0020  145 ALA D N     
7657 C CA    . ALA D 173 ? 1.1210 0.4156 0.6693 0.0074  0.3832  0.0048  145 ALA D CA    
7658 C C     . ALA D 173 ? 1.1573 0.4716 0.7157 -0.0005 0.3770  -0.0085 145 ALA D C     
7659 O O     . ALA D 173 ? 1.1162 0.4549 0.6818 0.0062  0.3647  -0.0062 145 ALA D O     
7660 C CB    . ALA D 173 ? 1.1313 0.4272 0.6833 0.0171  0.3799  0.0077  145 ALA D CB    
7661 N N     . VAL D 174 ? 1.2149 0.5294 0.7772 -0.0149 0.3826  -0.0223 146 VAL D N     
7662 C CA    . VAL D 174 ? 1.2250 0.5702 0.8007 -0.0229 0.3744  -0.0348 146 VAL D CA    
7663 C C     . VAL D 174 ? 1.2405 0.6015 0.8180 -0.0280 0.3729  -0.0338 146 VAL D C     
7664 O O     . VAL D 174 ? 1.2354 0.6248 0.8229 -0.0268 0.3623  -0.0376 146 VAL D O     
7665 C CB    . VAL D 174 ? 1.2653 0.6067 0.8447 -0.0372 0.3803  -0.0494 146 VAL D CB    
7666 C CG1   . VAL D 174 ? 1.3353 0.7079 0.9281 -0.0469 0.3731  -0.0620 146 VAL D CG1   
7667 C CG2   . VAL D 174 ? 1.2206 0.5612 0.8034 -0.0318 0.3756  -0.0483 146 VAL D CG2   
7668 N N     . LYS D 175 ? 1.2584 0.6009 0.8259 -0.0333 0.3838  -0.0283 147 LYS D N     
7669 C CA    . LYS D 175 ? 1.2091 0.5650 0.7766 -0.0374 0.3838  -0.0264 147 LYS D CA    
7670 C C     . LYS D 175 ? 1.2376 0.6056 0.8029 -0.0230 0.3728  -0.0159 147 LYS D C     
7671 O O     . LYS D 175 ? 1.2560 0.6476 0.8271 -0.0236 0.3659  -0.0186 147 LYS D O     
7672 C CB    . LYS D 175 ? 1.2082 0.5390 0.7638 -0.0452 0.3986  -0.0211 147 LYS D CB    
7673 N N     . ASN D 176 ? 1.2332 0.5855 0.7905 -0.0100 0.3709  -0.0040 148 ASN D N     
7674 C CA    . ASN D 176 ? 1.1352 0.4982 0.6903 0.0032  0.3598  0.0063  148 ASN D CA    
7675 C C     . ASN D 176 ? 1.1623 0.5525 0.7309 0.0086  0.3452  0.0007  148 ASN D C     
7676 O O     . ASN D 176 ? 1.1663 0.5736 0.7363 0.0146  0.3349  0.0041  148 ASN D O     
7677 C CB    . ASN D 176 ? 1.0550 0.3947 0.5991 0.0154  0.3617  0.0210  148 ASN D CB    
7678 C CG    . ASN D 176 ? 1.1106 0.4284 0.6394 0.0139  0.3722  0.0307  148 ASN D CG    
7679 O OD1   . ASN D 176 ? 1.2152 0.5377 0.7411 0.0051  0.3766  0.0277  148 ASN D OD1   
7680 N ND2   . ASN D 176 ? 1.1124 0.4180 0.6375 0.0243  0.3719  0.0391  148 ASN D ND2   
7681 N N     . ILE D 177 ? 1.1604 0.5539 0.7378 0.0065  0.3441  -0.0078 149 ILE D N     
7682 C CA    . ILE D 177 ? 1.1420 0.5618 0.7323 0.0102  0.3310  -0.0139 149 ILE D CA    
7683 C C     . ILE D 177 ? 1.1938 0.6377 0.7928 0.0007  0.3278  -0.0248 149 ILE D C     
7684 O O     . ILE D 177 ? 1.1755 0.6422 0.7820 0.0054  0.3160  -0.0261 149 ILE D O     
7685 C CB    . ILE D 177 ? 1.1150 0.5307 0.7108 0.0106  0.3317  -0.0198 149 ILE D CB    
7686 C CG1   . ILE D 177 ? 1.0789 0.4760 0.6684 0.0235  0.3324  -0.0076 149 ILE D CG1   
7687 C CG2   . ILE D 177 ? 1.0447 0.4884 0.6542 0.0113  0.3197  -0.0283 149 ILE D CG2   
7688 C CD1   . ILE D 177 ? 1.0460 0.4332 0.6374 0.0240  0.3364  -0.0128 149 ILE D CD1   
7689 N N     . HIS D 178 ? 1.2487 0.6879 0.8472 -0.0127 0.3382  -0.0324 150 HIS D N     
7690 C CA    . HIS D 178 ? 1.2652 0.7278 0.8727 -0.0218 0.3363  -0.0420 150 HIS D CA    
7691 C C     . HIS D 178 ? 1.2565 0.7277 0.8592 -0.0170 0.3328  -0.0354 150 HIS D C     
7692 O O     . HIS D 178 ? 1.2637 0.7593 0.8749 -0.0178 0.3256  -0.0411 150 HIS D O     
7693 C CB    . HIS D 178 ? 1.3057 0.7602 0.9137 -0.0376 0.3491  -0.0503 150 HIS D CB    
7694 C CG    . HIS D 178 ? 1.3068 0.7868 0.9262 -0.0476 0.3479  -0.0606 150 HIS D CG    
7695 N ND1   . HIS D 178 ? 1.3031 0.7888 0.9199 -0.0509 0.3522  -0.0583 150 HIS D ND1   
7696 C CD2   . HIS D 178 ? 1.3388 0.8407 0.9724 -0.0544 0.3431  -0.0730 150 HIS D CD2   
7697 C CE1   . HIS D 178 ? 1.3087 0.8193 0.9386 -0.0592 0.3504  -0.0688 150 HIS D CE1   
7698 N NE2   . HIS D 178 ? 1.3059 0.8270 0.9464 -0.0615 0.3445  -0.0777 150 HIS D NE2   
7699 N N     . LYS D 179 ? 1.2190 0.6702 0.8075 -0.0118 0.3377  -0.0234 151 LYS D N     
7700 C CA    . LYS D 179 ? 1.1510 0.6084 0.7323 -0.0064 0.3339  -0.0166 151 LYS D CA    
7701 C C     . LYS D 179 ? 1.1429 0.6171 0.7286 0.0054  0.3180  -0.0138 151 LYS D C     
7702 O O     . LYS D 179 ? 1.1428 0.6340 0.7298 0.0071  0.3115  -0.0155 151 LYS D O     
7703 C CB    . LYS D 179 ? 1.1266 0.5578 0.6907 -0.0025 0.3417  -0.0035 151 LYS D CB    
7704 C CG    . LYS D 179 ? 1.1311 0.5453 0.6886 -0.0142 0.3579  -0.0045 151 LYS D CG    
7705 C CD    . LYS D 179 ? 1.1679 0.5563 0.7075 -0.0085 0.3644  0.0099  151 LYS D CD    
7706 C CE    . LYS D 179 ? 1.1771 0.5464 0.7093 -0.0201 0.3810  0.0100  151 LYS D CE    
7707 N NZ    . LYS D 179 ? 1.1469 0.4919 0.6633 -0.0132 0.3854  0.0241  151 LYS D NZ    
7708 N N     . LEU D 180 ? 1.1115 0.5808 0.6995 0.0136  0.3119  -0.0095 152 LEU D N     
7709 C CA    . LEU D 180 ? 1.0488 0.5314 0.6404 0.0249  0.2971  -0.0048 152 LEU D CA    
7710 C C     . LEU D 180 ? 1.0525 0.5615 0.6589 0.0232  0.2876  -0.0156 152 LEU D C     
7711 O O     . LEU D 180 ? 1.0911 0.6139 0.7002 0.0305  0.2755  -0.0133 152 LEU D O     
7712 C CB    . LEU D 180 ? 1.0139 0.4833 0.6043 0.0342  0.2946  0.0041  152 LEU D CB    
7713 C CG    . LEU D 180 ? 1.0111 0.4574 0.5869 0.0406  0.2995  0.0182  152 LEU D CG    
7714 C CD1   . LEU D 180 ? 0.9404 0.3720 0.5170 0.0473  0.3014  0.0246  152 LEU D CD1   
7715 C CD2   . LEU D 180 ? 1.0447 0.4981 0.6146 0.0492  0.2887  0.0271  152 LEU D CD2   
7716 N N     . LEU D 181 ? 1.0847 0.6006 0.7004 0.0136  0.2925  -0.0271 153 LEU D N     
7717 C CA    . LEU D 181 ? 1.1507 0.6913 0.7806 0.0122  0.2836  -0.0371 153 LEU D CA    
7718 C C     . LEU D 181 ? 1.2125 0.7714 0.8460 0.0075  0.2824  -0.0435 153 LEU D C     
7719 O O     . LEU D 181 ? 1.2091 0.7628 0.8376 0.0000  0.2923  -0.0449 153 LEU D O     
7720 C CB    . LEU D 181 ? 1.1608 0.7015 0.7987 0.0041  0.2886  -0.0467 153 LEU D CB    
7721 C CG    . LEU D 181 ? 1.1141 0.6428 0.7515 0.0102  0.2875  -0.0429 153 LEU D CG    
7722 C CD1   . LEU D 181 ? 1.1857 0.7080 0.8262 0.0003  0.2957  -0.0526 153 LEU D CD1   
7723 C CD2   . LEU D 181 ? 1.0764 0.6224 0.7223 0.0196  0.2735  -0.0415 153 LEU D CD2   
7724 N N     . VAL D 182 ? 1.1711 0.7512 0.8135 0.0122  0.2705  -0.0470 154 VAL D N     
7725 C CA    . VAL D 182 ? 1.1770 0.7771 0.8253 0.0084  0.2687  -0.0545 154 VAL D CA    
7726 C C     . VAL D 182 ? 1.3081 0.9195 0.9682 -0.0030 0.2745  -0.0664 154 VAL D C     
7727 O O     . VAL D 182 ? 1.3830 0.9912 1.0480 -0.0055 0.2749  -0.0697 154 VAL D O     
7728 C CB    . VAL D 182 ? 1.0999 0.7175 0.7539 0.0174  0.2541  -0.0545 154 VAL D CB    
7729 C CG1   . VAL D 182 ? 1.1064 0.7129 0.7486 0.0276  0.2478  -0.0428 154 VAL D CG1   
7730 C CG2   . VAL D 182 ? 1.1459 0.7737 0.8118 0.0192  0.2465  -0.0585 154 VAL D CG2   
7731 N N     . PRO D 183 ? 1.3590 0.9835 1.0237 -0.0102 0.2792  -0.0731 155 PRO D N     
7732 C CA    . PRO D 183 ? 1.4141 1.0534 1.0922 -0.0211 0.2828  -0.0847 155 PRO D CA    
7733 C C     . PRO D 183 ? 1.3949 1.0528 1.0853 -0.0173 0.2709  -0.0904 155 PRO D C     
7734 O O     . PRO D 183 ? 1.3485 1.0226 1.0436 -0.0101 0.2611  -0.0908 155 PRO D O     
7735 C CB    . PRO D 183 ? 1.3891 1.0427 1.0704 -0.0260 0.2876  -0.0888 155 PRO D CB    
7736 C CG    . PRO D 183 ? 1.3697 1.0055 1.0348 -0.0219 0.2930  -0.0789 155 PRO D CG    
7737 C CD    . PRO D 183 ? 1.3425 0.9667 0.9990 -0.0095 0.2834  -0.0698 155 PRO D CD    
7738 N N     . GLY D 184 ? 1.3913 1.0455 1.0859 -0.0220 0.2719  -0.0949 156 GLY D N     
7739 C CA    . GLY D 184 ? 1.3570 1.0256 1.0611 -0.0181 0.2614  -0.0992 156 GLY D CA    
7740 C C     . GLY D 184 ? 1.3919 1.0465 1.0899 -0.0088 0.2563  -0.0917 156 GLY D C     
7741 O O     . GLY D 184 ? 1.4450 1.1087 1.1500 -0.0065 0.2491  -0.0949 156 GLY D O     
7742 N N     . GLY D 185 ? 1.3760 1.0101 1.0620 -0.0031 0.2595  -0.0811 157 GLY D N     
7743 C CA    . GLY D 185 ? 1.2919 0.9127 0.9730 0.0056  0.2557  -0.0732 157 GLY D CA    
7744 C C     . GLY D 185 ? 1.3028 0.9120 0.9839 0.0005  0.2618  -0.0768 157 GLY D C     
7745 O O     . GLY D 185 ? 1.2933 0.8991 0.9754 -0.0107 0.2702  -0.0839 157 GLY D O     
7746 N N     . GLU D 186 ? 1.2744 0.8778 0.9548 0.0087  0.2571  -0.0714 158 GLU D N     
7747 C CA    . GLU D 186 ? 1.2732 0.8681 0.9546 0.0055  0.2604  -0.0742 158 GLU D CA    
7748 C C     . GLU D 186 ? 1.2477 0.8171 0.9184 0.0124  0.2662  -0.0637 158 GLU D C     
7749 O O     . GLU D 186 ? 1.2103 0.7739 0.8755 0.0228  0.2634  -0.0537 158 GLU D O     
7750 C CB    . GLU D 186 ? 1.2510 0.8646 0.9426 0.0090  0.2499  -0.0783 158 GLU D CB    
7751 C CG    . GLU D 186 ? 1.3273 0.9664 1.0295 0.0033  0.2440  -0.0884 158 GLU D CG    
7752 C CD    . GLU D 186 ? 1.3873 1.0446 1.0979 0.0095  0.2327  -0.0901 158 GLU D CD    
7753 O OE1   . GLU D 186 ? 1.3703 1.0251 1.0791 0.0203  0.2271  -0.0815 158 GLU D OE1   
7754 O OE2   . GLU D 186 ? 1.4350 1.1088 1.1534 0.0035  0.2297  -0.1000 158 GLU D OE2   
7755 N N     . ALA D 187 ? 1.2207 0.7744 0.8880 0.0067  0.2744  -0.0661 159 ALA D N     
7756 C CA    . ALA D 187 ? 1.1022 0.6304 0.7594 0.0129  0.2814  -0.0567 159 ALA D CA    
7757 C C     . ALA D 187 ? 1.1110 0.6373 0.7715 0.0136  0.2805  -0.0590 159 ALA D C     
7758 O O     . ALA D 187 ? 1.1667 0.6948 0.8298 0.0033  0.2832  -0.0691 159 ALA D O     
7759 C CB    . ALA D 187 ? 1.1041 0.6093 0.7507 0.0054  0.2949  -0.0561 159 ALA D CB    
7760 N N     . VAL D 188 ? 1.0966 0.6192 0.7564 0.0258  0.2770  -0.0498 160 VAL D N     
7761 C CA    . VAL D 188 ? 1.0814 0.6026 0.7435 0.0285  0.2762  -0.0504 160 VAL D CA    
7762 C C     . VAL D 188 ? 1.1273 0.6212 0.7792 0.0318  0.2867  -0.0428 160 VAL D C     
7763 O O     . VAL D 188 ? 1.1588 0.6420 0.8058 0.0421  0.2883  -0.0310 160 VAL D O     
7764 C CB    . VAL D 188 ? 1.0148 0.5519 0.6839 0.0400  0.2658  -0.0453 160 VAL D CB    
7765 C CG1   . VAL D 188 ? 1.0072 0.5405 0.6770 0.0440  0.2667  -0.0444 160 VAL D CG1   
7766 C CG2   . VAL D 188 ? 0.9959 0.5593 0.6747 0.0365  0.2556  -0.0533 160 VAL D CG2   
7767 N N     . PHE D 189 ? 1.1111 0.5937 0.7596 0.0234  0.2938  -0.0495 161 PHE D N     
7768 C CA    . PHE D 189 ? 1.1044 0.5606 0.7429 0.0255  0.3045  -0.0434 161 PHE D CA    
7769 C C     . PHE D 189 ? 1.0650 0.5199 0.7045 0.0320  0.3036  -0.0417 161 PHE D C     
7770 O O     . PHE D 189 ? 1.0459 0.5175 0.6923 0.0307  0.2965  -0.0487 161 PHE D O     
7771 C CB    . PHE D 189 ? 1.1424 0.5830 0.7743 0.0113  0.3146  -0.0516 161 PHE D CB    
7772 C CG    . PHE D 189 ? 1.1816 0.6198 0.8109 0.0051  0.3182  -0.0522 161 PHE D CG    
7773 C CD1   . PHE D 189 ? 1.1605 0.5773 0.7794 0.0091  0.3267  -0.0423 161 PHE D CD1   
7774 C CD2   . PHE D 189 ? 1.1841 0.6418 0.8207 -0.0042 0.3135  -0.0624 161 PHE D CD2   
7775 C CE1   . PHE D 189 ? 1.0991 0.5128 0.7141 0.0037  0.3307  -0.0427 161 PHE D CE1   
7776 C CE2   . PHE D 189 ? 1.2118 0.6680 0.8457 -0.0096 0.3176  -0.0628 161 PHE D CE2   
7777 C CZ    . PHE D 189 ? 1.1655 0.5990 0.7879 -0.0058 0.3265  -0.0531 161 PHE D CZ    
7778 N N     . SER D 190 ? 1.0776 0.5123 0.7094 0.0395  0.3113  -0.0320 162 SER D N     
7779 C CA    . SER D 190 ? 1.0892 0.5185 0.7198 0.0463  0.3132  -0.0292 162 SER D CA    
7780 C C     . SER D 190 ? 1.0720 0.4739 0.6911 0.0469  0.3257  -0.0238 162 SER D C     
7781 O O     . SER D 190 ? 1.1157 0.5089 0.7318 0.0586  0.3291  -0.0116 162 SER D O     
7782 C CB    . SER D 190 ? 1.1281 0.5702 0.7654 0.0612  0.3061  -0.0188 162 SER D CB    
7783 O OG    . SER D 190 ? 1.0958 0.5347 0.7325 0.0673  0.3082  -0.0171 162 SER D OG    
7784 N N     . VAL D 191 ? 1.0891 0.4781 0.7020 0.0338  0.3328  -0.0329 163 VAL D N     
7785 C CA    . VAL D 191 ? 1.1358 0.4980 0.7371 0.0324  0.3453  -0.0290 163 VAL D CA    
7786 C C     . VAL D 191 ? 1.2245 0.5764 0.8213 0.0343  0.3497  -0.0313 163 VAL D C     
7787 O O     . VAL D 191 ? 1.2664 0.6265 0.8661 0.0280  0.3458  -0.0421 163 VAL D O     
7788 C CB    . VAL D 191 ? 1.1322 0.4845 0.7287 0.0168  0.3515  -0.0377 163 VAL D CB    
7789 C CG1   . VAL D 191 ? 1.1712 0.4956 0.7553 0.0159  0.3647  -0.0326 163 VAL D CG1   
7790 C CG2   . VAL D 191 ? 1.1517 0.5166 0.7529 0.0147  0.3467  -0.0369 163 VAL D CG2   
7791 N N     . ILE D 192 ? 1.1898 0.5241 0.7792 0.0434  0.3577  -0.0212 164 ILE D N     
7792 C CA    . ILE D 192 ? 1.2453 0.5664 0.8284 0.0456  0.3637  -0.0229 164 ILE D CA    
7793 C C     . ILE D 192 ? 1.3408 0.6407 0.9137 0.0319  0.3732  -0.0320 164 ILE D C     
7794 O O     . ILE D 192 ? 1.3865 0.6703 0.9524 0.0298  0.3813  -0.0278 164 ILE D O     
7795 C CB    . ILE D 192 ? 1.2021 0.5149 0.7823 0.0618  0.3685  -0.0083 164 ILE D CB    
7796 C CG1   . ILE D 192 ? 1.1797 0.5144 0.7709 0.0747  0.3590  -0.0003 164 ILE D CG1   
7797 C CG2   . ILE D 192 ? 1.3031 0.5973 0.8743 0.0631  0.3772  -0.0104 164 ILE D CG2   
7798 C CD1   . ILE D 192 ? 1.1461 0.4770 0.7370 0.0909  0.3627  0.0145  164 ILE D CD1   
7799 N N     . ALA D 193 ? 1.4230 0.7234 0.9949 0.0226  0.3721  -0.0448 165 ALA D N     
7800 C CA    . ALA D 193 ? 1.4508 0.7316 1.0132 0.0087  0.3805  -0.0547 165 ALA D CA    
7801 C C     . ALA D 193 ? 1.4394 0.6941 0.9899 0.0150  0.3919  -0.0483 165 ALA D C     
7802 O O     . ALA D 193 ? 1.4983 0.7356 1.0417 0.0130  0.4006  -0.0439 165 ALA D O     
7803 C CB    . ALA D 193 ? 1.4792 0.7685 1.0433 -0.0017 0.3753  -0.0699 165 ALA D CB    
7804 N N     . ASN D 194 ? 1.4337 0.6856 0.9815 0.0230  0.3921  -0.0478 166 ASN D N     
7805 C CA    . ASN D 194 ? 1.4946 0.7226 1.0313 0.0302  0.4028  -0.0422 166 ASN D CA    
7806 C C     . ASN D 194 ? 1.4541 0.6895 0.9939 0.0473  0.4005  -0.0328 166 ASN D C     
7807 O O     . ASN D 194 ? 1.3936 0.6491 0.9418 0.0504  0.3914  -0.0352 166 ASN D O     
7808 C CB    . ASN D 194 ? 1.5807 0.7898 1.1067 0.0183  0.4088  -0.0551 166 ASN D CB    
7809 C CG    . ASN D 194 ? 1.6360 0.8563 1.1639 0.0168  0.4018  -0.0650 166 ASN D CG    
7810 O OD1   . ASN D 194 ? 1.6400 0.8580 1.1654 0.0281  0.4028  -0.0611 166 ASN D OD1   
7811 N ND2   . ASN D 194 ? 1.6453 0.8785 1.1779 0.0029  0.3949  -0.0779 166 ASN D ND2   
7812 N N     . MET D 195 ? 1.4128 0.6325 0.9463 0.0586  0.4091  -0.0221 167 MET D N     
7813 C CA    . MET D 195 ? 1.4189 0.6441 0.9552 0.0753  0.4089  -0.0125 167 MET D CA    
7814 C C     . MET D 195 ? 1.5000 0.7003 1.0249 0.0827  0.4212  -0.0063 167 MET D C     
7815 O O     . MET D 195 ? 1.5388 0.7210 1.0560 0.0777  0.4288  -0.0058 167 MET D O     
7816 C CB    . MET D 195 ? 1.3943 0.6414 0.9429 0.0867  0.4016  0.0000  167 MET D CB    
7817 C CG    . MET D 195 ? 1.5539 0.7982 1.1027 0.0865  0.4034  0.0073  167 MET D CG    
7818 S SD    . MET D 195 ? 1.5512 0.8231 1.1145 0.0981  0.3927  0.0195  167 MET D SD    
7819 C CE    . MET D 195 ? 1.4297 0.7114 0.9988 0.1146  0.3915  0.0276  167 MET D CE    
7820 N N     . ALA D 196 ? 1.5214 0.7212 1.0456 0.0951  0.4234  -0.0013 168 ALA D N     
7821 C CA    . ALA D 196 ? 1.5795 0.7561 1.0932 0.1033  0.4352  0.0042  168 ALA D CA    
7822 C C     . ALA D 196 ? 1.5582 0.7342 1.0746 0.1153  0.4391  0.0193  168 ALA D C     
7823 O O     . ALA D 196 ? 1.5174 0.6729 1.0248 0.1210  0.4494  0.0240  168 ALA D O     
7824 C CB    . ALA D 196 ? 1.6034 0.7806 1.1157 0.1134  0.4366  0.0049  168 ALA D CB    
7825 N N     . LEU D 197 ? 1.5404 0.7383 1.0688 0.1194  0.4309  0.0269  169 LEU D N     
7826 C CA    . LEU D 197 ? 1.5995 0.7975 1.1304 0.1295  0.4335  0.0401  169 LEU D CA    
7827 C C     . LEU D 197 ? 1.6511 0.8289 1.1722 0.1203  0.4404  0.0373  169 LEU D C     
7828 O O     . LEU D 197 ? 1.5846 0.7518 1.1022 0.1284  0.4468  0.0464  169 LEU D O     
7829 C CB    . LEU D 197 ? 1.5881 0.8139 1.1334 0.1347  0.4222  0.0474  169 LEU D CB    
7830 C CG    . LEU D 197 ? 1.4907 0.7402 1.0484 0.1453  0.4145  0.0529  169 LEU D CG    
7831 C CD1   . LEU D 197 ? 1.3333 0.6067 0.9040 0.1500  0.4042  0.0609  169 LEU D CD1   
7832 C CD2   . LEU D 197 ? 1.4632 0.7084 1.0206 0.1602  0.4212  0.0618  169 LEU D CD2   
7833 N N     . CYS D 198 ? 1.7085 0.8814 1.2256 0.1033  0.4390  0.0250  170 CYS D N     
7834 C CA    . CYS D 198 ? 1.6383 0.7926 1.1465 0.0931  0.4458  0.0217  170 CYS D CA    
7835 C C     . CYS D 198 ? 1.6705 0.7955 1.1647 0.0906  0.4578  0.0175  170 CYS D C     
7836 O O     . CYS D 198 ? 1.6469 0.7542 1.1337 0.0921  0.4659  0.0222  170 CYS D O     
7837 C CB    . CYS D 198 ? 1.5845 0.7457 1.0949 0.0755  0.4403  0.0099  170 CYS D CB    
7838 S SG    . CYS D 198 ? 1.6791 0.8691 1.2032 0.0769  0.4281  0.0151  170 CYS D SG    
7839 N N     . ASP D 199 ? 1.7130 0.8319 1.2029 0.0868  0.4588  0.0085  171 ASP D N     
7840 C CA    . ASP D 199 ? 1.7002 0.7902 1.1759 0.0851  0.4699  0.0041  171 ASP D CA    
7841 C C     . ASP D 199 ? 1.7415 0.8221 1.2142 0.1030  0.4774  0.0173  171 ASP D C     
7842 O O     . ASP D 199 ? 1.7744 0.8298 1.2360 0.1034  0.4878  0.0183  171 ASP D O     
7843 C CB    . ASP D 199 ? 1.6094 0.6970 1.0813 0.0788  0.4682  -0.0082 171 ASP D CB    
7844 C CG    . ASP D 199 ? 1.6341 0.7287 1.1080 0.0600  0.4618  -0.0225 171 ASP D CG    
7845 O OD1   . ASP D 199 ? 1.6928 0.7798 1.1642 0.0483  0.4642  -0.0261 171 ASP D OD1   
7846 O OD2   . ASP D 199 ? 1.5982 0.7066 1.0765 0.0570  0.4543  -0.0303 171 ASP D OD2   
7847 N N     . ALA D 200 ? 1.7630 0.8640 1.2464 0.1179  0.4721  0.0275  172 ALA D N     
7848 C CA    . ALA D 200 ? 1.7206 0.8167 1.2038 0.1354  0.4783  0.0410  172 ALA D CA    
7849 C C     . ALA D 200 ? 1.7274 0.8188 1.2105 0.1383  0.4810  0.0497  172 ALA D C     
7850 O O     . ALA D 200 ? 1.6673 0.7441 1.1453 0.1485  0.4893  0.0578  172 ALA D O     
7851 C CB    . ALA D 200 ? 1.6499 0.7721 1.1466 0.1496  0.4711  0.0500  172 ALA D CB    
7852 N N     . TYR D 201 ? 1.7355 0.8391 1.2241 0.1297  0.4741  0.0481  173 TYR D N     
7853 C CA    . TYR D 201 ? 1.7569 0.8548 1.2441 0.1309  0.4765  0.0551  173 TYR D CA    
7854 C C     . TYR D 201 ? 1.7717 0.8386 1.2440 0.1208  0.4875  0.0487  173 TYR D C     
7855 O O     . TYR D 201 ? 1.7413 0.7933 1.2082 0.1277  0.4946  0.0564  173 TYR D O     
7856 C CB    . TYR D 201 ? 1.7074 0.8256 1.2034 0.1238  0.4664  0.0543  173 TYR D CB    
7857 C CG    . TYR D 201 ? 1.6799 0.8262 1.1905 0.1367  0.4563  0.0651  173 TYR D CG    
7858 C CD1   . TYR D 201 ? 1.6029 0.7538 1.1183 0.1541  0.4574  0.0775  173 TYR D CD1   
7859 C CD2   . TYR D 201 ? 1.6485 0.8169 1.1683 0.1313  0.4453  0.0629  173 TYR D CD2   
7860 C CE1   . TYR D 201 ? 1.5365 0.7140 1.0663 0.1651  0.4475  0.0872  173 TYR D CE1   
7861 C CE2   . TYR D 201 ? 1.5675 0.7610 1.1005 0.1425  0.4355  0.0724  173 TYR D CE2   
7862 C CZ    . TYR D 201 ? 1.5243 0.7226 1.0626 0.1591  0.4364  0.0845  173 TYR D CZ    
7863 O OH    . TYR D 201 ? 1.4496 0.6740 1.0023 0.1694  0.4260  0.0938  173 TYR D OH    
7864 N N     . GLU D 202 ? 1.7709 0.8282 1.2369 0.1043  0.4888  0.0347  174 GLU D N     
7865 C CA    . GLU D 202 ? 1.7896 0.8180 1.2420 0.0929  0.4988  0.0276  174 GLU D CA    
7866 C C     . GLU D 202 ? 1.7980 0.8016 1.2395 0.1013  0.5095  0.0299  174 GLU D C     
7867 O O     . GLU D 202 ? 1.8079 0.7868 1.2389 0.0984  0.5188  0.0301  174 GLU D O     
7868 C CB    . GLU D 202 ? 1.8163 0.8428 1.2662 0.0732  0.4965  0.0115  174 GLU D CB    
7869 C CG    . GLU D 202 ? 1.8882 0.9338 1.3468 0.0624  0.4883  0.0081  174 GLU D CG    
7870 C CD    . GLU D 202 ? 1.8921 0.9415 1.3512 0.0447  0.4842  -0.0076 174 GLU D CD    
7871 O OE1   . GLU D 202 ? 1.8155 0.8656 1.2737 0.0448  0.4824  -0.0139 174 GLU D OE1   
7872 O OE2   . GLU D 202 ? 1.8866 0.9389 1.3473 0.0308  0.4827  -0.0135 174 GLU D OE2   
7873 N N     . GLU D 203 ? 1.8297 0.8388 1.2732 0.1117  0.5086  0.0317  175 GLU D N     
7874 C CA    . GLU D 203 ? 1.8235 0.8094 1.2566 0.1209  0.5191  0.0342  175 GLU D CA    
7875 C C     . GLU D 203 ? 1.8403 0.8251 1.2758 0.1386  0.5233  0.0500  175 GLU D C     
7876 O O     . GLU D 203 ? 1.8972 0.8566 1.3219 0.1432  0.5339  0.0526  175 GLU D O     
7877 C CB    . GLU D 203 ? 1.7652 0.7574 1.1993 0.1258  0.5170  0.0303  175 GLU D CB    
7878 N N     . MET D 204 ? 1.8195 0.8313 1.2691 0.1485  0.5149  0.0604  176 MET D N     
7879 C CA    . MET D 204 ? 1.8150 0.8285 1.2686 0.1649  0.5174  0.0754  176 MET D CA    
7880 C C     . MET D 204 ? 1.8431 0.8404 1.2902 0.1603  0.5219  0.0778  176 MET D C     
7881 O O     . MET D 204 ? 1.7875 0.7721 1.2312 0.1714  0.5285  0.0873  176 MET D O     
7882 C CB    . MET D 204 ? 1.8001 0.8478 1.2712 0.1754  0.5059  0.0851  176 MET D CB    
7883 C CG    . MET D 204 ? 1.7969 0.8609 1.2757 0.1842  0.5024  0.0864  176 MET D CG    
7884 S SD    . MET D 204 ? 1.6732 0.7776 1.1734 0.1950  0.4884  0.0975  176 MET D SD    
7885 C CE    . MET D 204 ? 1.5718 0.6748 1.0762 0.2129  0.4921  0.1143  176 MET D CE    
7886 N N     . ALA D 205 ? 1.8533 0.8510 1.2989 0.1442  0.5187  0.0696  177 ALA D N     
7887 C CA    . ALA D 205 ? 1.8837 0.8680 1.3238 0.1394  0.5225  0.0723  177 ALA D CA    
7888 C C     . ALA D 205 ? 1.9353 0.8843 1.3599 0.1370  0.5358  0.0698  177 ALA D C     
7889 O O     . ALA D 205 ? 1.9314 0.8668 1.3514 0.1396  0.5408  0.0764  177 ALA D O     
7890 C CB    . ALA D 205 ? 1.8443 0.8364 1.2861 0.1219  0.5169  0.0631  177 ALA D CB    
7891 N N     . LYS D 206 ? 1.9211 0.8543 1.3372 0.1320  0.5414  0.0604  178 LYS D N     
7892 C CA    . LYS D 206 ? 1.8362 0.7344 1.2369 0.1296  0.5541  0.0573  178 LYS D CA    
7893 C C     . LYS D 206 ? 1.8893 0.7772 1.2876 0.1490  0.5610  0.0697  178 LYS D C     
7894 O O     . LYS D 206 ? 1.9544 0.8133 1.3406 0.1495  0.5715  0.0704  178 LYS D O     
7895 C CB    . LYS D 206 ? 1.7446 0.6292 1.1366 0.1179  0.5570  0.0426  178 LYS D CB    
7896 C CG    . LYS D 206 ? 1.7017 0.5916 1.0944 0.0968  0.5518  0.0292  178 LYS D CG    
7897 C CD    . LYS D 206 ? 1.6356 0.5148 1.0209 0.0863  0.5531  0.0148  178 LYS D CD    
7898 C CE    . LYS D 206 ? 1.6147 0.5028 1.0030 0.0657  0.5468  0.0016  178 LYS D CE    
7899 N NZ    . LYS D 206 ? 1.6622 0.5435 1.0447 0.0559  0.5460  -0.0125 178 LYS D NZ    
7900 N N     . GLU D 207 ? 1.8646 0.7757 1.2746 0.1648  0.5554  0.0794  179 GLU D N     
7901 C CA    . GLU D 207 ? 1.8551 0.7591 1.2647 0.1838  0.5616  0.0916  179 GLU D CA    
7902 C C     . GLU D 207 ? 1.8171 0.7165 1.2275 0.1899  0.5631  0.1028  179 GLU D C     
7903 O O     . GLU D 207 ? 1.8512 0.7713 1.2714 0.1884  0.5541  0.1071  179 GLU D O     
7904 C CB    . GLU D 207 ? 1.8586 0.7916 1.2826 0.1982  0.5544  0.0994  179 GLU D CB    
7905 N N     . PRO D 208 ? 1.8491 0.7213 1.2490 0.1968  0.5742  0.1078  180 PRO D N     
7906 C CA    . PRO D 208 ? 1.9310 0.7989 1.3318 0.2036  0.5753  0.1194  180 PRO D CA    
7907 C C     . PRO D 208 ? 1.9157 0.8139 1.3330 0.2194  0.5660  0.1336  180 PRO D C     
7908 O O     . PRO D 208 ? 1.9962 0.8978 1.4166 0.2229  0.5630  0.1425  180 PRO D O     
7909 C CB    . PRO D 208 ? 1.9571 0.7909 1.3441 0.2106  0.5892  0.1221  180 PRO D CB    
7910 C CG    . PRO D 208 ? 1.9948 0.8085 1.3697 0.1987  0.5956  0.1073  180 PRO D CG    
7911 C CD    . PRO D 208 ? 1.8962 0.7374 1.2813 0.1960  0.5862  0.1014  180 PRO D CD    
7912 N N     . ARG D 209 ? 1.8070 0.7273 1.2351 0.2289  0.5609  0.1362  181 ARG D N     
7913 C CA    . ARG D 209 ? 1.8161 0.7680 1.2616 0.2425  0.5507  0.1489  181 ARG D CA    
7914 C C     . ARG D 209 ? 1.8163 0.7954 1.2725 0.2335  0.5371  0.1464  181 ARG D C     
7915 O O     . ARG D 209 ? 1.6427 0.6452 1.1119 0.2422  0.5277  0.1569  181 ARG D O     
7916 C CB    . ARG D 209 ? 1.8119 0.7775 1.2655 0.2554  0.5507  0.1526  181 ARG D CB    
7917 C CG    . ARG D 209 ? 1.8251 0.8065 1.2828 0.2469  0.5449  0.1420  181 ARG D CG    
7918 C CD    . ARG D 209 ? 1.7423 0.7398 1.2094 0.2607  0.5444  0.1474  181 ARG D CD    
7919 N NE    . ARG D 209 ? 1.7536 0.7741 1.2365 0.2771  0.5386  0.1629  181 ARG D NE    
7920 C CZ    . ARG D 209 ? 1.5995 0.6427 1.0957 0.2891  0.5351  0.1696  181 ARG D CZ    
7921 N NH1   . ARG D 209 ? 1.5285 0.5743 1.0235 0.2874  0.5368  0.1626  181 ARG D NH1   
7922 N NH2   . ARG D 209 ? 1.5145 0.5785 1.0257 0.3030  0.5294  0.1839  181 ARG D NH2   
7923 N N     . TRP D 210 ? 1.8599 0.8362 1.3108 0.2163  0.5357  0.1327  182 TRP D N     
7924 C CA    . TRP D 210 ? 1.8752 0.8770 1.3359 0.2076  0.5234  0.1291  182 TRP D CA    
7925 C C     . TRP D 210 ? 1.8270 0.8180 1.2800 0.1916  0.5235  0.1223  182 TRP D C     
7926 O O     . TRP D 210 ? 1.8071 0.8186 1.2681 0.1864  0.5133  0.1219  182 TRP D O     
7927 C CB    . TRP D 210 ? 1.7994 0.8142 1.2638 0.2013  0.5194  0.1190  182 TRP D CB    
7928 C CG    . TRP D 210 ? 1.7445 0.7750 1.2183 0.2158  0.5176  0.1251  182 TRP D CG    
7929 C CD1   . TRP D 210 ? 1.7015 0.7292 1.1725 0.2147  0.5208  0.1179  182 TRP D CD1   
7930 C CD2   . TRP D 210 ? 1.7534 0.8056 1.2415 0.2329  0.5119  0.1395  182 TRP D CD2   
7931 N NE1   . TRP D 210 ? 1.7379 0.7836 1.2201 0.2303  0.5184  0.1271  182 TRP D NE1   
7932 C CE2   . TRP D 210 ? 1.7487 0.8102 1.2421 0.2414  0.5129  0.1403  182 TRP D CE2   
7933 C CE3   . TRP D 210 ? 1.7283 0.7934 1.2254 0.2415  0.5057  0.1517  182 TRP D CE3   
7934 C CZ2   . TRP D 210 ? 1.7306 0.8142 1.2389 0.2580  0.5084  0.1531  182 TRP D CZ2   
7935 C CZ3   . TRP D 210 ? 1.6780 0.7650 1.1897 0.2577  0.5004  0.1641  182 TRP D CZ3   
7936 C CH2   . TRP D 210 ? 1.6776 0.7740 1.1953 0.2656  0.5020  0.1647  182 TRP D CH2   
7937 N N     . ALA D 211 ? 1.8259 0.7855 1.2640 0.1837  0.5348  0.1169  183 ALA D N     
7938 C CA    . ALA D 211 ? 1.7588 0.7077 1.1896 0.1663  0.5358  0.1086  183 ALA D CA    
7939 C C     . ALA D 211 ? 1.7818 0.7417 1.2177 0.1681  0.5295  0.1174  183 ALA D C     
7940 O O     . ALA D 211 ? 1.8018 0.7654 1.2370 0.1548  0.5259  0.1114  183 ALA D O     
7941 C CB    . ALA D 211 ? 1.7867 0.6989 1.2010 0.1588  0.5494  0.1028  183 ALA D CB    
7942 N N     . LEU D 212 ? 1.8163 0.7814 1.2571 0.1843  0.5277  0.1317  184 LEU D N     
7943 C CA    . LEU D 212 ? 1.7586 0.7348 1.2039 0.1868  0.5205  0.1407  184 LEU D CA    
7944 C C     . LEU D 212 ? 1.7566 0.7654 1.2149 0.1843  0.5064  0.1398  184 LEU D C     
7945 O O     . LEU D 212 ? 1.6865 0.7003 1.1441 0.1744  0.5017  0.1372  184 LEU D O     
7946 C CB    . LEU D 212 ? 1.5904 0.5664 1.0391 0.2051  0.5209  0.1565  184 LEU D CB    
7947 N N     . TYR D 213 ? 1.7575 0.7884 1.2275 0.1931  0.4996  0.1419  185 TYR D N     
7948 C CA    . TYR D 213 ? 1.6473 0.7090 1.1300 0.1915  0.4859  0.1411  185 TYR D CA    
7949 C C     . TYR D 213 ? 1.6601 0.7240 1.1406 0.1751  0.4851  0.1262  185 TYR D C     
7950 O O     . TYR D 213 ? 1.6569 0.7439 1.1463 0.1717  0.4743  0.1244  185 TYR D O     
7951 C CB    . TYR D 213 ? 1.6130 0.6976 1.1097 0.2062  0.4792  0.1486  185 TYR D CB    
7952 C CG    . TYR D 213 ? 1.6308 0.7177 1.1325 0.2230  0.4787  0.1639  185 TYR D CG    
7953 C CD1   . TYR D 213 ? 1.5909 0.6966 1.1016 0.2289  0.4674  0.1744  185 TYR D CD1   
7954 C CD2   . TYR D 213 ? 1.7358 0.8063 1.2332 0.2329  0.4890  0.1680  185 TYR D CD2   
7955 C CE1   . TYR D 213 ? 1.5907 0.6996 1.1066 0.2438  0.4661  0.1887  185 TYR D CE1   
7956 C CE2   . TYR D 213 ? 1.7995 0.8728 1.3023 0.2485  0.4885  0.1823  185 TYR D CE2   
7957 C CZ    . TYR D 213 ? 1.6780 0.7710 1.1904 0.2537  0.4768  0.1927  185 TYR D CZ    
7958 O OH    . TYR D 213 ? 1.5988 0.6955 1.1171 0.2688  0.4756  0.2072  185 TYR D OH    
7959 N N     . MET D 214 ? 1.7080 0.7486 1.1770 0.1649  0.4957  0.1156  186 MET D N     
7960 C CA    . MET D 214 ? 1.7038 0.7469 1.1714 0.1496  0.4947  0.1013  186 MET D CA    
7961 C C     . MET D 214 ? 1.7763 0.7962 1.2316 0.1327  0.5028  0.0917  186 MET D C     
7962 O O     . MET D 214 ? 1.7736 0.7842 1.2237 0.1203  0.5069  0.0794  186 MET D O     
7963 C CB    . MET D 214 ? 1.6755 0.7172 1.1432 0.1522  0.4977  0.0961  186 MET D CB    
7964 N N     . GLN D 215 ? 1.7577 0.7684 1.2085 0.1316  0.5049  0.0973  187 GLN D N     
7965 C CA    . GLN D 215 ? 1.7415 0.7320 1.1819 0.1150  0.5123  0.0886  187 GLN D CA    
7966 C C     . GLN D 215 ? 1.7816 0.7872 1.2264 0.0999  0.5061  0.0782  187 GLN D C     
7967 O O     . GLN D 215 ? 1.7876 0.7796 1.2259 0.0837  0.5119  0.0669  187 GLN D O     
7968 C CB    . GLN D 215 ? 1.6611 0.6400 1.0963 0.1181  0.5154  0.0981  187 GLN D CB    
7969 N N     . ASP D 216 ? 1.7283 0.7617 1.1845 0.1047  0.4943  0.0817  188 ASP D N     
7970 C CA    . ASP D 216 ? 1.7021 0.7522 1.1636 0.0921  0.4874  0.0727  188 ASP D CA    
7971 C C     . ASP D 216 ? 1.6540 0.7191 1.1225 0.0918  0.4822  0.0660  188 ASP D C     
7972 O O     . ASP D 216 ? 1.6083 0.6975 1.0866 0.0925  0.4719  0.0656  188 ASP D O     
7973 C CB    . ASP D 216 ? 1.6908 0.7605 1.1591 0.0969  0.4776  0.0807  188 ASP D CB    
7974 C CG    . ASP D 216 ? 1.6571 0.7428 1.1338 0.1158  0.4698  0.0938  188 ASP D CG    
7975 O OD1   . ASP D 216 ? 1.6394 0.7172 1.1153 0.1260  0.4741  0.0982  188 ASP D OD1   
7976 O OD2   . ASP D 216 ? 1.7305 0.8364 1.2146 0.1202  0.4592  0.0996  188 ASP D OD2   
7977 N N     . VAL D 217 ? 1.6585 0.7088 1.1216 0.0907  0.4892  0.0606  189 VAL D N     
7978 C CA    . VAL D 217 ? 1.6272 0.6907 1.0964 0.0920  0.4844  0.0553  189 VAL D CA    
7979 C C     . VAL D 217 ? 1.6017 0.6763 1.0743 0.0758  0.4794  0.0428  189 VAL D C     
7980 O O     . VAL D 217 ? 1.6186 0.7143 1.1004 0.0777  0.4706  0.0409  189 VAL D O     
7981 C CB    . VAL D 217 ? 1.7047 0.7475 1.1656 0.0946  0.4935  0.0525  189 VAL D CB    
7982 C CG1   . VAL D 217 ? 1.7732 0.7902 1.2222 0.0781  0.5031  0.0414  189 VAL D CG1   
7983 C CG2   . VAL D 217 ? 1.7784 0.8354 1.2456 0.0980  0.4883  0.0487  189 VAL D CG2   
7984 N N     . GLU D 218 ? 1.6077 0.6693 1.0740 0.0597  0.4846  0.0344  190 GLU D N     
7985 C CA    . GLU D 218 ? 1.5951 0.6673 1.0654 0.0436  0.4803  0.0221  190 GLU D CA    
7986 C C     . GLU D 218 ? 1.5897 0.6875 1.0701 0.0448  0.4698  0.0252  190 GLU D C     
7987 O O     . GLU D 218 ? 1.5372 0.6490 1.0235 0.0347  0.4641  0.0164  190 GLU D O     
7988 C CB    . GLU D 218 ? 1.6099 0.6624 1.0719 0.0259  0.4889  0.0128  190 GLU D CB    
7989 C CG    . GLU D 218 ? 1.7490 0.7951 1.2077 0.0243  0.4924  0.0188  190 GLU D CG    
7990 C CD    . GLU D 218 ? 1.6957 0.7209 1.1458 0.0353  0.5003  0.0289  190 GLU D CD    
7991 O OE1   . GLU D 218 ? 1.6162 0.6340 1.0639 0.0459  0.5027  0.0324  190 GLU D OE1   
7992 O OE2   . GLU D 218 ? 1.6985 0.7148 1.1445 0.0333  0.5042  0.0336  190 GLU D OE2   
7993 N N     . LYS D 219 ? 1.5720 0.6761 1.0546 0.0569  0.4667  0.0374  191 LYS D N     
7994 C CA    . LYS D 219 ? 1.5493 0.6774 1.0410 0.0600  0.4560  0.0412  191 LYS D CA    
7995 C C     . LYS D 219 ? 1.5430 0.6923 1.0448 0.0730  0.4462  0.0465  191 LYS D C     
7996 O O     . LYS D 219 ? 1.5239 0.6944 1.0342 0.0735  0.4363  0.0469  191 LYS D O     
7997 C CB    . LYS D 219 ? 1.4675 0.5932 0.9567 0.0662  0.4559  0.0517  191 LYS D CB    
7998 N N     . PHE D 220 ? 1.5069 0.6509 1.0082 0.0836  0.4489  0.0508  192 PHE D N     
7999 C CA    . PHE D 220 ? 1.4097 0.5729 0.9209 0.0955  0.4408  0.0553  192 PHE D CA    
8000 C C     . PHE D 220 ? 1.3497 0.5168 0.8629 0.0879  0.4397  0.0445  192 PHE D C     
8001 O O     . PHE D 220 ? 1.3769 0.5574 0.8973 0.0972  0.4344  0.0475  192 PHE D O     
8002 C CB    . PHE D 220 ? 1.4038 0.5607 0.9145 0.1118  0.4445  0.0663  192 PHE D CB    
8003 C CG    . PHE D 220 ? 1.4062 0.5694 0.9203 0.1230  0.4407  0.0792  192 PHE D CG    
8004 C CD1   . PHE D 220 ? 1.4951 0.6425 1.0008 0.1194  0.4462  0.0816  192 PHE D CD1   
8005 C CD2   . PHE D 220 ? 1.4242 0.6091 0.9500 0.1371  0.4311  0.0893  192 PHE D CD2   
8006 C CE1   . PHE D 220 ? 1.5480 0.7012 1.0565 0.1296  0.4417  0.0936  192 PHE D CE1   
8007 C CE2   . PHE D 220 ? 1.4383 0.6299 0.9678 0.1468  0.4263  0.1011  192 PHE D CE2   
8008 C CZ    . PHE D 220 ? 1.4989 0.6745 1.0194 0.1432  0.4314  0.1033  192 PHE D CZ    
8009 N N     . VAL D 221 ? 1.3617 0.5180 0.8692 0.0713  0.4440  0.0321  193 VAL D N     
8010 C CA    . VAL D 221 ? 1.3982 0.5567 0.9069 0.0625  0.4425  0.0206  193 VAL D CA    
8011 C C     . VAL D 221 ? 1.4405 0.6141 0.9553 0.0492  0.4354  0.0116  193 VAL D C     
8012 O O     . VAL D 221 ? 1.5073 0.6784 1.0202 0.0409  0.4371  0.0102  193 VAL D O     
8013 C CB    . VAL D 221 ? 1.4527 0.5849 0.9498 0.0539  0.4535  0.0127  193 VAL D CB    
8014 C CG1   . VAL D 221 ? 1.5077 0.6430 1.0060 0.0440  0.4506  -0.0002 193 VAL D CG1   
8015 C CG2   . VAL D 221 ? 1.5594 0.6763 1.0503 0.0680  0.4607  0.0218  193 VAL D CG2   
8016 N N     . SER D 222 ? 1.2904 0.4801 0.8129 0.0475  0.4275  0.0056  194 SER D N     
8017 C CA    . SER D 222 ? 1.3976 0.6016 0.9265 0.0343  0.4207  -0.0045 194 SER D CA    
8018 C C     . SER D 222 ? 1.5730 0.7610 1.0948 0.0162  0.4282  -0.0163 194 SER D C     
8019 O O     . SER D 222 ? 1.5573 0.7271 1.0712 0.0124  0.4354  -0.0212 194 SER D O     
8020 C CB    . SER D 222 ? 1.3453 0.5672 0.8828 0.0354  0.4116  -0.0101 194 SER D CB    
8021 O OG    . SER D 222 ? 1.4113 0.6446 0.9541 0.0208  0.4061  -0.0225 194 SER D OG    
8022 N N     . PRO D 223 ? 1.6125 0.8064 1.1370 0.0047  0.4269  -0.0212 195 PRO D N     
8023 C CA    . PRO D 223 ? 1.6191 0.7991 1.1382 -0.0133 0.4342  -0.0326 195 PRO D CA    
8024 C C     . PRO D 223 ? 1.6177 0.8022 1.1397 -0.0244 0.4308  -0.0467 195 PRO D C     
8025 O O     . PRO D 223 ? 1.6714 0.8399 1.1869 -0.0370 0.4377  -0.0558 195 PRO D O     
8026 C CB    . PRO D 223 ? 1.5906 0.7805 1.1140 -0.0211 0.4324  -0.0334 195 PRO D CB    
8027 C CG    . PRO D 223 ? 1.5242 0.7378 1.0574 -0.0106 0.4211  -0.0277 195 PRO D CG    
8028 C CD    . PRO D 223 ? 1.5139 0.7276 1.0465 0.0073  0.4188  -0.0171 195 PRO D CD    
8029 N N     . TYR D 224 ? 1.5709 0.7769 1.1024 -0.0201 0.4200  -0.0491 196 TYR D N     
8030 C CA    . TYR D 224 ? 1.5879 0.8009 1.1225 -0.0286 0.4152  -0.0622 196 TYR D CA    
8031 C C     . TYR D 224 ? 1.5997 0.8009 1.1277 -0.0202 0.4176  -0.0611 196 TYR D C     
8032 O O     . TYR D 224 ? 1.6397 0.8491 1.1701 -0.0231 0.4120  -0.0701 196 TYR D O     
8033 C CB    . TYR D 224 ? 1.5456 0.7883 1.0935 -0.0276 0.4019  -0.0656 196 TYR D CB    
8034 C CG    . TYR D 224 ? 1.5451 0.8004 1.0995 -0.0327 0.3991  -0.0648 196 TYR D CG    
8035 C CD1   . TYR D 224 ? 1.6063 0.8628 1.1623 -0.0502 0.4012  -0.0761 196 TYR D CD1   
8036 C CD2   . TYR D 224 ? 1.5343 0.8000 1.0930 -0.0202 0.3947  -0.0530 196 TYR D CD2   
8037 C CE1   . TYR D 224 ? 1.5927 0.8603 1.1543 -0.0546 0.3996  -0.0755 196 TYR D CE1   
8038 C CE2   . TYR D 224 ? 1.5163 0.7922 1.0796 -0.0244 0.3924  -0.0525 196 TYR D CE2   
8039 C CZ    . TYR D 224 ? 1.5361 0.8127 1.1007 -0.0414 0.3952  -0.0638 196 TYR D CZ    
8040 O OH    . TYR D 224 ? 1.5715 0.8579 1.1403 -0.0453 0.3937  -0.0635 196 TYR D OH    
8041 N N     . GLN D 225 ? 1.5959 0.7787 1.1154 -0.0092 0.4259  -0.0503 197 GLN D N     
8042 C CA    . GLN D 225 ? 1.6137 0.7838 1.1263 -0.0005 0.4295  -0.0488 197 GLN D CA    
8043 C C     . GLN D 225 ? 1.6920 0.8456 1.1962 -0.0143 0.4344  -0.0625 197 GLN D C     
8044 O O     . GLN D 225 ? 1.7195 0.8766 1.2233 -0.0144 0.4305  -0.0697 197 GLN D O     
8045 C CB    . GLN D 225 ? 1.5837 0.7370 1.0891 0.0130  0.4382  -0.0349 197 GLN D CB    
8046 C CG    . GLN D 225 ? 1.5571 0.6963 1.0551 0.0233  0.4433  -0.0322 197 GLN D CG    
8047 C CD    . GLN D 225 ? 1.6015 0.7601 1.1078 0.0360  0.4350  -0.0280 197 GLN D CD    
8048 O OE1   . GLN D 225 ? 1.5905 0.7712 1.1077 0.0420  0.4266  -0.0219 197 GLN D OE1   
8049 N NE2   . GLN D 225 ? 1.6798 0.8298 1.1807 0.0401  0.4375  -0.0312 197 GLN D NE2   
8050 N N     . HIS D 226 ? 1.7248 0.8601 1.2217 -0.0261 0.4429  -0.0664 198 HIS D N     
8051 C CA    . HIS D 226 ? 1.7310 0.8486 1.2192 -0.0403 0.4480  -0.0793 198 HIS D CA    
8052 C C     . HIS D 226 ? 1.7523 0.8835 1.2472 -0.0590 0.4423  -0.0935 198 HIS D C     
8053 O O     . HIS D 226 ? 1.8225 0.9396 1.3111 -0.0737 0.4469  -0.1044 198 HIS D O     
8054 C CB    . HIS D 226 ? 1.6867 0.7753 1.1629 -0.0427 0.4610  -0.0756 198 HIS D CB    
8055 C CG    . HIS D 226 ? 1.7515 0.8276 1.2217 -0.0242 0.4669  -0.0613 198 HIS D CG    
8056 N ND1   . HIS D 226 ? 1.7788 0.8486 1.2444 -0.0126 0.4677  -0.0591 198 HIS D ND1   
8057 C CD2   . HIS D 226 ? 1.7869 0.8567 1.2554 -0.0150 0.4722  -0.0486 198 HIS D CD2   
8058 C CE1   . HIS D 226 ? 1.8089 0.8696 1.2710 0.0028  0.4734  -0.0455 198 HIS D CE1   
8059 N NE2   . HIS D 226 ? 1.8238 0.8845 1.2875 0.0017  0.4758  -0.0390 198 HIS D NE2   
8060 N N     . SER D 227 ? 1.7830 0.9416 1.2907 -0.0586 0.4322  -0.0937 199 SER D N     
8061 C CA    . SER D 227 ? 1.7913 0.9658 1.3068 -0.0755 0.4263  -0.1069 199 SER D CA    
8062 C C     . SER D 227 ? 1.8183 0.9988 1.3335 -0.0809 0.4200  -0.1198 199 SER D C     
8063 O O     . SER D 227 ? 1.8470 1.0374 1.3641 -0.0691 0.4137  -0.1173 199 SER D O     
8064 C CB    . SER D 227 ? 1.7732 0.9750 1.3021 -0.0720 0.4174  -0.1030 199 SER D CB    
8065 O OG    . SER D 227 ? 1.7723 0.9925 1.3099 -0.0867 0.4107  -0.1161 199 SER D OG    
8066 N N     . GLU D 228 ? 1.8325 1.0074 1.3451 -0.0990 0.4217  -0.1335 200 GLU D N     
8067 C CA    . GLU D 228 ? 1.8393 1.0215 1.3514 -0.1059 0.4148  -0.1470 200 GLU D CA    
8068 C C     . GLU D 228 ? 1.8140 1.0299 1.3402 -0.1080 0.4017  -0.1528 200 GLU D C     
8069 O O     . GLU D 228 ? 1.8294 1.0557 1.3560 -0.1099 0.3942  -0.1621 200 GLU D O     
8070 C CB    . GLU D 228 ? 1.8741 1.0397 1.3789 -0.1252 0.4203  -0.1599 200 GLU D CB    
8071 N N     . ASP D 229 ? 1.7804 1.0130 1.3174 -0.1074 0.3990  -0.1475 201 ASP D N     
8072 C CA    . ASP D 229 ? 1.7581 1.0231 1.3088 -0.1077 0.3867  -0.1518 201 ASP D CA    
8073 C C     . ASP D 229 ? 1.7001 0.9764 1.2588 -0.0974 0.3853  -0.1392 201 ASP D C     
8074 O O     . ASP D 229 ? 1.6778 0.9599 1.2421 -0.1056 0.3870  -0.1399 201 ASP D O     
8075 C CB    . ASP D 229 ? 1.7528 1.0295 1.3093 -0.1278 0.3838  -0.1668 201 ASP D CB    
8076 C CG    . ASP D 229 ? 1.7308 1.0417 1.3013 -0.1277 0.3711  -0.1717 201 ASP D CG    
8077 O OD1   . ASP D 229 ? 1.7039 1.0286 1.2778 -0.1134 0.3632  -0.1664 201 ASP D OD1   
8078 O OD2   . ASP D 229 ? 1.7461 1.0705 1.3244 -0.1420 0.3692  -0.1807 201 ASP D OD2   
8079 N N     . PRO D 230 ? 1.6688 0.9482 1.2280 -0.0792 0.3823  -0.1275 202 PRO D N     
8080 C CA    . PRO D 230 ? 1.5734 0.8626 1.1393 -0.0689 0.3806  -0.1151 202 PRO D CA    
8081 C C     . PRO D 230 ? 1.4886 0.8073 1.0680 -0.0728 0.3703  -0.1199 202 PRO D C     
8082 O O     . PRO D 230 ? 1.5350 0.8585 1.1187 -0.0725 0.3713  -0.1145 202 PRO D O     
8083 C CB    . PRO D 230 ? 1.6183 0.9067 1.1825 -0.0498 0.3783  -0.1036 202 PRO D CB    
8084 C CG    . PRO D 230 ? 1.6708 0.9396 1.2239 -0.0500 0.3837  -0.1076 202 PRO D CG    
8085 C CD    . PRO D 230 ? 1.7387 1.0099 1.2912 -0.0675 0.3820  -0.1243 202 PRO D CD    
8086 N N     . VAL D 231 ? 1.4122 0.7509 0.9978 -0.0758 0.3605  -0.1299 203 VAL D N     
8087 C CA    . VAL D 231 ? 1.4148 0.7830 1.0134 -0.0790 0.3505  -0.1349 203 VAL D CA    
8088 C C     . VAL D 231 ? 1.4632 0.8325 1.0647 -0.0962 0.3548  -0.1435 203 VAL D C     
8089 O O     . VAL D 231 ? 1.4616 0.8476 1.0719 -0.0973 0.3515  -0.1427 203 VAL D O     
8090 C CB    . VAL D 231 ? 1.4315 0.8200 1.0348 -0.0783 0.3396  -0.1438 203 VAL D CB    
8091 C CG1   . VAL D 231 ? 1.2731 0.6920 0.8894 -0.0838 0.3299  -0.1509 203 VAL D CG1   
8092 C CG2   . VAL D 231 ? 1.4668 0.8579 1.0694 -0.0604 0.3352  -0.1339 203 VAL D CG2   
8093 N N     . GLY D 232 ? 1.5263 0.8776 1.1203 -0.1099 0.3626  -0.1519 204 GLY D N     
8094 C CA    . GLY D 232 ? 1.5685 0.9199 1.1655 -0.1274 0.3677  -0.1602 204 GLY D CA    
8095 C C     . GLY D 232 ? 1.6166 0.9546 1.2112 -0.1261 0.3771  -0.1501 204 GLY D C     
8096 O O     . GLY D 232 ? 1.5929 0.9433 1.1949 -0.1327 0.3773  -0.1523 204 GLY D O     
8097 N N     . GLU D 233 ? 1.6063 0.9191 1.1899 -0.1171 0.3853  -0.1390 205 GLU D N     
8098 C CA    . GLU D 233 ? 1.5613 0.8596 1.1406 -0.1149 0.3945  -0.1286 205 GLU D CA    
8099 C C     . GLU D 233 ? 1.5313 0.8476 1.1181 -0.1030 0.3881  -0.1196 205 GLU D C     
8100 O O     . GLU D 233 ? 1.5171 0.8332 1.1050 -0.1064 0.3925  -0.1167 205 GLU D O     
8101 C CB    . GLU D 233 ? 1.5512 0.8205 1.1171 -0.1063 0.4038  -0.1184 205 GLU D CB    
8102 C CG    . GLU D 233 ? 1.6988 0.9453 1.2554 -0.1192 0.4130  -0.1260 205 GLU D CG    
8103 C CD    . GLU D 233 ? 1.7998 1.0177 1.3430 -0.1100 0.4231  -0.1151 205 GLU D CD    
8104 O OE1   . GLU D 233 ? 1.7819 0.9973 1.3234 -0.0962 0.4246  -0.1015 205 GLU D OE1   
8105 O OE2   . GLU D 233 ? 1.7785 0.9769 1.3128 -0.1165 0.4293  -0.1203 205 GLU D OE2   
8106 N N     . PHE D 234 ? 1.5222 0.8537 1.1136 -0.0889 0.3778  -0.1152 206 PHE D N     
8107 C CA    . PHE D 234 ? 1.4729 0.8212 1.0710 -0.0771 0.3708  -0.1065 206 PHE D CA    
8108 C C     . PHE D 234 ? 1.4593 0.8351 1.0694 -0.0850 0.3634  -0.1157 206 PHE D C     
8109 O O     . PHE D 234 ? 1.5170 0.9018 1.1307 -0.0813 0.3621  -0.1107 206 PHE D O     
8110 C CB    . PHE D 234 ? 1.4439 0.8004 1.0439 -0.0602 0.3623  -0.0987 206 PHE D CB    
8111 C CG    . PHE D 234 ? 1.4472 0.8133 1.0508 -0.0464 0.3573  -0.0866 206 PHE D CG    
8112 C CD1   . PHE D 234 ? 1.4014 0.7501 0.9973 -0.0411 0.3651  -0.0753 206 PHE D CD1   
8113 C CD2   . PHE D 234 ? 1.4305 0.8232 1.0447 -0.0387 0.3446  -0.0866 206 PHE D CD2   
8114 C CE1   . PHE D 234 ? 1.3676 0.7247 0.9658 -0.0286 0.3601  -0.0645 206 PHE D CE1   
8115 C CE2   . PHE D 234 ? 1.3242 0.7253 0.9413 -0.0265 0.3396  -0.0758 206 PHE D CE2   
8116 C CZ    . PHE D 234 ? 1.3173 0.7004 0.9261 -0.0215 0.3472  -0.0650 206 PHE D CZ    
8117 N N     . ARG D 235 ? 1.4499 0.8399 1.0660 -0.0953 0.3583  -0.1293 207 ARG D N     
8118 C CA    . ARG D 235 ? 1.4775 0.8949 1.1054 -0.1032 0.3517  -0.1387 207 ARG D CA    
8119 C C     . ARG D 235 ? 1.5436 0.9542 1.1711 -0.1171 0.3617  -0.1429 207 ARG D C     
8120 O O     . ARG D 235 ? 1.5288 0.9580 1.1639 -0.1184 0.3592  -0.1444 207 ARG D O     
8121 C CB    . ARG D 235 ? 1.4146 0.8479 1.0480 -0.1111 0.3442  -0.1521 207 ARG D CB    
8122 N N     . LEU D 236 ? 1.5385 0.9226 1.1567 -0.1275 0.3734  -0.1447 208 LEU D N     
8123 C CA    . LEU D 236 ? 1.5314 0.9065 1.1485 -0.1413 0.3842  -0.1481 208 LEU D CA    
8124 C C     . LEU D 236 ? 1.5415 0.9051 1.1529 -0.1318 0.3904  -0.1346 208 LEU D C     
8125 O O     . LEU D 236 ? 1.5197 0.8890 1.1340 -0.1379 0.3948  -0.1363 208 LEU D O     
8126 C CB    . LEU D 236 ? 1.5453 0.8954 1.1544 -0.1553 0.3945  -0.1534 208 LEU D CB    
8127 N N     . LEU D 237 ? 1.5347 0.8825 1.1374 -0.1166 0.3909  -0.1214 209 LEU D N     
8128 C CA    . LEU D 237 ? 1.4597 0.7954 1.0554 -0.1069 0.3963  -0.1080 209 LEU D CA    
8129 C C     . LEU D 237 ? 1.4247 0.7859 1.0286 -0.0988 0.3874  -0.1058 209 LEU D C     
8130 O O     . LEU D 237 ? 1.4574 0.8154 1.0579 -0.0985 0.3928  -0.1013 209 LEU D O     
8131 C CB    . LEU D 237 ? 1.4117 0.7289 0.9979 -0.0917 0.3973  -0.0946 209 LEU D CB    
8132 C CG    . LEU D 237 ? 1.3596 0.6651 0.9379 -0.0796 0.4013  -0.0796 209 LEU D CG    
8133 C CD1   . LEU D 237 ? 1.3854 0.6704 0.9555 -0.0900 0.4148  -0.0782 209 LEU D CD1   
8134 C CD2   . LEU D 237 ? 1.3413 0.6342 0.9126 -0.0638 0.4006  -0.0674 209 LEU D CD2   
8135 N N     . LEU D 238 ? 1.3733 0.7603 0.9872 -0.0920 0.3739  -0.1087 210 LEU D N     
8136 C CA    . LEU D 238 ? 1.4259 0.8396 1.0483 -0.0841 0.3642  -0.1066 210 LEU D CA    
8137 C C     . LEU D 238 ? 1.4736 0.9061 1.1038 -0.0971 0.3660  -0.1174 210 LEU D C     
8138 O O     . LEU D 238 ? 1.4991 0.9433 1.1322 -0.0945 0.3652  -0.1118 210 LEU D O     
8139 C CB    . LEU D 238 ? 1.3875 0.8231 1.0188 -0.0741 0.3496  -0.1068 210 LEU D CB    
8140 C CG    . LEU D 238 ? 1.3279 0.7510 0.9534 -0.0587 0.3468  -0.0947 210 LEU D CG    
8141 C CD1   . LEU D 238 ? 1.2308 0.6771 0.8658 -0.0504 0.3330  -0.0961 210 LEU D CD1   
8142 C CD2   . LEU D 238 ? 1.3500 0.7634 0.9687 -0.0473 0.3491  -0.0810 210 LEU D CD2   
8143 N N     . GLU D 239 ? 1.4503 0.8903 1.0867 -0.1112 0.3663  -0.1311 211 GLU D N     
8144 C CA    . GLU D 239 ? 1.4122 0.8771 1.0613 -0.1243 0.3654  -0.1394 211 GLU D CA    
8145 C C     . GLU D 239 ? 1.4754 0.9277 1.1213 -0.1335 0.3774  -0.1349 211 GLU D C     
8146 O O     . GLU D 239 ? 1.4353 0.9097 1.0910 -0.1379 0.3764  -0.1350 211 GLU D O     
8147 C CB    . GLU D 239 ? 1.3055 0.7793 0.9613 -0.1381 0.3632  -0.1547 211 GLU D CB    
8148 N N     . SER D 240 ? 1.5191 0.9359 1.1512 -0.1362 0.3891  -0.1307 212 SER D N     
8149 C CA    . SER D 240 ? 1.5183 0.9201 1.1455 -0.1442 0.4012  -0.1248 212 SER D CA    
8150 C C     . SER D 240 ? 1.5123 0.9168 1.1354 -0.1313 0.4006  -0.1108 212 SER D C     
8151 O O     . SER D 240 ? 1.5524 0.9462 1.1708 -0.1365 0.4103  -0.1048 212 SER D O     
8152 C CB    . SER D 240 ? 1.4813 0.8420 1.0935 -0.1493 0.4136  -0.1233 212 SER D CB    
8153 O OG    . SER D 240 ? 1.4469 0.7852 1.0460 -0.1325 0.4142  -0.1120 212 SER D OG    
8154 N N     . GLU D 241 ? 1.4838 0.9015 1.1080 -0.1151 0.3895  -0.1055 213 GLU D N     
8155 C CA    . GLU D 241 ? 1.4819 0.9046 1.1024 -0.1028 0.3869  -0.0931 213 GLU D CA    
8156 C C     . GLU D 241 ? 1.4717 0.9314 1.1054 -0.0984 0.3746  -0.0962 213 GLU D C     
8157 O O     . GLU D 241 ? 1.4831 0.9493 1.1141 -0.0853 0.3683  -0.0873 213 GLU D O     
8158 C CB    . GLU D 241 ? 1.4475 0.8494 1.0558 -0.0863 0.3850  -0.0816 213 GLU D CB    
8159 C CG    . GLU D 241 ? 1.4434 0.8068 1.0369 -0.0880 0.3979  -0.0757 213 GLU D CG    
8160 C CD    . GLU D 241 ? 1.5232 0.8738 1.1097 -0.0949 0.4092  -0.0692 213 GLU D CD    
8161 O OE1   . GLU D 241 ? 1.5238 0.8875 1.1103 -0.0893 0.4061  -0.0620 213 GLU D OE1   
8162 O OE2   . GLU D 241 ? 1.5838 0.9104 1.1641 -0.1061 0.4213  -0.0713 213 GLU D OE2   
8163 N N     . GLY D 242 ? 1.4530 0.9365 1.1008 -0.1090 0.3709  -0.1087 214 GLY D N     
8164 C CA    . GLY D 242 ? 1.4629 0.9813 1.1239 -0.1052 0.3601  -0.1120 214 GLY D CA    
8165 C C     . GLY D 242 ? 1.4816 1.0140 1.1472 -0.0937 0.3465  -0.1137 214 GLY D C     
8166 O O     . GLY D 242 ? 1.4719 1.0276 1.1445 -0.0858 0.3370  -0.1123 214 GLY D O     
8167 N N     . PHE D 243 ? 1.4887 1.0072 1.1502 -0.0924 0.3455  -0.1165 215 PHE D N     
8168 C CA    . PHE D 243 ? 1.4894 1.0201 1.1547 -0.0817 0.3334  -0.1176 215 PHE D CA    
8169 C C     . PHE D 243 ? 1.4145 0.9633 1.0906 -0.0910 0.3285  -0.1314 215 PHE D C     
8170 O O     . PHE D 243 ? 1.3851 0.9289 1.0627 -0.1056 0.3353  -0.1401 215 PHE D O     
8171 C CB    . PHE D 243 ? 1.5009 1.0054 1.1542 -0.0715 0.3349  -0.1098 215 PHE D CB    
8172 C CG    . PHE D 243 ? 1.5170 1.0123 1.1624 -0.0575 0.3337  -0.0955 215 PHE D CG    
8173 C CD1   . PHE D 243 ? 1.4602 0.9736 1.1112 -0.0446 0.3207  -0.0899 215 PHE D CD1   
8174 C CD2   . PHE D 243 ? 1.5038 0.9731 1.1369 -0.0575 0.3445  -0.0869 215 PHE D CD2   
8175 C CE1   . PHE D 243 ? 1.4314 0.9361 1.0744 -0.0324 0.3193  -0.0774 215 PHE D CE1   
8176 C CE2   . PHE D 243 ? 1.4870 0.9489 1.1126 -0.0446 0.3424  -0.0734 215 PHE D CE2   
8177 C CZ    . PHE D 243 ? 1.4410 0.9207 1.0715 -0.0323 0.3297  -0.0690 215 PHE D CZ    
8178 N N     . GLN D 244 ? 1.4171 0.9871 1.1006 -0.0825 0.3161  -0.1332 216 GLN D N     
8179 C CA    . GLN D 244 ? 1.4687 1.0570 1.1614 -0.0885 0.3093  -0.1450 216 GLN D CA    
8180 C C     . GLN D 244 ? 1.3881 0.9685 1.0775 -0.0794 0.3022  -0.1410 216 GLN D C     
8181 O O     . GLN D 244 ? 1.3751 0.9666 1.0678 -0.0662 0.2920  -0.1343 216 GLN D O     
8182 C CB    . GLN D 244 ? 1.4995 1.1231 1.2068 -0.0860 0.2985  -0.1482 216 GLN D CB    
8183 C CG    . GLN D 244 ? 1.5020 1.1465 1.2190 -0.0913 0.2905  -0.1596 216 GLN D CG    
8184 C CD    . GLN D 244 ? 1.5069 1.1846 1.2375 -0.0854 0.2787  -0.1607 216 GLN D CD    
8185 O OE1   . GLN D 244 ? 1.5018 1.1843 1.2325 -0.0742 0.2747  -0.1522 216 GLN D OE1   
8186 N NE2   . GLN D 244 ? 1.5716 1.2719 1.3132 -0.0928 0.2729  -0.1712 216 GLN D NE2   
8187 N N     . VAL D 245 ? 1.3858 0.9468 1.0686 -0.0865 0.3081  -0.1452 217 VAL D N     
8188 C CA    . VAL D 245 ? 1.4062 0.9584 1.0849 -0.0783 0.3033  -0.1415 217 VAL D CA    
8189 C C     . VAL D 245 ? 1.3930 0.9714 1.0811 -0.0765 0.2910  -0.1486 217 VAL D C     
8190 O O     . VAL D 245 ? 1.4285 1.0145 1.1195 -0.0879 0.2906  -0.1608 217 VAL D O     
8191 C CB    . VAL D 245 ? 1.3888 0.9135 1.0574 -0.0870 0.3132  -0.1447 217 VAL D CB    
8192 C CG1   . VAL D 245 ? 1.4046 0.9222 1.0690 -0.0779 0.3085  -0.1411 217 VAL D CG1   
8193 C CG2   . VAL D 245 ? 1.3558 0.8532 1.0142 -0.0879 0.3258  -0.1368 217 VAL D CG2   
8194 N N     . LEU D 246 ? 1.4020 0.9939 1.0943 -0.0625 0.2810  -0.1411 218 LEU D N     
8195 C CA    . LEU D 246 ? 1.3744 0.9908 1.0749 -0.0595 0.2694  -0.1466 218 LEU D CA    
8196 C C     . LEU D 246 ? 1.3549 0.9635 1.0505 -0.0567 0.2671  -0.1478 218 LEU D C     
8197 O O     . LEU D 246 ? 1.4941 1.1196 1.1940 -0.0586 0.2598  -0.1557 218 LEU D O     
8198 C CB    . LEU D 246 ? 1.3697 1.0027 1.0763 -0.0460 0.2600  -0.1381 218 LEU D CB    
8199 C CG    . LEU D 246 ? 1.3616 1.0052 1.0730 -0.0464 0.2606  -0.1364 218 LEU D CG    
8200 C CD1   . LEU D 246 ? 1.2775 0.9350 0.9934 -0.0326 0.2505  -0.1281 218 LEU D CD1   
8201 C CD2   . LEU D 246 ? 1.3812 1.0438 1.1007 -0.0588 0.2613  -0.1491 218 LEU D CD2   
8202 N N     . ARG D 247 ? 1.3293 0.9128 1.0153 -0.0520 0.2734  -0.1401 219 ARG D N     
8203 C CA    . ARG D 247 ? 1.3644 0.9399 1.0451 -0.0475 0.2719  -0.1399 219 ARG D CA    
8204 C C     . ARG D 247 ? 1.3088 0.8536 0.9785 -0.0449 0.2821  -0.1320 219 ARG D C     
8205 O O     . ARG D 247 ? 1.3098 0.8447 0.9774 -0.0381 0.2858  -0.1213 219 ARG D O     
8206 C CB    . ARG D 247 ? 1.3340 0.9256 1.0197 -0.0334 0.2615  -0.1335 219 ARG D CB    
8207 C CG    . ARG D 247 ? 1.3284 0.9164 1.0095 -0.0287 0.2592  -0.1344 219 ARG D CG    
8208 C CD    . ARG D 247 ? 1.3391 0.9465 1.0266 -0.0165 0.2489  -0.1292 219 ARG D CD    
8209 N NE    . ARG D 247 ? 1.4686 1.0722 1.1513 -0.0101 0.2476  -0.1282 219 ARG D NE    
8210 C CZ    . ARG D 247 ? 1.5149 1.1367 1.2014 -0.0049 0.2391  -0.1301 219 ARG D CZ    
8211 N NH1   . ARG D 247 ? 1.5114 1.1564 1.2065 -0.0049 0.2308  -0.1330 219 ARG D NH1   
8212 N NH2   . ARG D 247 ? 1.5213 1.1375 1.2021 0.0009  0.2394  -0.1288 219 ARG D NH2   
8213 N N     . CYS D 248 ? 1.2768 0.8067 0.9389 -0.0502 0.2868  -0.1374 220 CYS D N     
8214 C CA    . CYS D 248 ? 1.3281 0.8280 0.9791 -0.0483 0.2973  -0.1308 220 CYS D CA    
8215 C C     . CYS D 248 ? 1.4021 0.8928 1.0461 -0.0477 0.2978  -0.1350 220 CYS D C     
8216 O O     . CYS D 248 ? 1.4265 0.9195 1.0689 -0.0593 0.2973  -0.1475 220 CYS D O     
8217 C CB    . CYS D 248 ? 1.3246 0.8072 0.9707 -0.0614 0.3081  -0.1346 220 CYS D CB    
8218 S SG    . CYS D 248 ? 1.4959 0.9417 1.1286 -0.0570 0.3215  -0.1234 220 CYS D SG    
8219 N N     . ASP D 249 ? 1.3866 0.8672 1.0263 -0.0345 0.2988  -0.1248 221 ASP D N     
8220 C CA    . ASP D 249 ? 1.3597 0.8316 0.9922 -0.0318 0.2997  -0.1276 221 ASP D CA    
8221 C C     . ASP D 249 ? 1.3164 0.7625 0.9397 -0.0228 0.3090  -0.1165 221 ASP D C     
8222 O O     . ASP D 249 ? 1.3187 0.7583 0.9428 -0.0157 0.3123  -0.1051 221 ASP D O     
8223 C CB    . ASP D 249 ? 1.4032 0.8975 1.0417 -0.0226 0.2890  -0.1275 221 ASP D CB    
8224 C CG    . ASP D 249 ? 1.4491 0.9709 1.0973 -0.0290 0.2793  -0.1364 221 ASP D CG    
8225 O OD1   . ASP D 249 ? 1.4511 0.9762 1.0978 -0.0417 0.2787  -0.1493 221 ASP D OD1   
8226 O OD2   . ASP D 249 ? 1.4290 0.9691 1.0862 -0.0213 0.2722  -0.1306 221 ASP D OD2   
8227 N N     . LEU D 250 ? 1.3244 0.7558 0.9384 -0.0230 0.3132  -0.1201 222 LEU D N     
8228 C CA    . LEU D 250 ? 1.3395 0.7470 0.9443 -0.0139 0.3222  -0.1104 222 LEU D CA    
8229 C C     . LEU D 250 ? 1.3736 0.7847 0.9761 -0.0039 0.3191  -0.1095 222 LEU D C     
8230 O O     . LEU D 250 ? 1.3901 0.8102 0.9914 -0.0093 0.3142  -0.1205 222 LEU D O     
8231 C CB    . LEU D 250 ? 1.2946 0.6749 0.8878 -0.0246 0.3333  -0.1156 222 LEU D CB    
8232 C CG    . LEU D 250 ? 1.3815 0.7350 0.9634 -0.0162 0.3436  -0.1072 222 LEU D CG    
8233 C CD1   . LEU D 250 ? 1.4247 0.7725 1.0085 -0.0047 0.3475  -0.0914 222 LEU D CD1   
8234 C CD2   . LEU D 250 ? 1.3891 0.7178 0.9595 -0.0289 0.3534  -0.1152 222 LEU D CD2   
8235 N N     . GLY D 251 ? 1.3917 0.7961 0.9933 0.0107  0.3222  -0.0964 223 GLY D N     
8236 C CA    . GLY D 251 ? 1.3832 0.7904 0.9828 0.0213  0.3206  -0.0939 223 GLY D CA    
8237 C C     . GLY D 251 ? 1.4231 0.8148 1.0189 0.0352  0.3283  -0.0797 223 GLY D C     
8238 O O     . GLY D 251 ? 1.4626 0.8479 1.0601 0.0394  0.3319  -0.0694 223 GLY D O     
8239 N N     . PRO D 252 ? 1.3516 0.7373 0.9415 0.0428  0.3310  -0.0788 224 PRO D N     
8240 C CA    . PRO D 252 ? 1.3174 0.6901 0.9043 0.0570  0.3385  -0.0650 224 PRO D CA    
8241 C C     . PRO D 252 ? 1.2957 0.6881 0.8941 0.0704  0.3324  -0.0531 224 PRO D C     
8242 O O     . PRO D 252 ? 1.2837 0.6987 0.8904 0.0706  0.3228  -0.0564 224 PRO D O     
8243 C CB    . PRO D 252 ? 1.2722 0.6318 0.8481 0.0587  0.3437  -0.0705 224 PRO D CB    
8244 C CG    . PRO D 252 ? 1.3264 0.7041 0.9045 0.0516  0.3345  -0.0833 224 PRO D CG    
8245 C CD    . PRO D 252 ? 1.2737 0.6630 0.8583 0.0386  0.3281  -0.0906 224 PRO D CD    
8246 N N     . GLN D 253 ? 1.2683 0.6521 0.8672 0.0819  0.3382  -0.0389 225 GLN D N     
8247 C CA    . GLN D 253 ? 1.2325 0.6331 0.8422 0.0950  0.3334  -0.0261 225 GLN D CA    
8248 C C     . GLN D 253 ? 1.2380 0.6275 0.8445 0.1091  0.3417  -0.0140 225 GLN D C     
8249 O O     . GLN D 253 ? 1.2281 0.5958 0.8256 0.1098  0.3515  -0.0111 225 GLN D O     
8250 C CB    . GLN D 253 ? 1.2423 0.6499 0.8594 0.0946  0.3297  -0.0195 225 GLN D CB    
8251 C CG    . GLN D 253 ? 1.2923 0.7139 0.9143 0.0823  0.3211  -0.0300 225 GLN D CG    
8252 C CD    . GLN D 253 ? 1.3301 0.7777 0.9620 0.0847  0.3101  -0.0326 225 GLN D CD    
8253 O OE1   . GLN D 253 ? 1.3265 0.7837 0.9640 0.0968  0.3081  -0.0233 225 GLN D OE1   
8254 N NE2   . GLN D 253 ? 1.3329 0.7925 0.9671 0.0733  0.3034  -0.0450 225 GLN D NE2   
8255 N N     . LYS D 254 ? 1.1818 0.5870 0.7960 0.1205  0.3381  -0.0066 226 LYS D N     
8256 C CA    . LYS D 254 ? 1.1355 0.5358 0.7501 0.1352  0.3450  0.0067  226 LYS D CA    
8257 C C     . LYS D 254 ? 1.0152 0.4311 0.6424 0.1452  0.3407  0.0210  226 LYS D C     
8258 O O     . LYS D 254 ? 0.9911 0.4263 0.6279 0.1434  0.3308  0.0204  226 LYS D O     
8259 C CB    . LYS D 254 ? 1.1688 0.5747 0.7823 0.1414  0.3455  0.0049  226 LYS D CB    
8260 C CG    . LYS D 254 ? 1.1155 0.5040 0.7149 0.1341  0.3510  -0.0079 226 LYS D CG    
8261 C CD    . LYS D 254 ? 1.1131 0.5072 0.7110 0.1422  0.3521  -0.0079 226 LYS D CD    
8262 C CE    . LYS D 254 ? 1.1925 0.5693 0.7753 0.1352  0.3571  -0.0213 226 LYS D CE    
8263 N NZ    . LYS D 254 ? 1.0326 0.4141 0.6126 0.1439  0.3588  -0.0211 226 LYS D NZ    
8264 N N     . VAL D 255 ? 0.9961 0.4038 0.6232 0.1557  0.3479  0.0338  227 VAL D N     
8265 C CA    . VAL D 255 ? 0.9861 0.4087 0.6252 0.1660  0.3443  0.0482  227 VAL D CA    
8266 C C     . VAL D 255 ? 0.9817 0.4106 0.6259 0.1805  0.3486  0.0592  227 VAL D C     
8267 O O     . VAL D 255 ? 1.0039 0.4185 0.6423 0.1870  0.3584  0.0648  227 VAL D O     
8268 C CB    . VAL D 255 ? 0.9576 0.3691 0.5940 0.1659  0.3481  0.0542  227 VAL D CB    
8269 C CG1   . VAL D 255 ? 0.9209 0.3508 0.5706 0.1757  0.3422  0.0678  227 VAL D CG1   
8270 C CG2   . VAL D 255 ? 0.9768 0.3795 0.6066 0.1509  0.3458  0.0427  227 VAL D CG2   
8271 N N     . PHE D 256 ? 0.9187 0.3692 0.5739 0.1857  0.3416  0.0626  228 PHE D N     
8272 C CA    . PHE D 256 ? 0.9173 0.3761 0.5784 0.1988  0.3455  0.0727  228 PHE D CA    
8273 C C     . PHE D 256 ? 0.9117 0.3804 0.5842 0.2104  0.3464  0.0891  228 PHE D C     
8274 O O     . PHE D 256 ? 0.9462 0.4247 0.6265 0.2092  0.3395  0.0932  228 PHE D O     
8275 C CB    . PHE D 256 ? 0.9504 0.4298 0.6197 0.1998  0.3378  0.0707  228 PHE D CB    
8276 C CG    . PHE D 256 ? 0.9484 0.4404 0.6266 0.2134  0.3410  0.0827  228 PHE D CG    
8277 C CD1   . PHE D 256 ? 0.9797 0.4613 0.6497 0.2180  0.3497  0.0813  228 PHE D CD1   
8278 C CD2   . PHE D 256 ? 0.9568 0.4717 0.6519 0.2215  0.3352  0.0955  228 PHE D CD2   
8279 C CE1   . PHE D 256 ? 0.9954 0.4892 0.6738 0.2306  0.3532  0.0928  228 PHE D CE1   
8280 C CE2   . PHE D 256 ? 0.9336 0.4620 0.6384 0.2334  0.3383  0.1069  228 PHE D CE2   
8281 C CZ    . PHE D 256 ? 0.9536 0.4715 0.6500 0.2381  0.3476  0.1058  228 PHE D CZ    
8282 N N     . PHE D 257 ? 0.9268 0.3937 0.6005 0.2216  0.3547  0.0982  229 PHE D N     
8283 C CA    . PHE D 257 ? 0.9214 0.4023 0.6086 0.2336  0.3553  0.1139  229 PHE D CA    
8284 C C     . PHE D 257 ? 0.9229 0.4156 0.6174 0.2448  0.3593  0.1219  229 PHE D C     
8285 O O     . PHE D 257 ? 0.9607 0.4382 0.6439 0.2464  0.3682  0.1178  229 PHE D O     
8286 C CB    . PHE D 257 ? 0.9443 0.4081 0.6250 0.2365  0.3635  0.1181  229 PHE D CB    
8287 C CG    . PHE D 257 ? 0.9435 0.3967 0.6179 0.2265  0.3601  0.1121  229 PHE D CG    
8288 C CD1   . PHE D 257 ? 0.9607 0.3904 0.6184 0.2151  0.3644  0.0991  229 PHE D CD1   
8289 C CD2   . PHE D 257 ? 0.9260 0.3936 0.6118 0.2282  0.3521  0.1194  229 PHE D CD2   
8290 C CE1   . PHE D 257 ? 0.9606 0.3812 0.6129 0.2058  0.3620  0.0941  229 PHE D CE1   
8291 C CE2   . PHE D 257 ? 0.9264 0.3840 0.6057 0.2193  0.3494  0.1142  229 PHE D CE2   
8292 C CZ    . PHE D 257 ? 0.9437 0.3778 0.6061 0.2082  0.3549  0.1018  229 PHE D CZ    
8293 N N     . PRO D 258 ? 0.9005 0.4199 0.6137 0.2522  0.3529  0.1330  230 PRO D N     
8294 C CA    . PRO D 258 ? 0.9185 0.4507 0.6394 0.2621  0.3568  0.1407  230 PRO D CA    
8295 C C     . PRO D 258 ? 0.9560 0.4818 0.6769 0.2732  0.3682  0.1503  230 PRO D C     
8296 O O     . PRO D 258 ? 1.0430 0.5624 0.7579 0.2786  0.3765  0.1505  230 PRO D O     
8297 C CB    . PRO D 258 ? 0.8976 0.4613 0.6402 0.2651  0.3456  0.1498  230 PRO D CB    
8298 C CG    . PRO D 258 ? 0.8677 0.4344 0.6160 0.2613  0.3382  0.1515  230 PRO D CG    
8299 C CD    . PRO D 258 ? 0.9070 0.4466 0.6354 0.2511  0.3412  0.1386  230 PRO D CD    
8300 N N     . THR D 259 ? 0.9274 0.4548 0.6546 0.2771  0.3685  0.1580  231 THR D N     
8301 C CA    . THR D 259 ? 0.9734 0.4971 0.7027 0.2885  0.3786  0.1680  231 THR D CA    
8302 C C     . THR D 259 ? 1.0522 0.5447 0.7625 0.2857  0.3879  0.1617  231 THR D C     
8303 O O     . THR D 259 ? 1.0094 0.4863 0.7079 0.2748  0.3854  0.1512  231 THR D O     
8304 C CB    . THR D 259 ? 0.9326 0.4816 0.6843 0.2958  0.3721  0.1819  231 THR D CB    
8305 O OG1   . THR D 259 ? 0.9692 0.5123 0.7194 0.2902  0.3663  0.1798  231 THR D OG1   
8306 C CG2   . THR D 259 ? 0.9009 0.4807 0.6721 0.2958  0.3608  0.1869  231 THR D CG2   
8307 N N     . ALA D 260 ? 1.0971 0.5809 0.8049 0.2959  0.3991  0.1687  232 ALA D N     
8308 C CA    . ALA D 260 ? 1.0348 0.4892 0.7256 0.2947  0.4087  0.1643  232 ALA D CA    
8309 C C     . ALA D 260 ? 1.0630 0.5188 0.7590 0.2936  0.4043  0.1684  232 ALA D C     
8310 O O     . ALA D 260 ? 1.0884 0.5208 0.7696 0.2868  0.4079  0.1610  232 ALA D O     
8311 C CB    . ALA D 260 ? 1.0636 0.5086 0.7508 0.3069  0.4219  0.1712  232 ALA D CB    
8312 N N     . GLU D 261 ? 1.0754 0.5584 0.7926 0.2998  0.3961  0.1799  233 GLU D N     
8313 C CA    . GLU D 261 ? 1.0815 0.5672 0.8045 0.2991  0.3903  0.1841  233 GLU D CA    
8314 C C     . GLU D 261 ? 1.0791 0.5610 0.7963 0.2856  0.3808  0.1740  233 GLU D C     
8315 O O     . GLU D 261 ? 1.1090 0.5724 0.8148 0.2803  0.3827  0.1695  233 GLU D O     
8316 C CB    . GLU D 261 ? 1.0650 0.5822 0.8131 0.3080  0.3817  0.1985  233 GLU D CB    
8317 C CG    . GLU D 261 ? 1.1456 0.6656 0.8996 0.3076  0.3746  0.2033  233 GLU D CG    
8318 C CD    . GLU D 261 ? 1.2384 0.7881 1.0171 0.3161  0.3658  0.2179  233 GLU D CD    
8319 O OE1   . GLU D 261 ? 1.2483 0.8159 1.0399 0.3233  0.3672  0.2249  233 GLU D OE1   
8320 O OE2   . GLU D 261 ? 1.2773 0.8324 1.0623 0.3151  0.3571  0.2224  233 GLU D OE2   
8321 N N     . THR D 262 ? 1.0429 0.5423 0.7679 0.2802  0.3708  0.1708  234 THR D N     
8322 C CA    . THR D 262 ? 0.9892 0.4880 0.7108 0.2682  0.3610  0.1623  234 THR D CA    
8323 C C     . THR D 262 ? 0.9638 0.4323 0.6627 0.2578  0.3681  0.1488  234 THR D C     
8324 O O     . THR D 262 ? 0.9871 0.4489 0.6805 0.2487  0.3632  0.1429  234 THR D O     
8325 C CB    . THR D 262 ? 0.9154 0.4351 0.6471 0.2646  0.3509  0.1601  234 THR D CB    
8326 O OG1   . THR D 262 ? 0.9539 0.4705 0.6806 0.2669  0.3581  0.1572  234 THR D OG1   
8327 C CG2   . THR D 262 ? 0.8921 0.4430 0.6479 0.2711  0.3399  0.1726  234 THR D CG2   
8328 N N     . HIS D 263 ? 0.9870 0.4370 0.6728 0.2585  0.3793  0.1439  235 HIS D N     
8329 C CA    . HIS D 263 ? 1.0090 0.4296 0.6741 0.2482  0.3861  0.1314  235 HIS D CA    
8330 C C     . HIS D 263 ? 1.0419 0.4445 0.6994 0.2495  0.3927  0.1341  235 HIS D C     
8331 O O     . HIS D 263 ? 1.1267 0.5074 0.7693 0.2392  0.3961  0.1245  235 HIS D O     
8332 C CB    . HIS D 263 ? 1.0288 0.4352 0.6827 0.2488  0.3950  0.1255  235 HIS D CB    
8333 C CG    . HIS D 263 ? 1.0543 0.4307 0.6880 0.2382  0.4018  0.1126  235 HIS D CG    
8334 N ND1   . HIS D 263 ? 1.0460 0.4166 0.6729 0.2235  0.3961  0.0999  235 HIS D ND1   
8335 C CD2   . HIS D 263 ? 1.0886 0.4396 0.7082 0.2398  0.4137  0.1103  235 HIS D CD2   
8336 C CE1   . HIS D 263 ? 1.0736 0.4174 0.6838 0.2160  0.4039  0.0903  235 HIS D CE1   
8337 N NE2   . HIS D 263 ? 1.1001 0.4309 0.7051 0.2257  0.4147  0.0963  235 HIS D NE2   
8338 N N     . ARG D 264 ? 1.0643 0.4762 0.7324 0.2615  0.3941  0.1470  236 ARG D N     
8339 C CA    . ARG D 264 ? 1.0862 0.4815 0.7477 0.2644  0.4006  0.1508  236 ARG D CA    
8340 C C     . ARG D 264 ? 1.0594 0.4669 0.7304 0.2632  0.3905  0.1559  236 ARG D C     
8341 O O     . ARG D 264 ? 1.0979 0.4887 0.7580 0.2558  0.3917  0.1509  236 ARG D O     
8342 C CB    . ARG D 264 ? 1.1585 0.5536 0.8244 0.2791  0.4097  0.1617  236 ARG D CB    
8343 C CG    . ARG D 264 ? 1.1826 0.5738 0.8513 0.2861  0.4117  0.1708  236 ARG D CG    
8344 C CD    . ARG D 264 ? 1.1636 0.5399 0.8266 0.2972  0.4254  0.1765  236 ARG D CD    
8345 N NE    . ARG D 264 ? 1.2694 0.6619 0.9430 0.3071  0.4276  0.1831  236 ARG D NE    
8346 C CZ    . ARG D 264 ? 1.1913 0.6145 0.8867 0.3151  0.4195  0.1942  236 ARG D CZ    
8347 N NH1   . ARG D 264 ? 1.1194 0.5608 0.8288 0.3149  0.4079  0.2003  236 ARG D NH1   
8348 N NH2   . ARG D 264 ? 1.1159 0.5517 0.8193 0.3232  0.4230  0.1993  236 ARG D NH2   
8349 N N     . GLU D 265 ? 1.0344 0.4707 0.7255 0.2700  0.3801  0.1659  237 GLU D N     
8350 C CA    . GLU D 265 ? 1.0355 0.4840 0.7358 0.2689  0.3689  0.1713  237 GLU D CA    
8351 C C     . GLU D 265 ? 1.0539 0.4971 0.7463 0.2552  0.3621  0.1607  237 GLU D C     
8352 O O     . GLU D 265 ? 1.0874 0.5288 0.7788 0.2519  0.3568  0.1620  237 GLU D O     
8353 C CB    . GLU D 265 ? 1.0123 0.4938 0.7362 0.2764  0.3573  0.1826  237 GLU D CB    
8354 C CG    . GLU D 265 ? 1.1303 0.6210 0.8646 0.2898  0.3637  0.1931  237 GLU D CG    
8355 C CD    . GLU D 265 ? 1.1650 0.6543 0.9039 0.2988  0.3656  0.2041  237 GLU D CD    
8356 O OE1   . GLU D 265 ? 1.1566 0.6545 0.9022 0.2969  0.3549  0.2085  237 GLU D OE1   
8357 O OE2   . GLU D 265 ? 1.1202 0.5994 0.8558 0.3079  0.3777  0.2086  237 GLU D OE2   
8358 N N     . PHE D 266 ? 0.9822 0.4232 0.6687 0.2472  0.3621  0.1504  238 PHE D N     
8359 C CA    . PHE D 266 ? 0.9751 0.4070 0.6515 0.2335  0.3583  0.1391  238 PHE D CA    
8360 C C     . PHE D 266 ? 1.0037 0.4057 0.6614 0.2271  0.3688  0.1324  238 PHE D C     
8361 O O     . PHE D 266 ? 1.0458 0.4414 0.6987 0.2208  0.3659  0.1304  238 PHE D O     
8362 C CB    . PHE D 266 ? 0.9613 0.3971 0.6360 0.2268  0.3564  0.1297  238 PHE D CB    
8363 C CG    . PHE D 266 ? 0.9514 0.3814 0.6183 0.2130  0.3513  0.1186  238 PHE D CG    
8364 C CD1   . PHE D 266 ? 0.9272 0.3738 0.6032 0.2102  0.3389  0.1204  238 PHE D CD1   
8365 C CD2   . PHE D 266 ? 0.9676 0.3756 0.6184 0.2024  0.3586  0.1062  238 PHE D CD2   
8366 C CE1   . PHE D 266 ? 0.9192 0.3604 0.5880 0.1980  0.3350  0.1103  238 PHE D CE1   
8367 C CE2   . PHE D 266 ? 0.9588 0.3628 0.6039 0.1894  0.3541  0.0960  238 PHE D CE2   
8368 C CZ    . PHE D 266 ? 0.9347 0.3551 0.5885 0.1876  0.3428  0.0981  238 PHE D CZ    
8369 N N     . LEU D 267 ? 1.0288 0.4118 0.6755 0.2284  0.3810  0.1289  239 LEU D N     
8370 C CA    . LEU D 267 ? 1.0585 0.4122 0.6876 0.2220  0.3914  0.1226  239 LEU D CA    
8371 C C     . LEU D 267 ? 1.0853 0.4335 0.7147 0.2278  0.3932  0.1313  239 LEU D C     
8372 O O     . LEU D 267 ? 1.1229 0.4501 0.7394 0.2207  0.3987  0.1264  239 LEU D O     
8373 C CB    . LEU D 267 ? 1.0846 0.4200 0.7031 0.2242  0.4035  0.1189  239 LEU D CB    
8374 C CG    . LEU D 267 ? 1.0809 0.4117 0.6925 0.2142  0.4033  0.1064  239 LEU D CG    
8375 C CD1   . LEU D 267 ? 1.1067 0.4221 0.7096 0.2187  0.4139  0.1045  239 LEU D CD1   
8376 C CD2   . LEU D 267 ? 1.0845 0.4003 0.6846 0.1979  0.4027  0.0939  239 LEU D CD2   
8377 N N     . LYS D 268 ? 1.0877 0.4547 0.7320 0.2403  0.3883  0.1442  240 LYS D N     
8378 C CA    . LYS D 268 ? 1.0728 0.4382 0.7194 0.2453  0.3870  0.1529  240 LYS D CA    
8379 C C     . LYS D 268 ? 1.0854 0.4536 0.7307 0.2358  0.3777  0.1496  240 LYS D C     
8380 O O     . LYS D 268 ? 1.1805 0.5339 0.8173 0.2335  0.3806  0.1504  240 LYS D O     
8381 C CB    . LYS D 268 ? 1.0627 0.4520 0.7282 0.2592  0.3809  0.1673  240 LYS D CB    
8382 C CG    . LYS D 268 ? 1.1355 0.5165 0.8006 0.2712  0.3923  0.1743  240 LYS D CG    
8383 C CD    . LYS D 268 ? 1.1979 0.6038 0.8830 0.2841  0.3852  0.1892  240 LYS D CD    
8384 C CE    . LYS D 268 ? 1.2458 0.6435 0.9306 0.2967  0.3972  0.1968  240 LYS D CE    
8385 N NZ    . LYS D 268 ? 1.2899 0.7135 0.9957 0.3088  0.3902  0.2115  240 LYS D NZ    
8386 N N     . SER D 269 ? 1.0401 0.4266 0.6932 0.2302  0.3668  0.1460  241 SER D N     
8387 C CA    . SER D 269 ? 1.0143 0.4059 0.6672 0.2222  0.3570  0.1439  241 SER D CA    
8388 C C     . SER D 269 ? 1.0262 0.3951 0.6618 0.2086  0.3635  0.1314  241 SER D C     
8389 O O     . SER D 269 ? 1.1517 0.5123 0.7810 0.2039  0.3625  0.1313  241 SER D O     
8390 C CB    . SER D 269 ? 0.9803 0.3983 0.6472 0.2210  0.3433  0.1442  241 SER D CB    
8391 O OG    . SER D 269 ? 0.9718 0.3864 0.6330 0.2121  0.3451  0.1326  241 SER D OG    
8392 N N     . VAL D 270 ? 1.0300 0.3890 0.6579 0.2017  0.3699  0.1210  242 VAL D N     
8393 C CA    . VAL D 270 ? 1.0446 0.3849 0.6582 0.1872  0.3748  0.1085  242 VAL D CA    
8394 C C     . VAL D 270 ? 1.1447 0.4572 0.7440 0.1855  0.3879  0.1069  242 VAL D C     
8395 O O     . VAL D 270 ? 1.1343 0.4286 0.7212 0.1732  0.3938  0.0966  242 VAL D O     
8396 C CB    . VAL D 270 ? 1.0297 0.3714 0.6416 0.1794  0.3748  0.0977  242 VAL D CB    
8397 C CG1   . VAL D 270 ? 0.9961 0.3648 0.6222 0.1818  0.3621  0.0998  242 VAL D CG1   
8398 C CG2   . VAL D 270 ? 1.0492 0.3800 0.6566 0.1844  0.3844  0.0971  242 VAL D CG2   
8399 N N     . CYS D 271 ? 1.2055 0.5149 0.8069 0.1976  0.3923  0.1172  243 CYS D N     
8400 C CA    . CYS D 271 ? 1.2858 0.5689 0.8741 0.1974  0.4043  0.1173  243 CYS D CA    
8401 C C     . CYS D 271 ? 1.3131 0.5927 0.8989 0.1947  0.4013  0.1208  243 CYS D C     
8402 O O     . CYS D 271 ? 1.2670 0.5604 0.8623 0.2040  0.3942  0.1318  243 CYS D O     
8403 C CB    . CYS D 271 ? 1.3194 0.6005 0.9111 0.2120  0.4105  0.1270  243 CYS D CB    
8404 S SG    . CYS D 271 ? 1.5254 0.7718 1.1001 0.2127  0.4264  0.1268  243 CYS D SG    
8405 N N     . ALA D 272 ? 1.3767 0.6380 0.9497 0.1817  0.4064  0.1115  244 ALA D N     
8406 C CA    . ALA D 272 ? 1.3032 0.5618 0.8729 0.1771  0.4033  0.1133  244 ALA D CA    
8407 C C     . ALA D 272 ? 1.4054 0.6474 0.9687 0.1835  0.4104  0.1213  244 ALA D C     
8408 O O     . ALA D 272 ? 1.4567 0.6994 1.0190 0.1827  0.4064  0.1259  244 ALA D O     
8409 C CB    . ALA D 272 ? 1.3177 0.5645 0.8773 0.1600  0.4064  0.1003  244 ALA D CB    
8410 N N     . PHE D 273 ? 1.4737 0.7006 1.0322 0.1899  0.4206  0.1234  245 PHE D N     
8411 C CA    . PHE D 273 ? 1.4432 0.6519 0.9946 0.1958  0.4283  0.1307  245 PHE D CA    
8412 C C     . PHE D 273 ? 1.4099 0.6325 0.9728 0.2126  0.4237  0.1454  245 PHE D C     
8413 O O     . PHE D 273 ? 1.3801 0.5902 0.9385 0.2187  0.4284  0.1530  245 PHE D O     
8414 C CB    . PHE D 273 ? 1.4041 0.5847 0.9420 0.1927  0.4430  0.1244  245 PHE D CB    
8415 C CG    . PHE D 273 ? 1.4519 0.6123 0.9763 0.1759  0.4494  0.1121  245 PHE D CG    
8416 C CD1   . PHE D 273 ? 1.4751 0.6180 0.9902 0.1715  0.4545  0.1134  245 PHE D CD1   
8417 C CD2   . PHE D 273 ? 1.4615 0.6208 0.9831 0.1642  0.4502  0.0996  245 PHE D CD2   
8418 C CE1   . PHE D 273 ? 1.5296 0.6547 1.0335 0.1555  0.4606  0.1023  245 PHE D CE1   
8419 C CE2   . PHE D 273 ? 1.4896 0.6317 1.0002 0.1481  0.4557  0.0883  245 PHE D CE2   
8420 C CZ    . PHE D 273 ? 1.5488 0.6739 1.0508 0.1436  0.4611  0.0897  245 PHE D CZ    
8421 N N     . LEU D 274 ? 1.4240 0.6721 1.0018 0.2201  0.4147  0.1499  246 LEU D N     
8422 C CA    . LEU D 274 ? 1.4187 0.6805 1.0087 0.2357  0.4111  0.1637  246 LEU D CA    
8423 C C     . LEU D 274 ? 1.4340 0.7055 1.0293 0.2397  0.4018  0.1740  246 LEU D C     
8424 O O     . LEU D 274 ? 1.4856 0.7609 1.0871 0.2518  0.4013  0.1859  246 LEU D O     
8425 C CB    . LEU D 274 ? 1.3716 0.6594 0.9771 0.2414  0.4035  0.1657  246 LEU D CB    
8426 C CG    . LEU D 274 ? 1.3759 0.6556 0.9786 0.2449  0.4137  0.1618  246 LEU D CG    
8427 C CD1   . LEU D 274 ? 1.3276 0.6341 0.9458 0.2496  0.4057  0.1638  246 LEU D CD1   
8428 C CD2   . LEU D 274 ? 1.5301 0.7948 1.1292 0.2564  0.4243  0.1699  246 LEU D CD2   
8429 N N     . TYR D 275 ? 1.4190 0.6944 1.0117 0.2300  0.3943  0.1701  247 TYR D N     
8430 C CA    . TYR D 275 ? 1.4424 0.7254 1.0380 0.2330  0.3853  0.1798  247 TYR D CA    
8431 C C     . TYR D 275 ? 1.4698 0.7282 1.0528 0.2346  0.3948  0.1839  247 TYR D C     
8432 O O     . TYR D 275 ? 1.4031 0.6665 0.9889 0.2410  0.3888  0.1948  247 TYR D O     
8433 C CB    . TYR D 275 ? 1.3825 0.6753 0.9773 0.2221  0.3753  0.1742  247 TYR D CB    
8434 C CG    . TYR D 275 ? 1.3829 0.6529 0.9611 0.2090  0.3837  0.1640  247 TYR D CG    
8435 C CD1   . TYR D 275 ? 1.3839 0.6455 0.9561 0.1982  0.3900  0.1506  247 TYR D CD1   
8436 C CD2   . TYR D 275 ? 1.4596 0.7168 1.0285 0.2070  0.3853  0.1681  247 TYR D CD2   
8437 C CE1   . TYR D 275 ? 1.3848 0.6267 0.9432 0.1854  0.3976  0.1414  247 TYR D CE1   
8438 C CE2   . TYR D 275 ? 1.5022 0.7392 1.0569 0.1948  0.3935  0.1592  247 TYR D CE2   
8439 C CZ    . TYR D 275 ? 1.4637 0.6935 1.0137 0.1838  0.3995  0.1457  247 TYR D CZ    
8440 O OH    . TYR D 275 ? 1.5334 0.7441 1.0705 0.1708  0.4074  0.1370  247 TYR D OH    
8441 N N     . ARG D 276 ? 1.4943 0.7261 1.0632 0.2288  0.4091  0.1755  248 ARG D N     
8442 C CA    . ARG D 276 ? 1.5373 0.7437 1.0937 0.2299  0.4192  0.1790  248 ARG D CA    
8443 C C     . ARG D 276 ? 1.6432 0.8422 1.2016 0.2438  0.4265  0.1879  248 ARG D C     
8444 O O     . ARG D 276 ? 1.7202 0.9050 1.2726 0.2489  0.4311  0.1956  248 ARG D O     
8445 C CB    . ARG D 276 ? 1.5600 0.7399 1.1001 0.2162  0.4312  0.1659  248 ARG D CB    
8446 C CG    . ARG D 276 ? 1.5290 0.7116 1.0650 0.2020  0.4263  0.1576  248 ARG D CG    
8447 C CD    . ARG D 276 ? 1.5067 0.6633 1.0278 0.1881  0.4386  0.1452  248 ARG D CD    
8448 N NE    . ARG D 276 ? 1.5281 0.6879 1.0458 0.1744  0.4346  0.1375  248 ARG D NE    
8449 C CZ    . ARG D 276 ? 1.5919 0.7327 1.0983 0.1603  0.4432  0.1269  248 ARG D CZ    
8450 N NH1   . ARG D 276 ? 1.7012 0.8175 1.1977 0.1572  0.4561  0.1222  248 ARG D NH1   
8451 N NH2   . ARG D 276 ? 1.5845 0.7310 1.0895 0.1489  0.4389  0.1209  248 ARG D NH2   
8452 N N     . ILE D 277 ? 1.6045 0.8127 1.1709 0.2502  0.4280  0.1875  249 ILE D N     
8453 C CA    . ILE D 277 ? 1.6121 0.8111 1.1791 0.2629  0.4371  0.1945  249 ILE D CA    
8454 C C     . ILE D 277 ? 1.6095 0.8305 1.1921 0.2771  0.4277  0.2100  249 ILE D C     
8455 O O     . ILE D 277 ? 1.5044 0.7537 1.1021 0.2791  0.4150  0.2131  249 ILE D O     
8456 C CB    . ILE D 277 ? 1.5783 0.7762 1.1458 0.2633  0.4438  0.1871  249 ILE D CB    
8457 C CG1   . ILE D 277 ? 1.5628 0.7419 1.1160 0.2475  0.4508  0.1714  249 ILE D CG1   
8458 C CG2   . ILE D 277 ? 1.7270 0.9111 1.2922 0.2757  0.4552  0.1936  249 ILE D CG2   
8459 C CD1   . ILE D 277 ? 1.6994 0.8455 1.2348 0.2416  0.4629  0.1677  249 ILE D CD1   
8460 N N     . PRO D 278 ? 1.6737 0.8829 1.2535 0.2870  0.4330  0.2201  250 PRO D N     
8461 C CA    . PRO D 278 ? 1.5946 0.8249 1.1902 0.3013  0.4249  0.2352  250 PRO D CA    
8462 C C     . PRO D 278 ? 1.6916 0.9378 1.3002 0.3101  0.4259  0.2370  250 PRO D C     
8463 O O     . PRO D 278 ? 1.7553 0.9936 1.3589 0.3062  0.4340  0.2272  250 PRO D O     
8464 C CB    . PRO D 278 ? 1.6172 0.8253 1.2038 0.3092  0.4340  0.2437  250 PRO D CB    
8465 C CG    . PRO D 278 ? 1.6110 0.7909 1.1782 0.2967  0.4421  0.2342  250 PRO D CG    
8466 C CD    . PRO D 278 ? 1.6878 0.8644 1.2502 0.2846  0.4456  0.2188  250 PRO D CD    
8467 N N     . GLU D 279 ? 1.6758 0.9450 1.3011 0.3220  0.4173  0.2503  251 GLU D N     
8468 C CA    . GLU D 279 ? 1.6797 0.9703 1.3206 0.3297  0.4155  0.2531  251 GLU D CA    
8469 C C     . GLU D 279 ? 1.6548 0.9271 1.2893 0.3375  0.4321  0.2520  251 GLU D C     
8470 O O     . GLU D 279 ? 1.6973 0.9755 1.3352 0.3377  0.4356  0.2467  251 GLU D O     
8471 C CB    . GLU D 279 ? 1.6091 0.9284 1.2698 0.3400  0.4024  0.2682  251 GLU D CB    
8472 C CG    . GLU D 279 ? 1.7146 1.0588 1.3935 0.3477  0.3997  0.2721  251 GLU D CG    
8473 C CD    . GLU D 279 ? 1.8304 1.1875 1.5127 0.3376  0.3944  0.2611  251 GLU D CD    
8474 O OE1   . GLU D 279 ? 1.7942 1.1544 1.4730 0.3262  0.3852  0.2549  251 GLU D OE1   
8475 O OE2   . GLU D 279 ? 1.8531 1.2167 1.5411 0.3413  0.3997  0.2589  251 GLU D OE2   
8476 N N     . GLU D 280 ? 1.6438 0.8931 1.2683 0.3441  0.4424  0.2572  252 GLU D N     
8477 C CA    . GLU D 280 ? 1.7515 0.9836 1.3704 0.3532  0.4578  0.2580  252 GLU D CA    
8478 C C     . GLU D 280 ? 1.8190 1.0296 1.4222 0.3432  0.4688  0.2426  252 GLU D C     
8479 O O     . GLU D 280 ? 1.8918 1.0969 1.4936 0.3491  0.4784  0.2411  252 GLU D O     
8480 C CB    . GLU D 280 ? 1.7747 0.9840 1.3844 0.3613  0.4664  0.2662  252 GLU D CB    
8481 N N     . GLN D 281 ? 1.7379 0.9362 1.3290 0.3281  0.4675  0.2312  253 GLN D N     
8482 C CA    . GLN D 281 ? 1.8002 0.9783 1.3764 0.3168  0.4767  0.2162  253 GLN D CA    
8483 C C     . GLN D 281 ? 1.8428 1.0403 1.4251 0.3064  0.4674  0.2070  253 GLN D C     
8484 O O     . GLN D 281 ? 1.8235 1.0072 1.3946 0.2964  0.4734  0.1944  253 GLN D O     
8485 C CB    . GLN D 281 ? 1.6386 0.7855 1.1954 0.3063  0.4841  0.2092  253 GLN D CB    
8486 N N     . LYS D 282 ? 1.8282 1.0570 1.4278 0.3082  0.4526  0.2130  254 LYS D N     
8487 C CA    . LYS D 282 ? 1.7048 0.9523 1.3106 0.2988  0.4434  0.2048  254 LYS D CA    
8488 C C     . LYS D 282 ? 1.6986 0.9515 1.3077 0.3022  0.4483  0.2012  254 LYS D C     
8489 O O     . LYS D 282 ? 1.7117 0.9593 1.3135 0.2918  0.4500  0.1892  254 LYS D O     
8490 C CB    . LYS D 282 ? 1.5983 0.8776 1.2222 0.3010  0.4263  0.2131  254 LYS D CB    
8491 N N     . ASP D 283 ? 1.7398 1.0035 1.3598 0.3168  0.4508  0.2119  255 ASP D N     
8492 C CA    . ASP D 283 ? 1.7416 1.0108 1.3648 0.3211  0.4560  0.2098  255 ASP D CA    
8493 C C     . ASP D 283 ? 1.6848 0.9213 1.2873 0.3168  0.4713  0.1996  255 ASP D C     
8494 O O     . ASP D 283 ? 1.6339 0.8700 1.2330 0.3128  0.4740  0.1918  255 ASP D O     
8495 C CB    . ASP D 283 ? 1.7469 1.0340 1.3863 0.3381  0.4562  0.2244  255 ASP D CB    
8496 C CG    . ASP D 283 ? 1.8026 1.1224 1.4631 0.3418  0.4401  0.2348  255 ASP D CG    
8497 O OD1   . ASP D 283 ? 1.8433 1.1758 1.5075 0.3315  0.4284  0.2297  255 ASP D OD1   
8498 O OD2   . ASP D 283 ? 1.8032 1.1361 1.4768 0.3548  0.4390  0.2481  255 ASP D OD2   
8499 N N     . ASP D 284 ? 1.7169 0.9255 1.3053 0.3174  0.4809  0.1997  256 ASP D N     
8500 C CA    . ASP D 284 ? 1.7486 0.9241 1.3163 0.3114  0.4946  0.1893  256 ASP D CA    
8501 C C     . ASP D 284 ? 1.7174 0.8818 1.2734 0.2927  0.4923  0.1745  256 ASP D C     
8502 O O     . ASP D 284 ? 1.6624 0.8090 1.2055 0.2850  0.4994  0.1635  256 ASP D O     
8503 C CB    . ASP D 284 ? 1.6978 0.8465 1.2546 0.3179  0.5056  0.1945  256 ASP D CB    
8504 N N     . PHE D 285 ? 1.7021 0.8768 1.2624 0.2851  0.4822  0.1741  257 PHE D N     
8505 C CA    . PHE D 285 ? 1.7074 0.8750 1.2587 0.2674  0.4793  0.1607  257 PHE D CA    
8506 C C     . PHE D 285 ? 1.7212 0.9055 1.2780 0.2619  0.4735  0.1532  257 PHE D C     
8507 O O     . PHE D 285 ? 1.6713 0.8421 1.2169 0.2493  0.4766  0.1404  257 PHE D O     
8508 C CB    . PHE D 285 ? 1.6662 0.8439 1.2223 0.2622  0.4692  0.1633  257 PHE D CB    
8509 C CG    . PHE D 285 ? 1.6680 0.8356 1.2138 0.2443  0.4679  0.1504  257 PHE D CG    
8510 C CD1   . PHE D 285 ? 1.6851 0.8691 1.2359 0.2351  0.4596  0.1423  257 PHE D CD1   
8511 C CD2   . PHE D 285 ? 1.6986 0.8404 1.2300 0.2367  0.4750  0.1467  257 PHE D CD2   
8512 C CE1   . PHE D 285 ? 1.7114 0.8869 1.2536 0.2188  0.4585  0.1307  257 PHE D CE1   
8513 C CE2   . PHE D 285 ? 1.6882 0.8217 1.2113 0.2200  0.4741  0.1351  257 PHE D CE2   
8514 C CZ    . PHE D 285 ? 1.7107 0.8613 1.2393 0.2111  0.4659  0.1271  257 PHE D CZ    
8515 N N     . PHE D 286 ? 1.7123 0.9263 1.2870 0.2711  0.4648  0.1612  258 PHE D N     
8516 C CA    . PHE D 286 ? 1.6146 0.8463 1.1957 0.2665  0.4585  0.1552  258 PHE D CA    
8517 C C     . PHE D 286 ? 1.6142 0.8318 1.1863 0.2680  0.4686  0.1498  258 PHE D C     
8518 O O     . PHE D 286 ? 1.5760 0.7885 1.1409 0.2570  0.4682  0.1381  258 PHE D O     
8519 C CB    . PHE D 286 ? 1.4780 0.7447 1.0810 0.2762  0.4468  0.1660  258 PHE D CB    
8520 C CG    . PHE D 286 ? 1.4550 0.7420 1.0658 0.2700  0.4378  0.1603  258 PHE D CG    
8521 C CD1   . PHE D 286 ? 1.4221 0.7050 1.0258 0.2548  0.4333  0.1484  258 PHE D CD1   
8522 C CD2   . PHE D 286 ? 1.4562 0.7665 1.0819 0.2794  0.4341  0.1669  258 PHE D CD2   
8523 C CE1   . PHE D 286 ? 1.3542 0.6553 0.9650 0.2495  0.4249  0.1432  258 PHE D CE1   
8524 C CE2   . PHE D 286 ? 1.3946 0.7229 1.0272 0.2740  0.4259  0.1619  258 PHE D CE2   
8525 C CZ    . PHE D 286 ? 1.3305 0.6540 0.9555 0.2592  0.4212  0.1500  258 PHE D CZ    
8526 N N     . ASP D 287 ? 1.6788 0.8903 1.2512 0.2817  0.4773  0.1582  259 ASP D N     
8527 C CA    . ASP D 287 ? 1.7105 0.9075 1.2735 0.2842  0.4873  0.1536  259 ASP D CA    
8528 C C     . ASP D 287 ? 1.7249 0.8880 1.2662 0.2716  0.4960  0.1402  259 ASP D C     
8529 O O     . ASP D 287 ? 1.6927 0.8468 1.2254 0.2652  0.4987  0.1303  259 ASP D O     
8530 C CB    . ASP D 287 ? 1.7421 0.9376 1.3091 0.3018  0.4957  0.1658  259 ASP D CB    
8531 C CG    . ASP D 287 ? 1.7178 0.9482 1.3072 0.3138  0.4878  0.1780  259 ASP D CG    
8532 O OD1   . ASP D 287 ? 1.7136 0.9666 1.3170 0.3131  0.4761  0.1831  259 ASP D OD1   
8533 O OD2   . ASP D 287 ? 1.6899 0.9250 1.2828 0.3238  0.4933  0.1823  259 ASP D OD2   
8534 N N     . ASP D 288 ? 1.7374 0.8814 1.2697 0.2675  0.4999  0.1398  260 ASP D N     
8535 C CA    . ASP D 288 ? 1.7691 0.8824 1.2822 0.2536  0.5070  0.1269  260 ASP D CA    
8536 C C     . ASP D 288 ? 1.7322 0.8527 1.2446 0.2366  0.4985  0.1144  260 ASP D C     
8537 O O     . ASP D 288 ? 1.7294 0.8323 1.2292 0.2253  0.5024  0.1019  260 ASP D O     
8538 C CB    . ASP D 288 ? 1.7870 0.8812 1.2926 0.2527  0.5122  0.1301  260 ASP D CB    
8539 C CG    . ASP D 288 ? 1.8525 0.9105 1.3376 0.2425  0.5232  0.1193  260 ASP D CG    
8540 O OD1   . ASP D 288 ? 1.8693 0.9130 1.3454 0.2429  0.5302  0.1134  260 ASP D OD1   
8541 O OD2   . ASP D 288 ? 1.8537 0.8974 1.3317 0.2340  0.5248  0.1167  260 ASP D OD2   
8542 N N     . TRP D 289 ? 1.6751 0.8215 1.2010 0.2346  0.4865  0.1176  261 TRP D N     
8543 C CA    . TRP D 289 ? 1.6590 0.8152 1.1860 0.2198  0.4778  0.1068  261 TRP D CA    
8544 C C     . TRP D 289 ? 1.6815 0.8498 1.2124 0.2204  0.4747  0.1024  261 TRP D C     
8545 O O     . TRP D 289 ? 1.7142 0.8747 1.2374 0.2079  0.4740  0.0896  261 TRP D O     
8546 C CB    . TRP D 289 ? 1.6324 0.8130 1.1728 0.2190  0.4659  0.1121  261 TRP D CB    
8547 C CG    . TRP D 289 ? 1.6057 0.7915 1.1450 0.2028  0.4583  0.1009  261 TRP D CG    
8548 C CD1   . TRP D 289 ? 1.6276 0.7931 1.1537 0.1872  0.4623  0.0888  261 TRP D CD1   
8549 C CD2   . TRP D 289 ? 1.5051 0.7188 1.0576 0.2004  0.4454  0.1010  261 TRP D CD2   
8550 N NE1   . TRP D 289 ? 1.5768 0.7565 1.1077 0.1756  0.4528  0.0814  261 TRP D NE1   
8551 C CE2   . TRP D 289 ? 1.5113 0.7198 1.0577 0.1836  0.4425  0.0887  261 TRP D CE2   
8552 C CE3   . TRP D 289 ? 1.4223 0.6648 0.9917 0.2107  0.4360  0.1103  261 TRP D CE3   
8553 C CZ2   . TRP D 289 ? 1.4737 0.7040 1.0295 0.1776  0.4308  0.0856  261 TRP D CZ2   
8554 C CZ3   . TRP D 289 ? 1.3690 0.6325 0.9473 0.2043  0.4243  0.1070  261 TRP D CZ3   
8555 C CH2   . TRP D 289 ? 1.4142 0.6711 0.9854 0.1882  0.4219  0.0948  261 TRP D CH2   
8556 N N     . LEU D 290 ? 1.6779 0.8660 1.2215 0.2349  0.4725  0.1129  262 LEU D N     
8557 C CA    . LEU D 290 ? 1.5949 0.7964 1.1433 0.2365  0.4692  0.1100  262 LEU D CA    
8558 C C     . LEU D 290 ? 1.6556 0.8324 1.1884 0.2342  0.4793  0.1013  262 LEU D C     
8559 O O     . LEU D 290 ? 1.6911 0.8698 1.2211 0.2267  0.4760  0.0915  262 LEU D O     
8560 C CB    . LEU D 290 ? 1.4984 0.7254 1.0639 0.2530  0.4662  0.1241  262 LEU D CB    
8561 C CG    . LEU D 290 ? 1.3493 0.6070 0.9331 0.2549  0.4532  0.1315  262 LEU D CG    
8562 C CD1   . LEU D 290 ? 1.1989 0.4832 0.7996 0.2680  0.4494  0.1419  262 LEU D CD1   
8563 C CD2   . LEU D 290 ? 1.3885 0.6531 0.9720 0.2397  0.4436  0.1208  262 LEU D CD2   
8564 N N     . GLN D 291 ? 1.6425 0.7959 1.1650 0.2407  0.4911  0.1045  263 GLN D N     
8565 C CA    . GLN D 291 ? 1.7190 0.8471 1.2257 0.2393  0.5009  0.0963  263 GLN D CA    
8566 C C     . GLN D 291 ? 1.7812 0.8911 1.2745 0.2203  0.5002  0.0797  263 GLN D C     
8567 O O     . GLN D 291 ? 1.8319 0.9347 1.3177 0.2146  0.5008  0.0693  263 GLN D O     
8568 C CB    . GLN D 291 ? 1.7205 0.8262 1.2188 0.2502  0.5138  0.1034  263 GLN D CB    
8569 N N     . ARG D 292 ? 1.7309 0.8340 1.2216 0.2101  0.4987  0.0769  264 ARG D N     
8570 C CA    . ARG D 292 ? 1.7522 0.8393 1.2316 0.1914  0.4981  0.0616  264 ARG D CA    
8571 C C     . ARG D 292 ? 1.7100 0.8180 1.1969 0.1809  0.4862  0.0529  264 ARG D C     
8572 O O     . ARG D 292 ? 1.6878 0.7853 1.1664 0.1660  0.4851  0.0388  264 ARG D O     
8573 C CB    . ARG D 292 ? 1.7425 0.8190 1.2185 0.1838  0.4996  0.0620  264 ARG D CB    
8574 C CG    . ARG D 292 ? 1.7422 0.7875 1.2010 0.1699  0.5073  0.0498  264 ARG D CG    
8575 C CD    . ARG D 292 ? 1.7304 0.7600 1.1843 0.1692  0.5133  0.0549  264 ARG D CD    
8576 N NE    . ARG D 292 ? 1.7362 0.7438 1.1813 0.1812  0.5252  0.0617  264 ARG D NE    
8577 C CZ    . ARG D 292 ? 1.8130 0.8282 1.2653 0.1978  0.5272  0.0764  264 ARG D CZ    
8578 N NH1   . ARG D 292 ? 1.7654 0.8097 1.2339 0.2046  0.5179  0.0858  264 ARG D NH1   
8579 N NH2   . ARG D 292 ? 1.9542 0.9475 1.3977 0.2080  0.5385  0.0816  264 ARG D NH2   
8580 N N     . LEU D 293 ? 1.6326 0.7703 1.1355 0.1884  0.4771  0.0608  265 LEU D N     
8581 C CA    . LEU D 293 ? 1.6254 0.7837 1.1362 0.1790  0.4654  0.0532  265 LEU D CA    
8582 C C     . LEU D 293 ? 1.6588 0.8161 1.1654 0.1782  0.4652  0.0447  265 LEU D C     
8583 O O     . LEU D 293 ? 1.6468 0.8028 1.1493 0.1645  0.4605  0.0312  265 LEU D O     
8584 C CB    . LEU D 293 ? 1.5640 0.7534 1.0929 0.1874  0.4558  0.0644  265 LEU D CB    
8585 C CG    . LEU D 293 ? 1.5229 0.7165 1.0562 0.1843  0.4525  0.0692  265 LEU D CG    
8586 C CD1   . LEU D 293 ? 1.4540 0.6781 1.0051 0.1934  0.4427  0.0803  265 LEU D CD1   
8587 C CD2   . LEU D 293 ? 1.4814 0.6679 1.0087 0.1657  0.4491  0.0561  265 LEU D CD2   
8588 N N     . GLU D 294 ? 1.7158 0.8746 1.2236 0.1928  0.4702  0.0525  266 GLU D N     
8589 C CA    . GLU D 294 ? 1.8071 0.9625 1.3089 0.1930  0.4713  0.0446  266 GLU D CA    
8590 C C     . GLU D 294 ? 1.7995 0.9231 1.2821 0.1840  0.4797  0.0319  266 GLU D C     
8591 O O     . GLU D 294 ? 1.8376 0.9573 1.3134 0.1786  0.4784  0.0207  266 GLU D O     
8592 C CB    . GLU D 294 ? 1.8982 1.0624 1.4058 0.2114  0.4757  0.0567  266 GLU D CB    
8593 C CG    . GLU D 294 ? 1.9297 1.1281 1.4565 0.2185  0.4657  0.0660  266 GLU D CG    
8594 C CD    . GLU D 294 ? 2.0514 1.2597 1.5852 0.2366  0.4706  0.0788  266 GLU D CD    
8595 O OE1   . GLU D 294 ? 2.0655 1.2539 1.5886 0.2437  0.4818  0.0797  266 GLU D OE1   
8596 O OE2   . GLU D 294 ? 2.0292 1.2655 1.5796 0.2435  0.4633  0.0878  266 GLU D OE2   
8597 N N     . LYS D 295 ? 1.7669 0.8678 1.2404 0.1823  0.4882  0.0334  267 LYS D N     
8598 C CA    . LYS D 295 ? 1.7909 0.8615 1.2464 0.1711  0.4952  0.0204  267 LYS D CA    
8599 C C     . LYS D 295 ? 1.8267 0.9008 1.2814 0.1515  0.4867  0.0057  267 LYS D C     
8600 O O     . LYS D 295 ? 1.9021 0.9667 1.3474 0.1422  0.4862  -0.0080 267 LYS D O     
8601 C CB    . LYS D 295 ? 1.7884 0.8354 1.2357 0.1734  0.5056  0.0260  267 LYS D CB    
8602 N N     . LEU D 296 ? 1.7615 0.8503 1.2262 0.1451  0.4798  0.0082  268 LEU D N     
8603 C CA    . LEU D 296 ? 1.6797 0.7757 1.1461 0.1272  0.4713  -0.0045 268 LEU D CA    
8604 C C     . LEU D 296 ? 1.6829 0.8065 1.1603 0.1262  0.4594  -0.0084 268 LEU D C     
8605 O O     . LEU D 296 ? 1.5920 0.7244 1.0720 0.1120  0.4515  -0.0193 268 LEU D O     
8606 C CB    . LEU D 296 ? 1.5777 0.6781 1.0499 0.1214  0.4692  0.0001  268 LEU D CB    
8607 C CG    . LEU D 296 ? 1.6050 0.6776 1.0657 0.1196  0.4804  0.0021  268 LEU D CG    
8608 C CD1   . LEU D 296 ? 1.7140 0.7949 1.1822 0.1192  0.4783  0.0105  268 LEU D CD1   
8609 C CD2   . LEU D 296 ? 1.5932 0.6433 1.0405 0.1026  0.4841  -0.0138 268 LEU D CD2   
8610 N N     . LYS D 297 ? 1.6739 0.8119 1.1584 0.1410  0.4581  0.0004  269 LYS D N     
8611 C CA    . LYS D 297 ? 1.5999 0.7629 1.0939 0.1416  0.4477  -0.0027 269 LYS D CA    
8612 C C     . LYS D 297 ? 1.4972 0.6849 1.0053 0.1350  0.4360  -0.0021 269 LYS D C     
8613 O O     . LYS D 297 ? 1.4708 0.6704 0.9818 0.1241  0.4273  -0.0132 269 LYS D O     
8614 C CB    . LYS D 297 ? 1.6613 0.8158 1.1448 0.1320  0.4467  -0.0190 269 LYS D CB    
8615 N N     . GLY D 298 ? 1.3887 0.5844 0.9055 0.1420  0.4358  0.0108  270 GLY D N     
8616 C CA    . GLY D 298 ? 1.3313 0.5511 0.8618 0.1385  0.4250  0.0133  270 GLY D CA    
8617 C C     . GLY D 298 ? 1.3887 0.6340 0.9330 0.1516  0.4186  0.0236  270 GLY D C     
8618 O O     . GLY D 298 ? 1.3592 0.6267 0.9139 0.1481  0.4079  0.0213  270 GLY D O     
8619 N N     . THR D 299 ? 1.3949 0.6376 0.9398 0.1668  0.4254  0.0351  271 THR D N     
8620 C CA    . THR D 299 ? 1.3597 0.6254 0.9175 0.1801  0.4212  0.0455  271 THR D CA    
8621 C C     . THR D 299 ? 1.3892 0.6507 0.9412 0.1851  0.4251  0.0417  271 THR D C     
8622 O O     . THR D 299 ? 1.4436 0.6813 0.9816 0.1841  0.4343  0.0361  271 THR D O     
8623 C CB    . THR D 299 ? 1.3356 0.6053 0.9003 0.1944  0.4256  0.0622  271 THR D CB    
8624 O OG1   . THR D 299 ? 1.4519 0.6991 1.0057 0.2014  0.4382  0.0650  271 THR D OG1   
8625 C CG2   . THR D 299 ? 1.2527 0.5240 0.8207 0.1895  0.4225  0.0653  271 THR D CG2   
8626 N N     . SER D 300 ? 1.2985 0.5830 0.8613 0.1907  0.4181  0.0445  272 SER D N     
8627 C CA    . SER D 300 ? 1.3054 0.5891 0.8637 0.1958  0.4209  0.0410  272 SER D CA    
8628 C C     . SER D 300 ? 1.3446 0.6522 0.9174 0.2102  0.4184  0.0544  272 SER D C     
8629 O O     . SER D 300 ? 1.3207 0.6471 0.9076 0.2145  0.4128  0.0647  272 SER D O     
8630 C CB    . SER D 300 ? 1.2861 0.5725 0.8395 0.1826  0.4137  0.0244  272 SER D CB    
8631 O OG    . SER D 300 ? 1.3368 0.6366 0.8932 0.1892  0.4113  0.0242  272 SER D OG    
8632 N N     . GLN D 301 ? 1.3551 0.6619 0.9242 0.2175  0.4227  0.0541  273 GLN D N     
8633 C CA    . GLN D 301 ? 1.2709 0.6001 0.8532 0.2308  0.4213  0.0662  273 GLN D CA    
8634 C C     . GLN D 301 ? 1.3481 0.6835 0.9269 0.2292  0.4183  0.0573  273 GLN D C     
8635 O O     . GLN D 301 ? 1.4059 0.7223 0.9692 0.2243  0.4230  0.0455  273 GLN D O     
8636 C CB    . GLN D 301 ? 1.1532 0.4753 0.7357 0.2462  0.4328  0.0796  273 GLN D CB    
8637 C CG    . GLN D 301 ? 1.2228 0.5707 0.8219 0.2601  0.4314  0.0943  273 GLN D CG    
8638 C CD    . GLN D 301 ? 1.3258 0.6654 0.9210 0.2741  0.4436  0.1022  273 GLN D CD    
8639 O OE1   . GLN D 301 ? 1.2728 0.6010 0.8661 0.2812  0.4521  0.1099  273 GLN D OE1   
8640 N NE2   . GLN D 301 ? 1.3598 0.7054 0.9538 0.2785  0.4446  0.1005  273 GLN D NE2   
8641 N N     . GLY D 302 ? 1.3757 0.7378 0.9686 0.2334  0.4104  0.0628  274 GLY D N     
8642 C CA    . GLY D 302 ? 1.3801 0.7510 0.9707 0.2319  0.4066  0.0548  274 GLY D CA    
8643 C C     . GLY D 302 ? 1.3924 0.7847 0.9954 0.2454  0.4069  0.0674  274 GLY D C     
8644 O O     . GLY D 302 ? 1.3712 0.7693 0.9835 0.2572  0.4119  0.0827  274 GLY D O     
8645 N N     . VAL D 303 ? 1.4141 0.8192 1.0176 0.2437  0.4015  0.0612  275 VAL D N     
8646 C CA    . VAL D 303 ? 1.3765 0.8028 0.9914 0.2554  0.4014  0.0723  275 VAL D CA    
8647 C C     . VAL D 303 ? 1.3726 0.8234 0.9986 0.2496  0.3886  0.0697  275 VAL D C     
8648 O O     . VAL D 303 ? 1.3659 0.8152 0.9863 0.2368  0.3811  0.0558  275 VAL D O     
8649 C CB    . VAL D 303 ? 1.3283 0.7448 0.9309 0.2615  0.4097  0.0684  275 VAL D CB    
8650 C CG1   . VAL D 303 ? 1.2648 0.6619 0.8606 0.2715  0.4232  0.0759  275 VAL D CG1   
8651 C CG2   . VAL D 303 ? 1.3206 0.7241 0.9064 0.2488  0.4069  0.0484  275 VAL D CG2   
8652 N N     . GLY D 304 ? 1.3731 0.8475 1.0155 0.2593  0.3864  0.0834  276 GLY D N     
8653 C CA    . GLY D 304 ? 1.4031 0.9017 1.0574 0.2557  0.3750  0.0834  276 GLY D CA    
8654 C C     . GLY D 304 ? 1.4919 1.0031 1.1463 0.2606  0.3750  0.0831  276 GLY D C     
8655 O O     . GLY D 304 ? 1.4835 0.9865 1.1303 0.2683  0.3842  0.0848  276 GLY D O     
8656 N N     . ARG D 305 ? 1.5383 1.0698 1.2010 0.2561  0.3646  0.0808  277 ARG D N     
8657 C CA    . ARG D 305 ? 1.5482 1.0941 1.2119 0.2604  0.3638  0.0811  277 ARG D CA    
8658 C C     . ARG D 305 ? 1.5351 1.0949 1.2123 0.2752  0.3699  0.0998  277 ARG D C     
8659 O O     . ARG D 305 ? 1.4049 0.9673 1.0782 0.2819  0.3753  0.1014  277 ARG D O     
8660 C CB    . ARG D 305 ? 1.4571 1.0224 1.1277 0.2526  0.3513  0.0758  277 ARG D CB    
8661 N N     . ASN D 306 ? 1.6218 1.1917 1.3150 0.2803  0.3691  0.1141  278 ASN D N     
8662 C CA    . ASN D 306 ? 1.5077 1.0920 1.2153 0.2939  0.3752  0.1325  278 ASN D CA    
8663 C C     . ASN D 306 ? 1.3507 0.9168 1.0504 0.3022  0.3882  0.1371  278 ASN D C     
8664 O O     . ASN D 306 ? 1.1557 0.7327 0.8657 0.3139  0.3948  0.1517  278 ASN D O     
8665 C CB    . ASN D 306 ? 1.3796 0.9840 1.1083 0.2955  0.3688  0.1458  278 ASN D CB    
8666 N N     . GLY D 307 ? 1.3874 0.9269 1.0696 0.2962  0.3922  0.1251  279 GLY D N     
8667 C CA    . GLY D 307 ? 1.3655 0.8851 1.0382 0.3036  0.4047  0.1281  279 GLY D CA    
8668 C C     . GLY D 307 ? 1.3879 0.8995 1.0645 0.3045  0.4072  0.1347  279 GLY D C     
8669 O O     . GLY D 307 ? 1.2782 0.7705 0.9452 0.3096  0.4177  0.1358  279 GLY D O     
8670 N N     . GLU D 308 ? 1.4114 0.9371 1.1013 0.2999  0.3981  0.1388  280 GLU D N     
8671 C CA    . GLU D 308 ? 1.2688 0.7898 0.9634 0.3010  0.3999  0.1455  280 GLU D CA    
8672 C C     . GLU D 308 ? 1.3045 0.7964 0.9803 0.2913  0.4020  0.1315  280 GLU D C     
8673 O O     . GLU D 308 ? 1.3363 0.8151 0.9978 0.2817  0.3997  0.1160  280 GLU D O     
8674 C CB    . GLU D 308 ? 1.1411 0.6863 0.8548 0.2985  0.3888  0.1529  280 GLU D CB    
8675 N N     . ALA D 309 ? 1.2888 0.7718 0.9654 0.2935  0.4062  0.1372  281 ALA D N     
8676 C CA    . ALA D 309 ? 1.2821 0.7377 0.9421 0.2850  0.4092  0.1262  281 ALA D CA    
8677 C C     . ALA D 309 ? 1.2498 0.7094 0.9130 0.2731  0.3984  0.1202  281 ALA D C     
8678 O O     . ALA D 309 ? 1.1806 0.6608 0.8600 0.2750  0.3915  0.1294  281 ALA D O     
8679 C CB    . ALA D 309 ? 1.1879 0.6308 0.8461 0.2937  0.4198  0.1354  281 ALA D CB    
8680 N N     . GLU D 310 ? 1.2350 0.6754 0.8829 0.2606  0.3970  0.1044  282 GLU D N     
8681 C CA    . GLU D 310 ? 1.1566 0.5985 0.8055 0.2482  0.3875  0.0969  282 GLU D CA    
8682 C C     . GLU D 310 ? 1.1773 0.5943 0.8140 0.2423  0.3930  0.0919  282 GLU D C     
8683 O O     . GLU D 310 ? 1.2681 0.6625 0.8905 0.2427  0.4025  0.0870  282 GLU D O     
8684 C CB    . GLU D 310 ? 1.1620 0.6066 0.8054 0.2370  0.3797  0.0818  282 GLU D CB    
8685 C CG    . GLU D 310 ? 1.2145 0.6850 0.8703 0.2416  0.3728  0.0862  282 GLU D CG    
8686 C CD    . GLU D 310 ? 1.2693 0.7431 0.9191 0.2309  0.3654  0.0709  282 GLU D CD    
8687 O OE1   . GLU D 310 ? 1.3169 0.7718 0.9514 0.2216  0.3675  0.0568  282 GLU D OE1   
8688 O OE2   . GLU D 310 ? 1.2405 0.7363 0.9010 0.2317  0.3574  0.0730  282 GLU D OE2   
8689 N N     . TYR D 311 ? 1.0799 0.5008 0.7220 0.2369  0.3872  0.0933  283 TYR D N     
8690 C CA    . TYR D 311 ? 1.0296 0.4292 0.6618 0.2316  0.3921  0.0904  283 TYR D CA    
8691 C C     . TYR D 311 ? 1.0150 0.4136 0.6449 0.2169  0.3835  0.0795  283 TYR D C     
8692 O O     . TYR D 311 ? 1.0196 0.4385 0.6609 0.2147  0.3732  0.0809  283 TYR D O     
8693 C CB    . TYR D 311 ? 1.0298 0.4350 0.6714 0.2422  0.3954  0.1056  283 TYR D CB    
8694 C CG    . TYR D 311 ? 1.0522 0.4592 0.6971 0.2570  0.4045  0.1168  283 TYR D CG    
8695 C CD1   . TYR D 311 ? 1.1201 0.5521 0.7802 0.2663  0.4013  0.1265  283 TYR D CD1   
8696 C CD2   . TYR D 311 ? 1.1123 0.4962 0.7454 0.2615  0.4166  0.1177  283 TYR D CD2   
8697 C CE1   . TYR D 311 ? 1.1887 0.6235 0.8526 0.2798  0.4100  0.1371  283 TYR D CE1   
8698 C CE2   . TYR D 311 ? 1.1899 0.5755 0.8260 0.2754  0.4253  0.1280  283 TYR D CE2   
8699 C CZ    . TYR D 311 ? 1.1727 0.5843 0.8246 0.2845  0.4220  0.1377  283 TYR D CZ    
8700 O OH    . TYR D 311 ? 1.1673 0.5817 0.8231 0.2983  0.4310  0.1482  283 TYR D OH    
8701 N N     . TYR D 312 ? 1.0365 0.4113 0.6518 0.2069  0.3880  0.0689  284 TYR D N     
8702 C CA    . TYR D 312 ? 1.0398 0.4126 0.6516 0.1916  0.3808  0.0564  284 TYR D CA    
8703 C C     . TYR D 312 ? 1.1083 0.4607 0.7112 0.1850  0.3862  0.0544  284 TYR D C     
8704 O O     . TYR D 312 ? 1.1470 0.4816 0.7422 0.1905  0.3964  0.0590  284 TYR D O     
8705 C CB    . TYR D 312 ? 1.0765 0.4440 0.6792 0.1820  0.3792  0.0407  284 TYR D CB    
8706 C CG    . TYR D 312 ? 1.0128 0.4021 0.6240 0.1860  0.3723  0.0405  284 TYR D CG    
8707 C CD1   . TYR D 312 ? 1.0914 0.4819 0.7019 0.1970  0.3778  0.0456  284 TYR D CD1   
8708 C CD2   . TYR D 312 ? 0.9839 0.3924 0.6034 0.1790  0.3606  0.0353  284 TYR D CD2   
8709 C CE1   . TYR D 312 ? 1.1670 0.5773 0.7848 0.2007  0.3720  0.0458  284 TYR D CE1   
8710 C CE2   . TYR D 312 ? 1.0363 0.4647 0.6633 0.1827  0.3545  0.0353  284 TYR D CE2   
8711 C CZ    . TYR D 312 ? 1.1535 0.5827 0.7795 0.1935  0.3603  0.0407  284 TYR D CZ    
8712 O OH    . TYR D 312 ? 1.1762 0.6251 0.8091 0.1973  0.3548  0.0412  284 TYR D OH    
8713 N N     . ILE D 313 ? 1.0737 0.4289 0.6775 0.1732  0.3793  0.0474  285 ILE D N     
8714 C CA    . ILE D 313 ? 1.0492 0.3853 0.6437 0.1638  0.3835  0.0427  285 ILE D CA    
8715 C C     . ILE D 313 ? 1.1630 0.4972 0.7528 0.1473  0.3781  0.0264  285 ILE D C     
8716 O O     . ILE D 313 ? 1.1312 0.4846 0.7299 0.1427  0.3678  0.0231  285 ILE D O     
8717 C CB    . ILE D 313 ? 1.0325 0.3758 0.6344 0.1669  0.3808  0.0528  285 ILE D CB    
8718 C CG1   . ILE D 313 ? 1.0395 0.3851 0.6463 0.1830  0.3863  0.0683  285 ILE D CG1   
8719 C CG2   . ILE D 313 ? 1.0473 0.3721 0.6393 0.1555  0.3845  0.0465  285 ILE D CG2   
8720 C CD1   . ILE D 313 ? 1.0248 0.3815 0.6405 0.1872  0.3818  0.0785  285 ILE D CD1   
8721 N N     . HIS D 314 ? 1.2543 0.5663 0.8307 0.1383  0.3850  0.0162  286 HIS D N     
8722 C CA    . HIS D 314 ? 1.2674 0.5776 0.8392 0.1222  0.3806  0.0000  286 HIS D CA    
8723 C C     . HIS D 314 ? 1.2412 0.5405 0.8093 0.1110  0.3823  -0.0033 286 HIS D C     
8724 O O     . HIS D 314 ? 1.2474 0.5286 0.8088 0.1136  0.3912  0.0027  286 HIS D O     
8725 C CB    . HIS D 314 ? 1.2573 0.5511 0.8166 0.1183  0.3864  -0.0106 286 HIS D CB    
8726 C CG    . HIS D 314 ? 1.2792 0.5796 0.8397 0.1304  0.3872  -0.0065 286 HIS D CG    
8727 N ND1   . HIS D 314 ? 1.2928 0.6135 0.8597 0.1301  0.3784  -0.0116 286 HIS D ND1   
8728 C CD2   . HIS D 314 ? 1.2969 0.5869 0.8532 0.1432  0.3961  0.0023  286 HIS D CD2   
8729 C CE1   . HIS D 314 ? 1.3266 0.6486 0.8927 0.1421  0.3822  -0.0060 286 HIS D CE1   
8730 N NE2   . HIS D 314 ? 1.3150 0.6187 0.8750 0.1503  0.3929  0.0025  286 HIS D NE2   
8731 N N     . LEU D 315 ? 1.1769 0.4878 0.7494 0.0988  0.3741  -0.0129 287 LEU D N     
8732 C CA    . LEU D 315 ? 1.2751 0.5791 0.8457 0.0877  0.3749  -0.0162 287 LEU D CA    
8733 C C     . LEU D 315 ? 1.3390 0.6583 0.9148 0.0742  0.3655  -0.0291 287 LEU D C     
8734 O O     . LEU D 315 ? 1.3140 0.6549 0.8986 0.0765  0.3562  -0.0311 287 LEU D O     
8735 C CB    . LEU D 315 ? 1.2404 0.5500 0.8173 0.0961  0.3744  -0.0022 287 LEU D CB    
8736 C CG    . LEU D 315 ? 1.0445 0.3809 0.6355 0.1038  0.3636  0.0047  287 LEU D CG    
8737 C CD1   . LEU D 315 ? 1.1107 0.4596 0.7074 0.0935  0.3555  -0.0012 287 LEU D CD1   
8738 C CD2   . LEU D 315 ? 1.0076 0.3463 0.6028 0.1190  0.3659  0.0214  287 LEU D CD2   
8739 N N     . SER D 316 ? 1.3729 0.6814 0.9434 0.0601  0.3683  -0.0378 288 SER D N     
8740 C CA    . SER D 316 ? 1.3821 0.7045 0.9574 0.0462  0.3604  -0.0506 288 SER D CA    
8741 C C     . SER D 316 ? 1.3375 0.6737 0.9218 0.0447  0.3550  -0.0461 288 SER D C     
8742 O O     . SER D 316 ? 1.3773 0.7031 0.9592 0.0479  0.3604  -0.0371 288 SER D O     
8743 C CB    . SER D 316 ? 1.3943 0.6984 0.9595 0.0308  0.3667  -0.0631 288 SER D CB    
8744 O OG    . SER D 316 ? 1.5802 0.8706 1.1357 0.0318  0.3714  -0.0683 288 SER D OG    
8745 N N     . VAL D 317 ? 1.2919 0.6518 0.8860 0.0403  0.3442  -0.0526 289 VAL D N     
8746 C CA    . VAL D 317 ? 1.2198 0.5950 0.8227 0.0396  0.3378  -0.0492 289 VAL D CA    
8747 C C     . VAL D 317 ? 1.2392 0.6253 0.8455 0.0241  0.3329  -0.0632 289 VAL D C     
8748 O O     . VAL D 317 ? 1.2821 0.6799 0.8907 0.0191  0.3273  -0.0736 289 VAL D O     
8749 C CB    . VAL D 317 ? 1.2338 0.6308 0.8473 0.0522  0.3286  -0.0409 289 VAL D CB    
8750 C CG1   . VAL D 317 ? 1.2740 0.6869 0.8958 0.0503  0.3214  -0.0393 289 VAL D CG1   
8751 C CG2   . VAL D 317 ? 1.2144 0.6024 0.8259 0.0675  0.3337  -0.0262 289 VAL D CG2   
8752 N N     . ILE D 318 ? 1.2727 0.6557 0.8793 0.0168  0.3351  -0.0633 290 ILE D N     
8753 C CA    . ILE D 318 ? 1.2484 0.6458 0.8607 0.0036  0.3299  -0.0748 290 ILE D CA    
8754 C C     . ILE D 318 ? 1.1659 0.5873 0.7893 0.0097  0.3197  -0.0703 290 ILE D C     
8755 O O     . ILE D 318 ? 1.2128 0.6314 0.8366 0.0181  0.3206  -0.0589 290 ILE D O     
8756 C CB    . ILE D 318 ? 1.2646 0.6450 0.8707 -0.0084 0.3390  -0.0779 290 ILE D CB    
8757 C CG1   . ILE D 318 ? 1.2780 0.6316 0.8718 -0.0129 0.3499  -0.0804 290 ILE D CG1   
8758 C CG2   . ILE D 318 ? 1.2656 0.6617 0.8780 -0.0228 0.3344  -0.0908 290 ILE D CG2   
8759 C CD1   . ILE D 318 ? 1.3757 0.7083 0.9618 -0.0209 0.3608  -0.0789 290 ILE D CD1   
8760 N N     . THR D 319 ? 1.1426 0.5874 0.7744 0.0058  0.3100  -0.0792 291 THR D N     
8761 C CA    . THR D 319 ? 1.2155 0.6841 0.8578 0.0101  0.3000  -0.0768 291 THR D CA    
8762 C C     . THR D 319 ? 1.2381 0.7173 0.8845 -0.0031 0.2981  -0.0871 291 THR D C     
8763 O O     . THR D 319 ? 1.3526 0.8343 0.9986 -0.0147 0.2985  -0.0993 291 THR D O     
8764 C CB    . THR D 319 ? 1.2202 0.7092 0.8693 0.0171  0.2902  -0.0781 291 THR D CB    
8765 O OG1   . THR D 319 ? 1.2445 0.7228 0.8895 0.0286  0.2935  -0.0694 291 THR D OG1   
8766 C CG2   . THR D 319 ? 1.1219 0.6332 0.7811 0.0231  0.2805  -0.0739 291 THR D CG2   
8767 N N     . ALA D 320 ? 1.2257 0.7115 0.8759 -0.0014 0.2963  -0.0821 292 ALA D N     
8768 C CA    . ALA D 320 ? 1.2298 0.7248 0.8837 -0.0133 0.2960  -0.0906 292 ALA D CA    
8769 C C     . ALA D 320 ? 1.2363 0.7538 0.8990 -0.0076 0.2867  -0.0875 292 ALA D C     
8770 O O     . ALA D 320 ? 1.2495 0.7677 0.9126 0.0046  0.2833  -0.0765 292 ALA D O     
8771 C CB    . ALA D 320 ? 1.1975 0.6694 0.8427 -0.0202 0.3080  -0.0887 292 ALA D CB    
8772 N N     . LEU D 321 ? 1.1913 0.7273 0.8610 -0.0168 0.2826  -0.0975 293 LEU D N     
8773 C CA    . LEU D 321 ? 1.1941 0.7515 0.8718 -0.0132 0.2745  -0.0961 293 LEU D CA    
8774 C C     . LEU D 321 ? 1.2996 0.8612 0.9790 -0.0256 0.2789  -0.1040 293 LEU D C     
8775 O O     . LEU D 321 ? 1.3903 0.9609 1.0736 -0.0367 0.2791  -0.1158 293 LEU D O     
8776 C CB    . LEU D 321 ? 1.1517 0.7342 0.8387 -0.0091 0.2626  -0.1002 293 LEU D CB    
8777 C CG    . LEU D 321 ? 1.1932 0.7996 0.8891 -0.0073 0.2541  -0.1014 293 LEU D CG    
8778 C CD1   . LEU D 321 ? 1.1800 0.7820 0.8737 0.0033  0.2526  -0.0892 293 LEU D CD1   
8779 C CD2   . LEU D 321 ? 1.2560 0.8849 0.9599 -0.0041 0.2435  -0.1062 293 LEU D CD2   
8780 N N     . ALA D 322 ? 1.2255 0.7807 0.9015 -0.0237 0.2829  -0.0975 294 ALA D N     
8781 C CA    . ALA D 322 ? 1.1911 0.7475 0.8672 -0.0349 0.2894  -0.1035 294 ALA D CA    
8782 C C     . ALA D 322 ? 1.2108 0.7879 0.8932 -0.0306 0.2826  -0.1016 294 ALA D C     
8783 O O     . ALA D 322 ? 1.1764 0.7662 0.8631 -0.0197 0.2725  -0.0964 294 ALA D O     
8784 C CB    . ALA D 322 ? 1.2341 0.7611 0.8980 -0.0379 0.3027  -0.0979 294 ALA D CB    
8785 N N     . ARG D 323 ? 1.3046 0.8845 0.9874 -0.0393 0.2887  -0.1059 295 ARG D N     
8786 C CA    . ARG D 323 ? 1.3278 0.9265 1.0157 -0.0360 0.2836  -0.1046 295 ARG D CA    
8787 C C     . ARG D 323 ? 1.3808 0.9721 1.0641 -0.0447 0.2950  -0.1056 295 ARG D C     
8788 O O     . ARG D 323 ? 1.3629 0.9488 1.0462 -0.0576 0.3041  -0.1137 295 ARG D O     
8789 C CB    . ARG D 323 ? 1.3026 0.9315 1.0041 -0.0381 0.2740  -0.1140 295 ARG D CB    
8790 C CG    . ARG D 323 ? 1.3165 0.9649 1.0236 -0.0338 0.2685  -0.1128 295 ARG D CG    
8791 C CD    . ARG D 323 ? 1.3543 1.0314 1.0746 -0.0359 0.2601  -0.1223 295 ARG D CD    
8792 N NE    . ARG D 323 ? 1.4354 1.1188 1.1588 -0.0278 0.2496  -0.1211 295 ARG D NE    
8793 C CZ    . ARG D 323 ? 1.4266 1.1294 1.1590 -0.0300 0.2431  -0.1296 295 ARG D CZ    
8794 N NH1   . ARG D 323 ? 1.4439 1.1636 1.1847 -0.0400 0.2447  -0.1399 295 ARG D NH1   
8795 N NH2   . ARG D 323 ? 1.3745 1.0809 1.1080 -0.0218 0.2344  -0.1271 295 ARG D NH2   
8796 N N     . LYS D 324 ? 1.4273 1.0180 1.1059 -0.0378 0.2946  -0.0974 296 LYS D N     
8797 C CA    . LYS D 324 ? 1.4854 1.0716 1.1603 -0.0448 0.3038  -0.0962 296 LYS D CA    
8798 C C     . LYS D 324 ? 1.4979 1.1122 1.1858 -0.0515 0.3012  -0.1048 296 LYS D C     
8799 O O     . LYS D 324 ? 1.4112 1.0479 1.1082 -0.0459 0.2902  -0.1075 296 LYS D O     
8800 C CB    . LYS D 324 ? 1.4636 1.0385 1.1276 -0.0344 0.3035  -0.0835 296 LYS D CB    
8801 N N     . PHE D 325 ? 1.5206 1.1335 1.2096 -0.0637 0.3115  -0.1087 297 PHE D N     
8802 C CA    . PHE D 325 ? 1.5160 1.1557 1.2181 -0.0707 0.3109  -0.1163 297 PHE D CA    
8803 C C     . PHE D 325 ? 1.5428 1.1884 1.2414 -0.0645 0.3113  -0.1099 297 PHE D C     
8804 O O     . PHE D 325 ? 1.5460 1.1712 1.2308 -0.0602 0.3167  -0.1004 297 PHE D O     
8805 C CB    . PHE D 325 ? 1.4942 1.1318 1.2009 -0.0878 0.3219  -0.1239 297 PHE D CB    
8806 C CG    . PHE D 325 ? 1.5408 1.1883 1.2575 -0.0960 0.3181  -0.1350 297 PHE D CG    
8807 C CD1   . PHE D 325 ? 1.5819 1.2611 1.3148 -0.0988 0.3103  -0.1436 297 PHE D CD1   
8808 C CD2   . PHE D 325 ? 1.5392 1.1639 1.2483 -0.1006 0.3223  -0.1368 297 PHE D CD2   
8809 C CE1   . PHE D 325 ? 1.6446 1.3334 1.3857 -0.1064 0.3062  -0.1537 297 PHE D CE1   
8810 C CE2   . PHE D 325 ? 1.5249 1.1580 1.2413 -0.1083 0.3186  -0.1474 297 PHE D CE2   
8811 C CZ    . PHE D 325 ? 1.5756 1.2411 1.3079 -0.1114 0.3102  -0.1558 297 PHE D CZ    
8812 N N     . SAM E .   ? 0.8116 0.5917 0.6453 0.1890  -0.0820 -0.0050 301 SAM A N     
8813 C CA    . SAM E .   ? 0.7847 0.5721 0.6154 0.1945  -0.0758 -0.0166 301 SAM A CA    
8814 C C     . SAM E .   ? 0.8377 0.6480 0.6776 0.1996  -0.0720 -0.0179 301 SAM A C     
8815 O O     . SAM E .   ? 0.7971 0.6128 0.6435 0.2012  -0.0760 -0.0099 301 SAM A O     
8816 O OXT   . SAM E .   ? 0.8635 0.6880 0.7044 0.2021  -0.0648 -0.0271 301 SAM A OXT   
8817 C CB    . SAM E .   ? 0.6979 0.4665 0.5202 0.2009  -0.0803 -0.0214 301 SAM A CB    
8818 C CG    . SAM E .   ? 0.7302 0.4872 0.5548 0.2047  -0.0896 -0.0132 301 SAM A CG    
8819 S SD    . SAM E .   ? 0.8372 0.5679 0.6498 0.2122  -0.0947 -0.0195 301 SAM A SD    
8820 C CE    . SAM E .   ? 0.8750 0.5991 0.6923 0.2209  -0.1021 -0.0130 301 SAM A CE    
8821 C "C5'" . SAM E .   ? 0.7204 0.4230 0.5212 0.2034  -0.1018 -0.0171 301 SAM A "C5'" 
8822 C "C4'" . SAM E .   ? 0.6847 0.3856 0.4757 0.2007  -0.0957 -0.0264 301 SAM A "C4'" 
8823 O "O4'" . SAM E .   ? 0.7157 0.4003 0.4994 0.1930  -0.1009 -0.0235 301 SAM A "O4'" 
8824 C "C3'" . SAM E .   ? 0.6534 0.3444 0.4342 0.2099  -0.0932 -0.0374 301 SAM A "C3'" 
8825 O "O3'" . SAM E .   ? 0.6449 0.3506 0.4249 0.2113  -0.0832 -0.0459 301 SAM A "O3'" 
8826 C "C2'" . SAM E .   ? 0.6681 0.3304 0.4340 0.2066  -0.1000 -0.0388 301 SAM A "C2'" 
8827 O "O2'" . SAM E .   ? 0.6812 0.3358 0.4338 0.2117  -0.0944 -0.0507 301 SAM A "O2'" 
8828 C "C1'" . SAM E .   ? 0.6673 0.3301 0.4337 0.1963  -0.1018 -0.0333 301 SAM A "C1'" 
8829 N N9    . SAM E .   ? 0.7212 0.3589 0.4793 0.1909  -0.1125 -0.0289 301 SAM A N9    
8830 C C8    . SAM E .   ? 0.7906 0.4108 0.5469 0.1936  -0.1209 -0.0258 301 SAM A C8    
8831 N N7    . SAM E .   ? 0.8371 0.4366 0.5853 0.1860  -0.1300 -0.0224 301 SAM A N7    
8832 C C5    . SAM E .   ? 0.7870 0.3916 0.5319 0.1788  -0.1274 -0.0231 301 SAM A C5    
8833 C C6    . SAM E .   ? 0.7511 0.3425 0.4883 0.1695  -0.1340 -0.0203 301 SAM A C6    
8834 N N6    . SAM E .   ? 0.7284 0.2945 0.4595 0.1646  -0.1471 -0.0160 301 SAM A N6    
8835 N N1    . SAM E .   ? 0.7678 0.3696 0.5035 0.1650  -0.1286 -0.0214 301 SAM A N1    
8836 C C2    . SAM E .   ? 0.7250 0.3483 0.4662 0.1685  -0.1169 -0.0253 301 SAM A C2    
8837 N N3    . SAM E .   ? 0.7003 0.3366 0.4490 0.1764  -0.1109 -0.0284 301 SAM A N3    
8838 C C4    . SAM E .   ? 0.7311 0.3593 0.4820 0.1821  -0.1159 -0.0272 301 SAM A C4    
8839 N N     . SAM F .   ? 0.7014 0.5442 0.6430 0.2274  0.1832  0.2031  301 SAM B N     
8840 C CA    . SAM F .   ? 0.7368 0.5598 0.6613 0.2343  0.2004  0.1975  301 SAM B CA    
8841 C C     . SAM F .   ? 0.7845 0.5920 0.7002 0.2332  0.2014  0.1941  301 SAM B C     
8842 O O     . SAM F .   ? 0.7147 0.5316 0.6418 0.2300  0.1906  0.2001  301 SAM B O     
8843 O OXT   . SAM F .   ? 0.8000 0.5842 0.6958 0.2352  0.2130  0.1852  301 SAM B OXT   
8844 C CB    . SAM F .   ? 0.6526 0.4848 0.5855 0.2439  0.2127  0.2065  301 SAM B CB    
8845 C CG    . SAM F .   ? 0.6522 0.5050 0.6079 0.2453  0.2065  0.2199  301 SAM B CG    
8846 S SD    . SAM F .   ? 0.9103 0.7722 0.8742 0.2578  0.2235  0.2305  301 SAM B SD    
8847 C CE    . SAM F .   ? 0.7855 0.6633 0.7701 0.2611  0.2202  0.2441  301 SAM B CE    
8848 C "C5'" . SAM F .   ? 0.7381 0.6219 0.7157 0.2587  0.2227  0.2373  301 SAM B "C5'" 
8849 C "C4'" . SAM F .   ? 0.6859 0.5541 0.6432 0.2622  0.2344  0.2284  301 SAM B "C4'" 
8850 O "O4'" . SAM F .   ? 0.6995 0.5831 0.6657 0.2611  0.2309  0.2323  301 SAM B "O4'" 
8851 C "C3'" . SAM F .   ? 0.6604 0.5179 0.6077 0.2734  0.2541  0.2305  301 SAM B "C3'" 
8852 O "O3'" . SAM F .   ? 0.6719 0.5023 0.5930 0.2741  0.2630  0.2178  301 SAM B "O3'" 
8853 C "C2'" . SAM F .   ? 0.6582 0.5326 0.6151 0.2787  0.2598  0.2390  301 SAM B "C2'" 
8854 O "O2'" . SAM F .   ? 0.7364 0.5924 0.6721 0.2870  0.2776  0.2347  301 SAM B "O2'" 
8855 C "C1'" . SAM F .   ? 0.6553 0.5376 0.6153 0.2720  0.2490  0.2361  301 SAM B "C1'" 
8856 N N9    . SAM F .   ? 0.6371 0.5456 0.6181 0.2732  0.2465  0.2482  301 SAM B N9    
8857 C C8    . SAM F .   ? 0.6918 0.6202 0.6943 0.2761  0.2469  0.2615  301 SAM B C8    
8858 N N7    . SAM F .   ? 0.6463 0.5957 0.6642 0.2757  0.2446  0.2701  301 SAM B N7    
8859 C C5    . SAM F .   ? 0.5863 0.5290 0.5918 0.2728  0.2425  0.2623  301 SAM B C5    
8860 C C6    . SAM F .   ? 0.5773 0.5336 0.5892 0.2712  0.2397  0.2660  301 SAM B C6    
8861 N N6    . SAM F .   ? 0.5708 0.5551 0.6085 0.2721  0.2388  0.2815  301 SAM B N6    
8862 N N1    . SAM F .   ? 0.5892 0.5331 0.5838 0.2689  0.2379  0.2559  301 SAM B N1    
8863 C C2    . SAM F .   ? 0.5822 0.5013 0.5544 0.2678  0.2389  0.2423  301 SAM B C2    
8864 N N3    . SAM F .   ? 0.5906 0.4963 0.5567 0.2687  0.2419  0.2384  301 SAM B N3    
8865 C C4    . SAM F .   ? 0.6017 0.5184 0.5836 0.2713  0.2436  0.2482  301 SAM B C4    
8866 N N     . SAM G .   ? 0.6998 0.9241 0.6567 0.1409  -0.0087 -0.1326 301 SAM C N     
8867 C CA    . SAM G .   ? 0.6933 0.9125 0.6476 0.1534  -0.0168 -0.1233 301 SAM C CA    
8868 C C     . SAM G .   ? 0.7052 0.9095 0.6607 0.1628  -0.0152 -0.1192 301 SAM C C     
8869 O O     . SAM G .   ? 0.6290 0.8333 0.5898 0.1608  -0.0083 -0.1243 301 SAM C O     
8870 O OXT   . SAM G .   ? 0.7267 0.9180 0.6773 0.1726  -0.0208 -0.1106 301 SAM C OXT   
8871 C CB    . SAM G .   ? 0.6069 0.8548 0.5715 0.1592  -0.0258 -0.1232 301 SAM C CB    
8872 C CG    . SAM G .   ? 0.6012 0.8728 0.5829 0.1604  -0.0239 -0.1296 301 SAM C CG    
8873 S SD    . SAM G .   ? 0.6347 0.9399 0.6293 0.1699  -0.0357 -0.1274 301 SAM C SD    
8874 C CE    . SAM G .   ? 0.6030 0.9265 0.6165 0.1805  -0.0345 -0.1288 301 SAM C CE    
8875 C "C5'" . SAM G .   ? 0.5716 0.9051 0.5708 0.1567  -0.0385 -0.1357 301 SAM C "C5'" 
8876 C "C4'" . SAM G .   ? 0.5576 0.8911 0.5460 0.1589  -0.0474 -0.1303 301 SAM C "C4'" 
8877 O "O4'" . SAM G .   ? 0.5701 0.9180 0.5574 0.1477  -0.0487 -0.1370 301 SAM C "O4'" 
8878 C "C3'" . SAM G .   ? 0.5135 0.8654 0.5107 0.1736  -0.0577 -0.1236 301 SAM C "C3'" 
8879 O "O3'" . SAM G .   ? 0.5177 0.8500 0.5035 0.1825  -0.0616 -0.1137 301 SAM C "O3'" 
8880 C "C2'" . SAM G .   ? 0.5047 0.8856 0.5061 0.1686  -0.0652 -0.1275 301 SAM C "C2'" 
8881 O "O2'" . SAM G .   ? 0.5073 0.8912 0.5025 0.1790  -0.0756 -0.1184 301 SAM C "O2'" 
8882 C "C1'" . SAM G .   ? 0.4967 0.8699 0.4876 0.1544  -0.0612 -0.1336 301 SAM C "C1'" 
8883 N N9    . SAM G .   ? 0.4914 0.8926 0.4912 0.1439  -0.0634 -0.1427 301 SAM C N9    
8884 C C8    . SAM G .   ? 0.5285 0.9586 0.5479 0.1448  -0.0654 -0.1467 301 SAM C C8    
8885 N N7    . SAM G .   ? 0.5332 0.9836 0.5560 0.1321  -0.0676 -0.1551 301 SAM C N7    
8886 C C5    . SAM G .   ? 0.5061 0.9387 0.5099 0.1232  -0.0668 -0.1570 301 SAM C C5    
8887 C C6    . SAM G .   ? 0.5194 0.9581 0.5155 0.1087  -0.0681 -0.1651 301 SAM C C6    
8888 N N6    . SAM G .   ? 0.5635 1.0355 0.5748 0.0986  -0.0720 -0.1743 301 SAM C N6    
8889 N N1    . SAM G .   ? 0.5066 0.9209 0.4818 0.1042  -0.0658 -0.1646 301 SAM C N1    
8890 C C2    . SAM G .   ? 0.5231 0.9093 0.4861 0.1127  -0.0625 -0.1560 301 SAM C C2    
8891 N N3    . SAM G .   ? 0.5066 0.8868 0.4768 0.1253  -0.0618 -0.1483 301 SAM C N3    
8892 C C4    . SAM G .   ? 0.4885 0.8904 0.4782 0.1310  -0.0638 -0.1488 301 SAM C C4    
8893 C C2    . 4VP H .   ? 0.5507 1.0290 0.6524 0.2003  -0.0494 -0.1396 302 4VP C C2    
8894 C C3    . 4VP H .   ? 0.5746 1.0473 0.6802 0.1941  -0.0382 -0.1453 302 4VP C C3    
8895 C "C1'" . 4VP H .   ? 0.6644 1.0976 0.7515 0.1899  -0.0295 -0.1452 302 4VP C "C1'" 
8896 C "C6'" . 4VP H .   ? 0.6741 1.0786 0.7424 0.1933  -0.0335 -0.1389 302 4VP C "C6'" 
8897 C "C5'" . 4VP H .   ? 0.6372 1.0077 0.6900 0.1896  -0.0263 -0.1383 302 4VP C "C5'" 
8898 C "C4'" . 4VP H .   ? 0.6620 1.0256 0.7164 0.1827  -0.0151 -0.1441 302 4VP C "C4'" 
8899 O "O4'" . 4VP H .   ? 0.6329 0.9625 0.6712 0.1793  -0.0086 -0.1431 302 4VP C "O4'" 
8900 C "C3'" . 4VP H .   ? 0.6980 1.0892 0.7704 0.1793  -0.0105 -0.1504 302 4VP C "C3'" 
8901 C "C2'" . 4VP H .   ? 0.6911 1.1176 0.7805 0.1827  -0.0177 -0.1510 302 4VP C "C2'" 
8902 N N     . SAM I .   ? 0.9866 0.4166 0.6253 0.1223  0.3060  0.0523  301 SAM D N     
8903 C CA    . SAM I .   ? 1.0265 0.4683 0.6736 0.1354  0.2998  0.0662  301 SAM D CA    
8904 C C     . SAM I .   ? 1.0838 0.5392 0.7411 0.1432  0.2969  0.0689  301 SAM D C     
8905 O O     . SAM I .   ? 1.0486 0.4982 0.7030 0.1400  0.3030  0.0617  301 SAM D O     
8906 O OXT   . SAM I .   ? 1.0662 0.5395 0.7352 0.1524  0.2877  0.0786  301 SAM D OXT   
8907 C CB    . SAM I .   ? 0.9793 0.4087 0.6211 0.1408  0.3069  0.0748  301 SAM D CB    
8908 C CG    . SAM I .   ? 1.0421 0.4510 0.6738 0.1361  0.3205  0.0687  301 SAM D CG    
8909 S SD    . SAM I .   ? 1.1649 0.5588 0.7905 0.1436  0.3290  0.0789  301 SAM D SD    
8910 C CE    . SAM I .   ? 1.1812 0.5567 0.7995 0.1446  0.3428  0.0759  301 SAM D CE    
8911 C "C5'" . SAM I .   ? 1.0443 0.4221 0.6576 0.1337  0.3330  0.0756  301 SAM D "C5'" 
8912 C "C4'" . SAM I .   ? 0.9916 0.3833 0.6102 0.1380  0.3217  0.0836  301 SAM D "C4'" 
8913 O "O4'" . SAM I .   ? 1.0979 0.4807 0.7078 0.1290  0.3234  0.0791  301 SAM D "O4'" 
8914 C "C3'" . SAM I .   ? 0.9722 0.3655 0.5941 0.1499  0.3206  0.0969  301 SAM D "C3'" 
8915 O "O3'" . SAM I .   ? 0.9269 0.3417 0.5608 0.1572  0.3074  0.1054  301 SAM D "O3'" 
8916 C "C2'" . SAM I .   ? 1.0236 0.4009 0.6339 0.1449  0.3258  0.0972  301 SAM D "C2'" 
8917 O "O2'" . SAM I .   ? 1.1205 0.5069 0.7354 0.1540  0.3176  0.1098  301 SAM D "O2'" 
8918 C "C1'" . SAM I .   ? 1.0426 0.4194 0.6483 0.1345  0.3237  0.0892  301 SAM D "C1'" 
8919 N N9    . SAM I .   ? 1.0327 0.3886 0.6250 0.1249  0.3342  0.0835  301 SAM D N9    
8920 C C8    . SAM I .   ? 1.0961 0.4330 0.6806 0.1233  0.3463  0.0820  301 SAM D C8    
8921 N N7    . SAM I .   ? 1.0924 0.4142 0.6663 0.1129  0.3533  0.0766  301 SAM D N7    
8922 C C5    . SAM I .   ? 1.0321 0.3634 0.6066 0.1080  0.3459  0.0747  301 SAM D C5    
8923 C C6    . SAM I .   ? 1.0747 0.3987 0.6410 0.0974  0.3487  0.0696  301 SAM D C6    
8924 N N6    . SAM I .   ? 1.1225 0.4244 0.6775 0.0882  0.3620  0.0651  301 SAM D N6    
8925 N N1    . SAM I .   ? 1.0819 0.4190 0.6507 0.0957  0.3396  0.0694  301 SAM D N1    
8926 C C2    . SAM I .   ? 1.0602 0.4168 0.6392 0.1035  0.3274  0.0735  301 SAM D C2    
8927 N N3    . SAM I .   ? 1.0341 0.3988 0.6219 0.1130  0.3243  0.0783  301 SAM D N3    
8928 C C4    . SAM I .   ? 1.0230 0.3756 0.6087 0.1157  0.3336  0.0791  301 SAM D C4    
8929 O O     . HOH J .   ? 0.5811 0.2903 0.4043 0.0863  -0.1431 0.1054  401 HOH A O     
8930 O O     . HOH J .   ? 0.8042 0.3574 0.4911 0.2513  -0.0980 -0.0874 402 HOH A O     
8931 O O     . HOH J .   ? 0.6975 0.3981 0.6511 0.0486  -0.1935 0.1629  403 HOH A O     
8932 O O     . HOH J .   ? 0.8192 0.3142 0.4156 0.0838  -0.2062 -0.0016 404 HOH A O     
8933 O O     . HOH J .   ? 0.6106 0.3707 0.3330 0.1598  0.0209  -0.0921 405 HOH A O     
8934 O O     . HOH J .   ? 1.0178 0.3716 0.6088 0.2354  -0.1499 -0.0973 406 HOH A O     
8935 O O     . HOH J .   ? 0.4781 0.4519 0.3425 0.1549  0.0405  -0.1139 407 HOH A O     
8936 O O     . HOH J .   ? 0.8220 0.3114 0.3818 0.1467  -0.1274 -0.0730 408 HOH A O     
8937 O O     . HOH J .   ? 0.7670 0.2994 0.3967 0.1676  -0.1165 -0.0691 409 HOH A O     
8938 O O     . HOH J .   ? 0.6376 0.2877 0.3250 0.1070  -0.0842 0.0303  410 HOH A O     
8939 O O     . HOH J .   ? 0.4624 0.2887 0.2951 0.1276  0.0572  0.0309  411 HOH A O     
8940 O O     . HOH J .   ? 0.6528 0.3732 0.3195 0.1708  0.0347  -0.1106 412 HOH A O     
8941 O O     . HOH J .   ? 0.7725 0.3229 0.3643 0.0919  -0.1601 0.0130  413 HOH A O     
8942 O O     . HOH J .   ? 0.6806 0.3098 0.2958 0.1293  -0.0287 -0.0432 414 HOH A O     
8943 O O     . HOH K .   ? 0.6037 0.4139 0.5310 0.1932  0.0914  0.2211  401 HOH B O     
8944 O O     . HOH K .   ? 0.5895 0.5896 0.7007 0.1872  0.0018  0.3237  402 HOH B O     
8945 O O     . HOH K .   ? 0.7479 0.3310 0.4492 0.1550  0.2688  0.0214  403 HOH B O     
8946 O O     . HOH K .   ? 0.7031 0.4196 0.4179 0.1987  0.2552  0.0361  404 HOH B O     
8947 O O     . HOH K .   ? 0.6072 0.6254 0.7459 0.2291  0.0735  0.3409  405 HOH B O     
8948 O O     . HOH K .   ? 0.5946 0.4249 0.5317 0.1732  0.0346  0.2330  406 HOH B O     
8949 O O     . HOH K .   ? 0.5523 0.3662 0.3079 0.1260  0.1473  -0.0253 407 HOH B O     
8950 O O     . HOH K .   ? 0.7141 0.3902 0.4198 0.1764  0.2537  0.0152  408 HOH B O     
8951 O O     . HOH K .   ? 0.7787 0.4726 0.4504 0.2053  0.2772  0.0209  409 HOH B O     
8952 O O     . HOH K .   ? 0.6312 0.4769 0.5901 0.1924  0.0424  0.2614  410 HOH B O     
8953 O O     . HOH L .   ? 0.5039 1.4150 0.7564 0.2361  -0.1906 -0.1184 401 HOH C O     
8954 O O     . HOH M .   ? 1.1349 0.5344 0.8095 0.3223  0.4425  0.1865  401 HOH D O     
8955 O O     . HOH M .   ? 1.1559 0.6107 0.8801 0.3021  0.3617  0.2194  402 HOH D O     
8956 O O     . HOH M .   ? 0.6318 0.3085 0.3575 0.1166  0.2078  -0.0225 403 HOH D O     
8957 O O     . HOH M .   ? 1.0731 0.4240 0.6842 0.2058  0.3325  0.1720  404 HOH D O     
8958 O O     . HOH M .   ? 0.7922 0.3479 0.3946 0.1052  0.1638  0.0626  405 HOH D O     
8959 O O     . HOH M .   ? 1.0019 0.3585 0.5435 0.1212  0.3014  0.1222  406 HOH D O     
8960 O O     . HOH M .   ? 0.6001 0.3765 0.3557 0.0115  0.1850  -0.1296 407 HOH D O     
8961 O O     . HOH M .   ? 1.0383 0.3851 0.5292 0.1082  0.2959  0.1301  408 HOH D O     
8962 O O     . HOH M .   ? 0.8132 0.3871 0.4312 -0.0122 0.3083  -0.0496 409 HOH D O     
8963 O O     . HOH M .   ? 0.9400 0.4508 0.4775 0.0421  0.2742  0.0110  410 HOH D O     
8964 O O     . HOH M .   ? 0.9232 0.3888 0.3872 0.0618  0.2687  0.0469  411 HOH D O     
# 
