data_9H7Y
# 
_entry.id   9H7Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9H7Y         pdb_00009h7y 10.2210/pdb9h7y/pdb 
WWPDB D_1292142762 ?            ?                   
# 
_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       2025-06-04 
_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                        9H7Y 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              frederic.barras@pasteur.fr 
_pdbx_contact_author.name_first         Frederic 
_pdbx_contact_author.name_last          Barras 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3458-2574 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mechaly, A.E.'   1 0000-0002-5305-7495 
'Dussouchaud, M.' 2 0009-0002-4766-7411 
'Haouz, A.'       3 0000-0003-1196-1635 
'Betton, J.M.'    4 0000-0002-6523-6343 
'Barras, F.'      5 0000-0003-3458-2574 
# 
_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                     'SmsC2B2 complex from M. jannaschii (orthorhombic form)' 
_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 'Mechaly, A.E.'   1 0000-0002-5305-7495 
primary 'Dussouchaud, M.' 2 0009-0002-4766-7411 
primary 'Haouz, A.'       3 0000-0003-1196-1635 
primary 'Betton, J.M.'    4 0000-0002-6523-6343 
primary 'Barras, F.'      5 0000-0003-3458-2574 
# 
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 'Uncharacterized ABC transporter ATP-binding protein MJ0035' 28636.264 1  ? ? ? ? 
2 polymer     man 'Iron-sulfur cluster assembly SufBD family protein MJ0034'   35075.723 1  ? ? ? ? 
3 non-polymer syn 'MAGNESIUM ION'                                              24.305    1  ? ? ? ? 
4 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'                506.196   1  ? ? ? ? 
5 water       nat water                                                        18.015    17 ? ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 SmsC 
2 SmsB 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;GEFMVSIMLLKVEDLHVYRGNREILKGVNLTVEENEIHAIIGPNGAGKSTLAYTIMGISGYKPTKGRIIFKGVDIIDKNI
TERARMGMTLAWQEPARFEGIKVKNYLMLGMNEKYKKDKEIAEEKIREALKLVNLDPDKYLDRYVDETLSGGERKRIELA
SIICMEPDLAILDEPDSGIDIVSFDEIKRVFDYLKDKGCSLLVITHREELAEHADRVSLICAGEVIKSGDPKEVGEFYKK
ECGKCYKKVPDGK
;
;GEFMVSIMLLKVEDLHVYRGNREILKGVNLTVEENEIHAIIGPNGAGKSTLAYTIMGISGYKPTKGRIIFKGVDIIDKNI
TERARMGMTLAWQEPARFEGIKVKNYLMLGMNEKYKKDKEIAEEKIREALKLVNLDPDKYLDRYVDETLSGGERKRIELA
SIICMEPDLAILDEPDSGIDIVSFDEIKRVFDYLKDKGCSLLVITHREELAEHADRVSLICAGEVIKSGDPKEVGEFYKK
ECGKCYKKVPDGK
;
A ? 
2 'polypeptide(L)' no no 
;MSIKEELMEIIEAIKYTSEKPEEIVHGKGPRIIVKESRIIDVQGDEGIILEGKEEDGKIKAKIIVKKGYKFKYPIHMCFG
ITEENISQIIDVEIILEEDSSISLMSHCSFPKGKGIKHIMNGIIKIGKNAKFSYNEFHYHGMDGDILVKPTVKVEIDEGG
IYISNFTLTKGRIGTLDIEQEIIAKKDAIIDITTRTYAIKEDVVKVNEVVKLNGENAKCIIKSRGAAMDNSKISLKLKIE
GNAPYSKGHIDCAEIVKGNAEVESIPIVVVRDDKARITHEAAIGSVDKKQLETLMAKGLDEDEATEIIVKGMIGDL
;
;MSIKEELMEIIEAIKYTSEKPEEIVHGKGPRIIVKESRIIDVQGDEGIILEGKEEDGKIKAKIIVKKGYKFKYPIHMCFG
ITEENISQIIDVEIILEEDSSISLMSHCSFPKGKGIKHIMNGIIKIGKNAKFSYNEFHYHGMDGDILVKPTVKVEIDEGG
IYISNFTLTKGRIGTLDIEQEIIAKKDAIIDITTRTYAIKEDVVKVNEVVKLNGENAKCIIKSRGAAMDNSKISLKLKIE
GNAPYSKGHIDCAEIVKGNAEVESIPIVVVRDDKARITHEAAIGSVDKKQLETLMAKGLDEDEATEIIVKGMIGDL
;
B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'MAGNESIUM ION'                               MG  
4 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP 
5 water                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   GLU n 
1 3   PHE n 
1 4   MET n 
1 5   VAL n 
1 6   SER n 
1 7   ILE n 
1 8   MET n 
1 9   LEU n 
1 10  LEU n 
1 11  LYS n 
1 12  VAL n 
1 13  GLU n 
1 14  ASP n 
1 15  LEU n 
1 16  HIS n 
1 17  VAL n 
1 18  TYR n 
1 19  ARG n 
1 20  GLY n 
1 21  ASN n 
1 22  ARG n 
1 23  GLU n 
1 24  ILE n 
1 25  LEU n 
1 26  LYS n 
1 27  GLY n 
1 28  VAL n 
1 29  ASN n 
1 30  LEU n 
1 31  THR n 
1 32  VAL n 
1 33  GLU n 
1 34  GLU n 
1 35  ASN n 
1 36  GLU n 
1 37  ILE n 
1 38  HIS n 
1 39  ALA n 
1 40  ILE n 
1 41  ILE n 
1 42  GLY n 
1 43  PRO n 
1 44  ASN n 
1 45  GLY n 
1 46  ALA n 
1 47  GLY n 
1 48  LYS n 
1 49  SER n 
1 50  THR n 
1 51  LEU n 
1 52  ALA n 
1 53  TYR n 
1 54  THR n 
1 55  ILE n 
1 56  MET n 
1 57  GLY n 
1 58  ILE n 
1 59  SER n 
1 60  GLY n 
1 61  TYR n 
1 62  LYS n 
1 63  PRO n 
1 64  THR n 
1 65  LYS n 
1 66  GLY n 
1 67  ARG n 
1 68  ILE n 
1 69  ILE n 
1 70  PHE n 
1 71  LYS n 
1 72  GLY n 
1 73  VAL n 
1 74  ASP n 
1 75  ILE n 
1 76  ILE n 
1 77  ASP n 
1 78  LYS n 
1 79  ASN n 
1 80  ILE n 
1 81  THR n 
1 82  GLU n 
1 83  ARG n 
1 84  ALA n 
1 85  ARG n 
1 86  MET n 
1 87  GLY n 
1 88  MET n 
1 89  THR n 
1 90  LEU n 
1 91  ALA n 
1 92  TRP n 
1 93  GLN n 
1 94  GLU n 
1 95  PRO n 
1 96  ALA n 
1 97  ARG n 
1 98  PHE n 
1 99  GLU n 
1 100 GLY n 
1 101 ILE n 
1 102 LYS n 
1 103 VAL n 
1 104 LYS n 
1 105 ASN n 
1 106 TYR n 
1 107 LEU n 
1 108 MET n 
1 109 LEU n 
1 110 GLY n 
1 111 MET n 
1 112 ASN n 
1 113 GLU n 
1 114 LYS n 
1 115 TYR n 
1 116 LYS n 
1 117 LYS n 
1 118 ASP n 
1 119 LYS n 
1 120 GLU n 
1 121 ILE n 
1 122 ALA n 
1 123 GLU n 
1 124 GLU n 
1 125 LYS n 
1 126 ILE n 
1 127 ARG n 
1 128 GLU n 
1 129 ALA n 
1 130 LEU n 
1 131 LYS n 
1 132 LEU n 
1 133 VAL n 
1 134 ASN n 
1 135 LEU n 
1 136 ASP n 
1 137 PRO n 
1 138 ASP n 
1 139 LYS n 
1 140 TYR n 
1 141 LEU n 
1 142 ASP n 
1 143 ARG n 
1 144 TYR n 
1 145 VAL n 
1 146 ASP n 
1 147 GLU n 
1 148 THR n 
1 149 LEU n 
1 150 SER n 
1 151 GLY n 
1 152 GLY n 
1 153 GLU n 
1 154 ARG n 
1 155 LYS n 
1 156 ARG n 
1 157 ILE n 
1 158 GLU n 
1 159 LEU n 
1 160 ALA n 
1 161 SER n 
1 162 ILE n 
1 163 ILE n 
1 164 CYS n 
1 165 MET n 
1 166 GLU n 
1 167 PRO n 
1 168 ASP n 
1 169 LEU n 
1 170 ALA n 
1 171 ILE n 
1 172 LEU n 
1 173 ASP n 
1 174 GLU n 
1 175 PRO n 
1 176 ASP n 
1 177 SER n 
1 178 GLY n 
1 179 ILE n 
1 180 ASP n 
1 181 ILE n 
1 182 VAL n 
1 183 SER n 
1 184 PHE n 
1 185 ASP n 
1 186 GLU n 
1 187 ILE n 
1 188 LYS n 
1 189 ARG n 
1 190 VAL n 
1 191 PHE n 
1 192 ASP n 
1 193 TYR n 
1 194 LEU n 
1 195 LYS n 
1 196 ASP n 
1 197 LYS n 
1 198 GLY n 
1 199 CYS n 
1 200 SER n 
1 201 LEU n 
1 202 LEU n 
1 203 VAL n 
1 204 ILE n 
1 205 THR n 
1 206 HIS n 
1 207 ARG n 
1 208 GLU n 
1 209 GLU n 
1 210 LEU n 
1 211 ALA n 
1 212 GLU n 
1 213 HIS n 
1 214 ALA n 
1 215 ASP n 
1 216 ARG n 
1 217 VAL n 
1 218 SER n 
1 219 LEU n 
1 220 ILE n 
1 221 CYS n 
1 222 ALA n 
1 223 GLY n 
1 224 GLU n 
1 225 VAL n 
1 226 ILE n 
1 227 LYS n 
1 228 SER n 
1 229 GLY n 
1 230 ASP n 
1 231 PRO n 
1 232 LYS n 
1 233 GLU n 
1 234 VAL n 
1 235 GLY n 
1 236 GLU n 
1 237 PHE n 
1 238 TYR n 
1 239 LYS n 
1 240 LYS n 
1 241 GLU n 
1 242 CYS n 
1 243 GLY n 
1 244 LYS n 
1 245 CYS n 
1 246 TYR n 
1 247 LYS n 
1 248 LYS n 
1 249 VAL n 
1 250 PRO n 
1 251 ASP n 
1 252 GLY n 
1 253 LYS n 
2 1   MET n 
2 2   SER n 
2 3   ILE n 
2 4   LYS n 
2 5   GLU n 
2 6   GLU n 
2 7   LEU n 
2 8   MET n 
2 9   GLU n 
2 10  ILE n 
2 11  ILE n 
2 12  GLU n 
2 13  ALA n 
2 14  ILE n 
2 15  LYS n 
2 16  TYR n 
2 17  THR n 
2 18  SER n 
2 19  GLU n 
2 20  LYS n 
2 21  PRO n 
2 22  GLU n 
2 23  GLU n 
2 24  ILE n 
2 25  VAL n 
2 26  HIS n 
2 27  GLY n 
2 28  LYS n 
2 29  GLY n 
2 30  PRO n 
2 31  ARG n 
2 32  ILE n 
2 33  ILE n 
2 34  VAL n 
2 35  LYS n 
2 36  GLU n 
2 37  SER n 
2 38  ARG n 
2 39  ILE n 
2 40  ILE n 
2 41  ASP n 
2 42  VAL n 
2 43  GLN n 
2 44  GLY n 
2 45  ASP n 
2 46  GLU n 
2 47  GLY n 
2 48  ILE n 
2 49  ILE n 
2 50  LEU n 
2 51  GLU n 
2 52  GLY n 
2 53  LYS n 
2 54  GLU n 
2 55  GLU n 
2 56  ASP n 
2 57  GLY n 
2 58  LYS n 
2 59  ILE n 
2 60  LYS n 
2 61  ALA n 
2 62  LYS n 
2 63  ILE n 
2 64  ILE n 
2 65  VAL n 
2 66  LYS n 
2 67  LYS n 
2 68  GLY n 
2 69  TYR n 
2 70  LYS n 
2 71  PHE n 
2 72  LYS n 
2 73  TYR n 
2 74  PRO n 
2 75  ILE n 
2 76  HIS n 
2 77  MET n 
2 78  CYS n 
2 79  PHE n 
2 80  GLY n 
2 81  ILE n 
2 82  THR n 
2 83  GLU n 
2 84  GLU n 
2 85  ASN n 
2 86  ILE n 
2 87  SER n 
2 88  GLN n 
2 89  ILE n 
2 90  ILE n 
2 91  ASP n 
2 92  VAL n 
2 93  GLU n 
2 94  ILE n 
2 95  ILE n 
2 96  LEU n 
2 97  GLU n 
2 98  GLU n 
2 99  ASP n 
2 100 SER n 
2 101 SER n 
2 102 ILE n 
2 103 SER n 
2 104 LEU n 
2 105 MET n 
2 106 SER n 
2 107 HIS n 
2 108 CYS n 
2 109 SER n 
2 110 PHE n 
2 111 PRO n 
2 112 LYS n 
2 113 GLY n 
2 114 LYS n 
2 115 GLY n 
2 116 ILE n 
2 117 LYS n 
2 118 HIS n 
2 119 ILE n 
2 120 MET n 
2 121 ASN n 
2 122 GLY n 
2 123 ILE n 
2 124 ILE n 
2 125 LYS n 
2 126 ILE n 
2 127 GLY n 
2 128 LYS n 
2 129 ASN n 
2 130 ALA n 
2 131 LYS n 
2 132 PHE n 
2 133 SER n 
2 134 TYR n 
2 135 ASN n 
2 136 GLU n 
2 137 PHE n 
2 138 HIS n 
2 139 TYR n 
2 140 HIS n 
2 141 GLY n 
2 142 MET n 
2 143 ASP n 
2 144 GLY n 
2 145 ASP n 
2 146 ILE n 
2 147 LEU n 
2 148 VAL n 
2 149 LYS n 
2 150 PRO n 
2 151 THR n 
2 152 VAL n 
2 153 LYS n 
2 154 VAL n 
2 155 GLU n 
2 156 ILE n 
2 157 ASP n 
2 158 GLU n 
2 159 GLY n 
2 160 GLY n 
2 161 ILE n 
2 162 TYR n 
2 163 ILE n 
2 164 SER n 
2 165 ASN n 
2 166 PHE n 
2 167 THR n 
2 168 LEU n 
2 169 THR n 
2 170 LYS n 
2 171 GLY n 
2 172 ARG n 
2 173 ILE n 
2 174 GLY n 
2 175 THR n 
2 176 LEU n 
2 177 ASP n 
2 178 ILE n 
2 179 GLU n 
2 180 GLN n 
2 181 GLU n 
2 182 ILE n 
2 183 ILE n 
2 184 ALA n 
2 185 LYS n 
2 186 LYS n 
2 187 ASP n 
2 188 ALA n 
2 189 ILE n 
2 190 ILE n 
2 191 ASP n 
2 192 ILE n 
2 193 THR n 
2 194 THR n 
2 195 ARG n 
2 196 THR n 
2 197 TYR n 
2 198 ALA n 
2 199 ILE n 
2 200 LYS n 
2 201 GLU n 
2 202 ASP n 
2 203 VAL n 
2 204 VAL n 
2 205 LYS n 
2 206 VAL n 
2 207 ASN n 
2 208 GLU n 
2 209 VAL n 
2 210 VAL n 
2 211 LYS n 
2 212 LEU n 
2 213 ASN n 
2 214 GLY n 
2 215 GLU n 
2 216 ASN n 
2 217 ALA n 
2 218 LYS n 
2 219 CYS n 
2 220 ILE n 
2 221 ILE n 
2 222 LYS n 
2 223 SER n 
2 224 ARG n 
2 225 GLY n 
2 226 ALA n 
2 227 ALA n 
2 228 MET n 
2 229 ASP n 
2 230 ASN n 
2 231 SER n 
2 232 LYS n 
2 233 ILE n 
2 234 SER n 
2 235 LEU n 
2 236 LYS n 
2 237 LEU n 
2 238 LYS n 
2 239 ILE n 
2 240 GLU n 
2 241 GLY n 
2 242 ASN n 
2 243 ALA n 
2 244 PRO n 
2 245 TYR n 
2 246 SER n 
2 247 LYS n 
2 248 GLY n 
2 249 HIS n 
2 250 ILE n 
2 251 ASP n 
2 252 CYS n 
2 253 ALA n 
2 254 GLU n 
2 255 ILE n 
2 256 VAL n 
2 257 LYS n 
2 258 GLY n 
2 259 ASN n 
2 260 ALA n 
2 261 GLU n 
2 262 VAL n 
2 263 GLU n 
2 264 SER n 
2 265 ILE n 
2 266 PRO n 
2 267 ILE n 
2 268 VAL n 
2 269 VAL n 
2 270 VAL n 
2 271 ARG n 
2 272 ASP n 
2 273 ASP n 
2 274 LYS n 
2 275 ALA n 
2 276 ARG n 
2 277 ILE n 
2 278 THR n 
2 279 HIS n 
2 280 GLU n 
2 281 ALA n 
2 282 ALA n 
2 283 ILE n 
2 284 GLY n 
2 285 SER n 
2 286 VAL n 
2 287 ASP n 
2 288 LYS n 
2 289 LYS n 
2 290 GLN n 
2 291 LEU n 
2 292 GLU n 
2 293 THR n 
2 294 LEU n 
2 295 MET n 
2 296 ALA n 
2 297 LYS n 
2 298 GLY n 
2 299 LEU n 
2 300 ASP n 
2 301 GLU n 
2 302 ASP n 
2 303 GLU n 
2 304 ALA n 
2 305 THR n 
2 306 GLU n 
2 307 ILE n 
2 308 ILE n 
2 309 VAL n 
2 310 LYS n 
2 311 GLY n 
2 312 MET n 
2 313 ILE n 
2 314 GLY n 
2 315 ASP n 
2 316 LEU n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_entity_src_gen.pdbx_gene_src_gene 
_entity_src_gen.gene_src_species 
_entity_src_gen.gene_src_strain 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_entity_src_gen.pdbx_gene_src_variant 
_entity_src_gen.pdbx_gene_src_cell_line 
_entity_src_gen.pdbx_gene_src_atcc 
_entity_src_gen.pdbx_gene_src_organ 
_entity_src_gen.pdbx_gene_src_organelle 
_entity_src_gen.pdbx_gene_src_cell 
_entity_src_gen.pdbx_gene_src_cellular_location 
_entity_src_gen.host_org_common_name 
_entity_src_gen.pdbx_host_org_scientific_name 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_entity_src_gen.host_org_genus 
_entity_src_gen.pdbx_host_org_gene 
_entity_src_gen.pdbx_host_org_organ 
_entity_src_gen.host_org_species 
_entity_src_gen.pdbx_host_org_tissue 
_entity_src_gen.pdbx_host_org_tissue_fraction 
_entity_src_gen.pdbx_host_org_strain 
_entity_src_gen.pdbx_host_org_variant 
_entity_src_gen.pdbx_host_org_cell_line 
_entity_src_gen.pdbx_host_org_atcc 
_entity_src_gen.pdbx_host_org_culture_collection 
_entity_src_gen.pdbx_host_org_cell 
_entity_src_gen.pdbx_host_org_organelle 
_entity_src_gen.pdbx_host_org_cellular_location 
_entity_src_gen.pdbx_host_org_vector_type 
_entity_src_gen.pdbx_host_org_vector 
_entity_src_gen.host_org_details 
_entity_src_gen.expression_system_id 
_entity_src_gen.plasmid_name 
_entity_src_gen.plasmid_details 
_entity_src_gen.pdbx_description 
1 1 sample 'Biological sequence' 1 253 ? ? MJ0035 ? ? ? ? ? ? 'Methanocaldococcus jannaschii' 2190 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 316 ? ? MJ0034 ? ? ? ? ? ? 'Methanocaldococcus jannaschii' 2190 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                       ? 'C3 H7 N O2'        89.093  
ANP non-polymer         . 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ? 'C10 H17 N6 O12 P3' 506.196 
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 
MG  non-polymer         . 'MAGNESIUM ION'                               ? 'Mg 2'              24.305  
PHE 'L-peptide linking' y PHENYLALANINE                                 ? 'C9 H11 N O2'       165.189 
PRO 'L-peptide linking' y PROLINE                                       ? 'C5 H9 N O2'        115.130 
SER 'L-peptide linking' y SERINE                                        ? 'C3 H7 N O3'        105.093 
THR 'L-peptide linking' y THREONINE                                     ? 'C4 H9 N O3'        119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                    ? 'C11 H12 N2 O2'     204.225 
TYR 'L-peptide linking' y TYROSINE                                      ? 'C9 H11 N O3'       181.189 
VAL 'L-peptide linking' y VALINE                                        ? 'C5 H11 N O2'       117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   -2  -2  GLY GLY A . n 
A 1 2   GLU 2   -1  -1  GLU GLU A . n 
A 1 3   PHE 3   0   0   PHE PHE A . n 
A 1 4   MET 4   1   1   MET MET A . n 
A 1 5   VAL 5   2   2   VAL VAL A . n 
A 1 6   SER 6   3   3   SER SER A . n 
A 1 7   ILE 7   4   4   ILE ILE A . n 
A 1 8   MET 8   5   5   MET MET A . n 
A 1 9   LEU 9   6   6   LEU LEU A . n 
A 1 10  LEU 10  7   7   LEU LEU A . n 
A 1 11  LYS 11  8   8   LYS LYS A . n 
A 1 12  VAL 12  9   9   VAL VAL A . n 
A 1 13  GLU 13  10  10  GLU GLU A . n 
A 1 14  ASP 14  11  11  ASP ASP A . n 
A 1 15  LEU 15  12  12  LEU LEU A . n 
A 1 16  HIS 16  13  13  HIS HIS A . n 
A 1 17  VAL 17  14  14  VAL VAL A . n 
A 1 18  TYR 18  15  15  TYR TYR A . n 
A 1 19  ARG 19  16  16  ARG ARG A . n 
A 1 20  GLY 20  17  17  GLY GLY A . n 
A 1 21  ASN 21  18  18  ASN ASN A . n 
A 1 22  ARG 22  19  19  ARG ARG A . n 
A 1 23  GLU 23  20  20  GLU GLU A . n 
A 1 24  ILE 24  21  21  ILE ILE A . n 
A 1 25  LEU 25  22  22  LEU LEU A . n 
A 1 26  LYS 26  23  23  LYS LYS A . n 
A 1 27  GLY 27  24  24  GLY GLY A . n 
A 1 28  VAL 28  25  25  VAL VAL A . n 
A 1 29  ASN 29  26  26  ASN ASN A . n 
A 1 30  LEU 30  27  27  LEU LEU A . n 
A 1 31  THR 31  28  28  THR THR A . n 
A 1 32  VAL 32  29  29  VAL VAL A . n 
A 1 33  GLU 33  30  30  GLU GLU A . n 
A 1 34  GLU 34  31  31  GLU GLU A . n 
A 1 35  ASN 35  32  32  ASN ASN A . n 
A 1 36  GLU 36  33  33  GLU GLU A . n 
A 1 37  ILE 37  34  34  ILE ILE A . n 
A 1 38  HIS 38  35  35  HIS HIS A . n 
A 1 39  ALA 39  36  36  ALA ALA A . n 
A 1 40  ILE 40  37  37  ILE ILE A . n 
A 1 41  ILE 41  38  38  ILE ILE A . n 
A 1 42  GLY 42  39  39  GLY GLY A . n 
A 1 43  PRO 43  40  40  PRO PRO A . n 
A 1 44  ASN 44  41  41  ASN ASN A . n 
A 1 45  GLY 45  42  42  GLY GLY A . n 
A 1 46  ALA 46  43  43  ALA ALA A . n 
A 1 47  GLY 47  44  44  GLY GLY A . n 
A 1 48  LYS 48  45  45  LYS LYS A . n 
A 1 49  SER 49  46  46  SER SER A . n 
A 1 50  THR 50  47  47  THR THR A . n 
A 1 51  LEU 51  48  48  LEU LEU A . n 
A 1 52  ALA 52  49  49  ALA ALA A . n 
A 1 53  TYR 53  50  50  TYR TYR A . n 
A 1 54  THR 54  51  51  THR THR A . n 
A 1 55  ILE 55  52  52  ILE ILE A . n 
A 1 56  MET 56  53  53  MET MET A . n 
A 1 57  GLY 57  54  54  GLY GLY A . n 
A 1 58  ILE 58  55  55  ILE ILE A . n 
A 1 59  SER 59  56  56  SER SER A . n 
A 1 60  GLY 60  57  57  GLY GLY A . n 
A 1 61  TYR 61  58  58  TYR TYR A . n 
A 1 62  LYS 62  59  59  LYS LYS A . n 
A 1 63  PRO 63  60  60  PRO PRO A . n 
A 1 64  THR 64  61  61  THR THR A . n 
A 1 65  LYS 65  62  62  LYS LYS A . n 
A 1 66  GLY 66  63  63  GLY GLY A . n 
A 1 67  ARG 67  64  64  ARG ARG A . n 
A 1 68  ILE 68  65  65  ILE ILE A . n 
A 1 69  ILE 69  66  66  ILE ILE A . n 
A 1 70  PHE 70  67  67  PHE PHE A . n 
A 1 71  LYS 71  68  68  LYS LYS A . n 
A 1 72  GLY 72  69  69  GLY GLY A . n 
A 1 73  VAL 73  70  70  VAL VAL A . n 
A 1 74  ASP 74  71  71  ASP ASP A . n 
A 1 75  ILE 75  72  72  ILE ILE A . n 
A 1 76  ILE 76  73  73  ILE ILE A . n 
A 1 77  ASP 77  74  74  ASP ASP A . n 
A 1 78  LYS 78  75  75  LYS LYS A . n 
A 1 79  ASN 79  76  76  ASN ASN A . n 
A 1 80  ILE 80  77  77  ILE ILE A . n 
A 1 81  THR 81  78  78  THR THR A . n 
A 1 82  GLU 82  79  79  GLU GLU A . n 
A 1 83  ARG 83  80  80  ARG ARG A . n 
A 1 84  ALA 84  81  81  ALA ALA A . n 
A 1 85  ARG 85  82  82  ARG ARG A . n 
A 1 86  MET 86  83  83  MET MET A . n 
A 1 87  GLY 87  84  84  GLY GLY A . n 
A 1 88  MET 88  85  85  MET MET A . n 
A 1 89  THR 89  86  86  THR THR A . n 
A 1 90  LEU 90  87  87  LEU LEU A . n 
A 1 91  ALA 91  88  88  ALA ALA A . n 
A 1 92  TRP 92  89  89  TRP TRP A . n 
A 1 93  GLN 93  90  90  GLN GLN A . n 
A 1 94  GLU 94  91  91  GLU GLU A . n 
A 1 95  PRO 95  92  92  PRO PRO A . n 
A 1 96  ALA 96  93  93  ALA ALA A . n 
A 1 97  ARG 97  94  94  ARG ARG A . n 
A 1 98  PHE 98  95  95  PHE PHE A . n 
A 1 99  GLU 99  96  96  GLU GLU A . n 
A 1 100 GLY 100 97  97  GLY GLY A . n 
A 1 101 ILE 101 98  98  ILE ILE A . n 
A 1 102 LYS 102 99  99  LYS LYS A . n 
A 1 103 VAL 103 100 100 VAL VAL A . n 
A 1 104 LYS 104 101 101 LYS LYS A . n 
A 1 105 ASN 105 102 102 ASN ASN A . n 
A 1 106 TYR 106 103 103 TYR TYR A . n 
A 1 107 LEU 107 104 104 LEU LEU A . n 
A 1 108 MET 108 105 105 MET MET A . n 
A 1 109 LEU 109 106 106 LEU LEU A . n 
A 1 110 GLY 110 107 107 GLY GLY A . n 
A 1 111 MET 111 108 108 MET MET A . n 
A 1 112 ASN 112 109 109 ASN ASN A . n 
A 1 113 GLU 113 110 110 GLU GLU A . n 
A 1 114 LYS 114 111 111 LYS LYS A . n 
A 1 115 TYR 115 112 112 TYR TYR A . n 
A 1 116 LYS 116 113 113 LYS LYS A . n 
A 1 117 LYS 117 114 114 LYS LYS A . n 
A 1 118 ASP 118 115 115 ASP ASP A . n 
A 1 119 LYS 119 116 116 LYS LYS A . n 
A 1 120 GLU 120 117 117 GLU GLU A . n 
A 1 121 ILE 121 118 118 ILE ILE A . n 
A 1 122 ALA 122 119 119 ALA ALA A . n 
A 1 123 GLU 123 120 120 GLU GLU A . n 
A 1 124 GLU 124 121 121 GLU GLU A . n 
A 1 125 LYS 125 122 122 LYS LYS A . n 
A 1 126 ILE 126 123 123 ILE ILE A . n 
A 1 127 ARG 127 124 124 ARG ARG A . n 
A 1 128 GLU 128 125 125 GLU GLU A . n 
A 1 129 ALA 129 126 126 ALA ALA A . n 
A 1 130 LEU 130 127 127 LEU LEU A . n 
A 1 131 LYS 131 128 128 LYS LYS A . n 
A 1 132 LEU 132 129 129 LEU LEU A . n 
A 1 133 VAL 133 130 130 VAL VAL A . n 
A 1 134 ASN 134 131 131 ASN ASN A . n 
A 1 135 LEU 135 132 132 LEU LEU A . n 
A 1 136 ASP 136 133 133 ASP ASP A . n 
A 1 137 PRO 137 134 134 PRO PRO A . n 
A 1 138 ASP 138 135 135 ASP ASP A . n 
A 1 139 LYS 139 136 136 LYS LYS A . n 
A 1 140 TYR 140 137 137 TYR TYR A . n 
A 1 141 LEU 141 138 138 LEU LEU A . n 
A 1 142 ASP 142 139 139 ASP ASP A . n 
A 1 143 ARG 143 140 140 ARG ARG A . n 
A 1 144 TYR 144 141 141 TYR TYR A . n 
A 1 145 VAL 145 142 142 VAL VAL A . n 
A 1 146 ASP 146 143 143 ASP ASP A . n 
A 1 147 GLU 147 144 144 GLU GLU A . n 
A 1 148 THR 148 145 145 THR THR A . n 
A 1 149 LEU 149 146 146 LEU LEU A . n 
A 1 150 SER 150 147 147 SER SER A . n 
A 1 151 GLY 151 148 148 GLY GLY A . n 
A 1 152 GLY 152 149 149 GLY GLY A . n 
A 1 153 GLU 153 150 150 GLU GLU A . n 
A 1 154 ARG 154 151 151 ARG ARG A . n 
A 1 155 LYS 155 152 152 LYS LYS A . n 
A 1 156 ARG 156 153 153 ARG ARG A . n 
A 1 157 ILE 157 154 154 ILE ILE A . n 
A 1 158 GLU 158 155 155 GLU GLU A . n 
A 1 159 LEU 159 156 156 LEU LEU A . n 
A 1 160 ALA 160 157 157 ALA ALA A . n 
A 1 161 SER 161 158 158 SER SER A . n 
A 1 162 ILE 162 159 159 ILE ILE A . n 
A 1 163 ILE 163 160 160 ILE ILE A . n 
A 1 164 CYS 164 161 161 CYS CYS A . n 
A 1 165 MET 165 162 162 MET MET A . n 
A 1 166 GLU 166 163 163 GLU GLU A . n 
A 1 167 PRO 167 164 164 PRO PRO A . n 
A 1 168 ASP 168 165 165 ASP ASP A . n 
A 1 169 LEU 169 166 166 LEU LEU A . n 
A 1 170 ALA 170 167 167 ALA ALA A . n 
A 1 171 ILE 171 168 168 ILE ILE A . n 
A 1 172 LEU 172 169 169 LEU LEU A . n 
A 1 173 ASP 173 170 170 ASP ASP A . n 
A 1 174 GLU 174 171 171 GLU GLU A . n 
A 1 175 PRO 175 172 172 PRO PRO A . n 
A 1 176 ASP 176 173 173 ASP ASP A . n 
A 1 177 SER 177 174 174 SER SER A . n 
A 1 178 GLY 178 175 175 GLY GLY A . n 
A 1 179 ILE 179 176 176 ILE ILE A . n 
A 1 180 ASP 180 177 177 ASP ASP A . n 
A 1 181 ILE 181 178 178 ILE ILE A . n 
A 1 182 VAL 182 179 179 VAL VAL A . n 
A 1 183 SER 183 180 180 SER SER A . n 
A 1 184 PHE 184 181 181 PHE PHE A . n 
A 1 185 ASP 185 182 182 ASP ASP A . n 
A 1 186 GLU 186 183 183 GLU GLU A . n 
A 1 187 ILE 187 184 184 ILE ILE A . n 
A 1 188 LYS 188 185 185 LYS LYS A . n 
A 1 189 ARG 189 186 186 ARG ARG A . n 
A 1 190 VAL 190 187 187 VAL VAL A . n 
A 1 191 PHE 191 188 188 PHE PHE A . n 
A 1 192 ASP 192 189 189 ASP ASP A . n 
A 1 193 TYR 193 190 190 TYR TYR A . n 
A 1 194 LEU 194 191 191 LEU LEU A . n 
A 1 195 LYS 195 192 192 LYS LYS A . n 
A 1 196 ASP 196 193 193 ASP ASP A . n 
A 1 197 LYS 197 194 194 LYS LYS A . n 
A 1 198 GLY 198 195 195 GLY GLY A . n 
A 1 199 CYS 199 196 196 CYS CYS A . n 
A 1 200 SER 200 197 197 SER SER A . n 
A 1 201 LEU 201 198 198 LEU LEU A . n 
A 1 202 LEU 202 199 199 LEU LEU A . n 
A 1 203 VAL 203 200 200 VAL VAL A . n 
A 1 204 ILE 204 201 201 ILE ILE A . n 
A 1 205 THR 205 202 202 THR THR A . n 
A 1 206 HIS 206 203 203 HIS HIS A . n 
A 1 207 ARG 207 204 204 ARG ARG A . n 
A 1 208 GLU 208 205 205 GLU GLU A . n 
A 1 209 GLU 209 206 206 GLU GLU A . n 
A 1 210 LEU 210 207 207 LEU LEU A . n 
A 1 211 ALA 211 208 208 ALA ALA A . n 
A 1 212 GLU 212 209 209 GLU GLU A . n 
A 1 213 HIS 213 210 210 HIS HIS A . n 
A 1 214 ALA 214 211 211 ALA ALA A . n 
A 1 215 ASP 215 212 212 ASP ASP A . n 
A 1 216 ARG 216 213 213 ARG ARG A . n 
A 1 217 VAL 217 214 214 VAL VAL A . n 
A 1 218 SER 218 215 215 SER SER A . n 
A 1 219 LEU 219 216 216 LEU LEU A . n 
A 1 220 ILE 220 217 217 ILE ILE A . n 
A 1 221 CYS 221 218 218 CYS CYS A . n 
A 1 222 ALA 222 219 219 ALA ALA A . n 
A 1 223 GLY 223 220 220 GLY GLY A . n 
A 1 224 GLU 224 221 221 GLU GLU A . n 
A 1 225 VAL 225 222 222 VAL VAL A . n 
A 1 226 ILE 226 223 223 ILE ILE A . n 
A 1 227 LYS 227 224 224 LYS LYS A . n 
A 1 228 SER 228 225 225 SER SER A . n 
A 1 229 GLY 229 226 226 GLY GLY A . n 
A 1 230 ASP 230 227 227 ASP ASP A . n 
A 1 231 PRO 231 228 228 PRO PRO A . n 
A 1 232 LYS 232 229 229 LYS LYS A . n 
A 1 233 GLU 233 230 230 GLU GLU A . n 
A 1 234 VAL 234 231 231 VAL VAL A . n 
A 1 235 GLY 235 232 232 GLY GLY A . n 
A 1 236 GLU 236 233 233 GLU GLU A . n 
A 1 237 PHE 237 234 234 PHE PHE A . n 
A 1 238 TYR 238 235 235 TYR TYR A . n 
A 1 239 LYS 239 236 236 LYS LYS A . n 
A 1 240 LYS 240 237 237 LYS LYS A . n 
A 1 241 GLU 241 238 238 GLU GLU A . n 
A 1 242 CYS 242 239 239 CYS CYS A . n 
A 1 243 GLY 243 240 ?   ?   ?   A . n 
A 1 244 LYS 244 241 ?   ?   ?   A . n 
A 1 245 CYS 245 242 ?   ?   ?   A . n 
A 1 246 TYR 246 243 ?   ?   ?   A . n 
A 1 247 LYS 247 244 ?   ?   ?   A . n 
A 1 248 LYS 248 245 ?   ?   ?   A . n 
A 1 249 VAL 249 246 ?   ?   ?   A . n 
A 1 250 PRO 250 247 ?   ?   ?   A . n 
A 1 251 ASP 251 248 ?   ?   ?   A . n 
A 1 252 GLY 252 249 ?   ?   ?   A . n 
A 1 253 LYS 253 250 ?   ?   ?   A . n 
B 2 1   MET 1   1   ?   ?   ?   B . n 
B 2 2   SER 2   2   ?   ?   ?   B . n 
B 2 3   ILE 3   3   ?   ?   ?   B . n 
B 2 4   LYS 4   4   ?   ?   ?   B . n 
B 2 5   GLU 5   5   ?   ?   ?   B . n 
B 2 6   GLU 6   6   ?   ?   ?   B . n 
B 2 7   LEU 7   7   ?   ?   ?   B . n 
B 2 8   MET 8   8   ?   ?   ?   B . n 
B 2 9   GLU 9   9   ?   ?   ?   B . n 
B 2 10  ILE 10  10  ?   ?   ?   B . n 
B 2 11  ILE 11  11  ?   ?   ?   B . n 
B 2 12  GLU 12  12  ?   ?   ?   B . n 
B 2 13  ALA 13  13  ?   ?   ?   B . n 
B 2 14  ILE 14  14  ?   ?   ?   B . n 
B 2 15  LYS 15  15  ?   ?   ?   B . n 
B 2 16  TYR 16  16  ?   ?   ?   B . n 
B 2 17  THR 17  17  ?   ?   ?   B . n 
B 2 18  SER 18  18  ?   ?   ?   B . n 
B 2 19  GLU 19  19  ?   ?   ?   B . n 
B 2 20  LYS 20  20  ?   ?   ?   B . n 
B 2 21  PRO 21  21  ?   ?   ?   B . n 
B 2 22  GLU 22  22  ?   ?   ?   B . n 
B 2 23  GLU 23  23  ?   ?   ?   B . n 
B 2 24  ILE 24  24  ?   ?   ?   B . n 
B 2 25  VAL 25  25  ?   ?   ?   B . n 
B 2 26  HIS 26  26  ?   ?   ?   B . n 
B 2 27  GLY 27  27  ?   ?   ?   B . n 
B 2 28  LYS 28  28  28  LYS LYS B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  PRO 30  30  30  PRO PRO B . n 
B 2 31  ARG 31  31  31  ARG ARG B . n 
B 2 32  ILE 32  32  32  ILE ILE B . n 
B 2 33  ILE 33  33  33  ILE ILE B . n 
B 2 34  VAL 34  34  34  VAL VAL B . n 
B 2 35  LYS 35  35  35  LYS LYS B . n 
B 2 36  GLU 36  36  36  GLU GLU B . n 
B 2 37  SER 37  37  37  SER SER B . n 
B 2 38  ARG 38  38  38  ARG ARG B . n 
B 2 39  ILE 39  39  39  ILE ILE B . n 
B 2 40  ILE 40  40  40  ILE ILE B . n 
B 2 41  ASP 41  41  41  ASP ASP B . n 
B 2 42  VAL 42  42  42  VAL VAL B . n 
B 2 43  GLN 43  43  43  GLN GLN B . n 
B 2 44  GLY 44  44  44  GLY GLY B . n 
B 2 45  ASP 45  45  45  ASP ASP B . n 
B 2 46  GLU 46  46  46  GLU GLU B . n 
B 2 47  GLY 47  47  47  GLY GLY B . n 
B 2 48  ILE 48  48  48  ILE ILE B . n 
B 2 49  ILE 49  49  49  ILE ILE B . n 
B 2 50  LEU 50  50  50  LEU LEU B . n 
B 2 51  GLU 51  51  51  GLU GLU B . n 
B 2 52  GLY 52  52  52  GLY GLY B . n 
B 2 53  LYS 53  53  53  LYS LYS B . n 
B 2 54  GLU 54  54  54  GLU GLU B . n 
B 2 55  GLU 55  55  55  GLU GLU B . n 
B 2 56  ASP 56  56  56  ASP ASP B . n 
B 2 57  GLY 57  57  57  GLY GLY B . n 
B 2 58  LYS 58  58  58  LYS LYS B . n 
B 2 59  ILE 59  59  59  ILE ILE B . n 
B 2 60  LYS 60  60  60  LYS LYS B . n 
B 2 61  ALA 61  61  61  ALA ALA B . n 
B 2 62  LYS 62  62  62  LYS LYS B . n 
B 2 63  ILE 63  63  63  ILE ILE B . n 
B 2 64  ILE 64  64  64  ILE ILE B . n 
B 2 65  VAL 65  65  65  VAL VAL B . n 
B 2 66  LYS 66  66  66  LYS LYS B . n 
B 2 67  LYS 67  67  67  LYS LYS B . n 
B 2 68  GLY 68  68  68  GLY GLY B . n 
B 2 69  TYR 69  69  69  TYR TYR B . n 
B 2 70  LYS 70  70  70  LYS LYS B . n 
B 2 71  PHE 71  71  71  PHE PHE B . n 
B 2 72  LYS 72  72  72  LYS LYS B . n 
B 2 73  TYR 73  73  73  TYR TYR B . n 
B 2 74  PRO 74  74  74  PRO PRO B . n 
B 2 75  ILE 75  75  75  ILE ILE B . n 
B 2 76  HIS 76  76  76  HIS HIS B . n 
B 2 77  MET 77  77  77  MET MET B . n 
B 2 78  CYS 78  78  78  CYS CYS B . n 
B 2 79  PHE 79  79  79  PHE PHE B . n 
B 2 80  GLY 80  80  80  GLY GLY B . n 
B 2 81  ILE 81  81  81  ILE ILE B . n 
B 2 82  THR 82  82  82  THR THR B . n 
B 2 83  GLU 83  83  83  GLU GLU B . n 
B 2 84  GLU 84  84  84  GLU GLU B . n 
B 2 85  ASN 85  85  85  ASN ASN B . n 
B 2 86  ILE 86  86  86  ILE ILE B . n 
B 2 87  SER 87  87  87  SER SER B . n 
B 2 88  GLN 88  88  88  GLN GLN B . n 
B 2 89  ILE 89  89  89  ILE ILE B . n 
B 2 90  ILE 90  90  90  ILE ILE B . n 
B 2 91  ASP 91  91  91  ASP ASP B . n 
B 2 92  VAL 92  92  92  VAL VAL B . n 
B 2 93  GLU 93  93  93  GLU GLU B . n 
B 2 94  ILE 94  94  94  ILE ILE B . n 
B 2 95  ILE 95  95  95  ILE ILE B . n 
B 2 96  LEU 96  96  96  LEU LEU B . n 
B 2 97  GLU 97  97  97  GLU GLU B . n 
B 2 98  GLU 98  98  98  GLU GLU B . n 
B 2 99  ASP 99  99  99  ASP ASP B . n 
B 2 100 SER 100 100 100 SER SER B . n 
B 2 101 SER 101 101 101 SER SER B . n 
B 2 102 ILE 102 102 102 ILE ILE B . n 
B 2 103 SER 103 103 103 SER SER B . n 
B 2 104 LEU 104 104 104 LEU LEU B . n 
B 2 105 MET 105 105 105 MET MET B . n 
B 2 106 SER 106 106 106 SER SER B . n 
B 2 107 HIS 107 107 107 HIS HIS B . n 
B 2 108 CYS 108 108 108 CYS CYS B . n 
B 2 109 SER 109 109 109 SER SER B . n 
B 2 110 PHE 110 110 110 PHE PHE B . n 
B 2 111 PRO 111 111 111 PRO PRO B . n 
B 2 112 LYS 112 112 112 LYS LYS B . n 
B 2 113 GLY 113 113 113 GLY GLY B . n 
B 2 114 LYS 114 114 114 LYS LYS B . n 
B 2 115 GLY 115 115 115 GLY GLY B . n 
B 2 116 ILE 116 116 116 ILE ILE B . n 
B 2 117 LYS 117 117 117 LYS LYS B . n 
B 2 118 HIS 118 118 118 HIS HIS B . n 
B 2 119 ILE 119 119 119 ILE ILE B . n 
B 2 120 MET 120 120 120 MET MET B . n 
B 2 121 ASN 121 121 121 ASN ASN B . n 
B 2 122 GLY 122 122 122 GLY GLY B . n 
B 2 123 ILE 123 123 123 ILE ILE B . n 
B 2 124 ILE 124 124 124 ILE ILE B . n 
B 2 125 LYS 125 125 125 LYS LYS B . n 
B 2 126 ILE 126 126 126 ILE ILE B . n 
B 2 127 GLY 127 127 127 GLY GLY B . n 
B 2 128 LYS 128 128 128 LYS LYS B . n 
B 2 129 ASN 129 129 129 ASN ASN B . n 
B 2 130 ALA 130 130 130 ALA ALA B . n 
B 2 131 LYS 131 131 131 LYS LYS B . n 
B 2 132 PHE 132 132 132 PHE PHE B . n 
B 2 133 SER 133 133 133 SER SER B . n 
B 2 134 TYR 134 134 134 TYR TYR B . n 
B 2 135 ASN 135 135 135 ASN ASN B . n 
B 2 136 GLU 136 136 136 GLU GLU B . n 
B 2 137 PHE 137 137 137 PHE PHE B . n 
B 2 138 HIS 138 138 138 HIS HIS B . n 
B 2 139 TYR 139 139 139 TYR TYR B . n 
B 2 140 HIS 140 140 140 HIS HIS B . n 
B 2 141 GLY 141 141 141 GLY GLY B . n 
B 2 142 MET 142 142 142 MET MET B . n 
B 2 143 ASP 143 143 143 ASP ASP B . n 
B 2 144 GLY 144 144 144 GLY GLY B . n 
B 2 145 ASP 145 145 145 ASP ASP B . n 
B 2 146 ILE 146 146 146 ILE ILE B . n 
B 2 147 LEU 147 147 147 LEU LEU B . n 
B 2 148 VAL 148 148 148 VAL VAL B . n 
B 2 149 LYS 149 149 149 LYS LYS B . n 
B 2 150 PRO 150 150 150 PRO PRO B . n 
B 2 151 THR 151 151 151 THR THR B . n 
B 2 152 VAL 152 152 152 VAL VAL B . n 
B 2 153 LYS 153 153 153 LYS LYS B . n 
B 2 154 VAL 154 154 154 VAL VAL B . n 
B 2 155 GLU 155 155 155 GLU GLU B . n 
B 2 156 ILE 156 156 156 ILE ILE B . n 
B 2 157 ASP 157 157 157 ASP ASP B . n 
B 2 158 GLU 158 474 158 GLU GLU B . n 
B 2 159 GLY 159 475 159 GLY GLY B . n 
B 2 160 GLY 160 476 160 GLY GLY B . n 
B 2 161 ILE 161 477 161 ILE ILE B . n 
B 2 162 TYR 162 478 162 TYR TYR B . n 
B 2 163 ILE 163 479 163 ILE ILE B . n 
B 2 164 SER 164 480 164 SER SER B . n 
B 2 165 ASN 165 481 165 ASN ASN B . n 
B 2 166 PHE 166 482 166 PHE PHE B . n 
B 2 167 THR 167 483 167 THR THR B . n 
B 2 168 LEU 168 484 168 LEU LEU B . n 
B 2 169 THR 169 485 169 THR THR B . n 
B 2 170 LYS 170 486 170 LYS LYS B . n 
B 2 171 GLY 171 487 171 GLY GLY B . n 
B 2 172 ARG 172 488 172 ARG ARG B . n 
B 2 173 ILE 173 489 173 ILE ILE B . n 
B 2 174 GLY 174 490 174 GLY GLY B . n 
B 2 175 THR 175 491 175 THR THR B . n 
B 2 176 LEU 176 492 176 LEU LEU B . n 
B 2 177 ASP 177 493 177 ASP ASP B . n 
B 2 178 ILE 178 494 178 ILE ILE B . n 
B 2 179 GLU 179 495 179 GLU GLU B . n 
B 2 180 GLN 180 496 180 GLN GLN B . n 
B 2 181 GLU 181 497 181 GLU GLU B . n 
B 2 182 ILE 182 498 182 ILE ILE B . n 
B 2 183 ILE 183 499 183 ILE ILE B . n 
B 2 184 ALA 184 500 184 ALA ALA B . n 
B 2 185 LYS 185 501 185 LYS LYS B . n 
B 2 186 LYS 186 502 186 LYS LYS B . n 
B 2 187 ASP 187 503 187 ASP ASP B . n 
B 2 188 ALA 188 504 188 ALA ALA B . n 
B 2 189 ILE 189 505 189 ILE ILE B . n 
B 2 190 ILE 190 506 190 ILE ILE B . n 
B 2 191 ASP 191 507 191 ASP ASP B . n 
B 2 192 ILE 192 508 192 ILE ILE B . n 
B 2 193 THR 193 509 193 THR THR B . n 
B 2 194 THR 194 510 194 THR THR B . n 
B 2 195 ARG 195 511 195 ARG ARG B . n 
B 2 196 THR 196 512 196 THR THR B . n 
B 2 197 TYR 197 513 197 TYR TYR B . n 
B 2 198 ALA 198 514 198 ALA ALA B . n 
B 2 199 ILE 199 515 199 ILE ILE B . n 
B 2 200 LYS 200 516 200 LYS LYS B . n 
B 2 201 GLU 201 517 201 GLU GLU B . n 
B 2 202 ASP 202 518 202 ASP ASP B . n 
B 2 203 VAL 203 519 203 VAL VAL B . n 
B 2 204 VAL 204 520 204 VAL VAL B . n 
B 2 205 LYS 205 521 205 LYS LYS B . n 
B 2 206 VAL 206 522 206 VAL VAL B . n 
B 2 207 ASN 207 523 207 ASN ASN B . n 
B 2 208 GLU 208 524 208 GLU GLU B . n 
B 2 209 VAL 209 525 209 VAL VAL B . n 
B 2 210 VAL 210 526 210 VAL VAL B . n 
B 2 211 LYS 211 527 211 LYS LYS B . n 
B 2 212 LEU 212 528 212 LEU LEU B . n 
B 2 213 ASN 213 529 213 ASN ASN B . n 
B 2 214 GLY 214 530 214 GLY GLY B . n 
B 2 215 GLU 215 531 215 GLU GLU B . n 
B 2 216 ASN 216 532 216 ASN ASN B . n 
B 2 217 ALA 217 533 217 ALA ALA B . n 
B 2 218 LYS 218 534 218 LYS LYS B . n 
B 2 219 CYS 219 535 219 CYS CYS B . n 
B 2 220 ILE 220 536 220 ILE ILE B . n 
B 2 221 ILE 221 537 221 ILE ILE B . n 
B 2 222 LYS 222 538 222 LYS LYS B . n 
B 2 223 SER 223 539 223 SER SER B . n 
B 2 224 ARG 224 540 224 ARG ARG B . n 
B 2 225 GLY 225 541 225 GLY GLY B . n 
B 2 226 ALA 226 542 226 ALA ALA B . n 
B 2 227 ALA 227 543 227 ALA ALA B . n 
B 2 228 MET 228 544 228 MET MET B . n 
B 2 229 ASP 229 545 229 ASP ASP B . n 
B 2 230 ASN 230 546 230 ASN ASN B . n 
B 2 231 SER 231 547 231 SER SER B . n 
B 2 232 LYS 232 548 232 LYS LYS B . n 
B 2 233 ILE 233 549 233 ILE ILE B . n 
B 2 234 SER 234 550 234 SER SER B . n 
B 2 235 LEU 235 551 235 LEU LEU B . n 
B 2 236 LYS 236 552 236 LYS LYS B . n 
B 2 237 LEU 237 553 237 LEU LEU B . n 
B 2 238 LYS 238 554 238 LYS LYS B . n 
B 2 239 ILE 239 555 239 ILE ILE B . n 
B 2 240 GLU 240 556 240 GLU GLU B . n 
B 2 241 GLY 241 557 241 GLY GLY B . n 
B 2 242 ASN 242 558 242 ASN ASN B . n 
B 2 243 ALA 243 559 243 ALA ALA B . n 
B 2 244 PRO 244 560 244 PRO PRO B . n 
B 2 245 TYR 245 561 245 TYR TYR B . n 
B 2 246 SER 246 562 246 SER SER B . n 
B 2 247 LYS 247 563 247 LYS LYS B . n 
B 2 248 GLY 248 564 248 GLY GLY B . n 
B 2 249 HIS 249 565 249 HIS HIS B . n 
B 2 250 ILE 250 566 250 ILE ILE B . n 
B 2 251 ASP 251 567 251 ASP ASP B . n 
B 2 252 CYS 252 568 252 CYS CYS B . n 
B 2 253 ALA 253 569 253 ALA ALA B . n 
B 2 254 GLU 254 570 254 GLU GLU B . n 
B 2 255 ILE 255 571 255 ILE ILE B . n 
B 2 256 VAL 256 572 256 VAL VAL B . n 
B 2 257 LYS 257 573 257 LYS LYS B . n 
B 2 258 GLY 258 574 258 GLY GLY B . n 
B 2 259 ASN 259 575 259 ASN ASN B . n 
B 2 260 ALA 260 576 260 ALA ALA B . n 
B 2 261 GLU 261 577 261 GLU GLU B . n 
B 2 262 VAL 262 578 262 VAL VAL B . n 
B 2 263 GLU 263 579 263 GLU GLU B . n 
B 2 264 SER 264 580 264 SER SER B . n 
B 2 265 ILE 265 581 265 ILE ILE B . n 
B 2 266 PRO 266 582 266 PRO PRO B . n 
B 2 267 ILE 267 583 267 ILE ILE B . n 
B 2 268 VAL 268 584 268 VAL VAL B . n 
B 2 269 VAL 269 585 269 VAL VAL B . n 
B 2 270 VAL 270 586 270 VAL VAL B . n 
B 2 271 ARG 271 587 271 ARG ARG B . n 
B 2 272 ASP 272 588 272 ASP ASP B . n 
B 2 273 ASP 273 589 273 ASP ASP B . n 
B 2 274 LYS 274 590 274 LYS LYS B . n 
B 2 275 ALA 275 591 275 ALA ALA B . n 
B 2 276 ARG 276 592 276 ARG ARG B . n 
B 2 277 ILE 277 593 277 ILE ILE B . n 
B 2 278 THR 278 594 278 THR THR B . n 
B 2 279 HIS 279 595 279 HIS HIS B . n 
B 2 280 GLU 280 596 280 GLU GLU B . n 
B 2 281 ALA 281 597 281 ALA ALA B . n 
B 2 282 ALA 282 598 282 ALA ALA B . n 
B 2 283 ILE 283 599 283 ILE ILE B . n 
B 2 284 GLY 284 600 284 GLY GLY B . n 
B 2 285 SER 285 601 285 SER SER B . n 
B 2 286 VAL 286 602 286 VAL VAL B . n 
B 2 287 ASP 287 603 287 ASP ASP B . n 
B 2 288 LYS 288 604 288 LYS LYS B . n 
B 2 289 LYS 289 605 289 LYS LYS B . n 
B 2 290 GLN 290 606 290 GLN GLN B . n 
B 2 291 LEU 291 607 291 LEU LEU B . n 
B 2 292 GLU 292 608 292 GLU GLU B . n 
B 2 293 THR 293 609 293 THR THR B . n 
B 2 294 LEU 294 610 294 LEU LEU B . n 
B 2 295 MET 295 611 295 MET MET B . n 
B 2 296 ALA 296 612 296 ALA ALA B . n 
B 2 297 LYS 297 613 297 LYS LYS B . n 
B 2 298 GLY 298 614 298 GLY GLY B . n 
B 2 299 LEU 299 615 299 LEU LEU B . n 
B 2 300 ASP 300 616 300 ASP ASP B . n 
B 2 301 GLU 301 617 301 GLU GLU B . n 
B 2 302 ASP 302 618 302 ASP ASP B . n 
B 2 303 GLU 303 619 303 GLU GLU B . n 
B 2 304 ALA 304 620 304 ALA ALA B . n 
B 2 305 THR 305 621 305 THR THR B . n 
B 2 306 GLU 306 622 306 GLU GLU B . n 
B 2 307 ILE 307 623 307 ILE ILE B . n 
B 2 308 ILE 308 624 308 ILE ILE B . n 
B 2 309 VAL 309 625 309 VAL VAL B . n 
B 2 310 LYS 310 626 310 LYS LYS B . n 
B 2 311 GLY 311 627 311 GLY GLY B . n 
B 2 312 MET 312 628 312 MET MET B . n 
B 2 313 ILE 313 629 313 ILE ILE B . n 
B 2 314 GLY 314 630 314 GLY GLY B . n 
B 2 315 ASP 315 631 315 ASP ASP B . n 
B 2 316 LEU 316 632 316 LEU LEU B . 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 ANP ? ? ANP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 MG  ? ? MG  ? ? '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 
C 3 MG  1  301 1  MG  MG  A . 
D 4 ANP 1  302 2  ANP ANP A . 
E 5 HOH 1  401 5  HOH HOH A . 
E 5 HOH 2  402 24 HOH HOH A . 
E 5 HOH 3  403 21 HOH HOH A . 
E 5 HOH 4  404 17 HOH HOH A . 
E 5 HOH 5  405 4  HOH HOH A . 
E 5 HOH 6  406 23 HOH HOH A . 
F 5 HOH 1  701 1  HOH HOH B . 
F 5 HOH 2  702 7  HOH HOH B . 
F 5 HOH 3  703 2  HOH HOH B . 
F 5 HOH 4  704 6  HOH HOH B . 
F 5 HOH 5  705 3  HOH HOH B . 
F 5 HOH 6  706 8  HOH HOH B . 
F 5 HOH 7  707 9  HOH HOH B . 
F 5 HOH 8  708 14 HOH HOH B . 
F 5 HOH 9  709 15 HOH HOH B . 
F 5 HOH 10 710 16 HOH HOH B . 
F 5 HOH 11 711 10 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER   ? ? ? 2.10.4 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .      2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .      3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .      4 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9H7Y 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     85.167 
_cell.length_a_esd                 ? 
_cell.length_b                     125.038 
_cell.length_b_esd                 ? 
_cell.length_c                     133.056 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9H7Y 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_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                   9H7Y 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.78 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          55.75 
_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' 
_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    '5% PEG3350, 10% tacsimate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-05-31 
_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   1.27819 
_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                        'SOLEIL BEAMLINE PROXIMA 2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.27819 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 2' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9H7Y 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              3.198 
_reflns.d_resolution_low                               70.39 
_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                                     8240 
_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                           90.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                18.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.4 
_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                                0.317 
_reflns.pdbx_Rpim_I_all                                0.075 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.992 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.307 
_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                                    3.198 
_reflns_shell.d_res_low                                     3.532 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.5 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             412 
_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                               16.4 
_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                               4.344 
_reflns_shell.pdbx_Rpim_I_all                               1.075 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.450 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          57.8 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  4.205 
_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]                            40.8205 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            -21.8322 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -18.9883 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               150.03 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.891 
_refine.correlation_coeff_Fo_to_Fc_free          0.902 
_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                                 9H7Y 
_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                            3.198 
_refine.ls_d_res_low                             70.39 
_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                     8240 
_refine.ls_number_reflns_R_free                  428 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    68.2 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2730 
_refine.ls_R_factor_R_free                       0.2904 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2720 
_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                    ? 
_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                          ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.74 
_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                            ? 
_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_analyze.entry_id                        9H7Y 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.58 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       3.198 
_refine_hist.d_res_low                        70.39 
_refine_hist.number_atoms_solvent             17 
_refine_hist.number_atoms_total               4201 
_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        4152 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_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' ? 0.006 ? 4253 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.93  ? 5712 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1606 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 715  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 4253 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 582  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 3104 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 2.4   ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 19.87 ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       3.2 
_refine_ls_shell.d_res_low                        3.52 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                393 
_refine_ls_shell.number_reflns_R_free             17 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               13.04 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     0.314 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3135 
_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                  0.3243 
# 
_struct.entry_id                     9H7Y 
_struct.title                        'SmsC2B2 complex from M. jannaschii (orthorhombic form)' 
_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        9H7Y 
_struct_keywords.text            'Iron-sulfur cluster, biogenesis, SMS, Archaea, METAL TRANSPORT' 
_struct_keywords.pdbx_keywords   'METAL TRANSPORT' 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP Y035_METJA Q60350 ? 1 
;MVSIMLLKVEDLHVYRGNREILKGVNLTVEENEIHAIIGPNGAGKSTLAYTIMGISGYKPTKGRIIFKGVDIIDKNITER
ARMGMTLAWQEPARFEGIKVKNYLMLGMNEKYKKDKEIAEEKIREALKLVNLDPDKYLDRYVDETLSGGERKRIELASII
CMEPDLAILDEPDSGIDIVSFDEIKRVFDYLKDKGCSLLVITHREELAEHADRVSLICAGEVIKSGDPKEVGEFYKKECG
KCYKKVPDGK
;
1 
2 UNP Y034_METJA Q60349 ? 2 
;MSIKEELMEIIEAIKYTSEKPEEIVHGKGPRIIVKESRIIDVQGDEGIILEGKEEDGKIKAKIIVKKGYKFKYPIHMCFG
ITEENISQIIDVEIILEEDSSISLMSHCSFPKGKGIKHIMNGIIKIGKNAKFSYNEFHYHGMDGDILVKPTVKVEIDEGG
IYISNFTLTKGRIGTLDIEQEIIAKKDAIIDITTRTYAIKEDVVKVNEVVKLNGENAKCIIKSRGAAMDNSKISLKLKIE
GNAPYSKGHIDCAEIVKGNAEVESIPIVVVRDDKARITHEAAIGSVDKKQLETLMAKGLDEDEATEIIVKGMIGDL
;
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 9H7Y A 4 ? 253 ? Q60350 1 ? 250 ? 1 250 
2 2 9H7Y B 1 ? 316 ? Q60349 1 ? 316 ? 1 632 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9H7Y GLY A 1 ? UNP Q60350 ? ? 'expression tag' -2 1 
1 9H7Y GLU A 2 ? UNP Q60350 ? ? 'expression tag' -1 2 
1 9H7Y PHE A 3 ? UNP Q60350 ? ? 'expression tag' 0  3 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
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)' 9540  ? 
1 MORE         -37   ? 
1 'SSA (A^2)'  41230 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 3_554 -x,y,-z-1/2 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -66.5280000000 
# 
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 MET A 4   ? SER A 6   ? MET A 1   SER A 3   5 ? 3  
HELX_P HELX_P2  AA2 GLY A 47  ? GLY A 57  ? GLY A 44  GLY A 54  1 ? 11 
HELX_P HELX_P3  AA3 ILE A 76  ? LYS A 78  ? ILE A 73  LYS A 75  5 ? 3  
HELX_P HELX_P4  AA4 ASN A 79  ? ARG A 85  ? ASN A 76  ARG A 82  1 ? 7  
HELX_P HELX_P5  AA5 LYS A 102 ? LEU A 107 ? LYS A 99  LEU A 104 1 ? 6  
HELX_P HELX_P6  AA6 ASN A 112 ? LYS A 117 ? ASN A 109 LYS A 114 1 ? 6  
HELX_P HELX_P7  AA7 ASP A 118 ? VAL A 133 ? ASP A 115 VAL A 130 1 ? 16 
HELX_P HELX_P8  AA8 ASP A 136 ? LEU A 141 ? ASP A 133 LEU A 138 1 ? 6  
HELX_P HELX_P9  AA9 SER A 150 ? GLU A 166 ? SER A 147 GLU A 163 1 ? 17 
HELX_P HELX_P10 AB1 SER A 183 ? GLY A 198 ? SER A 180 GLY A 195 1 ? 16 
HELX_P HELX_P11 AB2 ARG A 207 ? GLU A 212 ? ARG A 204 GLU A 209 1 ? 6  
HELX_P HELX_P12 AB3 ASP A 230 ? GLU A 241 ? ASP A 227 GLU A 238 1 ? 12 
HELX_P HELX_P13 AB4 ASP B 287 ? ALA B 296 ? ASP B 603 ALA B 612 1 ? 10 
HELX_P HELX_P14 AB5 ASP B 300 ? ILE B 313 ? ASP B 616 ILE B 629 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A SER 49  OG  ? ? ? 1_555 C MG  . MG  ? ? A SER 46  A MG  301 1_555 ? ? ? ? ? ? ? 1.917 ? ? 
metalc2 metalc ? ? A GLU 174 OE1 ? ? ? 1_555 C MG  . MG  ? ? A GLU 171 A MG  301 1_555 ? ? ? ? ? ? ? 2.696 ? ? 
metalc3 metalc ? ? C MG  .   MG  ? ? ? 1_555 D ANP . O1G ? ? A MG  301 A ANP 302 1_555 ? ? ? ? ? ? ? 2.626 ? ? 
metalc4 metalc ? ? C MG  .   MG  ? ? ? 1_555 D ANP . O2G ? ? A MG  301 A ANP 302 1_555 ? ? ? ? ? ? ? 2.934 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 OG  ? A SER 49  ? A SER 46  ? 1_555 MG ? C MG . ? A MG 301 ? 1_555 OE1 ? A GLU 174 ? A GLU 171 ? 1_555 148.0 ? 
2 OG  ? A SER 49  ? A SER 46  ? 1_555 MG ? C MG . ? A MG 301 ? 1_555 O1G ? D ANP .   ? A ANP 302 ? 1_555 125.9 ? 
3 OE1 ? A GLU 174 ? A GLU 171 ? 1_555 MG ? C MG . ? A MG 301 ? 1_555 O1G ? D ANP .   ? A ANP 302 ? 1_555 51.9  ? 
4 OG  ? A SER 49  ? A SER 46  ? 1_555 MG ? C MG . ? A MG 301 ? 1_555 O2G ? D ANP .   ? A ANP 302 ? 1_555 95.2  ? 
5 OE1 ? A GLU 174 ? A GLU 171 ? 1_555 MG ? C MG . ? A MG 301 ? 1_555 O2G ? D ANP .   ? A ANP 302 ? 1_555 99.7  ? 
6 O1G ? D ANP .   ? A ANP 302 ? 1_555 MG ? C MG . ? A MG 301 ? 1_555 O2G ? D ANP .   ? A ANP 302 ? 1_555 50.5  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4  ? 
AA2 ? 6  ? 
AA3 ? 10 ? 
AA4 ? 9  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? anti-parallel 
AA1 2 3  ? anti-parallel 
AA1 3 4  ? anti-parallel 
AA2 1 2  ? parallel      
AA2 2 3  ? parallel      
AA2 3 4  ? parallel      
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? parallel      
AA3 3 4  ? parallel      
AA3 4 5  ? parallel      
AA3 5 6  ? parallel      
AA3 6 7  ? parallel      
AA3 7 8  ? parallel      
AA3 8 9  ? parallel      
AA3 9 10 ? parallel      
AA4 1 2  ? anti-parallel 
AA4 2 3  ? parallel      
AA4 3 4  ? parallel      
AA4 4 5  ? parallel      
AA4 5 6  ? parallel      
AA4 6 7  ? parallel      
AA4 7 8  ? parallel      
AA4 8 9  ? 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  ARG A 22  ? GLU A 33  ? ARG A 19  GLU A 30  
AA1 2  MET A 8   ? ARG A 19  ? MET A 5   ARG A 16  
AA1 3  PRO A 63  ? PHE A 70  ? PRO A 60  PHE A 67  
AA1 4  VAL A 73  ? ASP A 74  ? VAL A 70  ASP A 71  
AA2 1  MET A 88  ? LEU A 90  ? MET A 85  LEU A 87  
AA2 2  LEU A 169 ? ASP A 173 ? LEU A 166 ASP A 170 
AA2 3  SER A 200 ? ILE A 204 ? SER A 197 ILE A 201 
AA2 4  ILE A 37  ? ILE A 41  ? ILE A 34  ILE A 38  
AA2 5  ARG A 216 ? CYS A 221 ? ARG A 213 CYS A 218 
AA2 6  GLU A 224 ? GLY A 229 ? GLU A 221 GLY A 226 
AA3 1  ARG B 38  ? VAL B 42  ? ARG B 38  VAL B 42  
AA3 2  ARG B 31  ? LYS B 35  ? ARG B 31  LYS B 35  
AA3 3  ILE B 75  ? GLY B 80  ? ILE B 75  GLY B 80  
AA3 4  SER B 101 ? PHE B 110 ? SER B 101 PHE B 110 
AA3 5  LYS B 131 ? HIS B 140 ? LYS B 131 HIS B 140 
AA3 6  ILE B 161 ? LYS B 170 ? ILE B 477 LYS B 486 
AA3 7  ILE B 189 ? ALA B 198 ? ILE B 505 ALA B 514 
AA3 8  LYS B 218 ? ALA B 227 ? LYS B 534 ALA B 543 
AA3 9  LYS B 247 ? VAL B 256 ? LYS B 563 VAL B 572 
AA3 10 ARG B 276 ? GLY B 284 ? ARG B 592 GLY B 600 
AA4 1  ILE B 48  ? GLU B 54  ? ILE B 48  GLU B 54  
AA4 2  LYS B 58  ? VAL B 65  ? LYS B 58  VAL B 65  
AA4 3  SER B 87  ? LEU B 96  ? SER B 87  LEU B 96  
AA4 4  LYS B 114 ? ILE B 126 ? LYS B 114 ILE B 126 
AA4 5  ASP B 145 ? ILE B 156 ? ASP B 145 ILE B 156 
AA4 6  THR B 175 ? ALA B 184 ? THR B 491 ALA B 500 
AA4 7  VAL B 203 ? LEU B 212 ? VAL B 519 LEU B 528 
AA4 8  LYS B 232 ? GLY B 241 ? LYS B 548 GLY B 557 
AA4 9  GLU B 261 ? VAL B 270 ? GLU B 577 VAL B 586 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  O LEU A 30  ? O LEU A 27  N VAL A 12  ? N VAL A 9   
AA1 2 3  N GLU A 13  ? N GLU A 10  O ARG A 67  ? O ARG A 64  
AA1 3 4  N PHE A 70  ? N PHE A 67  O VAL A 73  ? O VAL A 70  
AA2 1 2  N THR A 89  ? N THR A 86  O ILE A 171 ? O ILE A 168 
AA2 2 3  N ALA A 170 ? N ALA A 167 O SER A 200 ? O SER A 197 
AA2 3 4  O VAL A 203 ? O VAL A 200 N ILE A 40  ? N ILE A 37  
AA2 4 5  N ILE A 41  ? N ILE A 38  O ILE A 220 ? O ILE A 217 
AA2 5 6  N LEU A 219 ? N LEU A 216 O LYS A 227 ? O LYS A 224 
AA3 1 2  O ILE B 40  ? O ILE B 40  N ILE B 33  ? N ILE B 33  
AA3 2 3  N VAL B 34  ? N VAL B 34  O CYS B 78  ? O CYS B 78  
AA3 3 4  N ILE B 75  ? N ILE B 75  O MET B 105 ? O MET B 105 
AA3 4 5  N LEU B 104 ? N LEU B 104 O SER B 133 ? O SER B 133 
AA3 5 6  N GLU B 136 ? N GLU B 136 O ASN B 165 ? O ASN B 481 
AA3 6 7  N TYR B 162 ? N TYR B 478 O ILE B 189 ? O ILE B 505 
AA3 7 8  N THR B 194 ? N THR B 510 O ARG B 224 ? O ARG B 540 
AA3 8 9  N ALA B 227 ? N ALA B 543 O ILE B 255 ? O ILE B 571 
AA3 9 10 N CYS B 252 ? N CYS B 568 O GLU B 280 ? O GLU B 596 
AA4 1 2  N LYS B 53  ? N LYS B 53  O LYS B 60  ? O LYS B 60  
AA4 2 3  N ILE B 63  ? N ILE B 63  O ILE B 95  ? O ILE B 95  
AA4 3 4  N ILE B 90  ? N ILE B 90  O ILE B 119 ? O ILE B 119 
AA4 4 5  N ILE B 124 ? N ILE B 124 O LYS B 153 ? O LYS B 153 
AA4 5 6  N VAL B 154 ? N VAL B 154 O GLU B 181 ? O GLU B 497 
AA4 6 7  N ILE B 182 ? N ILE B 498 O LYS B 211 ? O LYS B 527 
AA4 7 8  N VAL B 206 ? N VAL B 522 O LYS B 236 ? O LYS B 552 
AA4 8 9  N GLY B 241 ? N GLY B 557 O VAL B 269 ? O VAL B 585 
# 
_pdbx_entry_details.entry_id                   9H7Y 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 11  ? ? 27.92   60.94   
2  1 LYS A 23  ? ? -114.37 60.64   
3  1 TRP A 89  ? ? 95.76   -42.25  
4  1 GLN A 90  ? ? 99.92   -53.20  
5  1 LYS A 114 ? ? -62.29  -70.59  
6  1 VAL A 142 ? ? -84.53  47.37   
7  1 GLU B 36  ? ? 69.94   -136.33 
8  1 ASP B 56  ? ? 58.99   81.09   
9  1 ASP B 145 ? ? -95.48  50.54   
10 1 LYS B 502 ? ? -38.15  130.43  
11 1 LYS B 516 ? ? 49.56   -124.36 
12 1 ASP B 545 ? ? 54.93   -115.36 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? ? -13.1257 -60.7732 -23.4474 0.6411 ? -0.1854 ? 0.3577  ? -0.9434 ? 0.0881  ? -0.3509 ? 8.6913 ? 3.3577 ? 
0.2374 ? 7.1593 ? 2.4392  ? 12.6789 ? -1.0628 ? 0.1521 ? 1.2575  ? 0.1521 ? 0.2188  ? 0.8909 ? 1.2575  ? 0.8909 ? 0.8441 ? 
2 'X-RAY DIFFRACTION' ? ? 7.8189   -24.925  -15.1876 0.9116 ? -0.4033 ? -0.1374 ? -0.4316 ? -0.1181 ? -0.3901 ? 4.9547 ? 2.1596 ? 
2.2126 ? 6.0964 ? -1.2107 ? 3.6561  ? 0.5653  ? 1.4684 ? -0.3878 ? 1.4684 ? -0.6746 ? 0.0303 ? -0.3878 ? 0.0303 ? 0.1093 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A -2 ? ? ? A 239 ? ? '{ A|* }' 
2 'X-RAY DIFFRACTION' 2 ? ? B 28 ? ? ? B 316 ? ? '{ B|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 240 ? A GLY 243 
2  1 Y 1 A LYS 241 ? A LYS 244 
3  1 Y 1 A CYS 242 ? A CYS 245 
4  1 Y 1 A TYR 243 ? A TYR 246 
5  1 Y 1 A LYS 244 ? A LYS 247 
6  1 Y 1 A LYS 245 ? A LYS 248 
7  1 Y 1 A VAL 246 ? A VAL 249 
8  1 Y 1 A PRO 247 ? A PRO 250 
9  1 Y 1 A ASP 248 ? A ASP 251 
10 1 Y 1 A GLY 249 ? A GLY 252 
11 1 Y 1 A LYS 250 ? A LYS 253 
12 1 Y 1 B MET 1   ? B MET 1   
13 1 Y 1 B SER 2   ? B SER 2   
14 1 Y 1 B ILE 3   ? B ILE 3   
15 1 Y 1 B LYS 4   ? B LYS 4   
16 1 Y 1 B GLU 5   ? B GLU 5   
17 1 Y 1 B GLU 6   ? B GLU 6   
18 1 Y 1 B LEU 7   ? B LEU 7   
19 1 Y 1 B MET 8   ? B MET 8   
20 1 Y 1 B GLU 9   ? B GLU 9   
21 1 Y 1 B ILE 10  ? B ILE 10  
22 1 Y 1 B ILE 11  ? B ILE 11  
23 1 Y 1 B GLU 12  ? B GLU 12  
24 1 Y 1 B ALA 13  ? B ALA 13  
25 1 Y 1 B ILE 14  ? B ILE 14  
26 1 Y 1 B LYS 15  ? B LYS 15  
27 1 Y 1 B TYR 16  ? B TYR 16  
28 1 Y 1 B THR 17  ? B THR 17  
29 1 Y 1 B SER 18  ? B SER 18  
30 1 Y 1 B GLU 19  ? B GLU 19  
31 1 Y 1 B LYS 20  ? B LYS 20  
32 1 Y 1 B PRO 21  ? B PRO 21  
33 1 Y 1 B GLU 22  ? B GLU 22  
34 1 Y 1 B GLU 23  ? B GLU 23  
35 1 Y 1 B ILE 24  ? B ILE 24  
36 1 Y 1 B VAL 25  ? B VAL 25  
37 1 Y 1 B HIS 26  ? B HIS 26  
38 1 Y 1 B GLY 27  ? B GLY 27  
# 
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 
ALA N      N  N N 1   
ALA CA     C  N S 2   
ALA C      C  N N 3   
ALA O      O  N N 4   
ALA CB     C  N N 5   
ALA OXT    O  N N 6   
ALA H      H  N N 7   
ALA H2     H  N N 8   
ALA HA     H  N N 9   
ALA HB1    H  N N 10  
ALA HB2    H  N N 11  
ALA HB3    H  N N 12  
ALA HXT    H  N N 13  
ANP PG     P  N N 14  
ANP O1G    O  N N 15  
ANP O2G    O  N N 16  
ANP O3G    O  N N 17  
ANP PB     P  N N 18  
ANP O1B    O  N N 19  
ANP O2B    O  N N 20  
ANP N3B    N  N N 21  
ANP PA     P  N N 22  
ANP O1A    O  N N 23  
ANP O2A    O  N N 24  
ANP O3A    O  N N 25  
ANP "O5'"  O  N N 26  
ANP "C5'"  C  N N 27  
ANP "C4'"  C  N R 28  
ANP "O4'"  O  N N 29  
ANP "C3'"  C  N S 30  
ANP "O3'"  O  N N 31  
ANP "C2'"  C  N R 32  
ANP "O2'"  O  N N 33  
ANP "C1'"  C  N R 34  
ANP N9     N  Y N 35  
ANP C8     C  Y N 36  
ANP N7     N  Y N 37  
ANP C5     C  Y N 38  
ANP C6     C  Y N 39  
ANP N6     N  N N 40  
ANP N1     N  Y N 41  
ANP C2     C  Y N 42  
ANP N3     N  Y N 43  
ANP C4     C  Y N 44  
ANP HOG2   H  N N 45  
ANP HOG3   H  N N 46  
ANP HOB2   H  N N 47  
ANP HNB1   H  N N 48  
ANP HOA2   H  N N 49  
ANP "H5'1" H  N N 50  
ANP "H5'2" H  N N 51  
ANP "H4'"  H  N N 52  
ANP "H3'"  H  N N 53  
ANP "HO3'" H  N N 54  
ANP "H2'"  H  N N 55  
ANP "HO2'" H  N N 56  
ANP "H1'"  H  N N 57  
ANP H8     H  N N 58  
ANP HN61   H  N N 59  
ANP HN62   H  N N 60  
ANP H2     H  N N 61  
ARG N      N  N N 62  
ARG CA     C  N S 63  
ARG C      C  N N 64  
ARG O      O  N N 65  
ARG CB     C  N N 66  
ARG CG     C  N N 67  
ARG CD     C  N N 68  
ARG NE     N  N N 69  
ARG CZ     C  N N 70  
ARG NH1    N  N N 71  
ARG NH2    N  N N 72  
ARG OXT    O  N N 73  
ARG H      H  N N 74  
ARG H2     H  N N 75  
ARG HA     H  N N 76  
ARG HB2    H  N N 77  
ARG HB3    H  N N 78  
ARG HG2    H  N N 79  
ARG HG3    H  N N 80  
ARG HD2    H  N N 81  
ARG HD3    H  N N 82  
ARG HE     H  N N 83  
ARG HH11   H  N N 84  
ARG HH12   H  N N 85  
ARG HH21   H  N N 86  
ARG HH22   H  N N 87  
ARG HXT    H  N N 88  
ASN N      N  N N 89  
ASN CA     C  N S 90  
ASN C      C  N N 91  
ASN O      O  N N 92  
ASN CB     C  N N 93  
ASN CG     C  N N 94  
ASN OD1    O  N N 95  
ASN ND2    N  N N 96  
ASN OXT    O  N N 97  
ASN H      H  N N 98  
ASN H2     H  N N 99  
ASN HA     H  N N 100 
ASN HB2    H  N N 101 
ASN HB3    H  N N 102 
ASN HD21   H  N N 103 
ASN HD22   H  N N 104 
ASN HXT    H  N N 105 
ASP N      N  N N 106 
ASP CA     C  N S 107 
ASP C      C  N N 108 
ASP O      O  N N 109 
ASP CB     C  N N 110 
ASP CG     C  N N 111 
ASP OD1    O  N N 112 
ASP OD2    O  N N 113 
ASP OXT    O  N N 114 
ASP H      H  N N 115 
ASP H2     H  N N 116 
ASP HA     H  N N 117 
ASP HB2    H  N N 118 
ASP HB3    H  N N 119 
ASP HD2    H  N N 120 
ASP HXT    H  N N 121 
CYS N      N  N N 122 
CYS CA     C  N R 123 
CYS C      C  N N 124 
CYS O      O  N N 125 
CYS CB     C  N N 126 
CYS SG     S  N N 127 
CYS OXT    O  N N 128 
CYS H      H  N N 129 
CYS H2     H  N N 130 
CYS HA     H  N N 131 
CYS HB2    H  N N 132 
CYS HB3    H  N N 133 
CYS HG     H  N N 134 
CYS HXT    H  N N 135 
GLN N      N  N N 136 
GLN CA     C  N S 137 
GLN C      C  N N 138 
GLN O      O  N N 139 
GLN CB     C  N N 140 
GLN CG     C  N N 141 
GLN CD     C  N N 142 
GLN OE1    O  N N 143 
GLN NE2    N  N N 144 
GLN OXT    O  N N 145 
GLN H      H  N N 146 
GLN H2     H  N N 147 
GLN HA     H  N N 148 
GLN HB2    H  N N 149 
GLN HB3    H  N N 150 
GLN HG2    H  N N 151 
GLN HG3    H  N N 152 
GLN HE21   H  N N 153 
GLN HE22   H  N N 154 
GLN HXT    H  N N 155 
GLU N      N  N N 156 
GLU CA     C  N S 157 
GLU C      C  N N 158 
GLU O      O  N N 159 
GLU CB     C  N N 160 
GLU CG     C  N N 161 
GLU CD     C  N N 162 
GLU OE1    O  N N 163 
GLU OE2    O  N N 164 
GLU OXT    O  N N 165 
GLU H      H  N N 166 
GLU H2     H  N N 167 
GLU HA     H  N N 168 
GLU HB2    H  N N 169 
GLU HB3    H  N N 170 
GLU HG2    H  N N 171 
GLU HG3    H  N N 172 
GLU HE2    H  N N 173 
GLU HXT    H  N N 174 
GLY N      N  N N 175 
GLY CA     C  N N 176 
GLY C      C  N N 177 
GLY O      O  N N 178 
GLY OXT    O  N N 179 
GLY H      H  N N 180 
GLY H2     H  N N 181 
GLY HA2    H  N N 182 
GLY HA3    H  N N 183 
GLY HXT    H  N N 184 
HIS N      N  N N 185 
HIS CA     C  N S 186 
HIS C      C  N N 187 
HIS O      O  N N 188 
HIS CB     C  N N 189 
HIS CG     C  Y N 190 
HIS ND1    N  Y N 191 
HIS CD2    C  Y N 192 
HIS CE1    C  Y N 193 
HIS NE2    N  Y N 194 
HIS OXT    O  N N 195 
HIS H      H  N N 196 
HIS H2     H  N N 197 
HIS HA     H  N N 198 
HIS HB2    H  N N 199 
HIS HB3    H  N N 200 
HIS HD1    H  N N 201 
HIS HD2    H  N N 202 
HIS HE1    H  N N 203 
HIS HE2    H  N N 204 
HIS HXT    H  N N 205 
HOH O      O  N N 206 
HOH H1     H  N N 207 
HOH H2     H  N N 208 
ILE N      N  N N 209 
ILE CA     C  N S 210 
ILE C      C  N N 211 
ILE O      O  N N 212 
ILE CB     C  N S 213 
ILE CG1    C  N N 214 
ILE CG2    C  N N 215 
ILE CD1    C  N N 216 
ILE OXT    O  N N 217 
ILE H      H  N N 218 
ILE H2     H  N N 219 
ILE HA     H  N N 220 
ILE HB     H  N N 221 
ILE HG12   H  N N 222 
ILE HG13   H  N N 223 
ILE HG21   H  N N 224 
ILE HG22   H  N N 225 
ILE HG23   H  N N 226 
ILE HD11   H  N N 227 
ILE HD12   H  N N 228 
ILE HD13   H  N N 229 
ILE HXT    H  N N 230 
LEU N      N  N N 231 
LEU CA     C  N S 232 
LEU C      C  N N 233 
LEU O      O  N N 234 
LEU CB     C  N N 235 
LEU CG     C  N N 236 
LEU CD1    C  N N 237 
LEU CD2    C  N N 238 
LEU OXT    O  N N 239 
LEU H      H  N N 240 
LEU H2     H  N N 241 
LEU HA     H  N N 242 
LEU HB2    H  N N 243 
LEU HB3    H  N N 244 
LEU HG     H  N N 245 
LEU HD11   H  N N 246 
LEU HD12   H  N N 247 
LEU HD13   H  N N 248 
LEU HD21   H  N N 249 
LEU HD22   H  N N 250 
LEU HD23   H  N N 251 
LEU HXT    H  N N 252 
LYS N      N  N N 253 
LYS CA     C  N S 254 
LYS C      C  N N 255 
LYS O      O  N N 256 
LYS CB     C  N N 257 
LYS CG     C  N N 258 
LYS CD     C  N N 259 
LYS CE     C  N N 260 
LYS NZ     N  N N 261 
LYS OXT    O  N N 262 
LYS H      H  N N 263 
LYS H2     H  N N 264 
LYS HA     H  N N 265 
LYS HB2    H  N N 266 
LYS HB3    H  N N 267 
LYS HG2    H  N N 268 
LYS HG3    H  N N 269 
LYS HD2    H  N N 270 
LYS HD3    H  N N 271 
LYS HE2    H  N N 272 
LYS HE3    H  N N 273 
LYS HZ1    H  N N 274 
LYS HZ2    H  N N 275 
LYS HZ3    H  N N 276 
LYS HXT    H  N N 277 
MET N      N  N N 278 
MET CA     C  N S 279 
MET C      C  N N 280 
MET O      O  N N 281 
MET CB     C  N N 282 
MET CG     C  N N 283 
MET SD     S  N N 284 
MET CE     C  N N 285 
MET OXT    O  N N 286 
MET H      H  N N 287 
MET H2     H  N N 288 
MET HA     H  N N 289 
MET HB2    H  N N 290 
MET HB3    H  N N 291 
MET HG2    H  N N 292 
MET HG3    H  N N 293 
MET HE1    H  N N 294 
MET HE2    H  N N 295 
MET HE3    H  N N 296 
MET HXT    H  N N 297 
MG  MG     MG N N 298 
PHE N      N  N N 299 
PHE CA     C  N S 300 
PHE C      C  N N 301 
PHE O      O  N N 302 
PHE CB     C  N N 303 
PHE CG     C  Y N 304 
PHE CD1    C  Y N 305 
PHE CD2    C  Y N 306 
PHE CE1    C  Y N 307 
PHE CE2    C  Y N 308 
PHE CZ     C  Y N 309 
PHE OXT    O  N N 310 
PHE H      H  N N 311 
PHE H2     H  N N 312 
PHE HA     H  N N 313 
PHE HB2    H  N N 314 
PHE HB3    H  N N 315 
PHE HD1    H  N N 316 
PHE HD2    H  N N 317 
PHE HE1    H  N N 318 
PHE HE2    H  N N 319 
PHE HZ     H  N N 320 
PHE HXT    H  N N 321 
PRO N      N  N N 322 
PRO CA     C  N S 323 
PRO C      C  N N 324 
PRO O      O  N N 325 
PRO CB     C  N N 326 
PRO CG     C  N N 327 
PRO CD     C  N N 328 
PRO OXT    O  N N 329 
PRO H      H  N N 330 
PRO HA     H  N N 331 
PRO HB2    H  N N 332 
PRO HB3    H  N N 333 
PRO HG2    H  N N 334 
PRO HG3    H  N N 335 
PRO HD2    H  N N 336 
PRO HD3    H  N N 337 
PRO HXT    H  N N 338 
SER N      N  N N 339 
SER CA     C  N S 340 
SER C      C  N N 341 
SER O      O  N N 342 
SER CB     C  N N 343 
SER OG     O  N N 344 
SER OXT    O  N N 345 
SER H      H  N N 346 
SER H2     H  N N 347 
SER HA     H  N N 348 
SER HB2    H  N N 349 
SER HB3    H  N N 350 
SER HG     H  N N 351 
SER HXT    H  N N 352 
THR N      N  N N 353 
THR CA     C  N S 354 
THR C      C  N N 355 
THR O      O  N N 356 
THR CB     C  N R 357 
THR OG1    O  N N 358 
THR CG2    C  N N 359 
THR OXT    O  N N 360 
THR H      H  N N 361 
THR H2     H  N N 362 
THR HA     H  N N 363 
THR HB     H  N N 364 
THR HG1    H  N N 365 
THR HG21   H  N N 366 
THR HG22   H  N N 367 
THR HG23   H  N N 368 
THR HXT    H  N N 369 
TRP N      N  N N 370 
TRP CA     C  N S 371 
TRP C      C  N N 372 
TRP O      O  N N 373 
TRP CB     C  N N 374 
TRP CG     C  Y N 375 
TRP CD1    C  Y N 376 
TRP CD2    C  Y N 377 
TRP NE1    N  Y N 378 
TRP CE2    C  Y N 379 
TRP CE3    C  Y N 380 
TRP CZ2    C  Y N 381 
TRP CZ3    C  Y N 382 
TRP CH2    C  Y N 383 
TRP OXT    O  N N 384 
TRP H      H  N N 385 
TRP H2     H  N N 386 
TRP HA     H  N N 387 
TRP HB2    H  N N 388 
TRP HB3    H  N N 389 
TRP HD1    H  N N 390 
TRP HE1    H  N N 391 
TRP HE3    H  N N 392 
TRP HZ2    H  N N 393 
TRP HZ3    H  N N 394 
TRP HH2    H  N N 395 
TRP HXT    H  N N 396 
TYR N      N  N N 397 
TYR CA     C  N S 398 
TYR C      C  N N 399 
TYR O      O  N N 400 
TYR CB     C  N N 401 
TYR CG     C  Y N 402 
TYR CD1    C  Y N 403 
TYR CD2    C  Y N 404 
TYR CE1    C  Y N 405 
TYR CE2    C  Y N 406 
TYR CZ     C  Y N 407 
TYR OH     O  N N 408 
TYR OXT    O  N N 409 
TYR H      H  N N 410 
TYR H2     H  N N 411 
TYR HA     H  N N 412 
TYR HB2    H  N N 413 
TYR HB3    H  N N 414 
TYR HD1    H  N N 415 
TYR HD2    H  N N 416 
TYR HE1    H  N N 417 
TYR HE2    H  N N 418 
TYR HH     H  N N 419 
TYR HXT    H  N N 420 
VAL N      N  N N 421 
VAL CA     C  N S 422 
VAL C      C  N N 423 
VAL O      O  N N 424 
VAL CB     C  N N 425 
VAL CG1    C  N N 426 
VAL CG2    C  N N 427 
VAL OXT    O  N N 428 
VAL H      H  N N 429 
VAL H2     H  N N 430 
VAL HA     H  N N 431 
VAL HB     H  N N 432 
VAL HG11   H  N N 433 
VAL HG12   H  N N 434 
VAL HG13   H  N N 435 
VAL HG21   H  N N 436 
VAL HG22   H  N N 437 
VAL HG23   H  N N 438 
VAL HXT    H  N N 439 
# 
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 
ALA N     CA     sing N N 1   
ALA N     H      sing N N 2   
ALA N     H2     sing N N 3   
ALA CA    C      sing N N 4   
ALA CA    CB     sing N N 5   
ALA CA    HA     sing N N 6   
ALA C     O      doub N N 7   
ALA C     OXT    sing N N 8   
ALA CB    HB1    sing N N 9   
ALA CB    HB2    sing N N 10  
ALA CB    HB3    sing N N 11  
ALA OXT   HXT    sing N N 12  
ANP PG    O1G    doub N N 13  
ANP PG    O2G    sing N N 14  
ANP PG    O3G    sing N N 15  
ANP PG    N3B    sing N N 16  
ANP O2G   HOG2   sing N N 17  
ANP O3G   HOG3   sing N N 18  
ANP PB    O1B    doub N N 19  
ANP PB    O2B    sing N N 20  
ANP PB    N3B    sing N N 21  
ANP PB    O3A    sing N N 22  
ANP O2B   HOB2   sing N N 23  
ANP N3B   HNB1   sing N N 24  
ANP PA    O1A    doub N N 25  
ANP PA    O2A    sing N N 26  
ANP PA    O3A    sing N N 27  
ANP PA    "O5'"  sing N N 28  
ANP O2A   HOA2   sing N N 29  
ANP "O5'" "C5'"  sing N N 30  
ANP "C5'" "C4'"  sing N N 31  
ANP "C5'" "H5'1" sing N N 32  
ANP "C5'" "H5'2" sing N N 33  
ANP "C4'" "O4'"  sing N N 34  
ANP "C4'" "C3'"  sing N N 35  
ANP "C4'" "H4'"  sing N N 36  
ANP "O4'" "C1'"  sing N N 37  
ANP "C3'" "O3'"  sing N N 38  
ANP "C3'" "C2'"  sing N N 39  
ANP "C3'" "H3'"  sing N N 40  
ANP "O3'" "HO3'" sing N N 41  
ANP "C2'" "O2'"  sing N N 42  
ANP "C2'" "C1'"  sing N N 43  
ANP "C2'" "H2'"  sing N N 44  
ANP "O2'" "HO2'" sing N N 45  
ANP "C1'" N9     sing N N 46  
ANP "C1'" "H1'"  sing N N 47  
ANP N9    C8     sing Y N 48  
ANP N9    C4     sing Y N 49  
ANP C8    N7     doub Y N 50  
ANP C8    H8     sing N N 51  
ANP N7    C5     sing Y N 52  
ANP C5    C6     sing Y N 53  
ANP C5    C4     doub Y N 54  
ANP C6    N6     sing N N 55  
ANP C6    N1     doub Y N 56  
ANP N6    HN61   sing N N 57  
ANP N6    HN62   sing N N 58  
ANP N1    C2     sing Y N 59  
ANP C2    N3     doub Y N 60  
ANP C2    H2     sing N N 61  
ANP N3    C4     sing Y N 62  
ARG N     CA     sing N N 63  
ARG N     H      sing N N 64  
ARG N     H2     sing N N 65  
ARG CA    C      sing N N 66  
ARG CA    CB     sing N N 67  
ARG CA    HA     sing N N 68  
ARG C     O      doub N N 69  
ARG C     OXT    sing N N 70  
ARG CB    CG     sing N N 71  
ARG CB    HB2    sing N N 72  
ARG CB    HB3    sing N N 73  
ARG CG    CD     sing N N 74  
ARG CG    HG2    sing N N 75  
ARG CG    HG3    sing N N 76  
ARG CD    NE     sing N N 77  
ARG CD    HD2    sing N N 78  
ARG CD    HD3    sing N N 79  
ARG NE    CZ     sing N N 80  
ARG NE    HE     sing N N 81  
ARG CZ    NH1    sing N N 82  
ARG CZ    NH2    doub N N 83  
ARG NH1   HH11   sing N N 84  
ARG NH1   HH12   sing N N 85  
ARG NH2   HH21   sing N N 86  
ARG NH2   HH22   sing N N 87  
ARG OXT   HXT    sing N N 88  
ASN N     CA     sing N N 89  
ASN N     H      sing N N 90  
ASN N     H2     sing N N 91  
ASN CA    C      sing N N 92  
ASN CA    CB     sing N N 93  
ASN CA    HA     sing N N 94  
ASN C     O      doub N N 95  
ASN C     OXT    sing N N 96  
ASN CB    CG     sing N N 97  
ASN CB    HB2    sing N N 98  
ASN CB    HB3    sing N N 99  
ASN CG    OD1    doub N N 100 
ASN CG    ND2    sing N N 101 
ASN ND2   HD21   sing N N 102 
ASN ND2   HD22   sing N N 103 
ASN OXT   HXT    sing N N 104 
ASP N     CA     sing N N 105 
ASP N     H      sing N N 106 
ASP N     H2     sing N N 107 
ASP CA    C      sing N N 108 
ASP CA    CB     sing N N 109 
ASP CA    HA     sing N N 110 
ASP C     O      doub N N 111 
ASP C     OXT    sing N N 112 
ASP CB    CG     sing N N 113 
ASP CB    HB2    sing N N 114 
ASP CB    HB3    sing N N 115 
ASP CG    OD1    doub N N 116 
ASP CG    OD2    sing N N 117 
ASP OD2   HD2    sing N N 118 
ASP OXT   HXT    sing N N 119 
CYS N     CA     sing N N 120 
CYS N     H      sing N N 121 
CYS N     H2     sing N N 122 
CYS CA    C      sing N N 123 
CYS CA    CB     sing N N 124 
CYS CA    HA     sing N N 125 
CYS C     O      doub N N 126 
CYS C     OXT    sing N N 127 
CYS CB    SG     sing N N 128 
CYS CB    HB2    sing N N 129 
CYS CB    HB3    sing N N 130 
CYS SG    HG     sing N N 131 
CYS OXT   HXT    sing N N 132 
GLN N     CA     sing N N 133 
GLN N     H      sing N N 134 
GLN N     H2     sing N N 135 
GLN CA    C      sing N N 136 
GLN CA    CB     sing N N 137 
GLN CA    HA     sing N N 138 
GLN C     O      doub N N 139 
GLN C     OXT    sing N N 140 
GLN CB    CG     sing N N 141 
GLN CB    HB2    sing N N 142 
GLN CB    HB3    sing N N 143 
GLN CG    CD     sing N N 144 
GLN CG    HG2    sing N N 145 
GLN CG    HG3    sing N N 146 
GLN CD    OE1    doub N N 147 
GLN CD    NE2    sing N N 148 
GLN NE2   HE21   sing N N 149 
GLN NE2   HE22   sing N N 150 
GLN OXT   HXT    sing N N 151 
GLU N     CA     sing N N 152 
GLU N     H      sing N N 153 
GLU N     H2     sing N N 154 
GLU CA    C      sing N N 155 
GLU CA    CB     sing N N 156 
GLU CA    HA     sing N N 157 
GLU C     O      doub N N 158 
GLU C     OXT    sing N N 159 
GLU CB    CG     sing N N 160 
GLU CB    HB2    sing N N 161 
GLU CB    HB3    sing N N 162 
GLU CG    CD     sing N N 163 
GLU CG    HG2    sing N N 164 
GLU CG    HG3    sing N N 165 
GLU CD    OE1    doub N N 166 
GLU CD    OE2    sing N N 167 
GLU OE2   HE2    sing N N 168 
GLU OXT   HXT    sing N N 169 
GLY N     CA     sing N N 170 
GLY N     H      sing N N 171 
GLY N     H2     sing N N 172 
GLY CA    C      sing N N 173 
GLY CA    HA2    sing N N 174 
GLY CA    HA3    sing N N 175 
GLY C     O      doub N N 176 
GLY C     OXT    sing N N 177 
GLY OXT   HXT    sing N N 178 
HIS N     CA     sing N N 179 
HIS N     H      sing N N 180 
HIS N     H2     sing N N 181 
HIS CA    C      sing N N 182 
HIS CA    CB     sing N N 183 
HIS CA    HA     sing N N 184 
HIS C     O      doub N N 185 
HIS C     OXT    sing N N 186 
HIS CB    CG     sing N N 187 
HIS CB    HB2    sing N N 188 
HIS CB    HB3    sing N N 189 
HIS CG    ND1    sing Y N 190 
HIS CG    CD2    doub Y N 191 
HIS ND1   CE1    doub Y N 192 
HIS ND1   HD1    sing N N 193 
HIS CD2   NE2    sing Y N 194 
HIS CD2   HD2    sing N N 195 
HIS CE1   NE2    sing Y N 196 
HIS CE1   HE1    sing N N 197 
HIS NE2   HE2    sing N N 198 
HIS OXT   HXT    sing N N 199 
HOH O     H1     sing N N 200 
HOH O     H2     sing N N 201 
ILE N     CA     sing N N 202 
ILE N     H      sing N N 203 
ILE N     H2     sing N N 204 
ILE CA    C      sing N N 205 
ILE CA    CB     sing N N 206 
ILE CA    HA     sing N N 207 
ILE C     O      doub N N 208 
ILE C     OXT    sing N N 209 
ILE CB    CG1    sing N N 210 
ILE CB    CG2    sing N N 211 
ILE CB    HB     sing N N 212 
ILE CG1   CD1    sing N N 213 
ILE CG1   HG12   sing N N 214 
ILE CG1   HG13   sing N N 215 
ILE CG2   HG21   sing N N 216 
ILE CG2   HG22   sing N N 217 
ILE CG2   HG23   sing N N 218 
ILE CD1   HD11   sing N N 219 
ILE CD1   HD12   sing N N 220 
ILE CD1   HD13   sing N N 221 
ILE OXT   HXT    sing N N 222 
LEU N     CA     sing N N 223 
LEU N     H      sing N N 224 
LEU N     H2     sing N N 225 
LEU CA    C      sing N N 226 
LEU CA    CB     sing N N 227 
LEU CA    HA     sing N N 228 
LEU C     O      doub N N 229 
LEU C     OXT    sing N N 230 
LEU CB    CG     sing N N 231 
LEU CB    HB2    sing N N 232 
LEU CB    HB3    sing N N 233 
LEU CG    CD1    sing N N 234 
LEU CG    CD2    sing N N 235 
LEU CG    HG     sing N N 236 
LEU CD1   HD11   sing N N 237 
LEU CD1   HD12   sing N N 238 
LEU CD1   HD13   sing N N 239 
LEU CD2   HD21   sing N N 240 
LEU CD2   HD22   sing N N 241 
LEU CD2   HD23   sing N N 242 
LEU OXT   HXT    sing N N 243 
LYS N     CA     sing N N 244 
LYS N     H      sing N N 245 
LYS N     H2     sing N N 246 
LYS CA    C      sing N N 247 
LYS CA    CB     sing N N 248 
LYS CA    HA     sing N N 249 
LYS C     O      doub N N 250 
LYS C     OXT    sing N N 251 
LYS CB    CG     sing N N 252 
LYS CB    HB2    sing N N 253 
LYS CB    HB3    sing N N 254 
LYS CG    CD     sing N N 255 
LYS CG    HG2    sing N N 256 
LYS CG    HG3    sing N N 257 
LYS CD    CE     sing N N 258 
LYS CD    HD2    sing N N 259 
LYS CD    HD3    sing N N 260 
LYS CE    NZ     sing N N 261 
LYS CE    HE2    sing N N 262 
LYS CE    HE3    sing N N 263 
LYS NZ    HZ1    sing N N 264 
LYS NZ    HZ2    sing N N 265 
LYS NZ    HZ3    sing N N 266 
LYS OXT   HXT    sing N N 267 
MET N     CA     sing N N 268 
MET N     H      sing N N 269 
MET N     H2     sing N N 270 
MET CA    C      sing N N 271 
MET CA    CB     sing N N 272 
MET CA    HA     sing N N 273 
MET C     O      doub N N 274 
MET C     OXT    sing N N 275 
MET CB    CG     sing N N 276 
MET CB    HB2    sing N N 277 
MET CB    HB3    sing N N 278 
MET CG    SD     sing N N 279 
MET CG    HG2    sing N N 280 
MET CG    HG3    sing N N 281 
MET SD    CE     sing N N 282 
MET CE    HE1    sing N N 283 
MET CE    HE2    sing N N 284 
MET CE    HE3    sing N N 285 
MET OXT   HXT    sing N N 286 
PHE N     CA     sing N N 287 
PHE N     H      sing N N 288 
PHE N     H2     sing N N 289 
PHE CA    C      sing N N 290 
PHE CA    CB     sing N N 291 
PHE CA    HA     sing N N 292 
PHE C     O      doub N N 293 
PHE C     OXT    sing N N 294 
PHE CB    CG     sing N N 295 
PHE CB    HB2    sing N N 296 
PHE CB    HB3    sing N N 297 
PHE CG    CD1    doub Y N 298 
PHE CG    CD2    sing Y N 299 
PHE CD1   CE1    sing Y N 300 
PHE CD1   HD1    sing N N 301 
PHE CD2   CE2    doub Y N 302 
PHE CD2   HD2    sing N N 303 
PHE CE1   CZ     doub Y N 304 
PHE CE1   HE1    sing N N 305 
PHE CE2   CZ     sing Y N 306 
PHE CE2   HE2    sing N N 307 
PHE CZ    HZ     sing N N 308 
PHE OXT   HXT    sing N N 309 
PRO N     CA     sing N N 310 
PRO N     CD     sing N N 311 
PRO N     H      sing N N 312 
PRO CA    C      sing N N 313 
PRO CA    CB     sing N N 314 
PRO CA    HA     sing N N 315 
PRO C     O      doub N N 316 
PRO C     OXT    sing N N 317 
PRO CB    CG     sing N N 318 
PRO CB    HB2    sing N N 319 
PRO CB    HB3    sing N N 320 
PRO CG    CD     sing N N 321 
PRO CG    HG2    sing N N 322 
PRO CG    HG3    sing N N 323 
PRO CD    HD2    sing N N 324 
PRO CD    HD3    sing N N 325 
PRO OXT   HXT    sing N N 326 
SER N     CA     sing N N 327 
SER N     H      sing N N 328 
SER N     H2     sing N N 329 
SER CA    C      sing N N 330 
SER CA    CB     sing N N 331 
SER CA    HA     sing N N 332 
SER C     O      doub N N 333 
SER C     OXT    sing N N 334 
SER CB    OG     sing N N 335 
SER CB    HB2    sing N N 336 
SER CB    HB3    sing N N 337 
SER OG    HG     sing N N 338 
SER OXT   HXT    sing N N 339 
THR N     CA     sing N N 340 
THR N     H      sing N N 341 
THR N     H2     sing N N 342 
THR CA    C      sing N N 343 
THR CA    CB     sing N N 344 
THR CA    HA     sing N N 345 
THR C     O      doub N N 346 
THR C     OXT    sing N N 347 
THR CB    OG1    sing N N 348 
THR CB    CG2    sing N N 349 
THR CB    HB     sing N N 350 
THR OG1   HG1    sing N N 351 
THR CG2   HG21   sing N N 352 
THR CG2   HG22   sing N N 353 
THR CG2   HG23   sing N N 354 
THR OXT   HXT    sing N N 355 
TRP N     CA     sing N N 356 
TRP N     H      sing N N 357 
TRP N     H2     sing N N 358 
TRP CA    C      sing N N 359 
TRP CA    CB     sing N N 360 
TRP CA    HA     sing N N 361 
TRP C     O      doub N N 362 
TRP C     OXT    sing N N 363 
TRP CB    CG     sing N N 364 
TRP CB    HB2    sing N N 365 
TRP CB    HB3    sing N N 366 
TRP CG    CD1    doub Y N 367 
TRP CG    CD2    sing Y N 368 
TRP CD1   NE1    sing Y N 369 
TRP CD1   HD1    sing N N 370 
TRP CD2   CE2    doub Y N 371 
TRP CD2   CE3    sing Y N 372 
TRP NE1   CE2    sing Y N 373 
TRP NE1   HE1    sing N N 374 
TRP CE2   CZ2    sing Y N 375 
TRP CE3   CZ3    doub Y N 376 
TRP CE3   HE3    sing N N 377 
TRP CZ2   CH2    doub Y N 378 
TRP CZ2   HZ2    sing N N 379 
TRP CZ3   CH2    sing Y N 380 
TRP CZ3   HZ3    sing N N 381 
TRP CH2   HH2    sing N N 382 
TRP OXT   HXT    sing N N 383 
TYR N     CA     sing N N 384 
TYR N     H      sing N N 385 
TYR N     H2     sing N N 386 
TYR CA    C      sing N N 387 
TYR CA    CB     sing N N 388 
TYR CA    HA     sing N N 389 
TYR C     O      doub N N 390 
TYR C     OXT    sing N N 391 
TYR CB    CG     sing N N 392 
TYR CB    HB2    sing N N 393 
TYR CB    HB3    sing N N 394 
TYR CG    CD1    doub Y N 395 
TYR CG    CD2    sing Y N 396 
TYR CD1   CE1    sing Y N 397 
TYR CD1   HD1    sing N N 398 
TYR CD2   CE2    doub Y N 399 
TYR CD2   HD2    sing N N 400 
TYR CE1   CZ     doub Y N 401 
TYR CE1   HE1    sing N N 402 
TYR CE2   CZ     sing Y N 403 
TYR CE2   HE2    sing N N 404 
TYR CZ    OH     sing N N 405 
TYR OH    HH     sing N N 406 
TYR OXT   HXT    sing N N 407 
VAL N     CA     sing N N 408 
VAL N     H      sing N N 409 
VAL N     H2     sing N N 410 
VAL CA    C      sing N N 411 
VAL CA    CB     sing N N 412 
VAL CA    HA     sing N N 413 
VAL C     O      doub N N 414 
VAL C     OXT    sing N N 415 
VAL CB    CG1    sing N N 416 
VAL CB    CG2    sing N N 417 
VAL CB    HB     sing N N 418 
VAL CG1   HG11   sing N N 419 
VAL CG1   HG12   sing N N 420 
VAL CG1   HG13   sing N N 421 
VAL CG2   HG21   sing N N 422 
VAL CG2   HG22   sing N N 423 
VAL CG2   HG23   sing N N 424 
VAL OXT   HXT    sing N N 425 
# 
_pdbx_audit_support.funding_organization   'Agence Nationale de la Recherche (ANR)' 
_pdbx_audit_support.country                France 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             '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                    9H7Y 
_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]   0.011742 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007998 
_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]   0.007516 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLY A 1 1   ? -33.991 -68.503 -29.487 1   146.58 ? -2  GLY A N     1 
ATOM   2    C  CA    . GLY A 1 1   ? -34.533 -69.693 -28.838 1   147.22 ? -2  GLY A CA    1 
ATOM   3    C  C     . GLY A 1 1   ? -34.66  -69.557 -27.332 1   147.47 ? -2  GLY A C     1 
ATOM   4    O  O     . GLY A 1 1   ? -33.687 -69.192 -26.664 1   147.64 ? -2  GLY A O     1 
ATOM   5    N  N     . GLU A 1 2   ? -35.86  -69.852 -26.769 1   147.19 ? -1  GLU A N     1 
ATOM   6    C  CA    . GLU A 1 2   ? -36.045 -69.719 -25.321 1   147.27 ? -1  GLU A CA    1 
ATOM   7    C  C     . GLU A 1 2   ? -36.019 -71.066 -24.57  1   147.47 ? -1  GLU A C     1 
ATOM   8    O  O     . GLU A 1 2   ? -36.552 -71.163 -23.463 1   147.59 ? -1  GLU A O     1 
ATOM   9    C  CB    . GLU A 1 2   ? -37.285 -68.89  -24.947 1   148.73 ? -1  GLU A CB    1 
ATOM   10   C  CG    . GLU A 1 2   ? -37.307 -67.46  -25.497 1   151.71 ? -1  GLU A CG    1 
ATOM   11   C  CD    . GLU A 1 2   ? -36.03  -66.633 -25.586 1   154.1  ? -1  GLU A CD    1 
ATOM   12   O  OE1   . GLU A 1 2   ? -35.729 -66.138 -26.696 1   153.44 ? -1  GLU A OE1   1 
ATOM   13   O  OE2   . GLU A 1 2   ? -35.357 -66.437 -24.549 1   155.42 ? -1  GLU A OE2   1 
ATOM   14   N  N     . PHE A 1 3   ? -35.366 -72.088 -25.16  1   147.26 ? 0   PHE A N     1 
ATOM   15   C  CA    . PHE A 1 3   ? -35.15  -73.398 -24.532 1   147.41 ? 0   PHE A CA    1 
ATOM   16   C  C     . PHE A 1 3   ? -33.728 -73.388 -23.961 1   147.33 ? 0   PHE A C     1 
ATOM   17   O  O     . PHE A 1 3   ? -32.798 -72.945 -24.641 1   147.56 ? 0   PHE A O     1 
ATOM   18   C  CB    . PHE A 1 3   ? -35.3   -74.539 -25.551 1   147.46 ? 0   PHE A CB    1 
ATOM   19   C  CG    . PHE A 1 3   ? -34.892 -75.917 -25.06  1   148.18 ? 0   PHE A CG    1 
ATOM   20   C  CD1   . PHE A 1 3   ? -35.545 -76.517 -23.998 1   148.77 ? 0   PHE A CD1   1 
ATOM   21   C  CD2   . PHE A 1 3   ? -33.904 -76.638 -25.71  1   148.91 ? 0   PHE A CD2   1 
ATOM   22   C  CE1   . PHE A 1 3   ? -35.183 -77.789 -23.568 1   149.22 ? 0   PHE A CE1   1 
ATOM   23   C  CE2   . PHE A 1 3   ? -33.556 -77.916 -25.283 1   149.32 ? 0   PHE A CE2   1 
ATOM   24   C  CZ    . PHE A 1 3   ? -34.187 -78.475 -24.207 1   148.94 ? 0   PHE A CZ    1 
ATOM   25   N  N     . MET A 1 4   ? -33.568 -73.836 -22.703 1   146.78 ? 1   MET A N     1 
ATOM   26   C  CA    . MET A 1 4   ? -32.293 -73.851 -21.966 1   146.56 ? 1   MET A CA    1 
ATOM   27   C  C     . MET A 1 4   ? -31.762 -72.44  -21.652 1   145.47 ? 1   MET A C     1 
ATOM   28   O  O     . MET A 1 4   ? -30.563 -72.257 -21.446 1   145.4  ? 1   MET A O     1 
ATOM   29   C  CB    . MET A 1 4   ? -31.222 -74.72  -22.645 1   147.58 ? 1   MET A CB    1 
ATOM   30   C  CG    . MET A 1 4   ? -31.662 -76.155 -22.845 1   150.36 ? 1   MET A CG    1 
ATOM   31   S  SD    . MET A 1 4   ? -31.851 -77.119 -21.323 1   155.11 ? 1   MET A SD    1 
ATOM   32   C  CE    . MET A 1 4   ? -30.146 -77.257 -20.841 1   153.74 ? 1   MET A CE    1 
ATOM   33   N  N     . VAL A 1 5   ? -32.663 -71.462 -21.566 1   144.5  ? 2   VAL A N     1 
ATOM   34   C  CA    . VAL A 1 5   ? -32.285 -70.108 -21.222 1   144.36 ? 2   VAL A CA    1 
ATOM   35   C  C     . VAL A 1 5   ? -31.856 -69.966 -19.77  1   144.06 ? 2   VAL A C     1 
ATOM   36   O  O     . VAL A 1 5   ? -31.098 -69.05  -19.463 1   144.25 ? 2   VAL A O     1 
ATOM   37   C  CB    . VAL A 1 5   ? -33.375 -69.097 -21.584 1   145.23 ? 2   VAL A CB    1 
ATOM   38   C  CG1   . VAL A 1 5   ? -33.436 -68.901 -23.088 1   145.86 ? 2   VAL A CG1   1 
ATOM   39   C  CG2   . VAL A 1 5   ? -34.728 -69.52  -21.021 1   145.67 ? 2   VAL A CG2   1 
ATOM   40   N  N     . SER A 1 6   ? -32.301 -70.869 -18.881 1   143.56 ? 3   SER A N     1 
ATOM   41   C  CA    . SER A 1 6   ? -31.937 -70.829 -17.464 1   143.75 ? 3   SER A CA    1 
ATOM   42   C  C     . SER A 1 6   ? -30.435 -71.012 -17.206 1   143.77 ? 3   SER A C     1 
ATOM   43   O  O     . SER A 1 6   ? -29.941 -70.61  -16.156 1   143.9  ? 3   SER A O     1 
ATOM   44   C  CB    . SER A 1 6   ? -32.749 -71.841 -16.668 1   145.02 ? 3   SER A CB    1 
ATOM   45   O  OG    . SER A 1 6   ? -34.1   -71.426 -16.567 1   147.24 ? 3   SER A OG    1 
ATOM   46   N  N     . ILE A 1 7   ? -29.712 -71.61  -18.153 1   143.51 ? 4   ILE A N     1 
ATOM   47   C  CA    . ILE A 1 7   ? -28.263 -71.77  -18.041 1   143.84 ? 4   ILE A CA    1 
ATOM   48   C  C     . ILE A 1 7   ? -27.496 -70.862 -19.017 1   143.76 ? 4   ILE A C     1 
ATOM   49   O  O     . ILE A 1 7   ? -26.319 -71.095 -19.273 1   143.6  ? 4   ILE A O     1 
ATOM   50   C  CB    . ILE A 1 7   ? -27.854 -73.248 -18.196 1   144.67 ? 4   ILE A CB    1 
ATOM   51   C  CG1   . ILE A 1 7   ? -28.474 -73.874 -19.459 1   146.03 ? 4   ILE A CG1   1 
ATOM   52   C  CG2   . ILE A 1 7   ? -28.247 -74.034 -16.965 1   145.21 ? 4   ILE A CG2   1 
ATOM   53   C  CD1   . ILE A 1 7   ? -27.562 -73.96  -20.678 1   147.67 ? 4   ILE A CD1   1 
ATOM   54   N  N     . MET A 1 8   ? -28.154 -69.839 -19.561 1   143.82 ? 5   MET A N     1 
ATOM   55   C  CA    . MET A 1 8   ? -27.533 -68.931 -20.5   1   144.57 ? 5   MET A CA    1 
ATOM   56   C  C     . MET A 1 8   ? -27.232 -67.595 -19.86  1   144.73 ? 5   MET A C     1 
ATOM   57   O  O     . MET A 1 8   ? -28.107 -66.99  -19.246 1   144.9  ? 5   MET A O     1 
ATOM   58   C  CB    . MET A 1 8   ? -28.431 -68.733 -21.716 1   145.79 ? 5   MET A CB    1 
ATOM   59   C  CG    . MET A 1 8   ? -28.022 -69.567 -22.902 1   149.08 ? 5   MET A CG    1 
ATOM   60   S  SD    . MET A 1 8   ? -29.418 -69.94  -23.988 1   156.78 ? 5   MET A SD    1 
ATOM   61   C  CE    . MET A 1 8   ? -30.02  -68.313 -24.298 1   155.71 ? 5   MET A CE    1 
ATOM   62   N  N     . LEU A 1 9   ? -25.989 -67.137 -20.011 1   144.5  ? 6   LEU A N     1 
ATOM   63   C  CA    . LEU A 1 9   ? -25.515 -65.869 -19.488 1   144.67 ? 6   LEU A CA    1 
ATOM   64   C  C     . LEU A 1 9   ? -25.791 -64.802 -20.534 1   145.2  ? 6   LEU A C     1 
ATOM   65   O  O     . LEU A 1 9   ? -26.393 -63.782 -20.225 1   145.25 ? 6   LEU A O     1 
ATOM   66   C  CB    . LEU A 1 9   ? -24.001 -65.964 -19.224 1   144.55 ? 6   LEU A CB    1 
ATOM   67   C  CG    . LEU A 1 9   ? -23.503 -65.397 -17.921 1   145.68 ? 6   LEU A CG    1 
ATOM   68   C  CD1   . LEU A 1 9   ? -23.331 -66.468 -16.888 1   146.23 ? 6   LEU A CD1   1 
ATOM   69   C  CD2   . LEU A 1 9   ? -22.19  -64.715 -18.12  1   146.23 ? 6   LEU A CD2   1 
ATOM   70   N  N     . LEU A 1 10  ? -25.391 -65.059 -21.782 1   145.5  ? 7   LEU A N     1 
ATOM   71   C  CA    . LEU A 1 10  ? -25.533 -64.112 -22.873 1   146.48 ? 7   LEU A CA    1 
ATOM   72   C  C     . LEU A 1 10  ? -26.287 -64.754 -24.026 1   147.62 ? 7   LEU A C     1 
ATOM   73   O  O     . LEU A 1 10  ? -26.131 -65.938 -24.297 1   147.61 ? 7   LEU A O     1 
ATOM   74   C  CB    . LEU A 1 10  ? -24.112 -63.684 -23.31  1   146.57 ? 7   LEU A CB    1 
ATOM   75   C  CG    . LEU A 1 10  ? -23.869 -62.431 -24.182 1   147.76 ? 7   LEU A CG    1 
ATOM   76   C  CD1   . LEU A 1 10  ? -23.689 -62.782 -25.628 1   148.16 ? 7   LEU A CD1   1 
ATOM   77   C  CD2   . LEU A 1 10  ? -24.864 -61.318 -23.935 1   148.39 ? 7   LEU A CD2   1 
ATOM   78   N  N     . LYS A 1 11  ? -27.114 -63.97  -24.7   1   148.61 ? 8   LYS A N     1 
ATOM   79   C  CA    . LYS A 1 11  ? -27.882 -64.446 -25.837 1   150.04 ? 8   LYS A CA    1 
ATOM   80   C  C     . LYS A 1 11  ? -28.006 -63.346 -26.895 1   151.63 ? 8   LYS A C     1 
ATOM   81   O  O     . LYS A 1 11  ? -28.729 -62.376 -26.695 1   151.88 ? 8   LYS A O     1 
ATOM   82   C  CB    . LYS A 1 11  ? -29.27  -64.927 -25.392 1   151.3  ? 8   LYS A CB    1 
ATOM   83   C  CG    . LYS A 1 11  ? -30.113 -65.464 -26.531 1   154.3  ? 8   LYS A CG    1 
ATOM   84   C  CD    . LYS A 1 11  ? -31.545 -65.618 -26.09  1   158.14 ? 8   LYS A CD    1 
ATOM   85   C  CE    . LYS A 1 11  ? -32.356 -66.229 -27.182 1   161.78 ? 8   LYS A CE    1 
ATOM   86   N  NZ    . LYS A 1 11  ? -31.732 -67.485 -27.66  1   164.09 ? 8   LYS A NZ    1 
ATOM   87   N  N     . VAL A 1 12  ? -27.291 -63.486 -28.007 1   152.42 ? 9   VAL A N     1 
ATOM   88   C  CA    . VAL A 1 12  ? -27.369 -62.559 -29.122 1   153.7  ? 9   VAL A CA    1 
ATOM   89   C  C     . VAL A 1 12  ? -28.309 -63.172 -30.141 1   155.13 ? 9   VAL A C     1 
ATOM   90   O  O     . VAL A 1 12  ? -28.038 -64.255 -30.653 1   155.28 ? 9   VAL A O     1 
ATOM   91   C  CB    . VAL A 1 12  ? -25.991 -62.299 -29.747 1   154.45 ? 9   VAL A CB    1 
ATOM   92   C  CG1   . VAL A 1 12  ? -26.102 -61.298 -30.886 1   155.11 ? 9   VAL A CG1   1 
ATOM   93   C  CG2   . VAL A 1 12  ? -25.01  -61.808 -28.698 1   154.95 ? 9   VAL A CG2   1 
ATOM   94   N  N     . GLU A 1 13  ? -29.428 -62.508 -30.415 1   156.1  ? 10  GLU A N     1 
ATOM   95   C  CA    . GLU A 1 13  ? -30.418 -63.021 -31.352 1   157.59 ? 10  GLU A CA    1 
ATOM   96   C  C     . GLU A 1 13  ? -30.458 -62.176 -32.622 1   158.5  ? 10  GLU A C     1 
ATOM   97   O  O     . GLU A 1 13  ? -30.638 -60.966 -32.524 1   158.56 ? 10  GLU A O     1 
ATOM   98   C  CB    . GLU A 1 13  ? -31.801 -63.033 -30.688 1   160.43 ? 10  GLU A CB    1 
ATOM   99   C  CG    . GLU A 1 13  ? -32.432 -64.413 -30.625 1   166.37 ? 10  GLU A CG    1 
ATOM   100  C  CD    . GLU A 1 13  ? -33.829 -64.457 -30.034 1   173.93 ? 10  GLU A CD    1 
ATOM   101  O  OE1   . GLU A 1 13  ? -34.37  -65.576 -29.868 1   175.63 ? 10  GLU A OE1   1 
ATOM   102  O  OE2   . GLU A 1 13  ? -34.39  -63.373 -29.751 1   176    ? 10  GLU A OE2   1 
ATOM   103  N  N     . ASP A 1 14  ? -30.284 -62.82  -33.809 1   158.97 ? 11  ASP A N     1 
ATOM   104  C  CA    . ASP A 1 14  ? -30.296 -62.238 -35.169 1   159.85 ? 11  ASP A CA    1 
ATOM   105  C  C     . ASP A 1 14  ? -29.863 -60.771 -35.218 1   160.07 ? 11  ASP A C     1 
ATOM   106  O  O     . ASP A 1 14  ? -30.642 -59.901 -35.595 1   160.04 ? 11  ASP A O     1 
ATOM   107  C  CB    . ASP A 1 14  ? -31.674 -62.435 -35.832 1   162.18 ? 11  ASP A CB    1 
ATOM   108  C  CG    . ASP A 1 14  ? -31.674 -62.257 -37.34  1   167.67 ? 11  ASP A CG    1 
ATOM   109  O  OD1   . ASP A 1 14  ? -31.714 -61.095 -37.801 1   168.19 ? 11  ASP A OD1   1 
ATOM   110  O  OD2   . ASP A 1 14  ? -31.643 -63.281 -38.06  1   170.57 ? 11  ASP A OD2   1 
ATOM   111  N  N     . LEU A 1 15  ? -28.629 -60.505 -34.799 1   160.2  ? 12  LEU A N     1 
ATOM   112  C  CA    . LEU A 1 15  ? -28.081 -59.159 -34.681 1   160.84 ? 12  LEU A CA    1 
ATOM   113  C  C     . LEU A 1 15  ? -27.561 -58.531 -35.973 1   161.63 ? 12  LEU A C     1 
ATOM   114  O  O     . LEU A 1 15  ? -26.675 -59.083 -36.625 1   161.84 ? 12  LEU A O     1 
ATOM   115  C  CB    . LEU A 1 15  ? -26.967 -59.179 -33.644 1   160.89 ? 12  LEU A CB    1 
ATOM   116  C  CG    . LEU A 1 15  ? -26.532 -57.841 -33.123 1   162.2  ? 12  LEU A CG    1 
ATOM   117  C  CD1   . LEU A 1 15  ? -27.518 -57.328 -32.109 1   162.74 ? 12  LEU A CD1   1 
ATOM   118  C  CD2   . LEU A 1 15  ? -25.164 -57.941 -32.505 1   162.85 ? 12  LEU A CD2   1 
ATOM   119  N  N     . HIS A 1 16  ? -28.072 -57.341 -36.304 1   161.88 ? 13  HIS A N     1 
ATOM   120  C  CA    . HIS A 1 16  ? -27.656 -56.593 -37.484 1   162.65 ? 13  HIS A CA    1 
ATOM   121  C  C     . HIS A 1 16  ? -27.04  -55.281 -37.044 1   163.44 ? 13  HIS A C     1 
ATOM   122  O  O     . HIS A 1 16  ? -27.732 -54.444 -36.472 1   163.62 ? 13  HIS A O     1 
ATOM   123  C  CB    . HIS A 1 16  ? -28.845 -56.325 -38.42  1   163.37 ? 13  HIS A CB    1 
ATOM   124  C  CG    . HIS A 1 16  ? -29.374 -57.551 -39.094 1   165.44 ? 13  HIS A CG    1 
ATOM   125  N  ND1   . HIS A 1 16  ? -29.125 -57.806 -40.43  1   167.17 ? 13  HIS A ND1   1 
ATOM   126  C  CD2   . HIS A 1 16  ? -30.12  -58.559 -38.589 1   166.64 ? 13  HIS A CD2   1 
ATOM   127  C  CE1   . HIS A 1 16  ? -29.727 -58.954 -40.694 1   167.74 ? 13  HIS A CE1   1 
ATOM   128  N  NE2   . HIS A 1 16  ? -30.341 -59.443 -39.617 1   167.74 ? 13  HIS A NE2   1 
ATOM   129  N  N     . VAL A 1 17  ? -25.734 -55.109 -37.269 1   163.83 ? 14  VAL A N     1 
ATOM   130  C  CA    . VAL A 1 17  ? -25.05  -53.882 -36.883 1   164.75 ? 14  VAL A CA    1 
ATOM   131  C  C     . VAL A 1 17  ? -24.513 -53.199 -38.134 1   165.75 ? 14  VAL A C     1 
ATOM   132  O  O     . VAL A 1 17  ? -23.82  -53.825 -38.935 1   165.95 ? 14  VAL A O     1 
ATOM   133  C  CB    . VAL A 1 17  ? -23.949 -54.135 -35.825 1   165.37 ? 14  VAL A CB    1 
ATOM   134  C  CG1   . VAL A 1 17  ? -23.268 -52.837 -35.418 1   165.89 ? 14  VAL A CG1   1 
ATOM   135  C  CG2   . VAL A 1 17  ? -24.525 -54.83  -34.603 1   165.89 ? 14  VAL A CG2   1 
ATOM   136  N  N     . TYR A 1 18  ? -24.882 -51.93  -38.33  1   166.2  ? 15  TYR A N     1 
ATOM   137  C  CA    . TYR A 1 18  ? -24.46  -51.156 -39.489 1   167.07 ? 15  TYR A CA    1 
ATOM   138  C  C     . TYR A 1 18  ? -23.435 -50.109 -39.078 1   167.6  ? 15  TYR A C     1 
ATOM   139  O  O     . TYR A 1 18  ? -23.582 -49.479 -38.032 1   167.75 ? 15  TYR A O     1 
ATOM   140  C  CB    . TYR A 1 18  ? -25.668 -50.417 -40.089 1   167.28 ? 15  TYR A CB    1 
ATOM   141  C  CG    . TYR A 1 18  ? -26.445 -51.168 -41.148 1   168.16 ? 15  TYR A CG    1 
ATOM   142  C  CD1   . TYR A 1 18  ? -27.451 -52.056 -40.8   1   169.02 ? 15  TYR A CD1   1 
ATOM   143  C  CD2   . TYR A 1 18  ? -26.262 -50.894 -42.495 1   169.12 ? 15  TYR A CD2   1 
ATOM   144  C  CE1   . TYR A 1 18  ? -28.218 -52.693 -41.767 1   169.9  ? 15  TYR A CE1   1 
ATOM   145  C  CE2   . TYR A 1 18  ? -27.018 -51.528 -43.472 1   169.98 ? 15  TYR A CE2   1 
ATOM   146  C  CZ    . TYR A 1 18  ? -27.995 -52.429 -43.106 1   170.77 ? 15  TYR A CZ    1 
ATOM   147  O  OH    . TYR A 1 18  ? -28.734 -53.054 -44.083 1   172.1  ? 15  TYR A OH    1 
ATOM   148  N  N     . ARG A 1 19  ? -22.424 -49.887 -39.914 1   167.73 ? 16  ARG A N     1 
ATOM   149  C  CA    . ARG A 1 19  ? -21.449 -48.83  -39.678 1   168.32 ? 16  ARG A CA    1 
ATOM   150  C  C     . ARG A 1 19  ? -21.54  -47.929 -40.887 1   168.61 ? 16  ARG A C     1 
ATOM   151  O  O     . ARG A 1 19  ? -20.795 -48.109 -41.847 1   168.68 ? 16  ARG A O     1 
ATOM   152  C  CB    . ARG A 1 19  ? -20.028 -49.383 -39.539 1   169.71 ? 16  ARG A CB    1 
ATOM   153  C  CG    . ARG A 1 19  ? -19.323 -48.905 -38.287 1   172.59 ? 16  ARG A CG    1 
ATOM   154  C  CD    . ARG A 1 19  ? -17.828 -49.09  -38.397 1   175.47 ? 16  ARG A CD    1 
ATOM   155  N  NE    . ARG A 1 19  ? -17.17  -48.933 -37.099 1   178.16 ? 16  ARG A NE    1 
ATOM   156  C  CZ    . ARG A 1 19  ? -16.719 -47.779 -36.617 1   180.4  ? 16  ARG A CZ    1 
ATOM   157  N  NH1   . ARG A 1 19  ? -16.841 -46.663 -37.325 1   180.29 ? 16  ARG A NH1   1 
ATOM   158  N  NH2   . ARG A 1 19  ? -16.133 -47.733 -35.428 1   180.32 ? 16  ARG A NH2   1 
ATOM   159  N  N     . GLY A 1 20  ? -22.498 -47.014 -40.861 1   168.74 ? 17  GLY A N     1 
ATOM   160  C  CA    . GLY A 1 20  ? -22.747 -46.112 -41.975 1   169.44 ? 17  GLY A CA    1 
ATOM   161  C  C     . GLY A 1 20  ? -23.645 -46.78  -42.991 1   169.83 ? 17  GLY A C     1 
ATOM   162  O  O     . GLY A 1 20  ? -24.716 -47.271 -42.635 1   169.93 ? 17  GLY A O     1 
ATOM   163  N  N     . ASN A 1 21  ? -23.206 -46.843 -44.248 1   169.88 ? 18  ASN A N     1 
ATOM   164  C  CA    . ASN A 1 21  ? -23.982 -47.501 -45.297 1   170.45 ? 18  ASN A CA    1 
ATOM   165  C  C     . ASN A 1 21  ? -23.75  -49.027 -45.327 1   170.47 ? 18  ASN A C     1 
ATOM   166  O  O     . ASN A 1 21  ? -24.588 -49.76  -45.853 1   170.6  ? 18  ASN A O     1 
ATOM   167  C  CB    . ASN A 1 21  ? -23.668 -46.889 -46.664 1   172.02 ? 18  ASN A CB    1 
ATOM   168  C  CG    . ASN A 1 21  ? -23.869 -45.394 -46.739 1   175.68 ? 18  ASN A CG    1 
ATOM   169  O  OD1   . ASN A 1 21  ? -23.365 -44.629 -45.904 1   177.08 ? 18  ASN A OD1   1 
ATOM   170  N  ND2   . ASN A 1 21  ? -24.596 -44.942 -47.759 1   176.34 ? 18  ASN A ND2   1 
ATOM   171  N  N     . ARG A 1 22  ? -22.616 -49.501 -44.772 1   170.2  ? 19  ARG A N     1 
ATOM   172  C  CA    . ARG A 1 22  ? -22.254 -50.919 -44.745 1   170.43 ? 19  ARG A CA    1 
ATOM   173  C  C     . ARG A 1 22  ? -22.87  -51.678 -43.576 1   170.18 ? 19  ARG A C     1 
ATOM   174  O  O     . ARG A 1 22  ? -22.859 -51.188 -42.451 1   170.18 ? 19  ARG A O     1 
ATOM   175  C  CB    . ARG A 1 22  ? -20.725 -51.081 -44.662 1   171.98 ? 19  ARG A CB    1 
ATOM   176  C  CG    . ARG A 1 22  ? -19.936 -50.546 -45.86  1   175.31 ? 19  ARG A CG    1 
ATOM   177  C  CD    . ARG A 1 22  ? -19.092 -49.327 -45.514 1   178.5  ? 19  ARG A CD    1 
ATOM   178  N  NE    . ARG A 1 22  ? -18.262 -49.545 -44.325 1   181.12 ? 19  ARG A NE    1 
ATOM   179  C  CZ    . ARG A 1 22  ? -17.559 -48.598 -43.716 1   183.03 ? 19  ARG A CZ    1 
ATOM   180  N  NH1   . ARG A 1 22  ? -17.562 -47.355 -44.182 1   182.5  ? 19  ARG A NH1   1 
ATOM   181  N  NH2   . ARG A 1 22  ? -16.845 -48.886 -42.636 1   182.95 ? 19  ARG A NH2   1 
ATOM   182  N  N     . GLU A 1 23  ? -23.347 -52.901 -43.829 1   169.8  ? 20  GLU A N     1 
ATOM   183  C  CA    . GLU A 1 23  ? -23.876 -53.765 -42.778 1   169.9  ? 20  GLU A CA    1 
ATOM   184  C  C     . GLU A 1 23  ? -22.728 -54.71  -42.421 1   169.06 ? 20  GLU A C     1 
ATOM   185  O  O     . GLU A 1 23  ? -22.322 -55.496 -43.274 1   169.46 ? 20  GLU A O     1 
ATOM   186  C  CB    . GLU A 1 23  ? -25.074 -54.579 -43.303 1   172.91 ? 20  GLU A CB    1 
ATOM   187  C  CG    . GLU A 1 23  ? -25.807 -55.366 -42.228 1   178.76 ? 20  GLU A CG    1 
ATOM   188  C  CD    . GLU A 1 23  ? -26.835 -56.354 -42.748 1   186.54 ? 20  GLU A CD    1 
ATOM   189  O  OE1   . GLU A 1 23  ? -26.78  -56.695 -43.953 1   188.16 ? 20  GLU A OE1   1 
ATOM   190  O  OE2   . GLU A 1 23  ? -27.694 -56.791 -41.948 1   188.98 ? 20  GLU A OE2   1 
ATOM   191  N  N     . ILE A 1 24  ? -22.16  -54.606 -41.208 1   167.74 ? 21  ILE A N     1 
ATOM   192  C  CA    . ILE A 1 24  ? -21.047 -55.481 -40.826 1   167.1  ? 21  ILE A CA    1 
ATOM   193  C  C     . ILE A 1 24  ? -21.579 -56.82  -40.332 1   166.62 ? 21  ILE A C     1 
ATOM   194  O  O     . ILE A 1 24  ? -21.173 -57.861 -40.842 1   166.78 ? 21  ILE A O     1 
ATOM   195  C  CB    . ILE A 1 24  ? -20.093 -54.826 -39.8   1   167.43 ? 21  ILE A CB    1 
ATOM   196  C  CG1   . ILE A 1 24  ? -19.412 -53.586 -40.357 1   168.15 ? 21  ILE A CG1   1 
ATOM   197  C  CG2   . ILE A 1 24  ? -19.068 -55.832 -39.261 1   168.05 ? 21  ILE A CG2   1 
ATOM   198  C  CD1   . ILE A 1 24  ? -19.08  -52.68  -39.283 1   169.58 ? 21  ILE A CD1   1 
ATOM   199  N  N     . LEU A 1 25  ? -22.486 -56.799 -39.345 1   165.91 ? 22  LEU A N     1 
ATOM   200  C  CA    . LEU A 1 25  ? -23.073 -58.026 -38.826 1   165.75 ? 22  LEU A CA    1 
ATOM   201  C  C     . LEU A 1 25  ? -24.411 -58.223 -39.514 1   165.24 ? 22  LEU A C     1 
ATOM   202  O  O     . LEU A 1 25  ? -25.248 -57.326 -39.491 1   165.43 ? 22  LEU A O     1 
ATOM   203  C  CB    . LEU A 1 25  ? -23.239 -57.963 -37.302 1   166.1  ? 22  LEU A CB    1 
ATOM   204  C  CG    . LEU A 1 25  ? -21.965 -57.72  -36.487 1   167.77 ? 22  LEU A CG    1 
ATOM   205  C  CD1   . LEU A 1 25  ? -22.269 -57.756 -35.014 1   168.43 ? 22  LEU A CD1   1 
ATOM   206  C  CD2   . LEU A 1 25  ? -20.882 -58.749 -36.803 1   168.49 ? 22  LEU A CD2   1 
ATOM   207  N  N     . LYS A 1 26  ? -24.588 -59.358 -40.192 1   164.44 ? 23  LYS A N     1 
ATOM   208  C  CA    . LYS A 1 26  ? -25.803 -59.626 -40.954 1   164.12 ? 23  LYS A CA    1 
ATOM   209  C  C     . LYS A 1 26  ? -26.607 -60.798 -40.367 1   163.42 ? 23  LYS A C     1 
ATOM   210  O  O     . LYS A 1 26  ? -26.831 -61.804 -41.041 1   163.54 ? 23  LYS A O     1 
ATOM   211  C  CB    . LYS A 1 26  ? -25.454 -59.881 -42.437 1   165.9  ? 23  LYS A CB    1 
ATOM   212  C  CG    . LYS A 1 26  ? -24.362 -58.967 -43.008 1   169.55 ? 23  LYS A CG    1 
ATOM   213  C  CD    . LYS A 1 26  ? -24.302 -59.015 -44.523 1   173.73 ? 23  LYS A CD    1 
ATOM   214  C  CE    . LYS A 1 26  ? -23.33  -60.041 -45.041 1   177.58 ? 23  LYS A CE    1 
ATOM   215  N  NZ    . LYS A 1 26  ? -23.885 -61.421 -44.976 1   180.18 ? 23  LYS A NZ    1 
ATOM   216  N  N     . GLY A 1 27  ? -27.04  -60.655 -39.122 1   162.5  ? 24  GLY A N     1 
ATOM   217  C  CA    . GLY A 1 27  ? -27.806 -61.693 -38.444 1   162.1  ? 24  GLY A CA    1 
ATOM   218  C  C     . GLY A 1 27  ? -26.932 -62.622 -37.627 1   161.38 ? 24  GLY A C     1 
ATOM   219  O  O     . GLY A 1 27  ? -26.68  -63.76  -38.027 1   161.35 ? 24  GLY A O     1 
ATOM   220  N  N     . VAL A 1 28  ? -26.454 -62.138 -36.476 1   160.63 ? 25  VAL A N     1 
ATOM   221  C  CA    . VAL A 1 28  ? -25.597 -62.936 -35.611 1   160.36 ? 25  VAL A CA    1 
ATOM   222  C  C     . VAL A 1 28  ? -26.401 -63.655 -34.542 1   159.86 ? 25  VAL A C     1 
ATOM   223  O  O     . VAL A 1 28  ? -27.078 -63.015 -33.741 1   159.87 ? 25  VAL A O     1 
ATOM   224  C  CB    . VAL A 1 28  ? -24.465 -62.092 -34.975 1   161.08 ? 25  VAL A CB    1 
ATOM   225  C  CG1   . VAL A 1 28  ? -23.655 -62.92  -33.982 1   161.69 ? 25  VAL A CG1   1 
ATOM   226  C  CG2   . VAL A 1 28  ? -23.561 -61.49  -36.041 1   161.52 ? 25  VAL A CG2   1 
ATOM   227  N  N     . ASN A 1 29  ? -26.33  -64.983 -34.529 1   159.36 ? 26  ASN A N     1 
ATOM   228  C  CA    . ASN A 1 29  ? -26.973 -65.758 -33.483 1   159.46 ? 26  ASN A CA    1 
ATOM   229  C  C     . ASN A 1 29  ? -25.849 -66.423 -32.723 1   159.31 ? 26  ASN A C     1 
ATOM   230  O  O     . ASN A 1 29  ? -25.099 -67.223 -33.279 1   159.58 ? 26  ASN A O     1 
ATOM   231  C  CB    . ASN A 1 29  ? -27.985 -66.769 -34.015 1   160.44 ? 26  ASN A CB    1 
ATOM   232  C  CG    . ASN A 1 29  ? -28.969 -67.193 -32.944 1   162.89 ? 26  ASN A CG    1 
ATOM   233  O  OD1   . ASN A 1 29  ? -29.868 -66.434 -32.549 1   163.64 ? 26  ASN A OD1   1 
ATOM   234  N  ND2   . ASN A 1 29  ? -28.806 -68.406 -32.432 1   163.33 ? 26  ASN A ND2   1 
ATOM   235  N  N     . LEU A 1 30  ? -25.681 -66.029 -31.472 1   158.62 ? 27  LEU A N     1 
ATOM   236  C  CA    . LEU A 1 30  ? -24.602 -66.524 -30.635 1   158.28 ? 27  LEU A CA    1 
ATOM   237  C  C     . LEU A 1 30  ? -25.088 -66.571 -29.182 1   157.91 ? 27  LEU A C     1 
ATOM   238  O  O     . LEU A 1 30  ? -25.775 -65.654 -28.758 1   158.06 ? 27  LEU A O     1 
ATOM   239  C  CB    . LEU A 1 30  ? -23.436 -65.515 -30.783 1   158.26 ? 27  LEU A CB    1 
ATOM   240  C  CG    . LEU A 1 30  ? -22.057 -65.813 -30.173 1   159.46 ? 27  LEU A CG    1 
ATOM   241  C  CD1   . LEU A 1 30  ? -21.92  -65.258 -28.765 1   159.86 ? 27  LEU A CD1   1 
ATOM   242  C  CD2   . LEU A 1 30  ? -21.662 -67.277 -30.303 1   160.11 ? 27  LEU A CD2   1 
ATOM   243  N  N     . THR A 1 31  ? -24.766 -67.628 -28.422 1   157.27 ? 28  THR A N     1 
ATOM   244  C  CA    . THR A 1 31  ? -25.118 -67.675 -26.996 1   157.24 ? 28  THR A CA    1 
ATOM   245  C  C     . THR A 1 31  ? -23.894 -68.033 -26.162 1   156.99 ? 28  THR A C     1 
ATOM   246  O  O     . THR A 1 31  ? -23.03  -68.773 -26.626 1   157.04 ? 28  THR A O     1 
ATOM   247  C  CB    . THR A 1 31  ? -26.304 -68.606 -26.672 1   158.55 ? 28  THR A CB    1 
ATOM   248  O  OG1   . THR A 1 31  ? -25.89  -69.974 -26.665 1   159.65 ? 28  THR A OG1   1 
ATOM   249  C  CG2   . THR A 1 31  ? -27.506 -68.391 -27.577 1   158.93 ? 28  THR A CG2   1 
ATOM   250  N  N     . VAL A 1 32  ? -23.812 -67.509 -24.94  1   156.55 ? 29  VAL A N     1 
ATOM   251  C  CA    . VAL A 1 32  ? -22.73  -67.837 -24.022 1   156.56 ? 29  VAL A CA    1 
ATOM   252  C  C     . VAL A 1 32  ? -23.384 -68.396 -22.782 1   156.46 ? 29  VAL A C     1 
ATOM   253  O  O     . VAL A 1 32  ? -24.24  -67.744 -22.195 1   156.68 ? 29  VAL A O     1 
ATOM   254  C  CB    . VAL A 1 32  ? -21.798 -66.65  -23.695 1   157.2  ? 29  VAL A CB    1 
ATOM   255  C  CG1   . VAL A 1 32  ? -20.788 -67.031 -22.614 1   157.71 ? 29  VAL A CG1   1 
ATOM   256  C  CG2   . VAL A 1 32  ? -21.082 -66.162 -24.947 1   157.69 ? 29  VAL A CG2   1 
ATOM   257  N  N     . GLU A 1 33  ? -23.036 -69.624 -22.419 1   155.98 ? 30  GLU A N     1 
ATOM   258  C  CA    . GLU A 1 33  ? -23.603 -70.298 -21.258 1   155.96 ? 30  GLU A CA    1 
ATOM   259  C  C     . GLU A 1 33  ? -22.752 -70.074 -19.995 1   155.96 ? 30  GLU A C     1 
ATOM   260  O  O     . GLU A 1 33  ? -21.662 -69.505 -20.082 1   156.17 ? 30  GLU A O     1 
ATOM   261  C  CB    . GLU A 1 33  ? -23.842 -71.78  -21.581 1   157.6  ? 30  GLU A CB    1 
ATOM   262  C  CG    . GLU A 1 33  ? -24.685 -71.942 -22.837 1   161.04 ? 30  GLU A CG    1 
ATOM   263  C  CD    . GLU A 1 33  ? -24.909 -73.357 -23.326 1   165.8  ? 30  GLU A CD    1 
ATOM   264  O  OE1   . GLU A 1 33  ? -25.918 -73.585 -24.031 1   166.54 ? 30  GLU A OE1   1 
ATOM   265  O  OE2   . GLU A 1 33  ? -24.076 -74.237 -23.009 1   167.53 ? 30  GLU A OE2   1 
ATOM   266  N  N     . GLU A 1 34  ? -23.274 -70.443 -18.819 1   155.54 ? 31  GLU A N     1 
ATOM   267  C  CA    . GLU A 1 34  ? -22.558 -70.22  -17.564 1   155.69 ? 31  GLU A CA    1 
ATOM   268  C  C     . GLU A 1 34  ? -21.343 -71.128 -17.46  1   155.82 ? 31  GLU A C     1 
ATOM   269  O  O     . GLU A 1 34  ? -21.39  -72.268 -17.92  1   155.93 ? 31  GLU A O     1 
ATOM   270  C  CB    . GLU A 1 34  ? -23.492 -70.37  -16.357 1   157.64 ? 31  GLU A CB    1 
ATOM   271  C  CG    . GLU A 1 34  ? -24.841 -69.708 -16.566 1   162.03 ? 31  GLU A CG    1 
ATOM   272  C  CD    . GLU A 1 34  ? -25.662 -69.504 -15.313 1   168.04 ? 31  GLU A CD    1 
ATOM   273  O  OE1   . GLU A 1 34  ? -26.737 -70.135 -15.19  1   169.48 ? 31  GLU A OE1   1 
ATOM   274  O  OE2   . GLU A 1 34  ? -25.218 -68.721 -14.442 1   169.86 ? 31  GLU A OE2   1 
ATOM   275  N  N     . ASN A 1 35  ? -20.242 -70.597 -16.905 1   155.75 ? 32  ASN A N     1 
ATOM   276  C  CA    . ASN A 1 35  ? -18.949 -71.27  -16.751 1   156.26 ? 32  ASN A CA    1 
ATOM   277  C  C     . ASN A 1 35  ? -18.45  -71.921 -18.047 1   156.53 ? 32  ASN A C     1 
ATOM   278  O  O     . ASN A 1 35  ? -18.021 -73.082 -18.065 1   156.76 ? 32  ASN A O     1 
ATOM   279  C  CB    . ASN A 1 35  ? -18.935 -72.252 -15.581 1   157.35 ? 32  ASN A CB    1 
ATOM   280  C  CG    . ASN A 1 35  ? -17.716 -72.1   -14.686 1   160.22 ? 32  ASN A CG    1 
ATOM   281  O  OD1   . ASN A 1 35  ? -17.511 -72.866 -13.74  1   161.2  ? 32  ASN A OD1   1 
ATOM   282  N  ND2   . ASN A 1 35  ? -16.869 -71.114 -14.963 1   160.9  ? 32  ASN A ND2   1 
ATOM   283  N  N     . GLU A 1 36  ? -18.507 -71.154 -19.134 1   156.19 ? 33  GLU A N     1 
ATOM   284  C  CA    . GLU A 1 36  ? -18.1   -71.638 -20.438 1   156.29 ? 33  GLU A CA    1 
ATOM   285  C  C     . GLU A 1 36  ? -17.051 -70.738 -21.056 1   156.12 ? 33  GLU A C     1 
ATOM   286  O  O     . GLU A 1 36  ? -17.158 -69.513 -20.989 1   156.4  ? 33  GLU A O     1 
ATOM   287  C  CB    . GLU A 1 36  ? -19.335 -71.711 -21.361 1   158.52 ? 33  GLU A CB    1 
ATOM   288  C  CG    . GLU A 1 36  ? -19.056 -71.964 -22.834 1   163.34 ? 33  GLU A CG    1 
ATOM   289  C  CD    . GLU A 1 36  ? -20.287 -71.887 -23.711 1   169.22 ? 33  GLU A CD    1 
ATOM   290  O  OE1   . GLU A 1 36  ? -20.919 -70.809 -23.75  1   169.63 ? 33  GLU A OE1   1 
ATOM   291  O  OE2   . GLU A 1 36  ? -20.627 -72.906 -24.353 1   172.07 ? 33  GLU A OE2   1 
ATOM   292  N  N     . ILE A 1 37  ? -16.053 -71.346 -21.688 1   155.56 ? 34  ILE A N     1 
ATOM   293  C  CA    . ILE A 1 37  ? -15.079 -70.599 -22.459 1   155.57 ? 34  ILE A CA    1 
ATOM   294  C  C     . ILE A 1 37  ? -15.548 -70.796 -23.906 1   155.37 ? 34  ILE A C     1 
ATOM   295  O  O     . ILE A 1 37  ? -15.359 -71.877 -24.468 1   155.71 ? 34  ILE A O     1 
ATOM   296  C  CB    . ILE A 1 37  ? -13.629 -71.087 -22.237 1   156.03 ? 34  ILE A CB    1 
ATOM   297  C  CG1   . ILE A 1 37  ? -13.249 -71.037 -20.74  1   156.71 ? 34  ILE A CG1   1 
ATOM   298  C  CG2   . ILE A 1 37  ? -12.665 -70.255 -23.097 1   156.58 ? 34  ILE A CG2   1 
ATOM   299  C  CD1   . ILE A 1 37  ? -11.814 -71.472 -20.415 1   157.8  ? 34  ILE A CD1   1 
ATOM   300  N  N     . HIS A 1 38  ? -16.265 -69.804 -24.462 1   154.55 ? 35  HIS A N     1 
ATOM   301  C  CA    . HIS A 1 38  ? -16.8   -69.87  -25.822 1   154.22 ? 35  HIS A CA    1 
ATOM   302  C  C     . HIS A 1 38  ? -15.93  -69.008 -26.732 1   154.18 ? 35  HIS A C     1 
ATOM   303  O  O     . HIS A 1 38  ? -15.905 -67.789 -26.588 1   154.52 ? 35  HIS A O     1 
ATOM   304  C  CB    . HIS A 1 38  ? -18.268 -69.392 -25.836 1   154.44 ? 35  HIS A CB    1 
ATOM   305  C  CG    . HIS A 1 38  ? -18.989 -69.56  -27.142 1   155.82 ? 35  HIS A CG    1 
ATOM   306  N  ND1   . HIS A 1 38  ? -20.35  -69.345 -27.24  1   157.37 ? 35  HIS A ND1   1 
ATOM   307  C  CD2   . HIS A 1 38  ? -18.519 -69.911 -28.362 1   156.91 ? 35  HIS A CD2   1 
ATOM   308  C  CE1   . HIS A 1 38  ? -20.661 -69.566 -28.506 1   157.92 ? 35  HIS A CE1   1 
ATOM   309  N  NE2   . HIS A 1 38  ? -19.593 -69.908 -29.218 1   157.97 ? 35  HIS A NE2   1 
ATOM   310  N  N     . ALA A 1 39  ? -15.212 -69.636 -27.664 1   153.69 ? 36  ALA A N     1 
ATOM   311  C  CA    . ALA A 1 39  ? -14.349 -68.908 -28.582 1   153.73 ? 36  ALA A CA    1 
ATOM   312  C  C     . ALA A 1 39  ? -15.059 -68.536 -29.88  1   153.27 ? 36  ALA A C     1 
ATOM   313  O  O     . ALA A 1 39  ? -15.976 -69.225 -30.318 1   153.5  ? 36  ALA A O     1 
ATOM   314  C  CB    . ALA A 1 39  ? -13.098 -69.719 -28.883 1   154.06 ? 36  ALA A CB    1 
ATOM   315  N  N     . ILE A 1 40  ? -14.631 -67.439 -30.493 1   152.44 ? 37  ILE A N     1 
ATOM   316  C  CA    . ILE A 1 40  ? -15.175 -66.994 -31.759 1   152.13 ? 37  ILE A CA    1 
ATOM   317  C  C     . ILE A 1 40  ? -14.032 -66.891 -32.75  1   152.01 ? 37  ILE A C     1 
ATOM   318  O  O     . ILE A 1 40  ? -13.11  -66.111 -32.541 1   152.12 ? 37  ILE A O     1 
ATOM   319  C  CB    . ILE A 1 40  ? -15.963 -65.672 -31.61  1   152.35 ? 37  ILE A CB    1 
ATOM   320  C  CG1   . ILE A 1 40  ? -17.265 -65.916 -30.815 1   153.23 ? 37  ILE A CG1   1 
ATOM   321  C  CG2   . ILE A 1 40  ? -16.243 -65.046 -32.979 1   152.68 ? 37  ILE A CG2   1 
ATOM   322  C  CD1   . ILE A 1 40  ? -18.149 -64.727 -30.612 1   154.39 ? 37  ILE A CD1   1 
ATOM   323  N  N     . ILE A 1 41  ? -14.057 -67.72  -33.796 1   151.65 ? 38  ILE A N     1 
ATOM   324  C  CA    . ILE A 1 41  ? -13.027 -67.688 -34.835 1   151.71 ? 38  ILE A CA    1 
ATOM   325  C  C     . ILE A 1 41  ? -13.557 -67.061 -36.116 1   151.61 ? 38  ILE A C     1 
ATOM   326  O  O     . ILE A 1 41  ? -14.763 -67.03  -36.341 1   151.95 ? 38  ILE A O     1 
ATOM   327  C  CB    . ILE A 1 41  ? -12.382 -69.068 -35.089 1   152.2  ? 38  ILE A CB    1 
ATOM   328  C  CG1   . ILE A 1 41  ? -13.436 -70.112 -35.492 1   153.27 ? 38  ILE A CG1   1 
ATOM   329  C  CG2   . ILE A 1 41  ? -11.563 -69.501 -33.892 1   152.58 ? 38  ILE A CG2   1 
ATOM   330  C  CD1   . ILE A 1 41  ? -12.864 -71.458 -35.962 1   154.65 ? 38  ILE A CD1   1 
ATOM   331  N  N     . GLY A 1 42  ? -12.659 -66.553 -36.934 1   151.07 ? 39  GLY A N     1 
ATOM   332  C  CA    . GLY A 1 42  ? -13.044 -65.937 -38.189 1   151.23 ? 39  GLY A CA    1 
ATOM   333  C  C     . GLY A 1 42  ? -11.9   -65.195 -38.818 1   151.22 ? 39  GLY A C     1 
ATOM   334  O  O     . GLY A 1 42  ? -10.956 -64.784 -38.136 1   151.31 ? 39  GLY A O     1 
ATOM   335  N  N     . PRO A 1 43  ? -11.979 -65.001 -40.139 1   150.89 ? 40  PRO A N     1 
ATOM   336  C  CA    . PRO A 1 43  ? -10.915 -64.264 -40.826 1   150.9  ? 40  PRO A CA    1 
ATOM   337  C  C     . PRO A 1 43  ? -10.918 -62.761 -40.49  1   151.15 ? 40  PRO A C     1 
ATOM   338  O  O     . PRO A 1 43  ? -11.751 -62.285 -39.708 1   151.3  ? 40  PRO A O     1 
ATOM   339  C  CB    . PRO A 1 43  ? -11.204 -64.545 -42.306 1   151.54 ? 40  PRO A CB    1 
ATOM   340  C  CG    . PRO A 1 43  ? -12.671 -64.751 -42.363 1   151.88 ? 40  PRO A CG    1 
ATOM   341  C  CD    . PRO A 1 43  ? -13.047 -65.422 -41.068 1   150.32 ? 40  PRO A CD    1 
ATOM   342  N  N     . ASN A 1 44  ? -9.956  -62.016 -41.048 1   150.89 ? 41  ASN A N     1 
ATOM   343  C  CA    . ASN A 1 44  ? -9.876  -60.581 -40.819 1   151.02 ? 41  ASN A CA    1 
ATOM   344  C  C     . ASN A 1 44  ? -11.034 -59.899 -41.54  1   150.71 ? 41  ASN A C     1 
ATOM   345  O  O     . ASN A 1 44  ? -11.311 -60.231 -42.69  1   151.02 ? 41  ASN A O     1 
ATOM   346  C  CB    . ASN A 1 44  ? -8.543  -60.054 -41.321 1   152.33 ? 41  ASN A CB    1 
ATOM   347  C  CG    . ASN A 1 44  ? -7.401  -60.473 -40.444 1   155.7  ? 41  ASN A CG    1 
ATOM   348  O  OD1   . ASN A 1 44  ? -7.269  -60.01  -39.304 1   157.12 ? 41  ASN A OD1   1 
ATOM   349  N  ND2   . ASN A 1 44  ? -6.56   -61.366 -40.951 1   156.25 ? 41  ASN A ND2   1 
ATOM   350  N  N     . GLY A 1 45  ? -11.719 -58.988 -40.854 1   149.8  ? 42  GLY A N     1 
ATOM   351  C  CA    . GLY A 1 45  ? -12.852 -58.268 -41.428 1   149.24 ? 42  GLY A CA    1 
ATOM   352  C  C     . GLY A 1 45  ? -14.178 -59.006 -41.369 1   148.2  ? 42  GLY A C     1 
ATOM   353  O  O     . GLY A 1 45  ? -15.151 -58.595 -42.01  1   148.3  ? 42  GLY A O     1 
ATOM   354  N  N     . ALA A 1 46  ? -14.237 -60.1   -40.605 1   147.04 ? 43  ALA A N     1 
ATOM   355  C  CA    . ALA A 1 46  ? -15.468 -60.868 -40.472 1   146.6  ? 43  ALA A CA    1 
ATOM   356  C  C     . ALA A 1 46  ? -16.492 -60.215 -39.517 1   145.82 ? 43  ALA A C     1 
ATOM   357  O  O     . ALA A 1 46  ? -17.671 -60.557 -39.572 1   146.16 ? 43  ALA A O     1 
ATOM   358  C  CB    . ALA A 1 46  ? -15.15  -62.284 -40.025 1   146.85 ? 43  ALA A CB    1 
ATOM   359  N  N     . GLY A 1 47  ? -16.045 -59.301 -38.654 1   144.6  ? 44  GLY A N     1 
ATOM   360  C  CA    . GLY A 1 47  ? -16.923 -58.631 -37.7   1   143.91 ? 44  GLY A CA    1 
ATOM   361  C  C     . GLY A 1 47  ? -16.752 -59.09  -36.26  1   142.84 ? 44  GLY A C     1 
ATOM   362  O  O     . GLY A 1 47  ? -17.64  -58.87  -35.428 1   143.06 ? 44  GLY A O     1 
ATOM   363  N  N     . LYS A 1 48  ? -15.598 -59.723 -35.951 1   141.46 ? 45  LYS A N     1 
ATOM   364  C  CA    . LYS A 1 48  ? -15.25  -60.216 -34.615 1   140.51 ? 45  LYS A CA    1 
ATOM   365  C  C     . LYS A 1 48  ? -15.204 -59.055 -33.606 1   139.12 ? 45  LYS A C     1 
ATOM   366  O  O     . LYS A 1 48  ? -15.858 -59.114 -32.567 1   139.01 ? 45  LYS A O     1 
ATOM   367  C  CB    . LYS A 1 48  ? -13.899 -60.957 -34.656 1   142.44 ? 45  LYS A CB    1 
ATOM   368  C  CG    . LYS A 1 48  ? -13.918 -62.29  -35.406 1   146.98 ? 45  LYS A CG    1 
ATOM   369  C  CD    . LYS A 1 48  ? -12.668 -63.145 -35.163 1   151.88 ? 45  LYS A CD    1 
ATOM   370  C  CE    . LYS A 1 48  ? -11.378 -62.406 -35.394 1   156.04 ? 45  LYS A CE    1 
ATOM   371  N  NZ    . LYS A 1 48  ? -11.256 -61.936 -36.796 1   158.68 ? 45  LYS A NZ    1 
ATOM   372  N  N     . SER A 1 49  ? -14.463 -57.985 -33.942 1   137.92 ? 46  SER A N     1 
ATOM   373  C  CA    . SER A 1 49  ? -14.359 -56.792 -33.114 1   137.06 ? 46  SER A CA    1 
ATOM   374  C  C     . SER A 1 49  ? -15.718 -56.106 -32.994 1   136.12 ? 46  SER A C     1 
ATOM   375  O  O     . SER A 1 49  ? -16.155 -55.841 -31.877 1   136.33 ? 46  SER A O     1 
ATOM   376  C  CB    . SER A 1 49  ? -13.332 -55.825 -33.694 1   137.94 ? 46  SER A CB    1 
ATOM   377  O  OG    . SER A 1 49  ? -12.017 -56.302 -33.488 1   139.7  ? 46  SER A OG    1 
ATOM   378  N  N     . THR A 1 50  ? -16.42  -55.883 -34.129 1   134.87 ? 47  THR A N     1 
ATOM   379  C  CA    . THR A 1 50  ? -17.746 -55.251 -34.159 1   134.03 ? 47  THR A CA    1 
ATOM   380  C  C     . THR A 1 50  ? -18.726 -55.927 -33.19  1   133.04 ? 47  THR A C     1 
ATOM   381  O  O     . THR A 1 50  ? -19.409 -55.252 -32.416 1   133.32 ? 47  THR A O     1 
ATOM   382  C  CB    . THR A 1 50  ? -18.302 -55.264 -35.586 1   134.9  ? 47  THR A CB    1 
ATOM   383  O  OG1   . THR A 1 50  ? -17.411 -54.567 -36.458 1   135.58 ? 47  THR A OG1   1 
ATOM   384  C  CG2   . THR A 1 50  ? -19.708 -54.684 -35.664 1   135.3  ? 47  THR A CG2   1 
ATOM   385  N  N     . LEU A 1 51  ? -18.747 -57.265 -33.199 1   131.74 ? 48  LEU A N     1 
ATOM   386  C  CA    . LEU A 1 51  ? -19.608 -58.026 -32.32  1   131.04 ? 48  LEU A CA    1 
ATOM   387  C  C     . LEU A 1 51  ? -19.241 -57.781 -30.863 1   130.55 ? 48  LEU A C     1 
ATOM   388  O  O     . LEU A 1 51  ? -20.125 -57.543 -30.049 1   130.57 ? 48  LEU A O     1 
ATOM   389  C  CB    . LEU A 1 51  ? -19.523 -59.516 -32.666 1   131.09 ? 48  LEU A CB    1 
ATOM   390  C  CG    . LEU A 1 51  ? -20.278 -60.448 -31.728 1   132.48 ? 48  LEU A CG    1 
ATOM   391  C  CD1   . LEU A 1 51  ? -21.763 -60.181 -31.769 1   133.05 ? 48  LEU A CD1   1 
ATOM   392  C  CD2   . LEU A 1 51  ? -19.986 -61.88  -32.04  1   133.13 ? 48  LEU A CD2   1 
ATOM   393  N  N     . ALA A 1 52  ? -17.947 -57.799 -30.541 1   130.06 ? 49  ALA A N     1 
ATOM   394  C  CA    . ALA A 1 52  ? -17.496 -57.58  -29.17  1   130.21 ? 49  ALA A CA    1 
ATOM   395  C  C     . ALA A 1 52  ? -17.867 -56.19  -28.652 1   130.09 ? 49  ALA A C     1 
ATOM   396  O  O     . ALA A 1 52  ? -18.223 -56.043 -27.484 1   130.18 ? 49  ALA A O     1 
ATOM   397  C  CB    . ALA A 1 52  ? -15.996 -57.806 -29.067 1   130.39 ? 49  ALA A CB    1 
ATOM   398  N  N     . TYR A 1 53  ? -17.805 -55.174 -29.519 1   129.79 ? 50  TYR A N     1 
ATOM   399  C  CA    . TYR A 1 53  ? -18.146 -53.805 -29.127 1   129.97 ? 50  TYR A CA    1 
ATOM   400  C  C     . TYR A 1 53  ? -19.648 -53.6   -28.975 1   129.86 ? 50  TYR A C     1 
ATOM   401  O  O     . TYR A 1 53  ? -20.078 -52.764 -28.184 1   129.8  ? 50  TYR A O     1 
ATOM   402  C  CB    . TYR A 1 53  ? -17.598 -52.8   -30.142 1   130.11 ? 50  TYR A CB    1 
ATOM   403  C  CG    . TYR A 1 53  ? -16.09  -52.79  -30.241 1   131.09 ? 50  TYR A CG    1 
ATOM   404  C  CD1   . TYR A 1 53  ? -15.299 -52.962 -29.117 1   132.11 ? 50  TYR A CD1   1 
ATOM   405  C  CD2   . TYR A 1 53  ? -15.456 -52.547 -31.449 1   132.19 ? 50  TYR A CD2   1 
ATOM   406  C  CE1   . TYR A 1 53  ? -13.911 -52.941 -29.201 1   133.2  ? 50  TYR A CE1   1 
ATOM   407  C  CE2   . TYR A 1 53  ? -14.07  -52.515 -31.546 1   133.25 ? 50  TYR A CE2   1 
ATOM   408  C  CZ    . TYR A 1 53  ? -13.297 -52.712 -30.419 1   134.28 ? 50  TYR A CZ    1 
ATOM   409  O  OH    . TYR A 1 53  ? -11.924 -52.669 -30.524 1   136.04 ? 50  TYR A OH    1 
ATOM   410  N  N     . THR A 1 54  ? -20.443 -54.333 -29.756 1   129.71 ? 51  THR A N     1 
ATOM   411  C  CA    . THR A 1 54  ? -21.893 -54.229 -29.703 1   130.09 ? 51  THR A CA    1 
ATOM   412  C  C     . THR A 1 54  ? -22.429 -54.833 -28.407 1   130.17 ? 51  THR A C     1 
ATOM   413  O  O     . THR A 1 54  ? -23.351 -54.282 -27.809 1   130.21 ? 51  THR A O     1 
ATOM   414  C  CB    . THR A 1 54  ? -22.513 -54.861 -30.952 1   131.46 ? 51  THR A CB    1 
ATOM   415  O  OG1   . THR A 1 54  ? -21.909 -54.292 -32.119 1   132.63 ? 51  THR A OG1   1 
ATOM   416  C  CG2   . THR A 1 54  ? -24.018 -54.672 -31.007 1   131.75 ? 51  THR A CG2   1 
ATOM   417  N  N     . ILE A 1 55  ? -21.831 -55.941 -27.951 1   130.14 ? 52  ILE A N     1 
ATOM   418  C  CA    . ILE A 1 55  ? -22.233 -56.589 -26.703 1   130.48 ? 52  ILE A CA    1 
ATOM   419  C  C     . ILE A 1 55  ? -21.901 -55.669 -25.521 1   130.99 ? 52  ILE A C     1 
ATOM   420  O  O     . ILE A 1 55  ? -22.741 -55.456 -24.649 1   130.94 ? 52  ILE A O     1 
ATOM   421  C  CB    . ILE A 1 55  ? -21.569 -57.986 -26.568 1   130.61 ? 52  ILE A CB    1 
ATOM   422  C  CG1   . ILE A 1 55  ? -22.022 -58.925 -27.69  1   131.14 ? 52  ILE A CG1   1 
ATOM   423  C  CG2   . ILE A 1 55  ? -21.845 -58.601 -25.208 1   131.03 ? 52  ILE A CG2   1 
ATOM   424  C  CD1   . ILE A 1 55  ? -21.186 -60.13  -27.816 1   132.19 ? 52  ILE A CD1   1 
ATOM   425  N  N     . MET A 1 56  ? -20.707 -55.069 -25.534 1   131.29 ? 53  MET A N     1 
ATOM   426  C  CA    . MET A 1 56  ? -20.281 -54.163 -24.47  1   132.19 ? 53  MET A CA    1 
ATOM   427  C  C     . MET A 1 56  ? -21.034 -52.805 -24.471 1   133.7  ? 53  MET A C     1 
ATOM   428  O  O     . MET A 1 56  ? -21.084 -52.117 -23.451 1   133.97 ? 53  MET A O     1 
ATOM   429  C  CB    . MET A 1 56  ? -18.758 -53.973 -24.513 1   132.18 ? 53  MET A CB    1 
ATOM   430  C  CG    . MET A 1 56  ? -18.197 -53.322 -23.278 1   133.35 ? 53  MET A CG    1 
ATOM   431  S  SD    . MET A 1 56  ? -18.248 -54.386 -21.826 1   134.33 ? 53  MET A SD    1 
ATOM   432  C  CE    . MET A 1 56  ? -19.518 -53.566 -20.836 1   132.59 ? 53  MET A CE    1 
ATOM   433  N  N     . GLY A 1 57  ? -21.642 -52.449 -25.596 1   134.45 ? 54  GLY A N     1 
ATOM   434  C  CA    . GLY A 1 57  ? -22.424 -51.224 -25.697 1   135.56 ? 54  GLY A CA    1 
ATOM   435  C  C     . GLY A 1 57  ? -21.635 -49.994 -26.077 1   136.58 ? 54  GLY A C     1 
ATOM   436  O  O     . GLY A 1 57  ? -22.062 -48.871 -25.797 1   136.82 ? 54  GLY A O     1 
ATOM   437  N  N     . ILE A 1 58  ? -20.495 -50.197 -26.742 1   137.07 ? 55  ILE A N     1 
ATOM   438  C  CA    . ILE A 1 58  ? -19.622 -49.118 -27.2   1   138.03 ? 55  ILE A CA    1 
ATOM   439  C  C     . ILE A 1 58  ? -20.381 -48.173 -28.143 1   138.5  ? 55  ILE A C     1 
ATOM   440  O  O     . ILE A 1 58  ? -21.156 -48.644 -28.969 1   138.78 ? 55  ILE A O     1 
ATOM   441  C  CB    . ILE A 1 58  ? -18.374 -49.76  -27.859 1   138.88 ? 55  ILE A CB    1 
ATOM   442  C  CG1   . ILE A 1 58  ? -17.594 -50.642 -26.854 1   140.09 ? 55  ILE A CG1   1 
ATOM   443  C  CG2   . ILE A 1 58  ? -17.484 -48.734 -28.542 1   139.38 ? 55  ILE A CG2   1 
ATOM   444  C  CD1   . ILE A 1 58  ? -17.24  -49.984 -25.528 1   141.51 ? 55  ILE A CD1   1 
ATOM   445  N  N     . SER A 1 59  ? -20.226 -46.854 -27.976 1   138.52 ? 56  SER A N     1 
ATOM   446  C  CA    . SER A 1 59  ? -20.944 -45.886 -28.802 1   139.24 ? 56  SER A CA    1 
ATOM   447  C  C     . SER A 1 59  ? -20.646 -46.06  -30.284 1   139.74 ? 56  SER A C     1 
ATOM   448  O  O     . SER A 1 59  ? -19.497 -46.277 -30.661 1   139.78 ? 56  SER A O     1 
ATOM   449  C  CB    . SER A 1 59  ? -20.625 -44.46  -28.367 1   140.75 ? 56  SER A CB    1 
ATOM   450  O  OG    . SER A 1 59  ? -21.408 -43.516 -29.08  1   143.15 ? 56  SER A OG    1 
ATOM   451  N  N     . GLY A 1 60  ? -21.694 -46.003 -31.097 1   140    ? 57  GLY A N     1 
ATOM   452  C  CA    . GLY A 1 60  ? -21.59  -46.168 -32.541 1   140.87 ? 57  GLY A CA    1 
ATOM   453  C  C     . GLY A 1 60  ? -21.919 -47.57  -33.018 1   141.68 ? 57  GLY A C     1 
ATOM   454  O  O     . GLY A 1 60  ? -22.331 -47.76  -34.165 1   141.65 ? 57  GLY A O     1 
ATOM   455  N  N     . TYR A 1 61  ? -21.731 -48.569 -32.138 1   142.21 ? 58  TYR A N     1 
ATOM   456  C  CA    . TYR A 1 61  ? -21.999 -49.985 -32.405 1   143.11 ? 58  TYR A CA    1 
ATOM   457  C  C     . TYR A 1 61  ? -23.402 -50.31  -31.893 1   143.89 ? 58  TYR A C     1 
ATOM   458  O  O     . TYR A 1 61  ? -23.572 -51.046 -30.921 1   143.85 ? 58  TYR A O     1 
ATOM   459  C  CB    . TYR A 1 61  ? -20.92  -50.88  -31.757 1   143.14 ? 58  TYR A CB    1 
ATOM   460  C  CG    . TYR A 1 61  ? -19.549 -50.691 -32.378 1   143.94 ? 58  TYR A CG    1 
ATOM   461  C  CD1   . TYR A 1 61  ? -19.144 -51.454 -33.464 1   144.79 ? 58  TYR A CD1   1 
ATOM   462  C  CD2   . TYR A 1 61  ? -18.677 -49.716 -31.909 1   144.87 ? 58  TYR A CD2   1 
ATOM   463  C  CE1   . TYR A 1 61  ? -17.901 -51.265 -34.058 1   145.7  ? 58  TYR A CE1   1 
ATOM   464  C  CE2   . TYR A 1 61  ? -17.435 -49.511 -32.501 1   145.75 ? 58  TYR A CE2   1 
ATOM   465  C  CZ    . TYR A 1 61  ? -17.055 -50.278 -33.586 1   146.6  ? 58  TYR A CZ    1 
ATOM   466  O  OH    . TYR A 1 61  ? -15.817 -50.102 -34.164 1   148    ? 58  TYR A OH    1 
ATOM   467  N  N     . LYS A 1 62  ? -24.404 -49.695 -32.538 1   144.44 ? 59  LYS A N     1 
ATOM   468  C  CA    . LYS A 1 62  ? -25.818 -49.829 -32.202 1   145.39 ? 59  LYS A CA    1 
ATOM   469  C  C     . LYS A 1 62  ? -26.534 -50.769 -33.163 1   146.14 ? 59  LYS A C     1 
ATOM   470  O  O     . LYS A 1 62  ? -26.483 -50.58  -34.382 1   146.22 ? 59  LYS A O     1 
ATOM   471  C  CB    . LYS A 1 62  ? -26.541 -48.455 -32.151 1   147.05 ? 59  LYS A CB    1 
ATOM   472  C  CG    . LYS A 1 62  ? -25.789 -47.257 -32.754 1   150.63 ? 59  LYS A CG    1 
ATOM   473  C  CD    . LYS A 1 62  ? -25.981 -47.123 -34.258 1   154.62 ? 59  LYS A CD    1 
ATOM   474  C  CE    . LYS A 1 62  ? -25.112 -46.034 -34.845 1   158.14 ? 59  LYS A CE    1 
ATOM   475  N  NZ    . LYS A 1 62  ? -25.475 -44.688 -34.331 1   160.23 ? 59  LYS A NZ    1 
ATOM   476  N  N     . PRO A 1 63  ? -27.225 -51.786 -32.623 1   146.44 ? 60  PRO A N     1 
ATOM   477  C  CA    . PRO A 1 63  ? -27.949 -52.707 -33.501 1   146.81 ? 60  PRO A CA    1 
ATOM   478  C  C     . PRO A 1 63  ? -29.2   -52.086 -34.11  1   147.45 ? 60  PRO A C     1 
ATOM   479  O  O     . PRO A 1 63  ? -29.92  -51.332 -33.458 1   147.49 ? 60  PRO A O     1 
ATOM   480  C  CB    . PRO A 1 63  ? -28.297 -53.88  -32.586 1   147.37 ? 60  PRO A CB    1 
ATOM   481  C  CG    . PRO A 1 63  ? -28.313 -53.314 -31.224 1   147.67 ? 60  PRO A CG    1 
ATOM   482  C  CD    . PRO A 1 63  ? -27.377 -52.142 -31.198 1   145.98 ? 60  PRO A CD    1 
ATOM   483  N  N     . THR A 1 64  ? -29.433 -52.398 -35.38  1   147.73 ? 61  THR A N     1 
ATOM   484  C  CA    . THR A 1 64  ? -30.593 -51.951 -36.142 1   148.45 ? 61  THR A CA    1 
ATOM   485  C  C     . THR A 1 64  ? -31.715 -52.997 -36.002 1   148.58 ? 61  THR A C     1 
ATOM   486  O  O     . THR A 1 64  ? -32.88  -52.647 -35.81  1   148.73 ? 61  THR A O     1 
ATOM   487  C  CB    . THR A 1 64  ? -30.187 -51.684 -37.608 1   150.1  ? 61  THR A CB    1 
ATOM   488  O  OG1   . THR A 1 64  ? -29.438 -52.796 -38.118 1   151.24 ? 61  THR A OG1   1 
ATOM   489  C  CG2   . THR A 1 64  ? -29.37  -50.406 -37.76  1   150.54 ? 61  THR A CG2   1 
ATOM   490  N  N     . LYS A 1 65  ? -31.345 -54.282 -36.083 1   148.35 ? 62  LYS A N     1 
ATOM   491  C  CA    . LYS A 1 65  ? -32.241 -55.424 -35.932 1   148.64 ? 62  LYS A CA    1 
ATOM   492  C  C     . LYS A 1 65  ? -31.598 -56.411 -34.931 1   148.52 ? 62  LYS A C     1 
ATOM   493  O  O     . LYS A 1 65  ? -30.371 -56.476 -34.817 1   148.83 ? 62  LYS A O     1 
ATOM   494  C  CB    . LYS A 1 65  ? -32.475 -56.101 -37.298 1   150.55 ? 62  LYS A CB    1 
ATOM   495  C  CG    . LYS A 1 65  ? -33.627 -57.098 -37.322 1   154.65 ? 62  LYS A CG    1 
ATOM   496  C  CD    . LYS A 1 65  ? -33.613 -57.925 -38.6   1   159.33 ? 62  LYS A CD    1 
ATOM   497  C  CE    . LYS A 1 65  ? -34.44  -59.184 -38.494 1   163.39 ? 62  LYS A CE    1 
ATOM   498  N  NZ    . LYS A 1 65  ? -34.022 -60.211 -39.494 1   165.71 ? 62  LYS A NZ    1 
ATOM   499  N  N     . GLY A 1 66  ? -32.424 -57.139 -34.19  1   147.81 ? 63  GLY A N     1 
ATOM   500  C  CA    . GLY A 1 66  ? -31.927 -58.112 -33.226 1   147.54 ? 63  GLY A CA    1 
ATOM   501  C  C     . GLY A 1 66  ? -31.749 -57.61  -31.808 1   146.91 ? 63  GLY A C     1 
ATOM   502  O  O     . GLY A 1 66  ? -31.718 -56.4   -31.559 1   147.03 ? 63  GLY A O     1 
ATOM   503  N  N     . ARG A 1 67  ? -31.593 -58.551 -30.866 1   145.97 ? 64  ARG A N     1 
ATOM   504  C  CA    . ARG A 1 67  ? -31.459 -58.191 -29.46  1   145.47 ? 64  ARG A CA    1 
ATOM   505  C  C     . ARG A 1 67  ? -30.338 -58.914 -28.729 1   144.38 ? 64  ARG A C     1 
ATOM   506  O  O     . ARG A 1 67  ? -29.995 -60.039 -29.087 1   144.49 ? 64  ARG A O     1 
ATOM   507  C  CB    . ARG A 1 67  ? -32.794 -58.409 -28.732 1   146.87 ? 64  ARG A CB    1 
ATOM   508  C  CG    . ARG A 1 67  ? -33.314 -59.837 -28.773 1   149.76 ? 64  ARG A CG    1 
ATOM   509  C  CD    . ARG A 1 67  ? -34.654 -59.88  -28.07  1   152.85 ? 64  ARG A CD    1 
ATOM   510  N  NE    . ARG A 1 67  ? -34.851 -61.107 -27.296 1   155.48 ? 64  ARG A NE    1 
ATOM   511  C  CZ    . ARG A 1 67  ? -35.813 -61.994 -27.529 1   157.23 ? 64  ARG A CZ    1 
ATOM   512  N  NH1   . ARG A 1 67  ? -36.658 -61.818 -28.537 1   156.76 ? 64  ARG A NH1   1 
ATOM   513  N  NH2   . ARG A 1 67  ? -35.919 -63.081 -26.775 1   157.09 ? 64  ARG A NH2   1 
ATOM   514  N  N     . ILE A 1 68  ? -29.775 -58.257 -27.692 1   143.04 ? 65  ILE A N     1 
ATOM   515  C  CA    . ILE A 1 68  ? -28.729 -58.818 -26.838 1   142.08 ? 65  ILE A CA    1 
ATOM   516  C  C     . ILE A 1 68  ? -29.293 -58.965 -25.436 1   141.02 ? 65  ILE A C     1 
ATOM   517  O  O     . ILE A 1 68  ? -29.647 -57.971 -24.814 1   141.21 ? 65  ILE A O     1 
ATOM   518  C  CB    . ILE A 1 68  ? -27.441 -57.963 -26.836 1   142.29 ? 65  ILE A CB    1 
ATOM   519  C  CG1   . ILE A 1 68  ? -26.883 -57.816 -28.262 1   143.21 ? 65  ILE A CG1   1 
ATOM   520  C  CG2   . ILE A 1 68  ? -26.406 -58.578 -25.898 1   142.62 ? 65  ILE A CG2   1 
ATOM   521  C  CD1   . ILE A 1 68  ? -25.678 -56.934 -28.393 1   144.52 ? 65  ILE A CD1   1 
ATOM   522  N  N     . ILE A 1 69  ? -29.418 -60.196 -24.954 1   139.79 ? 66  ILE A N     1 
ATOM   523  C  CA    . ILE A 1 69  ? -29.958 -60.455 -23.632 1   139.17 ? 66  ILE A CA    1 
ATOM   524  C  C     . ILE A 1 69  ? -28.846 -60.933 -22.735 1   138.17 ? 66  ILE A C     1 
ATOM   525  O  O     . ILE A 1 69  ? -28.161 -61.882 -23.074 1   138.17 ? 66  ILE A O     1 
ATOM   526  C  CB    . ILE A 1 69  ? -31.07  -61.509 -23.73  1   139.97 ? 66  ILE A CB    1 
ATOM   527  C  CG1   . ILE A 1 69  ? -32.172 -61.067 -24.699 1   141.1  ? 66  ILE A CG1   1 
ATOM   528  C  CG2   . ILE A 1 69  ? -31.623 -61.851 -22.359 1   140.61 ? 66  ILE A CG2   1 
ATOM   529  C  CD1   . ILE A 1 69  ? -32.31  -61.964 -25.895 1   142.56 ? 66  ILE A CD1   1 
ATOM   530  N  N     . PHE A 1 70  ? -28.649 -60.275 -21.604 1   137.37 ? 67  PHE A N     1 
ATOM   531  C  CA    . PHE A 1 70  ? -27.618 -60.66  -20.654 1   137.23 ? 67  PHE A CA    1 
ATOM   532  C  C     . PHE A 1 70  ? -28.285 -60.841 -19.319 1   136.58 ? 67  PHE A C     1 
ATOM   533  O  O     . PHE A 1 70  ? -28.988 -59.936 -18.862 1   136.74 ? 67  PHE A O     1 
ATOM   534  C  CB    . PHE A 1 70  ? -26.527 -59.585 -20.556 1   137.42 ? 67  PHE A CB    1 
ATOM   535  C  CG    . PHE A 1 70  ? -25.388 -59.941 -19.629 1   138.28 ? 67  PHE A CG    1 
ATOM   536  C  CD1   . PHE A 1 70  ? -24.562 -61.016 -19.9   1   139.27 ? 67  PHE A CD1   1 
ATOM   537  C  CD2   . PHE A 1 70  ? -25.122 -59.178 -18.509 1   139    ? 67  PHE A CD2   1 
ATOM   538  C  CE1   . PHE A 1 70  ? -23.515 -61.342 -19.048 1   139.96 ? 67  PHE A CE1   1 
ATOM   539  C  CE2   . PHE A 1 70  ? -24.067 -59.502 -17.665 1   139.74 ? 67  PHE A CE2   1 
ATOM   540  C  CZ    . PHE A 1 70  ? -23.271 -60.581 -17.939 1   139.62 ? 67  PHE A CZ    1 
ATOM   541  N  N     . LYS A 1 71  ? -28.107 -62.022 -18.718 1   135.68 ? 68  LYS A N     1 
ATOM   542  C  CA    . LYS A 1 71  ? -28.707 -62.366 -17.438 1   135.39 ? 68  LYS A CA    1 
ATOM   543  C  C     . LYS A 1 71  ? -30.231 -62.217 -17.451 1   135.38 ? 68  LYS A C     1 
ATOM   544  O  O     . LYS A 1 71  ? -30.815 -61.71  -16.491 1   135.57 ? 68  LYS A O     1 
ATOM   545  C  CB    . LYS A 1 71  ? -28.069 -61.567 -16.298 1   136.5  ? 68  LYS A CB    1 
ATOM   546  C  CG    . LYS A 1 71  ? -26.627 -61.948 -16.047 1   139.4  ? 68  LYS A CG    1 
ATOM   547  C  CD    . LYS A 1 71  ? -26.075 -61.182 -14.873 1   143.07 ? 68  LYS A CD    1 
ATOM   548  C  CE    . LYS A 1 71  ? -24.855 -61.842 -14.297 1   146.46 ? 68  LYS A CE    1 
ATOM   549  N  NZ    . LYS A 1 71  ? -24.419 -61.162 -13.052 1   148.66 ? 68  LYS A NZ    1 
ATOM   550  N  N     . GLY A 1 72  ? -30.853 -62.634 -18.552 1   134.98 ? 69  GLY A N     1 
ATOM   551  C  CA    . GLY A 1 72  ? -32.3   -62.571 -18.724 1   135.12 ? 69  GLY A CA    1 
ATOM   552  C  C     . GLY A 1 72  ? -32.866 -61.194 -19.015 1   135.08 ? 69  GLY A C     1 
ATOM   553  O  O     . GLY A 1 72  ? -34.069 -61.056 -19.238 1   135.07 ? 69  GLY A O     1 
ATOM   554  N  N     . VAL A 1 73  ? -32.015 -60.162 -19.015 1   134.96 ? 70  VAL A N     1 
ATOM   555  C  CA    . VAL A 1 73  ? -32.441 -58.79  -19.263 1   135.26 ? 70  VAL A CA    1 
ATOM   556  C  C     . VAL A 1 73  ? -31.987 -58.322 -20.632 1   135.44 ? 70  VAL A C     1 
ATOM   557  O  O     . VAL A 1 73  ? -30.828 -58.519 -20.985 1   135.5  ? 70  VAL A O     1 
ATOM   558  C  CB    . VAL A 1 73  ? -31.89  -57.86  -18.165 1   135.88 ? 70  VAL A CB    1 
ATOM   559  C  CG1   . VAL A 1 73  ? -32.31  -56.414 -18.406 1   136.46 ? 70  VAL A CG1   1 
ATOM   560  C  CG2   . VAL A 1 73  ? -32.328 -58.337 -16.787 1   136.31 ? 70  VAL A CG2   1 
ATOM   561  N  N     . ASP A 1 74  ? -32.892 -57.709 -21.41  1   135.33 ? 71  ASP A N     1 
ATOM   562  C  CA    . ASP A 1 74  ? -32.529 -57.167 -22.715 1   135.61 ? 71  ASP A CA    1 
ATOM   563  C  C     . ASP A 1 74  ? -31.799 -55.857 -22.43  1   135.73 ? 71  ASP A C     1 
ATOM   564  O  O     . ASP A 1 74  ? -32.393 -54.905 -21.919 1   135.93 ? 71  ASP A O     1 
ATOM   565  C  CB    . ASP A 1 74  ? -33.776 -56.929 -23.59  1   136.95 ? 71  ASP A CB    1 
ATOM   566  C  CG    . ASP A 1 74  ? -33.474 -56.642 -25.051 1   140.36 ? 71  ASP A CG    1 
ATOM   567  O  OD1   . ASP A 1 74  ? -32.322 -56.293 -25.36  1   140.61 ? 71  ASP A OD1   1 
ATOM   568  O  OD2   . ASP A 1 74  ? -34.393 -56.778 -25.884 1   142.36 ? 71  ASP A OD2   1 
ATOM   569  N  N     . ILE A 1 75  ? -30.503 -55.824 -22.738 1   135.36 ? 72  ILE A N     1 
ATOM   570  C  CA    . ILE A 1 75  ? -29.663 -54.67  -22.465 1   135.4  ? 72  ILE A CA    1 
ATOM   571  C  C     . ILE A 1 75  ? -29.654 -53.627 -23.595 1   135.61 ? 72  ILE A C     1 
ATOM   572  O  O     . ILE A 1 75  ? -28.751 -52.792 -23.632 1   135.66 ? 72  ILE A O     1 
ATOM   573  C  CB    . ILE A 1 75  ? -28.242 -55.151 -22.099 1   135.59 ? 72  ILE A CB    1 
ATOM   574  C  CG1   . ILE A 1 75  ? -27.568 -55.849 -23.297 1   136.16 ? 72  ILE A CG1   1 
ATOM   575  C  CG2   . ILE A 1 75  ? -28.303 -56.062 -20.873 1   136.05 ? 72  ILE A CG2   1 
ATOM   576  C  CD1   . ILE A 1 75  ? -26.161 -56.31  -23.054 1   137.2  ? 72  ILE A CD1   1 
ATOM   577  N  N     . ILE A 1 76  ? -30.687 -53.616 -24.459 1   135.51 ? 73  ILE A N     1 
ATOM   578  C  CA    . ILE A 1 76  ? -30.826 -52.665 -25.569 1   135.84 ? 73  ILE A CA    1 
ATOM   579  C  C     . ILE A 1 76  ? -30.679 -51.208 -25.096 1   135.76 ? 73  ILE A C     1 
ATOM   580  O  O     . ILE A 1 76  ? -30.029 -50.406 -25.765 1   135.78 ? 73  ILE A O     1 
ATOM   581  C  CB    . ILE A 1 76  ? -32.164 -52.934 -26.351 1   136.56 ? 73  ILE A CB    1 
ATOM   582  C  CG1   . ILE A 1 76  ? -31.972 -53.984 -27.468 1   137.51 ? 73  ILE A CG1   1 
ATOM   583  C  CG2   . ILE A 1 76  ? -32.829 -51.659 -26.913 1   137.15 ? 73  ILE A CG2   1 
ATOM   584  C  CD1   . ILE A 1 76  ? -33.267 -54.437 -28.144 1   138.7  ? 73  ILE A CD1   1 
ATOM   585  N  N     . ASP A 1 77  ? -31.256 -50.88  -23.937 1   135.6  ? 74  ASP A N     1 
ATOM   586  C  CA    . ASP A 1 77  ? -31.21  -49.513 -23.421 1   136.05 ? 74  ASP A CA    1 
ATOM   587  C  C     . ASP A 1 77  ? -30.16  -49.285 -22.315 1   135.92 ? 74  ASP A C     1 
ATOM   588  O  O     . ASP A 1 77  ? -30.151 -48.215 -21.699 1   136.18 ? 74  ASP A O     1 
ATOM   589  C  CB    . ASP A 1 77  ? -32.606 -49.056 -22.944 1   138.01 ? 74  ASP A CB    1 
ATOM   590  C  CG    . ASP A 1 77  ? -33.769 -49.545 -23.79  1   142.51 ? 74  ASP A CG    1 
ATOM   591  O  OD1   . ASP A 1 77  ? -34.067 -50.762 -23.744 1   143.03 ? 74  ASP A OD1   1 
ATOM   592  O  OD2   . ASP A 1 77  ? -34.383 -48.712 -24.491 1   144.83 ? 74  ASP A OD2   1 
ATOM   593  N  N     . LYS A 1 78  ? -29.279 -50.271 -22.065 1   135.24 ? 75  LYS A N     1 
ATOM   594  C  CA    . LYS A 1 78  ? -28.245 -50.149 -21.042 1   135.09 ? 75  LYS A CA    1 
ATOM   595  C  C     . LYS A 1 78  ? -26.923 -49.64  -21.62  1   134.74 ? 75  LYS A C     1 
ATOM   596  O  O     . LYS A 1 78  ? -26.502 -50.128 -22.664 1   134.96 ? 75  LYS A O     1 
ATOM   597  C  CB    . LYS A 1 78  ? -28.044 -51.484 -20.32  1   136.72 ? 75  LYS A CB    1 
ATOM   598  C  CG    . LYS A 1 78  ? -28.936 -51.618 -19.1   1   140.68 ? 75  LYS A CG    1 
ATOM   599  C  CD    . LYS A 1 78  ? -29.404 -53.041 -18.89  1   145.21 ? 75  LYS A CD    1 
ATOM   600  C  CE    . LYS A 1 78  ? -30.311 -53.168 -17.689 1   149.05 ? 75  LYS A CE    1 
ATOM   601  N  NZ    . LYS A 1 78  ? -31.148 -51.957 -17.476 1   151.34 ? 75  LYS A NZ    1 
ATOM   602  N  N     . ASN A 1 79  ? -26.283 -48.64  -20.963 1   133.82 ? 76  ASN A N     1 
ATOM   603  C  CA    . ASN A 1 79  ? -25.001 -48.08  -21.419 1   133.04 ? 76  ASN A CA    1 
ATOM   604  C  C     . ASN A 1 79  ? -23.804 -48.934 -20.934 1   131.9  ? 76  ASN A C     1 
ATOM   605  O  O     . ASN A 1 79  ? -24.005 -49.876 -20.169 1   132.04 ? 76  ASN A O     1 
ATOM   606  C  CB    . ASN A 1 79  ? -24.868 -46.597 -21.025 1   133.96 ? 76  ASN A CB    1 
ATOM   607  C  CG    . ASN A 1 79  ? -24.799 -46.337 -19.541 1   136.96 ? 76  ASN A CG    1 
ATOM   608  O  OD1   . ASN A 1 79  ? -24.37  -47.176 -18.749 1   138.22 ? 76  ASN A OD1   1 
ATOM   609  N  ND2   . ASN A 1 79  ? -25.211 -45.15  -19.13  1   137.44 ? 76  ASN A ND2   1 
ATOM   610  N  N     . ILE A 1 80  ? -22.567 -48.606 -21.358 1   130.58 ? 77  ILE A N     1 
ATOM   611  C  CA    . ILE A 1 80  ? -21.367 -49.36  -20.977 1   129.8  ? 77  ILE A CA    1 
ATOM   612  C  C     . ILE A 1 80  ? -21.253 -49.583 -19.469 1   128.64 ? 77  ILE A C     1 
ATOM   613  O  O     . ILE A 1 80  ? -21.044 -50.717 -19.045 1   128.92 ? 77  ILE A O     1 
ATOM   614  C  CB    . ILE A 1 80  ? -20.092 -48.719 -21.557 1   130.45 ? 77  ILE A CB    1 
ATOM   615  C  CG1   . ILE A 1 80  ? -20.233 -48.499 -23.06  1   131.68 ? 77  ILE A CG1   1 
ATOM   616  C  CG2   . ILE A 1 80  ? -18.872 -49.569 -21.26  1   130.85 ? 77  ILE A CG2   1 
ATOM   617  C  CD1   . ILE A 1 80  ? -19.282 -47.554 -23.592 1   133.02 ? 77  ILE A CD1   1 
ATOM   618  N  N     . THR A 1 81  ? -21.46  -48.524 -18.667 1   127.16 ? 78  THR A N     1 
ATOM   619  C  CA    . THR A 1 81  ? -21.41  -48.607 -17.206 1   126.16 ? 78  THR A CA    1 
ATOM   620  C  C     . THR A 1 81  ? -22.473 -49.563 -16.653 1   124.73 ? 78  THR A C     1 
ATOM   621  O  O     . THR A 1 81  ? -22.163 -50.4   -15.807 1   124.86 ? 78  THR A O     1 
ATOM   622  C  CB    . THR A 1 81  ? -21.564 -47.217 -16.593 1   127.49 ? 78  THR A CB    1 
ATOM   623  O  OG1   . THR A 1 81  ? -20.46  -46.408 -16.992 1   128.5  ? 78  THR A OG1   1 
ATOM   624  C  CG2   . THR A 1 81  ? -21.661 -47.261 -15.079 1   127.91 ? 78  THR A CG2   1 
ATOM   625  N  N     . GLU A 1 82  ? -23.711 -49.462 -17.152 1   123.29 ? 79  GLU A N     1 
ATOM   626  C  CA    . GLU A 1 82  ? -24.809 -50.314 -16.715 1   122.56 ? 79  GLU A CA    1 
ATOM   627  C  C     . GLU A 1 82  ? -24.58  -51.777 -17.07  1   121.8  ? 79  GLU A C     1 
ATOM   628  O  O     . GLU A 1 82  ? -24.888 -52.64  -16.253 1   122.06 ? 79  GLU A O     1 
ATOM   629  C  CB    . GLU A 1 82  ? -26.147 -49.803 -17.255 1   124.39 ? 79  GLU A CB    1 
ATOM   630  C  CG    . GLU A 1 82  ? -26.614 -48.548 -16.545 1   128.5  ? 79  GLU A CG    1 
ATOM   631  C  CD    . GLU A 1 82  ? -27.693 -47.755 -17.258 1   134.12 ? 79  GLU A CD    1 
ATOM   632  O  OE1   . GLU A 1 82  ? -27.89  -47.971 -18.474 1   134.75 ? 79  GLU A OE1   1 
ATOM   633  O  OE2   . GLU A 1 82  ? -28.337 -46.907 -16.602 1   136.65 ? 79  GLU A OE2   1 
ATOM   634  N  N     . ARG A 1 83  ? -23.996 -52.06  -18.254 1   120.66 ? 80  ARG A N     1 
ATOM   635  C  CA    . ARG A 1 83  ? -23.662 -53.429 -18.669 1   119.87 ? 80  ARG A CA    1 
ATOM   636  C  C     . ARG A 1 83  ? -22.5   -53.973 -17.852 1   119.75 ? 80  ARG A C     1 
ATOM   637  O  O     . ARG A 1 83  ? -22.484 -55.154 -17.528 1   119.7  ? 80  ARG A O     1 
ATOM   638  C  CB    . ARG A 1 83  ? -23.315 -53.493 -20.155 1   120    ? 80  ARG A CB    1 
ATOM   639  C  CG    . ARG A 1 83  ? -24.47  -53.066 -21.018 1   121.11 ? 80  ARG A CG    1 
ATOM   640  C  CD    . ARG A 1 83  ? -24.155 -53.207 -22.481 1   122.36 ? 80  ARG A CD    1 
ATOM   641  N  NE    . ARG A 1 83  ? -25.125 -52.469 -23.28  1   123.24 ? 80  ARG A NE    1 
ATOM   642  C  CZ    . ARG A 1 83  ? -25.452 -52.763 -24.533 1   124.51 ? 80  ARG A CZ    1 
ATOM   643  N  NH1   . ARG A 1 83  ? -24.892 -53.794 -25.148 1   123.81 ? 80  ARG A NH1   1 
ATOM   644  N  NH2   . ARG A 1 83  ? -26.35  -52.034 -25.176 1   124.38 ? 80  ARG A NH2   1 
ATOM   645  N  N     . ALA A 1 84  ? -21.534 -53.117 -17.504 1   119.6  ? 81  ALA A N     1 
ATOM   646  C  CA    . ALA A 1 84  ? -20.406 -53.527 -16.681 1   119.9  ? 81  ALA A CA    1 
ATOM   647  C  C     . ALA A 1 84  ? -20.833 -53.816 -15.252 1   120.01 ? 81  ALA A C     1 
ATOM   648  O  O     . ALA A 1 84  ? -20.282 -54.726 -14.642 1   120.07 ? 81  ALA A O     1 
ATOM   649  C  CB    . ALA A 1 84  ? -19.327 -52.475 -16.703 1   120.06 ? 81  ALA A CB    1 
ATOM   650  N  N     . ARG A 1 85  ? -21.84  -53.081 -14.732 1   119.89 ? 82  ARG A N     1 
ATOM   651  C  CA    . ARG A 1 85  ? -22.392 -53.314 -13.392 1   120.26 ? 82  ARG A CA    1 
ATOM   652  C  C     . ARG A 1 85  ? -23.238 -54.61  -13.286 1   120.38 ? 82  ARG A C     1 
ATOM   653  O  O     . ARG A 1 85  ? -23.54  -55.073 -12.185 1   120.5  ? 82  ARG A O     1 
ATOM   654  C  CB    . ARG A 1 85  ? -23.161 -52.097 -12.897 1   121.57 ? 82  ARG A CB    1 
ATOM   655  C  CG    . ARG A 1 85  ? -22.221 -50.973 -12.505 1   125.03 ? 82  ARG A CG    1 
ATOM   656  C  CD    . ARG A 1 85  ? -22.978 -49.845 -11.845 1   128.57 ? 82  ARG A CD    1 
ATOM   657  N  NE    . ARG A 1 85  ? -22.249 -48.576 -11.842 1   131.6  ? 82  ARG A NE    1 
ATOM   658  C  CZ    . ARG A 1 85  ? -21.433 -48.179 -10.873 1   134.16 ? 82  ARG A CZ    1 
ATOM   659  N  NH1   . ARG A 1 85  ? -21.164 -48.984 -9.851  1   133.85 ? 82  ARG A NH1   1 
ATOM   660  N  NH2   . ARG A 1 85  ? -20.829 -46.999 -10.947 1   134.46 ? 82  ARG A NH2   1 
ATOM   661  N  N     . MET A 1 86  ? -23.598 -55.197 -14.434 1   120.07 ? 83  MET A N     1 
ATOM   662  C  CA    . MET A 1 86  ? -24.285 -56.482 -14.536 1   120.12 ? 83  MET A CA    1 
ATOM   663  C  C     . MET A 1 86  ? -23.258 -57.648 -14.493 1   120.25 ? 83  MET A C     1 
ATOM   664  O  O     . MET A 1 86  ? -23.664 -58.789 -14.311 1   120.47 ? 83  MET A O     1 
ATOM   665  C  CB    . MET A 1 86  ? -25.063 -56.545 -15.863 1   120.51 ? 83  MET A CB    1 
ATOM   666  C  CG    . MET A 1 86  ? -26.514 -56.921 -15.74  1   122.23 ? 83  MET A CG    1 
ATOM   667  S  SD    . MET A 1 86  ? -27.514 -55.856 -16.809 1   125.57 ? 83  MET A SD    1 
ATOM   668  C  CE    . MET A 1 86  ? -27.729 -54.469 -15.725 1   124.87 ? 83  MET A CE    1 
ATOM   669  N  N     . GLY A 1 87  ? -21.965 -57.368 -14.7   1   120.01 ? 84  GLY A N     1 
ATOM   670  C  CA    . GLY A 1 87  ? -20.908 -58.372 -14.675 1   120.24 ? 84  GLY A CA    1 
ATOM   671  C  C     . GLY A 1 87  ? -20.279 -58.672 -16.021 1   120.07 ? 84  GLY A C     1 
ATOM   672  O  O     . GLY A 1 87  ? -19.656 -59.719 -16.191 1   120.34 ? 84  GLY A O     1 
ATOM   673  N  N     . MET A 1 88  ? -20.429 -57.765 -16.985 1   119.46 ? 85  MET A N     1 
ATOM   674  C  CA    . MET A 1 88  ? -19.874 -57.961 -18.318 1   119.42 ? 85  MET A CA    1 
ATOM   675  C  C     . MET A 1 88  ? -18.725 -56.994 -18.534 1   119.67 ? 85  MET A C     1 
ATOM   676  O  O     . MET A 1 88  ? -18.869 -55.825 -18.215 1   119.79 ? 85  MET A O     1 
ATOM   677  C  CB    . MET A 1 88  ? -20.97  -57.708 -19.364 1   119.68 ? 85  MET A CB    1 
ATOM   678  C  CG    . MET A 1 88  ? -20.489 -57.765 -20.794 1   121.21 ? 85  MET A CG    1 
ATOM   679  S  SD    . MET A 1 88  ? -21.63  -56.936 -21.919 1   124.44 ? 85  MET A SD    1 
ATOM   680  C  CE    . MET A 1 88  ? -23.045 -57.929 -21.726 1   121.98 ? 85  MET A CE    1 
ATOM   681  N  N     . THR A 1 89  ? -17.592 -57.459 -19.073 1   119.78 ? 86  THR A N     1 
ATOM   682  C  CA    . THR A 1 89  ? -16.464 -56.563 -19.372 1   120.5  ? 86  THR A CA    1 
ATOM   683  C  C     . THR A 1 89  ? -15.781 -56.929 -20.714 1   120.54 ? 86  THR A C     1 
ATOM   684  O  O     . THR A 1 89  ? -16.049 -58     -21.257 1   120.9  ? 86  THR A O     1 
ATOM   685  C  CB    . THR A 1 89  ? -15.486 -56.459 -18.204 1   122.28 ? 86  THR A CB    1 
ATOM   686  O  OG1   . THR A 1 89  ? -14.796 -55.208 -18.304 1   123.22 ? 86  THR A OG1   1 
ATOM   687  C  CG2   . THR A 1 89  ? -14.497 -57.61  -18.181 1   122.98 ? 86  THR A CG2   1 
ATOM   688  N  N     . LEU A 1 90  ? -14.923 -56.033 -21.256 1   119.93 ? 87  LEU A N     1 
ATOM   689  C  CA    . LEU A 1 90  ? -14.271 -56.213 -22.556 1   119.84 ? 87  LEU A CA    1 
ATOM   690  C  C     . LEU A 1 90  ? -12.735 -55.966 -22.501 1   120.13 ? 87  LEU A C     1 
ATOM   691  O  O     . LEU A 1 90  ? -12.296 -55.169 -21.678 1   120.16 ? 87  LEU A O     1 
ATOM   692  C  CB    . LEU A 1 90  ? -14.963 -55.235 -23.523 1   119.7  ? 87  LEU A CB    1 
ATOM   693  C  CG    . LEU A 1 90  ? -14.418 -55.084 -24.919 1   120.8  ? 87  LEU A CG    1 
ATOM   694  C  CD1   . LEU A 1 90  ? -14.539 -56.373 -25.686 1   121.11 ? 87  LEU A CD1   1 
ATOM   695  C  CD2   . LEU A 1 90  ? -15.132 -53.972 -25.642 1   121.46 ? 87  LEU A CD2   1 
ATOM   696  N  N     . ALA A 1 91  ? -11.925 -56.654 -23.372 1   120.28 ? 88  ALA A N     1 
ATOM   697  C  CA    . ALA A 1 91  ? -10.449 -56.524 -23.466 1   121.02 ? 88  ALA A CA    1 
ATOM   698  C  C     . ALA A 1 91  ? -9.91   -55.51  -24.54  1   121.7  ? 88  ALA A C     1 
ATOM   699  O  O     . ALA A 1 91  ? -8.879  -54.878 -24.287 1   121.89 ? 88  ALA A O     1 
ATOM   700  C  CB    . ALA A 1 91  ? -9.799  -57.88  -23.668 1   121.09 ? 88  ALA A CB    1 
ATOM   701  N  N     . TRP A 1 92  ? -10.556 -55.399 -25.726 1   121.76 ? 89  TRP A N     1 
ATOM   702  C  CA    . TRP A 1 92  ? -10.27  -54.413 -26.789 1   122.24 ? 89  TRP A CA    1 
ATOM   703  C  C     . TRP A 1 92  ? -9.35   -54.815 -27.962 1   122.72 ? 89  TRP A C     1 
ATOM   704  O  O     . TRP A 1 92  ? -9.629  -54.398 -29.087 1   122.56 ? 89  TRP A O     1 
ATOM   705  C  CB    . TRP A 1 92  ? -9.739  -53.096 -26.214 1   122.12 ? 89  TRP A CB    1 
ATOM   706  C  CG    . TRP A 1 92  ? -10.769 -52.031 -26.296 1   122.44 ? 89  TRP A CG    1 
ATOM   707  C  CD1   . TRP A 1 92  ? -11.062 -51.265 -27.383 1   123.39 ? 89  TRP A CD1   1 
ATOM   708  C  CD2   . TRP A 1 92  ? -11.772 -51.75  -25.325 1   122.39 ? 89  TRP A CD2   1 
ATOM   709  N  NE1   . TRP A 1 92  ? -12.143 -50.467 -27.118 1   123.68 ? 89  TRP A NE1   1 
ATOM   710  C  CE2   . TRP A 1 92  ? -12.614 -50.761 -25.866 1   123.26 ? 89  TRP A CE2   1 
ATOM   711  C  CE3   . TRP A 1 92  ? -12.026 -52.218 -24.035 1   122.81 ? 89  TRP A CE3   1 
ATOM   712  C  CZ2   . TRP A 1 92  ? -13.69  -50.238 -25.166 1   123.86 ? 89  TRP A CZ2   1 
ATOM   713  C  CZ3   . TRP A 1 92  ? -13.095 -51.697 -23.343 1   123.7  ? 89  TRP A CZ3   1 
ATOM   714  C  CH2   . TRP A 1 92  ? -13.92  -50.727 -23.911 1   123.91 ? 89  TRP A CH2   1 
ATOM   715  N  N     . GLN A 1 93  ? -8.243  -55.518 -27.699 1   123.17 ? 90  GLN A N     1 
ATOM   716  C  CA    . GLN A 1 93  ? -7.191  -55.912 -28.658 1   124.08 ? 90  GLN A CA    1 
ATOM   717  C  C     . GLN A 1 93  ? -6.029  -54.938 -28.502 1   125.41 ? 90  GLN A C     1 
ATOM   718  O  O     . GLN A 1 93  ? -4.897  -55.365 -28.262 1   125.86 ? 90  GLN A O     1 
ATOM   719  C  CB    . GLN A 1 93  ? -7.662  -55.998 -30.125 1   124.71 ? 90  GLN A CB    1 
ATOM   720  C  CG    . GLN A 1 93  ? -6.991  -57.119 -30.889 1   126.21 ? 90  GLN A CG    1 
ATOM   721  C  CD    . GLN A 1 93  ? -6.176  -56.654 -32.055 1   128.28 ? 90  GLN A CD    1 
ATOM   722  O  OE1   . GLN A 1 93  ? -6.426  -55.595 -32.628 1   129.29 ? 90  GLN A OE1   1 
ATOM   723  N  NE2   . GLN A 1 93  ? -5.187  -57.446 -32.437 1   128.2  ? 90  GLN A NE2   1 
ATOM   724  N  N     . GLU A 1 94  ? -6.315  -53.624 -28.59  1   125.69 ? 91  GLU A N     1 
ATOM   725  C  CA    . GLU A 1 94  ? -5.336  -52.565 -28.358 1   126.43 ? 91  GLU A CA    1 
ATOM   726  C  C     . GLU A 1 94  ? -5.803  -51.807 -27.106 1   126.6  ? 91  GLU A C     1 
ATOM   727  O  O     . GLU A 1 94  ? -6.518  -50.816 -27.243 1   126.74 ? 91  GLU A O     1 
ATOM   728  C  CB    . GLU A 1 94  ? -5.283  -51.604 -29.557 1   129.26 ? 91  GLU A CB    1 
ATOM   729  C  CG    . GLU A 1 94  ? -4.052  -51.766 -30.426 1   135.22 ? 91  GLU A CG    1 
ATOM   730  C  CD    . GLU A 1 94  ? -4.205  -52.818 -31.503 1   142.75 ? 91  GLU A CD    1 
ATOM   731  O  OE1   . GLU A 1 94  ? -5.078  -52.643 -32.385 1   144.29 ? 91  GLU A OE1   1 
ATOM   732  O  OE2   . GLU A 1 94  ? -3.453  -53.819 -31.468 1   145.35 ? 91  GLU A OE2   1 
ATOM   733  N  N     . PRO A 1 95  ? -5.482  -52.27  -25.875 1   126.47 ? 92  PRO A N     1 
ATOM   734  C  CA    . PRO A 1 95  ? -5.987  -51.579 -24.681 1   126.67 ? 92  PRO A CA    1 
ATOM   735  C  C     . PRO A 1 95  ? -5.52   -50.131 -24.624 1   127.47 ? 92  PRO A C     1 
ATOM   736  O  O     . PRO A 1 95  ? -4.363  -49.854 -24.925 1   127.9  ? 92  PRO A O     1 
ATOM   737  C  CB    . PRO A 1 95  ? -5.458  -52.439 -23.531 1   127.12 ? 92  PRO A CB    1 
ATOM   738  C  CG    . PRO A 1 95  ? -5.228  -53.78  -24.14  1   127.5  ? 92  PRO A CG    1 
ATOM   739  C  CD    . PRO A 1 95  ? -4.686  -53.449 -25.497 1   125.94 ? 92  PRO A CD    1 
ATOM   740  N  N     . ALA A 1 96  ? -6.448  -49.203 -24.352 1   127.53 ? 93  ALA A N     1 
ATOM   741  C  CA    . ALA A 1 96  ? -6.167  -47.77  -24.331 1   128.08 ? 93  ALA A CA    1 
ATOM   742  C  C     . ALA A 1 96  ? -5.066  -47.381 -23.354 1   128.48 ? 93  ALA A C     1 
ATOM   743  O  O     . ALA A 1 96  ? -4.978  -47.955 -22.267 1   128.76 ? 93  ALA A O     1 
ATOM   744  C  CB    . ALA A 1 96  ? -7.436  -46.998 -24.007 1   128.26 ? 93  ALA A CB    1 
ATOM   745  N  N     . ARG A 1 97  ? -4.22   -46.409 -23.746 1   128.25 ? 94  ARG A N     1 
ATOM   746  C  CA    . ARG A 1 97  ? -3.166  -45.89  -22.874 1   128.44 ? 94  ARG A CA    1 
ATOM   747  C  C     . ARG A 1 97  ? -3.729  -44.73  -22.064 1   128.77 ? 94  ARG A C     1 
ATOM   748  O  O     . ARG A 1 97  ? -4.544  -43.962 -22.568 1   128.82 ? 94  ARG A O     1 
ATOM   749  C  CB    . ARG A 1 97  ? -1.935  -45.441 -23.674 1   129.31 ? 94  ARG A CB    1 
ATOM   750  C  CG    . ARG A 1 97  ? -1.366  -46.518 -24.589 1   131.66 ? 94  ARG A CG    1 
ATOM   751  C  CD    . ARG A 1 97  ? -0.956  -47.776 -23.848 1   134.05 ? 94  ARG A CD    1 
ATOM   752  N  NE    . ARG A 1 97  ? -0.46   -48.807 -24.759 1   136.22 ? 94  ARG A NE    1 
ATOM   753  C  CZ    . ARG A 1 97  ? 0.813   -49.174 -24.853 1   138.33 ? 94  ARG A CZ    1 
ATOM   754  N  NH1   . ARG A 1 97  ? 1.733   -48.607 -24.082 1   138.13 ? 94  ARG A NH1   1 
ATOM   755  N  NH2   . ARG A 1 97  ? 1.175   -50.114 -25.714 1   138.28 ? 94  ARG A NH2   1 
ATOM   756  N  N     . PHE A 1 98  ? -3.315  -44.612 -20.806 1   128.82 ? 95  PHE A N     1 
ATOM   757  C  CA    . PHE A 1 98  ? -3.828  -43.584 -19.912 1   129.25 ? 95  PHE A CA    1 
ATOM   758  C  C     . PHE A 1 98  ? -2.73   -42.717 -19.328 1   130.18 ? 95  PHE A C     1 
ATOM   759  O  O     . PHE A 1 98  ? -1.757  -43.248 -18.791 1   130.52 ? 95  PHE A O     1 
ATOM   760  C  CB    . PHE A 1 98  ? -4.582  -44.249 -18.749 1   128.53 ? 95  PHE A CB    1 
ATOM   761  C  CG    . PHE A 1 98  ? -5.856  -44.95  -19.138 1   128.43 ? 95  PHE A CG    1 
ATOM   762  C  CD1   . PHE A 1 98  ? -7.047  -44.257 -19.224 1   129.04 ? 95  PHE A CD1   1 
ATOM   763  C  CD2   . PHE A 1 98  ? -5.867  -46.308 -19.399 1   128.73 ? 95  PHE A CD2   1 
ATOM   764  C  CE1   . PHE A 1 98  ? -8.217  -44.902 -19.584 1   129.61 ? 95  PHE A CE1   1 
ATOM   765  C  CE2   . PHE A 1 98  ? -7.04   -46.95  -19.756 1   129.25 ? 95  PHE A CE2   1 
ATOM   766  C  CZ    . PHE A 1 98  ? -8.207  -46.245 -19.845 1   129.15 ? 95  PHE A CZ    1 
ATOM   767  N  N     . GLU A 1 99  ? -2.925  -41.39  -19.346 1   130.38 ? 96  GLU A N     1 
ATOM   768  C  CA    . GLU A 1 99  ? -1.969  -40.474 -18.734 1   131.19 ? 96  GLU A CA    1 
ATOM   769  C  C     . GLU A 1 99  ? -2.081  -40.548 -17.216 1   131.65 ? 96  GLU A C     1 
ATOM   770  O  O     . GLU A 1 99  ? -3.181  -40.429 -16.683 1   131.94 ? 96  GLU A O     1 
ATOM   771  C  CB    . GLU A 1 99  ? -2.225  -39.019 -19.187 1   133.51 ? 96  GLU A CB    1 
ATOM   772  C  CG    . GLU A 1 99  ? -1.318  -37.983 -18.531 1   137.46 ? 96  GLU A CG    1 
ATOM   773  C  CD    . GLU A 1 99  ? 0.094   -37.932 -19.08  1   142.3  ? 96  GLU A CD    1 
ATOM   774  O  OE1   . GLU A 1 99  ? 0.305   -38.427 -20.212 1   142.36 ? 96  GLU A OE1   1 
ATOM   775  O  OE2   . GLU A 1 99  ? 0.986   -37.39  -18.387 1   144.6  ? 96  GLU A OE2   1 
ATOM   776  N  N     . GLY A 1 100 ? -0.948  -40.766 -16.554 1   131.55 ? 97  GLY A N     1 
ATOM   777  C  CA    . GLY A 1 100 ? -0.817  -40.771 -15.101 1   131.89 ? 97  GLY A CA    1 
ATOM   778  C  C     . GLY A 1 100 ? -1.579  -41.773 -14.257 1   131.79 ? 97  GLY A C     1 
ATOM   779  O  O     . GLY A 1 100 ? -1.79   -41.519 -13.066 1   131.85 ? 97  GLY A O     1 
ATOM   780  N  N     . ILE A 1 101 ? -1.953  -42.932 -14.824 1   131.33 ? 98  ILE A N     1 
ATOM   781  C  CA    . ILE A 1 101 ? -2.638  -43.953 -14.033 1   131.36 ? 98  ILE A CA    1 
ATOM   782  C  C     . ILE A 1 101 ? -1.668  -45.089 -13.745 1   131.24 ? 98  ILE A C     1 
ATOM   783  O  O     . ILE A 1 101 ? -1.228  -45.736 -14.684 1   131.47 ? 98  ILE A O     1 
ATOM   784  C  CB    . ILE A 1 101 ? -3.933  -44.439 -14.719 1   131.71 ? 98  ILE A CB    1 
ATOM   785  C  CG1   . ILE A 1 101 ? -4.907  -43.261 -14.935 1   132.49 ? 98  ILE A CG1   1 
ATOM   786  C  CG2   . ILE A 1 101 ? -4.574  -45.553 -13.895 1   132.14 ? 98  ILE A CG2   1 
ATOM   787  C  CD1   . ILE A 1 101 ? -6.177  -43.584 -15.651 1   133.53 ? 98  ILE A CD1   1 
ATOM   788  N  N     . LYS A 1 102 ? -1.283  -45.305 -12.469 1   130.62 ? 99  LYS A N     1 
ATOM   789  C  CA    . LYS A 1 102 ? -0.353  -46.39  -12.135 1   130.38 ? 99  LYS A CA    1 
ATOM   790  C  C     . LYS A 1 102 ? -1.018  -47.757 -12.28  1   130.07 ? 99  LYS A C     1 
ATOM   791  O  O     . LYS A 1 102 ? -2.236  -47.861 -12.213 1   130.06 ? 99  LYS A O     1 
ATOM   792  C  CB    . LYS A 1 102 ? 0.214   -46.238 -10.715 1   131.72 ? 99  LYS A CB    1 
ATOM   793  C  CG    . LYS A 1 102 ? 1.205   -45.113 -10.559 1   135.2  ? 99  LYS A CG    1 
ATOM   794  C  CD    . LYS A 1 102 ? 1.923   -45.22  -9.232  1   139.34 ? 99  LYS A CD    1 
ATOM   795  C  CE    . LYS A 1 102 ? 2.693   -43.975 -8.883  1   142.93 ? 99  LYS A CE    1 
ATOM   796  N  NZ    . LYS A 1 102 ? 3.268   -44.062 -7.514  1   145.28 ? 99  LYS A NZ    1 
ATOM   797  N  N     . VAL A 1 103 ? -0.213  -48.805 -12.472 1   129.68 ? 100 VAL A N     1 
ATOM   798  C  CA    . VAL A 1 103 ? -0.688  -50.172 -12.6   1   129.89 ? 100 VAL A CA    1 
ATOM   799  C  C     . VAL A 1 103 ? -1.426  -50.593 -11.32  1   130.05 ? 100 VAL A C     1 
ATOM   800  O  O     . VAL A 1 103 ? -2.52   -51.149 -11.405 1   130.25 ? 100 VAL A O     1 
ATOM   801  C  CB    . VAL A 1 103 ? 0.5     -51.102 -12.934 1   130.58 ? 100 VAL A CB    1 
ATOM   802  C  CG1   . VAL A 1 103 ? 0.16    -52.569 -12.703 1   131.26 ? 100 VAL A CG1   1 
ATOM   803  C  CG2   . VAL A 1 103 ? 0.974   -50.876 -14.36  1   131.01 ? 100 VAL A CG2   1 
ATOM   804  N  N     . LYS A 1 104 ? -0.874  -50.248 -10.14  1   129.75 ? 101 LYS A N     1 
ATOM   805  C  CA    . LYS A 1 104 ? -1.497  -50.58  -8.858  1   129.75 ? 101 LYS A CA    1 
ATOM   806  C  C     . LYS A 1 104 ? -2.886  -49.95  -8.675  1   129.66 ? 101 LYS A C     1 
ATOM   807  O  O     . LYS A 1 104 ? -3.757  -50.565 -8.07   1   129.71 ? 101 LYS A O     1 
ATOM   808  C  CB    . LYS A 1 104 ? -0.567  -50.251 -7.679  1   131.27 ? 101 LYS A CB    1 
ATOM   809  C  CG    . LYS A 1 104 ? -0.34   -48.775 -7.436  1   134.8  ? 101 LYS A CG    1 
ATOM   810  C  CD    . LYS A 1 104 ? 0.644   -48.562 -6.302  1   138.98 ? 101 LYS A CD    1 
ATOM   811  C  CE    . LYS A 1 104 ? 0.784   -47.102 -5.956  1   142.67 ? 101 LYS A CE    1 
ATOM   812  N  NZ    . LYS A 1 104 ? 2.01    -46.83  -5.156  1   144.73 ? 101 LYS A NZ    1 
ATOM   813  N  N     . ASN A 1 105 ? -3.11   -48.751 -9.227  1   129.38 ? 102 ASN A N     1 
ATOM   814  C  CA    . ASN A 1 105 ? -4.417  -48.096 -9.141  1   129.51 ? 102 ASN A CA    1 
ATOM   815  C  C     . ASN A 1 105 ? -5.345  -48.548 -10.269 1   129.31 ? 102 ASN A C     1 
ATOM   816  O  O     . ASN A 1 105 ? -6.56   -48.543 -10.092 1   129.18 ? 102 ASN A O     1 
ATOM   817  C  CB    . ASN A 1 105 ? -4.271  -46.583 -9.199  1   130.77 ? 102 ASN A CB    1 
ATOM   818  C  CG    . ASN A 1 105 ? -3.303  -46.007 -8.205  1   134.22 ? 102 ASN A CG    1 
ATOM   819  O  OD1   . ASN A 1 105 ? -3.342  -46.307 -7.008  1   135.99 ? 102 ASN A OD1   1 
ATOM   820  N  ND2   . ASN A 1 105 ? -2.421  -45.148 -8.68   1   134.48 ? 102 ASN A ND2   1 
ATOM   821  N  N     . TYR A 1 106 ? -4.78   -48.882 -11.442 1   129.16 ? 103 TYR A N     1 
ATOM   822  C  CA    . TYR A 1 106 ? -5.533  -49.339 -12.602 1   129.57 ? 103 TYR A CA    1 
ATOM   823  C  C     . TYR A 1 106 ? -6.134  -50.707 -12.314 1   130.1  ? 103 TYR A C     1 
ATOM   824  O  O     . TYR A 1 106 ? -7.286  -50.951 -12.666 1   130.5  ? 103 TYR A O     1 
ATOM   825  C  CB    . TYR A 1 106 ? -4.642  -49.405 -13.862 1   129.44 ? 103 TYR A CB    1 
ATOM   826  C  CG    . TYR A 1 106 ? -5.41   -49.809 -15.103 1   129.93 ? 103 TYR A CG    1 
ATOM   827  C  CD1   . TYR A 1 106 ? -6.275  -48.923 -15.727 1   130.64 ? 103 TYR A CD1   1 
ATOM   828  C  CD2   . TYR A 1 106 ? -5.31   -51.094 -15.622 1   130.64 ? 103 TYR A CD2   1 
ATOM   829  C  CE1   . TYR A 1 106 ? -7.019  -49.301 -16.837 1   131.44 ? 103 TYR A CE1   1 
ATOM   830  C  CE2   . TYR A 1 106 ? -6.054  -51.485 -16.729 1   131.39 ? 103 TYR A CE2   1 
ATOM   831  C  CZ    . TYR A 1 106 ? -6.904  -50.583 -17.337 1   132.18 ? 103 TYR A CZ    1 
ATOM   832  O  OH    . TYR A 1 106 ? -7.632  -50.947 -18.442 1   133.41 ? 103 TYR A OH    1 
ATOM   833  N  N     . LEU A 1 107 ? -5.371  -51.6   -11.668 1   129.97 ? 104 LEU A N     1 
ATOM   834  C  CA    . LEU A 1 107 ? -5.868  -52.939 -11.356 1   130.4  ? 104 LEU A CA    1 
ATOM   835  C  C     . LEU A 1 107 ? -6.964  -52.965 -10.278 1   130.82 ? 104 LEU A C     1 
ATOM   836  O  O     . LEU A 1 107 ? -7.67   -53.963 -10.141 1   130.86 ? 104 LEU A O     1 
ATOM   837  C  CB    . LEU A 1 107 ? -4.714  -53.88  -11.011 1   130.63 ? 104 LEU A CB    1 
ATOM   838  C  CG    . LEU A 1 107 ? -3.686  -54.074 -12.134 1   132.25 ? 104 LEU A CG    1 
ATOM   839  C  CD1   . LEU A 1 107 ? -2.61   -55.032 -11.729 1   132.74 ? 104 LEU A CD1   1 
ATOM   840  C  CD2   . LEU A 1 107 ? -4.329  -54.565 -13.418 1   133.17 ? 104 LEU A CD2   1 
ATOM   841  N  N     . MET A 1 108 ? -7.135  -51.859 -9.551  1   130.95 ? 105 MET A N     1 
ATOM   842  C  CA    . MET A 1 108 ? -8.195  -51.703 -8.566  1   131.51 ? 105 MET A CA    1 
ATOM   843  C  C     . MET A 1 108 ? -9.528  -51.336 -9.25   1   131.58 ? 105 MET A C     1 
ATOM   844  O  O     . MET A 1 108 ? -10.58  -51.563 -8.669  1   131.83 ? 105 MET A O     1 
ATOM   845  C  CB    . MET A 1 108 ? -7.826  -50.598 -7.563  1   132.52 ? 105 MET A CB    1 
ATOM   846  C  CG    . MET A 1 108 ? -6.743  -50.992 -6.599  1   135.38 ? 105 MET A CG    1 
ATOM   847  S  SD    . MET A 1 108 ? -7.315  -52.266 -5.463  1   141.83 ? 105 MET A SD    1 
ATOM   848  C  CE    . MET A 1 108 ? -6.02   -52.203 -4.227  1   141.51 ? 105 MET A CE    1 
ATOM   849  N  N     . LEU A 1 109 ? -9.491  -50.733 -10.447 1   131.26 ? 106 LEU A N     1 
ATOM   850  C  CA    . LEU A 1 109 ? -10.697 -50.304 -11.143 1   131.45 ? 106 LEU A CA    1 
ATOM   851  C  C     . LEU A 1 109 ? -11.529 -51.477 -11.602 1   131.85 ? 106 LEU A C     1 
ATOM   852  O  O     . LEU A 1 109 ? -11.075 -52.309 -12.381 1   131.74 ? 106 LEU A O     1 
ATOM   853  C  CB    . LEU A 1 109 ? -10.357 -49.381 -12.322 1   131.39 ? 106 LEU A CB    1 
ATOM   854  C  CG    . LEU A 1 109 ? -9.43   -48.205 -12.013 1   132.21 ? 106 LEU A CG    1 
ATOM   855  C  CD1   . LEU A 1 109 ? -9.087  -47.457 -13.263 1   132.46 ? 106 LEU A CD1   1 
ATOM   856  C  CD2   . LEU A 1 109 ? -10.039 -47.276 -10.987 1   132.75 ? 106 LEU A CD2   1 
ATOM   857  N  N     . GLY A 1 110 ? -12.739 -51.545 -11.084 1   132.39 ? 107 GLY A N     1 
ATOM   858  C  CA    . GLY A 1 110 ? -13.657 -52.621 -11.415 1   133.5  ? 107 GLY A CA    1 
ATOM   859  C  C     . GLY A 1 110 ? -13.435 -53.914 -10.664 1   134.42 ? 107 GLY A C     1 
ATOM   860  O  O     . GLY A 1 110 ? -14.162 -54.88  -10.897 1   134.3  ? 107 GLY A O     1 
ATOM   861  N  N     . MET A 1 111 ? -12.448 -53.939 -9.739  1   135.19 ? 108 MET A N     1 
ATOM   862  C  CA    . MET A 1 111 ? -12.108 -55.107 -8.927  1   136.52 ? 108 MET A CA    1 
ATOM   863  C  C     . MET A 1 111 ? -13.335 -55.716 -8.254  1   138.38 ? 108 MET A C     1 
ATOM   864  O  O     . MET A 1 111 ? -14.212 -54.988 -7.789  1   138.62 ? 108 MET A O     1 
ATOM   865  C  CB    . MET A 1 111 ? -11.028 -54.771 -7.881  1   136.6  ? 108 MET A CB    1 
ATOM   866  C  CG    . MET A 1 111 ? -10.581 -55.977 -7.079  1   137.56 ? 108 MET A CG    1 
ATOM   867  S  SD    . MET A 1 111 ? -9.228  -55.691 -5.918  1   137.7  ? 108 MET A SD    1 
ATOM   868  C  CE    . MET A 1 111 ? -7.86   -55.649 -7.03   1   135.09 ? 108 MET A CE    1 
ATOM   869  N  N     . ASN A 1 112 ? -13.417 -57.05  -8.254  1   139.54 ? 109 ASN A N     1 
ATOM   870  C  CA    . ASN A 1 112 ? -14.528 -57.79  -7.678  1   141.19 ? 109 ASN A CA    1 
ATOM   871  C  C     . ASN A 1 112 ? -14.727 -57.451 -6.216  1   142.97 ? 109 ASN A C     1 
ATOM   872  O  O     . ASN A 1 112 ? -13.752 -57.275 -5.492  1   143.03 ? 109 ASN A O     1 
ATOM   873  C  CB    . ASN A 1 112 ? -14.291 -59.279 -7.829  1   142.31 ? 109 ASN A CB    1 
ATOM   874  C  CG    . ASN A 1 112 ? -15.573 -60.051 -7.869  1   145.6  ? 109 ASN A CG    1 
ATOM   875  O  OD1   . ASN A 1 112 ? -16.225 -60.274 -6.848  1   146.76 ? 109 ASN A OD1   1 
ATOM   876  N  ND2   . ASN A 1 112 ? -15.977 -60.459 -9.056  1   146.39 ? 109 ASN A ND2   1 
ATOM   877  N  N     . GLU A 1 113 ? -15.984 -57.363 -5.781  1   144.35 ? 110 GLU A N     1 
ATOM   878  C  CA    . GLU A 1 113 ? -16.323 -57.045 -4.396  1   146.26 ? 110 GLU A CA    1 
ATOM   879  C  C     . GLU A 1 113 ? -15.722 -58.017 -3.378  1   147.6  ? 110 GLU A C     1 
ATOM   880  O  O     . GLU A 1 113 ? -15.504 -57.639 -2.23   1   147.66 ? 110 GLU A O     1 
ATOM   881  C  CB    . GLU A 1 113 ? -17.839 -56.937 -4.22   1   149.3  ? 110 GLU A CB    1 
ATOM   882  C  CG    . GLU A 1 113 ? -18.363 -55.562 -4.584  1   155.54 ? 110 GLU A CG    1 
ATOM   883  C  CD    . GLU A 1 113 ? -17.99  -54.491 -3.579  1   163.45 ? 110 GLU A CD    1 
ATOM   884  O  OE1   . GLU A 1 113 ? -17.354 -53.49  -3.98   1   164.8  ? 110 GLU A OE1   1 
ATOM   885  O  OE2   . GLU A 1 113 ? -18.332 -54.656 -2.385  1   166.31 ? 110 GLU A OE2   1 
ATOM   886  N  N     . LYS A 1 114 ? -15.422 -59.253 -3.796  1   148.48 ? 111 LYS A N     1 
ATOM   887  C  CA    . LYS A 1 114 ? -14.806 -60.237 -2.904  1   149.61 ? 111 LYS A CA    1 
ATOM   888  C  C     . LYS A 1 114 ? -13.306 -59.957 -2.63   1   150.67 ? 111 LYS A C     1 
ATOM   889  O  O     . LYS A 1 114 ? -12.722 -60.591 -1.753  1   150.94 ? 111 LYS A O     1 
ATOM   890  C  CB    . LYS A 1 114 ? -15.032 -61.674 -3.416  1   151.18 ? 111 LYS A CB    1 
ATOM   891  C  CG    . LYS A 1 114 ? -14.384 -61.959 -4.763  1   154.66 ? 111 LYS A CG    1 
ATOM   892  C  CD    . LYS A 1 114 ? -14.861 -63.265 -5.359  1   158.55 ? 111 LYS A CD    1 
ATOM   893  C  CE    . LYS A 1 114 ? -13.917 -64.39  -5.033  1   162.26 ? 111 LYS A CE    1 
ATOM   894  N  NZ    . LYS A 1 114 ? -14.395 -65.686 -5.583  1   164.83 ? 111 LYS A NZ    1 
ATOM   895  N  N     . TYR A 1 115 ? -12.687 -59.014 -3.36   1   151.06 ? 112 TYR A N     1 
ATOM   896  C  CA    . TYR A 1 115 ? -11.29  -58.662 -3.135  1   151.97 ? 112 TYR A CA    1 
ATOM   897  C  C     . TYR A 1 115 ? -11.211 -57.208 -2.713  1   152.94 ? 112 TYR A C     1 
ATOM   898  O  O     . TYR A 1 115 ? -10.558 -56.898 -1.724  1   153.16 ? 112 TYR A O     1 
ATOM   899  C  CB    . TYR A 1 115 ? -10.451 -58.878 -4.398  1   152.04 ? 112 TYR A CB    1 
ATOM   900  C  CG    . TYR A 1 115 ? -10.585 -60.259 -4.986  1   152.79 ? 112 TYR A CG    1 
ATOM   901  C  CD1   . TYR A 1 115 ? -10.04  -61.357 -4.351  1   153.75 ? 112 TYR A CD1   1 
ATOM   902  C  CD2   . TYR A 1 115 ? -11.233 -60.463 -6.194  1   153.62 ? 112 TYR A CD2   1 
ATOM   903  C  CE1   . TYR A 1 115 ? -10.155 -62.629 -4.889  1   154.7  ? 112 TYR A CE1   1 
ATOM   904  C  CE2   . TYR A 1 115 ? -11.338 -61.729 -6.751  1   154.54 ? 112 TYR A CE2   1 
ATOM   905  C  CZ    . TYR A 1 115 ? -10.801 -62.812 -6.09   1   155.58 ? 112 TYR A CZ    1 
ATOM   906  O  OH    . TYR A 1 115 ? -10.896 -64.077 -6.606  1   157.25 ? 112 TYR A OH    1 
ATOM   907  N  N     . LYS A 1 116 ? -11.915 -56.327 -3.45   1   153.36 ? 113 LYS A N     1 
ATOM   908  C  CA    . LYS A 1 116 ? -12.007 -54.875 -3.284  1   154.22 ? 113 LYS A CA    1 
ATOM   909  C  C     . LYS A 1 116 ? -12.221 -54.393 -1.835  1   155.16 ? 113 LYS A C     1 
ATOM   910  O  O     . LYS A 1 116 ? -11.701 -53.343 -1.453  1   155.32 ? 113 LYS A O     1 
ATOM   911  C  CB    . LYS A 1 116 ? -13.139 -54.358 -4.182  1   155.71 ? 113 LYS A CB    1 
ATOM   912  C  CG    . LYS A 1 116 ? -13.208 -52.855 -4.319  1   159.33 ? 113 LYS A CG    1 
ATOM   913  C  CD    . LYS A 1 116 ? -14.375 -52.454 -5.193  1   163.28 ? 113 LYS A CD    1 
ATOM   914  C  CE    . LYS A 1 116 ? -14.664 -50.973 -5.083  1   166.74 ? 113 LYS A CE    1 
ATOM   915  N  NZ    . LYS A 1 116 ? -15.143 -50.594 -3.722  1   168.77 ? 113 LYS A NZ    1 
ATOM   916  N  N     . LYS A 1 117 ? -12.982 -55.166 -1.039  1   155.62 ? 114 LYS A N     1 
ATOM   917  C  CA    . LYS A 1 117 ? -13.336 -54.867 0.349   1   156.51 ? 114 LYS A CA    1 
ATOM   918  C  C     . LYS A 1 117 ? -12.119 -54.781 1.318   1   157.27 ? 114 LYS A C     1 
ATOM   919  O  O     . LYS A 1 117 ? -11.782 -53.684 1.784   1   157.52 ? 114 LYS A O     1 
ATOM   920  C  CB    . LYS A 1 117 ? -14.396 -55.875 0.848   1   158.2  ? 114 LYS A CB    1 
ATOM   921  C  CG    . LYS A 1 117 ? -15.757 -55.692 0.198   1   162.25 ? 114 LYS A CG    1 
ATOM   922  C  CD    . LYS A 1 117 ? -16.774 -55.079 1.159   1   166.96 ? 114 LYS A CD    1 
ATOM   923  C  CE    . LYS A 1 117 ? -17.072 -53.613 0.898   1   170.7  ? 114 LYS A CE    1 
ATOM   924  N  NZ    . LYS A 1 117 ? -17.891 -52.998 1.988   1   172.7  ? 114 LYS A NZ    1 
ATOM   925  N  N     . ASP A 1 118 ? -11.472 -55.918 1.625   1   157.42 ? 115 ASP A N     1 
ATOM   926  C  CA    . ASP A 1 118 ? -10.329 -55.929 2.532   1   158.03 ? 115 ASP A CA    1 
ATOM   927  C  C     . ASP A 1 118 ? -9.136  -55.309 1.821   1   158.11 ? 115 ASP A C     1 
ATOM   928  O  O     . ASP A 1 118 ? -8.88   -55.623 0.661   1   158.32 ? 115 ASP A O     1 
ATOM   929  C  CB    . ASP A 1 118 ? -10.012 -57.369 2.978   1   159.93 ? 115 ASP A CB    1 
ATOM   930  C  CG    . ASP A 1 118 ? -9.208  -57.483 4.261   1   164.39 ? 115 ASP A CG    1 
ATOM   931  O  OD1   . ASP A 1 118 ? -8.557  -56.488 4.647   1   165.16 ? 115 ASP A OD1   1 
ATOM   932  O  OD2   . ASP A 1 118 ? -9.223  -58.572 4.874   1   166.3  ? 115 ASP A OD2   1 
ATOM   933  N  N     . LYS A 1 119 ? -8.427  -54.411 2.506   1   157.73 ? 116 LYS A N     1 
ATOM   934  C  CA    . LYS A 1 119 ? -7.264  -53.731 1.951   1   157.94 ? 116 LYS A CA    1 
ATOM   935  C  C     . LYS A 1 119 ? -6.116  -54.711 1.645   1   157.86 ? 116 LYS A C     1 
ATOM   936  O  O     . LYS A 1 119 ? -5.649  -54.763 0.507   1   158.15 ? 116 LYS A O     1 
ATOM   937  C  CB    . LYS A 1 119 ? -6.836  -52.588 2.892   1   159.81 ? 116 LYS A CB    1 
ATOM   938  C  CG    . LYS A 1 119 ? -5.412  -52.064 2.716   1   163.89 ? 116 LYS A CG    1 
ATOM   939  C  CD    . LYS A 1 119 ? -5.054  -51.078 3.825   1   168.47 ? 116 LYS A CD    1 
ATOM   940  C  CE    . LYS A 1 119 ? -5.247  -51.649 5.22    1   172.36 ? 116 LYS A CE    1 
ATOM   941  N  NZ    . LYS A 1 119 ? -4.969  -50.652 6.297   1   174.82 ? 116 LYS A NZ    1 
ATOM   942  N  N     . GLU A 1 120 ? -5.696  -55.509 2.639   1   157.38 ? 117 GLU A N     1 
ATOM   943  C  CA    . GLU A 1 120 ? -4.612  -56.476 2.467   1   157.52 ? 117 GLU A CA    1 
ATOM   944  C  C     . GLU A 1 120 ? -4.953  -57.611 1.473   1   157.35 ? 117 GLU A C     1 
ATOM   945  O  O     . GLU A 1 120 ? -4.046  -58.237 0.928   1   157.53 ? 117 GLU A O     1 
ATOM   946  C  CB    . GLU A 1 120 ? -4.157  -57.022 3.832   1   159.69 ? 117 GLU A CB    1 
ATOM   947  C  CG    . GLU A 1 120 ? -3.567  -55.959 4.751   1   164.26 ? 117 GLU A CG    1 
ATOM   948  C  CD    . GLU A 1 120 ? -4.136  -55.898 6.159   1   170.55 ? 117 GLU A CD    1 
ATOM   949  O  OE1   . GLU A 1 120 ? -5.368  -55.719 6.296   1   172.09 ? 117 GLU A OE1   1 
ATOM   950  O  OE2   . GLU A 1 120 ? -3.349  -56.015 7.128   1   172.37 ? 117 GLU A OE2   1 
ATOM   951  N  N     . ILE A 1 121 ? -6.251  -57.85  1.214   1   156.81 ? 118 ILE A N     1 
ATOM   952  C  CA    . ILE A 1 121 ? -6.703  -58.863 0.257   1   156.78 ? 118 ILE A CA    1 
ATOM   953  C  C     . ILE A 1 121 ? -6.712  -58.291 -1.16   1   156.42 ? 118 ILE A C     1 
ATOM   954  O  O     . ILE A 1 121 ? -6.381  -59.005 -2.106  1   156.51 ? 118 ILE A O     1 
ATOM   955  C  CB    . ILE A 1 121 ? -8.081  -59.45  0.668   1   157.42 ? 118 ILE A CB    1 
ATOM   956  C  CG1   . ILE A 1 121 ? -7.912  -60.492 1.765   1   158.7  ? 118 ILE A CG1   1 
ATOM   957  C  CG2   . ILE A 1 121 ? -8.868  -60.035 -0.525  1   157.79 ? 118 ILE A CG2   1 
ATOM   958  C  CD1   . ILE A 1 121 ? -9.178  -60.951 2.283   1   160.24 ? 118 ILE A CD1   1 
ATOM   959  N  N     . ALA A 1 122 ? -7.104  -57.018 -1.31   1   155.88 ? 119 ALA A N     1 
ATOM   960  C  CA    . ALA A 1 122 ? -7.142  -56.365 -2.615  1   155.77 ? 119 ALA A CA    1 
ATOM   961  C  C     . ALA A 1 122 ? -5.726  -56.194 -3.154  1   155.37 ? 119 ALA A C     1 
ATOM   962  O  O     . ALA A 1 122 ? -5.481  -56.465 -4.33   1   155.43 ? 119 ALA A O     1 
ATOM   963  C  CB    . ALA A 1 122 ? -7.837  -55.012 -2.511  1   155.95 ? 119 ALA A CB    1 
ATOM   964  N  N     . GLU A 1 123 ? -4.786  -55.79  -2.282  1   154.82 ? 120 GLU A N     1 
ATOM   965  C  CA    . GLU A 1 123 ? -3.383  -55.595 -2.64   1   154.75 ? 120 GLU A CA    1 
ATOM   966  C  C     . GLU A 1 123 ? -2.687  -56.925 -2.989  1   154.05 ? 120 GLU A C     1 
ATOM   967  O  O     . GLU A 1 123 ? -1.778  -56.95  -3.817  1   154.14 ? 120 GLU A O     1 
ATOM   968  C  CB    . GLU A 1 123 ? -2.649  -54.851 -1.51   1   157.38 ? 120 GLU A CB    1 
ATOM   969  C  CG    . GLU A 1 123 ? -3.154  -53.431 -1.291  1   162.76 ? 120 GLU A CG    1 
ATOM   970  C  CD    . GLU A 1 123 ? -2.725  -52.763 0.006   1   169.51 ? 120 GLU A CD    1 
ATOM   971  O  OE1   . GLU A 1 123 ? -2.124  -53.451 0.864   1   170.48 ? 120 GLU A OE1   1 
ATOM   972  O  OE2   . GLU A 1 123 ? -2.997  -51.55  0.167   1   171.95 ? 120 GLU A OE2   1 
ATOM   973  N  N     . GLU A 1 124 ? -3.128  -58.026 -2.375  1   153.2  ? 121 GLU A N     1 
ATOM   974  C  CA    . GLU A 1 124 ? -2.575  -59.341 -2.66   1   152.91 ? 121 GLU A CA    1 
ATOM   975  C  C     . GLU A 1 124 ? -3.132  -59.893 -3.982  1   152.2  ? 121 GLU A C     1 
ATOM   976  O  O     . GLU A 1 124 ? -2.412  -60.574 -4.716  1   152.24 ? 121 GLU A O     1 
ATOM   977  C  CB    . GLU A 1 124 ? -2.866  -60.295 -1.504  1   155.26 ? 121 GLU A CB    1 
ATOM   978  C  CG    . GLU A 1 124 ? -2.08   -61.588 -1.593  1   160.63 ? 121 GLU A CG    1 
ATOM   979  C  CD    . GLU A 1 124 ? -2.806  -62.738 -2.264  1   167.84 ? 121 GLU A CD    1 
ATOM   980  O  OE1   . GLU A 1 124 ? -4.031  -62.619 -2.498  1   168.85 ? 121 GLU A OE1   1 
ATOM   981  O  OE2   . GLU A 1 124 ? -2.146  -63.76  -2.564  1   170.74 ? 121 GLU A OE2   1 
ATOM   982  N  N     . LYS A 1 125 ? -4.412  -59.601 -4.282  1   151.37 ? 122 LYS A N     1 
ATOM   983  C  CA    . LYS A 1 125 ? -5.061  -60.031 -5.522  1   150.95 ? 122 LYS A CA    1 
ATOM   984  C  C     . LYS A 1 125 ? -4.379  -59.421 -6.753  1   150.66 ? 122 LYS A C     1 
ATOM   985  O  O     . LYS A 1 125 ? -4.305  -60.065 -7.798  1   150.83 ? 122 LYS A O     1 
ATOM   986  C  CB    . LYS A 1 125 ? -6.563  -59.701 -5.503  1   152.07 ? 122 LYS A CB    1 
ATOM   987  C  CG    . LYS A 1 125 ? -7.325  -60.21  -6.722  1   154.84 ? 122 LYS A CG    1 
ATOM   988  C  CD    . LYS A 1 125 ? -7.272  -61.719 -6.848  1   157.67 ? 122 LYS A CD    1 
ATOM   989  C  CE    . LYS A 1 125 ? -7.557  -62.143 -8.258  1   160.22 ? 122 LYS A CE    1 
ATOM   990  N  NZ    . LYS A 1 125 ? -7.564  -63.611 -8.398  1   161.67 ? 122 LYS A NZ    1 
ATOM   991  N  N     . ILE A 1 126 ? -3.852  -58.198 -6.617  1   150.03 ? 123 ILE A N     1 
ATOM   992  C  CA    . ILE A 1 126 ? -3.124  -57.537 -7.685  1   149.94 ? 123 ILE A CA    1 
ATOM   993  C  C     . ILE A 1 126 ? -1.845  -58.326 -7.997  1   149.75 ? 123 ILE A C     1 
ATOM   994  O  O     . ILE A 1 126 ? -1.566  -58.602 -9.165  1   149.86 ? 123 ILE A O     1 
ATOM   995  C  CB    . ILE A 1 126 ? -2.813  -56.079 -7.277  1   150.41 ? 123 ILE A CB    1 
ATOM   996  C  CG1   . ILE A 1 126 ? -4.105  -55.246 -7.188  1   151.26 ? 123 ILE A CG1   1 
ATOM   997  C  CG2   . ILE A 1 126 ? -1.802  -55.452 -8.233  1   150.98 ? 123 ILE A CG2   1 
ATOM   998  C  CD1   . ILE A 1 126 ? -3.908  -53.799 -6.769  1   152.48 ? 123 ILE A CD1   1 
ATOM   999  N  N     . ARG A 1 127 ? -1.092  -58.713 -6.949  1   149.34 ? 124 ARG A N     1 
ATOM   1000 C  CA    . ARG A 1 127 ? 0.153   -59.473 -7.087  1   149.41 ? 124 ARG A CA    1 
ATOM   1001 C  C     . ARG A 1 127 ? -0.079  -60.818 -7.765  1   149.57 ? 124 ARG A C     1 
ATOM   1002 O  O     . ARG A 1 127 ? 0.691   -61.201 -8.636  1   149.63 ? 124 ARG A O     1 
ATOM   1003 C  CB    . ARG A 1 127 ? 0.82    -59.682 -5.726  1   150.38 ? 124 ARG A CB    1 
ATOM   1004 C  CG    . ARG A 1 127 ? 1.031   -58.405 -4.954  1   152.8  ? 124 ARG A CG    1 
ATOM   1005 C  CD    . ARG A 1 127 ? 2.121   -58.576 -3.932  1   155.48 ? 124 ARG A CD    1 
ATOM   1006 N  NE    . ARG A 1 127 ? 3.388   -58.089 -4.468  1   157.59 ? 124 ARG A NE    1 
ATOM   1007 C  CZ    . ARG A 1 127 ? 3.839   -56.849 -4.311  1   159.16 ? 124 ARG A CZ    1 
ATOM   1008 N  NH1   . ARG A 1 127 ? 3.147   -55.967 -3.598  1   158.44 ? 124 ARG A NH1   1 
ATOM   1009 N  NH2   . ARG A 1 127 ? 4.999   -56.487 -4.842  1   159.1  ? 124 ARG A NH2   1 
ATOM   1010 N  N     . GLU A 1 128 ? -1.161  -61.51  -7.387  1   149.47 ? 125 GLU A N     1 
ATOM   1011 C  CA    . GLU A 1 128 ? -1.572  -62.801 -7.935  1   149.82 ? 125 GLU A CA    1 
ATOM   1012 C  C     . GLU A 1 128 ? -1.916  -62.678 -9.422  1   150.24 ? 125 GLU A C     1 
ATOM   1013 O  O     . GLU A 1 128 ? -1.615  -63.582 -10.194 1   150.42 ? 125 GLU A O     1 
ATOM   1014 C  CB    . GLU A 1 128 ? -2.8    -63.282 -7.162  1   151.62 ? 125 GLU A CB    1 
ATOM   1015 C  CG    . GLU A 1 128 ? -3.199  -64.727 -7.363  1   156.06 ? 125 GLU A CG    1 
ATOM   1016 C  CD    . GLU A 1 128 ? -3.974  -65.197 -6.149  1   162.31 ? 125 GLU A CD    1 
ATOM   1017 O  OE1   . GLU A 1 128 ? -3.53   -64.901 -5.018  1   163.49 ? 125 GLU A OE1   1 
ATOM   1018 O  OE2   . GLU A 1 128 ? -5.038  -65.83  -6.319  1   164.52 ? 125 GLU A OE2   1 
ATOM   1019 N  N     . ALA A 1 129 ? -2.548  -61.558 -9.818  1   150.2  ? 126 ALA A N     1 
ATOM   1020 C  CA    . ALA A 1 129 ? -2.943  -61.295 -11.199 1   150.53 ? 126 ALA A CA    1 
ATOM   1021 C  C     . ALA A 1 129 ? -1.733  -60.977 -12.062 1   150.8  ? 126 ALA A C     1 
ATOM   1022 O  O     . ALA A 1 129 ? -1.646  -61.475 -13.181 1   150.79 ? 126 ALA A O     1 
ATOM   1023 C  CB    . ALA A 1 129 ? -3.937  -60.147 -11.249 1   150.64 ? 126 ALA A CB    1 
ATOM   1024 N  N     . LEU A 1 130 ? -0.792  -60.168 -11.545 1   150.95 ? 127 LEU A N     1 
ATOM   1025 C  CA    . LEU A 1 130 ? 0.419   -59.825 -12.289 1   151.65 ? 127 LEU A CA    1 
ATOM   1026 C  C     . LEU A 1 130 ? 1.353   -61.021 -12.403 1   152.08 ? 127 LEU A C     1 
ATOM   1027 O  O     . LEU A 1 130 ? 2.016   -61.183 -13.426 1   152.24 ? 127 LEU A O     1 
ATOM   1028 C  CB    . LEU A 1 130 ? 1.153   -58.638 -11.658 1   152.07 ? 127 LEU A CB    1 
ATOM   1029 C  CG    . LEU A 1 130 ? 0.525   -57.264 -11.88  1   153.93 ? 127 LEU A CG    1 
ATOM   1030 C  CD1   . LEU A 1 130 ? 1.313   -56.191 -11.161 1   154.68 ? 127 LEU A CD1   1 
ATOM   1031 C  CD2   . LEU A 1 130 ? 0.425   -56.927 -13.363 1   154.64 ? 127 LEU A CD2   1 
ATOM   1032 N  N     . LYS A 1 131 ? 1.413   -61.861 -11.363 1   152.18 ? 128 LYS A N     1 
ATOM   1033 C  CA    . LYS A 1 131 ? 2.238   -63.069 -11.404 1   152.85 ? 128 LYS A CA    1 
ATOM   1034 C  C     . LYS A 1 131 ? 1.668   -64.095 -12.403 1   153.25 ? 128 LYS A C     1 
ATOM   1035 O  O     . LYS A 1 131 ? 2.428   -64.861 -12.996 1   153.48 ? 128 LYS A O     1 
ATOM   1036 C  CB    . LYS A 1 131 ? 2.37    -63.701 -10.005 1   154.69 ? 128 LYS A CB    1 
ATOM   1037 C  CG    . LYS A 1 131 ? 3.346   -62.984 -9.075  1   158.49 ? 128 LYS A CG    1 
ATOM   1038 C  CD    . LYS A 1 131 ? 3.315   -63.584 -7.676  1   162.68 ? 128 LYS A CD    1 
ATOM   1039 C  CE    . LYS A 1 131 ? 3.902   -62.675 -6.624  1   166.48 ? 128 LYS A CE    1 
ATOM   1040 N  NZ    . LYS A 1 131 ? 4.086   -63.391 -5.328  1   168.65 ? 128 LYS A NZ    1 
ATOM   1041 N  N     . LEU A 1 132 ? 0.333   -64.105 -12.584 1   153.15 ? 129 LEU A N     1 
ATOM   1042 C  CA    . LEU A 1 132 ? -0.359  -64.993 -13.514 1   153.41 ? 129 LEU A CA    1 
ATOM   1043 C  C     . LEU A 1 132 ? -0.077  -64.62  -14.967 1   153.31 ? 129 LEU A C     1 
ATOM   1044 O  O     . LEU A 1 132 ? -0.018  -65.502 -15.82  1   153.49 ? 129 LEU A O     1 
ATOM   1045 C  CB    . LEU A 1 132 ? -1.87   -64.949 -13.266 1   153.78 ? 129 LEU A CB    1 
ATOM   1046 C  CG    . LEU A 1 132 ? -2.445  -66.086 -12.445 1   155.32 ? 129 LEU A CG    1 
ATOM   1047 C  CD1   . LEU A 1 132 ? -3.908  -65.851 -12.171 1   155.99 ? 129 LEU A CD1   1 
ATOM   1048 C  CD2   . LEU A 1 132 ? -2.244  -67.413 -13.149 1   155.97 ? 129 LEU A CD2   1 
ATOM   1049 N  N     . VAL A 1 133 ? 0.075   -63.322 -15.257 1   152.83 ? 130 VAL A N     1 
ATOM   1050 C  CA    . VAL A 1 133 ? 0.364   -62.889 -16.622 1   152.96 ? 130 VAL A CA    1 
ATOM   1051 C  C     . VAL A 1 133 ? 1.87    -62.72  -16.89  1   153.12 ? 130 VAL A C     1 
ATOM   1052 O  O     . VAL A 1 133 ? 2.247   -62.054 -17.851 1   153.05 ? 130 VAL A O     1 
ATOM   1053 C  CB    . VAL A 1 133 ? -0.442  -61.637 -16.992 1   153.58 ? 130 VAL A CB    1 
ATOM   1054 C  CG1   . VAL A 1 133 ? -1.93   -61.921 -16.876 1   154.06 ? 130 VAL A CG1   1 
ATOM   1055 C  CG2   . VAL A 1 133 ? -0.056  -60.46  -16.109 1   154.1  ? 130 VAL A CG2   1 
ATOM   1056 N  N     . ASN A 1 134 ? 2.716   -63.355 -16.059 1   153.26 ? 131 ASN A N     1 
ATOM   1057 C  CA    . ASN A 1 134 ? 4.172   -63.378 -16.139 1   153.96 ? 131 ASN A CA    1 
ATOM   1058 C  C     . ASN A 1 134 ? 4.826   -62.004 -16.07  1   154.19 ? 131 ASN A C     1 
ATOM   1059 O  O     . ASN A 1 134 ? 5.831   -61.756 -16.735 1   154.47 ? 131 ASN A O     1 
ATOM   1060 C  CB    . ASN A 1 134 ? 4.653   -64.158 -17.353 1   155.37 ? 131 ASN A CB    1 
ATOM   1061 C  CG    . ASN A 1 134 ? 4.505   -65.637 -17.156 1   158.99 ? 131 ASN A CG    1 
ATOM   1062 O  OD1   . ASN A 1 134 ? 3.639   -66.282 -17.756 1   160.58 ? 131 ASN A OD1   1 
ATOM   1063 N  ND2   . ASN A 1 134 ? 5.335   -66.201 -16.286 1   159.46 ? 131 ASN A ND2   1 
ATOM   1064 N  N     . LEU A 1 135 ? 4.281   -61.125 -15.237 1   153.86 ? 132 LEU A N     1 
ATOM   1065 C  CA    . LEU A 1 135 ? 4.874   -59.813 -15.014 1   153.99 ? 132 LEU A CA    1 
ATOM   1066 C  C     . LEU A 1 135 ? 5.363   -59.765 -13.565 1   154.22 ? 132 LEU A C     1 
ATOM   1067 O  O     . LEU A 1 135 ? 4.687   -60.281 -12.676 1   154.32 ? 132 LEU A O     1 
ATOM   1068 C  CB    . LEU A 1 135 ? 3.869   -58.682 -15.282 1   153.94 ? 132 LEU A CB    1 
ATOM   1069 C  CG    . LEU A 1 135 ? 3.449   -58.453 -16.731 1   154.98 ? 132 LEU A CG    1 
ATOM   1070 C  CD1   . LEU A 1 135 ? 2.485   -57.296 -16.827 1   155.49 ? 132 LEU A CD1   1 
ATOM   1071 C  CD2   . LEU A 1 135 ? 4.643   -58.18  -17.615 1   155.47 ? 132 LEU A CD2   1 
ATOM   1072 N  N     . ASP A 1 136 ? 6.544   -59.19  -13.329 1   154.08 ? 133 ASP A N     1 
ATOM   1073 C  CA    . ASP A 1 136 ? 7.081   -59.084 -11.978 1   154.47 ? 133 ASP A CA    1 
ATOM   1074 C  C     . ASP A 1 136 ? 6.31    -57.971 -11.279 1   154.46 ? 133 ASP A C     1 
ATOM   1075 O  O     . ASP A 1 136 ? 6.402   -56.824 -11.704 1   154.51 ? 133 ASP A O     1 
ATOM   1076 C  CB    . ASP A 1 136 ? 8.576   -58.748 -12.042 1   156.45 ? 133 ASP A CB    1 
ATOM   1077 C  CG    . ASP A 1 136 ? 9.324   -58.87  -10.728 1   161.67 ? 133 ASP A CG    1 
ATOM   1078 O  OD1   . ASP A 1 136 ? 8.69    -59.225 -9.709  1   162.34 ? 133 ASP A OD1   1 
ATOM   1079 O  OD2   . ASP A 1 136 ? 10.546  -58.619 -10.72  1   164.42 ? 133 ASP A OD2   1 
ATOM   1080 N  N     . PRO A 1 137 ? 5.516   -58.279 -10.233 1   154.3  ? 134 PRO A N     1 
ATOM   1081 C  CA    . PRO A 1 137 ? 4.727   -57.221 -9.58   1   154.09 ? 134 PRO A CA    1 
ATOM   1082 C  C     . PRO A 1 137 ? 5.528   -56.007 -9.126  1   153.71 ? 134 PRO A C     1 
ATOM   1083 O  O     . PRO A 1 137 ? 5.123   -54.888 -9.399  1   153.78 ? 134 PRO A O     1 
ATOM   1084 C  CB    . PRO A 1 137 ? 4.056   -57.943 -8.405  1   154.94 ? 134 PRO A CB    1 
ATOM   1085 C  CG    . PRO A 1 137 ? 4.022   -59.369 -8.801  1   155.47 ? 134 PRO A CG    1 
ATOM   1086 C  CD    . PRO A 1 137 ? 5.276   -59.594 -9.607  1   153.9  ? 134 PRO A CD    1 
ATOM   1087 N  N     . ASP A 1 138 ? 6.684   -56.219 -8.5    1   153.14 ? 135 ASP A N     1 
ATOM   1088 C  CA    . ASP A 1 138 ? 7.521   -55.123 -8.017  1   153.15 ? 135 ASP A CA    1 
ATOM   1089 C  C     . ASP A 1 138 ? 8.108   -54.258 -9.147  1   152.88 ? 135 ASP A C     1 
ATOM   1090 O  O     . ASP A 1 138 ? 8.395   -53.086 -8.931  1   153.17 ? 135 ASP A O     1 
ATOM   1091 C  CB    . ASP A 1 138 ? 8.627   -55.61  -7.051  1   154.73 ? 135 ASP A CB    1 
ATOM   1092 C  CG    . ASP A 1 138 ? 8.863   -57.11  -6.983  1   158.76 ? 135 ASP A CG    1 
ATOM   1093 O  OD1   . ASP A 1 138 ? 7.924   -57.844 -6.606  1   159.05 ? 135 ASP A OD1   1 
ATOM   1094 O  OD2   . ASP A 1 138 ? 9.988   -57.547 -7.297  1   161.07 ? 135 ASP A OD2   1 
ATOM   1095 N  N     . LYS A 1 139 ? 8.255   -54.818 -10.345 1   152.19 ? 136 LYS A N     1 
ATOM   1096 C  CA    . LYS A 1 139 ? 8.782   -54.087 -11.495 1   152.05 ? 136 LYS A CA    1 
ATOM   1097 C  C     . LYS A 1 139 ? 7.684   -53.261 -12.222 1   151.44 ? 136 LYS A C     1 
ATOM   1098 O  O     . LYS A 1 139 ? 8.008   -52.3   -12.924 1   151.51 ? 136 LYS A O     1 
ATOM   1099 C  CB    . LYS A 1 139 ? 9.513   -55.085 -12.43  1   154.14 ? 136 LYS A CB    1 
ATOM   1100 C  CG    . LYS A 1 139 ? 9.61    -54.727 -13.915 1   158.57 ? 136 LYS A CG    1 
ATOM   1101 C  CD    . LYS A 1 139 ? 10.698  -53.705 -14.229 1   163.01 ? 136 LYS A CD    1 
ATOM   1102 C  CE    . LYS A 1 139 ? 10.4    -52.941 -15.5   1   166.28 ? 136 LYS A CE    1 
ATOM   1103 N  NZ    . LYS A 1 139 ? 10.184  -53.838 -16.665 1   167.97 ? 136 LYS A NZ    1 
ATOM   1104 N  N     . TYR A 1 140 ? 6.395   -53.587 -12.008 1   150.75 ? 137 TYR A N     1 
ATOM   1105 C  CA    . TYR A 1 140 ? 5.319   -52.894 -12.711 1   150.61 ? 137 TYR A CA    1 
ATOM   1106 C  C     . TYR A 1 140 ? 4.317   -52.11  -11.862 1   149.69 ? 137 TYR A C     1 
ATOM   1107 O  O     . TYR A 1 140 ? 3.691   -51.209 -12.403 1   149.78 ? 137 TYR A O     1 
ATOM   1108 C  CB    . TYR A 1 140 ? 4.559   -53.88  -13.591 1   151.11 ? 137 TYR A CB    1 
ATOM   1109 C  CG    . TYR A 1 140 ? 5.4     -54.387 -14.739 1   152.51 ? 137 TYR A CG    1 
ATOM   1110 C  CD1   . TYR A 1 140 ? 5.527   -53.655 -15.909 1   153.72 ? 137 TYR A CD1   1 
ATOM   1111 C  CD2   . TYR A 1 140 ? 6.086   -55.589 -14.646 1   153.63 ? 137 TYR A CD2   1 
ATOM   1112 C  CE1   . TYR A 1 140 ? 6.304   -54.112 -16.963 1   154.8  ? 137 TYR A CE1   1 
ATOM   1113 C  CE2   . TYR A 1 140 ? 6.865   -56.057 -15.693 1   154.7  ? 137 TYR A CE2   1 
ATOM   1114 C  CZ    . TYR A 1 140 ? 6.976   -55.314 -16.85  1   155.82 ? 137 TYR A CZ    1 
ATOM   1115 O  OH    . TYR A 1 140 ? 7.75    -55.774 -17.886 1   157.7  ? 137 TYR A OH    1 
ATOM   1116 N  N     . LEU A 1 141 ? 4.148   -52.424 -10.571 1   148.68 ? 138 LEU A N     1 
ATOM   1117 C  CA    . LEU A 1 141 ? 3.169   -51.744 -9.706  1   148.12 ? 138 LEU A CA    1 
ATOM   1118 C  C     . LEU A 1 141 ? 3.179   -50.211 -9.733  1   146.99 ? 138 LEU A C     1 
ATOM   1119 O  O     . LEU A 1 141 ? 2.114   -49.598 -9.658  1   146.99 ? 138 LEU A O     1 
ATOM   1120 C  CB    . LEU A 1 141 ? 3.307   -52.212 -8.258  1   148.53 ? 138 LEU A CB    1 
ATOM   1121 C  CG    . LEU A 1 141 ? 2.686   -53.557 -7.95   1   150.2  ? 138 LEU A CG    1 
ATOM   1122 C  CD1   . LEU A 1 141 ? 3.088   -54.028 -6.576  1   150.9  ? 138 LEU A CD1   1 
ATOM   1123 C  CD2   . LEU A 1 141 ? 1.193   -53.521 -8.117  1   150.85 ? 138 LEU A CD2   1 
ATOM   1124 N  N     . ASP A 1 142 ? 4.364   -49.594 -9.797  1   145.9  ? 139 ASP A N     1 
ATOM   1125 C  CA    . ASP A 1 142 ? 4.452   -48.137 -9.814  1   145.36 ? 139 ASP A CA    1 
ATOM   1126 C  C     . ASP A 1 142 ? 4.697   -47.557 -11.226 1   144.73 ? 139 ASP A C     1 
ATOM   1127 O  O     . ASP A 1 142 ? 5.026   -46.384 -11.348 1   144.76 ? 139 ASP A O     1 
ATOM   1128 C  CB    . ASP A 1 142 ? 5.48    -47.628 -8.787  1   146.63 ? 139 ASP A CB    1 
ATOM   1129 C  CG    . ASP A 1 142 ? 5.035   -47.785 -7.337  1   150.2  ? 139 ASP A CG    1 
ATOM   1130 O  OD1   . ASP A 1 142 ? 4.696   -48.918 -6.938  1   150.74 ? 139 ASP A OD1   1 
ATOM   1131 O  OD2   . ASP A 1 142 ? 5.038   -46.775 -6.599  1   151.96 ? 139 ASP A OD2   1 
ATOM   1132 N  N     . ARG A 1 143 ? 4.503   -48.365 -12.285 1   144.06 ? 140 ARG A N     1 
ATOM   1133 C  CA    . ARG A 1 143 ? 4.625   -47.929 -13.681 1   143.85 ? 140 ARG A CA    1 
ATOM   1134 C  C     . ARG A 1 143 ? 3.27    -47.393 -14.143 1   143.37 ? 140 ARG A C     1 
ATOM   1135 O  O     . ARG A 1 143 ? 2.236   -47.859 -13.67  1   143.66 ? 140 ARG A O     1 
ATOM   1136 C  CB    . ARG A 1 143 ? 5.008   -49.107 -14.594 1   145.02 ? 140 ARG A CB    1 
ATOM   1137 C  CG    . ARG A 1 143 ? 6.431   -49.607 -14.422 1   147.7  ? 140 ARG A CG    1 
ATOM   1138 C  CD    . ARG A 1 143 ? 7.44    -48.713 -15.117 1   150.38 ? 140 ARG A CD    1 
ATOM   1139 N  NE    . ARG A 1 143 ? 7.205   -48.611 -16.559 1   152.74 ? 140 ARG A NE    1 
ATOM   1140 C  CZ    . ARG A 1 143 ? 7.636   -49.492 -17.456 1   154.68 ? 140 ARG A CZ    1 
ATOM   1141 N  NH1   . ARG A 1 143 ? 8.315   -50.564 -17.071 1   154.24 ? 140 ARG A NH1   1 
ATOM   1142 N  NH2   . ARG A 1 143 ? 7.388   -49.31  -18.744 1   154.64 ? 140 ARG A NH2   1 
ATOM   1143 N  N     . TYR A 1 144 ? 3.262   -46.442 -15.08  1   142.5  ? 141 TYR A N     1 
ATOM   1144 C  CA    . TYR A 1 144 ? 2.008   -45.896 -15.599 1   142.08 ? 141 TYR A CA    1 
ATOM   1145 C  C     . TYR A 1 144 ? 1.493   -46.739 -16.762 1   142.55 ? 141 TYR A C     1 
ATOM   1146 O  O     . TYR A 1 144 ? 2.299   -47.25  -17.534 1   142.74 ? 141 TYR A O     1 
ATOM   1147 C  CB    . TYR A 1 144 ? 2.198   -44.436 -16.02  1   141.34 ? 141 TYR A CB    1 
ATOM   1148 C  CG    . TYR A 1 144 ? 2.502   -43.545 -14.841 1   141.09 ? 141 TYR A CG    1 
ATOM   1149 C  CD1   . TYR A 1 144 ? 1.508   -43.184 -13.948 1   141.62 ? 141 TYR A CD1   1 
ATOM   1150 C  CD2   . TYR A 1 144 ? 3.797   -43.135 -14.569 1   141.48 ? 141 TYR A CD2   1 
ATOM   1151 C  CE1   . TYR A 1 144 ? 1.777   -42.372 -12.856 1   142.21 ? 141 TYR A CE1   1 
ATOM   1152 C  CE2   . TYR A 1 144 ? 4.085   -42.346 -13.462 1   142.12 ? 141 TYR A CE2   1 
ATOM   1153 C  CZ    . TYR A 1 144 ? 3.07    -41.963 -12.608 1   142.85 ? 141 TYR A CZ    1 
ATOM   1154 O  OH    . TYR A 1 144 ? 3.33    -41.176 -11.514 1   143.98 ? 141 TYR A OH    1 
ATOM   1155 N  N     . VAL A 1 145 ? 0.16    -46.889 -16.905 1   142.56 ? 142 VAL A N     1 
ATOM   1156 C  CA    . VAL A 1 145 ? -0.407  -47.65  -18.026 1   142.98 ? 142 VAL A CA    1 
ATOM   1157 C  C     . VAL A 1 145 ? -0.524  -46.738 -19.242 1   143.38 ? 142 VAL A C     1 
ATOM   1158 O  O     . VAL A 1 145 ? -1.555  -46.691 -19.905 1   143.48 ? 142 VAL A O     1 
ATOM   1159 C  CB    . VAL A 1 145 ? -1.732  -48.382 -17.699 1   143.54 ? 142 VAL A CB    1 
ATOM   1160 C  CG1   . VAL A 1 145 ? -1.487  -49.579 -16.791 1   143.92 ? 142 VAL A CG1   1 
ATOM   1161 C  CG2   . VAL A 1 145 ? -2.758  -47.437 -17.087 1   144.16 ? 142 VAL A CG2   1 
ATOM   1162 N  N     . ASP A 1 146 ? 0.559   -46.011 -19.522 1   143.49 ? 143 ASP A N     1 
ATOM   1163 C  CA    . ASP A 1 146 ? 0.664   -45.04  -20.599 1   144.01 ? 143 ASP A CA    1 
ATOM   1164 C  C     . ASP A 1 146 ? 1.433   -45.603 -21.82  1   144.35 ? 143 ASP A C     1 
ATOM   1165 O  O     . ASP A 1 146 ? 1.724   -46.8   -21.874 1   144.33 ? 143 ASP A O     1 
ATOM   1166 C  CB    . ASP A 1 146 ? 1.293   -43.734 -20.046 1   145.37 ? 143 ASP A CB    1 
ATOM   1167 C  CG    . ASP A 1 146 ? 2.671   -43.893 -19.426 1   148.98 ? 143 ASP A CG    1 
ATOM   1168 O  OD1   . ASP A 1 146 ? 3.161   -45.037 -19.347 1   149.02 ? 143 ASP A OD1   1 
ATOM   1169 O  OD2   . ASP A 1 146 ? 3.246   -42.875 -18.999 1   151.41 ? 143 ASP A OD2   1 
ATOM   1170 N  N     . GLU A 1 147 ? 1.746   -44.738 -22.793 1   144.46 ? 144 GLU A N     1 
ATOM   1171 C  CA    . GLU A 1 147 ? 2.483   -45.059 -24.009 1   145.07 ? 144 GLU A CA    1 
ATOM   1172 C  C     . GLU A 1 147 ? 3.874   -45.672 -23.741 1   145.13 ? 144 GLU A C     1 
ATOM   1173 O  O     . GLU A 1 147 ? 4.422   -46.358 -24.604 1   145.18 ? 144 GLU A O     1 
ATOM   1174 C  CB    . GLU A 1 147 ? 2.611   -43.786 -24.873 1   147.67 ? 144 GLU A CB    1 
ATOM   1175 C  CG    . GLU A 1 147 ? 3.294   -42.613 -24.176 1   152.88 ? 144 GLU A CG    1 
ATOM   1176 C  CD    . GLU A 1 147 ? 2.422   -41.596 -23.457 1   159.27 ? 144 GLU A CD    1 
ATOM   1177 O  OE1   . GLU A 1 147 ? 2.854   -40.424 -23.345 1   160.61 ? 144 GLU A OE1   1 
ATOM   1178 O  OE2   . GLU A 1 147 ? 1.315   -41.966 -23.002 1   161.01 ? 144 GLU A OE2   1 
ATOM   1179 N  N     . THR A 1 148 ? 4.426   -45.428 -22.541 1   145.02 ? 145 THR A N     1 
ATOM   1180 C  CA    . THR A 1 148 ? 5.738   -45.871 -22.085 1   145.44 ? 145 THR A CA    1 
ATOM   1181 C  C     . THR A 1 148 ? 5.834   -47.409 -22.075 1   145.18 ? 145 THR A C     1 
ATOM   1182 O  O     . THR A 1 148 ? 6.892   -47.953 -22.397 1   145.47 ? 145 THR A O     1 
ATOM   1183 C  CB    . THR A 1 148 ? 6.056   -45.164 -20.741 1   147.09 ? 145 THR A CB    1 
ATOM   1184 O  OG1   . THR A 1 148 ? 7.005   -44.117 -20.972 1   148.04 ? 145 THR A OG1   1 
ATOM   1185 C  CG2   . THR A 1 148 ? 6.524   -46.104 -19.62  1   147.65 ? 145 THR A CG2   1 
ATOM   1186 N  N     . LEU A 1 149 ? 4.734   -48.102 -21.759 1   144.41 ? 146 LEU A N     1 
ATOM   1187 C  CA    . LEU A 1 149 ? 4.725   -49.561 -21.76  1   144.04 ? 146 LEU A CA    1 
ATOM   1188 C  C     . LEU A 1 149 ? 4.781   -50.121 -23.174 1   143.45 ? 146 LEU A C     1 
ATOM   1189 O  O     . LEU A 1 149 ? 4.385   -49.443 -24.125 1   143.86 ? 146 LEU A O     1 
ATOM   1190 C  CB    . LEU A 1 149 ? 3.429   -50.053 -21.139 1   144.31 ? 146 LEU A CB    1 
ATOM   1191 C  CG    . LEU A 1 149 ? 3.297   -49.903 -19.663 1   146.22 ? 146 LEU A CG    1 
ATOM   1192 C  CD1   . LEU A 1 149 ? 1.913   -50.279 -19.249 1   147.15 ? 146 LEU A CD1   1 
ATOM   1193 C  CD2   . LEU A 1 149 ? 4.302   -50.771 -18.939 1   146.86 ? 146 LEU A CD2   1 
ATOM   1194 N  N     . SER A 1 150 ? 5.228   -51.374 -23.315 1   142.28 ? 147 SER A N     1 
ATOM   1195 C  CA    . SER A 1 150 ? 5.196   -52.039 -24.611 1   141.64 ? 147 SER A CA    1 
ATOM   1196 C  C     . SER A 1 150 ? 3.759   -52.57  -24.815 1   140.42 ? 147 SER A C     1 
ATOM   1197 O  O     . SER A 1 150 ? 2.982   -52.656 -23.858 1   140.44 ? 147 SER A O     1 
ATOM   1198 C  CB    . SER A 1 150 ? 6.209   -53.182 -24.661 1   143.12 ? 147 SER A CB    1 
ATOM   1199 O  OG    . SER A 1 150 ? 5.767   -54.34  -23.97  1   145.54 ? 147 SER A OG    1 
ATOM   1200 N  N     . GLY A 1 151 ? 3.423   -52.944 -26.044 1   139.19 ? 148 GLY A N     1 
ATOM   1201 C  CA    . GLY A 1 151 ? 2.11    -53.505 -26.342 1   138.38 ? 148 GLY A CA    1 
ATOM   1202 C  C     . GLY A 1 151 ? 1.84    -54.789 -25.579 1   137.14 ? 148 GLY A C     1 
ATOM   1203 O  O     . GLY A 1 151 ? 0.709   -55.044 -25.165 1   137.09 ? 148 GLY A O     1 
ATOM   1204 N  N     . GLY A 1 152 ? 2.896   -55.572 -25.368 1   136.08 ? 149 GLY A N     1 
ATOM   1205 C  CA    . GLY A 1 152 ? 2.839   -56.824 -24.629 1   135.57 ? 149 GLY A CA    1 
ATOM   1206 C  C     . GLY A 1 152 ? 2.625   -56.609 -23.15  1   134.62 ? 149 GLY A C     1 
ATOM   1207 O  O     . GLY A 1 152 ? 1.85    -57.332 -22.527 1   134.51 ? 149 GLY A O     1 
ATOM   1208 N  N     . GLU A 1 153 ? 3.302   -55.601 -22.583 1   133.75 ? 150 GLU A N     1 
ATOM   1209 C  CA    . GLU A 1 153 ? 3.162   -55.256 -21.174 1   133.32 ? 150 GLU A CA    1 
ATOM   1210 C  C     . GLU A 1 153 ? 1.752   -54.722 -20.918 1   132.43 ? 150 GLU A C     1 
ATOM   1211 O  O     . GLU A 1 153 ? 1.097   -55.198 -20     1   132.66 ? 150 GLU A O     1 
ATOM   1212 C  CB    . GLU A 1 153 ? 4.214   -54.214 -20.744 1   135.63 ? 150 GLU A CB    1 
ATOM   1213 C  CG    . GLU A 1 153 ? 5.641   -54.729 -20.691 1   140.39 ? 150 GLU A CG    1 
ATOM   1214 C  CD    . GLU A 1 153 ? 6.677   -53.629 -20.542 1   147.12 ? 150 GLU A CD    1 
ATOM   1215 O  OE1   . GLU A 1 153 ? 6.424   -52.505 -21.032 1   148.22 ? 150 GLU A OE1   1 
ATOM   1216 O  OE2   . GLU A 1 153 ? 7.746   -53.888 -19.944 1   149.74 ? 150 GLU A OE2   1 
ATOM   1217 N  N     . ARG A 1 154 ? 1.267   -53.775 -21.749 1   131.27 ? 151 ARG A N     1 
ATOM   1218 C  CA    . ARG A 1 154 ? -0.066  -53.184 -21.602 1   130.57 ? 151 ARG A CA    1 
ATOM   1219 C  C     . ARG A 1 154 ? -1.185  -54.21  -21.793 1   130.1  ? 151 ARG A C     1 
ATOM   1220 O  O     . ARG A 1 154 ? -2.17   -54.156 -21.059 1   130.37 ? 151 ARG A O     1 
ATOM   1221 C  CB    . ARG A 1 154 ? -0.246  -51.977 -22.533 1   131.21 ? 151 ARG A CB    1 
ATOM   1222 C  CG    . ARG A 1 154 ? -1.624  -51.318 -22.463 1   132.95 ? 151 ARG A CG    1 
ATOM   1223 C  CD    . ARG A 1 154 ? -1.878  -50.592 -21.154 1   134.71 ? 151 ARG A CD    1 
ATOM   1224 N  NE    . ARG A 1 154 ? -3.252  -50.092 -21.074 1   136.24 ? 151 ARG A NE    1 
ATOM   1225 C  CZ    . ARG A 1 154 ? -4.283  -50.811 -20.647 1   137.81 ? 151 ARG A CZ    1 
ATOM   1226 N  NH1   . ARG A 1 154 ? -4.111  -52.07  -20.267 1   137.71 ? 151 ARG A NH1   1 
ATOM   1227 N  NH2   . ARG A 1 154 ? -5.498  -50.281 -20.612 1   137.5  ? 151 ARG A NH2   1 
ATOM   1228 N  N     . LYS A 1 155 ? -1.033  -55.163 -22.737 1   129.26 ? 152 LYS A N     1 
ATOM   1229 C  CA    . LYS A 1 155 ? -2.058  -56.195 -22.92  1   128.95 ? 152 LYS A CA    1 
ATOM   1230 C  C     . LYS A 1 155 ? -2.021  -57.2   -21.77  1   128.38 ? 152 LYS A C     1 
ATOM   1231 O  O     . LYS A 1 155 ? -3.081  -57.661 -21.35  1   128.43 ? 152 LYS A O     1 
ATOM   1232 C  CB    . LYS A 1 155 ? -1.968  -56.884 -24.296 1   130.74 ? 152 LYS A CB    1 
ATOM   1233 C  CG    . LYS A 1 155 ? -3.069  -57.927 -24.565 1   134.42 ? 152 LYS A CG    1 
ATOM   1234 C  CD    . LYS A 1 155 ? -4.409  -57.334 -24.998 1   138.05 ? 152 LYS A CD    1 
ATOM   1235 C  CE    . LYS A 1 155 ? -5.472  -58.385 -25.214 1   140.83 ? 152 LYS A CE    1 
ATOM   1236 N  NZ    . LYS A 1 155 ? -6.793  -57.771 -25.506 1   142.36 ? 152 LYS A NZ    1 
ATOM   1237 N  N     . ARG A 1 156 ? -0.827  -57.476 -21.199 1   127.76 ? 153 ARG A N     1 
ATOM   1238 C  CA    . ARG A 1 156 ? -0.72   -58.368 -20.039 1   127.7  ? 153 ARG A CA    1 
ATOM   1239 C  C     . ARG A 1 156 ? -1.355  -57.707 -18.805 1   126.88 ? 153 ARG A C     1 
ATOM   1240 O  O     . ARG A 1 156 ? -2.071  -58.37  -18.058 1   127.07 ? 153 ARG A O     1 
ATOM   1241 C  CB    . ARG A 1 156 ? 0.732   -58.827 -19.783 1   129.35 ? 153 ARG A CB    1 
ATOM   1242 C  CG    . ARG A 1 156 ? 1.194   -59.941 -20.731 1   132.46 ? 153 ARG A CG    1 
ATOM   1243 C  CD    . ARG A 1 156 ? 2.69    -60.183 -20.652 1   135.39 ? 153 ARG A CD    1 
ATOM   1244 N  NE    . ARG A 1 156 ? 3.155   -61.102 -21.693 1   137.99 ? 153 ARG A NE    1 
ATOM   1245 C  CZ    . ARG A 1 156 ? 3.249   -62.42  -21.546 1   140.11 ? 153 ARG A CZ    1 
ATOM   1246 N  NH1   . ARG A 1 156 ? 2.908   -62.993 -20.398 1   139.41 ? 153 ARG A NH1   1 
ATOM   1247 N  NH2   . ARG A 1 156 ? 3.685   -63.176 -22.546 1   140.41 ? 153 ARG A NH2   1 
ATOM   1248 N  N     . ILE A 1 157 ? -1.181  -56.388 -18.647 1   125.85 ? 154 ILE A N     1 
ATOM   1249 C  CA    . ILE A 1 157 ? -1.824  -55.637 -17.566 1   125.42 ? 154 ILE A CA    1 
ATOM   1250 C  C     . ILE A 1 157 ? -3.36   -55.637 -17.758 1   125    ? 154 ILE A C     1 
ATOM   1251 O  O     . ILE A 1 157 ? -4.098  -55.703 -16.777 1   125.26 ? 154 ILE A O     1 
ATOM   1252 C  CB    . ILE A 1 157 ? -1.215  -54.217 -17.441 1   125.74 ? 154 ILE A CB    1 
ATOM   1253 C  CG1   . ILE A 1 157 ? 0.216   -54.293 -16.896 1   126.49 ? 154 ILE A CG1   1 
ATOM   1254 C  CG2   . ILE A 1 157 ? -2.071  -53.29  -16.578 1   126.16 ? 154 ILE A CG2   1 
ATOM   1255 C  CD1   . ILE A 1 157 ? 1.017   -53.111 -17.192 1   127.61 ? 154 ILE A CD1   1 
ATOM   1256 N  N     . GLU A 1 158 ? -3.839  -55.656 -19.013 1   124.26 ? 155 GLU A N     1 
ATOM   1257 C  CA    . GLU A 1 158 ? -5.267  -55.748 -19.289 1   124.14 ? 155 GLU A CA    1 
ATOM   1258 C  C     . GLU A 1 158 ? -5.799  -57.126 -18.904 1   124.03 ? 155 GLU A C     1 
ATOM   1259 O  O     . GLU A 1 158 ? -6.906  -57.224 -18.388 1   124.16 ? 155 GLU A O     1 
ATOM   1260 C  CB    . GLU A 1 158 ? -5.578  -55.418 -20.752 1   126.02 ? 155 GLU A CB    1 
ATOM   1261 C  CG    . GLU A 1 158 ? -7.037  -55.059 -20.985 1   130.35 ? 155 GLU A CG    1 
ATOM   1262 C  CD    . GLU A 1 158 ? -7.541  -53.771 -20.352 1   135.37 ? 155 GLU A CD    1 
ATOM   1263 O  OE1   . GLU A 1 158 ? -6.786  -53.149 -19.571 1   136.24 ? 155 GLU A OE1   1 
ATOM   1264 O  OE2   . GLU A 1 158 ? -8.694  -53.376 -20.641 1   136.81 ? 155 GLU A OE2   1 
ATOM   1265 N  N     . LEU A 1 159 ? -4.993  -58.181 -19.093 1   123.7  ? 156 LEU A N     1 
ATOM   1266 C  CA    . LEU A 1 159 ? -5.332  -59.544 -18.687 1   123.87 ? 156 LEU A CA    1 
ATOM   1267 C  C     . LEU A 1 159 ? -5.375  -59.637 -17.162 1   123.96 ? 156 LEU A C     1 
ATOM   1268 O  O     . LEU A 1 159 ? -6.254  -60.301 -16.621 1   123.99 ? 156 LEU A O     1 
ATOM   1269 C  CB    . LEU A 1 159 ? -4.305  -60.54  -19.236 1   124.05 ? 156 LEU A CB    1 
ATOM   1270 C  CG    . LEU A 1 159 ? -4.795  -61.479 -20.311 1   125.47 ? 156 LEU A CG    1 
ATOM   1271 C  CD1   . LEU A 1 159 ? -5.875  -62.388 -19.775 1   125.94 ? 156 LEU A CD1   1 
ATOM   1272 C  CD2   . LEU A 1 159 ? -5.254  -60.708 -21.542 1   126.25 ? 156 LEU A CD2   1 
ATOM   1273 N  N     . ALA A 1 160 ? -4.447  -58.95  -16.47  1   123.85 ? 157 ALA A N     1 
ATOM   1274 C  CA    . ALA A 1 160 ? -4.423  -58.898 -15.01  1   124.27 ? 157 ALA A CA    1 
ATOM   1275 C  C     . ALA A 1 160 ? -5.639  -58.124 -14.477 1   124.53 ? 157 ALA A C     1 
ATOM   1276 O  O     . ALA A 1 160 ? -6.164  -58.472 -13.422 1   124.83 ? 157 ALA A O     1 
ATOM   1277 C  CB    . ALA A 1 160 ? -3.135  -58.256 -14.524 1   124.43 ? 157 ALA A CB    1 
ATOM   1278 N  N     . SER A 1 161 ? -6.115  -57.113 -15.222 1   124.36 ? 158 SER A N     1 
ATOM   1279 C  CA    . SER A 1 161 ? -7.294  -56.336 -14.858 1   124.79 ? 158 SER A CA    1 
ATOM   1280 C  C     . SER A 1 161 ? -8.521  -57.24  -14.884 1   125.02 ? 158 SER A C     1 
ATOM   1281 O  O     . SER A 1 161 ? -9.301  -57.226 -13.94  1   125.19 ? 158 SER A O     1 
ATOM   1282 C  CB    . SER A 1 161 ? -7.468  -55.152 -15.804 1   126.14 ? 158 SER A CB    1 
ATOM   1283 O  OG    . SER A 1 161 ? -8.661  -54.438 -15.53  1   128.51 ? 158 SER A OG    1 
ATOM   1284 N  N     . ILE A 1 162 ? -8.643  -58.092 -15.918 1   124.85 ? 159 ILE A N     1 
ATOM   1285 C  CA    . ILE A 1 162 ? -9.719  -59.074 -16.052 1   125.22 ? 159 ILE A CA    1 
ATOM   1286 C  C     . ILE A 1 162 ? -9.719  -60.009 -14.839 1   125.74 ? 159 ILE A C     1 
ATOM   1287 O  O     . ILE A 1 162 ? -10.779 -60.338 -14.32  1   125.87 ? 159 ILE A O     1 
ATOM   1288 C  CB    . ILE A 1 162 ? -9.525  -59.875 -17.364 1   125.64 ? 159 ILE A CB    1 
ATOM   1289 C  CG1   . ILE A 1 162 ? -9.649  -58.982 -18.617 1   126.42 ? 159 ILE A CG1   1 
ATOM   1290 C  CG2   . ILE A 1 162 ? -10.451 -61.092 -17.434 1   126.17 ? 159 ILE A CG2   1 
ATOM   1291 C  CD1   . ILE A 1 162 ? -10.987 -58.417 -18.875 1   127.65 ? 159 ILE A CD1   1 
ATOM   1292 N  N     . ILE A 1 163 ? -8.525  -60.406 -14.374 1   126.07 ? 160 ILE A N     1 
ATOM   1293 C  CA    . ILE A 1 163 ? -8.347  -61.286 -13.219 1   127.04 ? 160 ILE A CA    1 
ATOM   1294 C  C     . ILE A 1 163 ? -8.841  -60.621 -11.938 1   127.73 ? 160 ILE A C     1 
ATOM   1295 O  O     . ILE A 1 163 ? -9.593  -61.233 -11.181 1   127.96 ? 160 ILE A O     1 
ATOM   1296 C  CB    . ILE A 1 163 ? -6.877  -61.779 -13.107 1   127.62 ? 160 ILE A CB    1 
ATOM   1297 C  CG1   . ILE A 1 163 ? -6.501  -62.663 -14.298 1   128.67 ? 160 ILE A CG1   1 
ATOM   1298 C  CG2   . ILE A 1 163 ? -6.64   -62.534 -11.812 1   128.07 ? 160 ILE A CG2   1 
ATOM   1299 C  CD1   . ILE A 1 163 ? -5.029  -62.925 -14.414 1   129.94 ? 160 ILE A CD1   1 
ATOM   1300 N  N     . CYS A 1 164 ? -8.462  -59.361 -11.717 1   128.03 ? 161 CYS A N     1 
ATOM   1301 C  CA    . CYS A 1 164 ? -8.895  -58.612 -10.54  1   128.99 ? 161 CYS A CA    1 
ATOM   1302 C  C     . CYS A 1 164 ? -10.391 -58.322 -10.569 1   129.39 ? 161 CYS A C     1 
ATOM   1303 O  O     . CYS A 1 164 ? -11.039 -58.317 -9.526  1   129.66 ? 161 CYS A O     1 
ATOM   1304 C  CB    . CYS A 1 164 ? -8.086  -57.329 -10.387 1   130.26 ? 161 CYS A CB    1 
ATOM   1305 S  SG    . CYS A 1 164 ? -6.316  -57.602 -10.117 1   134.94 ? 161 CYS A SG    1 
ATOM   1306 N  N     . MET A 1 165 ? -10.936 -58.073 -11.759 1   129.28 ? 162 MET A N     1 
ATOM   1307 C  CA    . MET A 1 165 ? -12.355 -57.795 -11.934 1   129.51 ? 162 MET A CA    1 
ATOM   1308 C  C     . MET A 1 165 ? -13.198 -59.05  -11.705 1   129.77 ? 162 MET A C     1 
ATOM   1309 O  O     . MET A 1 165 ? -14.316 -58.955 -11.196 1   129.82 ? 162 MET A O     1 
ATOM   1310 C  CB    . MET A 1 165 ? -12.622 -57.284 -13.357 1   129.62 ? 162 MET A CB    1 
ATOM   1311 C  CG    . MET A 1 165 ? -12.27  -55.854 -13.573 1   130.58 ? 162 MET A CG    1 
ATOM   1312 S  SD    . MET A 1 165 ? -13.018 -55.315 -15.123 1   131.43 ? 162 MET A SD    1 
ATOM   1313 C  CE    . MET A 1 165 ? -14.723 -55.203 -14.631 1   128.42 ? 162 MET A CE    1 
ATOM   1314 N  N     . GLU A 1 166 ? -12.689 -60.221 -12.147 1   129.73 ? 163 GLU A N     1 
ATOM   1315 C  CA    . GLU A 1 166 ? -13.377 -61.519 -12.091 1   130.14 ? 163 GLU A CA    1 
ATOM   1316 C  C     . GLU A 1 166 ? -14.848 -61.4   -12.535 1   130.03 ? 163 GLU A C     1 
ATOM   1317 O  O     . GLU A 1 166 ? -15.755 -61.534 -11.714 1   130.17 ? 163 GLU A O     1 
ATOM   1318 C  CB    . GLU A 1 166 ? -13.264 -62.128 -10.692 1   132.64 ? 163 GLU A CB    1 
ATOM   1319 C  CG    . GLU A 1 166 ? -13.519 -63.617 -10.677 1   138.16 ? 163 GLU A CG    1 
ATOM   1320 C  CD    . GLU A 1 166 ? -13.613 -64.187 -9.284  1   145.73 ? 163 GLU A CD    1 
ATOM   1321 O  OE1   . GLU A 1 166 ? -12.557 -64.264 -8.618  1   147.86 ? 163 GLU A OE1   1 
ATOM   1322 O  OE2   . GLU A 1 166 ? -14.733 -64.547 -8.855  1   147.9  ? 163 GLU A OE2   1 
ATOM   1323 N  N     . PRO A 1 167 ? -15.088 -60.979 -13.789 1   129.68 ? 164 PRO A N     1 
ATOM   1324 C  CA    . PRO A 1 167 ? -16.469 -60.741 -14.22  1   129.55 ? 164 PRO A CA    1 
ATOM   1325 C  C     . PRO A 1 167 ? -17.261 -62.007 -14.465 1   129.59 ? 164 PRO A C     1 
ATOM   1326 O  O     . PRO A 1 167 ? -16.691 -63.082 -14.635 1   129.69 ? 164 PRO A O     1 
ATOM   1327 C  CB    . PRO A 1 167 ? -16.286 -59.972 -15.528 1   130.22 ? 164 PRO A CB    1 
ATOM   1328 C  CG    . PRO A 1 167 ? -15.022 -60.506 -16.075 1   130.66 ? 164 PRO A CG    1 
ATOM   1329 C  CD    . PRO A 1 167 ? -14.132 -60.719 -14.884 1   129.13 ? 164 PRO A CD    1 
ATOM   1330 N  N     . ASP A 1 168 ? -18.581 -61.866 -14.528 1   129.46 ? 165 ASP A N     1 
ATOM   1331 C  CA    . ASP A 1 168 ? -19.447 -62.981 -14.872 1   130.04 ? 165 ASP A CA    1 
ATOM   1332 C  C     . ASP A 1 168 ? -19.189 -63.345 -16.357 1   129.93 ? 165 ASP A C     1 
ATOM   1333 O  O     . ASP A 1 168 ? -19.02  -64.522 -16.683 1   130.02 ? 165 ASP A O     1 
ATOM   1334 C  CB    . ASP A 1 168 ? -20.907 -62.619 -14.582 1   132.31 ? 165 ASP A CB    1 
ATOM   1335 C  CG    . ASP A 1 168 ? -21.162 -62.414 -13.098 1   137.69 ? 165 ASP A CG    1 
ATOM   1336 O  OD1   . ASP A 1 168 ? -20.832 -63.329 -12.304 1   138.9  ? 165 ASP A OD1   1 
ATOM   1337 O  OD2   . ASP A 1 168 ? -21.685 -61.337 -12.727 1   139.84 ? 165 ASP A OD2   1 
ATOM   1338 N  N     . LEU A 1 169 ? -19.037 -62.32  -17.221 1   129.49 ? 166 LEU A N     1 
ATOM   1339 C  CA    . LEU A 1 169 ? -18.675 -62.489 -18.618 1   129.63 ? 166 LEU A CA    1 
ATOM   1340 C  C     . LEU A 1 169 ? -17.492 -61.601 -18.96  1   129.74 ? 166 LEU A C     1 
ATOM   1341 O  O     . LEU A 1 169 ? -17.547 -60.39  -18.767 1   129.94 ? 166 LEU A O     1 
ATOM   1342 C  CB    . LEU A 1 169 ? -19.84  -62.18  -19.563 1   129.91 ? 166 LEU A CB    1 
ATOM   1343 C  CG    . LEU A 1 169 ? -19.523 -62.353 -21.054 1   131.62 ? 166 LEU A CG    1 
ATOM   1344 C  CD1   . LEU A 1 169 ? -19.097 -63.774 -21.375 1   132.32 ? 166 LEU A CD1   1 
ATOM   1345 C  CD2   . LEU A 1 169 ? -20.707 -61.982 -21.907 1   132.4  ? 166 LEU A CD2   1 
ATOM   1346 N  N     . ALA A 1 170 ? -16.428 -62.199 -19.475 1   129.6  ? 167 ALA A N     1 
ATOM   1347 C  CA    . ALA A 1 170 ? -15.252 -61.453 -19.88  1   130.17 ? 167 ALA A CA    1 
ATOM   1348 C  C     . ALA A 1 170 ? -15.108 -61.617 -21.376 1   130.78 ? 167 ALA A C     1 
ATOM   1349 O  O     . ALA A 1 170 ? -14.829 -62.721 -21.828 1   131.16 ? 167 ALA A O     1 
ATOM   1350 C  CB    . ALA A 1 170 ? -14.022 -62.009 -19.187 1   130.29 ? 167 ALA A CB    1 
ATOM   1351 N  N     . ILE A 1 171 ? -15.33  -60.555 -22.153 1   130.75 ? 168 ILE A N     1 
ATOM   1352 C  CA    . ILE A 1 171 ? -15.173 -60.618 -23.602 1   131.33 ? 168 ILE A CA    1 
ATOM   1353 C  C     . ILE A 1 171 ? -13.721 -60.281 -23.867 1   133    ? 168 ILE A C     1 
ATOM   1354 O  O     . ILE A 1 171 ? -13.283 -59.218 -23.459 1   133.18 ? 168 ILE A O     1 
ATOM   1355 C  CB    . ILE A 1 171 ? -16.124 -59.634 -24.308 1   131.06 ? 168 ILE A CB    1 
ATOM   1356 C  CG1   . ILE A 1 171 ? -17.568 -59.806 -23.819 1   131.36 ? 168 ILE A CG1   1 
ATOM   1357 C  CG2   . ILE A 1 171 ? -16.027 -59.804 -25.814 1   131.5  ? 168 ILE A CG2   1 
ATOM   1358 C  CD1   . ILE A 1 171 ? -18.392 -58.615 -23.976 1   132.35 ? 168 ILE A CD1   1 
ATOM   1359 N  N     . LEU A 1 172 ? -12.951 -61.185 -24.471 1   134.34 ? 169 LEU A N     1 
ATOM   1360 C  CA    . LEU A 1 172 ? -11.522 -60.948 -24.675 1   136.44 ? 169 LEU A CA    1 
ATOM   1361 C  C     . LEU A 1 172 ? -11.167 -60.822 -26.134 1   138.93 ? 169 LEU A C     1 
ATOM   1362 O  O     . LEU A 1 172 ? -11.082 -61.837 -26.813 1   139.24 ? 169 LEU A O     1 
ATOM   1363 C  CB    . LEU A 1 172 ? -10.7   -62.067 -24.026 1   136.66 ? 169 LEU A CB    1 
ATOM   1364 C  CG    . LEU A 1 172 ? -11.034 -62.356 -22.574 1   138.11 ? 169 LEU A CG    1 
ATOM   1365 C  CD1   . LEU A 1 172 ? -10.419 -63.667 -22.106 1   138.59 ? 169 LEU A CD1   1 
ATOM   1366 C  CD2   . LEU A 1 172 ? -10.645 -61.194 -21.704 1   138.87 ? 169 LEU A CD2   1 
ATOM   1367 N  N     . ASP A 1 173 ? -10.958 -59.597 -26.628 1   140.73 ? 170 ASP A N     1 
ATOM   1368 C  CA    . ASP A 1 173 ? -10.61  -59.415 -28.032 1   143.12 ? 170 ASP A CA    1 
ATOM   1369 C  C     . ASP A 1 173 ? -9.134  -59.692 -28.242 1   145.76 ? 170 ASP A C     1 
ATOM   1370 O  O     . ASP A 1 173 ? -8.288  -58.923 -27.785 1   145.95 ? 170 ASP A O     1 
ATOM   1371 C  CB    . ASP A 1 173 ? -11.002 -58.019 -28.547 1   144.65 ? 170 ASP A CB    1 
ATOM   1372 C  CG    . ASP A 1 173 ? -11.088 -57.907 -30.064 1   148.53 ? 170 ASP A CG    1 
ATOM   1373 O  OD1   . ASP A 1 173 ? -11.053 -58.955 -30.742 1   149.22 ? 170 ASP A OD1   1 
ATOM   1374 O  OD2   . ASP A 1 173 ? -11.2   -56.77  -30.57  1   150.32 ? 170 ASP A OD2   1 
ATOM   1375 N  N     . GLU A 1 174 ? -8.845  -60.815 -28.926 1   147.69 ? 171 GLU A N     1 
ATOM   1376 C  CA    . GLU A 1 174 ? -7.52   -61.333 -29.273 1   150    ? 171 GLU A CA    1 
ATOM   1377 C  C     . GLU A 1 174 ? -6.553  -61.311 -28.08  1   152.46 ? 171 GLU A C     1 
ATOM   1378 O  O     . GLU A 1 174 ? -5.562  -60.58  -28.083 1   152.67 ? 171 GLU A O     1 
ATOM   1379 C  CB    . GLU A 1 174 ? -6.967  -60.626 -30.522 1   151.78 ? 171 GLU A CB    1 
ATOM   1380 C  CG    . GLU A 1 174 ? -7.747  -61.026 -31.768 1   155.14 ? 171 GLU A CG    1 
ATOM   1381 C  CD    . GLU A 1 174 ? -7.867  -60.013 -32.887 1   159.78 ? 171 GLU A CD    1 
ATOM   1382 O  OE1   . GLU A 1 174 ? -8.998  -59.538 -33.139 1   160.55 ? 171 GLU A OE1   1 
ATOM   1383 O  OE2   . GLU A 1 174 ? -6.84   -59.719 -33.536 1   161.61 ? 171 GLU A OE2   1 
ATOM   1384 N  N     . PRO A 1 175 ? -6.836  -62.127 -27.047 1   154.07 ? 172 PRO A N     1 
ATOM   1385 C  CA    . PRO A 1 175 ? -5.965  -62.137 -25.866 1   155.56 ? 172 PRO A CA    1 
ATOM   1386 C  C     . PRO A 1 175 ? -4.548  -62.656 -26.102 1   157.76 ? 172 PRO A C     1 
ATOM   1387 O  O     . PRO A 1 175 ? -3.641  -62.262 -25.372 1   157.81 ? 172 PRO A O     1 
ATOM   1388 C  CB    . PRO A 1 175 ? -6.73   -63.015 -24.872 1   155.93 ? 172 PRO A CB    1 
ATOM   1389 C  CG    . PRO A 1 175 ? -7.576  -63.894 -25.715 1   155.99 ? 172 PRO A CG    1 
ATOM   1390 C  CD    . PRO A 1 175 ? -7.973  -63.055 -26.888 1   153.96 ? 172 PRO A CD    1 
ATOM   1391 N  N     . ASP A 1 176 ? -4.346  -63.524 -27.111 1   159.5  ? 173 ASP A N     1 
ATOM   1392 C  CA    . ASP A 1 176 ? -3.019  -64.084 -27.387 1   161.63 ? 173 ASP A CA    1 
ATOM   1393 C  C     . ASP A 1 176 ? -2.185  -63.271 -28.39  1   163.6  ? 173 ASP A C     1 
ATOM   1394 O  O     . ASP A 1 176 ? -0.993  -63.538 -28.537 1   163.66 ? 173 ASP A O     1 
ATOM   1395 C  CB    . ASP A 1 176 ? -3.101  -65.562 -27.815 1   163.54 ? 173 ASP A CB    1 
ATOM   1396 C  CG    . ASP A 1 176 ? -3.524  -65.805 -29.253 1   168.04 ? 173 ASP A CG    1 
ATOM   1397 O  OD1   . ASP A 1 176 ? -4.408  -65.07  -29.742 1   168.24 ? 173 ASP A OD1   1 
ATOM   1398 O  OD2   . ASP A 1 176 ? -2.98   -66.748 -29.884 1   170.64 ? 173 ASP A OD2   1 
ATOM   1399 N  N     . SER A 1 177 ? -2.802  -62.32  -29.101 1   165.07 ? 174 SER A N     1 
ATOM   1400 C  CA    . SER A 1 177 ? -2.062  -61.47  -30.032 1   166.98 ? 174 SER A CA    1 
ATOM   1401 C  C     . SER A 1 177 ? -1.785  -60.137 -29.343 1   168.71 ? 174 SER A C     1 
ATOM   1402 O  O     . SER A 1 177 ? -2.607  -59.657 -28.556 1   168.92 ? 174 SER A O     1 
ATOM   1403 C  CB    . SER A 1 177 ? -2.82   -61.279 -31.34  1   168.45 ? 174 SER A CB    1 
ATOM   1404 O  OG    . SER A 1 177 ? -2.153  -61.939 -32.407 1   170.73 ? 174 SER A OG    1 
ATOM   1405 N  N     . GLY A 1 178 ? -0.621  -59.567 -29.61  1   169.76 ? 175 GLY A N     1 
ATOM   1406 C  CA    . GLY A 1 178 ? -0.214  -58.339 -28.938 1   171.27 ? 175 GLY A CA    1 
ATOM   1407 C  C     . GLY A 1 178 ? 0.685   -58.61  -27.741 1   172.7  ? 175 GLY A C     1 
ATOM   1408 O  O     . GLY A 1 178 ? 1.362   -57.701 -27.267 1   172.91 ? 175 GLY A O     1 
ATOM   1409 N  N     . ILE A 1 179 ? 0.682   -59.856 -27.22  1   173.54 ? 176 ILE A N     1 
ATOM   1410 C  CA    . ILE A 1 179 ? 1.561   -60.314 -26.136 1   174.72 ? 176 ILE A CA    1 
ATOM   1411 C  C     . ILE A 1 179 ? 2.757   -61.134 -26.719 1   176.17 ? 176 ILE A C     1 
ATOM   1412 O  O     . ILE A 1 179 ? 3.683   -61.435 -25.968 1   176.23 ? 176 ILE A O     1 
ATOM   1413 C  CB    . ILE A 1 179 ? 0.778   -61.116 -25.05  1   174.98 ? 176 ILE A CB    1 
ATOM   1414 C  CG1   . ILE A 1 179 ? 0.469   -62.561 -25.509 1   175.63 ? 176 ILE A CG1   1 
ATOM   1415 C  CG2   . ILE A 1 179 ? -0.493  -60.376 -24.624 1   175.4  ? 176 ILE A CG2   1 
ATOM   1416 C  CD1   . ILE A 1 179 ? -0.139  -63.447 -24.479 1   176.71 ? 176 ILE A CD1   1 
ATOM   1417 N  N     . ASP A 1 180 ? 2.713   -61.496 -28.046 1   177.17 ? 177 ASP A N     1 
ATOM   1418 C  CA    . ASP A 1 180 ? 3.701   -62.274 -28.8   1   178.63 ? 177 ASP A CA    1 
ATOM   1419 C  C     . ASP A 1 180 ? 3.972   -63.585 -28.084 1   180.06 ? 177 ASP A C     1 
ATOM   1420 O  O     . ASP A 1 180 ? 5.114   -63.929 -27.767 1   180.11 ? 177 ASP A O     1 
ATOM   1421 C  CB    . ASP A 1 180 ? 4.974   -61.463 -29.06  1   180.16 ? 177 ASP A CB    1 
ATOM   1422 C  CG    . ASP A 1 180 ? 4.799   -60.322 -30.049 1   184.04 ? 177 ASP A CG    1 
ATOM   1423 O  OD1   . ASP A 1 180 ? 3.809   -60.345 -30.816 1   184.61 ? 177 ASP A OD1   1 
ATOM   1424 O  OD2   . ASP A 1 180 ? 5.661   -59.415 -30.067 1   185.86 ? 177 ASP A OD2   1 
ATOM   1425 N  N     . ILE A 1 181 ? 2.874   -64.292 -27.813 1   181.12 ? 178 ILE A N     1 
ATOM   1426 C  CA    . ILE A 1 181 ? 2.791   -65.53  -27.057 1   182.69 ? 178 ILE A CA    1 
ATOM   1427 C  C     . ILE A 1 181 ? 3.876   -66.568 -27.398 1   184.02 ? 178 ILE A C     1 
ATOM   1428 O  O     . ILE A 1 181 ? 4.146   -66.879 -28.558 1   184.11 ? 178 ILE A O     1 
ATOM   1429 C  CB    . ILE A 1 181 ? 1.368   -66.12  -27.158 1   183.4  ? 178 ILE A CB    1 
ATOM   1430 C  CG1   . ILE A 1 181 ? 1.053   -67.018 -25.949 1   184.44 ? 178 ILE A CG1   1 
ATOM   1431 C  CG2   . ILE A 1 181 ? 1.109   -66.817 -28.499 1   183.86 ? 178 ILE A CG2   1 
ATOM   1432 C  CD1   . ILE A 1 181 ? -0.381  -67.349 -25.825 1   185.69 ? 178 ILE A CD1   1 
ATOM   1433 N  N     . VAL A 1 182 ? 4.529   -67.051 -26.34  1   184.88 ? 179 VAL A N     1 
ATOM   1434 C  CA    . VAL A 1 182 ? 5.587   -68.05  -26.394 1   186.23 ? 179 VAL A CA    1 
ATOM   1435 C  C     . VAL A 1 182 ? 4.942   -69.428 -26.571 1   187.38 ? 179 VAL A C     1 
ATOM   1436 O  O     . VAL A 1 182 ? 5.352   -70.197 -27.444 1   187.4  ? 179 VAL A O     1 
ATOM   1437 C  CB    . VAL A 1 182 ? 6.413   -67.977 -25.087 1   187.14 ? 179 VAL A CB    1 
ATOM   1438 C  CG1   . VAL A 1 182 ? 7.405   -69.129 -24.988 1   187.75 ? 179 VAL A CG1   1 
ATOM   1439 C  CG2   . VAL A 1 182 ? 7.102   -66.625 -24.944 1   187.66 ? 179 VAL A CG2   1 
ATOM   1440 N  N     . SER A 1 183 ? 3.901   -69.718 -25.759 1   188.11 ? 180 SER A N     1 
ATOM   1441 C  CA    . SER A 1 183 ? 3.161   -70.978 -25.793 1   189.09 ? 180 SER A CA    1 
ATOM   1442 C  C     . SER A 1 183 ? 1.738   -70.807 -25.226 1   189.53 ? 180 SER A C     1 
ATOM   1443 O  O     . SER A 1 183 ? 1.5     -69.941 -24.383 1   189.59 ? 180 SER A O     1 
ATOM   1444 C  CB    . SER A 1 183 ? 3.91    -72.064 -25.023 1   190.51 ? 180 SER A CB    1 
ATOM   1445 O  OG    . SER A 1 183 ? 3.452   -73.363 -25.361 1   192.7  ? 180 SER A OG    1 
ATOM   1446 N  N     . PHE A 1 184 ? 0.79    -71.634 -25.707 1   189.53 ? 181 PHE A N     1 
ATOM   1447 C  CA    . PHE A 1 184 ? -0.597  -71.594 -25.237 1   189.74 ? 181 PHE A CA    1 
ATOM   1448 C  C     . PHE A 1 184 ? -0.744  -72.025 -23.784 1   188.99 ? 181 PHE A C     1 
ATOM   1449 O  O     . PHE A 1 184 ? -1.781  -71.754 -23.198 1   189.34 ? 181 PHE A O     1 
ATOM   1450 C  CB    . PHE A 1 184 ? -1.529  -72.431 -26.127 1   190.18 ? 181 PHE A CB    1 
ATOM   1451 C  CG    . PHE A 1 184 ? -1.732  -71.837 -27.495 1   191.32 ? 181 PHE A CG    1 
ATOM   1452 C  CD1   . PHE A 1 184 ? -2.269  -70.569 -27.645 1   192.23 ? 181 PHE A CD1   1 
ATOM   1453 C  CD2   . PHE A 1 184 ? -1.364  -72.534 -28.632 1   192.38 ? 181 PHE A CD2   1 
ATOM   1454 C  CE1   . PHE A 1 184 ? -2.438  -70.013 -28.907 1   193.04 ? 181 PHE A CE1   1 
ATOM   1455 C  CE2   . PHE A 1 184 ? -1.526  -71.973 -29.89  1   193.21 ? 181 PHE A CE2   1 
ATOM   1456 C  CZ    . PHE A 1 184 ? -2.075  -70.721 -30.022 1   192.98 ? 181 PHE A CZ    1 
ATOM   1457 N  N     . ASP A 1 185 ? 0.267   -72.695 -23.202 1   187.65 ? 182 ASP A N     1 
ATOM   1458 C  CA    . ASP A 1 185 ? 0.235   -73.113 -21.805 1   186.71 ? 182 ASP A CA    1 
ATOM   1459 C  C     . ASP A 1 185 ? 0.189   -71.895 -20.864 1   185.33 ? 182 ASP A C     1 
ATOM   1460 O  O     . ASP A 1 185 ? -0.387  -71.994 -19.778 1   185.61 ? 182 ASP A O     1 
ATOM   1461 C  CB    . ASP A 1 185 ? 1.444   -74.012 -21.493 1   188.24 ? 182 ASP A CB    1 
ATOM   1462 C  CG    . ASP A 1 185 ? 1.518   -75.258 -22.362 1   192.28 ? 182 ASP A CG    1 
ATOM   1463 O  OD1   . ASP A 1 185 ? 0.466   -75.672 -22.899 1   192.85 ? 182 ASP A OD1   1 
ATOM   1464 O  OD2   . ASP A 1 185 ? 2.627   -75.822 -22.501 1   194.2  ? 182 ASP A OD2   1 
ATOM   1465 N  N     . GLU A 1 186 ? 0.759   -70.74  -21.289 1   183.58 ? 183 GLU A N     1 
ATOM   1466 C  CA    . GLU A 1 186 ? 0.722   -69.548 -20.456 1   182.21 ? 183 GLU A CA    1 
ATOM   1467 C  C     . GLU A 1 186 ? -0.645  -68.871 -20.513 1   181.12 ? 183 GLU A C     1 
ATOM   1468 O  O     . GLU A 1 186 ? -1.112  -68.401 -19.482 1   181.01 ? 183 GLU A O     1 
ATOM   1469 C  CB    . GLU A 1 186 ? 1.888   -68.582 -20.735 1   183.18 ? 183 GLU A CB    1 
ATOM   1470 C  CG    . GLU A 1 186 ? 1.985   -67.997 -22.131 1   185.16 ? 183 GLU A CG    1 
ATOM   1471 C  CD    . GLU A 1 186 ? 3.406   -67.622 -22.5   1   187.21 ? 183 GLU A CD    1 
ATOM   1472 O  OE1   . GLU A 1 186 ? 3.619   -66.498 -23.007 1   187.22 ? 183 GLU A OE1   1 
ATOM   1473 O  OE2   . GLU A 1 186 ? 4.312   -68.453 -22.266 1   188.14 ? 183 GLU A OE2   1 
ATOM   1474 N  N     . ILE A 1 187 ? -1.318  -68.873 -21.678 1   180.24 ? 184 ILE A N     1 
ATOM   1475 C  CA    . ILE A 1 187 ? -2.66   -68.282 -21.774 1   179.83 ? 184 ILE A CA    1 
ATOM   1476 C  C     . ILE A 1 187 ? -3.722  -69.229 -21.173 1   178.61 ? 184 ILE A C     1 
ATOM   1477 O  O     . ILE A 1 187 ? -4.672  -68.761 -20.542 1   178.93 ? 184 ILE A O     1 
ATOM   1478 C  CB    . ILE A 1 187 ? -3.01   -67.793 -23.211 1   180.62 ? 184 ILE A CB    1 
ATOM   1479 C  CG1   . ILE A 1 187 ? -4.035  -66.636 -23.2   1   181.63 ? 184 ILE A CG1   1 
ATOM   1480 C  CG2   . ILE A 1 187 ? -3.453  -68.933 -24.125 1   181.15 ? 184 ILE A CG2   1 
ATOM   1481 C  CD1   . ILE A 1 187 ? -3.52   -65.368 -22.624 1   182.84 ? 184 ILE A CD1   1 
ATOM   1482 N  N     . LYS A 1 188 ? -3.52   -70.554 -21.316 1   176.98 ? 185 LYS A N     1 
ATOM   1483 C  CA    . LYS A 1 188 ? -4.395  -71.59  -20.772 1   176.04 ? 185 LYS A CA    1 
ATOM   1484 C  C     . LYS A 1 188 ? -4.404  -71.511 -19.257 1   175.29 ? 185 LYS A C     1 
ATOM   1485 O  O     . LYS A 1 188 ? -5.459  -71.662 -18.658 1   175.41 ? 185 LYS A O     1 
ATOM   1486 C  CB    . LYS A 1 188 ? -3.936  -72.989 -21.234 1   177.25 ? 185 LYS A CB    1 
ATOM   1487 C  CG    . LYS A 1 188 ? -4.694  -74.155 -20.607 1   180.28 ? 185 LYS A CG    1 
ATOM   1488 C  CD    . LYS A 1 188 ? -4.752  -75.368 -21.521 1   183.51 ? 185 LYS A CD    1 
ATOM   1489 C  CE    . LYS A 1 188 ? -3.394  -75.971 -21.785 1   186.54 ? 185 LYS A CE    1 
ATOM   1490 N  NZ    . LYS A 1 188 ? -3.482  -77.175 -22.658 1   188.52 ? 185 LYS A NZ    1 
ATOM   1491 N  N     . ARG A 1 189 ? -3.248  -71.223 -18.635 1   174.45 ? 186 ARG A N     1 
ATOM   1492 C  CA    . ARG A 1 189 ? -3.16   -71.103 -17.184 1   174.17 ? 186 ARG A CA    1 
ATOM   1493 C  C     . ARG A 1 189 ? -4.01   -69.942 -16.642 1   173.14 ? 186 ARG A C     1 
ATOM   1494 O  O     . ARG A 1 189 ? -4.56   -70.052 -15.549 1   173.44 ? 186 ARG A O     1 
ATOM   1495 C  CB    . ARG A 1 189 ? -1.697  -71.047 -16.713 1   175.91 ? 186 ARG A CB    1 
ATOM   1496 C  CG    . ARG A 1 189 ? -1.038  -69.679 -16.623 1   179.57 ? 186 ARG A CG    1 
ATOM   1497 C  CD    . ARG A 1 189 ? 0.458   -69.892 -16.576 1   183.11 ? 186 ARG A CD    1 
ATOM   1498 N  NE    . ARG A 1 189 ? 1.208   -68.731 -16.106 1   186.06 ? 186 ARG A NE    1 
ATOM   1499 C  CZ    . ARG A 1 189 ? 1.529   -68.507 -14.834 1   188.46 ? 186 ARG A CZ    1 
ATOM   1500 N  NH1   . ARG A 1 189 ? 1.1     -69.323 -13.879 1   188.3  ? 186 ARG A NH1   1 
ATOM   1501 N  NH2   . ARG A 1 189 ? 2.241   -67.438 -14.504 1   188.43 ? 186 ARG A NH2   1 
ATOM   1502 N  N     . VAL A 1 190 ? -4.182  -68.876 -17.434 1   171.59 ? 187 VAL A N     1 
ATOM   1503 C  CA    . VAL A 1 190 ? -5.011  -67.743 -17.056 1   170.51 ? 187 VAL A CA    1 
ATOM   1504 C  C     . VAL A 1 190 ? -6.481  -68.076 -17.309 1   169.19 ? 187 VAL A C     1 
ATOM   1505 O  O     . VAL A 1 190 ? -7.324  -67.829 -16.453 1   169.15 ? 187 VAL A O     1 
ATOM   1506 C  CB    . VAL A 1 190 ? -4.584  -66.492 -17.836 1   171.31 ? 187 VAL A CB    1 
ATOM   1507 C  CG1   . VAL A 1 190 ? -5.477  -65.309 -17.496 1   171.96 ? 187 VAL A CG1   1 
ATOM   1508 C  CG2   . VAL A 1 190 ? -3.125  -66.163 -17.57  1   171.82 ? 187 VAL A CG2   1 
ATOM   1509 N  N     . PHE A 1 191 ? -6.783  -68.666 -18.468 1   168.1  ? 188 PHE A N     1 
ATOM   1510 C  CA    . PHE A 1 191 ? -8.145  -69.051 -18.848 1   167.65 ? 188 PHE A CA    1 
ATOM   1511 C  C     . PHE A 1 191 ? -8.763  -70.052 -17.87  1   167.47 ? 188 PHE A C     1 
ATOM   1512 O  O     . PHE A 1 191 ? -9.935  -69.927 -17.522 1   167.38 ? 188 PHE A O     1 
ATOM   1513 C  CB    . PHE A 1 191 ? -8.15   -69.652 -20.257 1   167.3  ? 188 PHE A CB    1 
ATOM   1514 C  CG    . PHE A 1 191 ? -8.123  -68.677 -21.408 1   167.53 ? 188 PHE A CG    1 
ATOM   1515 C  CD1   . PHE A 1 191 ? -7.667  -67.383 -21.234 1   168.11 ? 188 PHE A CD1   1 
ATOM   1516 C  CD2   . PHE A 1 191 ? -8.524  -69.064 -22.669 1   168.17 ? 188 PHE A CD2   1 
ATOM   1517 C  CE1   . PHE A 1 191 ? -7.626  -66.497 -22.297 1   168.74 ? 188 PHE A CE1   1 
ATOM   1518 C  CE2   . PHE A 1 191 ? -8.477  -68.177 -23.73  1   168.79 ? 188 PHE A CE2   1 
ATOM   1519 C  CZ    . PHE A 1 191 ? -8.037  -66.897 -23.536 1   168.55 ? 188 PHE A CZ    1 
ATOM   1520 N  N     . ASP A 1 192 ? -7.977  -71.051 -17.44  1   167.28 ? 189 ASP A N     1 
ATOM   1521 C  CA    . ASP A 1 192 ? -8.413  -72.068 -16.485 1   167.63 ? 189 ASP A CA    1 
ATOM   1522 C  C     . ASP A 1 192 ? -8.618  -71.45  -15.099 1   167.24 ? 189 ASP A C     1 
ATOM   1523 O  O     . ASP A 1 192 ? -9.522  -71.863 -14.382 1   167.37 ? 189 ASP A O     1 
ATOM   1524 C  CB    . ASP A 1 192 ? -7.406  -73.242 -16.405 1   169.94 ? 189 ASP A CB    1 
ATOM   1525 C  CG    . ASP A 1 192 ? -7.366  -74.149 -17.628 1   175.4  ? 189 ASP A CG    1 
ATOM   1526 O  OD1   . ASP A 1 192 ? -8.184  -73.939 -18.55  1   176.48 ? 189 ASP A OD1   1 
ATOM   1527 O  OD2   . ASP A 1 192 ? -6.506  -75.067 -17.664 1   177.61 ? 189 ASP A OD2   1 
ATOM   1528 N  N     . TYR A 1 193 ? -7.802  -70.456 -14.725 1   166.63 ? 190 TYR A N     1 
ATOM   1529 C  CA    . TYR A 1 193 ? -7.931  -69.785 -13.438 1   166.62 ? 190 TYR A CA    1 
ATOM   1530 C  C     . TYR A 1 193 ? -9.26   -69.049 -13.373 1   165.67 ? 190 TYR A C     1 
ATOM   1531 O  O     . TYR A 1 193 ? -9.953  -69.13  -12.364 1   165.75 ? 190 TYR A O     1 
ATOM   1532 C  CB    . TYR A 1 193 ? -6.763  -68.808 -13.226 1   167.25 ? 190 TYR A CB    1 
ATOM   1533 C  CG    . TYR A 1 193 ? -6.773  -68.108 -11.884 1   168.77 ? 190 TYR A CG    1 
ATOM   1534 C  CD1   . TYR A 1 193 ? -6.113  -68.649 -10.79  1   170.28 ? 190 TYR A CD1   1 
ATOM   1535 C  CD2   . TYR A 1 193 ? -7.394  -66.877 -11.724 1   169.7  ? 190 TYR A CD2   1 
ATOM   1536 C  CE1   . TYR A 1 193 ? -6.094  -67.998 -9.564  1   171.33 ? 190 TYR A CE1   1 
ATOM   1537 C  CE2   . TYR A 1 193 ? -7.389  -66.22  -10.502 1   170.78 ? 190 TYR A CE2   1 
ATOM   1538 C  CZ    . TYR A 1 193 ? -6.73   -66.781 -9.426  1   172.12 ? 190 TYR A CZ    1 
ATOM   1539 O  OH    . TYR A 1 193 ? -6.727  -66.145 -8.215  1   173.98 ? 190 TYR A OH    1 
ATOM   1540 N  N     . LEU A 1 194 ? -9.62   -68.343 -14.446 1   164.73 ? 191 LEU A N     1 
ATOM   1541 C  CA    . LEU A 1 194 ? -10.88  -67.61  -14.486 1   164.35 ? 191 LEU A CA    1 
ATOM   1542 C  C     . LEU A 1 194 ? -12.055 -68.589 -14.517 1   163.38 ? 191 LEU A C     1 
ATOM   1543 O  O     . LEU A 1 194 ? -13.043 -68.388 -13.815 1   163.36 ? 191 LEU A O     1 
ATOM   1544 C  CB    . LEU A 1 194 ? -10.919 -66.664 -15.696 1   164.76 ? 191 LEU A CB    1 
ATOM   1545 C  CG    . LEU A 1 194 ? -9.92   -65.507 -15.682 1   166.42 ? 191 LEU A CG    1 
ATOM   1546 C  CD1   . LEU A 1 194 ? -9.923  -64.779 -17.006 1   167.19 ? 191 LEU A CD1   1 
ATOM   1547 C  CD2   . LEU A 1 194 ? -10.215 -64.537 -14.557 1   166.99 ? 191 LEU A CD2   1 
ATOM   1548 N  N     . LYS A 1 195 ? -11.928 -69.665 -15.29  1   162.51 ? 192 LYS A N     1 
ATOM   1549 C  CA    . LYS A 1 195 ? -12.957 -70.685 -15.386 1   162.45 ? 192 LYS A CA    1 
ATOM   1550 C  C     . LYS A 1 195 ? -13.218 -71.341 -14.016 1   162.2  ? 192 LYS A C     1 
ATOM   1551 O  O     . LYS A 1 195 ? -14.373 -71.544 -13.654 1   162.47 ? 192 LYS A O     1 
ATOM   1552 C  CB    . LYS A 1 195 ? -12.551 -71.74  -16.427 1   164.27 ? 192 LYS A CB    1 
ATOM   1553 C  CG    . LYS A 1 195 ? -13.655 -72.748 -16.766 1   167.77 ? 192 LYS A CG    1 
ATOM   1554 C  CD    . LYS A 1 195 ? -13.148 -73.889 -17.643 1   170.65 ? 192 LYS A CD    1 
ATOM   1555 C  CE    . LYS A 1 195 ? -14.269 -74.724 -18.205 1   173.07 ? 192 LYS A CE    1 
ATOM   1556 N  NZ    . LYS A 1 195 ? -13.787 -75.612 -19.291 1   174.71 ? 192 LYS A NZ    1 
ATOM   1557 N  N     . ASP A 1 196 ? -12.159 -71.633 -13.239 1   161.45 ? 193 ASP A N     1 
ATOM   1558 C  CA    . ASP A 1 196 ? -12.31  -72.236 -11.909 1   161.22 ? 193 ASP A CA    1 
ATOM   1559 C  C     . ASP A 1 196 ? -13.028 -71.319 -10.917 1   160.73 ? 193 ASP A C     1 
ATOM   1560 O  O     . ASP A 1 196 ? -13.674 -71.809 -9.99   1   160.82 ? 193 ASP A O     1 
ATOM   1561 C  CB    . ASP A 1 196 ? -10.956 -72.667 -11.342 1   162.95 ? 193 ASP A CB    1 
ATOM   1562 C  CG    . ASP A 1 196 ? -10.342 -73.832 -12.081 1   168    ? 193 ASP A CG    1 
ATOM   1563 O  OD1   . ASP A 1 196 ? -11.067 -74.819 -12.343 1   169.14 ? 193 ASP A OD1   1 
ATOM   1564 O  OD2   . ASP A 1 196 ? -9.143  -73.748 -12.422 1   170.11 ? 193 ASP A OD2   1 
ATOM   1565 N  N     . LYS A 1 197 ? -12.922 -69.993 -11.118 1   160.03 ? 194 LYS A N     1 
ATOM   1566 C  CA    . LYS A 1 197 ? -13.58  -68.976 -10.295 1   159.71 ? 194 LYS A CA    1 
ATOM   1567 C  C     . LYS A 1 197 ? -15.083 -68.804 -10.617 1   159.38 ? 194 LYS A C     1 
ATOM   1568 O  O     . LYS A 1 197 ? -15.793 -68.165 -9.844  1   159.67 ? 194 LYS A O     1 
ATOM   1569 C  CB    . LYS A 1 197 ? -12.867 -67.621 -10.445 1   161.02 ? 194 LYS A CB    1 
ATOM   1570 C  CG    . LYS A 1 197 ? -11.443 -67.597 -9.916  1   164.36 ? 194 LYS A CG    1 
ATOM   1571 C  CD    . LYS A 1 197 ? -11.396 -67.547 -8.403  1   168.48 ? 194 LYS A CD    1 
ATOM   1572 C  CE    . LYS A 1 197 ? -9.991  -67.344 -7.904  1   172.37 ? 194 LYS A CE    1 
ATOM   1573 N  NZ    . LYS A 1 197 ? -9.497  -65.971 -8.182  1   175.01 ? 194 LYS A NZ    1 
ATOM   1574 N  N     . GLY A 1 198 ? -15.542 -69.334 -11.751 1   158.57 ? 195 GLY A N     1 
ATOM   1575 C  CA    . GLY A 1 198 ? -16.937 -69.234 -12.169 1   158.1  ? 195 GLY A CA    1 
ATOM   1576 C  C     . GLY A 1 198 ? -17.198 -68.292 -13.334 1   157.21 ? 195 GLY A C     1 
ATOM   1577 O  O     . GLY A 1 198 ? -18.353 -68.041 -13.685 1   157.27 ? 195 GLY A O     1 
ATOM   1578 N  N     . CYS A 1 199 ? -16.137 -67.789 -13.968 1   156.25 ? 196 CYS A N     1 
ATOM   1579 C  CA    . CYS A 1 199 ? -16.277 -66.857 -15.081 1   155.96 ? 196 CYS A CA    1 
ATOM   1580 C  C     . CYS A 1 199 ? -16.603 -67.546 -16.388 1   154.85 ? 196 CYS A C     1 
ATOM   1581 O  O     . CYS A 1 199 ? -16.222 -68.699 -16.604 1   154.74 ? 196 CYS A O     1 
ATOM   1582 C  CB    . CYS A 1 199 ? -15.022 -66.001 -15.231 1   157.21 ? 196 CYS A CB    1 
ATOM   1583 S  SG    . CYS A 1 199 ? -14.43  -65.26  -13.692 1   161.88 ? 196 CYS A SG    1 
ATOM   1584 N  N     . SER A 1 200 ? -17.245 -66.796 -17.292 1   153.76 ? 197 SER A N     1 
ATOM   1585 C  CA    . SER A 1 200 ? -17.5   -67.217 -18.662 1   153.08 ? 197 SER A CA    1 
ATOM   1586 C  C     . SER A 1 200 ? -16.652 -66.301 -19.544 1   152.04 ? 197 SER A C     1 
ATOM   1587 O  O     . SER A 1 200 ? -16.597 -65.094 -19.301 1   152.17 ? 197 SER A O     1 
ATOM   1588 C  CB    . SER A 1 200 ? -18.975 -67.08  -19.023 1   154.27 ? 197 SER A CB    1 
ATOM   1589 O  OG    . SER A 1 200 ? -19.743 -68.11  -18.426 1   156.36 ? 197 SER A OG    1 
ATOM   1590 N  N     . LEU A 1 201 ? -15.949 -66.87  -20.522 1   150.92 ? 198 LEU A N     1 
ATOM   1591 C  CA    . LEU A 1 201 ? -15.098 -66.074 -21.392 1   150.48 ? 198 LEU A CA    1 
ATOM   1592 C  C     . LEU A 1 201 ? -15.618 -66.117 -22.804 1   150.3  ? 198 LEU A C     1 
ATOM   1593 O  O     . LEU A 1 201 ? -15.955 -67.19  -23.29  1   150.35 ? 198 LEU A O     1 
ATOM   1594 C  CB    . LEU A 1 201 ? -13.653 -66.591 -21.374 1   150.4  ? 198 LEU A CB    1 
ATOM   1595 C  CG    . LEU A 1 201 ? -13.005 -66.839 -20.023 1   151.48 ? 198 LEU A CG    1 
ATOM   1596 C  CD1   . LEU A 1 201 ? -11.585 -67.335 -20.198 1   152.04 ? 198 LEU A CD1   1 
ATOM   1597 C  CD2   . LEU A 1 201 ? -13.01  -65.595 -19.171 1   151.93 ? 198 LEU A CD2   1 
ATOM   1598 N  N     . LEU A 1 202 ? -15.682 -64.962 -23.47  1   149.92 ? 199 LEU A N     1 
ATOM   1599 C  CA    . LEU A 1 202 ? -16.077 -64.895 -24.87  1   150.09 ? 199 LEU A CA    1 
ATOM   1600 C  C     . LEU A 1 202 ? -14.821 -64.49  -25.599 1   150.59 ? 199 LEU A C     1 
ATOM   1601 O  O     . LEU A 1 202 ? -14.578 -63.315 -25.822 1   150.7  ? 199 LEU A O     1 
ATOM   1602 C  CB    . LEU A 1 202 ? -17.203 -63.882 -25.1   1   150.12 ? 199 LEU A CB    1 
ATOM   1603 C  CG    . LEU A 1 202 ? -17.736 -63.784 -26.529 1   151.52 ? 199 LEU A CG    1 
ATOM   1604 C  CD1   . LEU A 1 202 ? -18.22  -65.121 -27.037 1   152.08 ? 199 LEU A CD1   1 
ATOM   1605 C  CD2   . LEU A 1 202 ? -18.846 -62.774 -26.622 1   152.21 ? 199 LEU A CD2   1 
ATOM   1606 N  N     . VAL A 1 203 ? -13.971 -65.463 -25.872 1   151.1  ? 200 VAL A N     1 
ATOM   1607 C  CA    . VAL A 1 203 ? -12.674 -65.24  -26.483 1   152.49 ? 200 VAL A CA    1 
ATOM   1608 C  C     . VAL A 1 203 ? -12.754 -65.028 -27.977 1   153.93 ? 200 VAL A C     1 
ATOM   1609 O  O     . VAL A 1 203 ? -13.067 -65.951 -28.707 1   153.98 ? 200 VAL A O     1 
ATOM   1610 C  CB    . VAL A 1 203 ? -11.718 -66.398 -26.15  1   153.45 ? 200 VAL A CB    1 
ATOM   1611 C  CG1   . VAL A 1 203 ? -10.334 -66.143 -26.731 1   154.13 ? 200 VAL A CG1   1 
ATOM   1612 C  CG2   . VAL A 1 203 ? -11.639 -66.627 -24.646 1   154.04 ? 200 VAL A CG2   1 
ATOM   1613 N  N     . ILE A 1 204 ? -12.429 -63.83  -28.443 1   155.05 ? 201 ILE A N     1 
ATOM   1614 C  CA    . ILE A 1 204 ? -12.447 -63.519 -29.868 1   156.63 ? 201 ILE A CA    1 
ATOM   1615 C  C     . ILE A 1 204 ? -11.039 -63.784 -30.414 1   158.34 ? 201 ILE A C     1 
ATOM   1616 O  O     . ILE A 1 204 ? -10.081 -63.237 -29.886 1   158.34 ? 201 ILE A O     1 
ATOM   1617 C  CB    . ILE A 1 204 ? -12.887 -62.041 -30.087 1   157.14 ? 201 ILE A CB    1 
ATOM   1618 C  CG1   . ILE A 1 204 ? -14.163 -61.673 -29.283 1   158.18 ? 201 ILE A CG1   1 
ATOM   1619 C  CG2   . ILE A 1 204 ? -13.037 -61.714 -31.555 1   157.53 ? 201 ILE A CG2   1 
ATOM   1620 C  CD1   . ILE A 1 204 ? -15.391 -62.439 -29.629 1   159.5  ? 201 ILE A CD1   1 
ATOM   1621 N  N     . THR A 1 205 ? -10.894 -64.651 -31.428 1   159.7  ? 202 THR A N     1 
ATOM   1622 C  CA    . THR A 1 205 ? -9.575  -64.96  -31.994 1   161.56 ? 202 THR A CA    1 
ATOM   1623 C  C     . THR A 1 205 ? -9.612  -65.369 -33.483 1   163.65 ? 202 THR A C     1 
ATOM   1624 O  O     . THR A 1 205 ? -10.633 -65.833 -33.98  1   163.82 ? 202 THR A O     1 
ATOM   1625 C  CB    . THR A 1 205 ? -8.879  -66.048 -31.16  1   162.53 ? 202 THR A CB    1 
ATOM   1626 O  OG1   . THR A 1 205 ? -7.504  -66.125 -31.534 1   163.34 ? 202 THR A OG1   1 
ATOM   1627 C  CG2   . THR A 1 205 ? -9.549  -67.413 -31.295 1   162.9  ? 202 THR A CG2   1 
ATOM   1628 N  N     . HIS A 1 206 ? -8.493  -65.181 -34.195 1   165.02 ? 203 HIS A N     1 
ATOM   1629 C  CA    . HIS A 1 206 ? -8.341  -65.634 -35.585 1   166.86 ? 203 HIS A CA    1 
ATOM   1630 C  C     . HIS A 1 206 ? -7.537  -66.975 -35.612 1   168.55 ? 203 HIS A C     1 
ATOM   1631 O  O     . HIS A 1 206 ? -7.556  -67.67  -36.632 1   168.76 ? 203 HIS A O     1 
ATOM   1632 C  CB    . HIS A 1 206 ? -7.55   -64.634 -36.455 1   167.93 ? 203 HIS A CB    1 
ATOM   1633 C  CG    . HIS A 1 206 ? -7.936  -63.188 -36.382 1   170.61 ? 203 HIS A CG    1 
ATOM   1634 N  ND1   . HIS A 1 206 ? -7.609  -62.405 -35.288 1   172.59 ? 203 HIS A ND1   1 
ATOM   1635 C  CD2   . HIS A 1 206 ? -8.445  -62.388 -37.349 1   171.84 ? 203 HIS A CD2   1 
ATOM   1636 C  CE1   . HIS A 1 206 ? -7.999  -61.179 -35.593 1   173.08 ? 203 HIS A CE1   1 
ATOM   1637 N  NE2   . HIS A 1 206 ? -8.506  -61.118 -36.822 1   172.98 ? 203 HIS A NE2   1 
ATOM   1638 N  N     . ARG A 1 207 ? -6.766  -67.279 -34.526 1   169.48 ? 204 ARG A N     1 
ATOM   1639 C  CA    . ARG A 1 207 ? -5.906  -68.454 -34.36  1   170.71 ? 204 ARG A CA    1 
ATOM   1640 C  C     . ARG A 1 207 ? -6.727  -69.665 -33.966 1   172.04 ? 204 ARG A C     1 
ATOM   1641 O  O     . ARG A 1 207 ? -7.173  -69.75  -32.823 1   171.96 ? 204 ARG A O     1 
ATOM   1642 C  CB    . ARG A 1 207 ? -4.859  -68.209 -33.253 1   171.68 ? 204 ARG A CB    1 
ATOM   1643 C  CG    . ARG A 1 207 ? -3.589  -67.456 -33.658 1   173.91 ? 204 ARG A CG    1 
ATOM   1644 C  CD    . ARG A 1 207 ? -3.769  -65.949 -33.805 1   175.96 ? 204 ARG A CD    1 
ATOM   1645 N  NE    . ARG A 1 207 ? -4.485  -65.346 -32.678 1   177.22 ? 204 ARG A NE    1 
ATOM   1646 C  CZ    . ARG A 1 207 ? -4.88   -64.08  -32.629 1   178.08 ? 204 ARG A CZ    1 
ATOM   1647 N  NH1   . ARG A 1 207 ? -4.606  -63.252 -33.63  1   177.41 ? 204 ARG A NH1   1 
ATOM   1648 N  NH2   . ARG A 1 207 ? -5.538  -63.627 -31.572 1   177.53 ? 204 ARG A NH2   1 
ATOM   1649 N  N     . GLU A 1 208 ? -6.89   -70.617 -34.898 1   173.14 ? 205 GLU A N     1 
ATOM   1650 C  CA    . GLU A 1 208 ? -7.618  -71.881 -34.707 1   174.65 ? 205 GLU A CA    1 
ATOM   1651 C  C     . GLU A 1 208 ? -6.984  -72.739 -33.586 1   175.62 ? 205 GLU A C     1 
ATOM   1652 O  O     . GLU A 1 208 ? -7.69   -73.458 -32.875 1   175.77 ? 205 GLU A O     1 
ATOM   1653 C  CB    . GLU A 1 208 ? -7.648  -72.665 -36.039 1   177.23 ? 205 GLU A CB    1 
ATOM   1654 C  CG    . GLU A 1 208 ? -8.513  -73.915 -36.043 1   182.39 ? 205 GLU A CG    1 
ATOM   1655 C  CD    . GLU A 1 208 ? -7.794  -75.179 -36.482 1   189.38 ? 205 GLU A CD    1 
ATOM   1656 O  OE1   . GLU A 1 208 ? -8.351  -76.281 -36.274 1   191.1  ? 205 GLU A OE1   1 
ATOM   1657 O  OE2   . GLU A 1 208 ? -6.673  -75.071 -37.032 1   191.64 ? 205 GLU A OE2   1 
ATOM   1658 N  N     . GLU A 1 209 ? -5.657  -72.631 -33.413 1   176.02 ? 206 GLU A N     1 
ATOM   1659 C  CA    . GLU A 1 209 ? -4.923  -73.363 -32.387 1   176.78 ? 206 GLU A CA    1 
ATOM   1660 C  C     . GLU A 1 209 ? -5.357  -72.925 -30.985 1   177.33 ? 206 GLU A C     1 
ATOM   1661 O  O     . GLU A 1 209 ? -5.427  -73.765 -30.097 1   177.35 ? 206 GLU A O     1 
ATOM   1662 C  CB    . GLU A 1 209 ? -3.402  -73.189 -32.554 1   178.95 ? 206 GLU A CB    1 
ATOM   1663 C  CG    . GLU A 1 209 ? -2.881  -73.193 -33.984 1   183.26 ? 206 GLU A CG    1 
ATOM   1664 C  CD    . GLU A 1 209 ? -2.714  -71.818 -34.605 1   188.3  ? 206 GLU A CD    1 
ATOM   1665 O  OE1   . GLU A 1 209 ? -2.564  -71.742 -35.846 1   188.93 ? 206 GLU A OE1   1 
ATOM   1666 O  OE2   . GLU A 1 209 ? -2.735  -70.816 -33.853 1   190.15 ? 206 GLU A OE2   1 
ATOM   1667 N  N     . LEU A 1 210 ? -5.668  -71.624 -30.791 1   177.64 ? 207 LEU A N     1 
ATOM   1668 C  CA    . LEU A 1 210 ? -6.124  -71.088 -29.5   1   178.4  ? 207 LEU A CA    1 
ATOM   1669 C  C     . LEU A 1 210 ? -7.535  -71.557 -29.179 1   178.44 ? 207 LEU A C     1 
ATOM   1670 O  O     . LEU A 1 210 ? -7.842  -71.847 -28.025 1   178.33 ? 207 LEU A O     1 
ATOM   1671 C  CB    . LEU A 1 210 ? -6.091  -69.541 -29.488 1   179.05 ? 207 LEU A CB    1 
ATOM   1672 C  CG    . LEU A 1 210 ? -6.61   -68.853 -28.199 1   180.92 ? 207 LEU A CG    1 
ATOM   1673 C  CD1   . LEU A 1 210 ? -5.752  -69.207 -27.006 1   181.49 ? 207 LEU A CD1   1 
ATOM   1674 C  CD2   . LEU A 1 210 ? -6.676  -67.332 -28.35  1   181.79 ? 207 LEU A CD2   1 
ATOM   1675 N  N     . ALA A 1 211 ? -8.394  -71.621 -30.195 1   178.49 ? 208 ALA A N     1 
ATOM   1676 C  CA    . ALA A 1 211 ? -9.781  -72.017 -30.025 1   179.08 ? 208 ALA A CA    1 
ATOM   1677 C  C     . ALA A 1 211 ? -9.963  -73.463 -29.587 1   179.59 ? 208 ALA A C     1 
ATOM   1678 O  O     . ALA A 1 211 ? -10.96  -73.759 -28.944 1   179.75 ? 208 ALA A O     1 
ATOM   1679 C  CB    . ALA A 1 211 ? -10.557 -71.753 -31.298 1   179.27 ? 208 ALA A CB    1 
ATOM   1680 N  N     . GLU A 1 212 ? -9.014  -74.362 -29.899 1   179.72 ? 209 GLU A N     1 
ATOM   1681 C  CA    . GLU A 1 212 ? -9.128  -75.774 -29.512 1   180.27 ? 209 GLU A CA    1 
ATOM   1682 C  C     . GLU A 1 212 ? -9.097  -76.006 -27.988 1   180.55 ? 209 GLU A C     1 
ATOM   1683 O  O     . GLU A 1 212 ? -9.614  -77.018 -27.515 1   180.45 ? 209 GLU A O     1 
ATOM   1684 C  CB    . GLU A 1 212 ? -8.079  -76.623 -30.231 1   182.51 ? 209 GLU A CB    1 
ATOM   1685 C  CG    . GLU A 1 212 ? -8.481  -76.926 -31.662 1   187.47 ? 209 GLU A CG    1 
ATOM   1686 C  CD    . GLU A 1 212 ? -7.402  -77.589 -32.488 1   193.94 ? 209 GLU A CD    1 
ATOM   1687 O  OE1   . GLU A 1 212 ? -6.259  -77.078 -32.479 1   195.16 ? 209 GLU A OE1   1 
ATOM   1688 O  OE2   . GLU A 1 212 ? -7.694  -78.614 -33.146 1   196.27 ? 209 GLU A OE2   1 
ATOM   1689 N  N     . HIS A 1 213 ? -8.538  -75.04  -27.223 1   180.69 ? 210 HIS A N     1 
ATOM   1690 C  CA    . HIS A 1 213 ? -8.488  -75.073 -25.749 1   181.04 ? 210 HIS A CA    1 
ATOM   1691 C  C     . HIS A 1 213 ? -9.792  -74.555 -25.084 1   179.87 ? 210 HIS A C     1 
ATOM   1692 O  O     . HIS A 1 213 ? -9.916  -74.608 -23.863 1   179.76 ? 210 HIS A O     1 
ATOM   1693 C  CB    . HIS A 1 213 ? -7.268  -74.294 -25.208 1   183.07 ? 210 HIS A CB    1 
ATOM   1694 C  CG    . HIS A 1 213 ? -5.975  -74.578 -25.925 1   187.4  ? 210 HIS A CG    1 
ATOM   1695 N  ND1   . HIS A 1 213 ? -5.135  -75.618 -25.539 1   189.87 ? 210 HIS A ND1   1 
ATOM   1696 C  CD2   . HIS A 1 213 ? -5.41   -73.93  -26.971 1   188.99 ? 210 HIS A CD2   1 
ATOM   1697 C  CE1   . HIS A 1 213 ? -4.1    -75.571 -26.368 1   190.57 ? 210 HIS A CE1   1 
ATOM   1698 N  NE2   . HIS A 1 213 ? -4.221  -74.574 -27.248 1   190.4  ? 210 HIS A NE2   1 
ATOM   1699 N  N     . ALA A 1 214 ? -10.747 -74.053 -25.885 1   178.89 ? 211 ALA A N     1 
ATOM   1700 C  CA    . ALA A 1 214 ? -12.046 -73.573 -25.422 1   178.48 ? 211 ALA A CA    1 
ATOM   1701 C  C     . ALA A 1 214 ? -13.069 -74.734 -25.382 1   177.98 ? 211 ALA A C     1 
ATOM   1702 O  O     . ALA A 1 214 ? -12.824 -75.794 -25.964 1   178.2  ? 211 ALA A O     1 
ATOM   1703 C  CB    . ALA A 1 214 ? -12.538 -72.46  -26.342 1   178.55 ? 211 ALA A CB    1 
ATOM   1704 N  N     . ASP A 1 215 ? -14.199 -74.55  -24.681 1   177.16 ? 212 ASP A N     1 
ATOM   1705 C  CA    . ASP A 1 215 ? -15.217 -75.593 -24.588 1   176.89 ? 212 ASP A CA    1 
ATOM   1706 C  C     . ASP A 1 215 ? -16.046 -75.664 -25.876 1   176.37 ? 212 ASP A C     1 
ATOM   1707 O  O     . ASP A 1 215 ? -16.302 -76.751 -26.394 1   176.5  ? 212 ASP A O     1 
ATOM   1708 C  CB    . ASP A 1 215 ? -16.123 -75.354 -23.366 1   178.32 ? 212 ASP A CB    1 
ATOM   1709 C  CG    . ASP A 1 215 ? -15.373 -75.107 -22.071 1   182.16 ? 212 ASP A CG    1 
ATOM   1710 O  OD1   . ASP A 1 215 ? -14.181 -75.472 -21.995 1   182.56 ? 212 ASP A OD1   1 
ATOM   1711 O  OD2   . ASP A 1 215 ? -15.98  -74.551 -21.134 1   184.23 ? 212 ASP A OD2   1 
ATOM   1712 N  N     . ARG A 1 216 ? -16.448 -74.501 -26.394 1   175.66 ? 213 ARG A N     1 
ATOM   1713 C  CA    . ARG A 1 216 ? -17.257 -74.386 -27.607 1   175.62 ? 213 ARG A CA    1 
ATOM   1714 C  C     . ARG A 1 216 ? -16.66  -73.311 -28.528 1   175.79 ? 213 ARG A C     1 
ATOM   1715 O  O     . ARG A 1 216 ? -16.031 -72.377 -28.038 1   175.86 ? 213 ARG A O     1 
ATOM   1716 C  CB    . ARG A 1 216 ? -18.708 -74.042 -27.222 1   176.46 ? 213 ARG A CB    1 
ATOM   1717 C  CG    . ARG A 1 216 ? -19.693 -73.975 -28.385 1   178.7  ? 213 ARG A CG    1 
ATOM   1718 C  CD    . ARG A 1 216 ? -21.117 -74.266 -27.953 1   181.14 ? 213 ARG A CD    1 
ATOM   1719 N  NE    . ARG A 1 216 ? -21.601 -73.319 -26.95  1   182.91 ? 213 ARG A NE    1 
ATOM   1720 C  CZ    . ARG A 1 216 ? -22.513 -72.382 -27.177 1   184.32 ? 213 ARG A CZ    1 
ATOM   1721 N  NH1   . ARG A 1 216 ? -23.05  -72.245 -28.384 1   183.62 ? 213 ARG A NH1   1 
ATOM   1722 N  NH2   . ARG A 1 216 ? -22.899 -71.575 -26.199 1   184.22 ? 213 ARG A NH2   1 
ATOM   1723 N  N     . VAL A 1 217 ? -16.812 -73.454 -29.86  1   175.76 ? 214 VAL A N     1 
ATOM   1724 C  CA    . VAL A 1 217 ? -16.274 -72.486 -30.826 1   176.14 ? 214 VAL A CA    1 
ATOM   1725 C  C     . VAL A 1 217 ? -17.322 -72.119 -31.902 1   176.06 ? 214 VAL A C     1 
ATOM   1726 O  O     . VAL A 1 217 ? -18     -73.003 -32.42  1   176.38 ? 214 VAL A O     1 
ATOM   1727 C  CB    . VAL A 1 217 ? -14.95  -72.999 -31.46  1   177.08 ? 214 VAL A CB    1 
ATOM   1728 C  CG1   . VAL A 1 217 ? -14.521 -72.139 -32.641 1   177.71 ? 214 VAL A CG1   1 
ATOM   1729 C  CG2   . VAL A 1 217 ? -13.832 -73.076 -30.434 1   177.62 ? 214 VAL A CG2   1 
ATOM   1730 N  N     . SER A 1 218 ? -17.453 -70.823 -32.23  1   175.48 ? 215 SER A N     1 
ATOM   1731 C  CA    . SER A 1 218 ? -18.38  -70.37  -33.261 1   175.54 ? 215 SER A CA    1 
ATOM   1732 C  C     . SER A 1 218 ? -17.608 -69.681 -34.365 1   175.81 ? 215 SER A C     1 
ATOM   1733 O  O     . SER A 1 218 ? -16.793 -68.812 -34.088 1   175.67 ? 215 SER A O     1 
ATOM   1734 C  CB    . SER A 1 218 ? -19.41  -69.413 -32.68  1   176.41 ? 215 SER A CB    1 
ATOM   1735 O  OG    . SER A 1 218 ? -20.335 -70.122 -31.875 1   178.3  ? 215 SER A OG    1 
ATOM   1736 N  N     . LEU A 1 219 ? -17.851 -70.067 -35.611 1   176.18 ? 216 LEU A N     1 
ATOM   1737 C  CA    . LEU A 1 219 ? -17.151 -69.505 -36.762 1   177.08 ? 216 LEU A CA    1 
ATOM   1738 C  C     . LEU A 1 219 ? -17.953 -68.375 -37.393 1   177.67 ? 216 LEU A C     1 
ATOM   1739 O  O     . LEU A 1 219 ? -19.026 -68.608 -37.937 1   177.8  ? 216 LEU A O     1 
ATOM   1740 C  CB    . LEU A 1 219 ? -16.87  -70.628 -37.795 1   177.57 ? 216 LEU A CB    1 
ATOM   1741 C  CG    . LEU A 1 219 ? -16.011 -70.368 -39.061 1   179.33 ? 216 LEU A CG    1 
ATOM   1742 C  CD1   . LEU A 1 219 ? -16.861 -70.076 -40.283 1   179.93 ? 216 LEU A CD1   1 
ATOM   1743 C  CD2   . LEU A 1 219 ? -14.917 -69.338 -38.846 1   180.06 ? 216 LEU A CD2   1 
ATOM   1744 N  N     . ILE A 1 220 ? -17.418 -67.153 -37.339 1   177.92 ? 217 ILE A N     1 
ATOM   1745 C  CA    . ILE A 1 220 ? -18.041 -65.984 -37.946 1   178.52 ? 217 ILE A CA    1 
ATOM   1746 C  C     . ILE A 1 220 ? -17.361 -65.671 -39.262 1   178.8  ? 217 ILE A C     1 
ATOM   1747 O  O     . ILE A 1 220 ? -16.155 -65.448 -39.302 1   178.77 ? 217 ILE A O     1 
ATOM   1748 C  CB    . ILE A 1 220 ? -18.042 -64.766 -36.999 1   179.14 ? 217 ILE A CB    1 
ATOM   1749 C  CG1   . ILE A 1 220 ? -18.917 -65.077 -35.768 1   180.23 ? 217 ILE A CG1   1 
ATOM   1750 C  CG2   . ILE A 1 220 ? -18.504 -63.498 -37.744 1   179.54 ? 217 ILE A CG2   1 
ATOM   1751 C  CD1   . ILE A 1 220 ? -19.132 -63.968 -34.816 1   181.62 ? 217 ILE A CD1   1 
ATOM   1752 N  N     . CYS A 1 221 ? -18.138 -65.686 -40.34  1   178.89 ? 218 CYS A N     1 
ATOM   1753 C  CA    . CYS A 1 221 ? -17.658 -65.392 -41.679 1   179.4  ? 218 CYS A CA    1 
ATOM   1754 C  C     . CYS A 1 221 ? -18.6   -64.327 -42.254 1   179.62 ? 218 CYS A C     1 
ATOM   1755 O  O     . CYS A 1 221 ? -19.8   -64.583 -42.355 1   179.86 ? 218 CYS A O     1 
ATOM   1756 C  CB    . CYS A 1 221 ? -17.659 -66.663 -42.53  1   180.09 ? 218 CYS A CB    1 
ATOM   1757 S  SG    . CYS A 1 221 ? -16.085 -67.016 -43.36  1   183.22 ? 218 CYS A SG    1 
ATOM   1758 N  N     . ALA A 1 222 ? -18.069 -63.127 -42.579 1   179.31 ? 219 ALA A N     1 
ATOM   1759 C  CA    . ALA A 1 222 ? -18.818 -61.993 -43.136 1   179.54 ? 219 ALA A CA    1 
ATOM   1760 C  C     . ALA A 1 222 ? -20.094 -61.63  -42.36  1   179.62 ? 219 ALA A C     1 
ATOM   1761 O  O     . ALA A 1 222 ? -21.169 -61.48  -42.937 1   179.62 ? 219 ALA A O     1 
ATOM   1762 C  CB    . ALA A 1 222 ? -19.127 -62.225 -44.609 1   179.76 ? 219 ALA A CB    1 
ATOM   1763 N  N     . GLY A 1 223 ? -19.955 -61.502 -41.052 1   179.62 ? 220 GLY A N     1 
ATOM   1764 C  CA    . GLY A 1 223 ? -21.058 -61.13  -40.176 1   180.13 ? 220 GLY A CA    1 
ATOM   1765 C  C     . GLY A 1 223 ? -22.105 -62.198 -39.917 1   180.41 ? 220 GLY A C     1 
ATOM   1766 O  O     . GLY A 1 223 ? -23.22  -61.874 -39.5   1   180.79 ? 220 GLY A O     1 
ATOM   1767 N  N     . GLU A 1 224 ? -21.771 -63.476 -40.147 1   180    ? 221 GLU A N     1 
ATOM   1768 C  CA    . GLU A 1 224 ? -22.726 -64.561 -39.919 1   180.01 ? 221 GLU A CA    1 
ATOM   1769 C  C     . GLU A 1 224 ? -22.063 -65.753 -39.241 1   180.12 ? 221 GLU A C     1 
ATOM   1770 O  O     . GLU A 1 224 ? -20.938 -66.102 -39.59  1   180.32 ? 221 GLU A O     1 
ATOM   1771 C  CB    . GLU A 1 224 ? -23.366 -65.007 -41.241 1   181.57 ? 221 GLU A CB    1 
ATOM   1772 C  CG    . GLU A 1 224 ? -24.489 -64.11  -41.729 1   184.86 ? 221 GLU A CG    1 
ATOM   1773 C  CD    . GLU A 1 224 ? -24.979 -64.423 -43.13  1   189.26 ? 221 GLU A CD    1 
ATOM   1774 O  OE1   . GLU A 1 224 ? -24.68  -65.528 -43.636 1   190.25 ? 221 GLU A OE1   1 
ATOM   1775 O  OE2   . GLU A 1 224 ? -25.653 -63.556 -43.729 1   190.6  ? 221 GLU A OE2   1 
ATOM   1776 N  N     . VAL A 1 225 ? -22.758 -66.39  -38.288 1   179.83 ? 222 VAL A N     1 
ATOM   1777 C  CA    . VAL A 1 225 ? -22.212 -67.564 -37.611 1   180.08 ? 222 VAL A CA    1 
ATOM   1778 C  C     . VAL A 1 225 ? -22.507 -68.812 -38.452 1   180.47 ? 222 VAL A C     1 
ATOM   1779 O  O     . VAL A 1 225 ? -23.614 -69.351 -38.402 1   180.59 ? 222 VAL A O     1 
ATOM   1780 C  CB    . VAL A 1 225 ? -22.723 -67.698 -36.162 1   180.59 ? 222 VAL A CB    1 
ATOM   1781 C  CG1   . VAL A 1 225 ? -22.06  -68.873 -35.462 1   181.15 ? 222 VAL A CG1   1 
ATOM   1782 C  CG2   . VAL A 1 225 ? -22.477 -66.417 -35.384 1   180.94 ? 222 VAL A CG2   1 
ATOM   1783 N  N     . ILE A 1 226 ? -21.518 -69.246 -39.25  1   180.48 ? 223 ILE A N     1 
ATOM   1784 C  CA    . ILE A 1 226 ? -21.636 -70.39  -40.156 1   180.97 ? 223 ILE A CA    1 
ATOM   1785 C  C     . ILE A 1 226 ? -21.735 -71.755 -39.411 1   181.38 ? 223 ILE A C     1 
ATOM   1786 O  O     . ILE A 1 226 ? -22.774 -72.411 -39.497 1   181.52 ? 223 ILE A O     1 
ATOM   1787 C  CB    . ILE A 1 226 ? -20.501 -70.364 -41.216 1   181.41 ? 223 ILE A CB    1 
ATOM   1788 C  CG1   . ILE A 1 226 ? -20.46  -69.035 -41.992 1   182.21 ? 223 ILE A CG1   1 
ATOM   1789 C  CG2   . ILE A 1 226 ? -20.595 -71.56  -42.144 1   181.97 ? 223 ILE A CG2   1 
ATOM   1790 C  CD1   . ILE A 1 226 ? -21.744 -68.607 -42.64  1   183.44 ? 223 ILE A CD1   1 
ATOM   1791 N  N     . LYS A 1 227 ? -20.679 -72.183 -38.691 1   181.38 ? 224 LYS A N     1 
ATOM   1792 C  CA    . LYS A 1 227 ? -20.711 -73.443 -37.943 1   181.8  ? 224 LYS A CA    1 
ATOM   1793 C  C     . LYS A 1 227 ? -20.397 -73.201 -36.464 1   182.43 ? 224 LYS A C     1 
ATOM   1794 O  O     . LYS A 1 227 ? -19.721 -72.233 -36.122 1   182.62 ? 224 LYS A O     1 
ATOM   1795 C  CB    . LYS A 1 227 ? -19.748 -74.482 -38.543 1   183.04 ? 224 LYS A CB    1 
ATOM   1796 C  CG    . LYS A 1 227 ? -20.428 -75.79  -38.949 1   185.86 ? 224 LYS A CG    1 
ATOM   1797 C  CD    . LYS A 1 227 ? -21.092 -75.699 -40.322 1   189.03 ? 224 LYS A CD    1 
ATOM   1798 C  CE    . LYS A 1 227 ? -20.105 -75.457 -41.442 1   191.73 ? 224 LYS A CE    1 
ATOM   1799 N  NZ    . LYS A 1 227 ? -20.781 -74.984 -42.68  1   193.19 ? 224 LYS A NZ    1 
ATOM   1800 N  N     . SER A 1 228 ? -20.9   -74.07  -35.585 1   182.61 ? 225 SER A N     1 
ATOM   1801 C  CA    . SER A 1 228 ? -20.682 -73.924 -34.148 1   183.29 ? 225 SER A CA    1 
ATOM   1802 C  C     . SER A 1 228 ? -20.721 -75.27  -33.435 1   183.64 ? 225 SER A C     1 
ATOM   1803 O  O     . SER A 1 228 ? -21.392 -76.199 -33.886 1   183.8  ? 225 SER A O     1 
ATOM   1804 C  CB    . SER A 1 228 ? -21.743 -73.012 -33.536 1   184.75 ? 225 SER A CB    1 
ATOM   1805 O  OG    . SER A 1 228 ? -21.544 -71.649 -33.858 1   186.94 ? 225 SER A OG    1 
ATOM   1806 N  N     . GLY A 1 229 ? -20.026 -75.354 -32.31  1   183.62 ? 226 GLY A N     1 
ATOM   1807 C  CA    . GLY A 1 229 ? -20.02  -76.565 -31.505 1   184.16 ? 226 GLY A CA    1 
ATOM   1808 C  C     . GLY A 1 229 ? -18.654 -77.007 -31.035 1   184.5  ? 226 GLY A C     1 
ATOM   1809 O  O     . GLY A 1 229 ? -17.983 -76.295 -30.286 1   184.62 ? 226 GLY A O     1 
ATOM   1810 N  N     . ASP A 1 230 ? -18.254 -78.212 -31.442 1   184.47 ? 227 ASP A N     1 
ATOM   1811 C  CA    . ASP A 1 230 ? -16.973 -78.803 -31.072 1   184.92 ? 227 ASP A CA    1 
ATOM   1812 C  C     . ASP A 1 230 ? -15.832 -77.973 -31.679 1   185.27 ? 227 ASP A C     1 
ATOM   1813 O  O     . ASP A 1 230 ? -15.851 -77.664 -32.865 1   185.38 ? 227 ASP A O     1 
ATOM   1814 C  CB    . ASP A 1 230 ? -16.909 -80.263 -31.57  1   186.26 ? 227 ASP A CB    1 
ATOM   1815 C  CG    . ASP A 1 230 ? -16.631 -81.323 -30.523 1   189.84 ? 227 ASP A CG    1 
ATOM   1816 O  OD1   . ASP A 1 230 ? -15.615 -81.203 -29.814 1   190.32 ? 227 ASP A OD1   1 
ATOM   1817 O  OD2   . ASP A 1 230 ? -17.414 -82.295 -30.441 1   191.68 ? 227 ASP A OD2   1 
ATOM   1818 N  N     . PRO A 1 231 ? -14.833 -77.602 -30.867 1   185.25 ? 228 PRO A N     1 
ATOM   1819 C  CA    . PRO A 1 231 ? -13.719 -76.792 -31.387 1   185.4  ? 228 PRO A CA    1 
ATOM   1820 C  C     . PRO A 1 231 ? -12.949 -77.405 -32.574 1   185.89 ? 228 PRO A C     1 
ATOM   1821 O  O     . PRO A 1 231 ? -12.559 -76.671 -33.479 1   185.9  ? 228 PRO A O     1 
ATOM   1822 C  CB    . PRO A 1 231 ? -12.836 -76.586 -30.149 1   185.94 ? 228 PRO A CB    1 
ATOM   1823 C  CG    . PRO A 1 231 ? -13.757 -76.79  -28.98  1   186.33 ? 228 PRO A CG    1 
ATOM   1824 C  CD    . PRO A 1 231 ? -14.688 -77.865 -29.423 1   184.76 ? 228 PRO A CD    1 
ATOM   1825 N  N     . LYS A 1 232 ? -12.765 -78.741 -32.594 1   186.19 ? 229 LYS A N     1 
ATOM   1826 C  CA    . LYS A 1 232 ? -12.065 -79.458 -33.674 1   187.01 ? 229 LYS A CA    1 
ATOM   1827 C  C     . LYS A 1 232 ? -12.908 -79.62  -34.957 1   187.48 ? 229 LYS A C     1 
ATOM   1828 O  O     . LYS A 1 232 ? -12.354 -79.561 -36.058 1   187.51 ? 229 LYS A O     1 
ATOM   1829 C  CB    . LYS A 1 232 ? -11.541 -80.824 -33.199 1   188.97 ? 229 LYS A CB    1 
ATOM   1830 C  CG    . LYS A 1 232 ? -10.419 -80.733 -32.174 1   193.16 ? 229 LYS A CG    1 
ATOM   1831 C  CD    . LYS A 1 232 ? -10.933 -80.588 -30.748 1   197.7  ? 229 LYS A CD    1 
ATOM   1832 C  CE    . LYS A 1 232 ? -9.902  -79.947 -29.856 1   201.56 ? 229 LYS A CE    1 
ATOM   1833 N  NZ    . LYS A 1 232 ? -10.505 -79.424 -28.602 1   204    ? 229 LYS A NZ    1 
ATOM   1834 N  N     . GLU A 1 233 ? -14.241 -79.815 -34.822 1   187.67 ? 230 GLU A N     1 
ATOM   1835 C  CA    . GLU A 1 233 ? -15.131 -79.93  -35.989 1   188.27 ? 230 GLU A CA    1 
ATOM   1836 C  C     . GLU A 1 233 ? -15.253 -78.589 -36.713 1   188.64 ? 230 GLU A C     1 
ATOM   1837 O  O     . GLU A 1 233 ? -15.008 -78.523 -37.916 1   188.78 ? 230 GLU A O     1 
ATOM   1838 C  CB    . GLU A 1 233 ? -16.532 -80.506 -35.64  1   190.37 ? 230 GLU A CB    1 
ATOM   1839 C  CG    . GLU A 1 233 ? -17.44  -79.621 -34.79  1   194.5  ? 230 GLU A CG    1 
ATOM   1840 C  CD    . GLU A 1 233 ? -18.77  -79.124 -35.34  1   199.18 ? 230 GLU A CD    1 
ATOM   1841 O  OE1   . GLU A 1 233 ? -18.791 -78.598 -36.476 1   199.99 ? 230 GLU A OE1   1 
ATOM   1842 O  OE2   . GLU A 1 233 ? -19.779 -79.204 -34.603 1   200.49 ? 230 GLU A OE2   1 
ATOM   1843 N  N     . VAL A 1 234 ? -15.575 -77.515 -35.978 1   188.62 ? 231 VAL A N     1 
ATOM   1844 C  CA    . VAL A 1 234 ? -15.687 -76.194 -36.574 1   189.06 ? 231 VAL A CA    1 
ATOM   1845 C  C     . VAL A 1 234 ? -14.304 -75.661 -37.021 1   189.63 ? 231 VAL A C     1 
ATOM   1846 O  O     . VAL A 1 234 ? -14.223 -74.925 -38.002 1   189.77 ? 231 VAL A O     1 
ATOM   1847 C  CB    . VAL A 1 234 ? -16.466 -75.237 -35.657 1   189.61 ? 231 VAL A CB    1 
ATOM   1848 C  CG1   . VAL A 1 234 ? -15.753 -75.028 -34.339 1   190.15 ? 231 VAL A CG1   1 
ATOM   1849 C  CG2   . VAL A 1 234 ? -16.735 -73.916 -36.344 1   190.03 ? 231 VAL A CG2   1 
ATOM   1850 N  N     . GLY A 1 235 ? -13.234 -76.122 -36.369 1   189.85 ? 232 GLY A N     1 
ATOM   1851 C  CA    . GLY A 1 235 ? -11.862 -75.811 -36.741 1   190.61 ? 232 GLY A CA    1 
ATOM   1852 C  C     . GLY A 1 235 ? -11.497 -76.437 -38.076 1   191.15 ? 232 GLY A C     1 
ATOM   1853 O  O     . GLY A 1 235 ? -10.876 -75.775 -38.909 1   191.45 ? 232 GLY A O     1 
ATOM   1854 N  N     . GLU A 1 236 ? -11.918 -77.7   -38.32  1   191.1  ? 233 GLU A N     1 
ATOM   1855 C  CA    . GLU A 1 236 ? -11.682 -78.382 -39.606 1   191.53 ? 233 GLU A CA    1 
ATOM   1856 C  C     . GLU A 1 236 ? -12.447 -77.694 -40.757 1   191.62 ? 233 GLU A C     1 
ATOM   1857 O  O     . GLU A 1 236 ? -11.977 -77.67  -41.896 1   191.66 ? 233 GLU A O     1 
ATOM   1858 C  CB    . GLU A 1 236 ? -12.084 -79.862 -39.533 1   193.69 ? 233 GLU A CB    1 
ATOM   1859 C  CG    . GLU A 1 236 ? -11.014 -80.771 -38.961 1   198.17 ? 233 GLU A CG    1 
ATOM   1860 C  CD    . GLU A 1 236 ? -11.082 -82.2   -39.471 1   203.77 ? 233 GLU A CD    1 
ATOM   1861 O  OE1   . GLU A 1 236 ? -11.708 -82.434 -40.53  1   204.74 ? 233 GLU A OE1   1 
ATOM   1862 O  OE2   . GLU A 1 236 ? -10.495 -83.088 -38.812 1   205.63 ? 233 GLU A OE2   1 
ATOM   1863 N  N     . PHE A 1 237 ? -13.62  -77.13  -40.452 1   191.38 ? 234 PHE A N     1 
ATOM   1864 C  CA    . PHE A 1 237 ? -14.414 -76.416 -41.44  1   191.59 ? 234 PHE A CA    1 
ATOM   1865 C  C     . PHE A 1 237 ? -13.783 -75.061 -41.786 1   191.68 ? 234 PHE A C     1 
ATOM   1866 O  O     . PHE A 1 237 ? -13.832 -74.656 -42.943 1   191.67 ? 234 PHE A O     1 
ATOM   1867 C  CB    . PHE A 1 237 ? -15.864 -76.271 -40.959 1   191.56 ? 234 PHE A CB    1 
ATOM   1868 C  CG    . PHE A 1 237 ? -16.583 -77.594 -40.812 1   192.37 ? 234 PHE A CG    1 
ATOM   1869 C  CD1   . PHE A 1 237 ? -16.3   -78.656 -41.657 1   193.26 ? 234 PHE A CD1   1 
ATOM   1870 C  CD2   . PHE A 1 237 ? -17.547 -77.773 -39.84  1   193.24 ? 234 PHE A CD2   1 
ATOM   1871 C  CE1   . PHE A 1 237 ? -16.948 -79.875 -41.512 1   193.96 ? 234 PHE A CE1   1 
ATOM   1872 C  CE2   . PHE A 1 237 ? -18.199 -78.992 -39.704 1   194.01 ? 234 PHE A CE2   1 
ATOM   1873 C  CZ    . PHE A 1 237 ? -17.896 -80.034 -40.54  1   193.78 ? 234 PHE A CZ    1 
ATOM   1874 N  N     . TYR A 1 238 ? -13.153 -74.39  -40.789 1   191.63 ? 235 TYR A N     1 
ATOM   1875 C  CA    . TYR A 1 238 ? -12.452 -73.093 -40.911 1   191.92 ? 235 TYR A CA    1 
ATOM   1876 C  C     . TYR A 1 238 ? -11.206 -73.222 -41.802 1   192.01 ? 235 TYR A C     1 
ATOM   1877 O  O     . TYR A 1 238 ? -10.919 -72.32  -42.583 1   192.05 ? 235 TYR A O     1 
ATOM   1878 C  CB    . TYR A 1 238 ? -12.095 -72.552 -39.502 1   191.97 ? 235 TYR A CB    1 
ATOM   1879 C  CG    . TYR A 1 238 ? -11.3   -71.259 -39.423 1   192.68 ? 235 TYR A CG    1 
ATOM   1880 C  CD1   . TYR A 1 238 ? -11.682 -70.135 -40.145 1   193.54 ? 235 TYR A CD1   1 
ATOM   1881 C  CD2   . TYR A 1 238 ? -10.26  -71.117 -38.514 1   193.57 ? 235 TYR A CD2   1 
ATOM   1882 C  CE1   . TYR A 1 238 ? -10.987 -68.931 -40.036 1   194.43 ? 235 TYR A CE1   1 
ATOM   1883 C  CE2   . TYR A 1 238 ? -9.568  -69.916 -38.384 1   194.46 ? 235 TYR A CE2   1 
ATOM   1884 C  CZ    . TYR A 1 238 ? -9.936  -68.822 -39.144 1   195.29 ? 235 TYR A CZ    1 
ATOM   1885 O  OH    . TYR A 1 238 ? -9.232  -67.645 -39.025 1   196.61 ? 235 TYR A OH    1 
ATOM   1886 N  N     . LYS A 1 239 ? -10.501 -74.368 -41.724 1   191.84 ? 236 LYS A N     1 
ATOM   1887 C  CA    . LYS A 1 239 ? -9.325  -74.662 -42.554 1   192.07 ? 236 LYS A CA    1 
ATOM   1888 C  C     . LYS A 1 239 ? -9.696  -74.802 -44.041 1   192.16 ? 236 LYS A C     1 
ATOM   1889 O  O     . LYS A 1 239 ? -8.856  -74.548 -44.907 1   192.26 ? 236 LYS A O     1 
ATOM   1890 C  CB    . LYS A 1 239 ? -8.654  -75.975 -42.101 1   193.58 ? 236 LYS A CB    1 
ATOM   1891 C  CG    . LYS A 1 239 ? -7.987  -75.933 -40.729 1   196.87 ? 236 LYS A CG    1 
ATOM   1892 C  CD    . LYS A 1 239 ? -7.606  -77.336 -40.216 1   200.34 ? 236 LYS A CD    1 
ATOM   1893 C  CE    . LYS A 1 239 ? -6.935  -78.245 -41.23  1   203.52 ? 236 LYS A CE    1 
ATOM   1894 N  NZ    . LYS A 1 239 ? -5.647  -77.692 -41.723 1   205.6  ? 236 LYS A NZ    1 
ATOM   1895 N  N     . LYS A 1 240 ? -10.929 -75.235 -44.338 1   191.89 ? 237 LYS A N     1 
ATOM   1896 C  CA    . LYS A 1 240 ? -11.342 -75.442 -45.718 1   192.04 ? 237 LYS A CA    1 
ATOM   1897 C  C     . LYS A 1 240 ? -12.195 -74.306 -46.305 1   192.16 ? 237 LYS A C     1 
ATOM   1898 O  O     . LYS A 1 240 ? -11.873 -73.795 -47.376 1   192.22 ? 237 LYS A O     1 
ATOM   1899 C  CB    . LYS A 1 240 ? -12.044 -76.802 -45.872 1   193.44 ? 237 LYS A CB    1 
ATOM   1900 C  CG    . LYS A 1 240 ? -11.068 -77.958 -46.088 1   196.46 ? 237 LYS A CG    1 
ATOM   1901 C  CD    . LYS A 1 240 ? -10.462 -78.461 -44.784 1   199.6  ? 237 LYS A CD    1 
ATOM   1902 C  CE    . LYS A 1 240 ? -9.066  -79.002 -44.964 1   202.35 ? 237 LYS A CE    1 
ATOM   1903 N  NZ    . LYS A 1 240 ? -8.088  -77.922 -45.246 1   204.16 ? 237 LYS A NZ    1 
ATOM   1904 N  N     . GLU A 1 241 ? -13.272 -73.911 -45.62  1   192.02 ? 238 GLU A N     1 
ATOM   1905 C  CA    . GLU A 1 241 ? -14.196 -72.897 -46.127 1   192.38 ? 238 GLU A CA    1 
ATOM   1906 C  C     . GLU A 1 241 ? -13.841 -71.447 -45.773 1   192.77 ? 238 GLU A C     1 
ATOM   1907 O  O     . GLU A 1 241 ? -13.318 -71.18  -44.699 1   192.89 ? 238 GLU A O     1 
ATOM   1908 C  CB    . GLU A 1 241 ? -15.631 -73.217 -45.656 1   194.05 ? 238 GLU A CB    1 
ATOM   1909 C  CG    . GLU A 1 241 ? -16.719 -72.704 -46.59  1   197.32 ? 238 GLU A CG    1 
ATOM   1910 C  CD    . GLU A 1 241 ? -18.118 -72.629 -46.006 1   201.19 ? 238 GLU A CD    1 
ATOM   1911 O  OE1   . GLU A 1 241 ? -18.933 -71.829 -46.52  1   201.42 ? 238 GLU A OE1   1 
ATOM   1912 O  OE2   . GLU A 1 241 ? -18.4   -73.363 -45.031 1   202.74 ? 238 GLU A OE2   1 
ATOM   1913 N  N     . CYS A 1 242 ? -14.168 -70.502 -46.666 1   192.84 ? 239 CYS A N     1 
ATOM   1914 C  CA    . CYS A 1 242 ? -13.954 -69.079 -46.41  1   193.38 ? 239 CYS A CA    1 
ATOM   1915 C  C     . CYS A 1 242 ? -15.033 -68.23  -47.073 1   193.71 ? 239 CYS A C     1 
ATOM   1916 O  O     . CYS A 1 242 ? -14.993 -68.025 -48.283 1   193.82 ? 239 CYS A O     1 
ATOM   1917 C  CB    . CYS A 1 242 ? -12.558 -68.631 -46.829 1   194.07 ? 239 CYS A CB    1 
ATOM   1918 S  SG    . CYS A 1 242 ? -12.216 -66.883 -46.49  1   196.9  ? 239 CYS A SG    1 
ATOM   1919 N  N     . LYS B 2 28  ? 21.34   -28.122 7.539   1   222.08 ? 28  LYS B N     1 
ATOM   1920 C  CA    . LYS B 2 28  ? 20.241  -29.047 7.248   1   222.54 ? 28  LYS B CA    1 
ATOM   1921 C  C     . LYS B 2 28  ? 19.985  -29.258 5.74    1   223.12 ? 28  LYS B C     1 
ATOM   1922 O  O     . LYS B 2 28  ? 19.008  -29.909 5.387   1   223.15 ? 28  LYS B O     1 
ATOM   1923 C  CB    . LYS B 2 28  ? 18.94   -28.575 7.927   1   223.9  ? 28  LYS B CB    1 
ATOM   1924 C  CG    . LYS B 2 28  ? 19.089  -28.183 9.391   1   226.99 ? 28  LYS B CG    1 
ATOM   1925 C  CD    . LYS B 2 28  ? 17.849  -27.458 9.887   1   230.31 ? 28  LYS B CD    1 
ATOM   1926 C  CE    . LYS B 2 28  ? 18.058  -26.848 11.247  1   233.31 ? 28  LYS B CE    1 
ATOM   1927 N  NZ    . LYS B 2 28  ? 16.884  -26.045 11.667  1   235.21 ? 28  LYS B NZ    1 
ATOM   1928 N  N     . GLY B 2 29  ? 20.841  -28.709 4.878   1   223.45 ? 29  GLY B N     1 
ATOM   1929 C  CA    . GLY B 2 29  ? 20.695  -28.805 3.43    1   224.24 ? 29  GLY B CA    1 
ATOM   1930 C  C     . GLY B 2 29  ? 20.88   -27.459 2.756   1   224.89 ? 29  GLY B C     1 
ATOM   1931 O  O     . GLY B 2 29  ? 20.497  -26.425 3.311   1   225.12 ? 29  GLY B O     1 
ATOM   1932 N  N     . PRO B 2 30  ? 21.492  -27.428 1.561   1   224.97 ? 30  PRO B N     1 
ATOM   1933 C  CA    . PRO B 2 30  ? 21.708  -26.135 0.881   1   225.19 ? 30  PRO B CA    1 
ATOM   1934 C  C     . PRO B 2 30  ? 20.394  -25.544 0.38    1   225.49 ? 30  PRO B C     1 
ATOM   1935 O  O     . PRO B 2 30  ? 19.867  -25.997 -0.632  1   225.65 ? 30  PRO B O     1 
ATOM   1936 C  CB    . PRO B 2 30  ? 22.655  -26.491 -0.273  1   225.83 ? 30  PRO B CB    1 
ATOM   1937 C  CG    . PRO B 2 30  ? 23.123  -27.912 0.002   1   226.22 ? 30  PRO B CG    1 
ATOM   1938 C  CD    . PRO B 2 30  ? 22.027  -28.555 0.778   1   224.53 ? 30  PRO B CD    1 
ATOM   1939 N  N     . ARG B 2 31  ? 19.827  -24.58  1.124   1   225.48 ? 31  ARG B N     1 
ATOM   1940 C  CA    . ARG B 2 31  ? 18.519  -24.021 0.786   1   225.99 ? 31  ARG B CA    1 
ATOM   1941 C  C     . ARG B 2 31  ? 18.468  -22.47  0.842   1   226.4  ? 31  ARG B C     1 
ATOM   1942 O  O     . ARG B 2 31  ? 19.329  -21.832 1.457   1   226.46 ? 31  ARG B O     1 
ATOM   1943 C  CB    . ARG B 2 31  ? 17.434  -24.64  1.714   1   227.21 ? 31  ARG B CB    1 
ATOM   1944 C  CG    . ARG B 2 31  ? 17.524  -26.169 1.909   1   229.77 ? 31  ARG B CG    1 
ATOM   1945 C  CD    . ARG B 2 31  ? 16.62   -26.71  3.011   1   232.2  ? 31  ARG B CD    1 
ATOM   1946 N  NE    . ARG B 2 31  ? 17.026  -28.048 3.46    1   234.11 ? 31  ARG B NE    1 
ATOM   1947 C  CZ    . ARG B 2 31  ? 16.348  -29.165 3.213   1   235.66 ? 31  ARG B CZ    1 
ATOM   1948 N  NH1   . ARG B 2 31  ? 15.217  -29.124 2.523   1   235.34 ? 31  ARG B NH1   1 
ATOM   1949 N  NH2   . ARG B 2 31  ? 16.793  -30.33  3.662   1   235.31 ? 31  ARG B NH2   1 
ATOM   1950 N  N     . ILE B 2 32  ? 17.449  -21.877 0.181   1   226.54 ? 32  ILE B N     1 
ATOM   1951 C  CA    . ILE B 2 32  ? 17.184  -20.431 0.165   1   227.18 ? 32  ILE B CA    1 
ATOM   1952 C  C     . ILE B 2 32  ? 15.74   -20.217 0.623   1   227.75 ? 32  ILE B C     1 
ATOM   1953 O  O     . ILE B 2 32  ? 14.805  -20.51  -0.125  1   227.82 ? 32  ILE B O     1 
ATOM   1954 C  CB    . ILE B 2 32  ? 17.411  -19.8   -1.229  1   227.67 ? 32  ILE B CB    1 
ATOM   1955 C  CG1   . ILE B 2 32  ? 18.88   -19.904 -1.662  1   228.57 ? 32  ILE B CG1   1 
ATOM   1956 C  CG2   . ILE B 2 32  ? 16.916  -18.345 -1.269  1   228.16 ? 32  ILE B CG2   1 
ATOM   1957 C  CD1   . ILE B 2 32  ? 19.829  -19.144 -0.813  1   229.73 ? 32  ILE B CD1   1 
ATOM   1958 N  N     . ILE B 2 33  ? 15.552  -19.731 1.853   1   228.01 ? 33  ILE B N     1 
ATOM   1959 C  CA    . ILE B 2 33  ? 14.21   -19.531 2.396   1   228.66 ? 33  ILE B CA    1 
ATOM   1960 C  C     . ILE B 2 33  ? 13.74   -18.081 2.265   1   229.12 ? 33  ILE B C     1 
ATOM   1961 O  O     . ILE B 2 33  ? 14.488  -17.164 2.594   1   229.28 ? 33  ILE B O     1 
ATOM   1962 C  CB    . ILE B 2 33  ? 14.134  -20.049 3.855   1   229.23 ? 33  ILE B CB    1 
ATOM   1963 C  CG1   . ILE B 2 33  ? 14.557  -21.526 3.937   1   230.16 ? 33  ILE B CG1   1 
ATOM   1964 C  CG2   . ILE B 2 33  ? 12.742  -19.848 4.442   1   229.72 ? 33  ILE B CG2   1 
ATOM   1965 C  CD1   . ILE B 2 33  ? 14.73   -22.053 5.358   1   231.36 ? 33  ILE B CD1   1 
ATOM   1966 N  N     . VAL B 2 34  ? 12.518  -17.875 1.74    1   229.13 ? 34  VAL B N     1 
ATOM   1967 C  CA    . VAL B 2 34  ? 11.913  -16.553 1.582   1   229.62 ? 34  VAL B CA    1 
ATOM   1968 C  C     . VAL B 2 34  ? 10.493  -16.552 2.158   1   229.97 ? 34  VAL B C     1 
ATOM   1969 O  O     . VAL B 2 34  ? 9.564   -17.042 1.517   1   229.99 ? 34  VAL B O     1 
ATOM   1970 C  CB    . VAL B 2 34  ? 11.902  -16.053 0.114   1   230.3  ? 34  VAL B CB    1 
ATOM   1971 C  CG1   . VAL B 2 34  ? 11.236  -14.682 0.011   1   230.85 ? 34  VAL B CG1   1 
ATOM   1972 C  CG2   . VAL B 2 34  ? 13.307  -16.018 -0.477  1   230.77 ? 34  VAL B CG2   1 
ATOM   1973 N  N     . LYS B 2 35  ? 10.326  -16.023 3.372   1   230.14 ? 35  LYS B N     1 
ATOM   1974 C  CA    . LYS B 2 35  ? 9.006   -15.92  3.988   1   230.78 ? 35  LYS B CA    1 
ATOM   1975 C  C     . LYS B 2 35  ? 8.579   -14.463 3.822   1   231.47 ? 35  LYS B C     1 
ATOM   1976 O  O     . LYS B 2 35  ? 9.333   -13.572 4.214   1   231.71 ? 35  LYS B O     1 
ATOM   1977 C  CB    . LYS B 2 35  ? 9.062   -16.309 5.476   1   232.22 ? 35  LYS B CB    1 
ATOM   1978 C  CG    . LYS B 2 35  ? 7.699   -16.308 6.165   1   235.49 ? 35  LYS B CG    1 
ATOM   1979 C  CD    . LYS B 2 35  ? 6.907   -17.578 5.861   1   239    ? 35  LYS B CD    1 
ATOM   1980 C  CE    . LYS B 2 35  ? 5.45    -17.552 6.276   1   242.04 ? 35  LYS B CE    1 
ATOM   1981 N  NZ    . LYS B 2 35  ? 5.245   -17.085 7.672   1   243.86 ? 35  LYS B NZ    1 
ATOM   1982 N  N     . GLU B 2 36  ? 7.404   -14.221 3.198   1   231.6  ? 36  GLU B N     1 
ATOM   1983 C  CA    . GLU B 2 36  ? 6.889   -12.879 2.894   1   232.1  ? 36  GLU B CA    1 
ATOM   1984 C  C     . GLU B 2 36  ? 7.785   -12.264 1.772   1   232.27 ? 36  GLU B C     1 
ATOM   1985 O  O     . GLU B 2 36  ? 8.106   -12.98  0.821   1   232.34 ? 36  GLU B O     1 
ATOM   1986 C  CB    . GLU B 2 36  ? 6.775   -12.016 4.184   1   234.24 ? 36  GLU B CB    1 
ATOM   1987 C  CG    . GLU B 2 36  ? 5.406   -11.997 4.84    1   238.61 ? 36  GLU B CG    1 
ATOM   1988 C  CD    . GLU B 2 36  ? 4.699   -13.332 4.937   1   244.53 ? 36  GLU B CD    1 
ATOM   1989 O  OE1   . GLU B 2 36  ? 5.184   -14.224 5.669   1   245.51 ? 36  GLU B OE1   1 
ATOM   1990 O  OE2   . GLU B 2 36  ? 3.653   -13.487 4.267   1   246.71 ? 36  GLU B OE2   1 
ATOM   1991 N  N     . SER B 2 37  ? 8.191   -10.981 1.861   1   232.07 ? 37  SER B N     1 
ATOM   1992 C  CA    . SER B 2 37  ? 9.096   -10.393 0.873   1   232.27 ? 37  SER B CA    1 
ATOM   1993 C  C     . SER B 2 37  ? 10.514  -10.219 1.456   1   232.1  ? 37  SER B C     1 
ATOM   1994 O  O     . SER B 2 37  ? 11.259  -9.364  0.986   1   232.19 ? 37  SER B O     1 
ATOM   1995 C  CB    . SER B 2 37  ? 8.567   -9.05   0.38    1   233.61 ? 37  SER B CB    1 
ATOM   1996 O  OG    . SER B 2 37  ? 9.13    -8.715  -0.877  1   235.76 ? 37  SER B OG    1 
ATOM   1997 N  N     . ARG B 2 38  ? 10.887  -11.028 2.47    1   231.69 ? 38  ARG B N     1 
ATOM   1998 C  CA    . ARG B 2 38  ? 12.198  -10.952 3.106   1   231.71 ? 38  ARG B CA    1 
ATOM   1999 C  C     . ARG B 2 38  ? 12.952  -12.279 2.996   1   231.51 ? 38  ARG B C     1 
ATOM   2000 O  O     . ARG B 2 38  ? 12.336  -13.346 3.038   1   231.68 ? 38  ARG B O     1 
ATOM   2001 C  CB    . ARG B 2 38  ? 12.063  -10.583 4.594   1   232.91 ? 38  ARG B CB    1 
ATOM   2002 C  CG    . ARG B 2 38  ? 11.365  -9.264  4.879   1   235.56 ? 38  ARG B CG    1 
ATOM   2003 C  CD    . ARG B 2 38  ? 11.171  -9.106  6.373   1   238.3  ? 38  ARG B CD    1 
ATOM   2004 N  NE    . ARG B 2 38  ? 10.582  -7.814  6.726   1   240.74 ? 38  ARG B NE    1 
ATOM   2005 C  CZ    . ARG B 2 38  ? 10.218  -7.465  7.958   1   242.61 ? 38  ARG B CZ    1 
ATOM   2006 N  NH1   . ARG B 2 38  ? 10.371  -8.312  8.968   1   242.2  ? 38  ARG B NH1   1 
ATOM   2007 N  NH2   . ARG B 2 38  ? 9.694   -6.269  8.187   1   242.47 ? 38  ARG B NH2   1 
ATOM   2008 N  N     . ILE B 2 39  ? 14.286  -12.219 2.887   1   230.96 ? 39  ILE B N     1 
ATOM   2009 C  CA    . ILE B 2 39  ? 15.098  -13.434 2.849   1   230.83 ? 39  ILE B CA    1 
ATOM   2010 C  C     . ILE B 2 39  ? 15.262  -13.895 4.289   1   230.45 ? 39  ILE B C     1 
ATOM   2011 O  O     . ILE B 2 39  ? 15.689  -13.107 5.135   1   230.69 ? 39  ILE B O     1 
ATOM   2012 C  CB    . ILE B 2 39  ? 16.492  -13.2   2.221   1   231.35 ? 39  ILE B CB    1 
ATOM   2013 C  CG1   . ILE B 2 39  ? 16.43   -12.363 0.938   1   232.28 ? 39  ILE B CG1   1 
ATOM   2014 C  CG2   . ILE B 2 39  ? 17.203  -14.527 1.998   1   231.79 ? 39  ILE B CG2   1 
ATOM   2015 C  CD1   . ILE B 2 39  ? 17.8    -11.895 0.459   1   233.53 ? 39  ILE B CD1   1 
ATOM   2016 N  N     . ILE B 2 40  ? 14.923  -15.15  4.578   1   229.69 ? 40  ILE B N     1 
ATOM   2017 C  CA    . ILE B 2 40  ? 15.067  -15.679 5.928   1   229.43 ? 40  ILE B CA    1 
ATOM   2018 C  C     . ILE B 2 40  ? 16.464  -16.301 6.061   1   228.77 ? 40  ILE B C     1 
ATOM   2019 O  O     . ILE B 2 40  ? 17.167  -16.016 7.033   1   228.83 ? 40  ILE B O     1 
ATOM   2020 C  CB    . ILE B 2 40  ? 13.869  -16.602 6.321   1   230.07 ? 40  ILE B CB    1 
ATOM   2021 C  CG1   . ILE B 2 40  ? 12.753  -15.796 7.031   1   230.98 ? 40  ILE B CG1   1 
ATOM   2022 C  CG2   . ILE B 2 40  ? 14.295  -17.784 7.202   1   230.64 ? 40  ILE B CG2   1 
ATOM   2023 C  CD1   . ILE B 2 40  ? 12.214  -14.584 6.3     1   232.2  ? 40  ILE B CD1   1 
ATOM   2024 N  N     . ASP B 2 41  ? 16.899  -17.076 5.048   1   227.96 ? 41  ASP B N     1 
ATOM   2025 C  CA    . ASP B 2 41  ? 18.229  -17.681 5.074   1   227.61 ? 41  ASP B CA    1 
ATOM   2026 C  C     . ASP B 2 41  ? 18.881  -17.811 3.687   1   226.94 ? 41  ASP B C     1 
ATOM   2027 O  O     . ASP B 2 41  ? 18.204  -18.041 2.684   1   226.97 ? 41  ASP B O     1 
ATOM   2028 C  CB    . ASP B 2 41  ? 18.22   -19.029 5.814   1   229.11 ? 41  ASP B CB    1 
ATOM   2029 C  CG    . ASP B 2 41  ? 18.884  -18.965 7.181   1   232.98 ? 41  ASP B CG    1 
ATOM   2030 O  OD1   . ASP B 2 41  ? 19.919  -18.27  7.31    1   233.38 ? 41  ASP B OD1   1 
ATOM   2031 O  OD2   . ASP B 2 41  ? 18.369  -19.605 8.121   1   235.07 ? 41  ASP B OD2   1 
ATOM   2032 N  N     . VAL B 2 42  ? 20.212  -17.643 3.655   1   226.15 ? 42  VAL B N     1 
ATOM   2033 C  CA    . VAL B 2 42  ? 21.056  -17.726 2.461   1   225.76 ? 42  VAL B CA    1 
ATOM   2034 C  C     . VAL B 2 42  ? 22.355  -18.489 2.772   1   225.02 ? 42  VAL B C     1 
ATOM   2035 O  O     . VAL B 2 42  ? 23.354  -17.881 3.164   1   225.06 ? 42  VAL B O     1 
ATOM   2036 C  CB    . VAL B 2 42  ? 21.353  -16.343 1.815   1   226.55 ? 42  VAL B CB    1 
ATOM   2037 C  CG1   . VAL B 2 42  ? 20.261  -15.94  0.832   1   227.11 ? 42  VAL B CG1   1 
ATOM   2038 C  CG2   . VAL B 2 42  ? 21.59   -15.252 2.863   1   227.03 ? 42  VAL B CG2   1 
ATOM   2039 N  N     . GLN B 2 43  ? 22.341  -19.823 2.608   1   224.12 ? 43  GLN B N     1 
ATOM   2040 C  CA    . GLN B 2 43  ? 23.528  -20.63  2.887   1   223.67 ? 43  GLN B CA    1 
ATOM   2041 C  C     . GLN B 2 43  ? 23.941  -21.499 1.707   1   222.82 ? 43  GLN B C     1 
ATOM   2042 O  O     . GLN B 2 43  ? 23.134  -22.275 1.197   1   222.84 ? 43  GLN B O     1 
ATOM   2043 C  CB    . GLN B 2 43  ? 23.337  -21.488 4.146   1   225.15 ? 43  GLN B CB    1 
ATOM   2044 C  CG    . GLN B 2 43  ? 24.649  -22.043 4.689   1   228.14 ? 43  GLN B CG    1 
ATOM   2045 C  CD    . GLN B 2 43  ? 24.444  -22.86  5.936   1   231.89 ? 43  GLN B CD    1 
ATOM   2046 O  OE1   . GLN B 2 43  ? 23.777  -23.899 5.921   1   233.42 ? 43  GLN B OE1   1 
ATOM   2047 N  NE2   . GLN B 2 43  ? 25.022  -22.415 7.044   1   232.05 ? 43  GLN B NE2   1 
ATOM   2048 N  N     . GLY B 2 44  ? 25.202  -21.366 1.301   1   221.92 ? 44  GLY B N     1 
ATOM   2049 C  CA    . GLY B 2 44  ? 25.781  -22.119 0.196   1   221.48 ? 44  GLY B CA    1 
ATOM   2050 C  C     . GLY B 2 44  ? 26.97   -22.966 0.614   1   220.65 ? 44  GLY B C     1 
ATOM   2051 O  O     . GLY B 2 44  ? 27.835  -22.504 1.361   1   220.77 ? 44  GLY B O     1 
ATOM   2052 N  N     . ASP B 2 45  ? 27.027  -24.214 0.128   1   219.63 ? 45  ASP B N     1 
ATOM   2053 C  CA    . ASP B 2 45  ? 28.091  -25.168 0.458   1   219.06 ? 45  ASP B CA    1 
ATOM   2054 C  C     . ASP B 2 45  ? 29.351  -25.023 -0.451  1   218.28 ? 45  ASP B C     1 
ATOM   2055 O  O     . ASP B 2 45  ? 29.451  -24.053 -1.202  1   218.45 ? 45  ASP B O     1 
ATOM   2056 C  CB    . ASP B 2 45  ? 27.515  -26.603 0.452   1   220.37 ? 45  ASP B CB    1 
ATOM   2057 C  CG    . ASP B 2 45  ? 28.038  -27.475 1.575   1   223.96 ? 45  ASP B CG    1 
ATOM   2058 O  OD1   . ASP B 2 45  ? 29.238  -27.369 1.897   1   224.43 ? 45  ASP B OD1   1 
ATOM   2059 O  OD2   . ASP B 2 45  ? 27.245  -28.263 2.133   1   225.82 ? 45  ASP B OD2   1 
ATOM   2060 N  N     . GLU B 2 46  ? 30.324  -25.956 -0.34   1   217.28 ? 46  GLU B N     1 
ATOM   2061 C  CA    . GLU B 2 46  ? 31.561  -25.965 -1.122  1   216.82 ? 46  GLU B CA    1 
ATOM   2062 C  C     . GLU B 2 46  ? 31.249  -26.212 -2.595  1   216.07 ? 46  GLU B C     1 
ATOM   2063 O  O     . GLU B 2 46  ? 30.631  -27.22  -2.919  1   216.19 ? 46  GLU B O     1 
ATOM   2064 C  CB    . GLU B 2 46  ? 32.49   -27.077 -0.597  1   218.83 ? 46  GLU B CB    1 
ATOM   2065 C  CG    . GLU B 2 46  ? 33.744  -27.309 -1.422  1   222.94 ? 46  GLU B CG    1 
ATOM   2066 C  CD    . GLU B 2 46  ? 34.203  -28.753 -1.452  1   228.07 ? 46  GLU B CD    1 
ATOM   2067 O  OE1   . GLU B 2 46  ? 33.336  -29.654 -1.375  1   228.94 ? 46  GLU B OE1   1 
ATOM   2068 O  OE2   . GLU B 2 46  ? 35.428  -28.985 -1.566  1   229.91 ? 46  GLU B OE2   1 
ATOM   2069 N  N     . GLY B 2 47  ? 31.692  -25.312 -3.468  1   215.16 ? 47  GLY B N     1 
ATOM   2070 C  CA    . GLY B 2 47  ? 31.47   -25.442 -4.905  1   214.76 ? 47  GLY B CA    1 
ATOM   2071 C  C     . GLY B 2 47  ? 30.125  -24.956 -5.407  1   214.08 ? 47  GLY B C     1 
ATOM   2072 O  O     . GLY B 2 47  ? 29.804  -25.119 -6.586  1   214.21 ? 47  GLY B O     1 
ATOM   2073 N  N     . ILE B 2 48  ? 29.325  -24.364 -4.518  1   213.2  ? 48  ILE B N     1 
ATOM   2074 C  CA    . ILE B 2 48  ? 28.006  -23.839 -4.84   1   212.85 ? 48  ILE B CA    1 
ATOM   2075 C  C     . ILE B 2 48  ? 27.827  -22.476 -4.134  1   212.12 ? 48  ILE B C     1 
ATOM   2076 O  O     . ILE B 2 48  ? 27.434  -22.409 -2.969  1   212.24 ? 48  ILE B O     1 
ATOM   2077 C  CB    . ILE B 2 48  ? 26.89   -24.902 -4.569  1   213.46 ? 48  ILE B CB    1 
ATOM   2078 C  CG1   . ILE B 2 48  ? 25.479  -24.322 -4.702  1   214.5  ? 48  ILE B CG1   1 
ATOM   2079 C  CG2   . ILE B 2 48  ? 27.064  -25.63  -3.239  1   213.99 ? 48  ILE B CG2   1 
ATOM   2080 C  CD1   . ILE B 2 48  ? 25.048  -24.11  -6.076  1   215.83 ? 48  ILE B CD1   1 
ATOM   2081 N  N     . ILE B 2 49  ? 28.209  -21.39  -4.831  1   211.25 ? 49  ILE B N     1 
ATOM   2082 C  CA    . ILE B 2 49  ? 28.15   -20.023 -4.304  1   210.82 ? 49  ILE B CA    1 
ATOM   2083 C  C     . ILE B 2 49  ? 26.736  -19.471 -4.287  1   210.27 ? 49  ILE B C     1 
ATOM   2084 O  O     . ILE B 2 49  ? 26.162  -19.242 -5.35   1   210.45 ? 49  ILE B O     1 
ATOM   2085 C  CB    . ILE B 2 49  ? 29.058  -19.081 -5.123  1   211.26 ? 49  ILE B CB    1 
ATOM   2086 C  CG1   . ILE B 2 49  ? 30.483  -19.636 -5.254  1   212.18 ? 49  ILE B CG1   1 
ATOM   2087 C  CG2   . ILE B 2 49  ? 29.041  -17.667 -4.541  1   211.72 ? 49  ILE B CG2   1 
ATOM   2088 C  CD1   . ILE B 2 49  ? 31.338  -18.875 -6.238  1   213.43 ? 49  ILE B CD1   1 
ATOM   2089 N  N     . LEU B 2 50  ? 26.186  -19.214 -3.097  1   209.44 ? 50  LEU B N     1 
ATOM   2090 C  CA    . LEU B 2 50  ? 24.836  -18.67  -2.997  1   209.21 ? 50  LEU B CA    1 
ATOM   2091 C  C     . LEU B 2 50  ? 24.852  -17.265 -2.432  1   208.57 ? 50  LEU B C     1 
ATOM   2092 O  O     . LEU B 2 50  ? 25.033  -17.095 -1.231  1   208.74 ? 50  LEU B O     1 
ATOM   2093 C  CB    . LEU B 2 50  ? 23.929  -19.594 -2.163  1   209.57 ? 50  LEU B CB    1 
ATOM   2094 C  CG    . LEU B 2 50  ? 22.933  -20.466 -2.946  1   211.29 ? 50  LEU B CG    1 
ATOM   2095 C  CD1   . LEU B 2 50  ? 23.624  -21.295 -4.002  1   211.92 ? 50  LEU B CD1   1 
ATOM   2096 C  CD2   . LEU B 2 50  ? 22.207  -21.417 -2.028  1   212.05 ? 50  LEU B CD2   1 
ATOM   2097 N  N     . GLU B 2 51  ? 24.689  -16.255 -3.298  1   207.76 ? 51  GLU B N     1 
ATOM   2098 C  CA    . GLU B 2 51  ? 24.647  -14.855 -2.877  1   207.48 ? 51  GLU B CA    1 
ATOM   2099 C  C     . GLU B 2 51  ? 23.198  -14.382 -2.824  1   207.14 ? 51  GLU B C     1 
ATOM   2100 O  O     . GLU B 2 51  ? 22.366  -14.826 -3.615  1   207.25 ? 51  GLU B O     1 
ATOM   2101 C  CB    . GLU B 2 51  ? 25.456  -13.962 -3.828  1   209.22 ? 51  GLU B CB    1 
ATOM   2102 C  CG    . GLU B 2 51  ? 26.939  -14.282 -3.867  1   212.84 ? 51  GLU B CG    1 
ATOM   2103 C  CD    . GLU B 2 51  ? 27.716  -13.597 -4.977  1   217.47 ? 51  GLU B CD    1 
ATOM   2104 O  OE1   . GLU B 2 51  ? 27.133  -12.74  -5.679  1   218.1  ? 51  GLU B OE1   1 
ATOM   2105 O  OE2   . GLU B 2 51  ? 28.913  -13.922 -5.148  1   219.21 ? 51  GLU B OE2   1 
ATOM   2106 N  N     . GLY B 2 52  ? 22.904  -13.494 -1.891  1   206.6  ? 52  GLY B N     1 
ATOM   2107 C  CA    . GLY B 2 52  ? 21.553  -12.985 -1.727  1   206.61 ? 52  GLY B CA    1 
ATOM   2108 C  C     . GLY B 2 52  ? 21.516  -11.669 -0.995  1   206.36 ? 52  GLY B C     1 
ATOM   2109 O  O     . GLY B 2 52  ? 22.199  -11.49  0.015   1   206.4  ? 52  GLY B O     1 
ATOM   2110 N  N     . LYS B 2 53  ? 20.715  -10.741 -1.507  1   205.98 ? 53  LYS B N     1 
ATOM   2111 C  CA    . LYS B 2 53  ? 20.565  -9.415  -0.925  1   206.07 ? 53  LYS B CA    1 
ATOM   2112 C  C     . LYS B 2 53  ? 19.154  -8.857  -1.156  1   206.12 ? 53  LYS B C     1 
ATOM   2113 O  O     . LYS B 2 53  ? 18.412  -9.361  -2      1   206.27 ? 53  LYS B O     1 
ATOM   2114 C  CB    . LYS B 2 53  ? 21.647  -8.459  -1.467  1   207.47 ? 53  LYS B CB    1 
ATOM   2115 C  CG    . LYS B 2 53  ? 21.609  -8.252  -2.976  1   210.51 ? 53  LYS B CG    1 
ATOM   2116 C  CD    . LYS B 2 53  ? 22.993  -7.918  -3.525  1   213.91 ? 53  LYS B CD    1 
ATOM   2117 C  CE    . LYS B 2 53  ? 23.066  -7.929  -5.03   1   216.93 ? 53  LYS B CE    1 
ATOM   2118 N  NZ    . LYS B 2 53  ? 24.47   -7.873  -5.51   1   218.85 ? 53  LYS B NZ    1 
ATOM   2119 N  N     . GLU B 2 54  ? 18.773  -7.841  -0.379  1   205.81 ? 54  GLU B N     1 
ATOM   2120 C  CA    . GLU B 2 54  ? 17.458  -7.241  -0.515  1   205.92 ? 54  GLU B CA    1 
ATOM   2121 C  C     . GLU B 2 54  ? 17.558  -5.755  -0.806  1   205.78 ? 54  GLU B C     1 
ATOM   2122 O  O     . GLU B 2 54  ? 18.328  -5.033  -0.166  1   205.97 ? 54  GLU B O     1 
ATOM   2123 C  CB    . GLU B 2 54  ? 16.593  -7.504  0.725   1   207.92 ? 54  GLU B CB    1 
ATOM   2124 C  CG    . GLU B 2 54  ? 15.11   -7.341  0.452   1   211.99 ? 54  GLU B CG    1 
ATOM   2125 C  CD    . GLU B 2 54  ? 14.226  -7.885  1.55    1   217.41 ? 54  GLU B CD    1 
ATOM   2126 O  OE1   . GLU B 2 54  ? 13.095  -7.374  1.713   1   218.26 ? 54  GLU B OE1   1 
ATOM   2127 O  OE2   . GLU B 2 54  ? 14.664  -8.829  2.245   1   219.44 ? 54  GLU B OE2   1 
ATOM   2128 N  N     . GLU B 2 55  ? 16.781  -5.307  -1.794  1   205.18 ? 55  GLU B N     1 
ATOM   2129 C  CA    . GLU B 2 55  ? 16.685  -3.903  -2.194  1   204.89 ? 55  GLU B CA    1 
ATOM   2130 C  C     . GLU B 2 55  ? 15.251  -3.407  -1.849  1   204.1  ? 55  GLU B C     1 
ATOM   2131 O  O     . GLU B 2 55  ? 14.607  -2.735  -2.658  1   204.25 ? 55  GLU B O     1 
ATOM   2132 C  CB    . GLU B 2 55  ? 17.009  -3.71   -3.702  1   207.03 ? 55  GLU B CB    1 
ATOM   2133 C  CG    . GLU B 2 55  ? 17.606  -4.912  -4.432  1   211.27 ? 55  GLU B CG    1 
ATOM   2134 C  CD    . GLU B 2 55  ? 19.067  -4.806  -4.83   1   216.49 ? 55  GLU B CD    1 
ATOM   2135 O  OE1   . GLU B 2 55  ? 19.936  -5.149  -3.998  1   217.11 ? 55  GLU B OE1   1 
ATOM   2136 O  OE2   . GLU B 2 55  ? 19.341  -4.4    -5.983  1   218.5  ? 55  GLU B OE2   1 
ATOM   2137 N  N     . ASP B 2 56  ? 14.775  -3.765  -0.626  1   203    ? 56  ASP B N     1 
ATOM   2138 C  CA    . ASP B 2 56  ? 13.457  -3.466  -0.048  1   202.24 ? 56  ASP B CA    1 
ATOM   2139 C  C     . ASP B 2 56  ? 12.307  -4.011  -0.889  1   201.03 ? 56  ASP B C     1 
ATOM   2140 O  O     . ASP B 2 56  ? 11.7    -3.277  -1.667  1   201.14 ? 56  ASP B O     1 
ATOM   2141 C  CB    . ASP B 2 56  ? 13.282  -1.968  0.254   1   203.89 ? 56  ASP B CB    1 
ATOM   2142 C  CG    . ASP B 2 56  ? 12.86   -1.663  1.683   1   208.05 ? 56  ASP B CG    1 
ATOM   2143 O  OD1   . ASP B 2 56  ? 12.972  -2.565  2.545   1   208.61 ? 56  ASP B OD1   1 
ATOM   2144 O  OD2   . ASP B 2 56  ? 12.425  -0.522  1.94    1   210.13 ? 56  ASP B OD2   1 
ATOM   2145 N  N     . GLY B 2 57  ? 12.023  -5.296  -0.729  1   199.72 ? 57  GLY B N     1 
ATOM   2146 C  CA    . GLY B 2 57  ? 10.96   -5.949  -1.478  1   198.86 ? 57  GLY B CA    1 
ATOM   2147 C  C     . GLY B 2 57  ? 11.498  -6.783  -2.618  1   197.52 ? 57  GLY B C     1 
ATOM   2148 O  O     . GLY B 2 57  ? 10.975  -7.861  -2.899  1   197.5  ? 57  GLY B O     1 
ATOM   2149 N  N     . LYS B 2 58  ? 12.557  -6.294  -3.277  1   196.33 ? 58  LYS B N     1 
ATOM   2150 C  CA    . LYS B 2 58  ? 13.21   -6.981  -4.395  1   195.64 ? 58  LYS B CA    1 
ATOM   2151 C  C     . LYS B 2 58  ? 14.373  -7.825  -3.873  1   194.44 ? 58  LYS B C     1 
ATOM   2152 O  O     . LYS B 2 58  ? 15.255  -7.293  -3.207  1   194.51 ? 58  LYS B O     1 
ATOM   2153 C  CB    . LYS B 2 58  ? 13.719  -5.94   -5.417  1   197.55 ? 58  LYS B CB    1 
ATOM   2154 C  CG    . LYS B 2 58  ? 14.758  -6.447  -6.428  1   201.64 ? 58  LYS B CG    1 
ATOM   2155 C  CD    . LYS B 2 58  ? 14.15   -7.344  -7.496  1   206.24 ? 58  LYS B CD    1 
ATOM   2156 C  CE    . LYS B 2 58  ? 13.561  -6.544  -8.633  1   210.06 ? 58  LYS B CE    1 
ATOM   2157 N  NZ    . LYS B 2 58  ? 14.604  -5.787  -9.378  1   212.33 ? 58  LYS B NZ    1 
ATOM   2158 N  N     . ILE B 2 59  ? 14.391  -9.119  -4.189  1   193.15 ? 59  ILE B N     1 
ATOM   2159 C  CA    . ILE B 2 59  ? 15.462  -9.992  -3.73   1   192.36 ? 59  ILE B CA    1 
ATOM   2160 C  C     . ILE B 2 59  ? 16.407  -10.294 -4.871  1   191.36 ? 59  ILE B C     1 
ATOM   2161 O  O     . ILE B 2 59  ? 15.961  -10.726 -5.924  1   191.55 ? 59  ILE B O     1 
ATOM   2162 C  CB    . ILE B 2 59  ? 14.856  -11.264 -3.126  1   192.81 ? 59  ILE B CB    1 
ATOM   2163 C  CG1   . ILE B 2 59  ? 13.945  -10.907 -1.95   1   193.72 ? 59  ILE B CG1   1 
ATOM   2164 C  CG2   . ILE B 2 59  ? 15.942  -12.237 -2.715  1   193.3  ? 59  ILE B CG2   1 
ATOM   2165 C  CD1   . ILE B 2 59  ? 13.058  -11.977 -1.551  1   194.98 ? 59  ILE B CD1   1 
ATOM   2166 N  N     . LYS B 2 60  ? 17.702  -10.041 -4.689  1   190.23 ? 60  LYS B N     1 
ATOM   2167 C  CA    . LYS B 2 60  ? 18.689  -10.3   -5.731  1   189.66 ? 60  LYS B CA    1 
ATOM   2168 C  C     . LYS B 2 60  ? 19.529  -11.521 -5.383  1   188.66 ? 60  LYS B C     1 
ATOM   2169 O  O     . LYS B 2 60  ? 20.433  -11.426 -4.557  1   188.81 ? 60  LYS B O     1 
ATOM   2170 C  CB    . LYS B 2 60  ? 19.598  -9.078  -5.935  1   191.48 ? 60  LYS B CB    1 
ATOM   2171 C  CG    . LYS B 2 60  ? 18.938  -7.91   -6.65   1   195.49 ? 60  LYS B CG    1 
ATOM   2172 C  CD    . LYS B 2 60  ? 18.83   -8.16   -8.139  1   199.96 ? 60  LYS B CD    1 
ATOM   2173 C  CE    . LYS B 2 60  ? 18.253  -6.972  -8.872  1   203.6  ? 60  LYS B CE    1 
ATOM   2174 N  NZ    . LYS B 2 60  ? 16.982  -6.5    -8.26   1   205.76 ? 60  LYS B NZ    1 
ATOM   2175 N  N     . ALA B 2 61  ? 19.244  -12.657 -6.01   1   187.53 ? 61  ALA B N     1 
ATOM   2176 C  CA    . ALA B 2 61  ? 20.003  -13.873 -5.753  1   187.05 ? 61  ALA B CA    1 
ATOM   2177 C  C     . ALA B 2 61  ? 20.937  -14.211 -6.91   1   186.27 ? 61  ALA B C     1 
ATOM   2178 O  O     . ALA B 2 61  ? 20.697  -13.802 -8.044  1   186.19 ? 61  ALA B O     1 
ATOM   2179 C  CB    . ALA B 2 61  ? 19.058  -15.028 -5.478  1   187.31 ? 61  ALA B CB    1 
ATOM   2180 N  N     . LYS B 2 62  ? 22.009  -14.955 -6.62   1   185.58 ? 62  LYS B N     1 
ATOM   2181 C  CA    . LYS B 2 62  ? 22.985  -15.375 -7.62   1   185.43 ? 62  LYS B CA    1 
ATOM   2182 C  C     . LYS B 2 62  ? 23.579  -16.712 -7.186  1   185.22 ? 62  LYS B C     1 
ATOM   2183 O  O     . LYS B 2 62  ? 24.262  -16.79  -6.167  1   185.38 ? 62  LYS B O     1 
ATOM   2184 C  CB    . LYS B 2 62  ? 24.08   -14.312 -7.773  1   186.92 ? 62  LYS B CB    1 
ATOM   2185 C  CG    . LYS B 2 62  ? 25.03   -14.51  -8.949  1   190.28 ? 62  LYS B CG    1 
ATOM   2186 C  CD    . LYS B 2 62  ? 25.894  -13.249 -9.109  1   194    ? 62  LYS B CD    1 
ATOM   2187 C  CE    . LYS B 2 62  ? 27.246  -13.462 -9.741  1   197.17 ? 62  LYS B CE    1 
ATOM   2188 N  NZ    . LYS B 2 62  ? 28.117  -12.264 -9.587  1   198.92 ? 62  LYS B NZ    1 
ATOM   2189 N  N     . ILE B 2 63  ? 23.273  -17.771 -7.93   1   184.73 ? 63  ILE B N     1 
ATOM   2190 C  CA    . ILE B 2 63  ? 23.747  -19.117 -7.637  1   184.79 ? 63  ILE B CA    1 
ATOM   2191 C  C     . ILE B 2 63  ? 24.829  -19.487 -8.641  1   184.93 ? 63  ILE B C     1 
ATOM   2192 O  O     . ILE B 2 63  ? 24.614  -19.338 -9.838  1   185.09 ? 63  ILE B O     1 
ATOM   2193 C  CB    . ILE B 2 63  ? 22.553  -20.091 -7.71   1   185.08 ? 63  ILE B CB    1 
ATOM   2194 C  CG1   . ILE B 2 63  ? 21.513  -19.763 -6.628  1   185.93 ? 63  ILE B CG1   1 
ATOM   2195 C  CG2   . ILE B 2 63  ? 23.02   -21.536 -7.633  1   185.51 ? 63  ILE B CG2   1 
ATOM   2196 C  CD1   . ILE B 2 63  ? 20.245  -20.543 -6.721  1   187.24 ? 63  ILE B CD1   1 
ATOM   2197 N  N     . ILE B 2 64  ? 26.007  -19.92  -8.169  1   184.81 ? 64  ILE B N     1 
ATOM   2198 C  CA    . ILE B 2 64  ? 27.099  -20.293 -9.065  1   185.21 ? 64  ILE B CA    1 
ATOM   2199 C  C     . ILE B 2 64  ? 27.615  -21.692 -8.756  1   185.58 ? 64  ILE B C     1 
ATOM   2200 O  O     . ILE B 2 64  ? 28.173  -21.93  -7.687  1   185.52 ? 64  ILE B O     1 
ATOM   2201 C  CB    . ILE B 2 64  ? 28.248  -19.252 -9.058  1   185.76 ? 64  ILE B CB    1 
ATOM   2202 C  CG1   . ILE B 2 64  ? 27.761  -17.859 -9.489  1   186.67 ? 64  ILE B CG1   1 
ATOM   2203 C  CG2   . ILE B 2 64  ? 29.409  -19.715 -9.932  1   186.25 ? 64  ILE B CG2   1 
ATOM   2204 C  CD1   . ILE B 2 64  ? 27.8    -16.869 -8.407  1   187.98 ? 64  ILE B CD1   1 
ATOM   2205 N  N     . VAL B 2 65  ? 27.434  -22.616 -9.692  1   185.9  ? 65  VAL B N     1 
ATOM   2206 C  CA    . VAL B 2 65  ? 27.91   -23.982 -9.521  1   186.79 ? 65  VAL B CA    1 
ATOM   2207 C  C     . VAL B 2 65  ? 29.293  -24.058 -10.157 1   187.55 ? 65  VAL B C     1 
ATOM   2208 O  O     . VAL B 2 65  ? 29.439  -23.774 -11.344 1   187.73 ? 65  VAL B O     1 
ATOM   2209 C  CB    . VAL B 2 65  ? 26.928  -25.041 -10.084 1   187.5  ? 65  VAL B CB    1 
ATOM   2210 C  CG1   . VAL B 2 65  ? 27.322  -26.439 -9.628  1   188    ? 65  VAL B CG1   1 
ATOM   2211 C  CG2   . VAL B 2 65  ? 25.494  -24.735 -9.662  1   188.01 ? 65  VAL B CG2   1 
ATOM   2212 N  N     . LYS B 2 66  ? 30.314  -24.375 -9.349  1   187.84 ? 66  LYS B N     1 
ATOM   2213 C  CA    . LYS B 2 66  ? 31.708  -24.426 -9.784  1   188.57 ? 66  LYS B CA    1 
ATOM   2214 C  C     . LYS B 2 66  ? 32.035  -25.59  -10.734 1   189.14 ? 66  LYS B C     1 
ATOM   2215 O  O     . LYS B 2 66  ? 31.42   -26.654 -10.657 1   189.22 ? 66  LYS B O     1 
ATOM   2216 C  CB    . LYS B 2 66  ? 32.659  -24.422 -8.573  1   190.26 ? 66  LYS B CB    1 
ATOM   2217 C  CG    . LYS B 2 66  ? 32.477  -23.241 -7.623  1   193.95 ? 66  LYS B CG    1 
ATOM   2218 C  CD    . LYS B 2 66  ? 32.68   -21.89  -8.292  1   197.98 ? 66  LYS B CD    1 
ATOM   2219 C  CE    . LYS B 2 66  ? 34.081  -21.686 -8.813  1   201.46 ? 66  LYS B CE    1 
ATOM   2220 N  NZ    . LYS B 2 66  ? 34.11   -20.659 -9.886  1   203.64 ? 66  LYS B NZ    1 
ATOM   2221 N  N     . LYS B 2 67  ? 33.023  -25.365 -11.625 1   189.31 ? 67  LYS B N     1 
ATOM   2222 C  CA    . LYS B 2 67  ? 33.498  -26.295 -12.655 1   189.8  ? 67  LYS B CA    1 
ATOM   2223 C  C     . LYS B 2 67  ? 33.884  -27.677 -12.12  1   190.14 ? 67  LYS B C     1 
ATOM   2224 O  O     . LYS B 2 67  ? 34.869  -27.828 -11.4   1   190.11 ? 67  LYS B O     1 
ATOM   2225 C  CB    . LYS B 2 67  ? 34.659  -25.665 -13.454 1   191.4  ? 67  LYS B CB    1 
ATOM   2226 C  CG    . LYS B 2 67  ? 35.314  -26.597 -14.471 1   194.93 ? 67  LYS B CG    1 
ATOM   2227 C  CD    . LYS B 2 67  ? 36.489  -25.948 -15.168 1   198.76 ? 67  LYS B CD    1 
ATOM   2228 C  CE    . LYS B 2 67  ? 37.44   -26.977 -15.725 1   202.08 ? 67  LYS B CE    1 
ATOM   2229 N  NZ    . LYS B 2 67  ? 36.739  -27.96  -16.586 1   204.07 ? 67  LYS B NZ    1 
ATOM   2230 N  N     . GLY B 2 68  ? 33.105  -28.673 -12.505 1   190.35 ? 68  GLY B N     1 
ATOM   2231 C  CA    . GLY B 2 68  ? 33.341  -30.047 -12.092 1   191.17 ? 68  GLY B CA    1 
ATOM   2232 C  C     . GLY B 2 68  ? 32.444  -30.525 -10.968 1   191.9  ? 68  GLY B C     1 
ATOM   2233 O  O     . GLY B 2 68  ? 32.321  -31.731 -10.753 1   191.97 ? 68  GLY B O     1 
ATOM   2234 N  N     . TYR B 2 69  ? 31.807  -29.598 -10.241 1   192.34 ? 69  TYR B N     1 
ATOM   2235 C  CA    . TYR B 2 69  ? 30.948  -29.967 -9.12   1   193.35 ? 69  TYR B CA    1 
ATOM   2236 C  C     . TYR B 2 69  ? 29.601  -30.528 -9.536  1   193.93 ? 69  TYR B C     1 
ATOM   2237 O  O     . TYR B 2 69  ? 28.723  -29.78  -9.956  1   194.16 ? 69  TYR B O     1 
ATOM   2238 C  CB    . TYR B 2 69  ? 30.77   -28.798 -8.146  1   193.69 ? 69  TYR B CB    1 
ATOM   2239 C  CG    . TYR B 2 69  ? 31.975  -28.572 -7.262  1   194.88 ? 69  TYR B CG    1 
ATOM   2240 C  CD1   . TYR B 2 69  ? 32.017  -29.072 -5.97   1   196.01 ? 69  TYR B CD1   1 
ATOM   2241 C  CD2   . TYR B 2 69  ? 33.079  -27.871 -7.725  1   195.92 ? 69  TYR B CD2   1 
ATOM   2242 C  CE1   . TYR B 2 69  ? 33.127  -28.876 -5.156  1   197.03 ? 69  TYR B CE1   1 
ATOM   2243 C  CE2   . TYR B 2 69  ? 34.194  -27.666 -6.92   1   196.94 ? 69  TYR B CE2   1 
ATOM   2244 C  CZ    . TYR B 2 69  ? 34.218  -28.177 -5.636  1   197.94 ? 69  TYR B CZ    1 
ATOM   2245 O  OH    . TYR B 2 69  ? 35.316  -27.977 -4.831  1   199.45 ? 69  TYR B OH    1 
ATOM   2246 N  N     . LYS B 2 70  ? 29.425  -31.842 -9.381  1   194.09 ? 70  LYS B N     1 
ATOM   2247 C  CA    . LYS B 2 70  ? 28.176  -32.511 -9.716  1   194.83 ? 70  LYS B CA    1 
ATOM   2248 C  C     . LYS B 2 70  ? 27.445  -32.927 -8.435  1   195.72 ? 70  LYS B C     1 
ATOM   2249 O  O     . LYS B 2 70  ? 27.685  -34.017 -7.923  1   195.94 ? 70  LYS B O     1 
ATOM   2250 C  CB    . LYS B 2 70  ? 28.453  -33.747 -10.585 1   196.33 ? 70  LYS B CB    1 
ATOM   2251 C  CG    . LYS B 2 70  ? 29.244  -33.456 -11.852 1   199.74 ? 70  LYS B CG    1 
ATOM   2252 C  CD    . LYS B 2 70  ? 29.368  -34.703 -12.719 1   203.62 ? 70  LYS B CD    1 
ATOM   2253 C  CE    . LYS B 2 70  ? 30.21   -34.493 -13.955 1   206.88 ? 70  LYS B CE    1 
ATOM   2254 N  NZ    . LYS B 2 70  ? 29.517  -33.658 -14.972 1   208.72 ? 70  LYS B NZ    1 
ATOM   2255 N  N     . PHE B 2 71  ? 26.562  -32.069 -7.913  1   196.06 ? 71  PHE B N     1 
ATOM   2256 C  CA    . PHE B 2 71  ? 25.81   -32.387 -6.697  1   196.92 ? 71  PHE B CA    1 
ATOM   2257 C  C     . PHE B 2 71  ? 24.574  -33.212 -7.072  1   197.57 ? 71  PHE B C     1 
ATOM   2258 O  O     . PHE B 2 71  ? 23.691  -32.678 -7.739  1   197.66 ? 71  PHE B O     1 
ATOM   2259 C  CB    . PHE B 2 71  ? 25.373  -31.09  -5.992  1   196.96 ? 71  PHE B CB    1 
ATOM   2260 C  CG    . PHE B 2 71  ? 26.482  -30.086 -5.756  1   197.72 ? 71  PHE B CG    1 
ATOM   2261 C  CD1   . PHE B 2 71  ? 27.34   -30.218 -4.68   1   198.54 ? 71  PHE B CD1   1 
ATOM   2262 C  CD2   . PHE B 2 71  ? 26.651  -28.998 -6.599  1   198.53 ? 71  PHE B CD2   1 
ATOM   2263 C  CE1   . PHE B 2 71  ? 28.352  -29.291 -4.46   1   199.23 ? 71  PHE B CE1   1 
ATOM   2264 C  CE2   . PHE B 2 71  ? 27.664  -28.074 -6.376  1   199.21 ? 71  PHE B CE2   1 
ATOM   2265 C  CZ    . PHE B 2 71  ? 28.511  -28.231 -5.314  1   199.01 ? 71  PHE B CZ    1 
ATOM   2266 N  N     . LYS B 2 72  ? 24.502  -34.5   -6.682  1   197.9  ? 72  LYS B N     1 
ATOM   2267 C  CA    . LYS B 2 72  ? 23.333  -35.318 -7.045  1   198.74 ? 72  LYS B CA    1 
ATOM   2268 C  C     . LYS B 2 72  ? 22.138  -35.132 -6.08   1   199.68 ? 72  LYS B C     1 
ATOM   2269 O  O     . LYS B 2 72  ? 21.024  -35.552 -6.4    1   199.75 ? 72  LYS B O     1 
ATOM   2270 C  CB    . LYS B 2 72  ? 23.698  -36.804 -7.237  1   200.28 ? 72  LYS B CB    1 
ATOM   2271 C  CG    . LYS B 2 72  ? 23.536  -37.698 -6.012  1   203.85 ? 72  LYS B CG    1 
ATOM   2272 C  CD    . LYS B 2 72  ? 23.427  -39.154 -6.416  1   207.66 ? 72  LYS B CD    1 
ATOM   2273 C  CE    . LYS B 2 72  ? 23.263  -40.055 -5.221  1   211.04 ? 72  LYS B CE    1 
ATOM   2274 N  NZ    . LYS B 2 72  ? 21.92   -39.914 -4.609  1   213.11 ? 72  LYS B NZ    1 
ATOM   2275 N  N     . TYR B 2 73  ? 22.361  -34.506 -4.915  1   200.2  ? 73  TYR B N     1 
ATOM   2276 C  CA    . TYR B 2 73  ? 21.291  -34.272 -3.952  1   201.2  ? 73  TYR B CA    1 
ATOM   2277 C  C     . TYR B 2 73  ? 20.654  -32.896 -4.184  1   201.82 ? 73  TYR B C     1 
ATOM   2278 O  O     . TYR B 2 73  ? 21.354  -31.909 -4.411  1   201.91 ? 73  TYR B O     1 
ATOM   2279 C  CB    . TYR B 2 73  ? 21.779  -34.489 -2.512  1   201.47 ? 73  TYR B CB    1 
ATOM   2280 C  CG    . TYR B 2 73  ? 22.151  -35.935 -2.232  1   202.48 ? 73  TYR B CG    1 
ATOM   2281 C  CD1   . TYR B 2 73  ? 21.34   -36.978 -2.659  1   203.41 ? 73  TYR B CD1   1 
ATOM   2282 C  CD2   . TYR B 2 73  ? 23.308  -36.257 -1.535  1   203.39 ? 73  TYR B CD2   1 
ATOM   2283 C  CE1   . TYR B 2 73  ? 21.668  -38.305 -2.393  1   204.2  ? 73  TYR B CE1   1 
ATOM   2284 C  CE2   . TYR B 2 73  ? 23.65   -37.581 -1.27   1   204.2  ? 73  TYR B CE2   1 
ATOM   2285 C  CZ    . TYR B 2 73  ? 22.829  -38.604 -1.706  1   204.94 ? 73  TYR B CZ    1 
ATOM   2286 O  OH    . TYR B 2 73  ? 23.165  -39.912 -1.456  1   206.16 ? 73  TYR B OH    1 
ATOM   2287 N  N     . PRO B 2 74  ? 19.315  -32.837 -4.216  1   202.08 ? 74  PRO B N     1 
ATOM   2288 C  CA    . PRO B 2 74  ? 18.646  -31.585 -4.595  1   202.46 ? 74  PRO B CA    1 
ATOM   2289 C  C     . PRO B 2 74  ? 18.66   -30.437 -3.598  1   203.2  ? 74  PRO B C     1 
ATOM   2290 O  O     . PRO B 2 74  ? 18.391  -30.602 -2.417  1   203.28 ? 74  PRO B O     1 
ATOM   2291 C  CB    . PRO B 2 74  ? 17.205  -32.018 -4.885  1   203.02 ? 74  PRO B CB    1 
ATOM   2292 C  CG    . PRO B 2 74  ? 17.227  -33.517 -4.929  1   203.33 ? 74  PRO B CG    1 
ATOM   2293 C  CD    . PRO B 2 74  ? 18.349  -33.935 -4.05   1   201.64 ? 74  PRO B CD    1 
ATOM   2294 N  N     . ILE B 2 75  ? 18.917  -29.248 -4.13   1   203.68 ? 75  ILE B N     1 
ATOM   2295 C  CA    . ILE B 2 75  ? 18.918  -27.975 -3.419  1   204.74 ? 75  ILE B CA    1 
ATOM   2296 C  C     . ILE B 2 75  ? 17.452  -27.526 -3.246  1   205.59 ? 75  ILE B C     1 
ATOM   2297 O  O     . ILE B 2 75  ? 16.631  -27.812 -4.114  1   205.79 ? 75  ILE B O     1 
ATOM   2298 C  CB    . ILE B 2 75  ? 19.787  -26.972 -4.253  1   205.42 ? 75  ILE B CB    1 
ATOM   2299 C  CG1   . ILE B 2 75  ? 21.243  -26.916 -3.738  1   206.47 ? 75  ILE B CG1   1 
ATOM   2300 C  CG2   . ILE B 2 75  ? 19.196  -25.554 -4.347  1   205.95 ? 75  ILE B CG2   1 
ATOM   2301 C  CD1   . ILE B 2 75  ? 21.94   -28.255 -3.499  1   207.81 ? 75  ILE B CD1   1 
ATOM   2302 N  N     . HIS B 2 76  ? 17.114  -26.85  -2.135  1   206.02 ? 76  HIS B N     1 
ATOM   2303 C  CA    . HIS B 2 76  ? 15.741  -26.389 -1.93   1   207.03 ? 76  HIS B CA    1 
ATOM   2304 C  C     . HIS B 2 76  ? 15.601  -24.867 -2.015  1   207.78 ? 76  HIS B C     1 
ATOM   2305 O  O     . HIS B 2 76  ? 16.588  -24.142 -1.926  1   207.87 ? 76  HIS B O     1 
ATOM   2306 C  CB    . HIS B 2 76  ? 15.151  -26.946 -0.632  1   208.12 ? 76  HIS B CB    1 
ATOM   2307 C  CG    . HIS B 2 76  ? 14.908  -28.422 -0.686  1   210.96 ? 76  HIS B CG    1 
ATOM   2308 N  ND1   . HIS B 2 76  ? 15.95   -29.329 -0.595  1   213.02 ? 76  HIS B ND1   1 
ATOM   2309 C  CD2   . HIS B 2 76  ? 13.746  -29.103 -0.828  1   212.27 ? 76  HIS B CD2   1 
ATOM   2310 C  CE1   . HIS B 2 76  ? 15.393  -30.528 -0.68   1   213.59 ? 76  HIS B CE1   1 
ATOM   2311 N  NE2   . HIS B 2 76  ? 14.069  -30.444 -0.822  1   213.47 ? 76  HIS B NE2   1 
ATOM   2312 N  N     . MET B 2 77  ? 14.375  -24.389 -2.228  1   208.22 ? 77  MET B N     1 
ATOM   2313 C  CA    . MET B 2 77  ? 14.087  -22.965 -2.349  1   209.14 ? 77  MET B CA    1 
ATOM   2314 C  C     . MET B 2 77  ? 12.64   -22.757 -1.928  1   209.9  ? 77  MET B C     1 
ATOM   2315 O  O     . MET B 2 77  ? 11.734  -22.896 -2.75   1   210.21 ? 77  MET B O     1 
ATOM   2316 C  CB    . MET B 2 77  ? 14.291  -22.515 -3.803  1   209.81 ? 77  MET B CB    1 
ATOM   2317 C  CG    . MET B 2 77  ? 14.258  -21.019 -3.982  1   211.82 ? 77  MET B CG    1 
ATOM   2318 S  SD    . MET B 2 77  ? 14.657  -20.55  -5.678  1   214.43 ? 77  MET B SD    1 
ATOM   2319 C  CE    . MET B 2 77  ? 16.405  -20.795 -5.656  1   212.21 ? 77  MET B CE    1 
ATOM   2320 N  N     . CYS B 2 78  ? 12.414  -22.464 -0.642  1   210.05 ? 78  CYS B N     1 
ATOM   2321 C  CA    . CYS B 2 78  ? 11.057  -22.313 -0.13   1   210.63 ? 78  CYS B CA    1 
ATOM   2322 C  C     . CYS B 2 78  ? 10.548  -20.874 -0.148  1   211.17 ? 78  CYS B C     1 
ATOM   2323 O  O     . CYS B 2 78  ? 11.278  -19.949 0.193   1   211.21 ? 78  CYS B O     1 
ATOM   2324 C  CB    . CYS B 2 78  ? 10.931  -22.943 1.252   1   211.12 ? 78  CYS B CB    1 
ATOM   2325 S  SG    . CYS B 2 78  ? 11.182  -24.737 1.262   1   213.56 ? 78  CYS B SG    1 
ATOM   2326 N  N     . PHE B 2 79  ? 9.286   -20.699 -0.575  1   211.4  ? 79  PHE B N     1 
ATOM   2327 C  CA    . PHE B 2 79  ? 8.604   -19.409 -0.649  1   212.1  ? 79  PHE B CA    1 
ATOM   2328 C  C     . PHE B 2 79  ? 7.269   -19.513 0.076   1   212.69 ? 79  PHE B C     1 
ATOM   2329 O  O     . PHE B 2 79  ? 6.34    -20.147 -0.426  1   212.85 ? 79  PHE B O     1 
ATOM   2330 C  CB    . PHE B 2 79  ? 8.331   -19.009 -2.107  1   212    ? 79  PHE B CB    1 
ATOM   2331 C  CG    . PHE B 2 79  ? 9.552   -18.759 -2.954  1   212.54 ? 79  PHE B CG    1 
ATOM   2332 C  CD1   . PHE B 2 79  ? 10.254  -17.573 -2.852  1   213.25 ? 79  PHE B CD1   1 
ATOM   2333 C  CD2   . PHE B 2 79  ? 9.97    -19.691 -3.885  1   213.27 ? 79  PHE B CD2   1 
ATOM   2334 C  CE1   . PHE B 2 79  ? 11.367  -17.337 -3.643  1   213.89 ? 79  PHE B CE1   1 
ATOM   2335 C  CE2   . PHE B 2 79  ? 11.082  -19.452 -4.676  1   213.93 ? 79  PHE B CE2   1 
ATOM   2336 C  CZ    . PHE B 2 79  ? 11.776  -18.278 -4.549  1   213.69 ? 79  PHE B CZ    1 
ATOM   2337 N  N     . GLY B 2 80  ? 7.178   -18.889 1.239   1   212.85 ? 80  GLY B N     1 
ATOM   2338 C  CA    . GLY B 2 80  ? 5.946   -18.907 2.01    1   213.49 ? 80  GLY B CA    1 
ATOM   2339 C  C     . GLY B 2 80  ? 5.328   -17.533 2.092   1   213.95 ? 80  GLY B C     1 
ATOM   2340 O  O     . GLY B 2 80  ? 6.046   -16.552 2.276   1   214    ? 80  GLY B O     1 
ATOM   2341 N  N     . ILE B 2 81  ? 4.002   -17.439 1.904   1   214.1  ? 81  ILE B N     1 
ATOM   2342 C  CA    . ILE B 2 81  ? 3.282   -16.168 2.009   1   214.64 ? 81  ILE B CA    1 
ATOM   2343 C  C     . ILE B 2 81  ? 1.972   -16.331 2.795   1   214.77 ? 81  ILE B C     1 
ATOM   2344 O  O     . ILE B 2 81  ? 1.022   -16.962 2.326   1   214.73 ? 81  ILE B O     1 
ATOM   2345 C  CB    . ILE B 2 81  ? 3.056   -15.41  0.672   1   215.3  ? 81  ILE B CB    1 
ATOM   2346 C  CG1   . ILE B 2 81  ? 4.368   -15.151 -0.102  1   216.29 ? 81  ILE B CG1   1 
ATOM   2347 C  CG2   . ILE B 2 81  ? 2.335   -14.099 0.954   1   215.76 ? 81  ILE B CG2   1 
ATOM   2348 C  CD1   . ILE B 2 81  ? 4.184   -14.509 -1.471  1   217.58 ? 81  ILE B CD1   1 
ATOM   2349 N  N     . THR B 2 82  ? 1.935   -15.755 3.997   1   214.7  ? 82  THR B N     1 
ATOM   2350 C  CA    . THR B 2 82  ? 0.769   -15.797 4.874   1   215.06 ? 82  THR B CA    1 
ATOM   2351 C  C     . THR B 2 82  ? 0.168   -14.391 5.138   1   214.8  ? 82  THR B C     1 
ATOM   2352 O  O     . THR B 2 82  ? -0.947  -14.295 5.651   1   215.02 ? 82  THR B O     1 
ATOM   2353 C  CB    . THR B 2 82  ? 1.119   -16.544 6.173   1   216.69 ? 82  THR B CB    1 
ATOM   2354 O  OG1   . THR B 2 82  ? -0.062  -17.135 6.723   1   217.92 ? 82  THR B OG1   1 
ATOM   2355 C  CG2   . THR B 2 82  ? 1.811   -15.651 7.204   1   217.07 ? 82  THR B CG2   1 
ATOM   2356 N  N     . GLU B 2 83  ? 0.899   -13.311 4.791   1   214.06 ? 83  GLU B N     1 
ATOM   2357 C  CA    . GLU B 2 83  ? 0.458   -11.929 4.979   1   213.66 ? 83  GLU B CA    1 
ATOM   2358 C  C     . GLU B 2 83  ? -0.329  -11.431 3.766   1   213.01 ? 83  GLU B C     1 
ATOM   2359 O  O     . GLU B 2 83  ? -0.114  -11.881 2.637   1   213.11 ? 83  GLU B O     1 
ATOM   2360 C  CB    . GLU B 2 83  ? 1.665   -10.999 5.214   1   215.3  ? 83  GLU B CB    1 
ATOM   2361 C  CG    . GLU B 2 83  ? 1.712   -10.331 6.574   1   218.37 ? 83  GLU B CG    1 
ATOM   2362 C  CD    . GLU B 2 83  ? 2.605   -9.107  6.599   1   223.04 ? 83  GLU B CD    1 
ATOM   2363 O  OE1   . GLU B 2 83  ? 3.686   -9.141  5.97    1   223.56 ? 83  GLU B OE1   1 
ATOM   2364 O  OE2   . GLU B 2 83  ? 2.218   -8.107  7.245   1   225.23 ? 83  GLU B OE2   1 
ATOM   2365 N  N     . GLU B 2 84  ? -1.226  -10.474 4.007   1   212.11 ? 84  GLU B N     1 
ATOM   2366 C  CA    . GLU B 2 84  ? -2.021  -9.868  2.951   1   211.68 ? 84  GLU B CA    1 
ATOM   2367 C  C     . GLU B 2 84  ? -1.167  -8.844  2.189   1   210.9  ? 84  GLU B C     1 
ATOM   2368 O  O     . GLU B 2 84  ? -0.324  -8.168  2.792   1   211.23 ? 84  GLU B O     1 
ATOM   2369 C  CB    . GLU B 2 84  ? -3.261  -9.171  3.544   1   213.74 ? 84  GLU B CB    1 
ATOM   2370 C  CG    . GLU B 2 84  ? -4.089  -10.034 4.481   1   217.9  ? 84  GLU B CG    1 
ATOM   2371 C  CD    . GLU B 2 84  ? -5.015  -9.238  5.383   1   223.14 ? 84  GLU B CD    1 
ATOM   2372 O  OE1   . GLU B 2 84  ? -5.203  -9.641  6.555   1   223.64 ? 84  GLU B OE1   1 
ATOM   2373 O  OE2   . GLU B 2 84  ? -5.539  -8.2    4.921   1   224.95 ? 84  GLU B OE2   1 
ATOM   2374 N  N     . ASN B 2 85  ? -1.391  -8.734  0.866   1   209.62 ? 85  ASN B N     1 
ATOM   2375 C  CA    . ASN B 2 85  ? -0.699  -7.793  -0.024  1   208.8  ? 85  ASN B CA    1 
ATOM   2376 C  C     . ASN B 2 85  ? 0.838   -7.91   0.023   1   207.14 ? 85  ASN B C     1 
ATOM   2377 O  O     . ASN B 2 85  ? 1.521   -6.974  0.446   1   207.24 ? 85  ASN B O     1 
ATOM   2378 C  CB    . ASN B 2 85  ? -1.148  -6.34   0.228   1   210.3  ? 85  ASN B CB    1 
ATOM   2379 C  CG    . ASN B 2 85  ? -2.634  -6.148  0.44    1   213.74 ? 85  ASN B CG    1 
ATOM   2380 O  OD1   . ASN B 2 85  ? -3.474  -6.956  0.014   1   215.01 ? 85  ASN B OD1   1 
ATOM   2381 N  ND2   . ASN B 2 85  ? -2.987  -5.06   1.115   1   214.31 ? 85  ASN B ND2   1 
ATOM   2382 N  N     . ILE B 2 86  ? 1.373   -9.061  -0.406  1   205.37 ? 86  ILE B N     1 
ATOM   2383 C  CA    . ILE B 2 86  ? 2.813   -9.305  -0.435  1   204.09 ? 86  ILE B CA    1 
ATOM   2384 C  C     . ILE B 2 86  ? 3.28    -9.361  -1.889  1   202.48 ? 86  ILE B C     1 
ATOM   2385 O  O     . ILE B 2 86  ? 2.677   -10.065 -2.692  1   202.53 ? 86  ILE B O     1 
ATOM   2386 C  CB    . ILE B 2 86  ? 3.149   -10.62  0.323   1   204.51 ? 86  ILE B CB    1 
ATOM   2387 C  CG1   . ILE B 2 86  ? 2.957   -10.465 1.841   1   205.42 ? 86  ILE B CG1   1 
ATOM   2388 C  CG2   . ILE B 2 86  ? 4.546   -11.15  -0.007  1   204.96 ? 86  ILE B CG2   1 
ATOM   2389 C  CD1   . ILE B 2 86  ? 3.876   -9.465  2.505   1   206.62 ? 86  ILE B CD1   1 
ATOM   2390 N  N     . SER B 2 87  ? 4.333   -8.613  -2.236  1   200.95 ? 87  SER B N     1 
ATOM   2391 C  CA    . SER B 2 87  ? 4.879   -8.647  -3.588  1   199.88 ? 87  SER B CA    1 
ATOM   2392 C  C     . SER B 2 87  ? 6.287   -9.235  -3.513  1   198.52 ? 87  SER B C     1 
ATOM   2393 O  O     . SER B 2 87  ? 7.27    -8.512  -3.366  1   198.7  ? 87  SER B O     1 
ATOM   2394 C  CB    . SER B 2 87  ? 4.888   -7.259  -4.221  1   200.99 ? 87  SER B CB    1 
ATOM   2395 O  OG    . SER B 2 87  ? 4.866   -7.345  -5.637  1   202.81 ? 87  SER B OG    1 
ATOM   2396 N  N     . GLN B 2 88  ? 6.355   -10.568 -3.548  1   196.98 ? 88  GLN B N     1 
ATOM   2397 C  CA    . GLN B 2 88  ? 7.565   -11.381 -3.479  1   195.9  ? 88  GLN B CA    1 
ATOM   2398 C  C     . GLN B 2 88  ? 8.279   -11.357 -4.842  1   193.93 ? 88  GLN B C     1 
ATOM   2399 O  O     . GLN B 2 88  ? 8.137   -12.299 -5.62   1   194.11 ? 88  GLN B O     1 
ATOM   2400 C  CB    . GLN B 2 88  ? 7.161   -12.827 -3.101  1   197.86 ? 88  GLN B CB    1 
ATOM   2401 C  CG    . GLN B 2 88  ? 8.258   -13.708 -2.503  1   201.68 ? 88  GLN B CG    1 
ATOM   2402 C  CD    . GLN B 2 88  ? 7.71    -15.055 -2.065  1   206.35 ? 88  GLN B CD    1 
ATOM   2403 O  OE1   . GLN B 2 88  ? 7.101   -15.796 -2.846  1   207.87 ? 88  GLN B OE1   1 
ATOM   2404 N  NE2   . GLN B 2 88  ? 7.9     -15.399 -0.798  1   206.98 ? 88  GLN B NE2   1 
ATOM   2405 N  N     . ILE B 2 89  ? 9.032   -10.282 -5.14   1   191.86 ? 89  ILE B N     1 
ATOM   2406 C  CA    . ILE B 2 89  ? 9.757   -10.177 -6.407  1   190.36 ? 89  ILE B CA    1 
ATOM   2407 C  C     . ILE B 2 89  ? 11.196  -10.631 -6.249  1   189.14 ? 89  ILE B C     1 
ATOM   2408 O  O     . ILE B 2 89  ? 11.959  -10.025 -5.506  1   189.23 ? 89  ILE B O     1 
ATOM   2409 C  CB    . ILE B 2 89  ? 9.68    -8.762  -6.992  1   190.37 ? 89  ILE B CB    1 
ATOM   2410 C  CG1   . ILE B 2 89  ? 8.221   -8.313  -7.112  1   191.18 ? 89  ILE B CG1   1 
ATOM   2411 C  CG2   . ILE B 2 89  ? 10.403  -8.704  -8.328  1   190.64 ? 89  ILE B CG2   1 
ATOM   2412 C  CD1   . ILE B 2 89  ? 8.05    -6.893  -7.473  1   192.47 ? 89  ILE B CD1   1 
ATOM   2413 N  N     . ILE B 2 90  ? 11.568  -11.702 -6.945  1   187.93 ? 90  ILE B N     1 
ATOM   2414 C  CA    . ILE B 2 90  ? 12.909  -12.254 -6.849  1   187.23 ? 90  ILE B CA    1 
ATOM   2415 C  C     . ILE B 2 90  ? 13.609  -12.32  -8.205  1   186.29 ? 90  ILE B C     1 
ATOM   2416 O  O     . ILE B 2 90  ? 13.143  -12.983 -9.127  1   186.49 ? 90  ILE B O     1 
ATOM   2417 C  CB    . ILE B 2 90  ? 12.9    -13.627 -6.107  1   187.75 ? 90  ILE B CB    1 
ATOM   2418 C  CG1   . ILE B 2 90  ? 14.292  -14.298 -6.109  1   188.73 ? 90  ILE B CG1   1 
ATOM   2419 C  CG2   . ILE B 2 90  ? 11.812  -14.569 -6.632  1   188.18 ? 90  ILE B CG2   1 
ATOM   2420 C  CD1   . ILE B 2 90  ? 14.4    -15.53  -5.245  1   190.08 ? 90  ILE B CD1   1 
ATOM   2421 N  N     . ASP B 2 91  ? 14.737  -11.626 -8.315  1   185.14 ? 91  ASP B N     1 
ATOM   2422 C  CA    . ASP B 2 91  ? 15.577  -11.644 -9.502  1   184.6  ? 91  ASP B CA    1 
ATOM   2423 C  C     . ASP B 2 91  ? 16.749  -12.571 -9.182  1   183.75 ? 91  ASP B C     1 
ATOM   2424 O  O     . ASP B 2 91  ? 17.556  -12.249 -8.313  1   183.84 ? 91  ASP B O     1 
ATOM   2425 C  CB    . ASP B 2 91  ? 16.094  -10.235 -9.833  1   186.06 ? 91  ASP B CB    1 
ATOM   2426 C  CG    . ASP B 2 91  ? 15.052  -9.322  -10.443 1   189.82 ? 91  ASP B CG    1 
ATOM   2427 O  OD1   . ASP B 2 91  ? 13.849  -9.563  -10.217 1   190.37 ? 91  ASP B OD1   1 
ATOM   2428 O  OD2   . ASP B 2 91  ? 15.44   -8.359  -11.137 1   191.6  ? 91  ASP B OD2   1 
ATOM   2429 N  N     . VAL B 2 92  ? 16.823  -13.734 -9.839  1   182.73 ? 92  VAL B N     1 
ATOM   2430 C  CA    . VAL B 2 92  ? 17.89   -14.692 -9.57   1   182.25 ? 92  VAL B CA    1 
ATOM   2431 C  C     . VAL B 2 92  ? 18.675  -15.031 -10.829 1   181.58 ? 92  VAL B C     1 
ATOM   2432 O  O     . VAL B 2 92  ? 18.117  -15.047 -11.92  1   181.65 ? 92  VAL B O     1 
ATOM   2433 C  CB    . VAL B 2 92  ? 17.33   -15.954 -8.873  1   182.94 ? 92  VAL B CB    1 
ATOM   2434 C  CG1   . VAL B 2 92  ? 16.191  -16.567 -9.679  1   183.56 ? 92  VAL B CG1   1 
ATOM   2435 C  CG2   . VAL B 2 92  ? 18.424  -16.982 -8.593  1   183.42 ? 92  VAL B CG2   1 
ATOM   2436 N  N     . GLU B 2 93  ? 19.976  -15.262 -10.687 1   180.92 ? 93  GLU B N     1 
ATOM   2437 C  CA    . GLU B 2 93  ? 20.82   -15.634 -11.81  1   180.9  ? 93  GLU B CA    1 
ATOM   2438 C  C     . GLU B 2 93  ? 21.495  -16.939 -11.45  1   180.53 ? 93  GLU B C     1 
ATOM   2439 O  O     . GLU B 2 93  ? 22.17   -17.005 -10.433 1   180.5  ? 93  GLU B O     1 
ATOM   2440 C  CB    . GLU B 2 93  ? 21.863  -14.545 -12.089 1   183.22 ? 93  GLU B CB    1 
ATOM   2441 C  CG    . GLU B 2 93  ? 22.745  -14.841 -13.291 1   187.72 ? 93  GLU B CG    1 
ATOM   2442 C  CD    . GLU B 2 93  ? 23.599  -13.682 -13.771 1   192.69 ? 93  GLU B CD    1 
ATOM   2443 O  OE1   . GLU B 2 93  ? 23.494  -12.579 -13.187 1   193.48 ? 93  GLU B OE1   1 
ATOM   2444 O  OE2   . GLU B 2 93  ? 24.363  -13.872 -14.746 1   194.3  ? 93  GLU B OE2   1 
ATOM   2445 N  N     . ILE B 2 94  ? 21.272  -17.992 -12.239 1   180.14 ? 94  ILE B N     1 
ATOM   2446 C  CA    . ILE B 2 94  ? 21.871  -19.292 -11.968 1   180.25 ? 94  ILE B CA    1 
ATOM   2447 C  C     . ILE B 2 94  ? 22.904  -19.609 -13.037 1   180.4  ? 94  ILE B C     1 
ATOM   2448 O  O     . ILE B 2 94  ? 22.569  -19.69  -14.21  1   180.48 ? 94  ILE B O     1 
ATOM   2449 C  CB    . ILE B 2 94  ? 20.791  -20.392 -11.853 1   180.62 ? 94  ILE B CB    1 
ATOM   2450 C  CG1   . ILE B 2 94  ? 19.706  -19.992 -10.838 1   181.44 ? 94  ILE B CG1   1 
ATOM   2451 C  CG2   . ILE B 2 94  ? 21.426  -21.726 -11.491 1   180.98 ? 94  ILE B CG2   1 
ATOM   2452 C  CD1   . ILE B 2 94  ? 18.549  -20.934 -10.737 1   182.58 ? 94  ILE B CD1   1 
ATOM   2453 N  N     . ILE B 2 95  ? 24.167  -19.739 -12.644 1   180.38 ? 95  ILE B N     1 
ATOM   2454 C  CA    . ILE B 2 95  ? 25.246  -20.026 -13.579 1   181.05 ? 95  ILE B CA    1 
ATOM   2455 C  C     . ILE B 2 95  ? 25.869  -21.366 -13.246 1   181.78 ? 95  ILE B C     1 
ATOM   2456 O  O     . ILE B 2 95  ? 26.251  -21.596 -12.106 1   181.88 ? 95  ILE B O     1 
ATOM   2457 C  CB    . ILE B 2 95  ? 26.31   -18.911 -13.531 1   181.34 ? 95  ILE B CB    1 
ATOM   2458 C  CG1   . ILE B 2 95  ? 25.704  -17.549 -13.892 1   182.06 ? 95  ILE B CG1   1 
ATOM   2459 C  CG2   . ILE B 2 95  ? 27.498  -19.252 -14.428 1   181.8  ? 95  ILE B CG2   1 
ATOM   2460 C  CD1   . ILE B 2 95  ? 26.593  -16.396 -13.593 1   183.23 ? 95  ILE B CD1   1 
ATOM   2461 N  N     . LEU B 2 96  ? 25.979  -22.247 -14.231 1   182.22 ? 96  LEU B N     1 
ATOM   2462 C  CA    . LEU B 2 96  ? 26.591  -23.55  -14.037 1   183.11 ? 96  LEU B CA    1 
ATOM   2463 C  C     . LEU B 2 96  ? 27.839  -23.606 -14.891 1   184.17 ? 96  LEU B C     1 
ATOM   2464 O  O     . LEU B 2 96  ? 27.745  -23.447 -16.101 1   184.34 ? 96  LEU B O     1 
ATOM   2465 C  CB    . LEU B 2 96  ? 25.626  -24.65  -14.468 1   183.37 ? 96  LEU B CB    1 
ATOM   2466 C  CG    . LEU B 2 96  ? 24.671  -25.145 -13.404 1   185.03 ? 96  LEU B CG    1 
ATOM   2467 C  CD1   . LEU B 2 96  ? 23.416  -24.298 -13.353 1   185.59 ? 96  LEU B CD1   1 
ATOM   2468 C  CD2   . LEU B 2 96  ? 24.306  -26.576 -13.66  1   185.84 ? 96  LEU B CD2   1 
ATOM   2469 N  N     . GLU B 2 97  ? 29.009  -23.805 -14.279 1   184.79 ? 97  GLU B N     1 
ATOM   2470 C  CA    . GLU B 2 97  ? 30.259  -23.872 -15.035 1   185.89 ? 97  GLU B CA    1 
ATOM   2471 C  C     . GLU B 2 97  ? 30.465  -25.247 -15.691 1   186.8  ? 97  GLU B C     1 
ATOM   2472 O  O     . GLU B 2 97  ? 29.748  -26.195 -15.372 1   186.79 ? 97  GLU B O     1 
ATOM   2473 C  CB    . GLU B 2 97  ? 31.452  -23.46  -14.156 1   188.05 ? 97  GLU B CB    1 
ATOM   2474 C  CG    . GLU B 2 97  ? 31.302  -22.067 -13.569 1   192.39 ? 97  GLU B CG    1 
ATOM   2475 C  CD    . GLU B 2 97  ? 32.337  -21.681 -12.531 1   197.65 ? 97  GLU B CD    1 
ATOM   2476 O  OE1   . GLU B 2 97  ? 33.29   -22.463 -12.314 1   198.67 ? 97  GLU B OE1   1 
ATOM   2477 O  OE2   . GLU B 2 97  ? 32.192  -20.591 -11.931 1   199.56 ? 97  GLU B OE2   1 
ATOM   2478 N  N     . GLU B 2 98  ? 31.425  -25.346 -16.629 1   187.44 ? 98  GLU B N     1 
ATOM   2479 C  CA    . GLU B 2 98  ? 31.744  -26.566 -17.375 1   188.53 ? 98  GLU B CA    1 
ATOM   2480 C  C     . GLU B 2 98  ? 31.773  -27.833 -16.52  1   189.2  ? 98  GLU B C     1 
ATOM   2481 O  O     . GLU B 2 98  ? 32.393  -27.841 -15.461 1   189.26 ? 98  GLU B O     1 
ATOM   2482 C  CB    . GLU B 2 98  ? 33.067  -26.399 -18.153 1   191.05 ? 98  GLU B CB    1 
ATOM   2483 C  CG    . GLU B 2 98  ? 33.452  -27.606 -18.993 1   196.07 ? 98  GLU B CG    1 
ATOM   2484 C  CD    . GLU B 2 98  ? 34.593  -27.392 -19.967 1   202.17 ? 98  GLU B CD    1 
ATOM   2485 O  OE1   . GLU B 2 98  ? 35.389  -28.338 -20.165 1   203.28 ? 98  GLU B OE1   1 
ATOM   2486 O  OE2   . GLU B 2 98  ? 34.69   -26.281 -20.538 1   204.21 ? 98  GLU B OE2   1 
ATOM   2487 N  N     . ASP B 2 99  ? 31.033  -28.866 -16.954 1   189.56 ? 99  ASP B N     1 
ATOM   2488 C  CA    . ASP B 2 99  ? 30.931  -30.179 -16.313 1   190.27 ? 99  ASP B CA    1 
ATOM   2489 C  C     . ASP B 2 99  ? 30.273  -30.173 -14.917 1   190.53 ? 99  ASP B C     1 
ATOM   2490 O  O     . ASP B 2 99  ? 30.43   -31.148 -14.186 1   190.67 ? 99  ASP B O     1 
ATOM   2491 C  CB    . ASP B 2 99  ? 32.3    -30.89  -16.257 1   192.09 ? 99  ASP B CB    1 
ATOM   2492 C  CG    . ASP B 2 99  ? 33.011  -31.023 -17.594 1   196.62 ? 99  ASP B CG    1 
ATOM   2493 O  OD1   . ASP B 2 99  ? 32.394  -31.544 -18.545 1   197.27 ? 99  ASP B OD1   1 
ATOM   2494 O  OD2   . ASP B 2 99  ? 34.196  -30.629 -17.679 1   198.85 ? 99  ASP B OD2   1 
ATOM   2495 N  N     . SER B 2 100 ? 29.526  -29.116 -14.551 1   190.4  ? 100 SER B N     1 
ATOM   2496 C  CA    . SER B 2 100 ? 28.853  -29.076 -13.244 1   190.74 ? 100 SER B CA    1 
ATOM   2497 C  C     . SER B 2 100 ? 27.418  -29.661 -13.303 1   190.93 ? 100 SER B C     1 
ATOM   2498 O  O     . SER B 2 100 ? 26.915  -29.934 -14.388 1   191.13 ? 100 SER B O     1 
ATOM   2499 C  CB    . SER B 2 100 ? 28.854  -27.66  -12.677 1   191.94 ? 100 SER B CB    1 
ATOM   2500 O  OG    . SER B 2 100 ? 28.186  -26.766 -13.55  1   194.1  ? 100 SER B OG    1 
ATOM   2501 N  N     . SER B 2 101 ? 26.772  -29.884 -12.145 1   190.68 ? 101 SER B N     1 
ATOM   2502 C  CA    . SER B 2 101 ? 25.428  -30.465 -12.11  1   190.85 ? 101 SER B CA    1 
ATOM   2503 C  C     . SER B 2 101 ? 24.682  -30.028 -10.855 1   190.81 ? 101 SER B C     1 
ATOM   2504 O  O     . SER B 2 101 ? 25.243  -30.087 -9.765  1   191.01 ? 101 SER B O     1 
ATOM   2505 C  CB    . SER B 2 101 ? 25.519  -31.99  -12.174 1   192.08 ? 101 SER B CB    1 
ATOM   2506 O  OG    . SER B 2 101 ? 24.441  -32.675 -11.556 1   194.23 ? 101 SER B OG    1 
ATOM   2507 N  N     . ILE B 2 102 ? 23.412  -29.625 -10.996 1   190.43 ? 102 ILE B N     1 
ATOM   2508 C  CA    . ILE B 2 102 ? 22.601  -29.215 -9.849  1   190.56 ? 102 ILE B CA    1 
ATOM   2509 C  C     . ILE B 2 102 ? 21.104  -29.418 -10.118 1   190.36 ? 102 ILE B C     1 
ATOM   2510 O  O     . ILE B 2 102 ? 20.655  -29.327 -11.259 1   190.51 ? 102 ILE B O     1 
ATOM   2511 C  CB    . ILE B 2 102 ? 22.94   -27.765 -9.393  1   191.21 ? 102 ILE B CB    1 
ATOM   2512 C  CG1   . ILE B 2 102 ? 22.413  -27.455 -7.983  1   192.28 ? 102 ILE B CG1   1 
ATOM   2513 C  CG2   . ILE B 2 102 ? 22.49   -26.737 -10.404 1   191.69 ? 102 ILE B CG2   1 
ATOM   2514 C  CD1   . ILE B 2 102 ? 23.072  -28.242 -6.942  1   193.64 ? 102 ILE B CD1   1 
ATOM   2515 N  N     . SER B 2 103 ? 20.344  -29.744 -9.074  1   189.89 ? 103 SER B N     1 
ATOM   2516 C  CA    . SER B 2 103 ? 18.904  -29.912 -9.178  1   189.99 ? 103 SER B CA    1 
ATOM   2517 C  C     . SER B 2 103 ? 18.275  -29.026 -8.127  1   190.03 ? 103 SER B C     1 
ATOM   2518 O  O     . SER B 2 103 ? 18.651  -29.094 -6.965  1   190.1  ? 103 SER B O     1 
ATOM   2519 C  CB    . SER B 2 103 ? 18.507  -31.366 -8.962  1   191.14 ? 103 SER B CB    1 
ATOM   2520 O  OG    . SER B 2 103 ? 18.924  -32.162 -10.058 1   193.25 ? 103 SER B OG    1 
ATOM   2521 N  N     . LEU B 2 104 ? 17.36   -28.156 -8.543  1   189.89 ? 104 LEU B N     1 
ATOM   2522 C  CA    . LEU B 2 104 ? 16.692  -27.2   -7.673  1   190.21 ? 104 LEU B CA    1 
ATOM   2523 C  C     . LEU B 2 104 ? 15.217  -27.584 -7.503  1   190.49 ? 104 LEU B C     1 
ATOM   2524 O  O     . LEU B 2 104 ? 14.503  -27.77  -8.484  1   190.72 ? 104 LEU B O     1 
ATOM   2525 C  CB    . LEU B 2 104 ? 16.822  -25.792 -8.289  1   190.3  ? 104 LEU B CB    1 
ATOM   2526 C  CG    . LEU B 2 104 ? 16.856  -24.621 -7.319  1   191.58 ? 104 LEU B CG    1 
ATOM   2527 C  CD1   . LEU B 2 104 ? 17.775  -23.526 -7.827  1   192.08 ? 104 LEU B CD1   1 
ATOM   2528 C  CD2   . LEU B 2 104 ? 15.46   -24.086 -7.061  1   192.18 ? 104 LEU B CD2   1 
ATOM   2529 N  N     . MET B 2 105 ? 14.759  -27.686 -6.261  1   190.28 ? 105 MET B N     1 
ATOM   2530 C  CA    . MET B 2 105 ? 13.377  -28.034 -5.966  1   190.55 ? 105 MET B CA    1 
ATOM   2531 C  C     . MET B 2 105 ? 12.707  -26.871 -5.24   1   190.85 ? 105 MET B C     1 
ATOM   2532 O  O     . MET B 2 105 ? 12.811  -26.754 -4.023  1   191.05 ? 105 MET B O     1 
ATOM   2533 C  CB    . MET B 2 105 ? 13.35   -29.278 -5.088  1   191.14 ? 105 MET B CB    1 
ATOM   2534 C  CG    . MET B 2 105 ? 12.206  -30.196 -5.361  1   193.34 ? 105 MET B CG    1 
ATOM   2535 S  SD    . MET B 2 105 ? 12.041  -31.398 -4.013  1   197.54 ? 105 MET B SD    1 
ATOM   2536 C  CE    . MET B 2 105 ? 13.629  -32.207 -4.07   1   195.96 ? 105 MET B CE    1 
ATOM   2537 N  N     . SER B 2 106 ? 12.03   -26.006 -5.991  1   190.83 ? 106 SER B N     1 
ATOM   2538 C  CA    . SER B 2 106 ? 11.342  -24.841 -5.449  1   191.32 ? 106 SER B CA    1 
ATOM   2539 C  C     . SER B 2 106 ? 9.956   -25.234 -4.927  1   192.08 ? 106 SER B C     1 
ATOM   2540 O  O     . SER B 2 106 ? 9.24    -25.995 -5.576  1   192.22 ? 106 SER B O     1 
ATOM   2541 C  CB    . SER B 2 106 ? 11.233  -23.755 -6.517  1   192.02 ? 106 SER B CB    1 
ATOM   2542 O  OG    . SER B 2 106 ? 10.441  -22.649 -6.117  1   193.54 ? 106 SER B OG    1 
ATOM   2543 N  N     . HIS B 2 107 ? 9.593   -24.735 -3.742  1   192.43 ? 107 HIS B N     1 
ATOM   2544 C  CA    . HIS B 2 107 ? 8.3     -25.022 -3.127  1   193.2  ? 107 HIS B CA    1 
ATOM   2545 C  C     . HIS B 2 107 ? 7.571   -23.735 -2.774  1   193.66 ? 107 HIS B C     1 
ATOM   2546 O  O     . HIS B 2 107 ? 8.13    -22.898 -2.069  1   193.91 ? 107 HIS B O     1 
ATOM   2547 C  CB    . HIS B 2 107 ? 8.486   -25.855 -1.855  1   194.12 ? 107 HIS B CB    1 
ATOM   2548 C  CG    . HIS B 2 107 ? 8.003   -27.258 -1.987  1   196.59 ? 107 HIS B CG    1 
ATOM   2549 N  ND1   . HIS B 2 107 ? 8.56    -28.278 -1.243  1   198.55 ? 107 HIS B ND1   1 
ATOM   2550 C  CD2   . HIS B 2 107 ? 7.029   -27.77  -2.775  1   197.82 ? 107 HIS B CD2   1 
ATOM   2551 C  CE1   . HIS B 2 107 ? 7.907   -29.373 -1.594  1   199.15 ? 107 HIS B CE1   1 
ATOM   2552 N  NE2   . HIS B 2 107 ? 6.978   -29.115 -2.516  1   199.02 ? 107 HIS B NE2   1 
ATOM   2553 N  N     . CYS B 2 108 ? 6.324   -23.578 -3.236  1   193.53 ? 108 CYS B N     1 
ATOM   2554 C  CA    . CYS B 2 108 ? 5.55    -22.379 -2.927  1   193.78 ? 108 CYS B CA    1 
ATOM   2555 C  C     . CYS B 2 108 ? 4.314   -22.731 -2.11   1   193.69 ? 108 CYS B C     1 
ATOM   2556 O  O     . CYS B 2 108 ? 3.486   -23.525 -2.553  1   193.69 ? 108 CYS B O     1 
ATOM   2557 C  CB    . CYS B 2 108 ? 5.18    -21.616 -4.197  1   194.54 ? 108 CYS B CB    1 
ATOM   2558 S  SG    . CYS B 2 108 ? 6.583   -20.838 -5.047  1   197.55 ? 108 CYS B SG    1 
ATOM   2559 N  N     . SER B 2 109 ? 4.19    -22.145 -0.919  1   193.48 ? 109 SER B N     1 
ATOM   2560 C  CA    . SER B 2 109 ? 3.028   -22.383 -0.073  1   193.8  ? 109 SER B CA    1 
ATOM   2561 C  C     . SER B 2 109 ? 2.32    -21.057 0.192   1   194.18 ? 109 SER B C     1 
ATOM   2562 O  O     . SER B 2 109 ? 2.802   -20.242 0.981   1   194.3  ? 109 SER B O     1 
ATOM   2563 C  CB    . SER B 2 109 ? 3.436   -23.05  1.235   1   194.79 ? 109 SER B CB    1 
ATOM   2564 O  OG    . SER B 2 109 ? 2.363   -23.816 1.758   1   196.65 ? 109 SER B OG    1 
ATOM   2565 N  N     . PHE B 2 110 ? 1.195   -20.823 -0.502  1   194.13 ? 110 PHE B N     1 
ATOM   2566 C  CA    . PHE B 2 110 ? 0.411   -19.594 -0.355  1   194.47 ? 110 PHE B CA    1 
ATOM   2567 C  C     . PHE B 2 110 ? -1.012  -19.972 0.08    1   194.57 ? 110 PHE B C     1 
ATOM   2568 O  O     . PHE B 2 110 ? -1.922  -20.009 -0.751  1   194.62 ? 110 PHE B O     1 
ATOM   2569 C  CB    . PHE B 2 110 ? 0.368   -18.804 -1.685  1   194.42 ? 110 PHE B CB    1 
ATOM   2570 C  CG    . PHE B 2 110 ? 1.689   -18.59  -2.401  1   194.99 ? 110 PHE B CG    1 
ATOM   2571 C  CD1   . PHE B 2 110 ? 2.814   -18.18  -1.71   1   195.65 ? 110 PHE B CD1   1 
ATOM   2572 C  CD2   . PHE B 2 110 ? 1.783   -18.734 -3.775  1   195.67 ? 110 PHE B CD2   1 
ATOM   2573 C  CE1   . PHE B 2 110 ? 4.024   -17.992 -2.366  1   196.25 ? 110 PHE B CE1   1 
ATOM   2574 C  CE2   . PHE B 2 110 ? 2.99    -18.527 -4.43   1   196.28 ? 110 PHE B CE2   1 
ATOM   2575 C  CZ    . PHE B 2 110 ? 4.1     -18.153 -3.721  1   196.03 ? 110 PHE B CZ    1 
ATOM   2576 N  N     . PRO B 2 111 ? -1.226  -20.28  1.374   1   194.45 ? 111 PRO B N     1 
ATOM   2577 C  CA    . PRO B 2 111 ? -2.566  -20.71  1.807   1   194.36 ? 111 PRO B CA    1 
ATOM   2578 C  C     . PRO B 2 111 ? -3.577  -19.593 2.088   1   194.18 ? 111 PRO B C     1 
ATOM   2579 O  O     . PRO B 2 111 ? -4.776  -19.827 1.932   1   194.4  ? 111 PRO B O     1 
ATOM   2580 C  CB    . PRO B 2 111 ? -2.279  -21.542 3.056   1   195.14 ? 111 PRO B CB    1 
ATOM   2581 C  CG    . PRO B 2 111 ? -1.028  -20.942 3.621   1   195.66 ? 111 PRO B CG    1 
ATOM   2582 C  CD    . PRO B 2 111 ? -0.253  -20.315 2.487   1   194.04 ? 111 PRO B CD    1 
ATOM   2583 N  N     . LYS B 2 112 ? -3.115  -18.402 2.53    1   193.53 ? 112 LYS B N     1 
ATOM   2584 C  CA    . LYS B 2 112 ? -4.013  -17.282 2.823   1   193.25 ? 112 LYS B CA    1 
ATOM   2585 C  C     . LYS B 2 112 ? -4.559  -16.666 1.533   1   193.01 ? 112 LYS B C     1 
ATOM   2586 O  O     . LYS B 2 112 ? -5.754  -16.383 1.445   1   193.27 ? 112 LYS B O     1 
ATOM   2587 C  CB    . LYS B 2 112 ? -3.324  -16.232 3.699   1   194.5  ? 112 LYS B CB    1 
ATOM   2588 C  CG    . LYS B 2 112 ? -3.889  -16.169 5.111   1   197.75 ? 112 LYS B CG    1 
ATOM   2589 C  CD    . LYS B 2 112 ? -3.576  -17.428 5.897   1   201.36 ? 112 LYS B CD    1 
ATOM   2590 C  CE    . LYS B 2 112 ? -3.869  -17.257 7.366   1   204.6  ? 112 LYS B CE    1 
ATOM   2591 N  NZ    . LYS B 2 112 ? -3.006  -16.214 7.979   1   206.56 ? 112 LYS B NZ    1 
ATOM   2592 N  N     . GLY B 2 113 ? -3.673  -16.49  0.552   1   192.24 ? 113 GLY B N     1 
ATOM   2593 C  CA    . GLY B 2 113 ? -3.957  -16.021 -0.804  1   191.77 ? 113 GLY B CA    1 
ATOM   2594 C  C     . GLY B 2 113 ? -4.642  -14.689 -1.058  1   190.86 ? 113 GLY B C     1 
ATOM   2595 O  O     . GLY B 2 113 ? -5.261  -14.533 -2.117  1   191.06 ? 113 GLY B O     1 
ATOM   2596 N  N     . LYS B 2 114 ? -4.548  -13.718 -0.126  1   189.54 ? 114 LYS B N     1 
ATOM   2597 C  CA    . LYS B 2 114 ? -5.184  -12.421 -0.343  1   188.72 ? 114 LYS B CA    1 
ATOM   2598 C  C     . LYS B 2 114 ? -4.167  -11.336 -0.666  1   187.68 ? 114 LYS B C     1 
ATOM   2599 O  O     . LYS B 2 114 ? -3.406  -10.924 0.202   1   187.85 ? 114 LYS B O     1 
ATOM   2600 C  CB    . LYS B 2 114 ? -6.07   -12.018 0.84    1   190.31 ? 114 LYS B CB    1 
ATOM   2601 C  CG    . LYS B 2 114 ? -6.842  -10.731 0.579   1   193.97 ? 114 LYS B CG    1 
ATOM   2602 C  CD    . LYS B 2 114 ? -6.342  -9.58   1.443   1   197.92 ? 114 LYS B CD    1 
ATOM   2603 C  CE    . LYS B 2 114 ? -6.899  -8.245  1.013   1   201.57 ? 114 LYS B CE    1 
ATOM   2604 N  NZ    . LYS B 2 114 ? -6.221  -7.72   -0.203  1   203.98 ? 114 LYS B NZ    1 
ATOM   2605 N  N     . GLY B 2 115 ? -4.165  -10.887 -1.913  1   186.49 ? 115 GLY B N     1 
ATOM   2606 C  CA    . GLY B 2 115 ? -3.271  -9.836  -2.383  1   185.85 ? 115 GLY B CA    1 
ATOM   2607 C  C     . GLY B 2 115 ? -1.852  -10.274 -2.69   1   184.93 ? 115 GLY B C     1 
ATOM   2608 O  O     . GLY B 2 115 ? -0.982  -9.431  -2.91   1   184.85 ? 115 GLY B O     1 
ATOM   2609 N  N     . ILE B 2 116 ? -1.605  -11.593 -2.717  1   184.17 ? 116 ILE B N     1 
ATOM   2610 C  CA    . ILE B 2 116 ? -0.293  -12.191 -2.995  1   183.82 ? 116 ILE B CA    1 
ATOM   2611 C  C     . ILE B 2 116 ? 0.181   -11.96  -4.442  1   182.16 ? 116 ILE B C     1 
ATOM   2612 O  O     . ILE B 2 116 ? -0.628  -11.89  -5.367  1   182.28 ? 116 ILE B O     1 
ATOM   2613 C  CB    . ILE B 2 116 ? -0.32   -13.715 -2.65   1   185.14 ? 116 ILE B CB    1 
ATOM   2614 C  CG1   . ILE B 2 116 ? -0.551  -13.951 -1.134  1   186.64 ? 116 ILE B CG1   1 
ATOM   2615 C  CG2   . ILE B 2 116 ? 0.923   -14.471 -3.18   1   185.7  ? 116 ILE B CG2   1 
ATOM   2616 C  CD1   . ILE B 2 116 ? -0.527  -15.45  -0.681  1   188.25 ? 116 ILE B CD1   1 
ATOM   2617 N  N     . LYS B 2 117 ? 1.501   -11.862 -4.625  1   180.39 ? 117 LYS B N     1 
ATOM   2618 C  CA    . LYS B 2 117 ? 2.116   -11.705 -5.928  1   179.12 ? 117 LYS B CA    1 
ATOM   2619 C  C     . LYS B 2 117 ? 3.52    -12.276 -5.859  1   177.42 ? 117 LYS B C     1 
ATOM   2620 O  O     . LYS B 2 117 ? 4.399   -11.648 -5.289  1   177.55 ? 117 LYS B O     1 
ATOM   2621 C  CB    . LYS B 2 117 ? 2.172   -10.226 -6.328  1   180.91 ? 117 LYS B CB    1 
ATOM   2622 C  CG    . LYS B 2 117 ? 1.966   -9.998  -7.819  1   184.75 ? 117 LYS B CG    1 
ATOM   2623 C  CD    . LYS B 2 117 ? 1.724   -8.522  -8.122  1   189    ? 117 LYS B CD    1 
ATOM   2624 C  CE    . LYS B 2 117 ? 1.022   -8.324  -9.447  1   192.44 ? 117 LYS B CE    1 
ATOM   2625 N  NZ    . LYS B 2 117 ? 0.536   -6.928  -9.624  1   194.5  ? 117 LYS B NZ    1 
ATOM   2626 N  N     . HIS B 2 118 ? 3.73    -13.471 -6.398  1   175.79 ? 118 HIS B N     1 
ATOM   2627 C  CA    . HIS B 2 118 ? 5.055   -14.082 -6.422  1   174.71 ? 118 HIS B CA    1 
ATOM   2628 C  C     . HIS B 2 118 ? 5.603   -13.868 -7.824  1   172.56 ? 118 HIS B C     1 
ATOM   2629 O  O     . HIS B 2 118 ? 5.095   -14.469 -8.767  1   172.87 ? 118 HIS B O     1 
ATOM   2630 C  CB    . HIS B 2 118 ? 4.974   -15.59  -6.095  1   176.16 ? 118 HIS B CB    1 
ATOM   2631 C  CG    . HIS B 2 118 ? 6.222   -16.37  -6.414  1   179.12 ? 118 HIS B CG    1 
ATOM   2632 N  ND1   . HIS B 2 118 ? 7.279   -16.439 -5.523  1   181.11 ? 118 HIS B ND1   1 
ATOM   2633 C  CD2   . HIS B 2 118 ? 6.534   -17.094 -7.517  1   180.38 ? 118 HIS B CD2   1 
ATOM   2634 C  CE1   . HIS B 2 118 ? 8.196   -17.192 -6.109  1   181.69 ? 118 HIS B CE1   1 
ATOM   2635 N  NE2   . HIS B 2 118 ? 7.794   -17.608 -7.312  1   181.56 ? 118 HIS B NE2   1 
ATOM   2636 N  N     . ILE B 2 119 ? 6.609   -13.007 -7.976  1   170.19 ? 119 ILE B N     1 
ATOM   2637 C  CA    . ILE B 2 119 ? 7.193   -12.751 -9.286  1   168.27 ? 119 ILE B CA    1 
ATOM   2638 C  C     . ILE B 2 119 ? 8.636   -13.201 -9.292  1   166.31 ? 119 ILE B C     1 
ATOM   2639 O  O     . ILE B 2 119 ? 9.401   -12.752 -8.448  1   166.45 ? 119 ILE B O     1 
ATOM   2640 C  CB    . ILE B 2 119 ? 7.044   -11.259 -9.665  1   168.32 ? 119 ILE B CB    1 
ATOM   2641 C  CG1   . ILE B 2 119 ? 5.557   -10.904 -9.841  1   168.99 ? 119 ILE B CG1   1 
ATOM   2642 C  CG2   . ILE B 2 119 ? 7.858   -10.93  -10.918 1   168.82 ? 119 ILE B CG2   1 
ATOM   2643 C  CD1   . ILE B 2 119 ? 5.268   -9.486  -10.136 1   170.19 ? 119 ILE B CD1   1 
ATOM   2644 N  N     . MET B 2 120 ? 9.011   -14.097 -10.212 1   164.26 ? 120 MET B N     1 
ATOM   2645 C  CA    . MET B 2 120 ? 10.392  -14.546 -10.294 1   162.68 ? 120 MET B CA    1 
ATOM   2646 C  C     . MET B 2 120 ? 10.927  -14.241 -11.663 1   160.16 ? 120 MET B C     1 
ATOM   2647 O  O     . MET B 2 120 ? 10.318  -14.622 -12.649 1   160.3  ? 120 MET B O     1 
ATOM   2648 C  CB    . MET B 2 120 ? 10.509  -16.04  -10.004 1   163.85 ? 120 MET B CB    1 
ATOM   2649 C  CG    . MET B 2 120 ? 11.92   -16.56  -10.106 1   167.11 ? 120 MET B CG    1 
ATOM   2650 S  SD    . MET B 2 120 ? 11.912  -18.355 -9.932  1   175.45 ? 120 MET B SD    1 
ATOM   2651 C  CE    . MET B 2 120 ? 11.186  -18.836 -11.506 1   174.85 ? 120 MET B CE    1 
ATOM   2652 N  N     . ASN B 2 121 ? 12.05   -13.548 -11.731 1   157.78 ? 121 ASN B N     1 
ATOM   2653 C  CA    . ASN B 2 121 ? 12.683  -13.223 -12.995 1   156.03 ? 121 ASN B CA    1 
ATOM   2654 C  C     . ASN B 2 121 ? 14.037  -13.88  -12.923 1   153.86 ? 121 ASN B C     1 
ATOM   2655 O  O     . ASN B 2 121 ? 14.829  -13.542 -12.052 1   153.94 ? 121 ASN B O     1 
ATOM   2656 C  CB    . ASN B 2 121 ? 12.831  -11.718 -13.141 1   157.08 ? 121 ASN B CB    1 
ATOM   2657 C  CG    . ASN B 2 121 ? 11.538  -10.982 -12.932 1   160.04 ? 121 ASN B CG    1 
ATOM   2658 O  OD1   . ASN B 2 121 ? 10.502  -11.31  -13.521 1   160.87 ? 121 ASN B OD1   1 
ATOM   2659 N  ND2   . ASN B 2 121 ? 11.572  -9.981  -12.072 1   160.94 ? 121 ASN B ND2   1 
ATOM   2660 N  N     . GLY B 2 122 ? 14.274  -14.852 -13.784 1   151.83 ? 122 GLY B N     1 
ATOM   2661 C  CA    . GLY B 2 122 ? 15.519  -15.596 -13.759 1   150.41 ? 122 GLY B CA    1 
ATOM   2662 C  C     . GLY B 2 122 ? 16.296  -15.649 -15.052 1   148.6  ? 122 GLY B C     1 
ATOM   2663 O  O     . GLY B 2 122 ? 15.726  -15.629 -16.143 1   148.51 ? 122 GLY B O     1 
ATOM   2664 N  N     . ILE B 2 123 ? 17.613  -15.722 -14.924 1   147.15 ? 123 ILE B N     1 
ATOM   2665 C  CA    . ILE B 2 123 ? 18.529  -15.862 -16.044 1   146.4  ? 123 ILE B CA    1 
ATOM   2666 C  C     . ILE B 2 123 ? 19.364  -17.092 -15.724 1   145.29 ? 123 ILE B C     1 
ATOM   2667 O  O     . ILE B 2 123 ? 20.088  -17.097 -14.734 1   145.56 ? 123 ILE B O     1 
ATOM   2668 C  CB    . ILE B 2 123 ? 19.443  -14.627 -16.208 1   147.1  ? 123 ILE B CB    1 
ATOM   2669 C  CG1   . ILE B 2 123 ? 18.643  -13.331 -16.487 1   148.14 ? 123 ILE B CG1   1 
ATOM   2670 C  CG2   . ILE B 2 123 ? 20.523  -14.884 -17.264 1   147.65 ? 123 ILE B CG2   1 
ATOM   2671 C  CD1   . ILE B 2 123 ? 18.09   -13.146 -17.889 1   149.39 ? 123 ILE B CD1   1 
ATOM   2672 N  N     . ILE B 2 124 ? 19.232  -18.147 -16.513 1   143.93 ? 124 ILE B N     1 
ATOM   2673 C  CA    . ILE B 2 124 ? 19.968  -19.378 -16.295 1   143.09 ? 124 ILE B CA    1 
ATOM   2674 C  C     . ILE B 2 124 ? 20.974  -19.577 -17.415 1   142.15 ? 124 ILE B C     1 
ATOM   2675 O  O     . ILE B 2 124 ? 20.629  -19.448 -18.579 1   142.12 ? 124 ILE B O     1 
ATOM   2676 C  CB    . ILE B 2 124 ? 18.984  -20.551 -16.138 1   143.52 ? 124 ILE B CB    1 
ATOM   2677 C  CG1   . ILE B 2 124 ? 18.089  -20.32  -14.913 1   144.4  ? 124 ILE B CG1   1 
ATOM   2678 C  CG2   . ILE B 2 124 ? 19.721  -21.882 -16.044 1   144.07 ? 124 ILE B CG2   1 
ATOM   2679 C  CD1   . ILE B 2 124 ? 16.955  -21.237 -14.811 1   145.65 ? 124 ILE B CD1   1 
ATOM   2680 N  N     . LYS B 2 125 ? 22.235  -19.8   -17.064 1   141.33 ? 125 LYS B N     1 
ATOM   2681 C  CA    . LYS B 2 125 ? 23.303  -19.999 -18.031 1   141.17 ? 125 LYS B CA    1 
ATOM   2682 C  C     . LYS B 2 125 ? 23.979  -21.322 -17.717 1   140.66 ? 125 LYS B C     1 
ATOM   2683 O  O     . LYS B 2 125 ? 24.67   -21.435 -16.709 1   140.85 ? 125 LYS B O     1 
ATOM   2684 C  CB    . LYS B 2 125 ? 24.321  -18.854 -17.951 1   143.33 ? 125 LYS B CB    1 
ATOM   2685 C  CG    . LYS B 2 125 ? 23.705  -17.46  -18.097 1   147.77 ? 125 LYS B CG    1 
ATOM   2686 C  CD    . LYS B 2 125 ? 24.764  -16.347 -18.094 1   151.99 ? 125 LYS B CD    1 
ATOM   2687 C  CE    . LYS B 2 125 ? 24.16   -14.968 -18.183 1   155.42 ? 125 LYS B CE    1 
ATOM   2688 N  NZ    . LYS B 2 125 ? 24.922  -14.095 -19.111 1   157.71 ? 125 LYS B NZ    1 
ATOM   2689 N  N     . ILE B 2 126 ? 23.745  -22.33  -18.56  1   139.87 ? 126 ILE B N     1 
ATOM   2690 C  CA    . ILE B 2 126 ? 24.272  -23.683 -18.408 1   139.54 ? 126 ILE B CA    1 
ATOM   2691 C  C     . ILE B 2 126 ? 25.51   -23.841 -19.295 1   139.5  ? 126 ILE B C     1 
ATOM   2692 O  O     . ILE B 2 126 ? 25.424  -23.681 -20.507 1   139.55 ? 126 ILE B O     1 
ATOM   2693 C  CB    . ILE B 2 126 ? 23.147  -24.704 -18.737 1   139.6  ? 126 ILE B CB    1 
ATOM   2694 C  CG1   . ILE B 2 126 ? 21.914  -24.453 -17.855 1   140.28 ? 126 ILE B CG1   1 
ATOM   2695 C  CG2   . ILE B 2 126 ? 23.627  -26.143 -18.601 1   139.94 ? 126 ILE B CG2   1 
ATOM   2696 C  CD1   . ILE B 2 126 ? 20.674  -24.953 -18.407 1   141.45 ? 126 ILE B CD1   1 
ATOM   2697 N  N     . GLY B 2 127 ? 26.654  -24.108 -18.673 1   139.28 ? 127 GLY B N     1 
ATOM   2698 C  CA    . GLY B 2 127 ? 27.934  -24.241 -19.36  1   139.45 ? 127 GLY B CA    1 
ATOM   2699 C  C     . GLY B 2 127 ? 28.131  -25.53  -20.128 1   139.31 ? 127 GLY B C     1 
ATOM   2700 O  O     . GLY B 2 127 ? 27.246  -26.385 -20.161 1   139.35 ? 127 GLY B O     1 
ATOM   2701 N  N     . LYS B 2 128 ? 29.299  -25.661 -20.768 1   139.05 ? 128 LYS B N     1 
ATOM   2702 C  CA    . LYS B 2 128 ? 29.655  -26.823 -21.572 1   139.37 ? 128 LYS B CA    1 
ATOM   2703 C  C     . LYS B 2 128 ? 29.59   -28.107 -20.745 1   139.71 ? 128 LYS B C     1 
ATOM   2704 O  O     . LYS B 2 128 ? 30.302  -28.236 -19.759 1   139.79 ? 128 LYS B O     1 
ATOM   2705 C  CB    . LYS B 2 128 ? 31.051  -26.626 -22.189 1   140.84 ? 128 LYS B CB    1 
ATOM   2706 C  CG    . LYS B 2 128 ? 31.573  -27.831 -22.956 1   144.23 ? 128 LYS B CG    1 
ATOM   2707 C  CD    . LYS B 2 128 ? 32.966  -27.577 -23.492 1   147.97 ? 128 LYS B CD    1 
ATOM   2708 C  CE    . LYS B 2 128 ? 33.636  -28.858 -23.92  1   151.31 ? 128 LYS B CE    1 
ATOM   2709 N  NZ    . LYS B 2 128 ? 33.575  -29.897 -22.859 1   153.32 ? 128 LYS B NZ    1 
ATOM   2710 N  N     . ASN B 2 129 ? 28.691  -29.026 -21.126 1   139.79 ? 129 ASN B N     1 
ATOM   2711 C  CA    . ASN B 2 129 ? 28.46   -30.323 -20.478 1   140.25 ? 129 ASN B CA    1 
ATOM   2712 C  C     . ASN B 2 129 ? 27.949  -30.206 -19.032 1   140.01 ? 129 ASN B C     1 
ATOM   2713 O  O     . ASN B 2 129 ? 28.171  -31.109 -18.225 1   139.98 ? 129 ASN B O     1 
ATOM   2714 C  CB    . ASN B 2 129 ? 29.686  -31.237 -20.574 1   141.76 ? 129 ASN B CB    1 
ATOM   2715 C  CG    . ASN B 2 129 ? 30.059  -31.579 -21.998 1   145.38 ? 129 ASN B CG    1 
ATOM   2716 O  OD1   . ASN B 2 129 ? 29.214  -31.983 -22.806 1   146.81 ? 129 ASN B OD1   1 
ATOM   2717 N  ND2   . ASN B 2 129 ? 31.332  -31.425 -22.34  1   145.98 ? 129 ASN B ND2   1 
ATOM   2718 N  N     . ALA B 2 130 ? 27.231  -29.115 -18.725 1   139.64 ? 130 ALA B N     1 
ATOM   2719 C  CA    . ALA B 2 130 ? 26.632  -28.91  -17.407 1   139.84 ? 130 ALA B CA    1 
ATOM   2720 C  C     . ALA B 2 130 ? 25.167  -29.376 -17.402 1   139.96 ? 130 ALA B C     1 
ATOM   2721 O  O     . ALA B 2 130 ? 24.577  -29.522 -18.466 1   140.11 ? 130 ALA B O     1 
ATOM   2722 C  CB    . ALA B 2 130 ? 26.729  -27.447 -17.003 1   139.97 ? 130 ALA B CB    1 
ATOM   2723 N  N     . LYS B 2 131 ? 24.583  -29.633 -16.22  1   139.9  ? 131 LYS B N     1 
ATOM   2724 C  CA    . LYS B 2 131 ? 23.203  -30.118 -16.137 1   140.46 ? 131 LYS B CA    1 
ATOM   2725 C  C     . LYS B 2 131 ? 22.386  -29.417 -15.059 1   140.99 ? 131 LYS B C     1 
ATOM   2726 O  O     . LYS B 2 131 ? 22.705  -29.528 -13.878 1   140.97 ? 131 LYS B O     1 
ATOM   2727 C  CB    . LYS B 2 131 ? 23.189  -31.636 -15.901 1   142.2  ? 131 LYS B CB    1 
ATOM   2728 C  CG    . LYS B 2 131 ? 21.807  -32.24  -15.646 1   146.4  ? 131 LYS B CG    1 
ATOM   2729 C  CD    . LYS B 2 131 ? 21.905  -33.455 -14.711 1   151.16 ? 131 LYS B CD    1 
ATOM   2730 C  CE    . LYS B 2 131 ? 20.798  -33.525 -13.679 1   154.93 ? 131 LYS B CE    1 
ATOM   2731 N  NZ    . LYS B 2 131 ? 21.226  -34.212 -12.425 1   156.97 ? 131 LYS B NZ    1 
ATOM   2732 N  N     . PHE B 2 132 ? 21.292  -28.759 -15.457 1   141.34 ? 132 PHE B N     1 
ATOM   2733 C  CA    . PHE B 2 132 ? 20.399  -28.085 -14.521 1   142.16 ? 132 PHE B CA    1 
ATOM   2734 C  C     . PHE B 2 132 ? 18.999  -28.687 -14.588 1   143.16 ? 132 PHE B C     1 
ATOM   2735 O  O     . PHE B 2 132 ? 18.478  -28.94  -15.67  1   143.12 ? 132 PHE B O     1 
ATOM   2736 C  CB    . PHE B 2 132 ? 20.344  -26.566 -14.781 1   141.86 ? 132 PHE B CB    1 
ATOM   2737 C  CG    . PHE B 2 132 ? 19.489  -25.8   -13.793 1   142.1  ? 132 PHE B CG    1 
ATOM   2738 C  CD1   . PHE B 2 132 ? 19.818  -25.762 -12.452 1   142.71 ? 132 PHE B CD1   1 
ATOM   2739 C  CD2   . PHE B 2 132 ? 18.365  -25.109 -14.211 1   142.59 ? 132 PHE B CD2   1 
ATOM   2740 C  CE1   . PHE B 2 132 ? 19.029  -25.07  -11.545 1   143.27 ? 132 PHE B CE1   1 
ATOM   2741 C  CE2   . PHE B 2 132 ? 17.582  -24.411 -13.301 1   143.11 ? 132 PHE B CE2   1 
ATOM   2742 C  CZ    . PHE B 2 132 ? 17.918  -24.395 -11.976 1   142.94 ? 132 PHE B CZ    1 
ATOM   2743 N  N     . SER B 2 133 ? 18.398  -28.915 -13.427 1   143.96 ? 133 SER B N     1 
ATOM   2744 C  CA    . SER B 2 133 ? 17.058  -29.464 -13.316 1   145.38 ? 133 SER B CA    1 
ATOM   2745 C  C     . SER B 2 133 ? 16.284  -28.619 -12.33  1   147    ? 133 SER B C     1 
ATOM   2746 O  O     . SER B 2 133 ? 16.788  -28.322 -11.263 1   147.02 ? 133 SER B O     1 
ATOM   2747 C  CB    . SER B 2 133 ? 17.119  -30.9   -12.82  1   146.69 ? 133 SER B CB    1 
ATOM   2748 O  OG    . SER B 2 133 ? 17.972  -31.664 -13.654 1   148.9  ? 133 SER B OG    1 
ATOM   2749 N  N     . TYR B 2 134 ? 15.07   -28.223 -12.679 1   148.32 ? 134 TYR B N     1 
ATOM   2750 C  CA    . TYR B 2 134 ? 14.237  -27.368 -11.849 1   150.26 ? 134 TYR B CA    1 
ATOM   2751 C  C     . TYR B 2 134 ? 12.853  -27.979 -11.677 1   151.86 ? 134 TYR B C     1 
ATOM   2752 O  O     . TYR B 2 134 ? 12.238  -28.37  -12.661 1   152.23 ? 134 TYR B O     1 
ATOM   2753 C  CB    . TYR B 2 134 ? 14.099  -26.006 -12.532 1   150.69 ? 134 TYR B CB    1 
ATOM   2754 C  CG    . TYR B 2 134 ? 13.417  -24.964 -11.68  1   151.97 ? 134 TYR B CG    1 
ATOM   2755 C  CD1   . TYR B 2 134 ? 14.117  -24.268 -10.706 1   153.05 ? 134 TYR B CD1   1 
ATOM   2756 C  CD2   . TYR B 2 134 ? 12.084  -24.638 -11.882 1   153.1  ? 134 TYR B CD2   1 
ATOM   2757 C  CE1   . TYR B 2 134 ? 13.503  -23.291 -9.937  1   154.1  ? 134 TYR B CE1   1 
ATOM   2758 C  CE2   . TYR B 2 134 ? 11.46   -23.658 -11.122 1   154.18 ? 134 TYR B CE2   1 
ATOM   2759 C  CZ    . TYR B 2 134 ? 12.173  -22.989 -10.146 1   155.17 ? 134 TYR B CZ    1 
ATOM   2760 O  OH    . TYR B 2 134 ? 11.573  -22.016 -9.386  1   156.89 ? 134 TYR B OH    1 
ATOM   2761 N  N     . ASN B 2 135 ? 12.35   -28.042 -10.443 1   152.74 ? 135 ASN B N     1 
ATOM   2762 C  CA    . ASN B 2 135 ? 11.025  -28.593 -10.166 1   154.18 ? 135 ASN B CA    1 
ATOM   2763 C  C     . ASN B 2 135 ? 10.299  -27.659 -9.228  1   155.82 ? 135 ASN B C     1 
ATOM   2764 O  O     . ASN B 2 135 ? 10.718  -27.528 -8.084  1   156.02 ? 135 ASN B O     1 
ATOM   2765 C  CB    . ASN B 2 135 ? 11.151  -29.954 -9.491  1   155.2  ? 135 ASN B CB    1 
ATOM   2766 C  CG    . ASN B 2 135 ? 11.067  -31.122 -10.432 1   158.16 ? 135 ASN B CG    1 
ATOM   2767 O  OD1   . ASN B 2 135 ? 11.99   -31.405 -11.199 1   159.17 ? 135 ASN B OD1   1 
ATOM   2768 N  ND2   . ASN B 2 135 ? 9.96    -31.84  -10.382 1   158.87 ? 135 ASN B ND2   1 
ATOM   2769 N  N     . GLU B 2 136 ? 9.224   -27.012 -9.684  1   156.96 ? 136 GLU B N     1 
ATOM   2770 C  CA    . GLU B 2 136 ? 8.475   -26.085 -8.841  1   158.81 ? 136 GLU B CA    1 
ATOM   2771 C  C     . GLU B 2 136 ? 7.074   -26.59  -8.57   1   160.15 ? 136 GLU B C     1 
ATOM   2772 O  O     . GLU B 2 136 ? 6.322   -26.858 -9.5    1   160.21 ? 136 GLU B O     1 
ATOM   2773 C  CB    . GLU B 2 136 ? 8.433   -24.672 -9.453  1   161.71 ? 136 GLU B CB    1 
ATOM   2774 C  CG    . GLU B 2 136 ? 7.666   -23.658 -8.613  1   167.55 ? 136 GLU B CG    1 
ATOM   2775 C  CD    . GLU B 2 136 ? 7.83    -22.2   -9.005  1   174.8  ? 136 GLU B CD    1 
ATOM   2776 O  OE1   . GLU B 2 136 ? 8.986   -21.758 -9.191  1   176.17 ? 136 GLU B OE1   1 
ATOM   2777 O  OE2   . GLU B 2 136 ? 6.802   -21.495 -9.12   1   177.46 ? 136 GLU B OE2   1 
ATOM   2778 N  N     . PHE B 2 137 ? 6.72    -26.717 -7.294  1   161.2  ? 137 PHE B N     1 
ATOM   2779 C  CA    . PHE B 2 137 ? 5.397   -27.183 -6.903  1   162.87 ? 137 PHE B CA    1 
ATOM   2780 C  C     . PHE B 2 137 ? 4.681   -26.09  -6.12   1   164.28 ? 137 PHE B C     1 
ATOM   2781 O  O     . PHE B 2 137 ? 5.304   -25.385 -5.328  1   164.43 ? 137 PHE B O     1 
ATOM   2782 C  CB    . PHE B 2 137 ? 5.481   -28.471 -6.065  1   163.14 ? 137 PHE B CB    1 
ATOM   2783 C  CG    . PHE B 2 137 ? 6.525   -29.473 -6.503  1   164.19 ? 137 PHE B CG    1 
ATOM   2784 C  CD1   . PHE B 2 137 ? 6.501   -30.015 -7.778  1   165.18 ? 137 PHE B CD1   1 
ATOM   2785 C  CD2   . PHE B 2 137 ? 7.546   -29.849 -5.649  1   165.13 ? 137 PHE B CD2   1 
ATOM   2786 C  CE1   . PHE B 2 137 ? 7.459   -30.94  -8.173  1   166    ? 137 PHE B CE1   1 
ATOM   2787 C  CE2   . PHE B 2 137 ? 8.507   -30.765 -6.05   1   165.95 ? 137 PHE B CE2   1 
ATOM   2788 C  CZ    . PHE B 2 137 ? 8.458   -31.305 -7.308  1   165.83 ? 137 PHE B CZ    1 
ATOM   2789 N  N     . HIS B 2 138 ? 3.374   -25.947 -6.338  1   165.24 ? 138 HIS B N     1 
ATOM   2790 C  CA    . HIS B 2 138 ? 2.591   -24.93  -5.654  1   166.82 ? 138 HIS B CA    1 
ATOM   2791 C  C     . HIS B 2 138 ? 1.457   -25.531 -4.853  1   168.08 ? 138 HIS B C     1 
ATOM   2792 O  O     . HIS B 2 138 ? 0.783   -26.45  -5.313  1   168.3  ? 138 HIS B O     1 
ATOM   2793 C  CB    . HIS B 2 138 ? 2.028   -23.923 -6.658  1   167.99 ? 138 HIS B CB    1 
ATOM   2794 C  CG    . HIS B 2 138 ? 3.008   -22.875 -7.074  1   170.96 ? 138 HIS B CG    1 
ATOM   2795 N  ND1   . HIS B 2 138 ? 2.772   -21.528 -6.837  1   173.13 ? 138 HIS B ND1   1 
ATOM   2796 C  CD2   . HIS B 2 138 ? 4.201   -23.007 -7.697  1   172.23 ? 138 HIS B CD2   1 
ATOM   2797 C  CE1   . HIS B 2 138 ? 3.815   -20.886 -7.337  1   173.69 ? 138 HIS B CE1   1 
ATOM   2798 N  NE2   . HIS B 2 138 ? 4.708   -21.734 -7.854  1   173.52 ? 138 HIS B NE2   1 
ATOM   2799 N  N     . TYR B 2 139 ? 1.24    -24.999 -3.656  1   168.73 ? 139 TYR B N     1 
ATOM   2800 C  CA    . TYR B 2 139 ? 0.163   -25.422 -2.778  1   169.91 ? 139 TYR B CA    1 
ATOM   2801 C  C     . TYR B 2 139 ? -0.536  -24.131 -2.401  1   170.54 ? 139 TYR B C     1 
ATOM   2802 O  O     . TYR B 2 139 ? 0.055   -23.29  -1.726  1   170.62 ? 139 TYR B O     1 
ATOM   2803 C  CB    . TYR B 2 139 ? 0.731   -26.115 -1.531  1   170.43 ? 139 TYR B CB    1 
ATOM   2804 C  CG    . TYR B 2 139 ? -0.002  -27.378 -1.137  1   171.79 ? 139 TYR B CG    1 
ATOM   2805 C  CD1   . TYR B 2 139 ? 0.381   -28.614 -1.64   1   172.94 ? 139 TYR B CD1   1 
ATOM   2806 C  CD2   . TYR B 2 139 ? -1.063  -27.341 -0.243  1   172.96 ? 139 TYR B CD2   1 
ATOM   2807 C  CE1   . TYR B 2 139 ? -0.271  -29.783 -1.26   1   174.05 ? 139 TYR B CE1   1 
ATOM   2808 C  CE2   . TYR B 2 139 ? -1.736  -28.501 0.129   1   174.04 ? 139 TYR B CE2   1 
ATOM   2809 C  CZ    . TYR B 2 139 ? -1.342  -29.721 -0.387  1   175.02 ? 139 TYR B CZ    1 
ATOM   2810 O  OH    . TYR B 2 139 ? -2.011  -30.871 -0.027  1   176.53 ? 139 TYR B OH    1 
ATOM   2811 N  N     . HIS B 2 140 ? -1.752  -23.928 -2.903  1   170.94 ? 140 HIS B N     1 
ATOM   2812 C  CA    . HIS B 2 140 ? -2.48   -22.69  -2.651  1   172.01 ? 140 HIS B CA    1 
ATOM   2813 C  C     . HIS B 2 140 ? -3.774  -22.921 -1.89   1   172.66 ? 140 HIS B C     1 
ATOM   2814 O  O     . HIS B 2 140 ? -4.263  -24.049 -1.815  1   172.62 ? 140 HIS B O     1 
ATOM   2815 C  CB    . HIS B 2 140 ? -2.816  -21.997 -3.981  1   173.23 ? 140 HIS B CB    1 
ATOM   2816 C  CG    . HIS B 2 140 ? -1.646  -21.491 -4.759  1   176.11 ? 140 HIS B CG    1 
ATOM   2817 N  ND1   . HIS B 2 140 ? -1.825  -20.817 -5.953  1   178.15 ? 140 HIS B ND1   1 
ATOM   2818 C  CD2   . HIS B 2 140 ? -0.32   -21.578 -4.501  1   177.41 ? 140 HIS B CD2   1 
ATOM   2819 C  CE1   . HIS B 2 140 ? -0.612  -20.518 -6.383  1   178.73 ? 140 HIS B CE1   1 
ATOM   2820 N  NE2   . HIS B 2 140 ? 0.326   -20.954 -5.543  1   178.63 ? 140 HIS B NE2   1 
ATOM   2821 N  N     . GLY B 2 141 ? -4.338  -21.834 -1.368  1   173.13 ? 141 GLY B N     1 
ATOM   2822 C  CA    . GLY B 2 141 ? -5.624  -21.861 -0.687  1   174.03 ? 141 GLY B CA    1 
ATOM   2823 C  C     . GLY B 2 141 ? -6.782  -21.794 -1.666  1   174.61 ? 141 GLY B C     1 
ATOM   2824 O  O     . GLY B 2 141 ? -6.578  -21.888 -2.883  1   174.76 ? 141 GLY B O     1 
ATOM   2825 N  N     . MET B 2 142 ? -8.013  -21.615 -1.152  1   174.65 ? 142 MET B N     1 
ATOM   2826 C  CA    . MET B 2 142 ? -9.181  -21.577 -2.029  1   175.03 ? 142 MET B CA    1 
ATOM   2827 C  C     . MET B 2 142 ? -9.566  -20.172 -2.519  1   174.61 ? 142 MET B C     1 
ATOM   2828 O  O     . MET B 2 142 ? -10.573 -20.048 -3.222  1   174.96 ? 142 MET B O     1 
ATOM   2829 C  CB    . MET B 2 142 ? -10.387 -22.307 -1.42   1   176.09 ? 142 MET B CB    1 
ATOM   2830 C  CG    . MET B 2 142 ? -10.303 -23.829 -1.574  1   178.65 ? 142 MET B CG    1 
ATOM   2831 S  SD    . MET B 2 142 ? -9.986  -24.448 -3.266  1   183.07 ? 142 MET B SD    1 
ATOM   2832 C  CE    . MET B 2 142 ? -11.494 -23.977 -4.075  1   181.59 ? 142 MET B CE    1 
ATOM   2833 N  N     . ASP B 2 143 ? -8.764  -19.134 -2.21   1   173.61 ? 143 ASP B N     1 
ATOM   2834 C  CA    . ASP B 2 143 ? -9.041  -17.807 -2.763  1   173.03 ? 143 ASP B CA    1 
ATOM   2835 C  C     . ASP B 2 143 ? -8.014  -17.512 -3.85   1   171.43 ? 143 ASP B C     1 
ATOM   2836 O  O     . ASP B 2 143 ? -6.831  -17.82  -3.692  1   171.55 ? 143 ASP B O     1 
ATOM   2837 C  CB    . ASP B 2 143 ? -9.206  -16.697 -1.706  1   175.35 ? 143 ASP B CB    1 
ATOM   2838 C  CG    . ASP B 2 143 ? -7.934  -16.207 -1.066  1   180.79 ? 143 ASP B CG    1 
ATOM   2839 O  OD1   . ASP B 2 143 ? -7.014  -17.027 -0.881  1   181.75 ? 143 ASP B OD1   1 
ATOM   2840 O  OD2   . ASP B 2 143 ? -7.867  -15.001 -0.726  1   183.25 ? 143 ASP B OD2   1 
ATOM   2841 N  N     . GLY B 2 144 ? -8.503  -17.019 -4.981  1   169.77 ? 144 GLY B N     1 
ATOM   2842 C  CA    . GLY B 2 144 ? -7.689  -16.783 -6.165  1   168.62 ? 144 GLY B CA    1 
ATOM   2843 C  C     . GLY B 2 144 ? -7.101  -15.403 -6.385  1   167.17 ? 144 GLY B C     1 
ATOM   2844 O  O     . GLY B 2 144 ? -6.911  -15.003 -7.539  1   167.35 ? 144 GLY B O     1 
ATOM   2845 N  N     . ASP B 2 145 ? -6.752  -14.677 -5.299  1   165.43 ? 145 ASP B N     1 
ATOM   2846 C  CA    . ASP B 2 145 ? -6.106  -13.372 -5.448  1   164.17 ? 145 ASP B CA    1 
ATOM   2847 C  C     . ASP B 2 145 ? -4.591  -13.551 -5.35   1   162.19 ? 145 ASP B C     1 
ATOM   2848 O  O     . ASP B 2 145 ? -3.922  -12.894 -4.561  1   162.28 ? 145 ASP B O     1 
ATOM   2849 C  CB    . ASP B 2 145 ? -6.619  -12.342 -4.424  1   166.31 ? 145 ASP B CB    1 
ATOM   2850 C  CG    . ASP B 2 145 ? -6.407  -10.887 -4.837  1   171.49 ? 145 ASP B CG    1 
ATOM   2851 O  OD1   . ASP B 2 145 ? -5.941  -10.652 -5.983  1   172.57 ? 145 ASP B OD1   1 
ATOM   2852 O  OD2   . ASP B 2 145 ? -6.696  -9.981  -4.009  1   173.39 ? 145 ASP B OD2   1 
ATOM   2853 N  N     . ILE B 2 146 ? -4.067  -14.494 -6.129  1   160.31 ? 146 ILE B N     1 
ATOM   2854 C  CA    . ILE B 2 146 ? -2.651  -14.835 -6.19   1   158.68 ? 146 ILE B CA    1 
ATOM   2855 C  C     . ILE B 2 146 ? -2.194  -14.671 -7.628  1   156.5  ? 146 ILE B C     1 
ATOM   2856 O  O     . ILE B 2 146 ? -2.929  -15.025 -8.558  1   156.76 ? 146 ILE B O     1 
ATOM   2857 C  CB    . ILE B 2 146 ? -2.434  -16.314 -5.755  1   159.31 ? 146 ILE B CB    1 
ATOM   2858 C  CG1   . ILE B 2 146 ? -3.042  -16.608 -4.379  1   160.32 ? 146 ILE B CG1   1 
ATOM   2859 C  CG2   . ILE B 2 146 ? -0.957  -16.719 -5.812  1   159.72 ? 146 ILE B CG2   1 
ATOM   2860 C  CD1   . ILE B 2 146 ? -3.093  -18.078 -4.043  1   161.42 ? 146 ILE B CD1   1 
ATOM   2861 N  N     . LEU B 2 147 ? -0.983  -14.158 -7.822  1   154.14 ? 147 LEU B N     1 
ATOM   2862 C  CA    . LEU B 2 147 ? -0.425  -14.049 -9.156  1   152.23 ? 147 LEU B CA    1 
ATOM   2863 C  C     . LEU B 2 147 ? 0.98    -14.633 -9.166  1   149.48 ? 147 LEU B C     1 
ATOM   2864 O  O     . LEU B 2 147 ? 1.877   -14.063 -8.553  1   149.96 ? 147 LEU B O     1 
ATOM   2865 C  CB    . LEU B 2 147 ? -0.489  -12.605 -9.67   1   152.65 ? 147 LEU B CB    1 
ATOM   2866 C  CG    . LEU B 2 147 ? -1.841  -12.254 -10.31  1   154.3  ? 147 LEU B CG    1 
ATOM   2867 C  CD1   . LEU B 2 147 ? -2.773  -11.556 -9.322  1   154.9  ? 147 LEU B CD1   1 
ATOM   2868 C  CD2   . LEU B 2 147 ? -1.659  -11.443 -11.574 1   155    ? 147 LEU B CD2   1 
ATOM   2869 N  N     . VAL B 2 148 ? 1.152   -15.817 -9.772  1   146.44 ? 148 VAL B N     1 
ATOM   2870 C  CA    . VAL B 2 148 ? 2.458   -16.459 -9.863  1   144.11 ? 148 VAL B CA    1 
ATOM   2871 C  C     . VAL B 2 148 ? 3.016   -16.096 -11.235 1   141.95 ? 148 VAL B C     1 
ATOM   2872 O  O     . VAL B 2 148 ? 2.411   -16.456 -12.243 1   142.12 ? 148 VAL B O     1 
ATOM   2873 C  CB    . VAL B 2 148 ? 2.356   -17.986 -9.668  1   144.39 ? 148 VAL B CB    1 
ATOM   2874 C  CG1   . VAL B 2 148 ? 3.683   -18.665 -9.968  1   144.86 ? 148 VAL B CG1   1 
ATOM   2875 C  CG2   . VAL B 2 148 ? 1.891   -18.323 -8.261  1   144.7  ? 148 VAL B CG2   1 
ATOM   2876 N  N     . LYS B 2 149 ? 4.12    -15.332 -11.288 1   139.82 ? 149 LYS B N     1 
ATOM   2877 C  CA    . LYS B 2 149 ? 4.667   -14.896 -12.568 1   138.21 ? 149 LYS B CA    1 
ATOM   2878 C  C     . LYS B 2 149 ? 6.148   -15.188 -12.773 1   137.05 ? 149 LYS B C     1 
ATOM   2879 O  O     . LYS B 2 149 ? 6.984   -14.294 -12.638 1   136.94 ? 149 LYS B O     1 
ATOM   2880 C  CB    . LYS B 2 149 ? 4.385   -13.405 -12.814 1   138.71 ? 149 LYS B CB    1 
ATOM   2881 C  CG    . LYS B 2 149 ? 4.545   -13.009 -14.273 1   140.82 ? 149 LYS B CG    1 
ATOM   2882 C  CD    . LYS B 2 149 ? 4.504   -11.521 -14.488 1   143.32 ? 149 LYS B CD    1 
ATOM   2883 C  CE    . LYS B 2 149 ? 4.657   -11.169 -15.95  1   145.99 ? 149 LYS B CE    1 
ATOM   2884 N  NZ    . LYS B 2 149 ? 6.029   -11.446 -16.459 1   147.69 ? 149 LYS B NZ    1 
ATOM   2885 N  N     . PRO B 2 150 ? 6.481   -16.407 -13.229 1   136    ? 150 PRO B N     1 
ATOM   2886 C  CA    . PRO B 2 150 ? 7.887   -16.713 -13.533 1   135.24 ? 150 PRO B CA    1 
ATOM   2887 C  C     . PRO B 2 150 ? 8.283   -16.327 -14.97  1   134.2  ? 150 PRO B C     1 
ATOM   2888 O  O     . PRO B 2 150 ? 7.547   -16.609 -15.909 1   134.36 ? 150 PRO B O     1 
ATOM   2889 C  CB    . PRO B 2 150 ? 7.976   -18.238 -13.334 1   136.13 ? 150 PRO B CB    1 
ATOM   2890 C  CG    . PRO B 2 150 ? 6.552   -18.721 -13.063 1   136.8  ? 150 PRO B CG    1 
ATOM   2891 C  CD    . PRO B 2 150 ? 5.622   -17.591 -13.416 1   135.4  ? 150 PRO B CD    1 
ATOM   2892 N  N     . THR B 2 151 ? 9.434   -15.681 -15.138 1   133.04 ? 151 THR B N     1 
ATOM   2893 C  CA    . THR B 2 151 ? 9.984   -15.318 -16.441 1   132.37 ? 151 THR B CA    1 
ATOM   2894 C  C     . THR B 2 151 ? 11.387  -15.892 -16.423 1   131.31 ? 151 THR B C     1 
ATOM   2895 O  O     . THR B 2 151 ? 12.18   -15.476 -15.592 1   131.53 ? 151 THR B O     1 
ATOM   2896 C  CB    . THR B 2 151 ? 10.035  -13.804 -16.616 1   133.81 ? 151 THR B CB    1 
ATOM   2897 O  OG1   . THR B 2 151 ? 8.708   -13.284 -16.675 1   134.8  ? 151 THR B OG1   1 
ATOM   2898 C  CG2   . THR B 2 151 ? 10.777  -13.404 -17.865 1   134.38 ? 151 THR B CG2   1 
ATOM   2899 N  N     . VAL B 2 152 ? 11.682  -16.893 -17.26  1   130.1  ? 152 VAL B N     1 
ATOM   2900 C  CA    . VAL B 2 152 ? 12.978  -17.563 -17.222 1   129.58 ? 152 VAL B CA    1 
ATOM   2901 C  C     . VAL B 2 152 ? 13.711  -17.564 -18.562 1   128.9  ? 152 VAL B C     1 
ATOM   2902 O  O     . VAL B 2 152 ? 13.228  -18.146 -19.526 1   128.9  ? 152 VAL B O     1 
ATOM   2903 C  CB    . VAL B 2 152 ? 12.829  -19.013 -16.681 1   130.4  ? 152 VAL B CB    1 
ATOM   2904 C  CG1   . VAL B 2 152 ? 14.187  -19.667 -16.491 1   131.04 ? 152 VAL B CG1   1 
ATOM   2905 C  CG2   . VAL B 2 152 ? 12.023  -19.063 -15.383 1   130.81 ? 152 VAL B CG2   1 
ATOM   2906 N  N     . LYS B 2 153 ? 14.889  -16.953 -18.617 1   128.36 ? 153 LYS B N     1 
ATOM   2907 C  CA    . LYS B 2 153 ? 15.71   -16.959 -19.827 1   128.45 ? 153 LYS B CA    1 
ATOM   2908 C  C     . LYS B 2 153 ? 16.783  -18.013 -19.608 1   128.6  ? 153 LYS B C     1 
ATOM   2909 O  O     . LYS B 2 153 ? 17.453  -17.975 -18.59  1   128.92 ? 153 LYS B O     1 
ATOM   2910 C  CB    . LYS B 2 153 ? 16.358  -15.587 -20.052 1   129.84 ? 153 LYS B CB    1 
ATOM   2911 C  CG    . LYS B 2 153 ? 17.366  -15.563 -21.191 1   133.19 ? 153 LYS B CG    1 
ATOM   2912 C  CD    . LYS B 2 153 ? 16.683  -15.663 -22.532 1   137    ? 153 LYS B CD    1 
ATOM   2913 C  CE    . LYS B 2 153 ? 17.62   -16.1   -23.631 1   140.52 ? 153 LYS B CE    1 
ATOM   2914 N  NZ    . LYS B 2 153 ? 18.654  -15.078 -23.962 1   142.6  ? 153 LYS B NZ    1 
ATOM   2915 N  N     . VAL B 2 154 ? 16.926  -18.974 -20.519 1   128.15 ? 154 VAL B N     1 
ATOM   2916 C  CA    . VAL B 2 154 ? 17.906  -20.046 -20.367 1   128.17 ? 154 VAL B CA    1 
ATOM   2917 C  C     . VAL B 2 154 ? 18.865  -20.091 -21.553 1   128.24 ? 154 VAL B C     1 
ATOM   2918 O  O     . VAL B 2 154 ? 18.433  -20.041 -22.695 1   128.27 ? 154 VAL B O     1 
ATOM   2919 C  CB    . VAL B 2 154 ? 17.203  -21.401 -20.162 1   128.81 ? 154 VAL B CB    1 
ATOM   2920 C  CG1   . VAL B 2 154 ? 18.217  -22.506 -19.896 1   129.39 ? 154 VAL B CG1   1 
ATOM   2921 C  CG2   . VAL B 2 154 ? 16.183  -21.324 -19.036 1   129.32 ? 154 VAL B CG2   1 
ATOM   2922 N  N     . GLU B 2 155 ? 20.163  -20.154 -21.286 1   128.17 ? 155 GLU B N     1 
ATOM   2923 C  CA    . GLU B 2 155 ? 21.175  -20.21  -22.328 1   128.77 ? 155 GLU B CA    1 
ATOM   2924 C  C     . GLU B 2 155 ? 21.972  -21.47  -22.094 1   128.61 ? 155 GLU B C     1 
ATOM   2925 O  O     . GLU B 2 155 ? 22.553  -21.63  -21.034 1   128.59 ? 155 GLU B O     1 
ATOM   2926 C  CB    . GLU B 2 155 ? 22.064  -18.961 -22.274 1   132.04 ? 155 GLU B CB    1 
ATOM   2927 C  CG    . GLU B 2 155 ? 21.351  -17.712 -22.771 1   138.55 ? 155 GLU B CG    1 
ATOM   2928 C  CD    . GLU B 2 155 ? 21.463  -16.468 -21.907 1   146.28 ? 155 GLU B CD    1 
ATOM   2929 O  OE1   . GLU B 2 155 ? 22.324  -16.445 -20.998 1   147.78 ? 155 GLU B OE1   1 
ATOM   2930 O  OE2   . GLU B 2 155 ? 20.693  -15.509 -22.148 1   148.77 ? 155 GLU B OE2   1 
ATOM   2931 N  N     . ILE B 2 156 ? 21.944  -22.399 -23.042 1   128.48 ? 156 ILE B N     1 
ATOM   2932 C  CA    . ILE B 2 156 ? 22.603  -23.693 -22.888 1   128.81 ? 156 ILE B CA    1 
ATOM   2933 C  C     . ILE B 2 156 ? 23.784  -23.868 -23.836 1   129.48 ? 156 ILE B C     1 
ATOM   2934 O  O     . ILE B 2 156 ? 23.616  -23.79  -25.048 1   129.87 ? 156 ILE B O     1 
ATOM   2935 C  CB    . ILE B 2 156 ? 21.574  -24.832 -23.072 1   128.89 ? 156 ILE B CB    1 
ATOM   2936 C  CG1   . ILE B 2 156 ? 20.365  -24.647 -22.153 1   129.53 ? 156 ILE B CG1   1 
ATOM   2937 C  CG2   . ILE B 2 156 ? 22.225  -26.166 -22.837 1   129.27 ? 156 ILE B CG2   1 
ATOM   2938 C  CD1   . ILE B 2 156 ? 19.241  -25.409 -22.542 1   130.55 ? 156 ILE B CD1   1 
ATOM   2939 N  N     . ASP B 2 157 ? 24.969  -24.136 -23.296 1   129.46 ? 157 ASP B N     1 
ATOM   2940 C  CA    . ASP B 2 157 ? 26.17   -24.318 -24.104 1   129.94 ? 157 ASP B CA    1 
ATOM   2941 C  C     . ASP B 2 157 ? 26.294  -25.757 -24.643 1   129.54 ? 157 ASP B C     1 
ATOM   2942 O  O     . ASP B 2 157 ? 25.466  -26.61  -24.33  1   129.31 ? 157 ASP B O     1 
ATOM   2943 C  CB    . ASP B 2 157 ? 27.404  -23.908 -23.281 1   132.55 ? 157 ASP B CB    1 
ATOM   2944 C  CG    . ASP B 2 157 ? 28.542  -23.31  -24.088 1   138.55 ? 157 ASP B CG    1 
ATOM   2945 O  OD1   . ASP B 2 157 ? 28.299  -22.317 -24.816 1   139.28 ? 157 ASP B OD1   1 
ATOM   2946 O  OD2   . ASP B 2 157 ? 29.682  -23.818 -23.971 1   141.41 ? 157 ASP B OD2   1 
ATOM   2947 N  N     . GLU B 2 158 ? 27.316  -26.014 -25.478 1   129.39 ? 474 GLU B N     1 
ATOM   2948 C  CA    . GLU B 2 158 ? 27.578  -27.318 -26.072 1   129.8  ? 474 GLU B CA    1 
ATOM   2949 C  C     . GLU B 2 158 ? 27.584  -28.451 -25.059 1   129.48 ? 474 GLU B C     1 
ATOM   2950 O  O     . GLU B 2 158 ? 28.441  -28.489 -24.183 1   129.49 ? 474 GLU B O     1 
ATOM   2951 C  CB    . GLU B 2 158 ? 28.905  -27.317 -26.849 1   132.78 ? 474 GLU B CB    1 
ATOM   2952 C  CG    . GLU B 2 158 ? 28.996  -26.253 -27.93  1   139.01 ? 474 GLU B CG    1 
ATOM   2953 C  CD    . GLU B 2 158 ? 30.186  -26.413 -28.86  1   146.56 ? 474 GLU B CD    1 
ATOM   2954 O  OE1   . GLU B 2 158 ? 30.655  -27.563 -29.028 1   148.27 ? 474 GLU B OE1   1 
ATOM   2955 O  OE2   . GLU B 2 158 ? 30.643  -25.395 -29.429 1   148.7  ? 474 GLU B OE2   1 
ATOM   2956 N  N     . GLY B 2 159 ? 26.605  -29.339 -25.179 1   129.07 ? 475 GLY B N     1 
ATOM   2957 C  CA    . GLY B 2 159 ? 26.47   -30.51  -24.32  1   129.12 ? 475 GLY B CA    1 
ATOM   2958 C  C     . GLY B 2 159 ? 25.643  -30.336 -23.06  1   128.82 ? 475 GLY B C     1 
ATOM   2959 O  O     . GLY B 2 159 ? 25.493  -31.285 -22.287 1   128.83 ? 475 GLY B O     1 
ATOM   2960 N  N     . GLY B 2 160 ? 25.111  -29.134 -22.848 1   128.38 ? 476 GLY B N     1 
ATOM   2961 C  CA    . GLY B 2 160 ? 24.314  -28.813 -21.667 1   128.34 ? 476 GLY B CA    1 
ATOM   2962 C  C     . GLY B 2 160 ? 22.946  -29.47  -21.605 1   127.96 ? 476 GLY B C     1 
ATOM   2963 O  O     . GLY B 2 160 ? 22.43   -29.935 -22.621 1   128.21 ? 476 GLY B O     1 
ATOM   2964 N  N     . ILE B 2 161 ? 22.341  -29.523 -20.402 1   127.13 ? 477 ILE B N     1 
ATOM   2965 C  CA    . ILE B 2 161 ? 21.031  -30.15  -20.188 1   126.66 ? 477 ILE B CA    1 
ATOM   2966 C  C     . ILE B 2 161 ? 20.121  -29.278 -19.313 1   126.15 ? 477 ILE B C     1 
ATOM   2967 O  O     . ILE B 2 161 ? 20.535  -28.839 -18.25  1   126.24 ? 477 ILE B O     1 
ATOM   2968 C  CB    . ILE B 2 161 ? 21.211  -31.579 -19.586 1   127.01 ? 477 ILE B CB    1 
ATOM   2969 C  CG1   . ILE B 2 161 ? 21.775  -32.56  -20.626 1   127.76 ? 477 ILE B CG1   1 
ATOM   2970 C  CG2   . ILE B 2 161 ? 19.911  -32.13  -19.007 1   127.5  ? 477 ILE B CG2   1 
ATOM   2971 C  CD1   . ILE B 2 161 ? 23.187  -32.952 -20.422 1   128.9  ? 477 ILE B CD1   1 
ATOM   2972 N  N     . TYR B 2 162 ? 18.881  -29.057 -19.74  1   125.69 ? 478 TYR B N     1 
ATOM   2973 C  CA    . TYR B 2 162 ? 17.927  -28.286 -18.957 1   126.09 ? 478 TYR B CA    1 
ATOM   2974 C  C     . TYR B 2 162 ? 16.647  -29.077 -18.795 1   126.8  ? 478 TYR B C     1 
ATOM   2975 O  O     . TYR B 2 162 ? 16.065  -29.514 -19.782 1   127    ? 478 TYR B O     1 
ATOM   2976 C  CB    . TYR B 2 162 ? 17.638  -26.936 -19.622 1   125.93 ? 478 TYR B CB    1 
ATOM   2977 C  CG    . TYR B 2 162 ? 16.623  -26.09  -18.884 1   126.4  ? 478 TYR B CG    1 
ATOM   2978 C  CD1   . TYR B 2 162 ? 16.827  -25.719 -17.564 1   127.12 ? 478 TYR B CD1   1 
ATOM   2979 C  CD2   . TYR B 2 162 ? 15.488  -25.613 -19.525 1   127.18 ? 478 TYR B CD2   1 
ATOM   2980 C  CE1   . TYR B 2 162 ? 15.91   -24.922 -16.888 1   127.96 ? 478 TYR B CE1   1 
ATOM   2981 C  CE2   . TYR B 2 162 ? 14.565  -24.813 -18.86  1   128    ? 478 TYR B CE2   1 
ATOM   2982 C  CZ    . TYR B 2 162 ? 14.78   -24.468 -17.541 1   128.81 ? 478 TYR B CZ    1 
ATOM   2983 O  OH    . TYR B 2 162 ? 13.869  -23.675 -16.881 1   130.23 ? 478 TYR B OH    1 
ATOM   2984 N  N     . ILE B 2 163 ? 16.221  -29.294 -17.55  1   127.07 ? 479 ILE B N     1 
ATOM   2985 C  CA    . ILE B 2 163 ? 14.983  -30.008 -17.244 1   127.68 ? 479 ILE B CA    1 
ATOM   2986 C  C     . ILE B 2 163 ? 14.145  -29.101 -16.372 1   128.35 ? 479 ILE B C     1 
ATOM   2987 O  O     . ILE B 2 163 ? 14.639  -28.624 -15.368 1   128.41 ? 479 ILE B O     1 
ATOM   2988 C  CB    . ILE B 2 163 ? 15.281  -31.349 -16.555 1   128.17 ? 479 ILE B CB    1 
ATOM   2989 C  CG1   . ILE B 2 163 ? 15.951  -32.304 -17.535 1   129.19 ? 479 ILE B CG1   1 
ATOM   2990 C  CG2   . ILE B 2 163 ? 14.014  -31.969 -15.986 1   128.66 ? 479 ILE B CG2   1 
ATOM   2991 C  CD1   . ILE B 2 163 ? 16.912  -33.2   -16.893 1   130.58 ? 479 ILE B CD1   1 
ATOM   2992 N  N     . SER B 2 164 ? 12.916  -28.801 -16.775 1   128.81 ? 480 SER B N     1 
ATOM   2993 C  CA    . SER B 2 164 ? 12.057  -27.887 -16.031 1   129.91 ? 480 SER B CA    1 
ATOM   2994 C  C     . SER B 2 164 ? 10.692  -28.503 -15.827 1   131.47 ? 480 SER B C     1 
ATOM   2995 O  O     . SER B 2 164 ? 10.162  -29.122 -16.736 1   131.77 ? 480 SER B O     1 
ATOM   2996 C  CB    . SER B 2 164 ? 11.929  -26.564 -16.778 1   130.65 ? 480 SER B CB    1 
ATOM   2997 O  OG    . SER B 2 164 ? 10.935  -25.723 -16.217 1   132.17 ? 480 SER B OG    1 
ATOM   2998 N  N     . ASN B 2 165 ? 10.119  -28.34  -14.64  1   132.39 ? 481 ASN B N     1 
ATOM   2999 C  CA    . ASN B 2 165 ? 8.811   -28.899 -14.325 1   133.91 ? 481 ASN B CA    1 
ATOM   3000 C  C     . ASN B 2 165 ? 8.03    -27.932 -13.446 1   135.17 ? 481 ASN B C     1 
ATOM   3001 O  O     . ASN B 2 165 ? 8.461   -27.657 -12.331 1   135.51 ? 481 ASN B O     1 
ATOM   3002 C  CB    . ASN B 2 165 ? 8.972   -30.236 -13.587 1   135.46 ? 481 ASN B CB    1 
ATOM   3003 C  CG    . ASN B 2 165 ? 9.549   -31.364 -14.422 1   139.23 ? 481 ASN B CG    1 
ATOM   3004 O  OD1   . ASN B 2 165 ? 9.047   -31.697 -15.494 1   140.45 ? 481 ASN B OD1   1 
ATOM   3005 N  ND2   . ASN B 2 165 ? 10.62   -31.986 -13.951 1   140.09 ? 481 ASN B ND2   1 
ATOM   3006 N  N     . PHE B 2 166 ? 6.896   -27.408 -13.933 1   135.78 ? 482 PHE B N     1 
ATOM   3007 C  CA    . PHE B 2 166 ? 6.07    -26.508 -13.129 1   136.97 ? 482 PHE B CA    1 
ATOM   3008 C  C     . PHE B 2 166 ? 4.743   -27.195 -12.874 1   137.38 ? 482 PHE B C     1 
ATOM   3009 O  O     . PHE B 2 166 ? 4.076   -27.597 -13.82  1   137.4  ? 482 PHE B O     1 
ATOM   3010 C  CB    . PHE B 2 166 ? 5.851   -25.155 -13.824 1   137.45 ? 482 PHE B CB    1 
ATOM   3011 C  CG    . PHE B 2 166 ? 6.962   -24.137 -13.649 1   138.78 ? 482 PHE B CG    1 
ATOM   3012 C  CD1   . PHE B 2 166 ? 6.917   -23.201 -12.629 1   139.87 ? 482 PHE B CD1   1 
ATOM   3013 C  CD2   . PHE B 2 166 ? 8.023   -24.085 -14.536 1   139.85 ? 482 PHE B CD2   1 
ATOM   3014 C  CE1   . PHE B 2 166 ? 7.919   -22.236 -12.499 1   140.71 ? 482 PHE B CE1   1 
ATOM   3015 C  CE2   . PHE B 2 166 ? 9.021   -23.121 -14.403 1   140.65 ? 482 PHE B CE2   1 
ATOM   3016 C  CZ    . PHE B 2 166 ? 8.964   -22.204 -13.386 1   140.5  ? 482 PHE B CZ    1 
ATOM   3017 N  N     . THR B 2 167 ? 4.377   -27.372 -11.604 1   137.6  ? 483 THR B N     1 
ATOM   3018 C  CA    . THR B 2 167 ? 3.131   -28.043 -11.252 1   138.28 ? 483 THR B CA    1 
ATOM   3019 C  C     . THR B 2 167 ? 2.277   -27.177 -10.332 1   138.72 ? 483 THR B C     1 
ATOM   3020 O  O     . THR B 2 167 ? 2.713   -26.802 -9.246  1   139    ? 483 THR B O     1 
ATOM   3021 C  CB    . THR B 2 167 ? 3.399   -29.405 -10.606 1   139.71 ? 483 THR B CB    1 
ATOM   3022 O  OG1   . THR B 2 167 ? 4.43    -30.098 -11.316 1   140.67 ? 483 THR B OG1   1 
ATOM   3023 C  CG2   . THR B 2 167 ? 2.144   -30.264 -10.543 1   140.32 ? 483 THR B CG2   1 
ATOM   3024 N  N     . LEU B 2 168 ? 1.057   -26.866 -10.766 1   138.65 ? 484 LEU B N     1 
ATOM   3025 C  CA    . LEU B 2 168 ? 0.124   -26.063 -9.985  1   139.05 ? 484 LEU B CA    1 
ATOM   3026 C  C     . LEU B 2 168 ? -1.216  -26.77  -10.043 1   139.13 ? 484 LEU B C     1 
ATOM   3027 O  O     . LEU B 2 168 ? -2.017  -26.5   -10.931 1   139.5  ? 484 LEU B O     1 
ATOM   3028 C  CB    . LEU B 2 168 ? 0.003   -24.641 -10.563 1   139.51 ? 484 LEU B CB    1 
ATOM   3029 C  CG    . LEU B 2 168 ? 1.162   -23.685 -10.262 1   141.35 ? 484 LEU B CG    1 
ATOM   3030 C  CD1   . LEU B 2 168 ? 2.185   -23.674 -11.397 1   141.85 ? 484 LEU B CD1   1 
ATOM   3031 C  CD2   . LEU B 2 168 ? 0.652   -22.273 -9.999  1   142.25 ? 484 LEU B CD2   1 
ATOM   3032 N  N     . THR B 2 169 ? -1.428  -27.743 -9.161  1   138.66 ? 485 THR B N     1 
ATOM   3033 C  CA    . THR B 2 169 ? -2.671  -28.519 -9.15   1   138.75 ? 485 THR B CA    1 
ATOM   3034 C  C     . THR B 2 169 ? -3.389  -28.513 -7.784  1   138.65 ? 485 THR B C     1 
ATOM   3035 O  O     . THR B 2 169 ? -4.401  -29.203 -7.633  1   138.71 ? 485 THR B O     1 
ATOM   3036 C  CB    . THR B 2 169 ? -2.389  -29.963 -9.604  1   140    ? 485 THR B CB    1 
ATOM   3037 O  OG1   . THR B 2 169 ? -1.488  -30.577 -8.688  1   141.06 ? 485 THR B OG1   1 
ATOM   3038 C  CG2   . THR B 2 169 ? -1.801  -30.036 -10.999 1   140.39 ? 485 THR B CG2   1 
ATOM   3039 N  N     . LYS B 2 170 ? -2.861  -27.756 -6.795  1   138.27 ? 486 LYS B N     1 
ATOM   3040 C  CA    . LYS B 2 170 ? -3.394  -27.685 -5.435  1   138.41 ? 486 LYS B CA    1 
ATOM   3041 C  C     . LYS B 2 170 ? -3.997  -26.321 -5.101  1   138.71 ? 486 LYS B C     1 
ATOM   3042 O  O     . LYS B 2 170 ? -3.287  -25.317 -5.054  1   139.24 ? 486 LYS B O     1 
ATOM   3043 C  CB    . LYS B 2 170 ? -2.309  -28.057 -4.411  1   139.65 ? 486 LYS B CB    1 
ATOM   3044 C  CG    . LYS B 2 170 ? -2.273  -29.548 -4.088  1   142.63 ? 486 LYS B CG    1 
ATOM   3045 C  CD    . LYS B 2 170 ? -3.475  -29.997 -3.255  1   145.76 ? 486 LYS B CD    1 
ATOM   3046 C  CE    . LYS B 2 170 ? -3.526  -31.492 -3.097  1   148.57 ? 486 LYS B CE    1 
ATOM   3047 N  NZ    . LYS B 2 170 ? -3.757  -32.164 -4.401  1   150.44 ? 486 LYS B NZ    1 
ATOM   3048 N  N     . GLY B 2 171 ? -5.298  -26.308 -4.835  1   138.21 ? 487 GLY B N     1 
ATOM   3049 C  CA    . GLY B 2 171 ? -6.028  -25.085 -4.521  1   138.03 ? 487 GLY B CA    1 
ATOM   3050 C  C     . GLY B 2 171 ? -6.303  -24.258 -5.762  1   137.48 ? 487 GLY B C     1 
ATOM   3051 O  O     . GLY B 2 171 ? -6.252  -24.771 -6.89   1   137.83 ? 487 GLY B O     1 
ATOM   3052 N  N     . ARG B 2 172 ? -6.597  -22.97  -5.568  1   136.34 ? 488 ARG B N     1 
ATOM   3053 C  CA    . ARG B 2 172 ? -6.837  -22.075 -6.69   1   135.79 ? 488 ARG B CA    1 
ATOM   3054 C  C     . ARG B 2 172 ? -5.514  -21.496 -7.171  1   135.24 ? 488 ARG B C     1 
ATOM   3055 O  O     . ARG B 2 172 ? -4.75   -20.972 -6.367  1   135.58 ? 488 ARG B O     1 
ATOM   3056 C  CB    . ARG B 2 172 ? -7.791  -20.951 -6.292  1   136.57 ? 488 ARG B CB    1 
ATOM   3057 C  CG    . ARG B 2 172 ? -9.242  -21.375 -6.339  1   138.51 ? 488 ARG B CG    1 
ATOM   3058 C  CD    . ARG B 2 172 ? -10.155 -20.201 -6.578  1   140.71 ? 488 ARG B CD    1 
ATOM   3059 N  NE    . ARG B 2 172 ? -9.826  -19.486 -7.81   1   142.76 ? 488 ARG B NE    1 
ATOM   3060 C  CZ    . ARG B 2 172 ? -10.302 -18.289 -8.132  1   144.42 ? 488 ARG B CZ    1 
ATOM   3061 N  NH1   . ARG B 2 172 ? -11.139 -17.657 -7.317  1   143.67 ? 488 ARG B NH1   1 
ATOM   3062 N  NH2   . ARG B 2 172 ? -9.937  -17.707 -9.265  1   144.34 ? 488 ARG B NH2   1 
ATOM   3063 N  N     . ILE B 2 173 ? -5.227  -21.613 -8.467  1   134.18 ? 489 ILE B N     1 
ATOM   3064 C  CA    . ILE B 2 173 ? -4.008  -21.074 -9.051  1   133.54 ? 489 ILE B CA    1 
ATOM   3065 C  C     . ILE B 2 173 ? -3.993  -19.539 -8.921  1   132.68 ? 489 ILE B C     1 
ATOM   3066 O  O     . ILE B 2 173 ? -2.996  -18.953 -8.502  1   132.62 ? 489 ILE B O     1 
ATOM   3067 C  CB    . ILE B 2 173 ? -3.911  -21.525 -10.534 1   134.06 ? 489 ILE B CB    1 
ATOM   3068 C  CG1   . ILE B 2 173 ? -3.676  -23.046 -10.647 1   134.97 ? 489 ILE B CG1   1 
ATOM   3069 C  CG2   . ILE B 2 173 ? -2.858  -20.723 -11.296 1   134.66 ? 489 ILE B CG2   1 
ATOM   3070 C  CD1   . ILE B 2 173 ? -3.599  -23.576 -12.096 1   136.39 ? 489 ILE B CD1   1 
ATOM   3071 N  N     . GLY B 2 174 ? -5.122  -18.921 -9.24   1   131.87 ? 490 GLY B N     1 
ATOM   3072 C  CA    . GLY B 2 174 ? -5.272  -17.475 -9.276  1   131.51 ? 490 GLY B CA    1 
ATOM   3073 C  C     . GLY B 2 174 ? -5.006  -17.067 -10.709 1   130.78 ? 490 GLY B C     1 
ATOM   3074 O  O     . GLY B 2 174 ? -5.802  -17.363 -11.609 1   131.31 ? 490 GLY B O     1 
ATOM   3075 N  N     . THR B 2 175 ? -3.843  -16.473 -10.953 1   129.26 ? 491 THR B N     1 
ATOM   3076 C  CA    . THR B 2 175 ? -3.437  -16.116 -12.304 1   128.16 ? 491 THR B CA    1 
ATOM   3077 C  C     . THR B 2 175 ? -2.007  -16.58  -12.487 1   126.41 ? 491 THR B C     1 
ATOM   3078 O  O     . THR B 2 175 ? -1.114  -16.141 -11.763 1   126.51 ? 491 THR B O     1 
ATOM   3079 C  CB    . THR B 2 175 ? -3.587  -14.613 -12.564 1   129.63 ? 491 THR B CB    1 
ATOM   3080 O  OG1   . THR B 2 175 ? -4.96   -14.232 -12.426 1   130.44 ? 491 THR B OG1   1 
ATOM   3081 C  CG2   . THR B 2 175 ? -3.072  -14.216 -13.946 1   130.21 ? 491 THR B CG2   1 
ATOM   3082 N  N     . LEU B 2 176 ? -1.794  -17.504 -13.41  1   124.67 ? 492 LEU B N     1 
ATOM   3083 C  CA    . LEU B 2 176 ? -0.464  -18.015 -13.696 1   123.54 ? 492 LEU B CA    1 
ATOM   3084 C  C     . LEU B 2 176 ? 0.028   -17.361 -14.98  1   122.29 ? 492 LEU B C     1 
ATOM   3085 O  O     . LEU B 2 176 ? -0.725  -17.26  -15.945 1   122.27 ? 492 LEU B O     1 
ATOM   3086 C  CB    . LEU B 2 176 ? -0.501  -19.547 -13.844 1   123.56 ? 492 LEU B CB    1 
ATOM   3087 C  CG    . LEU B 2 176 ? 0.814   -20.243 -14.166 1   124.92 ? 492 LEU B CG    1 
ATOM   3088 C  CD1   . LEU B 2 176 ? 1.835   -20.009 -13.088 1   125.37 ? 492 LEU B CD1   1 
ATOM   3089 C  CD2   . LEU B 2 176 ? 0.605   -21.725 -14.346 1   125.79 ? 492 LEU B CD2   1 
ATOM   3090 N  N     . ASP B 2 177 ? 1.267   -16.876 -14.983 1   121.11 ? 493 ASP B N     1 
ATOM   3091 C  CA    . ASP B 2 177 ? 1.845   -16.259 -16.171 1   120.54 ? 493 ASP B CA    1 
ATOM   3092 C  C     . ASP B 2 177 ? 3.291   -16.738 -16.309 1   119.34 ? 493 ASP B C     1 
ATOM   3093 O  O     . ASP B 2 177 ? 4.2     -16.084 -15.804 1   119.46 ? 493 ASP B O     1 
ATOM   3094 C  CB    . ASP B 2 177 ? 1.754   -14.72  -16.086 1   122.51 ? 493 ASP B CB    1 
ATOM   3095 C  CG    . ASP B 2 177 ? 2.212   -13.933 -17.315 1   126.93 ? 493 ASP B CG    1 
ATOM   3096 O  OD1   . ASP B 2 177 ? 2.856   -14.533 -18.204 1   127.79 ? 493 ASP B OD1   1 
ATOM   3097 O  OD2   . ASP B 2 177 ? 1.931   -12.71  -17.38  1   128.54 ? 493 ASP B OD2   1 
ATOM   3098 N  N     . ILE B 2 178 ? 3.503   -17.883 -16.982 1   117.94 ? 494 ILE B N     1 
ATOM   3099 C  CA    . ILE B 2 178 ? 4.84    -18.432 -17.191 1   116.97 ? 494 ILE B CA    1 
ATOM   3100 C  C     . ILE B 2 178 ? 5.366   -17.984 -18.531 1   116.35 ? 494 ILE B C     1 
ATOM   3101 O  O     . ILE B 2 178 ? 4.648   -18.041 -19.519 1   116.26 ? 494 ILE B O     1 
ATOM   3102 C  CB    . ILE B 2 178 ? 4.843   -19.971 -17.125 1   117.08 ? 494 ILE B CB    1 
ATOM   3103 C  CG1   . ILE B 2 178 ? 4.306   -20.483 -15.789 1   117.88 ? 494 ILE B CG1   1 
ATOM   3104 C  CG2   . ILE B 2 178 ? 6.237   -20.528 -17.407 1   117.46 ? 494 ILE B CG2   1 
ATOM   3105 C  CD1   . ILE B 2 178 ? 4.041   -21.986 -15.784 1   119.23 ? 494 ILE B CD1   1 
ATOM   3106 N  N     . GLU B 2 179 ? 6.611   -17.538 -18.573 1   115.89 ? 495 GLU B N     1 
ATOM   3107 C  CA    . GLU B 2 179 ? 7.244   -17.126 -19.81  1   116.04 ? 495 GLU B CA    1 
ATOM   3108 C  C     . GLU B 2 179 ? 8.658   -17.666 -19.811 1   115.22 ? 495 GLU B C     1 
ATOM   3109 O  O     . GLU B 2 179 ? 9.393   -17.403 -18.876 1   115.44 ? 495 GLU B O     1 
ATOM   3110 C  CB    . GLU B 2 179 ? 7.215   -15.599 -19.963 1   119.42 ? 495 GLU B CB    1 
ATOM   3111 C  CG    . GLU B 2 179 ? 5.862   -15.097 -20.442 1   126.9  ? 495 GLU B CG    1 
ATOM   3112 C  CD    . GLU B 2 179 ? 5.688   -13.598 -20.572 1   137.6  ? 495 GLU B CD    1 
ATOM   3113 O  OE1   . GLU B 2 179 ? 6.25    -12.851 -19.736 1   140.84 ? 495 GLU B OE1   1 
ATOM   3114 O  OE2   . GLU B 2 179 ? 4.955   -13.171 -21.495 1   140.26 ? 495 GLU B OE2   1 
ATOM   3115 N  N     . GLN B 2 180 ? 9.026   -18.48  -20.805 1   114.2  ? 496 GLN B N     1 
ATOM   3116 C  CA    . GLN B 2 180 ? 10.376  -19.04  -20.878 1   113.74 ? 496 GLN B CA    1 
ATOM   3117 C  C     . GLN B 2 180 ? 10.964  -18.873 -22.268 1   113.84 ? 496 GLN B C     1 
ATOM   3118 O  O     . GLN B 2 180 ? 10.248  -18.98  -23.256 1   113.96 ? 496 GLN B O     1 
ATOM   3119 C  CB    . GLN B 2 180 ? 10.393  -20.534 -20.512 1   114.19 ? 496 GLN B CB    1 
ATOM   3120 C  CG    . GLN B 2 180 ? 10.054  -20.848 -19.068 1   115.49 ? 496 GLN B CG    1 
ATOM   3121 C  CD    . GLN B 2 180 ? 10.696  -22.142 -18.643 1   117.64 ? 496 GLN B CD    1 
ATOM   3122 O  OE1   . GLN B 2 180 ? 11.913  -22.317 -18.727 1   118.3  ? 496 GLN B OE1   1 
ATOM   3123 N  NE2   . GLN B 2 180 ? 9.895   -23.08  -18.176 1   117.99 ? 496 GLN B NE2   1 
ATOM   3124 N  N     . GLU B 2 181 ? 12.264  -18.625 -22.354 1   113.71 ? 497 GLU B N     1 
ATOM   3125 C  CA    . GLU B 2 181 ? 12.95   -18.539 -23.636 1   114.13 ? 497 GLU B CA    1 
ATOM   3126 C  C     . GLU B 2 181 ? 14.266  -19.253 -23.45  1   113.92 ? 497 GLU B C     1 
ATOM   3127 O  O     . GLU B 2 181 ? 15.061  -18.852 -22.613 1   114.18 ? 497 GLU B O     1 
ATOM   3128 C  CB    . GLU B 2 181 ? 13.16   -17.093 -24.11  1   117.02 ? 497 GLU B CB    1 
ATOM   3129 C  CG    . GLU B 2 181 ? 13.579  -17.022 -25.57  1   123.59 ? 497 GLU B CG    1 
ATOM   3130 C  CD    . GLU B 2 181 ? 14.139  -15.693 -26.049 1   132.79 ? 497 GLU B CD    1 
ATOM   3131 O  OE1   . GLU B 2 181 ? 14.787  -14.995 -25.237 1   134.63 ? 497 GLU B OE1   1 
ATOM   3132 O  OE2   . GLU B 2 181 ? 13.949  -15.353 -27.24  1   136.09 ? 497 GLU B OE2   1 
ATOM   3133 N  N     . ILE B 2 182 ? 14.462  -20.357 -24.172 1   113.3  ? 498 ILE B N     1 
ATOM   3134 C  CA    . ILE B 2 182 ? 15.652  -21.202 -24.083 1   113.09 ? 498 ILE B CA    1 
ATOM   3135 C  C     . ILE B 2 182 ? 16.44   -21.135 -25.404 1   112.91 ? 498 ILE B C     1 
ATOM   3136 O  O     . ILE B 2 182 ? 15.857  -21.239 -26.477 1   113.19 ? 498 ILE B O     1 
ATOM   3137 C  CB    . ILE B 2 182 ? 15.25   -22.671 -23.713 1   113.25 ? 498 ILE B CB    1 
ATOM   3138 C  CG1   . ILE B 2 182 ? 14.765  -22.784 -22.259 1   114.01 ? 498 ILE B CG1   1 
ATOM   3139 C  CG2   . ILE B 2 182 ? 16.387  -23.656 -23.964 1   113.57 ? 498 ILE B CG2   1 
ATOM   3140 C  CD1   . ILE B 2 182 ? 13.331  -22.432 -22.035 1   115.23 ? 498 ILE B CD1   1 
ATOM   3141 N  N     . ILE B 2 183 ? 17.749  -20.92  -25.329 1   112.21 ? 499 ILE B N     1 
ATOM   3142 C  CA    . ILE B 2 183 ? 18.605  -20.883 -26.508 1   111.96 ? 499 ILE B CA    1 
ATOM   3143 C  C     . ILE B 2 183 ? 19.571  -22.04  -26.335 1   111.25 ? 499 ILE B C     1 
ATOM   3144 O  O     . ILE B 2 183 ? 20.246  -22.102 -25.313 1   111.39 ? 499 ILE B O     1 
ATOM   3145 C  CB    . ILE B 2 183 ? 19.357  -19.54  -26.603 1   112.67 ? 499 ILE B CB    1 
ATOM   3146 C  CG1   . ILE B 2 183 ? 18.415  -18.329 -26.428 1   113.69 ? 499 ILE B CG1   1 
ATOM   3147 C  CG2   . ILE B 2 183 ? 20.173  -19.461 -27.885 1   113.16 ? 499 ILE B CG2   1 
ATOM   3148 C  CD1   . ILE B 2 183 ? 17.406  -18.131 -27.505 1   114.96 ? 499 ILE B CD1   1 
ATOM   3149 N  N     . ALA B 2 184 ? 19.619  -22.965 -27.289 1   110.39 ? 500 ALA B N     1 
ATOM   3150 C  CA    . ALA B 2 184 ? 20.471  -24.129 -27.15  1   110.35 ? 500 ALA B CA    1 
ATOM   3151 C  C     . ALA B 2 184 ? 21.531  -24.255 -28.213 1   110.37 ? 500 ALA B C     1 
ATOM   3152 O  O     . ALA B 2 184 ? 21.258  -24.045 -29.38  1   110.07 ? 500 ALA B O     1 
ATOM   3153 C  CB    . ALA B 2 184 ? 19.622  -25.374 -27.115 1   110.55 ? 500 ALA B CB    1 
ATOM   3154 N  N     . LYS B 2 185 ? 22.742  -24.624 -27.805 1   110.81 ? 501 LYS B N     1 
ATOM   3155 C  CA    . LYS B 2 185 ? 23.876  -24.84  -28.705 1   111.83 ? 501 LYS B CA    1 
ATOM   3156 C  C     . LYS B 2 185 ? 24.095  -26.358 -28.963 1   112.69 ? 501 LYS B C     1 
ATOM   3157 O  O     . LYS B 2 185 ? 23.287  -27.171 -28.521 1   112.97 ? 501 LYS B O     1 
ATOM   3158 C  CB    . LYS B 2 185 ? 25.139  -24.146 -28.146 1   113.77 ? 501 LYS B CB    1 
ATOM   3159 C  CG    . LYS B 2 185 ? 25.038  -22.62  -28.168 1   117.99 ? 501 LYS B CG    1 
ATOM   3160 C  CD    . LYS B 2 185 ? 25.764  -21.973 -26.985 1   122.23 ? 501 LYS B CD    1 
ATOM   3161 C  CE    . LYS B 2 185 ? 25.145  -20.655 -26.558 1   125.53 ? 501 LYS B CE    1 
ATOM   3162 N  NZ    . LYS B 2 185 ? 25.244  -20.441 -25.086 1   127.15 ? 501 LYS B NZ    1 
ATOM   3163 N  N     . LYS B 2 186 ? 25.155  -26.731 -29.704 1   112.91 ? 502 LYS B N     1 
ATOM   3164 C  CA    . LYS B 2 186 ? 25.507  -28.104 -30.078 1   113.49 ? 502 LYS B CA    1 
ATOM   3165 C  C     . LYS B 2 186 ? 25.259  -29.147 -28.986 1   113.52 ? 502 LYS B C     1 
ATOM   3166 O  O     . LYS B 2 186 ? 25.634  -28.932 -27.849 1   113.57 ? 502 LYS B O     1 
ATOM   3167 C  CB    . LYS B 2 186 ? 26.99   -28.144 -30.486 1   115.71 ? 502 LYS B CB    1 
ATOM   3168 C  CG    . LYS B 2 186 ? 27.369  -29.324 -31.368 1   120.33 ? 502 LYS B CG    1 
ATOM   3169 C  CD    . LYS B 2 186 ? 28.876  -29.394 -31.612 1   125.24 ? 502 LYS B CD    1 
ATOM   3170 C  CE    . LYS B 2 186 ? 29.244  -30.223 -32.83  1   129.02 ? 502 LYS B CE    1 
ATOM   3171 N  NZ    . LYS B 2 186 ? 28.898  -31.668 -32.684 1   131    ? 502 LYS B NZ    1 
ATOM   3172 N  N     . ASP B 2 187 ? 24.587  -30.244 -29.321 1   113.47 ? 503 ASP B N     1 
ATOM   3173 C  CA    . ASP B 2 187 ? 24.339  -31.38  -28.428 1   114.01 ? 503 ASP B CA    1 
ATOM   3174 C  C     . ASP B 2 187 ? 23.586  -31.082 -27.113 1   113.5  ? 503 ASP B C     1 
ATOM   3175 O  O     . ASP B 2 187 ? 23.684  -31.876 -26.179 1   113.57 ? 503 ASP B O     1 
ATOM   3176 C  CB    . ASP B 2 187 ? 25.662  -32.107 -28.111 1   116.55 ? 503 ASP B CB    1 
ATOM   3177 C  CG    . ASP B 2 187 ? 26.456  -32.51  -29.345 1   122.12 ? 503 ASP B CG    1 
ATOM   3178 O  OD1   . ASP B 2 187 ? 25.889  -33.213 -30.217 1   123.26 ? 503 ASP B OD1   1 
ATOM   3179 O  OD2   . ASP B 2 187 ? 27.647  -32.131 -29.435 1   124.31 ? 503 ASP B OD2   1 
ATOM   3180 N  N     . ALA B 2 188 ? 22.82   -29.99  -27.047 1   112.91 ? 504 ALA B N     1 
ATOM   3181 C  CA    . ALA B 2 188 ? 22.049  -29.68  -25.843 1   112.92 ? 504 ALA B CA    1 
ATOM   3182 C  C     . ALA B 2 188 ? 20.79   -30.543 -25.743 1   112.57 ? 504 ALA B C     1 
ATOM   3183 O  O     . ALA B 2 188 ? 20.337  -31.093 -26.742 1   112.75 ? 504 ALA B O     1 
ATOM   3184 C  CB    . ALA B 2 188 ? 21.672  -28.211 -25.824 1   113.23 ? 504 ALA B CB    1 
ATOM   3185 N  N     . ILE B 2 189 ? 20.242  -30.692 -24.531 1   111.93 ? 505 ILE B N     1 
ATOM   3186 C  CA    . ILE B 2 189 ? 19.031  -31.468 -24.32  1   111.82 ? 505 ILE B CA    1 
ATOM   3187 C  C     . ILE B 2 189 ? 18.094  -30.671 -23.419 1   111.22 ? 505 ILE B C     1 
ATOM   3188 O  O     . ILE B 2 189 ? 18.503  -30.234 -22.351 1   111.32 ? 505 ILE B O     1 
ATOM   3189 C  CB    . ILE B 2 189 ? 19.355  -32.863 -23.735 1   112.53 ? 505 ILE B CB    1 
ATOM   3190 C  CG1   . ILE B 2 189 ? 20.119  -33.747 -24.753 1   113.52 ? 505 ILE B CG1   1 
ATOM   3191 C  CG2   . ILE B 2 189 ? 18.08   -33.559 -23.272 1   113.18 ? 505 ILE B CG2   1 
ATOM   3192 C  CD1   . ILE B 2 189 ? 21.619  -33.903 -24.509 1   114.76 ? 505 ILE B CD1   1 
ATOM   3193 N  N     . ILE B 2 190 ? 16.852  -30.453 -23.859 1   110.55 ? 506 ILE B N     1 
ATOM   3194 C  CA    . ILE B 2 190 ? 15.873  -29.689 -23.096 1   110.4  ? 506 ILE B CA    1 
ATOM   3195 C  C     . ILE B 2 190 ? 14.613  -30.527 -22.892 1   110.47 ? 506 ILE B C     1 
ATOM   3196 O  O     . ILE B 2 190 ? 14.127  -31.141 -23.833 1   110.31 ? 506 ILE B O     1 
ATOM   3197 C  CB    . ILE B 2 190 ? 15.545  -28.345 -23.809 1   110.62 ? 506 ILE B CB    1 
ATOM   3198 C  CG1   . ILE B 2 190 ? 16.811  -27.542 -24.129 1   111.6  ? 506 ILE B CG1   1 
ATOM   3199 C  CG2   . ILE B 2 190 ? 14.552  -27.499 -23.016 1   110.87 ? 506 ILE B CG2   1 
ATOM   3200 C  CD1   . ILE B 2 190 ? 17.398  -27.762 -25.53  1   112.87 ? 506 ILE B CD1   1 
ATOM   3201 N  N     . ASP B 2 191 ? 14.09   -30.553 -21.666 1   110.58 ? 507 ASP B N     1 
ATOM   3202 C  CA    . ASP B 2 191 ? 12.858  -31.249 -21.318 1   111.36 ? 507 ASP B CA    1 
ATOM   3203 C  C     . ASP B 2 191 ? 12.059  -30.311 -20.42  1   111.93 ? 507 ASP B C     1 
ATOM   3204 O  O     . ASP B 2 191 ? 12.419  -30.142 -19.263 1   112.15 ? 507 ASP B O     1 
ATOM   3205 C  CB    . ASP B 2 191 ? 13.173  -32.538 -20.55  1   113.56 ? 507 ASP B CB    1 
ATOM   3206 C  CG    . ASP B 2 191 ? 11.957  -33.394 -20.203 1   119.15 ? 507 ASP B CG    1 
ATOM   3207 O  OD1   . ASP B 2 191 ? 10.817  -32.979 -20.534 1   119.98 ? 507 ASP B OD1   1 
ATOM   3208 O  OD2   . ASP B 2 191 ? 12.144  -34.486 -19.603 1   121.56 ? 507 ASP B OD2   1 
ATOM   3209 N  N     . ILE B 2 192 ? 10.99   -29.691 -20.941 1   112.05 ? 508 ILE B N     1 
ATOM   3210 C  CA    . ILE B 2 192 ? 10.157  -28.753 -20.177 1   112.45 ? 508 ILE B CA    1 
ATOM   3211 C  C     . ILE B 2 192 ? 8.761   -29.351 -20.008 1   112.83 ? 508 ILE B C     1 
ATOM   3212 O  O     . ILE B 2 192 ? 8.203   -29.837 -20.978 1   113.27 ? 508 ILE B O     1 
ATOM   3213 C  CB    . ILE B 2 192 ? 10.089  -27.388 -20.903 1   112.81 ? 508 ILE B CB    1 
ATOM   3214 C  CG1   . ILE B 2 192 ? 11.478  -26.756 -21.045 1   113.75 ? 508 ILE B CG1   1 
ATOM   3215 C  CG2   . ILE B 2 192 ? 9.126   -26.447 -20.215 1   113.19 ? 508 ILE B CG2   1 
ATOM   3216 C  CD1   . ILE B 2 192 ? 11.498  -25.525 -21.95  1   115.22 ? 508 ILE B CD1   1 
ATOM   3217 N  N     . THR B 2 193 ? 8.206   -29.341 -18.79  1   112.44 ? 509 THR B N     1 
ATOM   3218 C  CA    . THR B 2 193 ? 6.89    -29.911 -18.525 1   112.4  ? 509 THR B CA    1 
ATOM   3219 C  C     . THR B 2 193 ? 6.02    -28.98  -17.68  1   112.83 ? 509 THR B C     1 
ATOM   3220 O  O     . THR B 2 193 ? 6.533   -28.249 -16.834 1   113.11 ? 509 THR B O     1 
ATOM   3221 C  CB    . THR B 2 193 ? 7.051   -31.274 -17.877 1   113.03 ? 509 THR B CB    1 
ATOM   3222 O  OG1   . THR B 2 193 ? 7.887   -32.088 -18.699 1   113.68 ? 509 THR B OG1   1 
ATOM   3223 C  CG2   . THR B 2 193 ? 5.728   -31.961 -17.622 1   113.43 ? 509 THR B CG2   1 
ATOM   3224 N  N     . THR B 2 194 ? 4.707   -28.985 -17.922 1   112.79 ? 510 THR B N     1 
ATOM   3225 C  CA    . THR B 2 194 ? 3.783   -28.151 -17.157 1   113.31 ? 510 THR B CA    1 
ATOM   3226 C  C     . THR B 2 194 ? 2.552   -28.986 -16.794 1   113.72 ? 510 THR B C     1 
ATOM   3227 O  O     . THR B 2 194 ? 1.913   -29.531 -17.686 1   113.97 ? 510 THR B O     1 
ATOM   3228 C  CB    . THR B 2 194 ? 3.336   -26.899 -17.958 1   114.49 ? 510 THR B CB    1 
ATOM   3229 O  OG1   . THR B 2 194 ? 4.353   -26.45  -18.858 1   115.39 ? 510 THR B OG1   1 
ATOM   3230 C  CG2   . THR B 2 194 ? 2.891   -25.761 -17.053 1   114.91 ? 510 THR B CG2   1 
ATOM   3231 N  N     . ARG B 2 195 ? 2.214   -29.094 -15.504 1   113.56 ? 511 ARG B N     1 
ATOM   3232 C  CA    . ARG B 2 195 ? 1.014   -29.815 -15.078 1   113.85 ? 511 ARG B CA    1 
ATOM   3233 C  C     . ARG B 2 195 ? 0.132   -28.825 -14.316 1   113.53 ? 511 ARG B C     1 
ATOM   3234 O  O     . ARG B 2 195 ? 0.554   -28.338 -13.277 1   113.67 ? 511 ARG B O     1 
ATOM   3235 C  CB    . ARG B 2 195 ? 1.37    -31.039 -14.213 1   115.69 ? 511 ARG B CB    1 
ATOM   3236 C  CG    . ARG B 2 195 ? 2.042   -32.16  -15.011 1   119.86 ? 511 ARG B CG    1 
ATOM   3237 C  CD    . ARG B 2 195 ? 2.141   -33.487 -14.261 1   124.11 ? 511 ARG B CD    1 
ATOM   3238 N  NE    . ARG B 2 195 ? 1.193   -34.479 -14.787 1   127.78 ? 511 ARG B NE    1 
ATOM   3239 C  CZ    . ARG B 2 195 ? 1.532   -35.617 -15.394 1   130.32 ? 511 ARG B CZ    1 
ATOM   3240 N  NH1   . ARG B 2 195 ? 2.807   -35.965 -15.505 1   130.36 ? 511 ARG B NH1   1 
ATOM   3241 N  NH2   . ARG B 2 195 ? 0.595   -36.44  -15.844 1   130.12 ? 511 ARG B NH2   1 
ATOM   3242 N  N     . THR B 2 196 ? -1.051  -28.465 -14.852 1   112.94 ? 512 THR B N     1 
ATOM   3243 C  CA    . THR B 2 196 ? -1.921  -27.483 -14.204 1   112.87 ? 512 THR B CA    1 
ATOM   3244 C  C     . THR B 2 196 ? -3.34   -27.953 -13.996 1   113.44 ? 512 THR B C     1 
ATOM   3245 O  O     . THR B 2 196 ? -3.863  -28.714 -14.791 1   113.5  ? 512 THR B O     1 
ATOM   3246 C  CB    . THR B 2 196 ? -1.954  -26.191 -15.006 1   113.36 ? 512 THR B CB    1 
ATOM   3247 O  OG1   . THR B 2 196 ? -2.278  -26.484 -16.371 1   113.68 ? 512 THR B OG1   1 
ATOM   3248 C  CG2   . THR B 2 196 ? -0.656  -25.409 -14.899 1   113.7  ? 512 THR B CG2   1 
ATOM   3249 N  N     . TYR B 2 197 ? -3.98   -27.466 -12.946 1   113.99 ? 513 TYR B N     1 
ATOM   3250 C  CA    . TYR B 2 197 ? -5.363  -27.793 -12.667 1   115.36 ? 513 TYR B CA    1 
ATOM   3251 C  C     . TYR B 2 197 ? -6.09   -26.507 -12.348 1   115.62 ? 513 TYR B C     1 
ATOM   3252 O  O     . TYR B 2 197 ? -6.03   -26.026 -11.215 1   115.82 ? 513 TYR B O     1 
ATOM   3253 C  CB    . TYR B 2 197 ? -5.475  -28.789 -11.513 1   116.39 ? 513 TYR B CB    1 
ATOM   3254 C  CG    . TYR B 2 197 ? -6.898  -29.257 -11.294 1   118.31 ? 513 TYR B CG    1 
ATOM   3255 C  CD1   . TYR B 2 197 ? -7.665  -29.737 -12.351 1   119.38 ? 513 TYR B CD1   1 
ATOM   3256 C  CD2   . TYR B 2 197 ? -7.482  -29.206 -10.035 1   119.72 ? 513 TYR B CD2   1 
ATOM   3257 C  CE1   . TYR B 2 197 ? -8.978  -30.148 -12.161 1   120.42 ? 513 TYR B CE1   1 
ATOM   3258 C  CE2   . TYR B 2 197 ? -8.787  -29.638 -9.829  1   120.81 ? 513 TYR B CE2   1 
ATOM   3259 C  CZ    . TYR B 2 197 ? -9.536  -30.096 -10.898 1   121.76 ? 513 TYR B CZ    1 
ATOM   3260 O  OH    . TYR B 2 197 ? -10.828 -30.515 -10.696 1   123.76 ? 513 TYR B OH    1 
ATOM   3261 N  N     . ALA B 2 198 ? -6.745  -25.924 -13.361 1   115.53 ? 514 ALA B N     1 
ATOM   3262 C  CA    . ALA B 2 198 ? -7.458  -24.659 -13.212 1   115.98 ? 514 ALA B CA    1 
ATOM   3263 C  C     . ALA B 2 198 ? -8.924  -24.842 -12.838 1   116.19 ? 514 ALA B C     1 
ATOM   3264 O  O     . ALA B 2 198 ? -9.645  -25.608 -13.473 1   116.25 ? 514 ALA B O     1 
ATOM   3265 C  CB    . ALA B 2 198 ? -7.334  -23.838 -14.48  1   116.16 ? 514 ALA B CB    1 
ATOM   3266 N  N     . ILE B 2 199 ? -9.347  -24.142 -11.78  1   116.16 ? 515 ILE B N     1 
ATOM   3267 C  CA    . ILE B 2 199 ? -10.696 -24.181 -11.219 1   116.7  ? 515 ILE B CA    1 
ATOM   3268 C  C     . ILE B 2 199 ? -11.254 -22.759 -11.02  1   116.89 ? 515 ILE B C     1 
ATOM   3269 O  O     . ILE B 2 199 ? -10.51  -21.789 -11.11  1   117.14 ? 515 ILE B O     1 
ATOM   3270 C  CB    . ILE B 2 199 ? -10.628 -24.929 -9.863  1   117.54 ? 515 ILE B CB    1 
ATOM   3271 C  CG1   . ILE B 2 199 ? -9.727  -24.171 -8.867  1   118.72 ? 515 ILE B CG1   1 
ATOM   3272 C  CG2   . ILE B 2 199 ? -10.162 -26.365 -10.044 1   118.13 ? 515 ILE B CG2   1 
ATOM   3273 C  CD1   . ILE B 2 199 ? -9.816  -24.686 -7.471  1   120.24 ? 515 ILE B CD1   1 
ATOM   3274 N  N     . LYS B 2 200 ? -12.56  -22.637 -10.716 1   116.69 ? 516 LYS B N     1 
ATOM   3275 C  CA    . LYS B 2 200 ? -13.251 -21.365 -10.474 1   116.87 ? 516 LYS B CA    1 
ATOM   3276 C  C     . LYS B 2 200 ? -12.954 -20.341 -11.608 1   116.89 ? 516 LYS B C     1 
ATOM   3277 O  O     . LYS B 2 200 ? -13.131 -20.708 -12.764 1   117.25 ? 516 LYS B O     1 
ATOM   3278 C  CB    . LYS B 2 200 ? -12.961 -20.843 -9.051  1   118.46 ? 516 LYS B CB    1 
ATOM   3279 C  CG    . LYS B 2 200 ? -13.513 -21.714 -7.937  1   122.14 ? 516 LYS B CG    1 
ATOM   3280 C  CD    . LYS B 2 200 ? -13.781 -20.843 -6.717  1   126.22 ? 516 LYS B CD    1 
ATOM   3281 C  CE    . LYS B 2 200 ? -13.972 -21.605 -5.43   1   129.28 ? 516 LYS B CE    1 
ATOM   3282 N  NZ    . LYS B 2 200 ? -13.962 -20.693 -4.249  1   130.83 ? 516 LYS B NZ    1 
ATOM   3283 N  N     . GLU B 2 201 ? -12.443 -19.13  -11.319 1   116.35 ? 517 GLU B N     1 
ATOM   3284 C  CA    . GLU B 2 201 ? -12.143 -18.155 -12.361 1   116.48 ? 517 GLU B CA    1 
ATOM   3285 C  C     . GLU B 2 201 ? -10.638 -18.044 -12.623 1   115.36 ? 517 GLU B C     1 
ATOM   3286 O  O     . GLU B 2 201 ? -10.153 -16.957 -12.948 1   115.47 ? 517 GLU B O     1 
ATOM   3287 C  CB    . GLU B 2 201 ? -12.729 -16.785 -12     1   120.33 ? 517 GLU B CB    1 
ATOM   3288 C  CG    . GLU B 2 201 ? -14.247 -16.738 -12.025 1   128.13 ? 517 GLU B CG    1 
ATOM   3289 C  CD    . GLU B 2 201 ? -14.94  -17.514 -10.92  1   137.46 ? 517 GLU B CD    1 
ATOM   3290 O  OE1   . GLU B 2 201 ? -15.85  -18.315 -11.241 1   139.57 ? 517 GLU B OE1   1 
ATOM   3291 O  OE2   . GLU B 2 201 ? -14.558 -17.339 -9.739  1   140.25 ? 517 GLU B OE2   1 
ATOM   3292 N  N     . ASP B 2 202 ? -9.901  -19.162 -12.479 1   114.1  ? 518 ASP B N     1 
ATOM   3293 C  CA    . ASP B 2 202 ? -8.452  -19.201 -12.693 1   113.27 ? 518 ASP B CA    1 
ATOM   3294 C  C     . ASP B 2 202 ? -8.049  -18.819 -14.103 1   111.87 ? 518 ASP B C     1 
ATOM   3295 O  O     . ASP B 2 202 ? -8.771  -19.09  -15.059 1   112.17 ? 518 ASP B O     1 
ATOM   3296 C  CB    . ASP B 2 202 ? -7.886  -20.6   -12.395 1   114.96 ? 518 ASP B CB    1 
ATOM   3297 C  CG    . ASP B 2 202 ? -7.648  -20.899 -10.935 1   119.39 ? 518 ASP B CG    1 
ATOM   3298 O  OD1   . ASP B 2 202 ? -7.792  -19.973 -10.104 1   119.73 ? 518 ASP B OD1   1 
ATOM   3299 O  OD2   . ASP B 2 202 ? -7.304  -22.057 -10.616 1   121.99 ? 518 ASP B OD2   1 
ATOM   3300 N  N     . VAL B 2 203 ? -6.88   -18.211 -14.235 1   110.16 ? 519 VAL B N     1 
ATOM   3301 C  CA    . VAL B 2 203 ? -6.347  -17.86  -15.533 1   109.21 ? 519 VAL B CA    1 
ATOM   3302 C  C     . VAL B 2 203 ? -4.966  -18.464 -15.635 1   108.11 ? 519 VAL B C     1 
ATOM   3303 O  O     . VAL B 2 203 ? -4.158  -18.246 -14.742 1   108.22 ? 519 VAL B O     1 
ATOM   3304 C  CB    . VAL B 2 203 ? -6.321  -16.343 -15.716 1   110.1  ? 519 VAL B CB    1 
ATOM   3305 C  CG1   . VAL B 2 203 ? -5.458  -15.948 -16.913 1   110.9  ? 519 VAL B CG1   1 
ATOM   3306 C  CG2   . VAL B 2 203 ? -7.737  -15.807 -15.866 1   110.59 ? 519 VAL B CG2   1 
ATOM   3307 N  N     . VAL B 2 204 ? -4.701  -19.252 -16.694 1   106.81 ? 520 VAL B N     1 
ATOM   3308 C  CA    . VAL B 2 204 ? -3.395  -19.863 -16.926 1   105.83 ? 520 VAL B CA    1 
ATOM   3309 C  C     . VAL B 2 204 ? -2.84   -19.346 -18.245 1   105.54 ? 520 VAL B C     1 
ATOM   3310 O  O     . VAL B 2 204 ? -3.511  -19.406 -19.268 1   105.51 ? 520 VAL B O     1 
ATOM   3311 C  CB    . VAL B 2 204 ? -3.421  -21.409 -16.882 1   105.57 ? 520 VAL B CB    1 
ATOM   3312 C  CG1   . VAL B 2 204 ? -2.084  -21.991 -17.311 1   105.84 ? 520 VAL B CG1   1 
ATOM   3313 C  CG2   . VAL B 2 204 ? -3.804  -21.918 -15.5   1   105.72 ? 520 VAL B CG2   1 
ATOM   3314 N  N     . LYS B 2 205 ? -1.634  -18.805 -18.211 1   105.3  ? 521 LYS B N     1 
ATOM   3315 C  CA    . LYS B 2 205 ? -0.957  -18.297 -19.389 1   105.76 ? 521 LYS B CA    1 
ATOM   3316 C  C     . LYS B 2 205 ? 0.432   -18.927 -19.423 1   105.6  ? 521 LYS B C     1 
ATOM   3317 O  O     . LYS B 2 205 ? 1.19    -18.773 -18.47  1   105.87 ? 521 LYS B O     1 
ATOM   3318 C  CB    . LYS B 2 205 ? -0.842  -16.764 -19.317 1   108.51 ? 521 LYS B CB    1 
ATOM   3319 C  CG    . LYS B 2 205 ? -2.088  -16.034 -19.811 1   114.08 ? 521 LYS B CG    1 
ATOM   3320 C  CD    . LYS B 2 205 ? -2.43   -14.772 -18.984 1   119.8  ? 521 LYS B CD    1 
ATOM   3321 C  CE    . LYS B 2 205 ? -1.378  -13.682 -19.031 1   123.92 ? 521 LYS B CE    1 
ATOM   3322 N  NZ    . LYS B 2 205 ? -1.864  -12.406 -18.43  1   125.76 ? 521 LYS B NZ    1 
ATOM   3323 N  N     . VAL B 2 206 ? 0.754   -19.685 -20.473 1   105.09 ? 522 VAL B N     1 
ATOM   3324 C  CA    . VAL B 2 206 ? 2.073   -20.309 -20.597 1   105.19 ? 522 VAL B CA    1 
ATOM   3325 C  C     . VAL B 2 206 ? 2.636   -19.943 -21.944 1   105.4  ? 522 VAL B C     1 
ATOM   3326 O  O     . VAL B 2 206 ? 2.004   -20.208 -22.955 1   105.64 ? 522 VAL B O     1 
ATOM   3327 C  CB    . VAL B 2 206 ? 2.058   -21.841 -20.409 1   105.79 ? 522 VAL B CB    1 
ATOM   3328 C  CG1   . VAL B 2 206 ? 3.461   -22.418 -20.573 1   106.29 ? 522 VAL B CG1   1 
ATOM   3329 C  CG2   . VAL B 2 206 ? 1.472   -22.229 -19.054 1   106.22 ? 522 VAL B CG2   1 
ATOM   3330 N  N     . ASN B 2 207 ? 3.799   -19.317 -21.967 1   105.26 ? 523 ASN B N     1 
ATOM   3331 C  CA    . ASN B 2 207 ? 4.415   -18.892 -23.209 1   105.7  ? 523 ASN B CA    1 
ATOM   3332 C  C     . ASN B 2 207 ? 5.851   -19.355 -23.19  1   105.45 ? 523 ASN B C     1 
ATOM   3333 O  O     . ASN B 2 207 ? 6.671   -18.741 -22.52  1   105.56 ? 523 ASN B O     1 
ATOM   3334 C  CB    . ASN B 2 207 ? 4.333   -17.376 -23.312 1   107.64 ? 523 ASN B CB    1 
ATOM   3335 C  CG    . ASN B 2 207 ? 4.561   -16.841 -24.696 1   112.32 ? 523 ASN B CG    1 
ATOM   3336 O  OD1   . ASN B 2 207 ? 5.087   -17.533 -25.574 1   114.29 ? 523 ASN B OD1   1 
ATOM   3337 N  ND2   . ASN B 2 207 ? 4.184   -15.584 -24.92  1   113.18 ? 523 ASN B ND2   1 
ATOM   3338 N  N     . GLU B 2 208 ? 6.161   -20.45  -23.885 1   105.09 ? 524 GLU B N     1 
ATOM   3339 C  CA    . GLU B 2 208 ? 7.522   -20.972 -23.898 1   105.34 ? 524 GLU B CA    1 
ATOM   3340 C  C     . GLU B 2 208 ? 8.093   -21.008 -25.304 1   104.87 ? 524 GLU B C     1 
ATOM   3341 O  O     . GLU B 2 208 ? 7.39    -21.384 -26.228 1   105.36 ? 524 GLU B O     1 
ATOM   3342 C  CB    . GLU B 2 208 ? 7.57    -22.356 -23.237 1   108.28 ? 524 GLU B CB    1 
ATOM   3343 C  CG    . GLU B 2 208 ? 7.315   -22.29  -21.742 1   114.44 ? 524 GLU B CG    1 
ATOM   3344 C  CD    . GLU B 2 208 ? 6.948   -23.6   -21.073 1   122.41 ? 524 GLU B CD    1 
ATOM   3345 O  OE1   . GLU B 2 208 ? 6.506   -24.533 -21.783 1   124.31 ? 524 GLU B OE1   1 
ATOM   3346 O  OE2   . GLU B 2 208 ? 7.091   -23.69  -19.831 1   124.64 ? 524 GLU B OE2   1 
ATOM   3347 N  N     . VAL B 2 209 ? 9.347   -20.577 -25.481 1   103.77 ? 525 VAL B N     1 
ATOM   3348 C  CA    . VAL B 2 209 ? 10.011  -20.606 -26.781 1   103.23 ? 525 VAL B CA    1 
ATOM   3349 C  C     . VAL B 2 209 ? 11.35   -21.32  -26.626 1   102.69 ? 525 VAL B C     1 
ATOM   3350 O  O     . VAL B 2 209 ? 12.103  -20.977 -25.726 1   102.97 ? 525 VAL B O     1 
ATOM   3351 C  CB    . VAL B 2 209 ? 10.22   -19.19  -27.362 1   103.83 ? 525 VAL B CB    1 
ATOM   3352 C  CG1   . VAL B 2 209 ? 11.047  -19.245 -28.642 1   104.5  ? 525 VAL B CG1   1 
ATOM   3353 C  CG2   . VAL B 2 209 ? 8.886   -18.492 -27.61  1   104.27 ? 525 VAL B CG2   1 
ATOM   3354 N  N     . VAL B 2 210 ? 11.644  -22.323 -27.468 1   101.72 ? 526 VAL B N     1 
ATOM   3355 C  CA    . VAL B 2 210 ? 12.921  -23.026 -27.438 1   101.17 ? 526 VAL B CA    1 
ATOM   3356 C  C     . VAL B 2 210 ? 13.592  -22.898 -28.803 1   100.75 ? 526 VAL B C     1 
ATOM   3357 O  O     . VAL B 2 210 ? 13.026  -23.307 -29.807 1   100.69 ? 526 VAL B O     1 
ATOM   3358 C  CB    . VAL B 2 210 ? 12.794  -24.5   -27.006 1   101.66 ? 526 VAL B CB    1 
ATOM   3359 C  CG1   . VAL B 2 210 ? 14.136  -25.215 -27.14  1   102.26 ? 526 VAL B CG1   1 
ATOM   3360 C  CG2   . VAL B 2 210 ? 12.263  -24.609 -25.58  1   102.03 ? 526 VAL B CG2   1 
ATOM   3361 N  N     . LYS B 2 211 ? 14.783  -22.319 -28.845 1   100.41 ? 527 LYS B N     1 
ATOM   3362 C  CA    . LYS B 2 211 ? 15.52   -22.141 -30.082 1   100.8  ? 527 LYS B CA    1 
ATOM   3363 C  C     . LYS B 2 211 ? 16.699  -23.115 -30.152 1   101.31 ? 527 LYS B C     1 
ATOM   3364 O  O     . LYS B 2 211 ? 17.684  -22.944 -29.444 1   101.3  ? 527 LYS B O     1 
ATOM   3365 C  CB    . LYS B 2 211 ? 16.003  -20.691 -30.202 1   102.37 ? 527 LYS B CB    1 
ATOM   3366 C  CG    . LYS B 2 211 ? 14.897  -19.662 -29.987 1   106.26 ? 527 LYS B CG    1 
ATOM   3367 C  CD    . LYS B 2 211 ? 15.328  -18.262 -30.427 1   111.16 ? 527 LYS B CD    1 
ATOM   3368 C  CE    . LYS B 2 211 ? 14.216  -17.23  -30.359 1   115.09 ? 527 LYS B CE    1 
ATOM   3369 N  NZ    . LYS B 2 211 ? 14.289  -16.236 -31.479 1   117.28 ? 527 LYS B NZ    1 
ATOM   3370 N  N     . LEU B 2 212 ? 16.594  -24.143 -30.993 1   101.65 ? 528 LEU B N     1 
ATOM   3371 C  CA    . LEU B 2 212 ? 17.654  -25.133 -31.172 1   102.63 ? 528 LEU B CA    1 
ATOM   3372 C  C     . LEU B 2 212 ? 18.646  -24.593 -32.186 1   103.27 ? 528 LEU B C     1 
ATOM   3373 O  O     . LEU B 2 212 ? 18.515  -24.827 -33.386 1   103.25 ? 528 LEU B O     1 
ATOM   3374 C  CB    . LEU B 2 212 ? 17.067  -26.476 -31.631 1   103.23 ? 528 LEU B CB    1 
ATOM   3375 C  CG    . LEU B 2 212 ? 15.939  -27.026 -30.755 1   105.38 ? 528 LEU B CG    1 
ATOM   3376 C  CD1   . LEU B 2 212 ? 15.371  -28.285 -31.335 1   106.06 ? 528 LEU B CD1   1 
ATOM   3377 C  CD2   . LEU B 2 212 ? 16.404  -27.26  -29.324 1   106.33 ? 528 LEU B CD2   1 
ATOM   3378 N  N     . ASN B 2 213 ? 19.614  -23.821 -31.698 1   103.78 ? 529 ASN B N     1 
ATOM   3379 C  CA    . ASN B 2 213 ? 20.593  -23.131 -32.534 1   104.8  ? 529 ASN B CA    1 
ATOM   3380 C  C     . ASN B 2 213 ? 21.937  -23.85  -32.726 1   105.2  ? 529 ASN B C     1 
ATOM   3381 O  O     . ASN B 2 213 ? 22.87   -23.246 -33.265 1   105.73 ? 529 ASN B O     1 
ATOM   3382 C  CB    . ASN B 2 213 ? 20.834  -21.711 -32     1   106.21 ? 529 ASN B CB    1 
ATOM   3383 C  CG    . ASN B 2 213 ? 19.606  -20.839 -32.05  1   109.43 ? 529 ASN B CG    1 
ATOM   3384 O  OD1   . ASN B 2 213 ? 18.666  -21.097 -32.806 1   110.66 ? 529 ASN B OD1   1 
ATOM   3385 N  ND2   . ASN B 2 213 ? 19.586  -19.786 -31.248 1   109.95 ? 529 ASN B ND2   1 
ATOM   3386 N  N     . GLY B 2 214 ? 22.034  -25.106 -32.301 1   104.61 ? 530 GLY B N     1 
ATOM   3387 C  CA    . GLY B 2 214 ? 23.272  -25.86  -32.458 1   104.48 ? 530 GLY B CA    1 
ATOM   3388 C  C     . GLY B 2 214 ? 23.053  -27.247 -33.012 1   103.99 ? 530 GLY B C     1 
ATOM   3389 O  O     . GLY B 2 214 ? 21.966  -27.793 -32.846 1   104.18 ? 530 GLY B O     1 
ATOM   3390 N  N     . GLU B 2 215 ? 24.063  -27.821 -33.698 1   103.29 ? 531 GLU B N     1 
ATOM   3391 C  CA    . GLU B 2 215 ? 23.958  -29.16  -34.289 1   103.26 ? 531 GLU B CA    1 
ATOM   3392 C  C     . GLU B 2 215 ? 23.564  -30.217 -33.256 1   103.02 ? 531 GLU B C     1 
ATOM   3393 O  O     . GLU B 2 215 ? 24.155  -30.256 -32.184 1   103.33 ? 531 GLU B O     1 
ATOM   3394 C  CB    . GLU B 2 215 ? 25.276  -29.588 -34.979 1   105.3  ? 531 GLU B CB    1 
ATOM   3395 C  CG    . GLU B 2 215 ? 25.191  -30.965 -35.637 1   109.9  ? 531 GLU B CG    1 
ATOM   3396 C  CD    . GLU B 2 215 ? 26.461  -31.659 -36.105 1   115.71 ? 531 GLU B CD    1 
ATOM   3397 O  OE1   . GLU B 2 215 ? 27.475  -31.618 -35.371 1   116.89 ? 531 GLU B OE1   1 
ATOM   3398 O  OE2   . GLU B 2 215 ? 26.424  -32.292 -37.186 1   117.38 ? 531 GLU B OE2   1 
ATOM   3399 N  N     . ASN B 2 216 ? 22.55   -31.046 -33.574 1   102.2  ? 532 ASN B N     1 
ATOM   3400 C  CA    . ASN B 2 216 ? 22.063  -32.16  -32.755 1   101.84 ? 532 ASN B CA    1 
ATOM   3401 C  C     . ASN B 2 216 ? 21.398  -31.753 -31.43  1   101.11 ? 532 ASN B C     1 
ATOM   3402 O  O     . ASN B 2 216 ? 21.224  -32.614 -30.569 1   101.08 ? 532 ASN B O     1 
ATOM   3403 C  CB    . ASN B 2 216 ? 23.166  -33.204 -32.503 1   103.1  ? 532 ASN B CB    1 
ATOM   3404 C  CG    . ASN B 2 216 ? 23.045  -34.469 -33.346 1   106.73 ? 532 ASN B CG    1 
ATOM   3405 O  OD1   . ASN B 2 216 ? 22.118  -35.281 -33.191 1   107.85 ? 532 ASN B OD1   1 
ATOM   3406 N  ND2   . ASN B 2 216 ? 23.994  -34.678 -34.254 1   107.56 ? 532 ASN B ND2   1 
ATOM   3407 N  N     . ALA B 2 217 ? 20.992  -30.476 -31.271 1   100.38 ? 533 ALA B N     1 
ATOM   3408 C  CA    . ALA B 2 217 ? 20.315  -30.035 -30.047 1   100.22 ? 533 ALA B CA    1 
ATOM   3409 C  C     . ALA B 2 217 ? 18.907  -30.61  -30.026 1   99.97  ? 533 ALA B C     1 
ATOM   3410 O  O     . ALA B 2 217 ? 18.208  -30.51  -31.024 1   100.08 ? 533 ALA B O     1 
ATOM   3411 C  CB    . ALA B 2 217 ? 20.252  -28.522 -29.997 1   100.31 ? 533 ALA B CB    1 
ATOM   3412 N  N     . LYS B 2 218 ? 18.496  -31.244 -28.917 1   99.46  ? 534 LYS B N     1 
ATOM   3413 C  CA    . LYS B 2 218 ? 17.184  -31.878 -28.833 1   99.49  ? 534 LYS B CA    1 
ATOM   3414 C  C     . LYS B 2 218 ? 16.281  -31.272 -27.78  1   98.71  ? 534 LYS B C     1 
ATOM   3415 O  O     . LYS B 2 218 ? 16.754  -30.897 -26.722 1   98.58  ? 534 LYS B O     1 
ATOM   3416 C  CB    . LYS B 2 218 ? 17.333  -33.389 -28.621 1   102.27 ? 534 LYS B CB    1 
ATOM   3417 C  CG    . LYS B 2 218 ? 18.203  -34.05  -29.692 1   107.97 ? 534 LYS B CG    1 
ATOM   3418 C  CD    . LYS B 2 218 ? 17.586  -35.293 -30.347 1   113.66 ? 534 LYS B CD    1 
ATOM   3419 C  CE    . LYS B 2 218 ? 18.475  -35.868 -31.436 1   117.74 ? 534 LYS B CE    1 
ATOM   3420 N  NZ    . LYS B 2 218 ? 17.733  -36.796 -32.337 1   119.91 ? 534 LYS B NZ    1 
ATOM   3421 N  N     . CYS B 2 219 ? 14.977  -31.207 -28.054 1   98.28  ? 535 CYS B N     1 
ATOM   3422 C  CA    . CYS B 2 219 ? 14.029  -30.604 -27.129 1   98.62  ? 535 CYS B CA    1 
ATOM   3423 C  C     . CYS B 2 219 ? 12.681  -31.296 -27.065 1   98.46  ? 535 CYS B C     1 
ATOM   3424 O  O     . CYS B 2 219 ? 12.118  -31.651 -28.09  1   98.82  ? 535 CYS B O     1 
ATOM   3425 C  CB    . CYS B 2 219 ? 13.858  -29.123 -27.459 1   99.84  ? 535 CYS B CB    1 
ATOM   3426 S  SG    . CYS B 2 219 ? 12.437  -28.329 -26.657 1   104.65 ? 535 CYS B SG    1 
ATOM   3427 N  N     . ILE B 2 220 ? 12.09   -31.321 -25.871 1   97.84  ? 536 ILE B N     1 
ATOM   3428 C  CA    . ILE B 2 220 ? 10.731  -31.79  -25.693 1   97.81  ? 536 ILE B CA    1 
ATOM   3429 C  C     . ILE B 2 220 ? 9.983   -30.854 -24.741 1   97.25  ? 536 ILE B C     1 
ATOM   3430 O  O     . ILE B 2 220 ? 10.461  -30.561 -23.654 1   96.95  ? 536 ILE B O     1 
ATOM   3431 C  CB    . ILE B 2 220 ? 10.621  -33.285 -25.317 1   98.71  ? 536 ILE B CB    1 
ATOM   3432 C  CG1   . ILE B 2 220 ? 9.134   -33.706 -25.086 1   100.05 ? 536 ILE B CG1   1 
ATOM   3433 C  CG2   . ILE B 2 220 ? 11.542  -33.648 -24.155 1   99.35  ? 536 ILE B CG2   1 
ATOM   3434 C  CD1   . ILE B 2 220 ? 8.548   -33.665 -23.599 1   101.6  ? 536 ILE B CD1   1 
ATOM   3435 N  N     . ILE B 2 221 ? 8.836   -30.345 -25.183 1   97.02  ? 537 ILE B N     1 
ATOM   3436 C  CA    . ILE B 2 221 ? 7.972   -29.496 -24.378 1   97.26  ? 537 ILE B CA    1 
ATOM   3437 C  C     . ILE B 2 221 ? 6.691   -30.309 -24.188 1   97.71  ? 537 ILE B C     1 
ATOM   3438 O  O     . ILE B 2 221 ? 6.065   -30.704 -25.163 1   98.19  ? 537 ILE B O     1 
ATOM   3439 C  CB    . ILE B 2 221 ? 7.679   -28.118 -25.039 1   97.59  ? 537 ILE B CB    1 
ATOM   3440 C  CG1   . ILE B 2 221 ? 8.974   -27.364 -25.404 1   98.47  ? 537 ILE B CG1   1 
ATOM   3441 C  CG2   . ILE B 2 221 ? 6.784   -27.268 -24.138 1   98.12  ? 537 ILE B CG2   1 
ATOM   3442 C  CD1   . ILE B 2 221 ? 8.751   -25.934 -26.124 1   99.85  ? 537 ILE B CD1   1 
ATOM   3443 N  N     . LYS B 2 222 ? 6.333   -30.606 -22.95  1   97.44  ? 538 LYS B N     1 
ATOM   3444 C  CA    . LYS B 2 222 ? 5.159   -31.397 -22.64  1   97.65  ? 538 LYS B CA    1 
ATOM   3445 C  C     . LYS B 2 222 ? 4.209   -30.595 -21.774 1   98.28  ? 538 LYS B C     1 
ATOM   3446 O  O     . LYS B 2 222 ? 4.632   -30.043 -20.771 1   98.72  ? 538 LYS B O     1 
ATOM   3447 C  CB    . LYS B 2 222 ? 5.605   -32.637 -21.884 1   99.05  ? 538 LYS B CB    1 
ATOM   3448 C  CG    . LYS B 2 222 ? 4.523   -33.67  -21.737 1   103.55 ? 538 LYS B CG    1 
ATOM   3449 C  CD    . LYS B 2 222 ? 5.141   -35.045 -21.485 1   108.27 ? 538 LYS B CD    1 
ATOM   3450 C  CE    . LYS B 2 222 ? 4.186   -36.017 -20.829 1   111.67 ? 538 LYS B CE    1 
ATOM   3451 N  NZ    . LYS B 2 222 ? 4.561   -37.433 -21.095 1   113.68 ? 538 LYS B NZ    1 
ATOM   3452 N  N     . SER B 2 223 ? 2.94    -30.506 -22.153 1   98.39  ? 539 SER B N     1 
ATOM   3453 C  CA    . SER B 2 223 ? 1.949   -29.793 -21.357 1   99.27  ? 539 SER B CA    1 
ATOM   3454 C  C     . SER B 2 223 ? 0.793   -30.717 -21.044 1   100.18 ? 539 SER B C     1 
ATOM   3455 O  O     . SER B 2 223 ? 0.253   -31.372 -21.93  1   100.69 ? 539 SER B O     1 
ATOM   3456 C  CB    . SER B 2 223 ? 1.448   -28.543 -22.067 1   100.56 ? 539 SER B CB    1 
ATOM   3457 O  OG    . SER B 2 223 ? 0.433   -27.924 -21.292 1   102.81 ? 539 SER B OG    1 
ATOM   3458 N  N     . ARG B 2 224 ? 0.436   -30.797 -19.778 1   100.22 ? 540 ARG B N     1 
ATOM   3459 C  CA    . ARG B 2 224 ? -0.652  -31.632 -19.304 1   100.79 ? 540 ARG B CA    1 
ATOM   3460 C  C     . ARG B 2 224 ? -1.509  -30.787 -18.369 1   100.8  ? 540 ARG B C     1 
ATOM   3461 O  O     . ARG B 2 224 ? -0.974  -29.944 -17.655 1   100.73 ? 540 ARG B O     1 
ATOM   3462 C  CB    . ARG B 2 224 ? -0.088  -32.86  -18.551 1   102.65 ? 540 ARG B CB    1 
ATOM   3463 C  CG    . ARG B 2 224 ? 0.718   -33.848 -19.402 1   106.22 ? 540 ARG B CG    1 
ATOM   3464 C  CD    . ARG B 2 224 ? -0.119  -34.386 -20.539 1   109.98 ? 540 ARG B CD    1 
ATOM   3465 N  NE    . ARG B 2 224 ? 0.559   -35.425 -21.311 1   113.21 ? 540 ARG B NE    1 
ATOM   3466 C  CZ    . ARG B 2 224 ? 1.072   -35.246 -22.523 1   115.38 ? 540 ARG B CZ    1 
ATOM   3467 N  NH1   . ARG B 2 224 ? 1.013   -34.054 -23.107 1   114.78 ? 540 ARG B NH1   1 
ATOM   3468 N  NH2   . ARG B 2 224 ? 1.641   -36.258 -23.164 1   115.58 ? 540 ARG B NH2   1 
ATOM   3469 N  N     . GLY B 2 225 ? -2.82   -30.998 -18.382 1   100.91 ? 541 GLY B N     1 
ATOM   3470 C  CA    . GLY B 2 225 ? -3.707  -30.241 -17.508 1   101.66 ? 541 GLY B CA    1 
ATOM   3471 C  C     . GLY B 2 225 ? -5.2    -30.418 -17.693 1   102.29 ? 541 GLY B C     1 
ATOM   3472 O  O     . GLY B 2 225 ? -5.653  -31.031 -18.66  1   102.48 ? 541 GLY B O     1 
ATOM   3473 N  N     . ALA B 2 226 ? -5.977  -29.856 -16.76  1   102.54 ? 542 ALA B N     1 
ATOM   3474 C  CA    . ALA B 2 226 ? -7.432  -29.899 -16.796 1   103.43 ? 542 ALA B CA    1 
ATOM   3475 C  C     . ALA B 2 226 ? -7.978  -28.543 -16.402 1   104.42 ? 542 ALA B C     1 
ATOM   3476 O  O     . ALA B 2 226 ? -7.515  -27.962 -15.426 1   104.71 ? 542 ALA B O     1 
ATOM   3477 C  CB    . ALA B 2 226 ? -7.943  -30.948 -15.836 1   103.66 ? 542 ALA B CB    1 
ATOM   3478 N  N     . ALA B 2 227 ? -8.948  -28.026 -17.16  1   104.88 ? 543 ALA B N     1 
ATOM   3479 C  CA    . ALA B 2 227 ? -9.554  -26.727 -16.89  1   105.8  ? 543 ALA B CA    1 
ATOM   3480 C  C     . ALA B 2 227 ? -11.041 -26.908 -16.643 1   106.78 ? 543 ALA B C     1 
ATOM   3481 O  O     . ALA B 2 227 ? -11.727 -27.499 -17.475 1   106.94 ? 543 ALA B O     1 
ATOM   3482 C  CB    . ALA B 2 227 ? -9.336  -25.8   -18.069 1   105.88 ? 543 ALA B CB    1 
ATOM   3483 N  N     . MET B 2 228 ? -11.539 -26.425 -15.497 1   107.32 ? 544 MET B N     1 
ATOM   3484 C  CA    . MET B 2 228 ? -12.955 -26.55  -15.156 1   108.44 ? 544 MET B CA    1 
ATOM   3485 C  C     . MET B 2 228 ? -13.601 -25.208 -14.756 1   109.29 ? 544 MET B C     1 
ATOM   3486 O  O     . MET B 2 228 ? -12.928 -24.177 -14.782 1   109.56 ? 544 MET B O     1 
ATOM   3487 C  CB    . MET B 2 228 ? -13.164 -27.637 -14.091 1   109.4  ? 544 MET B CB    1 
ATOM   3488 C  CG    . MET B 2 228 ? -12.35  -27.448 -12.876 1   112.25 ? 544 MET B CG    1 
ATOM   3489 S  SD    . MET B 2 228 ? -12.878 -28.666 -11.674 1   119.36 ? 544 MET B SD    1 
ATOM   3490 C  CE    . MET B 2 228 ? -13.543 -27.607 -10.411 1   119.2  ? 544 MET B CE    1 
ATOM   3491 N  N     . ASP B 2 229 ? -14.917 -25.214 -14.445 1   109.68 ? 545 ASP B N     1 
ATOM   3492 C  CA    . ASP B 2 229 ? -15.686 -24.041 -14.025 1   110.8  ? 545 ASP B CA    1 
ATOM   3493 C  C     . ASP B 2 229 ? -15.585 -22.87  -15.047 1   110.98 ? 545 ASP B C     1 
ATOM   3494 O  O     . ASP B 2 229 ? -16.047 -23.042 -16.16  1   111.23 ? 545 ASP B O     1 
ATOM   3495 C  CB    . ASP B 2 229 ? -15.331 -23.623 -12.573 1   113.53 ? 545 ASP B CB    1 
ATOM   3496 C  CG    . ASP B 2 229 ? -15.557 -24.686 -11.515 1   119.4  ? 545 ASP B CG    1 
ATOM   3497 O  OD1   . ASP B 2 229 ? -16.049 -25.78  -11.869 1   120.87 ? 545 ASP B OD1   1 
ATOM   3498 O  OD2   . ASP B 2 229 ? -15.26  -24.416 -10.324 1   121.31 ? 545 ASP B OD2   1 
ATOM   3499 N  N     . ASN B 2 230 ? -14.997 -21.712 -14.702 1   110.81 ? 546 ASN B N     1 
ATOM   3500 C  CA    . ASN B 2 230 ? -14.887 -20.583 -15.629 1   111.29 ? 546 ASN B CA    1 
ATOM   3501 C  C     . ASN B 2 230 ? -13.424 -20.214 -15.898 1   110.61 ? 546 ASN B C     1 
ATOM   3502 O  O     . ASN B 2 230 ? -13.102 -19.035 -16.075 1   110.79 ? 546 ASN B O     1 
ATOM   3503 C  CB    . ASN B 2 230 ? -15.64  -19.363 -15.078 1   113.41 ? 546 ASN B CB    1 
ATOM   3504 C  CG    . ASN B 2 230 ? -17.051 -19.668 -14.657 1   117.82 ? 546 ASN B CG    1 
ATOM   3505 O  OD1   . ASN B 2 230 ? -17.946 -19.843 -15.492 1   119.3  ? 546 ASN B OD1   1 
ATOM   3506 N  ND2   . ASN B 2 230 ? -17.274 -19.748 -13.349 1   118.83 ? 546 ASN B ND2   1 
ATOM   3507 N  N     . SER B 2 231 ? -12.539 -21.212 -15.905 1   109.57 ? 547 SER B N     1 
ATOM   3508 C  CA    . SER B 2 231 ? -11.126 -20.968 -16.128 1   109.11 ? 547 SER B CA    1 
ATOM   3509 C  C     . SER B 2 231 ? -10.79  -20.619 -17.58  1   108.21 ? 547 SER B C     1 
ATOM   3510 O  O     . SER B 2 231 ? -11.564 -20.89  -18.496 1   108.2  ? 547 SER B O     1 
ATOM   3511 C  CB    . SER B 2 231 ? -10.292 -22.136 -15.622 1   110.67 ? 547 SER B CB    1 
ATOM   3512 O  OG    . SER B 2 231 ? -10.785 -23.361 -16.135 1   113.52 ? 547 SER B OG    1 
ATOM   3513 N  N     . LYS B 2 232 ? -9.65   -19.97  -17.773 1   107.39 ? 548 LYS B N     1 
ATOM   3514 C  CA    . LYS B 2 232 ? -9.185  -19.533 -19.079 1   107.12 ? 548 LYS B CA    1 
ATOM   3515 C  C     . LYS B 2 232 ? -7.728  -19.941 -19.259 1   105.94 ? 548 LYS B C     1 
ATOM   3516 O  O     . LYS B 2 232 ? -6.873  -19.504 -18.496 1   106.3  ? 548 LYS B O     1 
ATOM   3517 C  CB    . LYS B 2 232 ? -9.311  -18.005 -19.178 1   109.59 ? 548 LYS B CB    1 
ATOM   3518 C  CG    . LYS B 2 232 ? -10.714 -17.532 -19.524 1   114.08 ? 548 LYS B CG    1 
ATOM   3519 C  CD    . LYS B 2 232 ? -10.872 -17.359 -21.041 1   118.42 ? 548 LYS B CD    1 
ATOM   3520 C  CE    . LYS B 2 232 ? -10.012 -16.235 -21.589 1   121.79 ? 548 LYS B CE    1 
ATOM   3521 N  NZ    . LYS B 2 232 ? -9.927  -16.251 -23.076 1   123.78 ? 548 LYS B NZ    1 
ATOM   3522 N  N     . ILE B 2 233 ? -7.437  -20.757 -20.268 1   104.4  ? 549 ILE B N     1 
ATOM   3523 C  CA    . ILE B 2 233 ? -6.083  -21.236 -20.507 1   103.48 ? 549 ILE B CA    1 
ATOM   3524 C  C     . ILE B 2 233 ? -5.574  -20.727 -21.851 1   102.44 ? 549 ILE B C     1 
ATOM   3525 O  O     . ILE B 2 233 ? -6.311  -20.728 -22.832 1   102.5  ? 549 ILE B O     1 
ATOM   3526 C  CB    . ILE B 2 233 ? -6.032  -22.792 -20.474 1   104.03 ? 549 ILE B CB    1 
ATOM   3527 C  CG1   . ILE B 2 233 ? -6.884  -23.414 -19.342 1   105.35 ? 549 ILE B CG1   1 
ATOM   3528 C  CG2   . ILE B 2 233 ? -4.605  -23.304 -20.427 1   104.36 ? 549 ILE B CG2   1 
ATOM   3529 C  CD1   . ILE B 2 233 ? -6.463  -23.097 -17.968 1   107    ? 549 ILE B CD1   1 
ATOM   3530 N  N     . SER B 2 234 ? -4.313  -20.311 -21.901 1   101.43 ? 550 SER B N     1 
ATOM   3531 C  CA    . SER B 2 234 ? -3.657  -19.906 -23.14  1   100.96 ? 550 SER B CA    1 
ATOM   3532 C  C     . SER B 2 234 ? -2.262  -20.521 -23.133 1   100.26 ? 550 SER B C     1 
ATOM   3533 O  O     . SER B 2 234 ? -1.454  -20.172 -22.282 1   100.51 ? 550 SER B O     1 
ATOM   3534 C  CB    . SER B 2 234 ? -3.556  -18.391 -23.246 1   102.11 ? 550 SER B CB    1 
ATOM   3535 O  OG    . SER B 2 234 ? -3.03   -18.032 -24.514 1   104.26 ? 550 SER B OG    1 
ATOM   3536 N  N     . LEU B 2 235 ? -1.989  -21.458 -24.038 1   99.3   ? 551 LEU B N     1 
ATOM   3537 C  CA    . LEU B 2 235 ? -0.7    -22.135 -24.081 1   98.98  ? 551 LEU B CA    1 
ATOM   3538 C  C     . LEU B 2 235 ? -0.005  -21.92  -25.411 1   98.86  ? 551 LEU B C     1 
ATOM   3539 O  O     . LEU B 2 235 ? -0.373  -22.553 -26.396 1   99.38  ? 551 LEU B O     1 
ATOM   3540 C  CB    . LEU B 2 235 ? -0.887  -23.64  -23.885 1   99.08  ? 551 LEU B CB    1 
ATOM   3541 C  CG    . LEU B 2 235 ? -1.741  -24.073 -22.721 1   100.44 ? 551 LEU B CG    1 
ATOM   3542 C  CD1   . LEU B 2 235 ? -2.221  -25.476 -22.922 1   101.23 ? 551 LEU B CD1   1 
ATOM   3543 C  CD2   . LEU B 2 235 ? -0.997  -23.96  -21.428 1   100.93 ? 551 LEU B CD2   1 
ATOM   3544 N  N     . LYS B 2 236 ? 1.008   -21.062 -25.438 1   98     ? 552 LYS B N     1 
ATOM   3545 C  CA    A LYS B 2 236 ? 1.788   -20.779 -26.638 0.5 98.07  ? 552 LYS B CA    1 
ATOM   3546 C  CA    B LYS B 2 236 ? 1.791   -20.789 -26.64  0.5 98.14  ? 552 LYS B CA    1 
ATOM   3547 C  C     . LYS B 2 236 ? 3.153   -21.452 -26.476 1   98.24  ? 552 LYS B C     1 
ATOM   3548 O  O     . LYS B 2 236 ? 3.976   -20.982 -25.707 1   98.34  ? 552 LYS B O     1 
ATOM   3549 C  CB    A LYS B 2 236 ? 1.951   -19.262 -26.787 0.5 99.49  ? 552 LYS B CB    1 
ATOM   3550 C  CB    B LYS B 2 236 ? 1.952   -19.278 -26.845 0.5 99.79  ? 552 LYS B CB    1 
ATOM   3551 C  CG    A LYS B 2 236 ? 2.347   -18.795 -28.175 0.5 102.61 ? 552 LYS B CG    1 
ATOM   3552 C  CG    B LYS B 2 236 ? 0.623   -18.531 -26.851 0.5 103.34 ? 552 LYS B CG    1 
ATOM   3553 C  CD    A LYS B 2 236 ? 2.473   -17.265 -28.236 0.5 105.65 ? 552 LYS B CD    1 
ATOM   3554 C  CD    B LYS B 2 236 ? 0.77    -17.039 -27.143 0.5 106.88 ? 552 LYS B CD    1 
ATOM   3555 C  CE    A LYS B 2 236 ? 2.949   -16.776 -29.581 0.5 108.18 ? 552 LYS B CE    1 
ATOM   3556 C  CE    B LYS B 2 236 ? -0.554  -16.322 -27.038 0.5 109.81 ? 552 LYS B CE    1 
ATOM   3557 N  NZ    A LYS B 2 236 ? 3.386   -15.36  -29.535 0.5 109.77 ? 552 LYS B NZ    1 
ATOM   3558 N  NZ    B LYS B 2 236 ? -0.434  -14.892 -27.406 0.5 111.56 ? 552 LYS B NZ    1 
ATOM   3559 N  N     . LEU B 2 237 ? 3.376   -22.575 -27.152 1   98.12  ? 553 LEU B N     1 
ATOM   3560 C  CA    . LEU B 2 237 ? 4.629   -23.327 -27.033 1   98.45  ? 553 LEU B CA    1 
ATOM   3561 C  C     . LEU B 2 237 ? 5.322   -23.329 -28.381 1   98.31  ? 553 LEU B C     1 
ATOM   3562 O  O     . LEU B 2 237 ? 4.708   -23.699 -29.369 1   98.46  ? 553 LEU B O     1 
ATOM   3563 C  CB    . LEU B 2 237 ? 4.324   -24.768 -26.594 1   99.06  ? 553 LEU B CB    1 
ATOM   3564 C  CG    . LEU B 2 237 ? 3.379   -24.939 -25.385 1   100.8  ? 553 LEU B CG    1 
ATOM   3565 C  CD1   . LEU B 2 237 ? 2.99    -26.405 -25.185 1   101.46 ? 553 LEU B CD1   1 
ATOM   3566 C  CD2   . LEU B 2 237 ? 3.986   -24.368 -24.124 1   101.27 ? 553 LEU B CD2   1 
ATOM   3567 N  N     . LYS B 2 238 ? 6.59    -22.916 -28.436 1   97.83  ? 554 LYS B N     1 
ATOM   3568 C  CA    . LYS B 2 238 ? 7.3     -22.764 -29.703 1   97.72  ? 554 LYS B CA    1 
ATOM   3569 C  C     . LYS B 2 238 ? 8.663   -23.448 -29.766 1   98.21  ? 554 LYS B C     1 
ATOM   3570 O  O     . LYS B 2 238 ? 9.41    -23.417 -28.797 1   98.16  ? 554 LYS B O     1 
ATOM   3571 C  CB    . LYS B 2 238 ? 7.445   -21.259 -30.016 1   97.95  ? 554 LYS B CB    1 
ATOM   3572 C  CG    . LYS B 2 238 ? 8.161   -20.928 -31.314 1   100.21 ? 554 LYS B CG    1 
ATOM   3573 C  CD    . LYS B 2 238 ? 8.243   -19.42  -31.515 1   103.72 ? 554 LYS B CD    1 
ATOM   3574 C  CE    . LYS B 2 238 ? 8.673   -18.995 -32.904 1   106.62 ? 554 LYS B CE    1 
ATOM   3575 N  NZ    . LYS B 2 238 ? 8.643   -17.511 -33.075 1   108.21 ? 554 LYS B NZ    1 
ATOM   3576 N  N     . ILE B 2 239 ? 8.984   -24.078 -30.909 1   98.46  ? 555 ILE B N     1 
ATOM   3577 C  CA    . ILE B 2 239 ? 10.295  -24.675 -31.127 1   98.88  ? 555 ILE B CA    1 
ATOM   3578 C  C     . ILE B 2 239 ? 10.86   -24.189 -32.468 1   99.14  ? 555 ILE B C     1 
ATOM   3579 O  O     . ILE B 2 239 ? 10.168  -24.235 -33.482 1   99.03  ? 555 ILE B O     1 
ATOM   3580 C  CB    . ILE B 2 239 ? 10.34   -26.228 -31.013 1   99.3   ? 555 ILE B CB    1 
ATOM   3581 C  CG1   . ILE B 2 239 ? 9.805   -26.73  -29.654 1   100.19 ? 555 ILE B CG1   1 
ATOM   3582 C  CG2   . ILE B 2 239 ? 11.773  -26.73  -31.239 1   99.83  ? 555 ILE B CG2   1 
ATOM   3583 C  CD1   . ILE B 2 239 ? 9.993   -28.302 -29.358 1   101.43 ? 555 ILE B CD1   1 
ATOM   3584 N  N     . GLU B 2 240 ? 12.104  -23.708 -32.468 1   99.34  ? 556 GLU B N     1 
ATOM   3585 C  CA    . GLU B 2 240 ? 12.778  -23.299 -33.686 1   100.34 ? 556 GLU B CA    1 
ATOM   3586 C  C     . GLU B 2 240 ? 13.924  -24.276 -33.956 1   100.45 ? 556 GLU B C     1 
ATOM   3587 O  O     . GLU B 2 240 ? 14.86   -24.35  -33.176 1   100.47 ? 556 GLU B O     1 
ATOM   3588 C  CB    . GLU B 2 240 ? 13.346  -21.886 -33.547 1   103.96 ? 556 GLU B CB    1 
ATOM   3589 C  CG    . GLU B 2 240 ? 12.302  -20.797 -33.383 1   111.77 ? 556 GLU B CG    1 
ATOM   3590 C  CD    . GLU B 2 240 ? 12.862  -19.381 -33.438 1   121.31 ? 556 GLU B CD    1 
ATOM   3591 O  OE1   . GLU B 2 240 ? 13.967  -19.201 -34.002 1   123.18 ? 556 GLU B OE1   1 
ATOM   3592 O  OE2   . GLU B 2 240 ? 12.195  -18.449 -32.928 1   124.53 ? 556 GLU B OE2   1 
ATOM   3593 N  N     . GLY B 2 241 ? 13.835  -25.023 -35.045 1   100.37 ? 557 GLY B N     1 
ATOM   3594 C  CA    . GLY B 2 241 ? 14.856  -25.973 -35.458 1   100.79 ? 557 GLY B CA    1 
ATOM   3595 C  C     . GLY B 2 241 ? 15.751  -25.281 -36.454 1   101.08 ? 557 GLY B C     1 
ATOM   3596 O  O     . GLY B 2 241 ? 15.5    -25.331 -37.657 1   100.84 ? 557 GLY B O     1 
ATOM   3597 N  N     . ASN B 2 242 ? 16.768  -24.576 -35.944 1   101.43 ? 558 ASN B N     1 
ATOM   3598 C  CA    . ASN B 2 242 ? 17.658  -23.745 -36.744 1   102.16 ? 558 ASN B CA    1 
ATOM   3599 C  C     . ASN B 2 242 ? 19.002  -24.376 -37.156 1   103.12 ? 558 ASN B C     1 
ATOM   3600 O  O     . ASN B 2 242 ? 19.734  -23.764 -37.932 1   103.38 ? 558 ASN B O     1 
ATOM   3601 C  CB    . ASN B 2 242 ? 17.903  -22.431 -36.003 1   102.68 ? 558 ASN B CB    1 
ATOM   3602 C  CG    . ASN B 2 242 ? 16.632  -21.653 -35.771 1   104.76 ? 558 ASN B CG    1 
ATOM   3603 O  OD1   . ASN B 2 242 ? 15.708  -21.683 -36.584 1   105.98 ? 558 ASN B OD1   1 
ATOM   3604 N  ND2   . ASN B 2 242 ? 16.55   -20.94  -34.665 1   104.61 ? 558 ASN B ND2   1 
ATOM   3605 N  N     . ALA B 2 243 ? 19.329  -25.578 -36.666 1   103.44 ? 559 ALA B N     1 
ATOM   3606 C  CA    . ALA B 2 243 ? 20.608  -26.215 -36.99  1   104.09 ? 559 ALA B CA    1 
ATOM   3607 C  C     . ALA B 2 243 ? 20.455  -27.667 -37.468 1   105.03 ? 559 ALA B C     1 
ATOM   3608 O  O     . ALA B 2 243 ? 19.442  -28.3   -37.169 1   105.23 ? 559 ALA B O     1 
ATOM   3609 C  CB    . ALA B 2 243 ? 21.519  -26.155 -35.78  1   103.95 ? 559 ALA B CB    1 
ATOM   3610 N  N     . PRO B 2 244 ? 21.442  -28.223 -38.212 1   105.43 ? 560 PRO B N     1 
ATOM   3611 C  CA    . PRO B 2 244 ? 21.313  -29.617 -38.666 1   105.61 ? 560 PRO B CA    1 
ATOM   3612 C  C     . PRO B 2 244 ? 21.267  -30.615 -37.524 1   105.78 ? 560 PRO B C     1 
ATOM   3613 O  O     . PRO B 2 244 ? 21.945  -30.447 -36.516 1   105.87 ? 560 PRO B O     1 
ATOM   3614 C  CB    . PRO B 2 244 ? 22.543  -29.834 -39.559 1   106.27 ? 560 PRO B CB    1 
ATOM   3615 C  CG    . PRO B 2 244 ? 23.51   -28.816 -39.136 1   106.72 ? 560 PRO B CG    1 
ATOM   3616 C  CD    . PRO B 2 244 ? 22.708  -27.625 -38.679 1   105.12 ? 560 PRO B CD    1 
ATOM   3617 N  N     . TYR B 2 245 ? 20.396  -31.61  -37.674 1   105.64 ? 561 TYR B N     1 
ATOM   3618 C  CA    . TYR B 2 245 ? 20.151  -32.711 -36.749 1   106    ? 561 TYR B CA    1 
ATOM   3619 C  C     . TYR B 2 245 ? 19.463  -32.277 -35.438 1   104.91 ? 561 TYR B C     1 
ATOM   3620 O  O     . TYR B 2 245 ? 19.341  -33.095 -34.525 1   105.08 ? 561 TYR B O     1 
ATOM   3621 C  CB    . TYR B 2 245 ? 21.429  -33.521 -36.509 1   107.01 ? 561 TYR B CB    1 
ATOM   3622 C  CG    . TYR B 2 245 ? 21.989  -34.028 -37.82  1   109.1  ? 561 TYR B CG    1 
ATOM   3623 C  CD1   . TYR B 2 245 ? 21.279  -34.934 -38.594 1   110.7  ? 561 TYR B CD1   1 
ATOM   3624 C  CD2   . TYR B 2 245 ? 23.162  -33.505 -38.347 1   110.62 ? 561 TYR B CD2   1 
ATOM   3625 C  CE1   . TYR B 2 245 ? 21.757  -35.366 -39.826 1   112.03 ? 561 TYR B CE1   1 
ATOM   3626 C  CE2   . TYR B 2 245 ? 23.65   -33.922 -39.582 1   111.95 ? 561 TYR B CE2   1 
ATOM   3627 C  CZ    . TYR B 2 245 ? 22.944  -34.857 -40.321 1   113.14 ? 561 TYR B CZ    1 
ATOM   3628 O  OH    . TYR B 2 245 ? 23.41   -35.292 -41.544 1   114.84 ? 561 TYR B OH    1 
ATOM   3629 N  N     . SER B 2 246 ? 18.941  -31.036 -35.371 1   103.54 ? 562 SER B N     1 
ATOM   3630 C  CA    . SER B 2 246 ? 18.208  -30.592 -34.195 1   102.63 ? 562 SER B CA    1 
ATOM   3631 C  C     . SER B 2 246 ? 16.806  -31.184 -34.253 1   101.6  ? 562 SER B C     1 
ATOM   3632 O  O     . SER B 2 246 ? 16.171  -31.166 -35.306 1   101.57 ? 562 SER B O     1 
ATOM   3633 C  CB    . SER B 2 246 ? 18.138  -29.073 -34.133 1   103.69 ? 562 SER B CB    1 
ATOM   3634 O  OG    . SER B 2 246 ? 17.397  -28.565 -35.228 1   105.97 ? 562 SER B OG    1 
ATOM   3635 N  N     . LYS B 2 247 ? 16.342  -31.751 -33.141 1   100.61 ? 563 LYS B N     1 
ATOM   3636 C  CA    . LYS B 2 247 ? 15.029  -32.383 -33.091 1   100.13 ? 563 LYS B CA    1 
ATOM   3637 C  C     . LYS B 2 247 ? 14.174  -31.788 -31.987 1   99.09  ? 563 LYS B C     1 
ATOM   3638 O  O     . LYS B 2 247 ? 14.684  -31.511 -30.913 1   99.21  ? 563 LYS B O     1 
ATOM   3639 C  CB    . LYS B 2 247 ? 15.177  -33.896 -32.851 1   102.12 ? 563 LYS B CB    1 
ATOM   3640 C  CG    . LYS B 2 247 ? 16.012  -34.631 -33.886 1   106.45 ? 563 LYS B CG    1 
ATOM   3641 C  CD    . LYS B 2 247 ? 15.395  -34.551 -35.267 1   111.41 ? 563 LYS B CD    1 
ATOM   3642 C  CE    . LYS B 2 247 ? 16.015  -35.541 -36.216 1   115.48 ? 563 LYS B CE    1 
ATOM   3643 N  NZ    . LYS B 2 247 ? 15.536  -36.932 -35.952 1   117.69 ? 563 LYS B NZ    1 
ATOM   3644 N  N     . GLY B 2 248 ? 12.881  -31.648 -32.231 1   98.03  ? 564 GLY B N     1 
ATOM   3645 C  CA    . GLY B 2 248 ? 11.966  -31.128 -31.227 1   97.68  ? 564 GLY B CA    1 
ATOM   3646 C  C     . GLY B 2 248 ? 10.604  -31.79  -31.245 1   97.14  ? 564 GLY B C     1 
ATOM   3647 O  O     . GLY B 2 248 ? 10.149  -32.243 -32.294 1   97.15  ? 564 GLY B O     1 
ATOM   3648 N  N     . HIS B 2 249 ? 9.944   -31.864 -30.087 1   96.65  ? 565 HIS B N     1 
ATOM   3649 C  CA    . HIS B 2 249 ? 8.602   -32.428 -30.009 1   96.79  ? 565 HIS B CA    1 
ATOM   3650 C  C     . HIS B 2 249 ? 7.778   -31.738 -28.975 1   96.2   ? 565 HIS B C     1 
ATOM   3651 O  O     . HIS B 2 249 ? 8.18    -31.656 -27.823 1   96     ? 565 HIS B O     1 
ATOM   3652 C  CB    . HIS B 2 249 ? 8.586   -33.936 -29.761 1   98.36  ? 565 HIS B CB    1 
ATOM   3653 C  CG    . HIS B 2 249 ? 7.203   -34.538 -29.81  1   101.96 ? 565 HIS B CG    1 
ATOM   3654 N  ND1   . HIS B 2 249 ? 6.512   -34.665 -31.005 1   104.26 ? 565 HIS B ND1   1 
ATOM   3655 C  CD2   . HIS B 2 249 ? 6.44    -35.052 -28.813 1   103.34 ? 565 HIS B CD2   1 
ATOM   3656 C  CE1   . HIS B 2 249 ? 5.358   -35.243 -30.699 1   104.78 ? 565 HIS B CE1   1 
ATOM   3657 N  NE2   . HIS B 2 249 ? 5.271   -35.501 -29.394 1   104.5  ? 565 HIS B NE2   1 
ATOM   3658 N  N     . ILE B 2 250 ? 6.613   -31.247 -29.386 1   96.02  ? 566 ILE B N     1 
ATOM   3659 C  CA    . ILE B 2 250 ? 5.674   -30.593 -28.489 1   96.41  ? 566 ILE B CA    1 
ATOM   3660 C  C     . ILE B 2 250 ? 4.527   -31.584 -28.285 1   96.96  ? 566 ILE B C     1 
ATOM   3661 O  O     . ILE B 2 250 ? 3.978   -32.113 -29.246 1   96.95  ? 566 ILE B O     1 
ATOM   3662 C  CB    . ILE B 2 250 ? 5.156   -29.211 -29.019 1   96.68  ? 566 ILE B CB    1 
ATOM   3663 C  CG1   . ILE B 2 250 ? 6.293   -28.259 -29.471 1   97.63  ? 566 ILE B CG1   1 
ATOM   3664 C  CG2   . ILE B 2 250 ? 4.241   -28.531 -27.999 1   96.9   ? 566 ILE B CG2   1 
ATOM   3665 C  CD1   . ILE B 2 250 ? 5.827   -27.03  -30.417 1   98.85  ? 566 ILE B CD1   1 
ATOM   3666 N  N     . ASP B 2 251 ? 4.211   -31.882 -27.037 1   97.26  ? 567 ASP B N     1 
ATOM   3667 C  CA    . ASP B 2 251 ? 3.129   -32.788 -26.711 1   97.96  ? 567 ASP B CA    1 
ATOM   3668 C  C     . ASP B 2 251 ? 2.208   -32.013 -25.81  1   98.39  ? 567 ASP B C     1 
ATOM   3669 O  O     . ASP B 2 251 ? 2.62    -31.653 -24.715 1   98.93  ? 567 ASP B O     1 
ATOM   3670 C  CB    . ASP B 2 251 ? 3.68    -34.006 -25.986 1   99.91  ? 567 ASP B CB    1 
ATOM   3671 C  CG    . ASP B 2 251 ? 2.714   -35.154 -26.028 1   105.96 ? 567 ASP B CG    1 
ATOM   3672 O  OD1   . ASP B 2 251 ? 1.496   -34.906 -25.887 1   106.44 ? 567 ASP B OD1   1 
ATOM   3673 O  OD2   . ASP B 2 251 ? 3.172   -36.312 -26.194 1   109.57 ? 567 ASP B OD2   1 
ATOM   3674 N  N     . CYS B 2 252 ? 0.988   -31.715 -26.264 1   97.98  ? 568 CYS B N     1 
ATOM   3675 C  CA    . CYS B 2 252 ? 0.065   -30.931 -25.464 1   98.09  ? 568 CYS B CA    1 
ATOM   3676 C  C     . CYS B 2 252 ? -1.25   -31.647 -25.246 1   98.05  ? 568 CYS B C     1 
ATOM   3677 O  O     . CYS B 2 252 ? -1.782  -32.234 -26.174 1   98.29  ? 568 CYS B O     1 
ATOM   3678 C  CB    . CYS B 2 252 ? -0.14   -29.555 -26.079 1   98.79  ? 568 CYS B CB    1 
ATOM   3679 S  SG    . CYS B 2 252 ? -1.017  -28.404 -25.001 1   103.32 ? 568 CYS B SG    1 
ATOM   3680 N  N     . ALA B 2 253 ? -1.774  -31.613 -24.025 1   97.67  ? 569 ALA B N     1 
ATOM   3681 C  CA    . ALA B 2 253 ? -3.035  -32.26  -23.718 1   97.86  ? 569 ALA B CA    1 
ATOM   3682 C  C     . ALA B 2 253 ? -3.737  -31.476 -22.648 1   97.78  ? 569 ALA B C     1 
ATOM   3683 O  O     . ALA B 2 253 ? -3.161  -31.269 -21.589 1   97.8   ? 569 ALA B O     1 
ATOM   3684 C  CB    . ALA B 2 253 ? -2.782  -33.671 -23.245 1   98.3   ? 569 ALA B CB    1 
ATOM   3685 N  N     . GLU B 2 254 ? -4.961  -31.027 -22.91  1   97.76  ? 570 GLU B N     1 
ATOM   3686 C  CA    . GLU B 2 254 ? -5.696  -30.235 -21.941 1   98.58  ? 570 GLU B CA    1 
ATOM   3687 C  C     . GLU B 2 254 ? -7.163  -30.6   -21.932 1   99.1   ? 570 GLU B C     1 
ATOM   3688 O  O     . GLU B 2 254 ? -7.828  -30.468 -22.949 1   99.27  ? 570 GLU B O     1 
ATOM   3689 C  CB    . GLU B 2 254 ? -5.523  -28.745 -22.249 1   101.22 ? 570 GLU B CB    1 
ATOM   3690 C  CG    . GLU B 2 254 ? -6.109  -27.826 -21.19  1   107.34 ? 570 GLU B CG    1 
ATOM   3691 C  CD    . GLU B 2 254 ? -5.223  -27.576 -19.978 1   115.29 ? 570 GLU B CD    1 
ATOM   3692 O  OE1   . GLU B 2 254 ? -4.025  -27.939 -20.037 1   117.03 ? 570 GLU B OE1   1 
ATOM   3693 O  OE2   . GLU B 2 254 ? -5.715  -26.998 -18.979 1   117.5  ? 570 GLU B OE2   1 
ATOM   3694 N  N     . ILE B 2 255 ? -7.677  -31.046 -20.792 1   99.43  ? 571 ILE B N     1 
ATOM   3695 C  CA    . ILE B 2 255 ? -9.086  -31.404 -20.671 1   100.48 ? 571 ILE B CA    1 
ATOM   3696 C  C     . ILE B 2 255 ? -9.928  -30.164 -20.389 1   101.37 ? 571 ILE B C     1 
ATOM   3697 O  O     . ILE B 2 255 ? -9.507  -29.288 -19.641 1   101.44 ? 571 ILE B O     1 
ATOM   3698 C  CB    . ILE B 2 255 ? -9.281  -32.502 -19.598 1   101.31 ? 571 ILE B CB    1 
ATOM   3699 C  CG1   . ILE B 2 255 ? -8.457  -33.744 -19.955 1   102.61 ? 571 ILE B CG1   1 
ATOM   3700 C  CG2   . ILE B 2 255 ? -10.766 -32.857 -19.389 1   101.77 ? 571 ILE B CG2   1 
ATOM   3701 C  CD1   . ILE B 2 255 ? -8.384  -34.77  -18.887 1   104.04 ? 571 ILE B CD1   1 
ATOM   3702 N  N     . VAL B 2 256 ? -11.105 -30.078 -21.018 1   101.86 ? 572 VAL B N     1 
ATOM   3703 C  CA    . VAL B 2 256 ? -12.05  -28.98  -20.832 1   102.74 ? 572 VAL B CA    1 
ATOM   3704 C  C     . VAL B 2 256 ? -13.349 -29.499 -20.211 1   103.82 ? 572 VAL B C     1 
ATOM   3705 O  O     . VAL B 2 256 ? -13.986 -30.412 -20.754 1   104.19 ? 572 VAL B O     1 
ATOM   3706 C  CB    . VAL B 2 256 ? -12.352 -28.247 -22.156 1   103.05 ? 572 VAL B CB    1 
ATOM   3707 C  CG1   . VAL B 2 256 ? -13.398 -27.157 -21.953 1   103.37 ? 572 VAL B CG1   1 
ATOM   3708 C  CG2   . VAL B 2 256 ? -11.081 -27.68  -22.762 1   103.52 ? 572 VAL B CG2   1 
ATOM   3709 N  N     . LYS B 2 257 ? -13.733 -28.918 -19.066 1   103.96 ? 573 LYS B N     1 
ATOM   3710 C  CA    . LYS B 2 257 ? -14.982 -29.23  -18.386 1   104.35 ? 573 LYS B CA    1 
ATOM   3711 C  C     . LYS B 2 257 ? -15.682 -27.946 -17.954 1   104.68 ? 573 LYS B C     1 
ATOM   3712 O  O     . LYS B 2 257 ? -15.027 -26.931 -17.727 1   104.98 ? 573 LYS B O     1 
ATOM   3713 C  CB    . LYS B 2 257 ? -14.779 -30.202 -17.225 1   106.08 ? 573 LYS B CB    1 
ATOM   3714 C  CG    . LYS B 2 257 ? -15.376 -31.568 -17.552 1   110.59 ? 573 LYS B CG    1 
ATOM   3715 C  CD    . LYS B 2 257 ? -16.909 -31.517 -17.544 1   115.18 ? 573 LYS B CD    1 
ATOM   3716 C  CE    . LYS B 2 257 ? -17.592 -32.533 -18.424 1   118.73 ? 573 LYS B CE    1 
ATOM   3717 N  NZ    . LYS B 2 257 ? -19.074 -32.429 -18.307 1   120.86 ? 573 LYS B NZ    1 
ATOM   3718 N  N     . GLY B 2 258 ? -17.004 -27.982 -17.884 1   104.55 ? 574 GLY B N     1 
ATOM   3719 C  CA    . GLY B 2 258 ? -17.79  -26.811 -17.528 1   104.91 ? 574 GLY B CA    1 
ATOM   3720 C  C     . GLY B 2 258 ? -17.698 -25.725 -18.579 1   104.89 ? 574 GLY B C     1 
ATOM   3721 O  O     . GLY B 2 258 ? -17.712 -26.011 -19.776 1   105    ? 574 GLY B O     1 
ATOM   3722 N  N     . ASN B 2 259 ? -17.573 -24.473 -18.141 1   104.6  ? 575 ASN B N     1 
ATOM   3723 C  CA    . ASN B 2 259 ? -17.494 -23.333 -19.059 1   104.84 ? 575 ASN B CA    1 
ATOM   3724 C  C     . ASN B 2 259 ? -16.039 -22.888 -19.315 1   104.1  ? 575 ASN B C     1 
ATOM   3725 O  O     . ASN B 2 259 ? -15.811 -21.724 -19.664 1   104.44 ? 575 ASN B O     1 
ATOM   3726 C  CB    . ASN B 2 259 ? -18.307 -22.12  -18.55  1   106.73 ? 575 ASN B CB    1 
ATOM   3727 C  CG    . ASN B 2 259 ? -19.485 -22.381 -17.627 1   110.7  ? 575 ASN B CG    1 
ATOM   3728 O  OD1   . ASN B 2 259 ? -20.032 -23.491 -17.535 1   112.34 ? 575 ASN B OD1   1 
ATOM   3729 N  ND2   . ASN B 2 259 ? -19.917 -21.336 -16.934 1   111.24 ? 575 ASN B ND2   1 
ATOM   3730 N  N     . ALA B 2 260 ? -15.062 -23.79  -19.127 1   102.84 ? 576 ALA B N     1 
ATOM   3731 C  CA    . ALA B 2 260 ? -13.664 -23.444 -19.323 1   102.21 ? 576 ALA B CA    1 
ATOM   3732 C  C     . ALA B 2 260 ? -13.348 -23.174 -20.783 1   101.61 ? 576 ALA B C     1 
ATOM   3733 O  O     . ALA B 2 260 ? -13.989 -23.718 -21.68  1   101.56 ? 576 ALA B O     1 
ATOM   3734 C  CB    . ALA B 2 260 ? -12.771 -24.546 -18.795 1   102.23 ? 576 ALA B CB    1 
ATOM   3735 N  N     . GLU B 2 261 ? -12.376 -22.303 -21.021 1   101.05 ? 577 GLU B N     1 
ATOM   3736 C  CA    . GLU B 2 261 ? -11.954 -21.968 -22.372 1   100.91 ? 577 GLU B CA    1 
ATOM   3737 C  C     . GLU B 2 261 ? -10.457 -22.248 -22.488 1   100.34 ? 577 GLU B C     1 
ATOM   3738 O  O     . GLU B 2 261 ? -9.692  -21.861 -21.607 1   100.5  ? 577 GLU B O     1 
ATOM   3739 C  CB    . GLU B 2 261 ? -12.245 -20.485 -22.683 1   103.14 ? 577 GLU B CB    1 
ATOM   3740 C  CG    . GLU B 2 261 ? -12.024 -20.102 -24.143 1   107.27 ? 577 GLU B CG    1 
ATOM   3741 C  CD    . GLU B 2 261 ? -11.042 -18.978 -24.433 1   111.84 ? 577 GLU B CD    1 
ATOM   3742 O  OE1   . GLU B 2 261 ? -9.824  -19.176 -24.221 1   112.28 ? 577 GLU B OE1   1 
ATOM   3743 O  OE2   . GLU B 2 261 ? -11.491 -17.908 -24.905 1   113.82 ? 577 GLU B OE2   1 
ATOM   3744 N  N     . VAL B 2 262 ? -10.039 -22.945 -23.55  1   99.44  ? 578 VAL B N     1 
ATOM   3745 C  CA    . VAL B 2 262 ? -8.63   -23.247 -23.762 1   99.12  ? 578 VAL B CA    1 
ATOM   3746 C  C     . VAL B 2 262 ? -8.188  -22.817 -25.155 1   99.14  ? 578 VAL B C     1 
ATOM   3747 O  O     . VAL B 2 262 ? -8.917  -22.995 -26.13  1   99.22  ? 578 VAL B O     1 
ATOM   3748 C  CB    . VAL B 2 262 ? -8.336  -24.739 -23.528 1   99.53  ? 578 VAL B CB    1 
ATOM   3749 C  CG1   . VAL B 2 262 ? -6.894  -25.079 -23.876 1   100.01 ? 578 VAL B CG1   1 
ATOM   3750 C  CG2   . VAL B 2 262 ? -8.645  -25.136 -22.098 1   100    ? 578 VAL B CG2   1 
ATOM   3751 N  N     . GLU B 2 263 ? -6.992  -22.253 -25.247 1   98.99  ? 579 GLU B N     1 
ATOM   3752 C  CA    . GLU B 2 263 ? -6.427  -21.852 -26.515 1   99.41  ? 579 GLU B CA    1 
ATOM   3753 C  C     . GLU B 2 263 ? -5.014  -22.388 -26.596 1   99.65  ? 579 GLU B C     1 
ATOM   3754 O  O     . GLU B 2 263 ? -4.195  -22.074 -25.745 1   99.71  ? 579 GLU B O     1 
ATOM   3755 C  CB    . GLU B 2 263 ? -6.426  -20.337 -26.635 1   101.77 ? 579 GLU B CB    1 
ATOM   3756 C  CG    . GLU B 2 263 ? -5.924  -19.873 -27.98  1   106.94 ? 579 GLU B CG    1 
ATOM   3757 C  CD    . GLU B 2 263 ? -6.176  -18.402 -28.229 1   114    ? 579 GLU B CD    1 
ATOM   3758 O  OE1   . GLU B 2 263 ? -7.038  -18.085 -29.081 1   115.05 ? 579 GLU B OE1   1 
ATOM   3759 O  OE2   . GLU B 2 263 ? -5.526  -17.564 -27.561 1   116.83 ? 579 GLU B OE2   1 
ATOM   3760 N  N     . SER B 2 264 ? -4.733  -23.228 -27.586 1   99.81  ? 580 SER B N     1 
ATOM   3761 C  CA    . SER B 2 264 ? -3.407  -23.81  -27.747 1   100.61 ? 580 SER B CA    1 
ATOM   3762 C  C     . SER B 2 264 ? -2.773  -23.308 -29.038 1   101.05 ? 580 SER B C     1 
ATOM   3763 O  O     . SER B 2 264 ? -3.345  -23.439 -30.117 1   101.01 ? 580 SER B O     1 
ATOM   3764 C  CB    . SER B 2 264 ? -3.481  -25.335 -27.732 1   102.41 ? 580 SER B CB    1 
ATOM   3765 O  OG    . SER B 2 264 ? -2.188  -25.915 -27.8   1   104.99 ? 580 SER B OG    1 
ATOM   3766 N  N     . ILE B 2 265 ? -1.613  -22.679 -28.923 1   101.38 ? 581 ILE B N     1 
ATOM   3767 C  CA    . ILE B 2 265 ? -0.9    -22.131 -30.077 1   102.18 ? 581 ILE B CA    1 
ATOM   3768 C  C     . ILE B 2 265 ? 0.531   -22.688 -30.144 1   102.92 ? 581 ILE B C     1 
ATOM   3769 O  O     . ILE B 2 265 ? 1.484   -22.076 -29.656 1   103.19 ? 581 ILE B O     1 
ATOM   3770 C  CB    . ILE B 2 265 ? -0.91   -20.584 -30.113 1   102.54 ? 581 ILE B CB    1 
ATOM   3771 C  CG1   . ILE B 2 265 ? -2.29   -19.994 -29.765 1   103.45 ? 581 ILE B CG1   1 
ATOM   3772 C  CG2   . ILE B 2 265 ? -0.441  -20.1   -31.467 1   102.92 ? 581 ILE B CG2   1 
ATOM   3773 C  CD1   . ILE B 2 265 ? -2.43   -19.537 -28.32  1   104.76 ? 581 ILE B CD1   1 
ATOM   3774 N  N     . PRO B 2 266 ? 0.693   -23.862 -30.761 1   103.03 ? 582 PRO B N     1 
ATOM   3775 C  CA    . PRO B 2 266 ? 2.023   -24.482 -30.819 1   102.99 ? 582 PRO B CA    1 
ATOM   3776 C  C     . PRO B 2 266 ? 2.795   -24.182 -32.107 1   102.49 ? 582 PRO B C     1 
ATOM   3777 O  O     . PRO B 2 266 ? 2.635   -24.901 -33.092 1   103.08 ? 582 PRO B O     1 
ATOM   3778 C  CB    . PRO B 2 266 ? 1.703   -25.971 -30.699 1   104.02 ? 582 PRO B CB    1 
ATOM   3779 C  CG    . PRO B 2 266 ? 0.289   -26.103 -31.245 1   104.52 ? 582 PRO B CG    1 
ATOM   3780 C  CD    . PRO B 2 266 ? -0.338  -24.743 -31.343 1   102.85 ? 582 PRO B CD    1 
ATOM   3781 N  N     . ILE B 2 267 ? 3.667   -23.174 -32.083 1   101.14 ? 583 ILE B N     1 
ATOM   3782 C  CA    . ILE B 2 267 ? 4.441   -22.757 -33.257 1   100.43 ? 583 ILE B CA    1 
ATOM   3783 C  C     . ILE B 2 267 ? 5.684   -23.611 -33.54  1   99.46  ? 583 ILE B C     1 
ATOM   3784 O  O     . ILE B 2 267 ? 6.464   -23.903 -32.637 1   99.73  ? 583 ILE B O     1 
ATOM   3785 C  CB    . ILE B 2 267 ? 4.833   -21.27  -33.169 1   101.08 ? 583 ILE B CB    1 
ATOM   3786 C  CG1   . ILE B 2 267 ? 3.692   -20.38  -32.653 1   102.16 ? 583 ILE B CG1   1 
ATOM   3787 C  CG2   . ILE B 2 267 ? 5.383   -20.768 -34.495 1   101.65 ? 583 ILE B CG2   1 
ATOM   3788 C  CD1   . ILE B 2 267 ? 3.866   -20.062 -31.16  1   103.44 ? 583 ILE B CD1   1 
ATOM   3789 N  N     . VAL B 2 268 ? 5.886   -23.99  -34.802 1   98.26  ? 584 VAL B N     1 
ATOM   3790 C  CA    . VAL B 2 268 ? 7.051   -24.775 -35.19  1   97.57  ? 584 VAL B CA    1 
ATOM   3791 C  C     . VAL B 2 268 ? 7.759   -24.061 -36.338 1   96.4   ? 584 VAL B C     1 
ATOM   3792 O  O     . VAL B 2 268 ? 7.156   -23.839 -37.384 1   96.37  ? 584 VAL B O     1 
ATOM   3793 C  CB    . VAL B 2 268 ? 6.662   -26.238 -35.551 1   98.5   ? 584 VAL B CB    1 
ATOM   3794 C  CG1   . VAL B 2 268 ? 7.778   -26.938 -36.317 1   99.16  ? 584 VAL B CG1   1 
ATOM   3795 C  CG2   . VAL B 2 268 ? 6.275   -27.043 -34.307 1   99.01  ? 584 VAL B CG2   1 
ATOM   3796 N  N     . VAL B 2 269 ? 9.024   -23.677 -36.141 1   95.41  ? 585 VAL B N     1 
ATOM   3797 C  CA    . VAL B 2 269 ? 9.799   -23.03  -37.198 1   95.06  ? 585 VAL B CA    1 
ATOM   3798 C  C     . VAL B 2 269 ? 10.978  -23.914 -37.557 1   95.18  ? 585 VAL B C     1 
ATOM   3799 O  O     . VAL B 2 269 ? 11.679  -24.346 -36.66  1   95.43  ? 585 VAL B O     1 
ATOM   3800 C  CB    . VAL B 2 269 ? 10.313  -21.656 -36.766 1   95.25  ? 585 VAL B CB    1 
ATOM   3801 C  CG1   . VAL B 2 269 ? 11.079  -21.003 -37.903 1   95.6   ? 585 VAL B CG1   1 
ATOM   3802 C  CG2   . VAL B 2 269 ? 9.172   -20.768 -36.297 1   95.7   ? 585 VAL B CG2   1 
ATOM   3803 N  N     . VAL B 2 270 ? 11.206  -24.198 -38.843 1   94.88  ? 586 VAL B N     1 
ATOM   3804 C  CA    . VAL B 2 270 ? 12.337  -25.031 -39.251 1   95.16  ? 586 VAL B CA    1 
ATOM   3805 C  C     . VAL B 2 270 ? 13.185  -24.281 -40.283 1   95.55  ? 586 VAL B C     1 
ATOM   3806 O  O     . VAL B 2 270 ? 12.679  -23.886 -41.335 1   95.49  ? 586 VAL B O     1 
ATOM   3807 C  CB    . VAL B 2 270 ? 11.883  -26.432 -39.732 1   95.88  ? 586 VAL B CB    1 
ATOM   3808 C  CG1   . VAL B 2 270 ? 13.001  -27.16  -40.463 1   96.55  ? 586 VAL B CG1   1 
ATOM   3809 C  CG2   . VAL B 2 270 ? 11.385  -27.277 -38.57  1   96.29  ? 586 VAL B CG2   1 
ATOM   3810 N  N     . ARG B 2 271 ? 14.47   -24.051 -39.961 1   95.79  ? 587 ARG B N     1 
ATOM   3811 C  CA    . ARG B 2 271 ? 15.403  -23.314 -40.818 1   96.43  ? 587 ARG B CA    1 
ATOM   3812 C  C     . ARG B 2 271 ? 16.621  -24.136 -41.284 1   96.83  ? 587 ARG B C     1 
ATOM   3813 O  O     . ARG B 2 271 ? 17.631  -23.565 -41.7   1   96.99  ? 587 ARG B O     1 
ATOM   3814 C  CB    . ARG B 2 271 ? 15.853  -22.02  -40.125 1   97.75  ? 587 ARG B CB    1 
ATOM   3815 C  CG    . ARG B 2 271 ? 14.689  -21.136 -39.695 1   100.81 ? 587 ARG B CG    1 
ATOM   3816 C  CD    . ARG B 2 271 ? 15.157  -19.751 -39.345 1   104.37 ? 587 ARG B CD    1 
ATOM   3817 N  NE    . ARG B 2 271 ? 14.042  -18.852 -39.053 1   107.87 ? 587 ARG B NE    1 
ATOM   3818 C  CZ    . ARG B 2 271 ? 13.649  -18.518 -37.828 1   110.97 ? 587 ARG B CZ    1 
ATOM   3819 N  NH1   . ARG B 2 271 ? 14.262  -19.026 -36.764 1   111.13 ? 587 ARG B NH1   1 
ATOM   3820 N  NH2   . ARG B 2 271 ? 12.634  -17.681 -37.655 1   111.24 ? 587 ARG B NH2   1 
ATOM   3821 N  N     . ASP B 2 272 ? 16.516  -25.475 -41.227 1   96.76  ? 588 ASP B N     1 
ATOM   3822 C  CA    . ASP B 2 272 ? 17.559  -26.391 -41.69  1   96.91  ? 588 ASP B CA    1 
ATOM   3823 C  C     . ASP B 2 272 ? 16.928  -27.642 -42.333 1   96.49  ? 588 ASP B C     1 
ATOM   3824 O  O     . ASP B 2 272 ? 15.943  -28.161 -41.81  1   96.64  ? 588 ASP B O     1 
ATOM   3825 C  CB    . ASP B 2 272 ? 18.523  -26.782 -40.563 1   98.66  ? 588 ASP B CB    1 
ATOM   3826 C  CG    . ASP B 2 272 ? 19.808  -27.361 -41.119 1   103.29 ? 588 ASP B CG    1 
ATOM   3827 O  OD1   . ASP B 2 272 ? 20.757  -26.582 -41.35  1   104.38 ? 588 ASP B OD1   1 
ATOM   3828 O  OD2   . ASP B 2 272 ? 19.848  -28.585 -41.375 1   105.02 ? 588 ASP B OD2   1 
ATOM   3829 N  N     . ASP B 2 273 ? 17.494  -28.132 -43.459 1   95.71  ? 589 ASP B N     1 
ATOM   3830 C  CA    . ASP B 2 273 ? 16.951  -29.318 -44.138 1   95.36  ? 589 ASP B CA    1 
ATOM   3831 C  C     . ASP B 2 273 ? 17.197  -30.634 -43.399 1   94.53  ? 589 ASP B C     1 
ATOM   3832 O  O     . ASP B 2 273 ? 16.592  -31.639 -43.761 1   94.59  ? 589 ASP B O     1 
ATOM   3833 C  CB    . ASP B 2 273 ? 17.418  -29.431 -45.602 1   97.15  ? 589 ASP B CB    1 
ATOM   3834 C  CG    . ASP B 2 273 ? 18.913  -29.569 -45.844 1   101.4  ? 589 ASP B CG    1 
ATOM   3835 O  OD1   . ASP B 2 273 ? 19.692  -29.409 -44.878 1   101.94 ? 589 ASP B OD1   1 
ATOM   3836 O  OD2   . ASP B 2 273 ? 19.304  -29.809 -47.007 1   103.45 ? 589 ASP B OD2   1 
ATOM   3837 N  N     . LYS B 2 274 ? 18.087  -30.632 -42.383 1   93.55  ? 590 LYS B N     1 
ATOM   3838 C  CA    . LYS B 2 274 ? 18.384  -31.8   -41.551 1   92.92  ? 590 LYS B CA    1 
ATOM   3839 C  C     . LYS B 2 274 ? 17.777  -31.696 -40.137 1   91.98  ? 590 LYS B C     1 
ATOM   3840 O  O     . LYS B 2 274 ? 18.141  -32.484 -39.272 1   92.02  ? 590 LYS B O     1 
ATOM   3841 C  CB    . LYS B 2 274 ? 19.901  -32.058 -41.464 1   94.77  ? 590 LYS B CB    1 
ATOM   3842 C  CG    . LYS B 2 274 ? 20.544  -32.492 -42.782 1   99.02  ? 590 LYS B CG    1 
ATOM   3843 C  CD    . LYS B 2 274 ? 19.956  -33.797 -43.331 1   103.66 ? 590 LYS B CD    1 
ATOM   3844 C  CE    . LYS B 2 274 ? 20.235  -34.006 -44.802 1   107.3  ? 590 LYS B CE    1 
ATOM   3845 N  NZ    . LYS B 2 274 ? 19.424  -35.123 -45.361 1   109.26 ? 590 LYS B NZ    1 
ATOM   3846 N  N     . ALA B 2 275 ? 16.888  -30.715 -39.893 1   91.03  ? 591 ALA B N     1 
ATOM   3847 C  CA    . ALA B 2 275 ? 16.194  -30.495 -38.621 1   90.46  ? 591 ALA B CA    1 
ATOM   3848 C  C     . ALA B 2 275 ? 14.783  -31.081 -38.729 1   89.71  ? 591 ALA B C     1 
ATOM   3849 O  O     . ALA B 2 275 ? 14.209  -31.072 -39.82  1   90.01  ? 591 ALA B O     1 
ATOM   3850 C  CB    . ALA B 2 275 ? 16.099  -29.001 -38.345 1   90.48  ? 591 ALA B CB    1 
ATOM   3851 N  N     . ARG B 2 276 ? 14.218  -31.592 -37.62  1   88.49  ? 592 ARG B N     1 
ATOM   3852 C  CA    . ARG B 2 276 ? 12.864  -32.146 -37.66  1   87.83  ? 592 ARG B CA    1 
ATOM   3853 C  C     . ARG B 2 276 ? 12.128  -31.852 -36.388 1   86.77  ? 592 ARG B C     1 
ATOM   3854 O  O     . ARG B 2 276 ? 12.633  -32.146 -35.315 1   87.01  ? 592 ARG B O     1 
ATOM   3855 C  CB    . ARG B 2 276 ? 12.875  -33.657 -37.917 1   89.32  ? 592 ARG B CB    1 
ATOM   3856 C  CG    . ARG B 2 276 ? 11.48   -34.268 -38.036 1   92.67  ? 592 ARG B CG    1 
ATOM   3857 C  CD    . ARG B 2 276 ? 11.518  -35.738 -38.414 1   96.31  ? 592 ARG B CD    1 
ATOM   3858 N  NE    . ARG B 2 276 ? 10.522  -36.061 -39.436 1   99.72  ? 592 ARG B NE    1 
ATOM   3859 C  CZ    . ARG B 2 276 ? 9.369   -36.68  -39.198 1   102.47 ? 592 ARG B CZ    1 
ATOM   3860 N  NH1   . ARG B 2 276 ? 9.063   -37.077 -37.969 1   102.3  ? 592 ARG B NH1   1 
ATOM   3861 N  NH2   . ARG B 2 276 ? 8.522   -36.923 -40.192 1   102.68 ? 592 ARG B NH2   1 
ATOM   3862 N  N     . ILE B 2 277 ? 10.952  -31.242 -36.491 1   85.64  ? 593 ILE B N     1 
ATOM   3863 C  CA    . ILE B 2 277 ? 10.133  -30.945 -35.327 1   85.16  ? 593 ILE B CA    1 
ATOM   3864 C  C     . ILE B 2 277 ? 8.755   -31.494 -35.549 1   84.71  ? 593 ILE B C     1 
ATOM   3865 O  O     . ILE B 2 277 ? 8.203   -31.354 -36.634 1   84.99  ? 593 ILE B O     1 
ATOM   3866 C  CB    . ILE B 2 277 ? 10.053  -29.445 -35.018 1   85.46  ? 593 ILE B CB    1 
ATOM   3867 C  CG1   . ILE B 2 277 ? 11.437  -28.831 -34.908 1   86.55  ? 593 ILE B CG1   1 
ATOM   3868 C  CG2   . ILE B 2 277 ? 9.228   -29.193 -33.755 1   85.85  ? 593 ILE B CG2   1 
ATOM   3869 C  CD1   . ILE B 2 277 ? 11.402  -27.378 -34.89  1   88     ? 593 ILE B CD1   1 
ATOM   3870 N  N     . THR B 2 278 ? 8.204   -32.141 -34.538 1   83.87  ? 594 THR B N     1 
ATOM   3871 C  CA    . THR B 2 278 ? 6.854   -32.664 -34.6   1   83.68  ? 594 THR B CA    1 
ATOM   3872 C  C     . THR B 2 278 ? 6.061   -32.146 -33.414 1   83.75  ? 594 THR B C     1 
ATOM   3873 O  O     . THR B 2 278 ? 6.642   -31.784 -32.397 1   83.91  ? 594 THR B O     1 
ATOM   3874 C  CB    . THR B 2 278 ? 6.869   -34.182 -34.593 1   84.6   ? 594 THR B CB    1 
ATOM   3875 O  OG1   . THR B 2 278 ? 7.633   -34.625 -33.474 1   85.58  ? 594 THR B OG1   1 
ATOM   3876 C  CG2   . THR B 2 278 ? 7.433   -34.757 -35.863 1   84.89  ? 594 THR B CG2   1 
ATOM   3877 N  N     . HIS B 2 279 ? 4.741   -32.096 -33.542 1   83.63  ? 595 HIS B N     1 
ATOM   3878 C  CA    A HIS B 2 279 ? 3.878   -31.646 -32.459 0.5 84.16  ? 595 HIS B CA    1 
ATOM   3879 C  CA    B HIS B 2 279 ? 3.888   -31.676 -32.445 0.5 84.18  ? 595 HIS B CA    1 
ATOM   3880 C  C     . HIS B 2 279 ? 2.57    -32.412 -32.469 1   84.45  ? 595 HIS B C     1 
ATOM   3881 O  O     . HIS B 2 279 ? 2.022   -32.672 -33.528 1   84.76  ? 595 HIS B O     1 
ATOM   3882 C  CB    A HIS B 2 279 ? 3.616   -30.124 -32.521 0.5 85.21  ? 595 HIS B CB    1 
ATOM   3883 C  CB    B HIS B 2 279 ? 3.722   -30.138 -32.322 0.5 85.29  ? 595 HIS B CB    1 
ATOM   3884 C  CG    A HIS B 2 279 ? 2.502   -29.688 -31.619 0.5 87.72  ? 595 HIS B CG    1 
ATOM   3885 C  CG    B HIS B 2 279 ? 3.116   -29.409 -33.482 0.5 87.88  ? 595 HIS B CG    1 
ATOM   3886 N  ND1   A HIS B 2 279 ? 1.19    -29.679 -32.054 0.5 89.57  ? 595 HIS B ND1   1 
ATOM   3887 N  ND1   B HIS B 2 279 ? 1.768   -29.514 -33.778 0.5 89.8   ? 595 HIS B ND1   1 
ATOM   3888 C  CD2   A HIS B 2 279 ? 2.523   -29.409 -30.296 0.5 88.98  ? 595 HIS B CD2   1 
ATOM   3889 C  CD2   B HIS B 2 279 ? 3.661   -28.456 -34.275 0.5 89.04  ? 595 HIS B CD2   1 
ATOM   3890 C  CE1   A HIS B 2 279 ? 0.464   -29.363 -30.997 0.5 90.14  ? 595 HIS B CE1   1 
ATOM   3891 C  CE1   B HIS B 2 279 ? 1.561   -28.695 -34.797 0.5 90.32  ? 595 HIS B CE1   1 
ATOM   3892 N  NE2   A HIS B 2 279 ? 1.224   -29.182 -29.918 0.5 90.1   ? 595 HIS B NE2   1 
ATOM   3893 N  NE2   B HIS B 2 279 ? 2.67    -28.029 -35.125 0.5 90.15  ? 595 HIS B NE2   1 
ATOM   3894 N  N     . GLU B 2 280 ? 2.073   -32.753 -31.298 1   84.46  ? 596 GLU B N     1 
ATOM   3895 C  CA    . GLU B 2 280 ? 0.8     -33.428 -31.167 1   85.3   ? 596 GLU B CA    1 
ATOM   3896 C  C     . GLU B 2 280 ? 0.028   -32.753 -30.047 1   84.62  ? 596 GLU B C     1 
ATOM   3897 O  O     . GLU B 2 280 ? 0.616   -32.393 -29.03  1   84.55  ? 596 GLU B O     1 
ATOM   3898 C  CB    . GLU B 2 280 ? 0.969   -34.943 -30.939 1   89.78  ? 596 GLU B CB    1 
ATOM   3899 C  CG    . GLU B 2 280 ? 1.326   -35.37  -29.516 1   99.32  ? 596 GLU B CG    1 
ATOM   3900 C  CD    . GLU B 2 280 ? 0.388   -36.373 -28.843 1   110.98 ? 596 GLU B CD    1 
ATOM   3901 O  OE1   . GLU B 2 280 ? 0.553   -37.599 -29.064 1   113.78 ? 596 GLU B OE1   1 
ATOM   3902 O  OE2   . GLU B 2 280 ? -0.497  -35.932 -28.069 1   114.08 ? 596 GLU B OE2   1 
ATOM   3903 N  N     . ALA B 2 281 ? -1.266  -32.519 -30.251 1   84.13  ? 597 ALA B N     1 
ATOM   3904 C  CA    . ALA B 2 281 ? -2.093  -31.894 -29.233 1   84.36  ? 597 ALA B CA    1 
ATOM   3905 C  C     . ALA B 2 281 ? -3.504  -32.418 -29.23  1   84.68  ? 597 ALA B C     1 
ATOM   3906 O  O     . ALA B 2 281 ? -4.025  -32.83  -30.259 1   84.85  ? 597 ALA B O     1 
ATOM   3907 C  CB    . ALA B 2 281 ? -2.083  -30.385 -29.365 1   84.51  ? 597 ALA B CB    1 
ATOM   3908 N  N     . ALA B 2 282 ? -4.108  -32.439 -28.059 1   84.81  ? 598 ALA B N     1 
ATOM   3909 C  CA    . ALA B 2 282 ? -5.463  -32.905 -27.896 1   85.65  ? 598 ALA B CA    1 
ATOM   3910 C  C     . ALA B 2 282 ? -6.083  -32.004 -26.875 1   86.57  ? 598 ALA B C     1 
ATOM   3911 O  O     . ALA B 2 282 ? -5.628  -31.957 -25.739 1   86.7   ? 598 ALA B O     1 
ATOM   3912 C  CB    . ALA B 2 282 ? -5.453  -34.324 -27.392 1   85.99  ? 598 ALA B CB    1 
ATOM   3913 N  N     . ILE B 2 283 ? -7.053  -31.215 -27.295 1   87.31  ? 599 ILE B N     1 
ATOM   3914 C  CA    . ILE B 2 283 ? -7.709  -30.246 -26.434 1   88.8   ? 599 ILE B CA    1 
ATOM   3915 C  C     . ILE B 2 283 ? -9.198  -30.509 -26.461 1   90.26  ? 599 ILE B C     1 
ATOM   3916 O  O     . ILE B 2 283 ? -9.745  -30.842 -27.507 1   90.32  ? 599 ILE B O     1 
ATOM   3917 C  CB    . ILE B 2 283 ? -7.407  -28.814 -26.935 1   89.41  ? 599 ILE B CB    1 
ATOM   3918 C  CG1   . ILE B 2 283 ? -5.884  -28.569 -27.138 1   90.56  ? 599 ILE B CG1   1 
ATOM   3919 C  CG2   . ILE B 2 283 ? -8.054  -27.755 -26.049 1   89.79  ? 599 ILE B CG2   1 
ATOM   3920 C  CD1   . ILE B 2 283 ? -5.041  -28.464 -25.886 1   91.84  ? 599 ILE B CD1   1 
ATOM   3921 N  N     . GLY B 2 284 ? -9.845  -30.358 -25.318 1   91.32  ? 600 GLY B N     1 
ATOM   3922 C  CA    . GLY B 2 284 ? -11.28  -30.564 -25.223 1   92.76  ? 600 GLY B CA    1 
ATOM   3923 C  C     . GLY B 2 284 ? -11.657 -31.699 -24.302 1   94.03  ? 600 GLY B C     1 
ATOM   3924 O  O     . GLY B 2 284 ? -11.006 -31.918 -23.281 1   94.3   ? 600 GLY B O     1 
ATOM   3925 N  N     . SER B 2 285 ? -12.712 -32.416 -24.646 1   94.72  ? 601 SER B N     1 
ATOM   3926 C  CA    . SER B 2 285 ? -13.188 -33.524 -23.843 1   96.24  ? 601 SER B CA    1 
ATOM   3927 C  C     . SER B 2 285 ? -12.196 -34.704 -23.818 1   97.49  ? 601 SER B C     1 
ATOM   3928 O  O     . SER B 2 285 ? -11.315 -34.799 -24.672 1   97.56  ? 601 SER B O     1 
ATOM   3929 C  CB    . SER B 2 285 ? -14.529 -33.988 -24.387 1   98.14  ? 601 SER B CB    1 
ATOM   3930 O  OG    . SER B 2 285 ? -14.357 -34.508 -25.694 1   101.07 ? 601 SER B OG    1 
ATOM   3931 N  N     . VAL B 2 286 ? -12.345 -35.607 -22.835 1   98.32  ? 602 VAL B N     1 
ATOM   3932 C  CA    . VAL B 2 286 ? -11.49  -36.788 -22.708 1   99.38  ? 602 VAL B CA    1 
ATOM   3933 C  C     . VAL B 2 286 ? -11.68  -37.742 -23.9   1   100.65 ? 602 VAL B C     1 
ATOM   3934 O  O     . VAL B 2 286 ? -12.746 -37.75  -24.532 1   100.72 ? 602 VAL B O     1 
ATOM   3935 C  CB    . VAL B 2 286 ? -11.716 -37.506 -21.355 1   99.79  ? 602 VAL B CB    1 
ATOM   3936 C  CG1   . VAL B 2 286 ? -11.47  -36.555 -20.186 1   100.13 ? 602 VAL B CG1   1 
ATOM   3937 C  CG2   . VAL B 2 286 ? -13.119 -38.111 -21.278 1   100.24 ? 602 VAL B CG2   1 
ATOM   3938 N  N     . ASP B 2 287 ? -10.633 -38.525 -24.223 1   101.4  ? 603 ASP B N     1 
ATOM   3939 C  CA    . ASP B 2 287 ? -10.665 -39.488 -25.328 1   102.61 ? 603 ASP B CA    1 
ATOM   3940 C  C     . ASP B 2 287 ? -11.8   -40.497 -25.121 1   103.78 ? 603 ASP B C     1 
ATOM   3941 O  O     . ASP B 2 287 ? -11.993 -40.973 -24.005 1   104    ? 603 ASP B O     1 
ATOM   3942 C  CB    . ASP B 2 287 ? -9.305  -40.198 -25.457 1   104.22 ? 603 ASP B CB    1 
ATOM   3943 C  CG    . ASP B 2 287 ? -9.2    -41.138 -26.643 1   108.68 ? 603 ASP B CG    1 
ATOM   3944 O  OD1   . ASP B 2 287 ? -9.222  -40.647 -27.799 1   109    ? 603 ASP B OD1   1 
ATOM   3945 O  OD2   . ASP B 2 287 ? -9.087  -42.368 -26.417 1   111.08 ? 603 ASP B OD2   1 
ATOM   3946 N  N     . LYS B 2 288 ? -12.597 -40.75  -26.168 1   104.23 ? 604 LYS B N     1 
ATOM   3947 C  CA    . LYS B 2 288 ? -13.748 -41.649 -26.101 1   104.92 ? 604 LYS B CA    1 
ATOM   3948 C  C     . LYS B 2 288 ? -13.358 -43.072 -25.743 1   105.1  ? 604 LYS B C     1 
ATOM   3949 O  O     . LYS B 2 288 ? -14.039 -43.688 -24.94  1   105.01 ? 604 LYS B O     1 
ATOM   3950 C  CB    . LYS B 2 288 ? -14.538 -41.597 -27.418 1   107.45 ? 604 LYS B CB    1 
ATOM   3951 C  CG    . LYS B 2 288 ? -15.741 -42.521 -27.481 1   112.89 ? 604 LYS B CG    1 
ATOM   3952 C  CD    . LYS B 2 288 ? -16.426 -42.434 -28.845 1   118.66 ? 604 LYS B CD    1 
ATOM   3953 C  CE    . LYS B 2 288 ? -16.929 -43.774 -29.343 1   122.86 ? 604 LYS B CE    1 
ATOM   3954 N  NZ    . LYS B 2 288 ? -17.569 -43.654 -30.685 1   125.4  ? 604 LYS B NZ    1 
ATOM   3955 N  N     . LYS B 2 289 ? -12.254 -43.585 -26.296 1   105.49 ? 605 LYS B N     1 
ATOM   3956 C  CA    . LYS B 2 289 ? -11.81  -44.944 -25.995 1   106.55 ? 605 LYS B CA    1 
ATOM   3957 C  C     . LYS B 2 289 ? -11.339 -45.058 -24.557 1   107.59 ? 605 LYS B C     1 
ATOM   3958 O  O     . LYS B 2 289 ? -11.612 -46.064 -23.918 1   107.7  ? 605 LYS B O     1 
ATOM   3959 C  CB    . LYS B 2 289 ? -10.716 -45.398 -26.961 1   108.34 ? 605 LYS B CB    1 
ATOM   3960 C  CG    . LYS B 2 289 ? -10.427 -46.889 -26.914 1   112.09 ? 605 LYS B CG    1 
ATOM   3961 C  CD    . LYS B 2 289 ? -9.108  -47.188 -27.605 1   116.85 ? 605 LYS B CD    1 
ATOM   3962 C  CE    . LYS B 2 289 ? -8.88   -48.653 -27.86  1   121.44 ? 605 LYS B CE    1 
ATOM   3963 N  NZ    . LYS B 2 289 ? -9.82   -49.196 -28.895 1   124.08 ? 605 LYS B NZ    1 
ATOM   3964 N  N     . GLN B 2 290 ? -10.668 -44.028 -24.031 1   108.27 ? 606 GLN B N     1 
ATOM   3965 C  CA    . GLN B 2 290 ? -10.221 -44.032 -22.64  1   109.56 ? 606 GLN B CA    1 
ATOM   3966 C  C     . GLN B 2 290 ? -11.415 -44.027 -21.684 1   110.41 ? 606 GLN B C     1 
ATOM   3967 O  O     . GLN B 2 290 ? -11.418 -44.767 -20.703 1   110.8  ? 606 GLN B O     1 
ATOM   3968 C  CB    . GLN B 2 290 ? -9.358  -42.813 -22.353 1   111.67 ? 606 GLN B CB    1 
ATOM   3969 C  CG    . GLN B 2 290 ? -7.923  -42.976 -22.764 1   116.68 ? 606 GLN B CG    1 
ATOM   3970 C  CD    . GLN B 2 290 ? -7.193  -41.665 -22.619 1   123.86 ? 606 GLN B CD    1 
ATOM   3971 O  OE1   . GLN B 2 290 ? -7.452  -40.853 -21.714 1   125.99 ? 606 GLN B OE1   1 
ATOM   3972 N  NE2   . GLN B 2 290 ? -6.253  -41.428 -23.512 1   125.68 ? 606 GLN B NE2   1 
ATOM   3973 N  N     . LEU B 2 291 ? -12.431 -43.196 -21.976 1   110.51 ? 607 LEU B N     1 
ATOM   3974 C  CA    . LEU B 2 291 ? -13.649 -43.087 -21.176 1   110.9  ? 607 LEU B CA    1 
ATOM   3975 C  C     . LEU B 2 291 ? -14.402 -44.416 -21.207 1   111.04 ? 607 LEU B C     1 
ATOM   3976 O  O     . LEU B 2 291 ? -14.741 -44.939 -20.153 1   111.06 ? 607 LEU B O     1 
ATOM   3977 C  CB    . LEU B 2 291 ? -14.538 -41.952 -21.719 1   111.15 ? 607 LEU B CB    1 
ATOM   3978 C  CG    . LEU B 2 291 ? -15.865 -41.755 -20.998 1   112.52 ? 607 LEU B CG    1 
ATOM   3979 C  CD1   . LEU B 2 291 ? -15.647 -41.129 -19.65  1   113.12 ? 607 LEU B CD1   1 
ATOM   3980 C  CD2   . LEU B 2 291 ? -16.805 -40.895 -21.806 1   113.13 ? 607 LEU B CD2   1 
ATOM   3981 N  N     . GLU B 2 292 ? -14.594 -44.991 -22.408 1   111.06 ? 608 GLU B N     1 
ATOM   3982 C  CA    . GLU B 2 292 ? -15.29  -46.255 -22.589 1   111.71 ? 608 GLU B CA    1 
ATOM   3983 C  C     . GLU B 2 292 ? -14.552 -47.431 -21.997 1   112.6  ? 608 GLU B C     1 
ATOM   3984 O  O     . GLU B 2 292 ? -15.201 -48.392 -21.597 1   113.04 ? 608 GLU B O     1 
ATOM   3985 C  CB    . GLU B 2 292 ? -15.636 -46.49  -24.056 1   113.55 ? 608 GLU B CB    1 
ATOM   3986 C  CG    . GLU B 2 292 ? -16.603 -45.432 -24.544 1   118.54 ? 608 GLU B CG    1 
ATOM   3987 C  CD    . GLU B 2 292 ? -17.179 -45.642 -25.927 1   125.14 ? 608 GLU B CD    1 
ATOM   3988 O  OE1   . GLU B 2 292 ? -16.416 -46.041 -26.835 1   126.82 ? 608 GLU B OE1   1 
ATOM   3989 O  OE2   . GLU B 2 292 ? -18.388 -45.378 -26.111 1   127.04 ? 608 GLU B OE2   1 
ATOM   3990 N  N     . THR B 2 293 ? -13.212 -47.361 -21.902 1   112.77 ? 609 THR B N     1 
ATOM   3991 C  CA    . THR B 2 293 ? -12.422 -48.426 -21.279 1   113.47 ? 609 THR B CA    1 
ATOM   3992 C  C     . THR B 2 293 ? -12.66  -48.413 -19.771 1   113.5  ? 609 THR B C     1 
ATOM   3993 O  O     . THR B 2 293 ? -12.844 -49.477 -19.179 1   113.83 ? 609 THR B O     1 
ATOM   3994 C  CB    . THR B 2 293 ? -10.933 -48.297 -21.619 1   115.18 ? 609 THR B CB    1 
ATOM   3995 O  OG1   . THR B 2 293 ? -10.764 -48.484 -23.021 1   116.44 ? 609 THR B OG1   1 
ATOM   3996 C  CG2   . THR B 2 293 ? -10.08  -49.316 -20.883 1   115.76 ? 609 THR B CG2   1 
ATOM   3997 N  N     . LEU B 2 294 ? -12.701 -47.218 -19.157 1   112.92 ? 610 LEU B N     1 
ATOM   3998 C  CA    . LEU B 2 294 ? -12.967 -47.127 -17.732 1   112.98 ? 610 LEU B CA    1 
ATOM   3999 C  C     . LEU B 2 294 ? -14.415 -47.391 -17.396 1   113.37 ? 610 LEU B C     1 
ATOM   4000 O  O     . LEU B 2 294 ? -14.68  -47.959 -16.349 1   113.61 ? 610 LEU B O     1 
ATOM   4001 C  CB    . LEU B 2 294 ? -12.499 -45.812 -17.153 1   113.1  ? 610 LEU B CB    1 
ATOM   4002 C  CG    . LEU B 2 294 ? -11.018 -45.524 -17.312 1   114.73 ? 610 LEU B CG    1 
ATOM   4003 C  CD1   . LEU B 2 294 ? -10.666 -44.223 -16.644 1   115.6  ? 610 LEU B CD1   1 
ATOM   4004 C  CD2   . LEU B 2 294 ? -10.147 -46.65  -16.753 1   115.32 ? 610 LEU B CD2   1 
ATOM   4005 N  N     . MET B 2 295 ? -15.351 -47.052 -18.288 1   113.49 ? 611 MET B N     1 
ATOM   4006 C  CA    . MET B 2 295 ? -16.761 -47.374 -18.077 1   114.28 ? 611 MET B CA    1 
ATOM   4007 C  C     . MET B 2 295 ? -17.015 -48.882 -18.18  1   114.81 ? 611 MET B C     1 
ATOM   4008 O  O     . MET B 2 295 ? -17.957 -49.373 -17.566 1   114.74 ? 611 MET B O     1 
ATOM   4009 C  CB    . MET B 2 295 ? -17.651 -46.624 -19.054 1   115.21 ? 611 MET B CB    1 
ATOM   4010 C  CG    . MET B 2 295 ? -17.645 -45.155 -18.842 1   118.13 ? 611 MET B CG    1 
ATOM   4011 S  SD    . MET B 2 295 ? -19.112 -44.464 -19.63  1   125.6  ? 611 MET B SD    1 
ATOM   4012 C  CE    . MET B 2 295 ? -18.664 -44.634 -21.352 1   125.75 ? 611 MET B CE    1 
ATOM   4013 N  N     . ALA B 2 296 ? -16.175 -49.617 -18.939 1   115.3  ? 612 ALA B N     1 
ATOM   4014 C  CA    . ALA B 2 296 ? -16.252 -51.076 -19.034 1   116.45 ? 612 ALA B CA    1 
ATOM   4015 C  C     . ALA B 2 296 ? -15.797 -51.761 -17.728 1   117.76 ? 612 ALA B C     1 
ATOM   4016 O  O     . ALA B 2 296 ? -16.044 -52.955 -17.557 1   118.06 ? 612 ALA B O     1 
ATOM   4017 C  CB    . ALA B 2 296 ? -15.427 -51.579 -20.205 1   116.53 ? 612 ALA B CB    1 
ATOM   4018 N  N     . LYS B 2 297 ? -15.118 -51.011 -16.825 1   118.38 ? 613 LYS B N     1 
ATOM   4019 C  CA    . LYS B 2 297 ? -14.713 -51.437 -15.485 1   119.56 ? 613 LYS B CA    1 
ATOM   4020 C  C     . LYS B 2 297 ? -15.817 -51.128 -14.436 1   120.5  ? 613 LYS B C     1 
ATOM   4021 O  O     . LYS B 2 297 ? -15.555 -51.255 -13.248 1   120.84 ? 613 LYS B O     1 
ATOM   4022 C  CB    . LYS B 2 297 ? -13.429 -50.725 -15.026 1   121.86 ? 613 LYS B CB    1 
ATOM   4023 C  CG    . LYS B 2 297 ? -12.33  -50.603 -16.058 1   127.01 ? 613 LYS B CG    1 
ATOM   4024 C  CD    . LYS B 2 297 ? -11.603 -51.902 -16.231 1   132.51 ? 613 LYS B CD    1 
ATOM   4025 C  CE    . LYS B 2 297 ? -10.621 -51.82  -17.366 1   137.31 ? 613 LYS B CE    1 
ATOM   4026 N  NZ    . LYS B 2 297 ? -10.311 -53.168 -17.904 1   140.5  ? 613 LYS B NZ    1 
ATOM   4027 N  N     . GLY B 2 298 ? -16.998 -50.671 -14.858 1   120.85 ? 614 GLY B N     1 
ATOM   4028 C  CA    . GLY B 2 298 ? -18.102 -50.373 -13.953 1   121.66 ? 614 GLY B CA    1 
ATOM   4029 C  C     . GLY B 2 298 ? -18.175 -48.949 -13.453 1   122.31 ? 614 GLY B C     1 
ATOM   4030 O  O     . GLY B 2 298 ? -19.098 -48.606 -12.719 1   122.36 ? 614 GLY B O     1 
ATOM   4031 N  N     . LEU B 2 299 ? -17.199 -48.115 -13.825 1   122.64 ? 615 LEU B N     1 
ATOM   4032 C  CA    . LEU B 2 299 ? -17.158 -46.717 -13.414 1   123.37 ? 615 LEU B CA    1 
ATOM   4033 C  C     . LEU B 2 299 ? -18.182 -45.925 -14.212 1   124.48 ? 615 LEU B C     1 
ATOM   4034 O  O     . LEU B 2 299 ? -18.308 -46.154 -15.418 1   124.97 ? 615 LEU B O     1 
ATOM   4035 C  CB    . LEU B 2 299 ? -15.763 -46.126 -13.682 1   123.26 ? 615 LEU B CB    1 
ATOM   4036 C  CG    . LEU B 2 299 ? -14.676 -46.42  -12.661 1   124.57 ? 615 LEU B CG    1 
ATOM   4037 C  CD1   . LEU B 2 299 ? -14.059 -47.763 -12.884 1   125.21 ? 615 LEU B CD1   1 
ATOM   4038 C  CD2   . LEU B 2 299 ? -13.582 -45.421 -12.766 1   125.17 ? 615 LEU B CD2   1 
ATOM   4039 N  N     . ASP B 2 300 ? -18.9   -44.981 -13.566 1   124.7  ? 616 ASP B N     1 
ATOM   4040 C  CA    . ASP B 2 300 ? -19.842 -44.142 -14.317 1   125.25 ? 616 ASP B CA    1 
ATOM   4041 C  C     . ASP B 2 300 ? -19.087 -43.043 -15.085 1   124.89 ? 616 ASP B C     1 
ATOM   4042 O  O     . ASP B 2 300 ? -17.9   -42.83  -14.838 1   124.95 ? 616 ASP B O     1 
ATOM   4043 C  CB    . ASP B 2 300 ? -21.018 -43.608 -13.458 1   127.56 ? 616 ASP B CB    1 
ATOM   4044 C  CG    . ASP B 2 300 ? -20.685 -42.658 -12.325 1   132.63 ? 616 ASP B CG    1 
ATOM   4045 O  OD1   . ASP B 2 300 ? -19.87  -41.727 -12.545 1   133.43 ? 616 ASP B OD1   1 
ATOM   4046 O  OD2   . ASP B 2 300 ? -21.274 -42.82  -11.224 1   134.87 ? 616 ASP B OD2   1 
ATOM   4047 N  N     . GLU B 2 301 ? -19.756 -42.353 -16.014 1   124.35 ? 617 GLU B N     1 
ATOM   4048 C  CA    . GLU B 2 301 ? -19.121 -41.313 -16.817 1   124.4  ? 617 GLU B CA    1 
ATOM   4049 C  C     . GLU B 2 301 ? -18.359 -40.264 -15.997 1   124.03 ? 617 GLU B C     1 
ATOM   4050 O  O     . GLU B 2 301 ? -17.282 -39.826 -16.4   1   123.98 ? 617 GLU B O     1 
ATOM   4051 C  CB    . GLU B 2 301 ? -20.156 -40.65  -17.721 1   126.71 ? 617 GLU B CB    1 
ATOM   4052 C  CG    . GLU B 2 301 ? -19.538 -39.728 -18.749 1   131.93 ? 617 GLU B CG    1 
ATOM   4053 C  CD    . GLU B 2 301 ? -20.531 -39.264 -19.791 1   138.86 ? 617 GLU B CD    1 
ATOM   4054 O  OE1   . GLU B 2 301 ? -21.478 -40.027 -20.092 1   139.86 ? 617 GLU B OE1   1 
ATOM   4055 O  OE2   . GLU B 2 301 ? -20.366 -38.132 -20.302 1   141.54 ? 617 GLU B OE2   1 
ATOM   4056 N  N     . ASP B 2 302 ? -18.891 -39.911 -14.827 1   123.6  ? 618 ASP B N     1 
ATOM   4057 C  CA    . ASP B 2 302 ? -18.249 -38.932 -13.967 1   123.68 ? 618 ASP B CA    1 
ATOM   4058 C  C     . ASP B 2 302 ? -17.052 -39.513 -13.239 1   122.68 ? 618 ASP B C     1 
ATOM   4059 O  O     . ASP B 2 302 ? -16.042 -38.83  -13.122 1   122.77 ? 618 ASP B O     1 
ATOM   4060 C  CB    . ASP B 2 302 ? -19.254 -38.326 -12.984 1   126.53 ? 618 ASP B CB    1 
ATOM   4061 C  CG    . ASP B 2 302 ? -20.287 -37.45  -13.663 1   132.76 ? 618 ASP B CG    1 
ATOM   4062 O  OD1   . ASP B 2 302 ? -19.909 -36.697 -14.602 1   133.25 ? 618 ASP B OD1   1 
ATOM   4063 O  OD2   . ASP B 2 302 ? -21.473 -37.512 -13.258 1   135.98 ? 618 ASP B OD2   1 
ATOM   4064 N  N     . GLU B 2 303 ? -17.147 -40.758 -12.758 1   121.66 ? 619 GLU B N     1 
ATOM   4065 C  CA    . GLU B 2 303 ? -16.027 -41.393 -12.068 1   121.29 ? 619 GLU B CA    1 
ATOM   4066 C  C     . GLU B 2 303 ? -14.875 -41.615 -13.045 1   120.52 ? 619 GLU B C     1 
ATOM   4067 O  O     . GLU B 2 303 ? -13.726 -41.362 -12.695 1   120.55 ? 619 GLU B O     1 
ATOM   4068 C  CB    . GLU B 2 303 ? -16.45  -42.735 -11.447 1   123.72 ? 619 GLU B CB    1 
ATOM   4069 C  CG    . GLU B 2 303 ? -17.4   -42.611 -10.267 1   129.08 ? 619 GLU B CG    1 
ATOM   4070 C  CD    . GLU B 2 303 ? -18.168 -43.874 -9.912  1   135.65 ? 619 GLU B CD    1 
ATOM   4071 O  OE1   . GLU B 2 303 ? -18.154 -44.826 -10.724 1   137.24 ? 619 GLU B OE1   1 
ATOM   4072 O  OE2   . GLU B 2 303 ? -18.799 -43.907 -8.831  1   137.63 ? 619 GLU B OE2   1 
ATOM   4073 N  N     . ALA B 2 304 ? -15.19  -42.057 -14.279 1   119.73 ? 620 ALA B N     1 
ATOM   4074 C  CA    . ALA B 2 304 ? -14.214 -42.326 -15.337 1   119.45 ? 620 ALA B CA    1 
ATOM   4075 C  C     . ALA B 2 304 ? -13.505 -41.062 -15.785 1   118.96 ? 620 ALA B C     1 
ATOM   4076 O  O     . ALA B 2 304 ? -12.293 -41.082 -15.981 1   119.11 ? 620 ALA B O     1 
ATOM   4077 C  CB    . ALA B 2 304 ? -14.893 -42.989 -16.524 1   119.63 ? 620 ALA B CB    1 
ATOM   4078 N  N     . THR B 2 305 ? -14.252 -39.956 -15.918 1   118.21 ? 621 THR B N     1 
ATOM   4079 C  CA    . THR B 2 305 ? -13.685 -38.668 -16.306 1   117.81 ? 621 THR B CA    1 
ATOM   4080 C  C     . THR B 2 305 ? -12.777 -38.145 -15.191 1   116.76 ? 621 THR B C     1 
ATOM   4081 O  O     . THR B 2 305 ? -11.672 -37.69  -15.469 1   116.69 ? 621 THR B O     1 
ATOM   4082 C  CB    . THR B 2 305 ? -14.8   -37.682 -16.657 1   119.33 ? 621 THR B CB    1 
ATOM   4083 O  OG1   . THR B 2 305 ? -15.605 -38.226 -17.714 1   120.47 ? 621 THR B OG1   1 
ATOM   4084 C  CG2   . THR B 2 305 ? -14.26  -36.315 -17.048 1   119.74 ? 621 THR B CG2   1 
ATOM   4085 N  N     . GLU B 2 306 ? -13.217 -38.278 -13.927 1   115.83 ? 622 GLU B N     1 
ATOM   4086 C  CA    . GLU B 2 306 ? -12.439 -37.866 -12.757 1   115.48 ? 622 GLU B CA    1 
ATOM   4087 C  C     . GLU B 2 306 ? -11.134 -38.638 -12.657 1   114.25 ? 622 GLU B C     1 
ATOM   4088 O  O     . GLU B 2 306 ? -10.136 -38.079 -12.228 1   114.08 ? 622 GLU B O     1 
ATOM   4089 C  CB    . GLU B 2 306 ? -13.238 -38.065 -11.468 1   118.73 ? 622 GLU B CB    1 
ATOM   4090 C  CG    . GLU B 2 306 ? -12.662 -37.298 -10.288 1   125.74 ? 622 GLU B CG    1 
ATOM   4091 C  CD    . GLU B 2 306 ? -12.619 -38.041 -8.963  1   135.54 ? 622 GLU B CD    1 
ATOM   4092 O  OE1   . GLU B 2 306 ? -12.88  -39.268 -8.95   1   137.98 ? 622 GLU B OE1   1 
ATOM   4093 O  OE2   . GLU B 2 306 ? -12.315 -37.392 -7.934  1   138.4  ? 622 GLU B OE2   1 
ATOM   4094 N  N     . ILE B 2 307 ? -11.134 -39.913 -13.048 1   113.37 ? 623 ILE B N     1 
ATOM   4095 C  CA    . ILE B 2 307 ? -9.93   -40.728 -13.023 1   113.12 ? 623 ILE B CA    1 
ATOM   4096 C  C     . ILE B 2 307 ? -8.933  -40.257 -14.079 1   113.27 ? 623 ILE B C     1 
ATOM   4097 O  O     . ILE B 2 307 ? -7.748  -40.114 -13.772 1   113.42 ? 623 ILE B O     1 
ATOM   4098 C  CB    . ILE B 2 307 ? -10.287 -42.222 -13.142 1   113.2  ? 623 ILE B CB    1 
ATOM   4099 C  CG1   . ILE B 2 307 ? -10.979 -42.71  -11.858 1   114.13 ? 623 ILE B CG1   1 
ATOM   4100 C  CG2   . ILE B 2 307 ? -9.065  -43.075 -13.466 1   113.43 ? 623 ILE B CG2   1 
ATOM   4101 C  CD1   . ILE B 2 307 ? -10.204 -42.481 -10.559 1   115.37 ? 623 ILE B CD1   1 
ATOM   4102 N  N     . ILE B 2 308 ? -9.421  -39.973 -15.304 1   113.05 ? 624 ILE B N     1 
ATOM   4103 C  CA    . ILE B 2 308 ? -8.608  -39.476 -16.418 1   113.16 ? 624 ILE B CA    1 
ATOM   4104 C  C     . ILE B 2 308 ? -8.014  -38.107 -16.084 1   113.71 ? 624 ILE B C     1 
ATOM   4105 O  O     . ILE B 2 308 ? -6.823  -37.896 -16.283 1   113.57 ? 624 ILE B O     1 
ATOM   4106 C  CB    . ILE B 2 308 ? -9.433  -39.468 -17.724 1   113.14 ? 624 ILE B CB    1 
ATOM   4107 C  CG1   . ILE B 2 308 ? -9.708  -40.904 -18.196 1   113.44 ? 624 ILE B CG1   1 
ATOM   4108 C  CG2   . ILE B 2 308 ? -8.739  -38.659 -18.817 1   113.65 ? 624 ILE B CG2   1 
ATOM   4109 C  CD1   . ILE B 2 308 ? -10.868 -41.037 -19.088 1   114.27 ? 624 ILE B CD1   1 
ATOM   4110 N  N     . VAL B 2 309 ? -8.836  -37.204 -15.536 1   114.26 ? 625 VAL B N     1 
ATOM   4111 C  CA    . VAL B 2 309 ? -8.43   -35.867 -15.098 1   115.36 ? 625 VAL B CA    1 
ATOM   4112 C  C     . VAL B 2 309 ? -7.395  -35.942 -13.947 1   116.35 ? 625 VAL B C     1 
ATOM   4113 O  O     . VAL B 2 309 ? -6.385  -35.244 -14     1   116.32 ? 625 VAL B O     1 
ATOM   4114 C  CB    . VAL B 2 309 ? -9.676  -35.021 -14.724 1   116.14 ? 625 VAL B CB    1 
ATOM   4115 C  CG1   . VAL B 2 309 ? -9.306  -33.79  -13.906 1   116.72 ? 625 VAL B CG1   1 
ATOM   4116 C  CG2   . VAL B 2 309 ? -10.463 -34.629 -15.968 1   116.66 ? 625 VAL B CG2   1 
ATOM   4117 N  N     . LYS B 2 310 ? -7.616  -36.816 -12.94  1   116.99 ? 626 LYS B N     1 
ATOM   4118 C  CA    . LYS B 2 310 ? -6.67   -36.974 -11.835 1   117.92 ? 626 LYS B CA    1 
ATOM   4119 C  C     . LYS B 2 310 ? -5.337  -37.5   -12.314 1   118.91 ? 626 LYS B C     1 
ATOM   4120 O  O     . LYS B 2 310 ? -4.312  -37.027 -11.853 1   118.87 ? 626 LYS B O     1 
ATOM   4121 C  CB    . LYS B 2 310 ? -7.231  -37.866 -10.739 1   119.74 ? 626 LYS B CB    1 
ATOM   4122 C  CG    . LYS B 2 310 ? -8.225  -37.142 -9.864  1   124.54 ? 626 LYS B CG    1 
ATOM   4123 C  CD    . LYS B 2 310 ? -8.737  -38.044 -8.759  1   130.08 ? 626 LYS B CD    1 
ATOM   4124 C  CE    . LYS B 2 310 ? -8.096  -37.737 -7.423  1   134.52 ? 626 LYS B CE    1 
ATOM   4125 N  NZ    . LYS B 2 310 ? -8.592  -38.64  -6.349  1   137.03 ? 626 LYS B NZ    1 
ATOM   4126 N  N     . GLY B 2 311 ? -5.352  -38.435 -13.257 1   119.73 ? 627 GLY B N     1 
ATOM   4127 C  CA    . GLY B 2 311 ? -4.126  -38.963 -13.846 1   121.04 ? 627 GLY B CA    1 
ATOM   4128 C  C     . GLY B 2 311 ? -3.412  -37.931 -14.702 1   122.24 ? 627 GLY B C     1 
ATOM   4129 O  O     . GLY B 2 311 ? -2.182  -37.89  -14.747 1   122.28 ? 627 GLY B O     1 
ATOM   4130 N  N     . MET B 2 312 ? -4.188  -37.085 -15.38  1   123.01 ? 628 MET B N     1 
ATOM   4131 C  CA    . MET B 2 312 ? -3.708  -36.01  -16.229 1   124.35 ? 628 MET B CA    1 
ATOM   4132 C  C     . MET B 2 312 ? -2.934  -34.987 -15.399 1   125.94 ? 628 MET B C     1 
ATOM   4133 O  O     . MET B 2 312 ? -1.847  -34.583 -15.799 1   126    ? 628 MET B O     1 
ATOM   4134 C  CB    . MET B 2 312 ? -4.912  -35.344 -16.92  1   124.85 ? 628 MET B CB    1 
ATOM   4135 C  CG    . MET B 2 312 ? -4.566  -34.164 -17.778 1   126.77 ? 628 MET B CG    1 
ATOM   4136 S  SD    . MET B 2 312 ? -3.529  -34.632 -19.174 1   130.28 ? 628 MET B SD    1 
ATOM   4137 C  CE    . MET B 2 312 ? -4.627  -35.691 -20.069 1   127.96 ? 628 MET B CE    1 
ATOM   4138 N  N     . ILE B 2 313 ? -3.462  -34.603 -14.224 1   127.16 ? 629 ILE B N     1 
ATOM   4139 C  CA    . ILE B 2 313 ? -2.82   -33.608 -13.357 1   128.95 ? 629 ILE B CA    1 
ATOM   4140 C  C     . ILE B 2 313 ? -1.787  -34.194 -12.359 1   130.72 ? 629 ILE B C     1 
ATOM   4141 O  O     . ILE B 2 313 ? -1.213  -33.441 -11.57  1   130.72 ? 629 ILE B O     1 
ATOM   4142 C  CB    . ILE B 2 313 ? -3.88   -32.744 -12.633 1   129.65 ? 629 ILE B CB    1 
ATOM   4143 C  CG1   . ILE B 2 313 ? -4.64   -33.557 -11.568 1   130.81 ? 629 ILE B CG1   1 
ATOM   4144 C  CG2   . ILE B 2 313 ? -4.834  -32.1   -13.638 1   130.17 ? 629 ILE B CG2   1 
ATOM   4145 C  CD1   . ILE B 2 313 ? -5.663  -32.751 -10.751 1   132.15 ? 629 ILE B CD1   1 
ATOM   4146 N  N     . GLY B 2 314 ? -1.553  -35.505 -12.415 1   132.09 ? 630 GLY B N     1 
ATOM   4147 C  CA    . GLY B 2 314 ? -0.562  -36.19  -11.588 1   133.89 ? 630 GLY B CA    1 
ATOM   4148 C  C     . GLY B 2 314 ? -0.973  -36.602 -10.187 1   135.66 ? 630 GLY B C     1 
ATOM   4149 O  O     . GLY B 2 314 ? -0.109  -36.898 -9.36   1   135.79 ? 630 GLY B O     1 
ATOM   4150 N  N     . ASP B 2 315 ? -2.283  -36.654 -9.908  1   136.9  ? 631 ASP B N     1 
ATOM   4151 C  CA    . ASP B 2 315 ? -2.832  -37.031 -8.595  1   138.64 ? 631 ASP B CA    1 
ATOM   4152 C  C     . ASP B 2 315 ? -2.875  -38.557 -8.397  1   139.77 ? 631 ASP B C     1 
ATOM   4153 O  O     . ASP B 2 315 ? -2.634  -39.058 -7.294  1   139.77 ? 631 ASP B O     1 
ATOM   4154 C  CB    . ASP B 2 315 ? -4.269  -36.488 -8.449  1   140.88 ? 631 ASP B CB    1 
ATOM   4155 C  CG    . ASP B 2 315 ? -4.399  -35.032 -8.047  1   146.1  ? 631 ASP B CG    1 
ATOM   4156 O  OD1   . ASP B 2 315 ? -3.365  -34.324 -8.017  1   146.95 ? 631 ASP B OD1   1 
ATOM   4157 O  OD2   . ASP B 2 315 ? -5.536  -34.599 -7.761  1   148.46 ? 631 ASP B OD2   1 
ATOM   4158 N  N     . LEU B 2 316 ? -3.235  -39.275 -9.476  1   140.53 ? 632 LEU B N     1 
ATOM   4159 C  CA    . LEU B 2 316 ? -3.413  -40.729 -9.543  1   141.71 ? 632 LEU B CA    1 
ATOM   4160 C  C     . LEU B 2 316 ? -2.105  -41.525 -9.558  1   142.33 ? 632 LEU B C     1 
ATOM   4161 O  O     . LEU B 2 316 ? -2.067  -42.644 -10.077 1   142.47 ? 632 LEU B O     1 
ATOM   4162 C  CB    . LEU B 2 316 ? -4.253  -41.063 -10.795 1   142.19 ? 632 LEU B CB    1 
ATOM   4163 C  CG    . LEU B 2 316 ? -5.597  -41.784 -10.606 1   144.05 ? 632 LEU B CG    1 
ATOM   4164 C  CD1   . LEU B 2 316 ? -5.417  -43.277 -10.553 1   144.52 ? 632 LEU B CD1   1 
ATOM   4165 C  CD2   . LEU B 2 316 ? -6.391  -41.259 -9.401  1   145    ? 632 LEU B CD2   1 
HETATM 4166 MG MG    . MG  C 3 .   ? -10.333 -57.218 -33.462 1   37.91  2 301 MG  A MG    1 
HETATM 4167 P  PG    . ANP D 4 .   ? -9.366  -58.076 -36.558 1   153.81 ? 302 ANP A PG    1 
HETATM 4168 O  O1G   . ANP D 4 .   ? -9.432  -58.84  -35.32  1   153.8  ? 302 ANP A O1G   1 
HETATM 4169 O  O2G   . ANP D 4 .   ? -9.685  -56.662 -36.269 1   153.75 ? 302 ANP A O2G   1 
HETATM 4170 O  O3G   . ANP D 4 .   ? -8.051  -58.287 -37.203 1   153.61 ? 302 ANP A O3G   1 
HETATM 4171 P  PB    . ANP D 4 .   ? -12.157 -58.59  -37.341 1   154.9  ? 302 ANP A PB    1 
HETATM 4172 O  O1B   . ANP D 4 .   ? -12.774 -59.629 -38.188 1   154.74 ? 302 ANP A O1B   1 
HETATM 4173 O  O2B   . ANP D 4 .   ? -12.307 -58.792 -35.885 1   154.87 ? 302 ANP A O2B   1 
HETATM 4174 N  N3B   . ANP D 4 .   ? -10.549 -58.507 -37.588 1   154.27 ? 302 ANP A N3B   1 
HETATM 4175 P  PA    . ANP D 4 .   ? -13.925 -56.248 -36.976 1   157.11 ? 302 ANP A PA    1 
HETATM 4176 O  O1A   . ANP D 4 .   ? -14.682 -57.096 -36.034 1   157.09 ? 302 ANP A O1A   1 
HETATM 4177 O  O2A   . ANP D 4 .   ? -13.369 -54.96  -36.502 1   157.13 ? 302 ANP A O2A   1 
HETATM 4178 O  O3A   . ANP D 4 .   ? -12.732 -57.1   -37.615 1   155.98 ? 302 ANP A O3A   1 
HETATM 4179 O  "O5'" . ANP D 4 .   ? -14.88  -56.013 -38.232 1   158.39 ? 302 ANP A "O5'" 1 
HETATM 4180 C  "C5'" . ANP D 4 .   ? -14.361 -55.416 -39.44  1   159.82 ? 302 ANP A "C5'" 1 
HETATM 4181 C  "C4'" . ANP D 4 .   ? -15.464 -54.65  -40.13  1   161.25 ? 302 ANP A "C4'" 1 
HETATM 4182 O  "O4'" . ANP D 4 .   ? -15.735 -53.423 -39.412 1   162.05 ? 302 ANP A "O4'" 1 
HETATM 4183 C  "C3'" . ANP D 4 .   ? -15.185 -54.244 -41.578 1   161.79 ? 302 ANP A "C3'" 1 
HETATM 4184 O  "O3'" . ANP D 4 .   ? -16.345 -54.4   -42.392 1   161.79 ? 302 ANP A "O3'" 1 
HETATM 4185 C  "C2'" . ANP D 4 .   ? -14.719 -52.788 -41.444 1   162.3  ? 302 ANP A "C2'" 1 
HETATM 4186 O  "O2'" . ANP D 4 .   ? -14.993 -52.01  -42.606 1   162.41 ? 302 ANP A "O2'" 1 
HETATM 4187 C  "C1'" . ANP D 4 .   ? -15.56  -52.302 -40.262 1   162.6  ? 302 ANP A "C1'" 1 
HETATM 4188 N  N9    . ANP D 4 .   ? -14.958 -51.217 -39.486 1   163.32 ? 302 ANP A N9    1 
HETATM 4189 C  C8    . ANP D 4 .   ? -14.489 -51.293 -38.199 1   163.56 ? 302 ANP A C8    1 
HETATM 4190 N  N7    . ANP D 4 .   ? -13.979 -50.173 -37.747 1   163.69 ? 302 ANP A N7    1 
HETATM 4191 C  C5    . ANP D 4 .   ? -14.121 -49.294 -38.811 1   163.7  ? 302 ANP A C5    1 
HETATM 4192 C  C6    . ANP D 4 .   ? -13.77  -47.939 -38.977 1   163.67 ? 302 ANP A C6    1 
HETATM 4193 N  N6    . ANP D 4 .   ? -13.165 -47.204 -38.039 1   163.57 ? 302 ANP A N6    1 
HETATM 4194 N  N1    . ANP D 4 .   ? -14.052 -47.359 -40.165 1   163.73 ? 302 ANP A N1    1 
HETATM 4195 C  C2    . ANP D 4 .   ? -14.639 -48.091 -41.115 1   163.76 ? 302 ANP A C2    1 
HETATM 4196 N  N3    . ANP D 4 .   ? -15.014 -49.373 -41.075 1   163.73 ? 302 ANP A N3    1 
HETATM 4197 C  C4    . ANP D 4 .   ? -14.724 -49.923 -39.89  1   163.62 ? 302 ANP A C4    1 
HETATM 4198 O  O     . HOH E 5 .   ? -32.707 -54.049 -31.581 1   49.69  ? 401 HOH A O     1 
HETATM 4199 O  O     . HOH E 5 .   ? -24.181 -75.799 -34.955 1   52.2   ? 402 HOH A O     1 
HETATM 4200 O  O     . HOH E 5 .   ? -25.761 -70.192 -30.13  1   57.64  ? 403 HOH A O     1 
HETATM 4201 O  O     . HOH E 5 .   ? -13.259 -71.415 -49.784 1   45.53  ? 404 HOH A O     1 
HETATM 4202 O  O     . HOH E 5 .   ? 3.76    -48.812 -2.525  1   38.32  ? 405 HOH A O     1 
HETATM 4203 O  O     . HOH E 5 .   ? -10.906 -69.128 -49.857 1   75.85  ? 406 HOH A O     1 
HETATM 4204 O  O     . HOH F 5 .   ? -16.515 -24.927 -21.852 1   28.99  ? 701 HOH B O     1 
HETATM 4205 O  O     . HOH F 5 .   ? -1.394  -10.677 -16.484 1   39.32  ? 702 HOH B O     1 
HETATM 4206 O  O     . HOH F 5 .   ? 7.666   -25.137 -17.684 1   13.97  ? 703 HOH B O     1 
HETATM 4207 O  O     . HOH F 5 .   ? -6.348  -11.57  -8.459  1   55.44  ? 704 HOH B O     1 
HETATM 4208 O  O     . HOH F 5 .   ? 19.842  -29.587 -49.632 1   65     ? 705 HOH B O     1 
HETATM 4209 O  O     . HOH F 5 .   ? 21.944  -29.533 -42.81  1   52.7   ? 706 HOH B O     1 
HETATM 4210 O  O     . HOH F 5 .   ? -0.101  -10.434 -19.606 1   49.61  ? 707 HOH B O     1 
HETATM 4211 O  O     . HOH F 5 .   ? 23.559  -36.941 -36.015 1   36.27  ? 708 HOH B O     1 
HETATM 4212 O  O     . HOH F 5 .   ? 19.724  -26.46  -44.523 1   38.53  ? 709 HOH B O     1 
HETATM 4213 O  O     . HOH F 5 .   ? 16.061  -39.122 -33.157 1   69.66  ? 710 HOH B O     1 
HETATM 4214 O  O     . HOH F 5 .   ? -1.391  -9.391  -7.103  1   52.75  ? 711 HOH B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . GLY A 1   ? 2.2975 1.4253 1.8463 -1.2244 0.536   -0.6038 -2  GLY A N   
2    C CA  . GLY A 1   ? 2.313  1.4073 1.8734 -1.2578 0.5735  -0.613  -2  GLY A CA  
3    C C   . GLY A 1   ? 2.3199 1.3793 1.9041 -1.2313 0.6253  -0.596  -2  GLY A C   
4    O O   . GLY A 1   ? 2.4011 1.3126 1.896  -1.1919 0.6707  -0.5721 -2  GLY A O   
5    N N   . GLU A 2   ? 2.2323 1.4281 1.9323 -1.2507 0.6174  -0.6041 -1  GLU A N   
6    C CA  . GLU A 2   ? 2.2302 1.4136 1.9519 -1.2278 0.6629  -0.5869 -1  GLU A CA  
7    C C   . GLU A 2   ? 2.2893 1.3568 1.9569 -1.2284 0.6798  -0.5427 -1  GLU A C   
8    O O   . GLU A 2   ? 2.2643 1.372  1.9714 -1.2248 0.7011  -0.5257 -1  GLU A O   
9    C CB  . GLU A 2   ? 2.1116 1.5339 2.0055 -1.2224 0.6394  -0.6126 -1  GLU A CB  
10   C CG  . GLU A 2   ? 2.0758 1.6302 2.0585 -1.1886 0.6006  -0.6422 -1  GLU A CG  
11   C CD  . GLU A 2   ? 2.178  1.6    2.077  -1.1347 0.608   -0.6231 -1  GLU A CD  
12   O OE1 . GLU A 2   ? 2.1553 1.612  2.0626 -1.0989 0.5297  -0.6016 -1  GLU A OE1 
13   O OE2 . GLU A 2   ? 2.2485 1.5581 2.0985 -1.0819 0.6443  -0.5909 -1  GLU A OE2 
14   N N   . PHE A 3   ? 2.3639 1.289  1.9423 -1.2308 0.6694  -0.5255 0   PHE A N   
15   C CA  . PHE A 3   ? 2.4269 1.2216 1.9524 -1.2248 0.679   -0.4837 0   PHE A CA  
16   C C   . PHE A 3   ? 2.5369 1.1294 1.9317 -1.1724 0.7167  -0.4499 0   PHE A C   
17   O O   . PHE A 3   ? 2.5872 1.1043 1.9153 -1.1451 0.7181  -0.458  0   PHE A O   
18   C CB  . PHE A 3   ? 2.4361 1.2037 1.9631 -1.2477 0.6383  -0.4908 0   PHE A CB  
19   C CG  . PHE A 3   ? 2.514  1.1276 1.9886 -1.2314 0.6388  -0.4502 0   PHE A CG  
20   C CD1 . PHE A 3   ? 2.5013 1.1327 2.0187 -1.2436 0.6433  -0.414  0   PHE A CD1 
21   C CD2 . PHE A 3   ? 2.5966 1.0657 1.9955 -1.2001 0.6259  -0.4476 0   PHE A CD2 
22   C CE1 . PHE A 3   ? 2.5654 1.0596 2.0446 -1.2318 0.6368  -0.375  0   PHE A CE1 
23   C CE2 . PHE A 3   ? 2.6562 0.9924 2.025  -1.1827 0.6194  -0.415  0   PHE A CE2 
24   C CZ  . PHE A 3   ? 2.6373 0.9794 2.0424 -1.2032 0.6263  -0.3786 0   PHE A CZ  
25   N N   . MET A 4   ? 2.5684 1.0814 1.9272 -1.1575 0.7446  -0.4086 1   MET A N   
26   C CA  . MET A 4   ? 2.6642 0.997  1.9073 -1.1023 0.7743  -0.3674 1   MET A CA  
27   C C   . MET A 4   ? 2.6645 0.9906 1.8721 -1.0737 0.81    -0.3777 1   MET A C   
28   O O   . MET A 4   ? 2.7458 0.9249 1.854  -1.0208 0.8266  -0.3496 1   MET A O   
29   C CB  . MET A 4   ? 2.7538 0.9321 1.9212 -1.0642 0.7543  -0.3512 1   MET A CB  
30   C CG  . MET A 4   ? 2.7716 0.9503 1.991  -1.0753 0.7084  -0.3358 1   MET A CG  
31   S SD  . MET A 4   ? 2.8274 0.9848 2.0813 -1.0521 0.688   -0.2616 1   MET A SD  
32   C CE  . MET A 4   ? 2.9246 0.8686 2.0481 -0.9796 0.7089  -0.2233 1   MET A CE  
33   N N   . VAL A 5   ? 2.5686 1.0558 1.8659 -1.1037 0.82    -0.4174 2   VAL A N   
34   C CA  . VAL A 5   ? 2.5664 1.0612 1.8573 -1.0726 0.8478  -0.4304 2   VAL A CA  
35   C C   . VAL A 5   ? 2.6082 1.024  1.8416 -1.0362 0.8828  -0.3918 2   VAL A C   
36   O O   . VAL A 5   ? 2.6489 0.9978 1.834  -0.9921 0.9041  -0.3854 2   VAL A O   
37   C CB  . VAL A 5   ? 2.4554 1.1696 1.893  -1.0972 0.8321  -0.4858 2   VAL A CB  
38   C CG1 . VAL A 5   ? 2.4338 1.2066 1.9017 -1.1189 0.7914  -0.5174 2   VAL A CG1 
39   C CG2 . VAL A 5   ? 2.3652 1.2507 1.9188 -1.1296 0.8192  -0.4939 2   VAL A CG2 
40   N N   . SER A 6   ? 2.6004 1.0204 1.8338 -1.0544 0.8855  -0.3616 3   SER A N   
41   C CA  . SER A 6   ? 2.641  1.0031 1.8175 -1.0244 0.9088  -0.3187 3   SER A CA  
42   C C   . SER A 6   ? 2.7573 0.9111 1.7942 -0.9645 0.9137  -0.2676 3   SER A C   
43   O O   . SER A 6   ? 2.7929 0.8998 1.7749 -0.929  0.9306  -0.238  3   SER A O   
44   C CB  . SER A 6   ? 2.6206 1.0502 1.8393 -1.0533 0.8933  -0.2851 3   SER A CB  
45   O OG  . SER A 6   ? 2.5263 1.1805 1.8877 -1.08   0.8803  -0.3179 3   SER A OG  
46   N N   . ILE A 7   ? 2.8096 0.85   1.793  -0.9496 0.8964  -0.259  4   ILE A N   
47   C CA  . ILE A 7   ? 2.9105 0.7749 1.7798 -0.8807 0.8937  -0.2131 4   ILE A CA  
48   C C   . ILE A 7   ? 2.9366 0.7556 1.7699 -0.8476 0.8998  -0.2353 4   ILE A C   
49   O O   . ILE A 7   ? 3.0058 0.6946 1.7559 -0.791  0.8931  -0.2051 4   ILE A O   
50   C CB  . ILE A 7   ? 2.96   0.7315 1.8051 -0.8676 0.8615  -0.1767 4   ILE A CB  
51   C CG1 . ILE A 7   ? 2.9291 0.7693 1.85   -0.907  0.8313  -0.2165 4   ILE A CG1 
52   C CG2 . ILE A 7   ? 2.9607 0.741  1.8156 -0.8826 0.854   -0.1311 4   ILE A CG2 
53   C CD1 . ILE A 7   ? 2.9804 0.7567 1.8735 -0.8648 0.8096  -0.2295 4   ILE A CD1 
54   N N   . MET A 8   ? 2.8696 0.814  1.7808 -0.876  0.9028  -0.2836 5   MET A N   
55   C CA  . MET A 8   ? 2.8258 0.8597 1.8075 -0.8057 0.8309  -0.2745 5   MET A CA  
56   C C   . MET A 8   ? 2.7736 0.9024 1.8231 -0.7339 0.7914  -0.2502 5   MET A C   
57   O O   . MET A 8   ? 2.7131 0.952  1.8404 -0.7514 0.7999  -0.2737 5   MET A O   
58   C CB  . MET A 8   ? 2.7597 0.9383 1.8414 -0.8537 0.8006  -0.3232 5   MET A CB  
59   C CG  . MET A 8   ? 2.8481 0.9482 1.8682 -0.8762 0.797   -0.3356 5   MET A CG  
60   S SD  . MET A 8   ? 2.8428 1.1291 1.9851 -0.9499 0.755   -0.3874 5   MET A SD  
61   C CE  . MET A 8   ? 2.7259 1.2014 1.989  -0.9385 0.715   -0.4074 5   MET A CE  
62   N N   . LEU A 9   ? 2.793  0.8824 1.8149 -0.6553 0.7505  -0.2086 6   LEU A N   
63   C CA  . LEU A 9   ? 2.7554 0.9142 1.8271 -0.5882 0.7089  -0.184  6   LEU A CA  
64   C C   . LEU A 9   ? 2.6759 0.978  1.8629 -0.5703 0.6434  -0.1986 6   LEU A C   
65   O O   . LEU A 9   ? 2.6091 1.0201 1.8897 -0.5554 0.6196  -0.2126 6   LEU A O   
66   C CB  . LEU A 9   ? 2.819  0.8707 1.8026 -0.5216 0.6955  -0.1327 6   LEU A CB  
67   C CG  . LEU A 9   ? 2.8498 0.8821 1.8033 -0.4801 0.6971  -0.1027 6   LEU A CG  
68   C CD1 . LEU A 9   ? 2.9448 0.8348 1.7766 -0.4966 0.7522  -0.0803 6   LEU A CD1 
69   C CD2 . LEU A 9   ? 2.8559 0.8948 1.8056 -0.4093 0.6461  -0.066  6   LEU A CD2 
70   N N   . LEU A 10  ? 2.6848 0.9827 1.8606 -0.5728 0.6152  -0.1969 7   LEU A N   
71   C CA  . LEU A 10  ? 2.6303 1.0458 1.8894 -0.5589 0.5479  -0.1995 7   LEU A CA  
72   C C   . LEU A 10  ? 2.6239 1.0851 1.8998 -0.6222 0.546   -0.2364 7   LEU A C   
73   O O   . LEU A 10  ? 2.6815 1.0495 1.8774 -0.6613 0.5886  -0.2506 7   LEU A O   
74   C CB  . LEU A 10  ? 2.6603 1.0353 1.8734 -0.503  0.5106  -0.1567 7   LEU A CB  
75   C CG  . LEU A 10  ? 2.6245 1.0922 1.8975 -0.4752 0.4357  -0.1373 7   LEU A CG  
76   C CD1 . LEU A 10  ? 2.6304 1.119  1.8798 -0.5042 0.4133  -0.1432 7   LEU A CD1 
77   C CD2 . LEU A 10  ? 2.561  1.1333 1.9438 -0.4657 0.3978  -0.1483 7   LEU A CD2 
78   N N   . LYS A 11  ? 2.5559 1.1571 1.9335 -0.6313 0.4937  -0.2527 8   LYS A N   
79   C CA  . LYS A 11  ? 2.5427 1.2144 1.9439 -0.6933 0.4796  -0.2879 8   LYS A CA  
80   C C   . LYS A 11  ? 2.4998 1.2904 1.9712 -0.6697 0.3928  -0.2723 8   LYS A C   
81   O O   . LYS A 11  ? 2.431  1.33   2.0096 -0.6444 0.3514  -0.274  8   LYS A O   
82   C CB  . LYS A 11  ? 2.5137 1.257  1.9779 -0.757  0.5181  -0.3383 8   LYS A CB  
83   C CG  . LYS A 11  ? 2.515  1.343  2.0048 -0.8311 0.503   -0.3802 8   LYS A CG  
84   C CD  . LYS A 11  ? 2.491  1.4396 2.0778 -0.8884 0.5279  -0.4305 8   LYS A CD  
85   C CE  . LYS A 11  ? 2.5017 1.5372 2.1082 -0.9714 0.5145  -0.4755 8   LYS A CE  
86   N NZ  . LYS A 11  ? 2.631  1.5081 2.0955 -1.0258 0.5614  -0.4856 8   LYS A NZ  
87   N N   . VAL A 12  ? 2.5394 1.3053 1.9465 -0.6761 0.3655  -0.2567 9   VAL A N   
88   C CA  . VAL A 12  ? 2.5103 1.3736 1.9558 -0.6666 0.2832  -0.2357 9   VAL A CA  
89   C C   . VAL A 12  ? 2.4955 1.4435 1.9551 -0.7399 0.2705  -0.2775 9   VAL A C   
90   O O   . VAL A 12  ? 2.5473 1.4322 1.9203 -0.7906 0.3111  -0.304  9   VAL A O   
91   C CB  . VAL A 12  ? 2.5709 1.3692 1.9285 -0.6398 0.2634  -0.1941 9   VAL A CB  
92   C CG1 . VAL A 12  ? 2.5406 1.4304 1.9223 -0.6388 0.1768  -0.1648 9   VAL A CG1 
93   C CG2 . VAL A 12  ? 2.6095 1.3287 1.9493 -0.576  0.2799  -0.1579 9   VAL A CG2 
94   N N   . GLU A 13  ? 2.423  1.5148 1.9933 -0.7449 0.2145  -0.2879 10  GLU A N   
95   C CA  . GLU A 13  ? 2.397  1.597  1.9938 -0.8171 0.1934  -0.3293 10  GLU A CA  
96   C C   . GLU A 13  ? 2.3744 1.6666 1.9813 -0.8095 0.096   -0.2967 10  GLU A C   
97   O O   . GLU A 13  ? 2.3294 1.6807 2.0143 -0.7483 0.0298  -0.2588 10  GLU A O   
98   C CB  . GLU A 13  ? 2.3496 1.6707 2.0753 -0.8368 0.2047  -0.3733 10  GLU A CB  
99   C CG  . GLU A 13  ? 2.4385 1.7495 2.1334 -0.932  0.2761  -0.4355 10  GLU A CG  
100  C CD  . GLU A 13  ? 2.4394 1.9025 2.2667 -0.9692 0.287   -0.4856 10  GLU A CD  
101  O OE1 . GLU A 13  ? 2.4763 1.9204 2.2764 -1.0545 0.3551  -0.5361 10  GLU A OE1 
102  O OE2 . GLU A 13  ? 2.3751 1.9771 2.3348 -0.9144 0.2279  -0.4767 10  GLU A OE2 
103  N N   . ASP A 14  ? 2.4087 1.7037 1.9276 -0.8731 0.0876  -0.3118 11  ASP A N   
104  C CA  . ASP A 14  ? 2.4013 1.7781 1.8942 -0.888  0.0001  -0.2832 11  ASP A CA  
105  C C   . ASP A 14  ? 2.3925 1.7761 1.9134 -0.8109 -0.0771 -0.2095 11  ASP A C   
106  O O   . ASP A 14  ? 2.3267 1.8226 1.9314 -0.7895 -0.1622 -0.187  11  ASP A O   
107  C CB  . ASP A 14  ? 2.3508 1.8927 1.9183 -0.9472 -0.0468 -0.3231 11  ASP A CB  
108  C CG  . ASP A 14  ? 2.4193 2.0319 1.9194 -0.9907 -0.122  -0.3063 11  ASP A CG  
109  O OD1 . ASP A 14  ? 2.3961 2.0681 1.9262 -0.9446 -0.2147 -0.2468 11  ASP A OD1 
110  O OD2 . ASP A 14  ? 2.4899 2.0913 1.8997 -1.0731 -0.0886 -0.3528 11  ASP A OD2 
111  N N   . LEU A 15  ? 2.4578 1.7182 1.9109 -0.7685 -0.0478 -0.1729 12  LEU A N   
112  C CA  . LEU A 15  ? 2.4695 1.7055 1.9363 -0.7019 -0.1066 -0.1054 12  LEU A CA  
113  C C   . LEU A 15  ? 2.5025 1.7521 1.8865 -0.7201 -0.1786 -0.0533 12  LEU A C   
114  O O   . LEU A 15  ? 2.5596 1.7627 1.8269 -0.7617 -0.1473 -0.0556 12  LEU A O   
115  C CB  . LEU A 15  ? 2.525  1.6348 1.9534 -0.6592 -0.0424 -0.0925 12  LEU A CB  
116  C CG  . LEU A 15  ? 2.5416 1.6169 2.0043 -0.5909 -0.0868 -0.0374 12  LEU A CG  
117  C CD1 . LEU A 15  ? 2.4905 1.6086 2.0843 -0.543  -0.0951 -0.0546 12  LEU A CD1 
118  C CD2 . LEU A 15  ? 2.6118 1.5753 2.0005 -0.569  -0.0328 -0.0201 12  LEU A CD2 
119  N N   . HIS A 16  ? 2.4675 1.7741 1.909  -0.6853 -0.2739 -0.0047 13  HIS A N   
120  C CA  . HIS A 16  ? 2.5036 1.815  1.8616 -0.7025 -0.3527 0.0577  13  HIS A CA  
121  C C   . HIS A 16  ? 2.5381 1.7685 1.9035 -0.6386 -0.3928 0.1246  13  HIS A C   
122  O O   . HIS A 16  ? 2.4983 1.7448 1.9735 -0.5763 -0.4384 0.1386  13  HIS A O   
123  C CB  . HIS A 16  ? 2.4542 1.896  1.8572 -0.7233 -0.4459 0.0653  13  HIS A CB  
124  C CG  . HIS A 16  ? 2.4633 1.9883 1.8344 -0.8047 -0.4172 0.0023  13  HIS A CG  
125  N ND1 . HIS A 16  ? 2.5154 2.072  1.7644 -0.8757 -0.4491 0.0134  13  HIS A ND1 
126  C CD2 . HIS A 16  ? 2.4391 2.0147 1.8777 -0.8315 -0.3573 -0.0733 13  HIS A CD2 
127  C CE1 . HIS A 16  ? 2.5006 2.1234 1.7494 -0.9406 -0.4093 -0.0594 13  HIS A CE1 
128  N NE2 . HIS A 16  ? 2.4597 2.0929 1.8207 -0.9189 -0.3539 -0.1117 13  HIS A NE2 
129  N N   . VAL A 17  ? 2.6091 1.7536 1.8621 -0.6547 -0.3709 0.1596  14  VAL A N   
130  C CA  . VAL A 17  ? 2.652  1.7109 1.8967 -0.6093 -0.405  0.2219  14  VAL A CA  
131  C C   . VAL A 17  ? 2.7079 1.7536 1.8364 -0.6526 -0.4725 0.2909  14  VAL A C   
132  O O   . VAL A 17  ? 2.7437 1.8011 1.7605 -0.7172 -0.4396 0.2838  14  VAL A O   
133  C CB  . VAL A 17  ? 2.6947 1.6667 1.9218 -0.5882 -0.3192 0.2051  14  VAL A CB  
134  C CG1 . VAL A 17  ? 2.7325 1.6197 1.9508 -0.5511 -0.356  0.2643  14  VAL A CG1 
135  C CG2 . VAL A 17  ? 2.6663 1.646  1.9906 -0.5532 -0.2547 0.1427  14  VAL A CG2 
136  N N   . TYR A 18  ? 2.7145 1.7346 1.8657 -0.6183 -0.5669 0.3559  15  TYR A N   
137  C CA  . TYR A 18  ? 2.7741 1.7669 1.8068 -0.6611 -0.6411 0.4337  15  TYR A CA  
138  C C   . TYR A 18  ? 2.8379 1.7065 1.8237 -0.6454 -0.6464 0.4904  15  TYR A C   
139  O O   . TYR A 18  ? 2.8307 1.6369 1.9062 -0.5776 -0.6489 0.49    15  TYR A O   
140  C CB  . TYR A 18  ? 2.7451 1.7839 1.827  -0.6337 -0.7591 0.4776  15  TYR A CB  
141  C CG  . TYR A 18  ? 2.7212 1.8886 1.7795 -0.6867 -0.7906 0.456   15  TYR A CG  
142  C CD1 . TYR A 18  ? 2.6579 1.9343 1.8296 -0.675  -0.7623 0.3796  15  TYR A CD1 
143  C CD2 . TYR A 18  ? 2.7173 1.9827 1.7257 -0.6749 -0.7843 0.4714  15  TYR A CD2 
144  C CE1 . TYR A 18  ? 2.6336 2.0344 1.7874 -0.7289 -0.7977 0.3571  15  TYR A CE1 
145  C CE2 . TYR A 18  ? 2.6735 2.0902 1.6947 -0.6862 -0.7907 0.4287  15  TYR A CE2 
146  C CZ  . TYR A 18  ? 2.6349 2.1218 1.7319 -0.7138 -0.7977 0.3698  15  TYR A CZ  
147  O OH  . TYR A 18  ? 2.5927 2.236  1.7105 -0.7211 -0.7993 0.3174  15  TYR A OH  
148  N N   . ARG A 19  ? 2.8978 1.7342 1.7409 -0.7136 -0.6489 0.5368  16  ARG A N   
149  C CA  . ARG A 19  ? 2.9439 1.6951 1.7565 -0.6982 -0.6424 0.5867  16  ARG A CA  
150  C C   . ARG A 19  ? 2.9209 1.7505 1.7351 -0.6598 -0.6576 0.6317  16  ARG A C   
151  O O   . ARG A 19  ? 2.9239 1.8203 1.6649 -0.6958 -0.6137 0.6348  16  ARG A O   
152  C CB  . ARG A 19  ? 2.9939 1.7327 1.7215 -0.7556 -0.5566 0.5653  16  ARG A CB  
153  C CG  . ARG A 19  ? 3.0505 1.6948 1.8124 -0.724  -0.5263 0.5641  16  ARG A CG  
154  C CD  . ARG A 19  ? 3.091  1.7723 1.8036 -0.7564 -0.4448 0.5573  16  ARG A CD  
155  N NE  . ARG A 19  ? 3.1468 1.7464 1.8763 -0.742  -0.4142 0.5431  16  ARG A NE  
156  C CZ  . ARG A 19  ? 3.1693 1.7303 1.9546 -0.7007 -0.4166 0.5726  16  ARG A CZ  
157  N NH1 . ARG A 19  ? 3.1481 1.7307 1.9714 -0.6666 -0.4399 0.6188  16  ARG A NH1 
158  N NH2 . ARG A 19  ? 3.1984 1.6783 1.9745 -0.7028 -0.3975 0.5564  16  ARG A NH2 
159  N N   . GLY A 20  ? 2.897  1.7218 1.7926 -0.5806 -0.7154 0.6602  17  GLY A N   
160  C CA  . GLY A 20  ? 2.8867 1.7766 1.7747 -0.5278 -0.7274 0.7025  17  GLY A CA  
161  C C   . GLY A 20  ? 2.8447 1.8739 1.7343 -0.5278 -0.7521 0.6766  17  GLY A C   
162  O O   . GLY A 20  ? 2.8051 1.8781 1.7733 -0.5121 -0.7926 0.6427  17  GLY A O   
163  N N   . ASN A 21  ? 2.8481 1.9527 1.6539 -0.5478 -0.7268 0.6859  18  ASN A N   
164  C CA  . ASN A 21  ? 2.8127 2.0536 1.6099 -0.5476 -0.7458 0.6524  18  ASN A CA  
165  C C   . ASN A 21  ? 2.8068 2.0964 1.5737 -0.6354 -0.7079 0.5842  18  ASN A C   
166  O O   . ASN A 21  ? 2.7675 2.1595 1.5548 -0.6428 -0.7278 0.5398  18  ASN A O   
167  C CB  . ASN A 21  ? 2.8352 2.1386 1.5622 -0.5095 -0.7262 0.6806  18  ASN A CB  
168  C CG  . ASN A 21  ? 2.8814 2.1548 1.6388 -0.4033 -0.7303 0.7375  18  ASN A CG  
169  O OD1 . ASN A 21  ? 2.9229 2.0937 1.7115 -0.3823 -0.7089 0.7689  18  ASN A OD1 
170  N ND2 . ASN A 21  ? 2.8694 2.2253 1.6053 -0.3377 -0.7578 0.7531  18  ASN A ND2 
171  N N   . ARG A 22  ? 2.8439 2.0631 1.5598 -0.6993 -0.6493 0.5722  19  ARG A N   
172  C CA  . ARG A 22  ? 2.8495 2.1009 1.5253 -0.7742 -0.5934 0.5055  19  ARG A CA  
173  C C   . ARG A 22  ? 2.8485 2.0476 1.5699 -0.8038 -0.6031 0.4675  19  ARG A C   
174  O O   . ARG A 22  ? 2.8714 1.9637 1.6311 -0.7836 -0.6239 0.4916  19  ARG A O   
175  C CB  . ARG A 22  ? 2.8999 2.1197 1.5149 -0.8067 -0.5108 0.4999  19  ARG A CB  
176  C CG  . ARG A 22  ? 2.9272 2.2194 1.5145 -0.7703 -0.4725 0.519   19  ARG A CG  
177  C CD  . ARG A 22  ? 2.9806 2.2123 1.5895 -0.7269 -0.4549 0.5734  19  ARG A CD  
178  N NE  . ARG A 22  ? 3.0267 2.1938 1.6614 -0.7468 -0.4099 0.5581  19  ARG A NE  
179  C CZ  . ARG A 22  ? 3.0641 2.166  1.7242 -0.7233 -0.3966 0.5958  19  ARG A CZ  
180  N NH1 . ARG A 22  ? 3.0639 2.1464 1.7241 -0.6813 -0.4176 0.6522  19  ARG A NH1 
181  N NH2 . ARG A 22  ? 3.0849 2.1228 1.7437 -0.7565 -0.3685 0.5809  19  ARG A NH2 
182  N N   . GLU A 23  ? 2.8256 2.0905 1.5354 -0.8529 -0.5802 0.4026  20  GLU A N   
183  C CA  . GLU A 23  ? 2.8343 2.0503 1.5708 -0.8894 -0.5673 0.3557  20  GLU A CA  
184  C C   . GLU A 23  ? 2.8645 2.0306 1.5286 -0.9312 -0.4588 0.305   20  GLU A C   
185  O O   . GLU A 23  ? 2.8761 2.098  1.4647 -0.9811 -0.4115 0.2646  20  GLU A O   
186  C CB  . GLU A 23  ? 2.8018 2.1552 1.6128 -0.8862 -0.5717 0.292   20  GLU A CB  
187  C CG  . GLU A 23  ? 2.8456 2.1954 1.7511 -0.8808 -0.5362 0.2296  20  GLU A CG  
188  C CD  . GLU A 23  ? 2.8534 2.3644 1.87   -0.8576 -0.5035 0.1406  20  GLU A CD  
189  O OE1 . GLU A 23  ? 2.8447 2.4533 1.8513 -0.8446 -0.4905 0.111   20  GLU A OE1 
190  O OE2 . GLU A 23  ? 2.8519 2.3773 1.9513 -0.8622 -0.4976 0.1018  20  GLU A OE2 
191  N N   . ILE A 24  ? 2.8494 1.9441 1.5801 -0.8731 -0.4042 0.2954  21  ILE A N   
192  C CA  . ILE A 24  ? 2.8619 1.9295 1.5575 -0.8815 -0.2977 0.2447  21  ILE A CA  
193  C C   . ILE A 24  ? 2.8298 1.9168 1.5842 -0.8713 -0.2277 0.1584  21  ILE A C   
194  O O   . ILE A 24  ? 2.8486 1.953  1.5352 -0.9151 -0.1661 0.1048  21  ILE A O   
195  C CB  . ILE A 24  ? 2.8818 1.8715 1.6082 -0.8318 -0.2717 0.2734  21  ILE A CB  
196  C CG1 . ILE A 24  ? 2.9278 1.8864 1.5748 -0.8603 -0.3286 0.3546  21  ILE A CG1 
197  C CG2 . ILE A 24  ? 2.898  1.872  1.6152 -0.8228 -0.1655 0.2158  21  ILE A CG2 
198  C CD1 . ILE A 24  ? 2.9511 1.8322 1.6599 -0.8048 -0.3374 0.3874  21  ILE A CD1 
199  N N   . LEU A 25  ? 2.7826 1.8624 1.6588 -0.817  -0.2342 0.1424  22  LEU A N   
200  C CA  . LEU A 25  ? 2.76   1.8496 1.6881 -0.8161 -0.1694 0.066   22  LEU A CA  
201  C C   . LEU A 25  ? 2.7122 1.895  1.6711 -0.8533 -0.2236 0.0467  22  LEU A C   
202  O O   . LEU A 25  ? 2.6757 1.9027 1.7072 -0.8255 -0.3045 0.0854  22  LEU A O   
203  C CB  . LEU A 25  ? 2.7465 1.7835 1.7809 -0.7461 -0.1344 0.0549  22  LEU A CB  
204  C CG  . LEU A 25  ? 2.8017 1.7565 1.8163 -0.7052 -0.0884 0.0746  22  LEU A CG  
205  C CD1 . LEU A 25  ? 2.7935 1.7045 1.9016 -0.6457 -0.0548 0.0576  22  LEU A CD1 
206  C CD2 . LEU A 25  ? 2.8493 1.7778 1.7748 -0.7324 -0.0112 0.0387  22  LEU A CD2 
207  N N   . LYS A 26  ? 2.7105 1.9264 1.6111 -0.9168 -0.1837 -0.0134 23  LYS A N   
208  C CA  . LYS A 26  ? 2.6661 1.9856 1.584  -0.967  -0.235  -0.0379 23  LYS A CA  
209  C C   . LYS A 26  ? 2.6317 1.9623 1.6152 -0.9839 -0.1726 -0.119  23  LYS A C   
210  O O   . LYS A 26  ? 2.6452 2.0003 1.5683 -1.0542 -0.1413 -0.1781 23  LYS A O   
211  C CB  . LYS A 26  ? 2.7214 2.0835 1.4986 -1.0485 -0.2538 -0.0407 23  LYS A CB  
212  C CG  . LYS A 26  ? 2.8107 2.1415 1.4898 -1.0501 -0.2847 0.0306  23  LYS A CG  
213  C CD  . LYS A 26  ? 2.8111 2.2773 1.5124 -1.0143 -0.3002 0.0194  23  LYS A CD  
214  C CE  . LYS A 26  ? 2.8595 2.3405 1.5474 -0.9913 -0.2082 -0.0438 23  LYS A CE  
215  N NZ  . LYS A 26  ? 2.8639 2.3691 1.6128 -0.987  -0.1611 -0.1315 23  LYS A NZ  
216  N N   . GLY A 27  ? 2.5888 1.8977 1.6877 -0.926  -0.1531 -0.1232 24  GLY A N   
217  C CA  . GLY A 27  ? 2.5622 1.8747 1.722  -0.946  -0.091  -0.1932 24  GLY A CA  
218  C C   . GLY A 27  ? 2.6137 1.7916 1.7264 -0.9332 0.0155  -0.2266 24  GLY A C   
219  O O   . GLY A 27  ? 2.6558 1.7871 1.6877 -0.9858 0.0754  -0.2801 24  GLY A O   
220  N N   . VAL A 28  ? 2.6113 1.7213 1.7706 -0.8614 0.0372  -0.1957 25  VAL A N   
221  C CA  . VAL A 28  ? 2.6638 1.6476 1.7816 -0.838  0.1279  -0.2167 25  VAL A CA  
222  C C   . VAL A 28  ? 2.6454 1.6023 1.8263 -0.8415 0.182   -0.2589 25  VAL A C   
223  O O   . VAL A 28  ? 2.597  1.5992 1.8782 -0.8075 0.1597  -0.245  25  VAL A O   
224  C CB  . VAL A 28  ? 2.6947 1.6182 1.8075 -0.7666 0.1246  -0.1601 25  VAL A CB  
225  C CG1 . VAL A 28  ? 2.7524 1.5576 1.8336 -0.7345 0.2102  -0.1786 25  VAL A CG1 
226  C CG2 . VAL A 28  ? 2.7199 1.6628 1.7545 -0.7773 0.0845  -0.1212 25  VAL A CG2 
227  N N   . ASN A 29  ? 2.6865 1.5643 1.8041 -0.8848 0.2556  -0.3123 26  ASN A N   
228  C CA  . ASN A 29  ? 2.6935 1.5193 1.8459 -0.8978 0.3165  -0.3481 26  ASN A CA  
229  C C   . ASN A 29  ? 2.77   1.4348 1.8483 -0.8571 0.3887  -0.3428 26  ASN A C   
230  O O   . ASN A 29  ? 2.8323 1.414  1.8169 -0.8721 0.4271  -0.3662 26  ASN A O   
231  C CB  . ASN A 29  ? 2.6981 1.5563 1.8415 -0.9902 0.3391  -0.4141 26  ASN A CB  
232  C CG  . ASN A 29  ? 2.7064 1.5642 1.9185 -1.0119 0.3815  -0.4417 26  ASN A CG  
233  O OD1 . ASN A 29  ? 2.6351 1.6194 1.9632 -1.0023 0.3414  -0.4348 26  ASN A OD1 
234  N ND2 . ASN A 29  ? 2.7843 1.4967 1.925  -1.0395 0.4647  -0.473  26  ASN A ND2 
235  N N   . LEU A 30  ? 2.76   1.3864 1.8805 -0.7998 0.4026  -0.3116 27  LEU A N   
236  C CA  . LEU A 30  ? 2.8231 1.3096 1.8812 -0.7503 0.4582  -0.2957 27  LEU A CA  
237  C C   . LEU A 30  ? 2.8177 1.2649 1.9172 -0.7332 0.4917  -0.2898 27  LEU A C   
238  O O   . LEU A 30  ? 2.7573 1.3006 1.9475 -0.7212 0.4557  -0.2771 27  LEU A O   
239  C CB  . LEU A 30  ? 2.8175 1.3243 1.8713 -0.685  0.4171  -0.2428 27  LEU A CB  
240  C CG  . LEU A 30  ? 2.8876 1.2882 1.8828 -0.6244 0.4559  -0.2201 27  LEU A CG  
241  C CD1 . LEU A 30  ? 2.8879 1.2632 1.9229 -0.5704 0.4578  -0.1841 27  LEU A CD1 
242  C CD2 . LEU A 30  ? 2.9653 1.2429 1.8753 -0.6385 0.5239  -0.26   27  LEU A CD2 
243  N N   . THR A 31  ? 2.8801 1.185  1.9106 -0.7324 0.5601  -0.2997 28  THR A N   
244  C CA  . THR A 31  ? 2.8893 1.1479 1.9372 -0.7193 0.5947  -0.2877 28  THR A CA  
245  C C   . THR A 31  ? 2.9579 1.0782 1.9289 -0.6552 0.6271  -0.2518 28  THR A C   
246  O O   . THR A 31  ? 3.0151 1.0415 1.9102 -0.6396 0.6482  -0.2556 28  THR A O   
247  C CB  . THR A 31  ? 2.9156 1.1484 1.9601 -0.8006 0.6454  -0.3328 28  THR A CB  
248  O OG1 . THR A 31  ? 3.0245 1.0853 1.9562 -0.8255 0.7059  -0.3502 28  THR A OG1 
249  C CG2 . THR A 31  ? 2.8438 1.2281 1.9669 -0.8687 0.6119  -0.3747 28  THR A CG2 
250  N N   . VAL A 32  ? 2.9474 1.0615 1.9391 -0.6157 0.6296  -0.22   29  VAL A N   
251  C CA  . VAL A 32  ? 3.0117 1.0056 1.9313 -0.5566 0.6547  -0.1828 29  VAL A CA  
252  C C   . VAL A 32  ? 3.0472 0.9634 1.9344 -0.5846 0.7052  -0.1833 29  VAL A C   
253  O O   . VAL A 32  ? 2.9991 1.0022 1.952  -0.605  0.7004  -0.1903 29  VAL A O   
254  C CB  . VAL A 32  ? 2.9885 1.043  1.9414 -0.4846 0.6075  -0.1392 29  VAL A CB  
255  C CG1 . VAL A 32  ? 3.0552 1      1.937  -0.4282 0.6313  -0.1023 29  VAL A CG1 
256  C CG2 . VAL A 32  ? 2.9666 1.0896 1.9354 -0.4677 0.5636  -0.1357 29  VAL A CG2 
257  N N   . GLU A 33  ? 3.1303 0.8816 1.9147 -0.5894 0.7552  -0.1788 30  GLU A N   
258  C CA  . GLU A 33  ? 3.1831 0.8337 1.9089 -0.6262 0.8078  -0.1728 30  GLU A CA  
259  C C   . GLU A 33  ? 3.2221 0.8075 1.8961 -0.559  0.8071  -0.1177 30  GLU A C   
260  O O   . GLU A 33  ? 3.2115 0.8253 1.8969 -0.4838 0.7674  -0.0882 30  GLU A O   
261  C CB  . GLU A 33  ? 3.205  0.8319 1.9513 -0.6452 0.7929  -0.1806 30  GLU A CB  
262  C CG  . GLU A 33  ? 3.1707 0.9338 2.0144 -0.6953 0.7577  -0.2282 30  GLU A CG  
263  C CD  . GLU A 33  ? 3.1907 0.9965 2.1125 -0.692  0.7038  -0.2326 30  GLU A CD  
264  O OE1 . GLU A 33  ? 3.1442 1.0498 2.1336 -0.7487 0.6847  -0.2688 30  GLU A OE1 
265  O OE2 . GLU A 33  ? 3.2435 0.9703 2.1515 -0.6354 0.6847  -0.203  30  GLU A OE2 
266  N N   . GLU A 34  ? 3.2395 0.786  1.8843 -0.5856 0.8338  -0.1019 31  GLU A N   
267  C CA  . GLU A 34  ? 3.2797 0.771  1.8648 -0.5325 0.8321  -0.0505 31  GLU A CA  
268  C C   . GLU A 34  ? 3.3319 0.7222 1.8663 -0.4615 0.8064  -0.0052 31  GLU A C   
269  O O   . GLU A 34  ? 3.3322 0.6983 1.894  -0.4676 0.7902  -0.0097 31  GLU A O   
270  C CB  . GLU A 34  ? 3.2593 0.8359 1.8944 -0.5712 0.8279  -0.0394 31  GLU A CB  
271  C CG  . GLU A 34  ? 3.2105 0.9711 1.9749 -0.6278 0.8215  -0.0882 31  GLU A CG  
272  C CD  . GLU A 34  ? 3.2063 1.1207 2.0578 -0.6387 0.799   -0.0768 31  GLU A CD  
273  O OE1 . GLU A 34  ? 3.1664 1.1786 2.0943 -0.6861 0.7893  -0.0858 31  GLU A OE1 
274  O OE2 . GLU A 34  ? 3.2332 1.1588 2.0617 -0.6027 0.798   -0.0606 31  GLU A OE2 
275  N N   . ASN A 35  ? 3.3703 0.7091 1.8386 -0.3914 0.7995  0.0343  32  ASN A N   
276  C CA  . ASN A 35  ? 3.4116 0.68   1.8456 -0.3087 0.769   0.078   32  ASN A CA  
277  C C   . ASN A 35  ? 3.4128 0.6608 1.8737 -0.2829 0.7606  0.0514  32  ASN A C   
278  O O   . ASN A 35  ? 3.425  0.6275 1.9036 -0.2482 0.736   0.066   32  ASN A O   
279  C CB  . ASN A 35  ? 3.4279 0.6795 1.871  -0.3008 0.7387  0.1269  32  ASN A CB  
280  C CG  . ASN A 35  ? 3.4711 0.7247 1.8918 -0.2189 0.6962  0.186   32  ASN A CG  
281  O OD1 . ASN A 35  ? 3.4848 0.7276 1.9125 -0.2052 0.6641  0.2344  32  ASN A OD1 
282  N ND2 . ASN A 35  ? 3.4859 0.7525 1.8751 -0.1665 0.6948  0.1859  32  ASN A ND2 
283  N N   . GLU A 36  ? 3.387  0.6839 1.8634 -0.3005 0.7743  0.0111  33  GLU A N   
284  C CA  . GLU A 36  ? 3.3876 0.6743 1.8765 -0.2888 0.7757  -0.0232 33  GLU A CA  
285  C C   . GLU A 36  ? 3.3158 0.7408 1.8753 -0.2276 0.7276  -0.0175 33  GLU A C   
286  O O   . GLU A 36  ? 3.2474 0.8161 1.8789 -0.2329 0.6897  -0.0096 33  GLU A O   
287  C CB  . GLU A 36  ? 3.3618 0.7373 1.9238 -0.376  0.775   -0.077  33  GLU A CB  
288  C CG  . GLU A 36  ? 3.3746 0.8318 1.9998 -0.3725 0.7476  -0.1176 33  GLU A CG  
289  C CD  . GLU A 36  ? 3.36   0.9738 2.0956 -0.4464 0.7132  -0.1603 33  GLU A CD  
290  O OE1 . GLU A 36  ? 3.3415 1.0177 2.0861 -0.4882 0.7201  -0.1674 33  GLU A OE1 
291  O OE2 . GLU A 36  ? 3.3594 1.0175 2.1609 -0.4611 0.6825  -0.1879 33  GLU A OE2 
292  N N   . ILE A 37  ? 3.3302 0.7109 1.8695 -0.173  0.7318  -0.0258 34  ILE A N   
293  C CA  . ILE A 37  ? 3.2623 0.7824 1.8664 -0.1299 0.6956  -0.0301 34  ILE A CA  
294  C C   . ILE A 37  ? 3.2414 0.7974 1.8646 -0.1851 0.7088  -0.0871 34  ILE A C   
295  O O   . ILE A 37  ? 3.2968 0.748  1.8715 -0.1783 0.7449  -0.1204 34  ILE A O   
296  C CB  . ILE A 37  ? 3.2884 0.7694 1.8705 -0.0312 0.6922  -0.0086 34  ILE A CB  
297  C CG1 . ILE A 37  ? 3.326  0.7567 1.8714 0.0183  0.6768  0.0507  34  ILE A CG1 
298  C CG2 . ILE A 37  ? 3.214  0.8655 1.87   -0.0029 0.6601  -0.0193 34  ILE A CG2 
299  C CD1 . ILE A 37  ? 3.3502 0.7615 1.884  0.1236  0.6626  0.0778  34  ILE A CD1 
300  N N   . HIS A 38  ? 3.1656 0.8553 1.8512 -0.2433 0.6799  -0.0996 35  HIS A N   
301  C CA  . HIS A 38  ? 3.1392 0.8811 1.8393 -0.3037 0.6822  -0.1484 35  HIS A CA  
302  C C   . HIS A 38  ? 3.0776 0.9596 1.8211 -0.2829 0.6453  -0.1465 35  HIS A C   
303  O O   . HIS A 38  ? 3.0262 1.0212 1.8239 -0.2839 0.5999  -0.1162 35  HIS A O   
304  C CB  . HIS A 38  ? 3.1101 0.9085 1.8494 -0.3832 0.6701  -0.1608 35  HIS A CB  
305  C CG  . HIS A 38  ? 3.1079 0.9571 1.8555 -0.4537 0.6689  -0.2101 35  HIS A CG  
306  N ND1 . HIS A 38  ? 3.0971 0.9995 1.8828 -0.5258 0.6604  -0.2297 35  HIS A ND1 
307  C CD2 . HIS A 38  ? 3.1249 0.9899 1.8472 -0.463  0.6742  -0.245  35  HIS A CD2 
308  C CE1 . HIS A 38  ? 3.091  1.0386 1.8705 -0.5769 0.655   -0.2714 35  HIS A CE1 
309  N NE2 . HIS A 38  ? 3.1147 1.0373 1.8503 -0.5443 0.6649  -0.2829 35  HIS A NE2 
310  N N   . ALA A 39  ? 3.0848 0.9547 1.8002 -0.2671 0.6675  -0.1809 36  ALA A N   
311  C CA  . ALA A 39  ? 3.0299 1.0354 1.7757 -0.2575 0.6417  -0.1832 36  ALA A CA  
312  C C   . ALA A 39  ? 2.9948 1.0848 1.7438 -0.3376 0.6251  -0.2149 36  ALA A C   
313  O O   . ALA A 39  ? 3.0272 1.0596 1.7456 -0.3919 0.6472  -0.2547 36  ALA A O   
314  C CB  . ALA A 39  ? 3.0536 1.0258 1.7741 -0.192  0.6762  -0.2069 36  ALA A CB  
315  N N   . ILE A 40  ? 2.9287 1.1545 1.7089 -0.3499 0.5834  -0.195  37  ILE A N   
316  C CA  . ILE A 40  ? 2.898  1.211  1.6711 -0.4224 0.558   -0.2141 37  ILE A CA  
317  C C   . ILE A 40  ? 2.8772 1.2711 1.6273 -0.4174 0.566   -0.23   37  ILE A C   
318  O O   . ILE A 40  ? 2.8445 1.3133 1.6221 -0.3862 0.5449  -0.1941 37  ILE A O   
319  C CB  . ILE A 40  ? 2.8568 1.2507 1.6814 -0.455  0.4934  -0.1694 37  ILE A CB  
320  C CG1 . ILE A 40  ? 2.8794 1.2124 1.7301 -0.4723 0.4955  -0.1724 37  ILE A CG1 
321  C CG2 . ILE A 40  ? 2.8314 1.3277 1.642  -0.5191 0.4536  -0.1731 37  ILE A CG2 
322  C CD1 . ILE A 40  ? 2.8483 1.2562 1.7616 -0.4937 0.4372  -0.1397 37  ILE A CD1 
323  N N   . ILE A 41  ? 2.8949 1.2751 1.5921 -0.4514 0.6017  -0.2892 38  ILE A N   
324  C CA  . ILE A 41  ? 2.876  1.3433 1.5451 -0.4556 0.6186  -0.316  38  ILE A CA  
325  C C   . ILE A 41  ? 2.8533 1.4198 1.4872 -0.5453 0.5834  -0.321  38  ILE A C   
326  O O   . ILE A 41  ? 2.8656 1.4165 1.4913 -0.6006 0.5568  -0.3234 38  ILE A O   
327  C CB  . ILE A 41  ? 2.922  1.3082 1.5525 -0.4147 0.6909  -0.3852 38  ILE A CB  
328  C CG1 . ILE A 41  ? 2.9914 1.2649 1.5673 -0.4649 0.7214  -0.4425 38  ILE A CG1 
329  C CG2 . ILE A 41  ? 2.9389 1.2533 1.6053 -0.3135 0.7132  -0.3663 38  ILE A CG2 
330  C CD1 . ILE A 41  ? 3.0568 1.2372 1.5817 -0.4349 0.7935  -0.5217 38  ILE A CD1 
331  N N   . GLY A 42  ? 2.8174 1.4927 1.43   -0.5617 0.5814  -0.3204 39  GLY A N   
332  C CA  . GLY A 42  ? 2.8056 1.5738 1.3667 -0.6492 0.546   -0.3179 39  GLY A CA  
333  C C   . GLY A 42  ? 2.7714 1.6605 1.3137 -0.6638 0.5423  -0.2992 39  GLY A C   
334  O O   . GLY A 42  ? 2.7463 1.6661 1.3369 -0.611  0.5458  -0.269  39  GLY A O   
335  N N   . PRO A 43  ? 2.7667 1.7329 1.2334 -0.7438 0.5344  -0.3168 40  PRO A N   
336  C CA  . PRO A 43  ? 2.7366 1.825  1.1717 -0.7753 0.534   -0.2978 40  PRO A CA  
337  C C   . PRO A 43  ? 2.7177 1.8475 1.1777 -0.7939 0.4591  -0.2029 40  PRO A C   
338  O O   . PRO A 43  ? 2.7244 1.791  1.2331 -0.7736 0.4078  -0.1562 40  PRO A O   
339  C CB  . PRO A 43  ? 2.7619 1.9035 1.0925 -0.8647 0.5442  -0.343  40  PRO A CB  
340  C CG  . PRO A 43  ? 2.7934 1.8652 1.1121 -0.8971 0.503   -0.3423 40  PRO A CG  
341  C CD  . PRO A 43  ? 2.7858 1.7393 1.1863 -0.8173 0.5236  -0.3534 40  PRO A CD  
342  N N   . ASN A 44  ? 2.6912 1.9241 1.1179 -0.8332 0.4567  -0.178  41  ASN A N   
343  C CA  . ASN A 44  ? 2.682  1.9392 1.1169 -0.8605 0.3884  -0.0899 41  ASN A CA  
344  C C   . ASN A 44  ? 2.7046 1.9424 1.0792 -0.9304 0.3133  -0.0437 41  ASN A C   
345  O O   . ASN A 44  ? 2.7244 2.0006 1.0132 -0.9952 0.3187  -0.0721 41  ASN A O   
346  C CB  . ASN A 44  ? 2.6703 2.0435 1.0739 -0.899  0.4122  -0.0806 41  ASN A CB  
347  C CG  . ASN A 44  ? 2.6735 2.0825 1.16   -0.8215 0.4666  -0.1099 41  ASN A CG  
348  O OD1 . ASN A 44  ? 2.6799 2.0502 1.2398 -0.7688 0.4408  -0.0703 41  ASN A OD1 
349  N ND2 . ASN A 44  ? 2.657  2.1449 1.1347 -0.8101 0.5417  -0.183  41  ASN A ND2 
350  N N   . GLY A 45  ? 2.6969 1.8771 1.1178 -0.9131 0.2432  0.0229  42  GLY A N   
351  C CA  . GLY A 45  ? 2.7089 1.8701 1.0916 -0.962  0.1615  0.0726  42  GLY A CA  
352  C C   . GLY A 45  ? 2.7008 1.8182 1.112  -0.9472 0.1508  0.0362  42  GLY A C   
353  O O   . GLY A 45  ? 2.71   1.836  1.0889 -0.9901 0.0855  0.0644  42  GLY A O   
354  N N   . ALA A 46  ? 2.6819 1.7534 1.1515 -0.8894 0.212   -0.0248 43  ALA A N   
355  C CA  . ALA A 46  ? 2.6817 1.7094 1.1789 -0.8839 0.2107  -0.0641 43  ALA A CA  
356  C C   . ALA A 46  ? 2.6567 1.64   1.244  -0.8449 0.1525  -0.02   43  ALA A C   
357  O O   . ALA A 46  ? 2.655  1.6312 1.2672 -0.8571 0.1317  -0.0399 43  ALA A O   
358  C CB  . ALA A 46  ? 2.6972 1.673  1.2095 -0.8431 0.2987  -0.142  43  ALA A CB  
359  N N   . GLY A 47  ? 2.6318 1.5932 1.2692 -0.8016 0.1295  0.0326  44  GLY A N   
360  C CA  . GLY A 47  ? 2.6079 1.5284 1.3316 -0.76   0.0808  0.0675  44  GLY A CA  
361  C C   . GLY A 47  ? 2.5907 1.4492 1.3874 -0.6897 0.1284  0.0473  44  GLY A C   
362  O O   . GLY A 47  ? 2.5801 1.4068 1.4488 -0.6574 0.1064  0.0547  44  GLY A O   
363  N N   . LYS A 48  ? 2.583  1.4303 1.3614 -0.664  0.1934  0.0214  45  LYS A N   
364  C CA  . LYS A 48  ? 2.5735 1.3618 1.4034 -0.5966 0.2379  0.0075  45  LYS A CA  
365  C C   . LYS A 48  ? 2.5432 1.3148 1.4281 -0.5626 0.1957  0.0596  45  LYS A C   
366  O O   . LYS A 48  ? 2.5399 1.2621 1.4797 -0.5252 0.1974  0.0566  45  LYS A O   
367  C CB  . LYS A 48  ? 2.6042 1.4044 1.4033 -0.5732 0.3013  -0.0225 45  LYS A CB  
368  C CG  . LYS A 48  ? 2.6821 1.4692 1.4331 -0.5893 0.3581  -0.0889 45  LYS A CG  
369  C CD  . LYS A 48  ? 2.7489 1.5294 1.4924 -0.5392 0.4246  -0.1251 45  LYS A CD  
370  C CE  . LYS A 48  ? 2.7707 1.6463 1.5118 -0.539  0.4202  -0.1001 45  LYS A CE  
371  N NZ  . LYS A 48  ? 2.7968 1.7586 1.4737 -0.6172 0.4043  -0.1002 45  LYS A NZ  
372  N N   . SER A 49  ? 2.522  1.3324 1.3858 -0.5835 0.1593  0.1045  46  SER A N   
373  C CA  . SER A 49  ? 2.5059 1.2922 1.4095 -0.5619 0.1164  0.1513  46  SER A CA  
374  C C   . SER A 49  ? 2.4899 1.2451 1.437  -0.56   0.058   0.1712  46  SER A C   
375  O O   . SER A 49  ? 2.4865 1.1991 1.4944 -0.5163 0.0544  0.1708  46  SER A O   
376  C CB  . SER A 49  ? 2.5185 1.3468 1.3758 -0.6029 0.0898  0.1938  46  SER A CB  
377  O OG  . SER A 49  ? 2.5297 1.4035 1.3747 -0.5918 0.1429  0.1741  46  SER A OG  
378  N N   . THR A 50  ? 2.4741 1.2582 1.3922 -0.6049 0.0139  0.1836  47  THR A N   
379  C CA  . THR A 50  ? 2.4499 1.2241 1.4185 -0.5981 -0.0491 0.2013  47  THR A CA  
380  C C   . THR A 50  ? 2.4163 1.1735 1.4652 -0.5563 -0.019  0.1564  47  THR A C   
381  O O   . THR A 50  ? 2.4034 1.1381 1.524  -0.519  -0.0482 0.1661  47  THR A O   
382  C CB  . THR A 50  ? 2.4616 1.2858 1.3782 -0.6541 -0.0938 0.2129  47  THR A CB  
383  O OG1 . THR A 50  ? 2.4947 1.3268 1.3299 -0.6985 -0.127  0.264   47  THR A OG1 
384  C CG2 . THR A 50  ? 2.4413 1.2759 1.4236 -0.6397 -0.1613 0.2253  47  THR A CG2 
385  N N   . LEU A 51  ? 2.4037 1.1656 1.4362 -0.5642 0.0444  0.1049  48  LEU A N   
386  C CA  . LEU A 51  ? 2.3831 1.1222 1.4735 -0.5395 0.0822  0.0625  48  LEU A CA  
387  C C   . LEU A 51  ? 2.3815 1.0675 1.5115 -0.4853 0.1075  0.0683  48  LEU A C   
388  O O   . LEU A 51  ? 2.3617 1.0399 1.5594 -0.4612 0.1011  0.0589  48  LEU A O   
389  C CB  . LEU A 51  ? 2.4033 1.1309 1.4468 -0.5641 0.1479  0.0099  48  LEU A CB  
390  C CG  . LEU A 51  ? 2.4225 1.1064 1.5047 -0.5495 0.1981  -0.0324 48  LEU A CG  
391  C CD1 . LEU A 51  ? 2.3891 1.1241 1.542  -0.5683 0.1615  -0.0447 48  LEU A CD1 
392  C CD2 . LEU A 51  ? 2.4657 1.1059 1.4867 -0.5704 0.2641  -0.0795 48  LEU A CD2 
393  N N   . ALA A 52  ? 2.3964 1.0587 1.4865 -0.4681 0.1342  0.0818  49  ALA A N   
394  C CA  . ALA A 52  ? 2.4043 1.0231 1.5199 -0.4211 0.1547  0.0883  49  ALA A CA  
395  C C   . ALA A 52  ? 2.3882 1.0006 1.554  -0.4042 0.1     0.1185  49  ALA A C   
396  O O   . ALA A 52  ? 2.3854 0.9674 1.5935 -0.3707 0.1129  0.1076  49  ALA A O   
397  C CB  . ALA A 52  ? 2.4223 1.0413 1.4908 -0.4087 0.1836  0.0979  49  ALA A CB  
398  N N   . TYR A 53  ? 2.3813 1.0143 1.5359 -0.4287 0.0399  0.1553  50  TYR A N   
399  C CA  . TYR A 53  ? 2.3786 0.9847 1.575  -0.4104 -0.0168 0.1848  50  TYR A CA  
400  C C   . TYR A 53  ? 2.347  0.9644 1.6225 -0.3903 -0.0442 0.1665  50  TYR A C   
401  O O   . TYR A 53  ? 2.3371 0.9256 1.669  -0.3545 -0.0664 0.1673  50  TYR A O   
402  C CB  . TYR A 53  ? 2.3968 1.0032 1.5437 -0.4469 -0.0751 0.2363  50  TYR A CB  
403  C CG  . TYR A 53  ? 2.4287 1.042  1.5102 -0.4712 -0.0509 0.2538  50  TYR A CG  
404  C CD1 . TYR A 53  ? 2.4432 1.0425 1.5338 -0.4427 -0.0099 0.2396  50  TYR A CD1 
405  C CD2 . TYR A 53  ? 2.4556 1.1001 1.467  -0.5257 -0.0717 0.285   50  TYR A CD2 
406  C CE1 . TYR A 53  ? 2.4624 1.0913 1.5074 -0.4632 0.0093  0.2523  50  TYR A CE1 
407  C CE2 . TYR A 53  ? 2.476  1.1489 1.4381 -0.5518 -0.0458 0.2956  50  TYR A CE2 
408  C CZ  . TYR A 53  ? 2.4817 1.1526 1.468  -0.5181 -0.0063 0.2779  50  TYR A CZ  
409  O OH  . TYR A 53  ? 2.4988 1.2204 1.4496 -0.5429 0.0161  0.2856  50  TYR A OH  
410  N N   . THR A 54  ? 2.3261 0.9935 1.6088 -0.4145 -0.0436 0.1458  51  THR A N   
411  C CA  . THR A 54  ? 2.2888 0.9969 1.6573 -0.4001 -0.0698 0.1234  51  THR A CA  
412  C C   . THR A 54  ? 2.2729 0.9748 1.6982 -0.3724 -0.01   0.0754  51  THR A C   
413  O O   . THR A 54  ? 2.2382 0.9594 1.7498 -0.3403 -0.0276 0.0592  51  THR A O   
414  C CB  . THR A 54  ? 2.2892 1.0641 1.6414 -0.4453 -0.0876 0.1133  51  THR A CB  
415  O OG1 . THR A 54  ? 2.3278 1.1044 1.6072 -0.4776 -0.139  0.1616  51  THR A OG1 
416  C CG2 . THR A 54  ? 2.237  1.0803 1.6887 -0.4324 -0.126  0.0922  51  THR A CG2 
417  N N   . ILE A 55  ? 2.2993 0.9716 1.6737 -0.3829 0.0607  0.0532  52  ILE A N   
418  C CA  . ILE A 55  ? 2.3012 0.9525 1.7038 -0.3657 0.121   0.0155  52  ILE A CA  
419  C C   . ILE A 55  ? 2.3131 0.9252 1.7385 -0.3224 0.1171  0.0262  52  ILE A C   
420  O O   . ILE A 55  ? 2.2869 0.9117 1.7765 -0.3018 0.1297  -0.0019 52  ILE A O   
421  C CB  . ILE A 55  ? 2.3431 0.9496 1.6698 -0.3839 0.1901  -0.0011 52  ILE A CB  
422  C CG1 . ILE A 55  ? 2.3472 0.9845 1.651  -0.4316 0.1992  -0.0245 52  ILE A CG1 
423  C CG2 . ILE A 55  ? 2.3604 0.9247 1.6933 -0.3689 0.2496  -0.0271 52  ILE A CG2 
424  C CD1 . ILE A 55  ? 2.4072 0.9868 1.6287 -0.4435 0.2558  -0.0369 52  ILE A CD1 
425  N N   . MET A 56  ? 2.3465 0.9205 1.7215 -0.3137 0.0985  0.0626  53  MET A N   
426  C CA  . MET A 56  ? 2.368  0.9018 1.7529 -0.2815 0.0919  0.0708  53  MET A CA  
427  C C   . MET A 56  ? 2.3627 0.8979 1.8195 -0.258  0.0325  0.0751  53  MET A C   
428  O O   . MET A 56  ? 2.3677 0.8713 1.8514 -0.2286 0.035   0.0621  53  MET A O   
429  C CB  . MET A 56  ? 2.4015 0.9067 1.7139 -0.2878 0.0902  0.1045  53  MET A CB  
430  C CG  . MET A 56  ? 2.431  0.8975 1.7383 -0.2632 0.0958  0.1054  53  MET A CG  
431  S SD  . MET A 56  ? 2.4556 0.9029 1.7453 -0.2426 0.1679  0.0725  53  MET A SD  
432  C CE  . MET A 56  ? 2.4105 0.8521 1.7753 -0.2193 0.1641  0.0359  53  MET A CE  
433  N N   . GLY A 57  ? 2.3513 0.9205 1.8369 -0.2683 -0.021  0.0911  54  GLY A N   
434  C CA  . GLY A 57  ? 2.3424 0.9079 1.9004 -0.2364 -0.0844 0.0982  54  GLY A CA  
435  C C   . GLY A 57  ? 2.3927 0.8885 1.9082 -0.2367 -0.1433 0.1493  54  GLY A C   
436  O O   . GLY A 57  ? 2.3933 0.8468 1.9582 -0.2005 -0.1879 0.1531  54  GLY A O   
437  N N   . ILE A 58  ? 2.4341 0.9162 1.8577 -0.2797 -0.1426 0.1865  55  ILE A N   
438  C CA  . ILE A 58  ? 2.4862 0.9063 1.8519 -0.3001 -0.1921 0.2387  55  ILE A CA  
439  C C   . ILE A 58  ? 2.4918 0.8911 1.8793 -0.2943 -0.2756 0.2761  55  ILE A C   
440  O O   . ILE A 58  ? 2.4674 0.9296 1.8759 -0.3011 -0.2951 0.2757  55  ILE A O   
441  C CB  . ILE A 58  ? 2.5193 0.9657 1.7919 -0.3532 -0.1645 0.2615  55  ILE A CB  
442  C CG1 . ILE A 58  ? 2.5349 0.9961 1.7919 -0.3449 -0.0907 0.2288  55  ILE A CG1 
443  C CG2 . ILE A 58  ? 2.5638 0.9646 1.7672 -0.3938 -0.2124 0.3177  55  ILE A CG2 
444  C CD1 . ILE A 58  ? 2.5649 0.9747 1.8373 -0.3178 -0.0819 0.2173  55  ILE A CD1 
445  N N   . SER A 59  ? 2.524  0.8311 1.9079 -0.2795 -0.3271 0.3063  56  SER A N   
446  C CA  . SER A 59  ? 2.5416 0.8064 1.9425 -0.264  -0.4142 0.3487  56  SER A CA  
447  C C   . SER A 59  ? 2.5677 0.8589 1.8828 -0.3235 -0.4523 0.4047  56  SER A C   
448  O O   . SER A 59  ? 2.6003 0.8901 1.8207 -0.3834 -0.4272 0.4286  56  SER A O   
449  C CB  . SER A 59  ? 2.6091 0.7402 1.9985 -0.2452 -0.4582 0.3743  56  SER A CB  
450  O OG  . SER A 59  ? 2.6502 0.7242 2.0647 -0.2143 -0.5464 0.4148  56  SER A OG  
451  N N   . GLY A 60  ? 2.546  0.8759 1.8976 -0.3073 -0.5104 0.4207  57  GLY A N   
452  C CA  . GLY A 60  ? 2.5738 0.9376 1.841  -0.3644 -0.553  0.4717  57  GLY A CA  
453  C C   . GLY A 60  ? 2.5389 1.0314 1.813  -0.3911 -0.5085 0.4311  57  GLY A C   
454  O O   . GLY A 60  ? 2.5323 1.0775 1.7725 -0.4217 -0.5535 0.4566  57  GLY A O   
455  N N   . TYR A 61  ? 2.5193 1.0552 1.8287 -0.3831 -0.421  0.368   58  TYR A N   
456  C CA  . TYR A 61  ? 2.4971 1.1302 1.8102 -0.4085 -0.3661 0.3207  58  TYR A CA  
457  C C   . TYR A 61  ? 2.4448 1.1404 1.882  -0.3616 -0.3654 0.2709  58  TYR A C   
458  O O   . TYR A 61  ? 2.4217 1.1365 1.9075 -0.3439 -0.2962 0.216   58  TYR A O   
459  C CB  . TYR A 61  ? 2.5142 1.142  1.7825 -0.4272 -0.2745 0.2883  58  TYR A CB  
460  C CG  . TYR A 61  ? 2.5698 1.1715 1.7277 -0.478  -0.2707 0.329   58  TYR A CG  
461  C CD1 . TYR A 61  ? 2.5888 1.2449 1.6678 -0.5348 -0.2549 0.3311  58  TYR A CD1 
462  C CD2 . TYR A 61  ? 2.6142 1.1436 1.7465 -0.4752 -0.2823 0.3612  58  TYR A CD2 
463  C CE1 . TYR A 61  ? 2.6338 1.2848 1.6173 -0.5849 -0.2467 0.3631  58  TYR A CE1 
464  C CE2 . TYR A 61  ? 2.6593 1.1823 1.6963 -0.5306 -0.2775 0.3966  58  TYR A CE2 
465  C CZ  . TYR A 61  ? 2.6719 1.2613 1.6371 -0.5846 -0.2592 0.3979  58  TYR A CZ  
466  O OH  . TYR A 61  ? 2.715  1.3168 1.5915 -0.6423 -0.2466 0.4258  58  TYR A OH  
467  N N   . LYS A 62  ? 2.4237 1.1525 1.9117 -0.3413 -0.4465 0.2934  59  LYS A N   
468  C CA  . LYS A 62  ? 2.3631 1.1765 1.9845 -0.2957 -0.4606 0.2489  59  LYS A CA  
469  C C   . LYS A 62  ? 2.3328 1.2644 1.9554 -0.3408 -0.4697 0.2297  59  LYS A C   
470  O O   . LYS A 62  ? 2.3515 1.2993 1.9051 -0.3772 -0.5319 0.2764  59  LYS A O   
471  C CB  . LYS A 62  ? 2.3678 1.1486 2.071  -0.226  -0.5499 0.2795  59  LYS A CB  
472  C CG  . LYS A 62  ? 2.4843 1.1443 2.0945 -0.2314 -0.6234 0.3628  59  LYS A CG  
473  C CD  . LYS A 62  ? 2.546  1.2405 2.0884 -0.2713 -0.7048 0.4222  59  LYS A CD  
474  C CE  . LYS A 62  ? 2.6743 1.2377 2.0965 -0.2964 -0.7642 0.5085  59  LYS A CE  
475  N NZ  . LYS A 62  ? 2.7211 1.1667 2.2    -0.2224 -0.8199 0.5341  59  LYS A NZ  
476  N N   . PRO A 63  ? 2.2855 1.2994 1.9792 -0.3459 -0.4079 0.1604  60  PRO A N   
477  C CA  . PRO A 63  ? 2.2517 1.3788 1.9478 -0.3974 -0.414  0.1338  60  PRO A CA  
478  C C   . PRO A 63  ? 2.193  1.4225 1.9867 -0.368  -0.51   0.1458  60  PRO A C   
479  O O   . PRO A 63  ? 2.1451 1.3967 2.0621 -0.297  -0.5396 0.1354  60  PRO A O   
480  C CB  . PRO A 63  ? 2.231  1.3951 1.9735 -0.4129 -0.3166 0.058   60  PRO A CB  
481  C CG  . PRO A 63  ? 2.2259 1.342  2.0428 -0.3492 -0.2868 0.0424  60  PRO A CG  
482  C CD  . PRO A 63  ? 2.2594 1.264  2.0232 -0.3144 -0.3293 0.1036  60  PRO A CD  
483  N N   . THR A 64  ? 2.1934 1.4895 1.9301 -0.4209 -0.5603 0.166   61  THR A N   
484  C CA  . THR A 64  ? 2.1379 1.5499 1.9527 -0.4027 -0.6604 0.1815  61  THR A CA  
485  C C   . THR A 64  ? 2.054  1.6216 1.9697 -0.4313 -0.6243 0.1015  61  THR A C   
486  O O   . THR A 64  ? 1.9682 1.6511 2.0319 -0.383  -0.6699 0.0789  61  THR A O   
487  C CB  . THR A 64  ? 2.2072 1.6076 1.8882 -0.4536 -0.7378 0.2508  61  THR A CB  
488  O OG1 . THR A 64  ? 2.2669 1.66   1.8194 -0.5435 -0.6681 0.2265  61  THR A OG1 
489  C CG2 . THR A 64  ? 2.2849 1.5442 1.8908 -0.4204 -0.7946 0.3369  61  THR A CG2 
490  N N   . LYS A 65  ? 2.077  1.6456 1.9143 -0.5101 -0.5399 0.0558  62  LYS A N   
491  C CA  . LYS A 65  ? 2.0193 1.7063 1.9222 -0.559  -0.4888 -0.023  62  LYS A CA  
492  C C   . LYS A 65  ? 2.0635 1.6572 1.9225 -0.5848 -0.3619 -0.0715 62  LYS A C   
493  O O   . LYS A 65  ? 2.1493 1.6107 1.8948 -0.5888 -0.3212 -0.0447 62  LYS A O   
494  C CB  . LYS A 65  ? 2.0425 1.8121 1.8657 -0.6447 -0.524  -0.0283 62  LYS A CB  
495  C CG  . LYS A 65  ? 2.0164 1.9359 1.9235 -0.6999 -0.4989 -0.1063 62  LYS A CG  
496  C CD  . LYS A 65  ? 2.0976 2.065  1.8914 -0.799  -0.5124 -0.1212 62  LYS A CD  
497  C CE  . LYS A 65  ? 2.1034 2.1659 1.9388 -0.8773 -0.4511 -0.2101 62  LYS A CE  
498  N NZ  . LYS A 65  ? 2.1916 2.2286 1.8759 -0.9797 -0.4225 -0.2377 62  LYS A NZ  
499  N N   . GLY A 66  ? 2.0003 1.6656 1.9501 -0.6011 -0.3026 -0.1397 63  GLY A N   
500  C CA  . GLY A 66  ? 2.0433 1.6155 1.947  -0.6273 -0.1877 -0.1812 63  GLY A CA  
501  C C   . GLY A 66  ? 2.0359 1.5463 1.9997 -0.5598 -0.1451 -0.1831 63  GLY A C   
502  O O   . GLY A 66  ? 2.0189 1.5248 2.0429 -0.4858 -0.2009 -0.1475 63  GLY A O   
503  N N   . ARG A 67  ? 2.0537 1.5033 1.9894 -0.5872 -0.0455 -0.2241 64  ARG A N   
504  C CA  . ARG A 67  ? 2.0504 1.447  2.0298 -0.5345 0.0023  -0.2317 64  ARG A CA  
505  C C   . ARG A 67  ? 2.1274 1.3708 1.9877 -0.5475 0.0866  -0.227  64  ARG A C   
506  O O   . ARG A 67  ? 2.1762 1.3685 1.9452 -0.6068 0.1332  -0.2421 64  ARG A O   
507  C CB  . ARG A 67  ? 1.9803 1.5052 2.095  -0.5427 0.0328  -0.2942 64  ARG A CB  
508  C CG  . ARG A 67  ? 2.0151 1.572  2.1033 -0.6364 0.1023  -0.3487 64  ARG A CG  
509  C CD  . ARG A 67  ? 1.9593 1.6586 2.1896 -0.6463 0.1326  -0.4094 64  ARG A CD  
510  N NE  . ARG A 67  ? 2.0231 1.682  2.2023 -0.7265 0.235   -0.4554 64  ARG A NE  
511  C CZ  . ARG A 67  ? 1.9974 1.762  2.2146 -0.8125 0.2605  -0.5093 64  ARG A CZ  
512  N NH1 . ARG A 67  ? 1.9033 1.8375 2.2153 -0.8275 0.1878  -0.526  64  ARG A NH1 
513  N NH2 . ARG A 67  ? 2.0397 1.7364 2.1926 -0.8886 0.356   -0.5444 64  ARG A NH2 
514  N N   . ILE A 68  ? 2.1345 1.3039 1.9965 -0.4892 0.1035  -0.2078 65  ILE A N   
515  C CA  . ILE A 68  ? 2.2006 1.2363 1.9616 -0.4889 0.1748  -0.1991 65  ILE A CA  
516  C C   . ILE A 68  ? 2.1673 1.2105 1.9802 -0.48   0.2364  -0.2368 65  ILE A C   
517  O O   . ILE A 68  ? 2.1284 1.2117 2.0251 -0.4284 0.2145  -0.241  65  ILE A O   
518  C CB  . ILE A 68  ? 2.2541 1.1993 1.9529 -0.4397 0.1419  -0.1428 65  ILE A CB  
519  C CG1 . ILE A 68  ? 2.2853 1.2317 1.9246 -0.4586 0.0851  -0.1055 65  ILE A CG1 
520  C CG2 . ILE A 68  ? 2.328  1.1565 1.9343 -0.4352 0.2109  -0.136  65  ILE A CG2 
521  C CD1 . ILE A 68  ? 2.3443 1.22   1.9266 -0.4243 0.0497  -0.0506 65  ILE A CD1 
522  N N   . ILE A 69  ? 2.1834 1.1848 1.943  -0.5331 0.314   -0.2664 66  ILE A N   
523  C CA  . ILE A 69  ? 2.1648 1.1701 1.9528 -0.5405 0.3802  -0.3006 66  ILE A CA  
524  C C   . ILE A 69  ? 2.2437 1.097  1.9093 -0.5303 0.4341  -0.2736 66  ILE A C   
525  O O   . ILE A 69  ? 2.3108 1.067  1.8722 -0.5582 0.4602  -0.2584 66  ILE A O   
526  C CB  . ILE A 69  ? 2.1415 1.2175 1.9594 -0.6207 0.4275  -0.3537 66  ILE A CB  
527  C CG1 . ILE A 69  ? 2.0556 1.3044 2.001  -0.6316 0.3649  -0.3807 66  ILE A CG1 
528  C CG2 . ILE A 69  ? 2.1436 1.2228 1.9762 -0.6424 0.5043  -0.3883 66  ILE A CG2 
529  C CD1 . ILE A 69  ? 2.0862 1.3459 1.9843 -0.7008 0.3547  -0.3903 66  ILE A CD1 
530  N N   . PHE A 70  ? 2.2364 1.0697 1.9133 -0.4873 0.4482  -0.2692 67  PHE A N   
531  C CA  . PHE A 70  ? 2.3162 1.0187 1.879  -0.4745 0.4922  -0.2413 67  PHE A CA  
532  C C   . PHE A 70  ? 2.3002 1.0154 1.8739 -0.4927 0.5552  -0.2743 67  PHE A C   
533  O O   . PHE A 70  ? 2.2372 1.0472 1.9112 -0.4681 0.5445  -0.3046 67  PHE A O   
534  C CB  . PHE A 70  ? 2.3384 1.0001 1.8828 -0.409  0.4426  -0.1991 67  PHE A CB  
535  C CG  . PHE A 70  ? 2.4253 0.9712 1.8576 -0.3921 0.4769  -0.1682 67  PHE A CG  
536  C CD1 . PHE A 70  ? 2.5035 0.9554 1.8328 -0.407  0.5013  -0.1432 67  PHE A CD1 
537  C CD2 . PHE A 70  ? 2.4388 0.9726 1.8699 -0.3575 0.4806  -0.1659 67  PHE A CD2 
538  C CE1 . PHE A 70  ? 2.5761 0.9317 1.81   -0.3828 0.5247  -0.1118 67  PHE A CE1 
539  C CE2 . PHE A 70  ? 2.5143 0.9542 1.8409 -0.3429 0.5043  -0.1353 67  PHE A CE2 
540  C CZ  . PHE A 70  ? 2.5725 0.9278 1.8046 -0.3527 0.5234  -0.1057 67  PHE A CZ  
541  N N   . LYS A 71  ? 2.356  0.9743 1.825  -0.5371 0.622   -0.2705 68  LYS A N   
542  C CA  . LYS A 71  ? 2.3594 0.9756 1.8092 -0.571  0.6907  -0.2967 68  LYS A CA  
543  C C   . LYS A 71  ? 2.2644 1.0372 1.8424 -0.6126 0.71    -0.3601 68  LYS A C   
544  O O   . LYS A 71  ? 2.227  1.0683 1.8558 -0.608  0.7396  -0.3932 68  LYS A O   
545  C CB  . LYS A 71  ? 2.3955 0.9775 1.8136 -0.5186 0.6902  -0.2789 68  LYS A CB  
546  C CG  . LYS A 71  ? 2.5254 0.9623 1.809  -0.4899 0.6851  -0.22   68  LYS A CG  
547  C CD  . LYS A 71  ? 2.5892 1.0069 1.8399 -0.4496 0.6847  -0.2084 68  LYS A CD  
548  C CE  . LYS A 71  ? 2.7248 1.0083 1.8319 -0.4357 0.6967  -0.1551 68  LYS A CE  
549  N NZ  . LYS A 71  ? 2.7693 1.0439 1.8353 -0.4096 0.7001  -0.149  68  LYS A NZ  
550  N N   . GLY A 72  ? 2.218  1.0587 1.8518 -0.6521 0.6918  -0.3808 69  GLY A N   
551  C CA  . GLY A 72  ? 2.1183 1.1303 1.8855 -0.695  0.7028  -0.4425 69  GLY A CA  
552  C C   . GLY A 72  ? 2.0117 1.1799 1.9409 -0.6285 0.6376  -0.4657 69  GLY A C   
553  O O   . GLY A 72  ? 1.9123 1.246  1.9738 -0.6508 0.6349  -0.5179 69  GLY A O   
554  N N   . VAL A 73  ? 2.0292 1.1467 1.952  -0.5464 0.5828  -0.428  70  VAL A N   
555  C CA  . VAL A 73  ? 1.9501 1.1778 2.0113 -0.4745 0.5162  -0.4426 70  VAL A CA  
556  C C   . VAL A 73  ? 1.9517 1.1718 2.0226 -0.4425 0.426   -0.3999 70  VAL A C   
557  O O   . VAL A 73  ? 2.0328 1.1274 1.9883 -0.4382 0.411   -0.348  70  VAL A O   
558  C CB  . VAL A 73  ? 1.9829 1.1528 2.0272 -0.4123 0.5222  -0.4369 70  VAL A CB  
559  C CG1 . VAL A 73  ? 1.9148 1.1724 2.0976 -0.333  0.4538  -0.4542 70  VAL A CG1 
560  C CG2 . VAL A 73  ? 1.9957 1.1726 2.0111 -0.4516 0.6146  -0.478  70  VAL A CG2 
561  N N   . ASP A 74  ? 1.8581 1.2188 2.0651 -0.4205 0.3653  -0.421  71  ASP A N   
562  C CA  . ASP A 74  ? 1.8613 1.219  2.0724 -0.3915 0.2731  -0.3761 71  ASP A CA  
563  C C   . ASP A 74  ? 1.888  1.1711 2.0979 -0.309  0.2243  -0.3404 71  ASP A C   
564  O O   . ASP A 74  ? 1.8327 1.1789 2.1529 -0.2519 0.206   -0.369  71  ASP A O   
565  C CB  . ASP A 74  ? 1.7708 1.3067 2.1258 -0.393  0.2174  -0.4068 71  ASP A CB  
566  C CG  . ASP A 74  ? 1.8213 1.3573 2.1545 -0.3867 0.1263  -0.3582 71  ASP A CG  
567  O OD1 . ASP A 74  ? 1.9021 1.3085 2.1319 -0.3644 0.0975  -0.3007 71  ASP A OD1 
568  O OD2 . ASP A 74  ? 1.7725 1.4469 2.1897 -0.4092 0.0843  -0.3785 71  ASP A OD2 
569  N N   . ILE A 75  ? 1.9694 1.1183 2.0552 -0.305  0.2073  -0.2829 72  ILE A N   
570  C CA  . ILE A 75  ? 2.0066 1.069  2.069  -0.244  0.1669  -0.2466 72  ILE A CA  
571  C C   . ILE A 75  ? 1.9908 1.0669 2.095  -0.2046 0.0656  -0.2065 72  ILE A C   
572  O O   . ILE A 75  ? 2.0408 1.0211 2.0925 -0.1732 0.0278  -0.1631 72  ILE A O   
573  C CB  . ILE A 75  ? 2.1044 1.0299 2.0173 -0.2626 0.2035  -0.2079 72  ILE A CB  
574  C CG1 . ILE A 75  ? 2.1519 1.0431 1.9785 -0.3024 0.1842  -0.1682 72  ILE A CG1 
575  C CG2 . ILE A 75  ? 2.1338 1.0338 2.0016 -0.2927 0.2953  -0.2407 72  ILE A CG2 
576  C CD1 . ILE A 75  ? 2.2465 1.0228 1.9437 -0.3112 0.2144  -0.1327 72  ILE A CD1 
577  N N   . ILE A 76  ? 1.9177 1.1141 2.1169 -0.2074 0.0191  -0.2207 73  ILE A N   
578  C CA  . ILE A 76  ? 1.9025 1.1184 2.1403 -0.1708 -0.0845 -0.1784 73  ILE A CA  
579  C C   . ILE A 76  ? 1.9065 1.0598 2.1919 -0.0896 -0.1311 -0.1642 73  ILE A C   
580  O O   . ILE A 76  ? 1.9518 1.0217 2.1857 -0.0696 -0.2004 -0.1045 73  ILE A O   
581  C CB  . ILE A 76  ? 1.8169 1.2016 2.1702 -0.1832 -0.123  -0.208  73  ILE A CB  
582  C CG1 . ILE A 76  ? 1.8516 1.2558 2.1175 -0.2628 -0.1261 -0.1895 73  ILE A CG1 
583  C CG2 . ILE A 76  ? 1.7673 1.2095 2.2344 -0.1075 -0.2269 -0.1894 73  ILE A CG2 
584  C CD1 . ILE A 76  ? 1.7738 1.3537 2.1426 -0.2936 -0.1521 -0.2282 73  ILE A CD1 
585  N N   . ASP A 77  ? 1.8643 1.0497 2.238  -0.0492 -0.089  -0.2211 74  ASP A N   
586  C CA  . ASP A 77  ? 1.8742 0.9961 2.299  0.0296  -0.1266 -0.222  74  ASP A CA  
587  C C   . ASP A 77  ? 1.9489 0.9381 2.2775 0.0287  -0.0728 -0.2222 74  ASP A C   
588  O O   . ASP A 77  ? 1.9575 0.8913 2.3256 0.0869  -0.0877 -0.2391 74  ASP A O   
589  C CB  . ASP A 77  ? 1.7942 1.0501 2.3996 0.0904  -0.1281 -0.2925 74  ASP A CB  
590  C CG  . ASP A 77  ? 1.7555 1.1877 2.4716 0.0788  -0.1598 -0.3121 74  ASP A CG  
591  O OD1 . ASP A 77  ? 1.7385 1.2553 2.4405 0.0062  -0.0964 -0.342  74  ASP A OD1 
592  O OD2 . ASP A 77  ? 1.7351 1.2179 2.5497 0.141   -0.2502 -0.297  74  ASP A OD2 
593  N N   . LYS A 78  ? 1.9989 0.9367 2.2028 -0.0344 -0.0134 -0.2054 75  LYS A N   
594  C CA  . LYS A 78  ? 2.0651 0.8937 2.1741 -0.0389 0.0325  -0.2022 75  LYS A CA  
595  C C   . LYS A 78  ? 2.1365 0.8459 2.1372 -0.0472 -0.0157 -0.1326 75  LYS A C   
596  O O   . LYS A 78  ? 2.1584 0.8676 2.102  -0.0839 -0.0408 -0.0875 75  LYS A O   
597  C CB  . LYS A 78  ? 2.1047 0.9458 2.1443 -0.0943 0.1236  -0.2243 75  LYS A CB  
598  C CG  . LYS A 78  ? 2.1097 1.0174 2.2179 -0.0859 0.1906  -0.2964 75  LYS A CG  
599  C CD  . LYS A 78  ? 2.1522 1.1237 2.2414 -0.1483 0.2625  -0.3218 75  LYS A CD  
600  C CE  . LYS A 78  ? 2.1516 1.2031 2.3085 -0.1503 0.3319  -0.3942 75  LYS A CE  
601  N NZ  . LYS A 78  ? 2.1084 1.2331 2.4086 -0.0815 0.298   -0.4405 75  LYS A NZ  
602  N N   . ASN A 79  ? 2.1665 0.7799 2.1383 -0.0188 -0.0266 -0.1282 76  ASN A N   
603  C CA  . ASN A 79  ? 2.2263 0.732  2.0968 -0.0357 -0.0681 -0.0662 76  ASN A CA  
604  C C   . ASN A 79  ? 2.261  0.7353 2.015  -0.0833 -0.0113 -0.0513 76  ASN A C   
605  O O   . ASN A 79  ? 2.2523 0.7665 1.9984 -0.0971 0.0565  -0.0862 76  ASN A O   
606  C CB  . ASN A 79  ? 2.2626 0.6737 2.1535 0.0092  -0.1119 -0.0682 76  ASN A CB  
607  C CG  . ASN A 79  ? 2.3099 0.6926 2.2015 0.0263  -0.0561 -0.1249 76  ASN A CG  
608  O OD1 . ASN A 79  ? 2.3375 0.7417 2.1724 -0.0057 0.011   -0.1429 76  ASN A OD1 
609  N ND2 . ASN A 79  ? 2.3158 0.6415 2.2647 0.0779  -0.0845 -0.1543 76  ASN A ND2 
610  N N   . ILE A 80  ? 2.297  0.7028 1.9616 -0.1084 -0.0394 0.0008  77  ILE A N   
611  C CA  . ILE A 80  ? 2.3253 0.7148 1.8915 -0.1443 0.0047  0.0171  77  ILE A CA  
612  C C   . ILE A 80  ? 2.3198 0.6982 1.8696 -0.1344 0.0638  -0.0244 77  ILE A C   
613  O O   . ILE A 80  ? 2.3292 0.7327 1.8365 -0.152  0.1182  -0.0316 77  ILE A O   
614  C CB  . ILE A 80  ? 2.3777 0.7099 1.869  -0.1706 -0.0376 0.071   77  ILE A CB  
615  C CG1 . ILE A 80  ? 2.3899 0.7317 1.8815 -0.188  -0.095  0.1151  77  ILE A CG1 
616  C CG2 . ILE A 80  ? 2.4071 0.7499 1.8147 -0.2004 0.0049  0.0851  77  ILE A CG2 
617  C CD1 . ILE A 80  ? 2.4484 0.7258 1.8799 -0.2142 -0.1433 0.1643  77  ILE A CD1 
618  N N   . THR A 81  ? 2.3053 0.6412 1.8851 -0.1062 0.0534  -0.0538 78  THR A N   
619  C CA  . THR A 81  ? 2.3028 0.6302 1.8607 -0.1003 0.1068  -0.0982 78  THR A CA  
620  C C   . THR A 81  ? 2.2468 0.6457 1.8469 -0.0972 0.1685  -0.1439 78  THR A C   
621  O O   . THR A 81  ? 2.268  0.6717 1.8042 -0.1175 0.2237  -0.1524 78  THR A O   
622  C CB  . THR A 81  ? 2.3296 0.5958 1.9188 -0.0706 0.0817  -0.1303 78  THR A CB  
623  O OG1 . THR A 81  ? 2.3874 0.5773 1.9176 -0.0894 0.0322  -0.0866 78  THR A OG1 
624  C CG2 . THR A 81  ? 2.3419 0.6091 1.909  -0.0669 0.1394  -0.1863 78  THR A CG2 
625  N N   . GLU A 82  ? 2.1744 0.6316 1.8785 -0.0756 0.157   -0.1702 79  GLU A N   
626  C CA  . GLU A 82  ? 2.1198 0.6608 1.8761 -0.0821 0.2151  -0.2177 79  GLU A CA  
627  C C   . GLU A 82  ? 2.1241 0.6861 1.8177 -0.1282 0.2522  -0.1919 79  GLU A C   
628  O O   . GLU A 82  ? 2.13   0.7119 1.7957 -0.1517 0.3181  -0.2185 79  GLU A O   
629  C CB  . GLU A 82  ? 2.0708 0.6886 1.9669 -0.0464 0.1853  -0.2523 79  GLU A CB  
630  C CG  . GLU A 82  ? 2.1035 0.7062 2.0728 0.0071  0.1739  -0.302  79  GLU A CG  
631  C CD  . GLU A 82  ? 2.1098 0.7664 2.2197 0.0619  0.1179  -0.3217 79  GLU A CD  
632  O OE1 . GLU A 82  ? 2.0994 0.7866 2.2339 0.057   0.0665  -0.2796 79  GLU A OE1 
633  O OE2 . GLU A 82  ? 2.1092 0.779  2.304  0.1127  0.1237  -0.3809 79  GLU A OE2 
634  N N   . ARG A 83  ? 2.1256 0.6728 1.7861 -0.1441 0.213   -0.1408 80  ARG A N   
635  C CA  . ARG A 83  ? 2.1368 0.6865 1.7313 -0.1836 0.2466  -0.1191 80  ARG A CA  
636  C C   . ARG A 83  ? 2.1937 0.679  1.6773 -0.1939 0.2832  -0.0978 80  ARG A C   
637  O O   . ARG A 83  ? 2.2145 0.6886 1.6451 -0.2173 0.3348  -0.0994 80  ARG A O   
638  C CB  . ARG A 83  ? 2.1389 0.6949 1.7256 -0.1965 0.1961  -0.0779 80  ARG A CB  
639  C CG  . ARG A 83  ? 2.0955 0.7217 1.7842 -0.1873 0.1524  -0.0923 80  ARG A CG  
640  C CD  . ARG A 83  ? 2.1167 0.7521 1.7803 -0.2094 0.1046  -0.0513 80  ARG A CD  
641  N NE  . ARG A 83  ? 2.0778 0.7711 1.8335 -0.1905 0.0414  -0.0529 80  ARG A NE  
642  C CZ  . ARG A 83  ? 2.0757 0.8179 1.8372 -0.2151 0.0039  -0.0352 80  ARG A CZ  
643  N NH1 . ARG A 83  ? 2.0958 0.8321 1.7764 -0.2617 0.0298  -0.0217 80  ARG A NH1 
644  N NH2 . ARG A 83  ? 2.027  0.8247 1.8742 -0.1907 -0.0614 -0.0329 80  ARG A NH2 
645  N N   . ALA A 84  ? 2.2191 0.6596 1.6656 -0.1775 0.2544  -0.0774 81  ALA A N   
646  C CA  . ALA A 84  ? 2.2697 0.6667 1.6194 -0.1827 0.2796  -0.0575 81  ALA A CA  
647  C C   . ALA A 84  ? 2.2817 0.6721 1.606  -0.1839 0.3346  -0.0929 81  ALA A C   
648  O O   . ALA A 84  ? 2.32   0.6818 1.5605 -0.1948 0.3705  -0.0763 81  ALA A O   
649  C CB  . ALA A 84  ? 2.29   0.6574 1.6144 -0.1745 0.2323  -0.032  81  ALA A CB  
650  N N   . ARG A 85  ? 2.2474 0.6656 1.6424 -0.1718 0.3423  -0.1424 82  ARG A N   
651  C CA  . ARG A 85  ? 2.2562 0.683  1.6302 -0.1802 0.4016  -0.1855 82  ARG A CA  
652  C C   . ARG A 85  ? 2.25   0.7059 1.6182 -0.2126 0.4618  -0.1996 82  ARG A C   
653  O O   . ARG A 85  ? 2.2688 0.7216 1.5881 -0.2335 0.5186  -0.2229 82  ARG A O   
654  C CB  . ARG A 85  ? 2.2364 0.6898 1.6928 -0.1543 0.395   -0.2426 82  ARG A CB  
655  C CG  . ARG A 85  ? 2.3117 0.7079 1.7309 -0.1372 0.3562  -0.2359 82  ARG A CG  
656  C CD  . ARG A 85  ? 2.3307 0.7352 1.8194 -0.1097 0.3597  -0.3022 82  ARG A CD  
657  N NE  . ARG A 85  ? 2.3948 0.7316 1.8738 -0.092  0.3068  -0.2975 82  ARG A NE  
658  C CZ  . ARG A 85  ? 2.4704 0.7617 1.8652 -0.1058 0.3131  -0.3062 82  ARG A CZ  
659  N NH1 . ARG A 85  ? 2.4913 0.7978 1.7964 -0.1333 0.3646  -0.311  82  ARG A NH1 
660  N NH2 . ARG A 85  ? 2.4982 0.7231 1.8877 -0.0978 0.2643  -0.3055 82  ARG A NH2 
661  N N   . MET A 86  ? 2.2247 0.7047 1.6325 -0.2244 0.4501  -0.1854 83  MET A N   
662  C CA  . MET A 86  ? 2.2255 0.7192 1.6194 -0.2651 0.5017  -0.1942 83  MET A CA  
663  C C   . MET A 86  ? 2.2983 0.7043 1.5665 -0.2811 0.5208  -0.1442 83  MET A C   
664  O O   . MET A 86  ? 2.3246 0.7047 1.548  -0.3179 0.5708  -0.1468 83  MET A O   
665  C CB  . MET A 86  ? 2.1764 0.736  1.6664 -0.2724 0.4728  -0.2041 83  MET A CB  
666  C CG  . MET A 86  ? 2.1398 0.7895 1.715  -0.3004 0.5124  -0.2592 83  MET A CG  
667  S SD  . MET A 86  ? 2.0892 0.8524 1.8294 -0.267  0.4444  -0.2854 83  MET A SD  
668  C CE  . MET A 86  ? 2.0503 0.8375 1.8569 -0.2149 0.4415  -0.329  83  MET A CE  
669  N N   . GLY A 87  ? 2.3268 0.6891 1.544  -0.2539 0.481   -0.1012 84  GLY A N   
670  C CA  . GLY A 87  ? 2.3877 0.6787 1.5021 -0.253  0.4919  -0.0564 84  GLY A CA  
671  C C   . GLY A 87  ? 2.3838 0.6723 1.5059 -0.2456 0.4587  -0.0288 84  GLY A C   
672  O O   . GLY A 87  ? 2.4285 0.6618 1.4822 -0.2449 0.4769  -0.0036 84  GLY A O   
673  N N   . MET A 88  ? 2.3321 0.6751 1.5317 -0.2392 0.4102  -0.0336 85  MET A N   
674  C CA  . MET A 88  ? 2.3281 0.6796 1.5298 -0.2405 0.3792  -0.0102 85  MET A CA  
675  C C   . MET A 88  ? 2.3305 0.6916 1.5248 -0.2189 0.3297  0.0198  85  MET A C   
676  O O   . MET A 88  ? 2.3138 0.6911 1.5467 -0.2097 0.2996  0.0128  85  MET A O   
677  C CB  . MET A 88  ? 2.2841 0.694  1.569  -0.2606 0.3578  -0.0331 85  MET A CB  
678  C CG  . MET A 88  ? 2.2983 0.7261 1.5808 -0.2695 0.3214  -0.0113 85  MET A CG  
679  S SD  . MET A 88  ? 2.2805 0.7863 1.6611 -0.2826 0.2678  -0.0255 85  MET A SD  
680  C CE  . MET A 88  ? 2.2264 0.7638 1.6444 -0.3153 0.3176  -0.0726 85  MET A CE  
681  N N   . THR A 89  ? 2.3505 0.7028 1.4976 -0.2128 0.3232  0.0489  86  THR A N   
682  C CA  . THR A 89  ? 2.3526 0.7307 1.4951 -0.2045 0.2789  0.0758  86  THR A CA  
683  C C   . THR A 89  ? 2.3473 0.7535 1.4791 -0.2153 0.266   0.0934  86  THR A C   
684  O O   . THR A 89  ? 2.3613 0.7545 1.4779 -0.2218 0.2957  0.0831  86  THR A O   
685  C CB  . THR A 89  ? 2.3959 0.7605 1.4899 -0.1833 0.2834  0.09    86  THR A CB  
686  O OG1 . THR A 89  ? 2.393  0.7869 1.502  -0.1892 0.237   0.1033  86  THR A OG1 
687  C CG2 . THR A 89  ? 2.4271 0.7809 1.4646 -0.1627 0.3068  0.1101  86  THR A CG2 
688  N N   . LEU A 90  ? 2.3264 0.7693 1.4612 -0.2239 0.2249  0.1162  87  LEU A N   
689  C CA  . LEU A 90  ? 2.316  0.7995 1.438  -0.2429 0.2135  0.1304  87  LEU A CA  
690  C C   . LEU A 90  ? 2.3138 0.8412 1.4095 -0.2383 0.2038  0.1525  87  LEU A C   
691  O O   . LEU A 90  ? 2.3133 0.8422 1.41   -0.2349 0.1838  0.162   87  LEU A O   
692  C CB  . LEU A 90  ? 2.2983 0.7963 1.4536 -0.2744 0.1673  0.1379  87  LEU A CB  
693  C CG  . LEU A 90  ? 2.3049 0.8464 1.4386 -0.3085 0.1448  0.1574  87  LEU A CG  
694  C CD1 . LEU A 90  ? 2.3114 0.8675 1.4228 -0.3147 0.1823  0.1374  87  LEU A CD1 
695  C CD2 . LEU A 90  ? 2.3066 0.844  1.4641 -0.3346 0.0889  0.1751  87  LEU A CD2 
696  N N   . ALA A 91  ? 2.3077 0.8793 1.3831 -0.2405 0.2202  0.1544  88  ALA A N   
697  C CA  . ALA A 91  ? 2.297  0.9403 1.3611 -0.2372 0.2161  0.1685  88  ALA A CA  
698  C C   . ALA A 91  ? 2.2848 0.9908 1.3487 -0.2907 0.1816  0.1873  88  ALA A C   
699  O O   . ALA A 91  ? 2.2687 1.0299 1.3325 -0.303  0.1652  0.2019  88  ALA A O   
700  C CB  . ALA A 91  ? 2.2968 0.959  1.3449 -0.2003 0.259   0.1537  88  ALA A CB  
701  N N   . TRP A 92  ? 2.2892 0.991  1.3461 -0.3272 0.1707  0.1881  89  TRP A N   
702  C CA  . TRP A 92  ? 2.2887 1.028  1.3279 -0.3863 0.1342  0.2135  89  TRP A CA  
703  C C   . TRP A 92  ? 2.2753 1.1025 1.285  -0.4174 0.155   0.2101  89  TRP A C   
704  O O   . TRP A 92  ? 2.2798 1.117  1.2599 -0.4683 0.134   0.2242  89  TRP A O   
705  C CB  . TRP A 92  ? 2.2877 1.0229 1.3292 -0.4091 0.0953  0.2402  89  TRP A CB  
706  C CG  . TRP A 92  ? 2.3159 0.9721 1.3641 -0.4279 0.0474  0.2585  89  TRP A CG  
707  C CD1 . TRP A 92  ? 2.3412 0.9822 1.3648 -0.4762 0.0067  0.2878  89  TRP A CD1 
708  C CD2 . TRP A 92  ? 2.3281 0.9104 1.4117 -0.3917 0.0375  0.2454  89  TRP A CD2 
709  N NE1 . TRP A 92  ? 2.3642 0.9224 1.4128 -0.4642 -0.0342 0.2962  89  TRP A NE1 
710  C CE2 . TRP A 92  ? 2.3548 0.8827 1.4459 -0.4122 -0.0124 0.2654  89  TRP A CE2 
711  C CE3 . TRP A 92  ? 2.3339 0.8926 1.4399 -0.3448 0.0657  0.2191  89  TRP A CE3 
712  C CZ2 . TRP A 92  ? 2.3699 0.8315 1.5049 -0.3804 -0.0314 0.2521  89  TRP A CZ2 
713  C CZ3 . TRP A 92  ? 2.3554 0.8504 1.4944 -0.3244 0.0515  0.2057  89  TRP A CZ3 
714  C CH2 . TRP A 92  ? 2.365  0.8173 1.5258 -0.3386 0.005   0.2182  89  TRP A CH2 
715  N N   . GLN A 93  ? 2.2555 1.1517 1.2726 -0.3886 0.1917  0.193   90  GLN A N   
716  C CA  . GLN A 93  ? 2.2365 1.2389 1.239  -0.4099 0.2198  0.1797  90  GLN A CA  
717  C C   . GLN A 93  ? 2.2227 1.3113 1.2308 -0.448  0.1998  0.2023  90  GLN A C   
718  O O   . GLN A 93  ? 2.1866 1.3754 1.2202 -0.4244 0.2262  0.1859  90  GLN A O   
719  C CB  . GLN A 93  ? 2.2561 1.2668 1.2156 -0.4627 0.2216  0.1749  90  GLN A CB  
720  C CG  . GLN A 93  ? 2.2535 1.3394 1.2023 -0.4509 0.2766  0.1327  90  GLN A CG  
721  C CD  . GLN A 93  ? 2.2544 1.4506 1.1691 -0.5195 0.281   0.1369  90  GLN A CD  
722  O OE1 . GLN A 93  ? 2.2822 1.4727 1.1574 -0.5905 0.2396  0.1757  90  GLN A OE1 
723  N NE2 . GLN A 93  ? 2.2155 1.513  1.1424 -0.4994 0.3324  0.0966  90  GLN A NE2 
724  N N   . GLU A 94  ? 2.247  1.2944 1.2343 -0.5054 0.1514  0.2391  91  GLU A N   
725  C CA  . GLU A 94  ? 2.2389 1.3418 1.223  -0.5552 0.1277  0.2627  91  GLU A CA  
726  C C   . GLU A 94  ? 2.2666 1.2762 1.2674 -0.5354 0.0923  0.2761  91  GLU A C   
727  O O   . GLU A 94  ? 2.3068 1.223  1.2856 -0.5694 0.0506  0.3021  91  GLU A O   
728  C CB  . GLU A 94  ? 2.2932 1.3977 1.2204 -0.6479 0.0997  0.2967  91  GLU A CB  
729  C CG  . GLU A 94  ? 2.3257 1.5762 1.2357 -0.7011 0.131   0.2888  91  GLU A CG  
730  C CD  . GLU A 94  ? 2.4112 1.711  1.3017 -0.6944 0.1725  0.2594  91  GLU A CD  
731  O OE1 . GLU A 94  ? 2.4704 1.704  1.3081 -0.7296 0.1521  0.2773  91  GLU A OE1 
732  O OE2 . GLU A 94  ? 2.3969 1.8011 1.3247 -0.6516 0.2233  0.2166  91  GLU A OE2 
733  N N   . PRO A 95  ? 2.2481 1.2731 1.284  -0.4769 0.1066  0.2575  92  PRO A N   
734  C CA  . PRO A 95  ? 2.278  1.2146 1.3204 -0.462  0.0779  0.263   92  PRO A CA  
735  C C   . PRO A 95  ? 2.2982 1.2246 1.3204 -0.5324 0.037   0.2866  92  PRO A C   
736  O O   . PRO A 95  ? 2.2707 1.3002 1.2886 -0.5792 0.0389  0.2926  92  PRO A O   
737  C CB  . PRO A 95  ? 2.2598 1.2425 1.3279 -0.3965 0.1028  0.2424  92  PRO A CB  
738  C CG  . PRO A 95  ? 2.2418 1.2819 1.3207 -0.3555 0.1454  0.2245  92  PRO A CG  
739  C CD  . PRO A 95  ? 2.2006 1.3174 1.267  -0.418  0.1472  0.231   92  PRO A CD  
740  N N   . ALA A 96  ? 2.3448 1.1458 1.3549 -0.5438 0.0013  0.2982  93  ALA A N   
741  C CA  . ALA A 96  ? 2.3789 1.1273 1.3601 -0.6106 -0.0408 0.321   93  ALA A CA  
742  C C   . ALA A 96  ? 2.3619 1.173  1.3469 -0.6316 -0.0423 0.3096  93  ALA A C   
743  O O   . ALA A 96  ? 2.3479 1.1865 1.358  -0.577  -0.0255 0.284   93  ALA A O   
744  C CB  . ALA A 96  ? 2.432  1.0279 1.4135 -0.5927 -0.0745 0.3239  93  ALA A CB  
745  N N   . ARG A 97  ? 2.3615 1.1964 1.3152 -0.7171 -0.064  0.33    94  ARG A N   
746  C CA  . ARG A 97  ? 2.3418 1.241  1.2971 -0.7541 -0.0715 0.3176  94  ARG A CA  
747  C C   . ARG A 97  ? 2.4055 1.1517 1.3354 -0.7706 -0.1077 0.3135  94  ARG A C   
748  O O   . ARG A 97  ? 2.4626 1.0679 1.364  -0.7894 -0.1355 0.3343  94  ARG A O   
749  C CB  . ARG A 97  ? 2.3217 1.3343 1.2572 -0.8493 -0.0713 0.3354  94  ARG A CB  
750  C CG  . ARG A 97  ? 2.2905 1.46   1.2521 -0.8362 -0.0308 0.3318  94  ARG A CG  
751  C CD  . ARG A 97  ? 2.2602 1.5492 1.2839 -0.7461 0.0012  0.298   94  ARG A CD  
752  N NE  . ARG A 97  ? 2.2344 1.656  1.2855 -0.7243 0.0423  0.2875  94  ARG A NE  
753  C CZ  . ARG A 97  ? 2.1835 1.7954 1.2772 -0.7344 0.0648  0.2699  94  ARG A CZ  
754  N NH1 . ARG A 97  ? 2.1439 1.8461 1.2583 -0.771  0.0465  0.264   94  ARG A NH1 
755  N NH2 . ARG A 97  ? 2.1378 1.8584 1.2576 -0.7074 0.1061  0.2528  94  ARG A NH2 
756  N N   . PHE A 98  ? 2.3945 1.1666 1.3334 -0.7597 -0.1091 0.2847  95  PHE A N   
757  C CA  . PHE A 98  ? 2.4551 1.0867 1.3691 -0.7707 -0.1363 0.2673  95  PHE A CA  
758  C C   . PHE A 98  ? 2.4621 1.1347 1.3494 -0.851  -0.1548 0.2561  95  PHE A C   
759  O O   . PHE A 98  ? 2.4071 1.2361 1.316  -0.8503 -0.1421 0.241   95  PHE A O   
760  C CB  . PHE A 98  ? 2.4467 1.0526 1.3843 -0.6821 -0.118  0.2325  95  PHE A CB  
761  C CG  . PHE A 98  ? 2.458  1.0007 1.4212 -0.6106 -0.1013 0.2349  95  PHE A CG  
762  C CD1 . PHE A 98  ? 2.5154 0.9089 1.4786 -0.5963 -0.1201 0.2308  95  PHE A CD1 
763  C CD2 . PHE A 98  ? 2.4221 1.0561 1.4128 -0.5569 -0.0674 0.2376  95  PHE A CD2 
764  C CE1 . PHE A 98  ? 2.5236 0.8816 1.5194 -0.5358 -0.1064 0.2297  95  PHE A CE1 
765  C CE2 . PHE A 98  ? 2.4403 1.0188 1.4518 -0.503  -0.0513 0.2361  95  PHE A CE2 
766  C CZ  . PHE A 98  ? 2.4797 0.931  1.4965 -0.4953 -0.0712 0.232   95  PHE A CZ  
767  N N   . GLU A 99  ? 2.5289 1.055  1.37   -0.9155 -0.1873 0.2602  96  GLU A N   
768  C CA  . GLU A 99  ? 2.5454 1.0866 1.3526 -1.0023 -0.2058 0.2433  96  GLU A CA  
769  C C   . GLU A 99  ? 2.5507 1.0893 1.3622 -0.9604 -0.2031 0.1929  96  GLU A C   
770  O O   . GLU A 99  ? 2.5994 1.0047 1.4092 -0.9006 -0.2027 0.1707  96  GLU A O   
771  C CB  . GLU A 99  ? 2.6597 1.0087 1.4044 -1.0831 -0.2415 0.2621  96  GLU A CB  
772  C CG  . GLU A 99  ? 2.73   1.0635 1.4293 -1.184  -0.2607 0.239   96  GLU A CG  
773  C CD  . GLU A 99  ? 2.7369 1.2413 1.4285 -1.289  -0.2561 0.2581  96  GLU A CD  
774  O OE1 . GLU A 99  ? 2.7024 1.2981 1.4086 -1.2974 -0.2409 0.2964  96  GLU A OE1 
775  O OE2 . GLU A 99  ? 2.7384 1.3142 1.4417 -1.3473 -0.2601 0.2267  96  GLU A OE2 
776  N N   . GLY A 100 ? 2.4938 1.1925 1.3121 -0.992  -0.2012 0.1743  97  GLY A N   
777  C CA  . GLY A 100 ? 2.4951 1.2151 1.3011 -0.9728 -0.2046 0.1293  97  GLY A CA  
778  C C   . GLY A 100 ? 2.4864 1.2102 1.3107 -0.8634 -0.1823 0.1104  97  GLY A C   
779  O O   . GLY A 100 ? 2.5121 1.1928 1.3048 -0.8544 -0.1861 0.0709  97  GLY A O   
780  N N   . ILE A 101 ? 2.4488 1.2259 1.3152 -0.7873 -0.1569 0.1358  98  ILE A N   
781  C CA  . ILE A 101 ? 2.4459 1.2243 1.321  -0.6927 -0.1328 0.1222  98  ILE A CA  
782  C C   . ILE A 101 ? 2.3735 1.3395 1.2733 -0.6567 -0.1247 0.1341  98  ILE A C   
783  O O   . ILE A 101 ? 2.3318 1.3916 1.272  -0.6439 -0.1133 0.161   98  ILE A O   
784  C CB  . ILE A 101 ? 2.4766 1.1523 1.3753 -0.6294 -0.1101 0.1352  98  ILE A CB  
785  C CG1 . ILE A 101 ? 2.5522 1.0461 1.4355 -0.6531 -0.126  0.1224  98  ILE A CG1 
786  C CG2 . ILE A 101 ? 2.4785 1.1625 1.3799 -0.5448 -0.0804 0.1224  98  ILE A CG2 
787  C CD1 . ILE A 101 ? 2.5842 0.9905 1.4987 -0.598  -0.113  0.134   98  ILE A CD1 
788  N N   . LYS A 102 ? 2.3549 1.3797 1.2284 -0.6413 -0.133  0.1135  99  LYS A N   
789  C CA  . LYS A 102 ? 2.2854 1.4853 1.1831 -0.596  -0.1341 0.1293  99  LYS A CA  
790  C C   . LYS A 102 ? 2.2834 1.4621 1.1968 -0.4965 -0.1017 0.1497  99  LYS A C   
791  O O   . LYS A 102 ? 2.3364 1.3749 1.2305 -0.4658 -0.0793 0.1429  99  LYS A O   
792  C CB  . LYS A 102 ? 2.2952 1.5605 1.1493 -0.6079 -0.1599 0.1071  99  LYS A CB  
793  C CG  . LYS A 102 ? 2.3175 1.6567 1.163  -0.7101 -0.1944 0.0865  99  LYS A CG  
794  C CD  . LYS A 102 ? 2.3445 1.7952 1.1547 -0.7141 -0.2238 0.0691  99  LYS A CD  
795  C CE  . LYS A 102 ? 2.3852 1.8756 1.1699 -0.8277 -0.2569 0.036   99  LYS A CE  
796  N NZ  . LYS A 102 ? 2.3959 1.9892 1.135  -0.8341 -0.2888 0.015   99  LYS A NZ  
797  N N   . VAL A 103 ? 2.2189 1.5381 1.1703 -0.447  -0.0988 0.1715  100 VAL A N   
798  C CA  . VAL A 103 ? 2.226  1.5226 1.1866 -0.3547 -0.0691 0.191   100 VAL A CA  
799  C C   . VAL A 103 ? 2.2803 1.4853 1.1759 -0.3106 -0.0631 0.1864  100 VAL A C   
800  O O   . VAL A 103 ? 2.3273 1.4148 1.2067 -0.2709 -0.0306 0.1889  100 VAL A O   
801  C CB  . VAL A 103 ? 2.1583 1.6298 1.1734 -0.309  -0.0734 0.2094  100 VAL A CB  
802  C CG1 . VAL A 103 ? 2.1806 1.6188 1.1879 -0.2069 -0.0506 0.2291  100 VAL A CG1 
803  C CG2 . VAL A 103 ? 2.1186 1.6652 1.194  -0.3477 -0.0618 0.2107  100 VAL A CG2 
804  N N   . LYS A 104 ? 2.2728 1.5317 1.1254 -0.3291 -0.0933 0.1764  101 LYS A N   
805  C CA  . LYS A 104 ? 2.3245 1.5063 1.099  -0.2996 -0.0879 0.1714  101 LYS A CA  
806  C C   . LYS A 104 ? 2.391  1.4049 1.1307 -0.3245 -0.0594 0.1398  101 LYS A C   
807  O O   . LYS A 104 ? 2.4351 1.3648 1.1286 -0.2862 -0.0317 0.1397  101 LYS A O   
808  C CB  . LYS A 104 ? 2.3241 1.6104 1.053  -0.3247 -0.131  0.1645  101 LYS A CB  
809  C CG  . LYS A 104 ? 2.3734 1.6604 1.0881 -0.4206 -0.1542 0.1233  101 LYS A CG  
810  C CD  . LYS A 104 ? 2.3997 1.811  1.0699 -0.4482 -0.1995 0.1152  101 LYS A CD  
811  C CE  . LYS A 104 ? 2.4654 1.8503 1.1052 -0.5498 -0.2183 0.0662  101 LYS A CE  
812  N NZ  . LYS A 104 ? 2.4425 1.9935 1.0629 -0.594  -0.2692 0.0576  101 LYS A NZ  
813  N N   . ASN A 105 ? 2.3959 1.3604 1.1595 -0.3869 -0.0654 0.1136  102 ASN A N   
814  C CA  . ASN A 105 ? 2.4533 1.2656 1.2018 -0.4005 -0.0425 0.0803  102 ASN A CA  
815  C C   . ASN A 105 ? 2.4571 1.1991 1.2571 -0.3663 -0.0129 0.0952  102 ASN A C   
816  O O   . ASN A 105 ? 2.4916 1.1305 1.286  -0.3474 0.0147  0.0744  102 ASN A O   
817  C CB  . ASN A 105 ? 2.4848 1.2535 1.2305 -0.4769 -0.0674 0.0468  102 ASN A CB  
818  C CG  . ASN A 105 ? 2.5203 1.363  1.2166 -0.5278 -0.0997 0.0256  102 ASN A CG  
819  O OD1 . ASN A 105 ? 2.5585 1.4149 1.1935 -0.5131 -0.0977 0.0104  102 ASN A OD1 
820  N ND2 . ASN A 105 ? 2.5004 1.3938 1.2155 -0.5969 -0.1306 0.0238  102 ASN A ND2 
821  N N   . TYR A 106 ? 2.4162 1.2236 1.2676 -0.3638 -0.0183 0.1258  103 TYR A N   
822  C CA  . TYR A 106 ? 2.4237 1.1812 1.3181 -0.3387 0.0053  0.1402  103 TYR A CA  
823  C C   . TYR A 106 ? 2.4422 1.177  1.324  -0.2714 0.0413  0.1507  103 TYR A C   
824  O O   . TYR A 106 ? 2.471  1.1213 1.3661 -0.2542 0.0678  0.1428  103 TYR A O   
825  C CB  . TYR A 106 ? 2.3766 1.2257 1.3158 -0.3588 -0.006  0.1663  103 TYR A CB  
826  C CG  . TYR A 106 ? 2.3884 1.1876 1.361  -0.3426 0.0152  0.1784  103 TYR A CG  
827  C CD1 . TYR A 106 ? 2.4267 1.1277 1.4092 -0.3744 0.0065  0.1721  103 TYR A CD1 
828  C CD2 . TYR A 106 ? 2.3763 1.2205 1.3671 -0.2928 0.0416  0.1946  103 TYR A CD2 
829  C CE1 . TYR A 106 ? 2.4404 1.1045 1.4494 -0.361  0.02    0.1837  103 TYR A CE1 
830  C CE2 . TYR A 106 ? 2.3932 1.1924 1.4066 -0.2841 0.0611  0.1999  103 TYR A CE2 
831  C CZ  . TYR A 106 ? 2.4277 1.1449 1.4499 -0.3206 0.0484  0.1957  103 TYR A CZ  
832  O OH  . TYR A 106 ? 2.4474 1.1322 1.4892 -0.3157 0.0608  0.2023  103 TYR A OH  
833  N N   . LEU A 107 ? 2.4253 1.233  1.28   -0.2346 0.0399  0.1695  104 LEU A N   
834  C CA  . LEU A 107 ? 2.4534 1.2202 1.2811 -0.174  0.0723  0.1855  104 LEU A CA  
835  C C   . LEU A 107 ? 2.5111 1.1792 1.2804 -0.1722 0.0968  0.1651  104 LEU A C   
836  O O   . LEU A 107 ? 2.5399 1.1472 1.2852 -0.1378 0.1315  0.1744  104 LEU A O   
837  C CB  . LEU A 107 ? 2.429  1.2909 1.2434 -0.1272 0.0579  0.2167  104 LEU A CB  
838  C CG  . LEU A 107 ? 2.3894 1.3635 1.2721 -0.1189 0.0461  0.2303  104 LEU A CG  
839  C CD1 . LEU A 107 ? 2.3637 1.4346 1.245  -0.0581 0.0311  0.2564  104 LEU A CD1 
840  C CD2 . LEU A 107 ? 2.4055 1.3274 1.3271 -0.1073 0.0795  0.2299  104 LEU A CD2 
841  N N   . MET A 108 ? 2.5269 1.1759 1.2727 -0.2145 0.083   0.1327  105 MET A N   
842  C CA  . MET A 108 ? 2.5774 1.1448 1.2747 -0.2202 0.1111  0.1006  105 MET A CA  
843  C C   . MET A 108 ? 2.5871 1.073  1.3395 -0.2255 0.1385  0.0717  105 MET A C   
844  O O   . MET A 108 ? 2.6161 1.0453 1.3476 -0.2191 0.175   0.0466  105 MET A O   
845  C CB  . MET A 108 ? 2.6005 1.1818 1.2527 -0.2637 0.0865  0.0671  105 MET A CB  
846  C CG  . MET A 108 ? 2.6331 1.2949 1.216  -0.2589 0.0606  0.0898  105 MET A CG  
847  S SD  . MET A 108 ? 2.7635 1.3777 1.2477 -0.2212 0.0967  0.108   105 MET A SD  
848  C CE  . MET A 108 ? 2.7556 1.4686 1.1525 -0.232  0.0468  0.1254  105 MET A CE  
849  N N   . LEU A 109 ? 2.5597 1.0471 1.3807 -0.2401 0.1192  0.0747  106 LEU A N   
850  C CA  . LEU A 109 ? 2.5655 0.9858 1.4433 -0.2412 0.1322  0.0521  106 LEU A CA  
851  C C   . LEU A 109 ? 2.5703 0.9727 1.4668 -0.2089 0.1701  0.0632  106 LEU A C   
852  O O   . LEU A 109 ? 2.5547 0.9892 1.4616 -0.1934 0.1712  0.0964  106 LEU A O   
853  C CB  . LEU A 109 ? 2.5472 0.9691 1.4758 -0.2692 0.0946  0.063   106 LEU A CB  
854  C CG  . LEU A 109 ? 2.5604 0.9949 1.468  -0.3152 0.0556  0.0551  106 LEU A CG  
855  C CD1 . LEU A 109 ? 2.5536 0.9812 1.4982 -0.3493 0.023   0.0756  106 LEU A CD1 
856  C CD2 . LEU A 109 ? 2.5985 0.9619 1.4833 -0.3281 0.0583  0.0044  106 LEU A CD2 
857  N N   . GLY A 110 ? 2.5917 0.9466 1.4917 -0.2023 0.2043  0.0298  107 GLY A N   
858  C CA  . GLY A 110 ? 2.6069 0.9433 1.522  -0.1838 0.2448  0.0327  107 GLY A CA  
859  C C   . GLY A 110 ? 2.646  0.9764 1.4849 -0.1686 0.2773  0.0557  107 GLY A C   
860  O O   . GLY A 110 ? 2.6536 0.9561 1.493  -0.1608 0.3137  0.0596  107 GLY A O   
861  N N   . MET A 111 ? 2.6724 1.0242 1.4401 -0.1669 0.2619  0.0723  108 MET A N   
862  C CA  . MET A 111 ? 2.7231 1.0604 1.4038 -0.1476 0.2815  0.1039  108 MET A CA  
863  C C   . MET A 111 ? 2.7805 1.0569 1.4204 -0.1577 0.3369  0.0851  108 MET A C   
864  O O   . MET A 111 ? 2.7804 1.0499 1.4365 -0.1817 0.3567  0.0375  108 MET A O   
865  C CB  . MET A 111 ? 2.7335 1.1126 1.3443 -0.1501 0.2492  0.1166  108 MET A CB  
866  C CG  . MET A 111 ? 2.7832 1.1448 1.2985 -0.1225 0.2572  0.1604  108 MET A CG  
867  S SD  . MET A 111 ? 2.7881 1.2209 1.2231 -0.1202 0.2071  0.1831  108 MET A SD  
868  C CE  . MET A 111 ? 2.695  1.2259 1.2121 -0.0915 0.1582  0.2113  108 MET A CE  
869  N N   . ASN A 112 ? 2.8267 1.0576 1.4175 -0.141  0.3643  0.1191  109 ASN A N   
870  C CA  . ASN A 112 ? 2.8847 1.0536 1.4263 -0.1611 0.4211  0.1082  109 ASN A CA  
871  C C   . ASN A 112 ? 2.9376 1.1018 1.3928 -0.1864 0.4379  0.0907  109 ASN A C   
872  O O   . ASN A 112 ? 2.9542 1.1384 1.3419 -0.1771 0.4048  0.1141  109 ASN A O   
873  C CB  . ASN A 112 ? 2.9422 1.0433 1.4218 -0.1394 0.4389  0.1573  109 ASN A CB  
874  C CG  . ASN A 112 ? 3.0091 1.0463 1.4769 -0.1706 0.499   0.1412  109 ASN A CG  
875  O OD1 . ASN A 112 ? 3.0599 1.0625 1.4536 -0.2031 0.5387  0.1323  109 ASN A OD1 
876  N ND2 . ASN A 112 ? 2.9986 1.0266 1.5368 -0.1693 0.5088  0.1338  109 ASN A ND2 
877  N N   . GLU A 113 ? 2.9591 1.1087 1.4167 -0.2209 0.4899  0.046   110 GLU A N   
878  C CA  . GLU A 113 ? 3.0116 1.1616 1.384  -0.2527 0.5177  0.0184  110 GLU A CA  
879  C C   . GLU A 113 ? 3.0976 1.1959 1.3148 -0.2557 0.5222  0.0752  110 GLU A C   
880  O O   . GLU A 113 ? 3.1242 1.2349 1.2512 -0.2766 0.5217  0.0661  110 GLU A O   
881  C CB  . GLU A 113 ? 3.0333 1.1909 1.4483 -0.2886 0.5814  -0.0429 110 GLU A CB  
882  C CG  . GLU A 113 ? 3.0521 1.2681 1.5898 -0.2838 0.5699  -0.1115 110 GLU A CG  
883  C CD  . GLU A 113 ? 3.1596 1.3974 1.6531 -0.2943 0.558   -0.1505 110 GLU A CD  
884  O OE1 . GLU A 113 ? 3.1543 1.4091 1.6982 -0.2764 0.506   -0.1597 110 GLU A OE1 
885  O OE2 . GLU A 113 ? 3.2279 1.4627 1.6284 -0.3272 0.6026  -0.1734 110 GLU A OE2 
886  N N   . LYS A 114 ? 3.1422 1.177  1.3222 -0.233  0.5226  0.1343  111 LYS A N   
887  C CA  . LYS A 114 ? 3.2287 1.1964 1.2593 -0.2246 0.5175  0.1991  111 LYS A CA  
888  C C   . LYS A 114 ? 3.2369 1.2517 1.236  -0.1809 0.445   0.2398  111 LYS A C   
889  O O   . LYS A 114 ? 3.2952 1.271  1.1687 -0.1689 0.4279  0.2937  111 LYS A O   
890  C CB  . LYS A 114 ? 3.295  1.1575 1.2919 -0.2126 0.5442  0.2456  111 LYS A CB  
891  C CG  . LYS A 114 ? 3.3046 1.1741 1.3977 -0.1588 0.5094  0.2646  111 LYS A CG  
892  C CD  . LYS A 114 ? 3.3974 1.1572 1.4696 -0.1581 0.5468  0.2889  111 LYS A CD  
893  C CE  . LYS A 114 ? 3.5121 1.1768 1.4764 -0.1084 0.5229  0.3635  111 LYS A CE  
894  N NZ  . LYS A 114 ? 3.5591 1.1534 1.5502 -0.11   0.5463  0.3839  111 LYS A NZ  
895  N N   . TYR A 115 ? 3.1762 1.2778 1.2854 -0.1608 0.4005  0.2163  112 TYR A N   
896  C CA  . TYR A 115 ? 3.1692 1.3407 1.2643 -0.13   0.3338  0.2455  112 TYR A CA  
897  C C   . TYR A 115 ? 3.147  1.3949 1.2689 -0.1665 0.3149  0.1896  112 TYR A C   
898  O O   . TYR A 115 ? 3.1647 1.4503 1.2044 -0.1771 0.2845  0.1974  112 TYR A O   
899  C CB  . TYR A 115 ? 3.1238 1.3346 1.3185 -0.0805 0.2975  0.2694  112 TYR A CB  
900  C CG  . TYR A 115 ? 3.1658 1.2912 1.3482 -0.0428 0.3202  0.3112  112 TYR A CG  
901  C CD1 . TYR A 115 ? 3.2336 1.2982 1.31   -0.0047 0.3083  0.373   112 TYR A CD1 
902  C CD2 . TYR A 115 ? 3.155  1.2545 1.4273 -0.0448 0.35    0.2889  112 TYR A CD2 
903  C CE1 . TYR A 115 ? 3.2851 1.2487 1.3443 0.0311  0.3301  0.4085  112 TYR A CE1 
904  C CE2 . TYR A 115 ? 3.201  1.2141 1.4568 -0.0153 0.3726  0.3199  112 TYR A CE2 
905  C CZ  . TYR A 115 ? 3.275  1.2125 1.4239 0.0231  0.3647  0.3781  112 TYR A CZ  
906  O OH  . TYR A 115 ? 3.3403 1.1695 1.4649 0.0538  0.3879  0.4067  112 TYR A OH  
907  N N   . LYS A 116 ? 3.1108 1.3737 1.3424 -0.1863 0.3319  0.1326  113 LYS A N   
908  C CA  . LYS A 116 ? 3.0915 1.3994 1.3685 -0.2177 0.3184  0.0713  113 LYS A CA  
909  C C   . LYS A 116 ? 3.1379 1.4468 1.3109 -0.2571 0.3342  0.0356  113 LYS A C   
910  O O   . LYS A 116 ? 3.1267 1.4784 1.2965 -0.2786 0.3026  0.0022  113 LYS A O   
911  C CB  . LYS A 116 ? 3.0787 1.3669 1.4708 -0.2252 0.3492  0.0222  113 LYS A CB  
912  C CG  . LYS A 116 ? 3.0938 1.4064 1.5535 -0.2444 0.3277  -0.0349 113 LYS A CG  
913  C CD  . LYS A 116 ? 3.1137 1.4044 1.6857 -0.2405 0.3526  -0.0751 113 LYS A CD  
914  C CE  . LYS A 116 ? 3.1418 1.4289 1.7648 -0.2556 0.3395  -0.1385 113 LYS A CE  
915  N NZ  . LYS A 116 ? 3.1933 1.4734 1.7459 -0.2807 0.3755  -0.1947 113 LYS A NZ  
916  N N   . LYS A 117 ? 3.1909 1.4503 1.2715 -0.2736 0.3853  0.0407  114 LYS A N   
917  C CA  . LYS A 117 ? 3.241  1.4987 1.2069 -0.3177 0.4136  0.0057  114 LYS A CA  
918  C C   . LYS A 117 ? 3.2765 1.5745 1.1245 -0.3239 0.3595  0.0389  114 LYS A C   
919  O O   . LYS A 117 ? 3.266  1.6106 1.1084 -0.3515 0.3371  -0.0106 114 LYS A O   
920  C CB  . LYS A 117 ? 3.3086 1.5044 1.1977 -0.3403 0.4835  0.0146  114 LYS A CB  
921  C CG  . LYS A 117 ? 3.3251 1.5113 1.3285 -0.3502 0.5418  -0.0416 114 LYS A CG  
922  C CD  . LYS A 117 ? 3.3871 1.5929 1.3638 -0.3981 0.6034  -0.1229 114 LYS A CD  
923  C CE  . LYS A 117 ? 3.3817 1.6331 1.4711 -0.3936 0.5935  -0.2072 114 LYS A CE  
924  N NZ  . LYS A 117 ? 3.3598 1.7167 1.4854 -0.4123 0.6233  -0.2845 114 LYS A NZ  
925  N N   . ASP A 118 ? 3.3166 1.5944 1.0703 -0.298  0.3358  0.1204  115 ASP A N   
926  C CA  . ASP A 118 ? 3.3441 1.6719 0.9885 -0.2975 0.277   0.1588  115 ASP A CA  
927  C C   . ASP A 118 ? 3.2814 1.6997 1.0265 -0.2695 0.2071  0.1643  115 ASP A C   
928  O O   . ASP A 118 ? 3.2467 1.6687 1.1    -0.2264 0.1948  0.1894  115 ASP A O   
929  C CB  . ASP A 118 ? 3.428  1.6979 0.9509 -0.266  0.2666  0.2508  115 ASP A CB  
930  C CG  . ASP A 118 ? 3.525  1.8302 0.8907 -0.2782 0.2192  0.2894  115 ASP A CG  
931  O OD1 . ASP A 118 ? 3.5016 1.9018 0.8717 -0.3014 0.1768  0.2526  115 ASP A OD1 
932  O OD2 . ASP A 118 ? 3.5544 1.8818 0.8824 -0.2544 0.2157  0.3593  115 ASP A OD2 
933  N N   . LYS A 119 ? 3.2639 1.7587 0.9706 -0.3021 0.1649  0.1359  116 LYS A N   
934  C CA  . LYS A 119 ? 3.2047 1.7984 0.9977 -0.2932 0.1001  0.1353  116 LYS A CA  
935  C C   . LYS A 119 ? 3.1824 1.8344 0.9813 -0.2304 0.0438  0.2197  116 LYS A C   
936  O O   . LYS A 119 ? 3.1329 1.8234 1.0525 -0.1952 0.0257  0.2337  116 LYS A O   
937  C CB  . LYS A 119 ? 3.2281 1.8839 0.9601 -0.3545 0.0718  0.0804  116 LYS A CB  
938  C CG  . LYS A 119 ? 3.2231 2.0025 1.0015 -0.3585 -0.0047 0.091   116 LYS A CG  
939  C CD  . LYS A 119 ? 3.2939 2.1275 0.9798 -0.4267 -0.0319 0.0399  116 LYS A CD  
940  C CE  . LYS A 119 ? 3.4029 2.231  0.915  -0.4375 -0.0326 0.0658  116 LYS A CE  
941  N NZ  . LYS A 119 ? 3.3844 2.3517 0.9062 -0.4709 -0.049  0.002   116 LYS A NZ  
942  N N   . GLU A 120 ? 3.2185 1.8749 0.8864 -0.2136 0.0174  0.2753  117 GLU A N   
943  C CA  . GLU A 120 ? 3.202  1.9115 0.8716 -0.142  -0.0405 0.3558  117 GLU A CA  
944  C C   . GLU A 120 ? 3.2087 1.8306 0.9392 -0.0755 -0.01   0.4006  117 GLU A C   
945  O O   . GLU A 120 ? 3.174  1.8488 0.9626 -0.0081 -0.0517 0.448   117 GLU A O   
946  C CB  . GLU A 120 ? 3.2816 2.0031 0.7828 -0.1394 -0.0811 0.4079  117 GLU A CB  
947  C CG  . GLU A 120 ? 3.3224 2.1531 0.7655 -0.2037 -0.123  0.3641  117 GLU A CG  
948  C CD  . GLU A 120 ? 3.4796 2.2593 0.7412 -0.2626 -0.1008 0.3516  117 GLU A CD  
949  O OE1 . GLU A 120 ? 3.4968 2.2401 0.8019 -0.2824 -0.0198 0.3117  117 GLU A OE1 
950  O OE2 . GLU A 120 ? 3.4484 2.4013 0.6995 -0.2499 -0.1532 0.3759  117 GLU A OE2 
951  N N   . ILE A 121 ? 3.245  1.7428 0.9701 -0.0963 0.0637  0.3785  118 ILE A N   
952  C CA  . ILE A 121 ? 3.2576 1.6636 1.0356 -0.0489 0.0994  0.4087  118 ILE A CA  
953  C C   . ILE A 121 ? 3.1819 1.633  1.1284 -0.0433 0.1075  0.3673  118 ILE A C   
954  O O   . ILE A 121 ? 3.1627 1.6057 1.1784 0.0111  0.1034  0.3969  118 ILE A O   
955  C CB  . ILE A 121 ? 3.3424 1.6069 1.0318 -0.0832 0.1734  0.4049  118 ILE A CB  
956  C CG1 . ILE A 121 ? 3.4413 1.6311 0.9575 -0.0696 0.1621  0.4766  118 ILE A CG1 
957  C CG2 . ILE A 121 ? 3.3441 1.527  1.124  -0.0653 0.2242  0.3987  118 ILE A CG2 
958  C CD1 . ILE A 121 ? 3.5339 1.6023 0.952  -0.12   0.2348  0.4702  118 ILE A CD1 
959  N N   . ALA A 122 ? 3.1428 1.632  1.1477 -0.0994 0.1198  0.2988  119 ALA A N   
960  C CA  . ALA A 122 ? 3.0821 1.6054 1.2309 -0.1026 0.123   0.2636  119 ALA A CA  
961  C C   . ALA A 122 ? 3.0127 1.6596 1.2313 -0.0737 0.0623  0.2857  119 ALA A C   
962  O O   . ALA A 122 ? 2.9749 1.6413 1.2893 -0.0434 0.0632  0.2947  119 ALA A O   
963  C CB  . ALA A 122 ? 3.075  1.5958 1.2546 -0.1651 0.1424  0.1903  119 ALA A CB  
964  N N   . GLU A 123 ? 2.9914 1.7317 1.1595 -0.0859 0.0108  0.2926  120 GLU A N   
965  C CA  . GLU A 123 ? 2.9195 1.8065 1.1539 -0.0654 -0.0493 0.3097  120 GLU A CA  
966  C C   . GLU A 123 ? 2.8972 1.8076 1.1485 0.023   -0.0684 0.3732  120 GLU A C   
967  O O   . GLU A 123 ? 2.8289 1.8476 1.1802 0.0529  -0.0949 0.3797  120 GLU A O   
968  C CB  . GLU A 123 ? 2.9428 1.9269 1.1099 -0.1076 -0.0999 0.2971  120 GLU A CB  
969  C CG  . GLU A 123 ? 3.0174 1.9837 1.183  -0.1932 -0.0853 0.225   120 GLU A CG  
970  C CD  . GLU A 123 ? 3.1163 2.1416 1.1829 -0.2451 -0.1215 0.2022  120 GLU A CD  
971  O OE1 . GLU A 123 ? 3.1389 2.2172 1.1215 -0.2158 -0.1593 0.2486  120 GLU A OE1 
972  O OE2 . GLU A 123 ? 3.1509 2.1635 1.2189 -0.3148 -0.1139 0.1375  120 GLU A OE2 
973  N N   . GLU A 124 ? 2.955  1.7587 1.1074 0.0636  -0.052  0.4177  121 GLU A N   
974  C CA  . GLU A 124 ? 2.9549 1.7433 1.1119 0.1542  -0.0671 0.4777  121 GLU A CA  
975  C C   . GLU A 124 ? 2.944  1.6534 1.1855 0.1799  -0.0162 0.468   121 GLU A C   
976  O O   . GLU A 124 ? 2.9072 1.6592 1.218  0.2476  -0.0305 0.4901  121 GLU A O   
977  C CB  . GLU A 124 ? 3.0731 1.75   1.0758 0.1803  -0.0689 0.5333  121 GLU A CB  
978  C CG  . GLU A 124 ? 3.1473 1.8142 1.1419 0.2833  -0.1043 0.6022  121 GLU A CG  
979  C CD  . GLU A 124 ? 3.2938 1.796  1.2875 0.3272  -0.0514 0.6232  121 GLU A CD  
980  O OE1 . GLU A 124 ? 3.3464 1.7391 1.33   0.2711  0.0142  0.5894  121 GLU A OE1 
981  O OE2 . GLU A 124 ? 3.3314 1.8171 1.339  0.419   -0.0764 0.67    121 GLU A OE2 
982  N N   . LYS A 125 ? 2.9703 1.5731 1.2081 0.1271  0.0427  0.431   122 LYS A N   
983  C CA  . LYS A 125 ? 2.964  1.496  1.2756 0.1377  0.0901  0.4159  122 LYS A CA  
984  C C   . LYS A 125 ? 2.8754 1.5274 1.3215 0.1385  0.0732  0.3888  122 LYS A C   
985  O O   . LYS A 125 ? 2.862  1.4996 1.369  0.1763  0.0915  0.3926  122 LYS A O   
986  C CB  . LYS A 125 ? 3.0213 1.4464 1.3104 0.0757  0.1484  0.3772  122 LYS A CB  
987  C CG  . LYS A 125 ? 3.0585 1.4113 1.4133 0.0811  0.1948  0.3624  122 LYS A CG  
988  C CD  . LYS A 125 ? 3.1439 1.3963 1.4504 0.1392  0.212   0.4076  122 LYS A CD  
989  C CE  . LYS A 125 ? 3.1567 1.3829 1.5482 0.1533  0.2411  0.3895  122 LYS A CE  
990  N NZ  . LYS A 125 ? 3.2318 1.3396 1.5715 0.2071  0.2618  0.4262  122 LYS A NZ  
991  N N   . ILE A 126 ? 2.8166 1.584  1.2997 0.0917  0.0396  0.361   123 ILE A N   
992  C CA  . ILE A 126 ? 2.7381 1.6252 1.3335 0.0781  0.0216  0.3392  123 ILE A CA  
993  C C   . ILE A 126 ? 2.6831 1.6812 1.3255 0.1511  -0.0099 0.3713  123 ILE A C   
994  O O   . ILE A 126 ? 2.6442 1.6803 1.3696 0.1733  0.0049  0.3637  123 ILE A O   
995  C CB  . ILE A 126 ? 2.7142 1.6833 1.3175 0.0046  -0.0092 0.3052  123 ILE A CB  
996  C CG1 . ILE A 126 ? 2.7694 1.6271 1.3506 -0.057  0.0256  0.2641  123 ILE A CG1 
997  C CG2 . ILE A 126 ? 2.6405 1.751  1.3449 -0.0151 -0.0352 0.2924  123 ILE A CG2 
998  C CD1 . ILE A 126 ? 2.7707 1.6729 1.3499 -0.1283 0       0.2246  123 ILE A CD1 
999  N N   . ARG A 127 ? 2.6778 1.7303 1.266  0.1913  -0.0533 0.4057  124 ARG A N   
1000 C CA  . ARG A 127 ? 2.6232 1.7931 1.2607 0.2739  -0.0909 0.4368  124 ARG A CA  
1001 C C   . ARG A 127 ? 2.6559 1.7227 1.3044 0.3548  -0.0565 0.459   124 ARG A C   
1002 O O   . ARG A 127 ? 2.5945 1.7539 1.3367 0.4055  -0.0592 0.4535  124 ARG A O   
1003 C CB  . ARG A 127 ? 2.6425 1.8685 1.2028 0.3046  -0.1487 0.4757  124 ARG A CB  
1004 C CG  . ARG A 127 ? 2.6506 1.9703 1.1847 0.22    -0.1826 0.4487  124 ARG A CG  
1005 C CD  . ARG A 127 ? 2.6512 2.1044 1.1521 0.2566  -0.2543 0.4829  124 ARG A CD  
1006 N NE  . ARG A 127 ? 2.5616 2.2386 1.1876 0.2576  -0.2942 0.4642  124 ARG A NE  
1007 C CZ  . ARG A 127 ? 2.5288 2.3359 1.1825 0.1708  -0.3209 0.4254  124 ARG A CZ  
1008 N NH1 . ARG A 127 ? 2.5753 2.3051 1.1395 0.0847  -0.3145 0.3989  124 ARG A NH1 
1009 N NH2 . ARG A 127 ? 2.4194 2.4365 1.1893 0.1671  -0.3524 0.4092  124 ARG A NH2 
1010 N N   . GLU A 128 ? 2.7505 1.6257 1.3029 0.3598  -0.0195 0.4779  125 GLU A N   
1011 C CA  . GLU A 128 ? 2.8058 1.5422 1.3445 0.4218  0.0193  0.4964  125 GLU A CA  
1012 C C   . GLU A 128 ? 2.778  1.5175 1.4129 0.4001  0.0642  0.4515  125 GLU A C   
1013 O O   . GLU A 128 ? 2.7731 1.4928 1.4495 0.4632  0.0809  0.4529  125 GLU A O   
1014 C CB  . GLU A 128 ? 2.9376 1.477  1.3464 0.3949  0.0544  0.5172  125 GLU A CB  
1015 C CG  . GLU A 128 ? 3.0699 1.4366 1.423  0.455   0.0865  0.5497  125 GLU A CG  
1016 C CD  . GLU A 128 ? 3.2525 1.4624 1.452  0.4314  0.0995  0.5887  125 GLU A CD  
1017 O OE1 . GLU A 128 ? 3.2745 1.534  1.4031 0.4246  0.0565  0.6165  125 GLU A OE1 
1018 O OE2 . GLU A 128 ? 3.3541 1.3977 1.4992 0.4111  0.1538  0.5892  125 GLU A OE2 
1019 N N   . ALA A 129 ? 2.7604 1.5207 1.4259 0.3122  0.0817  0.411   126 ALA A N   
1020 C CA  . ALA A 129 ? 2.7366 1.5023 1.4805 0.2796  0.1172  0.3724  126 ALA A CA  
1021 C C   . ALA A 129 ? 2.6465 1.5887 1.4945 0.295   0.0952  0.3569  126 ALA A C   
1022 O O   . ALA A 129 ? 2.6267 1.5744 1.5284 0.3173  0.1233  0.3399  126 ALA A O   
1023 C CB  . ALA A 129 ? 2.75   1.4834 1.4904 0.189   0.1317  0.3412  126 ALA A CB  
1024 N N   . LEU A 130 ? 2.5895 1.6824 1.4636 0.2777  0.0477  0.3589  127 LEU A N   
1025 C CA  . LEU A 130 ? 2.5005 1.7851 1.4763 0.2824  0.0279  0.3422  127 LEU A CA  
1026 C C   . LEU A 130 ? 2.472  1.8188 1.4876 0.3905  0.02    0.3593  127 LEU A C   
1027 O O   . LEU A 130 ? 2.4076 1.8648 1.5119 0.4105  0.0337  0.3354  127 LEU A O   
1028 C CB  . LEU A 130 ? 2.4523 1.8827 1.4429 0.225   -0.0206 0.3367  127 LEU A CB  
1029 C CG  . LEU A 130 ? 2.4879 1.8901 1.4706 0.1164  -0.0148 0.3086  127 LEU A CG  
1030 C CD1 . LEU A 130 ? 2.4531 1.985  1.4391 0.0609  -0.063  0.3012  127 LEU A CD1 
1031 C CD2 . LEU A 130 ? 2.4671 1.8922 1.5165 0.0763  0.0155  0.2837  127 LEU A CD2 
1032 N N   . LYS A 131 ? 2.5198 1.7947 1.4676 0.4619  -0.002  0.4     128 LYS A N   
1033 C CA  . LYS A 131 ? 2.5075 1.813  1.4873 0.5798  -0.0142 0.4209  128 LYS A CA  
1034 C C   . LYS A 131 ? 2.5581 1.7224 1.5424 0.6214  0.0444  0.4058  128 LYS A C   
1035 O O   . LYS A 131 ? 2.5175 1.7433 1.5709 0.7042  0.0499  0.3955  128 LYS A O   
1036 C CB  . LYS A 131 ? 2.5846 1.8224 1.4707 0.643   -0.0582 0.478   128 LYS A CB  
1037 C CG  . LYS A 131 ? 2.5651 1.9905 1.4662 0.6346  -0.128  0.4928  128 LYS A CG  
1038 C CD  . LYS A 131 ? 2.6871 2.0248 1.4692 0.6842  -0.1721 0.5537  128 LYS A CD  
1039 C CE  . LYS A 131 ? 2.6934 2.1796 1.4522 0.6375  -0.235  0.5624  128 LYS A CE  
1040 N NZ  . LYS A 131 ? 2.7815 2.2032 1.4232 0.6968  -0.2859 0.6275  128 LYS A NZ  
1041 N N   . LEU A 132 ? 2.6405 1.6236 1.5549 0.5632  0.0887  0.399   129 LEU A N   
1042 C CA  . LEU A 132 ? 2.6937 1.5347 1.6006 0.5811  0.1454  0.3794  129 LEU A CA  
1043 C C   . LEU A 132 ? 2.6211 1.5768 1.6271 0.5505  0.1738  0.3276  129 LEU A C   
1044 O O   . LEU A 132 ? 2.6293 1.5422 1.6603 0.5977  0.2099  0.3049  129 LEU A O   
1045 C CB  . LEU A 132 ? 2.7919 1.4442 1.6068 0.5123  0.1803  0.3824  129 LEU A CB  
1046 C CG  . LEU A 132 ? 2.9152 1.367  1.6193 0.5567  0.1925  0.4226  129 LEU A CG  
1047 C CD1 . LEU A 132 ? 2.9957 1.3069 1.6243 0.4724  0.2283  0.4175  129 LEU A CD1 
1048 C CD2 . LEU A 132 ? 2.9523 1.3092 1.6646 0.6364  0.2221  0.4173  129 LEU A CD2 
1049 N N   . VAL A 133 ? 2.5552 1.6445 1.6072 0.4671  0.1594  0.3082  130 VAL A N   
1050 C CA  . VAL A 133 ? 2.4933 1.6941 1.6243 0.4256  0.1837  0.2657  130 VAL A CA  
1051 C C   . VAL A 133 ? 2.3855 1.8171 1.6154 0.4608  0.1605  0.2521  130 VAL A C   
1052 O O   . VAL A 133 ? 2.3215 1.8815 1.6121 0.4036  0.1729  0.2209  130 VAL A O   
1053 C CB  . VAL A 133 ? 2.5098 1.6975 1.6279 0.3104  0.1872  0.253   130 VAL A CB  
1054 C CG1 . VAL A 133 ? 2.6087 1.5937 1.6512 0.2841  0.2158  0.257   130 VAL A CG1 
1055 C CG2 . VAL A 133 ? 2.4863 1.7659 1.6031 0.2607  0.1394  0.268   130 VAL A CG2 
1056 N N   . ASN A 134 ? 2.3639 1.8508 1.6086 0.5545  0.1267  0.2763  131 ASN A N   
1057 C CA  . ASN A 134 ? 2.2611 1.979  1.6095 0.6091  0.0996  0.2646  131 ASN A CA  
1058 C C   . ASN A 134 ? 2.1795 2.0995 1.5794 0.5185  0.0672  0.2543  131 ASN A C   
1059 O O   . ASN A 134 ? 2.0807 2.2083 1.5803 0.5134  0.0706  0.223   131 ASN A O   
1060 C CB  . ASN A 134 ? 2.2335 2.0102 1.6598 0.6674  0.145   0.2208  131 ASN A CB  
1061 C CG  . ASN A 134 ? 2.3417 1.9625 1.7367 0.7901  0.159   0.2333  131 ASN A CG  
1062 O OD1 . ASN A 134 ? 2.4395 1.8789 1.7829 0.7901  0.2076  0.2182  131 ASN A OD1 
1063 N ND2 . ASN A 134 ? 2.3187 2.0006 1.7395 0.8953  0.1129  0.2629  131 ASN A ND2 
1064 N N   . LEU A 135 ? 2.2181 2.079  1.5487 0.4453  0.0381  0.2775  132 LEU A N   
1065 C CA  . LEU A 135 ? 2.1543 2.1791 1.5174 0.3561  0.0031  0.2692  132 LEU A CA  
1066 C C   . LEU A 135 ? 2.1503 2.2257 1.4835 0.389   -0.0582 0.302   132 LEU A C   
1067 O O   . LEU A 135 ? 2.2366 2.1487 1.4781 0.4276  -0.0675 0.3352  132 LEU A O   
1068 C CB  . LEU A 135 ? 2.209  2.1245 1.5155 0.2355  0.0179  0.2609  132 LEU A CB  
1069 C CG  . LEU A 135 ? 2.2218 2.1141 1.5527 0.1807  0.0656  0.2325  132 LEU A CG  
1070 C CD1 . LEU A 135 ? 2.2838 2.0656 1.5584 0.0743  0.0657  0.2325  132 LEU A CD1 
1071 C CD2 . LEU A 135 ? 2.1203 2.2384 1.5485 0.159   0.0714  0.2044  132 LEU A CD2 
1072 N N   . ASP A 136 ? 2.0468 2.3543 1.4532 0.3712  -0.0998 0.2927  133 ASP A N   
1073 C CA  . ASP A 136 ? 2.0363 2.4178 1.4152 0.3949  -0.1648 0.3213  133 ASP A CA  
1074 C C   . ASP A 136 ? 2.1037 2.3799 1.3854 0.2855  -0.1774 0.3239  133 ASP A C   
1075 O O   . ASP A 136 ? 2.0745 2.4166 1.3796 0.1787  -0.1733 0.2951  133 ASP A O   
1076 C CB  . ASP A 136 ? 1.92   2.6051 1.4192 0.3966  -0.2037 0.3018  133 ASP A CB  
1077 C CG  . ASP A 136 ? 1.95   2.7521 1.4407 0.446   -0.2787 0.3319  133 ASP A CG  
1078 O OD1 . ASP A 136 ? 2.0515 2.6884 1.4282 0.4771  -0.3014 0.3722  133 ASP A OD1 
1079 O OD2 . ASP A 136 ? 1.8612 2.9286 1.4575 0.45    -0.3152 0.315   133 ASP A OD2 
1080 N N   . PRO A 137 ? 2.1973 2.3005 1.3649 0.3068  -0.1889 0.3557  134 PRO A N   
1081 C CA  . PRO A 137 ? 2.2584 2.2597 1.3368 0.2063  -0.1932 0.3476  134 PRO A CA  
1082 C C   . PRO A 137 ? 2.19   2.3607 1.2895 0.1199  -0.2391 0.3264  134 PRO A C   
1083 O O   . PRO A 137 ? 2.2083 2.34   1.2946 0.0171  -0.2254 0.2974  134 PRO A O   
1084 C CB  . PRO A 137 ? 2.3617 2.2038 1.3216 0.2589  -0.2033 0.3868  134 PRO A CB  
1085 C CG  . PRO A 137 ? 2.3871 2.1591 1.3611 0.3708  -0.1814 0.4137  134 PRO A CG  
1086 C CD  . PRO A 137 ? 2.252  2.2356 1.3601 0.4193  -0.1948 0.399   134 PRO A CD  
1087 N N   . ASP A 138 ? 2.1067 2.4678 1.2443 0.1606  -0.2947 0.3393  135 ASP A N   
1088 C CA  . ASP A 138 ? 2.0404 2.58   1.1987 0.0734  -0.342  0.3163  135 ASP A CA  
1089 C C   . ASP A 138 ? 1.9561 2.6369 1.2159 -0.0128 -0.3231 0.2757  135 ASP A C   
1090 O O   . ASP A 138 ? 1.9414 2.6864 1.1918 -0.1235 -0.3431 0.2492  135 ASP A O   
1091 C CB  . ASP A 138 ? 1.9903 2.7197 1.1689 0.1403  -0.4132 0.3413  135 ASP A CB  
1092 C CG  . ASP A 138 ? 2.037  2.7589 1.236  0.293   -0.423  0.3852  135 ASP A CG  
1093 O OD1 . ASP A 138 ? 2.148  2.6496 1.2457 0.3448  -0.4034 0.4188  135 ASP A OD1 
1094 O OD2 . ASP A 138 ? 1.956  2.8912 1.2726 0.3597  -0.4497 0.3843  135 ASP A OD2 
1095 N N   . LYS A 139 ? 1.9069 2.6238 1.2519 0.03    -0.2821 0.2696  136 LYS A N   
1096 C CA  . LYS A 139 ? 1.8335 2.6799 1.2639 -0.0535 -0.2574 0.235   136 LYS A CA  
1097 C C   . LYS A 139 ? 1.9116 2.5594 1.2831 -0.148  -0.2122 0.2221  136 LYS A C   
1098 O O   . LYS A 139 ? 1.8794 2.5962 1.2812 -0.2518 -0.2027 0.199   136 LYS A O   
1099 C CB  . LYS A 139 ? 1.7708 2.7672 1.3186 0.0371  -0.2332 0.2288  136 LYS A CB  
1100 C CG  . LYS A 139 ? 1.7897 2.8353 1.3998 -0.0258 -0.1792 0.1981  136 LYS A CG  
1101 C CD  . LYS A 139 ? 1.7409 3.0277 1.4251 -0.1353 -0.1938 0.168   136 LYS A CD  
1102 C CE  . LYS A 139 ? 1.7985 3.0415 1.4778 -0.2454 -0.1444 0.1489  136 LYS A CE  
1103 N NZ  . LYS A 139 ? 1.8141 3.034  1.5341 -0.1794 -0.0873 0.1406  136 LYS A NZ  
1104 N N   . TYR A 140 ? 2.0128 2.4176 1.2972 -0.1171 -0.1882 0.2383  137 TYR A N   
1105 C CA  . TYR A 140 ? 2.0856 2.3108 1.3258 -0.1891 -0.1507 0.2278  137 TYR A CA  
1106 C C   . TYR A 140 ? 2.1682 2.2114 1.308  -0.2415 -0.1597 0.2246  137 TYR A C   
1107 O O   . TYR A 140 ? 2.2116 2.1489 1.3303 -0.3177 -0.1429 0.2106  137 TYR A O   
1108 C CB  . TYR A 140 ? 2.1292 2.2359 1.3762 -0.12   -0.1011 0.237   137 TYR A CB  
1109 C CG  . TYR A 140 ? 2.0624 2.3267 1.4057 -0.0941 -0.0778 0.2254  137 TYR A CG  
1110 C CD1 . TYR A 140 ? 2.0525 2.3612 1.4268 -0.181  -0.0542 0.207   137 TYR A CD1 
1111 C CD2 . TYR A 140 ? 2.023  2.3913 1.4227 0.0174  -0.0792 0.2318  137 TYR A CD2 
1112 C CE1 . TYR A 140 ? 1.9865 2.4511 1.4441 -0.164  -0.0264 0.1903  137 TYR A CE1 
1113 C CE2 . TYR A 140 ? 1.9539 2.4755 1.4483 0.0456  -0.0523 0.211   137 TYR A CE2 
1114 C CZ  . TYR A 140 ? 1.9403 2.5172 1.4631 -0.049  -0.023  0.1876  137 TYR A CZ  
1115 O OH  . TYR A 140 ? 1.8805 2.6194 1.4919 -0.0272 0.0099  0.1613  137 TYR A OH  
1116 N N   . LEU A 141 ? 2.1898 2.1936 1.2657 -0.2017 -0.1851 0.2362  138 LEU A N   
1117 C CA  . LEU A 141 ? 2.2703 2.1079 1.2495 -0.2465 -0.1863 0.2248  138 LEU A CA  
1118 C C   . LEU A 141 ? 2.2665 2.0883 1.23   -0.3657 -0.1991 0.191   138 LEU A C   
1119 O O   . LEU A 141 ? 2.3417 1.9903 1.253  -0.401  -0.1799 0.1746  138 LEU A O   
1120 C CB  . LEU A 141 ? 2.2955 2.1438 1.2041 -0.2018 -0.2188 0.2404  138 LEU A CB  
1121 C CG  . LEU A 141 ? 2.3657 2.1082 1.233  -0.0991 -0.1976 0.2754  138 LEU A CG  
1122 C CD1 . LEU A 141 ? 2.3844 2.1688 1.1805 -0.0573 -0.24   0.3006  138 LEU A CD1 
1123 C CD2 . LEU A 141 ? 2.4631 1.991  1.2777 -0.1104 -0.1482 0.2663  138 LEU A CD2 
1124 N N   . ASP A 142 ? 2.1787 2.1777 1.1871 -0.4272 -0.2317 0.1783  139 ASP A N   
1125 C CA  . ASP A 142 ? 2.1882 2.1614 1.1735 -0.5485 -0.245  0.1466  139 ASP A CA  
1126 C C   . ASP A 142 ? 2.1534 2.1499 1.1958 -0.6154 -0.2255 0.1445  139 ASP A C   
1127 O O   . ASP A 142 ? 2.1569 2.1569 1.1862 -0.7229 -0.2403 0.1239  139 ASP A O   
1128 C CB  . ASP A 142 ? 2.1576 2.2854 1.1283 -0.6013 -0.296  0.1278  139 ASP A CB  
1129 C CG  . ASP A 142 ? 2.2572 2.3149 1.1347 -0.5718 -0.3161 0.1225  139 ASP A CG  
1130 O OD1 . ASP A 142 ? 2.2748 2.3171 1.1357 -0.4703 -0.3115 0.1528  139 ASP A OD1 
1131 O OD2 . ASP A 142 ? 2.3156 2.329  1.1291 -0.6544 -0.3352 0.0869  139 ASP A OD2 
1132 N N   . ARG A 143 ? 2.1271 2.1262 1.2205 -0.5579 -0.1912 0.1653  140 ARG A N   
1133 C CA  . ARG A 143 ? 2.1078 2.118  1.24   -0.6175 -0.1682 0.1675  140 ARG A CA  
1134 C C   . ARG A 143 ? 2.2    1.9703 1.2771 -0.6389 -0.1473 0.1705  140 ARG A C   
1135 O O   . ARG A 143 ? 2.2624 1.8929 1.3029 -0.5735 -0.1348 0.1733  140 ARG A O   
1136 C CB  . ARG A 143 ? 2.0592 2.1848 1.2661 -0.5417 -0.1387 0.182   140 ARG A CB  
1137 C CG  . ARG A 143 ? 1.9782 2.3676 1.266  -0.5168 -0.1566 0.1761  140 ARG A CG  
1138 C CD  . ARG A 143 ? 1.9421 2.4953 1.2764 -0.63   -0.1603 0.16    140 ARG A CD  
1139 N NE  . ARG A 143 ? 1.9791 2.498  1.3264 -0.6678 -0.1187 0.1648  140 ARG A NE  
1140 C CZ  . ARG A 143 ? 1.9382 2.5828 1.3562 -0.6158 -0.085  0.1623  140 ARG A CZ  
1141 N NH1 . ARG A 143 ? 1.855  2.6593 1.3461 -0.5127 -0.0889 0.1559  140 ARG A NH1 
1142 N NH2 . ARG A 143 ? 1.9519 2.5594 1.3641 -0.664  -0.0485 0.1654  140 ARG A NH2 
1143 N N   . TYR A 144 ? 2.2058 1.9317 1.2771 -0.7293 -0.1443 0.1719  141 TYR A N   
1144 C CA  . TYR A 144 ? 2.2884 1.7953 1.3149 -0.7445 -0.1329 0.1788  141 TYR A CA  
1145 C C   . TYR A 144 ? 2.2915 1.778  1.3469 -0.6919 -0.099  0.2006  141 TYR A C   
1146 O O   . TYR A 144 ? 2.2276 1.8649 1.3309 -0.6924 -0.0838 0.2078  141 TYR A O   
1147 C CB  . TYR A 144 ? 2.313  1.7535 1.3038 -0.8666 -0.1528 0.1763  141 TYR A CB  
1148 C CG  . TYR A 144 ? 2.3312 1.7496 1.28   -0.9224 -0.184  0.1464  141 TYR A CG  
1149 C CD1 . TYR A 144 ? 2.4126 1.6579 1.3103 -0.8959 -0.1899 0.1248  141 TYR A CD1 
1150 C CD2 . TYR A 144 ? 2.2748 1.8625 1.2383 -0.9999 -0.2051 0.1332  141 TYR A CD2 
1151 C CE1 . TYR A 144 ? 2.4436 1.665  1.2948 -0.9497 -0.2152 0.0893  141 TYR A CE1 
1152 C CE2 . TYR A 144 ? 2.303  1.8748 1.2222 -1.0565 -0.2347 0.1005  141 TYR A CE2 
1153 C CZ  . TYR A 144 ? 2.3962 1.7773 1.2542 -1.0313 -0.2391 0.0777  141 TYR A CZ  
1154 O OH  . TYR A 144 ? 2.4356 1.7941 1.241  -1.0901 -0.2651 0.0378  141 TYR A OH  
1155 N N   . VAL A 145 ? 2.3586 1.67   1.3881 -0.6491 -0.0857 0.2058  142 VAL A N   
1156 C CA  . VAL A 145 ? 2.3659 1.6511 1.4154 -0.6084 -0.0562 0.2228  142 VAL A CA  
1157 C C   . VAL A 145 ? 2.3954 1.6263 1.4259 -0.6917 -0.0635 0.241   142 VAL A C   
1158 O O   . VAL A 145 ? 2.4438 1.5499 1.4579 -0.6804 -0.0588 0.2537  142 VAL A O   
1159 C CB  . VAL A 145 ? 2.4208 1.574  1.4591 -0.5255 -0.0371 0.2199  142 VAL A CB  
1160 C CG1 . VAL A 145 ? 2.3995 1.619  1.4497 -0.4417 -0.023  0.2138  142 VAL A CG1 
1161 C CG2 . VAL A 145 ? 2.497  1.4838 1.4965 -0.5438 -0.0542 0.2075  142 VAL A CG2 
1162 N N   . ASP A 146 ? 2.3638 1.6949 1.3935 -0.7801 -0.0774 0.244   143 ASP A N   
1163 C CA  . ASP A 146 ? 2.3968 1.683  1.3919 -0.8792 -0.0877 0.2668  143 ASP A CA  
1164 C C   . ASP A 146 ? 2.339  1.7833 1.3622 -0.9037 -0.0587 0.2783  143 ASP A C   
1165 O O   . ASP A 146 ? 2.281  1.8467 1.3562 -0.8286 -0.0292 0.2649  143 ASP A O   
1166 C CB  . ASP A 146 ? 2.4312 1.7007 1.3915 -0.9794 -0.12   0.2598  143 ASP A CB  
1167 C CG  . ASP A 146 ? 2.3923 1.8753 1.3931 -1.0068 -0.1211 0.2375  143 ASP A CG  
1168 O OD1 . ASP A 146 ? 2.3184 1.9637 1.38   -0.9348 -0.0994 0.2286  143 ASP A OD1 
1169 O OD2 . ASP A 146 ? 2.4316 1.9171 1.4043 -1.0981 -0.1459 0.2275  143 ASP A OD2 
1170 N N   . GLU A 147 ? 2.3574 1.7913 1.34   -1.0097 -0.0655 0.3018  144 GLU A N   
1171 C CA  . GLU A 147 ? 2.3124 1.8935 1.3062 -1.0566 -0.0355 0.3106  144 GLU A CA  
1172 C C   . GLU A 147 ? 2.2    2.0435 1.2709 -1.0503 -0.0112 0.2794  144 GLU A C   
1173 O O   . GLU A 147 ? 2.1391 2.1316 1.2454 -1.0443 0.0262  0.2709  144 GLU A O   
1174 C CB  . GLU A 147 ? 2.3968 1.9009 1.3132 -1.1915 -0.0543 0.346   144 GLU A CB  
1175 C CG  . GLU A 147 ? 2.4719 1.9725 1.3642 -1.289  -0.083  0.3422  144 GLU A CG  
1176 C CD  . GLU A 147 ? 2.6298 1.9085 1.5131 -1.2626 -0.1176 0.3447  144 GLU A CD  
1177 O OE1 . GLU A 147 ? 2.6239 1.8934 1.5852 -1.2685 -0.1155 0.3375  144 GLU A OE1 
1178 O OE2 . GLU A 147 ? 2.7135 1.8471 1.557  -1.2029 -0.1352 0.3436  144 GLU A OE2 
1179 N N   . THR A 148 ? 2.1692 2.0732 1.2677 -1.0483 -0.0336 0.2592  145 THR A N   
1180 C CA  . THR A 148 ? 2.064  2.2202 1.2417 -1.0405 -0.0253 0.2303  145 THR A CA  
1181 C C   . THR A 148 ? 1.9984 2.2676 1.2503 -0.9068 0.0055  0.2122  145 THR A C   
1182 O O   . THR A 148 ? 1.902  2.3974 1.2278 -0.8978 0.0289  0.1911  145 THR A O   
1183 C CB  . THR A 148 ? 2.0893 2.2405 1.2591 -1.0699 -0.0666 0.2163  145 THR A CB  
1184 O OG1 . THR A 148 ? 2.074  2.3194 1.2314 -1.2097 -0.0771 0.2137  145 THR A OG1 
1185 C CG2 . THR A 148 ? 2.0267 2.3184 1.2648 -0.9662 -0.0745 0.192   145 THR A CG2 
1186 N N   . LEU A 149 ? 2.0473 2.1591 1.2804 -0.8063 0.0079  0.2183  146 LEU A N   
1187 C CA  . LEU A 149 ? 2.003  2.1796 1.2904 -0.6828 0.037   0.204   146 LEU A CA  
1188 C C   . LEU A 149 ? 1.9727 2.204  1.2736 -0.6849 0.0819  0.1988  146 LEU A C   
1189 O O   . LEU A 149 ? 2.0231 2.1745 1.2684 -0.7673 0.0867  0.2166  146 LEU A O   
1190 C CB  . LEU A 149 ? 2.0873 2.0607 1.3353 -0.5984 0.0316  0.2135  146 LEU A CB  
1191 C CG  . LEU A 149 ? 2.1315 2.0578 1.3662 -0.5646 -0.0015 0.2118  146 LEU A CG  
1192 C CD1 . LEU A 149 ? 2.2263 1.9493 1.4154 -0.5019 0.0025  0.2197  146 LEU A CD1 
1193 C CD2 . LEU A 149 ? 2.0589 2.1642 1.3569 -0.4905 -0.0057 0.1988  146 LEU A CD2 
1194 N N   . SER A 150 ? 1.8949 2.249  1.2621 -0.5908 0.1136  0.1745  147 SER A N   
1195 C CA  . SER A 150 ? 1.8707 2.2648 1.2461 -0.5815 0.1621  0.1594  147 SER A CA  
1196 C C   . SER A 150 ? 1.949  2.1202 1.2662 -0.528  0.1702  0.1718  147 SER A C   
1197 O O   . SER A 150 ? 2.005  2.0328 1.2984 -0.478  0.1457  0.1855  147 SER A O   
1198 C CB  . SER A 150 ? 1.7891 2.3876 1.2613 -0.4932 0.1941  0.1212  147 SER A CB  
1199 O OG  . SER A 150 ? 1.8417 2.3579 1.3304 -0.3604 0.1952  0.1168  147 SER A OG  
1200 N N   . GLY A 151 ? 1.9465 2.1014 1.2407 -0.5428 0.2063  0.1634  148 GLY A N   
1201 C CA  . GLY A 151 ? 2.0138 1.9844 1.2597 -0.4992 0.2157  0.1693  148 GLY A CA  
1202 C C   . GLY A 151 ? 2.0022 1.9278 1.2807 -0.3727 0.2299  0.1515  148 GLY A C   
1203 O O   . GLY A 151 ? 2.0711 1.8256 1.312  -0.3364 0.2211  0.1636  148 GLY A O   
1204 N N   . GLY A 152 ? 1.913  1.9948 1.2624 -0.3069 0.2502  0.1239  149 GLY A N   
1205 C CA  . GLY A 152 ? 1.9092 1.9539 1.2878 -0.1821 0.2603  0.1117  149 GLY A CA  
1206 C C   . GLY A 152 ? 1.9252 1.8972 1.2924 -0.1479 0.2164  0.1395  149 GLY A C   
1207 O O   . GLY A 152 ? 1.9822 1.8097 1.3188 -0.0794 0.2173  0.1482  149 GLY A O   
1208 N N   . GLU A 153 ? 1.8759 1.9463 1.2595 -0.2044 0.1796  0.1518  150 GLU A N   
1209 C CA  . GLU A 153 ? 1.8955 1.9106 1.2593 -0.1871 0.1363  0.1734  150 GLU A CA  
1210 C C   . GLU A 153 ? 1.9828 1.7804 1.2685 -0.2217 0.1247  0.1933  150 GLU A C   
1211 O O   . GLU A 153 ? 2.0344 1.7166 1.2896 -0.1634 0.1178  0.203   150 GLU A O   
1212 C CB  . GLU A 153 ? 1.8611 2.036  1.2561 -0.2572 0.1013  0.1743  150 GLU A CB  
1213 C CG  . GLU A 153 ? 1.8098 2.2266 1.298  -0.2121 0.1035  0.1531  150 GLU A CG  
1214 C CD  . GLU A 153 ? 1.8231 2.4203 1.3465 -0.3079 0.0764  0.1475  150 GLU A CD  
1215 O OE1 . GLU A 153 ? 1.8692 2.4163 1.3462 -0.4246 0.073   0.1553  150 GLU A OE1 
1216 O OE2 . GLU A 153 ? 1.7683 2.5563 1.3647 -0.268  0.0563  0.1359  150 GLU A OE2 
1217 N N   . ARG A 154 ? 1.9973 1.74   1.2504 -0.3132 0.1234  0.1995  151 ARG A N   
1218 C CA  . ARG A 154 ? 2.072  1.6235 1.2657 -0.343  0.1092  0.2151  151 ARG A CA  
1219 C C   . ARG A 154 ? 2.1158 1.5377 1.2899 -0.2782 0.1374  0.2109  151 ARG A C   
1220 O O   . ARG A 154 ? 2.1741 1.4626 1.3168 -0.2594 0.1281  0.2174  151 ARG A O   
1221 C CB  . ARG A 154 ? 2.0982 1.6242 1.2628 -0.448  0.096   0.2279  151 ARG A CB  
1222 C CG  . ARG A 154 ? 2.1999 1.536  1.3155 -0.4701 0.0761  0.243   151 ARG A CG  
1223 C CD  . ARG A 154 ? 2.2523 1.5146 1.3513 -0.4734 0.044   0.2443  151 ARG A CD  
1224 N NE  . ARG A 154 ? 2.3396 1.4295 1.4073 -0.4761 0.0311  0.2498  151 ARG A NE  
1225 C CZ  . ARG A 154 ? 2.3897 1.3904 1.4561 -0.4116 0.0473  0.2407  151 ARG A CZ  
1226 N NH1 . ARG A 154 ? 2.3699 1.412  1.4505 -0.342  0.076   0.2311  151 ARG A NH1 
1227 N NH2 . ARG A 154 ? 2.4344 1.3035 1.4863 -0.4167 0.0351  0.2408  151 ARG A NH2 
1228 N N   . LYS A 155 ? 2.0851 1.5492 1.277  -0.2469 0.1751  0.1947  152 LYS A N   
1229 C CA  . LYS A 155 ? 2.1299 1.4699 1.2996 -0.1928 0.2039  0.186   152 LYS A CA  
1230 C C   . LYS A 155 ? 2.1353 1.4355 1.3069 -0.1012 0.2102  0.1861  152 LYS A C   
1231 O O   . LYS A 155 ? 2.1944 1.3548 1.3304 -0.075  0.2194  0.1895  152 LYS A O   
1232 C CB  . LYS A 155 ? 2.1367 1.5181 1.3129 -0.1943 0.2434  0.1626  152 LYS A CB  
1233 C CG  . LYS A 155 ? 2.2378 1.4848 1.3846 -0.1542 0.2732  0.1489  152 LYS A CG  
1234 C CD  . LYS A 155 ? 2.3362 1.465  1.444  -0.2099 0.2571  0.1613  152 LYS A CD  
1235 C CE  . LYS A 155 ? 2.4155 1.4354 1.4998 -0.1816 0.2875  0.1424  152 LYS A CE  
1236 N NZ  . LYS A 155 ? 2.4728 1.4021 1.5343 -0.2311 0.2657  0.1534  152 LYS A NZ  
1237 N N   . ARG A 156 ? 2.0733 1.4976 1.2834 -0.0569 0.2011  0.1856  153 ARG A N   
1238 C CA  . ARG A 156 ? 2.0891 1.4727 1.29   0.0308  0.1967  0.1959  153 ARG A CA  
1239 C C   . ARG A 156 ? 2.1251 1.4175 1.2782 0.0095  0.1653  0.2175  153 ARG A C   
1240 O O   . ARG A 156 ? 2.1837 1.3525 1.2919 0.0533  0.1736  0.2278  153 ARG A O   
1241 C CB  . ARG A 156 ? 2.0333 1.5866 1.2947 0.0909  0.1876  0.1912  153 ARG A CB  
1242 C CG  . ARG A 156 ? 2.0421 1.6452 1.3454 0.1517  0.2293  0.1629  153 ARG A CG  
1243 C CD  . ARG A 156 ? 1.9824 1.7932 1.3685 0.2028  0.2193  0.1503  153 ARG A CD  
1244 N NE  . ARG A 156 ? 1.9775 1.8531 1.4125 0.2533  0.265   0.1114  153 ARG A NE  
1245 C CZ  . ARG A 156 ? 2.0221 1.8366 1.465  0.3637  0.2851  0.1019  153 ARG A CZ  
1246 N NH1 . ARG A 156 ? 2.0718 1.7557 1.4694 0.4314  0.2614  0.1363  153 ARG A NH1 
1247 N NH2 . ARG A 156 ? 1.9901 1.8656 1.4791 0.4052  0.3303  0.0568  153 ARG A NH2 
1248 N N   . ILE A 157 ? 2.0958 1.4351 1.2508 -0.0654 0.1341  0.221   154 ILE A N   
1249 C CA  . ILE A 157 ? 2.1352 1.3856 1.2444 -0.0932 0.1085  0.2303  154 ILE A CA  
1250 C C   . ILE A 157 ? 2.1981 1.2811 1.2704 -0.1069 0.1288  0.2267  154 ILE A C   
1251 O O   . ILE A 157 ? 2.247  1.2338 1.2785 -0.0915 0.1286  0.2294  154 ILE A O   
1252 C CB  . ILE A 157 ? 2.1087 1.4406 1.2283 -0.1735 0.0722  0.2285  154 ILE A CB  
1253 C CG1 . ILE A 157 ? 2.0489 1.5533 1.204  -0.1558 0.048   0.2301  154 ILE A CG1 
1254 C CG2 . ILE A 157 ? 2.1691 1.3839 1.2405 -0.2127 0.0526  0.2269  154 ILE A CG2 
1255 C CD1 . ILE A 157 ? 2.0166 1.6353 1.1966 -0.2423 0.0238  0.2233  154 ILE A CD1 
1256 N N   . GLU A 158 ? 2.192  1.2511 1.2783 -0.1335 0.1479  0.2188  155 GLU A N   
1257 C CA  . GLU A 158 ? 2.2422 1.168  1.3064 -0.1428 0.1644  0.2132  155 GLU A CA  
1258 C C   . GLU A 158 ? 2.275  1.1216 1.3159 -0.0783 0.199   0.21    155 GLU A C   
1259 O O   . GLU A 158 ? 2.3209 1.0618 1.3348 -0.0777 0.2095  0.2067  155 GLU A O   
1260 C CB  . GLU A 158 ? 2.2587 1.192  1.3376 -0.1906 0.1687  0.2088  155 GLU A CB  
1261 C CG  . GLU A 158 ? 2.3558 1.1743 1.4227 -0.2146 0.1666  0.2053  155 GLU A CG  
1262 C CD  . GLU A 158 ? 2.4383 1.2041 1.501  -0.2497 0.1325  0.2095  155 GLU A CD  
1263 O OE1 . GLU A 158 ? 2.4382 1.2427 1.4957 -0.2605 0.1115  0.2136  155 GLU A OE1 
1264 O OE2 . GLU A 158 ? 2.481  1.1692 1.5481 -0.2651 0.1257  0.2051  155 GLU A OE2 
1265 N N   . LEU A 159 ? 2.2509 1.1471 1.3019 -0.024  0.2174  0.2097  156 LEU A N   
1266 C CA  . LEU A 159 ? 2.2939 1.0996 1.313  0.0402  0.2482  0.211   156 LEU A CA  
1267 C C   . LEU A 159 ? 2.3258 1.0838 1.3003 0.0701  0.2336  0.2323  156 LEU A C   
1268 O O   . LEU A 159 ? 2.383  1.0196 1.3085 0.0864  0.2564  0.2367  156 LEU A O   
1269 C CB  . LEU A 159 ? 2.2642 1.1385 1.3106 0.0988  0.2658  0.2035  156 LEU A CB  
1270 C CG  . LEU A 159 ? 2.3037 1.117  1.3468 0.1073  0.3084  0.1785  156 LEU A CG  
1271 C CD1 . LEU A 159 ? 2.3839 1.031  1.3702 0.1293  0.3347  0.1816  156 LEU A CD1 
1272 C CD2 . LEU A 159 ? 2.2967 1.143  1.3574 0.0304  0.3093  0.1614  156 LEU A CD2 
1273 N N   . ALA A 160 ? 2.288  1.1446 1.273  0.068   0.1962  0.2444  157 ALA A N   
1274 C CA  . ALA A 160 ? 2.3202 1.1477 1.2536 0.0855  0.1761  0.2635  157 ALA A CA  
1275 C C   . ALA A 160 ? 2.3664 1.1009 1.2643 0.0314  0.1799  0.2528  157 ALA A C   
1276 O O   . ALA A 160 ? 2.4171 1.0723 1.2536 0.0451  0.188   0.2622  157 ALA A O   
1277 C CB  . ALA A 160 ? 2.265  1.239  1.2238 0.0841  0.1322  0.2718  157 ALA A CB  
1278 N N   . SER A 161 ? 2.3499 1.0909 1.2841 -0.0275 0.1754  0.233   158 SER A N   
1279 C CA  . SER A 161 ? 2.3874 1.0474 1.3068 -0.0694 0.1787  0.216   158 SER A CA  
1280 C C   . SER A 161 ? 2.4341 0.9852 1.3309 -0.0539 0.2205  0.2092  158 SER A C   
1281 O O   . SER A 161 ? 2.4711 0.9566 1.329  -0.0593 0.2343  0.2019  158 SER A O   
1282 C CB  . SER A 161 ? 2.3811 1.0649 1.3468 -0.1248 0.1591  0.2029  158 SER A CB  
1283 O OG  . SER A 161 ? 2.4382 1.0422 1.4024 -0.1523 0.1606  0.1834  158 SER A OG  
1284 N N   . ILE A 162 ? 2.4304 0.9673 1.3461 -0.038  0.2441  0.2085  159 ILE A N   
1285 C CA  . ILE A 162 ? 2.4758 0.9132 1.3687 -0.0301 0.2856  0.2     159 ILE A CA  
1286 C C   . ILE A 162 ? 2.5302 0.8966 1.3509 0.0067  0.3045  0.2188  159 ILE A C   
1287 O O   . ILE A 162 ? 2.5718 0.8539 1.3569 -0.0092 0.3339  0.2109  159 ILE A O   
1288 C CB  . ILE A 162 ? 2.471  0.9153 1.3875 -0.0178 0.3044  0.1937  159 ILE A CB  
1289 C CG1 . ILE A 162 ? 2.4423 0.9484 1.4127 -0.0635 0.2861  0.1797  159 ILE A CG1 
1290 C CG2 . ILE A 162 ? 2.5262 0.8602 1.4075 -0.0096 0.3491  0.1844  159 ILE A CG2 
1291 C CD1 . ILE A 162 ? 2.4661 0.9287 1.4554 -0.1056 0.2862  0.1628  159 ILE A CD1 
1292 N N   . ILE A 163 ? 2.528  0.9353 1.3267 0.0536  0.2855  0.245   160 ILE A N   
1293 C CA  . ILE A 163 ? 2.5889 0.9296 1.3083 0.0949  0.2916  0.2745  160 ILE A CA  
1294 C C   . ILE A 163 ? 2.6213 0.9427 1.2891 0.0626  0.2846  0.2751  160 ILE A C   
1295 O O   . ILE A 163 ? 2.6813 0.9034 1.2773 0.0579  0.314   0.2834  160 ILE A O   
1296 C CB  . ILE A 163 ? 2.5712 0.9831 1.2948 0.1612  0.2623  0.3025  160 ILE A CB  
1297 C CG1 . ILE A 163 ? 2.5711 0.9818 1.336  0.2006  0.2826  0.2939  160 ILE A CG1 
1298 C CG2 . ILE A 163 ? 2.6293 0.9747 1.2621 0.2053  0.2543  0.3424  160 ILE A CG2 
1299 C CD1 . ILE A 163 ? 2.5369 1.0592 1.3409 0.2641  0.2539  0.3073  160 ILE A CD1 
1300 N N   . CYS A 164 ? 2.5849 0.9956 1.284  0.0331  0.2502  0.262   161 CYS A N   
1301 C CA  . CYS A 164 ? 2.6169 1.0152 1.2691 -0.0005 0.2449  0.2509  161 CYS A CA  
1302 C C   . CYS A 164 ? 2.6428 0.9707 1.3027 -0.0424 0.2831  0.2162  161 CYS A C   
1303 O O   . CYS A 164 ? 2.6822 0.9629 1.2813 -0.0602 0.304   0.2078  161 CYS A O   
1304 C CB  . CYS A 164 ? 2.5875 1.0893 1.2723 -0.0255 0.1993  0.2392  161 CYS A CB  
1305 S SG  . CYS A 164 ? 2.6082 1.2286 1.2903 0.0184  0.151   0.2748  161 CYS A SG  
1306 N N   . MET A 165 ? 2.615  0.9468 1.3501 -0.0592 0.2915  0.1945  162 MET A N   
1307 C CA  . MET A 165 ? 2.623  0.9106 1.3872 -0.0926 0.3217  0.1596  162 MET A CA  
1308 C C   . MET A 165 ? 2.6705 0.8732 1.3871 -0.0908 0.3721  0.1637  162 MET A C   
1309 O O   . MET A 165 ? 2.6844 0.8552 1.3931 -0.12   0.4045  0.1368  162 MET A O   
1310 C CB  . MET A 165 ? 2.5844 0.9044 1.4361 -0.1075 0.308   0.1442  162 MET A CB  
1311 C CG  . MET A 165 ? 2.5638 0.9372 1.4606 -0.1283 0.2658  0.1329  162 MET A CG  
1312 S SD  . MET A 165 ? 2.5437 0.9256 1.5244 -0.1507 0.2532  0.1187  162 MET A SD  
1313 C CE  . MET A 165 ? 2.5127 0.8474 1.5192 -0.1619 0.2851  0.0785  162 MET A CE  
1314 N N   . GLU A 166 ? 2.6914 0.8571 1.3805 -0.059  0.3814  0.1927  163 GLU A N   
1315 C CA  . GLU A 166 ? 2.7481 0.812  1.3845 -0.0605 0.4286  0.1998  163 GLU A CA  
1316 C C   . GLU A 166 ? 2.7363 0.7854 1.4189 -0.1097 0.4638  0.1585  163 GLU A C   
1317 O O   . GLU A 166 ? 2.7639 0.7737 1.4083 -0.1406 0.4993  0.1452  163 GLU A O   
1318 C CB  . GLU A 166 ? 2.8404 0.8345 1.3646 -0.0515 0.4429  0.2305  163 GLU A CB  
1319 C CG  . GLU A 166 ? 2.977  0.8459 1.4266 -0.0411 0.481   0.2556  163 GLU A CG  
1320 C CD  . GLU A 166 ? 3.1436 0.9265 1.467  -0.0462 0.4984  0.2897  163 GLU A CD  
1321 O OE1 . GLU A 166 ? 3.1867 0.9768 1.4545 -0.0015 0.4616  0.3311  163 GLU A OE1 
1322 O OE2 . GLU A 166 ? 3.2083 0.9246 1.4866 -0.0982 0.5475  0.2758  163 GLU A OE2 
1323 N N   . PRO A 167 ? 2.6857 0.7859 1.4555 -0.1207 0.4499  0.1358  164 PRO A N   
1324 C CA  . PRO A 167 ? 2.6614 0.772  1.489  -0.1627 0.472   0.0962  164 PRO A CA  
1325 C C   . PRO A 167 ? 2.6969 0.7338 1.4932 -0.1869 0.5211  0.0884  164 PRO A C   
1326 O O   . PRO A 167 ? 2.7422 0.7069 1.4787 -0.167  0.535   0.1131  164 PRO A O   
1327 C CB  . PRO A 167 ? 2.6177 0.7997 1.5303 -0.163  0.432   0.0865  164 PRO A CB  
1328 C CG  . PRO A 167 ? 2.6323 0.8136 1.5185 -0.1308 0.4166  0.1161  164 PRO A CG  
1329 C CD  . PRO A 167 ? 2.6435 0.8024 1.4606 -0.0987 0.4132  0.1454  164 PRO A CD  
1330 N N   . ASP A 168 ? 2.673  0.7305 1.5153 -0.23   0.5468  0.0506  165 ASP A N   
1331 C CA  . ASP A 168 ? 2.7051 0.7069 1.5287 -0.2689 0.5933  0.0351  165 ASP A CA  
1332 C C   . ASP A 168 ? 2.689  0.6991 1.5485 -0.2649 0.5758  0.0317  165 ASP A C   
1333 O O   . ASP A 168 ? 2.738  0.6621 1.5402 -0.269  0.6034  0.0392  165 ASP A O   
1334 C CB  . ASP A 168 ? 2.6962 0.7527 1.5782 -0.3177 0.6218  -0.0106 165 ASP A CB  
1335 C CG  . ASP A 168 ? 2.7855 0.8299 1.6163 -0.328  0.6509  -0.0129 165 ASP A CG  
1336 O OD1 . ASP A 168 ? 2.8715 0.8178 1.5884 -0.3339 0.6821  0.0181  165 ASP A OD1 
1337 O OD2 . ASP A 168 ? 2.7622 0.8898 1.6613 -0.3291 0.6417  -0.0461 165 ASP A OD2 
1338 N N   . LEU A 169 ? 2.6253 0.728  1.5666 -0.2548 0.5283  0.0232  166 LEU A N   
1339 C CA  . LEU A 169 ? 2.611  0.7368 1.5776 -0.2536 0.5068  0.022   166 LEU A CA  
1340 C C   . LEU A 169 ? 2.5885 0.7685 1.5725 -0.2173 0.4573  0.0469  166 LEU A C   
1341 O O   . LEU A 169 ? 2.5559 0.7942 1.587  -0.2147 0.4221  0.0475  166 LEU A O   
1342 C CB  . LEU A 169 ? 2.5667 0.7588 1.6108 -0.2955 0.4969  -0.0128 166 LEU A CB  
1343 C CG  . LEU A 169 ? 2.5747 0.7947 1.6317 -0.304  0.474   -0.0156 166 LEU A CG  
1344 C CD1 . LEU A 169 ? 2.6378 0.7688 1.6209 -0.3064 0.5151  -0.0184 166 LEU A CD1 
1345 C CD2 . LEU A 169 ? 2.535  0.8301 1.6655 -0.345  0.4547  -0.0453 166 LEU A CD2 
1346 N N   . ALA A 170 ? 2.6052 0.7659 1.5529 -0.1913 0.4567  0.0639  167 ALA A N   
1347 C CA  . ALA A 170 ? 2.5846 0.8115 1.5498 -0.1662 0.4158  0.0843  167 ALA A CA  
1348 C C   . ALA A 170 ? 2.5733 0.8375 1.558  -0.1833 0.408   0.0723  167 ALA A C   
1349 O O   . ALA A 170 ? 2.6049 0.8248 1.5537 -0.1736 0.4386  0.0629  167 ALA A O   
1350 C CB  . ALA A 170 ? 2.613  0.8118 1.5254 -0.1168 0.4222  0.1111  167 ALA A CB  
1351 N N   . ILE A 171 ? 2.5327 0.8686 1.5664 -0.2102 0.3679  0.0715  168 ILE A N   
1352 C CA  . ILE A 171 ? 2.5235 0.9029 1.5634 -0.2347 0.3564  0.0637  168 ILE A CA  
1353 C C   . ILE A 171 ? 2.5311 0.9629 1.5594 -0.2143 0.3401  0.0848  168 ILE A C   
1354 O O   . ILE A 171 ? 2.5149 0.9841 1.5614 -0.2117 0.3062  0.1068  168 ILE A O   
1355 C CB  . ILE A 171 ? 2.4877 0.9152 1.5766 -0.2739 0.3149  0.0606  168 ILE A CB  
1356 C CG1 . ILE A 171 ? 2.4884 0.8919 1.6106 -0.2885 0.3284  0.0365  168 ILE A CG1 
1357 C CG2 . ILE A 171 ? 2.4834 0.9526 1.5605 -0.307  0.3039  0.0538  168 ILE A CG2 
1358 C CD1 . ILE A 171 ? 2.464  0.9145 1.6502 -0.3007 0.2814  0.0385  168 ILE A CD1 
1359 N N   . LEU A 172 ? 2.5559 0.9922 1.5561 -0.1995 0.3669  0.0739  169 LEU A N   
1360 C CA  . LEU A 172 ? 2.5586 1.0668 1.5587 -0.1777 0.3578  0.0876  169 LEU A CA  
1361 C C   . LEU A 172 ? 2.5676 1.146  1.5653 -0.2137 0.3538  0.0756  169 LEU A C   
1362 O O   . LEU A 172 ? 2.5847 1.1467 1.5592 -0.2085 0.3899  0.0457  169 LEU A O   
1363 C CB  . LEU A 172 ? 2.5817 1.0531 1.5575 -0.1151 0.3926  0.0844  169 LEU A CB  
1364 C CG  . LEU A 172 ? 2.634  1.024  1.5896 -0.083  0.4001  0.1002  169 LEU A CG  
1365 C CD1 . LEU A 172 ? 2.6755 0.9975 1.5927 -0.0216 0.434   0.0996  169 LEU A CD1 
1366 C CD2 . LEU A 172 ? 2.6196 1.062  1.5948 -0.0823 0.3612  0.1273  169 LEU A CD2 
1367 N N   . ASP A 173 ? 2.5623 1.2104 1.5746 -0.2539 0.3119  0.0975  170 ASP A N   
1368 C CA  . ASP A 173 ? 2.5752 1.2927 1.5701 -0.2986 0.3073  0.0913  170 ASP A CA  
1369 C C   . ASP A 173 ? 2.5812 1.3824 1.5747 -0.2778 0.3303  0.0841  170 ASP A C   
1370 O O   . ASP A 173 ? 2.5572 1.4184 1.5696 -0.2763 0.3088  0.108   170 ASP A O   
1371 C CB  . ASP A 173 ? 2.5846 1.3288 1.5825 -0.355  0.2515  0.1236  170 ASP A CB  
1372 C CG  . ASP A 173 ? 2.6298 1.4221 1.5915 -0.413  0.2425  0.1207  170 ASP A CG  
1373 O OD1 . ASP A 173 ? 2.6439 1.445  1.5808 -0.4135 0.2826  0.084   170 ASP A OD1 
1374 O OD2 . ASP A 173 ? 2.6495 1.4619 1.5999 -0.4597 0.1945  0.1553  170 ASP A OD2 
1375 N N   . GLU A 174 ? 2.6096 1.4176 1.5842 -0.262  0.3757  0.0454  171 GLU A N   
1376 C CA  . GLU A 174 ? 2.6076 1.502  1.5899 -0.2318 0.4089  0.0226  171 GLU A CA  
1377 C C   . GLU A 174 ? 2.6155 1.5408 1.6364 -0.168  0.4049  0.0399  171 GLU A C   
1378 O O   . GLU A 174 ? 2.5718 1.6105 1.6185 -0.1805 0.3882  0.0545  171 GLU A O   
1379 C CB  . GLU A 174 ? 2.5962 1.6077 1.5633 -0.2991 0.4008  0.0224  171 GLU A CB  
1380 C CG  . GLU A 174 ? 2.6622 1.6524 1.58   -0.3491 0.416   -0.0067 171 GLU A CG  
1381 C CD  . GLU A 174 ? 2.713  1.7661 1.5918 -0.4382 0.3821  0.0167  171 GLU A CD  
1382 O OE1 . GLU A 174 ? 2.7491 1.7432 1.608  -0.477  0.3425  0.0394  171 GLU A OE1 
1383 O OE2 . GLU A 174 ? 2.7031 1.8676 1.5697 -0.47   0.395   0.0122  171 GLU A OE2 
1384 N N   . PRO A 175 ? 2.6693 1.4958 1.6889 -0.1046 0.4187  0.0397  172 PRO A N   
1385 C CA  . PRO A 175 ? 2.6697 1.5243 1.7166 -0.043  0.4077  0.0607  172 PRO A CA  
1386 C C   . PRO A 175 ? 2.6489 1.6143 1.7311 0.011   0.4294  0.0399  172 PRO A C   
1387 O O   . PRO A 175 ? 2.6096 1.6591 1.7274 0.041   0.4068  0.0599  172 PRO A O   
1388 C CB  . PRO A 175 ? 2.734  1.4397 1.751  0.0033  0.4211  0.0664  172 PRO A CB  
1389 C CG  . PRO A 175 ? 2.7751 1.3929 1.7587 -0.014  0.4581  0.0314  172 PRO A CG  
1390 C CD  . PRO A 175 ? 2.7261 1.4116 1.7119 -0.094  0.443   0.0231  172 PRO A CD  
1391 N N   . ASP A 176 ? 2.6694 1.6449 1.7458 0.0237  0.4729  -0.0049 173 ASP A N   
1392 C CA  . ASP A 176 ? 2.6433 1.7332 1.7648 0.0841  0.4995  -0.0352 173 ASP A CA  
1393 C C   . ASP A 176 ? 2.5963 1.8714 1.7484 0.0246  0.5012  -0.05   173 ASP A C   
1394 O O   . ASP A 176 ? 2.5346 1.9433 1.7405 0.0693  0.5207  -0.0757 173 ASP A O   
1395 C CB  . ASP A 176 ? 2.7048 1.7019 1.807  0.1453  0.5522  -0.0842 173 ASP A CB  
1396 C CG  . ASP A 176 ? 2.7734 1.7712 1.8403 0.0849  0.5891  -0.133  173 ASP A CG  
1397 O OD1 . ASP A 176 ? 2.7934 1.7749 1.8242 -0.004  0.569   -0.1177 173 ASP A OD1 
1398 O OD2 . ASP A 176 ? 2.7993 1.8114 1.873  0.1299  0.6369  -0.1885 173 ASP A OD2 
1399 N N   . SER A 177 ? 2.6231 1.9084 1.7403 -0.0748 0.4817  -0.0343 174 SER A N   
1400 C CA  . SER A 177 ? 2.5906 2.0359 1.7177 -0.1466 0.481   -0.0385 174 SER A CA  
1401 C C   . SER A 177 ? 2.589  2.0875 1.7337 -0.1909 0.4284  0.0129  174 SER A C   
1402 O O   . SER A 177 ? 2.6346 2.0226 1.7608 -0.1977 0.3906  0.0497  174 SER A O   
1403 C CB  . SER A 177 ? 2.6389 2.0592 1.7021 -0.2311 0.4911  -0.0514 174 SER A CB  
1404 O OG  . SER A 177 ? 2.6387 2.1475 1.7006 -0.2267 0.546   -0.1096 174 SER A OG  
1405 N N   . GLY A 178 ? 2.5333 2.2022 1.7147 -0.2218 0.4295  0.0097  175 GLY A N   
1406 C CA  . GLY A 178 ? 2.5284 2.2526 1.7263 -0.2677 0.3828  0.0518  175 GLY A CA  
1407 C C   . GLY A 178 ? 2.4989 2.2983 1.7647 -0.1897 0.3725  0.0519  175 GLY A C   
1408 O O   . GLY A 178 ? 2.4594 2.3581 1.7521 -0.2277 0.3426  0.0721  175 GLY A O   
1409 N N   . ILE A 179 ? 2.5203 2.2654 1.8081 -0.0824 0.3934  0.0318  176 ILE A N   
1410 C CA  . ILE A 179 ? 2.4918 2.3063 1.8406 0.0086  0.3816  0.0331  176 ILE A CA  
1411 C C   . ILE A 179 ? 2.4298 2.4121 1.852  0.07    0.4236  -0.0171 176 ILE A C   
1412 O O   . ILE A 179 ? 2.3734 2.4596 1.8628 0.145   0.4101  -0.0186 176 ILE A O   
1413 C CB  . ILE A 179 ? 2.5667 2.1985 1.8831 0.0902  0.3712  0.0525  176 ILE A CB  
1414 C CG1 . ILE A 179 ? 2.6114 2.1469 1.9148 0.1649  0.4194  0.0164  176 ILE A CG1 
1415 C CG2 . ILE A 179 ? 2.6454 2.1226 1.8964 0.0295  0.342   0.0882  176 ILE A CG2 
1416 C CD1 . ILE A 179 ? 2.6946 2.0574 1.9622 0.2434  0.4144  0.0359  176 ILE A CD1 
1417 N N   . ASP A 180 ? 2.4371 2.4484 1.8461 0.0405  0.4735  -0.0609 177 ASP A N   
1418 C CA  . ASP A 180 ? 2.3841 2.5471 1.856  0.0901  0.5256  -0.1223 177 ASP A CA  
1419 C C   . ASP A 180 ? 2.4072 2.5127 1.9216 0.2363  0.5364  -0.141  177 ASP A C   
1420 O O   . ASP A 180 ? 2.3253 2.5868 1.9313 0.3145  0.5378  -0.1611 177 ASP A O   
1421 C CB  . ASP A 180 ? 2.2928 2.7148 1.8377 0.04    0.5238  -0.1325 177 ASP A CB  
1422 C CG  . ASP A 180 ? 2.3419 2.8185 1.8324 -0.1084 0.527   -0.1218 177 ASP A CG  
1423 O OD1 . ASP A 180 ? 2.4228 2.7644 1.8273 -0.1614 0.5399  -0.1197 177 ASP A OD1 
1424 O OD2 . ASP A 180 ? 2.2923 2.9471 1.8225 -0.1746 0.5149  -0.1143 177 ASP A OD2 
1425 N N   . ILE A 181 ? 2.5204 2.396  1.9652 0.2699  0.5409  -0.1314 178 ILE A N   
1426 C CA  . ILE A 181 ? 2.5841 2.3262 2.031  0.3947  0.5459  -0.1337 178 ILE A CA  
1427 C C   . ILE A 181 ? 2.5378 2.3879 2.0662 0.5061  0.5847  -0.1915 178 ILE A C   
1428 O O   . ILE A 181 ? 2.5076 2.4347 2.0531 0.493   0.6385  -0.2547 178 ILE A O   
1429 C CB  . ILE A 181 ? 2.7097 2.1998 2.0589 0.3794  0.5629  -0.1307 178 ILE A CB  
1430 C CG1 . ILE A 181 ? 2.791  2.1044 2.1126 0.4742  0.5442  -0.0971 178 ILE A CG1 
1431 C CG2 . ILE A 181 ? 2.7339 2.1933 2.0585 0.3674  0.6255  -0.1983 178 ILE A CG2 
1432 C CD1 . ILE A 181 ? 2.9152 1.998  2.1422 0.438   0.555   -0.0858 178 ILE A CD1 
1433 N N   . VAL A 182 ? 2.5261 2.3923 2.1064 0.6174  0.5535  -0.1688 179 VAL A N   
1434 C CA  . VAL A 182 ? 2.4817 2.4421 2.1521 0.7503  0.5748  -0.2129 179 VAL A CA  
1435 C C   . VAL A 182 ? 2.5961 2.3156 2.2079 0.8315  0.6136  -0.2399 179 VAL A C   
1436 O O   . VAL A 182 ? 2.5724 2.3259 2.2219 0.8848  0.6685  -0.3117 179 VAL A O   
1437 C CB  . VAL A 182 ? 2.4416 2.4926 2.1761 0.8343  0.5111  -0.164  179 VAL A CB  
1438 C CG1 . VAL A 182 ? 2.3955 2.5109 2.2271 0.9914  0.5202  -0.201  179 VAL A CG1 
1439 C CG2 . VAL A 182 ? 2.3477 2.6419 2.1405 0.7453  0.4758  -0.1459 179 VAL A CG2 
1440 N N   . SER A 183 ? 2.72   2.1931 2.2343 0.8316  0.5889  -0.1862 180 SER A N   
1441 C CA  . SER A 183 ? 2.8341 2.0608 2.2897 0.879   0.6135  -0.2056 180 SER A CA  
1442 C C   . SER A 183 ? 2.9616 1.9534 2.2864 0.8105  0.6014  -0.1485 180 SER A C   
1443 O O   . SER A 183 ? 2.9617 1.9748 2.267  0.7638  0.5542  -0.0875 180 SER A O   
1444 C CB  . SER A 183 ? 2.781  2.051  2.4064 0.9524  0.544   -0.2281 180 SER A CB  
1445 O OG  . SER A 183 ? 2.8342 1.9727 2.5149 0.9453  0.5337  -0.2854 180 SER A OG  
1446 N N   . PHE A 184 ? 3.0215 1.8589 2.321  0.7691  0.6153  -0.1882 181 PHE A N   
1447 C CA  . PHE A 184 ? 3.1196 1.7658 2.3238 0.6962  0.6016  -0.1472 181 PHE A CA  
1448 C C   . PHE A 184 ? 3.1373 1.6917 2.3516 0.7354  0.5391  -0.0873 181 PHE A C   
1449 O O   . PHE A 184 ? 3.2091 1.6406 2.3443 0.676   0.5283  -0.0429 181 PHE A O   
1450 C CB  . PHE A 184 ? 3.1601 1.7088 2.357  0.6389  0.62    -0.2091 181 PHE A CB  
1451 C CG  . PHE A 184 ? 3.1649 1.7835 2.3209 0.5617  0.6739  -0.2536 181 PHE A CG  
1452 C CD1 . PHE A 184 ? 3.2059 1.8214 2.2764 0.475   0.693   -0.2114 181 PHE A CD1 
1453 C CD2 . PHE A 184 ? 3.13   1.8339 2.3458 0.5681  0.6951  -0.3418 181 PHE A CD2 
1454 C CE1 . PHE A 184 ? 3.1803 1.9042 2.2502 0.3835  0.7131  -0.2518 181 PHE A CE1 
1455 C CE2 . PHE A 184 ? 3.1305 1.9091 2.3013 0.4886  0.7419  -0.3792 181 PHE A CE2 
1456 C CZ  . PHE A 184 ? 3.1656 1.9234 2.2433 0.3959  0.7637  -0.3288 181 PHE A CZ  
1457 N N   . ASP A 185 ? 3.0651 1.6835 2.3814 0.8282  0.4983  -0.0872 182 ASP A N   
1458 C CA  . ASP A 185 ? 3.0738 1.6162 2.4041 0.8598  0.4345  -0.0245 182 ASP A CA  
1459 C C   . ASP A 185 ? 3.0857 1.6424 2.3138 0.8498  0.4221  0.0549  182 ASP A C   
1460 O O   . ASP A 185 ? 3.1371 1.5919 2.3232 0.8274  0.3833  0.1097  182 ASP A O   
1461 C CB  . ASP A 185 ? 2.995  1.6504 2.5071 0.9389  0.38    -0.0489 182 ASP A CB  
1462 C CG  . ASP A 185 ? 2.9963 1.657  2.6526 0.937   0.3768  -0.1413 182 ASP A CG  
1463 O OD1 . ASP A 185 ? 3.0638 1.6011 2.6626 0.8811  0.399   -0.1701 182 ASP A OD1 
1464 O OD2 . ASP A 185 ? 2.9199 1.7085 2.7502 0.9911  0.3531  -0.1879 182 ASP A OD2 
1465 N N   . GLU A 186 ? 3.0362 1.7196 2.2195 0.8624  0.4572  0.0603  183 GLU A N   
1466 C CA  . GLU A 186 ? 2.9966 1.7643 2.1622 0.8094  0.4128  0.1126  183 GLU A CA  
1467 C C   . GLU A 186 ? 3.0408 1.7072 2.1339 0.6859  0.4229  0.1225  183 GLU A C   
1468 O O   . GLU A 186 ? 3.0729 1.6888 2.1158 0.6552  0.3898  0.1706  183 GLU A O   
1469 C CB  . GLU A 186 ? 2.8767 1.9299 2.1532 0.7986  0.3873  0.0969  183 GLU A CB  
1470 C CG  . GLU A 186 ? 2.8397 2.0276 2.1679 0.7214  0.426   0.0386  183 GLU A CG  
1471 C CD  . GLU A 186 ? 2.7362 2.1941 2.183  0.7532  0.4182  0.0093  183 GLU A CD  
1472 O OE1 . GLU A 186 ? 2.6705 2.291  2.152  0.6576  0.4126  -0.0001 183 GLU A OE1 
1473 O OE2 . GLU A 186 ? 2.7118 2.2189 2.2178 0.8742  0.4166  -0.0036 183 GLU A OE2 
1474 N N   . ILE A 187 ? 3.0435 1.6767 2.1279 0.619   0.4678  0.0757  184 ILE A N   
1475 C CA  . ILE A 187 ? 3.0875 1.6315 2.1135 0.5101  0.4738  0.083   184 ILE A CA  
1476 C C   . ILE A 187 ? 3.1848 1.4865 2.1149 0.5183  0.4934  0.102   184 ILE A C   
1477 O O   . ILE A 187 ? 3.2281 1.4608 2.1098 0.457   0.4813  0.1309  184 ILE A O   
1478 C CB  . ILE A 187 ? 3.066  1.6821 2.1146 0.4265  0.503   0.0337  184 ILE A CB  
1479 C CG1 . ILE A 187 ? 3.0865 1.7025 2.1121 0.3175  0.4823  0.0526  184 ILE A CG1 
1480 C CG2 . ILE A 187 ? 3.1258 1.6174 2.1395 0.4388  0.5579  -0.0166 184 ILE A CG2 
1481 C CD1 . ILE A 187 ? 3.0429 1.797  2.107  0.2893  0.4343  0.0855  184 ILE A CD1 
1482 N N   . LYS A 188 ? 3.2161 1.3894 2.119  0.5953  0.5243  0.0849  185 LYS A N   
1483 C CA  . LYS A 188 ? 3.3014 1.2571 2.1303 0.5969  0.5361  0.1002  185 LYS A CA  
1484 C C   . LYS A 188 ? 3.3161 1.2317 2.1124 0.6182  0.4886  0.169   185 LYS A C   
1485 O O   . LYS A 188 ? 3.3657 1.1792 2.1198 0.5558  0.4831  0.1904  185 LYS A O   
1486 C CB  . LYS A 188 ? 3.2685 1.247  2.2191 0.6427  0.5139  0.0505  185 LYS A CB  
1487 C CG  . LYS A 188 ? 3.3124 1.2087 2.3289 0.6058  0.4633  0.0555  185 LYS A CG  
1488 C CD  . LYS A 188 ? 3.3082 1.2225 2.4417 0.5996  0.4505  -0.0202 185 LYS A CD  
1489 C CE  . LYS A 188 ? 3.2523 1.2988 2.5366 0.6822  0.4147  -0.0622 185 LYS A CE  
1490 N NZ  . LYS A 188 ? 3.2483 1.283  2.6317 0.6819  0.4045  -0.1421 185 LYS A NZ  
1491 N N   . ARG A 189 ? 3.2663 1.2797 2.0825 0.7003  0.4541  0.2025  186 ARG A N   
1492 C CA  . ARG A 189 ? 3.2776 1.277  2.0631 0.7166  0.4012  0.2678  186 ARG A CA  
1493 C C   . ARG A 189 ? 3.2877 1.2853 2.0055 0.626   0.4005  0.2909  186 ARG A C   
1494 O O   . ARG A 189 ? 3.3576 1.2442 1.9882 0.6115  0.3896  0.3357  186 ARG A O   
1495 C CB  . ARG A 189 ? 3.2061 1.3864 2.0913 0.8016  0.3404  0.2863  186 ARG A CB  
1496 C CG  . ARG A 189 ? 3.1911 1.5498 2.0818 0.7964  0.3224  0.2969  186 ARG A CG  
1497 C CD  . ARG A 189 ? 3.1059 1.6909 2.1607 0.8633  0.2639  0.2871  186 ARG A CD  
1498 N NE  . ARG A 189 ? 3.0786 1.8461 2.1448 0.8618  0.2292  0.3074  186 ARG A NE  
1499 C CZ  . ARG A 189 ? 3.0821 1.9144 2.1641 0.8553  0.1596  0.354   186 ARG A CZ  
1500 N NH1 . ARG A 189 ? 3.1179 1.8403 2.1964 0.846   0.1213  0.3941  186 ARG A NH1 
1501 N NH2 . ARG A 189 ? 3.0332 2.0242 2.102  0.8653  0.1359  0.3666  186 ARG A NH2 
1502 N N   . VAL A 190 ? 3.1978 1.3382 1.9837 0.5504  0.4034  0.2544  187 VAL A N   
1503 C CA  . VAL A 190 ? 3.1774 1.3506 1.9506 0.4562  0.3907  0.2625  187 VAL A CA  
1504 C C   . VAL A 190 ? 3.2308 1.2508 1.9469 0.3867  0.4339  0.2458  187 VAL A C   
1505 O O   . VAL A 190 ? 3.2721 1.2225 1.9322 0.342   0.433   0.2677  187 VAL A O   
1506 C CB  . VAL A 190 ? 3.0916 1.4618 1.9554 0.4073  0.3725  0.2349  187 VAL A CB  
1507 C CG1 . VAL A 190 ? 3.0984 1.4838 1.9515 0.3168  0.3586  0.2396  187 VAL A CG1 
1508 C CG2 . VAL A 190 ? 3.0212 1.5604 1.9466 0.4655  0.332   0.2475  187 VAL A CG2 
1509 N N   . PHE A 191 ? 3.2274 1.2025 1.9572 0.3758  0.4733  0.2029  188 PHE A N   
1510 C CA  . PHE A 191 ? 3.2797 1.1263 1.9641 0.3064  0.5142  0.1795  188 PHE A CA  
1511 C C   . PHE A 191 ? 3.3783 1.025  1.9598 0.317   0.5355  0.2106  188 PHE A C   
1512 O O   . PHE A 191 ? 3.413  0.9926 1.9542 0.2453  0.5535  0.2112  188 PHE A O   
1513 C CB  . PHE A 191 ? 3.2714 1.1055 1.9796 0.3022  0.5507  0.1255  188 PHE A CB  
1514 C CG  . PHE A 191 ? 3.1969 1.1907 1.9778 0.2471  0.5429  0.0899  188 PHE A CG  
1515 C CD1 . PHE A 191 ? 3.1328 1.2857 1.9689 0.2286  0.5008  0.108   188 PHE A CD1 
1516 C CD2 . PHE A 191 ? 3.2092 1.1871 1.9934 0.2103  0.5765  0.0396  188 PHE A CD2 
1517 C CE1 . PHE A 191 ? 3.0805 1.3619 1.969  0.1742  0.4918  0.0829  188 PHE A CE1 
1518 C CE2 . PHE A 191 ? 3.1524 1.2724 1.9884 0.1571  0.5658  0.0141  188 PHE A CE2 
1519 C CZ  . PHE A 191 ? 3.0845 1.3497 1.97   0.1393  0.5231  0.0393  188 PHE A CZ  
1520 N N   . ASP A 192 ? 3.4215 0.9738 1.9605 0.4062  0.5338  0.2364  189 ASP A N   
1521 C CA  . ASP A 192 ? 3.4633 0.9165 1.9892 0.4019  0.5127  0.2701  189 ASP A CA  
1522 C C   . ASP A 192 ? 3.483  0.9305 1.9408 0.3852  0.4904  0.3251  189 ASP A C   
1523 O O   . ASP A 192 ? 3.5053 0.9013 1.9527 0.3274  0.4857  0.3441  189 ASP A O   
1524 C CB  . ASP A 192 ? 3.4408 0.9372 2.079  0.4805  0.4593  0.2772  189 ASP A CB  
1525 C CG  . ASP A 192 ? 3.4463 0.9973 2.221  0.4742  0.4529  0.2101  189 ASP A CG  
1526 O OD1 . ASP A 192 ? 3.4653 1.0093 2.2307 0.4071  0.4915  0.1632  189 ASP A OD1 
1527 O OD2 . ASP A 192 ? 3.4224 1.0179 2.308  0.5373  0.4095  0.2017  189 ASP A OD2 
1528 N N   . TYR A 193 ? 3.4555 0.9879 1.8879 0.4259  0.4701  0.3459  190 TYR A N   
1529 C CA  . TYR A 193 ? 3.4613 1.0233 1.8463 0.4028  0.4399  0.3876  190 TYR A CA  
1530 C C   . TYR A 193 ? 3.4492 1.0158 1.8298 0.2958  0.4664  0.3621  190 TYR A C   
1531 O O   . TYR A 193 ? 3.5067 0.9892 1.8019 0.2581  0.4779  0.3875  190 TYR A O   
1532 C CB  . TYR A 193 ? 3.3775 1.14   1.8372 0.4412  0.3829  0.3969  190 TYR A CB  
1533 C CG  . TYR A 193 ? 3.4023 1.2019 1.8082 0.4191  0.3483  0.4348  190 TYR A CG  
1534 C CD1 . TYR A 193 ? 3.4641 1.2145 1.7911 0.4832  0.3139  0.493   190 TYR A CD1 
1535 C CD2 . TYR A 193 ? 3.3761 1.2627 1.809  0.3377  0.3465  0.4107  190 TYR A CD2 
1536 C CE1 . TYR A 193 ? 3.4835 1.275  1.7511 0.4572  0.2815  0.5242  190 TYR A CE1 
1537 C CE2 . TYR A 193 ? 3.3963 1.3165 1.7761 0.3152  0.3189  0.4356  190 TYR A CE2 
1538 C CZ  . TYR A 193 ? 3.4561 1.3335 1.7503 0.371   0.2872  0.4912  190 TYR A CZ  
1539 O OH  . TYR A 193 ? 3.4891 1.4024 1.719  0.3423  0.2603  0.5129  190 TYR A OH  
1540 N N   . LEU A 194 ? 3.3733 1.0409 1.8446 0.2483  0.4757  0.3121  191 LEU A N   
1541 C CA  . LEU A 194 ? 3.3572 1.0433 1.8438 0.158   0.4955  0.284   191 LEU A CA  
1542 C C   . LEU A 194 ? 3.4204 0.9467 1.8407 0.1118  0.5495  0.2732  191 LEU A C   
1543 O O   . LEU A 194 ? 3.4445 0.9363 1.8261 0.0529  0.5698  0.2735  191 LEU A O   
1544 C CB  . LEU A 194 ? 3.2808 1.1047 1.8747 0.126   0.4843  0.2407  191 LEU A CB  
1545 C CG  . LEU A 194 ? 3.2267 1.2115 1.8849 0.1456  0.4347  0.2473  191 LEU A CG  
1546 C CD1 . LEU A 194 ? 3.1726 1.2635 1.9165 0.1129  0.4276  0.2116  191 LEU A CD1 
1547 C CD2 . LEU A 194 ? 3.2275 1.2491 1.8684 0.115   0.4128  0.2612  191 LEU A CD2 
1548 N N   . LYS A 195 ? 3.447  0.8762 1.8515 0.1359  0.5755  0.2603  192 LYS A N   
1549 C CA  . LYS A 195 ? 3.5144 0.7949 1.8631 0.0863  0.6229  0.247   192 LYS A CA  
1550 C C   . LYS A 195 ? 3.5241 0.7792 1.8594 0.0766  0.5958  0.2961  192 LYS A C   
1551 O O   . LYS A 195 ? 3.524  0.7773 1.8718 0       0.611   0.2883  192 LYS A O   
1552 C CB  . LYS A 195 ? 3.5044 0.7979 1.9392 0.1173  0.6092  0.22    192 LYS A CB  
1553 C CG  . LYS A 195 ? 3.5093 0.8244 2.0409 0.0471  0.5981  0.191   192 LYS A CG  
1554 C CD  . LYS A 195 ? 3.5044 0.8434 2.1363 0.0845  0.5672  0.1634  192 LYS A CD  
1555 C CE  . LYS A 195 ? 3.505  0.8581 2.2129 0.0129  0.5612  0.1247  192 LYS A CE  
1556 N NZ  . LYS A 195 ? 3.4974 0.8624 2.2784 0.0456  0.5438  0.0794  192 LYS A NZ  
1557 N N   . ASP A 196 ? 3.5251 0.7732 1.8362 0.1508  0.5552  0.348   193 ASP A N   
1558 C CA  . ASP A 196 ? 3.5327 0.7649 1.828  0.1392  0.524   0.4038  193 ASP A CA  
1559 C C   . ASP A 196 ? 3.5422 0.7967 1.7681 0.078   0.5425  0.4122  193 ASP A C   
1560 O O   . ASP A 196 ? 3.5443 0.7986 1.7677 0.0288  0.5371  0.4407  193 ASP A O   
1561 C CB  . ASP A 196 ? 3.5299 0.8044 1.8569 0.2295  0.4588  0.4572  193 ASP A CB  
1562 C CG  . ASP A 196 ? 3.5251 0.8486 2.0094 0.2745  0.4132  0.4479  193 ASP A CG  
1563 O OD1 . ASP A 196 ? 3.5308 0.8173 2.0787 0.2299  0.4119  0.4389  193 ASP A OD1 
1564 O OD2 . ASP A 196 ? 3.5088 0.9048 2.0498 0.3532  0.3817  0.4442  193 ASP A OD2 
1565 N N   . LYS A 197 ? 3.5439 0.8198 1.7168 0.0783  0.5652  0.3851  194 LYS A N   
1566 C CA  . LYS A 197 ? 3.5489 0.8519 1.6676 0.0215  0.5843  0.3763  194 LYS A CA  
1567 C C   . LYS A 197 ? 3.5317 0.8397 1.6843 -0.0725 0.6357  0.3253  194 LYS A C   
1568 O O   . LYS A 197 ? 3.5259 0.8774 1.6634 -0.125  0.6514  0.3129  194 LYS A O   
1569 C CB  . LYS A 197 ? 3.4767 0.956  1.6851 0.0465  0.537   0.3597  194 LYS A CB  
1570 C CG  . LYS A 197 ? 3.5133 1.0326 1.6989 0.1267  0.4817  0.4061  194 LYS A CG  
1571 C CD  . LYS A 197 ? 3.5913 1.1121 1.6981 0.1163  0.4599  0.4493  194 LYS A CD  
1572 C CE  . LYS A 197 ? 3.5981 1.2244 1.7269 0.1862  0.3894  0.4894  194 LYS A CE  
1573 N NZ  . LYS A 197 ? 3.5775 1.3244 1.7475 0.1867  0.3676  0.4569  194 LYS A NZ  
1574 N N   . GLY A 198 ? 3.5157 0.7919 1.7172 -0.0924 0.6608  0.291   195 GLY A N   
1575 C CA  . GLY A 198 ? 3.4874 0.7859 1.7337 -0.1785 0.7035  0.2404  195 GLY A CA  
1576 C C   . GLY A 198 ? 3.3939 0.8201 1.7591 -0.1912 0.6926  0.1877  195 GLY A C   
1577 O O   . GLY A 198 ? 3.3605 0.8355 1.7797 -0.2565 0.718   0.1442  195 GLY A O   
1578 N N   . CYS A 199 ? 3.3349 0.8414 1.7605 -0.1305 0.6461  0.1925  196 CYS A N   
1579 C CA  . CYS A 199 ? 3.2463 0.8892 1.7901 -0.1422 0.6212  0.1532  196 CYS A CA  
1580 C C   . CYS A 199 ? 3.2333 0.8469 1.8035 -0.162  0.6407  0.121   196 CYS A C   
1581 O O   . CYS A 199 ? 3.2917 0.7877 1.7999 -0.1388 0.6624  0.1306  196 CYS A O   
1582 C CB  . CYS A 199 ? 3.2125 0.9588 1.8021 -0.0845 0.567   0.1709  196 CYS A CB  
1583 S SG  . CYS A 199 ? 3.2763 1.0538 1.8206 -0.0593 0.5386  0.2078  196 CYS A SG  
1584 N N   . SER A 200 ? 3.1533 0.8744 1.8144 -0.2006 0.6283  0.0827  197 SER A N   
1585 C CA  . SER A 200 ? 3.1319 0.8594 1.8251 -0.224  0.6359  0.0485  197 SER A CA  
1586 C C   . SER A 200 ? 3.0561 0.9036 1.8172 -0.192  0.5876  0.0488  197 SER A C   
1587 O O   . SER A 200 ? 3.0072 0.9528 1.8215 -0.1892 0.551   0.0568  197 SER A O   
1588 C CB  . SER A 200 ? 3.1183 0.8852 1.8579 -0.3003 0.6544  0.0074  197 SER A CB  
1589 O OG  . SER A 200 ? 3.2064 0.8578 1.8769 -0.3444 0.7078  0.0011  197 SER A OG  
1590 N N   . LEU A 201 ? 3.0492 0.8832 1.802  -0.1694 0.5902  0.039   198 LEU A N   
1591 C CA  . LEU A 201 ? 2.9872 0.937  1.7935 -0.1484 0.5513  0.0392  198 LEU A CA  
1592 C C   . LEU A 201 ? 2.9612 0.9534 1.7963 -0.1954 0.5526  0.0012  198 LEU A C   
1593 O O   . LEU A 201 ? 3.0016 0.913  1.7979 -0.2138 0.5897  -0.0272 198 LEU A O   
1594 C CB  . LEU A 201 ? 3.0006 0.9339 1.7799 -0.0776 0.5511  0.0567  198 LEU A CB  
1595 C CG  . LEU A 201 ? 3.048  0.9251 1.7823 -0.0219 0.5483  0.0974  198 LEU A CG  
1596 C CD1 . LEU A 201 ? 3.0532 0.9413 1.7823 0.0539  0.5421  0.1088  198 LEU A CD1 
1597 C CD2 . LEU A 201 ? 3.0167 0.9763 1.7798 -0.0296 0.5118  0.1212  198 LEU A CD2 
1598 N N   . LEU A 202 ? 2.8973 1.0075 1.7916 -0.218  0.5104  0.0013  199 LEU A N   
1599 C CA  . LEU A 202 ? 2.8748 1.0395 1.7885 -0.2631 0.5012  -0.0275 199 LEU A CA  
1600 C C   . LEU A 202 ? 2.8551 1.0938 1.773  -0.2386 0.4805  -0.0176 199 LEU A C   
1601 O O   . LEU A 202 ? 2.8144 1.1425 1.7689 -0.248  0.4367  0.0036  199 LEU A O   
1602 C CB  . LEU A 202 ? 2.8307 1.0696 1.8035 -0.3097 0.4642  -0.0302 199 LEU A CB  
1603 C CG  . LEU A 202 ? 2.8231 1.1234 1.8104 -0.3604 0.4451  -0.0544 199 LEU A CG  
1604 C CD1 . LEU A 202 ? 2.8672 1.1005 1.8104 -0.3933 0.4917  -0.0973 199 LEU A CD1 
1605 C CD2 . LEU A 202 ? 2.786  1.1578 1.8393 -0.3911 0.4014  -0.0514 199 LEU A CD2 
1606 N N   . VAL A 203 ? 2.8881 1.0851 1.7679 -0.2041 0.514   -0.0327 200 VAL A N   
1607 C CA  . VAL A 203 ? 2.8764 1.1538 1.7636 -0.1755 0.5061  -0.0307 200 VAL A CA  
1608 C C   . VAL A 203 ? 2.8701 1.222  1.7564 -0.2272 0.4999  -0.058  200 VAL A C   
1609 O O   . VAL A 203 ? 2.8978 1.203  1.7498 -0.2464 0.534   -0.0997 200 VAL A O   
1610 C CB  . VAL A 203 ? 2.9217 1.1308 1.7778 -0.1061 0.5453  -0.0409 200 VAL A CB  
1611 C CG1 . VAL A 203 ? 2.8853 1.2054 1.7655 -0.0727 0.5402  -0.045  200 VAL A CG1 
1612 C CG2 . VAL A 203 ? 2.9603 1.0908 1.8017 -0.0572 0.5452  -0.0055 200 VAL A CG2 
1613 N N   . ILE A 204 ? 2.8391 1.2998 1.7524 -0.2534 0.4572  -0.0347 201 ILE A N   
1614 C CA  . ILE A 204 ? 2.8387 1.3753 1.7372 -0.3087 0.4456  -0.0512 201 ILE A CA  
1615 C C   . ILE A 204 ? 2.8413 1.4461 1.7287 -0.2836 0.4707  -0.0668 201 ILE A C   
1616 O O   . ILE A 204 ? 2.813  1.4752 1.728  -0.2515 0.4573  -0.0397 201 ILE A O   
1617 C CB  . ILE A 204 ? 2.8144 1.4176 1.7388 -0.3537 0.3827  -0.011  201 ILE A CB  
1618 C CG1 . ILE A 204 ? 2.8336 1.3847 1.7918 -0.3585 0.3583  0.0028  201 ILE A CG1 
1619 C CG2 . ILE A 204 ? 2.8071 1.4777 1.7008 -0.4172 0.3635  -0.0187 201 ILE A CG2 
1620 C CD1 . ILE A 204 ? 2.8679 1.3745 1.8179 -0.39   0.3755  -0.0318 201 ILE A CD1 
1621 N N   . THR A 205 ? 2.871  1.4758 1.7211 -0.2976 0.5101  -0.1164 202 THR A N   
1622 C CA  . THR A 205 ? 2.8694 1.5524 1.7166 -0.2708 0.5421  -0.143  202 THR A CA  
1623 C C   . THR A 205 ? 2.8983 1.6235 1.6961 -0.3247 0.5696  -0.1948 202 THR A C   
1624 O O   . THR A 205 ? 2.9343 1.5964 1.6938 -0.368  0.5757  -0.2217 202 THR A O   
1625 C CB  . THR A 205 ? 2.9007 1.5134 1.7614 -0.1783 0.584   -0.162  202 THR A CB  
1626 O OG1 . THR A 205 ? 2.8671 1.5878 1.7514 -0.1406 0.606   -0.1821 202 THR A OG1 
1627 C CG2 . THR A 205 ? 2.9675 1.4383 1.7837 -0.1678 0.6298  -0.2101 202 THR A CG2 
1628 N N   . HIS A 206 ? 2.8765 1.7199 1.6737 -0.3283 0.5873  -0.212  203 HIS A N   
1629 C CA  . HIS A 206 ? 2.9004 1.7955 1.644  -0.3758 0.6237  -0.2696 203 HIS A CA  
1630 C C   . HIS A 206 ? 2.9307 1.7934 1.6799 -0.3007 0.6949  -0.3393 203 HIS A C   
1631 O O   . HIS A 206 ? 2.9497 1.8127 1.6496 -0.3279 0.7381  -0.4047 203 HIS A O   
1632 C CB  . HIS A 206 ? 2.8643 1.9203 1.5959 -0.4332 0.6095  -0.2536 203 HIS A CB  
1633 C CG  . HIS A 206 ? 2.8858 1.9807 1.6158 -0.4936 0.539   -0.179  203 HIS A CG  
1634 N ND1 . HIS A 206 ? 2.8898 1.9912 1.6765 -0.4605 0.503   -0.1237 203 HIS A ND1 
1635 C CD2 . HIS A 206 ? 2.907  2.0428 1.5795 -0.5837 0.5006  -0.1542 203 HIS A CD2 
1636 C CE1 . HIS A 206 ? 2.8947 2.0224 1.6593 -0.5285 0.446   -0.0701 203 HIS A CE1 
1637 N NE2 . HIS A 206 ? 2.9095 2.0572 1.6057 -0.6012 0.4397  -0.0818 203 HIS A NE2 
1638 N N   . ARG A 207 ? 2.9289 1.7732 1.7374 -0.2054 0.7042  -0.3257 204 ARG A N   
1639 C CA  . ARG A 207 ? 2.9479 1.7605 1.7776 -0.1121 0.7603  -0.3796 204 ARG A CA  
1640 C C   . ARG A 207 ? 3.0453 1.6549 1.8365 -0.0784 0.7867  -0.4064 204 ARG A C   
1641 O O   . ARG A 207 ? 3.0763 1.5795 1.878  -0.0432 0.7634  -0.3609 204 ARG A O   
1642 C CB  . ARG A 207 ? 2.9138 1.7877 1.8213 -0.0242 0.7441  -0.3414 204 ARG A CB  
1643 C CG  . ARG A 207 ? 2.8537 1.9414 1.8127 -0.0326 0.7427  -0.3416 204 ARG A CG  
1644 C CD  . ARG A 207 ? 2.8495 2.0327 1.8036 -0.1253 0.6878  -0.2806 204 ARG A CD  
1645 N NE  . ARG A 207 ? 2.8927 1.9854 1.8555 -0.1215 0.6333  -0.213  204 ARG A NE  
1646 C CZ  . ARG A 207 ? 2.8956 2.0199 1.8508 -0.1916 0.5807  -0.1582 204 ARG A CZ  
1647 N NH1 . ARG A 207 ? 2.8575 2.0939 1.7893 -0.2744 0.5702  -0.1528 204 ARG A NH1 
1648 N NH2 . ARG A 207 ? 2.9136 1.9524 1.8795 -0.1797 0.5395  -0.1092 204 ARG A NH2 
1649 N N   . GLU A 208 ? 3.0949 1.6486 1.8349 -0.0936 0.8387  -0.4829 205 GLU A N   
1650 C CA  . GLU A 208 ? 3.1815 1.561  1.8933 -0.0687 0.8572  -0.5195 205 GLU A CA  
1651 C C   . GLU A 208 ? 3.197  1.5041 1.9717 0.0577  0.8507  -0.5089 205 GLU A C   
1652 O O   . GLU A 208 ? 3.2318 1.4239 2.0225 0.0786  0.8189  -0.4947 205 GLU A O   
1653 C CB  . GLU A 208 ? 3.1611 1.663  1.9099 -0.0775 0.8354  -0.5978 205 GLU A CB  
1654 C CG  . GLU A 208 ? 3.2118 1.6882 2.0299 -0.0474 0.7647  -0.6261 205 GLU A CG  
1655 C CD  . GLU A 208 ? 3.2291 1.8139 2.1525 0.0558  0.7132  -0.6951 205 GLU A CD  
1656 O OE1 . GLU A 208 ? 3.2593 1.7766 2.225  0.0821  0.6675  -0.7216 205 GLU A OE1 
1657 O OE2 . GLU A 208 ? 3.2017 1.9261 2.1539 0.1055  0.7245  -0.7274 205 GLU A OE2 
1658 N N   . GLU A 209 ? 3.1624 1.5486 1.977  0.1365  0.8762  -0.5128 206 GLU A N   
1659 C CA  . GLU A 209 ? 3.1609 1.5102 2.0456 0.2617  0.8577  -0.4998 206 GLU A CA  
1660 C C   . GLU A 209 ? 3.2103 1.4527 2.0748 0.2741  0.8267  -0.4103 206 GLU A C   
1661 O O   . GLU A 209 ? 3.2251 1.3833 2.1302 0.3388  0.79    -0.3954 206 GLU A O   
1662 C CB  . GLU A 209 ? 3.1062 1.6271 2.0659 0.3394  0.8754  -0.5223 206 GLU A CB  
1663 C CG  . GLU A 209 ? 3.0744 1.8086 2.0801 0.3066  0.8798  -0.6014 206 GLU A CG  
1664 C CD  . GLU A 209 ? 3.0808 1.9953 2.0784 0.2118  0.8726  -0.5731 206 GLU A CD  
1665 O OE1 . GLU A 209 ? 3.0497 2.0935 2.0354 0.1582  0.8819  -0.6229 206 GLU A OE1 
1666 O OE2 . GLU A 209 ? 3.1091 2.0186 2.0971 0.1903  0.8604  -0.4992 206 GLU A OE2 
1667 N N   . LEU A 210 ? 3.1932 1.5096 2.0465 0.2055  0.8002  -0.3544 207 LEU A N   
1668 C CA  . LEU A 210 ? 3.2176 1.4855 2.0753 0.2084  0.7516  -0.2765 207 LEU A CA  
1669 C C   . LEU A 210 ? 3.3032 1.3855 2.0913 0.1574  0.7572  -0.2687 207 LEU A C   
1670 O O   . LEU A 210 ? 3.3481 1.3114 2.1162 0.1912  0.7448  -0.2251 207 LEU A O   
1671 C CB  . LEU A 210 ? 3.1557 1.5935 2.0539 0.144   0.7006  -0.2303 207 LEU A CB  
1672 C CG  . LEU A 210 ? 3.1914 1.5895 2.0933 0.1376  0.6522  -0.159  207 LEU A CG  
1673 C CD1 . LEU A 210 ? 3.1973 1.5746 2.1241 0.2384  0.6404  -0.1259 207 LEU A CD1 
1674 C CD2 . LEU A 210 ? 3.1447 1.6848 2.0776 0.0663  0.6056  -0.124  207 LEU A CD2 
1675 N N   . ALA A 211 ? 3.3215 1.3898 2.0706 0.0698  0.7752  -0.3109 208 ALA A N   
1676 C CA  . ALA A 211 ? 3.3536 1.3491 2.1017 0.0103  0.7472  -0.31   208 ALA A CA  
1677 C C   . ALA A 211 ? 3.3606 1.2933 2.1697 0.061   0.7173  -0.3315 208 ALA A C   
1678 O O   . ALA A 211 ? 3.3863 1.245  2.1985 0.0288  0.6942  -0.3084 208 ALA A O   
1679 C CB  . ALA A 211 ? 3.3423 1.4001 2.0692 -0.0881 0.7488  -0.3511 208 ALA A CB  
1680 N N   . GLU A 212 ? 3.3344 1.298  2.1961 0.1374  0.7153  -0.3769 209 GLU A N   
1681 C CA  . GLU A 212 ? 3.3424 1.2384 2.2688 0.1842  0.6763  -0.4006 209 GLU A CA  
1682 C C   . GLU A 212 ? 3.3656 1.1789 2.3156 0.2303  0.6428  -0.3336 209 GLU A C   
1683 O O   . GLU A 212 ? 3.3814 1.1094 2.3654 0.2313  0.6098  -0.3341 209 GLU A O   
1684 C CB  . GLU A 212 ? 3.3147 1.2981 2.3216 0.2583  0.6627  -0.4732 209 GLU A CB  
1685 C CG  . GLU A 212 ? 3.3229 1.4335 2.3667 0.2087  0.6376  -0.5477 209 GLU A CG  
1686 C CD  . GLU A 212 ? 3.3127 1.5909 2.4652 0.2823  0.5978  -0.6275 209 GLU A CD  
1687 O OE1 . GLU A 212 ? 3.2834 1.6671 2.4647 0.3347  0.6147  -0.6283 209 GLU A OE1 
1688 O OE2 . GLU A 212 ? 3.3251 1.6139 2.5183 0.2882  0.5593  -0.6929 209 GLU A OE2 
1689 N N   . HIS A 213 ? 3.3666 1.2062 2.2927 0.26    0.6495  -0.2735 210 HIS A N   
1690 C CA  . HIS A 213 ? 3.3873 1.1686 2.323  0.2972  0.6151  -0.2035 210 HIS A CA  
1691 C C   . HIS A 213 ? 3.4197 1.1233 2.2913 0.2156  0.6181  -0.1571 210 HIS A C   
1692 O O   . HIS A 213 ? 3.4373 1.0884 2.3043 0.2316  0.5934  -0.1016 210 HIS A O   
1693 C CB  . HIS A 213 ? 3.3744 1.2516 2.3296 0.3675  0.606   -0.1642 210 HIS A CB  
1694 C CG  . HIS A 213 ? 3.3433 1.375  2.4019 0.4348  0.593   -0.2175 210 HIS A CG  
1695 N ND1 . HIS A 213 ? 3.3237 1.3902 2.5005 0.5164  0.5439  -0.2364 210 HIS A ND1 
1696 C CD2 . HIS A 213 ? 3.3205 1.4797 2.3806 0.4251  0.626   -0.2563 210 HIS A CD2 
1697 C CE1 . HIS A 213 ? 3.2746 1.4657 2.5004 0.5632  0.5647  -0.2914 210 HIS A CE1 
1698 N NE2 . HIS A 213 ? 3.2734 1.5309 2.43   0.5086  0.6147  -0.3038 210 HIS A NE2 
1699 N N   . ALA A 214 ? 3.4205 1.1287 2.2479 0.127   0.6467  -0.1825 211 ALA A N   
1700 C CA  . ALA A 214 ? 3.4401 1.1085 2.2329 0.0457  0.6473  -0.1554 211 ALA A CA  
1701 C C   . ALA A 214 ? 3.4418 1.0516 2.2689 0.0042  0.6283  -0.1779 211 ALA A C   
1702 O O   . ALA A 214 ? 3.4323 1.0348 2.3036 0.028   0.6148  -0.2229 211 ALA A O   
1703 C CB  . ALA A 214 ? 3.4335 1.163  2.1876 -0.0285 0.6729  -0.1735 211 ALA A CB  
1704 N N   . ASP A 215 ? 3.4499 1.0218 2.2597 -0.0571 0.6269  -0.1497 212 ASP A N   
1705 C CA  . ASP A 215 ? 3.4475 0.9794 2.2942 -0.1041 0.6082  -0.1657 212 ASP A CA  
1706 C C   . ASP A 215 ? 3.4237 1.0016 2.276  -0.1756 0.6192  -0.2254 212 ASP A C   
1707 O O   . ASP A 215 ? 3.4173 0.9801 2.3089 -0.1839 0.6002  -0.2648 212 ASP A O   
1708 C CB  . ASP A 215 ? 3.463  0.9926 2.3196 -0.1448 0.5932  -0.1159 212 ASP A CB  
1709 C CG  . ASP A 215 ? 3.4952 1.0482 2.3777 -0.0834 0.5588  -0.0526 212 ASP A CG  
1710 O OD1 . ASP A 215 ? 3.4987 1.0407 2.397  -0.0051 0.542   -0.0445 212 ASP A OD1 
1711 O OD2 . ASP A 215 ? 3.5093 1.0955 2.3951 -0.1147 0.5506  -0.015  212 ASP A OD2 
1712 N N   . ARG A 216 ? 3.4088 1.0427 2.2226 -0.2276 0.6447  -0.2314 213 ARG A N   
1713 C CA  . ARG A 216 ? 3.3823 1.0855 2.2049 -0.3007 0.6461  -0.2807 213 ARG A CA  
1714 C C   . ARG A 216 ? 3.3743 1.1465 2.1586 -0.3057 0.6644  -0.2929 213 ARG A C   
1715 O O   . ARG A 216 ? 3.3884 1.1553 2.1381 -0.2766 0.6779  -0.2545 213 ARG A O   
1716 C CB  . ARG A 216 ? 3.3705 1.1132 2.2208 -0.3778 0.6353  -0.2695 213 ARG A CB  
1717 C CG  . ARG A 216 ? 3.3443 1.2029 2.2426 -0.4472 0.6105  -0.3126 213 ARG A CG  
1718 C CD  . ARG A 216 ? 3.3324 1.2464 2.3036 -0.5009 0.5814  -0.3081 213 ARG A CD  
1719 N NE  . ARG A 216 ? 3.3392 1.2852 2.3255 -0.5126 0.5839  -0.2677 213 ARG A NE  
1720 C CZ  . ARG A 216 ? 3.314  1.3579 2.3316 -0.5638 0.5759  -0.2735 213 ARG A CZ  
1721 N NH1 . ARG A 216 ? 3.2763 1.3945 2.3059 -0.6134 0.5636  -0.3126 213 ARG A NH1 
1722 N NH2 . ARG A 216 ? 3.311  1.3591 2.3294 -0.5718 0.5894  -0.2461 213 ARG A NH2 
1723 N N   . VAL A 217 ? 3.3506 1.1897 2.1376 -0.3434 0.6615  -0.3441 214 VAL A N   
1724 C CA  . VAL A 217 ? 3.34   1.2604 2.092  -0.3605 0.6718  -0.3544 214 VAL A CA  
1725 C C   . VAL A 217 ? 3.3091 1.3177 2.0626 -0.4526 0.6535  -0.3843 214 VAL A C   
1726 O O   . VAL A 217 ? 3.2926 1.3253 2.0837 -0.4773 0.6329  -0.4229 214 VAL A O   
1727 C CB  . VAL A 217 ? 3.3394 1.2909 2.0978 -0.2927 0.6797  -0.3856 214 VAL A CB  
1728 C CG1 . VAL A 217 ? 3.3202 1.3831 2.049  -0.3281 0.6852  -0.403  214 VAL A CG1 
1729 C CG2 . VAL A 217 ? 3.3623 1.26   2.1266 -0.1994 0.6897  -0.3493 214 VAL A CG2 
1730 N N   . SER A 218 ? 3.2996 1.3561 2.0118 -0.5023 0.6531  -0.3645 215 SER A N   
1731 C CA  . SER A 218 ? 3.2661 1.4217 1.9819 -0.5858 0.6224  -0.3853 215 SER A CA  
1732 C C   . SER A 218 ? 3.2564 1.4959 1.9276 -0.603  0.615   -0.3903 215 SER A C   
1733 O O   . SER A 218 ? 3.2517 1.5106 1.9123 -0.5726 0.6109  -0.3504 215 SER A O   
1734 C CB  . SER A 218 ? 3.2665 1.4378 1.9986 -0.6324 0.601   -0.3522 215 SER A CB  
1735 O OG  . SER A 218 ? 3.2698 1.4277 2.077  -0.6261 0.5922  -0.3532 215 SER A OG  
1736 N N   . LEU A 219 ? 3.2251 1.5612 1.9077 -0.6366 0.5909  -0.4309 216 LEU A N   
1737 C CA  . LEU A 219 ? 3.2105 1.6562 1.8615 -0.6539 0.5754  -0.4352 216 LEU A CA  
1738 C C   . LEU A 219 ? 3.1912 1.7311 1.8284 -0.7318 0.52    -0.406  216 LEU A C   
1739 O O   . LEU A 219 ? 3.1611 1.7621 1.8325 -0.7729 0.483   -0.4243 216 LEU A O   
1740 C CB  . LEU A 219 ? 3.1886 1.6959 1.8623 -0.6298 0.5737  -0.4955 216 LEU A CB  
1741 C CG  . LEU A 219 ? 3.1706 1.8137 1.8293 -0.6252 0.5601  -0.5107 216 LEU A CG  
1742 C CD1 . LEU A 219 ? 3.1367 1.9018 1.7981 -0.6851 0.5039  -0.5156 216 LEU A CD1 
1743 C CD2 . LEU A 219 ? 3.1819 1.8517 1.8078 -0.615  0.5764  -0.4699 216 LEU A CD2 
1744 N N   . ILE A 220 ? 3.1977 1.7637 1.7987 -0.7431 0.5014  -0.3559 217 ILE A N   
1745 C CA  . ILE A 220 ? 3.1632 1.8417 1.778  -0.7916 0.4225  -0.3108 217 ILE A CA  
1746 C C   . ILE A 220 ? 3.1579 1.9297 1.7061 -0.8317 0.41    -0.3154 217 ILE A C   
1747 O O   . ILE A 220 ? 3.1603 1.9471 1.685  -0.8046 0.435   -0.3058 217 ILE A O   
1748 C CB  . ILE A 220 ? 3.1374 1.8394 1.8298 -0.7441 0.3707  -0.2346 217 ILE A CB  
1749 C CG1 . ILE A 220 ? 3.1524 1.7836 1.9119 -0.715  0.3809  -0.2355 217 ILE A CG1 
1750 C CG2 . ILE A 220 ? 3.1074 1.911  1.8032 -0.7862 0.2856  -0.1833 217 ILE A CG2 
1751 C CD1 . ILE A 220 ? 3.1383 1.7884 1.9742 -0.6737 0.3347  -0.1756 217 ILE A CD1 
1752 N N   . CYS A 221 ? 3.1156 1.9969 1.6846 -0.8677 0.3576  -0.3239 218 CYS A N   
1753 C CA  . CYS A 221 ? 3.082  2.0975 1.6368 -0.8762 0.3252  -0.3171 218 CYS A CA  
1754 C C   . CYS A 221 ? 3.0559 2.1521 1.6165 -0.9221 0.2363  -0.2638 218 CYS A C   
1755 O O   . CYS A 221 ? 3.037  2.1539 1.6428 -0.9378 0.2033  -0.2791 218 CYS A O   
1756 C CB  . CYS A 221 ? 3.0625 2.1308 1.6493 -0.8432 0.3452  -0.3849 218 CYS A CB  
1757 S SG  . CYS A 221 ? 3.0701 2.2325 1.6591 -0.7765 0.3748  -0.405  218 CYS A SG  
1758 N N   . ALA A 222 ? 3.0497 2.1908 1.5724 -0.9388 0.1942  -0.1988 219 ALA A N   
1759 C CA  . ALA A 222 ? 3.025  2.2376 1.5591 -0.9623 0.1005  -0.1349 219 ALA A CA  
1760 C C   . ALA A 222 ? 3.0309 2.1931 1.6008 -0.9802 0.0531  -0.1144 219 ALA A C   
1761 O O   . ALA A 222 ? 2.9912 2.2295 1.604  -0.9909 -0.007  -0.1107 219 ALA A O   
1762 C CB  . ALA A 222 ? 2.9805 2.3198 1.5297 -0.9565 0.069   -0.1532 219 ALA A CB  
1763 N N   . GLY A 223 ? 3.0666 2.1165 1.6417 -0.9636 0.0804  -0.1037 220 GLY A N   
1764 C CA  . GLY A 223 ? 3.0388 2.0811 1.7243 -0.9256 0.0392  -0.0841 220 GLY A CA  
1765 C C   . GLY A 223 ? 3.0309 2.0661 1.7577 -0.943  0.0707  -0.1501 220 GLY A C   
1766 O O   . GLY A 223 ? 2.9951 2.0653 1.809  -0.9329 0.0265  -0.1403 220 GLY A O   
1767 N N   . GLU A 224 ? 3.0606 2.0502 1.7283 -0.9703 0.1487  -0.221  221 GLU A N   
1768 C CA  . GLU A 224 ? 3.0447 2.0284 1.7664 -0.981  0.1796  -0.2835 221 GLU A CA  
1769 C C   . GLU A 224 ? 3.0807 1.9596 1.8033 -0.9382 0.2705  -0.3311 221 GLU A C   
1770 O O   . GLU A 224 ? 3.0995 1.9661 1.7858 -0.9067 0.3048  -0.3416 221 GLU A O   
1771 C CB  . GLU A 224 ? 2.9967 2.1253 1.7768 -0.9823 0.1332  -0.3113 221 GLU A CB  
1772 C CG  . GLU A 224 ? 2.9685 2.2278 1.8274 -0.9836 0.0354  -0.2733 221 GLU A CG  
1773 C CD  . GLU A 224 ? 2.9519 2.3567 1.8826 -0.9446 -0.0161 -0.2908 221 GLU A CD  
1774 O OE1 . GLU A 224 ? 2.9631 2.3681 1.8975 -0.9202 0.0198  -0.3404 221 GLU A OE1 
1775 O OE2 . GLU A 224 ? 2.9234 2.4262 1.8922 -0.9376 -0.0945 -0.2554 221 GLU A OE2 
1776 N N   . VAL A 225 ? 3.0829 1.8958 1.8541 -0.932  0.3053  -0.3582 222 VAL A N   
1777 C CA  . VAL A 225 ? 3.1148 1.8278 1.8994 -0.8795 0.375   -0.3919 222 VAL A CA  
1778 C C   . VAL A 225 ? 3.0869 1.8549 1.9152 -0.8713 0.3693  -0.445  222 VAL A C   
1779 O O   . VAL A 225 ? 3.0565 1.8554 1.9495 -0.891  0.351   -0.4682 222 VAL A O   
1780 C CB  . VAL A 225 ? 3.1377 1.7601 1.9637 -0.8618 0.4069  -0.3843 222 VAL A CB  
1781 C CG1 . VAL A 225 ? 3.1744 1.6956 2.0129 -0.7972 0.4615  -0.4028 222 VAL A CG1 
1782 C CG2 . VAL A 225 ? 3.1393 1.7559 1.9795 -0.8308 0.3832  -0.3232 222 VAL A CG2 
1783 N N   . ILE A 226 ? 3.0939 1.8782 1.8855 -0.8423 0.382   -0.4655 223 ILE A N   
1784 C CA  . ILE A 226 ? 3.077  1.9047 1.8944 -0.8252 0.3715  -0.517  223 ILE A CA  
1785 C C   . ILE A 226 ? 3.1018 1.8291 1.9609 -0.7824 0.4027  -0.5509 223 ILE A C   
1786 O O   . ILE A 226 ? 3.0805 1.8246 1.9919 -0.8016 0.3772  -0.5735 223 ILE A O   
1787 C CB  . ILE A 226 ? 3.0792 1.9656 1.848  -0.799  0.374   -0.5283 223 ILE A CB  
1788 C CG1 . ILE A 226 ? 3.0593 2.061  1.8029 -0.8344 0.3247  -0.4826 223 ILE A CG1 
1789 C CG2 . ILE A 226 ? 3.0705 1.987  1.8566 -0.7721 0.3627  -0.5855 223 ILE A CG2 
1790 C CD1 . ILE A 226 ? 3.0243 2.1296 1.8161 -0.8709 0.2526  -0.4715 223 ILE A CD1 
1791 N N   . LYS A 227 ? 3.1426 1.7684 1.9804 -0.7244 0.4508  -0.5513 224 LYS A N   
1792 C CA  . LYS A 227 ? 3.1685 1.6948 2.0442 -0.6787 0.4675  -0.5732 224 LYS A CA  
1793 C C   . LYS A 227 ? 3.2074 1.6335 2.0905 -0.6444 0.4992  -0.5308 224 LYS A C   
1794 O O   . LYS A 227 ? 3.224  1.6434 2.0715 -0.634  0.5185  -0.4951 224 LYS A O   
1795 C CB  . LYS A 227 ? 3.1893 1.7054 2.06   -0.6135 0.4716  -0.6183 224 LYS A CB  
1796 C CG  . LYS A 227 ? 3.2019 1.7245 2.1353 -0.5952 0.4268  -0.6574 224 LYS A CG  
1797 C CD  . LYS A 227 ? 3.1872 1.8487 2.1465 -0.6187 0.3679  -0.675  224 LYS A CD  
1798 C CE  . LYS A 227 ? 3.2018 1.9513 2.1318 -0.5759 0.3577  -0.6933 224 LYS A CE  
1799 N NZ  . LYS A 227 ? 3.1765 2.0553 2.1087 -0.611  0.3093  -0.6896 224 LYS A NZ  
1800 N N   . SER A 228 ? 3.2211 1.57   2.1472 -0.6286 0.5003  -0.5311 225 SER A N   
1801 C CA  . SER A 228 ? 3.2563 1.5159 2.1918 -0.5935 0.5231  -0.4873 225 SER A CA  
1802 C C   . SER A 228 ? 3.2784 1.4473 2.2515 -0.5535 0.5189  -0.496  225 SER A C   
1803 O O   . SER A 228 ? 3.2644 1.446  2.2731 -0.5729 0.491   -0.5293 225 SER A O   
1804 C CB  . SER A 228 ? 3.2477 1.5536 2.2184 -0.6399 0.5088  -0.4503 225 SER A CB  
1805 O OG  . SER A 228 ? 3.2532 1.6399 2.2098 -0.6552 0.4955  -0.4243 225 SER A OG  
1806 N N   . GLY A 229 ? 3.3119 1.3887 2.2761 -0.4994 0.5406  -0.4621 226 GLY A N   
1807 C CA  . GLY A 229 ? 3.3355 1.3244 2.3372 -0.4617 0.5273  -0.4583 226 GLY A CA  
1808 C C   . GLY A 229 ? 3.3686 1.2817 2.3597 -0.3735 0.5375  -0.4511 226 GLY A C   
1809 O O   . GLY A 229 ? 3.3859 1.2757 2.353  -0.3377 0.5583  -0.409  226 GLY A O   
1810 N N   . ASP A 230 ? 3.3737 1.2478 2.3876 -0.3352 0.5185  -0.4937 227 ASP A N   
1811 C CA  . ASP A 230 ? 3.3963 1.209  2.4208 -0.2446 0.5178  -0.498  227 ASP A CA  
1812 C C   . ASP A 230 ? 3.3893 1.2707 2.3792 -0.2046 0.5456  -0.5095 227 ASP A C   
1813 O O   . ASP A 230 ? 3.3689 1.3368 2.3379 -0.2327 0.5507  -0.5489 227 ASP A O   
1814 C CB  . ASP A 230 ? 3.4048 1.1892 2.4829 -0.2148 0.4758  -0.5533 227 ASP A CB  
1815 C CG  . ASP A 230 ? 3.4442 1.1618 2.6072 -0.1584 0.4266  -0.5298 227 ASP A CG  
1816 O OD1 . ASP A 230 ? 3.4565 1.1456 2.6292 -0.0906 0.4318  -0.5043 227 ASP A OD1 
1817 O OD2 . ASP A 230 ? 3.4561 1.1492 2.6775 -0.1841 0.3818  -0.5372 227 ASP A OD2 
1818 N N   . PRO A 231 ? 3.4017 1.2522 2.3848 -0.1412 0.5622  -0.472  228 PRO A N   
1819 C CA  . PRO A 231 ? 3.3888 1.3124 2.3431 -0.1051 0.5912  -0.479  228 PRO A CA  
1820 C C   . PRO A 231 ? 3.3685 1.3573 2.3373 -0.0665 0.5898  -0.553  228 PRO A C   
1821 O O   . PRO A 231 ? 3.3474 1.4335 2.2824 -0.0847 0.6129  -0.5707 228 PRO A O   
1822 C CB  . PRO A 231 ? 3.4065 1.2842 2.3742 -0.032  0.5934  -0.4258 228 PRO A CB  
1823 C CG  . PRO A 231 ? 3.4316 1.2336 2.4143 -0.0597 0.5707  -0.3747 228 PRO A CG  
1824 C CD  . PRO A 231 ? 3.4223 1.1769 2.4208 -0.1037 0.5544  -0.4167 228 PRO A CD  
1825 N N   . LYS A 232 ? 3.3729 1.3105 2.391  -0.0175 0.5605  -0.598  229 LYS A N   
1826 C CA  . LYS A 232 ? 3.3563 1.3545 2.3947 0.0287  0.5517  -0.6786 229 LYS A CA  
1827 C C   . LYS A 232 ? 3.348  1.4127 2.3628 -0.0367 0.5365  -0.7262 229 LYS A C   
1828 O O   . LYS A 232 ? 3.3261 1.4817 2.3166 -0.0235 0.5485  -0.7777 229 LYS A O   
1829 C CB  . LYS A 232 ? 3.3726 1.3093 2.4979 0.1121  0.5043  -0.7124 229 LYS A CB  
1830 C CG  . LYS A 232 ? 3.3864 1.3574 2.5955 0.2009  0.4805  -0.6799 229 LYS A CG  
1831 C CD  . LYS A 232 ? 3.4318 1.3769 2.7029 0.1882  0.4347  -0.5926 229 LYS A CD  
1832 C CE  . LYS A 232 ? 3.4381 1.4528 2.7674 0.2519  0.4216  -0.5475 229 LYS A CE  
1833 N NZ  . LYS A 232 ? 3.472  1.4715 2.8075 0.2175  0.4037  -0.4568 229 LYS A NZ  
1834 N N   . GLU A 233 ? 3.3601 1.3888 2.3816 -0.1061 0.5099  -0.708  230 GLU A N   
1835 C CA  . GLU A 233 ? 3.3483 1.4491 2.3561 -0.1676 0.4868  -0.7446 230 GLU A CA  
1836 C C   . GLU A 233 ? 3.327  1.551  2.2897 -0.2235 0.5072  -0.7226 230 GLU A C   
1837 O O   . GLU A 233 ? 3.3079 1.6227 2.2422 -0.2294 0.5052  -0.7645 230 GLU A O   
1838 C CB  . GLU A 233 ? 3.3687 1.4373 2.4272 -0.2185 0.438   -0.7275 230 GLU A CB  
1839 C CG  . GLU A 233 ? 3.3923 1.506  2.4918 -0.2665 0.4213  -0.6492 230 GLU A CG  
1840 C CD  . GLU A 233 ? 3.3957 1.6367 2.5354 -0.3339 0.3792  -0.6308 230 GLU A CD  
1841 O OE1 . GLU A 233 ? 3.3798 1.7234 2.4955 -0.3531 0.3741  -0.6523 230 GLU A OE1 
1842 O OE2 . GLU A 233 ? 3.402  1.6298 2.5859 -0.3705 0.3605  -0.594  230 GLU A OE2 
1843 N N   . VAL A 234 ? 3.3294 1.5543 2.2828 -0.2617 0.5243  -0.6566 231 VAL A N   
1844 C CA  . VAL A 234 ? 3.3108 1.6434 2.2293 -0.3158 0.5344  -0.6305 231 VAL A CA  
1845 C C   . VAL A 234 ? 3.3022 1.7078 2.1949 -0.2709 0.562   -0.6388 231 VAL A C   
1846 O O   . VAL A 234 ? 3.2791 1.7926 2.1388 -0.3106 0.5626  -0.6419 231 VAL A O   
1847 C CB  . VAL A 234 ? 3.3215 1.6363 2.2466 -0.3638 0.5338  -0.5637 231 VAL A CB  
1848 C CG1 . VAL A 234 ? 3.3511 1.5894 2.2845 -0.308  0.5543  -0.5187 231 VAL A CG1 
1849 C CG2 . VAL A 234 ? 3.3018 1.722  2.1964 -0.4262 0.5301  -0.5402 231 VAL A CG2 
1850 N N   . GLY A 235 ? 3.3145 1.6709 2.228  -0.1879 0.5796  -0.6459 232 GLY A N   
1851 C CA  . GLY A 235 ? 3.2994 1.7369 2.2061 -0.1336 0.6052  -0.6632 232 GLY A CA  
1852 C C   . GLY A 235 ? 3.2788 1.8063 2.1776 -0.1145 0.5955  -0.7358 232 GLY A C   
1853 O O   . GLY A 235 ? 3.2536 1.8994 2.1211 -0.1249 0.6131  -0.7434 232 GLY A O   
1854 N N   . GLU A 236 ? 3.289  1.7613 2.2105 -0.0903 0.5641  -0.7881 233 GLU A N   
1855 C CA  . GLU A 236 ? 3.276  1.8207 2.1806 -0.0668 0.5469  -0.8604 233 GLU A CA  
1856 C C   . GLU A 236 ? 3.2591 1.9051 2.1163 -0.1493 0.533   -0.8492 233 GLU A C   
1857 O O   . GLU A 236 ? 3.2394 1.9845 2.0584 -0.138  0.5347  -0.8846 233 GLU A O   
1858 C CB  . GLU A 236 ? 3.3104 1.7811 2.268  -0.0207 0.4911  -0.9094 233 GLU A CB  
1859 C CG  . GLU A 236 ? 3.3406 1.8057 2.3832 0.0975  0.4573  -0.9452 233 GLU A CG  
1860 C CD  . GLU A 236 ? 3.3622 1.8825 2.4976 0.1751  0.3454  -1.0084 233 GLU A CD  
1861 O OE1 . GLU A 236 ? 3.3669 1.9404 2.4721 0.1522  0.3111  -1.032  233 GLU A OE1 
1862 O OE2 . GLU A 236 ? 3.358  1.8603 2.5947 0.2577  0.2908  -1.0361 233 GLU A OE2 
1863 N N   . PHE A 237 ? 3.2625 1.8862 2.1229 -0.2283 0.5172  -0.7986 234 PHE A N   
1864 C CA  . PHE A 237 ? 3.2424 1.9635 2.0737 -0.3037 0.4938  -0.7811 234 PHE A CA  
1865 C C   . PHE A 237 ? 3.2201 2.0467 2.0163 -0.3315 0.5158  -0.7398 234 PHE A C   
1866 O O   . PHE A 237 ? 3.1965 2.128  1.958  -0.3612 0.4995  -0.7433 234 PHE A O   
1867 C CB  . PHE A 237 ? 3.2475 1.9234 2.1077 -0.3702 0.4654  -0.7449 234 PHE A CB  
1868 C CG  . PHE A 237 ? 3.2683 1.8709 2.1701 -0.353  0.4301  -0.782  234 PHE A CG  
1869 C CD1 . PHE A 237 ? 3.2773 1.8917 2.1739 -0.3069 0.4055  -0.8462 234 PHE A CD1 
1870 C CD2 . PHE A 237 ? 3.2851 1.8192 2.2378 -0.3794 0.4124  -0.7497 234 PHE A CD2 
1871 C CE1 . PHE A 237 ? 3.2984 1.8381 2.2333 -0.2944 0.3667  -0.8796 234 PHE A CE1 
1872 C CE2 . PHE A 237 ? 3.3017 1.7733 2.2963 -0.3698 0.3761  -0.7797 234 PHE A CE2 
1873 C CZ  . PHE A 237 ? 3.3053 1.7707 2.287  -0.3316 0.3551  -0.8456 234 PHE A CZ  
1874 N N   . TYR A 238 ? 3.2276 2.0223 2.0311 -0.3189 0.5493  -0.6988 235 TYR A N   
1875 C CA  . TYR A 238 ? 3.2111 2.0934 1.9877 -0.3434 0.5681  -0.6547 235 TYR A CA  
1876 C C   . TYR A 238 ? 3.1835 2.1726 1.9393 -0.2964 0.5893  -0.6936 235 TYR A C   
1877 O O   . TYR A 238 ? 3.1575 2.2592 1.8804 -0.3351 0.586   -0.6689 235 TYR A O   
1878 C CB  . TYR A 238 ? 3.2336 2.034  2.0263 -0.3279 0.5949  -0.6063 235 TYR A CB  
1879 C CG  . TYR A 238 ? 3.2247 2.0999 1.9965 -0.3471 0.6107  -0.5588 235 TYR A CG  
1880 C CD1 . TYR A 238 ? 3.2122 2.1841 1.9574 -0.4205 0.5788  -0.5186 235 TYR A CD1 
1881 C CD2 . TYR A 238 ? 3.237  2.0879 2.0299 -0.2884 0.6422  -0.5435 235 TYR A CD2 
1882 C CE1 . TYR A 238 ? 3.2073 2.2438 1.9364 -0.443  0.5818  -0.4696 235 TYR A CE1 
1883 C CE2 . TYR A 238 ? 3.2304 2.1502 2.0081 -0.3113 0.6512  -0.4977 235 TYR A CE2 
1884 C CZ  . TYR A 238 ? 3.2194 2.2334 1.9672 -0.3907 0.6177  -0.4601 235 TYR A CZ  
1885 O OH  . TYR A 238 ? 3.215  2.3016 1.9536 -0.4151 0.6149  -0.412  235 TYR A OH  
1886 N N   . LYS A 239 ? 3.1859 2.1422 1.9611 -0.2111 0.6057  -0.7547 236 LYS A N   
1887 C CA  . LYS A 239 ? 3.1597 2.2194 1.9189 -0.1498 0.6251  -0.8021 236 LYS A CA  
1888 C C   . LYS A 239 ? 3.1478 2.2942 1.8591 -0.1732 0.5955  -0.8251 236 LYS A C   
1889 O O   . LYS A 239 ? 3.1227 2.3828 1.7995 -0.1547 0.61    -0.8328 236 LYS A O   
1890 C CB  . LYS A 239 ? 3.1815 2.1859 1.9878 -0.0376 0.6248  -0.8651 236 LYS A CB  
1891 C CG  . LYS A 239 ? 3.208  2.1799 2.0921 0.027   0.628   -0.8385 236 LYS A CG  
1892 C CD  . LYS A 239 ? 3.2448 2.1632 2.2039 0.1367  0.5894  -0.8942 236 LYS A CD  
1893 C CE  . LYS A 239 ? 3.2349 2.2804 2.2174 0.2349  0.5333  -0.9635 236 LYS A CE  
1894 N NZ  . LYS A 239 ? 3.1987 2.4287 2.1847 0.2979  0.5396  -0.9619 236 LYS A NZ  
1895 N N   . LYS A 240 ? 3.1637 2.2552 1.8718 -0.2096 0.555   -0.8344 237 LYS A N   
1896 C CA  . LYS A 240 ? 3.1572 2.3182 1.8214 -0.223  0.5215  -0.8557 237 LYS A CA  
1897 C C   . LYS A 240 ? 3.1404 2.3732 1.7877 -0.3109 0.4884  -0.793  237 LYS A C   
1898 O O   . LYS A 240 ? 3.1218 2.4563 1.7255 -0.3186 0.4806  -0.7804 237 LYS A O   
1899 C CB  . LYS A 240 ? 3.1947 2.278  1.8772 -0.1856 0.4807  -0.9107 237 LYS A CB  
1900 C CG  . LYS A 240 ? 3.2312 2.3147 1.9188 -0.0677 0.4752  -0.978  237 LYS A CG  
1901 C CD  . LYS A 240 ? 3.2635 2.2881 2.0323 0.0078  0.4743  -0.985  237 LYS A CD  
1902 C CE  . LYS A 240 ? 3.256  2.3772 2.0552 0.1455  0.4519  -1.0181 237 LYS A CE  
1903 N NZ  . LYS A 240 ? 3.2384 2.4965 2.0224 0.1534  0.4827  -0.9715 237 LYS A NZ  
1904 N N   . GLU A 241 ? 3.1456 2.3242 1.8262 -0.3714 0.4668  -0.7532 238 GLU A N   
1905 C CA  . GLU A 241 ? 3.1303 2.3736 1.8056 -0.4445 0.4246  -0.6986 238 GLU A CA  
1906 C C   . GLU A 241 ? 3.1187 2.4146 1.791  -0.4849 0.4307  -0.6273 238 GLU A C   
1907 O O   . GLU A 241 ? 3.1301 2.3784 1.8204 -0.4744 0.4639  -0.6094 238 GLU A O   
1908 C CB  . GLU A 241 ? 3.152  2.3374 1.8837 -0.473  0.3813  -0.6895 238 GLU A CB  
1909 C CG  . GLU A 241 ? 3.1548 2.4316 1.9107 -0.5015 0.3111  -0.6569 238 GLU A CG  
1910 C CD  . GLU A 241 ? 3.1793 2.4416 2.0234 -0.5211 0.2607  -0.6271 238 GLU A CD  
1911 O OE1 . GLU A 241 ? 3.1569 2.4847 2.0115 -0.5619 0.2188  -0.5922 238 GLU A OE1 
1912 O OE2 . GLU A 241 ? 3.2089 2.3902 2.1039 -0.5006 0.2668  -0.6419 238 GLU A OE2 
1913 N N   . CYS A 242 ? 3.0977 2.4832 1.746  -0.5291 0.3927  -0.5847 239 CYS A N   
1914 C CA  . CYS A 242 ? 3.0903 2.5217 1.7357 -0.5697 0.3819  -0.5117 239 CYS A CA  
1915 C C   . CYS A 242 ? 3.0777 2.5595 1.723  -0.6199 0.3172  -0.4658 239 CYS A C   
1916 O O   . CYS A 242 ? 3.0629 2.6226 1.6788 -0.6141 0.291   -0.4611 239 CYS A O   
1917 C CB  . CYS A 242 ? 3.08   2.5939 1.6999 -0.5387 0.4097  -0.4981 239 CYS A CB  
1918 S SG  . CYS A 242 ? 3.0904 2.6613 1.7296 -0.5698 0.3838  -0.4    239 CYS A SG  
1919 N N   . LYS B 28  ? 3.3254 2.8189 2.2935 -0.4025 -0.4486 0.0723  28  LYS B N   
1920 C CA  . LYS B 28  ? 3.3403 2.8237 2.2915 -0.3986 -0.4294 0.0872  28  LYS B CA  
1921 C C   . LYS B 28  ? 3.3487 2.7962 2.3328 -0.4069 -0.4221 0.0953  28  LYS B C   
1922 O O   . LYS B 28  ? 3.3603 2.7931 2.3253 -0.4075 -0.4063 0.1035  28  LYS B O   
1923 C CB  . LYS B 28  ? 3.3694 2.8768 2.2611 -0.3832 -0.4012 0.0568  28  LYS B CB  
1924 C CG  . LYS B 28  ? 3.3846 2.9628 2.2772 -0.3485 -0.3938 0.035   28  LYS B CG  
1925 C CD  . LYS B 28  ? 3.4218 3.0441 2.2848 -0.3173 -0.3613 -0.0058 28  LYS B CD  
1926 C CE  . LYS B 28  ? 3.4364 3.1276 2.3008 -0.2813 -0.3592 -0.0345 28  LYS B CE  
1927 N NZ  . LYS B 28  ? 3.4627 3.1861 2.2883 -0.2561 -0.3359 -0.0768 28  LYS B NZ  
1928 N N   . GLY B 29  ? 3.3416 2.7759 2.3725 -0.413  -0.4334 0.0932  29  GLY B N   
1929 C CA  . GLY B 29  ? 3.3506 2.7547 2.4149 -0.4171 -0.427  0.0986  29  GLY B CA  
1930 C C   . GLY B 29  ? 3.3616 2.7524 2.4307 -0.4225 -0.4242 0.0706  29  GLY B C   
1931 O O   . GLY B 29  ? 3.3751 2.7739 2.4044 -0.4217 -0.4158 0.0371  29  GLY B O   
1932 N N   . PRO B 30  ? 3.3534 2.7233 2.4711 -0.4274 -0.4325 0.0832  30  PRO B N   
1933 C CA  . PRO B 30  ? 3.3606 2.7135 2.4819 -0.4345 -0.4315 0.0602  30  PRO B CA  
1934 C C   . PRO B 30  ? 3.393  2.7139 2.4608 -0.4378 -0.4084 0.0316  30  PRO B C   
1935 O O   . PRO B 30  ? 3.4034 2.6959 2.4742 -0.439  -0.3996 0.0402  30  PRO B O   
1936 C CB  . PRO B 30  ? 3.3445 2.6954 2.5408 -0.4314 -0.4412 0.0854  30  PRO B CB  
1937 C CG  . PRO B 30  ? 3.3276 2.7018 2.5659 -0.4198 -0.4489 0.1177  30  PRO B CG  
1938 C CD  . PRO B 30  ? 3.3339 2.6934 2.5039 -0.4263 -0.4448 0.1188  30  PRO B CD  
1939 N N   . ARG B 31  ? 3.4083 2.7336 2.4254 -0.4378 -0.3982 -0.0043 31  ARG B N   
1940 C CA  . ARG B 31  ? 3.4389 2.7404 2.4074 -0.4359 -0.372  -0.0362 31  ARG B CA  
1941 C C   . ARG B 31  ? 3.4509 2.7459 2.4053 -0.4358 -0.367  -0.0786 31  ARG B C   
1942 O O   . ARG B 31  ? 3.4377 2.7558 2.4109 -0.4359 -0.3825 -0.0872 31  ARG B O   
1943 C CB  . ARG B 31  ? 3.4555 2.789  2.3884 -0.4206 -0.3505 -0.0437 31  ARG B CB  
1944 C CG  . ARG B 31  ? 3.4576 2.8322 2.4405 -0.4032 -0.3473 -0.0067 31  ARG B CG  
1945 C CD  . ARG B 31  ? 3.4762 2.9031 2.4433 -0.3791 -0.3253 -0.0123 31  ARG B CD  
1946 N NE  . ARG B 31  ? 3.4721 2.9365 2.4865 -0.3639 -0.3289 0.0232  31  ARG B NE  
1947 C CZ  . ARG B 31  ? 3.4835 2.9556 2.5151 -0.354  -0.3139 0.0438  31  ARG B CZ  
1948 N NH1 . ARG B 31  ? 3.4979 2.9435 2.5004 -0.3596 -0.2951 0.0342  31  ARG B NH1 
1949 N NH2 . ARG B 31  ? 3.4681 2.9514 2.5211 -0.3512 -0.325  0.0769  31  ARG B NH2 
1950 N N   . ILE B 32  ? 3.475  2.7355 2.397  -0.4356 -0.3454 -0.106  32  ILE B N   
1951 C CA  . ILE B 32  ? 3.4896 2.7406 2.4014 -0.4316 -0.3366 -0.1508 32  ILE B CA  
1952 C C   . ILE B 32  ? 3.5131 2.7679 2.3724 -0.4177 -0.3072 -0.1878 32  ILE B C   
1953 O O   . ILE B 32  ? 3.5283 2.7568 2.371  -0.4154 -0.2855 -0.1894 32  ILE B O   
1954 C CB  . ILE B 32  ? 3.4967 2.711  2.4428 -0.4363 -0.3351 -0.1508 32  ILE B CB  
1955 C CG1 . ILE B 32  ? 3.4774 2.7111 2.4962 -0.4404 -0.3584 -0.1175 32  ILE B CG1 
1956 C CG2 . ILE B 32  ? 3.5116 2.7109 2.4465 -0.4303 -0.3226 -0.1997 32  ILE B CG2 
1957 C CD1 . ILE B 32  ? 3.4653 2.7423 2.5209 -0.436  -0.3719 -0.1298 32  ILE B CD1 
1958 N N   . ILE B 33  ? 3.514  2.8027 2.3466 -0.4073 -0.3064 -0.2177 33  ILE B N   
1959 C CA  . ILE B 33  ? 3.5323 2.8361 2.3196 -0.3889 -0.2782 -0.2539 33  ILE B CA  
1960 C C   . ILE B 33  ? 3.5454 2.8332 2.327  -0.3793 -0.2672 -0.3094 33  ILE B C   
1961 O O   . ILE B 33  ? 3.538  2.8329 2.3405 -0.3808 -0.2852 -0.3299 33  ILE B O   
1962 C CB  . ILE B 33  ? 3.5271 2.8902 2.2924 -0.374  -0.2806 -0.2521 33  ILE B CB  
1963 C CG1 . ILE B 33  ? 3.5203 2.9093 2.3155 -0.3747 -0.2881 -0.1975 33  ILE B CG1 
1964 C CG2 . ILE B 33  ? 3.5416 2.927  2.2597 -0.3515 -0.2508 -0.2882 33  ILE B CG2 
1965 C CD1 . ILE B 33  ? 3.5159 2.9681 2.3066 -0.3563 -0.2937 -0.1893 33  ILE B CD1 
1966 N N   . VAL B 34  ? 3.562  2.8249 2.3191 -0.3702 -0.2378 -0.3336 34  VAL B N   
1967 C CA  . VAL B 34  ? 3.5738 2.8197 2.3308 -0.3565 -0.2241 -0.3891 34  VAL B CA  
1968 C C   . VAL B 34  ? 3.5838 2.8535 2.3006 -0.3311 -0.1925 -0.4237 34  VAL B C   
1969 O O   . VAL B 34  ? 3.5924 2.8463 2.3    -0.3269 -0.1663 -0.4158 34  VAL B O   
1970 C CB  . VAL B 34  ? 3.585  2.7822 2.383  -0.3615 -0.2183 -0.3881 34  VAL B CB  
1971 C CG1 . VAL B 34  ? 3.5947 2.7753 2.4013 -0.3444 -0.2047 -0.4469 34  VAL B CG1 
1972 C CG2 . VAL B 34  ? 3.5762 2.7657 2.4264 -0.3794 -0.2471 -0.3529 34  VAL B CG2 
1973 N N   . LYS B 35  ? 3.581  2.8902 2.2728 -0.3134 -0.1948 -0.4613 35  LYS B N   
1974 C CA  . LYS B 35  ? 3.5895 2.9315 2.2474 -0.2825 -0.1655 -0.4973 35  LYS B CA  
1975 C C   . LYS B 35  ? 3.5978 2.9227 2.2743 -0.2635 -0.1594 -0.5617 35  LYS B C   
1976 O O   . LYS B 35  ? 3.5935 2.9214 2.289  -0.265  -0.1835 -0.5891 35  LYS B O   
1977 C CB  . LYS B 35  ? 3.5873 3.009  2.2271 -0.2596 -0.1732 -0.4977 35  LYS B CB  
1978 C CG  . LYS B 35  ? 3.6041 3.1003 2.2433 -0.2081 -0.1445 -0.527  35  LYS B CG  
1979 C CD  . LYS B 35  ? 3.6196 3.1662 2.2949 -0.1889 -0.1213 -0.4801 35  LYS B CD  
1980 C CE  . LYS B 35  ? 3.6187 3.2527 2.3252 -0.1276 -0.093  -0.5014 35  LYS B CE  
1981 N NZ  . LYS B 35  ? 3.5995 3.3393 2.3268 -0.0669 -0.1029 -0.5344 35  LYS B NZ  
1982 N N   . GLU B 36  ? 3.607  2.91   2.2826 -0.2472 -0.1282 -0.5853 36  GLU B N   
1983 C CA  . GLU B 36  ? 3.6128 2.8912 2.3147 -0.2269 -0.1208 -0.646  36  GLU B CA  
1984 C C   . GLU B 36  ? 3.6156 2.8376 2.372  -0.2516 -0.1404 -0.6356 36  GLU B C   
1985 O O   . GLU B 36  ? 3.6198 2.8164 2.3919 -0.2722 -0.1403 -0.5859 36  GLU B O   
1986 C CB  . GLU B 36  ? 3.5927 2.969  2.3384 -0.1771 -0.1356 -0.7027 36  GLU B CB  
1987 C CG  . GLU B 36  ? 3.5805 3.0895 2.3962 -0.0965 -0.1207 -0.7339 36  GLU B CG  
1988 C CD  . GLU B 36  ? 3.603  3.2139 2.4742 -0.0616 -0.1042 -0.6736 36  GLU B CD  
1989 O OE1 . GLU B 36  ? 3.6046 3.2641 2.4595 -0.0626 -0.1135 -0.6377 36  GLU B OE1 
1990 O OE2 . GLU B 36  ? 3.6181 3.2297 2.526  -0.0464 -0.0775 -0.6575 36  GLU B OE2 
1991 N N   . SER B 37  ? 3.6116 2.8123 2.3938 -0.2503 -0.1571 -0.6799 37  SER B N   
1992 C CA  . SER B 37  ? 3.6113 2.7665 2.4474 -0.2734 -0.1759 -0.6646 37  SER B CA  
1993 C C   . SER B 37  ? 3.5978 2.774  2.4469 -0.2949 -0.2109 -0.6491 37  SER B C   
1994 O O   . SER B 37  ? 3.5928 2.742  2.4873 -0.309  -0.2282 -0.6538 37  SER B O   
1995 C CB  . SER B 37  ? 3.6167 2.7487 2.5107 -0.2527 -0.1702 -0.7192 37  SER B CB  
1996 O OG  . SER B 37  ? 3.6259 2.7347 2.5974 -0.2642 -0.1779 -0.6919 37  SER B OG  
1997 N N   . ARG B 38  ? 3.5899 2.8128 2.4003 -0.2979 -0.2207 -0.6282 38  ARG B N   
1998 C CA  . ARG B 38  ? 3.5756 2.8261 2.4021 -0.3143 -0.2526 -0.6122 38  ARG B CA  
1999 C C   . ARG B 38  ? 3.5691 2.8351 2.392  -0.3332 -0.2631 -0.5424 38  ARG B C   
2000 O O   . ARG B 38  ? 3.5758 2.8572 2.3698 -0.3264 -0.2465 -0.5167 38  ARG B O   
2001 C CB  . ARG B 38  ? 3.5712 2.8912 2.3871 -0.2874 -0.2597 -0.6578 38  ARG B CB  
2002 C CG  . ARG B 38  ? 3.552  2.9394 2.4588 -0.2367 -0.2535 -0.7346 38  ARG B CG  
2003 C CD  . ARG B 38  ? 3.528  3.0471 2.4791 -0.1836 -0.2622 -0.7755 38  ARG B CD  
2004 N NE  . ARG B 38  ? 3.553  3.0509 2.5432 -0.1697 -0.235  -0.7671 38  ARG B NE  
2005 C CZ  . ARG B 38  ? 3.5696 3.0933 2.5552 -0.1526 -0.2176 -0.7428 38  ARG B CZ  
2006 N NH1 . ARG B 38  ? 3.5644 3.1318 2.5063 -0.1468 -0.2231 -0.726  38  ARG B NH1 
2007 N NH2 . ARG B 38  ? 3.5758 3.0658 2.5711 -0.1462 -0.2016 -0.7569 38  ARG B NH2 
2008 N N   . ILE B 39  ? 3.5533 2.8152 2.4069 -0.3565 -0.2907 -0.5122 39  ILE B N   
2009 C CA  . ILE B 39  ? 3.5433 2.8234 2.4037 -0.3709 -0.3037 -0.4498 39  ILE B CA  
2010 C C   . ILE B 39  ? 3.5328 2.8649 2.3585 -0.3627 -0.3138 -0.4527 39  ILE B C   
2011 O O   . ILE B 39  ? 3.5251 2.8832 2.3568 -0.3574 -0.3286 -0.4864 39  ILE B O   
2012 C CB  . ILE B 39  ? 3.5301 2.8048 2.4552 -0.3896 -0.327  -0.4166 39  ILE B CB  
2013 C CG1 . ILE B 39  ? 3.5399 2.7749 2.5108 -0.3923 -0.3193 -0.424  39  ILE B CG1 
2014 C CG2 . ILE B 39  ? 3.5224 2.8171 2.4674 -0.3974 -0.3356 -0.3542 39  ILE B CG2 
2015 C CD1 . ILE B 39  ? 3.5268 2.774  2.5722 -0.4041 -0.3387 -0.3993 39  ILE B CD1 
2016 N N   . ILE B 40  ? 3.5311 2.8767 2.3196 -0.3622 -0.3064 -0.4181 40  ILE B N   
2017 C CA  . ILE B 40  ? 3.521  2.9181 2.2781 -0.3522 -0.3152 -0.4146 40  ILE B CA  
2018 C C   . ILE B 40  ? 3.498  2.9062 2.2881 -0.3707 -0.3437 -0.3654 40  ILE B C   
2019 O O   . ILE B 40  ? 3.4856 2.929  2.2799 -0.3672 -0.3628 -0.3754 40  ILE B O   
2020 C CB  . ILE B 40  ? 3.5345 2.9584 2.2486 -0.3318 -0.2887 -0.4087 40  ILE B CB  
2021 C CG1 . ILE B 40  ? 3.5477 2.9999 2.2286 -0.2999 -0.2695 -0.471  40  ILE B CG1 
2022 C CG2 . ILE B 40  ? 3.5269 2.9994 2.237  -0.3269 -0.2985 -0.3664 40  ILE B CG2 
2023 C CD1 . ILE B 40  ? 3.561  2.9884 2.273  -0.289  -0.257  -0.5209 40  ILE B CD1 
2024 N N   . ASP B 41  ? 3.49   2.8661 2.3053 -0.3897 -0.3475 -0.3157 41  ASP B N   
2025 C CA  . ASP B 41  ? 3.4668 2.8564 2.3252 -0.4026 -0.3727 -0.2699 41  ASP B CA  
2026 C C   . ASP B 41  ? 3.4574 2.8048 2.3605 -0.422  -0.3804 -0.2353 41  ASP B C   
2027 O O   . ASP B 41  ? 3.4709 2.7841 2.3687 -0.424  -0.3638 -0.2284 41  ASP B O   
2028 C CB  . ASP B 41  ? 3.4671 2.9074 2.3304 -0.3869 -0.3701 -0.2361 41  ASP B CB  
2029 C CG  . ASP B 41  ? 3.4698 3.0016 2.3809 -0.3547 -0.3771 -0.2467 41  ASP B CG  
2030 O OD1 . ASP B 41  ? 3.457  3.0008 2.4096 -0.3591 -0.3945 -0.2541 41  ASP B OD1 
2031 O OD2 . ASP B 41  ? 3.4826 3.0675 2.3814 -0.3275 -0.366  -0.2463 41  ASP B OD2 
2032 N N   . VAL B 42  ? 3.432  2.7834 2.3773 -0.4354 -0.406  -0.2141 42  VAL B N   
2033 C CA  . VAL B 42  ? 3.418  2.7442 2.4157 -0.4495 -0.4164 -0.1796 42  VAL B CA  
2034 C C   . VAL B 42  ? 3.3871 2.7385 2.4241 -0.4565 -0.441  -0.1371 42  VAL B C   
2035 O O   . VAL B 42  ? 3.369  2.7422 2.44   -0.4595 -0.4569 -0.1412 42  VAL B O   
2036 C CB  . VAL B 42  ? 3.4212 2.732  2.4547 -0.4523 -0.4155 -0.2056 42  VAL B CB  
2037 C CG1 . VAL B 42  ? 3.447  2.7178 2.4645 -0.4482 -0.3921 -0.2251 42  VAL B CG1 
2038 C CG2 . VAL B 42  ? 3.4181 2.7568 2.4512 -0.4467 -0.422  -0.2495 42  VAL B CG2 
2039 N N   . GLN B 43  ? 3.3784 2.7255 2.4117 -0.4593 -0.4445 -0.0973 43  GLN B N   
2040 C CA  . GLN B 43  ? 3.3488 2.7224 2.4273 -0.4612 -0.4656 -0.0585 43  GLN B CA  
2041 C C   . GLN B 43  ? 3.3334 2.683  2.4499 -0.4693 -0.4731 -0.0156 43  GLN B C   
2042 O O   . GLN B 43  ? 3.3469 2.6758 2.4441 -0.4675 -0.4613 -0.0046 43  GLN B O   
2043 C CB  . GLN B 43  ? 3.3549 2.7771 2.4228 -0.4418 -0.4604 -0.0553 43  GLN B CB  
2044 C CG  . GLN B 43  ? 3.3427 2.8311 2.4945 -0.4201 -0.4655 -0.033  43  GLN B CG  
2045 C CD  . GLN B 43  ? 3.3633 2.9197 2.5279 -0.3852 -0.449  -0.0354 43  GLN B CD  
2046 O OE1 . GLN B 43  ? 3.3799 2.9453 2.5438 -0.3713 -0.4335 -0.0195 43  GLN B OE1 
2047 N NE2 . GLN B 43  ? 3.3546 2.9462 2.5159 -0.3781 -0.4592 -0.0518 43  GLN B NE2 
2048 N N   . GLY B 44  ? 3.3021 2.6569 2.473  -0.4777 -0.4934 0.0072  44  GLY B N   
2049 C CA  . GLY B 44  ? 3.2827 2.6279 2.5046 -0.4801 -0.5017 0.0454  44  GLY B CA  
2050 C C   . GLY B 44  ? 3.2453 2.6218 2.5165 -0.4776 -0.5229 0.0787  44  GLY B C   
2051 O O   . GLY B 44  ? 3.2291 2.637  2.5223 -0.4763 -0.5329 0.0735  44  GLY B O   
2052 N N   . ASP B 45  ? 3.2294 2.596  2.5194 -0.4764 -0.5308 0.112   45  ASP B N   
2053 C CA  . ASP B 45  ? 3.1939 2.5914 2.5378 -0.4689 -0.5481 0.1428  45  ASP B CA  
2054 C C   . ASP B 45  ? 3.1549 2.5644 2.5744 -0.4706 -0.5632 0.1649  45  ASP B C   
2055 O O   . ASP B 45  ? 3.1576 2.556  2.5865 -0.4782 -0.5596 0.1551  45  ASP B O   
2056 C CB  . ASP B 45  ? 3.2077 2.6094 2.5561 -0.4525 -0.537  0.159   45  ASP B CB  
2057 C CG  . ASP B 45  ? 3.218  2.6834 2.608  -0.4215 -0.5234 0.1623  45  ASP B CG  
2058 O OD1 . ASP B 45  ? 3.1959 2.6966 2.6349 -0.4137 -0.5315 0.1679  45  ASP B OD1 
2059 O OD2 . ASP B 45  ? 3.245  2.7211 2.6139 -0.407  -0.5066 0.1605  45  ASP B OD2 
2060 N N   . GLU B 46  ? 3.1158 2.5504 2.5894 -0.4629 -0.5802 0.1937  46  GLU B N   
2061 C CA  . GLU B 46  ? 3.0748 2.5345 2.6289 -0.4583 -0.591  0.2137  46  GLU B CA  
2062 C C   . GLU B 46  ? 3.067  2.5    2.6428 -0.4605 -0.5916 0.228   46  GLU B C   
2063 O O   . GLU B 46  ? 3.076  2.4922 2.6462 -0.4523 -0.5886 0.2381  46  GLU B O   
2064 C CB  . GLU B 46  ? 3.0619 2.5745 2.6783 -0.4303 -0.5869 0.2276  46  GLU B CB  
2065 C CG  . GLU B 46  ? 3.0584 2.633  2.7791 -0.398  -0.5636 0.2301  46  GLU B CG  
2066 C CD  . GLU B 46  ? 3.085  2.7125 2.8681 -0.3517 -0.5317 0.2315  46  GLU B CD  
2067 O OE1 . GLU B 46  ? 3.1091 2.7198 2.8697 -0.3425 -0.5233 0.2347  46  GLU B OE1 
2068 O OE2 . GLU B 46  ? 3.0708 2.7478 2.9171 -0.3307 -0.5227 0.2323  46  GLU B OE2 
2069 N N   . GLY B 47  ? 3.0477 2.4779 2.6496 -0.4713 -0.5965 0.2295  47  GLY B N   
2070 C CA  . GLY B 47  ? 3.0398 2.4524 2.6677 -0.4709 -0.5951 0.2413  47  GLY B CA  
2071 C C   . GLY B 47  ? 3.0776 2.4288 2.6276 -0.4873 -0.5887 0.2261  47  GLY B C   
2072 O O   . GLY B 47  ? 3.0801 2.4147 2.6442 -0.4843 -0.5842 0.2327  47  GLY B O   
2073 N N   . ILE B 48  ? 3.1059 2.4235 2.5713 -0.5035 -0.5875 0.2035  48  ILE B N   
2074 C CA  . ILE B 48  ? 3.1474 2.4088 2.5312 -0.516  -0.5752 0.181   48  ILE B CA  
2075 C C   . ILE B 48  ? 3.1607 2.4072 2.4918 -0.5321 -0.5735 0.1516  48  ILE B C   
2076 O O   . ILE B 48  ? 3.1773 2.4257 2.4611 -0.5331 -0.5698 0.1327  48  ILE B O   
2077 C CB  . ILE B 48  ? 3.1782 2.4178 2.5145 -0.5084 -0.564  0.178   48  ILE B CB  
2078 C CG1 . ILE B 48  ? 3.2317 2.4298 2.4885 -0.5124 -0.5384 0.1452  48  ILE B CG1 
2079 C CG2 . ILE B 48  ? 3.1745 2.4462 2.5098 -0.4999 -0.5664 0.1815  48  ILE B CG2 
2080 C CD1 . ILE B 48  ? 3.2528 2.4288 2.5188 -0.5069 -0.5236 0.1414  48  ILE B CD1 
2081 N N   . ILE B 49  ? 3.1482 2.3841 2.4942 -0.5441 -0.5782 0.1487  49  ILE B N   
2082 C CA  . ILE B 49  ? 3.1584 2.382  2.4697 -0.5567 -0.5767 0.1196  49  ILE B CA  
2083 C C   . ILE B 49  ? 3.2014 2.3668 2.421  -0.5647 -0.561  0.0856  49  ILE B C   
2084 O O   . ILE B 49  ? 3.2191 2.3513 2.4258 -0.5655 -0.5498 0.0827  49  ILE B O   
2085 C CB  . ILE B 49  ? 3.1361 2.3799 2.5111 -0.5602 -0.5793 0.1275  49  ILE B CB  
2086 C CG1 . ILE B 49  ? 3.0932 2.4022 2.5665 -0.5478 -0.5878 0.1581  49  ILE B CG1 
2087 C CG2 . ILE B 49  ? 3.1509 2.3895 2.504  -0.5676 -0.5742 0.0938  49  ILE B CG2 
2088 C CD1 . ILE B 49  ? 3.0738 2.4155 2.6201 -0.5453 -0.5809 0.1676  49  ILE B CD1 
2089 N N   . LEU B 50  ? 3.2162 2.37   2.3716 -0.5696 -0.5592 0.0578  50  LEU B N   
2090 C CA  . LEU B 50  ? 3.2569 2.3629 2.3293 -0.5726 -0.539  0.0195  50  LEU B CA  
2091 C C   . LEU B 50  ? 3.2599 2.3557 2.309  -0.5806 -0.5396 -0.0174 50  LEU B C   
2092 O O   . LEU B 50  ? 3.257  2.38   2.2943 -0.5785 -0.5439 -0.0348 50  LEU B O   
2093 C CB  . LEU B 50  ? 3.2787 2.3866 2.2974 -0.5649 -0.5264 0.011   50  LEU B CB  
2094 C CG  . LEU B 50  ? 3.3106 2.4018 2.3157 -0.5526 -0.5031 0.0162  50  LEU B CG  
2095 C CD1 . LEU B 50  ? 3.2914 2.3952 2.3653 -0.5473 -0.5139 0.0565  50  LEU B CD1 
2096 C CD2 . LEU B 50  ? 3.326  2.4351 2.2959 -0.5432 -0.4909 0.0131  50  LEU B CD2 
2097 N N   . GLU B 51  ? 3.2644 2.3209 2.3088 -0.5892 -0.5367 -0.0294 51  GLU B N   
2098 C CA  . GLU B 51  ? 3.2694 2.3134 2.3005 -0.5942 -0.5353 -0.0681 51  GLU B CA  
2099 C C   . GLU B 51  ? 3.3076 2.3009 2.2619 -0.5902 -0.5109 -0.1131 51  GLU B C   
2100 O O   . GLU B 51  ? 3.3292 2.2894 2.2557 -0.5856 -0.4941 -0.1095 51  GLU B O   
2101 C CB  . GLU B 51  ? 3.2589 2.3209 2.3695 -0.5927 -0.5361 -0.0574 51  GLU B CB  
2102 C CG  . GLU B 51  ? 3.237  2.3876 2.4624 -0.5772 -0.5383 -0.0255 51  GLU B CG  
2103 C CD  . GLU B 51  ? 3.2442 2.4443 2.5743 -0.5605 -0.5187 -0.0152 51  GLU B CD  
2104 O OE1 . GLU B 51  ? 3.2654 2.4346 2.5866 -0.5613 -0.5063 -0.0328 51  GLU B OE1 
2105 O OE2 . GLU B 51  ? 3.2204 2.4791 2.6293 -0.552  -0.5202 0.0126  51  GLU B OE2 
2106 N N   . GLY B 52  ? 3.3138 2.3013 2.2348 -0.5908 -0.5085 -0.1573 52  GLY B N   
2107 C CA  . GLY B 52  ? 3.3477 2.2967 2.206  -0.5818 -0.4821 -0.2069 52  GLY B CA  
2108 C C   . GLY B 52  ? 3.3479 2.2932 2.1996 -0.5817 -0.4836 -0.257  52  GLY B C   
2109 O O   . GLY B 52  ? 3.3299 2.3158 2.1965 -0.5838 -0.4995 -0.2642 52  GLY B O   
2110 N N   . LYS B 53  ? 3.3673 2.2615 2.1975 -0.5788 -0.4677 -0.2933 53  LYS B N   
2111 C CA  . LYS B 53  ? 3.3702 2.2569 2.2025 -0.5756 -0.4666 -0.3477 53  LYS B CA  
2112 C C   . LYS B 53  ? 3.402  2.2387 2.1907 -0.561  -0.4369 -0.3982 53  LYS B C   
2113 O O   . LYS B 53  ? 3.4208 2.2268 2.1898 -0.5544 -0.4173 -0.3855 53  LYS B O   
2114 C CB  . LYS B 53  ? 3.3515 2.258  2.2732 -0.5815 -0.482  -0.3351 53  LYS B CB  
2115 C CG  . LYS B 53  ? 3.3656 2.2742 2.3588 -0.5696 -0.4655 -0.3114 53  LYS B CG  
2116 C CD  . LYS B 53  ? 3.347  2.3237 2.4568 -0.5669 -0.4725 -0.2751 53  LYS B CD  
2117 C CE  . LYS B 53  ? 3.3588 2.3479 2.5357 -0.5553 -0.4559 -0.2437 53  LYS B CE  
2118 N NZ  . LYS B 53  ? 3.3337 2.3824 2.5993 -0.5572 -0.4635 -0.2012 53  LYS B NZ  
2119 N N   . GLU B 54  ? 3.4058 2.2343 2.1797 -0.5548 -0.433  -0.4577 54  GLU B N   
2120 C CA  . GLU B 54  ? 3.4312 2.2177 2.1751 -0.5364 -0.4037 -0.5119 54  GLU B CA  
2121 C C   . GLU B 54  ? 3.4276 2.1787 2.2123 -0.5385 -0.4092 -0.549  54  GLU B C   
2122 O O   . GLU B 54  ? 3.4098 2.1878 2.2284 -0.546  -0.4287 -0.5668 54  GLU B O   
2123 C CB  . GLU B 54  ? 3.4472 2.2889 2.1638 -0.5088 -0.3821 -0.5601 54  GLU B CB  
2124 C CG  . GLU B 54  ? 3.4834 2.3459 2.2254 -0.467  -0.3387 -0.603  54  GLU B CG  
2125 C CD  . GLU B 54  ? 3.5058 2.4823 2.2726 -0.4211 -0.3136 -0.6354 54  GLU B CD  
2126 O OE1 . GLU B 54  ? 3.518  2.4952 2.2799 -0.3934 -0.2898 -0.6912 54  GLU B OE1 
2127 O OE2 . GLU B 54  ? 3.5055 2.5533 2.2791 -0.4168 -0.321  -0.603  54  GLU B OE2 
2128 N N   . GLU B 55  ? 3.4425 2.1295 2.2238 -0.5326 -0.3922 -0.5597 55  GLU B N   
2129 C CA  . GLU B 55  ? 3.4404 2.0826 2.2618 -0.5327 -0.3943 -0.5949 55  GLU B CA  
2130 C C   . GLU B 55  ? 3.4592 2.0569 2.2387 -0.5089 -0.3646 -0.666  55  GLU B C   
2131 O O   . GLU B 55  ? 3.4705 2.0161 2.2738 -0.4983 -0.3503 -0.6835 55  GLU B O   
2132 C CB  . GLU B 55  ? 3.4444 2.0808 2.3411 -0.5335 -0.3946 -0.5479 55  GLU B CB  
2133 C CG  . GLU B 55  ? 3.4525 2.1678 2.4069 -0.5268 -0.3915 -0.4782 55  GLU B CG  
2134 C CD  . GLU B 55  ? 3.443  2.2583 2.5244 -0.5257 -0.4018 -0.4322 55  GLU B CD  
2135 O OE1 . GLU B 55  ? 3.4282 2.2987 2.5222 -0.5313 -0.4156 -0.422  55  GLU B OE1 
2136 O OE2 . GLU B 55  ? 3.445  2.2651 2.592  -0.524  -0.3979 -0.4045 55  GLU B OE2 
2137 N N   . ASP B 56  ? 3.4589 2.0788 2.1752 -0.4996 -0.3557 -0.7054 56  ASP B N   
2138 C CA  . ASP B 56  ? 3.4704 2.0703 2.1436 -0.4721 -0.3254 -0.7752 56  ASP B CA  
2139 C C   . ASP B 56  ? 3.4868 2.0326 2.1187 -0.4581 -0.2914 -0.7676 56  ASP B C   
2140 O O   . ASP B 56  ? 3.4951 1.9876 2.1597 -0.4453 -0.2778 -0.7892 56  ASP B O   
2141 C CB  . ASP B 56  ? 3.4688 2.0679 2.2101 -0.4566 -0.3265 -0.8454 56  ASP B CB  
2142 C CG  . ASP B 56  ? 3.4525 2.1872 2.2654 -0.4107 -0.3151 -0.9184 56  ASP B CG  
2143 O OD1 . ASP B 56  ? 3.4545 2.2496 2.222  -0.4067 -0.3179 -0.9054 56  ASP B OD1 
2144 O OD2 . ASP B 56  ? 3.424  2.2125 2.3475 -0.3765 -0.3062 -0.9883 56  ASP B OD2 
2145 N N   . GLY B 57  ? 3.4891 2.0476 2.0518 -0.4616 -0.2775 -0.7353 57  GLY B N   
2146 C CA  . GLY B 57  ? 3.5034 2.0228 2.0295 -0.4491 -0.2415 -0.7245 57  GLY B CA  
2147 C C   . GLY B 57  ? 3.5025 1.9878 2.0147 -0.4753 -0.2534 -0.6493 57  GLY B C   
2148 O O   . GLY B 57  ? 3.5112 2.0039 1.989  -0.4725 -0.231  -0.6225 57  GLY B O   
2149 N N   . LYS B 58  ? 3.4889 1.9405 2.0301 -0.5008 -0.2898 -0.6148 58  LYS B N   
2150 C CA  . LYS B 58  ? 3.4847 1.9185 2.0305 -0.5217 -0.3078 -0.5441 58  LYS B CA  
2151 C C   . LYS B 58  ? 3.4604 1.9369 1.9904 -0.5496 -0.3405 -0.4968 58  LYS B C   
2152 O O   . LYS B 58  ? 3.4417 1.9482 2.0005 -0.5607 -0.3679 -0.5025 58  LYS B O   
2153 C CB  . LYS B 58  ? 3.4846 1.9037 2.1175 -0.5211 -0.326  -0.5314 58  LYS B CB  
2154 C CG  . LYS B 58  ? 3.4847 1.9703 2.2065 -0.5261 -0.3451 -0.4612 58  LYS B CG  
2155 C CD  . LYS B 58  ? 3.5153 2.04   2.2806 -0.5008 -0.3168 -0.432  58  LYS B CD  
2156 C CE  . LYS B 58  ? 3.5366 2.0599 2.3848 -0.4749 -0.2993 -0.4417 58  LYS B CE  
2157 N NZ  . LYS B 58  ? 3.5241 2.0787 2.4647 -0.4829 -0.3224 -0.4102 58  LYS B NZ  
2158 N N   . ILE B 59  ? 3.4575 1.9346 1.9467 -0.5611 -0.3386 -0.4506 59  ILE B N   
2159 C CA  . ILE B 59  ? 3.4323 1.9547 1.9218 -0.5834 -0.3698 -0.4039 59  ILE B CA  
2160 C C   . ILE B 59  ? 3.414  1.9205 1.9365 -0.6034 -0.4    -0.3427 59  ILE B C   
2161 O O   . ILE B 59  ? 3.4276 1.9052 1.9452 -0.5983 -0.3864 -0.3225 59  ILE B O   
2162 C CB  . ILE B 59  ? 3.4401 1.9995 1.8865 -0.5765 -0.3473 -0.3972 59  ILE B CB  
2163 C CG1 . ILE B 59  ? 3.4513 2.0391 1.8701 -0.5542 -0.3183 -0.4584 59  ILE B CG1 
2164 C CG2 . ILE B 59  ? 3.4181 2.0367 1.8899 -0.5918 -0.3785 -0.3462 59  ILE B CG2 
2165 C CD1 . ILE B 59  ? 3.4636 2.0911 1.8537 -0.5391 -0.2861 -0.4574 59  ILE B CD1 
2166 N N   . LYS B 60  ? 3.3804 1.9083 1.9392 -0.6249 -0.4405 -0.3141 60  LYS B N   
2167 C CA  . LYS B 60  ? 3.3563 1.8875 1.9624 -0.6411 -0.4697 -0.2557 60  LYS B CA  
2168 C C   . LYS B 60  ? 3.3282 1.902  1.938  -0.6568 -0.4942 -0.2075 60  LYS B C   
2169 O O   . LYS B 60  ? 3.3029 1.9246 1.9465 -0.6645 -0.5169 -0.2004 60  LYS B O   
2170 C CB  . LYS B 60  ? 3.3399 1.9007 2.0348 -0.6419 -0.4887 -0.2562 60  LYS B CB  
2171 C CG  . LYS B 60  ? 3.3712 1.929  2.1275 -0.6148 -0.4615 -0.2898 60  LYS B CG  
2172 C CD  . LYS B 60  ? 3.3911 1.9833 2.2232 -0.5946 -0.4443 -0.2555 60  LYS B CD  
2173 C CE  . LYS B 60  ? 3.4161 2.0061 2.3136 -0.5705 -0.4215 -0.283  60  LYS B CE  
2174 N NZ  . LYS B 60  ? 3.4511 2.0307 2.3361 -0.5422 -0.3864 -0.3462 60  LYS B NZ  
2175 N N   . ALA B 61  ? 3.3306 1.8855 1.9091 -0.6609 -0.4906 -0.1752 61  ALA B N   
2176 C CA  . ALA B 61  ? 3.3032 1.9024 1.9014 -0.6714 -0.5136 -0.1294 61  ALA B CA  
2177 C C   . ALA B 61  ? 3.2718 1.8784 1.9272 -0.6828 -0.5422 -0.0753 61  ALA B C   
2178 O O   . ALA B 61  ? 3.2805 1.8528 1.9412 -0.6809 -0.5361 -0.0714 61  ALA B O   
2179 C CB  . ALA B 61  ? 3.3265 1.9211 1.8695 -0.663  -0.4882 -0.1329 61  ALA B CB  
2180 N N   . LYS B 62  ? 3.2307 1.8866 1.934  -0.6933 -0.5733 -0.0339 62  LYS B N   
2181 C CA  . LYS B 62  ? 3.1935 1.8797 1.9724 -0.6988 -0.5983 0.0169  62  LYS B CA  
2182 C C   . LYS B 62  ? 3.1644 1.8972 1.9761 -0.6993 -0.6175 0.0529  62  LYS B C   
2183 O O   . LYS B 62  ? 3.1417 1.9195 1.9825 -0.701  -0.632  0.0571  62  LYS B O   
2184 C CB  . LYS B 62  ? 3.1662 1.901  2.035  -0.6994 -0.6116 0.0248  62  LYS B CB  
2185 C CG  . LYS B 62  ? 3.1447 1.9518 2.1333 -0.6854 -0.6114 0.065   62  LYS B CG  
2186 C CD  . LYS B 62  ? 3.1362 2.0091 2.226  -0.6741 -0.6027 0.0602  62  LYS B CD  
2187 C CE  . LYS B 62  ? 3.1011 2.0703 2.3201 -0.6611 -0.6019 0.1002  62  LYS B CE  
2188 N NZ  . LYS B 62  ? 3.0836 2.0998 2.3747 -0.6598 -0.5993 0.0953  62  LYS B NZ  
2189 N N   . ILE B 63  ? 3.1655 1.8835 1.97   -0.6966 -0.6176 0.0766  63  ILE B N   
2190 C CA  . ILE B 63  ? 3.1391 1.8984 1.9836 -0.6926 -0.635  0.1102  63  ILE B CA  
2191 C C   . ILE B 63  ? 3.0918 1.8962 2.0386 -0.69   -0.6591 0.1546  63  ILE B C   
2192 O O   . ILE B 63  ? 3.0989 1.8826 2.0509 -0.6883 -0.653  0.1604  63  ILE B O   
2193 C CB  . ILE B 63  ? 3.1784 1.8992 1.9546 -0.6843 -0.6118 0.0991  63  ILE B CB  
2194 C CG1 . ILE B 63  ? 3.2213 1.9246 1.9184 -0.6803 -0.5797 0.054   63  ILE B CG1 
2195 C CG2 . ILE B 63  ? 3.1515 1.9137 1.9835 -0.6758 -0.6302 0.1358  63  ILE B CG2 
2196 C CD1 . ILE B 63  ? 3.2641 1.9435 1.9066 -0.6673 -0.5449 0.0372  63  ILE B CD1 
2197 N N   . ILE B 64  ? 3.0407 1.9098 2.0715 -0.6886 -0.6848 0.1848  64  ILE B N   
2198 C CA  . ILE B 64  ? 2.9881 1.9158 2.1332 -0.6811 -0.7026 0.2249  64  ILE B CA  
2199 C C   . ILE B 64  ? 2.9558 1.9302 2.1653 -0.6654 -0.717  0.2525  64  ILE B C   
2200 O O   . ILE B 64  ? 2.936  1.9452 2.1678 -0.6634 -0.7268 0.2566  64  ILE B O   
2201 C CB  . ILE B 64  ? 2.9514 1.9329 2.1736 -0.6857 -0.7101 0.2331  64  ILE B CB  
2202 C CG1 . ILE B 64  ? 2.9875 1.9351 2.17   -0.6923 -0.6896 0.2044  64  ILE B CG1 
2203 C CG2 . ILE B 64  ? 2.8905 1.9462 2.24   -0.6752 -0.7224 0.2739  64  ILE B CG2 
2204 C CD1 . ILE B 64  ? 3.02   1.9598 2.1626 -0.6921 -0.6761 0.1654  64  ILE B CD1 
2205 N N   . VAL B 65  ? 2.9495 1.9235 2.1904 -0.6524 -0.7185 0.27    65  VAL B N   
2206 C CA  . VAL B 65  ? 2.9197 1.9404 2.2371 -0.6301 -0.7292 0.2937  65  VAL B CA  
2207 C C   . VAL B 65  ? 2.8542 1.9587 2.313  -0.6153 -0.7398 0.3237  65  VAL B C   
2208 O O   . VAL B 65  ? 2.8392 1.955  2.3387 -0.6138 -0.7366 0.3329  65  VAL B O   
2209 C CB  . VAL B 65  ? 2.9536 1.934  2.2367 -0.6159 -0.7199 0.2895  65  VAL B CB  
2210 C CG1 . VAL B 65  ? 2.9243 1.9437 2.2751 -0.594  -0.7325 0.3098  65  VAL B CG1 
2211 C CG2 . VAL B 65  ? 3.0281 1.9378 2.1776 -0.6254 -0.6919 0.252   65  VAL B CG2 
2212 N N   . LYS B 66  ? 2.814  1.9791 2.3439 -0.6054 -0.7495 0.3372  66  LYS B N   
2213 C CA  . LYS B 66  ? 2.7495 2.0016 2.4138 -0.5888 -0.7528 0.3606  66  LYS B CA  
2214 C C   . LYS B 66  ? 2.709  2.0029 2.4745 -0.5588 -0.7539 0.3815  66  LYS B C   
2215 O O   . LYS B 66  ? 2.7258 1.9912 2.4725 -0.5452 -0.7576 0.3808  66  LYS B O   
2216 C CB  . LYS B 66  ? 2.7404 2.0472 2.4416 -0.5781 -0.7487 0.3568  66  LYS B CB  
2217 C CG  . LYS B 66  ? 2.8098 2.113  2.4463 -0.5826 -0.7198 0.3188  66  LYS B CG  
2218 C CD  . LYS B 66  ? 2.8431 2.1745 2.5046 -0.5782 -0.6866 0.2989  66  LYS B CD  
2219 C CE  . LYS B 66  ? 2.8148 2.2408 2.5988 -0.5541 -0.6664 0.3067  66  LYS B CE  
2220 N NZ  . LYS B 66  ? 2.8269 2.2707 2.6397 -0.5545 -0.6427 0.3017  66  LYS B NZ  
2221 N N   . LYS B 67  ? 2.6504 2.015  2.5274 -0.5481 -0.7499 0.399   67  LYS B N   
2222 C CA  . LYS B 67  ? 2.5982 2.0199 2.5935 -0.516  -0.7455 0.4159  67  LYS B CA  
2223 C C   . LYS B 67  ? 2.5737 2.0233 2.6275 -0.4829 -0.7508 0.4209  67  LYS B C   
2224 O O   . LYS B 67  ? 2.54   2.0401 2.6431 -0.4737 -0.753  0.4262  67  LYS B O   
2225 C CB  . LYS B 67  ? 2.5499 2.0663 2.6563 -0.5056 -0.7225 0.4245  67  LYS B CB  
2226 C CG  . LYS B 67  ? 2.5202 2.1262 2.76   -0.4555 -0.689  0.4245  67  LYS B CG  
2227 C CD  . LYS B 67  ? 2.5036 2.2141 2.8343 -0.4386 -0.6436 0.4176  67  LYS B CD  
2228 C CE  . LYS B 67  ? 2.4727 2.2805 2.9248 -0.3852 -0.6078 0.4081  67  LYS B CE  
2229 N NZ  . LYS B 67  ? 2.4935 2.2923 2.968  -0.352  -0.5907 0.3988  67  LYS B NZ  
2230 N N   . GLY B 68  ? 2.5913 2.0046 2.6365 -0.4649 -0.753  0.4176  68  GLY B N   
2231 C CA  . GLY B 68  ? 2.5777 2.0117 2.674  -0.4295 -0.7528 0.4188  68  GLY B CA  
2232 C C   . GLY B 68  ? 2.6435 2.0158 2.632  -0.4377 -0.754  0.4059  68  GLY B C   
2233 O O   . GLY B 68  ? 2.6374 2.0063 2.6504 -0.4134 -0.7579 0.4087  68  GLY B O   
2234 N N   . TYR B 69  ? 2.7025 2.0297 2.5758 -0.4701 -0.7481 0.3906  69  TYR B N   
2235 C CA  . TYR B 69  ? 2.7623 2.0455 2.5385 -0.4774 -0.7415 0.3763  69  TYR B CA  
2236 C C   . TYR B 69  ? 2.8138 2.0329 2.5216 -0.4754 -0.7336 0.3634  69  TYR B C   
2237 O O   . TYR B 69  ? 2.8603 2.0299 2.487  -0.4939 -0.7229 0.3459  69  TYR B O   
2238 C CB  . TYR B 69  ? 2.8009 2.0685 2.49   -0.5064 -0.7338 0.3596  69  TYR B CB  
2239 C CG  . TYR B 69  ? 2.7769 2.1091 2.5185 -0.499  -0.7316 0.3627  69  TYR B CG  
2240 C CD1 . TYR B 69  ? 2.7969 2.1399 2.5108 -0.4936 -0.7274 0.3571  69  TYR B CD1 
2241 C CD2 . TYR B 69  ? 2.7447 2.1349 2.5644 -0.4926 -0.7251 0.3663  69  TYR B CD2 
2242 C CE1 . TYR B 69  ? 2.7778 2.1756 2.533  -0.4858 -0.726  0.3572  69  TYR B CE1 
2243 C CE2 . TYR B 69  ? 2.7252 2.171  2.5867 -0.4854 -0.7223 0.3656  69  TYR B CE2 
2244 C CZ  . TYR B 69  ? 2.7477 2.1973 2.576  -0.4796 -0.7206 0.3587  69  TYR B CZ  
2245 O OH  . TYR B 69  ? 2.7367 2.2403 2.6011 -0.4697 -0.7152 0.3539  69  TYR B OH  
2246 N N   . LYS B 70  ? 2.8072 2.0246 2.5428 -0.4528 -0.7377 0.3702  70  LYS B N   
2247 C CA  . LYS B 70  ? 2.8552 2.0153 2.5323 -0.4478 -0.7293 0.3576  70  LYS B CA  
2248 C C   . LYS B 70  ? 2.8993 2.0406 2.4965 -0.4577 -0.7178 0.3503  70  LYS B C   
2249 O O   . LYS B 70  ? 2.8813 2.0441 2.5195 -0.4393 -0.7219 0.3624  70  LYS B O   
2250 C CB  . LYS B 70  ? 2.8311 2.0169 2.6116 -0.4034 -0.726  0.3618  70  LYS B CB  
2251 C CG  . LYS B 70  ? 2.8179 2.0673 2.704  -0.3707 -0.7009 0.3539  70  LYS B CG  
2252 C CD  . LYS B 70  ? 2.8241 2.109  2.8035 -0.3144 -0.6729 0.3414  70  LYS B CD  
2253 C CE  . LYS B 70  ? 2.8061 2.163  2.8914 -0.2796 -0.6425 0.3314  70  LYS B CE  
2254 N NZ  . LYS B 70  ? 2.8517 2.1829 2.8957 -0.2887 -0.626  0.3136  70  LYS B NZ  
2255 N N   . PHE B 71  ? 2.9525 2.0575 2.4394 -0.4848 -0.7014 0.33    71  PHE B N   
2256 C CA  . PHE B 71  ? 2.9901 2.0867 2.4051 -0.4932 -0.6861 0.3211  71  PHE B CA  
2257 C C   . PHE B 71  ? 3.027  2.0804 2.3993 -0.4871 -0.6736 0.3133  71  PHE B C   
2258 O O   . PHE B 71  ? 3.065  2.0719 2.3734 -0.497  -0.6601 0.2939  71  PHE B O   
2259 C CB  . PHE B 71  ? 3.0258 2.1084 2.3493 -0.5197 -0.6703 0.2979  71  PHE B CB  
2260 C CG  . PHE B 71  ? 3.0058 2.1341 2.3724 -0.5211 -0.6722 0.2963  71  PHE B CG  
2261 C CD1 . PHE B 71  ? 2.9862 2.1671 2.3903 -0.5134 -0.6751 0.3034  71  PHE B CD1 
2262 C CD2 . PHE B 71  ? 3.015  2.1404 2.3877 -0.5254 -0.6638 0.2841  71  PHE B CD2 
2263 C CE1 . PHE B 71  ? 2.9688 2.19   2.4109 -0.5142 -0.6761 0.2999  71  PHE B CE1 
2264 C CE2 . PHE B 71  ? 2.9951 2.1637 2.4101 -0.5272 -0.6649 0.2831  71  PHE B CE2 
2265 C CZ  . PHE B 71  ? 2.9678 2.1793 2.4143 -0.5241 -0.6747 0.2921  71  PHE B CZ  
2266 N N   . LYS B 72  ? 3.0158 2.0818 2.4215 -0.4706 -0.677  0.3276  72  LYS B N   
2267 C CA  . LYS B 72  ? 3.0498 2.0789 2.4224 -0.4637 -0.6639 0.3204  72  LYS B CA  
2268 C C   . LYS B 72  ? 3.0996 2.1156 2.3718 -0.4834 -0.637  0.3054  72  LYS B C   
2269 O O   . LYS B 72  ? 3.1285 2.1071 2.3542 -0.486  -0.6244 0.2969  72  LYS B O   
2270 C CB  . LYS B 72  ? 3.0279 2.086  2.4957 -0.4273 -0.6661 0.3353  72  LYS B CB  
2271 C CG  . LYS B 72  ? 3.0532 2.1608 2.5315 -0.4113 -0.6372 0.338   72  LYS B CG  
2272 C CD  . LYS B 72  ? 3.0687 2.1999 2.6215 -0.3694 -0.6149 0.3379  72  LYS B CD  
2273 C CE  . LYS B 72  ? 3.095  2.2703 2.6531 -0.3545 -0.5866 0.342   72  LYS B CE  
2274 N NZ  . LYS B 72  ? 3.1475 2.3198 2.6299 -0.3689 -0.5568 0.3285  72  LYS B NZ  
2275 N N   . TYR B 73  ? 3.1056 2.1539 2.3473 -0.4954 -0.628  0.3009  73  TYR B N   
2276 C CA  . TYR B 73  ? 3.1466 2.1944 2.3038 -0.5086 -0.6001 0.2842  73  TYR B CA  
2277 C C   . TYR B 73  ? 3.1867 2.2113 2.2702 -0.5234 -0.5764 0.2512  73  TYR B C   
2278 O O   . TYR B 73  ? 3.1805 2.2131 2.2781 -0.5261 -0.5812 0.2426  73  TYR B O   
2279 C CB  . TYR B 73  ? 3.1319 2.2269 2.296  -0.5072 -0.6021 0.2944  73  TYR B CB  
2280 C CG  . TYR B 73  ? 3.1115 2.2355 2.3462 -0.4841 -0.6093 0.3197  73  TYR B CG  
2281 C CD1 . TYR B 73  ? 3.1258 2.2339 2.3688 -0.4735 -0.5996 0.3252  73  TYR B CD1 
2282 C CD2 . TYR B 73  ? 3.0852 2.2589 2.3837 -0.4671 -0.6183 0.3333  73  TYR B CD2 
2283 C CE1 . TYR B 73  ? 3.1073 2.238  2.4132 -0.4516 -0.6051 0.3465  73  TYR B CE1 
2284 C CE2 . TYR B 73  ? 3.0682 2.2642 2.426  -0.4444 -0.622  0.3536  73  TYR B CE2 
2285 C CZ  . TYR B 73  ? 3.082  2.2587 2.4461 -0.4347 -0.6129 0.359   73  TYR B CZ  
2286 O OH  . TYR B 73  ? 3.0699 2.2692 2.4939 -0.409  -0.6119 0.3757  73  TYR B OH  
2287 N N   . PRO B 74  ? 3.2252 2.2191 2.2336 -0.5321 -0.5501 0.2324  74  PRO B N   
2288 C CA  . PRO B 74  ? 3.2625 2.2269 2.2032 -0.5424 -0.5249 0.1983  74  PRO B CA  
2289 C C   . PRO B 74  ? 3.2773 2.2667 2.1768 -0.5497 -0.5089 0.174   74  PRO B C   
2290 O O   . PRO B 74  ? 3.2773 2.2958 2.1507 -0.5516 -0.5007 0.1726  74  PRO B O   
2291 C CB  . PRO B 74  ? 3.2963 2.2328 2.1847 -0.5424 -0.4957 0.185   74  PRO B CB  
2292 C CG  . PRO B 74  ? 3.2784 2.2264 2.2209 -0.5304 -0.5104 0.2143  74  PRO B CG  
2293 C CD  . PRO B 74  ? 3.232  2.2116 2.2177 -0.5328 -0.5428 0.2424  74  PRO B CD  
2294 N N   . ILE B 75  ? 3.2909 2.2656 2.1822 -0.5525 -0.5041 0.1529  75  ILE B N   
2295 C CA  . ILE B 75  ? 3.309  2.3015 2.1685 -0.5553 -0.4883 0.1224  75  ILE B CA  
2296 C C   . ILE B 75  ? 3.3522 2.3251 2.1341 -0.5557 -0.4476 0.0866  75  ILE B C   
2297 O O   . ILE B 75  ? 3.3729 2.3112 2.135  -0.5535 -0.4305 0.0813  75  ILE B O   
2298 C CB  . ILE B 75  ? 3.3047 2.2938 2.2064 -0.5533 -0.4978 0.1167  75  ILE B CB  
2299 C CG1 . ILE B 75  ? 3.2719 2.3184 2.2545 -0.5458 -0.5215 0.1358  75  ILE B CG1 
2300 C CG2 . ILE B 75  ? 3.3362 2.3033 2.1858 -0.5565 -0.4721 0.0753  75  ILE B CG2 
2301 C CD1 . ILE B 75  ? 3.2474 2.3395 2.3088 -0.5286 -0.5361 0.1696  75  ILE B CD1 
2302 N N   . HIS B 76  ? 3.3635 2.3601 2.1041 -0.5561 -0.4316 0.0608  76  HIS B N   
2303 C CA  . HIS B 76  ? 3.3993 2.3885 2.0785 -0.551  -0.3902 0.0241  76  HIS B CA  
2304 C C   . HIS B 76  ? 3.4202 2.3972 2.0772 -0.5474 -0.3738 -0.0188 76  HIS B C   
2305 O O   . HIS B 76  ? 3.4079 2.3943 2.096  -0.5491 -0.3946 -0.0207 76  HIS B O   
2306 C CB  . HIS B 76  ? 3.4023 2.4422 2.0632 -0.5422 -0.3746 0.0237  76  HIS B CB  
2307 C CG  . HIS B 76  ? 3.4073 2.4851 2.1233 -0.5259 -0.3707 0.0561  76  HIS B CG  
2308 N ND1 . HIS B 76  ? 3.3915 2.5096 2.1926 -0.5125 -0.3953 0.0908  76  HIS B ND1 
2309 C CD2 . HIS B 76  ? 3.4257 2.5094 2.1302 -0.5183 -0.3427 0.0564  76  HIS B CD2 
2310 C CE1 . HIS B 76  ? 3.3926 2.5161 2.2068 -0.5078 -0.3894 0.1128  76  HIS B CE1 
2311 N NE2 . HIS B 76  ? 3.4141 2.5213 2.1754 -0.5106 -0.358  0.0943  76  HIS B NE2 
2312 N N   . MET B 77  ? 3.4488 2.4047 2.0579 -0.5417 -0.3364 -0.0532 77  MET B N   
2313 C CA  . MET B 77  ? 3.4695 2.4128 2.0642 -0.5333 -0.3173 -0.0981 77  MET B CA  
2314 C C   . MET B 77  ? 3.4914 2.4435 2.0405 -0.52   -0.2734 -0.1345 77  MET B C   
2315 O O   . MET B 77  ? 3.5088 2.4323 2.046  -0.5151 -0.2462 -0.1426 77  MET B O   
2316 C CB  . MET B 77  ? 3.4824 2.3837 2.1059 -0.5314 -0.3181 -0.0978 77  MET B CB  
2317 C CG  . MET B 77  ? 3.5017 2.4034 2.143  -0.5175 -0.3047 -0.1384 77  MET B CG  
2318 S SD  . MET B 77  ? 3.5204 2.4012 2.2256 -0.5065 -0.3056 -0.1301 77  MET B SD  
2319 C CE  . MET B 77  ? 3.4783 2.3644 2.2202 -0.5282 -0.3578 -0.086  77  MET B CE  
2320 N N   . CYS B 78  ? 3.4879 2.4813 2.0118 -0.513  -0.2663 -0.1555 78  CYS B N   
2321 C CA  . CYS B 78  ? 3.5018 2.5148 1.9864 -0.4973 -0.2248 -0.1885 78  CYS B CA  
2322 C C   . CYS B 78  ? 3.5169 2.5176 1.989  -0.4814 -0.2023 -0.2453 78  CYS B C   
2323 O O   . CYS B 78  ? 3.5128 2.5158 1.9963 -0.4806 -0.222  -0.2649 78  CYS B O   
2324 C CB  . CYS B 78  ? 3.4916 2.5678 1.9621 -0.49   -0.2255 -0.178  78  CYS B CB  
2325 S SG  . CYS B 78  ? 3.4873 2.6099 2.017  -0.4868 -0.2401 -0.1156 78  CYS B SG  
2326 N N   . PHE B 79  ? 3.5308 2.5169 1.9847 -0.4687 -0.1613 -0.2717 79  PHE B N   
2327 C CA  . PHE B 79  ? 3.5436 2.5194 1.9958 -0.4476 -0.1354 -0.3279 79  PHE B CA  
2328 C C   . PHE B 79  ? 3.5456 2.5639 1.9716 -0.4253 -0.0943 -0.3551 79  PHE B C   
2329 O O   . PHE B 79  ? 3.549  2.5645 1.9738 -0.4224 -0.0644 -0.3448 79  PHE B O   
2330 C CB  . PHE B 79  ? 3.5563 2.4704 2.0282 -0.4475 -0.1228 -0.3337 79  PHE B CB  
2331 C CG  . PHE B 79  ? 3.5577 2.4445 2.0733 -0.459  -0.1591 -0.3094 79  PHE B CG  
2332 C CD1 . PHE B 79  ? 3.5576 2.4425 2.1023 -0.4545 -0.1784 -0.333  79  PHE B CD1 
2333 C CD2 . PHE B 79  ? 3.5598 2.4377 2.1059 -0.4675 -0.1727 -0.2642 79  PHE B CD2 
2334 C CE1 . PHE B 79  ? 3.5556 2.4242 2.1471 -0.4644 -0.2093 -0.3072 79  PHE B CE1 
2335 C CE2 . PHE B 79  ? 3.5587 2.4202 2.1492 -0.4743 -0.2036 -0.2418 79  PHE B CE2 
2336 C CZ  . PHE B 79  ? 3.5538 2.4059 2.1594 -0.4761 -0.2214 -0.2612 79  PHE B CZ  
2337 N N   . GLY B 80  ? 3.5415 2.5993 1.9465 -0.4093 -0.0931 -0.3895 80  GLY B N   
2338 C CA  . GLY B 80  ? 3.5405 2.6485 1.9226 -0.382  -0.0555 -0.4168 80  GLY B CA  
2339 C C   . GLY B 80  ? 3.547  2.6489 1.9331 -0.3532 -0.0354 -0.4828 80  GLY B C   
2340 O O   . GLY B 80  ? 3.5494 2.636  1.9456 -0.3519 -0.0604 -0.5113 80  GLY B O   
2341 N N   . ILE B 81  ? 3.5468 2.6572 1.9307 -0.3305 0.009   -0.5074 81  ILE B N   
2342 C CA  . ILE B 81  ? 3.5494 2.6594 1.9465 -0.2955 0.0296  -0.5728 81  ILE B CA  
2343 C C   . ILE B 81  ? 3.5379 2.7095 1.9127 -0.2617 0.0706  -0.5945 81  ILE B C   
2344 O O   . ILE B 81  ? 3.5314 2.7117 1.9156 -0.2582 0.1061  -0.5767 81  ILE B O   
2345 C CB  . ILE B 81  ? 3.561  2.6097 2.0097 -0.2903 0.0385  -0.5927 81  ILE B CB  
2346 C CG1 . ILE B 81  ? 3.5749 2.5814 2.0618 -0.3141 -0.0041 -0.5691 81  ILE B CG1 
2347 C CG2 . ILE B 81  ? 3.5602 2.6116 2.0263 -0.2508 0.0549  -0.6625 81  ILE B CG2 
2348 C CD1 . ILE B 81  ? 3.5891 2.5437 2.1341 -0.3068 0.0016  -0.5783 81  ILE B CD1 
2349 N N   . THR B 82  ? 3.5326 2.748  1.8772 -0.2362 0.0653  -0.6323 82  THR B N   
2350 C CA  . THR B 82  ? 3.5218 2.806  1.8437 -0.1953 0.1     -0.6549 82  THR B CA  
2351 C C   . THR B 82  ? 3.5039 2.8044 1.853  -0.1427 0.1066  -0.7305 82  THR B C   
2352 O O   . THR B 82  ? 3.4786 2.851  1.84   -0.0911 0.1332  -0.7514 82  THR B O   
2353 C CB  . THR B 82  ? 3.5231 2.8913 1.8188 -0.1854 0.0814  -0.624  82  THR B CB  
2354 O OG1 . THR B 82  ? 3.5045 2.964  1.8115 -0.1423 0.114   -0.6104 82  THR B OG1 
2355 C CG2 . THR B 82  ? 3.5123 2.9229 1.8124 -0.1565 0.0437  -0.6644 82  THR B CG2 
2356 N N   . GLU B 83  ? 3.5077 2.7494 1.8762 -0.1507 0.0784  -0.7687 83  GLU B N   
2357 C CA  . GLU B 83  ? 3.4832 2.7388 1.8962 -0.0997 0.0734  -0.8417 83  GLU B CA  
2358 C C   . GLU B 83  ? 3.4815 2.6738 1.9379 -0.0919 0.1022  -0.8618 83  GLU B C   
2359 O O   . GLU B 83  ? 3.5065 2.6257 1.9651 -0.1339 0.1125  -0.8241 83  GLU B O   
2360 C CB  . GLU B 83  ? 3.4868 2.7458 1.9478 -0.1002 0.0182  -0.8683 83  GLU B CB  
2361 C CG  . GLU B 83  ? 3.4604 2.8552 1.9814 -0.0304 -0.0189 -0.9134 83  GLU B CG  
2362 C CD  . GLU B 83  ? 3.4796 2.877  2.1177 -0.0358 -0.0538 -0.9082 83  GLU B CD  
2363 O OE1 . GLU B 83  ? 3.4812 2.8642 2.1488 -0.0608 -0.0891 -0.9131 83  GLU B OE1 
2364 O OE2 . GLU B 83  ? 3.493  2.8889 2.1758 -0.026  -0.0384 -0.8932 83  GLU B OE2 
2365 N N   . GLU B 84  ? 3.4507 2.6681 1.9405 -0.0348 0.1125  -0.9223 84  GLU B N   
2366 C CA  . GLU B 84  ? 3.4432 2.6096 1.9902 -0.0152 0.1347  -0.9464 84  GLU B CA  
2367 C C   . GLU B 84  ? 3.4555 2.5238 2.0337 -0.0404 0.1058  -0.9716 84  GLU B C   
2368 O O   . GLU B 84  ? 3.4532 2.5334 2.0394 -0.04   0.0647  -0.9996 84  GLU B O   
2369 C CB  . GLU B 84  ? 3.4113 2.6829 2.027  0.0794  0.1319  -0.9952 84  GLU B CB  
2370 C CG  . GLU B 84  ? 3.4168 2.8118 2.0505 0.1035  0.1543  -0.9278 84  GLU B CG  
2371 C CD  . GLU B 84  ? 3.4352 2.8789 2.164  0.1171  0.1749  -0.8665 84  GLU B CD  
2372 O OE1 . GLU B 84  ? 3.4321 2.9316 2.1334 0.1175  0.1863  -0.8353 84  GLU B OE1 
2373 O OE2 . GLU B 84  ? 3.442  2.8555 2.2495 0.1274  0.1797  -0.8644 84  GLU B OE2 
2374 N N   . ASN B 85  ? 3.466  2.4369 2.0618 -0.0628 0.1289  -0.9594 85  ASN B N   
2375 C CA  . ASN B 85  ? 3.4781 2.3489 2.1064 -0.0848 0.1057  -0.9734 85  ASN B CA  
2376 C C   . ASN B 85  ? 3.5018 2.3068 2.0616 -0.1498 0.0738  -0.9439 85  ASN B C   
2377 O O   . ASN B 85  ? 3.4921 2.3002 2.0819 -0.1452 0.0357  -0.9784 85  ASN B O   
2378 C CB  . ASN B 85  ? 3.4506 2.3587 2.1811 -0.0198 0.0773  -1.0455 85  ASN B CB  
2379 C CG  . ASN B 85  ? 3.4298 2.4442 2.2471 0.0666  0.0826  -1.0737 85  ASN B CG  
2380 O OD1 . ASN B 85  ? 3.4351 2.4762 2.2583 0.0764  0.1158  -1.0378 85  ASN B OD1 
2381 N ND2 . ASN B 85  ? 3.4281 2.445  2.2698 0.0829  0.09    -1.0741 85  ASN B ND2 
2382 N N   . ILE B 86  ? 3.5165 2.2812 2.0054 -0.2035 0.0816  -0.8782 86  ILE B N   
2383 C CA  . ILE B 86  ? 3.5218 2.2563 1.9765 -0.2525 0.0394  -0.8374 86  ILE B CA  
2384 C C   . ILE B 86  ? 3.5283 2.1716 1.9933 -0.2837 0.0321  -0.7951 86  ILE B C   
2385 O O   . ILE B 86  ? 3.5304 2.1626 2.0022 -0.2837 0.0602  -0.7652 86  ILE B O   
2386 C CB  . ILE B 86  ? 3.5191 2.3246 1.9269 -0.2716 0.0345  -0.7902 86  ILE B CB  
2387 C CG1 . ILE B 86  ? 3.5131 2.3981 1.8936 -0.2455 0.0315  -0.8279 86  ILE B CG1 
2388 C CG2 . ILE B 86  ? 3.5275 2.3227 1.9373 -0.3132 -0.0094 -0.7314 86  ILE B CG2 
2389 C CD1 . ILE B 86  ? 3.5185 2.4136 1.9185 -0.2428 -0.0126 -0.8635 86  ILE B CD1 
2390 N N   . SER B 87  ? 3.5303 2.1093 1.9955 -0.3091 -0.0063 -0.7915 87  SER B N   
2391 C CA  . SER B 87  ? 3.5382 2.0421 2.0141 -0.3346 -0.0215 -0.7458 87  SER B CA  
2392 C C   . SER B 87  ? 3.5349 2.0359 1.972  -0.379  -0.0646 -0.6913 87  SER B C   
2393 O O   . SER B 87  ? 3.5322 2.0255 1.9919 -0.3923 -0.1038 -0.6933 87  SER B O   
2394 C CB  . SER B 87  ? 3.5444 2.0009 2.0916 -0.3175 -0.0354 -0.778  87  SER B CB  
2395 O OG  . SER B 87  ? 3.5589 1.987  2.16   -0.317  -0.0379 -0.738  87  SER B OG  
2396 N N   . GLN B 88  ? 3.5304 2.0411 1.9128 -0.4016 -0.0571 -0.6436 88  GLN B N   
2397 C CA  . GLN B 88  ? 3.5239 2.042  1.8773 -0.4392 -0.0961 -0.5869 88  GLN B CA  
2398 C C   . GLN B 88  ? 3.5266 1.9646 1.8772 -0.4644 -0.1216 -0.5422 88  GLN B C   
2399 O O   . GLN B 88  ? 3.5329 1.9641 1.8781 -0.4708 -0.1135 -0.5018 88  GLN B O   
2400 C CB  . GLN B 88  ? 3.525  2.1193 1.8737 -0.4362 -0.0778 -0.555  88  GLN B CB  
2401 C CG  . GLN B 88  ? 3.5256 2.2168 1.9205 -0.4439 -0.1173 -0.5078 88  GLN B CG  
2402 C CD  . GLN B 88  ? 3.5343 2.335  1.971  -0.4222 -0.0994 -0.4806 88  GLN B CD  
2403 O OE1 . GLN B 88  ? 3.5447 2.3502 2.0034 -0.4154 -0.0779 -0.4577 88  GLN B OE1 
2404 N NE2 . GLN B 88  ? 3.5248 2.3918 1.9477 -0.4187 -0.1086 -0.4817 88  GLN B NE2 
2405 N N   . ILE B 89  ? 3.5201 1.897  1.8729 -0.4782 -0.1542 -0.5488 89  ILE B N   
2406 C CA  . ILE B 89  ? 3.5199 1.8345 1.8786 -0.4985 -0.1842 -0.5038 89  ILE B CA  
2407 C C   . ILE B 89  ? 3.5008 1.833  1.8525 -0.5334 -0.2344 -0.4539 89  ILE B C   
2408 O O   . ILE B 89  ? 3.4867 1.8446 1.8586 -0.542  -0.2622 -0.4652 89  ILE B O   
2409 C CB  . ILE B 89  ? 3.5237 1.7853 1.9242 -0.486  -0.1919 -0.5316 89  ILE B CB  
2410 C CG1 . ILE B 89  ? 3.5376 1.7769 1.9494 -0.4493 -0.1427 -0.5824 89  ILE B CG1 
2411 C CG2 . ILE B 89  ? 3.5242 1.7591 1.9604 -0.4985 -0.2233 -0.4796 89  ILE B CG2 
2412 C CD1 . ILE B 89  ? 3.5421 1.7502 2.0206 -0.4291 -0.1498 -0.6171 89  ILE B CD1 
2413 N N   . ILE B 90  ? 3.4975 1.8174 1.8255 -0.5524 -0.2466 -0.4    90  ILE B N   
2414 C CA  . ILE B 90  ? 3.4753 1.8237 1.815  -0.5806 -0.2936 -0.3496 90  ILE B CA  
2415 C C   . ILE B 90  ? 3.4677 1.7813 1.8292 -0.5944 -0.3229 -0.3018 90  ILE B C   
2416 O O   . ILE B 90  ? 3.4807 1.7739 1.8311 -0.5884 -0.3073 -0.2824 90  ILE B O   
2417 C CB  . ILE B 90  ? 3.471  1.8741 1.7884 -0.5871 -0.2889 -0.3278 90  ILE B CB  
2418 C CG1 . ILE B 90  ? 3.4486 1.9049 1.8173 -0.6044 -0.3351 -0.2729 90  ILE B CG1 
2419 C CG2 . ILE B 90  ? 3.4901 1.881  1.779  -0.5754 -0.249  -0.3237 90  ILE B CG2 
2420 C CD1 . ILE B 90  ? 3.4421 1.966  1.8139 -0.6051 -0.3361 -0.2531 90  ILE B CD1 
2421 N N   . ASP B 91  ? 3.4429 1.7543 1.8373 -0.6131 -0.3659 -0.2827 91  ASP B N   
2422 C CA  . ASP B 91  ? 3.4265 1.7288 1.8585 -0.6267 -0.3983 -0.2338 91  ASP B CA  
2423 C C   . ASP B 91  ? 3.3935 1.7445 1.8436 -0.6499 -0.435  -0.1859 91  ASP B C   
2424 O O   . ASP B 91  ? 3.3706 1.763  1.8515 -0.6597 -0.4582 -0.1855 91  ASP B O   
2425 C CB  . ASP B 91  ? 3.4193 1.7278 1.9224 -0.6234 -0.4162 -0.242  91  ASP B CB  
2426 C CG  . ASP B 91  ? 3.4569 1.7532 2.0021 -0.5885 -0.3813 -0.2801 91  ASP B CG  
2427 O OD1 . ASP B 91  ? 3.4848 1.7589 1.9896 -0.5677 -0.3415 -0.3156 91  ASP B OD1 
2428 O OD2 . ASP B 91  ? 3.4518 1.7583 2.07   -0.5844 -0.3953 -0.2723 91  ASP B OD2 
2429 N N   . VAL B 92  ? 3.3885 1.7335 1.821  -0.6575 -0.4407 -0.1477 92  VAL B N   
2430 C CA  . VAL B 92  ? 3.3544 1.7503 1.8198 -0.6744 -0.4755 -0.1022 92  VAL B CA  
2431 C C   . VAL B 92  ? 3.3287 1.7307 1.8398 -0.684  -0.5038 -0.0533 92  VAL B C   
2432 O O   . VAL B 92  ? 3.3192 1.7256 1.8571 -0.6599 -0.476  -0.0565 92  VAL B O   
2433 C CB  . VAL B 92  ? 3.3678 1.7845 1.7986 -0.6683 -0.4564 -0.1035 92  VAL B CB  
2434 C CG1 . VAL B 92  ? 3.4023 1.7801 1.7919 -0.6528 -0.4196 -0.112  92  VAL B CG1 
2435 C CG2 . VAL B 92  ? 3.333  1.814  1.8221 -0.6773 -0.4917 -0.0565 92  VAL B CG2 
2436 N N   . GLU B 93  ? 3.2814 1.736  1.8567 -0.7001 -0.5444 -0.0133 93  GLU B N   
2437 C CA  . GLU B 93  ? 3.249  1.7344 1.89   -0.706  -0.569  0.0335  93  GLU B CA  
2438 C C   . GLU B 93  ? 3.2163 1.7494 1.8935 -0.7099 -0.5924 0.0687  93  GLU B C   
2439 O O   . GLU B 93  ? 3.1898 1.7677 1.9009 -0.715  -0.6099 0.0751  93  GLU B O   
2440 C CB  . GLU B 93  ? 3.2232 1.7711 1.9672 -0.706  -0.5832 0.0472  93  GLU B CB  
2441 C CG  . GLU B 93  ? 3.2079 1.8482 2.0765 -0.6906 -0.582  0.0872  93  GLU B CG  
2442 C CD  . GLU B 93  ? 3.2018 1.927  2.1925 -0.676  -0.5701 0.0928  93  GLU B CD  
2443 O OE1 . GLU B 93  ? 3.2164 1.9299 2.2052 -0.6737 -0.5627 0.0629  93  GLU B OE1 
2444 O OE2 . GLU B 93  ? 3.1724 1.9626 2.2474 -0.6734 -0.5726 0.1286  93  GLU B OE2 
2445 N N   . ILE B 94  ? 3.1676 1.7633 1.9136 -0.6726 -0.5624 0.0775  94  ILE B N   
2446 C CA  . ILE B 94  ? 3.1399 1.7785 1.9304 -0.671  -0.5847 0.1097  94  ILE B CA  
2447 C C   . ILE B 94  ? 3.0682 1.7948 1.9913 -0.6519 -0.5896 0.1439  94  ILE B C   
2448 O O   . ILE B 94  ? 3.036  1.8066 2.0149 -0.6162 -0.5476 0.1342  94  ILE B O   
2449 C CB  . ILE B 94  ? 3.1562 1.7908 1.9157 -0.6447 -0.5494 0.0909  94  ILE B CB  
2450 C CG1 . ILE B 94  ? 3.2364 1.7914 1.8661 -0.6633 -0.5349 0.0541  94  ILE B CG1 
2451 C CG2 . ILE B 94  ? 3.1348 1.8032 1.9383 -0.6458 -0.58   0.1257  94  ILE B CG2 
2452 C CD1 . ILE B 94  ? 3.2622 1.8146 1.8604 -0.6411 -0.4965 0.0356  94  ILE B CD1 
2453 N N   . ILE B 95  ? 3.0423 1.7958 2.0158 -0.6774 -0.6407 0.1838  95  ILE B N   
2454 C CA  . ILE B 95  ? 2.9757 1.8201 2.0831 -0.6611 -0.6448 0.2174  95  ILE B CA  
2455 C C   . ILE B 95  ? 2.9504 1.8352 2.1213 -0.652  -0.6702 0.2464  95  ILE B C   
2456 O O   . ILE B 95  ? 2.976  1.8255 2.1092 -0.6854 -0.721  0.2662  95  ILE B O   
2457 C CB  . ILE B 95  ? 2.9662 1.8193 2.1045 -0.6987 -0.6851 0.2446  95  ILE B CB  
2458 C CG1 . ILE B 95  ? 3.0102 1.8169 2.0903 -0.7079 -0.6647 0.2171  95  ILE B CG1 
2459 C CG2 . ILE B 95  ? 2.8883 1.846  2.1732 -0.6844 -0.6882 0.2829  95  ILE B CG2 
2460 C CD1 . ILE B 95  ? 2.9964 1.8375 2.1278 -0.7234 -0.6795 0.2251  95  ILE B CD1 
2461 N N   . LEU B 96  ? 2.9012 1.8558 2.1665 -0.6081 -0.6378 0.2489  96  LEU B N   
2462 C CA  . LEU B 96  ? 2.8733 1.8683 2.2157 -0.5926 -0.6607 0.2747  96  LEU B CA  
2463 C C   . LEU B 96  ? 2.8071 1.8976 2.293  -0.5774 -0.6625 0.3036  96  LEU B C   
2464 O O   . LEU B 96  ? 2.7762 1.9171 2.3108 -0.5469 -0.6134 0.2889  96  LEU B O   
2465 C CB  . LEU B 96  ? 2.8797 1.8729 2.2145 -0.55   -0.619  0.2485  96  LEU B CB  
2466 C CG  . LEU B 96  ? 2.9623 1.8798 2.1883 -0.5651 -0.6305 0.236   96  LEU B CG  
2467 C CD1 . LEU B 96  ? 3.0267 1.8853 2.1394 -0.5719 -0.5933 0.1963  96  LEU B CD1 
2468 C CD2 . LEU B 96  ? 2.9541 1.8876 2.2193 -0.5292 -0.6172 0.2336  96  LEU B CD2 
2469 N N   . GLU B 97  ? 2.7829 1.9011 2.3371 -0.6003 -0.7187 0.3457  97  GLU B N   
2470 C CA  . GLU B 97  ? 2.7135 1.932  2.4174 -0.5863 -0.7201 0.3758  97  GLU B CA  
2471 C C   . GLU B 97  ? 2.6686 1.9501 2.479  -0.533  -0.6951 0.374   97  GLU B C   
2472 O O   . GLU B 97  ? 2.6962 1.936  2.465  -0.5144 -0.6925 0.358   97  GLU B O   
2473 C CB  . GLU B 97  ? 2.7046 1.9712 2.4691 -0.6021 -0.7461 0.3981  97  GLU B CB  
2474 C CG  . GLU B 97  ? 2.7838 2.0435 2.4825 -0.6085 -0.7097 0.3628  97  GLU B CG  
2475 C CD  . GLU B 97  ? 2.8044 2.1421 2.5632 -0.5841 -0.6795 0.3445  97  GLU B CD  
2476 O OE1 . GLU B 97  ? 2.7641 2.1693 2.6151 -0.5606 -0.6794 0.3577  97  GLU B OE1 
2477 O OE2 . GLU B 97  ? 2.8504 2.1729 2.559  -0.5913 -0.6625 0.3177  97  GLU B OE2 
2478 N N   . GLU B 98  ? 2.5979 1.9791 2.5449 -0.5086 -0.6746 0.389   98  GLU B N   
2479 C CA  . GLU B 98  ? 2.5517 1.9997 2.6118 -0.4543 -0.6454 0.3828  98  GLU B CA  
2480 C C   . GLU B 98  ? 2.564  1.9806 2.6441 -0.444  -0.6891 0.3951  98  GLU B C   
2481 O O   . GLU B 98  ? 2.5664 1.9652 2.6593 -0.4792 -0.756  0.4332  98  GLU B O   
2482 C CB  . GLU B 98  ? 2.4931 2.0572 2.7086 -0.4422 -0.6337 0.4086  98  GLU B CB  
2483 C CG  . GLU B 98  ? 2.4914 2.1288 2.8296 -0.3823 -0.5969 0.3963  98  GLU B CG  
2484 C CD  . GLU B 98  ? 2.4796 2.2394 2.9624 -0.3647 -0.5642 0.411   98  GLU B CD  
2485 O OE1 . GLU B 98  ? 2.4262 2.2528 3.0446 -0.3278 -0.5637 0.4194  98  GLU B OE1 
2486 O OE2 . GLU B 98  ? 2.502  2.2918 2.9652 -0.3877 -0.5383 0.4143  98  GLU B OE2 
2487 N N   . ASP B 99  ? 2.5767 1.9777 2.648  -0.4003 -0.6551 0.3638  99  ASP B N   
2488 C CA  . ASP B 99  ? 2.5899 1.9583 2.6813 -0.3846 -0.6905 0.3718  99  ASP B CA  
2489 C C   . ASP B 99  ? 2.6688 1.9383 2.6322 -0.4303 -0.7428 0.3842  99  ASP B C   
2490 O O   . ASP B 99  ? 2.6691 1.9195 2.6558 -0.4277 -0.7822 0.4026  99  ASP B O   
2491 C CB  . ASP B 99  ? 2.5325 1.9741 2.7921 -0.3669 -0.7273 0.4084  99  ASP B CB  
2492 C CG  . ASP B 99  ? 2.5097 2.0563 2.9047 -0.3189 -0.672  0.3949  99  ASP B CG  
2493 O OD1 . ASP B 99  ? 2.5186 2.0707 2.9062 -0.2743 -0.6133 0.3527  99  ASP B OD1 
2494 O OD2 . ASP B 99  ? 2.4764 2.1128 2.9663 -0.3162 -0.6616 0.4111  99  ASP B OD2 
2495 N N   . SER B 100 ? 2.7309 1.9431 2.5603 -0.4676 -0.7346 0.3698  100 SER B N   
2496 C CA  . SER B 100 ? 2.8066 1.9335 2.5073 -0.507  -0.768  0.3725  100 SER B CA  
2497 C C   . SER B 100 ? 2.8633 1.9263 2.465  -0.4927 -0.7377 0.339   100 SER B C   
2498 O O   . SER B 100 ? 2.8482 1.9377 2.4762 -0.4493 -0.6813 0.3072  100 SER B O   
2499 C CB  . SER B 100 ? 2.8463 1.9721 2.4743 -0.5361 -0.7487 0.3585  100 SER B CB  
2500 O OG  . SER B 100 ? 2.9042 1.9994 2.4713 -0.544  -0.7217 0.3373  100 SER B OG  
2501 N N   . SER B 101 ? 2.9152 1.9152 2.4146 -0.5205 -0.7582 0.3402  101 SER B N   
2502 C CA  . SER B 101 ? 2.9693 1.9068 2.3753 -0.5149 -0.7375 0.316   101 SER B CA  
2503 C C   . SER B 101 ? 3.0226 1.9202 2.3072 -0.5467 -0.7282 0.3033  101 SER B C   
2504 O O   . SER B 101 ? 3.0012 1.9435 2.3126 -0.55   -0.7321 0.3133  101 SER B O   
2505 C CB  . SER B 101 ? 2.956  1.9047 2.4375 -0.4837 -0.7537 0.329   101 SER B CB  
2506 O OG  . SER B 101 ? 3.0164 1.936  2.4275 -0.4796 -0.7298 0.3127  101 SER B OG  
2507 N N   . ILE B 102 ? 3.0837 1.9086 2.2431 -0.5624 -0.7052 0.2756  102 ILE B N   
2508 C CA  . ILE B 102 ? 3.1245 1.9308 2.1852 -0.5818 -0.6802 0.2547  102 ILE B CA  
2509 C C   . ILE B 102 ? 3.1811 1.9174 2.1344 -0.5851 -0.6516 0.2283  102 ILE B C   
2510 O O   . ILE B 102 ? 3.1663 1.9206 2.1515 -0.5502 -0.609  0.2034  102 ILE B O   
2511 C CB  . ILE B 102 ? 3.1342 1.9593 2.1715 -0.598  -0.6666 0.239   102 ILE B CB  
2512 C CG1 . ILE B 102 ? 3.1644 2.0009 2.1403 -0.6068 -0.6431 0.2182  102 ILE B CG1 
2513 C CG2 . ILE B 102 ? 3.1696 1.9541 2.1595 -0.6023 -0.6456 0.2159  102 ILE B CG2 
2514 C CD1 . ILE B 102 ? 3.138  2.0396 2.1798 -0.5949 -0.6534 0.2375  102 ILE B CD1 
2515 N N   . SER B 103 ? 3.1977 1.9269 2.0904 -0.5958 -0.6368 0.2207  103 SER B N   
2516 C CA  . SER B 103 ? 3.247  1.925  2.0465 -0.5989 -0.6024 0.1955  103 SER B CA  
2517 C C   . SER B 103 ? 3.2722 1.9537 1.9943 -0.6161 -0.5699 0.1687  103 SER B C   
2518 O O   . SER B 103 ? 3.2527 1.9796 1.9906 -0.6221 -0.5772 0.1774  103 SER B O   
2519 C CB  . SER B 103 ? 3.2446 1.9391 2.0788 -0.5836 -0.6054 0.2113  103 SER B CB  
2520 O OG  . SER B 103 ? 3.238  1.9431 2.1615 -0.5514 -0.619  0.222   103 SER B OG  
2521 N N   . LEU B 104 ? 3.3129 1.9469 1.9551 -0.6209 -0.5339 0.134   104 LEU B N   
2522 C CA  . LEU B 104 ? 3.3372 1.9749 1.915  -0.6299 -0.4982 0.1003  104 LEU B CA  
2523 C C   . LEU B 104 ? 3.3698 1.9862 1.8819 -0.6283 -0.4559 0.0786  104 LEU B C   
2524 O O   . LEU B 104 ? 3.3947 1.9682 1.8837 -0.6197 -0.4365 0.0684  104 LEU B O   
2525 C CB  . LEU B 104 ? 3.3536 1.9641 1.9127 -0.6303 -0.4856 0.0746  104 LEU B CB  
2526 C CG  . LEU B 104 ? 3.3626 2.0055 1.9113 -0.6314 -0.4676 0.0456  104 LEU B CG  
2527 C CD1 . LEU B 104 ? 3.3534 2.001  1.9439 -0.6307 -0.4822 0.0436  104 LEU B CD1 
2528 C CD2 . LEU B 104 ? 3.402  2.0214 1.8784 -0.6263 -0.4163 0.0017  104 LEU B CD2 
2529 N N   . MET B 105 ? 3.3667 2.0144 1.8486 -0.6362 -0.4406 0.0717  105 MET B N   
2530 C CA  . MET B 105 ? 3.3891 2.0322 1.8187 -0.6357 -0.3985 0.0537  105 MET B CA  
2531 C C   . MET B 105 ? 3.4069 2.06   1.7846 -0.6352 -0.3576 0.0103  105 MET B C   
2532 O O   . MET B 105 ? 3.3956 2.0952 1.7682 -0.6379 -0.3574 0.007   105 MET B O   
2533 C CB  . MET B 105 ? 3.3694 2.063  1.8301 -0.6363 -0.4112 0.0842  105 MET B CB  
2534 C CG  . MET B 105 ? 3.3914 2.0968 1.8579 -0.6244 -0.3805 0.0846  105 MET B CG  
2535 S SD  . MET B 105 ? 3.3853 2.1985 1.922  -0.6063 -0.3749 0.1102  105 MET B SD  
2536 C CE  . MET B 105 ? 3.3415 2.1556 1.9484 -0.6092 -0.4397 0.156   105 MET B CE  
2537 N N   . SER B 106 ? 3.433  2.0421 1.7756 -0.6283 -0.3239 -0.0243 106 SER B N   
2538 C CA  . SER B 106 ? 3.449  2.0647 1.7555 -0.6209 -0.2835 -0.0709 106 SER B CA  
2539 C C   . SER B 106 ? 3.4596 2.1009 1.7377 -0.6141 -0.2359 -0.0887 106 SER B C   
2540 O O   . SER B 106 ? 3.4678 2.0916 1.7441 -0.6124 -0.2193 -0.0792 106 SER B O   
2541 C CB  . SER B 106 ? 3.4714 2.0432 1.7811 -0.6075 -0.2672 -0.0987 106 SER B CB  
2542 O OG  . SER B 106 ? 3.4893 2.0755 1.7886 -0.5899 -0.2249 -0.1475 106 SER B OG  
2543 N N   . HIS B 107 ? 3.456  2.1417 1.7139 -0.6098 -0.2156 -0.1137 107 HIS B N   
2544 C CA  . HIS B 107 ? 3.4598 2.1838 1.6971 -0.6009 -0.1694 -0.1306 107 HIS B CA  
2545 C C   . HIS B 107 ? 3.4707 2.2011 1.6863 -0.5822 -0.1274 -0.1868 107 HIS B C   
2546 O O   . HIS B 107 ? 3.4678 2.2173 1.6825 -0.5766 -0.1408 -0.2073 107 HIS B O   
2547 C CB  . HIS B 107 ? 3.4427 2.2397 1.6934 -0.6025 -0.1842 -0.1038 107 HIS B CB  
2548 C CG  . HIS B 107 ? 3.4448 2.282  1.7426 -0.5965 -0.1824 -0.0661 107 HIS B CG  
2549 N ND1 . HIS B 107 ? 3.4327 2.33   1.7813 -0.592  -0.2125 -0.0256 107 HIS B ND1 
2550 C CD2 . HIS B 107 ? 3.4581 2.2875 1.7706 -0.5903 -0.1541 -0.0645 107 HIS B CD2 
2551 C CE1 . HIS B 107 ? 3.4321 2.3346 1.8002 -0.5938 -0.205  0.0002  107 HIS B CE1 
2552 N NE2 . HIS B 107 ? 3.4481 2.3149 1.799  -0.5922 -0.1708 -0.0218 107 HIS B NE2 
2553 N N   . CYS B 108 ? 3.4791 2.1933 1.6808 -0.5716 -0.0777 -0.2127 108 CYS B N   
2554 C CA  . CYS B 108 ? 3.4837 2.2044 1.6747 -0.5492 -0.0362 -0.2684 108 CYS B CA  
2555 C C   . CYS B 108 ? 3.4691 2.2459 1.6445 -0.5393 0.0094  -0.2819 108 CYS B C   
2556 O O   . CYS B 108 ? 3.4651 2.2459 1.6484 -0.5426 0.0353  -0.2655 108 CYS B O   
2557 C CB  . CYS B 108 ? 3.5039 2.1698 1.718  -0.5335 -0.0152 -0.2932 108 CYS B CB  
2558 S SG  . CYS B 108 ? 3.5271 2.1744 1.8044 -0.5236 -0.0652 -0.2853 108 CYS B SG  
2559 N N   . SER B 109 ? 3.4586 2.2802 1.6124 -0.5267 0.0185  -0.3111 109 SER B N   
2560 C CA  . SER B 109 ? 3.4436 2.3317 1.5881 -0.5097 0.0618  -0.3248 109 SER B CA  
2561 C C   . SER B 109 ? 3.4449 2.3424 1.5908 -0.476  0.0988  -0.3893 109 SER B C   
2562 O O   . SER B 109 ? 3.4465 2.3587 1.5774 -0.4637 0.082   -0.4188 109 SER B O   
2563 C CB  . SER B 109 ? 3.4341 2.396  1.5709 -0.5097 0.0373  -0.2966 109 SER B CB  
2564 O OG  . SER B 109 ? 3.4257 2.4647 1.5813 -0.4925 0.0705  -0.2814 109 SER B OG  
2565 N N   . PHE B 110 ? 3.4406 2.3262 1.6093 -0.4603 0.1471  -0.4125 110 PHE B N   
2566 C CA  . PHE B 110 ? 3.4368 2.3307 1.6216 -0.4229 0.1842  -0.4745 110 PHE B CA  
2567 C C   . PHE B 110 ? 3.4123 2.3732 1.6074 -0.4025 0.2393  -0.4822 110 PHE B C   
2568 O O   . PHE B 110 ? 3.4032 2.353  1.6386 -0.3936 0.2776  -0.4881 110 PHE B O   
2569 C CB  . PHE B 110 ? 3.4499 2.2666 1.6707 -0.4158 0.1917  -0.4967 110 PHE B CB  
2570 C CG  . PHE B 110 ? 3.4746 2.2319 1.7023 -0.4342 0.1388  -0.476  110 PHE B CG  
2571 C CD1 . PHE B 110 ? 3.4818 2.252  1.7    -0.4388 0.0923  -0.4771 110 PHE B CD1 
2572 C CD2 . PHE B 110 ? 3.4899 2.1937 1.7509 -0.439  0.1345  -0.4558 110 PHE B CD2 
2573 C CE1 . PHE B 110 ? 3.4982 2.2249 1.7336 -0.4547 0.0451  -0.4543 110 PHE B CE1 
2574 C CE2 . PHE B 110 ? 3.5097 2.1681 1.7799 -0.4522 0.0863  -0.4343 110 PHE B CE2 
2575 C CZ  . PHE B 110 ? 3.5097 2.1756 1.763  -0.463  0.0436  -0.4333 110 PHE B CZ  
2576 N N   . PRO B 111 ? 3.3983 2.4308 1.559  -0.3945 0.2442  -0.4787 111 PRO B N   
2577 C CA  . PRO B 111 ? 3.3709 2.4731 1.5407 -0.3761 0.2965  -0.4778 111 PRO B CA  
2578 C C   . PRO B 111 ? 3.3543 2.4834 1.5404 -0.3292 0.3422  -0.5405 111 PRO B C   
2579 O O   . PRO B 111 ? 3.3294 2.5035 1.5536 -0.311  0.3897  -0.5405 111 PRO B O   
2580 C CB  . PRO B 111 ? 3.3689 2.5421 1.5034 -0.3804 0.2757  -0.4395 111 PRO B CB  
2581 C CG  . PRO B 111 ? 3.3905 2.5465 1.4973 -0.3799 0.2247  -0.454  111 PRO B CG  
2582 C CD  . PRO B 111 ? 3.4032 2.4557 1.5139 -0.4036 0.2028  -0.47   111 PRO B CD  
2583 N N   . LYS B 112 ? 3.3637 2.4663 1.5233 -0.3096 0.3273  -0.5934 112 LYS B N   
2584 C CA  . LYS B 112 ? 3.3483 2.4704 1.5239 -0.2604 0.3645  -0.6581 112 LYS B CA  
2585 C C   . LYS B 112 ? 3.3428 2.4061 1.5846 -0.2492 0.3909  -0.6841 112 LYS B C   
2586 O O   . LYS B 112 ? 3.3168 2.4199 1.6066 -0.2122 0.437   -0.7079 112 LYS B O   
2587 C CB  . LYS B 112 ? 3.3698 2.4991 1.5211 -0.2327 0.3268  -0.7043 112 LYS B CB  
2588 C CG  . LYS B 112 ? 3.3727 2.6226 1.5184 -0.1774 0.331   -0.7183 112 LYS B CG  
2589 C CD  . LYS B 112 ? 3.3894 2.7299 1.5315 -0.182  0.3068  -0.6503 112 LYS B CD  
2590 C CE  . LYS B 112 ? 3.3777 2.8573 1.5389 -0.1059 0.2877  -0.6574 112 LYS B CE  
2591 N NZ  . LYS B 112 ? 3.3927 2.8884 1.5673 -0.0727 0.2338  -0.7011 112 LYS B NZ  
2592 N N   . GLY B 113 ? 3.3647 2.3328 1.6069 -0.2811 0.3617  -0.6751 113 GLY B N   
2593 C CA  . GLY B 113 ? 3.3649 2.2595 1.6619 -0.2784 0.3787  -0.6872 113 GLY B CA  
2594 C C   . GLY B 113 ? 3.3496 2.2129 1.6892 -0.2351 0.407   -0.7521 113 GLY B C   
2595 O O   . GLY B 113 ? 3.3397 2.173  1.7468 -0.2232 0.4326  -0.7538 113 GLY B O   
2596 N N   . LYS B 114 ? 3.3449 2.2091 1.6477 -0.2105 0.402   -0.8065 114 LYS B N   
2597 C CA  . LYS B 114 ? 3.3302 2.1611 1.6791 -0.1645 0.4231  -0.871  114 LYS B CA  
2598 C C   . LYS B 114 ? 3.3562 2.0856 1.6893 -0.1749 0.3813  -0.9006 114 LYS B C   
2599 O O   . LYS B 114 ? 3.3731 2.1071 1.6574 -0.1784 0.3438  -0.9208 114 LYS B O   
2600 C CB  . LYS B 114 ? 3.314  2.2454 1.6713 -0.1053 0.4406  -0.9136 114 LYS B CB  
2601 C CG  . LYS B 114 ? 3.3051 2.2779 1.7871 -0.0189 0.4233  -0.9649 114 LYS B CG  
2602 C CD  . LYS B 114 ? 3.3217 2.3561 1.8424 0.0428  0.3473  -1.0119 114 LYS B CD  
2603 C CE  . LYS B 114 ? 3.3192 2.3743 1.9654 0.1234  0.3078  -1.0582 114 LYS B CE  
2604 N NZ  . LYS B 114 ? 3.3543 2.3267 2.0694 0.1003  0.2729  -1.0509 114 LYS B NZ  
2605 N N   . GLY B 115 ? 3.3574 1.9955 1.7328 -0.1804 0.3876  -0.9002 115 GLY B N   
2606 C CA  . GLY B 115 ? 3.3824 1.9227 1.7564 -0.1884 0.3467  -0.9203 115 GLY B CA  
2607 C C   . GLY B 115 ? 3.4112 1.8944 1.7209 -0.246  0.2985  -0.8709 115 GLY B C   
2608 O O   . GLY B 115 ? 3.4324 1.8519 1.7392 -0.2547 0.2559  -0.8818 115 GLY B O   
2609 N N   . ILE B 116 ? 3.4097 1.9159 1.6718 -0.2848 0.3016  -0.8143 116 ILE B N   
2610 C CA  . ILE B 116 ? 3.4342 1.904  1.6461 -0.3337 0.2511  -0.76   116 ILE B CA  
2611 C C   . ILE B 116 ? 3.4497 1.8078 1.6639 -0.3532 0.2366  -0.7333 116 ILE B C   
2612 O O   . ILE B 116 ? 3.4437 1.7754 1.7068 -0.3343 0.2716  -0.7349 116 ILE B O   
2613 C CB  . ILE B 116 ? 3.4317 1.9786 1.6239 -0.3563 0.2535  -0.7062 116 ILE B CB  
2614 C CG1 . ILE B 116 ? 3.421  2.0746 1.5958 -0.3401 0.2549  -0.7221 116 ILE B CG1 
2615 C CG2 . ILE B 116 ? 3.4562 1.9743 1.6255 -0.398  0.201   -0.6438 116 ILE B CG2 
2616 C CD1 . ILE B 116 ? 3.4198 2.1529 1.58   -0.3608 0.2503  -0.6642 116 ILE B CD1 
2617 N N   . LYS B 117 ? 3.4659 1.7613 1.6266 -0.3901 0.1828  -0.7052 117 LYS B N   
2618 C CA  . LYS B 117 ? 3.4835 1.6843 1.6381 -0.408  0.156   -0.6706 117 LYS B CA  
2619 C C   . LYS B 117 ? 3.4898 1.6697 1.5815 -0.4545 0.0982  -0.6202 117 LYS B C   
2620 O O   . LYS B 117 ? 3.4916 1.675  1.5793 -0.4629 0.0557  -0.6297 117 LYS B O   
2621 C CB  . LYS B 117 ? 3.4966 1.6601 1.7171 -0.3778 0.1378  -0.7072 117 LYS B CB  
2622 C CG  . LYS B 117 ? 3.5206 1.6672 1.832  -0.3561 0.1282  -0.6806 117 LYS B CG  
2623 C CD  . LYS B 117 ? 3.5318 1.6881 1.9612 -0.3119 0.1116  -0.7207 117 LYS B CD  
2624 C CE  . LYS B 117 ? 3.5451 1.6957 2.0709 -0.2816 0.1205  -0.7047 117 LYS B CE  
2625 N NZ  . LYS B 117 ? 3.5457 1.6802 2.164  -0.2419 0.1161  -0.7504 117 LYS B NZ  
2626 N N   . HIS B 118 ? 3.489  1.6518 1.5385 -0.4838 0.0945  -0.5677 118 HIS B N   
2627 C CA  . HIS B 118 ? 3.4909 1.6449 1.5024 -0.5224 0.0352  -0.5161 118 HIS B CA  
2628 C C   . HIS B 118 ? 3.4218 1.5939 1.5408 -0.5011 -0.0018 -0.4817 118 HIS B C   
2629 O O   . HIS B 118 ? 3.3752 1.6071 1.5858 -0.4731 0.012   -0.459  118 HIS B O   
2630 C CB  . HIS B 118 ? 3.4866 1.7119 1.4949 -0.5368 0.0386  -0.4767 118 HIS B CB  
2631 C CG  . HIS B 118 ? 3.4977 1.7636 1.5444 -0.5529 -0.0228 -0.4175 118 HIS B CG  
2632 N ND1 . HIS B 118 ? 3.4923 1.8244 1.5647 -0.5619 -0.0692 -0.402  118 HIS B ND1 
2633 C CD2 . HIS B 118 ? 3.4907 1.7711 1.5918 -0.5481 -0.0424 -0.3735 118 HIS B CD2 
2634 C CE1 . HIS B 118 ? 3.493  1.8268 1.5837 -0.5791 -0.1112 -0.3496 118 HIS B CE1 
2635 N NE2 . HIS B 118 ? 3.5051 1.7958 1.5975 -0.5752 -0.0973 -0.3324 118 HIS B NE2 
2636 N N   . ILE B 119 ? 3.4097 1.5357 1.5212 -0.5149 -0.0488 -0.4773 119 ILE B N   
2637 C CA  . ILE B 119 ? 3.3435 1.4938 1.5563 -0.4983 -0.0835 -0.4428 119 ILE B CA  
2638 C C   . ILE B 119 ? 3.3189 1.4798 1.5202 -0.5318 -0.1408 -0.3945 119 ILE B C   
2639 O O   . ILE B 119 ? 3.3646 1.4726 1.4873 -0.5668 -0.1722 -0.4008 119 ILE B O   
2640 C CB  . ILE B 119 ? 3.3537 1.448  1.5937 -0.4812 -0.0883 -0.4756 119 ILE B CB  
2641 C CG1 . ILE B 119 ? 3.3475 1.4444 1.6289 -0.4401 -0.0316 -0.5183 119 ILE B CG1 
2642 C CG2 . ILE B 119 ? 3.3244 1.4386 1.6515 -0.4764 -0.1322 -0.434  119 ILE B CG2 
2643 C CD1 . ILE B 119 ? 3.3722 1.4098 1.6842 -0.4197 -0.034  -0.5542 119 ILE B CD1 
2644 N N   . MET B 120 ? 3.2447 1.4728 1.5234 -0.5219 -0.1548 -0.3477 120 MET B N   
2645 C CA  . MET B 120 ? 3.2157 1.4629 1.5024 -0.5486 -0.2067 -0.3013 120 MET B CA  
2646 C C   . MET B 120 ? 3.1383 1.4212 1.5257 -0.5304 -0.2264 -0.2726 120 MET B C   
2647 O O   . MET B 120 ? 3.1012 1.43   1.5597 -0.4986 -0.202  -0.2655 120 MET B O   
2648 C CB  . MET B 120 ? 3.2169 1.512  1.4966 -0.5576 -0.2078 -0.27   120 MET B CB  
2649 C CG  . MET B 120 ? 3.2424 1.562  1.5451 -0.5807 -0.2611 -0.2219 120 MET B CG  
2650 S SD  . MET B 120 ? 3.3254 1.7002 1.6407 -0.5825 -0.2626 -0.1855 120 MET B SD  
2651 C CE  . MET B 120 ? 3.2592 1.6975 1.6866 -0.5314 -0.227  -0.1804 120 MET B CE  
2652 N N   . ASN B 121 ? 3.1138 1.376  1.5051 -0.5533 -0.271  -0.2552 121 ASN B N   
2653 C CA  . ASN B 121 ? 3.0492 1.3485 1.5308 -0.5431 -0.291  -0.2239 121 ASN B CA  
2654 C C   . ASN B 121 ? 3.0032 1.3407 1.5021 -0.5685 -0.3323 -0.1783 121 ASN B C   
2655 O O   . ASN B 121 ? 3.0342 1.3339 1.4808 -0.6041 -0.3693 -0.1735 121 ASN B O   
2656 C CB  . ASN B 121 ? 3.0825 1.3241 1.5618 -0.5504 -0.3093 -0.2412 121 ASN B CB  
2657 C CG  . ASN B 121 ? 3.1454 1.3355 1.5998 -0.5276 -0.2727 -0.2926 121 ASN B CG  
2658 O OD1 . ASN B 121 ? 3.1315 1.3517 1.629  -0.4936 -0.2339 -0.3029 121 ASN B OD1 
2659 N ND2 . ASN B 121 ? 3.206  1.3164 1.5924 -0.5457 -0.2851 -0.3269 121 ASN B ND2 
2660 N N   . GLY B 122 ? 2.9295 1.3394 1.5    -0.5503 -0.3264 -0.1468 122 GLY B N   
2661 C CA  . GLY B 122 ? 2.886  1.3404 1.4883 -0.5679 -0.3614 -0.1044 122 GLY B CA  
2662 C C   . GLY B 122 ? 2.8089 1.3282 1.5088 -0.5559 -0.3698 -0.0702 122 GLY B C   
2663 O O   . GLY B 122 ? 2.7821 1.3304 1.5302 -0.5269 -0.3409 -0.074  122 GLY B O   
2664 N N   . ILE B 123 ? 2.7725 1.3168 1.5016 -0.5803 -0.4099 -0.0354 123 ILE B N   
2665 C CA  . ILE B 123 ? 2.7075 1.3236 1.5316 -0.5729 -0.4173 0.0002  123 ILE B CA  
2666 C C   . ILE B 123 ? 2.6655 1.3304 1.5243 -0.5759 -0.4361 0.0296  123 ILE B C   
2667 O O   . ILE B 123 ? 2.6849 1.3293 1.5166 -0.6076 -0.4762 0.0447  123 ILE B O   
2668 C CB  . ILE B 123 ? 2.7136 1.3188 1.5567 -0.6025 -0.4518 0.0186  123 ILE B CB  
2669 C CG1 . ILE B 123 ? 2.7567 1.3036 1.5683 -0.6009 -0.4404 -0.0097 123 ILE B CG1 
2670 C CG2 . ILE B 123 ? 2.6582 1.35   1.602  -0.5993 -0.4578 0.0599  123 ILE B CG2 
2671 C CD1 . ILE B 123 ? 2.7422 1.325  1.6091 -0.5718 -0.4077 -0.0092 123 ILE B CD1 
2672 N N   . ILE B 124 ? 2.6099 1.3331 1.5257 -0.5436 -0.4102 0.0369  124 ILE B N   
2673 C CA  . ILE B 124 ? 2.5693 1.3378 1.5295 -0.5399 -0.4267 0.0626  124 ILE B CA  
2674 C C   . ILE B 124 ? 2.4955 1.345  1.5605 -0.5261 -0.4251 0.0907  124 ILE B C   
2675 O O   . ILE B 124 ? 2.4736 1.3542 1.5721 -0.5019 -0.391  0.0829  124 ILE B O   
2676 C CB  . ILE B 124 ? 2.585  1.3474 1.5207 -0.5148 -0.4005 0.0453  124 ILE B CB  
2677 C CG1 . ILE B 124 ? 2.6559 1.3445 1.4861 -0.5345 -0.4013 0.0202  124 ILE B CG1 
2678 C CG2 . ILE B 124 ? 2.5579 1.3656 1.5505 -0.506  -0.4186 0.0719  124 ILE B CG2 
2679 C CD1 . ILE B 124 ? 2.6836 1.3643 1.486  -0.5138 -0.3709 0.002   124 ILE B CD1 
2680 N N   . LYS B 125 ? 2.4567 1.3406 1.5727 -0.5445 -0.4626 0.1243  125 LYS B N   
2681 C CA  . LYS B 125 ? 2.3904 1.3595 1.614  -0.5331 -0.4599 0.1523  125 LYS B CA  
2682 C C   . LYS B 125 ? 2.3499 1.3607 1.6338 -0.5203 -0.4768 0.1723  125 LYS B C   
2683 O O   . LYS B 125 ? 2.3569 1.3546 1.6402 -0.5477 -0.5236 0.1953  125 LYS B O   
2684 C CB  . LYS B 125 ? 2.4057 1.3852 1.6551 -0.5701 -0.4936 0.1793  125 LYS B CB  
2685 C CG  . LYS B 125 ? 2.5011 1.4251 1.6882 -0.5876 -0.4878 0.1612  125 LYS B CG  
2686 C CD  . LYS B 125 ? 2.5408 1.4749 1.7591 -0.6267 -0.5252 0.1917  125 LYS B CD  
2687 C CE  . LYS B 125 ? 2.6267 1.4949 1.7838 -0.6448 -0.5263 0.1737  125 LYS B CE  
2688 N NZ  . LYS B 125 ? 2.6178 1.5344 1.84   -0.6592 -0.5285 0.2022  125 LYS B NZ  
2689 N N   . ILE B 126 ? 2.3088 1.3636 1.6419 -0.4794 -0.442  0.163   126 ILE B N   
2690 C CA  . ILE B 126 ? 2.2707 1.3622 1.669  -0.4585 -0.4536 0.1769  126 ILE B CA  
2691 C C   . ILE B 126 ? 2.1985 1.383  1.7188 -0.4435 -0.4471 0.2     126 ILE B C   
2692 O O   . ILE B 126 ? 2.1741 1.4023 1.7257 -0.4208 -0.404  0.1881  126 ILE B O   
2693 C CB  . ILE B 126 ? 2.2881 1.3592 1.657  -0.4231 -0.42   0.1477  126 ILE B CB  
2694 C CG1 . ILE B 126 ? 2.3629 1.3509 1.6163 -0.4407 -0.4218 0.1262  126 ILE B CG1 
2695 C CG2 . ILE B 126 ? 2.2604 1.36   1.6966 -0.3996 -0.4344 0.1599  126 ILE B CG2 
2696 C CD1 . ILE B 126 ? 2.3947 1.3649 1.6149 -0.4121 -0.3818 0.0963  126 ILE B CD1 
2697 N N   . GLY B 127 ? 2.163  1.3783 1.7505 -0.4587 -0.4903 0.234   127 GLY B N   
2698 C CA  . GLY B 127 ? 2.0906 1.4013 1.8065 -0.4472 -0.4874 0.2598  127 GLY B CA  
2699 C C   . GLY B 127 ? 2.0413 1.4089 1.843  -0.3969 -0.4568 0.2497  127 GLY B C   
2700 O O   . GLY B 127 ? 2.0683 1.3977 1.8286 -0.3705 -0.4402 0.2232  127 GLY B O   
2701 N N   . LYS B 128 ? 1.9661 1.4267 1.8905 -0.3834 -0.4481 0.2698  128 LYS B N   
2702 C CA  . LYS B 128 ? 1.9175 1.4406 1.9372 -0.333  -0.4156 0.2576  128 LYS B CA  
2703 C C   . LYS B 128 ? 1.9273 1.4153 1.9659 -0.3153 -0.451  0.2597  128 LYS B C   
2704 O O   . LYS B 128 ? 1.9151 1.4014 1.9948 -0.3373 -0.5071 0.2941  128 LYS B O   
2705 C CB  . LYS B 128 ? 1.854  1.4877 2.0097 -0.3281 -0.4052 0.2839  128 LYS B CB  
2706 C CG  . LYS B 128 ? 1.8359 1.54   2.1041 -0.2737 -0.3714 0.2697  128 LYS B CG  
2707 C CD  . LYS B 128 ? 1.7981 1.6189 2.2054 -0.271  -0.3578 0.2966  128 LYS B CD  
2708 C CE  . LYS B 128 ? 1.7752 1.6623 2.3116 -0.217  -0.3372 0.2859  128 LYS B CE  
2709 N NZ  . LYS B 128 ? 1.8092 1.6454 2.3708 -0.2065 -0.3939 0.2957  128 LYS B NZ  
2710 N N   . ASN B 129 ? 1.9515 1.4057 1.9542 -0.2797 -0.4228 0.2253  129 ASN B N   
2711 C CA  . ASN B 129 ? 1.9672 1.3811 1.9806 -0.2606 -0.4524 0.2241  129 ASN B CA  
2712 C C   . ASN B 129 ? 2.0234 1.3528 1.9434 -0.3028 -0.5076 0.2424  129 ASN B C   
2713 O O   . ASN B 129 ? 2.0218 1.328  1.9687 -0.3027 -0.5523 0.2611  129 ASN B O   
2714 C CB  . ASN B 129 ? 1.913  1.3956 2.0777 -0.2306 -0.4688 0.2429  129 ASN B CB  
2715 C CG  . ASN B 129 ? 1.9053 1.4652 2.1532 -0.1825 -0.4065 0.2155  129 ASN B CG  
2716 O OD1 . ASN B 129 ? 1.9471 1.4856 2.1455 -0.1536 -0.3614 0.1755  129 ASN B OD1 
2717 N ND2 . ASN B 129 ? 1.8395 1.4926 2.2145 -0.1744 -0.4022 0.2364  129 ASN B ND2 
2718 N N   . ALA B 130 ? 2.0724 1.3534 1.88   -0.3384 -0.5033 0.2352  130 ALA B N   
2719 C CA  . ALA B 130 ? 2.1376 1.3365 1.8392 -0.379  -0.545  0.2445  130 ALA B CA  
2720 C C   . ALA B 130 ? 2.193  1.328  1.797  -0.367  -0.5184 0.2114  130 ALA B C   
2721 O O   . ALA B 130 ? 2.1897 1.3394 1.7945 -0.3344 -0.4684 0.1811  130 ALA B O   
2722 C CB  . ALA B 130 ? 2.1665 1.3461 1.8058 -0.4241 -0.5573 0.2533  130 ALA B CB  
2723 N N   . LYS B 131 ? 2.2431 1.3095 1.7632 -0.3952 -0.5521 0.2188  131 LYS B N   
2724 C CA  . LYS B 131 ? 2.2968 1.3083 1.7316 -0.3871 -0.5287 0.1921  131 LYS B CA  
2725 C C   . LYS B 131 ? 2.3694 1.3118 1.6757 -0.4305 -0.5401 0.1882  131 LYS B C   
2726 O O   . LYS B 131 ? 2.3916 1.3016 1.663  -0.466  -0.5881 0.2138  131 LYS B O   
2727 C CB  . LYS B 131 ? 2.3078 1.3101 1.7849 -0.3666 -0.5516 0.2024  131 LYS B CB  
2728 C CG  . LYS B 131 ? 2.4085 1.3533 1.8009 -0.3653 -0.5368 0.1833  131 LYS B CG  
2729 C CD  . LYS B 131 ? 2.4767 1.3895 1.8773 -0.3749 -0.5867 0.211   131 LYS B CD  
2730 C CE  . LYS B 131 ? 2.5872 1.4332 1.8663 -0.411  -0.5951 0.2119  131 LYS B CE  
2731 N NZ  . LYS B 131 ? 2.6281 1.4419 1.8943 -0.4449 -0.659  0.2528  131 LYS B NZ  
2732 N N   . PHE B 132 ? 2.4056 1.3239 1.6409 -0.4271 -0.4959 0.1554  132 PHE B N   
2733 C CA  . PHE B 132 ? 2.4767 1.3318 1.593  -0.4618 -0.4959 0.1434  132 PHE B CA  
2734 C C   . PHE B 132 ? 2.5178 1.3417 1.5798 -0.4474 -0.4635 0.1191  132 PHE B C   
2735 O O   . PHE B 132 ? 2.4988 1.345  1.594  -0.4122 -0.4255 0.0986  132 PHE B O   
2736 C CB  . PHE B 132 ? 2.4862 1.3358 1.5679 -0.4757 -0.477  0.1272  132 PHE B CB  
2737 C CG  . PHE B 132 ? 2.5513 1.3339 1.5139 -0.5089 -0.4752 0.1095  132 PHE B CG  
2738 C CD1 . PHE B 132 ? 2.5936 1.335  1.4935 -0.5508 -0.5184 0.1271  132 PHE B CD1 
2739 C CD2 . PHE B 132 ? 2.5809 1.3419 1.495  -0.4983 -0.4306 0.0747  132 PHE B CD2 
2740 C CE1 . PHE B 132 ? 2.6599 1.3394 1.4441 -0.5804 -0.5115 0.1056  132 PHE B CE1 
2741 C CE2 . PHE B 132 ? 2.6414 1.3434 1.4527 -0.5247 -0.4244 0.0541  132 PHE B CE2 
2742 C CZ  . PHE B 132 ? 2.6752 1.3369 1.4191 -0.5652 -0.4622 0.0675  132 PHE B CZ  
2743 N N   . SER B 133 ? 2.5732 1.3466 1.5501 -0.4775 -0.4795 0.123   133 SER B N   
2744 C CA  . SER B 133 ? 2.6188 1.3639 1.541  -0.4716 -0.4515 0.1048  133 SER B CA  
2745 C C   . SER B 133 ? 2.6932 1.3898 1.5023 -0.507  -0.4408 0.0892  133 SER B C   
2746 O O   . SER B 133 ? 2.7201 1.3891 1.4771 -0.5452 -0.4752 0.1049  133 SER B O   
2747 C CB  . SER B 133 ? 2.633  1.3692 1.5714 -0.4738 -0.4833 0.1304  133 SER B CB  
2748 O OG  . SER B 133 ? 2.6102 1.3884 1.6587 -0.4399 -0.4968 0.1431  133 SER B OG  
2749 N N   . TYR B 134 ? 2.7259 1.4117 1.4979 -0.4945 -0.3938 0.0574  134 TYR B N   
2750 C CA  . TYR B 134 ? 2.7976 1.4412 1.4704 -0.5207 -0.3734 0.0345  134 TYR B CA  
2751 C C   . TYR B 134 ? 2.8344 1.4666 1.4689 -0.5162 -0.3404 0.0208  134 TYR B C   
2752 O O   . TYR B 134 ? 2.814  1.4704 1.4997 -0.483  -0.3136 0.0107  134 TYR B O   
2753 C CB  . TYR B 134 ? 2.8002 1.446  1.4795 -0.5076 -0.345  0.0064  134 TYR B CB  
2754 C CG  . TYR B 134 ? 2.8635 1.4622 1.4485 -0.532  -0.3268 -0.0214 134 TYR B CG  
2755 C CD1 . TYR B 134 ? 2.9092 1.4722 1.4337 -0.5692 -0.3576 -0.0171 134 TYR B CD1 
2756 C CD2 . TYR B 134 ? 2.8892 1.4784 1.4494 -0.5167 -0.2791 -0.0536 134 TYR B CD2 
2757 C CE1 . TYR B 134 ? 2.9688 1.4833 1.4028 -0.5896 -0.3388 -0.0488 134 TYR B CE1 
2758 C CE2 . TYR B 134 ? 2.9433 1.4905 1.4243 -0.5343 -0.2582 -0.0841 134 TYR B CE2 
2759 C CZ  . TYR B 134 ? 2.9913 1.4988 1.4055 -0.5702 -0.2868 -0.0839 134 TYR B CZ  
2760 O OH  . TYR B 134 ? 3.0568 1.5169 1.3874 -0.5864 -0.2648 -0.1195 134 TYR B OH  
2761 N N   . ASN B 135 ? 2.8879 1.4847 1.4308 -0.5516 -0.3416 0.0208  135 ASN B N   
2762 C CA  . ASN B 135 ? 2.9211 1.5118 1.4254 -0.5533 -0.3085 0.0106  135 ASN B CA  
2763 C C   . ASN B 135 ? 2.986  1.5435 1.391  -0.5797 -0.2791 -0.0175 135 ASN B C   
2764 O O   . ASN B 135 ? 3.0255 1.5511 1.3516 -0.6199 -0.3034 -0.008  135 ASN B O   
2765 C CB  . ASN B 135 ? 2.94   1.5249 1.432  -0.575  -0.3424 0.0471  135 ASN B CB  
2766 C CG  . ASN B 135 ? 2.9389 1.5518 1.5186 -0.5424 -0.3482 0.0619  135 ASN B CG  
2767 O OD1 . ASN B 135 ? 2.9177 1.5523 1.5778 -0.5176 -0.3715 0.0731  135 ASN B OD1 
2768 N ND2 . ASN B 135 ? 2.9524 1.5653 1.5187 -0.5425 -0.3267 0.0616  135 ASN B ND2 
2769 N N   . GLU B 136 ? 2.9977 1.5607 1.4054 -0.5579 -0.2283 -0.0527 136 GLU B N   
2770 C CA  . GLU B 136 ? 3.0597 1.5927 1.3816 -0.5766 -0.1935 -0.0864 136 GLU B CA  
2771 C C   . GLU B 136 ? 3.0798 1.625  1.38   -0.5764 -0.1497 -0.097  136 GLU B C   
2772 O O   . GLU B 136 ? 3.0474 1.6233 1.4165 -0.544  -0.1244 -0.1027 136 GLU B O   
2773 C CB  . GLU B 136 ? 3.0922 1.6164 1.4356 -0.5537 -0.172  -0.1216 136 GLU B CB  
2774 C CG  . GLU B 136 ? 3.2054 1.6939 1.467  -0.5673 -0.1344 -0.163  136 GLU B CG  
2775 C CD  . GLU B 136 ? 3.3016 1.7659 1.574  -0.5521 -0.1263 -0.1951 136 GLU B CD  
2776 O OE1 . GLU B 136 ? 3.3188 1.7707 1.604  -0.5596 -0.1664 -0.1818 136 GLU B OE1 
2777 O OE2 . GLU B 136 ? 3.337  1.7953 1.6103 -0.5332 -0.0815 -0.2322 136 GLU B OE2 
2778 N N   . PHE B 137 ? 3.1331 1.6558 1.3358 -0.6155 -0.1413 -0.098  137 PHE B N   
2779 C CA  . PHE B 137 ? 3.1576 1.6969 1.334  -0.622  -0.0967 -0.1057 137 PHE B CA  
2780 C C   . PHE B 137 ? 3.2089 1.7265 1.3066 -0.633  -0.0475 -0.1515 137 PHE B C   
2781 O O   . PHE B 137 ? 3.2516 1.7275 1.2686 -0.659  -0.0611 -0.165  137 PHE B O   
2782 C CB  . PHE B 137 ? 3.1773 1.7153 1.306  -0.6617 -0.1244 -0.0638 137 PHE B CB  
2783 C CG  . PHE B 137 ? 3.1696 1.7122 1.3565 -0.6594 -0.1858 -0.0185 137 PHE B CG  
2784 C CD1 . PHE B 137 ? 3.1357 1.7089 1.4315 -0.6182 -0.1913 -0.0097 137 PHE B CD1 
2785 C CD2 . PHE B 137 ? 3.2085 1.7234 1.3422 -0.6982 -0.239  0.014   137 PHE B CD2 
2786 C CE1 . PHE B 137 ? 3.126  1.703  1.4782 -0.6125 -0.2436 0.0266  137 PHE B CE1 
2787 C CE2 . PHE B 137 ? 3.1948 1.716  1.3946 -0.6923 -0.2951 0.0544  137 PHE B CE2 
2788 C CZ  . PHE B 137 ? 3.1462 1.6987 1.4559 -0.6477 -0.2947 0.0583  137 PHE B CZ  
2789 N N   . HIS B 138 ? 3.2033 1.7481 1.327  -0.6128 0.0088  -0.1766 138 HIS B N   
2790 C CA  . HIS B 138 ? 3.2486 1.7781 1.3116 -0.6161 0.063   -0.2251 138 HIS B CA  
2791 C C   . HIS B 138 ? 3.2714 1.8267 1.288  -0.6386 0.109   -0.2259 138 HIS B C   
2792 O O   . HIS B 138 ? 3.2392 1.8378 1.3175 -0.63   0.1172  -0.2009 138 HIS B O   
2793 C CB  . HIS B 138 ? 3.2316 1.7719 1.3794 -0.567  0.0946  -0.2616 138 HIS B CB  
2794 C CG  . HIS B 138 ? 3.2785 1.7813 1.436  -0.5544 0.0645  -0.2763 138 HIS B CG  
2795 N ND1 . HIS B 138 ? 3.3264 1.7948 1.457  -0.544  0.0921  -0.325  138 HIS B ND1 
2796 C CD2 . HIS B 138 ? 3.2844 1.7808 1.4787 -0.5516 0.0102  -0.2476 138 HIS B CD2 
2797 C CE1 . HIS B 138 ? 3.3361 1.7767 1.4866 -0.5379 0.0506  -0.3211 138 HIS B CE1 
2798 N NE2 . HIS B 138 ? 3.3146 1.7747 1.5037 -0.5429 0.0027  -0.2747 138 HIS B NE2 
2799 N N   . TYR B 139 ? 3.3257 1.8541 1.231  -0.6693 0.1397  -0.2553 139 TYR B N   
2800 C CA  . TYR B 139 ? 3.3355 1.9117 1.2087 -0.6842 0.1893  -0.2602 139 TYR B CA  
2801 C C   . TYR B 139 ? 3.3297 1.9327 1.2173 -0.648  0.2445  -0.3226 139 TYR B C   
2802 O O   . TYR B 139 ? 3.3361 1.944  1.2028 -0.6357 0.228   -0.3485 139 TYR B O   
2803 C CB  . TYR B 139 ? 3.3244 1.9673 1.1839 -0.6975 0.1493  -0.2244 139 TYR B CB  
2804 C CG  . TYR B 139 ? 3.3066 2.0225 1.1981 -0.7062 0.1579  -0.1824 139 TYR B CG  
2805 C CD1 . TYR B 139 ? 3.3133 2.0218 1.236  -0.7237 0.11    -0.127  139 TYR B CD1 
2806 C CD2 . TYR B 139 ? 3.2853 2.0912 1.1953 -0.6871 0.2095  -0.1959 139 TYR B CD2 
2807 C CE1 . TYR B 139 ? 3.2951 2.0669 1.2509 -0.7321 0.1132  -0.086  139 TYR B CE1 
2808 C CE2 . TYR B 139 ? 3.2663 2.139  1.2073 -0.6958 0.2159  -0.1523 139 TYR B CE2 
2809 C CZ  . TYR B 139 ? 3.2741 2.1317 1.2442 -0.7169 0.1666  -0.0969 139 TYR B CZ  
2810 O OH  . TYR B 139 ? 3.2572 2.1813 1.2688 -0.7222 0.1697  -0.0521 139 TYR B OH  
2811 N N   . HIS B 140 ? 3.316  1.9323 1.2468 -0.629  0.3061  -0.348  140 HIS B N   
2812 C CA  . HIS B 140 ? 3.307  1.9536 1.2748 -0.5856 0.3566  -0.4083 140 HIS B CA  
2813 C C   . HIS B 140 ? 3.2691 2.0181 1.2732 -0.5674 0.4127  -0.4189 140 HIS B C   
2814 O O   . HIS B 140 ? 3.2509 2.0426 1.2653 -0.5889 0.4195  -0.3778 140 HIS B O   
2815 C CB  . HIS B 140 ? 3.3187 1.9132 1.3502 -0.5577 0.3773  -0.4327 140 HIS B CB  
2816 C CG  . HIS B 140 ? 3.3597 1.9105 1.421  -0.542  0.3154  -0.4237 140 HIS B CG  
2817 N ND1 . HIS B 140 ? 3.3455 1.9029 1.5206 -0.494  0.3108  -0.4348 140 HIS B ND1 
2818 C CD2 . HIS B 140 ? 3.4013 1.9236 1.4158 -0.563  0.2532  -0.4008 140 HIS B CD2 
2819 C CE1 . HIS B 140 ? 3.3672 1.8853 1.5386 -0.4956 0.2535  -0.4201 140 HIS B CE1 
2820 N NE2 . HIS B 140 ? 3.4098 1.8975 1.4797 -0.5394 0.2198  -0.4006 140 HIS B NE2 
2821 N N   . GLY B 141 ? 3.2549 2.0414 1.2817 -0.5262 0.4506  -0.4734 141 GLY B N   
2822 C CA  . GLY B 141 ? 3.2164 2.1071 1.2889 -0.4965 0.5055  -0.4884 141 GLY B CA  
2823 C C   . GLY B 141 ? 3.1902 2.0897 1.3543 -0.4775 0.5586  -0.5006 141 GLY B C   
2824 O O   . GLY B 141 ? 3.2083 2.0345 1.3973 -0.4898 0.5498  -0.4904 141 GLY B O   
2825 N N   . MET B 142 ? 3.1435 2.1327 1.3599 -0.4452 0.6143  -0.5217 142 MET B N   
2826 C CA  . MET B 142 ? 3.1054 2.1176 1.4271 -0.4252 0.6647  -0.5303 142 MET B CA  
2827 C C   . MET B 142 ? 3.0894 2.0707 1.4743 -0.3759 0.694   -0.5932 142 MET B C   
2828 O O   . MET B 142 ? 3.0502 2.0579 1.5397 -0.3524 0.7346  -0.6016 142 MET B O   
2829 C CB  . MET B 142 ? 3.0593 2.1973 1.4341 -0.4155 0.703   -0.5041 142 MET B CB  
2830 C CG  . MET B 142 ? 3.079  2.2489 1.4602 -0.4552 0.6701  -0.4295 142 MET B CG  
2831 S SD  . MET B 142 ? 3.1294 2.2403 1.5862 -0.4675 0.6266  -0.3928 142 MET B SD  
2832 C CE  . MET B 142 ? 3.0622 2.1995 1.6377 -0.4418 0.7015  -0.4239 142 MET B CE  
2833 N N   . ASP B 143 ? 3.1155 2.0362 1.4446 -0.3624 0.6705  -0.6348 143 ASP B N   
2834 C CA  . ASP B 143 ? 3.1038 1.9776 1.493  -0.3191 0.6906  -0.6913 143 ASP B CA  
2835 C C   . ASP B 143 ? 3.1432 1.8759 1.4946 -0.3485 0.6599  -0.6868 143 ASP B C   
2836 O O   . ASP B 143 ? 3.1916 1.8738 1.4525 -0.3845 0.6073  -0.6615 143 ASP B O   
2837 C CB  . ASP B 143 ? 3.1097 2.0453 1.5076 -0.2588 0.6819  -0.7433 143 ASP B CB  
2838 C CG  . ASP B 143 ? 3.1934 2.1304 1.5456 -0.2452 0.5991  -0.7466 143 ASP B CG  
2839 O OD1 . ASP B 143 ? 3.2282 2.1577 1.5197 -0.2871 0.5568  -0.701  143 ASP B OD1 
2840 O OD2 . ASP B 143 ? 3.215  2.1559 1.5919 -0.1955 0.5794  -0.7972 143 ASP B OD2 
2841 N N   . GLY B 144 ? 3.1082 1.7961 1.546  -0.3276 0.6847  -0.7003 144 GLY B N   
2842 C CA  . GLY B 144 ? 3.0856 1.7387 1.5826 -0.3108 0.6107  -0.6701 144 GLY B CA  
2843 C C   . GLY B 144 ? 3.0945 1.6691 1.5881 -0.2867 0.5875  -0.7107 144 GLY B C   
2844 O O   . GLY B 144 ? 3.0684 1.633  1.6572 -0.2583 0.5454  -0.6934 144 GLY B O   
2845 N N   . ASP B 145 ? 3.1314 1.645  1.509  -0.3017 0.6098  -0.7625 145 ASP B N   
2846 C CA  . ASP B 145 ? 3.1482 1.5771 1.5126 -0.2842 0.5809  -0.8001 145 ASP B CA  
2847 C C   . ASP B 145 ? 3.1752 1.5474 1.4399 -0.3249 0.5103  -0.7685 145 ASP B C   
2848 O O   . ASP B 145 ? 3.2371 1.537  1.3916 -0.3458 0.502   -0.8029 145 ASP B O   
2849 C CB  . ASP B 145 ? 3.1802 1.6112 1.5277 -0.2541 0.6195  -0.8732 145 ASP B CB  
2850 C CG  . ASP B 145 ? 3.2217 1.6326 1.6617 -0.1987 0.5702  -0.9079 145 ASP B CG  
2851 O OD1 . ASP B 145 ? 3.2523 1.5854 1.7193 -0.2073 0.5449  -0.8831 145 ASP B OD1 
2852 O OD2 . ASP B 145 ? 3.2195 1.6789 1.6897 -0.1506 0.5587  -0.9603 145 ASP B OD2 
2853 N N   . ILE B 146 ? 3.1264 1.5339 1.4307 -0.3372 0.4603  -0.7029 146 ILE B N   
2854 C CA  . ILE B 146 ? 3.1396 1.5118 1.3777 -0.3723 0.3918  -0.6629 146 ILE B CA  
2855 C C   . ILE B 146 ? 3.0741 1.4515 1.4207 -0.3476 0.3389  -0.6269 146 ILE B C   
2856 O O   . ILE B 146 ? 3.0221 1.454  1.48   -0.3191 0.3475  -0.6062 146 ILE B O   
2857 C CB  . ILE B 146 ? 3.1507 1.5682 1.3341 -0.4124 0.3837  -0.6142 146 ILE B CB  
2858 C CG1 . ILE B 146 ? 3.1953 1.6211 1.2749 -0.4405 0.4415  -0.6429 146 ILE B CG1 
2859 C CG2 . ILE B 146 ? 3.1851 1.5711 1.3126 -0.4465 0.3119  -0.5711 146 ILE B CG2 
2860 C CD1 . ILE B 146 ? 3.2026 1.6809 1.2496 -0.4765 0.4382  -0.5921 146 ILE B CD1 
2861 N N   . LEU B 147 ? 3.0735 1.3965 1.3866 -0.3615 0.2835  -0.617  147 LEU B N   
2862 C CA  . LEU B 147 ? 3.0167 1.3475 1.4199 -0.3451 0.2331  -0.579  147 LEU B CA  
2863 C C   . LEU B 147 ? 3.0023 1.3241 1.3533 -0.381  0.1754  -0.5341 147 LEU B C   
2864 O O   . LEU B 147 ? 3.0538 1.3181 1.326  -0.4062 0.1483  -0.5461 147 LEU B O   
2865 C CB  . LEU B 147 ? 3.0219 1.3018 1.4762 -0.3162 0.2242  -0.6114 147 LEU B CB  
2866 C CG  . LEU B 147 ? 2.994  1.3064 1.5624 -0.2703 0.2631  -0.6304 147 LEU B CG  
2867 C CD1 . LEU B 147 ? 3.0187 1.3069 1.5599 -0.2545 0.3238  -0.6963 147 LEU B CD1 
2868 C CD2 . LEU B 147 ? 2.9769 1.2715 1.6409 -0.2451 0.2234  -0.6159 147 LEU B CD2 
2869 N N   . VAL B 148 ? 2.9313 1.3093 1.3233 -0.3849 0.1574  -0.4842 148 VAL B N   
2870 C CA  . VAL B 148 ? 2.9118 1.2902 1.2735 -0.4137 0.1042  -0.4399 148 VAL B CA  
2871 C C   . VAL B 148 ? 2.8522 1.2391 1.3023 -0.3934 0.0666  -0.4144 148 VAL B C   
2872 O O   . VAL B 148 ? 2.811  1.2415 1.3473 -0.3667 0.0752  -0.3986 148 VAL B O   
2873 C CB  . VAL B 148 ? 2.9018 1.331  1.2535 -0.43   0.1059  -0.4029 148 VAL B CB  
2874 C CG1 . VAL B 148 ? 2.9068 1.3422 1.2552 -0.4504 0.0493  -0.3559 148 VAL B CG1 
2875 C CG2 . VAL B 148 ? 2.9418 1.3618 1.1943 -0.4582 0.1401  -0.423  148 VAL B CG2 
2876 N N   . LYS B 149 ? 2.8463 1.1913 1.2748 -0.4077 0.0255  -0.4105 149 LYS B N   
2877 C CA  . LYS B 149 ? 2.7966 1.151  1.3038 -0.3927 -0.0079 -0.3856 149 LYS B CA  
2878 C C   . LYS B 149 ? 2.7837 1.1431 1.2803 -0.4181 -0.0588 -0.3458 149 LYS B C   
2879 O O   . LYS B 149 ? 2.8036 1.1213 1.278  -0.4342 -0.0899 -0.3483 149 LYS B O   
2880 C CB  . LYS B 149 ? 2.8115 1.1163 1.3426 -0.376  -0.0069 -0.4184 149 LYS B CB  
2881 C CG  . LYS B 149 ? 2.801  1.1247 1.4248 -0.3567 -0.0316 -0.3915 149 LYS B CG  
2882 C CD  . LYS B 149 ? 2.8462 1.112  1.4874 -0.3486 -0.0447 -0.4157 149 LYS B CD  
2883 C CE  . LYS B 149 ? 2.8423 1.1289 1.5757 -0.3301 -0.0648 -0.3881 149 LYS B CE  
2884 N NZ  . LYS B 149 ? 2.8582 1.1557 1.5977 -0.353  -0.1108 -0.346  149 LYS B NZ  
2885 N N   . PRO B 150 ? 2.7429 1.1555 1.2689 -0.4192 -0.0695 -0.3073 150 PRO B N   
2886 C CA  . PRO B 150 ? 2.7254 1.1525 1.2607 -0.4377 -0.1152 -0.2689 150 PRO B CA  
2887 C C   . PRO B 150 ? 2.6753 1.129  1.2946 -0.4194 -0.1318 -0.2473 150 PRO B C   
2888 O O   . PRO B 150 ? 2.6471 1.1334 1.3247 -0.3927 -0.1127 -0.2436 150 PRO B O   
2889 C CB  . PRO B 150 ? 2.7239 1.1932 1.2552 -0.4438 -0.1159 -0.2419 150 PRO B CB  
2890 C CG  . PRO B 150 ? 2.7309 1.2114 1.2554 -0.4289 -0.0702 -0.263  150 PRO B CG  
2891 C CD  . PRO B 150 ? 2.7108 1.171  1.2627 -0.405  -0.0419 -0.2977 150 PRO B CD  
2892 N N   . THR B 151 ? 2.6641 1.1042 1.2869 -0.4369 -0.1684 -0.2313 151 THR B N   
2893 C CA  . THR B 151 ? 2.6222 1.0911 1.3161 -0.4276 -0.186  -0.2058 151 THR B CA  
2894 C C   . THR B 151 ? 2.5957 1.0961 1.2974 -0.4486 -0.2197 -0.1694 151 THR B C   
2895 O O   . THR B 151 ? 2.6232 1.0927 1.2817 -0.4773 -0.2474 -0.1672 151 THR B O   
2896 C CB  . THR B 151 ? 2.6556 1.0764 1.3523 -0.4325 -0.1997 -0.22   151 THR B CB  
2897 O OG1 . THR B 151 ? 2.6747 1.0685 1.3786 -0.4085 -0.1689 -0.2539 151 THR B OG1 
2898 C CG2 . THR B 151 ? 2.6315 1.0828 1.3916 -0.4333 -0.2232 -0.1867 151 THR B CG2 
2899 N N   . VAL B 152 ? 2.5425 1.1026 1.298  -0.4345 -0.218  -0.1424 152 VAL B N   
2900 C CA  . VAL B 152 ? 2.5171 1.1138 1.2926 -0.4492 -0.2465 -0.1093 152 VAL B CA  
2901 C C   . VAL B 152 ? 2.466  1.1158 1.3157 -0.4391 -0.2527 -0.0823 152 VAL B C   
2902 O O   . VAL B 152 ? 2.4416 1.1264 1.3296 -0.4138 -0.2307 -0.0804 152 VAL B O   
2903 C CB  . VAL B 152 ? 2.5249 1.1423 1.2874 -0.4456 -0.2414 -0.1025 152 VAL B CB  
2904 C CG1 . VAL B 152 ? 2.5145 1.1631 1.3014 -0.4611 -0.2759 -0.0692 152 VAL B CG1 
2905 C CG2 . VAL B 152 ? 2.5721 1.1427 1.2555 -0.4583 -0.2294 -0.1278 152 VAL B CG2 
2906 N N   . LYS B 153 ? 2.4505 1.1082 1.3186 -0.461  -0.2824 -0.0607 153 LYS B N   
2907 C CA  . LYS B 153 ? 2.4089 1.125  1.3465 -0.456  -0.2861 -0.0326 153 LYS B CA  
2908 C C   . LYS B 153 ? 2.3834 1.1482 1.3545 -0.4599 -0.302  -0.007  153 LYS B C   
2909 O O   . LYS B 153 ? 2.4009 1.1477 1.3496 -0.4848 -0.3321 0.0023  153 LYS B O   
2910 C CB  . LYS B 153 ? 2.4291 1.1287 1.3756 -0.4805 -0.3099 -0.0205 153 LYS B CB  
2911 C CG  . LYS B 153 ? 2.4258 1.1928 1.442  -0.483  -0.3141 0.0135  153 LYS B CG  
2912 C CD  . LYS B 153 ? 2.4559 1.2504 1.499  -0.458  -0.2832 0.0106  153 LYS B CD  
2913 C CE  . LYS B 153 ? 2.4534 1.3272 1.5585 -0.4543 -0.2754 0.0394  153 LYS B CE  
2914 N NZ  . LYS B 153 ? 2.4629 1.3567 1.5985 -0.4843 -0.2983 0.0693  153 LYS B NZ  
2915 N N   . VAL B 154 ? 2.3412 1.1635 1.3645 -0.4353 -0.2839 0.003   154 VAL B N   
2916 C CA  . VAL B 154 ? 2.3109 1.1805 1.3784 -0.4325 -0.2972 0.0246  154 VAL B CA  
2917 C C   . VAL B 154 ? 2.2624 1.2035 1.4067 -0.4241 -0.2903 0.0468  154 VAL B C   
2918 O O   . VAL B 154 ? 2.2503 1.2131 1.4101 -0.4059 -0.2621 0.0401  154 VAL B O   
2919 C CB  . VAL B 154 ? 2.3229 1.1911 1.3803 -0.409  -0.2824 0.0124  154 VAL B CB  
2920 C CG1 . VAL B 154 ? 2.3007 1.2086 1.4069 -0.4058 -0.3025 0.0347  154 VAL B CG1 
2921 C CG2 . VAL B 154 ? 2.3765 1.1809 1.356  -0.4196 -0.2824 -0.0091 154 VAL B CG2 
2922 N N   . GLU B 155 ? 2.2328 1.212  1.4249 -0.4396 -0.3161 0.0743  155 GLU B N   
2923 C CA  . GLU B 155 ? 2.1881 1.2446 1.4599 -0.4333 -0.3067 0.0966  155 GLU B CA  
2924 C C   . GLU B 155 ? 2.1506 1.2537 1.4824 -0.4178 -0.3148 0.1094  155 GLU B C   
2925 O O   . GLU B 155 ? 2.1537 1.2437 1.4883 -0.4364 -0.3514 0.1248  155 GLU B O   
2926 C CB  . GLU B 155 ? 2.2206 1.2861 1.5102 -0.469  -0.3322 0.122   155 GLU B CB  
2927 C CG  . GLU B 155 ? 2.3308 1.3566 1.5771 -0.4806 -0.3234 0.1119  155 GLU B CG  
2928 C CD  . GLU B 155 ? 2.4633 1.4279 1.6668 -0.5178 -0.3601 0.116   155 GLU B CD  
2929 O OE1 . GLU B 155 ? 2.4802 1.4426 1.6922 -0.542  -0.3963 0.1337  155 GLU B OE1 
2930 O OE2 . GLU B 155 ? 2.5246 1.4405 1.6873 -0.523  -0.3553 0.1013  155 GLU B OE2 
2931 N N   . ILE B 156 ? 2.1186 1.2689 1.4943 -0.3836 -0.2831 0.1013  156 ILE B N   
2932 C CA  . ILE B 156 ? 2.0888 1.2781 1.5274 -0.3617 -0.2888 0.1083  156 ILE B CA  
2933 C C   . ILE B 156 ? 2.035  1.3145 1.5702 -0.3487 -0.2719 0.1246  156 ILE B C   
2934 O O   . ILE B 156 ? 2.0256 1.3391 1.5697 -0.3323 -0.2328 0.1131  156 ILE B O   
2935 C CB  . ILE B 156 ? 2.1084 1.27   1.5186 -0.3292 -0.2679 0.0806  156 ILE B CB  
2936 C CG1 . ILE B 156 ? 2.1738 1.2552 1.4927 -0.3429 -0.2787 0.0651  156 ILE B CG1 
2937 C CG2 . ILE B 156 ? 2.0818 1.2726 1.5571 -0.3065 -0.2797 0.0874  156 ILE B CG2 
2938 C CD1 . ILE B 156 ? 2.2048 1.2622 1.4933 -0.3174 -0.2543 0.0402  156 ILE B CD1 
2939 N N   . ASP B 157 ? 1.9965 1.3171 1.6052 -0.3563 -0.3005 0.1517  157 ASP B N   
2940 C CA  . ASP B 157 ? 1.9357 1.3514 1.6502 -0.3435 -0.2832 0.1686  157 ASP B CA  
2941 C C   . ASP B 157 ? 1.8988 1.3509 1.672  -0.2958 -0.2575 0.1502  157 ASP B C   
2942 O O   . ASP B 157 ? 1.9277 1.3268 1.6587 -0.2766 -0.26   0.1286  157 ASP B O   
2943 C CB  . ASP B 157 ? 1.9371 1.3838 1.7155 -0.3742 -0.3289 0.2087  157 ASP B CB  
2944 C CG  . ASP B 157 ? 1.9528 1.4923 1.819  -0.3837 -0.3133 0.2343  157 ASP B CG  
2945 O OD1 . ASP B 157 ? 1.9714 1.5173 1.8033 -0.399  -0.2891 0.2331  157 ASP B OD1 
2946 O OD2 . ASP B 157 ? 1.931  1.5381 1.9039 -0.3778 -0.3273 0.2586  157 ASP B OD2 
2947 N N   . GLU B 158 ? 1.8343 1.3767 1.7052 -0.2769 -0.2312 0.1576  474 GLU B N   
2948 C CA  . GLU B 158 ? 1.8042 1.3863 1.7414 -0.229  -0.2037 0.1368  474 GLU B CA  
2949 C C   . GLU B 158 ? 1.8042 1.3485 1.7668 -0.213  -0.2431 0.1382  474 GLU B C   
2950 O O   . GLU B 158 ? 1.7776 1.3395 1.8028 -0.2279 -0.286  0.1699  474 GLU B O   
2951 C CB  . GLU B 158 ? 1.7657 1.4589 1.8204 -0.2163 -0.1757 0.1506  474 GLU B CB  
2952 C CG  . GLU B 158 ? 1.8362 1.5755 1.8699 -0.2353 -0.1354 0.154   474 GLU B CG  
2953 C CD  . GLU B 158 ? 1.8568 1.7119 2      -0.2174 -0.0932 0.1601  474 GLU B CD  
2954 O OE1 . GLU B 158 ? 1.8401 1.7323 2.0611 -0.1743 -0.0768 0.1426  474 GLU B OE1 
2955 O OE2 . GLU B 158 ? 1.8626 1.7717 2.0155 -0.2463 -0.0755 0.1819  474 GLU B OE2 
2956 N N   . GLY B 159 ? 1.834  1.324  1.7459 -0.1866 -0.2324 0.107   475 GLY B N   
2957 C CA  . GLY B 159 ? 1.8434 1.2908 1.7716 -0.171  -0.2683 0.1073  475 GLY B CA  
2958 C C   . GLY B 159 ? 1.8991 1.2602 1.7354 -0.2041 -0.3118 0.118   475 GLY B C   
2959 O O   . GLY B 159 ? 1.9105 1.2328 1.7516 -0.1977 -0.3451 0.123   475 GLY B O   
2960 N N   . GLY B 160 ? 1.9314 1.2619 1.6847 -0.2397 -0.3115 0.1213  476 GLY B N   
2961 C CA  . GLY B 160 ? 1.9885 1.2401 1.6476 -0.2729 -0.3454 0.127   476 GLY B CA  
2962 C C   . GLY B 160 ? 2.0307 1.2183 1.6129 -0.2597 -0.3332 0.0999  476 GLY B C   
2963 O O   . GLY B 160 ? 2.0305 1.2267 1.6141 -0.2286 -0.2955 0.0732  476 GLY B O   
2964 N N   . ILE B 161 ? 2.0648 1.1884 1.5771 -0.2859 -0.3654 0.1074  477 ILE B N   
2965 C CA  . ILE B 161 ? 2.1018 1.1672 1.5434 -0.2793 -0.3571 0.0872  477 ILE B CA  
2966 C C   . ILE B 161 ? 2.15   1.1568 1.4865 -0.3156 -0.3631 0.0839  477 ILE B C   
2967 O O   . ILE B 161 ? 2.1663 1.1532 1.477  -0.3493 -0.398  0.1043  477 ILE B O   
2968 C CB  . ILE B 161 ? 2.0995 1.1492 1.577  -0.267  -0.3898 0.0994  477 ILE B CB  
2969 C CG1 . ILE B 161 ? 2.0617 1.1577 1.6351 -0.2205 -0.3724 0.0882  477 ILE B CG1 
2970 C CG2 . ILE B 161 ? 2.1547 1.1394 1.5506 -0.2752 -0.393  0.0895  477 ILE B CG2 
2971 C CD1 . ILE B 161 ? 2.0242 1.169  1.7045 -0.2119 -0.4014 0.1136  477 ILE B CD1 
2972 N N   . TYR B 162 ? 2.1735 1.1517 1.4506 -0.3088 -0.3303 0.0576  478 TYR B N   
2973 C CA  . TYR B 162 ? 2.2268 1.1523 1.4118 -0.3371 -0.329  0.0491  478 TYR B CA  
2974 C C   . TYR B 162 ? 2.2632 1.1516 1.403  -0.3285 -0.3161 0.0338  478 TYR B C   
2975 O O   . TYR B 162 ? 2.2566 1.1552 1.4135 -0.3006 -0.2889 0.0164  478 TYR B O   
2976 C CB  . TYR B 162 ? 2.2306 1.1604 1.3939 -0.3413 -0.3018 0.0343  478 TYR B CB  
2977 C CG  . TYR B 162 ? 2.2834 1.1589 1.3604 -0.3647 -0.2962 0.0197  478 TYR B CG  
2978 C CD1 . TYR B 162 ? 2.3218 1.1609 1.3473 -0.3988 -0.3249 0.0292  478 TYR B CD1 
2979 C CD2 . TYR B 162 ? 2.3077 1.1684 1.3561 -0.353  -0.2624 -0.0045 478 TYR B CD2 
2980 C CE1 . TYR B 162 ? 2.3757 1.1652 1.3209 -0.4179 -0.3146 0.0101  478 TYR B CE1 
2981 C CE2 . TYR B 162 ? 2.3561 1.1706 1.3365 -0.3702 -0.254  -0.0208 478 TYR B CE2 
2982 C CZ  . TYR B 162 ? 2.3958 1.1749 1.3237 -0.4014 -0.2774 -0.0159 478 TYR B CZ  
2983 O OH  . TYR B 162 ? 2.4519 1.1851 1.3111 -0.416  -0.2641 -0.0376 478 TYR B OH  
2984 N N   . ILE B 163 ? 2.3005 1.1465 1.3811 -0.355  -0.3368 0.0418  479 ILE B N   
2985 C CA  . ILE B 163 ? 2.3345 1.1474 1.3694 -0.354  -0.3256 0.032   479 ILE B CA  
2986 C C   . ILE B 163 ? 2.3847 1.1593 1.3325 -0.3834 -0.3144 0.0207  479 ILE B C   
2987 O O   . ILE B 163 ? 2.405  1.1605 1.3136 -0.4144 -0.3383 0.0323  479 ILE B O   
2988 C CB  . ILE B 163 ? 2.3392 1.1407 1.39   -0.3585 -0.3614 0.0556  479 ILE B CB  
2989 C CG1 . ILE B 163 ? 2.3102 1.146  1.4524 -0.3211 -0.3656 0.058   479 ILE B CG1 
2990 C CG2 . ILE B 163 ? 2.3775 1.1419 1.369  -0.3701 -0.3545 0.052   479 ILE B CG2 
2991 C CD1 . ILE B 163 ? 2.3116 1.1497 1.5002 -0.3255 -0.4116 0.0873  479 ILE B CD1 
2992 N N   . SER B 164 ? 2.4034 1.1672 1.3234 -0.3737 -0.2784 -0.0033 480 SER B N   
2993 C CA  . SER B 164 ? 2.4528 1.1839 1.2994 -0.3954 -0.2603 -0.0201 480 SER B CA  
2994 C C   . SER B 164 ? 2.4873 1.2039 1.304  -0.3935 -0.2378 -0.0298 480 SER B C   
2995 O O   . SER B 164 ? 2.4726 1.2049 1.329  -0.3682 -0.2241 -0.0342 480 SER B O   
2996 C CB  . SER B 164 ? 2.4576 1.1942 1.312  -0.3857 -0.237  -0.0402 480 SER B CB  
2997 O OG  . SER B 164 ? 2.5072 1.2119 1.3027 -0.3978 -0.214  -0.0627 480 SER B OG  
2998 N N   . ASN B 165 ? 2.5327 1.2199 1.2778 -0.4219 -0.2335 -0.0332 481 ASN B N   
2999 C CA  . ASN B 165 ? 2.564  1.2433 1.2806 -0.4252 -0.2097 -0.0396 481 ASN B CA  
3000 C C   . ASN B 165 ? 2.6116 1.2673 1.257  -0.4457 -0.1814 -0.0626 481 ASN B C   
3001 O O   . ASN B 165 ? 2.6454 1.2762 1.2273 -0.477  -0.1962 -0.0587 481 ASN B O   
3002 C CB  . ASN B 165 ? 2.5911 1.2624 1.2935 -0.4443 -0.2392 -0.0104 481 ASN B CB  
3003 C CG  . ASN B 165 ? 2.6081 1.2976 1.3844 -0.4201 -0.2646 0.0081  481 ASN B CG  
3004 O OD1 . ASN B 165 ? 2.6028 1.3079 1.4257 -0.3909 -0.2478 -0.0022 481 ASN B OD1 
3005 N ND2 . ASN B 165 ? 2.616  1.3014 1.4054 -0.4315 -0.3072 0.035   481 ASN B ND2 
3006 N N   . PHE B 166 ? 2.6137 1.2758 1.2696 -0.4282 -0.1418 -0.0874 482 PHE B N   
3007 C CA  . PHE B 166 ? 2.6547 1.297  1.2526 -0.442  -0.1088 -0.1143 482 PHE B CA  
3008 C C   . PHE B 166 ? 2.6576 1.3127 1.2494 -0.4437 -0.0793 -0.1159 482 PHE B C   
3009 O O   . PHE B 166 ? 2.6302 1.3088 1.2816 -0.4193 -0.0679 -0.1148 482 PHE B O   
3010 C CB  . PHE B 166 ? 2.6533 1.2919 1.2771 -0.4203 -0.0877 -0.1428 482 PHE B CB  
3011 C CG  . PHE B 166 ? 2.6846 1.3    1.2885 -0.4306 -0.11   -0.1472 482 PHE B CG  
3012 C CD1 . PHE B 166 ? 2.7345 1.312  1.2681 -0.452  -0.1015 -0.1701 482 PHE B CD1 
3013 C CD2 . PHE B 166 ? 2.6754 1.3069 1.3315 -0.4193 -0.138  -0.1299 482 PHE B CD2 
3014 C CE1 . PHE B 166 ? 2.7593 1.3111 1.276  -0.4636 -0.1263 -0.1734 482 PHE B CE1 
3015 C CE2 . PHE B 166 ? 2.6952 1.3092 1.3396 -0.4314 -0.1596 -0.1306 482 PHE B CE2 
3016 C CZ  . PHE B 166 ? 2.7304 1.3023 1.3056 -0.4543 -0.1565 -0.1512 482 PHE B CZ  
3017 N N   . THR B 167 ? 2.6897 1.3306 1.2079 -0.4757 -0.0687 -0.116  483 THR B N   
3018 C CA  . THR B 167 ? 2.6951 1.3537 1.2053 -0.4835 -0.039  -0.1136 483 THR B CA  
3019 C C   . THR B 167 ? 2.7231 1.3735 1.174  -0.4967 0.0078  -0.1461 483 THR B C   
3020 O O   . THR B 167 ? 2.7645 1.3863 1.1308 -0.5268 0.0052  -0.1532 483 THR B O   
3021 C CB  . THR B 167 ? 2.7238 1.3803 1.2044 -0.5132 -0.0694 -0.0756 483 THR B CB  
3022 O OG1 . THR B 167 ? 2.719  1.3756 1.25   -0.5006 -0.1163 -0.0499 483 THR B OG1 
3023 C CG2 . THR B 167 ? 2.7186 1.3999 1.213  -0.5187 -0.0454 -0.0649 483 THR B CG2 
3024 N N   . LEU B 168 ? 2.699  1.3742 1.1948 -0.4744 0.0502  -0.1667 484 LEU B N   
3025 C CA  . LEU B 168 ? 2.7173 1.3922 1.1738 -0.4798 0.1023  -0.2019 484 LEU B CA  
3026 C C   . LEU B 168 ? 2.6908 1.409  1.1864 -0.4775 0.1364  -0.1943 484 LEU B C   
3027 O O   . LEU B 168 ? 2.66   1.4036 1.2367 -0.446  0.1556  -0.2046 484 LEU B O   
3028 C CB  . LEU B 168 ? 2.7155 1.3771 1.2083 -0.4478 0.1204  -0.2402 484 LEU B CB  
3029 C CG  . LEU B 168 ? 2.7717 1.3863 1.2128 -0.4562 0.0961  -0.2553 484 LEU B CG  
3030 C CD1 . LEU B 168 ? 2.7597 1.3722 1.2579 -0.4388 0.0504  -0.2343 484 LEU B CD1 
3031 C CD2 . LEU B 168 ? 2.7952 1.3862 1.2235 -0.4423 0.1334  -0.3041 484 LEU B CD2 
3032 N N   . THR B 169 ? 2.6992 1.4267 1.1426 -0.5132 0.1376  -0.1703 485 THR B N   
3033 C CA  . THR B 169 ? 2.6735 1.4454 1.1531 -0.518  0.1668  -0.1563 485 THR B CA  
3034 C C   . THR B 169 ? 2.6943 1.479  1.0946 -0.5536 0.2138  -0.1664 485 THR B C   
3035 O O   . THR B 169 ? 2.6731 1.4996 1.0978 -0.565  0.2396  -0.1504 485 THR B O   
3036 C CB  . THR B 169 ? 2.677  1.4553 1.187  -0.528  0.1201  -0.1081 485 THR B CB  
3037 O OG1 . THR B 169 ? 2.7271 1.4766 1.1558 -0.5664 0.0854  -0.0827 485 THR B OG1 
3038 C CG2 . THR B 169 ? 2.6582 1.4295 1.2463 -0.4919 0.0821  -0.1017 485 THR B CG2 
3039 N N   . LYS B 170 ? 2.7336 1.4831 1.0368 -0.5738 0.2245  -0.192  486 LYS B N   
3040 C CA  . LYS B 170 ? 2.7659 1.5205 0.9725 -0.6116 0.2693  -0.2058 486 LYS B CA  
3041 C C   . LYS B 170 ? 2.7751 1.5277 0.9677 -0.5916 0.331   -0.2663 486 LYS B C   
3042 O O   . LYS B 170 ? 2.8082 1.5145 0.9677 -0.5804 0.3211  -0.2979 486 LYS B O   
3043 C CB  . LYS B 170 ? 2.8366 1.5459 0.9237 -0.6598 0.2289  -0.1845 486 LYS B CB  
3044 C CG  . LYS B 170 ? 2.8761 1.6002 0.9429 -0.6994 0.1977  -0.1274 486 LYS B CG  
3045 C CD  . LYS B 170 ? 2.9123 1.6806 0.9453 -0.7289 0.2543  -0.1245 486 LYS B CD  
3046 C CE  . LYS B 170 ? 2.9414 1.7269 0.9767 -0.7644 0.2199  -0.0635 486 LYS B CE  
3047 N NZ  . LYS B 170 ? 2.9151 1.7224 1.0786 -0.7286 0.1907  -0.0394 486 LYS B NZ  
3048 N N   . GLY B 171 ? 2.743  1.5458 0.9627 -0.5883 0.3936  -0.2818 487 GLY B N   
3049 C CA  . GLY B 171 ? 2.7382 1.5464 0.9599 -0.5647 0.459   -0.3417 487 GLY B CA  
3050 C C   . GLY B 171 ? 2.6887 1.5011 1.0337 -0.5071 0.4584  -0.3644 487 GLY B C   
3051 O O   . GLY B 171 ? 2.6569 1.486  1.0941 -0.487  0.4202  -0.3315 487 GLY B O   
3052 N N   . ARG B 172 ? 2.6808 1.4741 1.0256 -0.4811 0.499   -0.4212 488 ARG B N   
3053 C CA  . ARG B 172 ? 2.6373 1.4273 1.0949 -0.4287 0.4949  -0.4426 488 ARG B CA  
3054 C C   . ARG B 172 ? 2.6602 1.3846 1.0938 -0.4222 0.4351  -0.4426 488 ARG B C   
3055 O O   . ARG B 172 ? 2.7167 1.3878 1.0471 -0.443  0.4286  -0.4653 488 ARG B O   
3056 C CB  . ARG B 172 ? 2.6363 1.4345 1.1182 -0.4008 0.5635  -0.5033 488 ARG B CB  
3057 C CG  . ARG B 172 ? 2.6043 1.4835 1.175  -0.3888 0.619   -0.5    488 ARG B CG  
3058 C CD  . ARG B 172 ? 2.5977 1.4892 1.2594 -0.3406 0.6678  -0.5518 488 ARG B CD  
3059 N NE  . ARG B 172 ? 2.6045 1.4639 1.3559 -0.3008 0.6215  -0.5516 488 ARG B NE  
3060 C CZ  . ARG B 172 ? 2.6054 1.4509 1.4311 -0.2574 0.6434  -0.5952 488 ARG B CZ  
3061 N NH1 . ARG B 172 ? 2.59   1.4518 1.4168 -0.2433 0.7148  -0.6478 488 ARG B NH1 
3062 N NH2 . ARG B 172 ? 2.5903 1.4046 1.4893 -0.2283 0.5944  -0.5869 488 ARG B NH2 
3063 N N   . ILE B 173 ? 2.6148 1.3439 1.1395 -0.3968 0.3909  -0.4155 489 ILE B N   
3064 C CA  . ILE B 173 ? 2.6264 1.3043 1.1434 -0.3898 0.3365  -0.4113 489 ILE B CA  
3065 C C   . ILE B 173 ? 2.6323 1.2647 1.1444 -0.3672 0.3545  -0.464  489 ILE B C   
3066 O O   . ILE B 173 ? 2.6753 1.2513 1.1122 -0.3823 0.3291  -0.4772 489 ILE B O   
3067 C CB  . ILE B 173 ? 2.5904 1.2918 1.2116 -0.3656 0.296   -0.3743 489 ILE B CB  
3068 C CG1 . ILE B 173 ? 2.5944 1.3242 1.2096 -0.3892 0.2674  -0.324  489 ILE B CG1 
3069 C CG2 . ILE B 173 ? 2.6084 1.2661 1.242  -0.3514 0.2513  -0.3758 489 ILE B CG2 
3070 C CD1 . ILE B 173 ? 2.5749 1.3246 1.2827 -0.3665 0.2295  -0.2913 489 ILE B CD1 
3071 N N   . GLY B 174 ? 2.5866 1.2427 1.1811 -0.3323 0.3965  -0.4929 490 GLY B N   
3072 C CA  . GLY B 174 ? 2.5889 1.2034 1.2045 -0.3032 0.4126  -0.5426 490 GLY B CA  
3073 C C   . GLY B 174 ? 2.549  1.1565 1.2634 -0.2739 0.367   -0.5218 490 GLY B C   
3074 O O   . GLY B 174 ? 2.5055 1.159  1.3248 -0.2502 0.3701  -0.5029 490 GLY B O   
3075 N N   . THR B 175 ? 2.5603 1.1127 1.2384 -0.2806 0.3206  -0.5195 491 THR B N   
3076 C CA  . THR B 175 ? 2.5223 1.0679 1.2795 -0.2605 0.2746  -0.4948 491 THR B CA  
3077 C C   . THR B 175 ? 2.5248 1.0515 1.2265 -0.2884 0.2209  -0.4591 491 THR B C   
3078 O O   . THR B 175 ? 2.5699 1.0485 1.1885 -0.3104 0.2055  -0.4728 491 THR B O   
3079 C CB  . THR B 175 ? 2.5434 1.0414 1.3406 -0.2329 0.2749  -0.5322 491 THR B CB  
3080 O OG1 . THR B 175 ? 2.522  1.0446 1.3893 -0.2021 0.3253  -0.5642 491 THR B OG1 
3081 C CG2 . THR B 175 ? 2.5315 1.0189 1.397  -0.2202 0.2226  -0.5015 491 THR B CG2 
3082 N N   . LEU B 176 ? 2.475  1.0398 1.222  -0.2884 0.1928  -0.4144 492 LEU B N   
3083 C CA  . LEU B 176 ? 2.475  1.0314 1.1877 -0.3096 0.1444  -0.3795 492 LEU B CA  
3084 C C   . LEU B 176 ? 2.4413 0.988  1.2172 -0.292  0.1092  -0.3653 492 LEU B C   
3085 O O   . LEU B 176 ? 2.4064 0.9763 1.2631 -0.2671 0.1134  -0.3593 492 LEU B O   
3086 C CB  . LEU B 176 ? 2.4582 1.0609 1.1757 -0.3213 0.1374  -0.3415 492 LEU B CB  
3087 C CG  . LEU B 176 ? 2.4828 1.0848 1.1787 -0.3388 0.0904  -0.3051 492 LEU B CG  
3088 C CD1 . LEU B 176 ? 2.5317 1.095  1.1367 -0.3694 0.074   -0.3109 492 LEU B CD1 
3089 C CD2 . LEU B 176 ? 2.4759 1.1177 1.1857 -0.3452 0.0856  -0.273  492 LEU B CD2 
3090 N N   . ASP B 177 ? 2.45   0.9627 1.1891 -0.3075 0.0735  -0.3585 493 ASP B N   
3091 C CA  . ASP B 177 ? 2.4274 0.9335 1.219  -0.2973 0.0394  -0.3406 493 ASP B CA  
3092 C C   . ASP B 177 ? 2.4209 0.9315 1.1819 -0.3205 -0.0001 -0.3082 493 ASP B C   
3093 O O   . ASP B 177 ? 2.4501 0.9236 1.1653 -0.3396 -0.0212 -0.3135 493 ASP B O   
3094 C CB  . ASP B 177 ? 2.4681 0.9214 1.2654 -0.2883 0.0382  -0.3721 493 ASP B CB  
3095 C CG  . ASP B 177 ? 2.5083 0.9515 1.363  -0.2797 0.0035  -0.3528 493 ASP B CG  
3096 O OD1 . ASP B 177 ? 2.5013 0.977  1.377  -0.2857 -0.0219 -0.3149 493 ASP B OD1 
3097 O OD2 . ASP B 177 ? 2.535  0.9365 1.4125 -0.2678 0.0019  -0.376  493 ASP B OD2 
3098 N N   . ILE B 178 ? 2.3787 0.934  1.1683 -0.3185 -0.0109 -0.2754 494 ILE B N   
3099 C CA  . ILE B 178 ? 2.3665 0.9347 1.1433 -0.3351 -0.0449 -0.2448 494 ILE B CA  
3100 C C   . ILE B 178 ? 2.336  0.9171 1.1676 -0.3249 -0.0671 -0.2254 494 ILE B C   
3101 O O   . ILE B 178 ? 2.3111 0.9118 1.1945 -0.3048 -0.0589 -0.221  494 ILE B O   
3102 C CB  . ILE B 178 ? 2.3562 0.9614 1.131  -0.3382 -0.0445 -0.2228 494 ILE B CB  
3103 C CG1 . ILE B 178 ? 2.3893 0.9847 1.105  -0.3541 -0.0236 -0.2361 494 ILE B CG1 
3104 C CG2 . ILE B 178 ? 2.3549 0.9764 1.1316 -0.3499 -0.0792 -0.1928 494 ILE B CG2 
3105 C CD1 . ILE B 178 ? 2.393  1.0218 1.1155 -0.3561 -0.0225 -0.2138 494 ILE B CD1 
3106 N N   . GLU B 179 ? 2.3373 0.909  1.157  -0.3416 -0.0962 -0.2116 495 GLU B N   
3107 C CA  . GLU B 179 ? 2.3176 0.9073 1.1839 -0.3378 -0.1163 -0.1893 495 GLU B CA  
3108 C C   . GLU B 179 ? 2.3005 0.9156 1.1617 -0.3548 -0.1414 -0.1622 495 GLU B C   
3109 O O   . GLU B 179 ? 2.324  0.9167 1.1455 -0.3767 -0.1578 -0.1632 495 GLU B O   
3110 C CB  . GLU B 179 ? 2.3719 0.9204 1.245  -0.3408 -0.1266 -0.2011 495 GLU B CB  
3111 C CG  . GLU B 179 ? 2.4588 0.9947 1.368  -0.3171 -0.1066 -0.2193 495 GLU B CG  
3112 C CD  . GLU B 179 ? 2.6043 1.094  1.5297 -0.3163 -0.1189 -0.2317 495 GLU B CD  
3113 O OE1 . GLU B 179 ? 2.6723 1.1195 1.5594 -0.3339 -0.1334 -0.2439 495 GLU B OE1 
3114 O OE2 . GLU B 179 ? 2.6202 1.1121 1.5969 -0.2989 -0.1172 -0.2286 495 GLU B OE2 
3115 N N   . GLN B 180 ? 2.2589 0.9205 1.1596 -0.3446 -0.1441 -0.1395 496 GLN B N   
3116 C CA  . GLN B 180 ? 2.239  0.9326 1.1501 -0.3557 -0.1647 -0.1145 496 GLN B CA  
3117 C C   . GLN B 180 ? 2.2114 0.9434 1.1708 -0.3492 -0.1693 -0.0942 496 GLN B C   
3118 O O   . GLN B 180 ? 2.2014 0.9456 1.1829 -0.3321 -0.155  -0.096  496 GLN B O   
3119 C CB  . GLN B 180 ? 2.2382 0.9548 1.1457 -0.3496 -0.1611 -0.1085 496 GLN B CB  
3120 C CG  . GLN B 180 ? 2.2832 0.9686 1.1361 -0.3641 -0.1607 -0.1203 496 GLN B CG  
3121 C CD  . GLN B 180 ? 2.3029 1.0101 1.1568 -0.3689 -0.1757 -0.1014 496 GLN B CD  
3122 O OE1 . GLN B 180 ? 2.2961 1.0251 1.1737 -0.3764 -0.1995 -0.0805 496 GLN B OE1 
3123 N NE2 . GLN B 180 ? 2.3153 1.0183 1.1496 -0.3653 -0.1637 -0.1062 496 GLN B NE2 
3124 N N   . GLU B 181 ? 2.1973 0.9507 1.1725 -0.3651 -0.1896 -0.0734 497 GLU B N   
3125 C CA  . GLU B 181 ? 2.1725 0.972  1.1919 -0.3622 -0.1899 -0.0523 497 GLU B CA  
3126 C C   . GLU B 181 ? 2.1472 0.9895 1.1919 -0.3686 -0.2025 -0.0323 497 GLU B C   
3127 O O   . GLU B 181 ? 2.1568 0.9882 1.1933 -0.3904 -0.2256 -0.0233 497 GLU B O   
3128 C CB  . GLU B 181 ? 2.212  0.996  1.2382 -0.3786 -0.202  -0.0434 497 GLU B CB  
3129 C CG  . GLU B 181 ? 2.2668 1.0987 1.3302 -0.376  -0.1957 -0.0223 497 GLU B CG  
3130 C CD  . GLU B 181 ? 2.381  1.2081 1.4565 -0.3997 -0.2134 -0.0026 497 GLU B CD  
3131 O OE1 . GLU B 181 ? 2.4131 1.2197 1.4825 -0.4224 -0.2367 0.004   497 GLU B OE1 
3132 O OE2 . GLU B 181 ? 2.4135 1.2553 1.5021 -0.3986 -0.2071 0.0085  497 GLU B OE2 
3133 N N   . ILE B 182 ? 2.1139 1.0013 1.1899 -0.3488 -0.1888 -0.0272 498 ILE B N   
3134 C CA  . ILE B 182 ? 2.0829 1.0164 1.1977 -0.347  -0.1974 -0.0107 498 ILE B CA  
3135 C C   . ILE B 182 ? 2.0446 1.038  1.2074 -0.3413 -0.1846 0.0044  498 ILE B C   
3136 O O   . ILE B 182 ? 2.0455 1.0488 1.2065 -0.3268 -0.1629 -0.0035 498 ILE B O   
3137 C CB  . ILE B 182 ? 2.086  1.0181 1.1987 -0.3264 -0.1918 -0.021  498 ILE B CB  
3138 C CG1 . ILE B 182 ? 2.128  1.0109 1.1931 -0.3399 -0.2068 -0.0285 498 ILE B CG1 
3139 C CG2 . ILE B 182 ? 2.0541 1.0385 1.2225 -0.3146 -0.1962 -0.0068 498 ILE B CG2 
3140 C CD1 . ILE B 182 ? 2.1741 1.0117 1.1923 -0.3374 -0.191  -0.051  498 ILE B CD1 
3141 N N   . ILE B 183 ? 2.0083 1.0426 1.2125 -0.3557 -0.1983 0.0272  499 ILE B N   
3142 C CA  . ILE B 183 ? 1.9664 1.0676 1.22   -0.3525 -0.1821 0.0428  499 ILE B CA  
3143 C C   . ILE B 183 ? 1.9221 1.0732 1.2316 -0.3364 -0.1821 0.0492  499 ILE B C   
3144 O O   . ILE B 183 ? 1.9182 1.0678 1.2464 -0.3497 -0.21   0.063   499 ILE B O   
3145 C CB  . ILE B 183 ? 1.9667 1.0803 1.2339 -0.3855 -0.1985 0.0681  499 ILE B CB  
3146 C CG1 . ILE B 183 ? 2.0197 1.0666 1.2333 -0.4027 -0.2096 0.0607  499 ILE B CG1 
3147 C CG2 . ILE B 183 ? 1.9321 1.1208 1.2468 -0.3859 -0.1766 0.0862  499 ILE B CG2 
3148 C CD1 . ILE B 183 ? 2.0464 1.0832 1.2382 -0.3918 -0.1878 0.0507  499 ILE B CD1 
3149 N N   . ALA B 184 ? 1.8896 1.0798 1.225  -0.308  -0.1537 0.0382  500 ALA B N   
3150 C CA  . ALA B 184 ? 1.8546 1.0879 1.2504 -0.2866 -0.1529 0.0399  500 ALA B CA  
3151 C C   . ALA B 184 ? 1.8059 1.1213 1.2664 -0.2765 -0.1266 0.0484  500 ALA B C   
3152 O O   . ALA B 184 ? 1.8014 1.1361 1.2448 -0.2711 -0.0958 0.0396  500 ALA B O   
3153 C CB  . ALA B 184 ? 1.875  1.0758 1.2498 -0.2573 -0.1452 0.0145  500 ALA B CB  
3154 N N   . LYS B 185 ? 1.7693 1.1352 1.3057 -0.2743 -0.1384 0.0661  501 LYS B N   
3155 C CA  . LYS B 185 ? 1.7264 1.1818 1.341  -0.2618 -0.1104 0.0741  501 LYS B CA  
3156 C C   . LYS B 185 ? 1.7132 1.1919 1.3766 -0.2173 -0.0927 0.0512  501 LYS B C   
3157 O O   . LYS B 185 ? 1.7478 1.1685 1.3761 -0.2001 -0.1041 0.0316  501 LYS B O   
3158 C CB  . LYS B 185 ? 1.7121 1.2168 1.3939 -0.29   -0.1356 0.1121  501 LYS B CB  
3159 C CG  . LYS B 185 ? 1.7847 1.2734 1.4251 -0.3328 -0.148  0.1334  501 LYS B CG  
3160 C CD  . LYS B 185 ? 1.8331 1.3125 1.4984 -0.3669 -0.1969 0.1648  501 LYS B CD  
3161 C CE  . LYS B 185 ? 1.9229 1.3341 1.5126 -0.4039 -0.2217 0.1712  501 LYS B CE  
3162 N NZ  . LYS B 185 ? 1.9701 1.3241 1.5371 -0.4262 -0.2717 0.18    501 LYS B NZ  
3163 N N   . LYS B 186 ? 1.6609 1.2237 1.4056 -0.1986 -0.0635 0.0525  502 LYS B N   
3164 C CA  . LYS B 186 ? 1.639  1.2309 1.4422 -0.153  -0.0422 0.0278  502 LYS B CA  
3165 C C   . LYS B 186 ? 1.6527 1.1908 1.4697 -0.1355 -0.081  0.0229  502 LYS B C   
3166 O O   . LYS B 186 ? 1.6494 1.1753 1.4904 -0.1561 -0.1245 0.0508  502 LYS B O   
3167 C CB  . LYS B 186 ? 1.5942 1.2911 1.5111 -0.1441 -0.0211 0.0433  502 LYS B CB  
3168 C CG  . LYS B 186 ? 1.6191 1.3616 1.5914 -0.0949 0.0221  0.0094  502 LYS B CG  
3169 C CD  . LYS B 186 ? 1.6015 1.4539 1.703  -0.0842 0.0419  0.0262  502 LYS B CD  
3170 C CE  . LYS B 186 ? 1.6166 1.5264 1.7593 -0.0392 0.1027  -0.0128 502 LYS B CE  
3171 N NZ  . LYS B 186 ? 1.6589 1.5132 1.8052 0.0072  0.0967  -0.0513 502 LYS B NZ  
3172 N N   . ASP B 187 ? 1.672  1.1729 1.4665 -0.1019 -0.0686 -0.0105 503 ASP B N   
3173 C CA  . ASP B 187 ? 1.6903 1.1409 1.5007 -0.0833 -0.1036 -0.0155 503 ASP B CA  
3174 C C   . ASP B 187 ? 1.73   1.1059 1.4767 -0.1152 -0.1514 0.0036  503 ASP B C   
3175 O O   . ASP B 187 ? 1.7317 1.0788 1.5045 -0.11   -0.1884 0.013   503 ASP B O   
3176 C CB  . ASP B 187 ? 1.6614 1.17   1.597  -0.06   -0.116  -0.003  503 ASP B CB  
3177 C CG  . ASP B 187 ? 1.682  1.2684 1.6896 -0.0232 -0.064  -0.0266 503 ASP B CG  
3178 O OD1 . ASP B 187 ? 1.7149 1.2797 1.6886 0.0069  -0.0322 -0.0663 503 ASP B OD1 
3179 O OD2 . ASP B 187 ? 1.6519 1.3215 1.7498 -0.0255 -0.0548 -0.0058 503 ASP B OD2 
3180 N N   . ALA B 188 ? 1.7612 1.1041 1.4248 -0.1472 -0.1503 0.0079  504 ALA B N   
3181 C CA  . ALA B 188 ? 1.8065 1.0798 1.4042 -0.1756 -0.1873 0.0196  504 ALA B CA  
3182 C C   . ALA B 188 ? 1.8431 1.0514 1.3827 -0.1611 -0.1879 -0.0037 504 ALA B C   
3183 O O   . ALA B 188 ? 1.848  1.0569 1.3792 -0.135  -0.1584 -0.0301 504 ALA B O   
3184 C CB  . ALA B 188 ? 1.8349 1.0947 1.3725 -0.2108 -0.1846 0.0287  504 ALA B CB  
3185 N N   . ILE B 189 ? 1.8673 1.02   1.3656 -0.1802 -0.2221 0.007   505 ILE B N   
3186 C CA  . ILE B 189 ? 1.9033 0.9971 1.3482 -0.1728 -0.225  -0.0093 505 ILE B CA  
3187 C C   . ILE B 189 ? 1.9397 0.9832 1.3029 -0.2071 -0.237  -0.0032 505 ILE B C   
3188 O O   . ILE B 189 ? 1.9471 0.981  1.3014 -0.2342 -0.2653 0.018   505 ILE B O   
3189 C CB  . ILE B 189 ? 1.902  0.9815 1.3922 -0.1557 -0.2545 -0.0031 505 ILE B CB  
3190 C CG1 . ILE B 189 ? 1.8728 0.9959 1.4444 -0.1134 -0.236  -0.0194 505 ILE B CG1 
3191 C CG2 . ILE B 189 ? 1.9522 0.9671 1.3811 -0.1592 -0.2648 -0.0114 505 ILE B CG2 
3192 C CD1 . ILE B 189 ? 1.8367 1.0153 1.5084 -0.1051 -0.2532 0.0013  505 ILE B CD1 
3193 N N   . ILE B 190 ? 1.9609 0.9734 1.2659 -0.2062 -0.215  -0.0226 506 ILE B N   
3194 C CA  . ILE B 190 ? 1.9974 0.9659 1.2314 -0.2334 -0.2187 -0.0223 506 ILE B CA  
3195 C C   . ILE B 190 ? 2.0253 0.9511 1.221  -0.2277 -0.217  -0.0342 506 ILE B C   
3196 O O   . ILE B 190 ? 2.0203 0.947  1.2242 -0.2047 -0.2002 -0.0504 506 ILE B O   
3197 C CB  . ILE B 190 ? 2.0057 0.9824 1.2148 -0.242  -0.1947 -0.0304 506 ILE B CB  
3198 C CG1 . ILE B 190 ? 1.9883 1.012  1.2398 -0.2501 -0.1963 -0.0153 506 ILE B CG1 
3199 C CG2 . ILE B 190 ? 2.0457 0.9767 1.1902 -0.2659 -0.1965 -0.0343 506 ILE B CG2 
3200 C CD1 . ILE B 190 ? 1.9706 1.0476 1.2703 -0.2265 -0.1702 -0.0215 506 ILE B CD1 
3201 N N   . ASP B 191 ? 2.0538 0.9424 1.2052 -0.2511 -0.2345 -0.0255 507 ASP B N   
3202 C CA  . ASP B 191 ? 2.0886 0.9403 1.2021 -0.253  -0.2327 -0.0317 507 ASP B CA  
3203 C C   . ASP B 191 ? 2.1262 0.9504 1.1762 -0.2812 -0.2262 -0.0337 507 ASP B C   
3204 O O   . ASP B 191 ? 2.1431 0.9523 1.1657 -0.3063 -0.2465 -0.0199 507 ASP B O   
3205 C CB  . ASP B 191 ? 2.1164 0.9528 1.2456 -0.2548 -0.2646 -0.0147 507 ASP B CB  
3206 C CG  . ASP B 191 ? 2.21   1.0111 1.306  -0.2594 -0.266  -0.0161 507 ASP B CG  
3207 O OD1 . ASP B 191 ? 2.2343 1.026  1.2985 -0.2601 -0.2403 -0.0313 507 ASP B OD1 
3208 O OD2 . ASP B 191 ? 2.2427 1.0265 1.3496 -0.2635 -0.2952 0.0008  507 ASP B OD2 
3209 N N   . ILE B 192 ? 2.1379 0.9544 1.1649 -0.2774 -0.1989 -0.0513 508 ILE B N   
3210 C CA  . ILE B 192 ? 2.1686 0.9605 1.1436 -0.2983 -0.1867 -0.0592 508 ILE B CA  
3211 C C   . ILE B 192 ? 2.1864 0.9604 1.1403 -0.2976 -0.173  -0.0663 508 ILE B C   
3212 O O   . ILE B 192 ? 2.1812 0.9625 1.16   -0.2779 -0.1632 -0.073  508 ILE B O   
3213 C CB  . ILE B 192 ? 2.1695 0.9691 1.1475 -0.2946 -0.1685 -0.0718 508 ILE B CB  
3214 C CG1 . ILE B 192 ? 2.1667 0.9876 1.1679 -0.3002 -0.1829 -0.0608 508 ILE B CG1 
3215 C CG2 . ILE B 192 ? 2.1987 0.9701 1.132  -0.3094 -0.1531 -0.0857 508 ILE B CG2 
3216 C CD1 . ILE B 192 ? 2.1786 1.0096 1.1897 -0.2973 -0.1689 -0.0678 508 ILE B CD1 
3217 N N   . THR B 193 ? 2.2043 0.9563 1.1114 -0.321  -0.1726 -0.0638 509 THR B N   
3218 C CA  . THR B 193 ? 2.2127 0.9547 1.1034 -0.3245 -0.1579 -0.0668 509 THR B CA  
3219 C C   . THR B 193 ? 2.2381 0.9666 1.0823 -0.3421 -0.1328 -0.081  509 THR B C   
3220 O O   . THR B 193 ? 2.2595 0.9741 1.0641 -0.3608 -0.1362 -0.0839 509 THR B O   
3221 C CB  . THR B 193 ? 2.2256 0.9583 1.1106 -0.336  -0.183  -0.0452 509 THR B CB  
3222 O OG1 . THR B 193 ? 2.2135 0.9568 1.1489 -0.3144 -0.2044 -0.0374 509 THR B OG1 
3223 C CG2 . THR B 193 ? 2.2374 0.9631 1.1091 -0.3437 -0.1706 -0.0428 509 THR B CG2 
3224 N N   . THR B 194 ? 2.234  0.9664 1.0852 -0.3357 -0.1074 -0.0913 510 THR B N   
3225 C CA  . THR B 194 ? 2.2543 0.9791 1.0719 -0.3476 -0.0773 -0.1086 510 THR B CA  
3226 C C   . THR B 194 ? 2.2572 0.9903 1.0732 -0.3553 -0.0613 -0.1029 510 THR B C   
3227 O O   . THR B 194 ? 2.2408 0.9874 1.102  -0.3392 -0.0605 -0.0987 510 THR B O   
3228 C CB  . THR B 194 ? 2.2585 0.9865 1.1049 -0.328  -0.0567 -0.1305 510 THR B CB  
3229 O OG1 . THR B 194 ? 2.2607 0.9916 1.1319 -0.3155 -0.0749 -0.1278 510 THR B OG1 
3230 C CG2 . THR B 194 ? 2.282  0.9933 1.0908 -0.3386 -0.0315 -0.1535 510 THR B CG2 
3231 N N   . ARG B 195 ? 2.2756 1.0012 1.0378 -0.3825 -0.0492 -0.1016 511 ARG B N   
3232 C CA  . ARG B 195 ? 2.2752 1.015  1.0355 -0.3945 -0.0298 -0.094  511 ARG B CA  
3233 C C   . ARG B 195 ? 2.2793 1.0235 1.0107 -0.402  0.0147  -0.1199 511 ARG B C   
3234 O O   . ARG B 195 ? 2.3092 1.0346 0.9752 -0.4229 0.0206  -0.1293 511 ARG B O   
3235 C CB  . ARG B 195 ? 2.3144 1.045  1.0361 -0.4241 -0.0556 -0.0641 511 ARG B CB  
3236 C CG  . ARG B 195 ? 2.3549 1.0808 1.1185 -0.4118 -0.0976 -0.041  511 ARG B CG  
3237 C CD  . ARG B 195 ? 2.4198 1.1351 1.1608 -0.439  -0.1254 -0.0083 511 ARG B CD  
3238 N NE  . ARG B 195 ? 2.4492 1.1742 1.2318 -0.4339 -0.1271 0.0043  511 ARG B NE  
3239 C CZ  . ARG B 195 ? 2.4744 1.1862 1.2909 -0.4263 -0.1642 0.0238  511 ARG B CZ  
3240 N NH1 . ARG B 195 ? 2.4802 1.1732 1.2995 -0.4219 -0.2011 0.0342  511 ARG B NH1 
3241 N NH2 . ARG B 195 ? 2.4593 1.1754 1.3092 -0.4243 -0.1664 0.0334  511 ARG B NH2 
3242 N N   . THR B 196 ? 2.2476 1.0147 1.029  -0.3839 0.0451  -0.1335 512 THR B N   
3243 C CA  . THR B 196 ? 2.2486 1.023  1.0171 -0.3843 0.0913  -0.1626 512 THR B CA  
3244 C C   . THR B 196 ? 2.2331 1.044  1.0332 -0.3883 0.1246  -0.1589 512 THR B C   
3245 O O   . THR B 196 ? 2.2079 1.039  1.0658 -0.3795 0.1121  -0.1391 512 THR B O   
3246 C CB  . THR B 196 ? 2.2429 1.01   1.0541 -0.3543 0.0996  -0.1888 512 THR B CB  
3247 O OG1 . THR B 196 ? 2.2166 0.9999 1.1028 -0.3308 0.0832  -0.176  512 THR B OG1 
3248 C CG2 . THR B 196 ? 2.2727 1.0045 1.043  -0.3563 0.0777  -0.1985 512 THR B CG2 
3249 N N   . TYR B 197 ? 2.2489 1.0694 1.0128 -0.4016 0.1685  -0.1795 513 TYR B N   
3250 C CA  . TYR B 197 ? 2.2398 1.1041 1.0391 -0.406  0.2082  -0.1779 513 TYR B CA  
3251 C C   . TYR B 197 ? 2.2347 1.1087 1.0498 -0.3881 0.2593  -0.2203 513 TYR B C   
3252 O O   . TYR B 197 ? 2.2649 1.128  1.0078 -0.4051 0.2909  -0.2441 513 TYR B O   
3253 C CB  . TYR B 197 ? 2.2717 1.1462 1.0043 -0.4484 0.2149  -0.1549 513 TYR B CB  
3254 C CG  . TYR B 197 ? 2.2637 1.1917 1.04   -0.4568 0.2546  -0.1463 513 TYR B CG  
3255 C CD1 . TYR B 197 ? 2.235  1.1929 1.1081 -0.4386 0.2442  -0.1282 513 TYR B CD1 
3256 C CD2 . TYR B 197 ? 2.2929 1.2431 1.0128 -0.4851 0.3027  -0.1559 513 TYR B CD2 
3257 C CE1 . TYR B 197 ? 2.2137 1.2254 1.1364 -0.448  0.2786  -0.1171 513 TYR B CE1 
3258 C CE2 . TYR B 197 ? 2.272  1.2799 1.0384 -0.4948 0.3422  -0.1455 513 TYR B CE2 
3259 C CZ  . TYR B 197 ? 2.2376 1.2777 1.1109 -0.4756 0.3292  -0.1252 513 TYR B CZ  
3260 O OH  . TYR B 197 ? 2.2245 1.3259 1.1521 -0.4869 0.3662  -0.1118 513 TYR B OH  
3261 N N   . ALA B 198 ? 2.1974 1.0872 1.1051 -0.3535 0.265   -0.2308 514 ALA B N   
3262 C CA  . ALA B 198 ? 2.1889 1.0855 1.1325 -0.3293 0.3085  -0.2713 514 ALA B CA  
3263 C C   . ALA B 198 ? 2.1536 1.1082 1.1529 -0.3283 0.3596  -0.2755 514 ALA B C   
3264 O O   . ALA B 198 ? 2.1178 1.1107 1.1884 -0.3267 0.3503  -0.2461 514 ALA B O   
3265 C CB  . ALA B 198 ? 2.1723 1.0523 1.1888 -0.2941 0.2831  -0.2781 514 ALA B CB  
3266 N N   . ILE B 199 ? 2.1626 1.1236 1.1272 -0.3307 0.4145  -0.313  515 ILE B N   
3267 C CA  . ILE B 199 ? 2.1341 1.1552 1.1448 -0.3302 0.4755  -0.3246 515 ILE B CA  
3268 C C   . ILE B 199 ? 2.1236 1.1426 1.1751 -0.2956 0.5231  -0.379  515 ILE B C   
3269 O O   . ILE B 199 ? 2.1561 1.1188 1.1757 -0.28   0.508   -0.4076 515 ILE B O   
3270 C CB  . ILE B 199 ? 2.1757 1.2093 1.0811 -0.3762 0.5035  -0.3172 515 ILE B CB  
3271 C CG1 . ILE B 199 ? 2.25   1.2273 1.0333 -0.3893 0.5145  -0.3544 515 ILE B CG1 
3272 C CG2 . ILE B 199 ? 2.1918 1.2268 1.0697 -0.4092 0.4545  -0.2617 515 ILE B CG2 
3273 C CD1 . ILE B 199 ? 2.3005 1.2907 0.9773 -0.434  0.5513  -0.3547 515 ILE B CD1 
3274 N N   . LYS B 200 ? 2.0761 1.1566 1.2009 -0.284  0.5806  -0.3933 516 LYS B N   
3275 C CA  . LYS B 200 ? 2.0582 1.1447 1.2375 -0.2477 0.6326  -0.447  516 LYS B CA  
3276 C C   . LYS B 200 ? 2.0489 1.091  1.3015 -0.2065 0.5912  -0.4586 516 LYS B C   
3277 O O   . LYS B 200 ? 2.0212 1.0777 1.3562 -0.1963 0.5476  -0.4212 516 LYS B O   
3278 C CB  . LYS B 200 ? 2.1273 1.1872 1.1864 -0.264  0.684   -0.4954 516 LYS B CB  
3279 C CG  . LYS B 200 ? 2.175  1.2897 1.176  -0.3031 0.7356  -0.4864 516 LYS B CG  
3280 C CD  . LYS B 200 ? 2.253  1.3591 1.1836 -0.3015 0.8082  -0.55   516 LYS B CD  
3281 C CE  . LYS B 200 ? 2.313  1.457  1.142  -0.3501 0.8574  -0.5447 516 LYS B CE  
3282 N NZ  . LYS B 200 ? 2.3739 1.4914 1.1054 -0.3517 0.9215  -0.6117 516 LYS B NZ  
3283 N N   . GLU B 201 ? 2.074  1.0576 1.289  -0.1879 0.5982  -0.5055 517 GLU B N   
3284 C CA  . GLU B 201 ? 2.0687 1.008  1.3491 -0.154  0.556   -0.5121 517 GLU B CA  
3285 C C   . GLU B 201 ? 2.1093 0.9774 1.2962 -0.1712 0.4973  -0.5003 517 GLU B C   
3286 O O   . GLU B 201 ? 2.1272 0.9407 1.3193 -0.1516 0.476   -0.5231 517 GLU B O   
3287 C CB  . GLU B 201 ? 2.1066 1.0293 1.4362 -0.1162 0.5999  -0.5713 517 GLU B CB  
3288 C CG  . GLU B 201 ? 2.1364 1.134  1.5978 -0.0885 0.6512  -0.5807 517 GLU B CG  
3289 C CD  . GLU B 201 ? 2.2438 1.3076 1.6717 -0.112  0.718   -0.5864 517 GLU B CD  
3290 O OE1 . GLU B 201 ? 2.2159 1.3554 1.7318 -0.115  0.7285  -0.5514 517 GLU B OE1 
3291 O OE2 . GLU B 201 ? 2.3271 1.3659 1.6359 -0.1313 0.7571  -0.6231 517 GLU B OE2 
3292 N N   . ASP B 202 ? 2.1194 0.989  1.227  -0.2081 0.4697  -0.4633 518 ASP B N   
3293 C CA  . ASP B 202 ? 2.1548 0.9679 1.1809 -0.2263 0.4153  -0.4477 518 ASP B CA  
3294 C C   . ASP B 202 ? 2.1213 0.9139 1.2155 -0.205  0.3617  -0.4267 518 ASP B C   
3295 O O   . ASP B 202 ? 2.081  0.9094 1.2718 -0.1881 0.3509  -0.4035 518 ASP B O   
3296 C CB  . ASP B 202 ? 2.195  1.0228 1.1503 -0.2652 0.3937  -0.4069 518 ASP B CB  
3297 C CG  . ASP B 202 ? 2.2921 1.1122 1.1321 -0.2998 0.4251  -0.422  518 ASP B CG  
3298 O OD1 . ASP B 202 ? 2.3183 1.1146 1.116  -0.2952 0.4642  -0.4693 518 ASP B OD1 
3299 O OD2 . ASP B 202 ? 2.3377 1.1714 1.1259 -0.3328 0.4084  -0.3868 518 ASP B OD2 
3300 N N   . VAL B 203 ? 2.1366 0.8722 1.1769 -0.2095 0.3263  -0.4321 519 VAL B N   
3301 C CA  . VAL B 203 ? 2.1149 0.8307 1.204  -0.1961 0.2752  -0.4094 519 VAL B CA  
3302 C C   . VAL B 203 ? 2.1332 0.8275 1.1468 -0.2229 0.2325  -0.3815 519 VAL B C   
3303 O O   . VAL B 203 ? 2.1755 0.8347 1.1018 -0.2425 0.2321  -0.3969 519 VAL B O   
3304 C CB  . VAL B 203 ? 2.1318 0.8011 1.2503 -0.1721 0.273   -0.4427 519 VAL B CB  
3305 C CG1 . VAL B 203 ? 2.1444 0.7851 1.284  -0.1694 0.2159  -0.4161 519 VAL B CG1 
3306 C CG2 . VAL B 203 ? 2.0945 0.791  1.3162 -0.1392 0.3087  -0.4646 519 VAL B CG2 
3307 N N   . VAL B 204 ? 2.0987 0.814  1.1455 -0.2242 0.1966  -0.3415 520 VAL B N   
3308 C CA  . VAL B 204 ? 2.1092 0.8105 1.1013 -0.2444 0.1567  -0.3148 520 VAL B CA  
3309 C C   . VAL B 204 ? 2.0959 0.7833 1.1307 -0.2314 0.1177  -0.2988 520 VAL B C   
3310 O O   . VAL B 204 ? 2.0651 0.7732 1.1707 -0.215  0.1097  -0.2848 520 VAL B O   
3311 C CB  . VAL B 204 ? 2.0994 0.8347 1.0772 -0.2614 0.1502  -0.2836 520 VAL B CB  
3312 C CG1 . VAL B 204 ? 2.1188 0.8413 1.0612 -0.2745 0.1073  -0.2573 520 VAL B CG1 
3313 C CG2 . VAL B 204 ? 2.1167 0.8628 1.0374 -0.2826 0.1848  -0.2941 520 VAL B CG2 
3314 N N   . LYS B 205 ? 2.1191 0.772  1.1096 -0.2417 0.0928  -0.2995 521 LYS B N   
3315 C CA  . LYS B 205 ? 2.119  0.7604 1.1391 -0.2356 0.0569  -0.282  521 LYS B CA  
3316 C C   . LYS B 205 ? 2.1332 0.7749 1.1042 -0.2558 0.0284  -0.2591 521 LYS B C   
3317 O O   . LYS B 205 ? 2.1643 0.7838 1.0745 -0.274  0.0261  -0.268  521 LYS B O   
3318 C CB  . LYS B 205 ? 2.1659 0.7637 1.1933 -0.228  0.0536  -0.306  521 LYS B CB  
3319 C CG  . LYS B 205 ? 2.2098 0.8083 1.3165 -0.2014 0.0669  -0.3191 521 LYS B CG  
3320 C CD  . LYS B 205 ? 2.2976 0.8536 1.4008 -0.191  0.0882  -0.3617 521 LYS B CD  
3321 C CE  . LYS B 205 ? 2.3781 0.8804 1.4498 -0.2006 0.058   -0.3673 521 LYS B CE  
3322 N NZ  . LYS B 205 ? 2.4142 0.8683 1.4956 -0.1853 0.075   -0.4107 521 LYS B NZ  
3323 N N   . VAL B 206 ? 2.1096 0.7768 1.1064 -0.2532 0.007   -0.2305 522 VAL B N   
3324 C CA  . VAL B 206 ? 2.1194 0.793  1.0844 -0.2675 -0.0178 -0.2098 522 VAL B CA  
3325 C C   . VAL B 206 ? 2.1087 0.7891 1.1068 -0.2613 -0.0414 -0.1919 522 VAL B C   
3326 O O   . VAL B 206 ? 2.0927 0.7899 1.1312 -0.2486 -0.0431 -0.1823 522 VAL B O   
3327 C CB  . VAL B 206 ? 2.1225 0.8219 1.0753 -0.2728 -0.0176 -0.1942 522 VAL B CB  
3328 C CG1 . VAL B 206 ? 2.1333 0.8393 1.066  -0.2831 -0.044  -0.1746 522 VAL B CG1 
3329 C CG2 . VAL B 206 ? 2.142  0.8372 1.0565 -0.2846 0.0061  -0.2074 522 VAL B CG2 
3330 N N   . ASN B 207 ? 2.1172 0.7854 1.0969 -0.273  -0.0604 -0.1859 523 ASN B N   
3331 C CA  . ASN B 207 ? 2.1105 0.7888 1.1167 -0.272  -0.0805 -0.167  523 ASN B CA  
3332 C C   . ASN B 207 ? 2.108  0.804  1.0944 -0.2855 -0.0969 -0.1499 523 ASN B C   
3333 O O   . ASN B 207 ? 2.1233 0.8018 1.0858 -0.3012 -0.1079 -0.1513 523 ASN B O   
3334 C CB  . ASN B 207 ? 2.1423 0.7873 1.1602 -0.2739 -0.0884 -0.1752 523 ASN B CB  
3335 C CG  . ASN B 207 ? 2.1878 0.8416 1.2385 -0.2734 -0.1072 -0.1538 523 ASN B CG  
3336 O OD1 . ASN B 207 ? 2.2001 0.887  1.2552 -0.2749 -0.1138 -0.1334 523 ASN B OD1 
3337 N ND2 . ASN B 207 ? 2.2019 0.8242 1.2743 -0.2723 -0.1164 -0.1583 523 ASN B ND2 
3338 N N   . GLU B 208 ? 2.0883 0.8178 1.0869 -0.2792 -0.0993 -0.1348 524 GLU B N   
3339 C CA  . GLU B 208 ? 2.0855 0.8381 1.0788 -0.2876 -0.1127 -0.1193 524 GLU B CA  
3340 C C   . GLU B 208 ? 2.0602 0.844  1.0806 -0.2824 -0.1179 -0.1032 524 GLU B C   
3341 O O   . GLU B 208 ? 2.059  0.8514 1.0927 -0.2697 -0.1111 -0.1032 524 GLU B O   
3342 C CB  . GLU B 208 ? 2.1237 0.8864 1.1042 -0.2854 -0.1106 -0.1187 524 GLU B CB  
3343 C CG  . GLU B 208 ? 2.224  0.9591 1.1653 -0.2991 -0.1076 -0.1302 524 GLU B CG  
3344 C CD  . GLU B 208 ? 2.3287 1.0677 1.2548 -0.2993 -0.104  -0.1283 524 GLU B CD  
3345 O OE1 . GLU B 208 ? 2.3388 1.0953 1.2892 -0.2848 -0.1005 -0.1233 524 GLU B OE1 
3346 O OE2 . GLU B 208 ? 2.3761 1.0974 1.2622 -0.3167 -0.1068 -0.131  524 GLU B OE2 
3347 N N   . VAL B 209 ? 2.0383 0.8395 1.0651 -0.2945 -0.1298 -0.0888 525 VAL B N   
3348 C CA  . VAL B 209 ? 2.0116 0.8497 1.0608 -0.2926 -0.1299 -0.0731 525 VAL B CA  
3349 C C   . VAL B 209 ? 1.9873 0.8631 1.0512 -0.2944 -0.1341 -0.0619 525 VAL B C   
3350 O O   . VAL B 209 ? 1.9931 0.8646 1.0547 -0.3094 -0.1478 -0.0557 525 VAL B O   
3351 C CB  . VAL B 209 ? 2.0195 0.8505 1.0751 -0.3079 -0.1394 -0.0612 525 VAL B CB  
3352 C CG1 . VAL B 209 ? 2.0072 0.8836 1.0797 -0.3115 -0.1368 -0.0419 525 VAL B CG1 
3353 C CG2 . VAL B 209 ? 2.038  0.8323 1.0916 -0.303  -0.1386 -0.0706 525 VAL B CG2 
3354 N N   . VAL B 210 ? 1.9579 0.8685 1.0385 -0.279  -0.1239 -0.0603 526 VAL B N   
3355 C CA  . VAL B 210 ? 1.9279 0.8796 1.0366 -0.2756 -0.1256 -0.0511 526 VAL B CA  
3356 C C   . VAL B 210 ? 1.9002 0.898  1.0299 -0.273  -0.1121 -0.0421 526 VAL B C   
3357 O O   . VAL B 210 ? 1.9019 0.9029 1.021  -0.2605 -0.098  -0.0508 526 VAL B O   
3358 C CB  . VAL B 210 ? 1.9328 0.8833 1.0466 -0.2571 -0.1251 -0.0608 526 VAL B CB  
3359 C CG1 . VAL B 210 ? 1.9108 0.9071 1.0675 -0.2489 -0.1268 -0.0517 526 VAL B CG1 
3360 C CG2 . VAL B 210 ? 1.9593 0.8699 1.0474 -0.2662 -0.138  -0.065  526 VAL B CG2 
3361 N N   . LYS B 211 ? 1.8749 0.9087 1.0315 -0.2876 -0.1166 -0.0237 527 LYS B N   
3362 C CA  . LYS B 211 ? 1.8557 0.9417 1.0326 -0.2895 -0.1001 -0.0126 527 LYS B CA  
3363 C C   . LYS B 211 ? 1.8278 0.9695 1.0522 -0.2746 -0.0897 -0.011  527 LYS B C   
3364 O O   . LYS B 211 ? 1.8078 0.9727 1.0685 -0.285  -0.1036 0.0047  527 LYS B O   
3365 C CB  . LYS B 211 ? 1.8723 0.9648 1.0527 -0.3198 -0.1115 0.0109  527 LYS B CB  
3366 C CG  . LYS B 211 ? 1.9538 0.9858 1.0977 -0.3324 -0.1261 0.0081  527 LYS B CG  
3367 C CD  . LYS B 211 ? 2.0134 1.0492 1.1611 -0.3617 -0.1384 0.0326  527 LYS B CD  
3368 C CE  . LYS B 211 ? 2.0928 1.0669 1.2131 -0.3702 -0.1535 0.0287  527 LYS B CE  
3369 N NZ  . LYS B 211 ? 2.1179 1.0987 1.2397 -0.3949 -0.1625 0.0544  527 LYS B NZ  
3370 N N   . LEU B 212 ? 1.8249 0.9858 1.0517 -0.2498 -0.0674 -0.028  528 LEU B N   
3371 C CA  . LEU B 212 ? 1.8027 1.0157 1.0811 -0.229  -0.0536 -0.0321 528 LEU B CA  
3372 C C   . LEU B 212 ? 1.7795 1.0599 1.0844 -0.2384 -0.0302 -0.0185 528 LEU B C   
3373 O O   . LEU B 212 ? 1.7791 1.0798 1.0641 -0.2297 -0.0022 -0.0307 528 LEU B O   
3374 C CB  . LEU B 212 ? 1.8201 1.0163 1.086  -0.1973 -0.04   -0.0608 528 LEU B CB  
3375 C CG  . LEU B 212 ? 1.8791 1.0102 1.1147 -0.1915 -0.0611 -0.0718 528 LEU B CG  
3376 C CD1 . LEU B 212 ? 1.8978 1.0109 1.121  -0.1644 -0.0508 -0.0973 528 LEU B CD1 
3377 C CD2 . LEU B 212 ? 1.8845 1.0062 1.1492 -0.1961 -0.0876 -0.0599 528 LEU B CD2 
3378 N N   . ASN B 213 ? 1.7615 1.0753 1.1063 -0.2604 -0.0428 0.0083  529 ASN B N   
3379 C CA  . ASN B 213 ? 1.7415 1.1239 1.1164 -0.2777 -0.0238 0.0293  529 ASN B CA  
3380 C C   . ASN B 213 ? 1.6929 1.1565 1.1478 -0.2602 -0.0029 0.0319  529 ASN B C   
3381 O O   . ASN B 213 ? 1.6651 1.1953 1.1568 -0.2778 0.0124  0.054   529 ASN B O   
3382 C CB  . ASN B 213 ? 1.7636 1.1348 1.137  -0.3172 -0.052  0.0608  529 ASN B CB  
3383 C CG  . ASN B 213 ? 1.8504 1.1517 1.1558 -0.3337 -0.067  0.0588  529 ASN B CG  
3384 O OD1 . ASN B 213 ? 1.8888 1.1658 1.1498 -0.3222 -0.0523 0.0415  529 ASN B OD1 
3385 N ND2 . ASN B 213 ? 1.8711 1.1368 1.1695 -0.3605 -0.0984 0.0758  529 ASN B ND2 
3386 N N   . GLY B 214 ? 1.6762 1.136  1.1627 -0.2268 -0.0029 0.0113  530 GLY B N   
3387 C CA  . GLY B 214 ? 1.6203 1.1552 1.1943 -0.2042 0.0159  0.0107  530 GLY B CA  
3388 C C   . GLY B 214 ? 1.6133 1.1459 1.1918 -0.1606 0.0418  -0.0273 530 GLY B C   
3389 O O   . GLY B 214 ? 1.6576 1.1202 1.1807 -0.1487 0.0303  -0.0486 530 GLY B O   
3390 N N   . GLU B 215 ? 1.557  1.1655 1.2021 -0.1367 0.0779  -0.0374 531 GLU B N   
3391 C CA  . GLU B 215 ? 1.5547 1.1607 1.2079 -0.0921 0.1049  -0.0787 531 GLU B CA  
3392 C C   . GLU B 215 ? 1.5662 1.1112 1.2367 -0.0682 0.0681  -0.0901 531 GLU B C   
3393 O O   . GLU B 215 ? 1.5466 1.0999 1.2796 -0.0724 0.0349  -0.0663 531 GLU B O   
3394 C CB  . GLU B 215 ? 1.518  1.2222 1.2607 -0.0675 0.1485  -0.0872 531 GLU B CB  
3395 C CG  . GLU B 215 ? 1.5767 1.2733 1.3258 -0.0187 0.179   -0.1363 531 GLU B CG  
3396 C CD  . GLU B 215 ? 1.5856 1.3689 1.4419 0.0187  0.2179  -0.1532 531 GLU B CD  
3397 O OE1 . GLU B 215 ? 1.549  1.3799 1.5123 0.0228  0.1986  -0.1276 531 GLU B OE1 
3398 O OE2 . GLU B 215 ? 1.6083 1.4089 1.4427 0.0453  0.2665  -0.194  531 GLU B OE2 
3399 N N   . ASN B 216 ? 1.5965 1.0783 1.2084 -0.0475 0.0704  -0.1231 532 ASN B N   
3400 C CA  . ASN B 216 ? 1.61   1.0296 1.2299 -0.0255 0.0378  -0.1355 532 ASN B CA  
3401 C C   . ASN B 216 ? 1.6308 0.9913 1.2196 -0.0537 -0.0111 -0.1089 532 ASN B C   
3402 O O   . ASN B 216 ? 1.6376 0.9578 1.2453 -0.0414 -0.0422 -0.1095 532 ASN B O   
3403 C CB  . ASN B 216 ? 1.5766 1.037  1.3037 0.0112  0.0379  -0.143  532 ASN B CB  
3404 C CG  . ASN B 216 ? 1.6266 1.0713 1.3574 0.0555  0.0632  -0.1892 532 ASN B CG  
3405 O OD1 . ASN B 216 ? 1.6816 1.0507 1.3657 0.0663  0.0434  -0.208  532 ASN B OD1 
3406 N ND2 . ASN B 216 ? 1.5943 1.1105 1.3818 0.0818  0.1085  -0.2097 532 ASN B ND2 
3407 N N   . ALA B 217 ? 1.6415 0.9927 1.1797 -0.0914 -0.018  -0.0872 533 ALA B N   
3408 C CA  . ALA B 217 ? 1.6712 0.965  1.1719 -0.1176 -0.0581 -0.0679 533 ALA B CA  
3409 C C   . ALA B 217 ? 1.7149 0.9361 1.1476 -0.1108 -0.0648 -0.0887 533 ALA B C   
3410 O O   . ALA B 217 ? 1.7361 0.946  1.1207 -0.1073 -0.0417 -0.1069 533 ALA B O   
3411 C CB  . ALA B 217 ? 1.6811 0.9815 1.1488 -0.1553 -0.0606 -0.0452 533 ALA B CB  
3412 N N   . LYS B 218 ? 1.7252 0.8992 1.1547 -0.1111 -0.0976 -0.0839 534 LYS B N   
3413 C CA  . LYS B 218 ? 1.765  0.8755 1.1395 -0.1062 -0.1052 -0.1001 534 LYS B CA  
3414 C C   . LYS B 218 ? 1.7878 0.8514 1.1112 -0.1357 -0.1281 -0.0851 534 LYS B C   
3415 O O   . LYS B 218 ? 1.7815 0.8463 1.1177 -0.1543 -0.1509 -0.0638 534 LYS B O   
3416 C CB  . LYS B 218 ? 1.7939 0.8861 1.2059 -0.0772 -0.119  -0.1125 534 LYS B CB  
3417 C CG  . LYS B 218 ? 1.8335 0.97   1.2987 -0.0424 -0.0916 -0.1349 534 LYS B CG  
3418 C CD  . LYS B 218 ? 1.9243 1.0212 1.373  -0.0132 -0.0853 -0.1679 534 LYS B CD  
3419 C CE  . LYS B 218 ? 1.9457 1.0867 1.441  0.0221  -0.0519 -0.1962 534 LYS B CE  
3420 N NZ  . LYS B 218 ? 2.002  1.0993 1.4548 0.0443  -0.0396 -0.2338 534 LYS B NZ  
3421 N N   . CYS B 219 ? 1.8152 0.8376 1.0815 -0.1401 -0.1223 -0.097  535 CYS B N   
3422 C CA  . CYS B 219 ? 1.8481 0.8304 1.0686 -0.1652 -0.1364 -0.0875 535 CYS B CA  
3423 C C   . CYS B 219 ? 1.8737 0.8094 1.058  -0.1617 -0.14   -0.0987 535 CYS B C   
3424 O O   . CYS B 219 ? 1.8846 0.8136 1.0565 -0.1478 -0.1265 -0.1152 535 CYS B O   
3425 C CB  . CYS B 219 ? 1.8688 0.8606 1.064  -0.1851 -0.1241 -0.082  535 CYS B CB  
3426 S SG  . CYS B 219 ? 1.9653 0.9063 1.1048 -0.2079 -0.1307 -0.0812 535 CYS B SG  
3427 N N   . ILE B 220 ? 1.8842 0.7883 1.0451 -0.1794 -0.157  -0.0886 536 ILE B N   
3428 C CA  . ILE B 220 ? 1.9073 0.7733 1.0356 -0.1825 -0.1587 -0.0945 536 ILE B CA  
3429 C C   . ILE B 220 ? 1.9187 0.7664 1.0099 -0.208  -0.1577 -0.0875 536 ILE B C   
3430 O O   . ILE B 220 ? 1.9184 0.7633 1.0019 -0.2252 -0.1702 -0.0753 536 ILE B O   
3431 C CB  . ILE B 220 ? 1.9219 0.7648 1.0636 -0.1727 -0.1787 -0.0929 536 ILE B CB  
3432 C CG1 . ILE B 220 ? 1.9617 0.7687 1.0709 -0.1817 -0.1806 -0.0946 536 ILE B CG1 
3433 C CG2 . ILE B 220 ? 1.9228 0.7674 1.0848 -0.1818 -0.2041 -0.0736 536 ILE B CG2 
3434 C CD1 . ILE B 220 ? 1.9978 0.7839 1.0785 -0.2092 -0.1922 -0.0776 536 ILE B CD1 
3435 N N   . ILE B 221 ? 1.9271 0.7626 0.9966 -0.2103 -0.143  -0.0964 537 ILE B N   
3436 C CA  . ILE B 221 ? 1.9456 0.7637 0.9863 -0.229  -0.1366 -0.0958 537 ILE B CA  
3437 C C   . ILE B 221 ? 1.9613 0.7586 0.9925 -0.2291 -0.1359 -0.0978 537 ILE B C   
3438 O O   . ILE B 221 ? 1.9649 0.76   1.0057 -0.2167 -0.1327 -0.1044 537 ILE B O   
3439 C CB  . ILE B 221 ? 1.9492 0.7728 0.9861 -0.2311 -0.1217 -0.102  537 ILE B CB  
3440 C CG1 . ILE B 221 ? 1.9475 0.7957 0.9981 -0.2332 -0.1237 -0.0962 537 ILE B CG1 
3441 C CG2 . ILE B 221 ? 1.9706 0.7734 0.9842 -0.246  -0.1135 -0.1063 537 ILE B CG2 
3442 C CD1 . ILE B 221 ? 1.9653 0.8158 1.013  -0.239  -0.1142 -0.0977 537 ILE B CD1 
3443 N N   . LYS B 222 ? 1.9698 0.7523 0.9803 -0.2458 -0.1406 -0.0905 538 LYS B N   
3444 C CA  . LYS B 222 ? 1.9795 0.7475 0.9834 -0.2511 -0.1401 -0.0876 538 LYS B CA  
3445 C C   . LYS B 222 ? 1.9971 0.7606 0.9765 -0.2682 -0.1208 -0.0911 538 LYS B C   
3446 O O   . LYS B 222 ? 2.0135 0.7725 0.965  -0.2838 -0.1188 -0.0903 538 LYS B O   
3447 C CB  . LYS B 222 ? 2.0019 0.7583 1.0031 -0.2584 -0.1635 -0.0724 538 LYS B CB  
3448 C CG  . LYS B 222 ? 2.064  0.8056 1.0648 -0.2642 -0.1691 -0.065  538 LYS B CG  
3449 C CD  . LYS B 222 ? 2.1251 0.8509 1.138  -0.2629 -0.2003 -0.0507 538 LYS B CD  
3450 C CE  . LYS B 222 ? 2.1779 0.8853 1.1797 -0.2818 -0.2118 -0.0339 538 LYS B CE  
3451 N NZ  . LYS B 222 ? 2.2027 0.8873 1.2295 -0.2718 -0.2446 -0.025  538 LYS B NZ  
3452 N N   . SER B 223 ? 1.9942 0.7588 0.9852 -0.2653 -0.1066 -0.0961 539 SER B N   
3453 C CA  . SER B 223 ? 2.0093 0.7749 0.9876 -0.2776 -0.0831 -0.1023 539 SER B CA  
3454 C C   . SER B 223 ? 2.0175 0.7856 1.0031 -0.2864 -0.0795 -0.0929 539 SER B C   
3455 O O   . SER B 223 ? 2.0138 0.7834 1.0285 -0.2768 -0.0888 -0.0883 539 SER B O   
3456 C CB  . SER B 223 ? 2.0166 0.7878 1.0166 -0.2657 -0.0667 -0.1166 539 SER B CB  
3457 O OG  . SER B 223 ? 2.045  0.8185 1.0427 -0.2731 -0.0414 -0.1258 539 SER B OG  
3458 N N   . ARG B 224 ? 2.028  0.7962 0.9837 -0.3076 -0.067  -0.0888 540 ARG B N   
3459 C CA  . ARG B 224 ? 2.031  0.8072 0.9912 -0.3223 -0.0604 -0.0761 540 ARG B CA  
3460 C C   . ARG B 224 ? 2.0315 0.8218 0.9765 -0.3343 -0.0224 -0.0884 540 ARG B C   
3461 O O   . ARG B 224 ? 2.0464 0.828  0.953  -0.3407 -0.0105 -0.1019 540 ARG B O   
3462 C CB  . ARG B 224 ? 2.069  0.8312 0.9999 -0.3424 -0.0861 -0.0535 540 ARG B CB  
3463 C CG  . ARG B 224 ? 2.1124 0.8586 1.0649 -0.3278 -0.1229 -0.0439 540 ARG B CG  
3464 C CD  . ARG B 224 ? 2.1456 0.8932 1.1398 -0.3132 -0.1286 -0.0441 540 ARG B CD  
3465 N NE  . ARG B 224 ? 2.1882 0.9154 1.1978 -0.299  -0.1613 -0.0398 540 ARG B NE  
3466 C CZ  . ARG B 224 ? 2.2104 0.935  1.2383 -0.2739 -0.1665 -0.0549 540 ARG B CZ  
3467 N NH1 . ARG B 224 ? 2.1959 0.936  1.229  -0.263  -0.1459 -0.0705 540 ARG B NH1 
3468 N NH2 . ARG B 224 ? 2.2155 0.9205 1.2556 -0.2601 -0.1923 -0.0551 540 ARG B NH2 
3469 N N   . GLY B 225 ? 2.015  0.8271 0.992  -0.3371 -0.0033 -0.085  541 GLY B N   
3470 C CA  . GLY B 225 ? 2.0199 0.8517 0.9911 -0.3455 0.039   -0.0995 541 GLY B CA  
3471 C C   . GLY B 225 ? 1.9979 0.8636 1.0252 -0.3445 0.0613  -0.0946 541 GLY B C   
3472 O O   . GLY B 225 ? 1.9821 0.8535 1.058  -0.3361 0.0403  -0.0801 541 GLY B O   
3473 N N   . ALA B 226 ? 1.9951 0.8843 1.0168 -0.3535 0.1047  -0.1081 542 ALA B N   
3474 C CA  . ALA B 226 ? 1.9713 0.9029 1.0557 -0.3525 0.1335  -0.1049 542 ALA B CA  
3475 C C   . ALA B 226 ? 1.9726 0.9194 1.0756 -0.3367 0.1793  -0.1389 542 ALA B C   
3476 O O   . ALA B 226 ? 2.002  0.9342 1.0423 -0.345  0.2021  -0.1604 542 ALA B O   
3477 C CB  . ALA B 226 ? 1.975  0.9293 1.0344 -0.3866 0.1451  -0.0814 542 ALA B CB  
3478 N N   . ALA B 227 ? 1.9411 0.9131 1.1306 -0.314  0.1899  -0.1444 543 ALA B N   
3479 C CA  . ALA B 227 ? 1.9362 0.922  1.162  -0.2934 0.2313  -0.1776 543 ALA B CA  
3480 C C   . ALA B 227 ? 1.9038 0.9483 1.2052 -0.2942 0.2684  -0.1725 543 ALA B C   
3481 O O   . ALA B 227 ? 1.8747 0.9426 1.2461 -0.2921 0.2468  -0.146  543 ALA B O   
3482 C CB  . ALA B 227 ? 1.9287 0.8915 1.2028 -0.263  0.2066  -0.1874 543 ALA B CB  
3483 N N   . MET B 228 ? 1.9074 0.9767 1.1935 -0.2988 0.3245  -0.1977 544 MET B N   
3484 C CA  . MET B 228 ? 1.8744 1.0095 1.2362 -0.2998 0.3693  -0.1952 544 MET B CA  
3485 C C   . MET B 228 ? 1.8638 1.0169 1.272  -0.2711 0.4237  -0.2402 544 MET B C   
3486 O O   . MET B 228 ? 1.893  0.9997 1.2703 -0.2517 0.4211  -0.2724 544 MET B O   
3487 C CB  . MET B 228 ? 1.8958 1.0604 1.2003 -0.3413 0.3909  -0.1739 544 MET B CB  
3488 C CG  . MET B 228 ? 1.9841 1.1157 1.1651 -0.3631 0.4083  -0.1931 544 MET B CG  
3489 S SD  . MET B 228 ? 2.0776 1.2537 1.2039 -0.4143 0.4392  -0.165  544 MET B SD  
3490 C CE  . MET B 228 ? 2.0636 1.281  1.1847 -0.4074 0.5294  -0.215  544 MET B CE  
3491 N N   . ASP B 229 ? 1.8186 1.0392 1.3096 -0.2672 0.4709  -0.2419 545 ASP B N   
3492 C CA  . ASP B 229 ? 1.8039 1.0508 1.3551 -0.2373 0.529   -0.2859 545 ASP B CA  
3493 C C   . ASP B 229 ? 1.7938 1.0051 1.418  -0.1944 0.5011  -0.3047 545 ASP B C   
3494 O O   . ASP B 229 ? 1.7607 0.9872 1.4783 -0.1824 0.4638  -0.2759 545 ASP B O   
3495 C CB  . ASP B 229 ? 1.8791 1.1125 1.3219 -0.2507 0.5846  -0.3277 545 ASP B CB  
3496 C CG  . ASP B 229 ? 1.96   1.2375 1.3392 -0.2942 0.6214  -0.3104 545 ASP B CG  
3497 O OD1 . ASP B 229 ? 1.9472 1.2706 1.3748 -0.3143 0.6063  -0.2646 545 ASP B OD1 
3498 O OD2 . ASP B 229 ? 2.0225 1.2864 1.3002 -0.3107 0.664   -0.3419 545 ASP B OD2 
3499 N N   . ASN B 230 ? 1.8228 0.9841 1.4034 -0.1749 0.514   -0.3491 546 ASN B N   
3500 C CA  . ASN B 230 ? 1.8191 0.9429 1.4664 -0.1381 0.4846  -0.3637 546 ASN B CA  
3501 C C   . ASN B 230 ? 1.8695 0.9139 1.4194 -0.1435 0.4386  -0.3683 546 ASN B C   
3502 O O   . ASN B 230 ? 1.8833 0.8832 1.4429 -0.1194 0.4325  -0.3976 546 ASN B O   
3503 C CB  . ASN B 230 ? 1.8201 0.9564 1.5325 -0.1035 0.5406  -0.4146 546 ASN B CB  
3504 C CG  . ASN B 230 ? 1.8148 1.0378 1.624  -0.0977 0.5969  -0.4148 546 ASN B CG  
3505 O OD1 . ASN B 230 ? 1.776  1.0448 1.712  -0.0842 0.5802  -0.3859 546 ASN B OD1 
3506 N ND2 . ASN B 230 ? 1.8386 1.088  1.5885 -0.1108 0.6643  -0.4458 546 ASN B ND2 
3507 N N   . SER B 231 ? 1.8915 0.9188 1.3526 -0.1755 0.4059  -0.3388 547 SER B N   
3508 C CA  . SER B 231 ? 1.9362 0.8985 1.3109 -0.1831 0.3639  -0.3394 547 SER B CA  
3509 C C   . SER B 231 ? 1.9156 0.8522 1.3437 -0.1657 0.3081  -0.3189 547 SER B C   
3510 O O   . SER B 231 ? 1.8755 0.8423 1.3933 -0.1553 0.2908  -0.2944 547 SER B O   
3511 C CB  . SER B 231 ? 1.9924 0.9474 1.2649 -0.2205 0.3481  -0.3154 547 SER B CB  
3512 O OG  . SER B 231 ? 2.0025 0.9965 1.3142 -0.2334 0.3295  -0.2741 547 SER B OG  
3513 N N   . LYS B 232 ? 1.9425 0.8234 1.3143 -0.165  0.2801  -0.3287 548 LYS B N   
3514 C CA  . LYS B 232 ? 1.937  0.79   1.343  -0.153  0.2297  -0.3108 548 LYS B CA  
3515 C C   . LYS B 232 ? 1.9636 0.7822 1.2795 -0.174  0.1929  -0.2948 548 LYS B C   
3516 O O   . LYS B 232 ? 2.0042 0.7892 1.2455 -0.1838 0.1992  -0.3151 548 LYS B O   
3517 C CB  . LYS B 232 ? 1.9657 0.7852 1.413  -0.1268 0.2346  -0.3419 548 LYS B CB  
3518 C CG  . LYS B 232 ? 1.9705 0.8233 1.5405 -0.0988 0.253   -0.348  548 LYS B CG  
3519 C CD  . LYS B 232 ? 2.0019 0.8514 1.6459 -0.0893 0.2006  -0.3135 548 LYS B CD  
3520 C CE  . LYS B 232 ? 2.0698 0.8602 1.6974 -0.0826 0.1646  -0.3186 548 LYS B CE  
3521 N NZ  . LYS B 232 ? 2.0839 0.8687 1.7506 -0.0846 0.1097  -0.2788 548 LYS B NZ  
3522 N N   . ILE B 233 ? 1.9387 0.7649 1.263  -0.1809 0.1544  -0.2598 549 ILE B N   
3523 C CA  . ILE B 233 ? 1.9592 0.7611 1.2114 -0.1977 0.1221  -0.2442 549 ILE B CA  
3524 C C   . ILE B 233 ? 1.9447 0.7265 1.2212 -0.1887 0.0817  -0.2292 549 ILE B C   
3525 O O   . ILE B 233 ? 1.919  0.7146 1.2609 -0.1779 0.0668  -0.214  549 ILE B O   
3526 C CB  . ILE B 233 ? 1.9665 0.7924 1.1936 -0.216  0.1134  -0.218  549 ILE B CB  
3527 C CG1 . ILE B 233 ? 1.9745 0.8318 1.1966 -0.2276 0.152   -0.2231 549 ILE B CG1 
3528 C CG2 . ILE B 233 ? 2.0027 0.8057 1.1567 -0.2317 0.0874  -0.2075 549 ILE B CG2 
3529 C CD1 . ILE B 233 ? 2.024  0.8669 1.1745 -0.241  0.1815  -0.2475 549 ILE B CD1 
3530 N N   . SER B 234 ? 1.9599 0.711  1.183  -0.1965 0.0627  -0.2305 550 SER B N   
3531 C CA  . SER B 234 ? 1.9556 0.6918 1.1888 -0.1942 0.0262  -0.213  550 SER B CA  
3532 C C   . SER B 234 ? 1.9704 0.7006 1.1383 -0.2106 0.0087  -0.2013 550 SER B C   
3533 O O   . SER B 234 ? 1.9959 0.7077 1.1152 -0.2206 0.0139  -0.2139 550 SER B O   
3534 C CB  . SER B 234 ? 1.9738 0.6779 1.2279 -0.1846 0.021   -0.2279 550 SER B CB  
3535 O OG  . SER B 234 ? 2.0006 0.695  1.2659 -0.1865 -0.0147 -0.2053 550 SER B OG  
3536 N N   . LEU B 235 ? 1.9532 0.6986 1.1211 -0.2135 -0.0121 -0.1786 551 LEU B N   
3537 C CA  . LEU B 235 ? 1.9652 0.7108 1.0846 -0.2248 -0.0268 -0.1682 551 LEU B CA  
3538 C C   . LEU B 235 ? 1.9619 0.7075 1.0868 -0.2235 -0.052  -0.1524 551 LEU B C   
3539 O O   . LEU B 235 ? 1.959  0.7162 1.1009 -0.2194 -0.0633 -0.1396 551 LEU B O   
3540 C CB  . LEU B 235 ? 1.9644 0.7279 1.0721 -0.2296 -0.0257 -0.1584 551 LEU B CB  
3541 C CG  . LEU B 235 ? 1.9797 0.7518 1.0847 -0.2349 -0.0007 -0.1668 551 LEU B CG  
3542 C CD1 . LEU B 235 ? 1.9827 0.7711 1.0926 -0.2396 -0.0074 -0.1506 551 LEU B CD1 
3543 C CD2 . LEU B 235 ? 2.0084 0.767  1.0595 -0.2487 0.0111  -0.1789 551 LEU B CD2 
3544 N N   . LYS B 236 ? 1.9614 0.6941 1.0679 -0.2297 -0.061  -0.1526 552 LYS B N   
3545 C CA  A LYS B 236 ? 1.9605 0.6981 1.0675 -0.2328 -0.0812 -0.1362 552 LYS B CA  
3546 C CA  B LYS B 236 ? 1.9614 0.6992 1.0683 -0.2328 -0.0812 -0.1361 552 LYS B CA  
3547 C C   . LYS B 236 ? 1.9692 0.7209 1.0425 -0.2409 -0.0859 -0.1298 552 LYS B C   
3548 O O   . LYS B 236 ? 1.98   0.7235 1.0331 -0.2505 -0.0867 -0.1336 552 LYS B O   
3549 C CB  A LYS B 236 ? 1.9819 0.6971 1.1012 -0.2366 -0.0902 -0.1369 552 LYS B CB  
3550 C CB  B LYS B 236 ? 1.9852 0.7011 1.1051 -0.2365 -0.0908 -0.1361 552 LYS B CB  
3551 C CG  A LYS B 236 ? 2.0168 0.7368 1.1453 -0.242  -0.1111 -0.1158 552 LYS B CG  
3552 C CG  B LYS B 236 ? 2.0211 0.7203 1.1849 -0.2252 -0.0868 -0.1449 552 LYS B CG  
3553 C CD  A LYS B 236 ? 2.0596 0.7517 1.203  -0.2485 -0.1245 -0.1137 552 LYS B CD  
3554 C CD  B LYS B 236 ? 2.0693 0.74   1.2516 -0.2281 -0.1024 -0.1431 552 LYS B CD  
3555 C CE  A LYS B 236 ? 2.0886 0.7864 1.2353 -0.2602 -0.1468 -0.0876 552 LYS B CE  
3556 C CE  B LYS B 236 ? 2.0945 0.7474 1.3304 -0.2126 -0.0973 -0.1554 552 LYS B CE  
3557 N NZ  A LYS B 236 ? 2.1153 0.7852 1.27   -0.2721 -0.1639 -0.0814 552 LYS B NZ  
3558 N NZ  B LYS B 236 ? 2.1196 0.7392 1.3801 -0.2146 -0.1192 -0.1507 552 LYS B NZ  
3559 N N   . LEU B 237 ? 1.9623 0.7334 1.0323 -0.2366 -0.0901 -0.1214 553 LEU B N   
3560 C CA  . LEU B 237 ? 1.9672 0.7551 1.0185 -0.2393 -0.0938 -0.1165 553 LEU B CA  
3561 C C   . LEU B 237 ? 1.9579 0.7651 1.0121 -0.2379 -0.1008 -0.1058 553 LEU B C   
3562 O O   . LEU B 237 ? 1.958  0.7668 1.0163 -0.2319 -0.103  -0.1038 553 LEU B O   
3563 C CB  . LEU B 237 ? 1.9754 0.767  1.0215 -0.2335 -0.0913 -0.1192 553 LEU B CB  
3564 C CG  . LEU B 237 ? 2.0036 0.7815 1.0447 -0.2374 -0.0807 -0.1272 553 LEU B CG  
3565 C CD1 . LEU B 237 ? 2.0114 0.7928 1.0506 -0.2349 -0.083  -0.1237 553 LEU B CD1 
3566 C CD2 . LEU B 237 ? 2.0215 0.7887 1.0377 -0.2501 -0.0774 -0.1325 553 LEU B CD2 
3567 N N   . LYS B 238 ? 1.9478 0.771  0.9984 -0.2457 -0.104  -0.0983 554 LYS B N   
3568 C CA  . LYS B 238 ? 1.9378 0.7856 0.9898 -0.2478 -0.1054 -0.0874 554 LYS B CA  
3569 C C   . LYS B 238 ? 1.9313 0.8131 0.9873 -0.2452 -0.1015 -0.084  554 LYS B C   
3570 O O   . LYS B 238 ? 1.9271 0.8135 0.9891 -0.2505 -0.1055 -0.0817 554 LYS B O   
3571 C CB  . LYS B 238 ? 1.9417 0.7821 0.9978 -0.2633 -0.1135 -0.0755 554 LYS B CB  
3572 C CG  . LYS B 238 ? 1.9622 0.83   1.0153 -0.2725 -0.1145 -0.0594 554 LYS B CG  
3573 C CD  . LYS B 238 ? 2.0095 0.8633 1.0682 -0.2916 -0.1282 -0.0436 554 LYS B CD  
3574 C CE  . LYS B 238 ? 2.0411 0.9185 1.0915 -0.3061 -0.1311 -0.0228 554 LYS B CE  
3575 N NZ  . LYS B 238 ? 2.0656 0.9221 1.124  -0.327  -0.1506 -0.0037 554 LYS B NZ  
3576 N N   . ILE B 239 ? 1.9273 0.8327 0.9809 -0.2369 -0.094  -0.0845 555 ILE B N   
3577 C CA  . ILE B 239 ? 1.9149 0.8593 0.9827 -0.2307 -0.0858 -0.0833 555 ILE B CA  
3578 C C   . ILE B 239 ? 1.9095 0.886  0.9715 -0.2379 -0.0751 -0.0747 555 ILE B C   
3579 O O   . ILE B 239 ? 1.9195 0.8863 0.9569 -0.2377 -0.0724 -0.0777 555 ILE B O   
3580 C CB  . ILE B 239 ? 1.918  0.8634 0.9917 -0.2092 -0.0823 -0.0983 555 ILE B CB  
3581 C CG1 . ILE B 239 ? 1.9385 0.8542 1.0141 -0.2079 -0.0944 -0.1015 555 ILE B CG1 
3582 C CG2 . ILE B 239 ? 1.9004 0.8903 1.0023 -0.2    -0.0728 -0.0977 555 ILE B CG2 
3583 C CD1 . ILE B 239 ? 1.9512 0.8639 1.0387 -0.1896 -0.0985 -0.1109 555 ILE B CD1 
3584 N N   . GLU B 240 ? 1.8919 0.9074 0.975  -0.2474 -0.0704 -0.0616 556 GLU B N   
3585 C CA  . GLU B 240 ? 1.8926 0.9484 0.9714 -0.2571 -0.056  -0.051  556 GLU B CA  
3586 C C   . GLU B 240 ? 1.8684 0.9744 0.9739 -0.24   -0.0353 -0.0597 556 GLU B C   
3587 O O   . GLU B 240 ? 1.8467 0.9781 0.9927 -0.2386 -0.0382 -0.053  556 GLU B O   
3588 C CB  . GLU B 240 ? 1.9306 0.9985 1.0208 -0.2848 -0.066  -0.0252 556 GLU B CB  
3589 C CG  . GLU B 240 ? 2.0525 1.0707 1.1235 -0.3003 -0.0865 -0.0173 556 GLU B CG  
3590 C CD  . GLU B 240 ? 2.1684 1.1927 1.2483 -0.3293 -0.0997 0.0089  556 GLU B CD  
3591 O OE1 . GLU B 240 ? 2.1707 1.2458 1.2638 -0.342  -0.0894 0.0256  556 GLU B OE1 
3592 O OE2 . GLU B 240 ? 2.2254 1.2041 1.3019 -0.3393 -0.12   0.0127  556 GLU B OE2 
3593 N N   . GLY B 241 ? 1.8705 0.9884 0.9545 -0.2268 -0.0158 -0.0756 557 GLY B N   
3594 C CA  . GLY B 241 ? 1.8517 1.0164 0.9616 -0.2059 0.0091  -0.0902 557 GLY B CA  
3595 C C   . GLY B 241 ? 1.8361 1.0586 0.946  -0.2227 0.0327  -0.076  557 GLY B C   
3596 O O   . GLY B 241 ? 1.8463 1.074  0.9111 -0.2269 0.0501  -0.0834 557 GLY B O   
3597 N N   . ASN B 242 ? 1.811  1.0755 0.9674 -0.2371 0.0306  -0.0526 558 ASN B N   
3598 C CA  . ASN B 242 ? 1.7979 1.122  0.9617 -0.2604 0.0497  -0.0306 558 ASN B CA  
3599 C C   . ASN B 242 ? 1.7667 1.1704 0.9811 -0.2445 0.0853  -0.0374 558 ASN B C   
3600 O O   . ASN B 242 ? 1.7493 1.2107 0.9678 -0.2645 0.1077  -0.0199 558 ASN B O   
3601 C CB  . ASN B 242 ? 1.799  1.1193 0.9832 -0.2919 0.0224  0.0034  558 ASN B CB  
3602 C CG  . ASN B 242 ? 1.8644 1.113  1.0031 -0.3075 -0.0069 0.0092  558 ASN B CG  
3603 O OD1 . ASN B 242 ? 1.9059 1.1255 0.9952 -0.3085 -0.0047 0.0015  558 ASN B OD1 
3604 N ND2 . ASN B 242 ? 1.8673 1.0849 1.0227 -0.32   -0.0355 0.0219  558 ASN B ND2 
3605 N N   . ALA B 243 ? 1.7549 1.1641 1.0115 -0.2094 0.0908  -0.0612 559 ALA B N   
3606 C CA  . ALA B 243 ? 1.7161 1.2023 1.0365 -0.1888 0.1243  -0.0699 559 ALA B CA  
3607 C C   . ALA B 243 ? 1.733  1.2093 1.0483 -0.1471 0.1475  -0.1136 559 ALA B C   
3608 O O   . ALA B 243 ? 1.7712 1.1774 1.0497 -0.1333 0.1269  -0.1327 559 ALA B O   
3609 C CB  . ALA B 243 ? 1.6768 1.1908 1.0822 -0.1876 0.1028  -0.0493 559 ALA B CB  
3610 N N   . PRO B 244 ? 1.7021 1.2475 1.0562 -0.1264 0.1907  -0.1311 560 PRO B N   
3611 C CA  . PRO B 244 ? 1.7116 1.2402 1.061  -0.0841 0.2119  -0.1777 560 PRO B CA  
3612 C C   . PRO B 244 ? 1.7076 1.1982 1.1133 -0.0535 0.1806  -0.1882 560 PRO B C   
3613 O O   . PRO B 244 ? 1.6753 1.1912 1.156  -0.0552 0.1594  -0.1636 560 PRO B O   
3614 C CB  . PRO B 244 ? 1.6739 1.2956 1.0684 -0.0695 0.2673  -0.1912 560 PRO B CB  
3615 C CG  . PRO B 244 ? 1.634  1.3268 1.0941 -0.0967 0.2655  -0.1473 560 PRO B CG  
3616 C CD  . PRO B 244 ? 1.6486 1.2908 1.0547 -0.1401 0.2237  -0.1108 560 PRO B CD  
3617 N N   . TYR B 245 ? 1.7425 1.1661 1.105  -0.0306 0.1724  -0.2211 561 TYR B N   
3618 C CA  . TYR B 245 ? 1.7515 1.1253 1.1506 -0.0027 0.1411  -0.234  561 TYR B CA  
3619 C C   . TYR B 245 ? 1.7569 1.0799 1.1494 -0.0261 0.0908  -0.2026 561 TYR B C   
3620 O O   . TYR B 245 ? 1.7602 1.0471 1.1854 -0.01   0.0614  -0.2046 561 TYR B O   
3621 C CB  . TYR B 245 ? 1.7111 1.1393 1.2155 0.0335  0.1552  -0.2453 561 TYR B CB  
3622 C CG  . TYR B 245 ? 1.7228 1.1954 1.2273 0.0606  0.2102  -0.2848 561 TYR B CG  
3623 C CD1 . TYR B 245 ? 1.7827 1.1996 1.2239 0.0826  0.2214  -0.3291 561 TYR B CD1 
3624 C CD2 . TYR B 245 ? 1.6921 1.2619 1.2491 0.059   0.2526  -0.2773 561 TYR B CD2 
3625 C CE1 . TYR B 245 ? 1.7924 1.2449 1.2193 0.1056  0.2747  -0.3701 561 TYR B CE1 
3626 C CE2 . TYR B 245 ? 1.6969 1.3113 1.2454 0.0818  0.31    -0.316  561 TYR B CE2 
3627 C CZ  . TYR B 245 ? 1.7555 1.3086 1.2348 0.1058  0.3218  -0.3647 561 TYR B CZ  
3628 O OH  . TYR B 245 ? 1.7705 1.3619 1.2308 0.1283  0.3805  -0.4084 561 TYR B OH  
3629 N N   . SER B 246 ? 1.7582 1.0726 1.1031 -0.064  0.0809  -0.1758 562 SER B N   
3630 C CA  . SER B 246 ? 1.7687 1.0324 1.0984 -0.0851 0.0397  -0.1528 562 SER B CA  
3631 C C   . SER B 246 ? 1.8013 0.99   1.0689 -0.0802 0.0246  -0.1712 562 SER B C   
3632 O O   . SER B 246 ? 1.8249 0.9982 1.0361 -0.0814 0.0407  -0.1877 562 SER B O   
3633 C CB  . SER B 246 ? 1.7856 1.0623 1.0919 -0.1235 0.0346  -0.1222 562 SER B CB  
3634 O OG  . SER B 246 ? 1.841  1.1053 1.08   -0.1372 0.0505  -0.1279 562 SER B OG  
3635 N N   . LYS B 247 ? 1.8002 0.9439 1.0785 -0.0765 -0.0074 -0.167  563 LYS B N   
3636 C CA  . LYS B 247 ? 1.8323 0.9096 1.0625 -0.0736 -0.0238 -0.1805 563 LYS B CA  
3637 C C   . LYS B 247 ? 1.8387 0.8786 1.0478 -0.0987 -0.0516 -0.1583 563 LYS B C   
3638 O O   . LYS B 247 ? 1.8263 0.8763 1.0669 -0.1083 -0.0676 -0.1388 563 LYS B O   
3639 C CB  . LYS B 247 ? 1.855  0.9084 1.1169 -0.0425 -0.0344 -0.2008 563 LYS B CB  
3640 C CG  . LYS B 247 ? 1.8909 0.9756 1.1781 -0.011  -0.0048 -0.2309 563 LYS B CG  
3641 C CD  . LYS B 247 ? 1.9812 1.0529 1.1989 -0.0123 0.0195  -0.2548 563 LYS B CD  
3642 C CE  . LYS B 247 ? 2.0229 1.1118 1.2532 0.0214  0.0493  -0.2931 563 LYS B CE  
3643 N NZ  . LYS B 247 ? 2.0683 1.0975 1.3059 0.0483  0.0278  -0.3183 563 LYS B NZ  
3644 N N   . GLY B 248 ? 1.8567 0.8538 1.0143 -0.1089 -0.0576 -0.1622 564 GLY B N   
3645 C CA  . GLY B 248 ? 1.8694 0.8332 1.0088 -0.1297 -0.0778 -0.146  564 GLY B CA  
3646 C C   . GLY B 248 ? 1.8896 0.8035 0.9977 -0.1284 -0.0898 -0.1549 564 GLY B C   
3647 O O   . GLY B 248 ? 1.9021 0.803  0.986  -0.1196 -0.0832 -0.1712 564 GLY B O   
3648 N N   . HIS B 249 ? 1.893  0.7796 0.9995 -0.1396 -0.1077 -0.1438 565 HIS B N   
3649 C CA  . HIS B 249 ? 1.9159 0.7618 0.9999 -0.1425 -0.1188 -0.1473 565 HIS B CA  
3650 C C   . HIS B 249 ? 1.9163 0.7488 0.99   -0.1632 -0.1244 -0.133  565 HIS B C   
3651 O O   . HIS B 249 ? 1.9102 0.745  0.9925 -0.1721 -0.1315 -0.1221 565 HIS B O   
3652 C CB  . HIS B 249 ? 1.9398 0.7604 1.037  -0.1277 -0.1351 -0.1548 565 HIS B CB  
3653 C CG  . HIS B 249 ? 2.0055 0.7866 1.0819 -0.1335 -0.1479 -0.1562 565 HIS B CG  
3654 N ND1 . HIS B 249 ? 2.0477 0.8137 1.1    -0.1296 -0.145  -0.1696 565 HIS B ND1 
3655 C CD2 . HIS B 249 ? 2.0309 0.7874 1.1081 -0.1454 -0.1648 -0.1437 565 HIS B CD2 
3656 C CE1 . HIS B 249 ? 2.0671 0.801  1.1131 -0.1383 -0.1618 -0.1641 565 HIS B CE1 
3657 N NE2 . HIS B 249 ? 2.0599 0.7893 1.1215 -0.1479 -0.1722 -0.1484 565 HIS B NE2 
3658 N N   . ILE B 250 ? 1.9249 0.743  0.9804 -0.1713 -0.1215 -0.1334 566 ILE B N   
3659 C CA  . ILE B 250 ? 1.9353 0.742  0.9859 -0.1875 -0.1216 -0.1244 566 ILE B CA  
3660 C C   . ILE B 250 ? 1.951  0.7327 1.0005 -0.1884 -0.1318 -0.1241 566 ILE B C   
3661 O O   . ILE B 250 ? 1.9562 0.7256 1.0017 -0.1819 -0.1375 -0.1303 566 ILE B O   
3662 C CB  . ILE B 250 ? 1.9387 0.7505 0.9842 -0.1957 -0.1124 -0.1224 566 ILE B CB  
3663 C CG1 . ILE B 250 ? 1.9424 0.7787 0.9885 -0.1977 -0.1052 -0.1196 566 ILE B CG1 
3664 C CG2 . ILE B 250 ? 1.9444 0.7454 0.9921 -0.208  -0.1085 -0.1183 566 ILE B CG2 
3665 C CD1 . ILE B 250 ? 1.9595 0.7967 0.9996 -0.2059 -0.1022 -0.1149 566 ILE B CD1 
3666 N N   . ASP B 251 ? 1.9574 0.731  1.0072 -0.1993 -0.1357 -0.1155 567 ASP B N   
3667 C CA  . ASP B 251 ? 1.9719 0.7267 1.0236 -0.2054 -0.145  -0.1101 567 ASP B CA  
3668 C C   . ASP B 251 ? 1.9762 0.7361 1.0261 -0.2215 -0.1312 -0.104  567 ASP B C   
3669 O O   . ASP B 251 ? 1.9858 0.7499 1.0232 -0.2321 -0.1253 -0.1003 567 ASP B O   
3670 C CB  . ASP B 251 ? 2.0003 0.7423 1.0536 -0.2059 -0.1626 -0.103  567 ASP B CB  
3671 C CG  . ASP B 251 ? 2.0833 0.8019 1.1408 -0.2102 -0.1784 -0.0971 567 ASP B CG  
3672 O OD1 . ASP B 251 ? 2.0883 0.8083 1.1476 -0.2226 -0.1716 -0.0912 567 ASP B OD1 
3673 O OD2 . ASP B 251 ? 2.1334 0.8323 1.1975 -0.2012 -0.1988 -0.0979 567 ASP B OD2 
3674 N N   . CYS B 252 ? 1.9666 0.7264 1.0297 -0.2235 -0.126  -0.1039 568 CYS B N   
3675 C CA  . CYS B 252 ? 1.9622 0.7314 1.0335 -0.2345 -0.1079 -0.102  568 CYS B CA  
3676 C C   . CYS B 252 ? 1.9552 0.7246 1.0456 -0.2434 -0.1094 -0.0923 568 CYS B C   
3677 O O   . CYS B 252 ? 1.9558 0.7174 1.0613 -0.2392 -0.1251 -0.0889 568 CYS B O   
3678 C CB  . CYS B 252 ? 1.9643 0.741  1.0483 -0.2285 -0.0969 -0.1094 568 CYS B CB  
3679 S SG  . CYS B 252 ? 2.0145 0.8001 1.1112 -0.2361 -0.0702 -0.1152 568 CYS B SG  
3680 N N   . ALA B 253 ? 1.9482 0.727  1.0356 -0.2581 -0.0936 -0.0873 569 ALA B N   
3681 C CA  . ALA B 253 ? 1.9402 0.7277 1.0505 -0.2702 -0.0913 -0.0749 569 ALA B CA  
3682 C C   . ALA B 253 ? 1.9301 0.7396 1.0455 -0.2802 -0.0582 -0.0788 569 ALA B C   
3683 O O   . ALA B 253 ? 1.9433 0.7511 1.0215 -0.2905 -0.0458 -0.0825 569 ALA B O   
3684 C CB  . ALA B 253 ? 1.9564 0.7293 1.0491 -0.283  -0.1117 -0.0596 569 ALA B CB  
3685 N N   . GLU B 254 ? 1.9077 0.7375 1.0693 -0.2772 -0.044  -0.079  570 GLU B N   
3686 C CA  . GLU B 254 ? 1.9055 0.7596 1.0803 -0.2822 -0.0067 -0.0879 570 GLU B CA  
3687 C C   . GLU B 254 ? 1.8833 0.7678 1.1142 -0.2888 0.0039  -0.0752 570 GLU B C   
3688 O O   . GLU B 254 ? 1.8664 0.7567 1.1487 -0.2783 -0.0097 -0.07   570 GLU B O   
3689 C CB  . GLU B 254 ? 1.9358 0.7869 1.1232 -0.2641 0.0069  -0.109  570 GLU B CB  
3690 C CG  . GLU B 254 ? 2.0053 0.8733 1.1997 -0.2651 0.0478  -0.1268 570 GLU B CG  
3691 C CD  . GLU B 254 ? 2.134  0.9874 1.259  -0.2778 0.0633  -0.1398 570 GLU B CD  
3692 O OE1 . GLU B 254 ? 2.1788 1.0093 1.2584 -0.2829 0.0388  -0.1342 570 GLU B OE1 
3693 O OE2 . GLU B 254 ? 2.1609 1.0259 1.2776 -0.2826 0.0997  -0.1565 570 GLU B OE2 
3694 N N   . ILE B 255 ? 1.8833 0.7894 1.1052 -0.3089 0.027   -0.0677 571 ILE B N   
3695 C CA  . ILE B 255 ? 1.864  0.8086 1.1449 -0.3185 0.0414  -0.0528 571 ILE B CA  
3696 C C   . ILE B 255 ? 1.8477 0.8256 1.1784 -0.3047 0.0833  -0.0724 571 ILE B C   
3697 O O   . ILE B 255 ? 1.8614 0.835  1.1577 -0.2999 0.1128  -0.0967 571 ILE B O   
3698 C CB  . ILE B 255 ? 1.8809 0.8377 1.1308 -0.3501 0.0477  -0.032  571 ILE B CB  
3699 C CG1 . ILE B 255 ? 1.9231 0.8408 1.1347 -0.36   0.0006  -0.013  571 ILE B CG1 
3700 C CG2 . ILE B 255 ? 1.8486 0.854  1.1643 -0.3638 0.0665  -0.0136 571 ILE B CG2 
3701 C CD1 . ILE B 255 ? 1.9547 0.8726 1.1257 -0.3923 -0.0018 0.0093  571 ILE B CD1 
3702 N N   . VAL B 256 ? 1.8158 0.824  1.2305 -0.2975 0.0832  -0.0624 572 VAL B N   
3703 C CA  . VAL B 256 ? 1.7918 0.836  1.2757 -0.2808 0.1207  -0.0789 572 VAL B CA  
3704 C C   . VAL B 256 ? 1.7667 0.8689 1.3093 -0.2966 0.1502  -0.0629 572 VAL B C   
3705 O O   . VAL B 256 ? 1.7522 0.8693 1.3374 -0.3096 0.1232  -0.0325 572 VAL B O   
3706 C CB  . VAL B 256 ? 1.7769 0.8122 1.3263 -0.2568 0.0937  -0.079  572 VAL B CB  
3707 C CG1 . VAL B 256 ? 1.7391 0.8124 1.3759 -0.2374 0.1291  -0.0939 572 VAL B CG1 
3708 C CG2 . VAL B 256 ? 1.8187 0.8032 1.3113 -0.2443 0.0686  -0.0928 572 VAL B CG2 
3709 N N   . LYS B 257 ? 1.757  0.8921 1.3008 -0.2966 0.2064  -0.084  573 LYS B N   
3710 C CA  . LYS B 257 ? 1.7196 0.9206 1.3246 -0.3098 0.2467  -0.0731 573 LYS B CA  
3711 C C   . LYS B 257 ? 1.692  0.928  1.3575 -0.2839 0.3011  -0.1071 573 LYS B C   
3712 O O   . LYS B 257 ? 1.7205 0.9231 1.345  -0.265  0.3156  -0.1423 573 LYS B O   
3713 C CB  . LYS B 257 ? 1.7624 0.975  1.2932 -0.3474 0.2651  -0.0589 573 LYS B CB  
3714 C CG  . LYS B 257 ? 1.8006 1.0348 1.3664 -0.375  0.2339  -0.0131 573 LYS B CG  
3715 C CD  . LYS B 257 ? 1.7945 1.103  1.4788 -0.3748 0.2618  0.0009  573 LYS B CD  
3716 C CE  . LYS B 257 ? 1.816  1.1344 1.5608 -0.392  0.2132  0.0447  573 LYS B CE  
3717 N NZ  . LYS B 257 ? 1.7755 1.1738 1.6427 -0.3938 0.2426  0.0603  573 LYS B NZ  
3718 N N   . GLY B 258 ? 1.6338 0.9361 1.4024 -0.2822 0.3291  -0.0967 574 GLY B N   
3719 C CA  . GLY B 258 ? 1.5992 0.9411 1.4459 -0.2534 0.3824  -0.1295 574 GLY B CA  
3720 C C   . GLY B 258 ? 1.5902 0.8991 1.4959 -0.2157 0.3534  -0.1445 574 GLY B C   
3721 O O   . GLY B 258 ? 1.5857 0.8757 1.528  -0.2137 0.2961  -0.1167 574 GLY B O   
3722 N N   . ASN B 259 ? 1.5899 0.8863 1.4982 -0.1879 0.39    -0.1886 575 ASN B N   
3723 C CA  . ASN B 259 ? 1.5853 0.8471 1.5511 -0.153  0.3625  -0.2029 575 ASN B CA  
3724 C C   . ASN B 259 ? 1.6389 0.82   1.4965 -0.1519 0.3285  -0.2173 575 ASN B C   
3725 O O   . ASN B 259 ? 1.6474 0.7939 1.5269 -0.1253 0.3212  -0.2407 575 ASN B O   
3726 C CB  . ASN B 259 ? 1.5706 0.8617 1.623  -0.1184 0.4172  -0.2432 575 ASN B CB  
3727 C CG  . ASN B 259 ? 1.5679 0.9438 1.6945 -0.1198 0.4827  -0.2489 575 ASN B CG  
3728 O OD1 . ASN B 259 ? 1.5662 0.9931 1.7093 -0.1479 0.4848  -0.2136 575 ASN B OD1 
3729 N ND2 . ASN B 259 ? 1.5518 0.9454 1.7294 -0.0887 0.5389  -0.2948 575 ASN B ND2 
3730 N N   . ALA B 260 ? 1.6691 0.8216 1.4168 -0.1808 0.3075  -0.2026 576 ALA B N   
3731 C CA  . ALA B 260 ? 1.7154 0.8008 1.3675 -0.1817 0.2773  -0.2134 576 ALA B CA  
3732 C C   . ALA B 260 ? 1.7078 0.7608 1.3921 -0.1695 0.2192  -0.1945 576 ALA B C   
3733 O O   . ALA B 260 ? 1.6794 0.7529 1.4266 -0.1719 0.1892  -0.1637 576 ALA B O   
3734 C CB  . ALA B 260 ? 1.757  0.8263 1.301  -0.2141 0.2671  -0.1988 576 ALA B CB  
3735 N N   . GLU B 261 ? 1.7328 0.7346 1.3721 -0.1589 0.2025  -0.2122 577 GLU B N   
3736 C CA  . GLU B 261 ? 1.7365 0.7057 1.3921 -0.1512 0.1497  -0.1946 577 GLU B CA  
3737 C C   . GLU B 261 ? 1.7793 0.7042 1.3289 -0.1659 0.1242  -0.1925 577 GLU B C   
3738 O O   . GLU B 261 ? 1.8107 0.7134 1.2943 -0.1693 0.1443  -0.2164 577 GLU B O   
3739 C CB  . GLU B 261 ? 1.7482 0.7005 1.4701 -0.1234 0.1499  -0.2138 577 GLU B CB  
3740 C CG  . GLU B 261 ? 1.8025 0.7252 1.5481 -0.1192 0.0938  -0.19   577 GLU B CG  
3741 C CD  . GLU B 261 ? 1.8904 0.7606 1.5984 -0.1117 0.0771  -0.2051 577 GLU B CD  
3742 O OE1 . GLU B 261 ? 1.9369 0.7793 1.55   -0.1264 0.0707  -0.2088 577 GLU B OE1 
3743 O OE2 . GLU B 261 ? 1.8962 0.7532 1.6752 -0.092  0.0671  -0.2103 577 GLU B OE2 
3744 N N   . VAL B 262 ? 1.7773 0.6906 1.3104 -0.1755 0.0806  -0.1647 578 VAL B N   
3745 C CA  . VAL B 262 ? 1.8137 0.6925 1.2599 -0.1867 0.0574  -0.1618 578 VAL B CA  
3746 C C   . VAL B 262 ? 1.8195 0.6736 1.2739 -0.1812 0.0157  -0.1478 578 VAL B C   
3747 O O   . VAL B 262 ? 1.7996 0.663  1.3072 -0.1786 -0.0082 -0.1284 578 VAL B O   
3748 C CB  . VAL B 262 ? 1.8318 0.7194 1.2305 -0.2068 0.0504  -0.145  578 VAL B CB  
3749 C CG1 . VAL B 262 ? 1.8728 0.729  1.198  -0.2141 0.0243  -0.1411 578 VAL B CG1 
3750 C CG2 . VAL B 262 ? 1.838  0.7472 1.2142 -0.2185 0.09    -0.1554 578 VAL B CG2 
3751 N N   . GLU B 263 ? 1.846  0.6695 1.2456 -0.1827 0.0057  -0.1556 579 GLU B N   
3752 C CA  . GLU B 263 ? 1.8599 0.6623 1.2548 -0.1822 -0.0302 -0.1414 579 GLU B CA  
3753 C C   . GLU B 263 ? 1.8934 0.6818 1.2112 -0.1939 -0.0411 -0.1388 579 GLU B C   
3754 O O   . GLU B 263 ? 1.9117 0.6889 1.1878 -0.1973 -0.0271 -0.1535 579 GLU B O   
3755 C CB  . GLU B 263 ? 1.8866 0.668  1.3123 -0.1706 -0.0317 -0.1524 579 GLU B CB  
3756 C CG  . GLU B 263 ? 1.9604 0.7215 1.3812 -0.1747 -0.0698 -0.1331 579 GLU B CG  
3757 C CD  . GLU B 263 ? 2.0428 0.7807 1.5081 -0.1643 -0.0776 -0.1387 579 GLU B CD  
3758 O OE1 . GLU B 263 ? 2.0366 0.7735 1.5613 -0.1595 -0.1023 -0.1211 579 GLU B OE1 
3759 O OE2 . GLU B 263 ? 2.0932 0.8104 1.5355 -0.1617 -0.0623 -0.1601 579 GLU B OE2 
3760 N N   . SER B 264 ? 1.9011 0.6903 1.2011 -0.2    -0.0659 -0.1213 580 SER B N   
3761 C CA  . SER B 264 ? 1.9343 0.7157 1.1727 -0.2074 -0.0746 -0.1197 580 SER B CA  
3762 C C   . SER B 264 ? 1.9475 0.7177 1.1741 -0.209  -0.0987 -0.109  580 SER B C   
3763 O O   . SER B 264 ? 1.941  0.7099 1.1871 -0.2098 -0.119  -0.0954 580 SER B O   
3764 C CB  . SER B 264 ? 1.9606 0.7501 1.1805 -0.2127 -0.0795 -0.1128 580 SER B CB  
3765 O OG  . SER B 264 ? 2.0118 0.7953 1.182  -0.2159 -0.0857 -0.1139 580 SER B OG  
3766 N N   . ILE B 265 ? 1.9649 0.7277 1.1595 -0.2126 -0.0976 -0.113  581 ILE B N   
3767 C CA  . ILE B 265 ? 1.9817 0.739  1.1617 -0.2182 -0.1166 -0.1009 581 ILE B CA  
3768 C C   . ILE B 265 ? 2.0035 0.7701 1.1368 -0.2233 -0.1148 -0.1012 581 ILE B C   
3769 O O   . ILE B 265 ? 2.0121 0.7781 1.1307 -0.228  -0.11   -0.1042 581 ILE B O   
3770 C CB  . ILE B 265 ? 1.984  0.7252 1.187  -0.2195 -0.1223 -0.0993 581 ILE B CB  
3771 C CG1 . ILE B 265 ? 1.9786 0.7121 1.2399 -0.2089 -0.1179 -0.1052 581 ILE B CG1 
3772 C CG2 . ILE B 265 ? 1.9936 0.7311 1.1858 -0.2298 -0.1462 -0.0792 581 ILE B CG2 
3773 C CD1 . ILE B 265 ? 1.9951 0.7243 1.2611 -0.202  -0.0897 -0.1294 581 ILE B CD1 
3774 N N   . PRO B 266 ? 2.0088 0.7836 1.1224 -0.2218 -0.1199 -0.0987 582 PRO B N   
3775 C CA  . PRO B 266 ? 2.0149 0.8023 1.0958 -0.2221 -0.1158 -0.1015 582 PRO B CA  
3776 C C   . PRO B 266 ? 2.0123 0.8092 1.0727 -0.2277 -0.123  -0.0928 582 PRO B C   
3777 O O   . PRO B 266 ? 2.0256 0.8223 1.0688 -0.2264 -0.1296 -0.0922 582 PRO B O   
3778 C CB  . PRO B 266 ? 2.0304 0.8171 1.1048 -0.2152 -0.1165 -0.1073 582 PRO B CB  
3779 C CG  . PRO B 266 ? 2.0336 0.8092 1.1284 -0.2156 -0.1277 -0.1019 582 PRO B CG  
3780 C CD  . PRO B 266 ? 2.0042 0.7755 1.1281 -0.2192 -0.1301 -0.0951 582 PRO B CD  
3781 N N   . ILE B 267 ? 1.9934 0.7984 1.0512 -0.2362 -0.1212 -0.0863 583 ILE B N   
3782 C CA  . ILE B 267 ? 1.9859 0.8059 1.0242 -0.2463 -0.1251 -0.0743 583 ILE B CA  
3783 C C   . ILE B 267 ? 1.9706 0.8195 0.989  -0.2418 -0.1121 -0.08   583 ILE B C   
3784 O O   . ILE B 267 ? 1.9667 0.8281 0.9944 -0.2369 -0.1039 -0.0857 583 ILE B O   
3785 C CB  . ILE B 267 ? 1.9917 0.8084 1.0405 -0.2608 -0.1319 -0.0606 583 ILE B CB  
3786 C CG1 . ILE B 267 ? 2.0056 0.7915 1.0845 -0.2601 -0.1426 -0.0601 583 ILE B CG1 
3787 C CG2 . ILE B 267 ? 2.0006 0.833  1.0285 -0.2768 -0.1381 -0.0423 583 ILE B CG2 
3788 C CD1 . ILE B 267 ? 2.0211 0.7962 1.1128 -0.2555 -0.1328 -0.0743 583 ILE B CD1 
3789 N N   . VAL B 268 ? 1.9607 0.8203 0.9523 -0.2438 -0.1107 -0.0788 584 VAL B N   
3790 C CA  . VAL B 268 ? 1.9465 0.8367 0.9242 -0.2362 -0.0938 -0.088  584 VAL B CA  
3791 C C   . VAL B 268 ? 1.9303 0.8468 0.8858 -0.2529 -0.0875 -0.0743 584 VAL B C   
3792 O O   . VAL B 268 ? 1.944  0.8481 0.8694 -0.2644 -0.0963 -0.067  584 VAL B O   
3793 C CB  . VAL B 268 ? 1.9682 0.8459 0.9287 -0.2195 -0.0919 -0.1079 584 VAL B CB  
3794 C CG1 . VAL B 268 ? 1.9724 0.8798 0.9155 -0.2103 -0.0724 -0.1207 584 VAL B CG1 
3795 C CG2 . VAL B 268 ? 1.9721 0.8326 0.9572 -0.2058 -0.0962 -0.1175 584 VAL B CG2 
3796 N N   . VAL B 269 ? 1.9002 0.8541 0.8707 -0.2575 -0.0743 -0.0675 585 VAL B N   
3797 C CA  . VAL B 269 ? 1.8906 0.8786 0.8425 -0.2762 -0.0645 -0.0518 585 VAL B CA  
3798 C C   . VAL B 269 ? 1.8761 0.9106 0.8296 -0.2627 -0.036  -0.0662 585 VAL B C   
3799 O O   . VAL B 269 ? 1.8608 0.9129 0.8522 -0.2483 -0.0297 -0.0734 585 VAL B O   
3800 C CB  . VAL B 269 ? 1.8819 0.8797 0.8575 -0.2978 -0.0742 -0.0266 585 VAL B CB  
3801 C CG1 . VAL B 269 ? 1.8802 0.9163 0.8359 -0.3218 -0.0647 -0.0056 585 VAL B CG1 
3802 C CG2 . VAL B 269 ? 1.9015 0.8502 0.8845 -0.3059 -0.1009 -0.0174 585 VAL B CG2 
3803 N N   . VAL B 270 ? 1.8793 0.9332 0.7925 -0.2671 -0.019  -0.0713 586 VAL B N   
3804 C CA  . VAL B 270 ? 1.8651 0.9668 0.7836 -0.2509 0.0138  -0.0897 586 VAL B CA  
3805 C C   . VAL B 270 ? 1.8601 1.0124 0.758  -0.2755 0.0348  -0.0716 586 VAL B C   
3806 O O   . VAL B 270 ? 1.8824 1.0219 0.724  -0.297  0.0311  -0.0624 586 VAL B O   
3807 C CB  . VAL B 270 ? 1.8931 0.9698 0.7802 -0.2263 0.0219  -0.1242 586 VAL B CB  
3808 C CG1 . VAL B 270 ? 1.8863 1.0116 0.7706 -0.2106 0.0603  -0.1464 586 VAL B CG1 
3809 C CG2 . VAL B 270 ? 1.8994 0.9393 0.8198 -0.2026 0.0045  -0.1386 586 VAL B CG2 
3810 N N   . ARG B 271 ? 1.8278 1.0389 0.773  -0.276  0.054   -0.0623 587 ARG B N   
3811 C CA  . ARG B 271 ? 1.8188 1.0896 0.7555 -0.3019 0.0767  -0.0408 587 ARG B CA  
3812 C C   . ARG B 271 ? 1.7933 1.1336 0.7522 -0.2825 0.1226  -0.0615 587 ARG B C   
3813 O O   . ARG B 271 ? 1.7674 1.1736 0.744  -0.3012 0.1459  -0.0418 587 ARG B O   
3814 C CB  . ARG B 271 ? 1.8168 1.1019 0.7952 -0.3288 0.0565  -0.0029 587 ARG B CB  
3815 C CG  . ARG B 271 ? 1.8837 1.1012 0.8456 -0.3457 0.0145  0.0143  587 ARG B CG  
3816 C CD  . ARG B 271 ? 1.9158 1.1452 0.9047 -0.3776 -0.0039 0.0516  587 ARG B CD  
3817 N NE  . ARG B 271 ? 1.986  1.1499 0.9626 -0.3921 -0.0425 0.0658  587 ARG B NE  
3818 C CZ  . ARG B 271 ? 2.0285 1.1515 1.0363 -0.384  -0.0662 0.0621  587 ARG B CZ  
3819 N NH1 . ARG B 271 ? 2.013  1.1504 1.0591 -0.3649 -0.0595 0.0476  587 ARG B NH1 
3820 N NH2 . ARG B 271 ? 2.0532 1.1197 1.0538 -0.3948 -0.0969 0.0722  587 ARG B NH2 
3821 N N   . ASP B 272 ? 1.7961 1.1223 0.7579 -0.245  0.1357  -0.1008 588 ASP B N   
3822 C CA  . ASP B 272 ? 1.7703 1.1547 0.7571 -0.2189 0.18    -0.1284 588 ASP B CA  
3823 C C   . ASP B 272 ? 1.7966 1.1393 0.7301 -0.1918 0.1916  -0.1732 588 ASP B C   
3824 O O   . ASP B 272 ? 1.8255 1.1001 0.7461 -0.1792 0.1605  -0.1851 588 ASP B O   
3825 C CB  . ASP B 272 ? 1.7478 1.168  0.8328 -0.1943 0.1802  -0.1285 588 ASP B CB  
3826 C CG  . ASP B 272 ? 1.7635 1.2667 0.8942 -0.1753 0.2289  -0.1444 588 ASP B CG  
3827 O OD1 . ASP B 272 ? 1.7421 1.3157 0.908  -0.1976 0.2462  -0.1161 588 ASP B OD1 
3828 O OD2 . ASP B 272 ? 1.7868 1.2847 0.9187 -0.1387 0.2507  -0.1858 588 ASP B OD2 
3829 N N   . ASP B 273 ? 1.784  1.1671 0.6856 -0.184  0.2367  -0.199  589 ASP B N   
3830 C CA  . ASP B 273 ? 1.8137 1.1525 0.6572 -0.1593 0.248   -0.2458 589 ASP B CA  
3831 C C   . ASP B 273 ? 1.7878 1.1103 0.6936 -0.1105 0.248   -0.2815 589 ASP B C   
3832 O O   . ASP B 273 ? 1.821  1.0898 0.6833 -0.0898 0.2454  -0.3189 589 ASP B O   
3833 C CB  . ASP B 273 ? 1.8457 1.2249 0.6208 -0.1679 0.2976  -0.267  589 ASP B CB  
3834 C CG  . ASP B 273 ? 1.8469 1.3237 0.6819 -0.1521 0.3539  -0.2775 589 ASP B CG  
3835 O OD1 . ASP B 273 ? 1.8047 1.3251 0.7434 -0.1382 0.351   -0.261  589 ASP B OD1 
3836 O OD2 . ASP B 273 ? 1.8803 1.392  0.6582 -0.1558 0.4008  -0.3009 589 ASP B OD2 
3837 N N   . LYS B 274 ? 1.7274 1.093  0.7339 -0.0944 0.247   -0.2683 590 LYS B N   
3838 C CA  . LYS B 274 ? 1.7008 1.0519 0.778  -0.0515 0.239   -0.2932 590 LYS B CA  
3839 C C   . LYS B 274 ? 1.6929 0.9954 0.8065 -0.0554 0.1866  -0.2679 590 LYS B C   
3840 O O   . LYS B 274 ? 1.673  0.9699 0.8536 -0.0275 0.1738  -0.2762 590 LYS B O   
3841 C CB  . LYS B 274 ? 1.6642 1.1022 0.8345 -0.0266 0.277   -0.3003 590 LYS B CB  
3842 C CG  . LYS B 274 ? 1.7114 1.1962 0.8548 -0.0102 0.3364  -0.3389 590 LYS B CG  
3843 C CD  . LYS B 274 ? 1.8101 1.2272 0.9012 0.0225  0.3402  -0.3937 590 LYS B CD  
3844 C CE  . LYS B 274 ? 1.871  1.3142 0.8918 0.0267  0.3959  -0.4331 590 LYS B CE  
3845 N NZ  . LYS B 274 ? 1.9513 1.3071 0.893  0.046   0.3872  -0.4815 590 LYS B NZ  
3846 N N   . ALA B 275 ? 1.7061 0.975  0.7776 -0.0903 0.1571  -0.237  591 ALA B N   
3847 C CA  . ALA B 275 ? 1.7075 0.9301 0.7995 -0.0982 0.1129  -0.215  591 ALA B CA  
3848 C C   . ALA B 275 ? 1.7438 0.8873 0.7774 -0.0961 0.088   -0.2305 591 ALA B C   
3849 O O   . ALA B 275 ? 1.777  0.9012 0.7419 -0.1054 0.0966  -0.2427 591 ALA B O   
3850 C CB  . ALA B 275 ? 1.705  0.9416 0.7914 -0.1362 0.0995  -0.1746 591 ALA B CB  
3851 N N   . ARG B 276 ? 1.735  0.8339 0.7934 -0.0872 0.0561  -0.2279 592 ARG B N   
3852 C CA  . ARG B 276 ? 1.7652 0.7944 0.7774 -0.0878 0.0313  -0.2383 592 ARG B CA  
3853 C C   . ARG B 276 ? 1.7561 0.7533 0.7877 -0.0997 -0.0017 -0.2152 592 ARG B C   
3854 O O   . ARG B 276 ? 1.7396 0.7443 0.8221 -0.0901 -0.0116 -0.2086 592 ARG B O   
3855 C CB  . ARG B 276 ? 1.7942 0.7932 0.8063 -0.0558 0.0331  -0.2749 592 ARG B CB  
3856 C CG  . ARG B 276 ? 1.8769 0.8046 0.8394 -0.0601 0.0057  -0.2843 592 ARG B CG  
3857 C CD  . ARG B 276 ? 1.9371 0.8277 0.8945 -0.0303 0.0046  -0.3221 592 ARG B CD  
3858 N NE  . ARG B 276 ? 2.0223 0.8625 0.9042 -0.0392 -0.0041 -0.3397 592 ARG B NE  
3859 C CZ  . ARG B 276 ? 2.0836 0.8621 0.9479 -0.044  -0.0388 -0.3395 592 ARG B CZ  
3860 N NH1 . ARG B 276 ? 2.071  0.8314 0.9845 -0.0406 -0.0646 -0.3235 592 ARG B NH1 
3861 N NH2 . ARG B 276 ? 2.1236 0.8585 0.9193 -0.055  -0.0492 -0.3536 592 ARG B NH2 
3862 N N   . ILE B 277 ? 1.7658 0.7296 0.7584 -0.1214 -0.0184 -0.2022 593 ILE B N   
3863 C CA  . ILE B 277 ? 1.7646 0.6991 0.772  -0.1324 -0.0441 -0.1841 593 ILE B CA  
3864 C C   . ILE B 277 ? 1.7867 0.6695 0.7624 -0.1343 -0.0629 -0.1911 593 ILE B C   
3865 O O   . ILE B 277 ? 1.809  0.6786 0.7418 -0.1425 -0.0624 -0.196  593 ILE B O   
3866 C CB  . ILE B 277 ? 1.7629 0.7123 0.772  -0.1577 -0.0468 -0.1577 593 ILE B CB  
3867 C CG1 . ILE B 277 ? 1.7489 0.7511 0.7885 -0.1611 -0.0309 -0.147  593 ILE B CG1 
3868 C CG2 . ILE B 277 ? 1.7731 0.6925 0.7963 -0.1659 -0.0676 -0.1455 593 ILE B CG2 
3869 C CD1 . ILE B 277 ? 1.7658 0.7778 0.7999 -0.1872 -0.0347 -0.123  593 ILE B CD1 
3870 N N   . THR B 278 ? 1.7789 0.6332 0.7747 -0.1298 -0.0816 -0.189  594 THR B N   
3871 C CA  . THR B 278 ? 1.7979 0.6075 0.7741 -0.1347 -0.1017 -0.1906 594 THR B CA  
3872 C C   . THR B 278 ? 1.7949 0.5957 0.7913 -0.1492 -0.114  -0.1702 594 THR B C   
3873 O O   . THR B 278 ? 1.7827 0.6014 0.804  -0.1512 -0.1106 -0.1604 594 THR B O   
3874 C CB  . THR B 278 ? 1.8184 0.5983 0.7978 -0.1156 -0.1122 -0.2101 594 THR B CB  
3875 O OG1 . THR B 278 ? 1.8131 0.604  0.8347 -0.1051 -0.115  -0.2058 594 THR B OG1 
3876 C CG2 . THR B 278 ? 1.832  0.6106 0.7829 -0.0998 -0.0987 -0.2378 594 THR B CG2 
3877 N N   . HIS B 279 ? 1.8057 0.5804 0.7916 -0.16   -0.1277 -0.1641 595 HIS B N   
3878 C CA  A HIS B 279 ? 1.8071 0.5764 0.8141 -0.1721 -0.134  -0.1483 595 HIS B CA  
3879 C CA  B HIS B 279 ? 1.8074 0.5765 0.8146 -0.1718 -0.1341 -0.1484 595 HIS B CA  
3880 C C   . HIS B 279 ? 1.8204 0.5598 0.8286 -0.1765 -0.1519 -0.1461 595 HIS B C   
3881 O O   . HIS B 279 ? 1.8366 0.5587 0.8251 -0.178  -0.1625 -0.1508 595 HIS B O   
3882 C CB  A HIS B 279 ? 1.8142 0.5984 0.8249 -0.1853 -0.1271 -0.1358 595 HIS B CB  
3883 C CB  B HIS B 279 ? 1.8137 0.5996 0.8271 -0.1848 -0.126  -0.1356 595 HIS B CB  
3884 C CG  A HIS B 279 ? 1.8416 0.6174 0.8742 -0.1946 -0.1305 -0.1256 595 HIS B CG  
3885 C CG  B HIS B 279 ? 1.8531 0.6348 0.8511 -0.1934 -0.131  -0.1307 595 HIS B CG  
3886 N ND1 A HIS B 279 ? 1.8672 0.6282 0.9078 -0.2004 -0.142  -0.1199 595 HIS B ND1 
3887 N ND1 B HIS B 279 ? 1.8827 0.6435 0.8859 -0.2    -0.1466 -0.1246 595 HIS B ND1 
3888 C CD2 A HIS B 279 ? 1.8508 0.6316 0.8985 -0.1986 -0.1233 -0.1217 595 HIS B CD2 
3889 C CD2 B HIS B 279 ? 1.8677 0.6652 0.8503 -0.1999 -0.125  -0.126  595 HIS B CD2 
3890 C CE1 A HIS B 279 ? 1.865  0.6281 0.9319 -0.2054 -0.137  -0.1138 595 HIS B CE1 
3891 C CE1 B HIS B 279 ? 1.8942 0.655  0.8827 -0.2093 -0.1525 -0.1172 595 HIS B CE1 
3892 N NE2 A HIS B 279 ? 1.8616 0.6345 0.9274 -0.2053 -0.1245 -0.1162 595 HIS B NE2 
3893 N NE2 B HIS B 279 ? 1.8903 0.6721 0.863  -0.2107 -0.1395 -0.1172 595 HIS B NE2 
3894 N N   . GLU B 280 ? 1.8152 0.5496 0.8443 -0.1818 -0.1562 -0.1372 596 GLU B N   
3895 C CA  . GLU B 280 ? 1.8297 0.543  0.8683 -0.1899 -0.172  -0.1301 596 GLU B CA  
3896 C C   . GLU B 280 ? 1.8079 0.5357 0.8715 -0.2025 -0.1625 -0.116  596 GLU B C   
3897 O O   . GLU B 280 ? 1.802  0.5434 0.8673 -0.2042 -0.1495 -0.1142 596 GLU B O   
3898 C CB  . GLU B 280 ? 1.8957 0.5836 0.932  -0.184  -0.1888 -0.1349 596 GLU B CB  
3899 C CG  . GLU B 280 ? 2.0103 0.7025 1.061  -0.1876 -0.1882 -0.1254 596 GLU B CG  
3900 C CD  . GLU B 280 ? 2.1605 0.8332 1.2229 -0.201  -0.2058 -0.1111 596 GLU B CD  
3901 O OE1 . GLU B 280 ? 2.2067 0.8493 1.267  -0.1956 -0.2278 -0.1148 596 GLU B OE1 
3902 O OE2 . GLU B 280 ? 2.1904 0.8785 1.2657 -0.2174 -0.1967 -0.0963 596 GLU B OE2 
3903 N N   . ALA B 281 ? 1.7956 0.5219 0.879  -0.2114 -0.168  -0.1068 597 ALA B N   
3904 C CA  . ALA B 281 ? 1.7829 0.5268 0.8957 -0.2208 -0.1537 -0.0971 597 ALA B CA  
3905 C C   . ALA B 281 ? 1.7773 0.5196 0.9206 -0.2309 -0.1646 -0.0845 597 ALA B C   
3906 O O   . ALA B 281 ? 1.7839 0.5108 0.9291 -0.2322 -0.1864 -0.0815 597 ALA B O   
3907 C CB  . ALA B 281 ? 1.776  0.535  0.8998 -0.2188 -0.1391 -0.0991 597 ALA B CB  
3908 N N   . ALA B 282 ? 1.7662 0.525  0.9312 -0.2405 -0.1499 -0.0764 598 ALA B N   
3909 C CA  . ALA B 282 ? 1.761  0.5289 0.9643 -0.2527 -0.1554 -0.0612 598 ALA B CA  
3910 C C   . ALA B 282 ? 1.7519 0.5517 0.9857 -0.2563 -0.1237 -0.0603 598 ALA B C   
3911 O O   . ALA B 282 ? 1.7581 0.5653 0.9707 -0.2612 -0.1034 -0.0643 598 ALA B O   
3912 C CB  . ALA B 282 ? 1.7743 0.5277 0.965  -0.2641 -0.1702 -0.0513 598 ALA B CB  
3913 N N   . ILE B 283 ? 1.7396 0.5564 1.0215 -0.2531 -0.1196 -0.057  599 ILE B N   
3914 C CA  . ILE B 283 ? 1.7356 0.5826 1.0559 -0.2513 -0.0865 -0.0614 599 ILE B CA  
3915 C C   . ILE B 283 ? 1.7223 0.597  1.1102 -0.2591 -0.0868 -0.0447 599 ILE B C   
3916 O O   . ILE B 283 ? 1.7172 0.584  1.1306 -0.2614 -0.1178 -0.0311 599 ILE B O   
3917 C CB  . ILE B 283 ? 1.7416 0.5844 1.0712 -0.2359 -0.0815 -0.0741 599 ILE B CB  
3918 C CG1 . ILE B 283 ? 1.7849 0.6032 1.0528 -0.2306 -0.0867 -0.0861 599 ILE B CG1 
3919 C CG2 . ILE B 283 ? 1.7243 0.5916 1.0956 -0.2297 -0.0468 -0.0848 599 ILE B CG2 
3920 C CD1 . ILE B 283 ? 1.8143 0.6328 1.0423 -0.234  -0.0639 -0.0978 599 ILE B CD1 
3921 N N   . GLY B 284 ? 1.7153 0.6234 1.1311 -0.2648 -0.0523 -0.0453 600 GLY B N   
3922 C CA  . GLY B 284 ? 1.6957 0.6418 1.1869 -0.2725 -0.046  -0.0284 600 GLY B CA  
3923 C C   . GLY B 284 ? 1.7082 0.673  1.1916 -0.296  -0.0365 -0.0124 600 GLY B C   
3924 O O   . GLY B 284 ? 1.7312 0.6922 1.1597 -0.3046 -0.0162 -0.0198 600 GLY B O   
3925 N N   . SER B 285 ? 1.6923 0.6766 1.2302 -0.3097 -0.0542 0.0125  601 SER B N   
3926 C CA  . SER B 285 ? 1.7046 0.7087 1.2432 -0.3366 -0.0494 0.0341  601 SER B CA  
3927 C C   . SER B 285 ? 1.7622 0.7186 1.2234 -0.3496 -0.0804 0.0401  601 SER B C   
3928 O O   . SER B 285 ? 1.792  0.703  1.2116 -0.3363 -0.1094 0.0288  601 SER B O   
3929 C CB  . SER B 285 ? 1.6915 0.7245 1.313  -0.3492 -0.0695 0.0624  601 SER B CB  
3930 O OG  . SER B 285 ? 1.7474 0.7352 1.3578 -0.349  -0.1246 0.0711  601 SER B OG  
3931 N N   . VAL B 286 ? 1.7743 0.7422 1.219  -0.3758 -0.0737 0.0586  602 VAL B N   
3932 C CA  . VAL B 286 ? 1.8235 0.7459 1.2065 -0.3893 -0.1065 0.0681  602 VAL B CA  
3933 C C   . VAL B 286 ? 1.8481 0.7319 1.2442 -0.3915 -0.1607 0.0813  602 VAL B C   
3934 O O   . VAL B 286 ? 1.8225 0.7249 1.2793 -0.3961 -0.1731 0.0951  602 VAL B O   
3935 C CB  . VAL B 286 ? 1.8275 0.7717 1.1923 -0.4219 -0.0896 0.0903  602 VAL B CB  
3936 C CG1 . VAL B 286 ? 1.831  0.8062 1.1673 -0.4211 -0.0359 0.0726  602 VAL B CG1 
3937 C CG2 . VAL B 286 ? 1.7977 0.7817 1.2292 -0.4475 -0.0918 0.1225  602 VAL B CG2 
3938 N N   . ASP B 287 ? 1.8944 0.7231 1.2353 -0.3874 -0.194  0.0756  603 ASP B N   
3939 C CA  . ASP B 287 ? 1.9261 0.7072 1.2654 -0.3879 -0.245  0.0808  603 ASP B CA  
3940 C C   . ASP B 287 ? 1.9242 0.7141 1.3047 -0.4199 -0.2676 0.1157  603 ASP B C   
3941 O O   . ASP B 287 ? 1.9207 0.7307 1.3002 -0.444  -0.2555 0.1368  603 ASP B O   
3942 C CB  . ASP B 287 ? 1.9856 0.7107 1.2635 -0.3768 -0.2693 0.0665  603 ASP B CB  
3943 C CG  . ASP B 287 ? 2.0647 0.7332 1.3313 -0.3719 -0.318  0.0619  603 ASP B CG  
3944 O OD1 . ASP B 287 ? 2.0731 0.7302 1.3383 -0.3552 -0.3256 0.0444  603 ASP B OD1 
3945 O OD2 . ASP B 287 ? 2.1111 0.7429 1.3666 -0.3861 -0.3501 0.0754  603 ASP B OD2 
3946 N N   . LYS B 288 ? 1.9213 0.7004 1.3388 -0.4235 -0.2998 0.1243  604 LYS B N   
3947 C CA  . LYS B 288 ? 1.9105 0.6997 1.3762 -0.4559 -0.326  0.16    604 LYS B CA  
3948 C C   . LYS B 288 ? 1.9412 0.6809 1.3712 -0.4762 -0.3628 0.1756  604 LYS B C   
3949 O O   . LYS B 288 ? 1.9225 0.6871 1.3802 -0.5086 -0.3637 0.2092  604 LYS B O   
3950 C CB  . LYS B 288 ? 1.9333 0.7109 1.4385 -0.4554 -0.3613 0.1643  604 LYS B CB  
3951 C CG  . LYS B 288 ? 1.9802 0.7673 1.5417 -0.4908 -0.3949 0.2035  604 LYS B CG  
3952 C CD  . LYS B 288 ? 2.0488 0.8174 1.6421 -0.4914 -0.4362 0.2071  604 LYS B CD  
3953 C CE  . LYS B 288 ? 2.122  0.8354 1.7105 -0.5192 -0.4995 0.228   604 LYS B CE  
3954 N NZ  . LYS B 288 ? 2.1573 0.8447 1.7625 -0.5215 -0.5438 0.2292  604 LYS B NZ  
3955 N N   . LYS B 289 ? 1.9883 0.6602 1.3599 -0.4577 -0.3915 0.1521  605 LYS B N   
3956 C CA  . LYS B 289 ? 2.0297 0.6465 1.3723 -0.4725 -0.4307 0.1643  605 LYS B CA  
3957 C C   . LYS B 289 ? 2.0414 0.6808 1.3656 -0.4863 -0.4057 0.1793  605 LYS B C   
3958 O O   . LYS B 289 ? 2.0462 0.6718 1.3742 -0.517  -0.4302 0.2108  605 LYS B O   
3959 C CB  . LYS B 289 ? 2.0942 0.6362 1.3858 -0.4438 -0.4625 0.1302  605 LYS B CB  
3960 C CG  . LYS B 289 ? 2.1705 0.6438 1.4447 -0.4565 -0.5138 0.1406  605 LYS B CG  
3961 C CD  . LYS B 289 ? 2.2678 0.679  1.4932 -0.4208 -0.5288 0.1006  605 LYS B CD  
3962 C CE  . LYS B 289 ? 2.3569 0.6874 1.5698 -0.4262 -0.5854 0.1018  605 LYS B CE  
3963 N NZ  . LYS B 289 ? 2.401  0.6921 1.6215 -0.4396 -0.6264 0.1033  605 LYS B NZ  
3964 N N   . GLN B 290 ? 2.0465 0.7188 1.3486 -0.4677 -0.3601 0.1595  606 GLN B N   
3965 C CA  . GLN B 290 ? 2.0646 0.7581 1.3403 -0.4837 -0.3359 0.173   606 GLN B CA  
3966 C C   . GLN B 290 ? 2.0434 0.7973 1.3546 -0.5217 -0.3107 0.2083  606 GLN B C   
3967 O O   . GLN B 290 ? 2.0543 0.8069 1.3489 -0.5536 -0.3189 0.2381  606 GLN B O   
3968 C CB  . GLN B 290 ? 2.0937 0.8096 1.3394 -0.4573 -0.2932 0.1427  606 GLN B CB  
3969 C CG  . GLN B 290 ? 2.188  0.8533 1.3918 -0.4291 -0.313  0.117   606 GLN B CG  
3970 C CD  . GLN B 290 ? 2.2773 0.9686 1.46   -0.4053 -0.2727 0.0892  606 GLN B CD  
3971 O OE1 . GLN B 290 ? 2.2907 1.0265 1.47   -0.4157 -0.2326 0.0921  606 GLN B OE1 
3972 N NE2 . GLN B 290 ? 2.3153 0.9782 1.4818 -0.3738 -0.2821 0.0608  606 GLN B NE2 
3973 N N   . LEU B 291 ? 2.009  0.8175 1.3724 -0.519  -0.2804 0.2065  607 LEU B N   
3974 C CA  . LEU B 291 ? 1.9748 0.8525 1.3864 -0.5505 -0.2487 0.2363  607 LEU B CA  
3975 C C   . LEU B 291 ? 1.9719 0.8349 1.4124 -0.5885 -0.2936 0.2788  607 LEU B C   
3976 O O   . LEU B 291 ? 1.9643 0.8538 1.4015 -0.6257 -0.284  0.3117  607 LEU B O   
3977 C CB  . LEU B 291 ? 1.9382 0.8702 1.4149 -0.5321 -0.2161 0.2228  607 LEU B CB  
3978 C CG  . LEU B 291 ? 1.9058 0.9192 1.4502 -0.5587 -0.1778 0.2497  607 LEU B CG  
3979 C CD1 . LEU B 291 ? 1.9094 0.9678 1.4208 -0.5654 -0.117  0.2418  607 LEU B CD1 
3980 C CD2 . LEU B 291 ? 1.8724 0.9271 1.4991 -0.5395 -0.1656 0.2418  607 LEU B CD2 
3981 N N   . GLU B 292 ? 1.9814 0.7963 1.442  -0.5817 -0.3454 0.2782  608 GLU B N   
3982 C CA  . GLU B 292 ? 1.9892 0.778  1.4771 -0.6169 -0.397  0.3161  608 GLU B CA  
3983 C C   . GLU B 292 ? 2.0367 0.7674 1.4742 -0.6365 -0.4338 0.3334  608 GLU B C   
3984 O O   . GLU B 292 ? 2.0354 0.7646 1.495  -0.6778 -0.4622 0.3759  608 GLU B O   
3985 C CB  . GLU B 292 ? 2.0194 0.7638 1.5312 -0.6039 -0.4444 0.3058  608 GLU B CB  
3986 C CG  . GLU B 292 ? 2.0391 0.8475 1.6173 -0.5948 -0.4159 0.3028  608 GLU B CG  
3987 C CD  . GLU B 292 ? 2.1246 0.8979 1.7321 -0.5922 -0.4656 0.3022  608 GLU B CD  
3988 O OE1 . GLU B 292 ? 2.1908 0.8848 1.7429 -0.5733 -0.5049 0.2758  608 GLU B OE1 
3989 O OE2 . GLU B 292 ? 2.1048 0.9313 1.791  -0.6091 -0.4642 0.3272  608 GLU B OE2 
3990 N N   . THR B 293 ? 2.0747 0.7598 1.4504 -0.6091 -0.4353 0.3042  609 THR B N   
3991 C CA  . THR B 293 ? 2.116  0.7457 1.4496 -0.6249 -0.4719 0.3211  609 THR B CA  
3992 C C   . THR B 293 ? 2.1027 0.7853 1.4245 -0.6643 -0.4399 0.3569  609 THR B C   
3993 O O   . THR B 293 ? 2.1153 0.7762 1.4334 -0.7035 -0.4746 0.3979  609 THR B O   
3994 C CB  . THR B 293 ? 2.1726 0.7477 1.456  -0.5831 -0.4806 0.2808  609 THR B CB  
3995 O OG1 . THR B 293 ? 2.2042 0.7275 1.4923 -0.5523 -0.5116 0.2498  609 THR B OG1 
3996 C CG2 . THR B 293 ? 2.2087 0.7309 1.4587 -0.5974 -0.5184 0.2999  609 THR B CG2 
3997 N N   . LEU B 294 ? 2.0756 0.8255 1.3893 -0.6566 -0.375  0.3421  610 LEU B N   
3998 C CA  . LEU B 294 ? 2.0659 0.8683 1.3585 -0.695  -0.3379 0.3712  610 LEU B CA  
3999 C C   . LEU B 294 ? 2.0313 0.896  1.3803 -0.7369 -0.3234 0.4116  610 LEU B C   
4000 O O   . LEU B 294 ? 2.0336 0.9183 1.3646 -0.7829 -0.3209 0.452   610 LEU B O   
4001 C CB  . LEU B 294 ? 2.0647 0.9097 1.3228 -0.674  -0.2753 0.3388  610 LEU B CB  
4002 C CG  . LEU B 294 ? 2.1213 0.9135 1.3244 -0.6391 -0.2875 0.3049  610 LEU B CG  
4003 C CD1 . LEU B 294 ? 2.1295 0.9644 1.2983 -0.6259 -0.2274 0.2773  610 LEU B CD1 
4004 C CD2 . LEU B 294 ? 2.1634 0.8961 1.322  -0.66   -0.3375 0.3306  610 LEU B CD2 
4005 N N   . MET B 295 ? 1.9996 0.8941 1.4184 -0.7249 -0.3188 0.4057  611 MET B N   
4006 C CA  . MET B 295 ? 1.9658 0.9223 1.4541 -0.7648 -0.3109 0.4476  611 MET B CA  
4007 C C   . MET B 295 ? 1.987  0.8919 1.4834 -0.8052 -0.3809 0.4937  611 MET B C   
4008 O O   . MET B 295 ? 1.9577 0.9114 1.4904 -0.8533 -0.3762 0.541   611 MET B O   
4009 C CB  . MET B 295 ? 1.937  0.9355 1.5049 -0.7407 -0.2955 0.4313  611 MET B CB  
4010 C CG  . MET B 295 ? 1.9515 1.0095 1.5272 -0.7081 -0.2254 0.394   611 MET B CG  
4011 S SD  . MET B 295 ? 1.981  1.1132 1.678  -0.6992 -0.2058 0.398   611 MET B SD  
4012 C CE  . MET B 295 ? 2.013  1.0572 1.7076 -0.6649 -0.2754 0.3741  611 MET B CE  
4013 N N   . ALA B 296 ? 2.0368 0.8436 1.5006 -0.7863 -0.4448 0.4797  612 ALA B N   
4014 C CA  . ALA B 296 ? 2.0735 0.8135 1.5376 -0.8201 -0.5174 0.5177  612 ALA B CA  
4015 C C   . ALA B 296 ? 2.1099 0.84   1.5246 -0.86   -0.5249 0.5551  612 ALA B C   
4016 O O   . ALA B 296 ? 2.1251 0.8139 1.5467 -0.8998 -0.5804 0.5986  612 ALA B O   
4017 C CB  . ALA B 296 ? 2.1162 0.7537 1.5576 -0.7824 -0.5764 0.4833  612 ALA B CB  
4018 N N   . LYS B 297 ? 2.1247 0.8866 1.4866 -0.8513 -0.4741 0.5393  613 LYS B N   
4019 C CA  . LYS B 297 ? 2.1574 0.9217 1.4638 -0.8921 -0.472  0.5745  613 LYS B CA  
4020 C C   . LYS B 297 ? 2.1301 0.9963 1.4521 -0.9417 -0.4139 0.6121  613 LYS B C   
4021 O O   . LYS B 297 ? 2.1476 1.0303 1.4134 -0.9776 -0.3972 0.6378  613 LYS B O   
4022 C CB  . LYS B 297 ? 2.2149 0.9635 1.4516 -0.8606 -0.4462 0.5378  613 LYS B CB  
4023 C CG  . LYS B 297 ? 2.3074 0.9841 1.5343 -0.802  -0.4766 0.4887  613 LYS B CG  
4024 C CD  . LYS B 297 ? 2.413  0.9952 1.6264 -0.8071 -0.5547 0.5063  613 LYS B CD  
4025 C CE  . LYS B 297 ? 2.4954 1.0129 1.7089 -0.7474 -0.5801 0.4547  613 LYS B CE  
4026 N NZ  . LYS B 297 ? 2.5625 0.9873 1.7887 -0.748  -0.6583 0.4663  613 LYS B NZ  
4027 N N   . GLY B 298 ? 2.0865 1.0227 1.4824 -0.9425 -0.3806 0.6131  614 GLY B N   
4028 C CA  . GLY B 298 ? 2.052  1.0931 1.4774 -0.9854 -0.3205 0.6455  614 GLY B CA  
4029 C C   . GLY B 298 ? 2.0379 1.157  1.4522 -0.9603 -0.2306 0.6058  614 GLY B C   
4030 O O   . GLY B 298 ? 1.9987 1.2104 1.4401 -0.9901 -0.1713 0.6248  614 GLY B O   
4031 N N   . LEU B 299 ? 2.0673 1.1503 1.4423 -0.9063 -0.2189 0.5503  615 LEU B N   
4032 C CA  . LEU B 299 ? 2.0615 1.2039 1.422  -0.8783 -0.1399 0.5074  615 LEU B CA  
4033 C C   . LEU B 299 ? 2.0219 1.2265 1.4811 -0.8502 -0.1058 0.4877  615 LEU B C   
4034 O O   . LEU B 299 ? 2.0233 1.1909 1.534  -0.8265 -0.1522 0.4818  615 LEU B O   
4035 C CB  . LEU B 299 ? 2.1034 1.1813 1.3987 -0.8307 -0.1485 0.4581  615 LEU B CB  
4036 C CG  . LEU B 299 ? 2.1674 1.2035 1.3622 -0.8511 -0.1596 0.4661  615 LEU B CG  
4037 C CD1 . LEU B 299 ? 2.2093 1.1621 1.3861 -0.8677 -0.2425 0.4981  615 LEU B CD1 
4038 C CD2 . LEU B 299 ? 2.2    1.2093 1.3465 -0.8051 -0.1408 0.4137  615 LEU B CD2 
4039 N N   . ASP B 300 ? 1.9853 1.2815 1.4711 -0.8515 -0.0263 0.4758  616 ASP B N   
4040 C CA  . ASP B 300 ? 1.9378 1.2937 1.5276 -0.8199 0.0053  0.4557  616 ASP B CA  
4041 C C   . ASP B 300 ? 1.9502 1.2672 1.5277 -0.7572 0.0104  0.3965  616 ASP B C   
4042 O O   . ASP B 300 ? 1.9994 1.2603 1.4879 -0.7413 0.0046  0.3703  616 ASP B O   
4043 C CB  . ASP B 300 ? 1.9093 1.3817 1.5555 -0.8413 0.0863  0.4656  616 ASP B CB  
4044 C CG  . ASP B 300 ? 1.9839 1.4931 1.5623 -0.8352 0.1647  0.4307  616 ASP B CG  
4045 O OD1 . ASP B 300 ? 2.0209 1.4912 1.5575 -0.7896 0.1762  0.3795  616 ASP B OD1 
4046 O OD2 . ASP B 300 ? 1.9928 1.5715 1.56   -0.8775 0.2162  0.454   616 ASP B OD2 
4047 N N   . GLU B 301 ? 1.9035 1.2499 1.5715 -0.7243 0.0177  0.3789  617 GLU B N   
4048 C CA  . GLU B 301 ? 1.9178 1.2289 1.58   -0.669  0.0185  0.3286  617 GLU B CA  
4049 C C   . GLU B 301 ? 1.935  1.2507 1.5269 -0.6477 0.0753  0.286   617 GLU B C   
4050 O O   . GLU B 301 ? 1.973  1.2283 1.5095 -0.616  0.0579  0.2531  617 GLU B O   
4051 C CB  . GLU B 301 ? 1.8927 1.2508 1.6711 -0.6447 0.0257  0.3233  617 GLU B CB  
4052 C CG  . GLU B 301 ? 1.9749 1.2877 1.75   -0.5934 0.0113  0.2804  617 GLU B CG  
4053 C CD  . GLU B 301 ? 2.0138 1.3599 1.9022 -0.575  -0.0003 0.2841  617 GLU B CD  
4054 O OE1 . GLU B 301 ? 1.9952 1.3658 1.9528 -0.6029 -0.0302 0.3245  617 GLU B OE1 
4055 O OE2 . GLU B 301 ? 2.0406 1.3869 1.9504 -0.5349 0.017   0.2494  617 GLU B OE2 
4056 N N   . ASP B 302 ? 1.9071 1.2927 1.4964 -0.6684 0.1419  0.2876  618 ASP B N   
4057 C CA  . ASP B 302 ? 1.9315 1.3197 1.4482 -0.6531 0.1966  0.2465  618 ASP B CA  
4058 C C   . ASP B 302 ? 1.9808 1.3074 1.3731 -0.677  0.1728  0.2528  618 ASP B C   
4059 O O   . ASP B 302 ? 2.0184 1.3025 1.344  -0.6522 0.178   0.2164  618 ASP B O   
4060 C CB  . ASP B 302 ? 1.9237 1.4067 1.4771 -0.6654 0.2801  0.2401  618 ASP B CB  
4061 C CG  . ASP B 302 ? 1.9406 1.4823 1.6213 -0.6291 0.3099  0.2217  618 ASP B CG  
4062 O OD1 . ASP B 302 ? 1.9524 1.4545 1.656  -0.5837 0.2884  0.1906  618 ASP B OD1 
4063 O OD2 . ASP B 302 ? 1.9254 1.5547 1.6867 -0.6471 0.354   0.2404  618 ASP B OD2 
4064 N N   . GLU B 303 ? 1.9792 1.2993 1.3439 -0.7259 0.1427  0.3012  619 GLU B N   
4065 C CA  . GLU B 303 ? 2.0316 1.2909 1.286  -0.7513 0.1114  0.314   619 GLU B CA  
4066 C C   . GLU B 303 ? 2.0587 1.2291 1.2914 -0.7178 0.0454  0.2987  619 GLU B C   
4067 O O   . GLU B 303 ? 2.1007 1.225  1.2545 -0.7084 0.038   0.279   619 GLU B O   
4068 C CB  . GLU B 303 ? 2.0636 1.3315 1.3056 -0.8121 0.0846  0.3748  619 GLU B CB  
4069 C CG  . GLU B 303 ? 2.1034 1.459  1.342  -0.8549 0.153   0.3938  619 GLU B CG  
4070 C CD  . GLU B 303 ? 2.17   1.5521 1.4321 -0.9148 0.1285  0.4596  619 GLU B CD  
4071 O OE1 . GLU B 303 ? 2.1927 1.5276 1.4944 -0.919  0.0567  0.4892  619 GLU B OE1 
4072 O OE2 . GLU B 303 ? 2.1798 1.6296 1.4198 -0.9588 0.1815  0.4812  619 GLU B OE2 
4073 N N   . ALA B 304 ? 2.0324 1.1811 1.3358 -0.7002 -0.0008 0.3067  620 ALA B N   
4074 C CA  . ALA B 304 ? 2.0599 1.129  1.3498 -0.6678 -0.0603 0.2907  620 ALA B CA  
4075 C C   . ALA B 304 ? 2.0626 1.1194 1.3379 -0.6188 -0.0369 0.2389  620 ALA B C   
4076 O O   . ALA B 304 ? 2.1018 1.1007 1.3233 -0.6005 -0.0647 0.2218  620 ALA B O   
4077 C CB  . ALA B 304 ? 2.0415 1.0968 1.4069 -0.6638 -0.107  0.3083  620 ALA B CB  
4078 N N   . THR B 305 ? 2.0169 1.1295 1.3449 -0.5982 0.0138  0.2153  621 THR B N   
4079 C CA  . THR B 305 ? 2.0176 1.1211 1.3377 -0.5545 0.0374  0.1683  621 THR B CA  
4080 C C   . THR B 305 ? 2.0382 1.1306 1.2678 -0.5599 0.0677  0.1486  621 THR B C   
4081 O O   . THR B 305 ? 2.0671 1.1136 1.253  -0.5352 0.0524  0.1231  621 THR B O   
4082 C CB  . THR B 305 ? 1.9869 1.1522 1.3949 -0.5343 0.0805  0.1528  621 THR B CB  
4083 O OG1 . THR B 305 ? 1.9728 1.1428 1.4618 -0.533  0.0428  0.1752  621 THR B OG1 
4084 C CG2 . THR B 305 ? 1.9976 1.1511 1.4009 -0.4914 0.1028  0.1067  621 THR B CG2 
4085 N N   . GLU B 306 ? 2.0235 1.1566 1.221  -0.5963 0.1072  0.1634  622 GLU B N   
4086 C CA  . GLU B 306 ? 2.0552 1.1765 1.1559 -0.6106 0.134   0.1486  622 GLU B CA  
4087 C C   . GLU B 306 ? 2.0869 1.1388 1.1152 -0.6218 0.0767  0.1639  622 GLU B C   
4088 O O   . GLU B 306 ? 2.1172 1.1389 1.0784 -0.6141 0.08    0.1416  622 GLU B O   
4089 C CB  . GLU B 306 ? 2.086  1.2642 1.1611 -0.6553 0.1832  0.168   622 GLU B CB  
4090 C CG  . GLU B 306 ? 2.2078 1.3835 1.1865 -0.6651 0.2271  0.1403  622 GLU B CG  
4091 C CD  . GLU B 306 ? 2.3611 1.5392 1.2497 -0.7234 0.2302  0.1743  622 GLU B CD  
4092 O OE1 . GLU B 306 ? 2.39   1.5636 1.2889 -0.7573 0.1896  0.2238  622 GLU B OE1 
4093 O OE2 . GLU B 306 ? 2.4247 1.6053 1.2285 -0.7374 0.2707  0.1519  622 GLU B OE2 
4094 N N   . ILE B 307 ? 2.0788 1.1037 1.125  -0.6394 0.022   0.2019  623 ILE B N   
4095 C CA  . ILE B 307 ? 2.1153 1.0733 1.1093 -0.6459 -0.0365 0.2171  623 ILE B CA  
4096 C C   . ILE B 307 ? 2.129  1.0424 1.1324 -0.5971 -0.0622 0.1831  623 ILE B C   
4097 O O   . ILE B 307 ? 2.1616 1.0382 1.1099 -0.5914 -0.0783 0.1732  623 ILE B O   
4098 C CB  . ILE B 307 ? 2.1153 1.0537 1.1318 -0.6773 -0.0878 0.2653  623 ILE B CB  
4099 C CG1 . ILE B 307 ? 2.1251 1.1027 1.1085 -0.7349 -0.0653 0.3047  623 ILE B CG1 
4100 C CG2 . ILE B 307 ? 2.1526 1.0155 1.1419 -0.6699 -0.155  0.2745  623 ILE B CG2 
4101 C CD1 . ILE B 307 ? 2.1778 1.1448 1.0611 -0.7626 -0.0518 0.3075  623 ILE B CD1 
4102 N N   . ILE B 308 ? 2.1007 1.0208 1.1737 -0.5644 -0.0651 0.1667  624 ILE B N   
4103 C CA  . ILE B 308 ? 2.11   0.995  1.1944 -0.5202 -0.0848 0.1352  624 ILE B CA  
4104 C C   . ILE B 308 ? 2.1252 1.0193 1.176  -0.4998 -0.0462 0.099   624 ILE B C   
4105 O O   . ILE B 308 ? 2.1465 1.0043 1.1645 -0.482  -0.0658 0.0838  624 ILE B O   
4106 C CB  . ILE B 308 ? 2.0819 0.9752 1.2416 -0.4986 -0.0957 0.1308  624 ILE B CB  
4107 C CG1 . ILE B 308 ? 2.089  0.9512 1.2702 -0.5158 -0.1485 0.1626  624 ILE B CG1 
4108 C CG2 . ILE B 308 ? 2.0939 0.9637 1.2606 -0.4557 -0.102  0.0958  624 ILE B CG2 
4109 C CD1 . ILE B 308 ? 2.0694 0.9514 1.3211 -0.5137 -0.156  0.1709  624 ILE B CD1 
4110 N N   . VAL B 309 ? 2.1125 1.0552 1.1737 -0.5036 0.0083  0.0857  625 VAL B N   
4111 C CA  . VAL B 309 ? 2.135  1.0847 1.1635 -0.4877 0.0481  0.0498  625 VAL B CA  
4112 C C   . VAL B 309 ? 2.1872 1.1104 1.1233 -0.5114 0.0442  0.0525  625 VAL B C   
4113 O O   . VAL B 309 ? 2.2072 1.1028 1.1097 -0.4938 0.039   0.0295  625 VAL B O   
4114 C CB  . VAL B 309 ? 2.1122 1.1201 1.1804 -0.487  0.1082  0.035   625 VAL B CB  
4115 C CG1 . VAL B 309 ? 2.136  1.1465 1.1524 -0.4809 0.1527  -0.0009 625 VAL B CG1 
4116 C CG2 . VAL B 309 ? 2.0813 1.1082 1.243  -0.4559 0.1065  0.0266  625 VAL B CG2 
4117 N N   . LYS B 310 ? 2.2066 1.1365 1.1021 -0.5542 0.0415  0.0845  626 LYS B N   
4118 C CA  . LYS B 310 ? 2.2577 1.1598 1.0628 -0.5826 0.0304  0.0935  626 LYS B CA  
4119 C C   . LYS B 310 ? 2.2921 1.1401 1.0858 -0.5698 -0.0292 0.1015  626 LYS B C   
4120 O O   . LYS B 310 ? 2.3176 1.141  1.0578 -0.5698 -0.0361 0.0899  626 LYS B O   
4121 C CB  . LYS B 310 ? 2.288  1.2079 1.0535 -0.6349 0.0347  0.1321  626 LYS B CB  
4122 C CG  . LYS B 310 ? 2.3375 1.3114 1.0829 -0.6529 0.1047  0.1174  626 LYS B CG  
4123 C CD  . LYS B 310 ? 2.4164 1.4111 1.1148 -0.7103 0.1103  0.1591  626 LYS B CD  
4124 C CE  . LYS B 310 ? 2.5166 1.4959 1.0986 -0.7453 0.1259  0.1558  626 LYS B CE  
4125 N NZ  . LYS B 310 ? 2.5594 1.559  1.0881 -0.8067 0.1297  0.2009  626 LYS B NZ  
4126 N N   . GLY B 311 ? 2.2907 1.1207 1.1376 -0.5576 -0.0711 0.119   627 GLY B N   
4127 C CA  . GLY B 311 ? 2.3225 1.1046 1.172  -0.5388 -0.1239 0.122   627 GLY B CA  
4128 C C   . GLY B 311 ? 2.3342 1.1097 1.2007 -0.496  -0.1163 0.084   627 GLY B C   
4129 O O   . GLY B 311 ? 2.3505 1.0979 1.1975 -0.4852 -0.1421 0.0794  627 GLY B O   
4130 N N   . MET B 312 ? 2.3211 1.1246 1.2282 -0.4733 -0.0822 0.0596  628 MET B N   
4131 C CA  . MET B 312 ? 2.3324 1.1337 1.2585 -0.4365 -0.0721 0.0264  628 MET B CA  
4132 C C   . MET B 312 ? 2.3724 1.1697 1.2432 -0.4405 -0.0522 0.0079  628 MET B C   
4133 O O   . MET B 312 ? 2.382  1.1592 1.2464 -0.4219 -0.0691 -0.0046 628 MET B O   
4134 C CB  . MET B 312 ? 2.3093 1.1433 1.2912 -0.4198 -0.0408 0.0113  628 MET B CB  
4135 C CG  . MET B 312 ? 2.3273 1.1596 1.3297 -0.3861 -0.0303 -0.0192 628 MET B CG  
4136 S SD  . MET B 312 ? 2.3774 1.1754 1.3971 -0.3588 -0.0759 -0.0214 628 MET B SD  
4137 C CE  . MET B 312 ? 2.3302 1.13   1.4018 -0.3596 -0.0969 -0.0034 628 MET B CE  
4138 N N   . ILE B 313 ? 2.3959 1.2117 1.2238 -0.467  -0.017  0.0065  629 ILE B N   
4139 C CA  . ILE B 313 ? 2.4427 1.2489 1.2081 -0.4747 0.0024  -0.014  629 ILE B CA  
4140 C C   . ILE B 313 ? 2.4983 1.2752 1.1932 -0.5063 -0.0299 0.0085  629 ILE B C   
4141 O O   . ILE B 313 ? 2.5229 1.2866 1.1573 -0.5184 -0.0202 -0.0055 629 ILE B O   
4142 C CB  . ILE B 313 ? 2.4463 1.2837 1.1962 -0.4838 0.0611  -0.0357 629 ILE B CB  
4143 C CG1 . ILE B 313 ? 2.4657 1.3244 1.18   -0.5255 0.077   -0.01   629 ILE B CG1 
4144 C CG2 . ILE B 313 ? 2.4168 1.2819 1.2473 -0.4503 0.0869  -0.0561 629 ILE B CG2 
4145 C CD1 . ILE B 313 ? 2.4769 1.372  1.1722 -0.5358 0.1423  -0.0338 629 ILE B CD1 
4146 N N   . GLY B 314 ? 2.5171 1.2799 1.2218 -0.5196 -0.0718 0.0431  630 GLY B N   
4147 C CA  . GLY B 314 ? 2.5671 1.2997 1.2203 -0.5478 -0.1129 0.0707  630 GLY B CA  
4148 C C   . GLY B 314 ? 2.613  1.348  1.1934 -0.5991 -0.1051 0.0957  630 GLY B C   
4149 O O   . GLY B 314 ? 2.6426 1.3507 1.1663 -0.6268 -0.1368 0.1161  630 GLY B O   
4150 N N   . ASP B 315 ? 2.6165 1.3857 1.1993 -0.6148 -0.0645 0.0974  631 ASP B N   
4151 C CA  . ASP B 315 ? 2.6582 1.4393 1.1704 -0.6669 -0.0474 0.1212  631 ASP B CA  
4152 C C   . ASP B 315 ? 2.6751 1.4422 1.1933 -0.6981 -0.0952 0.1737  631 ASP B C   
4153 O O   . ASP B 315 ? 2.7038 1.4571 1.1497 -0.7455 -0.1122 0.205   631 ASP B O   
4154 C CB  . ASP B 315 ? 2.6643 1.4972 1.1913 -0.6685 0.0203  0.1016  631 ASP B CB  
4155 C CG  . ASP B 315 ? 2.739  1.5842 1.2281 -0.6572 0.0757  0.0543  631 ASP B CG  
4156 O OD1 . ASP B 315 ? 2.7725 1.5837 1.2271 -0.6447 0.0606  0.0336  631 ASP B OD1 
4157 O OD2 . ASP B 315 ? 2.7513 1.64   1.2495 -0.6605 0.1337  0.0375  631 ASP B OD2 
4158 N N   . LEU B 316 ? 2.6564 1.4245 1.2586 -0.6738 -0.1177 0.1833  632 LEU B N   
4159 C CA  . LEU B 316 ? 2.669  1.4197 1.2955 -0.696  -0.165  0.2289  632 LEU B CA  
4160 C C   . LEU B 316 ? 2.6966 1.3931 1.3181 -0.696  -0.2345 0.2525  632 LEU B C   
4161 O O   . LEU B 316 ? 2.6915 1.3624 1.3594 -0.6931 -0.2808 0.2778  632 LEU B O   
4162 C CB  . LEU B 316 ? 2.6398 1.4056 1.3569 -0.6659 -0.1636 0.2228  632 LEU B CB  
4163 C CG  . LEU B 316 ? 2.6449 1.4425 1.3857 -0.6981 -0.1515 0.2535  632 LEU B CG  
4164 C CD1 . LEU B 316 ? 2.661  1.4194 1.4107 -0.724  -0.2152 0.301   632 LEU B CD1 
4165 C CD2 . LEU B 316 ? 2.6596 1.5057 1.344  -0.7378 -0.0935 0.2571  632 LEU B CD2 
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