data_9CFP
# 
_entry.id   9CFP 
# 
_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   9CFP         pdb_00009cfp 10.2210/pdb9cfp/pdb 
WWPDB D_1000285425 ?            ?                   
EMDB  EMD-45554    ?            ?                   
# 
_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       2025-04-23 
_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                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9CFP 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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           N 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB  .                                                                              9CFL      unspecified            
EMDB 'Cryo-EM structure of S. aureus TarGH in complex with AMP-PNP and targocil-II' EMD-45554 'associated EM volume' 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              natalie.strynadka@ubc.ca 
_pdbx_contact_author.name_first         Natalie 
_pdbx_contact_author.name_last          Strynadka 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4058-9425 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Peters, S.C.'      1 ? 
'Worrall, L.J.'     2 ? 
'Strynadka, N.C.J.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            16 
_citation.language                  ? 
_citation.page_first                3224 
_citation.page_last                 3224 
_citation.title                     
'Cryo-EM analyses unveil details of mechanism and targocil-II mediated inhibition of S. aureus WTA transporter TarGH.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-025-58202-w 
_citation.pdbx_database_id_PubMed   40185711 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Li, F.K.K.'        1  0000-0001-7318-9754 
primary 'Peters, S.C.'      2  0000-0002-5997-9685 
primary 'Worrall, L.J.'     3  ?                   
primary 'Sun, T.'           4  ?                   
primary 'Hu, J.'            5  ?                   
primary 'Vuckovic, M.'      6  ?                   
primary 'Farha, M.'         7  ?                   
primary 'Palacios, A.'      8  ?                   
primary 'Caveney, N.A.'     9  0000-0003-4828-3479 
primary 'Brown, E.D.'       10 0000-0002-7624-8112 
primary 'Strynadka, N.C.J.' 11 0000-0002-4058-9425 
# 
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 'Transport permease protein'                     34240.527 2 ?       ? ? ? 
2 polymer     man 'Teichoic acids export ATP-binding protein TagH' 29806.553 2 7.5.2.4 ? ? ? 
3 non-polymer syn Targocil-II                                      479.909   2 ?       ? ? ? 
4 non-polymer syn 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER'    506.196   2 ?       ? ? ? 
5 non-polymer syn 'MAGNESIUM ION'                                  24.305    2 ?       ? ? ? 
6 water       nat water                                            18.015    6 ?       ? ? ? 
# 
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 
;MGSSHHHHHHHHHHSSGLVPRGSHMSAIGTVFKEHVKNFYLIQRLAQFQVKIINHSNYLGVAWELINPVMQIMVYWMVFG
LGIRSNAPIHGVPFVYWLLVGISMWFFINQGILEGTKAITQKFNQVSKMNFPLSIIPTYIVTSRFYGHLGLLLLVIIACM
FTGIYPSIHIIQLLIYVPFCFFLTASVTLLTSTLGVLVRDTQMLMQAILRILFYFSPILWLPKNHGISGLIHEMMKYNPV
YFIAESYRAAILYHEWYFMDHWKLMLYNFGIVAIFFAIGAYLHMKYRDQFADFL
;
;MGSSHHHHHHHHHHSSGLVPRGSHMSAIGTVFKEHVKNFYLIQRLAQFQVKIINHSNYLGVAWELINPVMQIMVYWMVFG
LGIRSNAPIHGVPFVYWLLVGISMWFFINQGILEGTKAITQKFNQVSKMNFPLSIIPTYIVTSRFYGHLGLLLLVIIACM
FTGIYPSIHIIQLLIYVPFCFFLTASVTLLTSTLGVLVRDTQMLMQAILRILFYFSPILWLPKNHGISGLIHEMMKYNPV
YFIAESYRAAILYHEWYFMDHWKLMLYNFGIVAIFFAIGAYLHMKYRDQFADFL
;
A,C ? 
2 'polypeptide(L)' no no 
;MNVSVNIKNVTKEYRIYRTNKERMKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK
VDRNGEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITV
NPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLND
FKKKSKAEQKEFRNKLDESRFVIK
;
;MNVSVNIKNVTKEYRIYRTNKERMKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK
VDRNGEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITV
NPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLND
FKKKSKAEQKEFRNKLDESRFVIK
;
B,D ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 Targocil-II                                   A1AV9 
4 'PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER' ANP   
5 'MAGNESIUM ION'                               MG    
6 water                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  HIS n 
1 12  HIS n 
1 13  HIS n 
1 14  HIS n 
1 15  SER n 
1 16  SER n 
1 17  GLY n 
1 18  LEU n 
1 19  VAL n 
1 20  PRO n 
1 21  ARG n 
1 22  GLY n 
1 23  SER n 
1 24  HIS n 
1 25  MET n 
1 26  SER n 
1 27  ALA n 
1 28  ILE n 
1 29  GLY n 
1 30  THR n 
1 31  VAL n 
1 32  PHE n 
1 33  LYS n 
1 34  GLU n 
1 35  HIS n 
1 36  VAL n 
1 37  LYS n 
1 38  ASN n 
1 39  PHE n 
1 40  TYR n 
1 41  LEU n 
1 42  ILE n 
1 43  GLN n 
1 44  ARG n 
1 45  LEU n 
1 46  ALA n 
1 47  GLN n 
1 48  PHE n 
1 49  GLN n 
1 50  VAL n 
1 51  LYS n 
1 52  ILE n 
1 53  ILE n 
1 54  ASN n 
1 55  HIS n 
1 56  SER n 
1 57  ASN n 
1 58  TYR n 
1 59  LEU n 
1 60  GLY n 
1 61  VAL n 
1 62  ALA n 
1 63  TRP n 
1 64  GLU n 
1 65  LEU n 
1 66  ILE n 
1 67  ASN n 
1 68  PRO n 
1 69  VAL n 
1 70  MET n 
1 71  GLN n 
1 72  ILE n 
1 73  MET n 
1 74  VAL n 
1 75  TYR n 
1 76  TRP n 
1 77  MET n 
1 78  VAL n 
1 79  PHE n 
1 80  GLY n 
1 81  LEU n 
1 82  GLY n 
1 83  ILE n 
1 84  ARG n 
1 85  SER n 
1 86  ASN n 
1 87  ALA n 
1 88  PRO n 
1 89  ILE n 
1 90  HIS n 
1 91  GLY n 
1 92  VAL n 
1 93  PRO n 
1 94  PHE n 
1 95  VAL n 
1 96  TYR n 
1 97  TRP n 
1 98  LEU n 
1 99  LEU n 
1 100 VAL n 
1 101 GLY n 
1 102 ILE n 
1 103 SER n 
1 104 MET n 
1 105 TRP n 
1 106 PHE n 
1 107 PHE n 
1 108 ILE n 
1 109 ASN n 
1 110 GLN n 
1 111 GLY n 
1 112 ILE n 
1 113 LEU n 
1 114 GLU n 
1 115 GLY n 
1 116 THR n 
1 117 LYS n 
1 118 ALA n 
1 119 ILE n 
1 120 THR n 
1 121 GLN n 
1 122 LYS n 
1 123 PHE n 
1 124 ASN n 
1 125 GLN n 
1 126 VAL n 
1 127 SER n 
1 128 LYS n 
1 129 MET n 
1 130 ASN n 
1 131 PHE n 
1 132 PRO n 
1 133 LEU n 
1 134 SER n 
1 135 ILE n 
1 136 ILE n 
1 137 PRO n 
1 138 THR n 
1 139 TYR n 
1 140 ILE n 
1 141 VAL n 
1 142 THR n 
1 143 SER n 
1 144 ARG n 
1 145 PHE n 
1 146 TYR n 
1 147 GLY n 
1 148 HIS n 
1 149 LEU n 
1 150 GLY n 
1 151 LEU n 
1 152 LEU n 
1 153 LEU n 
1 154 LEU n 
1 155 VAL n 
1 156 ILE n 
1 157 ILE n 
1 158 ALA n 
1 159 CYS n 
1 160 MET n 
1 161 PHE n 
1 162 THR n 
1 163 GLY n 
1 164 ILE n 
1 165 TYR n 
1 166 PRO n 
1 167 SER n 
1 168 ILE n 
1 169 HIS n 
1 170 ILE n 
1 171 ILE n 
1 172 GLN n 
1 173 LEU n 
1 174 LEU n 
1 175 ILE n 
1 176 TYR n 
1 177 VAL n 
1 178 PRO n 
1 179 PHE n 
1 180 CYS n 
1 181 PHE n 
1 182 PHE n 
1 183 LEU n 
1 184 THR n 
1 185 ALA n 
1 186 SER n 
1 187 VAL n 
1 188 THR n 
1 189 LEU n 
1 190 LEU n 
1 191 THR n 
1 192 SER n 
1 193 THR n 
1 194 LEU n 
1 195 GLY n 
1 196 VAL n 
1 197 LEU n 
1 198 VAL n 
1 199 ARG n 
1 200 ASP n 
1 201 THR n 
1 202 GLN n 
1 203 MET n 
1 204 LEU n 
1 205 MET n 
1 206 GLN n 
1 207 ALA n 
1 208 ILE n 
1 209 LEU n 
1 210 ARG n 
1 211 ILE n 
1 212 LEU n 
1 213 PHE n 
1 214 TYR n 
1 215 PHE n 
1 216 SER n 
1 217 PRO n 
1 218 ILE n 
1 219 LEU n 
1 220 TRP n 
1 221 LEU n 
1 222 PRO n 
1 223 LYS n 
1 224 ASN n 
1 225 HIS n 
1 226 GLY n 
1 227 ILE n 
1 228 SER n 
1 229 GLY n 
1 230 LEU n 
1 231 ILE n 
1 232 HIS n 
1 233 GLU n 
1 234 MET n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 PRO n 
1 240 VAL n 
1 241 TYR n 
1 242 PHE n 
1 243 ILE n 
1 244 ALA n 
1 245 GLU n 
1 246 SER n 
1 247 TYR n 
1 248 ARG n 
1 249 ALA n 
1 250 ALA n 
1 251 ILE n 
1 252 LEU n 
1 253 TYR n 
1 254 HIS n 
1 255 GLU n 
1 256 TRP n 
1 257 TYR n 
1 258 PHE n 
1 259 MET n 
1 260 ASP n 
1 261 HIS n 
1 262 TRP n 
1 263 LYS n 
1 264 LEU n 
1 265 MET n 
1 266 LEU n 
1 267 TYR n 
1 268 ASN n 
1 269 PHE n 
1 270 GLY n 
1 271 ILE n 
1 272 VAL n 
1 273 ALA n 
1 274 ILE n 
1 275 PHE n 
1 276 PHE n 
1 277 ALA n 
1 278 ILE n 
1 279 GLY n 
1 280 ALA n 
1 281 TYR n 
1 282 LEU n 
1 283 HIS n 
1 284 MET n 
1 285 LYS n 
1 286 TYR n 
1 287 ARG n 
1 288 ASP n 
1 289 GLN n 
1 290 PHE n 
1 291 ALA n 
1 292 ASP n 
1 293 PHE n 
1 294 LEU n 
2 1   MET n 
2 2   ASN n 
2 3   VAL n 
2 4   SER n 
2 5   VAL n 
2 6   ASN n 
2 7   ILE n 
2 8   LYS n 
2 9   ASN n 
2 10  VAL n 
2 11  THR n 
2 12  LYS n 
2 13  GLU n 
2 14  TYR n 
2 15  ARG n 
2 16  ILE n 
2 17  TYR n 
2 18  ARG n 
2 19  THR n 
2 20  ASN n 
2 21  LYS n 
2 22  GLU n 
2 23  ARG n 
2 24  MET n 
2 25  LYS n 
2 26  ASP n 
2 27  ALA n 
2 28  LEU n 
2 29  ILE n 
2 30  PRO n 
2 31  LYS n 
2 32  HIS n 
2 33  LYS n 
2 34  ASN n 
2 35  LYS n 
2 36  THR n 
2 37  PHE n 
2 38  PHE n 
2 39  ALA n 
2 40  LEU n 
2 41  ASP n 
2 42  ASP n 
2 43  ILE n 
2 44  SER n 
2 45  LEU n 
2 46  LYS n 
2 47  ALA n 
2 48  TYR n 
2 49  GLU n 
2 50  GLY n 
2 51  ASP n 
2 52  VAL n 
2 53  ILE n 
2 54  GLY n 
2 55  LEU n 
2 56  VAL n 
2 57  GLY n 
2 58  ILE n 
2 59  ASN n 
2 60  GLY n 
2 61  SER n 
2 62  GLY n 
2 63  LYS n 
2 64  SER n 
2 65  THR n 
2 66  LEU n 
2 67  SER n 
2 68  ASN n 
2 69  ILE n 
2 70  ILE n 
2 71  GLY n 
2 72  GLY n 
2 73  SER n 
2 74  LEU n 
2 75  SER n 
2 76  PRO n 
2 77  THR n 
2 78  VAL n 
2 79  GLY n 
2 80  LYS n 
2 81  VAL n 
2 82  ASP n 
2 83  ARG n 
2 84  ASN n 
2 85  GLY n 
2 86  GLU n 
2 87  VAL n 
2 88  SER n 
2 89  VAL n 
2 90  ILE n 
2 91  ALA n 
2 92  ILE n 
2 93  SER n 
2 94  ALA n 
2 95  GLY n 
2 96  LEU n 
2 97  SER n 
2 98  GLY n 
2 99  GLN n 
2 100 LEU n 
2 101 THR n 
2 102 GLY n 
2 103 ILE n 
2 104 GLU n 
2 105 ASN n 
2 106 ILE n 
2 107 GLU n 
2 108 PHE n 
2 109 LYS n 
2 110 MET n 
2 111 LEU n 
2 112 CYS n 
2 113 MET n 
2 114 GLY n 
2 115 PHE n 
2 116 LYS n 
2 117 ARG n 
2 118 LYS n 
2 119 GLU n 
2 120 ILE n 
2 121 LYS n 
2 122 ALA n 
2 123 MET n 
2 124 THR n 
2 125 PRO n 
2 126 LYS n 
2 127 ILE n 
2 128 ILE n 
2 129 GLU n 
2 130 PHE n 
2 131 SER n 
2 132 GLU n 
2 133 LEU n 
2 134 GLY n 
2 135 GLU n 
2 136 PHE n 
2 137 ILE n 
2 138 TYR n 
2 139 GLN n 
2 140 PRO n 
2 141 VAL n 
2 142 LYS n 
2 143 LYS n 
2 144 TYR n 
2 145 SER n 
2 146 SER n 
2 147 GLY n 
2 148 MET n 
2 149 ARG n 
2 150 ALA n 
2 151 LYS n 
2 152 LEU n 
2 153 GLY n 
2 154 PHE n 
2 155 SER n 
2 156 ILE n 
2 157 ASN n 
2 158 ILE n 
2 159 THR n 
2 160 VAL n 
2 161 ASN n 
2 162 PRO n 
2 163 ASP n 
2 164 ILE n 
2 165 LEU n 
2 166 VAL n 
2 167 ILE n 
2 168 ASP n 
2 169 GLU n 
2 170 ALA n 
2 171 LEU n 
2 172 SER n 
2 173 VAL n 
2 174 GLY n 
2 175 ASP n 
2 176 GLN n 
2 177 THR n 
2 178 PHE n 
2 179 ALA n 
2 180 GLN n 
2 181 LYS n 
2 182 CYS n 
2 183 LEU n 
2 184 ASP n 
2 185 LYS n 
2 186 ILE n 
2 187 TYR n 
2 188 GLU n 
2 189 PHE n 
2 190 LYS n 
2 191 GLU n 
2 192 GLN n 
2 193 ASN n 
2 194 LYS n 
2 195 THR n 
2 196 ILE n 
2 197 PHE n 
2 198 PHE n 
2 199 VAL n 
2 200 SER n 
2 201 HIS n 
2 202 ASN n 
2 203 LEU n 
2 204 GLY n 
2 205 GLN n 
2 206 VAL n 
2 207 ARG n 
2 208 GLN n 
2 209 PHE n 
2 210 CYS n 
2 211 THR n 
2 212 LYS n 
2 213 ILE n 
2 214 ALA n 
2 215 TRP n 
2 216 ILE n 
2 217 GLU n 
2 218 GLY n 
2 219 GLY n 
2 220 LYS n 
2 221 LEU n 
2 222 LYS n 
2 223 ASP n 
2 224 TYR n 
2 225 GLY n 
2 226 GLU n 
2 227 LEU n 
2 228 ASP n 
2 229 ASP n 
2 230 VAL n 
2 231 LEU n 
2 232 PRO n 
2 233 LYS n 
2 234 TYR n 
2 235 GLU n 
2 236 ALA n 
2 237 PHE n 
2 238 LEU n 
2 239 ASN n 
2 240 ASP n 
2 241 PHE n 
2 242 LYS n 
2 243 LYS n 
2 244 LYS n 
2 245 SER n 
2 246 LYS n 
2 247 ALA n 
2 248 GLU n 
2 249 GLN n 
2 250 LYS n 
2 251 GLU n 
2 252 PHE n 
2 253 ARG n 
2 254 ASN n 
2 255 LYS n 
2 256 LEU n 
2 257 ASP n 
2 258 GLU n 
2 259 SER n 
2 260 ARG n 
2 261 PHE n 
2 262 VAL n 
2 263 ILE n 
2 264 LYS 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' 1 294 ? ? 'tagG, SAUSA300_0625' ? ? ? ? ? ? 'Staphylococcus aureus' 1280 ? ? ? ? ? ? ? ? 
'Lactococcus lactis' 1358 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 264 ? ? 'tagH, SAUSA300_0624' ? ? ? ? ? ? 'Staphylococcus aureus' 1280 ? ? ? ? ? ? ? ? 
'Lactococcus lactis' 1358 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
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 
A1AV9 non-polymer         . Targocil-II                                   
'1-{[3-(4-chlorophenyl)-5,9-dimethyl-7-oxo-7H-furo[3,2-g][1]benzopyran-6-yl]acetyl}-D-proline' 'C26 H22 Cl N O6'   479.909 
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   MET 1   -23 ?   ?   ?   A . n 
A 1 2   GLY 2   -22 ?   ?   ?   A . n 
A 1 3   SER 3   -21 ?   ?   ?   A . n 
A 1 4   SER 4   -20 ?   ?   ?   A . n 
A 1 5   HIS 5   -19 ?   ?   ?   A . n 
A 1 6   HIS 6   -18 ?   ?   ?   A . n 
A 1 7   HIS 7   -17 ?   ?   ?   A . n 
A 1 8   HIS 8   -16 ?   ?   ?   A . n 
A 1 9   HIS 9   -15 ?   ?   ?   A . n 
A 1 10  HIS 10  -14 ?   ?   ?   A . n 
A 1 11  HIS 11  -13 ?   ?   ?   A . n 
A 1 12  HIS 12  -12 ?   ?   ?   A . n 
A 1 13  HIS 13  -11 ?   ?   ?   A . n 
A 1 14  HIS 14  -10 ?   ?   ?   A . n 
A 1 15  SER 15  -9  ?   ?   ?   A . n 
A 1 16  SER 16  -8  ?   ?   ?   A . n 
A 1 17  GLY 17  -7  ?   ?   ?   A . n 
A 1 18  LEU 18  -6  ?   ?   ?   A . n 
A 1 19  VAL 19  -5  ?   ?   ?   A . n 
A 1 20  PRO 20  -4  ?   ?   ?   A . n 
A 1 21  ARG 21  -3  ?   ?   ?   A . n 
A 1 22  GLY 22  -2  ?   ?   ?   A . n 
A 1 23  SER 23  -1  ?   ?   ?   A . n 
A 1 24  HIS 24  0   ?   ?   ?   A . n 
A 1 25  MET 25  1   1   MET MET A . n 
A 1 26  SER 26  2   2   SER SER A . n 
A 1 27  ALA 27  3   3   ALA ALA A . n 
A 1 28  ILE 28  4   4   ILE ILE A . n 
A 1 29  GLY 29  5   5   GLY GLY A . n 
A 1 30  THR 30  6   6   THR THR A . n 
A 1 31  VAL 31  7   7   VAL VAL A . n 
A 1 32  PHE 32  8   8   PHE PHE A . n 
A 1 33  LYS 33  9   9   LYS LYS A . n 
A 1 34  GLU 34  10  10  GLU GLU A . n 
A 1 35  HIS 35  11  11  HIS HIS A . n 
A 1 36  VAL 36  12  12  VAL VAL A . n 
A 1 37  LYS 37  13  13  LYS LYS A . n 
A 1 38  ASN 38  14  14  ASN ASN A . n 
A 1 39  PHE 39  15  15  PHE PHE A . n 
A 1 40  TYR 40  16  16  TYR TYR A . n 
A 1 41  LEU 41  17  17  LEU LEU A . n 
A 1 42  ILE 42  18  18  ILE ILE A . n 
A 1 43  GLN 43  19  19  GLN GLN A . n 
A 1 44  ARG 44  20  20  ARG ARG A . n 
A 1 45  LEU 45  21  21  LEU LEU A . n 
A 1 46  ALA 46  22  22  ALA ALA A . n 
A 1 47  GLN 47  23  23  GLN GLN A . n 
A 1 48  PHE 48  24  24  PHE PHE A . n 
A 1 49  GLN 49  25  25  GLN GLN A . n 
A 1 50  VAL 50  26  26  VAL VAL A . n 
A 1 51  LYS 51  27  27  LYS LYS A . n 
A 1 52  ILE 52  28  28  ILE ILE A . n 
A 1 53  ILE 53  29  29  ILE ILE A . n 
A 1 54  ASN 54  30  30  ASN ASN A . n 
A 1 55  HIS 55  31  31  HIS HIS A . n 
A 1 56  SER 56  32  32  SER SER A . n 
A 1 57  ASN 57  33  33  ASN ASN A . n 
A 1 58  TYR 58  34  34  TYR TYR A . n 
A 1 59  LEU 59  35  35  LEU LEU A . n 
A 1 60  GLY 60  36  36  GLY GLY A . n 
A 1 61  VAL 61  37  37  VAL VAL A . n 
A 1 62  ALA 62  38  38  ALA ALA A . n 
A 1 63  TRP 63  39  39  TRP TRP A . n 
A 1 64  GLU 64  40  40  GLU GLU A . n 
A 1 65  LEU 65  41  41  LEU LEU A . n 
A 1 66  ILE 66  42  42  ILE ILE A . n 
A 1 67  ASN 67  43  43  ASN ASN A . n 
A 1 68  PRO 68  44  44  PRO PRO A . n 
A 1 69  VAL 69  45  45  VAL VAL A . n 
A 1 70  MET 70  46  46  MET MET A . n 
A 1 71  GLN 71  47  47  GLN GLN A . n 
A 1 72  ILE 72  48  48  ILE ILE A . n 
A 1 73  MET 73  49  49  MET MET A . n 
A 1 74  VAL 74  50  50  VAL VAL A . n 
A 1 75  TYR 75  51  51  TYR TYR A . n 
A 1 76  TRP 76  52  52  TRP TRP A . n 
A 1 77  MET 77  53  53  MET MET A . n 
A 1 78  VAL 78  54  54  VAL VAL A . n 
A 1 79  PHE 79  55  55  PHE PHE A . n 
A 1 80  GLY 80  56  56  GLY GLY A . n 
A 1 81  LEU 81  57  57  LEU LEU A . n 
A 1 82  GLY 82  58  58  GLY GLY A . n 
A 1 83  ILE 83  59  59  ILE ILE A . n 
A 1 84  ARG 84  60  60  ARG ARG A . n 
A 1 85  SER 85  61  61  SER SER A . n 
A 1 86  ASN 86  62  62  ASN ASN A . n 
A 1 87  ALA 87  63  63  ALA ALA A . n 
A 1 88  PRO 88  64  64  PRO PRO A . n 
A 1 89  ILE 89  65  65  ILE ILE A . n 
A 1 90  HIS 90  66  66  HIS HIS A . n 
A 1 91  GLY 91  67  67  GLY GLY A . n 
A 1 92  VAL 92  68  68  VAL VAL A . n 
A 1 93  PRO 93  69  69  PRO PRO A . n 
A 1 94  PHE 94  70  70  PHE PHE A . n 
A 1 95  VAL 95  71  71  VAL VAL A . n 
A 1 96  TYR 96  72  72  TYR TYR A . n 
A 1 97  TRP 97  73  73  TRP TRP A . n 
A 1 98  LEU 98  74  74  LEU LEU A . n 
A 1 99  LEU 99  75  75  LEU LEU A . n 
A 1 100 VAL 100 76  76  VAL VAL A . n 
A 1 101 GLY 101 77  77  GLY GLY A . n 
A 1 102 ILE 102 78  78  ILE ILE A . n 
A 1 103 SER 103 79  79  SER SER A . n 
A 1 104 MET 104 80  80  MET MET A . n 
A 1 105 TRP 105 81  81  TRP TRP A . n 
A 1 106 PHE 106 82  82  PHE PHE A . n 
A 1 107 PHE 107 83  83  PHE PHE A . n 
A 1 108 ILE 108 84  84  ILE ILE A . n 
A 1 109 ASN 109 85  85  ASN ASN A . n 
A 1 110 GLN 110 86  86  GLN GLN A . n 
A 1 111 GLY 111 87  87  GLY GLY A . n 
A 1 112 ILE 112 88  88  ILE ILE A . n 
A 1 113 LEU 113 89  89  LEU LEU A . n 
A 1 114 GLU 114 90  90  GLU GLU A . n 
A 1 115 GLY 115 91  91  GLY GLY A . n 
A 1 116 THR 116 92  92  THR THR A . n 
A 1 117 LYS 117 93  93  LYS LYS A . n 
A 1 118 ALA 118 94  94  ALA ALA A . n 
A 1 119 ILE 119 95  95  ILE ILE A . n 
A 1 120 THR 120 96  96  THR THR A . n 
A 1 121 GLN 121 97  97  GLN GLN A . n 
A 1 122 LYS 122 98  98  LYS LYS A . n 
A 1 123 PHE 123 99  99  PHE PHE A . n 
A 1 124 ASN 124 100 100 ASN ASN A . n 
A 1 125 GLN 125 101 101 GLN GLN A . n 
A 1 126 VAL 126 102 102 VAL VAL A . n 
A 1 127 SER 127 103 103 SER SER A . n 
A 1 128 LYS 128 104 104 LYS LYS A . n 
A 1 129 MET 129 105 105 MET MET A . n 
A 1 130 ASN 130 106 106 ASN ASN A . n 
A 1 131 PHE 131 107 107 PHE PHE A . n 
A 1 132 PRO 132 108 108 PRO PRO A . n 
A 1 133 LEU 133 109 109 LEU LEU A . n 
A 1 134 SER 134 110 110 SER SER A . n 
A 1 135 ILE 135 111 111 ILE ILE A . n 
A 1 136 ILE 136 112 112 ILE ILE A . n 
A 1 137 PRO 137 113 113 PRO PRO A . n 
A 1 138 THR 138 114 114 THR THR A . n 
A 1 139 TYR 139 115 115 TYR TYR A . n 
A 1 140 ILE 140 116 116 ILE ILE A . n 
A 1 141 VAL 141 117 117 VAL VAL A . n 
A 1 142 THR 142 118 118 THR THR A . n 
A 1 143 SER 143 119 119 SER SER A . n 
A 1 144 ARG 144 120 120 ARG ARG A . n 
A 1 145 PHE 145 121 121 PHE PHE A . n 
A 1 146 TYR 146 122 122 TYR TYR A . n 
A 1 147 GLY 147 123 123 GLY GLY A . n 
A 1 148 HIS 148 124 124 HIS HIS A . n 
A 1 149 LEU 149 125 125 LEU LEU A . n 
A 1 150 GLY 150 126 126 GLY GLY A . n 
A 1 151 LEU 151 127 127 LEU LEU A . n 
A 1 152 LEU 152 128 128 LEU LEU A . n 
A 1 153 LEU 153 129 129 LEU LEU A . n 
A 1 154 LEU 154 130 130 LEU LEU A . n 
A 1 155 VAL 155 131 131 VAL VAL A . n 
A 1 156 ILE 156 132 132 ILE ILE A . n 
A 1 157 ILE 157 133 133 ILE ILE A . n 
A 1 158 ALA 158 134 134 ALA ALA A . n 
A 1 159 CYS 159 135 135 CYS CYS A . n 
A 1 160 MET 160 136 136 MET MET A . n 
A 1 161 PHE 161 137 137 PHE PHE A . n 
A 1 162 THR 162 138 138 THR THR A . n 
A 1 163 GLY 163 139 139 GLY GLY A . n 
A 1 164 ILE 164 140 140 ILE ILE A . n 
A 1 165 TYR 165 141 141 TYR TYR A . n 
A 1 166 PRO 166 142 142 PRO PRO A . n 
A 1 167 SER 167 143 143 SER SER A . n 
A 1 168 ILE 168 144 144 ILE ILE A . n 
A 1 169 HIS 169 145 145 HIS HIS A . n 
A 1 170 ILE 170 146 146 ILE ILE A . n 
A 1 171 ILE 171 147 147 ILE ILE A . n 
A 1 172 GLN 172 148 148 GLN GLN A . n 
A 1 173 LEU 173 149 149 LEU LEU A . n 
A 1 174 LEU 174 150 150 LEU LEU A . n 
A 1 175 ILE 175 151 151 ILE ILE A . n 
A 1 176 TYR 176 152 152 TYR TYR A . n 
A 1 177 VAL 177 153 153 VAL VAL A . n 
A 1 178 PRO 178 154 154 PRO PRO A . n 
A 1 179 PHE 179 155 155 PHE PHE A . n 
A 1 180 CYS 180 156 156 CYS CYS A . n 
A 1 181 PHE 181 157 157 PHE PHE A . n 
A 1 182 PHE 182 158 158 PHE PHE A . n 
A 1 183 LEU 183 159 159 LEU LEU A . n 
A 1 184 THR 184 160 160 THR THR A . n 
A 1 185 ALA 185 161 161 ALA ALA A . n 
A 1 186 SER 186 162 162 SER SER A . n 
A 1 187 VAL 187 163 163 VAL VAL A . n 
A 1 188 THR 188 164 164 THR THR A . n 
A 1 189 LEU 189 165 165 LEU LEU A . n 
A 1 190 LEU 190 166 166 LEU LEU A . n 
A 1 191 THR 191 167 167 THR THR A . n 
A 1 192 SER 192 168 168 SER SER A . n 
A 1 193 THR 193 169 169 THR THR A . n 
A 1 194 LEU 194 170 170 LEU LEU A . n 
A 1 195 GLY 195 171 171 GLY GLY A . n 
A 1 196 VAL 196 172 172 VAL VAL A . n 
A 1 197 LEU 197 173 173 LEU LEU A . n 
A 1 198 VAL 198 174 174 VAL VAL A . n 
A 1 199 ARG 199 175 175 ARG ARG A . n 
A 1 200 ASP 200 176 176 ASP ASP A . n 
A 1 201 THR 201 177 177 THR THR A . n 
A 1 202 GLN 202 178 178 GLN GLN A . n 
A 1 203 MET 203 179 179 MET MET A . n 
A 1 204 LEU 204 180 180 LEU LEU A . n 
A 1 205 MET 205 181 181 MET MET A . n 
A 1 206 GLN 206 182 182 GLN GLN A . n 
A 1 207 ALA 207 183 183 ALA ALA A . n 
A 1 208 ILE 208 184 184 ILE ILE A . n 
A 1 209 LEU 209 185 185 LEU LEU A . n 
A 1 210 ARG 210 186 186 ARG ARG A . n 
A 1 211 ILE 211 187 187 ILE ILE A . n 
A 1 212 LEU 212 188 188 LEU LEU A . n 
A 1 213 PHE 213 189 189 PHE PHE A . n 
A 1 214 TYR 214 190 190 TYR TYR A . n 
A 1 215 PHE 215 191 191 PHE PHE A . n 
A 1 216 SER 216 192 192 SER SER A . n 
A 1 217 PRO 217 193 193 PRO PRO A . n 
A 1 218 ILE 218 194 194 ILE ILE A . n 
A 1 219 LEU 219 195 195 LEU LEU A . n 
A 1 220 TRP 220 196 196 TRP TRP A . n 
A 1 221 LEU 221 197 197 LEU LEU A . n 
A 1 222 PRO 222 198 198 PRO PRO A . n 
A 1 223 LYS 223 199 199 LYS LYS A . n 
A 1 224 ASN 224 200 200 ASN ASN A . n 
A 1 225 HIS 225 201 201 HIS HIS A . n 
A 1 226 GLY 226 202 202 GLY GLY A . n 
A 1 227 ILE 227 203 203 ILE ILE A . n 
A 1 228 SER 228 204 204 SER SER A . n 
A 1 229 GLY 229 205 205 GLY GLY A . n 
A 1 230 LEU 230 206 206 LEU LEU A . n 
A 1 231 ILE 231 207 207 ILE ILE A . n 
A 1 232 HIS 232 208 208 HIS HIS A . n 
A 1 233 GLU 233 209 209 GLU GLU A . n 
A 1 234 MET 234 210 210 MET MET A . n 
A 1 235 MET 235 211 211 MET MET A . n 
A 1 236 LYS 236 212 212 LYS LYS A . n 
A 1 237 TYR 237 213 213 TYR TYR A . n 
A 1 238 ASN 238 214 214 ASN ASN A . n 
A 1 239 PRO 239 215 215 PRO PRO A . n 
A 1 240 VAL 240 216 216 VAL VAL A . n 
A 1 241 TYR 241 217 217 TYR TYR A . n 
A 1 242 PHE 242 218 218 PHE PHE A . n 
A 1 243 ILE 243 219 219 ILE ILE A . n 
A 1 244 ALA 244 220 220 ALA ALA A . n 
A 1 245 GLU 245 221 221 GLU GLU A . n 
A 1 246 SER 246 222 222 SER SER A . n 
A 1 247 TYR 247 223 223 TYR TYR A . n 
A 1 248 ARG 248 224 224 ARG ARG A . n 
A 1 249 ALA 249 225 225 ALA ALA A . n 
A 1 250 ALA 250 226 226 ALA ALA A . n 
A 1 251 ILE 251 227 227 ILE ILE A . n 
A 1 252 LEU 252 228 228 LEU LEU A . n 
A 1 253 TYR 253 229 229 TYR TYR A . n 
A 1 254 HIS 254 230 230 HIS HIS A . n 
A 1 255 GLU 255 231 231 GLU GLU A . n 
A 1 256 TRP 256 232 232 TRP TRP A . n 
A 1 257 TYR 257 233 233 TYR TYR A . n 
A 1 258 PHE 258 234 234 PHE PHE A . n 
A 1 259 MET 259 235 235 MET MET A . n 
A 1 260 ASP 260 236 236 ASP ASP A . n 
A 1 261 HIS 261 237 237 HIS HIS A . n 
A 1 262 TRP 262 238 238 TRP TRP A . n 
A 1 263 LYS 263 239 239 LYS LYS A . n 
A 1 264 LEU 264 240 240 LEU LEU A . n 
A 1 265 MET 265 241 241 MET MET A . n 
A 1 266 LEU 266 242 242 LEU LEU A . n 
A 1 267 TYR 267 243 243 TYR TYR A . n 
A 1 268 ASN 268 244 244 ASN ASN A . n 
A 1 269 PHE 269 245 245 PHE PHE A . n 
A 1 270 GLY 270 246 246 GLY GLY A . n 
A 1 271 ILE 271 247 247 ILE ILE A . n 
A 1 272 VAL 272 248 248 VAL VAL A . n 
A 1 273 ALA 273 249 249 ALA ALA A . n 
A 1 274 ILE 274 250 250 ILE ILE A . n 
A 1 275 PHE 275 251 251 PHE PHE A . n 
A 1 276 PHE 276 252 252 PHE PHE A . n 
A 1 277 ALA 277 253 253 ALA ALA A . n 
A 1 278 ILE 278 254 254 ILE ILE A . n 
A 1 279 GLY 279 255 255 GLY GLY A . n 
A 1 280 ALA 280 256 256 ALA ALA A . n 
A 1 281 TYR 281 257 257 TYR TYR A . n 
A 1 282 LEU 282 258 258 LEU LEU A . n 
A 1 283 HIS 283 259 259 HIS HIS A . n 
A 1 284 MET 284 260 260 MET MET A . n 
A 1 285 LYS 285 261 261 LYS LYS A . n 
A 1 286 TYR 286 262 262 TYR TYR A . n 
A 1 287 ARG 287 263 263 ARG ARG A . n 
A 1 288 ASP 288 264 264 ASP ASP A . n 
A 1 289 GLN 289 265 265 GLN GLN A . n 
A 1 290 PHE 290 266 266 PHE PHE A . n 
A 1 291 ALA 291 267 267 ALA ALA A . n 
A 1 292 ASP 292 268 268 ASP ASP A . n 
A 1 293 PHE 293 269 269 PHE PHE A . n 
A 1 294 LEU 294 270 270 LEU LEU A . n 
B 2 1   MET 1   1   1   MET MET B . n 
B 2 2   ASN 2   2   2   ASN ASN B . n 
B 2 3   VAL 3   3   3   VAL VAL B . n 
B 2 4   SER 4   4   4   SER SER B . n 
B 2 5   VAL 5   5   5   VAL VAL B . n 
B 2 6   ASN 6   6   6   ASN ASN B . n 
B 2 7   ILE 7   7   7   ILE ILE B . n 
B 2 8   LYS 8   8   8   LYS LYS B . n 
B 2 9   ASN 9   9   9   ASN ASN B . n 
B 2 10  VAL 10  10  10  VAL VAL B . n 
B 2 11  THR 11  11  11  THR THR B . n 
B 2 12  LYS 12  12  12  LYS LYS B . n 
B 2 13  GLU 13  13  13  GLU GLU B . n 
B 2 14  TYR 14  14  14  TYR TYR B . n 
B 2 15  ARG 15  15  15  ARG ARG B . n 
B 2 16  ILE 16  16  16  ILE ILE B . n 
B 2 17  TYR 17  17  17  TYR TYR B . n 
B 2 18  ARG 18  18  18  ARG ARG B . n 
B 2 19  THR 19  19  19  THR THR B . n 
B 2 20  ASN 20  20  20  ASN ASN B . n 
B 2 21  LYS 21  21  21  LYS LYS B . n 
B 2 22  GLU 22  22  22  GLU GLU B . n 
B 2 23  ARG 23  23  23  ARG ARG B . n 
B 2 24  MET 24  24  24  MET MET B . n 
B 2 25  LYS 25  25  25  LYS LYS B . n 
B 2 26  ASP 26  26  26  ASP ASP B . n 
B 2 27  ALA 27  27  27  ALA ALA B . n 
B 2 28  LEU 28  28  28  LEU LEU B . n 
B 2 29  ILE 29  29  29  ILE ILE B . n 
B 2 30  PRO 30  30  30  PRO PRO B . n 
B 2 31  LYS 31  31  31  LYS LYS B . n 
B 2 32  HIS 32  32  32  HIS HIS B . n 
B 2 33  LYS 33  33  33  LYS LYS B . n 
B 2 34  ASN 34  34  34  ASN ASN B . n 
B 2 35  LYS 35  35  35  LYS LYS B . n 
B 2 36  THR 36  36  36  THR THR B . n 
B 2 37  PHE 37  37  37  PHE PHE B . n 
B 2 38  PHE 38  38  38  PHE PHE B . n 
B 2 39  ALA 39  39  39  ALA ALA B . n 
B 2 40  LEU 40  40  40  LEU LEU B . n 
B 2 41  ASP 41  41  41  ASP ASP B . n 
B 2 42  ASP 42  42  42  ASP ASP B . n 
B 2 43  ILE 43  43  43  ILE ILE B . n 
B 2 44  SER 44  44  44  SER SER B . n 
B 2 45  LEU 45  45  45  LEU LEU B . n 
B 2 46  LYS 46  46  46  LYS LYS B . n 
B 2 47  ALA 47  47  47  ALA ALA B . n 
B 2 48  TYR 48  48  48  TYR TYR B . n 
B 2 49  GLU 49  49  49  GLU GLU B . n 
B 2 50  GLY 50  50  50  GLY GLY B . n 
B 2 51  ASP 51  51  51  ASP ASP B . n 
B 2 52  VAL 52  52  52  VAL VAL B . n 
B 2 53  ILE 53  53  53  ILE ILE B . n 
B 2 54  GLY 54  54  54  GLY GLY B . n 
B 2 55  LEU 55  55  55  LEU LEU B . n 
B 2 56  VAL 56  56  56  VAL VAL B . n 
B 2 57  GLY 57  57  57  GLY GLY B . n 
B 2 58  ILE 58  58  58  ILE ILE B . n 
B 2 59  ASN 59  59  59  ASN ASN B . n 
B 2 60  GLY 60  60  60  GLY GLY B . n 
B 2 61  SER 61  61  61  SER SER B . n 
B 2 62  GLY 62  62  62  GLY GLY B . n 
B 2 63  LYS 63  63  63  LYS LYS B . n 
B 2 64  SER 64  64  64  SER SER B . n 
B 2 65  THR 65  65  65  THR THR B . n 
B 2 66  LEU 66  66  66  LEU LEU B . n 
B 2 67  SER 67  67  67  SER SER B . n 
B 2 68  ASN 68  68  68  ASN ASN B . n 
B 2 69  ILE 69  69  69  ILE ILE B . n 
B 2 70  ILE 70  70  70  ILE ILE B . n 
B 2 71  GLY 71  71  71  GLY GLY B . n 
B 2 72  GLY 72  72  72  GLY GLY B . n 
B 2 73  SER 73  73  73  SER SER B . n 
B 2 74  LEU 74  74  74  LEU LEU B . n 
B 2 75  SER 75  75  75  SER SER B . n 
B 2 76  PRO 76  76  76  PRO PRO B . n 
B 2 77  THR 77  77  77  THR THR B . n 
B 2 78  VAL 78  78  78  VAL VAL B . n 
B 2 79  GLY 79  79  79  GLY GLY B . n 
B 2 80  LYS 80  80  80  LYS LYS B . n 
B 2 81  VAL 81  81  81  VAL VAL B . n 
B 2 82  ASP 82  82  82  ASP ASP B . n 
B 2 83  ARG 83  83  83  ARG ARG B . n 
B 2 84  ASN 84  84  84  ASN ASN B . n 
B 2 85  GLY 85  85  85  GLY GLY B . n 
B 2 86  GLU 86  86  86  GLU GLU B . n 
B 2 87  VAL 87  87  87  VAL VAL B . n 
B 2 88  SER 88  88  88  SER SER B . n 
B 2 89  VAL 89  89  89  VAL VAL B . n 
B 2 90  ILE 90  90  90  ILE ILE B . n 
B 2 91  ALA 91  91  91  ALA ALA B . n 
B 2 92  ILE 92  92  92  ILE ILE B . n 
B 2 93  SER 93  93  93  SER SER B . n 
B 2 94  ALA 94  94  94  ALA ALA B . n 
B 2 95  GLY 95  95  95  GLY GLY B . n 
B 2 96  LEU 96  96  96  LEU LEU B . n 
B 2 97  SER 97  97  97  SER SER B . n 
B 2 98  GLY 98  98  98  GLY GLY B . n 
B 2 99  GLN 99  99  99  GLN GLN B . n 
B 2 100 LEU 100 100 100 LEU LEU B . n 
B 2 101 THR 101 101 101 THR THR B . n 
B 2 102 GLY 102 102 102 GLY GLY B . n 
B 2 103 ILE 103 103 103 ILE ILE B . n 
B 2 104 GLU 104 104 104 GLU GLU B . n 
B 2 105 ASN 105 105 105 ASN ASN B . n 
B 2 106 ILE 106 106 106 ILE ILE B . n 
B 2 107 GLU 107 107 107 GLU GLU B . n 
B 2 108 PHE 108 108 108 PHE PHE B . n 
B 2 109 LYS 109 109 109 LYS LYS B . n 
B 2 110 MET 110 110 110 MET MET B . n 
B 2 111 LEU 111 111 111 LEU LEU B . n 
B 2 112 CYS 112 112 112 CYS CYS B . n 
B 2 113 MET 113 113 113 MET MET B . n 
B 2 114 GLY 114 114 114 GLY GLY B . n 
B 2 115 PHE 115 115 115 PHE PHE B . n 
B 2 116 LYS 116 116 116 LYS LYS B . n 
B 2 117 ARG 117 117 117 ARG ARG B . n 
B 2 118 LYS 118 118 118 LYS LYS B . n 
B 2 119 GLU 119 119 119 GLU GLU B . n 
B 2 120 ILE 120 120 120 ILE ILE B . n 
B 2 121 LYS 121 121 121 LYS LYS B . n 
B 2 122 ALA 122 122 122 ALA ALA B . n 
B 2 123 MET 123 123 123 MET MET B . n 
B 2 124 THR 124 124 124 THR THR B . n 
B 2 125 PRO 125 125 125 PRO PRO B . n 
B 2 126 LYS 126 126 126 LYS LYS B . n 
B 2 127 ILE 127 127 127 ILE ILE B . n 
B 2 128 ILE 128 128 128 ILE ILE B . n 
B 2 129 GLU 129 129 129 GLU GLU B . n 
B 2 130 PHE 130 130 130 PHE PHE B . n 
B 2 131 SER 131 131 131 SER SER B . n 
B 2 132 GLU 132 132 132 GLU GLU B . n 
B 2 133 LEU 133 133 133 LEU LEU B . n 
B 2 134 GLY 134 134 134 GLY GLY B . n 
B 2 135 GLU 135 135 135 GLU GLU B . n 
B 2 136 PHE 136 136 136 PHE PHE B . n 
B 2 137 ILE 137 137 137 ILE ILE B . n 
B 2 138 TYR 138 138 138 TYR TYR B . n 
B 2 139 GLN 139 139 139 GLN GLN B . n 
B 2 140 PRO 140 140 140 PRO PRO B . n 
B 2 141 VAL 141 141 141 VAL VAL B . n 
B 2 142 LYS 142 142 142 LYS LYS B . n 
B 2 143 LYS 143 143 143 LYS LYS B . n 
B 2 144 TYR 144 144 144 TYR TYR B . n 
B 2 145 SER 145 145 145 SER SER B . n 
B 2 146 SER 146 146 146 SER SER B . n 
B 2 147 GLY 147 147 147 GLY GLY B . n 
B 2 148 MET 148 148 148 MET MET B . n 
B 2 149 ARG 149 149 149 ARG ARG B . n 
B 2 150 ALA 150 150 150 ALA ALA B . n 
B 2 151 LYS 151 151 151 LYS LYS B . n 
B 2 152 LEU 152 152 152 LEU LEU B . n 
B 2 153 GLY 153 153 153 GLY GLY B . n 
B 2 154 PHE 154 154 154 PHE PHE B . n 
B 2 155 SER 155 155 155 SER SER B . n 
B 2 156 ILE 156 156 156 ILE ILE B . n 
B 2 157 ASN 157 157 157 ASN ASN B . n 
B 2 158 ILE 158 158 158 ILE ILE B . n 
B 2 159 THR 159 159 159 THR THR B . n 
B 2 160 VAL 160 160 160 VAL VAL B . n 
B 2 161 ASN 161 161 161 ASN ASN B . n 
B 2 162 PRO 162 162 162 PRO PRO B . n 
B 2 163 ASP 163 163 163 ASP ASP B . n 
B 2 164 ILE 164 164 164 ILE ILE B . n 
B 2 165 LEU 165 165 165 LEU LEU B . n 
B 2 166 VAL 166 166 166 VAL VAL B . n 
B 2 167 ILE 167 167 167 ILE ILE B . n 
B 2 168 ASP 168 168 168 ASP ASP B . n 
B 2 169 GLU 169 169 169 GLU GLU B . n 
B 2 170 ALA 170 170 170 ALA ALA B . n 
B 2 171 LEU 171 171 171 LEU LEU B . n 
B 2 172 SER 172 172 172 SER SER B . n 
B 2 173 VAL 173 173 173 VAL VAL B . n 
B 2 174 GLY 174 174 174 GLY GLY B . n 
B 2 175 ASP 175 175 175 ASP ASP B . n 
B 2 176 GLN 176 176 176 GLN GLN B . n 
B 2 177 THR 177 177 177 THR THR B . n 
B 2 178 PHE 178 178 178 PHE PHE B . n 
B 2 179 ALA 179 179 179 ALA ALA B . n 
B 2 180 GLN 180 180 180 GLN GLN B . n 
B 2 181 LYS 181 181 181 LYS LYS B . n 
B 2 182 CYS 182 182 182 CYS CYS B . n 
B 2 183 LEU 183 183 183 LEU LEU B . n 
B 2 184 ASP 184 184 184 ASP ASP B . n 
B 2 185 LYS 185 185 185 LYS LYS B . n 
B 2 186 ILE 186 186 186 ILE ILE B . n 
B 2 187 TYR 187 187 187 TYR TYR B . n 
B 2 188 GLU 188 188 188 GLU GLU B . n 
B 2 189 PHE 189 189 189 PHE PHE B . n 
B 2 190 LYS 190 190 190 LYS LYS B . n 
B 2 191 GLU 191 191 191 GLU GLU B . n 
B 2 192 GLN 192 192 192 GLN GLN B . n 
B 2 193 ASN 193 193 193 ASN ASN B . n 
B 2 194 LYS 194 194 194 LYS LYS B . n 
B 2 195 THR 195 195 195 THR THR B . n 
B 2 196 ILE 196 196 196 ILE ILE B . n 
B 2 197 PHE 197 197 197 PHE PHE B . n 
B 2 198 PHE 198 198 198 PHE PHE B . n 
B 2 199 VAL 199 199 199 VAL VAL B . n 
B 2 200 SER 200 200 200 SER SER B . n 
B 2 201 HIS 201 201 201 HIS HIS B . n 
B 2 202 ASN 202 202 202 ASN ASN B . n 
B 2 203 LEU 203 203 203 LEU LEU B . n 
B 2 204 GLY 204 204 204 GLY GLY B . n 
B 2 205 GLN 205 205 205 GLN GLN B . n 
B 2 206 VAL 206 206 206 VAL VAL B . n 
B 2 207 ARG 207 207 207 ARG ARG B . n 
B 2 208 GLN 208 208 208 GLN GLN B . n 
B 2 209 PHE 209 209 209 PHE PHE B . n 
B 2 210 CYS 210 210 210 CYS CYS B . n 
B 2 211 THR 211 211 211 THR THR B . n 
B 2 212 LYS 212 212 212 LYS LYS B . n 
B 2 213 ILE 213 213 213 ILE ILE B . n 
B 2 214 ALA 214 214 214 ALA ALA B . n 
B 2 215 TRP 215 215 215 TRP TRP B . n 
B 2 216 ILE 216 216 216 ILE ILE B . n 
B 2 217 GLU 217 217 217 GLU GLU B . n 
B 2 218 GLY 218 218 218 GLY GLY B . n 
B 2 219 GLY 219 219 219 GLY GLY B . n 
B 2 220 LYS 220 220 220 LYS LYS B . n 
B 2 221 LEU 221 221 221 LEU LEU B . n 
B 2 222 LYS 222 222 222 LYS LYS B . n 
B 2 223 ASP 223 223 223 ASP ASP B . n 
B 2 224 TYR 224 224 224 TYR TYR B . n 
B 2 225 GLY 225 225 225 GLY GLY B . n 
B 2 226 GLU 226 226 226 GLU GLU B . n 
B 2 227 LEU 227 227 227 LEU LEU B . n 
B 2 228 ASP 228 228 228 ASP ASP B . n 
B 2 229 ASP 229 229 229 ASP ASP B . n 
B 2 230 VAL 230 230 230 VAL VAL B . n 
B 2 231 LEU 231 231 231 LEU LEU B . n 
B 2 232 PRO 232 232 232 PRO PRO B . n 
B 2 233 LYS 233 233 233 LYS LYS B . n 
B 2 234 TYR 234 234 234 TYR TYR B . n 
B 2 235 GLU 235 235 235 GLU GLU B . n 
B 2 236 ALA 236 236 236 ALA ALA B . n 
B 2 237 PHE 237 237 237 PHE PHE B . n 
B 2 238 LEU 238 238 238 LEU LEU B . n 
B 2 239 ASN 239 239 239 ASN ASN B . n 
B 2 240 ASP 240 240 240 ASP ASP B . n 
B 2 241 PHE 241 241 241 PHE PHE B . n 
B 2 242 LYS 242 242 242 LYS LYS B . n 
B 2 243 LYS 243 243 243 LYS LYS B . n 
B 2 244 LYS 244 244 244 LYS LYS B . n 
B 2 245 SER 245 245 245 SER SER B . n 
B 2 246 LYS 246 246 246 LYS LYS B . n 
B 2 247 ALA 247 247 247 ALA ALA B . n 
B 2 248 GLU 248 248 248 GLU GLU B . n 
B 2 249 GLN 249 249 249 GLN GLN B . n 
B 2 250 LYS 250 250 250 LYS LYS B . n 
B 2 251 GLU 251 251 251 GLU GLU B . n 
B 2 252 PHE 252 252 252 PHE PHE B . n 
B 2 253 ARG 253 253 253 ARG ARG B . n 
B 2 254 ASN 254 254 254 ASN ASN B . n 
B 2 255 LYS 255 255 255 LYS LYS B . n 
B 2 256 LEU 256 256 256 LEU LEU B . n 
B 2 257 ASP 257 257 257 ASP ASP B . n 
B 2 258 GLU 258 258 258 GLU GLU B . n 
B 2 259 SER 259 259 259 SER SER B . n 
B 2 260 ARG 260 260 260 ARG ARG B . n 
B 2 261 PHE 261 261 261 PHE PHE B . n 
B 2 262 VAL 262 262 262 VAL VAL B . n 
B 2 263 ILE 263 263 263 ILE ILE B . n 
B 2 264 LYS 264 264 264 LYS LYS B . n 
C 2 1   MET 1   1   1   MET MET D . n 
C 2 2   ASN 2   2   2   ASN ASN D . n 
C 2 3   VAL 3   3   3   VAL VAL D . n 
C 2 4   SER 4   4   4   SER SER D . n 
C 2 5   VAL 5   5   5   VAL VAL D . n 
C 2 6   ASN 6   6   6   ASN ASN D . n 
C 2 7   ILE 7   7   7   ILE ILE D . n 
C 2 8   LYS 8   8   8   LYS LYS D . n 
C 2 9   ASN 9   9   9   ASN ASN D . n 
C 2 10  VAL 10  10  10  VAL VAL D . n 
C 2 11  THR 11  11  11  THR THR D . n 
C 2 12  LYS 12  12  12  LYS LYS D . n 
C 2 13  GLU 13  13  13  GLU GLU D . n 
C 2 14  TYR 14  14  14  TYR TYR D . n 
C 2 15  ARG 15  15  15  ARG ARG D . n 
C 2 16  ILE 16  16  16  ILE ILE D . n 
C 2 17  TYR 17  17  17  TYR TYR D . n 
C 2 18  ARG 18  18  18  ARG ARG D . n 
C 2 19  THR 19  19  19  THR THR D . n 
C 2 20  ASN 20  20  20  ASN ASN D . n 
C 2 21  LYS 21  21  21  LYS LYS D . n 
C 2 22  GLU 22  22  22  GLU GLU D . n 
C 2 23  ARG 23  23  23  ARG ARG D . n 
C 2 24  MET 24  24  24  MET MET D . n 
C 2 25  LYS 25  25  25  LYS LYS D . n 
C 2 26  ASP 26  26  26  ASP ASP D . n 
C 2 27  ALA 27  27  27  ALA ALA D . n 
C 2 28  LEU 28  28  28  LEU LEU D . n 
C 2 29  ILE 29  29  29  ILE ILE D . n 
C 2 30  PRO 30  30  30  PRO PRO D . n 
C 2 31  LYS 31  31  31  LYS LYS D . n 
C 2 32  HIS 32  32  32  HIS HIS D . n 
C 2 33  LYS 33  33  33  LYS LYS D . n 
C 2 34  ASN 34  34  34  ASN ASN D . n 
C 2 35  LYS 35  35  35  LYS LYS D . n 
C 2 36  THR 36  36  36  THR THR D . n 
C 2 37  PHE 37  37  37  PHE PHE D . n 
C 2 38  PHE 38  38  38  PHE PHE D . n 
C 2 39  ALA 39  39  39  ALA ALA D . n 
C 2 40  LEU 40  40  40  LEU LEU D . n 
C 2 41  ASP 41  41  41  ASP ASP D . n 
C 2 42  ASP 42  42  42  ASP ASP D . n 
C 2 43  ILE 43  43  43  ILE ILE D . n 
C 2 44  SER 44  44  44  SER SER D . n 
C 2 45  LEU 45  45  45  LEU LEU D . n 
C 2 46  LYS 46  46  46  LYS LYS D . n 
C 2 47  ALA 47  47  47  ALA ALA D . n 
C 2 48  TYR 48  48  48  TYR TYR D . n 
C 2 49  GLU 49  49  49  GLU GLU D . n 
C 2 50  GLY 50  50  50  GLY GLY D . n 
C 2 51  ASP 51  51  51  ASP ASP D . n 
C 2 52  VAL 52  52  52  VAL VAL D . n 
C 2 53  ILE 53  53  53  ILE ILE D . n 
C 2 54  GLY 54  54  54  GLY GLY D . n 
C 2 55  LEU 55  55  55  LEU LEU D . n 
C 2 56  VAL 56  56  56  VAL VAL D . n 
C 2 57  GLY 57  57  57  GLY GLY D . n 
C 2 58  ILE 58  58  58  ILE ILE D . n 
C 2 59  ASN 59  59  59  ASN ASN D . n 
C 2 60  GLY 60  60  60  GLY GLY D . n 
C 2 61  SER 61  61  61  SER SER D . n 
C 2 62  GLY 62  62  62  GLY GLY D . n 
C 2 63  LYS 63  63  63  LYS LYS D . n 
C 2 64  SER 64  64  64  SER SER D . n 
C 2 65  THR 65  65  65  THR THR D . n 
C 2 66  LEU 66  66  66  LEU LEU D . n 
C 2 67  SER 67  67  67  SER SER D . n 
C 2 68  ASN 68  68  68  ASN ASN D . n 
C 2 69  ILE 69  69  69  ILE ILE D . n 
C 2 70  ILE 70  70  70  ILE ILE D . n 
C 2 71  GLY 71  71  71  GLY GLY D . n 
C 2 72  GLY 72  72  72  GLY GLY D . n 
C 2 73  SER 73  73  73  SER SER D . n 
C 2 74  LEU 74  74  74  LEU LEU D . n 
C 2 75  SER 75  75  75  SER SER D . n 
C 2 76  PRO 76  76  76  PRO PRO D . n 
C 2 77  THR 77  77  77  THR THR D . n 
C 2 78  VAL 78  78  78  VAL VAL D . n 
C 2 79  GLY 79  79  79  GLY GLY D . n 
C 2 80  LYS 80  80  80  LYS LYS D . n 
C 2 81  VAL 81  81  81  VAL VAL D . n 
C 2 82  ASP 82  82  82  ASP ASP D . n 
C 2 83  ARG 83  83  83  ARG ARG D . n 
C 2 84  ASN 84  84  84  ASN ASN D . n 
C 2 85  GLY 85  85  85  GLY GLY D . n 
C 2 86  GLU 86  86  86  GLU GLU D . n 
C 2 87  VAL 87  87  87  VAL VAL D . n 
C 2 88  SER 88  88  88  SER SER D . n 
C 2 89  VAL 89  89  89  VAL VAL D . n 
C 2 90  ILE 90  90  90  ILE ILE D . n 
C 2 91  ALA 91  91  91  ALA ALA D . n 
C 2 92  ILE 92  92  92  ILE ILE D . n 
C 2 93  SER 93  93  93  SER SER D . n 
C 2 94  ALA 94  94  94  ALA ALA D . n 
C 2 95  GLY 95  95  95  GLY GLY D . n 
C 2 96  LEU 96  96  96  LEU LEU D . n 
C 2 97  SER 97  97  97  SER SER D . n 
C 2 98  GLY 98  98  98  GLY GLY D . n 
C 2 99  GLN 99  99  99  GLN GLN D . n 
C 2 100 LEU 100 100 100 LEU LEU D . n 
C 2 101 THR 101 101 101 THR THR D . n 
C 2 102 GLY 102 102 102 GLY GLY D . n 
C 2 103 ILE 103 103 103 ILE ILE D . n 
C 2 104 GLU 104 104 104 GLU GLU D . n 
C 2 105 ASN 105 105 105 ASN ASN D . n 
C 2 106 ILE 106 106 106 ILE ILE D . n 
C 2 107 GLU 107 107 107 GLU GLU D . n 
C 2 108 PHE 108 108 108 PHE PHE D . n 
C 2 109 LYS 109 109 109 LYS LYS D . n 
C 2 110 MET 110 110 110 MET MET D . n 
C 2 111 LEU 111 111 111 LEU LEU D . n 
C 2 112 CYS 112 112 112 CYS CYS D . n 
C 2 113 MET 113 113 113 MET MET D . n 
C 2 114 GLY 114 114 114 GLY GLY D . n 
C 2 115 PHE 115 115 115 PHE PHE D . n 
C 2 116 LYS 116 116 116 LYS LYS D . n 
C 2 117 ARG 117 117 117 ARG ARG D . n 
C 2 118 LYS 118 118 118 LYS LYS D . n 
C 2 119 GLU 119 119 119 GLU GLU D . n 
C 2 120 ILE 120 120 120 ILE ILE D . n 
C 2 121 LYS 121 121 121 LYS LYS D . n 
C 2 122 ALA 122 122 122 ALA ALA D . n 
C 2 123 MET 123 123 123 MET MET D . n 
C 2 124 THR 124 124 124 THR THR D . n 
C 2 125 PRO 125 125 125 PRO PRO D . n 
C 2 126 LYS 126 126 126 LYS LYS D . n 
C 2 127 ILE 127 127 127 ILE ILE D . n 
C 2 128 ILE 128 128 128 ILE ILE D . n 
C 2 129 GLU 129 129 129 GLU GLU D . n 
C 2 130 PHE 130 130 130 PHE PHE D . n 
C 2 131 SER 131 131 131 SER SER D . n 
C 2 132 GLU 132 132 132 GLU GLU D . n 
C 2 133 LEU 133 133 133 LEU LEU D . n 
C 2 134 GLY 134 134 134 GLY GLY D . n 
C 2 135 GLU 135 135 135 GLU GLU D . n 
C 2 136 PHE 136 136 136 PHE PHE D . n 
C 2 137 ILE 137 137 137 ILE ILE D . n 
C 2 138 TYR 138 138 138 TYR TYR D . n 
C 2 139 GLN 139 139 139 GLN GLN D . n 
C 2 140 PRO 140 140 140 PRO PRO D . n 
C 2 141 VAL 141 141 141 VAL VAL D . n 
C 2 142 LYS 142 142 142 LYS LYS D . n 
C 2 143 LYS 143 143 143 LYS LYS D . n 
C 2 144 TYR 144 144 144 TYR TYR D . n 
C 2 145 SER 145 145 145 SER SER D . n 
C 2 146 SER 146 146 146 SER SER D . n 
C 2 147 GLY 147 147 147 GLY GLY D . n 
C 2 148 MET 148 148 148 MET MET D . n 
C 2 149 ARG 149 149 149 ARG ARG D . n 
C 2 150 ALA 150 150 150 ALA ALA D . n 
C 2 151 LYS 151 151 151 LYS LYS D . n 
C 2 152 LEU 152 152 152 LEU LEU D . n 
C 2 153 GLY 153 153 153 GLY GLY D . n 
C 2 154 PHE 154 154 154 PHE PHE D . n 
C 2 155 SER 155 155 155 SER SER D . n 
C 2 156 ILE 156 156 156 ILE ILE D . n 
C 2 157 ASN 157 157 157 ASN ASN D . n 
C 2 158 ILE 158 158 158 ILE ILE D . n 
C 2 159 THR 159 159 159 THR THR D . n 
C 2 160 VAL 160 160 160 VAL VAL D . n 
C 2 161 ASN 161 161 161 ASN ASN D . n 
C 2 162 PRO 162 162 162 PRO PRO D . n 
C 2 163 ASP 163 163 163 ASP ASP D . n 
C 2 164 ILE 164 164 164 ILE ILE D . n 
C 2 165 LEU 165 165 165 LEU LEU D . n 
C 2 166 VAL 166 166 166 VAL VAL D . n 
C 2 167 ILE 167 167 167 ILE ILE D . n 
C 2 168 ASP 168 168 168 ASP ASP D . n 
C 2 169 GLU 169 169 169 GLU GLU D . n 
C 2 170 ALA 170 170 170 ALA ALA D . n 
C 2 171 LEU 171 171 171 LEU LEU D . n 
C 2 172 SER 172 172 172 SER SER D . n 
C 2 173 VAL 173 173 173 VAL VAL D . n 
C 2 174 GLY 174 174 174 GLY GLY D . n 
C 2 175 ASP 175 175 175 ASP ASP D . n 
C 2 176 GLN 176 176 176 GLN GLN D . n 
C 2 177 THR 177 177 177 THR THR D . n 
C 2 178 PHE 178 178 178 PHE PHE D . n 
C 2 179 ALA 179 179 179 ALA ALA D . n 
C 2 180 GLN 180 180 180 GLN GLN D . n 
C 2 181 LYS 181 181 181 LYS LYS D . n 
C 2 182 CYS 182 182 182 CYS CYS D . n 
C 2 183 LEU 183 183 183 LEU LEU D . n 
C 2 184 ASP 184 184 184 ASP ASP D . n 
C 2 185 LYS 185 185 185 LYS LYS D . n 
C 2 186 ILE 186 186 186 ILE ILE D . n 
C 2 187 TYR 187 187 187 TYR TYR D . n 
C 2 188 GLU 188 188 188 GLU GLU D . n 
C 2 189 PHE 189 189 189 PHE PHE D . n 
C 2 190 LYS 190 190 190 LYS LYS D . n 
C 2 191 GLU 191 191 191 GLU GLU D . n 
C 2 192 GLN 192 192 192 GLN GLN D . n 
C 2 193 ASN 193 193 193 ASN ASN D . n 
C 2 194 LYS 194 194 194 LYS LYS D . n 
C 2 195 THR 195 195 195 THR THR D . n 
C 2 196 ILE 196 196 196 ILE ILE D . n 
C 2 197 PHE 197 197 197 PHE PHE D . n 
C 2 198 PHE 198 198 198 PHE PHE D . n 
C 2 199 VAL 199 199 199 VAL VAL D . n 
C 2 200 SER 200 200 200 SER SER D . n 
C 2 201 HIS 201 201 201 HIS HIS D . n 
C 2 202 ASN 202 202 202 ASN ASN D . n 
C 2 203 LEU 203 203 203 LEU LEU D . n 
C 2 204 GLY 204 204 204 GLY GLY D . n 
C 2 205 GLN 205 205 205 GLN GLN D . n 
C 2 206 VAL 206 206 206 VAL VAL D . n 
C 2 207 ARG 207 207 207 ARG ARG D . n 
C 2 208 GLN 208 208 208 GLN GLN D . n 
C 2 209 PHE 209 209 209 PHE PHE D . n 
C 2 210 CYS 210 210 210 CYS CYS D . n 
C 2 211 THR 211 211 211 THR THR D . n 
C 2 212 LYS 212 212 212 LYS LYS D . n 
C 2 213 ILE 213 213 213 ILE ILE D . n 
C 2 214 ALA 214 214 214 ALA ALA D . n 
C 2 215 TRP 215 215 215 TRP TRP D . n 
C 2 216 ILE 216 216 216 ILE ILE D . n 
C 2 217 GLU 217 217 217 GLU GLU D . n 
C 2 218 GLY 218 218 218 GLY GLY D . n 
C 2 219 GLY 219 219 219 GLY GLY D . n 
C 2 220 LYS 220 220 220 LYS LYS D . n 
C 2 221 LEU 221 221 221 LEU LEU D . n 
C 2 222 LYS 222 222 222 LYS LYS D . n 
C 2 223 ASP 223 223 223 ASP ASP D . n 
C 2 224 TYR 224 224 224 TYR TYR D . n 
C 2 225 GLY 225 225 225 GLY GLY D . n 
C 2 226 GLU 226 226 226 GLU GLU D . n 
C 2 227 LEU 227 227 227 LEU LEU D . n 
C 2 228 ASP 228 228 228 ASP ASP D . n 
C 2 229 ASP 229 229 229 ASP ASP D . n 
C 2 230 VAL 230 230 230 VAL VAL D . n 
C 2 231 LEU 231 231 231 LEU LEU D . n 
C 2 232 PRO 232 232 232 PRO PRO D . n 
C 2 233 LYS 233 233 233 LYS LYS D . n 
C 2 234 TYR 234 234 234 TYR TYR D . n 
C 2 235 GLU 235 235 235 GLU GLU D . n 
C 2 236 ALA 236 236 236 ALA ALA D . n 
C 2 237 PHE 237 237 237 PHE PHE D . n 
C 2 238 LEU 238 238 238 LEU LEU D . n 
C 2 239 ASN 239 239 239 ASN ASN D . n 
C 2 240 ASP 240 240 240 ASP ASP D . n 
C 2 241 PHE 241 241 241 PHE PHE D . n 
C 2 242 LYS 242 242 242 LYS LYS D . n 
C 2 243 LYS 243 243 243 LYS LYS D . n 
C 2 244 LYS 244 244 244 LYS LYS D . n 
C 2 245 SER 245 245 245 SER SER D . n 
C 2 246 LYS 246 246 246 LYS LYS D . n 
C 2 247 ALA 247 247 247 ALA ALA D . n 
C 2 248 GLU 248 248 248 GLU GLU D . n 
C 2 249 GLN 249 249 249 GLN GLN D . n 
C 2 250 LYS 250 250 250 LYS LYS D . n 
C 2 251 GLU 251 251 251 GLU GLU D . n 
C 2 252 PHE 252 252 252 PHE PHE D . n 
C 2 253 ARG 253 253 253 ARG ARG D . n 
C 2 254 ASN 254 254 254 ASN ASN D . n 
C 2 255 LYS 255 255 255 LYS LYS D . n 
C 2 256 LEU 256 256 256 LEU LEU D . n 
C 2 257 ASP 257 257 257 ASP ASP D . n 
C 2 258 GLU 258 258 258 GLU GLU D . n 
C 2 259 SER 259 259 259 SER SER D . n 
C 2 260 ARG 260 260 260 ARG ARG D . n 
C 2 261 PHE 261 261 261 PHE PHE D . n 
C 2 262 VAL 262 262 262 VAL VAL D . n 
C 2 263 ILE 263 263 263 ILE ILE D . n 
C 2 264 LYS 264 264 264 LYS LYS D . n 
D 1 1   MET 1   -23 ?   ?   ?   C . n 
D 1 2   GLY 2   -22 ?   ?   ?   C . n 
D 1 3   SER 3   -21 ?   ?   ?   C . n 
D 1 4   SER 4   -20 ?   ?   ?   C . n 
D 1 5   HIS 5   -19 ?   ?   ?   C . n 
D 1 6   HIS 6   -18 ?   ?   ?   C . n 
D 1 7   HIS 7   -17 ?   ?   ?   C . n 
D 1 8   HIS 8   -16 ?   ?   ?   C . n 
D 1 9   HIS 9   -15 ?   ?   ?   C . n 
D 1 10  HIS 10  -14 ?   ?   ?   C . n 
D 1 11  HIS 11  -13 ?   ?   ?   C . n 
D 1 12  HIS 12  -12 ?   ?   ?   C . n 
D 1 13  HIS 13  -11 ?   ?   ?   C . n 
D 1 14  HIS 14  -10 ?   ?   ?   C . n 
D 1 15  SER 15  -9  ?   ?   ?   C . n 
D 1 16  SER 16  -8  ?   ?   ?   C . n 
D 1 17  GLY 17  -7  ?   ?   ?   C . n 
D 1 18  LEU 18  -6  ?   ?   ?   C . n 
D 1 19  VAL 19  -5  ?   ?   ?   C . n 
D 1 20  PRO 20  -4  ?   ?   ?   C . n 
D 1 21  ARG 21  -3  ?   ?   ?   C . n 
D 1 22  GLY 22  -2  ?   ?   ?   C . n 
D 1 23  SER 23  -1  ?   ?   ?   C . n 
D 1 24  HIS 24  0   ?   ?   ?   C . n 
D 1 25  MET 25  1   1   MET MET C . n 
D 1 26  SER 26  2   2   SER SER C . n 
D 1 27  ALA 27  3   3   ALA ALA C . n 
D 1 28  ILE 28  4   4   ILE ILE C . n 
D 1 29  GLY 29  5   5   GLY GLY C . n 
D 1 30  THR 30  6   6   THR THR C . n 
D 1 31  VAL 31  7   7   VAL VAL C . n 
D 1 32  PHE 32  8   8   PHE PHE C . n 
D 1 33  LYS 33  9   9   LYS LYS C . n 
D 1 34  GLU 34  10  10  GLU GLU C . n 
D 1 35  HIS 35  11  11  HIS HIS C . n 
D 1 36  VAL 36  12  12  VAL VAL C . n 
D 1 37  LYS 37  13  13  LYS LYS C . n 
D 1 38  ASN 38  14  14  ASN ASN C . n 
D 1 39  PHE 39  15  15  PHE PHE C . n 
D 1 40  TYR 40  16  16  TYR TYR C . n 
D 1 41  LEU 41  17  17  LEU LEU C . n 
D 1 42  ILE 42  18  18  ILE ILE C . n 
D 1 43  GLN 43  19  19  GLN GLN C . n 
D 1 44  ARG 44  20  20  ARG ARG C . n 
D 1 45  LEU 45  21  21  LEU LEU C . n 
D 1 46  ALA 46  22  22  ALA ALA C . n 
D 1 47  GLN 47  23  23  GLN GLN C . n 
D 1 48  PHE 48  24  24  PHE PHE C . n 
D 1 49  GLN 49  25  25  GLN GLN C . n 
D 1 50  VAL 50  26  26  VAL VAL C . n 
D 1 51  LYS 51  27  27  LYS LYS C . n 
D 1 52  ILE 52  28  28  ILE ILE C . n 
D 1 53  ILE 53  29  29  ILE ILE C . n 
D 1 54  ASN 54  30  30  ASN ASN C . n 
D 1 55  HIS 55  31  31  HIS HIS C . n 
D 1 56  SER 56  32  32  SER SER C . n 
D 1 57  ASN 57  33  33  ASN ASN C . n 
D 1 58  TYR 58  34  34  TYR TYR C . n 
D 1 59  LEU 59  35  35  LEU LEU C . n 
D 1 60  GLY 60  36  36  GLY GLY C . n 
D 1 61  VAL 61  37  37  VAL VAL C . n 
D 1 62  ALA 62  38  38  ALA ALA C . n 
D 1 63  TRP 63  39  39  TRP TRP C . n 
D 1 64  GLU 64  40  40  GLU GLU C . n 
D 1 65  LEU 65  41  41  LEU LEU C . n 
D 1 66  ILE 66  42  42  ILE ILE C . n 
D 1 67  ASN 67  43  43  ASN ASN C . n 
D 1 68  PRO 68  44  44  PRO PRO C . n 
D 1 69  VAL 69  45  45  VAL VAL C . n 
D 1 70  MET 70  46  46  MET MET C . n 
D 1 71  GLN 71  47  47  GLN GLN C . n 
D 1 72  ILE 72  48  48  ILE ILE C . n 
D 1 73  MET 73  49  49  MET MET C . n 
D 1 74  VAL 74  50  50  VAL VAL C . n 
D 1 75  TYR 75  51  51  TYR TYR C . n 
D 1 76  TRP 76  52  52  TRP TRP C . n 
D 1 77  MET 77  53  53  MET MET C . n 
D 1 78  VAL 78  54  54  VAL VAL C . n 
D 1 79  PHE 79  55  55  PHE PHE C . n 
D 1 80  GLY 80  56  56  GLY GLY C . n 
D 1 81  LEU 81  57  57  LEU LEU C . n 
D 1 82  GLY 82  58  58  GLY GLY C . n 
D 1 83  ILE 83  59  59  ILE ILE C . n 
D 1 84  ARG 84  60  60  ARG ARG C . n 
D 1 85  SER 85  61  61  SER SER C . n 
D 1 86  ASN 86  62  62  ASN ASN C . n 
D 1 87  ALA 87  63  63  ALA ALA C . n 
D 1 88  PRO 88  64  64  PRO PRO C . n 
D 1 89  ILE 89  65  65  ILE ILE C . n 
D 1 90  HIS 90  66  66  HIS HIS C . n 
D 1 91  GLY 91  67  67  GLY GLY C . n 
D 1 92  VAL 92  68  68  VAL VAL C . n 
D 1 93  PRO 93  69  69  PRO PRO C . n 
D 1 94  PHE 94  70  70  PHE PHE C . n 
D 1 95  VAL 95  71  71  VAL VAL C . n 
D 1 96  TYR 96  72  72  TYR TYR C . n 
D 1 97  TRP 97  73  73  TRP TRP C . n 
D 1 98  LEU 98  74  74  LEU LEU C . n 
D 1 99  LEU 99  75  75  LEU LEU C . n 
D 1 100 VAL 100 76  76  VAL VAL C . n 
D 1 101 GLY 101 77  77  GLY GLY C . n 
D 1 102 ILE 102 78  78  ILE ILE C . n 
D 1 103 SER 103 79  79  SER SER C . n 
D 1 104 MET 104 80  80  MET MET C . n 
D 1 105 TRP 105 81  81  TRP TRP C . n 
D 1 106 PHE 106 82  82  PHE PHE C . n 
D 1 107 PHE 107 83  83  PHE PHE C . n 
D 1 108 ILE 108 84  84  ILE ILE C . n 
D 1 109 ASN 109 85  85  ASN ASN C . n 
D 1 110 GLN 110 86  86  GLN GLN C . n 
D 1 111 GLY 111 87  87  GLY GLY C . n 
D 1 112 ILE 112 88  88  ILE ILE C . n 
D 1 113 LEU 113 89  89  LEU LEU C . n 
D 1 114 GLU 114 90  90  GLU GLU C . n 
D 1 115 GLY 115 91  91  GLY GLY C . n 
D 1 116 THR 116 92  92  THR THR C . n 
D 1 117 LYS 117 93  93  LYS LYS C . n 
D 1 118 ALA 118 94  94  ALA ALA C . n 
D 1 119 ILE 119 95  95  ILE ILE C . n 
D 1 120 THR 120 96  96  THR THR C . n 
D 1 121 GLN 121 97  97  GLN GLN C . n 
D 1 122 LYS 122 98  98  LYS LYS C . n 
D 1 123 PHE 123 99  99  PHE PHE C . n 
D 1 124 ASN 124 100 100 ASN ASN C . n 
D 1 125 GLN 125 101 101 GLN GLN C . n 
D 1 126 VAL 126 102 102 VAL VAL C . n 
D 1 127 SER 127 103 103 SER SER C . n 
D 1 128 LYS 128 104 104 LYS LYS C . n 
D 1 129 MET 129 105 105 MET MET C . n 
D 1 130 ASN 130 106 106 ASN ASN C . n 
D 1 131 PHE 131 107 107 PHE PHE C . n 
D 1 132 PRO 132 108 108 PRO PRO C . n 
D 1 133 LEU 133 109 109 LEU LEU C . n 
D 1 134 SER 134 110 110 SER SER C . n 
D 1 135 ILE 135 111 111 ILE ILE C . n 
D 1 136 ILE 136 112 112 ILE ILE C . n 
D 1 137 PRO 137 113 113 PRO PRO C . n 
D 1 138 THR 138 114 114 THR THR C . n 
D 1 139 TYR 139 115 115 TYR TYR C . n 
D 1 140 ILE 140 116 116 ILE ILE C . n 
D 1 141 VAL 141 117 117 VAL VAL C . n 
D 1 142 THR 142 118 118 THR THR C . n 
D 1 143 SER 143 119 119 SER SER C . n 
D 1 144 ARG 144 120 120 ARG ARG C . n 
D 1 145 PHE 145 121 121 PHE PHE C . n 
D 1 146 TYR 146 122 122 TYR TYR C . n 
D 1 147 GLY 147 123 123 GLY GLY C . n 
D 1 148 HIS 148 124 124 HIS HIS C . n 
D 1 149 LEU 149 125 125 LEU LEU C . n 
D 1 150 GLY 150 126 126 GLY GLY C . n 
D 1 151 LEU 151 127 127 LEU LEU C . n 
D 1 152 LEU 152 128 128 LEU LEU C . n 
D 1 153 LEU 153 129 129 LEU LEU C . n 
D 1 154 LEU 154 130 130 LEU LEU C . n 
D 1 155 VAL 155 131 131 VAL VAL C . n 
D 1 156 ILE 156 132 132 ILE ILE C . n 
D 1 157 ILE 157 133 133 ILE ILE C . n 
D 1 158 ALA 158 134 134 ALA ALA C . n 
D 1 159 CYS 159 135 135 CYS CYS C . n 
D 1 160 MET 160 136 136 MET MET C . n 
D 1 161 PHE 161 137 137 PHE PHE C . n 
D 1 162 THR 162 138 138 THR THR C . n 
D 1 163 GLY 163 139 139 GLY GLY C . n 
D 1 164 ILE 164 140 140 ILE ILE C . n 
D 1 165 TYR 165 141 141 TYR TYR C . n 
D 1 166 PRO 166 142 142 PRO PRO C . n 
D 1 167 SER 167 143 143 SER SER C . n 
D 1 168 ILE 168 144 144 ILE ILE C . n 
D 1 169 HIS 169 145 145 HIS HIS C . n 
D 1 170 ILE 170 146 146 ILE ILE C . n 
D 1 171 ILE 171 147 147 ILE ILE C . n 
D 1 172 GLN 172 148 148 GLN GLN C . n 
D 1 173 LEU 173 149 149 LEU LEU C . n 
D 1 174 LEU 174 150 150 LEU LEU C . n 
D 1 175 ILE 175 151 151 ILE ILE C . n 
D 1 176 TYR 176 152 152 TYR TYR C . n 
D 1 177 VAL 177 153 153 VAL VAL C . n 
D 1 178 PRO 178 154 154 PRO PRO C . n 
D 1 179 PHE 179 155 155 PHE PHE C . n 
D 1 180 CYS 180 156 156 CYS CYS C . n 
D 1 181 PHE 181 157 157 PHE PHE C . n 
D 1 182 PHE 182 158 158 PHE PHE C . n 
D 1 183 LEU 183 159 159 LEU LEU C . n 
D 1 184 THR 184 160 160 THR THR C . n 
D 1 185 ALA 185 161 161 ALA ALA C . n 
D 1 186 SER 186 162 162 SER SER C . n 
D 1 187 VAL 187 163 163 VAL VAL C . n 
D 1 188 THR 188 164 164 THR THR C . n 
D 1 189 LEU 189 165 165 LEU LEU C . n 
D 1 190 LEU 190 166 166 LEU LEU C . n 
D 1 191 THR 191 167 167 THR THR C . n 
D 1 192 SER 192 168 168 SER SER C . n 
D 1 193 THR 193 169 169 THR THR C . n 
D 1 194 LEU 194 170 170 LEU LEU C . n 
D 1 195 GLY 195 171 171 GLY GLY C . n 
D 1 196 VAL 196 172 172 VAL VAL C . n 
D 1 197 LEU 197 173 173 LEU LEU C . n 
D 1 198 VAL 198 174 174 VAL VAL C . n 
D 1 199 ARG 199 175 175 ARG ARG C . n 
D 1 200 ASP 200 176 176 ASP ASP C . n 
D 1 201 THR 201 177 177 THR THR C . n 
D 1 202 GLN 202 178 178 GLN GLN C . n 
D 1 203 MET 203 179 179 MET MET C . n 
D 1 204 LEU 204 180 180 LEU LEU C . n 
D 1 205 MET 205 181 181 MET MET C . n 
D 1 206 GLN 206 182 182 GLN GLN C . n 
D 1 207 ALA 207 183 183 ALA ALA C . n 
D 1 208 ILE 208 184 184 ILE ILE C . n 
D 1 209 LEU 209 185 185 LEU LEU C . n 
D 1 210 ARG 210 186 186 ARG ARG C . n 
D 1 211 ILE 211 187 187 ILE ILE C . n 
D 1 212 LEU 212 188 188 LEU LEU C . n 
D 1 213 PHE 213 189 189 PHE PHE C . n 
D 1 214 TYR 214 190 190 TYR TYR C . n 
D 1 215 PHE 215 191 191 PHE PHE C . n 
D 1 216 SER 216 192 192 SER SER C . n 
D 1 217 PRO 217 193 193 PRO PRO C . n 
D 1 218 ILE 218 194 194 ILE ILE C . n 
D 1 219 LEU 219 195 195 LEU LEU C . n 
D 1 220 TRP 220 196 196 TRP TRP C . n 
D 1 221 LEU 221 197 197 LEU LEU C . n 
D 1 222 PRO 222 198 198 PRO PRO C . n 
D 1 223 LYS 223 199 199 LYS LYS C . n 
D 1 224 ASN 224 200 200 ASN ASN C . n 
D 1 225 HIS 225 201 201 HIS HIS C . n 
D 1 226 GLY 226 202 202 GLY GLY C . n 
D 1 227 ILE 227 203 203 ILE ILE C . n 
D 1 228 SER 228 204 204 SER SER C . n 
D 1 229 GLY 229 205 205 GLY GLY C . n 
D 1 230 LEU 230 206 206 LEU LEU C . n 
D 1 231 ILE 231 207 207 ILE ILE C . n 
D 1 232 HIS 232 208 208 HIS HIS C . n 
D 1 233 GLU 233 209 209 GLU GLU C . n 
D 1 234 MET 234 210 210 MET MET C . n 
D 1 235 MET 235 211 211 MET MET C . n 
D 1 236 LYS 236 212 212 LYS LYS C . n 
D 1 237 TYR 237 213 213 TYR TYR C . n 
D 1 238 ASN 238 214 214 ASN ASN C . n 
D 1 239 PRO 239 215 215 PRO PRO C . n 
D 1 240 VAL 240 216 216 VAL VAL C . n 
D 1 241 TYR 241 217 217 TYR TYR C . n 
D 1 242 PHE 242 218 218 PHE PHE C . n 
D 1 243 ILE 243 219 219 ILE ILE C . n 
D 1 244 ALA 244 220 220 ALA ALA C . n 
D 1 245 GLU 245 221 221 GLU GLU C . n 
D 1 246 SER 246 222 222 SER SER C . n 
D 1 247 TYR 247 223 223 TYR TYR C . n 
D 1 248 ARG 248 224 224 ARG ARG C . n 
D 1 249 ALA 249 225 225 ALA ALA C . n 
D 1 250 ALA 250 226 226 ALA ALA C . n 
D 1 251 ILE 251 227 227 ILE ILE C . n 
D 1 252 LEU 252 228 228 LEU LEU C . n 
D 1 253 TYR 253 229 229 TYR TYR C . n 
D 1 254 HIS 254 230 230 HIS HIS C . n 
D 1 255 GLU 255 231 231 GLU GLU C . n 
D 1 256 TRP 256 232 232 TRP TRP C . n 
D 1 257 TYR 257 233 233 TYR TYR C . n 
D 1 258 PHE 258 234 234 PHE PHE C . n 
D 1 259 MET 259 235 235 MET MET C . n 
D 1 260 ASP 260 236 236 ASP ASP C . n 
D 1 261 HIS 261 237 237 HIS HIS C . n 
D 1 262 TRP 262 238 238 TRP TRP C . n 
D 1 263 LYS 263 239 239 LYS LYS C . n 
D 1 264 LEU 264 240 240 LEU LEU C . n 
D 1 265 MET 265 241 241 MET MET C . n 
D 1 266 LEU 266 242 242 LEU LEU C . n 
D 1 267 TYR 267 243 243 TYR TYR C . n 
D 1 268 ASN 268 244 244 ASN ASN C . n 
D 1 269 PHE 269 245 245 PHE PHE C . n 
D 1 270 GLY 270 246 246 GLY GLY C . n 
D 1 271 ILE 271 247 247 ILE ILE C . n 
D 1 272 VAL 272 248 248 VAL VAL C . n 
D 1 273 ALA 273 249 249 ALA ALA C . n 
D 1 274 ILE 274 250 250 ILE ILE C . n 
D 1 275 PHE 275 251 251 PHE PHE C . n 
D 1 276 PHE 276 252 252 PHE PHE C . n 
D 1 277 ALA 277 253 253 ALA ALA C . n 
D 1 278 ILE 278 254 254 ILE ILE C . n 
D 1 279 GLY 279 255 255 GLY GLY C . n 
D 1 280 ALA 280 256 256 ALA ALA C . n 
D 1 281 TYR 281 257 257 TYR TYR C . n 
D 1 282 LEU 282 258 258 LEU LEU C . n 
D 1 283 HIS 283 259 259 HIS HIS C . n 
D 1 284 MET 284 260 260 MET MET C . n 
D 1 285 LYS 285 261 261 LYS LYS C . n 
D 1 286 TYR 286 262 262 TYR TYR C . n 
D 1 287 ARG 287 263 263 ARG ARG C . n 
D 1 288 ASP 288 264 264 ASP ASP C . n 
D 1 289 GLN 289 265 265 GLN GLN C . n 
D 1 290 PHE 290 266 266 PHE PHE C . n 
D 1 291 ALA 291 267 267 ALA ALA C . n 
D 1 292 ASP 292 268 268 ASP ASP C . n 
D 1 293 PHE 293 269 269 PHE PHE C . n 
D 1 294 LEU 294 270 270 LEU LEU C . 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 A1AV9 ? ? A1AV9 ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ANP   ? ? ANP   ? ? 'SUBJECT OF INVESTIGATION' ? 
3 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 
E 3 A1AV9 1 301 301 A1AV9 A1A A . 
F 4 ANP   1 301 301 ANP   ANP B . 
G 5 MG    1 302 302 MG    MG  B . 
H 4 ANP   1 301 301 ANP   ANP D . 
I 5 MG    1 302 302 MG    MG  D . 
J 3 A1AV9 1 301 301 A1AV9 A1A C . 
K 6 HOH   1 401 402 HOH   HOH B . 
K 6 HOH   2 402 404 HOH   HOH B . 
K 6 HOH   3 403 403 HOH   HOH B . 
L 6 HOH   1 401 402 HOH   HOH D . 
L 6 HOH   2 402 404 HOH   HOH D . 
L 6 HOH   3 403 403 HOH   HOH D . 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CFP 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     1.00 
_cell.length_a_esd                 ? 
_cell.length_b                     1.00 
_cell.length_b_esd                 ? 
_cell.length_c                     1.00 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        ? 
_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                         9CFP 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                1 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9CFP 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON MICROSCOPY' 
_exptl.method_details             ? 
# 
_refine.pdbx_refine_id                           'ELECTRON MICROSCOPY' 
_refine.entry_id                                 9CFP 
_refine.pdbx_diffrn_id                           ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             ? 
_refine.ls_d_res_high                            . 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
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 
'ELECTRON MICROSCOPY' ? 0.002  ? 9024  ? f_bond_d           ? ? 
'ELECTRON MICROSCOPY' ? 0.548  ? 12208 ? f_angle_d          ? ? 
'ELECTRON MICROSCOPY' ? 10.348 ? 1196  ? f_dihedral_angle_d ? ? 
'ELECTRON MICROSCOPY' ? 0.041  ? 1344  ? f_chiral_restr     ? ? 
'ELECTRON MICROSCOPY' ? 0.004  ? 1494  ? f_plane_restr      ? ? 
# 
_struct.entry_id                     9CFP 
_struct.title                        'Cryo-EM structure of S. aureus TarGH in complex with AMP-PNP and targocil-II' 
_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        9CFP 
_struct_keywords.text            'ABC transporter, teichoic acid, bacteria, MEMBRANE PROTEIN' 
_struct_keywords.pdbx_keywords   'MEMBRANE PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 1 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 4 ? 
I N N 5 ? 
J N N 3 ? 
K N N 6 ? 
L N N 6 ? 
# 
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 A0A0H2XIF1_STAA3 A0A0H2XIF1 ? 1 
;MSAIGTVFKEHVKNFYLIQRLAQFQVKIINHSNYLGVAWELINPVMQIMVYWMVFGLGIRSNAPIHGVPFVYWLLVGISM
WFFINQGILEGTKAITQKFNQVSKMNFPLSIIPTYIVTSRFYGHLGLLLLVIIACMFTGIYPSIHIIQLLIYVPFCFFLT
ASVTLLTSTLGVLVRDTQMLMQAILRILFYFSPILWLPKNHGISGLIHEMMKYNPVYFIAESYRAAILYHEWYFMDHWKL
MLYNFGIVAIFFAIGAYLHMKYRDQFADFL
;
1 
2 UNP TAGH_STAA3       Q2FJ01     ? 2 
;MNVSVNIKNVTKEYRIYRTNKERMKDALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK
VDRNGEVSVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITV
NPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLND
FKKKSKAEQKEFRNKLDESRFVIK
;
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 9CFP A 25 ? 294 ? A0A0H2XIF1 1 ? 270 ? 1 270 
2 2 9CFP B 1  ? 264 ? Q2FJ01     1 ? 264 ? 1 264 
3 2 9CFP D 1  ? 264 ? Q2FJ01     1 ? 264 ? 1 264 
4 1 9CFP C 25 ? 294 ? A0A0H2XIF1 1 ? 270 ? 1 270 
# 
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 9CFP MET A 1  ? UNP A0A0H2XIF1 ? ? 'initiating methionine' -23 1  
1 9CFP GLY A 2  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -22 2  
1 9CFP SER A 3  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -21 3  
1 9CFP SER A 4  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -20 4  
1 9CFP HIS A 5  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -19 5  
1 9CFP HIS A 6  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -18 6  
1 9CFP HIS A 7  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -17 7  
1 9CFP HIS A 8  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -16 8  
1 9CFP HIS A 9  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -15 9  
1 9CFP HIS A 10 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -14 10 
1 9CFP HIS A 11 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -13 11 
1 9CFP HIS A 12 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -12 12 
1 9CFP HIS A 13 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -11 13 
1 9CFP HIS A 14 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -10 14 
1 9CFP SER A 15 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -9  15 
1 9CFP SER A 16 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -8  16 
1 9CFP GLY A 17 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -7  17 
1 9CFP LEU A 18 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -6  18 
1 9CFP VAL A 19 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -5  19 
1 9CFP PRO A 20 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -4  20 
1 9CFP ARG A 21 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -3  21 
1 9CFP GLY A 22 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -2  22 
1 9CFP SER A 23 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -1  23 
1 9CFP HIS A 24 ? UNP A0A0H2XIF1 ? ? 'expression tag'        0   24 
4 9CFP MET C 1  ? UNP A0A0H2XIF1 ? ? 'initiating methionine' -23 25 
4 9CFP GLY C 2  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -22 26 
4 9CFP SER C 3  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -21 27 
4 9CFP SER C 4  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -20 28 
4 9CFP HIS C 5  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -19 29 
4 9CFP HIS C 6  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -18 30 
4 9CFP HIS C 7  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -17 31 
4 9CFP HIS C 8  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -16 32 
4 9CFP HIS C 9  ? UNP A0A0H2XIF1 ? ? 'expression tag'        -15 33 
4 9CFP HIS C 10 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -14 34 
4 9CFP HIS C 11 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -13 35 
4 9CFP HIS C 12 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -12 36 
4 9CFP HIS C 13 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -11 37 
4 9CFP HIS C 14 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -10 38 
4 9CFP SER C 15 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -9  39 
4 9CFP SER C 16 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -8  40 
4 9CFP GLY C 17 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -7  41 
4 9CFP LEU C 18 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -6  42 
4 9CFP VAL C 19 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -5  43 
4 9CFP PRO C 20 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -4  44 
4 9CFP ARG C 21 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -3  45 
4 9CFP GLY C 22 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -2  46 
4 9CFP SER C 23 ? UNP A0A0H2XIF1 ? ? 'expression tag'        -1  47 
4 9CFP HIS C 24 ? UNP A0A0H2XIF1 ? ? 'expression tag'        0   48 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'electron microscopy' 
_pdbx_struct_assembly_auth_evidence.details                'not applicable' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0 
_pdbx_struct_oper_list.matrix[1][2]         0.0 
_pdbx_struct_oper_list.matrix[1][3]         0.0 
_pdbx_struct_oper_list.vector[1]            0.0 
_pdbx_struct_oper_list.matrix[2][1]         0.0 
_pdbx_struct_oper_list.matrix[2][2]         1.0 
_pdbx_struct_oper_list.matrix[2][3]         0.0 
_pdbx_struct_oper_list.vector[2]            0.0 
_pdbx_struct_oper_list.matrix[3][1]         0.0 
_pdbx_struct_oper_list.matrix[3][2]         0.0 
_pdbx_struct_oper_list.matrix[3][3]         1.0 
_pdbx_struct_oper_list.vector[3]            0.0 
# 
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 25  ? ASN A 38  ? MET A 1   ASN A 14  1 ? 14 
HELX_P HELX_P2  AA2 ASN A 38  ? ASN A 54  ? ASN A 14  ASN A 30  1 ? 17 
HELX_P HELX_P3  AA3 LEU A 59  ? VAL A 61  ? LEU A 35  VAL A 37  5 ? 3  
HELX_P HELX_P4  AA4 ALA A 62  ? GLY A 80  ? ALA A 38  GLY A 56  1 ? 19 
HELX_P HELX_P5  AA5 ILE A 83  ? ALA A 87  ? ILE A 59  ALA A 63  5 ? 5  
HELX_P HELX_P6  AA6 PRO A 93  ? THR A 116 ? PRO A 69  THR A 92  1 ? 24 
HELX_P HELX_P7  AA7 LYS A 117 ? LYS A 122 ? LYS A 93  LYS A 98  1 ? 6  
HELX_P HELX_P8  AA8 PHE A 123 ? LYS A 128 ? PHE A 99  LYS A 104 1 ? 6  
HELX_P HELX_P9  AA9 PRO A 132 ? SER A 134 ? PRO A 108 SER A 110 5 ? 3  
HELX_P HELX_P10 AB1 ILE A 135 ? MET A 160 ? ILE A 111 MET A 136 1 ? 26 
HELX_P HELX_P11 AB2 SER A 167 ? ILE A 171 ? SER A 143 ILE A 147 5 ? 5  
HELX_P HELX_P12 AB3 GLN A 172 ? VAL A 198 ? GLN A 148 VAL A 174 1 ? 27 
HELX_P HELX_P13 AB4 ASP A 200 ? PHE A 215 ? ASP A 176 PHE A 191 1 ? 16 
HELX_P HELX_P14 AB5 GLY A 226 ? LYS A 236 ? GLY A 202 LYS A 212 1 ? 11 
HELX_P HELX_P15 AB6 ASN A 238 ? LEU A 252 ? ASN A 214 LEU A 228 1 ? 15 
HELX_P HELX_P16 AB7 TRP A 256 ? ASP A 260 ? TRP A 232 ASP A 236 5 ? 5  
HELX_P HELX_P17 AB8 HIS A 261 ? TYR A 286 ? HIS A 237 TYR A 262 1 ? 26 
HELX_P HELX_P18 AB9 GLN A 289 ? LEU A 294 ? GLN A 265 LEU A 270 1 ? 6  
HELX_P HELX_P19 AC1 THR B 19  ? ARG B 23  ? THR B 19  ARG B 23  5 ? 5  
HELX_P HELX_P20 AC2 MET B 24  ? ILE B 29  ? MET B 24  ILE B 29  1 ? 6  
HELX_P HELX_P21 AC3 GLY B 62  ? GLY B 72  ? GLY B 62  GLY B 72  1 ? 11 
HELX_P HELX_P22 AC4 THR B 101 ? MET B 113 ? THR B 101 MET B 113 1 ? 13 
HELX_P HELX_P23 AC5 LYS B 116 ? GLU B 132 ? LYS B 116 GLU B 132 1 ? 17 
HELX_P HELX_P24 AC6 LEU B 133 ? TYR B 138 ? LEU B 133 TYR B 138 5 ? 6  
HELX_P HELX_P25 AC7 PRO B 140 ? TYR B 144 ? PRO B 140 TYR B 144 5 ? 5  
HELX_P HELX_P26 AC8 SER B 145 ? VAL B 160 ? SER B 145 VAL B 160 1 ? 16 
HELX_P HELX_P27 AC9 ALA B 170 ? VAL B 173 ? ALA B 170 VAL B 173 5 ? 4  
HELX_P HELX_P28 AD1 ASP B 175 ? GLN B 192 ? ASP B 175 GLN B 192 1 ? 18 
HELX_P HELX_P29 AD2 ASN B 202 ? CYS B 210 ? ASN B 202 CYS B 210 1 ? 9  
HELX_P HELX_P30 AD3 LEU B 227 ? LYS B 244 ? LEU B 227 LYS B 244 1 ? 18 
HELX_P HELX_P31 AD4 SER B 245 ? ARG B 260 ? SER B 245 ARG B 260 1 ? 16 
HELX_P HELX_P32 AD5 THR C 19  ? ARG C 23  ? THR D 19  ARG D 23  5 ? 5  
HELX_P HELX_P33 AD6 MET C 24  ? ILE C 29  ? MET D 24  ILE D 29  1 ? 6  
HELX_P HELX_P34 AD7 GLY C 62  ? GLY C 72  ? GLY D 62  GLY D 72  1 ? 11 
HELX_P HELX_P35 AD8 THR C 101 ? MET C 113 ? THR D 101 MET D 113 1 ? 13 
HELX_P HELX_P36 AD9 LYS C 116 ? GLU C 132 ? LYS D 116 GLU D 132 1 ? 17 
HELX_P HELX_P37 AE1 LEU C 133 ? TYR C 138 ? LEU D 133 TYR D 138 5 ? 6  
HELX_P HELX_P38 AE2 PRO C 140 ? TYR C 144 ? PRO D 140 TYR D 144 5 ? 5  
HELX_P HELX_P39 AE3 SER C 145 ? VAL C 160 ? SER D 145 VAL D 160 1 ? 16 
HELX_P HELX_P40 AE4 ALA C 170 ? VAL C 173 ? ALA D 170 VAL D 173 5 ? 4  
HELX_P HELX_P41 AE5 ASP C 175 ? GLN C 192 ? ASP D 175 GLN D 192 1 ? 18 
HELX_P HELX_P42 AE6 ASN C 202 ? CYS C 210 ? ASN D 202 CYS D 210 1 ? 9  
HELX_P HELX_P43 AE7 LEU C 227 ? LYS C 244 ? LEU D 227 LYS D 244 1 ? 18 
HELX_P HELX_P44 AE8 SER C 245 ? ARG C 260 ? SER D 245 ARG D 260 1 ? 16 
HELX_P HELX_P45 AE9 SER D 26  ? ASN D 38  ? SER C 2   ASN C 14  1 ? 13 
HELX_P HELX_P46 AF1 ASN D 38  ? ASN D 54  ? ASN C 14  ASN C 30  1 ? 17 
HELX_P HELX_P47 AF2 LEU D 59  ? VAL D 61  ? LEU C 35  VAL C 37  5 ? 3  
HELX_P HELX_P48 AF3 ALA D 62  ? GLY D 80  ? ALA C 38  GLY C 56  1 ? 19 
HELX_P HELX_P49 AF4 ILE D 83  ? ALA D 87  ? ILE C 59  ALA C 63  5 ? 5  
HELX_P HELX_P50 AF5 PRO D 93  ? THR D 116 ? PRO C 69  THR C 92  1 ? 24 
HELX_P HELX_P51 AF6 LYS D 117 ? LYS D 122 ? LYS C 93  LYS C 98  1 ? 6  
HELX_P HELX_P52 AF7 PHE D 123 ? LYS D 128 ? PHE C 99  LYS C 104 1 ? 6  
HELX_P HELX_P53 AF8 PRO D 132 ? SER D 134 ? PRO C 108 SER C 110 5 ? 3  
HELX_P HELX_P54 AF9 ILE D 135 ? MET D 160 ? ILE C 111 MET C 136 1 ? 26 
HELX_P HELX_P55 AG1 SER D 167 ? ILE D 171 ? SER C 143 ILE C 147 5 ? 5  
HELX_P HELX_P56 AG2 GLN D 172 ? VAL D 198 ? GLN C 148 VAL C 174 1 ? 27 
HELX_P HELX_P57 AG3 ASP D 200 ? PHE D 215 ? ASP C 176 PHE C 191 1 ? 16 
HELX_P HELX_P58 AG4 GLY D 226 ? LYS D 236 ? GLY C 202 LYS C 212 1 ? 11 
HELX_P HELX_P59 AG5 ASN D 238 ? LEU D 252 ? ASN C 214 LEU C 228 1 ? 15 
HELX_P HELX_P60 AG6 TRP D 256 ? ASP D 260 ? TRP C 232 ASP C 236 5 ? 5  
HELX_P HELX_P61 AG7 HIS D 261 ? TYR D 286 ? HIS C 237 TYR C 262 1 ? 26 
HELX_P HELX_P62 AG8 GLN D 289 ? LEU D 294 ? GLN C 265 LEU C 270 1 ? 6  
# 
_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 ? ? B SER 64 OG  ? ? ? 1_555 G MG  . MG ? ? B SER 64  B MG  302 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc2  metalc ? ? F ANP .  O1G ? ? ? 1_555 G MG  . MG ? ? B ANP 301 B MG  302 1_555 ? ? ? ? ? ? ? 2.107 ? ? 
metalc3  metalc ? ? F ANP .  O2B ? ? ? 1_555 G MG  . MG ? ? B ANP 301 B MG  302 1_555 ? ? ? ? ? ? ? 2.588 ? ? 
metalc4  metalc ? ? G MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? B MG  302 B HOH 401 1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc5  metalc ? ? G MG  .  MG  ? ? ? 1_555 K HOH . O  ? ? B MG  302 B HOH 403 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc6  metalc ? ? C SER 64 OG  ? ? ? 1_555 I MG  . MG ? ? D SER 64  D MG  302 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc7  metalc ? ? H ANP .  O1G ? ? ? 1_555 I MG  . MG ? ? D ANP 301 D MG  302 1_555 ? ? ? ? ? ? ? 2.106 ? ? 
metalc8  metalc ? ? H ANP .  O2B ? ? ? 1_555 I MG  . MG ? ? D ANP 301 D MG  302 1_555 ? ? ? ? ? ? ? 2.589 ? ? 
metalc9  metalc ? ? I MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? D MG  302 D HOH 401 1_555 ? ? ? ? ? ? ? 1.992 ? ? 
metalc10 metalc ? ? I MG  .  MG  ? ? ? 1_555 L HOH . O  ? ? D MG  302 D HOH 403 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
# 
_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  ? B SER 64 ? B SER 64  ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O1G ? F ANP . ? B ANP 301 ? 1_555 119.5 ? 
2  OG  ? B SER 64 ? B SER 64  ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O2B ? F ANP . ? B ANP 301 ? 1_555 68.0  ? 
3  O1G ? F ANP .  ? B ANP 301 ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O2B ? F ANP . ? B ANP 301 ? 1_555 53.0  ? 
4  OG  ? B SER 64 ? B SER 64  ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O   ? K HOH . ? B HOH 401 ? 1_555 69.0  ? 
5  O1G ? F ANP .  ? B ANP 301 ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O   ? K HOH . ? B HOH 401 ? 1_555 81.9  ? 
6  O2B ? F ANP .  ? B ANP 301 ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O   ? K HOH . ? B HOH 401 ? 1_555 73.6  ? 
7  OG  ? B SER 64 ? B SER 64  ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O   ? K HOH . ? B HOH 403 ? 1_555 92.5  ? 
8  O1G ? F ANP .  ? B ANP 301 ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O   ? K HOH . ? B HOH 403 ? 1_555 107.0 ? 
9  O2B ? F ANP .  ? B ANP 301 ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O   ? K HOH . ? B HOH 403 ? 1_555 98.4  ? 
10 O   ? K HOH .  ? B HOH 401 ? 1_555 MG ? G MG . ? B MG 302 ? 1_555 O   ? K HOH . ? B HOH 403 ? 1_555 161.5 ? 
11 OG  ? C SER 64 ? D SER 64  ? 1_555 MG ? I MG . ? D MG 302 ? 1_555 O1G ? H ANP . ? D ANP 301 ? 1_555 119.5 ? 
12 OG  ? C SER 64 ? D SER 64  ? 1_555 MG ? I MG . ? D MG 302 ? 1_555 O2B ? H ANP . ? D ANP 301 ? 1_555 68.0  ? 
13 O1G ? H ANP .  ? D ANP 301 ? 1_555 MG ? I MG . ? D MG 302 ? 1_555 O2B ? H ANP . ? D ANP 301 ? 1_555 53.0  ? 
14 OG  ? C SER 64 ? D SER 64  ? 1_555 MG ? I MG . ? D MG 302 ? 1_555 O   ? L HOH . ? D HOH 401 ? 1_555 69.0  ? 
15 O1G ? H ANP .  ? D ANP 301 ? 1_555 MG ? I MG . ? D MG 302 ? 1_555 O   ? L HOH . ? D HOH 401 ? 1_555 81.9  ? 
16 O2B ? H ANP .  ? D ANP 301 ? 1_555 MG ? I MG . ? D MG 302 ? 1_555 O   ? L HOH . ? D HOH 401 ? 1_555 73.5  ? 
17 OG  ? C SER 64 ? D SER 64  ? 1_555 MG ? I MG . ? D MG 302 ? 1_555 O   ? L HOH . ? D HOH 403 ? 1_555 92.5  ? 
18 O1G ? H ANP .  ? D ANP 301 ? 1_555 MG ? I MG . ? D MG 302 ? 1_555 O   ? L HOH . ? D HOH 403 ? 1_555 107.0 ? 
19 O2B ? H ANP .  ? D ANP 301 ? 1_555 MG ? I MG . ? D MG 302 ? 1_555 O   ? L HOH . ? D HOH 403 ? 1_555 98.4  ? 
20 O   ? L HOH .  ? D HOH 401 ? 1_555 MG ? I MG . ? D MG 302 ? 1_555 O   ? L HOH . ? D HOH 403 ? 1_555 161.4 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 4 ? 
AA4 ? 6 ? 
# 
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 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? parallel      
AA4 4 5 ? parallel      
AA4 5 6 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL B 78  ? ARG B 83  ? VAL B 78  ARG B 83  
AA1 2 VAL B 5   ? ARG B 15  ? VAL B 5   ARG B 15  
AA1 3 LYS B 35  ? ALA B 47  ? LYS B 35  ALA B 47  
AA1 4 PHE B 261 ? ILE B 263 ? PHE B 261 ILE B 263 
AA2 1 VAL B 87  ? ILE B 90  ? VAL B 87  ILE B 90  
AA2 2 ILE B 164 ? ASP B 168 ? ILE B 164 ASP B 168 
AA2 3 THR B 195 ? VAL B 199 ? THR B 195 VAL B 199 
AA2 4 VAL B 52  ? VAL B 56  ? VAL B 52  VAL B 56  
AA2 5 LYS B 212 ? GLU B 217 ? LYS B 212 GLU B 217 
AA2 6 LYS B 220 ? GLU B 226 ? LYS B 220 GLU B 226 
AA3 1 VAL C 78  ? ARG C 83  ? VAL D 78  ARG D 83  
AA3 2 VAL C 5   ? ARG C 15  ? VAL D 5   ARG D 15  
AA3 3 LYS C 35  ? ALA C 47  ? LYS D 35  ALA D 47  
AA3 4 PHE C 261 ? ILE C 263 ? PHE D 261 ILE D 263 
AA4 1 VAL C 87  ? ILE C 90  ? VAL D 87  ILE D 90  
AA4 2 ILE C 164 ? ASP C 168 ? ILE D 164 ASP D 168 
AA4 3 THR C 195 ? VAL C 199 ? THR D 195 VAL D 199 
AA4 4 VAL C 52  ? VAL C 56  ? VAL D 52  VAL D 56  
AA4 5 LYS C 212 ? GLU C 217 ? LYS D 212 GLU D 217 
AA4 6 LYS C 220 ? GLU C 226 ? LYS D 220 GLU D 226 
# 
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 ASP B 82  ? O ASP B 82  N ASN B 6   ? N ASN B 6   
AA1 2 3 N ILE B 7   ? N ILE B 7   O LEU B 45  ? O LEU B 45  
AA1 3 4 N THR B 36  ? N THR B 36  O VAL B 262 ? O VAL B 262 
AA2 1 2 N SER B 88  ? N SER B 88  O VAL B 166 ? O VAL B 166 
AA2 2 3 N ILE B 167 ? N ILE B 167 O PHE B 197 ? O PHE B 197 
AA2 3 4 O PHE B 198 ? O PHE B 198 N ILE B 53  ? N ILE B 53  
AA2 4 5 N GLY B 54  ? N GLY B 54  O LYS B 212 ? O LYS B 212 
AA2 5 6 N TRP B 215 ? N TRP B 215 O ASP B 223 ? O ASP B 223 
AA3 1 2 O ASP C 82  ? O ASP D 82  N ASN C 6   ? N ASN D 6   
AA3 2 3 N ILE C 7   ? N ILE D 7   O LEU C 45  ? O LEU D 45  
AA3 3 4 N THR C 36  ? N THR D 36  O VAL C 262 ? O VAL D 262 
AA4 1 2 N SER C 88  ? N SER D 88  O VAL C 166 ? O VAL D 166 
AA4 2 3 N ILE C 167 ? N ILE D 167 O PHE C 197 ? O PHE D 197 
AA4 3 4 O PHE C 198 ? O PHE D 198 N ILE C 53  ? N ILE D 53  
AA4 4 5 N GLY C 54  ? N GLY D 54  O LYS C 212 ? O LYS D 212 
AA4 5 6 N TRP C 215 ? N TRP D 215 O ASP C 223 ? O ASP D 223 
# 
_pdbx_entry_details.entry_id                   9CFP 
_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 ARG A 60  ? ? 71.96  -10.47  
2 1 ASN A 200 ? ? 67.95  -169.67 
3 1 GLN A 265 ? ? -97.41 32.70   
4 1 ARG C 60  ? ? 71.93  -10.44  
5 1 ASN C 200 ? ? 67.92  -169.62 
6 1 GLN C 265 ? ? -97.40 32.73   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9CFP 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_reconstruction.entry_id                    9CFP 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.9 
_em_3d_reconstruction.resolution_method           'FSC 0.143 CUT-OFF' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               117415 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               POINT 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            8 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               RECOMBINANT 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 TarGH 
_em_entity_assembly.details              'Hetero tetramer TarG2H2' 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1,2 
# 
_em_imaging.entry_id                        9CFP 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS KRIOS' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            300 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            'BRIGHT FIELD' 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             500 
_em_imaging.nominal_defocus_max             3000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            ? 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
# 
_em_vitrification.entry_id              9CFP 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9CFP 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   'SINGLE PARTICLE' 
_em_experiment.aggregation_state       PARTICLE 
_em_experiment.entity_assembly_id      1 
# 
_em_single_particle_entity.entry_id              9CFP 
_em_single_particle_entity.id                    1 
_em_single_particle_entity.image_processing_id   1 
_em_single_particle_entity.point_symmetry        C2 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET -23 ? A MET 1  
2  1 Y 1 A GLY -22 ? A GLY 2  
3  1 Y 1 A SER -21 ? A SER 3  
4  1 Y 1 A SER -20 ? A SER 4  
5  1 Y 1 A HIS -19 ? A HIS 5  
6  1 Y 1 A HIS -18 ? A HIS 6  
7  1 Y 1 A HIS -17 ? A HIS 7  
8  1 Y 1 A HIS -16 ? A HIS 8  
9  1 Y 1 A HIS -15 ? A HIS 9  
10 1 Y 1 A HIS -14 ? A HIS 10 
11 1 Y 1 A HIS -13 ? A HIS 11 
12 1 Y 1 A HIS -12 ? A HIS 12 
13 1 Y 1 A HIS -11 ? A HIS 13 
14 1 Y 1 A HIS -10 ? A HIS 14 
15 1 Y 1 A SER -9  ? A SER 15 
16 1 Y 1 A SER -8  ? A SER 16 
17 1 Y 1 A GLY -7  ? A GLY 17 
18 1 Y 1 A LEU -6  ? A LEU 18 
19 1 Y 1 A VAL -5  ? A VAL 19 
20 1 Y 1 A PRO -4  ? A PRO 20 
21 1 Y 1 A ARG -3  ? A ARG 21 
22 1 Y 1 A GLY -2  ? A GLY 22 
23 1 Y 1 A SER -1  ? A SER 23 
24 1 Y 1 A HIS 0   ? A HIS 24 
25 1 Y 1 C MET -23 ? D MET 1  
26 1 Y 1 C GLY -22 ? D GLY 2  
27 1 Y 1 C SER -21 ? D SER 3  
28 1 Y 1 C SER -20 ? D SER 4  
29 1 Y 1 C HIS -19 ? D HIS 5  
30 1 Y 1 C HIS -18 ? D HIS 6  
31 1 Y 1 C HIS -17 ? D HIS 7  
32 1 Y 1 C HIS -16 ? D HIS 8  
33 1 Y 1 C HIS -15 ? D HIS 9  
34 1 Y 1 C HIS -14 ? D HIS 10 
35 1 Y 1 C HIS -13 ? D HIS 11 
36 1 Y 1 C HIS -12 ? D HIS 12 
37 1 Y 1 C HIS -11 ? D HIS 13 
38 1 Y 1 C HIS -10 ? D HIS 14 
39 1 Y 1 C SER -9  ? D SER 15 
40 1 Y 1 C SER -8  ? D SER 16 
41 1 Y 1 C GLY -7  ? D GLY 17 
42 1 Y 1 C LEU -6  ? D LEU 18 
43 1 Y 1 C VAL -5  ? D VAL 19 
44 1 Y 1 C PRO -4  ? D PRO 20 
45 1 Y 1 C ARG -3  ? D ARG 21 
46 1 Y 1 C GLY -2  ? D GLY 22 
47 1 Y 1 C SER -1  ? D SER 23 
48 1 Y 1 C HIS 0   ? D HIS 24 
# 
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 
A1AV9 C4     C  Y N 1   
A1AV9 C5     C  Y N 2   
A1AV9 C6     C  Y N 3   
A1AV9 C7     C  Y N 4   
A1AV9 C8     C  Y N 5   
A1AV9 C10    C  Y N 6   
A1AV9 C20    C  Y N 7   
A1AV9 C21    C  Y N 8   
A1AV9 C24    C  N N 9   
A1AV9 C26    C  N N 10  
A1AV9 C1     C  Y N 11  
A1AV9 C11    C  Y N 12  
A1AV9 C18    C  Y N 13  
A1AV9 C19    C  Y N 14  
A1AV9 C2     C  Y N 15  
A1AV9 C23    C  N N 16  
A1AV9 C25    C  N N 17  
A1AV9 C27    C  N N 18  
A1AV9 C29    C  N N 19  
A1AV9 C3     C  Y N 20  
A1AV9 C30    C  N N 21  
A1AV9 C32    C  N N 22  
A1AV9 C33    C  N N 23  
A1AV9 C34    C  N N 24  
A1AV9 C35    C  N R 25  
A1AV9 C41    C  N N 26  
A1AV9 N31    N  N N 27  
A1AV9 O22    O  N N 28  
A1AV9 O28    O  N N 29  
A1AV9 O42    O  N N 30  
A1AV9 O43    O  N N 31  
A1AV9 O44    O  N N 32  
A1AV9 O9     O  Y N 33  
A1AV9 CL1    CL N N 34  
A1AV9 H1     H  N N 35  
A1AV9 H2     H  N N 36  
A1AV9 H3     H  N N 37  
A1AV9 H4     H  N N 38  
A1AV9 H5     H  N N 39  
A1AV9 H6     H  N N 40  
A1AV9 H7     H  N N 41  
A1AV9 H8     H  N N 42  
A1AV9 H9     H  N N 43  
A1AV9 H10    H  N N 44  
A1AV9 H11    H  N N 45  
A1AV9 H12    H  N N 46  
A1AV9 H13    H  N N 47  
A1AV9 H14    H  N N 48  
A1AV9 H15    H  N N 49  
A1AV9 H16    H  N N 50  
A1AV9 H17    H  N N 51  
A1AV9 H18    H  N N 52  
A1AV9 H19    H  N N 53  
A1AV9 H20    H  N N 54  
A1AV9 H21    H  N N 55  
A1AV9 H22    H  N N 56  
ALA   N      N  N N 57  
ALA   CA     C  N S 58  
ALA   C      C  N N 59  
ALA   O      O  N N 60  
ALA   CB     C  N N 61  
ALA   OXT    O  N N 62  
ALA   H      H  N N 63  
ALA   H2     H  N N 64  
ALA   HA     H  N N 65  
ALA   HB1    H  N N 66  
ALA   HB2    H  N N 67  
ALA   HB3    H  N N 68  
ALA   HXT    H  N N 69  
ANP   PG     P  N N 70  
ANP   O1G    O  N N 71  
ANP   O2G    O  N N 72  
ANP   O3G    O  N N 73  
ANP   PB     P  N N 74  
ANP   O1B    O  N N 75  
ANP   O2B    O  N N 76  
ANP   N3B    N  N N 77  
ANP   PA     P  N N 78  
ANP   O1A    O  N N 79  
ANP   O2A    O  N N 80  
ANP   O3A    O  N N 81  
ANP   "O5'"  O  N N 82  
ANP   "C5'"  C  N N 83  
ANP   "C4'"  C  N R 84  
ANP   "O4'"  O  N N 85  
ANP   "C3'"  C  N S 86  
ANP   "O3'"  O  N N 87  
ANP   "C2'"  C  N R 88  
ANP   "O2'"  O  N N 89  
ANP   "C1'"  C  N R 90  
ANP   N9     N  Y N 91  
ANP   C8     C  Y N 92  
ANP   N7     N  Y N 93  
ANP   C5     C  Y N 94  
ANP   C6     C  Y N 95  
ANP   N6     N  N N 96  
ANP   N1     N  Y N 97  
ANP   C2     C  Y N 98  
ANP   N3     N  Y N 99  
ANP   C4     C  Y N 100 
ANP   HOG2   H  N N 101 
ANP   HOG3   H  N N 102 
ANP   HOB2   H  N N 103 
ANP   HNB1   H  N N 104 
ANP   HOA2   H  N N 105 
ANP   "H5'1" H  N N 106 
ANP   "H5'2" H  N N 107 
ANP   "H4'"  H  N N 108 
ANP   "H3'"  H  N N 109 
ANP   "HO3'" H  N N 110 
ANP   "H2'"  H  N N 111 
ANP   "HO2'" H  N N 112 
ANP   "H1'"  H  N N 113 
ANP   H8     H  N N 114 
ANP   HN61   H  N N 115 
ANP   HN62   H  N N 116 
ANP   H2     H  N N 117 
ARG   N      N  N N 118 
ARG   CA     C  N S 119 
ARG   C      C  N N 120 
ARG   O      O  N N 121 
ARG   CB     C  N N 122 
ARG   CG     C  N N 123 
ARG   CD     C  N N 124 
ARG   NE     N  N N 125 
ARG   CZ     C  N N 126 
ARG   NH1    N  N N 127 
ARG   NH2    N  N N 128 
ARG   OXT    O  N N 129 
ARG   H      H  N N 130 
ARG   H2     H  N N 131 
ARG   HA     H  N N 132 
ARG   HB2    H  N N 133 
ARG   HB3    H  N N 134 
ARG   HG2    H  N N 135 
ARG   HG3    H  N N 136 
ARG   HD2    H  N N 137 
ARG   HD3    H  N N 138 
ARG   HE     H  N N 139 
ARG   HH11   H  N N 140 
ARG   HH12   H  N N 141 
ARG   HH21   H  N N 142 
ARG   HH22   H  N N 143 
ARG   HXT    H  N N 144 
ASN   N      N  N N 145 
ASN   CA     C  N S 146 
ASN   C      C  N N 147 
ASN   O      O  N N 148 
ASN   CB     C  N N 149 
ASN   CG     C  N N 150 
ASN   OD1    O  N N 151 
ASN   ND2    N  N N 152 
ASN   OXT    O  N N 153 
ASN   H      H  N N 154 
ASN   H2     H  N N 155 
ASN   HA     H  N N 156 
ASN   HB2    H  N N 157 
ASN   HB3    H  N N 158 
ASN   HD21   H  N N 159 
ASN   HD22   H  N N 160 
ASN   HXT    H  N N 161 
ASP   N      N  N N 162 
ASP   CA     C  N S 163 
ASP   C      C  N N 164 
ASP   O      O  N N 165 
ASP   CB     C  N N 166 
ASP   CG     C  N N 167 
ASP   OD1    O  N N 168 
ASP   OD2    O  N N 169 
ASP   OXT    O  N N 170 
ASP   H      H  N N 171 
ASP   H2     H  N N 172 
ASP   HA     H  N N 173 
ASP   HB2    H  N N 174 
ASP   HB3    H  N N 175 
ASP   HD2    H  N N 176 
ASP   HXT    H  N N 177 
CYS   N      N  N N 178 
CYS   CA     C  N R 179 
CYS   C      C  N N 180 
CYS   O      O  N N 181 
CYS   CB     C  N N 182 
CYS   SG     S  N N 183 
CYS   OXT    O  N N 184 
CYS   H      H  N N 185 
CYS   H2     H  N N 186 
CYS   HA     H  N N 187 
CYS   HB2    H  N N 188 
CYS   HB3    H  N N 189 
CYS   HG     H  N N 190 
CYS   HXT    H  N N 191 
GLN   N      N  N N 192 
GLN   CA     C  N S 193 
GLN   C      C  N N 194 
GLN   O      O  N N 195 
GLN   CB     C  N N 196 
GLN   CG     C  N N 197 
GLN   CD     C  N N 198 
GLN   OE1    O  N N 199 
GLN   NE2    N  N N 200 
GLN   OXT    O  N N 201 
GLN   H      H  N N 202 
GLN   H2     H  N N 203 
GLN   HA     H  N N 204 
GLN   HB2    H  N N 205 
GLN   HB3    H  N N 206 
GLN   HG2    H  N N 207 
GLN   HG3    H  N N 208 
GLN   HE21   H  N N 209 
GLN   HE22   H  N N 210 
GLN   HXT    H  N N 211 
GLU   N      N  N N 212 
GLU   CA     C  N S 213 
GLU   C      C  N N 214 
GLU   O      O  N N 215 
GLU   CB     C  N N 216 
GLU   CG     C  N N 217 
GLU   CD     C  N N 218 
GLU   OE1    O  N N 219 
GLU   OE2    O  N N 220 
GLU   OXT    O  N N 221 
GLU   H      H  N N 222 
GLU   H2     H  N N 223 
GLU   HA     H  N N 224 
GLU   HB2    H  N N 225 
GLU   HB3    H  N N 226 
GLU   HG2    H  N N 227 
GLU   HG3    H  N N 228 
GLU   HE2    H  N N 229 
GLU   HXT    H  N N 230 
GLY   N      N  N N 231 
GLY   CA     C  N N 232 
GLY   C      C  N N 233 
GLY   O      O  N N 234 
GLY   OXT    O  N N 235 
GLY   H      H  N N 236 
GLY   H2     H  N N 237 
GLY   HA2    H  N N 238 
GLY   HA3    H  N N 239 
GLY   HXT    H  N N 240 
HIS   N      N  N N 241 
HIS   CA     C  N S 242 
HIS   C      C  N N 243 
HIS   O      O  N N 244 
HIS   CB     C  N N 245 
HIS   CG     C  Y N 246 
HIS   ND1    N  Y N 247 
HIS   CD2    C  Y N 248 
HIS   CE1    C  Y N 249 
HIS   NE2    N  Y N 250 
HIS   OXT    O  N N 251 
HIS   H      H  N N 252 
HIS   H2     H  N N 253 
HIS   HA     H  N N 254 
HIS   HB2    H  N N 255 
HIS   HB3    H  N N 256 
HIS   HD1    H  N N 257 
HIS   HD2    H  N N 258 
HIS   HE1    H  N N 259 
HIS   HE2    H  N N 260 
HIS   HXT    H  N N 261 
HOH   O      O  N N 262 
HOH   H1     H  N N 263 
HOH   H2     H  N N 264 
ILE   N      N  N N 265 
ILE   CA     C  N S 266 
ILE   C      C  N N 267 
ILE   O      O  N N 268 
ILE   CB     C  N S 269 
ILE   CG1    C  N N 270 
ILE   CG2    C  N N 271 
ILE   CD1    C  N N 272 
ILE   OXT    O  N N 273 
ILE   H      H  N N 274 
ILE   H2     H  N N 275 
ILE   HA     H  N N 276 
ILE   HB     H  N N 277 
ILE   HG12   H  N N 278 
ILE   HG13   H  N N 279 
ILE   HG21   H  N N 280 
ILE   HG22   H  N N 281 
ILE   HG23   H  N N 282 
ILE   HD11   H  N N 283 
ILE   HD12   H  N N 284 
ILE   HD13   H  N N 285 
ILE   HXT    H  N N 286 
LEU   N      N  N N 287 
LEU   CA     C  N S 288 
LEU   C      C  N N 289 
LEU   O      O  N N 290 
LEU   CB     C  N N 291 
LEU   CG     C  N N 292 
LEU   CD1    C  N N 293 
LEU   CD2    C  N N 294 
LEU   OXT    O  N N 295 
LEU   H      H  N N 296 
LEU   H2     H  N N 297 
LEU   HA     H  N N 298 
LEU   HB2    H  N N 299 
LEU   HB3    H  N N 300 
LEU   HG     H  N N 301 
LEU   HD11   H  N N 302 
LEU   HD12   H  N N 303 
LEU   HD13   H  N N 304 
LEU   HD21   H  N N 305 
LEU   HD22   H  N N 306 
LEU   HD23   H  N N 307 
LEU   HXT    H  N N 308 
LYS   N      N  N N 309 
LYS   CA     C  N S 310 
LYS   C      C  N N 311 
LYS   O      O  N N 312 
LYS   CB     C  N N 313 
LYS   CG     C  N N 314 
LYS   CD     C  N N 315 
LYS   CE     C  N N 316 
LYS   NZ     N  N N 317 
LYS   OXT    O  N N 318 
LYS   H      H  N N 319 
LYS   H2     H  N N 320 
LYS   HA     H  N N 321 
LYS   HB2    H  N N 322 
LYS   HB3    H  N N 323 
LYS   HG2    H  N N 324 
LYS   HG3    H  N N 325 
LYS   HD2    H  N N 326 
LYS   HD3    H  N N 327 
LYS   HE2    H  N N 328 
LYS   HE3    H  N N 329 
LYS   HZ1    H  N N 330 
LYS   HZ2    H  N N 331 
LYS   HZ3    H  N N 332 
LYS   HXT    H  N N 333 
MET   N      N  N N 334 
MET   CA     C  N S 335 
MET   C      C  N N 336 
MET   O      O  N N 337 
MET   CB     C  N N 338 
MET   CG     C  N N 339 
MET   SD     S  N N 340 
MET   CE     C  N N 341 
MET   OXT    O  N N 342 
MET   H      H  N N 343 
MET   H2     H  N N 344 
MET   HA     H  N N 345 
MET   HB2    H  N N 346 
MET   HB3    H  N N 347 
MET   HG2    H  N N 348 
MET   HG3    H  N N 349 
MET   HE1    H  N N 350 
MET   HE2    H  N N 351 
MET   HE3    H  N N 352 
MET   HXT    H  N N 353 
MG    MG     MG N N 354 
PHE   N      N  N N 355 
PHE   CA     C  N S 356 
PHE   C      C  N N 357 
PHE   O      O  N N 358 
PHE   CB     C  N N 359 
PHE   CG     C  Y N 360 
PHE   CD1    C  Y N 361 
PHE   CD2    C  Y N 362 
PHE   CE1    C  Y N 363 
PHE   CE2    C  Y N 364 
PHE   CZ     C  Y N 365 
PHE   OXT    O  N N 366 
PHE   H      H  N N 367 
PHE   H2     H  N N 368 
PHE   HA     H  N N 369 
PHE   HB2    H  N N 370 
PHE   HB3    H  N N 371 
PHE   HD1    H  N N 372 
PHE   HD2    H  N N 373 
PHE   HE1    H  N N 374 
PHE   HE2    H  N N 375 
PHE   HZ     H  N N 376 
PHE   HXT    H  N N 377 
PRO   N      N  N N 378 
PRO   CA     C  N S 379 
PRO   C      C  N N 380 
PRO   O      O  N N 381 
PRO   CB     C  N N 382 
PRO   CG     C  N N 383 
PRO   CD     C  N N 384 
PRO   OXT    O  N N 385 
PRO   H      H  N N 386 
PRO   HA     H  N N 387 
PRO   HB2    H  N N 388 
PRO   HB3    H  N N 389 
PRO   HG2    H  N N 390 
PRO   HG3    H  N N 391 
PRO   HD2    H  N N 392 
PRO   HD3    H  N N 393 
PRO   HXT    H  N N 394 
SER   N      N  N N 395 
SER   CA     C  N S 396 
SER   C      C  N N 397 
SER   O      O  N N 398 
SER   CB     C  N N 399 
SER   OG     O  N N 400 
SER   OXT    O  N N 401 
SER   H      H  N N 402 
SER   H2     H  N N 403 
SER   HA     H  N N 404 
SER   HB2    H  N N 405 
SER   HB3    H  N N 406 
SER   HG     H  N N 407 
SER   HXT    H  N N 408 
THR   N      N  N N 409 
THR   CA     C  N S 410 
THR   C      C  N N 411 
THR   O      O  N N 412 
THR   CB     C  N R 413 
THR   OG1    O  N N 414 
THR   CG2    C  N N 415 
THR   OXT    O  N N 416 
THR   H      H  N N 417 
THR   H2     H  N N 418 
THR   HA     H  N N 419 
THR   HB     H  N N 420 
THR   HG1    H  N N 421 
THR   HG21   H  N N 422 
THR   HG22   H  N N 423 
THR   HG23   H  N N 424 
THR   HXT    H  N N 425 
TRP   N      N  N N 426 
TRP   CA     C  N S 427 
TRP   C      C  N N 428 
TRP   O      O  N N 429 
TRP   CB     C  N N 430 
TRP   CG     C  Y N 431 
TRP   CD1    C  Y N 432 
TRP   CD2    C  Y N 433 
TRP   NE1    N  Y N 434 
TRP   CE2    C  Y N 435 
TRP   CE3    C  Y N 436 
TRP   CZ2    C  Y N 437 
TRP   CZ3    C  Y N 438 
TRP   CH2    C  Y N 439 
TRP   OXT    O  N N 440 
TRP   H      H  N N 441 
TRP   H2     H  N N 442 
TRP   HA     H  N N 443 
TRP   HB2    H  N N 444 
TRP   HB3    H  N N 445 
TRP   HD1    H  N N 446 
TRP   HE1    H  N N 447 
TRP   HE3    H  N N 448 
TRP   HZ2    H  N N 449 
TRP   HZ3    H  N N 450 
TRP   HH2    H  N N 451 
TRP   HXT    H  N N 452 
TYR   N      N  N N 453 
TYR   CA     C  N S 454 
TYR   C      C  N N 455 
TYR   O      O  N N 456 
TYR   CB     C  N N 457 
TYR   CG     C  Y N 458 
TYR   CD1    C  Y N 459 
TYR   CD2    C  Y N 460 
TYR   CE1    C  Y N 461 
TYR   CE2    C  Y N 462 
TYR   CZ     C  Y N 463 
TYR   OH     O  N N 464 
TYR   OXT    O  N N 465 
TYR   H      H  N N 466 
TYR   H2     H  N N 467 
TYR   HA     H  N N 468 
TYR   HB2    H  N N 469 
TYR   HB3    H  N N 470 
TYR   HD1    H  N N 471 
TYR   HD2    H  N N 472 
TYR   HE1    H  N N 473 
TYR   HE2    H  N N 474 
TYR   HH     H  N N 475 
TYR   HXT    H  N N 476 
VAL   N      N  N N 477 
VAL   CA     C  N S 478 
VAL   C      C  N N 479 
VAL   O      O  N N 480 
VAL   CB     C  N N 481 
VAL   CG1    C  N N 482 
VAL   CG2    C  N N 483 
VAL   OXT    O  N N 484 
VAL   H      H  N N 485 
VAL   H2     H  N N 486 
VAL   HA     H  N N 487 
VAL   HB     H  N N 488 
VAL   HG11   H  N N 489 
VAL   HG12   H  N N 490 
VAL   HG13   H  N N 491 
VAL   HG21   H  N N 492 
VAL   HG22   H  N N 493 
VAL   HG23   H  N N 494 
VAL   HXT    H  N N 495 
# 
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 
A1AV9 O9    C8     sing Y N 1   
A1AV9 O9    C10    sing Y N 2   
A1AV9 C26   C18    sing N N 3   
A1AV9 C8    C7     doub Y N 4   
A1AV9 C10   C18    doub Y N 5   
A1AV9 C10   C11    sing Y N 6   
A1AV9 C18   C19    sing Y N 7   
A1AV9 C7    C11    sing Y N 8   
A1AV9 C7    C4     sing N N 9   
A1AV9 C3    C4     doub Y N 10  
A1AV9 C3    C2     sing Y N 11  
A1AV9 C11   C21    doub Y N 12  
A1AV9 C4    C5     sing Y N 13  
A1AV9 C2    C1     doub Y N 14  
A1AV9 C19   O22    sing N N 15  
A1AV9 C19   C20    doub Y N 16  
A1AV9 O22   C23    sing N N 17  
A1AV9 C21   C20    sing Y N 18  
A1AV9 C5    C6     doub Y N 19  
A1AV9 C1    C6     sing Y N 20  
A1AV9 C1    CL1    sing N N 21  
A1AV9 C20   C25    sing N N 22  
A1AV9 C23   O28    doub N N 23  
A1AV9 C23   C24    sing N N 24  
A1AV9 C25   C24    doub N N 25  
A1AV9 C25   C27    sing N N 26  
A1AV9 C24   C29    sing N N 27  
A1AV9 O44   C30    doub N N 28  
A1AV9 C29   C30    sing N N 29  
A1AV9 C30   N31    sing N N 30  
A1AV9 C32   N31    sing N N 31  
A1AV9 C32   C33    sing N N 32  
A1AV9 N31   C35    sing N N 33  
A1AV9 C33   C34    sing N N 34  
A1AV9 O42   C41    doub N N 35  
A1AV9 C41   C35    sing N N 36  
A1AV9 C41   O43    sing N N 37  
A1AV9 C35   C34    sing N N 38  
A1AV9 C5    H1     sing N N 39  
A1AV9 C6    H2     sing N N 40  
A1AV9 C8    H3     sing N N 41  
A1AV9 C21   H4     sing N N 42  
A1AV9 C26   H5     sing N N 43  
A1AV9 C26   H6     sing N N 44  
A1AV9 C26   H7     sing N N 45  
A1AV9 C2    H8     sing N N 46  
A1AV9 C27   H9     sing N N 47  
A1AV9 C27   H10    sing N N 48  
A1AV9 C27   H11    sing N N 49  
A1AV9 C29   H12    sing N N 50  
A1AV9 C29   H13    sing N N 51  
A1AV9 C3    H14    sing N N 52  
A1AV9 C32   H15    sing N N 53  
A1AV9 C32   H16    sing N N 54  
A1AV9 C33   H17    sing N N 55  
A1AV9 C33   H18    sing N N 56  
A1AV9 C34   H19    sing N N 57  
A1AV9 C34   H20    sing N N 58  
A1AV9 C35   H21    sing N N 59  
A1AV9 O43   H22    sing N N 60  
ALA   N     CA     sing N N 61  
ALA   N     H      sing N N 62  
ALA   N     H2     sing N N 63  
ALA   CA    C      sing N N 64  
ALA   CA    CB     sing N N 65  
ALA   CA    HA     sing N N 66  
ALA   C     O      doub N N 67  
ALA   C     OXT    sing N N 68  
ALA   CB    HB1    sing N N 69  
ALA   CB    HB2    sing N N 70  
ALA   CB    HB3    sing N N 71  
ALA   OXT   HXT    sing N N 72  
ANP   PG    O1G    doub N N 73  
ANP   PG    O2G    sing N N 74  
ANP   PG    O3G    sing N N 75  
ANP   PG    N3B    sing N N 76  
ANP   O2G   HOG2   sing N N 77  
ANP   O3G   HOG3   sing N N 78  
ANP   PB    O1B    doub N N 79  
ANP   PB    O2B    sing N N 80  
ANP   PB    N3B    sing N N 81  
ANP   PB    O3A    sing N N 82  
ANP   O2B   HOB2   sing N N 83  
ANP   N3B   HNB1   sing N N 84  
ANP   PA    O1A    doub N N 85  
ANP   PA    O2A    sing N N 86  
ANP   PA    O3A    sing N N 87  
ANP   PA    "O5'"  sing N N 88  
ANP   O2A   HOA2   sing N N 89  
ANP   "O5'" "C5'"  sing N N 90  
ANP   "C5'" "C4'"  sing N N 91  
ANP   "C5'" "H5'1" sing N N 92  
ANP   "C5'" "H5'2" sing N N 93  
ANP   "C4'" "O4'"  sing N N 94  
ANP   "C4'" "C3'"  sing N N 95  
ANP   "C4'" "H4'"  sing N N 96  
ANP   "O4'" "C1'"  sing N N 97  
ANP   "C3'" "O3'"  sing N N 98  
ANP   "C3'" "C2'"  sing N N 99  
ANP   "C3'" "H3'"  sing N N 100 
ANP   "O3'" "HO3'" sing N N 101 
ANP   "C2'" "O2'"  sing N N 102 
ANP   "C2'" "C1'"  sing N N 103 
ANP   "C2'" "H2'"  sing N N 104 
ANP   "O2'" "HO2'" sing N N 105 
ANP   "C1'" N9     sing N N 106 
ANP   "C1'" "H1'"  sing N N 107 
ANP   N9    C8     sing Y N 108 
ANP   N9    C4     sing Y N 109 
ANP   C8    N7     doub Y N 110 
ANP   C8    H8     sing N N 111 
ANP   N7    C5     sing Y N 112 
ANP   C5    C6     sing Y N 113 
ANP   C5    C4     doub Y N 114 
ANP   C6    N6     sing N N 115 
ANP   C6    N1     doub Y N 116 
ANP   N6    HN61   sing N N 117 
ANP   N6    HN62   sing N N 118 
ANP   N1    C2     sing Y N 119 
ANP   C2    N3     doub Y N 120 
ANP   C2    H2     sing N N 121 
ANP   N3    C4     sing Y N 122 
ARG   N     CA     sing N N 123 
ARG   N     H      sing N N 124 
ARG   N     H2     sing N N 125 
ARG   CA    C      sing N N 126 
ARG   CA    CB     sing N N 127 
ARG   CA    HA     sing N N 128 
ARG   C     O      doub N N 129 
ARG   C     OXT    sing N N 130 
ARG   CB    CG     sing N N 131 
ARG   CB    HB2    sing N N 132 
ARG   CB    HB3    sing N N 133 
ARG   CG    CD     sing N N 134 
ARG   CG    HG2    sing N N 135 
ARG   CG    HG3    sing N N 136 
ARG   CD    NE     sing N N 137 
ARG   CD    HD2    sing N N 138 
ARG   CD    HD3    sing N N 139 
ARG   NE    CZ     sing N N 140 
ARG   NE    HE     sing N N 141 
ARG   CZ    NH1    sing N N 142 
ARG   CZ    NH2    doub N N 143 
ARG   NH1   HH11   sing N N 144 
ARG   NH1   HH12   sing N N 145 
ARG   NH2   HH21   sing N N 146 
ARG   NH2   HH22   sing N N 147 
ARG   OXT   HXT    sing N N 148 
ASN   N     CA     sing N N 149 
ASN   N     H      sing N N 150 
ASN   N     H2     sing N N 151 
ASN   CA    C      sing N N 152 
ASN   CA    CB     sing N N 153 
ASN   CA    HA     sing N N 154 
ASN   C     O      doub N N 155 
ASN   C     OXT    sing N N 156 
ASN   CB    CG     sing N N 157 
ASN   CB    HB2    sing N N 158 
ASN   CB    HB3    sing N N 159 
ASN   CG    OD1    doub N N 160 
ASN   CG    ND2    sing N N 161 
ASN   ND2   HD21   sing N N 162 
ASN   ND2   HD22   sing N N 163 
ASN   OXT   HXT    sing N N 164 
ASP   N     CA     sing N N 165 
ASP   N     H      sing N N 166 
ASP   N     H2     sing N N 167 
ASP   CA    C      sing N N 168 
ASP   CA    CB     sing N N 169 
ASP   CA    HA     sing N N 170 
ASP   C     O      doub N N 171 
ASP   C     OXT    sing N N 172 
ASP   CB    CG     sing N N 173 
ASP   CB    HB2    sing N N 174 
ASP   CB    HB3    sing N N 175 
ASP   CG    OD1    doub N N 176 
ASP   CG    OD2    sing N N 177 
ASP   OD2   HD2    sing N N 178 
ASP   OXT   HXT    sing N N 179 
CYS   N     CA     sing N N 180 
CYS   N     H      sing N N 181 
CYS   N     H2     sing N N 182 
CYS   CA    C      sing N N 183 
CYS   CA    CB     sing N N 184 
CYS   CA    HA     sing N N 185 
CYS   C     O      doub N N 186 
CYS   C     OXT    sing N N 187 
CYS   CB    SG     sing N N 188 
CYS   CB    HB2    sing N N 189 
CYS   CB    HB3    sing N N 190 
CYS   SG    HG     sing N N 191 
CYS   OXT   HXT    sing N N 192 
GLN   N     CA     sing N N 193 
GLN   N     H      sing N N 194 
GLN   N     H2     sing N N 195 
GLN   CA    C      sing N N 196 
GLN   CA    CB     sing N N 197 
GLN   CA    HA     sing N N 198 
GLN   C     O      doub N N 199 
GLN   C     OXT    sing N N 200 
GLN   CB    CG     sing N N 201 
GLN   CB    HB2    sing N N 202 
GLN   CB    HB3    sing N N 203 
GLN   CG    CD     sing N N 204 
GLN   CG    HG2    sing N N 205 
GLN   CG    HG3    sing N N 206 
GLN   CD    OE1    doub N N 207 
GLN   CD    NE2    sing N N 208 
GLN   NE2   HE21   sing N N 209 
GLN   NE2   HE22   sing N N 210 
GLN   OXT   HXT    sing N N 211 
GLU   N     CA     sing N N 212 
GLU   N     H      sing N N 213 
GLU   N     H2     sing N N 214 
GLU   CA    C      sing N N 215 
GLU   CA    CB     sing N N 216 
GLU   CA    HA     sing N N 217 
GLU   C     O      doub N N 218 
GLU   C     OXT    sing N N 219 
GLU   CB    CG     sing N N 220 
GLU   CB    HB2    sing N N 221 
GLU   CB    HB3    sing N N 222 
GLU   CG    CD     sing N N 223 
GLU   CG    HG2    sing N N 224 
GLU   CG    HG3    sing N N 225 
GLU   CD    OE1    doub N N 226 
GLU   CD    OE2    sing N N 227 
GLU   OE2   HE2    sing N N 228 
GLU   OXT   HXT    sing N N 229 
GLY   N     CA     sing N N 230 
GLY   N     H      sing N N 231 
GLY   N     H2     sing N N 232 
GLY   CA    C      sing N N 233 
GLY   CA    HA2    sing N N 234 
GLY   CA    HA3    sing N N 235 
GLY   C     O      doub N N 236 
GLY   C     OXT    sing N N 237 
GLY   OXT   HXT    sing N N 238 
HIS   N     CA     sing N N 239 
HIS   N     H      sing N N 240 
HIS   N     H2     sing N N 241 
HIS   CA    C      sing N N 242 
HIS   CA    CB     sing N N 243 
HIS   CA    HA     sing N N 244 
HIS   C     O      doub N N 245 
HIS   C     OXT    sing N N 246 
HIS   CB    CG     sing N N 247 
HIS   CB    HB2    sing N N 248 
HIS   CB    HB3    sing N N 249 
HIS   CG    ND1    sing Y N 250 
HIS   CG    CD2    doub Y N 251 
HIS   ND1   CE1    doub Y N 252 
HIS   ND1   HD1    sing N N 253 
HIS   CD2   NE2    sing Y N 254 
HIS   CD2   HD2    sing N N 255 
HIS   CE1   NE2    sing Y N 256 
HIS   CE1   HE1    sing N N 257 
HIS   NE2   HE2    sing N N 258 
HIS   OXT   HXT    sing N N 259 
HOH   O     H1     sing N N 260 
HOH   O     H2     sing N N 261 
ILE   N     CA     sing N N 262 
ILE   N     H      sing N N 263 
ILE   N     H2     sing N N 264 
ILE   CA    C      sing N N 265 
ILE   CA    CB     sing N N 266 
ILE   CA    HA     sing N N 267 
ILE   C     O      doub N N 268 
ILE   C     OXT    sing N N 269 
ILE   CB    CG1    sing N N 270 
ILE   CB    CG2    sing N N 271 
ILE   CB    HB     sing N N 272 
ILE   CG1   CD1    sing N N 273 
ILE   CG1   HG12   sing N N 274 
ILE   CG1   HG13   sing N N 275 
ILE   CG2   HG21   sing N N 276 
ILE   CG2   HG22   sing N N 277 
ILE   CG2   HG23   sing N N 278 
ILE   CD1   HD11   sing N N 279 
ILE   CD1   HD12   sing N N 280 
ILE   CD1   HD13   sing N N 281 
ILE   OXT   HXT    sing N N 282 
LEU   N     CA     sing N N 283 
LEU   N     H      sing N N 284 
LEU   N     H2     sing N N 285 
LEU   CA    C      sing N N 286 
LEU   CA    CB     sing N N 287 
LEU   CA    HA     sing N N 288 
LEU   C     O      doub N N 289 
LEU   C     OXT    sing N N 290 
LEU   CB    CG     sing N N 291 
LEU   CB    HB2    sing N N 292 
LEU   CB    HB3    sing N N 293 
LEU   CG    CD1    sing N N 294 
LEU   CG    CD2    sing N N 295 
LEU   CG    HG     sing N N 296 
LEU   CD1   HD11   sing N N 297 
LEU   CD1   HD12   sing N N 298 
LEU   CD1   HD13   sing N N 299 
LEU   CD2   HD21   sing N N 300 
LEU   CD2   HD22   sing N N 301 
LEU   CD2   HD23   sing N N 302 
LEU   OXT   HXT    sing N N 303 
LYS   N     CA     sing N N 304 
LYS   N     H      sing N N 305 
LYS   N     H2     sing N N 306 
LYS   CA    C      sing N N 307 
LYS   CA    CB     sing N N 308 
LYS   CA    HA     sing N N 309 
LYS   C     O      doub N N 310 
LYS   C     OXT    sing N N 311 
LYS   CB    CG     sing N N 312 
LYS   CB    HB2    sing N N 313 
LYS   CB    HB3    sing N N 314 
LYS   CG    CD     sing N N 315 
LYS   CG    HG2    sing N N 316 
LYS   CG    HG3    sing N N 317 
LYS   CD    CE     sing N N 318 
LYS   CD    HD2    sing N N 319 
LYS   CD    HD3    sing N N 320 
LYS   CE    NZ     sing N N 321 
LYS   CE    HE2    sing N N 322 
LYS   CE    HE3    sing N N 323 
LYS   NZ    HZ1    sing N N 324 
LYS   NZ    HZ2    sing N N 325 
LYS   NZ    HZ3    sing N N 326 
LYS   OXT   HXT    sing N N 327 
MET   N     CA     sing N N 328 
MET   N     H      sing N N 329 
MET   N     H2     sing N N 330 
MET   CA    C      sing N N 331 
MET   CA    CB     sing N N 332 
MET   CA    HA     sing N N 333 
MET   C     O      doub N N 334 
MET   C     OXT    sing N N 335 
MET   CB    CG     sing N N 336 
MET   CB    HB2    sing N N 337 
MET   CB    HB3    sing N N 338 
MET   CG    SD     sing N N 339 
MET   CG    HG2    sing N N 340 
MET   CG    HG3    sing N N 341 
MET   SD    CE     sing N N 342 
MET   CE    HE1    sing N N 343 
MET   CE    HE2    sing N N 344 
MET   CE    HE3    sing N N 345 
MET   OXT   HXT    sing N N 346 
PHE   N     CA     sing N N 347 
PHE   N     H      sing N N 348 
PHE   N     H2     sing N N 349 
PHE   CA    C      sing N N 350 
PHE   CA    CB     sing N N 351 
PHE   CA    HA     sing N N 352 
PHE   C     O      doub N N 353 
PHE   C     OXT    sing N N 354 
PHE   CB    CG     sing N N 355 
PHE   CB    HB2    sing N N 356 
PHE   CB    HB3    sing N N 357 
PHE   CG    CD1    doub Y N 358 
PHE   CG    CD2    sing Y N 359 
PHE   CD1   CE1    sing Y N 360 
PHE   CD1   HD1    sing N N 361 
PHE   CD2   CE2    doub Y N 362 
PHE   CD2   HD2    sing N N 363 
PHE   CE1   CZ     doub Y N 364 
PHE   CE1   HE1    sing N N 365 
PHE   CE2   CZ     sing Y N 366 
PHE   CE2   HE2    sing N N 367 
PHE   CZ    HZ     sing N N 368 
PHE   OXT   HXT    sing N N 369 
PRO   N     CA     sing N N 370 
PRO   N     CD     sing N N 371 
PRO   N     H      sing N N 372 
PRO   CA    C      sing N N 373 
PRO   CA    CB     sing N N 374 
PRO   CA    HA     sing N N 375 
PRO   C     O      doub N N 376 
PRO   C     OXT    sing N N 377 
PRO   CB    CG     sing N N 378 
PRO   CB    HB2    sing N N 379 
PRO   CB    HB3    sing N N 380 
PRO   CG    CD     sing N N 381 
PRO   CG    HG2    sing N N 382 
PRO   CG    HG3    sing N N 383 
PRO   CD    HD2    sing N N 384 
PRO   CD    HD3    sing N N 385 
PRO   OXT   HXT    sing N N 386 
SER   N     CA     sing N N 387 
SER   N     H      sing N N 388 
SER   N     H2     sing N N 389 
SER   CA    C      sing N N 390 
SER   CA    CB     sing N N 391 
SER   CA    HA     sing N N 392 
SER   C     O      doub N N 393 
SER   C     OXT    sing N N 394 
SER   CB    OG     sing N N 395 
SER   CB    HB2    sing N N 396 
SER   CB    HB3    sing N N 397 
SER   OG    HG     sing N N 398 
SER   OXT   HXT    sing N N 399 
THR   N     CA     sing N N 400 
THR   N     H      sing N N 401 
THR   N     H2     sing N N 402 
THR   CA    C      sing N N 403 
THR   CA    CB     sing N N 404 
THR   CA    HA     sing N N 405 
THR   C     O      doub N N 406 
THR   C     OXT    sing N N 407 
THR   CB    OG1    sing N N 408 
THR   CB    CG2    sing N N 409 
THR   CB    HB     sing N N 410 
THR   OG1   HG1    sing N N 411 
THR   CG2   HG21   sing N N 412 
THR   CG2   HG22   sing N N 413 
THR   CG2   HG23   sing N N 414 
THR   OXT   HXT    sing N N 415 
TRP   N     CA     sing N N 416 
TRP   N     H      sing N N 417 
TRP   N     H2     sing N N 418 
TRP   CA    C      sing N N 419 
TRP   CA    CB     sing N N 420 
TRP   CA    HA     sing N N 421 
TRP   C     O      doub N N 422 
TRP   C     OXT    sing N N 423 
TRP   CB    CG     sing N N 424 
TRP   CB    HB2    sing N N 425 
TRP   CB    HB3    sing N N 426 
TRP   CG    CD1    doub Y N 427 
TRP   CG    CD2    sing Y N 428 
TRP   CD1   NE1    sing Y N 429 
TRP   CD1   HD1    sing N N 430 
TRP   CD2   CE2    doub Y N 431 
TRP   CD2   CE3    sing Y N 432 
TRP   NE1   CE2    sing Y N 433 
TRP   NE1   HE1    sing N N 434 
TRP   CE2   CZ2    sing Y N 435 
TRP   CE3   CZ3    doub Y N 436 
TRP   CE3   HE3    sing N N 437 
TRP   CZ2   CH2    doub Y N 438 
TRP   CZ2   HZ2    sing N N 439 
TRP   CZ3   CH2    sing Y N 440 
TRP   CZ3   HZ3    sing N N 441 
TRP   CH2   HH2    sing N N 442 
TRP   OXT   HXT    sing N N 443 
TYR   N     CA     sing N N 444 
TYR   N     H      sing N N 445 
TYR   N     H2     sing N N 446 
TYR   CA    C      sing N N 447 
TYR   CA    CB     sing N N 448 
TYR   CA    HA     sing N N 449 
TYR   C     O      doub N N 450 
TYR   C     OXT    sing N N 451 
TYR   CB    CG     sing N N 452 
TYR   CB    HB2    sing N N 453 
TYR   CB    HB3    sing N N 454 
TYR   CG    CD1    doub Y N 455 
TYR   CG    CD2    sing Y N 456 
TYR   CD1   CE1    sing Y N 457 
TYR   CD1   HD1    sing N N 458 
TYR   CD2   CE2    doub Y N 459 
TYR   CD2   HD2    sing N N 460 
TYR   CE1   CZ     doub Y N 461 
TYR   CE1   HE1    sing N N 462 
TYR   CE2   CZ     sing Y N 463 
TYR   CE2   HE2    sing N N 464 
TYR   CZ    OH     sing N N 465 
TYR   OH    HH     sing N N 466 
TYR   OXT   HXT    sing N N 467 
VAL   N     CA     sing N N 468 
VAL   N     H      sing N N 469 
VAL   N     H2     sing N N 470 
VAL   CA    C      sing N N 471 
VAL   CA    CB     sing N N 472 
VAL   CA    HA     sing N N 473 
VAL   C     O      doub N N 474 
VAL   C     OXT    sing N N 475 
VAL   CB    CG1    sing N N 476 
VAL   CB    CG2    sing N N 477 
VAL   CB    HB     sing N N 478 
VAL   CG1   HG11   sing N N 479 
VAL   CG1   HG12   sing N N 480 
VAL   CG1   HG13   sing N N 481 
VAL   CG2   HG21   sing N N 482 
VAL   CG2   HG22   sing N N 483 
VAL   CG2   HG23   sing N N 484 
VAL   OXT   HXT    sing N N 485 
# 
_em_admin.current_status     REL 
_em_admin.deposition_date    2024-06-27 
_em_admin.deposition_site    RCSB 
_em_admin.entry_id           9CFP 
_em_admin.last_update        2025-04-23 
_em_admin.map_release_date   2025-04-23 
_em_admin.title              'Cryo-EM structure of S. aureus TarGH in complex with AMP-PNP and targocil-II' 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     'PHASE FLIPPING AND AMPLITUDE CORRECTION' 
# 
_em_entity_assembly_molwt.entity_assembly_id   1 
_em_entity_assembly_molwt.experimental_flag    NO 
_em_entity_assembly_molwt.id                   1 
_em_entity_assembly_molwt.units                ? 
_em_entity_assembly_molwt.value                ? 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          1280 
_em_entity_assembly_naturalsource.organism             'Staphylococcus aureus' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_entity_assembly_recombinant.cell                 ? 
_em_entity_assembly_recombinant.entity_assembly_id   1 
_em_entity_assembly_recombinant.id                   2 
_em_entity_assembly_recombinant.ncbi_tax_id          1358 
_em_entity_assembly_recombinant.organism             'Lactococcus lactis' 
_em_entity_assembly_recombinant.plasmid              ? 
_em_entity_assembly_recombinant.strain               ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         50 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'TFS FALCON 4i (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'MODEL REFINEMENT'              ? 1  ? ? ? PHENIX 1.20.1_4487: 
'IMAGE ACQUISITION'             ? 2  1 1 1 ?      ?            
'PARTICLE SELECTION'            ? 3  1 1 1 ?      ?            
'VOLUME SELECTION'              ? 4  1 1 1 ?      ?            
CLASSIFICATION                  ? 5  1 1 1 ?      ?            
MASKING                         ? 6  1 1 1 ?      ?            
RECONSTRUCTION                  ? 7  1 1 1 ?      ?            
'INITIAL EULER ASSIGNMENT'      ? 8  1 1 1 ?      ?            
'FINAL EULER ASSIGNMENT'        ? 9  1 1 1 ?      ?            
'CTF CORRECTION'                ? 10 1 1 1 ?      ?            
'LAYERLINE INDEXING'            ? 11 1 1 1 ?      ?            
'DIFFRACTION INDEXING'          ? 12 1 1 1 ?      ?            
'MODEL FITTING'                 ? 13 1 1 1 ?      ?            
'SERIES ALIGNMENT'              ? 14 1 1 1 ?      ?            
'MOLECULAR REPLACEMENT'         ? 15 1 1 1 ?      ?            
'LATTICE DISTORTION CORRECTION' ? 16 1 1 1 ?      ?            
'SYMMETRY DETERMINATION'        ? 17 1 1 1 ?      ?            
'CRYSTALLOGRAPHY MERGING'       ? 18 1 1 1 ?      ?            
OTHER                           ? 19 1 1 1 ?      ?            
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
_pdbx_audit_support.funding_organization   'Canadian Institutes of Health Research (CIHR)' 
_pdbx_audit_support.country                Canada 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_atom_sites.entry_id                    9CFP 
_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]   1.000000 
_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]   1.000000 
_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]   1.000000 
_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  
CL 
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     . MET   A 1 25  ? 178.869 130.740 121.332 1.00 101.97 ? 1   MET   A N     1 
ATOM   2    C  CA    . MET   A 1 25  ? 179.924 131.722 121.556 1.00 104.66 ? 1   MET   A CA    1 
ATOM   3    C  C     . MET   A 1 25  ? 179.989 132.719 120.406 1.00 102.93 ? 1   MET   A C     1 
ATOM   4    O  O     . MET   A 1 25  ? 180.320 133.888 120.603 1.00 100.90 ? 1   MET   A O     1 
ATOM   5    C  CB    . MET   A 1 25  ? 181.276 131.027 121.733 1.00 105.47 ? 1   MET   A CB    1 
ATOM   6    C  CG    . MET   A 1 25  ? 181.209 129.742 122.541 1.00 105.07 ? 1   MET   A CG    1 
ATOM   7    S  SD    . MET   A 1 25  ? 181.757 129.961 124.244 1.00 103.73 ? 1   MET   A SD    1 
ATOM   8    C  CE    . MET   A 1 25  ? 181.806 128.261 124.804 1.00 101.50 ? 1   MET   A CE    1 
ATOM   9    N  N     . SER   A 1 26  ? 179.677 132.247 119.198 1.00 105.23 ? 2   SER   A N     1 
ATOM   10   C  CA    . SER   A 1 26  ? 179.628 133.137 118.044 1.00 105.82 ? 2   SER   A CA    1 
ATOM   11   C  C     . SER   A 1 26  ? 178.387 134.018 118.061 1.00 106.45 ? 2   SER   A C     1 
ATOM   12   O  O     . SER   A 1 26  ? 178.422 135.141 117.544 1.00 107.20 ? 2   SER   A O     1 
ATOM   13   C  CB    . SER   A 1 26  ? 179.675 132.324 116.750 1.00 106.08 ? 2   SER   A CB    1 
ATOM   14   O  OG    . SER   A 1 26  ? 180.499 131.181 116.895 1.00 108.53 ? 2   SER   A OG    1 
ATOM   15   N  N     . ALA   A 1 27  ? 177.290 133.529 118.644 1.00 92.17  ? 3   ALA   A N     1 
ATOM   16   C  CA    . ALA   A 1 27  ? 176.063 134.314 118.711 1.00 90.22  ? 3   ALA   A CA    1 
ATOM   17   C  C     . ALA   A 1 27  ? 176.249 135.568 119.556 1.00 90.52  ? 3   ALA   A C     1 
ATOM   18   O  O     . ALA   A 1 27  ? 175.780 136.651 119.183 1.00 89.96  ? 3   ALA   A O     1 
ATOM   19   C  CB    . ALA   A 1 27  ? 174.928 133.456 119.265 1.00 91.60  ? 3   ALA   A CB    1 
ATOM   20   N  N     . ILE   A 1 28  ? 176.925 135.439 120.699 1.00 80.75  ? 4   ILE   A N     1 
ATOM   21   C  CA    . ILE   A 1 28  ? 177.142 136.587 121.574 1.00 80.27  ? 4   ILE   A CA    1 
ATOM   22   C  C     . ILE   A 1 28  ? 177.977 137.645 120.866 1.00 79.39  ? 4   ILE   A C     1 
ATOM   23   O  O     . ILE   A 1 28  ? 177.648 138.837 120.886 1.00 80.39  ? 4   ILE   A O     1 
ATOM   24   C  CB    . ILE   A 1 28  ? 177.799 136.137 122.891 1.00 80.90  ? 4   ILE   A CB    1 
ATOM   25   C  CG1   . ILE   A 1 28  ? 176.859 135.212 123.666 1.00 78.66  ? 4   ILE   A CG1   1 
ATOM   26   C  CG2   . ILE   A 1 28  ? 178.191 137.342 123.731 1.00 81.96  ? 4   ILE   A CG2   1 
ATOM   27   C  CD1   . ILE   A 1 28  ? 177.265 134.994 125.103 1.00 79.67  ? 4   ILE   A CD1   1 
ATOM   28   N  N     . GLY   A 1 29  ? 179.068 137.223 120.224 1.00 78.59  ? 5   GLY   A N     1 
ATOM   29   C  CA    . GLY   A 1 29  ? 179.896 138.169 119.496 1.00 77.14  ? 5   GLY   A CA    1 
ATOM   30   C  C     . GLY   A 1 29  ? 179.158 138.821 118.344 1.00 79.57  ? 5   GLY   A C     1 
ATOM   31   O  O     . GLY   A 1 29  ? 179.305 140.022 118.103 1.00 81.53  ? 5   GLY   A O     1 
ATOM   32   N  N     . THR   A 1 30  ? 178.346 138.043 117.624 1.00 83.80  ? 6   THR   A N     1 
ATOM   33   C  CA    . THR   A 1 30  ? 177.582 138.596 116.510 1.00 85.99  ? 6   THR   A CA    1 
ATOM   34   C  C     . THR   A 1 30  ? 176.595 139.653 116.991 1.00 85.88  ? 6   THR   A C     1 
ATOM   35   O  O     . THR   A 1 30  ? 176.510 140.744 116.415 1.00 83.67  ? 6   THR   A O     1 
ATOM   36   C  CB    . THR   A 1 30  ? 176.851 137.477 115.770 1.00 87.00  ? 6   THR   A CB    1 
ATOM   37   O  OG1   . THR   A 1 30  ? 177.727 136.353 115.615 1.00 87.64  ? 6   THR   A OG1   1 
ATOM   38   C  CG2   . THR   A 1 30  ? 176.402 137.952 114.399 1.00 84.83  ? 6   THR   A CG2   1 
ATOM   39   N  N     . VAL   A 1 31  ? 175.847 139.351 118.056 1.00 78.20  ? 7   VAL   A N     1 
ATOM   40   C  CA    . VAL   A 1 31  ? 174.870 140.306 118.573 1.00 77.42  ? 7   VAL   A CA    1 
ATOM   41   C  C     . VAL   A 1 31  ? 175.566 141.553 119.107 1.00 77.51  ? 7   VAL   A C     1 
ATOM   42   O  O     . VAL   A 1 31  ? 175.104 142.681 118.888 1.00 73.42  ? 7   VAL   A O     1 
ATOM   43   C  CB    . VAL   A 1 31  ? 173.989 139.639 119.644 1.00 74.31  ? 7   VAL   A CB    1 
ATOM   44   C  CG1   . VAL   A 1 31  ? 173.130 140.675 120.350 1.00 75.56  ? 7   VAL   A CG1   1 
ATOM   45   C  CG2   . VAL   A 1 31  ? 173.116 138.566 119.016 1.00 72.17  ? 7   VAL   A CG2   1 
ATOM   46   N  N     . PHE   A 1 32  ? 176.689 141.374 119.810 1.00 82.82  ? 8   PHE   A N     1 
ATOM   47   C  CA    . PHE   A 1 32  ? 177.424 142.523 120.328 1.00 79.71  ? 8   PHE   A CA    1 
ATOM   48   C  C     . PHE   A 1 32  ? 177.933 143.408 119.197 1.00 81.38  ? 8   PHE   A C     1 
ATOM   49   O  O     . PHE   A 1 32  ? 177.852 144.638 119.280 1.00 85.27  ? 8   PHE   A O     1 
ATOM   50   C  CB    . PHE   A 1 32  ? 178.582 142.049 121.205 1.00 79.08  ? 8   PHE   A CB    1 
ATOM   51   C  CG    . PHE   A 1 32  ? 179.315 143.163 121.895 1.00 83.61  ? 8   PHE   A CG    1 
ATOM   52   C  CD1   . PHE   A 1 32  ? 178.772 143.780 123.009 1.00 83.92  ? 8   PHE   A CD1   1 
ATOM   53   C  CD2   . PHE   A 1 32  ? 180.545 143.594 121.430 1.00 85.35  ? 8   PHE   A CD2   1 
ATOM   54   C  CE1   . PHE   A 1 32  ? 179.443 144.805 123.645 1.00 83.63  ? 8   PHE   A CE1   1 
ATOM   55   C  CE2   . PHE   A 1 32  ? 181.220 144.619 122.062 1.00 84.15  ? 8   PHE   A CE2   1 
ATOM   56   C  CZ    . PHE   A 1 32  ? 180.667 145.225 123.172 1.00 82.85  ? 8   PHE   A CZ    1 
ATOM   57   N  N     . LYS   A 1 33  ? 178.459 142.801 118.130 1.00 94.33  ? 9   LYS   A N     1 
ATOM   58   C  CA    . LYS   A 1 33  ? 178.932 143.583 116.992 1.00 94.42  ? 9   LYS   A CA    1 
ATOM   59   C  C     . LYS   A 1 33  ? 177.785 144.320 116.311 1.00 96.79  ? 9   LYS   A C     1 
ATOM   60   O  O     . LYS   A 1 33  ? 177.928 145.492 115.936 1.00 100.61 ? 9   LYS   A O     1 
ATOM   61   C  CB    . LYS   A 1 33  ? 179.655 142.674 116.000 1.00 97.44  ? 9   LYS   A CB    1 
ATOM   62   C  CG    . LYS   A 1 33  ? 181.100 142.384 116.371 1.00 100.07 ? 9   LYS   A CG    1 
ATOM   63   C  CD    . LYS   A 1 33  ? 181.694 141.297 115.491 1.00 99.02  ? 9   LYS   A CD    1 
ATOM   64   C  CE    . LYS   A 1 33  ? 182.493 140.299 116.314 1.00 99.11  ? 9   LYS   A CE    1 
ATOM   65   N  NZ    . LYS   A 1 33  ? 182.638 138.991 115.617 1.00 100.33 ? 9   LYS   A NZ    1 
ATOM   66   N  N     . GLU   A 1 34  ? 176.638 143.654 116.150 1.00 86.43  ? 10  GLU   A N     1 
ATOM   67   C  CA    . GLU   A 1 34  ? 175.482 144.300 115.534 1.00 84.77  ? 10  GLU   A CA    1 
ATOM   68   C  C     . GLU   A 1 34  ? 175.023 145.499 116.351 1.00 87.03  ? 10  GLU   A C     1 
ATOM   69   O  O     . GLU   A 1 34  ? 174.679 146.549 115.796 1.00 86.34  ? 10  GLU   A O     1 
ATOM   70   C  CB    . GLU   A 1 34  ? 174.340 143.296 115.371 1.00 85.78  ? 10  GLU   A CB    1 
ATOM   71   C  CG    . GLU   A 1 34  ? 174.631 142.157 114.413 1.00 88.64  ? 10  GLU   A CG    1 
ATOM   72   C  CD    . GLU   A 1 34  ? 173.514 141.134 114.371 1.00 91.89  ? 10  GLU   A CD    1 
ATOM   73   O  OE1   . GLU   A 1 34  ? 173.815 139.923 114.381 1.00 92.26  ? 10  GLU   A OE1   1 
ATOM   74   O  OE2   . GLU   A 1 34  ? 172.334 141.537 114.341 1.00 91.88  ? 10  GLU   A OE2   1 
ATOM   75   N  N     . HIS   A 1 35  ? 175.001 145.360 117.678 1.00 82.20  ? 11  HIS   A N     1 
ATOM   76   C  CA    . HIS   A 1 35  ? 174.555 146.467 118.519 1.00 76.80  ? 11  HIS   A CA    1 
ATOM   77   C  C     . HIS   A 1 35  ? 175.574 147.601 118.543 1.00 74.07  ? 11  HIS   A C     1 
ATOM   78   O  O     . HIS   A 1 35  ? 175.196 148.778 118.544 1.00 75.16  ? 11  HIS   A O     1 
ATOM   79   C  CB    . HIS   A 1 35  ? 174.261 145.971 119.933 1.00 74.41  ? 11  HIS   A CB    1 
ATOM   80   C  CG    . HIS   A 1 35  ? 172.883 145.413 120.097 1.00 77.20  ? 11  HIS   A CG    1 
ATOM   81   N  ND1   . HIS   A 1 35  ? 172.595 144.076 119.933 1.00 73.88  ? 11  HIS   A ND1   1 
ATOM   82   C  CD2   . HIS   A 1 35  ? 171.709 146.016 120.397 1.00 75.95  ? 11  HIS   A CD2   1 
ATOM   83   C  CE1   . HIS   A 1 35  ? 171.305 143.877 120.133 1.00 72.67  ? 11  HIS   A CE1   1 
ATOM   84   N  NE2   . HIS   A 1 35  ? 170.744 145.039 120.415 1.00 71.63  ? 11  HIS   A NE2   1 
ATOM   85   N  N     . VAL   A 1 36  ? 176.867 147.272 118.564 1.00 71.90  ? 12  VAL   A N     1 
ATOM   86   C  CA    . VAL   A 1 36  ? 177.893 148.309 118.602 1.00 71.29  ? 12  VAL   A CA    1 
ATOM   87   C  C     . VAL   A 1 36  ? 177.913 149.096 117.297 1.00 76.38  ? 12  VAL   A C     1 
ATOM   88   O  O     . VAL   A 1 36  ? 178.075 150.323 117.299 1.00 81.87  ? 12  VAL   A O     1 
ATOM   89   C  CB    . VAL   A 1 36  ? 179.266 147.684 118.915 1.00 77.57  ? 12  VAL   A CB    1 
ATOM   90   C  CG1   . VAL   A 1 36  ? 180.392 148.616 118.499 1.00 76.86  ? 12  VAL   A CG1   1 
ATOM   91   C  CG2   . VAL   A 1 36  ? 179.368 147.355 120.395 1.00 78.38  ? 12  VAL   A CG2   1 
ATOM   92   N  N     . LYS   A 1 37  ? 177.738 148.412 116.164 1.00 82.63  ? 13  LYS   A N     1 
ATOM   93   C  CA    . LYS   A 1 37  ? 177.830 149.091 114.875 1.00 80.98  ? 13  LYS   A CA    1 
ATOM   94   C  C     . LYS   A 1 37  ? 176.672 150.058 114.643 1.00 84.20  ? 13  LYS   A C     1 
ATOM   95   O  O     . LYS   A 1 37  ? 176.854 151.085 113.980 1.00 83.42  ? 13  LYS   A O     1 
ATOM   96   C  CB    . LYS   A 1 37  ? 177.893 148.062 113.745 1.00 80.37  ? 13  LYS   A CB    1 
ATOM   97   C  CG    . LYS   A 1 37  ? 179.294 147.545 113.446 1.00 85.69  ? 13  LYS   A CG    1 
ATOM   98   C  CD    . LYS   A 1 37  ? 180.349 148.616 113.675 1.00 86.13  ? 13  LYS   A CD    1 
ATOM   99   C  CE    . LYS   A 1 37  ? 181.558 148.406 112.779 1.00 86.09  ? 13  LYS   A CE    1 
ATOM   100  N  NZ    . LYS   A 1 37  ? 182.778 149.058 113.329 1.00 83.95  ? 13  LYS   A NZ    1 
ATOM   101  N  N     . ASN   A 1 38  ? 175.485 149.758 115.174 1.00 85.09  ? 14  ASN   A N     1 
ATOM   102  C  CA    . ASN   A 1 38  ? 174.271 150.507 114.866 1.00 80.29  ? 14  ASN   A CA    1 
ATOM   103  C  C     . ASN   A 1 38  ? 173.760 151.319 116.055 1.00 82.96  ? 14  ASN   A C     1 
ATOM   104  O  O     . ASN   A 1 38  ? 172.552 151.389 116.289 1.00 87.19  ? 14  ASN   A O     1 
ATOM   105  C  CB    . ASN   A 1 38  ? 173.182 149.559 114.369 1.00 79.92  ? 14  ASN   A CB    1 
ATOM   106  C  CG    . ASN   A 1 38  ? 173.492 148.986 113.004 1.00 83.84  ? 14  ASN   A CG    1 
ATOM   107  O  OD1   . ASN   A 1 38  ? 174.608 149.114 112.504 1.00 87.19  ? 14  ASN   A OD1   1 
ATOM   108  N  ND2   . ASN   A 1 38  ? 172.502 148.351 112.391 1.00 85.11  ? 14  ASN   A ND2   1 
ATOM   109  N  N     . PHE   A 1 39  ? 174.668 151.936 116.813 1.00 88.25  ? 15  PHE   A N     1 
ATOM   110  C  CA    . PHE   A 1 39  ? 174.269 152.700 117.993 1.00 88.65  ? 15  PHE   A CA    1 
ATOM   111  C  C     . PHE   A 1 39  ? 173.462 153.941 117.613 1.00 91.24  ? 15  PHE   A C     1 
ATOM   112  O  O     . PHE   A 1 39  ? 172.367 154.179 118.142 1.00 94.36  ? 15  PHE   A O     1 
ATOM   113  C  CB    . PHE   A 1 39  ? 175.521 153.079 118.789 1.00 88.80  ? 15  PHE   A CB    1 
ATOM   114  C  CG    . PHE   A 1 39  ? 175.265 154.021 119.928 1.00 95.43  ? 15  PHE   A CG    1 
ATOM   115  C  CD1   . PHE   A 1 39  ? 174.569 153.605 121.049 1.00 95.40  ? 15  PHE   A CD1   1 
ATOM   116  C  CD2   . PHE   A 1 39  ? 175.744 155.319 119.887 1.00 95.23  ? 15  PHE   A CD2   1 
ATOM   117  C  CE1   . PHE   A 1 39  ? 174.343 154.470 122.101 1.00 92.15  ? 15  PHE   A CE1   1 
ATOM   118  C  CE2   . PHE   A 1 39  ? 175.521 156.188 120.936 1.00 93.20  ? 15  PHE   A CE2   1 
ATOM   119  C  CZ    . PHE   A 1 39  ? 174.819 155.763 122.044 1.00 92.26  ? 15  PHE   A CZ    1 
ATOM   120  N  N     . TYR   A 1 40  ? 173.986 154.737 116.677 1.00 95.09  ? 16  TYR   A N     1 
ATOM   121  C  CA    . TYR   A 1 40  ? 173.309 155.970 116.286 1.00 95.45  ? 16  TYR   A CA    1 
ATOM   122  C  C     . TYR   A 1 40  ? 172.003 155.677 115.559 1.00 93.04  ? 16  TYR   A C     1 
ATOM   123  O  O     . TYR   A 1 40  ? 171.022 156.415 115.711 1.00 95.94  ? 16  TYR   A O     1 
ATOM   124  C  CB    . TYR   A 1 40  ? 174.232 156.821 115.415 1.00 94.96  ? 16  TYR   A CB    1 
ATOM   125  C  CG    . TYR   A 1 40  ? 175.469 157.310 116.135 1.00 99.73  ? 16  TYR   A CG    1 
ATOM   126  C  CD1   . TYR   A 1 40  ? 175.479 158.537 116.783 1.00 100.96 ? 16  TYR   A CD1   1 
ATOM   127  C  CD2   . TYR   A 1 40  ? 176.627 156.544 116.166 1.00 99.26  ? 16  TYR   A CD2   1 
ATOM   128  C  CE1   . TYR   A 1 40  ? 176.607 158.988 117.441 1.00 100.16 ? 16  TYR   A CE1   1 
ATOM   129  C  CE2   . TYR   A 1 40  ? 177.759 156.986 116.821 1.00 98.28  ? 16  TYR   A CE2   1 
ATOM   130  C  CZ    . TYR   A 1 40  ? 177.744 158.208 117.458 1.00 99.51  ? 16  TYR   A CZ    1 
ATOM   131  O  OH    . TYR   A 1 40  ? 178.868 158.654 118.113 1.00 99.62  ? 16  TYR   A OH    1 
ATOM   132  N  N     . LEU   A 1 41  ? 171.973 154.609 114.760 1.00 67.38  ? 17  LEU   A N     1 
ATOM   133  C  CA    . LEU   A 1 41  ? 170.728 154.205 114.118 1.00 68.52  ? 17  LEU   A CA    1 
ATOM   134  C  C     . LEU   A 1 41  ? 169.676 153.836 115.155 1.00 74.00  ? 17  LEU   A C     1 
ATOM   135  O  O     . LEU   A 1 41  ? 168.500 154.191 115.012 1.00 75.54  ? 17  LEU   A O     1 
ATOM   136  C  CB    . LEU   A 1 41  ? 170.983 153.034 113.169 1.00 68.05  ? 17  LEU   A CB    1 
ATOM   137  C  CG    . LEU   A 1 41  ? 169.785 152.551 112.351 1.00 70.83  ? 17  LEU   A CG    1 
ATOM   138  C  CD1   . LEU   A 1 41  ? 169.610 153.406 111.110 1.00 74.32  ? 17  LEU   A CD1   1 
ATOM   139  C  CD2   . LEU   A 1 41  ? 169.939 151.086 111.979 1.00 69.86  ? 17  LEU   A CD2   1 
ATOM   140  N  N     . ILE   A 1 42  ? 170.083 153.126 116.210 1.00 77.43  ? 18  ILE   A N     1 
ATOM   141  C  CA    . ILE   A 1 42  ? 169.159 152.776 117.285 1.00 71.56  ? 18  ILE   A CA    1 
ATOM   142  C  C     . ILE   A 1 42  ? 168.616 154.037 117.945 1.00 75.00  ? 18  ILE   A C     1 
ATOM   143  O  O     . ILE   A 1 42  ? 167.409 154.162 118.193 1.00 80.43  ? 18  ILE   A O     1 
ATOM   144  C  CB    . ILE   A 1 42  ? 169.853 151.857 118.308 1.00 67.54  ? 18  ILE   A CB    1 
ATOM   145  C  CG1   . ILE   A 1 42  ? 169.844 150.407 117.823 1.00 71.54  ? 18  ILE   A CG1   1 
ATOM   146  C  CG2   . ILE   A 1 42  ? 169.192 151.968 119.672 1.00 74.63  ? 18  ILE   A CG2   1 
ATOM   147  C  CD1   . ILE   A 1 42  ? 170.890 149.542 118.484 1.00 71.47  ? 18  ILE   A CD1   1 
ATOM   148  N  N     . GLN   A 1 43  ? 169.502 154.997 118.229 1.00 72.87  ? 19  GLN   A N     1 
ATOM   149  C  CA    . GLN   A 1 43  ? 169.059 156.237 118.862 1.00 72.53  ? 19  GLN   A CA    1 
ATOM   150  C  C     . GLN   A 1 43  ? 168.062 156.986 117.983 1.00 74.49  ? 19  GLN   A C     1 
ATOM   151  O  O     . GLN   A 1 43  ? 167.021 157.451 118.466 1.00 78.60  ? 19  GLN   A O     1 
ATOM   152  C  CB    . GLN   A 1 43  ? 170.263 157.122 119.177 1.00 73.45  ? 19  GLN   A CB    1 
ATOM   153  C  CG    . GLN   A 1 43  ? 171.087 156.651 120.362 1.00 75.91  ? 19  GLN   A CG    1 
ATOM   154  C  CD    . GLN   A 1 43  ? 172.058 157.706 120.846 1.00 78.15  ? 19  GLN   A CD    1 
ATOM   155  O  OE1   . GLN   A 1 43  ? 172.721 158.369 120.049 1.00 76.15  ? 19  GLN   A OE1   1 
ATOM   156  N  NE2   . GLN   A 1 43  ? 172.148 157.870 122.160 1.00 78.12  ? 19  GLN   A NE2   1 
ATOM   157  N  N     . ARG   A 1 44  ? 168.360 157.104 116.686 1.00 74.52  ? 20  ARG   A N     1 
ATOM   158  C  CA    . ARG   A 1 44  ? 167.475 157.838 115.786 1.00 70.93  ? 20  ARG   A CA    1 
ATOM   159  C  C     . ARG   A 1 44  ? 166.129 157.140 115.631 1.00 67.97  ? 20  ARG   A C     1 
ATOM   160  O  O     . ARG   A 1 44  ? 165.081 157.797 115.605 1.00 72.28  ? 20  ARG   A O     1 
ATOM   161  C  CB    . ARG   A 1 44  ? 168.147 158.022 114.427 1.00 69.97  ? 20  ARG   A CB    1 
ATOM   162  C  CG    . ARG   A 1 44  ? 168.958 159.300 114.309 1.00 72.92  ? 20  ARG   A CG    1 
ATOM   163  C  CD    . ARG   A 1 44  ? 169.831 159.286 113.066 1.00 77.16  ? 20  ARG   A CD    1 
ATOM   164  N  NE    . ARG   A 1 44  ? 171.200 159.696 113.351 1.00 75.53  ? 20  ARG   A NE    1 
ATOM   165  C  CZ    . ARG   A 1 44  ? 172.275 159.150 112.798 1.00 75.54  ? 20  ARG   A CZ    1 
ATOM   166  N  NH1   . ARG   A 1 44  ? 172.176 158.162 111.925 1.00 73.30  ? 20  ARG   A NH1   1 
ATOM   167  N  NH2   . ARG   A 1 44  ? 173.479 159.605 113.132 1.00 75.57  ? 20  ARG   A NH2   1 
ATOM   168  N  N     . LEU   A 1 45  ? 166.134 155.809 115.524 1.00 60.18  ? 21  LEU   A N     1 
ATOM   169  C  CA    . LEU   A 1 45  ? 164.877 155.080 115.412 1.00 63.31  ? 21  LEU   A CA    1 
ATOM   170  C  C     . LEU   A 1 45  ? 164.039 155.209 116.678 1.00 69.35  ? 21  LEU   A C     1 
ATOM   171  O  O     . LEU   A 1 45  ? 162.811 155.325 116.595 1.00 70.21  ? 21  LEU   A O     1 
ATOM   172  C  CB    . LEU   A 1 45  ? 165.149 153.611 115.090 1.00 75.08  ? 21  LEU   A CB    1 
ATOM   173  C  CG    . LEU   A 1 45  ? 165.657 153.331 113.673 1.00 71.20  ? 21  LEU   A CG    1 
ATOM   174  C  CD1   . LEU   A 1 45  ? 166.063 151.875 113.520 1.00 65.57  ? 21  LEU   A CD1   1 
ATOM   175  C  CD2   . LEU   A 1 45  ? 164.611 153.709 112.638 1.00 70.30  ? 21  LEU   A CD2   1 
ATOM   176  N  N     . ALA   A 1 46  ? 164.676 155.196 117.853 1.00 78.20  ? 22  ALA   A N     1 
ATOM   177  C  CA    . ALA   A 1 46  ? 163.936 155.426 119.091 1.00 71.71  ? 22  ALA   A CA    1 
ATOM   178  C  C     . ALA   A 1 46  ? 163.332 156.825 119.125 1.00 75.65  ? 22  ALA   A C     1 
ATOM   179  O  O     . ALA   A 1 46  ? 162.172 157.001 119.528 1.00 79.33  ? 22  ALA   A O     1 
ATOM   180  C  CB    . ALA   A 1 46  ? 164.850 155.208 120.295 1.00 65.29  ? 22  ALA   A CB    1 
ATOM   181  N  N     . GLN   A 1 47  ? 164.104 157.833 118.707 1.00 70.16  ? 23  GLN   A N     1 
ATOM   182  C  CA    . GLN   A 1 47  ? 163.582 159.196 118.669 1.00 68.28  ? 23  GLN   A CA    1 
ATOM   183  C  C     . GLN   A 1 47  ? 162.404 159.318 117.713 1.00 68.92  ? 23  GLN   A C     1 
ATOM   184  O  O     . GLN   A 1 47  ? 161.455 160.060 117.988 1.00 71.26  ? 23  GLN   A O     1 
ATOM   185  C  CB    . GLN   A 1 47  ? 164.685 160.175 118.271 1.00 65.55  ? 23  GLN   A CB    1 
ATOM   186  C  CG    . GLN   A 1 47  ? 165.802 160.301 119.289 1.00 72.02  ? 23  GLN   A CG    1 
ATOM   187  C  CD    . GLN   A 1 47  ? 166.541 161.617 119.180 1.00 72.33  ? 23  GLN   A CD    1 
ATOM   188  O  OE1   . GLN   A 1 47  ? 167.770 161.651 119.164 1.00 73.37  ? 23  GLN   A OE1   1 
ATOM   189  N  NE2   . GLN   A 1 47  ? 165.793 162.710 119.104 1.00 72.39  ? 23  GLN   A NE2   1 
ATOM   190  N  N     . PHE   A 1 48  ? 162.448 158.607 116.585 1.00 74.85  ? 24  PHE   A N     1 
ATOM   191  C  CA    . PHE   A 1 48  ? 161.328 158.639 115.649 1.00 74.97  ? 24  PHE   A CA    1 
ATOM   192  C  C     . PHE   A 1 48  ? 160.107 157.913 116.203 1.00 72.45  ? 24  PHE   A C     1 
ATOM   193  O  O     . PHE   A 1 48  ? 158.973 158.364 116.010 1.00 75.53  ? 24  PHE   A O     1 
ATOM   194  C  CB    . PHE   A 1 48  ? 161.739 158.033 114.308 1.00 81.08  ? 24  PHE   A CB    1 
ATOM   195  C  CG    . PHE   A 1 48  ? 161.178 158.760 113.125 1.00 77.48  ? 24  PHE   A CG    1 
ATOM   196  C  CD1   . PHE   A 1 48  ? 159.902 158.481 112.669 1.00 78.24  ? 24  PHE   A CD1   1 
ATOM   197  C  CD2   . PHE   A 1 48  ? 161.921 159.726 112.473 1.00 77.28  ? 24  PHE   A CD2   1 
ATOM   198  C  CE1   . PHE   A 1 48  ? 159.380 159.151 111.585 1.00 79.77  ? 24  PHE   A CE1   1 
ATOM   199  C  CE2   . PHE   A 1 48  ? 161.403 160.398 111.387 1.00 81.50  ? 24  PHE   A CE2   1 
ATOM   200  C  CZ    . PHE   A 1 48  ? 160.131 160.111 110.942 1.00 80.46  ? 24  PHE   A CZ    1 
ATOM   201  N  N     . GLN   A 1 49  ? 160.316 156.784 116.884 1.00 78.85  ? 25  GLN   A N     1 
ATOM   202  C  CA    . GLN   A 1 49  ? 159.195 156.056 117.469 1.00 79.17  ? 25  GLN   A CA    1 
ATOM   203  C  C     . GLN   A 1 49  ? 158.508 156.868 118.560 1.00 77.42  ? 25  GLN   A C     1 
ATOM   204  O  O     . GLN   A 1 49  ? 157.279 156.802 118.702 1.00 73.18  ? 25  GLN   A O     1 
ATOM   205  C  CB    . GLN   A 1 49  ? 159.671 154.715 118.023 1.00 74.97  ? 25  GLN   A CB    1 
ATOM   206  C  CG    . GLN   A 1 49  ? 158.607 153.941 118.776 1.00 74.49  ? 25  GLN   A CG    1 
ATOM   207  C  CD    . GLN   A 1 49  ? 158.327 152.593 118.154 1.00 81.85  ? 25  GLN   A CD    1 
ATOM   208  O  OE1   . GLN   A 1 49  ? 159.245 151.816 117.896 1.00 85.96  ? 25  GLN   A OE1   1 
ATOM   209  N  NE2   . GLN   A 1 49  ? 157.055 152.307 117.905 1.00 80.50  ? 25  GLN   A NE2   1 
ATOM   210  N  N     . VAL   A 1 50  ? 159.282 157.633 119.336 1.00 82.57  ? 26  VAL   A N     1 
ATOM   211  C  CA    . VAL   A 1 50  ? 158.687 158.490 120.358 1.00 82.85  ? 26  VAL   A CA    1 
ATOM   212  C  C     . VAL   A 1 50  ? 157.694 159.459 119.726 1.00 90.65  ? 26  VAL   A C     1 
ATOM   213  O  O     . VAL   A 1 50  ? 156.582 159.653 120.234 1.00 88.56  ? 26  VAL   A O     1 
ATOM   214  C  CB    . VAL   A 1 50  ? 159.787 159.232 121.141 1.00 81.68  ? 26  VAL   A CB    1 
ATOM   215  C  CG1   . VAL   A 1 50  ? 159.264 160.547 121.696 1.00 83.22  ? 26  VAL   A CG1   1 
ATOM   216  C  CG2   . VAL   A 1 50  ? 160.323 158.356 122.257 1.00 83.69  ? 26  VAL   A CG2   1 
ATOM   217  N  N     . LYS   A 1 51  ? 158.073 160.074 118.602 1.00 100.16 ? 27  LYS   A N     1 
ATOM   218  C  CA    . LYS   A 1 51  ? 157.158 160.966 117.897 1.00 94.80  ? 27  LYS   A CA    1 
ATOM   219  C  C     . LYS   A 1 51  ? 155.991 160.207 117.278 1.00 90.89  ? 27  LYS   A C     1 
ATOM   220  O  O     . LYS   A 1 51  ? 154.871 160.727 117.232 1.00 91.13  ? 27  LYS   A O     1 
ATOM   221  C  CB    . LYS   A 1 51  ? 157.906 161.739 116.811 1.00 91.06  ? 27  LYS   A CB    1 
ATOM   222  C  CG    . LYS   A 1 51  ? 158.841 162.816 117.330 1.00 93.32  ? 27  LYS   A CG    1 
ATOM   223  C  CD    . LYS   A 1 51  ? 159.290 163.730 116.201 1.00 95.60  ? 27  LYS   A CD    1 
ATOM   224  C  CE    . LYS   A 1 51  ? 160.799 163.904 116.193 1.00 96.68  ? 27  LYS   A CE    1 
ATOM   225  N  NZ    . LYS   A 1 51  ? 161.376 163.655 114.843 1.00 95.48  ? 27  LYS   A NZ    1 
ATOM   226  N  N     . ILE   A 1 52  ? 156.236 158.991 116.786 1.00 85.30  ? 28  ILE   A N     1 
ATOM   227  C  CA    . ILE   A 1 52  ? 155.179 158.229 116.128 1.00 83.25  ? 28  ILE   A CA    1 
ATOM   228  C  C     . ILE   A 1 52  ? 154.066 157.884 117.112 1.00 85.09  ? 28  ILE   A C     1 
ATOM   229  O  O     . ILE   A 1 52  ? 152.879 158.032 116.800 1.00 84.18  ? 28  ILE   A O     1 
ATOM   230  C  CB    . ILE   A 1 52  ? 155.762 156.968 115.464 1.00 84.96  ? 28  ILE   A CB    1 
ATOM   231  C  CG1   . ILE   A 1 52  ? 156.251 157.287 114.051 1.00 84.94  ? 28  ILE   A CG1   1 
ATOM   232  C  CG2   . ILE   A 1 52  ? 154.729 155.850 115.419 1.00 81.37  ? 28  ILE   A CG2   1 
ATOM   233  C  CD1   . ILE   A 1 52  ? 156.702 156.069 113.273 1.00 87.88  ? 28  ILE   A CD1   1 
ATOM   234  N  N     . ILE   A 1 53  ? 154.425 157.428 118.317 1.00 90.73  ? 29  ILE   A N     1 
ATOM   235  C  CA    . ILE   A 1 53  ? 153.402 156.994 119.270 1.00 90.29  ? 29  ILE   A CA    1 
ATOM   236  C  C     . ILE   A 1 53  ? 152.638 158.147 119.900 1.00 90.74  ? 29  ILE   A C     1 
ATOM   237  O  O     . ILE   A 1 53  ? 151.589 157.916 120.514 1.00 89.41  ? 29  ILE   A O     1 
ATOM   238  C  CB    . ILE   A 1 53  ? 154.003 156.131 120.396 1.00 86.94  ? 29  ILE   A CB    1 
ATOM   239  C  CG1   . ILE   A 1 53  ? 154.935 156.964 121.277 1.00 85.40  ? 29  ILE   A CG1   1 
ATOM   240  C  CG2   . ILE   A 1 53  ? 154.735 154.931 119.816 1.00 89.86  ? 29  ILE   A CG2   1 
ATOM   241  C  CD1   . ILE   A 1 53  ? 155.536 156.188 122.428 1.00 87.36  ? 29  ILE   A CD1   1 
ATOM   242  N  N     . ASN   A 1 54  ? 153.122 159.379 119.762 1.00 97.05  ? 30  ASN   A N     1 
ATOM   243  C  CA    . ASN   A 1 54  ? 152.472 160.564 120.314 1.00 95.30  ? 30  ASN   A CA    1 
ATOM   244  C  C     . ASN   A 1 54  ? 152.022 161.508 119.203 1.00 94.68  ? 30  ASN   A C     1 
ATOM   245  O  O     . ASN   A 1 54  ? 152.223 162.722 119.275 1.00 94.50  ? 30  ASN   A O     1 
ATOM   246  C  CB    . ASN   A 1 54  ? 153.400 161.287 121.285 1.00 97.04  ? 30  ASN   A CB    1 
ATOM   247  C  CG    . ASN   A 1 54  ? 153.384 160.676 122.671 1.00 96.87  ? 30  ASN   A CG    1 
ATOM   248  O  OD1   . ASN   A 1 54  ? 153.395 159.456 122.824 1.00 99.77  ? 30  ASN   A OD1   1 
ATOM   249  N  ND2   . ASN   A 1 54  ? 153.358 161.525 123.691 1.00 93.75  ? 30  ASN   A ND2   1 
ATOM   250  N  N     . HIS   A 1 55  ? 151.406 160.954 118.159 1.00 111.00 ? 31  HIS   A N     1 
ATOM   251  C  CA    . HIS   A 1 55  ? 151.118 161.726 116.954 1.00 113.03 ? 31  HIS   A CA    1 
ATOM   252  C  C     . HIS   A 1 55  ? 149.922 162.654 117.141 1.00 111.55 ? 31  HIS   A C     1 
ATOM   253  O  O     . HIS   A 1 55  ? 150.049 163.878 117.030 1.00 112.44 ? 31  HIS   A O     1 
ATOM   254  C  CB    . HIS   A 1 55  ? 150.878 160.777 115.776 1.00 113.14 ? 31  HIS   A CB    1 
ATOM   255  C  CG    . HIS   A 1 55  ? 151.082 161.414 114.437 1.00 113.49 ? 31  HIS   A CG    1 
ATOM   256  N  ND1   . HIS   A 1 55  ? 152.315 161.846 113.998 1.00 112.43 ? 31  HIS   A ND1   1 
ATOM   257  C  CD2   . HIS   A 1 55  ? 150.209 161.693 113.440 1.00 113.17 ? 31  HIS   A CD2   1 
ATOM   258  C  CE1   . HIS   A 1 55  ? 152.193 162.364 112.789 1.00 112.51 ? 31  HIS   A CE1   1 
ATOM   259  N  NE2   . HIS   A 1 55  ? 150.925 162.283 112.428 1.00 114.95 ? 31  HIS   A NE2   1 
ATOM   260  N  N     . SER   A 1 56  ? 148.751 162.090 117.423 1.00 89.34  ? 32  SER   A N     1 
ATOM   261  C  CA    . SER   A 1 56  ? 147.506 162.845 117.397 1.00 91.73  ? 32  SER   A CA    1 
ATOM   262  C  C     . SER   A 1 56  ? 147.145 163.475 118.737 1.00 91.01  ? 32  SER   A C     1 
ATOM   263  O  O     . SER   A 1 56  ? 146.098 164.122 118.834 1.00 89.42  ? 32  SER   A O     1 
ATOM   264  C  CB    . SER   A 1 56  ? 146.361 161.946 116.925 1.00 90.47  ? 32  SER   A CB    1 
ATOM   265  O  OG    . SER   A 1 56  ? 146.754 161.159 115.816 1.00 91.01  ? 32  SER   A OG    1 
ATOM   266  N  N     . ASN   A 1 57  ? 147.971 163.305 119.765 1.00 85.47  ? 33  ASN   A N     1 
ATOM   267  C  CA    . ASN   A 1 57  ? 147.701 163.948 121.043 1.00 82.26  ? 33  ASN   A CA    1 
ATOM   268  C  C     . ASN   A 1 57  ? 147.955 165.447 120.946 1.00 84.28  ? 33  ASN   A C     1 
ATOM   269  O  O     . ASN   A 1 57  ? 148.918 165.891 120.314 1.00 83.93  ? 33  ASN   A O     1 
ATOM   270  C  CB    . ASN   A 1 57  ? 148.568 163.336 122.142 1.00 82.17  ? 33  ASN   A CB    1 
ATOM   271  C  CG    . ASN   A 1 57  ? 148.419 161.833 122.230 1.00 83.72  ? 33  ASN   A CG    1 
ATOM   272  O  OD1   . ASN   A 1 57  ? 147.503 161.254 121.648 1.00 83.95  ? 33  ASN   A OD1   1 
ATOM   273  N  ND2   . ASN   A 1 57  ? 149.323 161.192 122.959 1.00 85.77  ? 33  ASN   A ND2   1 
ATOM   274  N  N     . TYR   A 1 58  ? 147.081 166.231 121.579 1.00 95.69  ? 34  TYR   A N     1 
ATOM   275  C  CA    . TYR   A 1 58  ? 147.219 167.682 121.531 1.00 95.91  ? 34  TYR   A CA    1 
ATOM   276  C  C     . TYR   A 1 58  ? 148.398 168.165 122.367 1.00 95.29  ? 34  TYR   A C     1 
ATOM   277  O  O     . TYR   A 1 58  ? 149.093 169.109 121.974 1.00 95.82  ? 34  TYR   A O     1 
ATOM   278  C  CB    . TYR   A 1 58  ? 145.926 168.351 121.994 1.00 98.08  ? 34  TYR   A CB    1 
ATOM   279  C  CG    . TYR   A 1 58  ? 144.885 168.484 120.904 1.00 98.93  ? 34  TYR   A CG    1 
ATOM   280  C  CD1   . TYR   A 1 58  ? 144.226 167.367 120.408 1.00 98.97  ? 34  TYR   A CD1   1 
ATOM   281  C  CD2   . TYR   A 1 58  ? 144.568 169.724 120.368 1.00 96.87  ? 34  TYR   A CD2   1 
ATOM   282  C  CE1   . TYR   A 1 58  ? 143.276 167.484 119.411 1.00 98.77  ? 34  TYR   A CE1   1 
ATOM   283  C  CE2   . TYR   A 1 58  ? 143.621 169.850 119.371 1.00 97.02  ? 34  TYR   A CE2   1 
ATOM   284  C  CZ    . TYR   A 1 58  ? 142.978 168.727 118.896 1.00 99.50  ? 34  TYR   A CZ    1 
ATOM   285  O  OH    . TYR   A 1 58  ? 142.033 168.847 117.903 1.00 99.16  ? 34  TYR   A OH    1 
ATOM   286  N  N     . LEU   A 1 59  ? 148.638 167.538 123.519 1.00 81.37  ? 35  LEU   A N     1 
ATOM   287  C  CA    . LEU   A 1 59  ? 149.770 167.927 124.352 1.00 80.74  ? 35  LEU   A CA    1 
ATOM   288  C  C     . LEU   A 1 59  ? 151.096 167.458 123.767 1.00 82.57  ? 35  LEU   A C     1 
ATOM   289  O  O     . LEU   A 1 59  ? 152.125 168.109 123.979 1.00 79.19  ? 35  LEU   A O     1 
ATOM   290  C  CB    . LEU   A 1 59  ? 149.594 167.382 125.770 1.00 79.26  ? 35  LEU   A CB    1 
ATOM   291  C  CG    . LEU   A 1 59  ? 148.287 167.757 126.472 1.00 81.81  ? 35  LEU   A CG    1 
ATOM   292  C  CD1   . LEU   A 1 59  ? 148.141 167.003 127.783 1.00 79.72  ? 35  LEU   A CD1   1 
ATOM   293  C  CD2   . LEU   A 1 59  ? 148.213 169.258 126.703 1.00 80.97  ? 35  LEU   A CD2   1 
ATOM   294  N  N     . GLY   A 1 60  ? 151.095 166.347 123.037 1.00 83.80  ? 36  GLY   A N     1 
ATOM   295  C  CA    . GLY   A 1 60  ? 152.294 165.879 122.371 1.00 78.20  ? 36  GLY   A CA    1 
ATOM   296  C  C     . GLY   A 1 60  ? 153.101 164.878 123.171 1.00 82.47  ? 36  GLY   A C     1 
ATOM   297  O  O     . GLY   A 1 60  ? 152.580 163.837 123.583 1.00 84.94  ? 36  GLY   A O     1 
ATOM   298  N  N     . VAL   A 1 61  ? 154.378 165.183 123.396 1.00 85.71  ? 37  VAL   A N     1 
ATOM   299  C  CA    . VAL   A 1 61  ? 155.280 164.276 124.097 1.00 82.66  ? 37  VAL   A CA    1 
ATOM   300  C  C     . VAL   A 1 61  ? 155.215 164.543 125.593 1.00 81.26  ? 37  VAL   A C     1 
ATOM   301  O  O     . VAL   A 1 61  ? 155.895 163.879 126.383 1.00 84.03  ? 37  VAL   A O     1 
ATOM   302  C  CB    . VAL   A 1 61  ? 156.723 164.411 123.579 1.00 81.26  ? 37  VAL   A CB    1 
ATOM   303  C  CG1   . VAL   A 1 61  ? 156.827 163.888 122.157 1.00 82.62  ? 37  VAL   A CG1   1 
ATOM   304  C  CG2   . VAL   A 1 61  ? 157.180 165.857 123.659 1.00 76.08  ? 37  VAL   A CG2   1 
ATOM   305  N  N     . ALA   A 1 62  ? 154.400 165.521 125.995 1.00 73.04  ? 38  ALA   A N     1 
ATOM   306  C  CA    . ALA   A 1 62  ? 154.233 165.810 127.413 1.00 73.32  ? 38  ALA   A CA    1 
ATOM   307  C  C     . ALA   A 1 62  ? 153.591 164.653 128.165 1.00 76.60  ? 38  ALA   A C     1 
ATOM   308  O  O     . ALA   A 1 62  ? 153.834 164.500 129.367 1.00 79.29  ? 38  ALA   A O     1 
ATOM   309  C  CB    . ALA   A 1 62  ? 153.400 167.078 127.600 1.00 73.39  ? 38  ALA   A CB    1 
ATOM   310  N  N     . TRP   A 1 63  ? 152.789 163.830 127.484 1.00 84.84  ? 39  TRP   A N     1 
ATOM   311  C  CA    . TRP   A 1 63  ? 152.142 162.702 128.141 1.00 81.34  ? 39  TRP   A CA    1 
ATOM   312  C  C     . TRP   A 1 63  ? 153.147 161.703 128.694 1.00 82.08  ? 39  TRP   A C     1 
ATOM   313  O  O     . TRP   A 1 63  ? 152.852 161.040 129.694 1.00 89.33  ? 39  TRP   A O     1 
ATOM   314  C  CB    . TRP   A 1 63  ? 151.187 162.007 127.171 1.00 82.30  ? 39  TRP   A CB    1 
ATOM   315  C  CG    . TRP   A 1 63  ? 149.832 162.638 127.133 1.00 85.43  ? 39  TRP   A CG    1 
ATOM   316  C  CD1   . TRP   A 1 63  ? 149.335 163.450 126.158 1.00 83.21  ? 39  TRP   A CD1   1 
ATOM   317  C  CD2   . TRP   A 1 63  ? 148.800 162.517 128.119 1.00 90.98  ? 39  TRP   A CD2   1 
ATOM   318  N  NE1   . TRP   A 1 63  ? 148.057 163.841 126.473 1.00 87.48  ? 39  TRP   A NE1   1 
ATOM   319  C  CE2   . TRP   A 1 63  ? 147.705 163.280 127.672 1.00 87.99  ? 39  TRP   A CE2   1 
ATOM   320  C  CE3   . TRP   A 1 63  ? 148.695 161.834 129.335 1.00 88.13  ? 39  TRP   A CE3   1 
ATOM   321  C  CZ2   . TRP   A 1 63  ? 146.521 163.381 128.398 1.00 85.75  ? 39  TRP   A CZ2   1 
ATOM   322  C  CZ3   . TRP   A 1 63  ? 147.519 161.936 130.053 1.00 84.36  ? 39  TRP   A CZ3   1 
ATOM   323  C  CH2   . TRP   A 1 63  ? 146.448 162.704 129.583 1.00 83.55  ? 39  TRP   A CH2   1 
ATOM   324  N  N     . GLU   A 1 64  ? 154.329 161.594 128.080 1.00 84.21  ? 40  GLU   A N     1 
ATOM   325  C  CA    . GLU   A 1 64  ? 155.374 160.731 128.619 1.00 84.91  ? 40  GLU   A CA    1 
ATOM   326  C  C     . GLU   A 1 64  ? 155.759 161.123 130.038 1.00 82.10  ? 40  GLU   A C     1 
ATOM   327  O  O     . GLU   A 1 64  ? 156.234 160.273 130.798 1.00 81.61  ? 40  GLU   A O     1 
ATOM   328  C  CB    . GLU   A 1 64  ? 156.609 160.769 127.716 1.00 82.42  ? 40  GLU   A CB    1 
ATOM   329  C  CG    . GLU   A 1 64  ? 156.323 160.476 126.253 1.00 84.85  ? 40  GLU   A CG    1 
ATOM   330  C  CD    . GLU   A 1 64  ? 156.733 159.074 125.846 1.00 88.55  ? 40  GLU   A CD    1 
ATOM   331  O  OE1   . GLU   A 1 64  ? 155.982 158.434 125.081 1.00 91.00  ? 40  GLU   A OE1   1 
ATOM   332  O  OE2   . GLU   A 1 64  ? 157.803 158.610 126.293 1.00 84.50  ? 40  GLU   A OE2   1 
ATOM   333  N  N     . LEU   A 1 65  ? 155.566 162.387 130.410 1.00 76.25  ? 41  LEU   A N     1 
ATOM   334  C  CA    . LEU   A 1 65  ? 155.762 162.831 131.782 1.00 75.19  ? 41  LEU   A CA    1 
ATOM   335  C  C     . LEU   A 1 65  ? 154.470 162.878 132.581 1.00 76.05  ? 41  LEU   A C     1 
ATOM   336  O  O     . LEU   A 1 65  ? 154.519 162.899 133.814 1.00 77.16  ? 41  LEU   A O     1 
ATOM   337  C  CB    . LEU   A 1 65  ? 156.412 164.219 131.804 1.00 76.35  ? 41  LEU   A CB    1 
ATOM   338  C  CG    . LEU   A 1 65  ? 157.902 164.286 132.147 1.00 77.55  ? 41  LEU   A CG    1 
ATOM   339  C  CD1   . LEU   A 1 65  ? 158.123 164.017 133.627 1.00 76.39  ? 41  LEU   A CD1   1 
ATOM   340  C  CD2   . LEU   A 1 65  ? 158.702 163.313 131.296 1.00 78.80  ? 41  LEU   A CD2   1 
ATOM   341  N  N     . ILE   A 1 66  ? 153.316 162.892 131.910 1.00 77.90  ? 42  ILE   A N     1 
ATOM   342  C  CA    . ILE   A 1 66  ? 152.050 163.050 132.618 1.00 76.22  ? 42  ILE   A CA    1 
ATOM   343  C  C     . ILE   A 1 66  ? 151.475 161.694 133.003 1.00 77.71  ? 42  ILE   A C     1 
ATOM   344  O  O     . ILE   A 1 66  ? 150.925 161.526 134.099 1.00 79.68  ? 42  ILE   A O     1 
ATOM   345  C  CB    . ILE   A 1 66  ? 151.064 163.867 131.762 1.00 75.95  ? 42  ILE   A CB    1 
ATOM   346  C  CG1   . ILE   A 1 66  ? 151.479 165.338 131.730 1.00 78.47  ? 42  ILE   A CG1   1 
ATOM   347  C  CG2   . ILE   A 1 66  ? 149.649 163.740 132.295 1.00 77.53  ? 42  ILE   A CG2   1 
ATOM   348  C  CD1   . ILE   A 1 66  ? 150.672 166.176 130.767 1.00 76.34  ? 42  ILE   A CD1   1 
ATOM   349  N  N     . ASN   A 1 67  ? 151.593 160.706 132.117 1.00 86.37  ? 43  ASN   A N     1 
ATOM   350  C  CA    . ASN   A 1 67  ? 151.016 159.393 132.394 1.00 83.68  ? 43  ASN   A CA    1 
ATOM   351  C  C     . ASN   A 1 67  ? 151.578 158.732 133.650 1.00 88.31  ? 43  ASN   A C     1 
ATOM   352  O  O     . ASN   A 1 67  ? 150.772 158.250 134.464 1.00 88.88  ? 43  ASN   A O     1 
ATOM   353  C  CB    . ASN   A 1 67  ? 151.189 158.483 131.171 1.00 85.92  ? 43  ASN   A CB    1 
ATOM   354  C  CG    . ASN   A 1 67  ? 149.982 157.602 130.926 1.00 93.31  ? 43  ASN   A CG    1 
ATOM   355  O  OD1   . ASN   A 1 67  ? 148.868 158.092 130.744 1.00 96.91  ? 43  ASN   A OD1   1 
ATOM   356  N  ND2   . ASN   A 1 67  ? 150.197 156.292 130.924 1.00 92.57  ? 43  ASN   A ND2   1 
ATOM   357  N  N     . PRO   A 1 68  ? 152.897 158.660 133.876 1.00 77.61  ? 44  PRO   A N     1 
ATOM   358  C  CA    . PRO   A 1 68  ? 153.375 158.070 135.136 1.00 72.78  ? 44  PRO   A CA    1 
ATOM   359  C  C     . PRO   A 1 68  ? 153.029 158.888 136.367 1.00 72.48  ? 44  PRO   A C     1 
ATOM   360  O  O     . PRO   A 1 68  ? 152.635 158.299 137.383 1.00 76.30  ? 44  PRO   A O     1 
ATOM   361  C  CB    . PRO   A 1 68  ? 154.894 157.990 134.932 1.00 69.50  ? 44  PRO   A CB    1 
ATOM   362  C  CG    . PRO   A 1 68  ? 155.186 159.048 133.939 1.00 66.48  ? 44  PRO   A CG    1 
ATOM   363  C  CD    . PRO   A 1 68  ? 154.026 159.011 132.996 1.00 74.00  ? 44  PRO   A CD    1 
ATOM   364  N  N     . VAL   A 1 69  ? 153.133 160.219 136.299 1.00 72.19  ? 45  VAL   A N     1 
ATOM   365  C  CA    . VAL   A 1 69  ? 152.959 161.053 137.486 1.00 72.64  ? 45  VAL   A CA    1 
ATOM   366  C  C     . VAL   A 1 69  ? 151.604 160.797 138.131 1.00 75.96  ? 45  VAL   A C     1 
ATOM   367  O  O     . VAL   A 1 69  ? 151.517 160.556 139.342 1.00 77.68  ? 45  VAL   A O     1 
ATOM   368  C  CB    . VAL   A 1 69  ? 153.145 162.538 137.123 1.00 70.22  ? 45  VAL   A CB    1 
ATOM   369  C  CG1   . VAL   A 1 69  ? 152.426 163.428 138.124 1.00 71.71  ? 45  VAL   A CG1   1 
ATOM   370  C  CG2   . VAL   A 1 69  ? 154.621 162.887 137.063 1.00 71.91  ? 45  VAL   A CG2   1 
ATOM   371  N  N     . MET   A 1 70  ? 150.532 160.811 137.331 1.00 81.44  ? 46  MET   A N     1 
ATOM   372  C  CA    . MET   A 1 70  ? 149.204 160.531 137.867 1.00 79.52  ? 46  MET   A CA    1 
ATOM   373  C  C     . MET   A 1 70  ? 149.186 159.212 138.624 1.00 78.93  ? 46  MET   A C     1 
ATOM   374  O  O     . MET   A 1 70  ? 148.689 159.149 139.756 1.00 81.26  ? 46  MET   A O     1 
ATOM   375  C  CB    . MET   A 1 70  ? 148.171 160.509 136.741 1.00 78.81  ? 46  MET   A CB    1 
ATOM   376  C  CG    . MET   A 1 70  ? 148.090 161.789 135.932 1.00 79.69  ? 46  MET   A CG    1 
ATOM   377  S  SD    . MET   A 1 70  ? 146.844 161.681 134.634 1.00 90.72  ? 46  MET   A SD    1 
ATOM   378  C  CE    . MET   A 1 70  ? 146.392 163.403 134.448 1.00 83.56  ? 46  MET   A CE    1 
ATOM   379  N  N     . GLN   A 1 71  ? 149.766 158.162 138.035 1.00 71.13  ? 47  GLN   A N     1 
ATOM   380  C  CA    . GLN   A 1 71  ? 149.814 156.871 138.712 1.00 68.16  ? 47  GLN   A CA    1 
ATOM   381  C  C     . GLN   A 1 71  ? 150.458 157.003 140.082 1.00 67.01  ? 47  GLN   A C     1 
ATOM   382  O  O     . GLN   A 1 71  ? 149.915 156.511 141.080 1.00 70.84  ? 47  GLN   A O     1 
ATOM   383  C  CB    . GLN   A 1 71  ? 150.573 155.857 137.858 1.00 71.22  ? 47  GLN   A CB    1 
ATOM   384  C  CG    . GLN   A 1 71  ? 149.959 155.610 136.494 1.00 73.58  ? 47  GLN   A CG    1 
ATOM   385  C  CD    . GLN   A 1 71  ? 150.587 154.431 135.782 1.00 78.61  ? 47  GLN   A CD    1 
ATOM   386  O  OE1   . GLN   A 1 71  ? 150.982 153.449 136.410 1.00 74.38  ? 47  GLN   A OE1   1 
ATOM   387  N  NE2   . GLN   A 1 71  ? 150.687 154.522 134.461 1.00 80.37  ? 47  GLN   A NE2   1 
ATOM   388  N  N     . ILE   A 1 72  ? 151.583 157.720 140.156 1.00 64.02  ? 48  ILE   A N     1 
ATOM   389  C  CA    . ILE   A 1 72  ? 152.259 157.915 141.434 1.00 65.54  ? 48  ILE   A CA    1 
ATOM   390  C  C     . ILE   A 1 72  ? 151.297 158.517 142.444 1.00 67.50  ? 48  ILE   A C     1 
ATOM   391  O  O     . ILE   A 1 72  ? 151.189 158.040 143.582 1.00 69.83  ? 48  ILE   A O     1 
ATOM   392  C  CB    . ILE   A 1 72  ? 153.507 158.797 141.247 1.00 69.03  ? 48  ILE   A CB    1 
ATOM   393  C  CG1   . ILE   A 1 72  ? 154.502 158.121 140.304 1.00 65.19  ? 48  ILE   A CG1   1 
ATOM   394  C  CG2   . ILE   A 1 72  ? 154.162 159.082 142.589 1.00 66.65  ? 48  ILE   A CG2   1 
ATOM   395  C  CD1   . ILE   A 1 72  ? 155.623 159.030 139.855 1.00 65.79  ? 48  ILE   A CD1   1 
ATOM   396  N  N     . MET   A 1 73  ? 150.544 159.540 142.026 1.00 74.28  ? 49  MET   A N     1 
ATOM   397  C  CA    . MET   A 1 73  ? 149.574 160.159 142.922 1.00 73.07  ? 49  MET   A CA    1 
ATOM   398  C  C     . MET   A 1 73  ? 148.631 159.116 143.499 1.00 74.89  ? 49  MET   A C     1 
ATOM   399  O  O     . MET   A 1 73  ? 148.437 159.052 144.720 1.00 79.22  ? 49  MET   A O     1 
ATOM   400  C  CB    . MET   A 1 73  ? 148.793 161.244 142.183 1.00 77.58  ? 49  MET   A CB    1 
ATOM   401  C  CG    . MET   A 1 73  ? 149.633 162.444 141.783 1.00 83.18  ? 49  MET   A CG    1 
ATOM   402  S  SD    . MET   A 1 73  ? 148.661 163.947 141.582 1.00 88.72  ? 49  MET   A SD    1 
ATOM   403  C  CE    . MET   A 1 73  ? 148.643 164.104 139.799 1.00 81.85  ? 49  MET   A CE    1 
ATOM   404  N  N     . VAL   A 1 74  ? 148.082 158.251 142.643 1.00 61.74  ? 50  VAL   A N     1 
ATOM   405  C  CA    . VAL   A 1 74  ? 147.179 157.216 143.130 1.00 53.97  ? 50  VAL   A CA    1 
ATOM   406  C  C     . VAL   A 1 74  ? 147.897 156.328 144.135 1.00 56.91  ? 50  VAL   A C     1 
ATOM   407  O  O     . VAL   A 1 74  ? 147.377 156.051 145.223 1.00 63.89  ? 50  VAL   A O     1 
ATOM   408  C  CB    . VAL   A 1 74  ? 146.611 156.404 141.953 1.00 55.17  ? 50  VAL   A CB    1 
ATOM   409  C  CG1   . VAL   A 1 74  ? 145.960 155.126 142.454 1.00 56.64  ? 50  VAL   A CG1   1 
ATOM   410  C  CG2   . VAL   A 1 74  ? 145.618 157.241 141.164 1.00 56.35  ? 50  VAL   A CG2   1 
ATOM   411  N  N     . TYR   A 1 75  ? 149.127 155.920 143.815 1.00 52.00  ? 51  TYR   A N     1 
ATOM   412  C  CA    . TYR   A 1 75  ? 149.852 155.030 144.710 1.00 45.67  ? 51  TYR   A CA    1 
ATOM   413  C  C     . TYR   A 1 75  ? 150.212 155.725 146.015 1.00 42.99  ? 51  TYR   A C     1 
ATOM   414  O  O     . TYR   A 1 75  ? 150.514 155.054 147.007 1.00 44.98  ? 51  TYR   A O     1 
ATOM   415  C  CB    . TYR   A 1 75  ? 151.102 154.493 144.017 1.00 53.15  ? 51  TYR   A CB    1 
ATOM   416  C  CG    . TYR   A 1 75  ? 150.820 153.311 143.119 1.00 58.39  ? 51  TYR   A CG    1 
ATOM   417  C  CD1   . TYR   A 1 75  ? 150.142 152.198 143.597 1.00 57.32  ? 51  TYR   A CD1   1 
ATOM   418  C  CD2   . TYR   A 1 75  ? 151.219 153.312 141.790 1.00 55.50  ? 51  TYR   A CD2   1 
ATOM   419  C  CE1   . TYR   A 1 75  ? 149.876 151.118 142.781 1.00 55.12  ? 51  TYR   A CE1   1 
ATOM   420  C  CE2   . TYR   A 1 75  ? 150.958 152.236 140.966 1.00 53.94  ? 51  TYR   A CE2   1 
ATOM   421  C  CZ    . TYR   A 1 75  ? 150.286 151.142 141.467 1.00 55.91  ? 51  TYR   A CZ    1 
ATOM   422  O  OH    . TYR   A 1 75  ? 150.024 150.068 140.649 1.00 57.65  ? 51  TYR   A OH    1 
ATOM   423  N  N     . TRP   A 1 76  ? 150.188 157.060 146.038 1.00 44.02  ? 52  TRP   A N     1 
ATOM   424  C  CA    . TRP   A 1 76  ? 150.413 157.757 147.298 1.00 42.81  ? 52  TRP   A CA    1 
ATOM   425  C  C     . TRP   A 1 76  ? 149.119 157.884 148.089 1.00 51.93  ? 52  TRP   A C     1 
ATOM   426  O  O     . TRP   A 1 76  ? 149.141 157.924 149.324 1.00 53.08  ? 52  TRP   A O     1 
ATOM   427  C  CB    . TRP   A 1 76  ? 151.024 159.134 147.049 1.00 50.26  ? 52  TRP   A CB    1 
ATOM   428  C  CG    . TRP   A 1 76  ? 151.235 159.901 148.314 1.00 54.52  ? 52  TRP   A CG    1 
ATOM   429  C  CD1   . TRP   A 1 76  ? 152.193 159.674 149.257 1.00 57.16  ? 52  TRP   A CD1   1 
ATOM   430  C  CD2   . TRP   A 1 76  ? 150.458 161.004 148.790 1.00 49.26  ? 52  TRP   A CD2   1 
ATOM   431  N  NE1   . TRP   A 1 76  ? 152.067 160.573 150.286 1.00 53.52  ? 52  TRP   A NE1   1 
ATOM   432  C  CE2   . TRP   A 1 76  ? 151.009 161.401 150.023 1.00 51.64  ? 52  TRP   A CE2   1 
ATOM   433  C  CE3   . TRP   A 1 76  ? 149.353 161.698 148.291 1.00 49.66  ? 52  TRP   A CE3   1 
ATOM   434  C  CZ2   . TRP   A 1 76  ? 150.493 162.459 150.764 1.00 53.57  ? 52  TRP   A CZ2   1 
ATOM   435  C  CZ3   . TRP   A 1 76  ? 148.842 162.748 149.028 1.00 56.74  ? 52  TRP   A CZ3   1 
ATOM   436  C  CH2   . TRP   A 1 76  ? 149.412 163.119 150.250 1.00 57.71  ? 52  TRP   A CH2   1 
ATOM   437  N  N     . MET   A 1 77  ? 147.980 157.947 147.396 1.00 59.29  ? 53  MET   A N     1 
ATOM   438  C  CA    . MET   A 1 77  ? 146.712 158.120 148.094 1.00 48.09  ? 53  MET   A CA    1 
ATOM   439  C  C     . MET   A 1 77  ? 146.256 156.820 148.740 1.00 43.50  ? 53  MET   A C     1 
ATOM   440  O  O     . MET   A 1 77  ? 145.634 156.836 149.808 1.00 47.08  ? 53  MET   A O     1 
ATOM   441  C  CB    . MET   A 1 77  ? 145.652 158.648 147.130 1.00 50.91  ? 53  MET   A CB    1 
ATOM   442  C  CG    . MET   A 1 77  ? 145.212 160.073 147.417 1.00 56.36  ? 53  MET   A CG    1 
ATOM   443  S  SD    . MET   A 1 77  ? 143.956 160.661 146.266 1.00 77.06  ? 53  MET   A SD    1 
ATOM   444  C  CE    . MET   A 1 77  ? 144.801 160.448 144.703 1.00 56.00  ? 53  MET   A CE    1 
ATOM   445  N  N     . VAL   A 1 78  ? 146.561 155.686 148.114 1.00 41.08  ? 54  VAL   A N     1 
ATOM   446  C  CA    . VAL   A 1 78  ? 146.098 154.399 148.622 1.00 37.50  ? 54  VAL   A CA    1 
ATOM   447  C  C     . VAL   A 1 78  ? 147.052 153.861 149.681 1.00 38.50  ? 54  VAL   A C     1 
ATOM   448  O  O     . VAL   A 1 78  ? 146.665 153.628 150.831 1.00 37.23  ? 54  VAL   A O     1 
ATOM   449  C  CB    . VAL   A 1 78  ? 145.927 153.398 147.465 1.00 31.98  ? 54  VAL   A CB    1 
ATOM   450  C  CG1   . VAL   A 1 78  ? 145.590 152.019 148.003 1.00 30.84  ? 54  VAL   A CG1   1 
ATOM   451  C  CG2   . VAL   A 1 78  ? 144.861 153.883 146.502 1.00 34.23  ? 54  VAL   A CG2   1 
ATOM   452  N  N     . PHE   A 1 79  ? 148.312 153.653 149.304 1.00 42.03  ? 55  PHE   A N     1 
ATOM   453  C  CA    . PHE   A 1 79  ? 149.282 153.014 150.182 1.00 38.45  ? 55  PHE   A CA    1 
ATOM   454  C  C     . PHE   A 1 79  ? 149.952 153.980 151.148 1.00 34.53  ? 55  PHE   A C     1 
ATOM   455  O  O     . PHE   A 1 79  ? 150.546 153.532 152.134 1.00 39.91  ? 55  PHE   A O     1 
ATOM   456  C  CB    . PHE   A 1 79  ? 150.354 152.306 149.348 1.00 30.46  ? 55  PHE   A CB    1 
ATOM   457  C  CG    . PHE   A 1 79  ? 149.880 151.032 148.709 1.00 44.70  ? 55  PHE   A CG    1 
ATOM   458  C  CD1   . PHE   A 1 79  ? 149.182 151.059 147.514 1.00 46.56  ? 55  PHE   A CD1   1 
ATOM   459  C  CD2   . PHE   A 1 79  ? 150.131 149.808 149.303 1.00 33.01  ? 55  PHE   A CD2   1 
ATOM   460  C  CE1   . PHE   A 1 79  ? 148.742 149.893 146.924 1.00 33.64  ? 55  PHE   A CE1   1 
ATOM   461  C  CE2   . PHE   A 1 79  ? 149.694 148.638 148.717 1.00 40.25  ? 55  PHE   A CE2   1 
ATOM   462  C  CZ    . PHE   A 1 79  ? 148.999 148.681 147.526 1.00 38.52  ? 55  PHE   A CZ    1 
ATOM   463  N  N     . GLY   A 1 80  ? 149.875 155.283 150.894 1.00 36.64  ? 56  GLY   A N     1 
ATOM   464  C  CA    . GLY   A 1 80  ? 150.514 156.253 151.760 1.00 35.99  ? 56  GLY   A CA    1 
ATOM   465  C  C     . GLY   A 1 80  ? 149.568 156.913 152.738 1.00 37.51  ? 56  GLY   A C     1 
ATOM   466  O  O     . GLY   A 1 80  ? 149.859 156.993 153.934 1.00 41.60  ? 56  GLY   A O     1 
ATOM   467  N  N     . LEU   A 1 81  ? 148.424 157.387 152.243 1.00 48.67  ? 57  LEU   A N     1 
ATOM   468  C  CA    . LEU   A 1 81  ? 147.447 158.034 153.112 1.00 49.84  ? 57  LEU   A CA    1 
ATOM   469  C  C     . LEU   A 1 81  ? 146.532 157.012 153.776 1.00 49.51  ? 57  LEU   A C     1 
ATOM   470  O  O     . LEU   A 1 81  ? 146.302 157.071 154.988 1.00 45.11  ? 57  LEU   A O     1 
ATOM   471  C  CB    . LEU   A 1 81  ? 146.625 159.048 152.315 1.00 53.21  ? 57  LEU   A CB    1 
ATOM   472  C  CG    . LEU   A 1 81  ? 147.154 160.481 152.276 1.00 51.13  ? 57  LEU   A CG    1 
ATOM   473  C  CD1   . LEU   A 1 81  ? 146.202 161.375 151.503 1.00 51.28  ? 57  LEU   A CD1   1 
ATOM   474  C  CD2   . LEU   A 1 81  ? 147.367 161.009 153.683 1.00 52.83  ? 57  LEU   A CD2   1 
ATOM   475  N  N     . GLY   A 1 82  ? 146.003 156.071 152.999 1.00 47.25  ? 58  GLY   A N     1 
ATOM   476  C  CA    . GLY   A 1 82  ? 145.117 155.061 153.540 1.00 43.91  ? 58  GLY   A CA    1 
ATOM   477  C  C     . GLY   A 1 82  ? 145.833 154.100 154.463 1.00 46.22  ? 58  GLY   A C     1 
ATOM   478  O  O     . GLY   A 1 82  ? 145.586 154.088 155.672 1.00 57.18  ? 58  GLY   A O     1 
ATOM   479  N  N     . ILE   A 1 83  ? 146.721 153.292 153.905 1.00 38.52  ? 59  ILE   A N     1 
ATOM   480  C  CA    . ILE   A 1 83  ? 147.568 152.422 154.710 1.00 46.36  ? 59  ILE   A CA    1 
ATOM   481  C  C     . ILE   A 1 83  ? 148.771 153.217 155.197 1.00 59.47  ? 59  ILE   A C     1 
ATOM   482  O  O     . ILE   A 1 83  ? 149.122 154.258 154.632 1.00 69.09  ? 59  ILE   A O     1 
ATOM   483  C  CB    . ILE   A 1 83  ? 147.992 151.179 153.902 1.00 50.18  ? 59  ILE   A CB    1 
ATOM   484  C  CG1   . ILE   A 1 83  ? 146.909 150.809 152.889 1.00 40.94  ? 59  ILE   A CG1   1 
ATOM   485  C  CG2   . ILE   A 1 83  ? 148.267 150.008 154.829 1.00 52.13  ? 59  ILE   A CG2   1 
ATOM   486  C  CD1   . ILE   A 1 83  ? 147.325 149.731 151.920 1.00 37.58  ? 59  ILE   A CD1   1 
ATOM   487  N  N     . ARG   A 1 84  ? 149.378 152.742 156.288 1.00 62.68  ? 60  ARG   A N     1 
ATOM   488  C  CA    . ARG   A 1 84  ? 150.569 153.326 156.905 1.00 64.40  ? 60  ARG   A CA    1 
ATOM   489  C  C     . ARG   A 1 84  ? 150.267 154.643 157.613 1.00 63.39  ? 60  ARG   A C     1 
ATOM   490  O  O     . ARG   A 1 84  ? 151.109 155.147 158.363 1.00 70.11  ? 60  ARG   A O     1 
ATOM   491  C  CB    . ARG   A 1 84  ? 151.680 153.553 155.874 1.00 62.04  ? 60  ARG   A CB    1 
ATOM   492  C  CG    . ARG   A 1 84  ? 152.269 152.298 155.269 1.00 64.48  ? 60  ARG   A CG    1 
ATOM   493  C  CD    . ARG   A 1 84  ? 153.678 152.564 154.777 1.00 59.55  ? 60  ARG   A CD    1 
ATOM   494  N  NE    . ARG   A 1 84  ? 154.370 153.502 155.650 1.00 61.67  ? 60  ARG   A NE    1 
ATOM   495  C  CZ    . ARG   A 1 84  ? 155.276 153.156 156.553 1.00 65.59  ? 60  ARG   A CZ    1 
ATOM   496  N  NH1   . ARG   A 1 84  ? 155.648 151.897 156.712 1.00 67.39  ? 60  ARG   A NH1   1 
ATOM   497  N  NH2   . ARG   A 1 84  ? 155.823 154.097 157.317 1.00 59.11  ? 60  ARG   A NH2   1 
ATOM   498  N  N     . SER   A 1 85  ? 149.067 155.188 157.405 1.00 68.70  ? 61  SER   A N     1 
ATOM   499  C  CA    . SER   A 1 85  ? 148.644 156.450 158.018 1.00 71.86  ? 61  SER   A CA    1 
ATOM   500  C  C     . SER   A 1 85  ? 149.693 157.549 157.844 1.00 74.50  ? 61  SER   A C     1 
ATOM   501  O  O     . SER   A 1 85  ? 149.891 158.390 158.723 1.00 80.07  ? 61  SER   A O     1 
ATOM   502  C  CB    . SER   A 1 85  ? 148.308 156.248 159.496 1.00 79.37  ? 61  SER   A CB    1 
ATOM   503  O  OG    . SER   A 1 85  ? 147.437 155.144 159.672 1.00 81.34  ? 61  SER   A OG    1 
ATOM   504  N  N     . ASN   A 1 86  ? 150.369 157.540 156.692 1.00 76.55  ? 62  ASN   A N     1 
ATOM   505  C  CA    . ASN   A 1 86  ? 151.408 158.521 156.363 1.00 78.73  ? 62  ASN   A CA    1 
ATOM   506  C  C     . ASN   A 1 86  ? 152.527 158.526 157.405 1.00 78.39  ? 62  ASN   A C     1 
ATOM   507  O  O     . ASN   A 1 86  ? 152.886 159.566 157.962 1.00 77.96  ? 62  ASN   A O     1 
ATOM   508  C  CB    . ASN   A 1 86  ? 150.811 159.921 156.194 1.00 76.71  ? 62  ASN   A CB    1 
ATOM   509  C  CG    . ASN   A 1 86  ? 151.413 160.674 155.024 1.00 79.89  ? 62  ASN   A CG    1 
ATOM   510  O  OD1   . ASN   A 1 86  ? 152.208 160.126 154.261 1.00 83.15  ? 62  ASN   A OD1   1 
ATOM   511  N  ND2   . ASN   A 1 86  ? 151.038 161.939 154.880 1.00 77.17  ? 62  ASN   A ND2   1 
ATOM   512  N  N     . ALA   A 1 87  ? 153.084 157.346 157.665 1.00 81.37  ? 63  ALA   A N     1 
ATOM   513  C  CA    . ALA   A 1 87  ? 154.186 157.249 158.616 1.00 79.79  ? 63  ALA   A CA    1 
ATOM   514  C  C     . ALA   A 1 87  ? 155.524 157.219 157.881 1.00 85.17  ? 63  ALA   A C     1 
ATOM   515  O  O     . ALA   A 1 87  ? 155.674 156.493 156.895 1.00 83.74  ? 63  ALA   A O     1 
ATOM   516  C  CB    . ALA   A 1 87  ? 154.049 155.998 159.477 1.00 76.32  ? 63  ALA   A CB    1 
ATOM   517  N  N     . PRO   A 1 88  ? 156.505 157.993 158.342 1.00 86.44  ? 64  PRO   A N     1 
ATOM   518  C  CA    . PRO   A 1 88  ? 157.799 158.035 157.655 1.00 82.13  ? 64  PRO   A CA    1 
ATOM   519  C  C     . PRO   A 1 88  ? 158.579 156.740 157.830 1.00 82.90  ? 64  PRO   A C     1 
ATOM   520  O  O     . PRO   A 1 88  ? 158.358 155.964 158.762 1.00 80.51  ? 64  PRO   A O     1 
ATOM   521  C  CB    . PRO   A 1 88  ? 158.516 159.209 158.327 1.00 79.63  ? 64  PRO   A CB    1 
ATOM   522  C  CG    . PRO   A 1 88  ? 157.919 159.268 159.688 1.00 82.20  ? 64  PRO   A CG    1 
ATOM   523  C  CD    . PRO   A 1 88  ? 156.477 158.874 159.522 1.00 84.68  ? 64  PRO   A CD    1 
ATOM   524  N  N     . ILE   A 1 89  ? 159.507 156.515 156.903 1.00 74.06  ? 65  ILE   A N     1 
ATOM   525  C  CA    . ILE   A 1 89  ? 160.363 155.334 156.900 1.00 72.81  ? 65  ILE   A CA    1 
ATOM   526  C  C     . ILE   A 1 89  ? 161.815 155.787 156.932 1.00 74.85  ? 65  ILE   A C     1 
ATOM   527  O  O     . ILE   A 1 89  ? 162.232 156.603 156.101 1.00 74.65  ? 65  ILE   A O     1 
ATOM   528  C  CB    . ILE   A 1 89  ? 160.105 154.443 155.671 1.00 66.71  ? 65  ILE   A CB    1 
ATOM   529  C  CG1   . ILE   A 1 89  ? 158.695 153.859 155.714 1.00 69.63  ? 65  ILE   A CG1   1 
ATOM   530  C  CG2   . ILE   A 1 89  ? 161.128 153.325 155.603 1.00 65.22  ? 65  ILE   A CG2   1 
ATOM   531  C  CD1   . ILE   A 1 89  ? 158.399 152.906 154.580 1.00 63.61  ? 65  ILE   A CD1   1 
ATOM   532  N  N     . HIS   A 1 90  ? 162.578 155.256 157.889 1.00 86.57  ? 66  HIS   A N     1 
ATOM   533  C  CA    . HIS   A 1 90  ? 164.019 155.494 157.988 1.00 80.10  ? 66  HIS   A CA    1 
ATOM   534  C  C     . HIS   A 1 90  ? 164.349 156.977 158.126 1.00 78.61  ? 66  HIS   A C     1 
ATOM   535  O  O     . HIS   A 1 90  ? 165.383 157.439 157.640 1.00 85.29  ? 66  HIS   A O     1 
ATOM   536  C  CB    . HIS   A 1 90  ? 164.761 154.898 156.787 1.00 82.67  ? 66  HIS   A CB    1 
ATOM   537  C  CG    . HIS   A 1 90  ? 164.926 153.412 156.852 1.00 84.31  ? 66  HIS   A CG    1 
ATOM   538  N  ND1   . HIS   A 1 90  ? 166.028 152.763 156.338 1.00 79.66  ? 66  HIS   A ND1   1 
ATOM   539  C  CD2   . HIS   A 1 90  ? 164.126 152.447 157.364 1.00 85.61  ? 66  HIS   A CD2   1 
ATOM   540  C  CE1   . HIS   A 1 90  ? 165.901 151.462 156.534 1.00 80.94  ? 66  HIS   A CE1   1 
ATOM   541  N  NE2   . HIS   A 1 90  ? 164.756 151.245 157.154 1.00 88.69  ? 66  HIS   A NE2   1 
ATOM   542  N  N     . GLY   A 1 91  ? 163.478 157.736 158.785 1.00 65.82  ? 67  GLY   A N     1 
ATOM   543  C  CA    . GLY   A 1 91  ? 163.687 159.158 158.949 1.00 67.13  ? 67  GLY   A CA    1 
ATOM   544  C  C     . GLY   A 1 91  ? 163.365 159.998 157.734 1.00 70.38  ? 67  GLY   A C     1 
ATOM   545  O  O     . GLY   A 1 91  ? 163.616 161.210 157.756 1.00 69.95  ? 67  GLY   A O     1 
ATOM   546  N  N     . VAL   A 1 92  ? 162.826 159.400 156.678 1.00 72.17  ? 68  VAL   A N     1 
ATOM   547  C  CA    . VAL   A 1 92  ? 162.488 160.111 155.448 1.00 70.37  ? 68  VAL   A CA    1 
ATOM   548  C  C     . VAL   A 1 92  ? 160.971 160.117 155.308 1.00 68.68  ? 68  VAL   A C     1 
ATOM   549  O  O     . VAL   A 1 92  ? 160.323 159.112 155.635 1.00 66.76  ? 68  VAL   A O     1 
ATOM   550  C  CB    . VAL   A 1 92  ? 163.163 159.459 154.229 1.00 72.17  ? 68  VAL   A CB    1 
ATOM   551  C  CG1   . VAL   A 1 92  ? 163.039 160.343 152.999 1.00 67.57  ? 68  VAL   A CG1   1 
ATOM   552  C  CG2   . VAL   A 1 92  ? 164.623 159.158 154.527 1.00 69.45  ? 68  VAL   A CG2   1 
ATOM   553  N  N     . PRO   A 1 93  ? 160.361 161.211 154.851 1.00 73.61  ? 69  PRO   A N     1 
ATOM   554  C  CA    . PRO   A 1 93  ? 158.920 161.186 154.583 1.00 72.93  ? 69  PRO   A CA    1 
ATOM   555  C  C     . PRO   A 1 93  ? 158.578 160.141 153.532 1.00 68.84  ? 69  PRO   A C     1 
ATOM   556  O  O     . PRO   A 1 93  ? 159.350 159.882 152.607 1.00 72.99  ? 69  PRO   A O     1 
ATOM   557  C  CB    . PRO   A 1 93  ? 158.625 162.604 154.084 1.00 70.23  ? 69  PRO   A CB    1 
ATOM   558  C  CG    . PRO   A 1 93  ? 159.705 163.438 154.670 1.00 69.09  ? 69  PRO   A CG    1 
ATOM   559  C  CD    . PRO   A 1 93  ? 160.924 162.566 154.716 1.00 69.38  ? 69  PRO   A CD    1 
ATOM   560  N  N     . PHE   A 1 94  ? 157.402 159.530 153.691 1.00 50.25  ? 70  PHE   A N     1 
ATOM   561  C  CA    . PHE   A 1 94  ? 157.016 158.434 152.811 1.00 49.50  ? 70  PHE   A CA    1 
ATOM   562  C  C     . PHE   A 1 94  ? 156.845 158.890 151.368 1.00 50.29  ? 70  PHE   A C     1 
ATOM   563  O  O     . PHE   A 1 94  ? 157.019 158.086 150.445 1.00 57.12  ? 70  PHE   A O     1 
ATOM   564  C  CB    . PHE   A 1 94  ? 155.727 157.784 153.309 1.00 49.79  ? 70  PHE   A CB    1 
ATOM   565  C  CG    . PHE   A 1 94  ? 155.309 156.585 152.510 1.00 50.18  ? 70  PHE   A CG    1 
ATOM   566  C  CD1   . PHE   A 1 94  ? 155.928 155.363 152.698 1.00 53.39  ? 70  PHE   A CD1   1 
ATOM   567  C  CD2   . PHE   A 1 94  ? 154.306 156.683 151.561 1.00 46.94  ? 70  PHE   A CD2   1 
ATOM   568  C  CE1   . PHE   A 1 94  ? 155.551 154.261 151.962 1.00 53.47  ? 70  PHE   A CE1   1 
ATOM   569  C  CE2   . PHE   A 1 94  ? 153.925 155.584 150.823 1.00 35.98  ? 70  PHE   A CE2   1 
ATOM   570  C  CZ    . PHE   A 1 94  ? 154.548 154.371 151.024 1.00 42.35  ? 70  PHE   A CZ    1 
ATOM   571  N  N     . VAL   A 1 95  ? 156.508 160.162 151.149 1.00 46.91  ? 71  VAL   A N     1 
ATOM   572  C  CA    . VAL   A 1 95  ? 156.250 160.631 149.791 1.00 42.52  ? 71  VAL   A CA    1 
ATOM   573  C  C     . VAL   A 1 95  ? 157.511 160.535 148.939 1.00 49.94  ? 71  VAL   A C     1 
ATOM   574  O  O     . VAL   A 1 95  ? 157.480 160.004 147.824 1.00 53.04  ? 71  VAL   A O     1 
ATOM   575  C  CB    . VAL   A 1 95  ? 155.681 162.061 149.819 1.00 41.14  ? 71  VAL   A CB    1 
ATOM   576  C  CG1   . VAL   A 1 95  ? 156.328 162.873 150.930 1.00 47.84  ? 71  VAL   A CG1   1 
ATOM   577  C  CG2   . VAL   A 1 95  ? 155.861 162.738 148.470 1.00 41.71  ? 71  VAL   A CG2   1 
ATOM   578  N  N     . TYR   A 1 96  ? 158.646 161.006 149.458 1.00 52.66  ? 72  TYR   A N     1 
ATOM   579  C  CA    . TYR   A 1 96  ? 159.891 160.945 148.699 1.00 45.14  ? 72  TYR   A CA    1 
ATOM   580  C  C     . TYR   A 1 96  ? 160.478 159.540 148.672 1.00 49.29  ? 72  TYR   A C     1 
ATOM   581  O  O     . TYR   A 1 96  ? 161.105 159.151 147.678 1.00 56.31  ? 72  TYR   A O     1 
ATOM   582  C  CB    . TYR   A 1 96  ? 160.894 161.942 149.276 1.00 42.13  ? 72  TYR   A CB    1 
ATOM   583  C  CG    . TYR   A 1 96  ? 160.344 163.347 149.330 1.00 48.63  ? 72  TYR   A CG    1 
ATOM   584  C  CD1   . TYR   A 1 96  ? 160.319 164.146 148.197 1.00 49.41  ? 72  TYR   A CD1   1 
ATOM   585  C  CD2   . TYR   A 1 96  ? 159.821 163.864 150.506 1.00 50.23  ? 72  TYR   A CD2   1 
ATOM   586  C  CE1   . TYR   A 1 96  ? 159.805 165.424 148.237 1.00 41.81  ? 72  TYR   A CE1   1 
ATOM   587  C  CE2   . TYR   A 1 96  ? 159.302 165.139 150.555 1.00 51.80  ? 72  TYR   A CE2   1 
ATOM   588  C  CZ    . TYR   A 1 96  ? 159.298 165.916 149.418 1.00 49.62  ? 72  TYR   A CZ    1 
ATOM   589  O  OH    . TYR   A 1 96  ? 158.785 167.191 149.462 1.00 55.26  ? 72  TYR   A OH    1 
ATOM   590  N  N     . TRP   A 1 97  ? 160.271 158.768 149.741 1.00 38.11  ? 73  TRP   A N     1 
ATOM   591  C  CA    . TRP   A 1 97  ? 160.667 157.364 149.740 1.00 35.64  ? 73  TRP   A CA    1 
ATOM   592  C  C     . TRP   A 1 97  ? 159.971 156.602 148.618 1.00 45.81  ? 73  TRP   A C     1 
ATOM   593  O  O     . TRP   A 1 97  ? 160.585 155.760 147.953 1.00 51.58  ? 73  TRP   A O     1 
ATOM   594  C  CB    . TRP   A 1 97  ? 160.349 156.743 151.100 1.00 40.52  ? 73  TRP   A CB    1 
ATOM   595  C  CG    . TRP   A 1 97  ? 161.086 155.478 151.412 1.00 39.52  ? 73  TRP   A CG    1 
ATOM   596  C  CD1   . TRP   A 1 97  ? 162.356 155.367 151.893 1.00 39.28  ? 73  TRP   A CD1   1 
ATOM   597  C  CD2   . TRP   A 1 97  ? 160.584 154.141 151.293 1.00 46.85  ? 73  TRP   A CD2   1 
ATOM   598  N  NE1   . TRP   A 1 97  ? 162.684 154.045 152.069 1.00 30.74  ? 73  TRP   A NE1   1 
ATOM   599  C  CE2   . TRP   A 1 97  ? 161.612 153.272 151.708 1.00 39.13  ? 73  TRP   A CE2   1 
ATOM   600  C  CE3   . TRP   A 1 97  ? 159.368 153.594 150.872 1.00 41.38  ? 73  TRP   A CE3   1 
ATOM   601  C  CZ2   . TRP   A 1 97  ? 161.461 151.888 151.712 1.00 40.27  ? 73  TRP   A CZ2   1 
ATOM   602  C  CZ3   . TRP   A 1 97  ? 159.222 152.221 150.877 1.00 41.07  ? 73  TRP   A CZ3   1 
ATOM   603  C  CH2   . TRP   A 1 97  ? 160.262 151.384 151.293 1.00 42.03  ? 73  TRP   A CH2   1 
ATOM   604  N  N     . LEU   A 1 98  ? 158.687 156.888 148.392 1.00 36.94  ? 74  LEU   A N     1 
ATOM   605  C  CA    . LEU   A 1 98  ? 157.970 156.261 147.285 1.00 34.91  ? 74  LEU   A CA    1 
ATOM   606  C  C     . LEU   A 1 98  ? 158.377 156.863 145.945 1.00 44.73  ? 74  LEU   A C     1 
ATOM   607  O  O     . LEU   A 1 98  ? 158.453 156.152 144.936 1.00 52.37  ? 74  LEU   A O     1 
ATOM   608  C  CB    . LEU   A 1 98  ? 156.463 156.397 147.498 1.00 37.44  ? 74  LEU   A CB    1 
ATOM   609  C  CG    . LEU   A 1 98  ? 155.560 155.855 146.390 1.00 42.84  ? 74  LEU   A CG    1 
ATOM   610  C  CD1   . LEU   A 1 98  ? 155.240 154.391 146.624 1.00 46.32  ? 74  LEU   A CD1   1 
ATOM   611  C  CD2   . LEU   A 1 98  ? 154.288 156.675 146.295 1.00 43.29  ? 74  LEU   A CD2   1 
ATOM   612  N  N     . LEU   A 1 99  ? 158.628 158.175 145.914 1.00 44.17  ? 75  LEU   A N     1 
ATOM   613  C  CA    . LEU   A 1 99  ? 158.994 158.844 144.671 1.00 41.94  ? 75  LEU   A CA    1 
ATOM   614  C  C     . LEU   A 1 99  ? 160.295 158.304 144.096 1.00 42.24  ? 75  LEU   A C     1 
ATOM   615  O  O     . LEU   A 1 99  ? 160.398 158.114 142.880 1.00 47.94  ? 75  LEU   A O     1 
ATOM   616  C  CB    . LEU   A 1 99  ? 159.108 160.350 144.910 1.00 48.90  ? 75  LEU   A CB    1 
ATOM   617  C  CG    . LEU   A 1 99  ? 158.601 161.284 143.813 1.00 52.93  ? 75  LEU   A CG    1 
ATOM   618  C  CD1   . LEU   A 1 99  ? 157.086 161.338 143.819 1.00 48.06  ? 75  LEU   A CD1   1 
ATOM   619  C  CD2   . LEU   A 1 99  ? 159.188 162.674 143.995 1.00 50.15  ? 75  LEU   A CD2   1 
ATOM   620  N  N     . VAL   A 1 100 ? 161.295 158.064 144.943 1.00 36.15  ? 76  VAL   A N     1 
ATOM   621  C  CA    . VAL   A 1 100 ? 162.578 157.570 144.451 1.00 33.66  ? 76  VAL   A CA    1 
ATOM   622  C  C     . VAL   A 1 100 ? 162.447 156.143 143.927 1.00 41.22  ? 76  VAL   A C     1 
ATOM   623  O  O     . VAL   A 1 100 ? 163.057 155.779 142.916 1.00 46.36  ? 76  VAL   A O     1 
ATOM   624  C  CB    . VAL   A 1 100 ? 163.649 157.678 145.553 1.00 36.32  ? 76  VAL   A CB    1 
ATOM   625  C  CG1   . VAL   A 1 100 ? 164.917 156.957 145.140 1.00 37.21  ? 76  VAL   A CG1   1 
ATOM   626  C  CG2   . VAL   A 1 100 ? 163.944 159.135 145.855 1.00 32.67  ? 76  VAL   A CG2   1 
ATOM   627  N  N     . GLY   A 1 101 ? 161.641 155.317 144.597 1.00 46.03  ? 77  GLY   A N     1 
ATOM   628  C  CA    . GLY   A 1 101 ? 161.558 153.913 144.220 1.00 34.09  ? 77  GLY   A CA    1 
ATOM   629  C  C     . GLY   A 1 101 ? 160.623 153.649 143.053 1.00 40.49  ? 77  GLY   A C     1 
ATOM   630  O  O     . GLY   A 1 101 ? 160.754 152.637 142.362 1.00 44.86  ? 77  GLY   A O     1 
ATOM   631  N  N     . ILE   A 1 102 ? 159.665 154.548 142.819 1.00 49.83  ? 78  ILE   A N     1 
ATOM   632  C  CA    . ILE   A 1 102 ? 158.661 154.303 141.786 1.00 46.65  ? 78  ILE   A CA    1 
ATOM   633  C  C     . ILE   A 1 102 ? 159.147 154.731 140.406 1.00 51.52  ? 78  ILE   A C     1 
ATOM   634  O  O     . ILE   A 1 102 ? 158.499 154.436 139.395 1.00 51.77  ? 78  ILE   A O     1 
ATOM   635  C  CB    . ILE   A 1 102 ? 157.346 155.017 142.160 1.00 46.93  ? 78  ILE   A CB    1 
ATOM   636  C  CG1   . ILE   A 1 102 ? 156.136 154.281 141.581 1.00 47.08  ? 78  ILE   A CG1   1 
ATOM   637  C  CG2   . ILE   A 1 102 ? 157.376 156.460 141.700 1.00 52.90  ? 78  ILE   A CG2   1 
ATOM   638  C  CD1   . ILE   A 1 102 ? 155.569 153.219 142.478 1.00 53.10  ? 78  ILE   A CD1   1 
ATOM   639  N  N     . SER   A 1 103 ? 160.282 155.430 140.334 1.00 50.14  ? 79  SER   A N     1 
ATOM   640  C  CA    . SER   A 1 103 ? 160.682 156.063 139.078 1.00 55.75  ? 79  SER   A CA    1 
ATOM   641  C  C     . SER   A 1 103 ? 161.003 155.038 137.993 1.00 62.21  ? 79  SER   A C     1 
ATOM   642  O  O     . SER   A 1 103 ? 160.638 155.227 136.827 1.00 67.20  ? 79  SER   A O     1 
ATOM   643  C  CB    . SER   A 1 103 ? 161.876 156.987 139.315 1.00 55.65  ? 79  SER   A CB    1 
ATOM   644  O  OG    . SER   A 1 103 ? 162.889 156.339 140.060 1.00 54.53  ? 79  SER   A OG    1 
ATOM   645  N  N     . MET   A 1 104 ? 161.687 153.949 138.351 1.00 51.19  ? 80  MET   A N     1 
ATOM   646  C  CA    . MET   A 1 104 ? 162.177 153.022 137.334 1.00 47.23  ? 80  MET   A CA    1 
ATOM   647  C  C     . MET   A 1 104 ? 161.092 152.050 136.884 1.00 54.28  ? 80  MET   A C     1 
ATOM   648  O  O     . MET   A 1 104 ? 161.231 151.393 135.842 1.00 54.27  ? 80  MET   A O     1 
ATOM   649  C  CB    . MET   A 1 104 ? 163.379 152.247 137.872 1.00 46.00  ? 80  MET   A CB    1 
ATOM   650  C  CG    . MET   A 1 104 ? 163.048 151.371 139.069 1.00 45.52  ? 80  MET   A CG    1 
ATOM   651  S  SD    . MET   A 1 104 ? 164.143 151.621 140.474 1.00 69.36  ? 80  MET   A SD    1 
ATOM   652  C  CE    . MET   A 1 104 ? 164.007 153.388 140.700 1.00 49.06  ? 80  MET   A CE    1 
ATOM   653  N  N     . TRP   A 1 105 ? 160.017 151.925 137.668 1.00 44.89  ? 81  TRP   A N     1 
ATOM   654  C  CA    . TRP   A 1 105 ? 159.040 150.869 137.431 1.00 33.67  ? 81  TRP   A CA    1 
ATOM   655  C  C     . TRP   A 1 105 ? 158.311 151.058 136.108 1.00 40.92  ? 81  TRP   A C     1 
ATOM   656  O  O     . TRP   A 1 105 ? 158.072 150.095 135.376 1.00 47.66  ? 81  TRP   A O     1 
ATOM   657  C  CB    . TRP   A 1 105 ? 158.033 150.796 138.577 1.00 44.56  ? 81  TRP   A CB    1 
ATOM   658  C  CG    . TRP   A 1 105 ? 156.968 149.775 138.310 1.00 44.27  ? 81  TRP   A CG    1 
ATOM   659  C  CD1   . TRP   A 1 105 ? 155.627 149.998 138.205 1.00 33.87  ? 81  TRP   A CD1   1 
ATOM   660  C  CD2   . TRP   A 1 105 ? 157.160 148.372 138.087 1.00 46.07  ? 81  TRP   A CD2   1 
ATOM   661  N  NE1   . TRP   A 1 105 ? 154.971 148.822 137.941 1.00 36.84  ? 81  TRP   A NE1   1 
ATOM   662  C  CE2   . TRP   A 1 105 ? 155.890 147.809 137.864 1.00 41.46  ? 81  TRP   A CE2   1 
ATOM   663  C  CE3   . TRP   A 1 105 ? 158.282 147.538 138.061 1.00 42.81  ? 81  TRP   A CE3   1 
ATOM   664  C  CZ2   . TRP   A 1 105 ? 155.711 146.451 137.616 1.00 37.13  ? 81  TRP   A CZ2   1 
ATOM   665  C  CZ3   . TRP   A 1 105 ? 158.102 146.192 137.816 1.00 38.37  ? 81  TRP   A CZ3   1 
ATOM   666  C  CH2   . TRP   A 1 105 ? 156.827 145.662 137.597 1.00 43.13  ? 81  TRP   A CH2   1 
ATOM   667  N  N     . PHE   A 1 106 ? 157.917 152.294 135.803 1.00 54.59  ? 82  PHE   A N     1 
ATOM   668  C  CA    . PHE   A 1 106 ? 157.190 152.534 134.562 1.00 54.81  ? 82  PHE   A CA    1 
ATOM   669  C  C     . PHE   A 1 106 ? 158.048 152.191 133.353 1.00 54.48  ? 82  PHE   A C     1 
ATOM   670  O  O     . PHE   A 1 106 ? 157.581 151.530 132.417 1.00 55.07  ? 82  PHE   A O     1 
ATOM   671  C  CB    . PHE   A 1 106 ? 156.715 153.985 134.505 1.00 50.51  ? 82  PHE   A CB    1 
ATOM   672  C  CG    . PHE   A 1 106 ? 155.998 154.432 135.745 1.00 52.90  ? 82  PHE   A CG    1 
ATOM   673  C  CD1   . PHE   A 1 106 ? 154.697 154.026 135.991 1.00 51.66  ? 82  PHE   A CD1   1 
ATOM   674  C  CD2   . PHE   A 1 106 ? 156.624 155.251 136.668 1.00 53.06  ? 82  PHE   A CD2   1 
ATOM   675  C  CE1   . PHE   A 1 106 ? 154.035 154.431 137.131 1.00 48.37  ? 82  PHE   A CE1   1 
ATOM   676  C  CE2   . PHE   A 1 106 ? 155.965 155.659 137.810 1.00 56.21  ? 82  PHE   A CE2   1 
ATOM   677  C  CZ    . PHE   A 1 106 ? 154.668 155.248 138.041 1.00 56.55  ? 82  PHE   A CZ    1 
ATOM   678  N  N     . PHE   A 1 107 ? 159.318 152.603 133.371 1.00 49.02  ? 83  PHE   A N     1 
ATOM   679  C  CA    . PHE   A 1 107 ? 160.222 152.264 132.278 1.00 38.73  ? 83  PHE   A CA    1 
ATOM   680  C  C     . PHE   A 1 107 ? 160.387 150.757 132.146 1.00 43.27  ? 83  PHE   A C     1 
ATOM   681  O  O     . PHE   A 1 107 ? 160.284 150.213 131.042 1.00 40.96  ? 83  PHE   A O     1 
ATOM   682  C  CB    . PHE   A 1 107 ? 161.579 152.936 132.490 1.00 37.47  ? 83  PHE   A CB    1 
ATOM   683  C  CG    . PHE   A 1 107 ? 162.709 152.272 131.753 1.00 45.26  ? 83  PHE   A CG    1 
ATOM   684  C  CD1   . PHE   A 1 107 ? 162.716 152.215 130.370 1.00 50.75  ? 83  PHE   A CD1   1 
ATOM   685  C  CD2   . PHE   A 1 107 ? 163.767 151.708 132.444 1.00 46.84  ? 83  PHE   A CD2   1 
ATOM   686  C  CE1   . PHE   A 1 107 ? 163.752 151.605 129.693 1.00 39.87  ? 83  PHE   A CE1   1 
ATOM   687  C  CE2   . PHE   A 1 107 ? 164.805 151.098 131.771 1.00 44.56  ? 83  PHE   A CE2   1 
ATOM   688  C  CZ    . PHE   A 1 107 ? 164.797 151.046 130.394 1.00 40.34  ? 83  PHE   A CZ    1 
ATOM   689  N  N     . ILE   A 1 108 ? 160.624 150.061 133.262 1.00 47.12  ? 84  ILE   A N     1 
ATOM   690  C  CA    . ILE   A 1 108 ? 160.855 148.619 133.194 1.00 42.10  ? 84  ILE   A CA    1 
ATOM   691  C  C     . ILE   A 1 108 ? 159.618 147.901 132.668 1.00 45.06  ? 84  ILE   A C     1 
ATOM   692  O  O     . ILE   A 1 108 ? 159.700 147.075 131.748 1.00 54.84  ? 84  ILE   A O     1 
ATOM   693  C  CB    . ILE   A 1 108 ? 161.277 148.076 134.571 1.00 40.99  ? 84  ILE   A CB    1 
ATOM   694  C  CG1   . ILE   A 1 108 ? 162.658 148.608 134.955 1.00 42.60  ? 84  ILE   A CG1   1 
ATOM   695  C  CG2   . ILE   A 1 108 ? 161.270 146.558 134.570 1.00 44.43  ? 84  ILE   A CG2   1 
ATOM   696  C  CD1   . ILE   A 1 108 ? 163.177 148.062 136.264 1.00 43.13  ? 84  ILE   A CD1   1 
ATOM   697  N  N     . ASN   A 1 109 ? 158.452 148.217 133.236 1.00 50.17  ? 85  ASN   A N     1 
ATOM   698  C  CA    . ASN   A 1 109 ? 157.212 147.564 132.836 1.00 51.55  ? 85  ASN   A CA    1 
ATOM   699  C  C     . ASN   A 1 109 ? 156.902 147.815 131.367 1.00 60.07  ? 85  ASN   A C     1 
ATOM   700  O  O     . ASN   A 1 109 ? 156.618 146.876 130.615 1.00 60.11  ? 85  ASN   A O     1 
ATOM   701  C  CB    . ASN   A 1 109 ? 156.067 148.055 133.723 1.00 51.07  ? 85  ASN   A CB    1 
ATOM   702  C  CG    . ASN   A 1 109 ? 154.763 147.342 133.444 1.00 60.80  ? 85  ASN   A CG    1 
ATOM   703  O  OD1   . ASN   A 1 109 ? 154.715 146.117 133.374 1.00 65.30  ? 85  ASN   A OD1   1 
ATOM   704  N  ND2   . ASN   A 1 109 ? 153.691 148.110 133.293 1.00 57.62  ? 85  ASN   A ND2   1 
ATOM   705  N  N     . GLN   A 1 110 ? 156.955 149.080 130.936 1.00 66.11  ? 86  GLN   A N     1 
ATOM   706  C  CA    . GLN   A 1 110 ? 156.629 149.398 129.551 1.00 56.08  ? 86  GLN   A CA    1 
ATOM   707  C  C     . GLN   A 1 110 ? 157.621 148.764 128.585 1.00 62.46  ? 86  GLN   A C     1 
ATOM   708  O  O     . GLN   A 1 110 ? 157.219 148.223 127.549 1.00 68.85  ? 86  GLN   A O     1 
ATOM   709  C  CB    . GLN   A 1 110 ? 156.582 150.912 129.359 1.00 56.96  ? 86  GLN   A CB    1 
ATOM   710  C  CG    . GLN   A 1 110 ? 155.241 151.534 129.705 1.00 62.06  ? 86  GLN   A CG    1 
ATOM   711  C  CD    . GLN   A 1 110 ? 155.317 153.041 129.841 1.00 69.12  ? 86  GLN   A CD    1 
ATOM   712  O  OE1   . GLN   A 1 110 ? 156.398 153.626 129.799 1.00 71.11  ? 86  GLN   A OE1   1 
ATOM   713  N  NE2   . GLN   A 1 110 ? 154.164 153.678 130.006 1.00 67.19  ? 86  GLN   A NE2   1 
ATOM   714  N  N     . GLY   A 1 111 ? 158.917 148.815 128.901 1.00 57.62  ? 87  GLY   A N     1 
ATOM   715  C  CA    . GLY   A 1 111 ? 159.901 148.216 128.019 1.00 55.65  ? 87  GLY   A CA    1 
ATOM   716  C  C     . GLY   A 1 111 ? 159.720 146.719 127.873 1.00 58.21  ? 87  GLY   A C     1 
ATOM   717  O  O     . GLY   A 1 111 ? 159.762 146.189 126.760 1.00 62.99  ? 87  GLY   A O     1 
ATOM   718  N  N     . ILE   A 1 112 ? 159.495 146.018 128.987 1.00 58.39  ? 88  ILE   A N     1 
ATOM   719  C  CA    . ILE   A 1 112 ? 159.326 144.571 128.909 1.00 56.77  ? 88  ILE   A CA    1 
ATOM   720  C  C     . ILE   A 1 112 ? 158.027 144.218 128.193 1.00 57.70  ? 88  ILE   A C     1 
ATOM   721  O  O     . ILE   A 1 112 ? 157.971 143.250 127.426 1.00 60.45  ? 88  ILE   A O     1 
ATOM   722  C  CB    . ILE   A 1 112 ? 159.400 143.945 130.314 1.00 59.05  ? 88  ILE   A CB    1 
ATOM   723  C  CG1   . ILE   A 1 112 ? 160.814 144.084 130.878 1.00 53.91  ? 88  ILE   A CG1   1 
ATOM   724  C  CG2   . ILE   A 1 112 ? 159.000 142.480 130.273 1.00 58.06  ? 88  ILE   A CG2   1 
ATOM   725  C  CD1   . ILE   A 1 112 ? 160.985 143.493 132.255 1.00 54.16  ? 88  ILE   A CD1   1 
ATOM   726  N  N     . LEU   A 1 113 ? 156.966 144.999 128.415 1.00 61.75  ? 89  LEU   A N     1 
ATOM   727  C  CA    . LEU   A 1 113 ? 155.685 144.682 127.791 1.00 64.65  ? 89  LEU   A CA    1 
ATOM   728  C  C     . LEU   A 1 113 ? 155.694 144.947 126.290 1.00 66.59  ? 89  LEU   A C     1 
ATOM   729  O  O     . LEU   A 1 113 ? 155.134 144.155 125.524 1.00 68.64  ? 89  LEU   A O     1 
ATOM   730  C  CB    . LEU   A 1 113 ? 154.563 145.476 128.458 1.00 66.63  ? 89  LEU   A CB    1 
ATOM   731  C  CG    . LEU   A 1 113 ? 153.972 144.875 129.735 1.00 65.66  ? 89  LEU   A CG    1 
ATOM   732  C  CD1   . LEU   A 1 113 ? 152.780 145.691 130.204 1.00 64.53  ? 89  LEU   A CD1   1 
ATOM   733  C  CD2   . LEU   A 1 113 ? 153.579 143.424 129.516 1.00 66.23  ? 89  LEU   A CD2   1 
ATOM   734  N  N     . GLU   A 1 114 ? 156.312 146.042 125.846 1.00 77.48  ? 90  GLU   A N     1 
ATOM   735  C  CA    . GLU   A 1 114 ? 156.296 146.386 124.430 1.00 75.85  ? 90  GLU   A CA    1 
ATOM   736  C  C     . GLU   A 1 114 ? 157.399 145.704 123.632 1.00 79.36  ? 90  GLU   A C     1 
ATOM   737  O  O     . GLU   A 1 114 ? 157.236 145.498 122.425 1.00 80.42  ? 90  GLU   A O     1 
ATOM   738  C  CB    . GLU   A 1 114 ? 156.403 147.903 124.252 1.00 72.63  ? 90  GLU   A CB    1 
ATOM   739  C  CG    . GLU   A 1 114 ? 155.376 148.690 125.045 1.00 73.95  ? 90  GLU   A CG    1 
ATOM   740  C  CD    . GLU   A 1 114 ? 155.339 150.153 124.656 1.00 82.44  ? 90  GLU   A CD    1 
ATOM   741  O  OE1   . GLU   A 1 114 ? 156.324 150.634 124.058 1.00 82.29  ? 90  GLU   A OE1   1 
ATOM   742  O  OE2   . GLU   A 1 114 ? 154.327 150.823 124.949 1.00 82.74  ? 90  GLU   A OE2   1 
ATOM   743  N  N     . GLY   A 1 115 ? 158.519 145.347 124.268 1.00 67.56  ? 91  GLY   A N     1 
ATOM   744  C  CA    . GLY   A 1 115 ? 159.578 144.662 123.551 1.00 57.07  ? 91  GLY   A CA    1 
ATOM   745  C  C     . GLY   A 1 115 ? 159.276 143.219 123.214 1.00 62.42  ? 91  GLY   A C     1 
ATOM   746  O  O     . GLY   A 1 115 ? 159.905 142.662 122.309 1.00 68.53  ? 91  GLY   A O     1 
ATOM   747  N  N     . THR   A 1 116 ? 158.329 142.601 123.921 1.00 62.46  ? 92  THR   A N     1 
ATOM   748  C  CA    . THR   A 1 116 ? 157.961 141.221 123.624 1.00 61.57  ? 92  THR   A CA    1 
ATOM   749  C  C     . THR   A 1 116 ? 157.197 141.114 122.309 1.00 64.41  ? 92  THR   A C     1 
ATOM   750  O  O     . THR   A 1 116 ? 157.236 140.068 121.653 1.00 68.54  ? 92  THR   A O     1 
ATOM   751  C  CB    . THR   A 1 116 ? 157.131 140.645 124.773 1.00 61.32  ? 92  THR   A CB    1 
ATOM   752  O  OG1   . THR   A 1 116 ? 157.769 140.947 126.019 1.00 68.60  ? 92  THR   A OG1   1 
ATOM   753  C  CG2   . THR   A 1 116 ? 156.992 139.138 124.640 1.00 60.74  ? 92  THR   A CG2   1 
ATOM   754  N  N     . LYS   A 1 117 ? 156.510 142.180 121.906 1.00 79.90  ? 93  LYS   A N     1 
ATOM   755  C  CA    . LYS   A 1 117 ? 155.725 142.196 120.681 1.00 77.55  ? 93  LYS   A CA    1 
ATOM   756  C  C     . LYS   A 1 117 ? 156.393 142.985 119.562 1.00 80.62  ? 93  LYS   A C     1 
ATOM   757  O  O     . LYS   A 1 117 ? 155.748 143.264 118.547 1.00 86.01  ? 93  LYS   A O     1 
ATOM   758  C  CB    . LYS   A 1 117 ? 154.334 142.768 120.961 1.00 79.39  ? 93  LYS   A CB    1 
ATOM   759  C  CG    . LYS   A 1 117 ? 153.833 142.509 122.372 1.00 82.11  ? 93  LYS   A CG    1 
ATOM   760  C  CD    . LYS   A 1 117 ? 152.434 143.065 122.582 1.00 81.54  ? 93  LYS   A CD    1 
ATOM   761  C  CE    . LYS   A 1 117 ? 152.299 144.463 122.000 1.00 82.16  ? 93  LYS   A CE    1 
ATOM   762  N  NZ    . LYS   A 1 117 ? 151.198 145.229 122.646 1.00 83.58  ? 93  LYS   A NZ    1 
ATOM   763  N  N     . ALA   A 1 118 ? 157.665 143.353 119.723 1.00 82.52  ? 94  ALA   A N     1 
ATOM   764  C  CA    . ALA   A 1 118 ? 158.323 144.201 118.733 1.00 83.68  ? 94  ALA   A CA    1 
ATOM   765  C  C     . ALA   A 1 118 ? 158.529 143.464 117.415 1.00 85.35  ? 94  ALA   A C     1 
ATOM   766  O  O     . ALA   A 1 118 ? 158.214 143.992 116.342 1.00 87.21  ? 94  ALA   A O     1 
ATOM   767  C  CB    . ALA   A 1 118 ? 159.656 144.709 119.280 1.00 82.97  ? 94  ALA   A CB    1 
ATOM   768  N  N     . ILE   A 1 119 ? 159.066 142.244 117.473 1.00 88.87  ? 95  ILE   A N     1 
ATOM   769  C  CA    . ILE   A 1 119 ? 159.324 141.493 116.248 1.00 90.76  ? 95  ILE   A CA    1 
ATOM   770  C  C     . ILE   A 1 119 ? 158.017 141.042 115.607 1.00 89.19  ? 95  ILE   A C     1 
ATOM   771  O  O     . ILE   A 1 119 ? 157.845 141.135 114.386 1.00 87.61  ? 95  ILE   A O     1 
ATOM   772  C  CB    . ILE   A 1 119 ? 160.258 140.304 116.537 1.00 89.22  ? 95  ILE   A CB    1 
ATOM   773  C  CG1   . ILE   A 1 119 ? 161.677 140.801 116.819 1.00 89.62  ? 95  ILE   A CG1   1 
ATOM   774  C  CG2   . ILE   A 1 119 ? 160.257 139.321 115.376 1.00 86.21  ? 95  ILE   A CG2   1 
ATOM   775  C  CD1   . ILE   A 1 119 ? 162.718 139.705 116.845 1.00 89.69  ? 95  ILE   A CD1   1 
ATOM   776  N  N     . THR   A 1 120 ? 157.074 140.555 116.417 1.00 92.03  ? 96  THR   A N     1 
ATOM   777  C  CA    . THR   A 1 120 ? 155.818 140.042 115.880 1.00 90.29  ? 96  THR   A CA    1 
ATOM   778  C  C     . THR   A 1 120 ? 155.029 141.128 115.158 1.00 93.77  ? 96  THR   A C     1 
ATOM   779  O  O     . THR   A 1 120 ? 154.492 140.896 114.068 1.00 95.74  ? 96  THR   A O     1 
ATOM   780  C  CB    . THR   A 1 120 ? 154.980 139.437 117.006 1.00 90.38  ? 96  THR   A CB    1 
ATOM   781  O  OG1   . THR   A 1 120 ? 155.673 138.319 117.575 1.00 90.88  ? 96  THR   A OG1   1 
ATOM   782  C  CG2   . THR   A 1 120 ? 153.630 138.980 116.484 1.00 90.51  ? 96  THR   A CG2   1 
ATOM   783  N  N     . GLN   A 1 121 ? 154.950 142.322 115.746 1.00 102.74 ? 97  GLN   A N     1 
ATOM   784  C  CA    . GLN   A 1 121 ? 154.135 143.384 115.167 1.00 101.01 ? 97  GLN   A CA    1 
ATOM   785  C  C     . GLN   A 1 121 ? 154.789 144.004 113.937 1.00 104.17 ? 97  GLN   A C     1 
ATOM   786  O  O     . GLN   A 1 121 ? 154.105 144.294 112.949 1.00 107.23 ? 97  GLN   A O     1 
ATOM   787  C  CB    . GLN   A 1 121 ? 153.861 144.461 116.217 1.00 99.16  ? 97  GLN   A CB    1 
ATOM   788  C  CG    . GLN   A 1 121 ? 152.754 144.106 117.192 1.00 102.41 ? 97  GLN   A CG    1 
ATOM   789  C  CD    . GLN   A 1 121 ? 152.289 145.300 118.000 1.00 104.51 ? 97  GLN   A CD    1 
ATOM   790  O  OE1   . GLN   A 1 121 ? 152.926 146.353 117.995 1.00 105.12 ? 97  GLN   A OE1   1 
ATOM   791  N  NE2   . GLN   A 1 121 ? 151.173 145.141 118.701 1.00 102.13 ? 97  GLN   A NE2   1 
ATOM   792  N  N     . LYS   A 1 122 ? 156.101 144.216 113.977 1.00 102.40 ? 98  LYS   A N     1 
ATOM   793  C  CA    . LYS   A 1 122 ? 156.814 144.978 112.957 1.00 104.29 ? 98  LYS   A CA    1 
ATOM   794  C  C     . LYS   A 1 122 ? 157.751 144.102 112.130 1.00 105.93 ? 98  LYS   A C     1 
ATOM   795  O  O     . LYS   A 1 122 ? 158.870 144.502 111.809 1.00 105.00 ? 98  LYS   A O     1 
ATOM   796  C  CB    . LYS   A 1 122 ? 157.592 146.125 113.597 1.00 102.11 ? 98  LYS   A CB    1 
ATOM   797  C  CG    . LYS   A 1 122 ? 156.875 146.772 114.771 1.00 103.69 ? 98  LYS   A CG    1 
ATOM   798  C  CD    . LYS   A 1 122 ? 157.808 147.665 115.574 1.00 102.64 ? 98  LYS   A CD    1 
ATOM   799  C  CE    . LYS   A 1 122 ? 158.634 148.563 114.670 1.00 100.50 ? 98  LYS   A CE    1 
ATOM   800  N  NZ    . LYS   A 1 122 ? 157.982 149.885 114.463 1.00 99.39  ? 98  LYS   A NZ    1 
ATOM   801  N  N     . PHE   A 1 123 ? 157.311 142.893 111.776 1.00 110.26 ? 99  PHE   A N     1 
ATOM   802  C  CA    . PHE   A 1 123 ? 158.167 142.009 110.991 1.00 110.93 ? 99  PHE   A CA    1 
ATOM   803  C  C     . PHE   A 1 123 ? 158.098 142.323 109.501 1.00 112.94 ? 99  PHE   A C     1 
ATOM   804  O  O     . PHE   A 1 123 ? 159.137 142.411 108.837 1.00 113.04 ? 99  PHE   A O     1 
ATOM   805  C  CB    . PHE   A 1 123 ? 157.790 140.549 111.236 1.00 111.38 ? 99  PHE   A CB    1 
ATOM   806  C  CG    . PHE   A 1 123 ? 158.772 139.567 110.663 1.00 112.17 ? 99  PHE   A CG    1 
ATOM   807  C  CD1   . PHE   A 1 123 ? 160.125 139.860 110.629 1.00 111.64 ? 99  PHE   A CD1   1 
ATOM   808  C  CD2   . PHE   A 1 123 ? 158.342 138.353 110.154 1.00 110.71 ? 99  PHE   A CD2   1 
ATOM   809  C  CE1   . PHE   A 1 123 ? 161.030 138.961 110.101 1.00 112.57 ? 99  PHE   A CE1   1 
ATOM   810  C  CE2   . PHE   A 1 123 ? 159.243 137.449 109.625 1.00 111.18 ? 99  PHE   A CE2   1 
ATOM   811  C  CZ    . PHE   A 1 123 ? 160.588 137.753 109.598 1.00 112.62 ? 99  PHE   A CZ    1 
ATOM   812  N  N     . ASN   A 1 124 ? 156.889 142.489 108.958 1.00 116.19 ? 100 ASN   A N     1 
ATOM   813  C  CA    . ASN   A 1 124 ? 156.740 142.677 107.518 1.00 115.63 ? 100 ASN   A CA    1 
ATOM   814  C  C     . ASN   A 1 124 ? 157.394 143.965 107.037 1.00 114.72 ? 100 ASN   A C     1 
ATOM   815  O  O     . ASN   A 1 124 ? 158.019 143.978 105.971 1.00 116.80 ? 100 ASN   A O     1 
ATOM   816  C  CB    . ASN   A 1 124 ? 155.260 142.660 107.136 1.00 115.71 ? 100 ASN   A CB    1 
ATOM   817  C  CG    . ASN   A 1 124 ? 154.634 141.289 107.291 1.00 116.93 ? 100 ASN   A CG    1 
ATOM   818  O  OD1   . ASN   A 1 124 ? 155.335 140.280 107.375 1.00 115.34 ? 100 ASN   A OD1   1 
ATOM   819  N  ND2   . ASN   A 1 124 ? 153.307 141.245 107.331 1.00 116.76 ? 100 ASN   A ND2   1 
ATOM   820  N  N     . GLN   A 1 125 ? 157.266 145.052 107.798 1.00 114.32 ? 101 GLN   A N     1 
ATOM   821  C  CA    . GLN   A 1 125 ? 157.859 146.322 107.398 1.00 115.54 ? 101 GLN   A CA    1 
ATOM   822  C  C     . GLN   A 1 125 ? 159.380 146.307 107.463 1.00 116.44 ? 101 GLN   A C     1 
ATOM   823  O  O     . GLN   A 1 125 ? 160.020 147.158 106.836 1.00 115.34 ? 101 GLN   A O     1 
ATOM   824  C  CB    . GLN   A 1 125 ? 157.332 147.481 108.258 1.00 114.95 ? 101 GLN   A CB    1 
ATOM   825  C  CG    . GLN   A 1 125 ? 155.813 147.735 108.244 1.00 114.53 ? 101 GLN   A CG    1 
ATOM   826  C  CD    . GLN   A 1 125 ? 154.968 146.524 108.586 1.00 115.45 ? 101 GLN   A CD    1 
ATOM   827  O  OE1   . GLN   A 1 125 ? 154.579 145.757 107.705 1.00 114.07 ? 101 GLN   A OE1   1 
ATOM   828  N  NE2   . GLN   A 1 125 ? 154.674 146.349 109.868 1.00 115.65 ? 101 GLN   A NE2   1 
ATOM   829  N  N     . VAL   A 1 126 ? 159.972 145.368 108.200 1.00 110.05 ? 102 VAL   A N     1 
ATOM   830  C  CA    . VAL   A 1 126 ? 161.423 145.286 108.327 1.00 111.29 ? 102 VAL   A CA    1 
ATOM   831  C  C     . VAL   A 1 126 ? 162.011 144.070 107.631 1.00 111.45 ? 102 VAL   A C     1 
ATOM   832  O  O     . VAL   A 1 126 ? 163.240 144.013 107.461 1.00 110.71 ? 102 VAL   A O     1 
ATOM   833  C  CB    . VAL   A 1 126 ? 161.865 145.300 109.805 1.00 109.68 ? 102 VAL   A CB    1 
ATOM   834  C  CG1   . VAL   A 1 126 ? 161.129 146.389 110.571 1.00 107.44 ? 102 VAL   A CG1   1 
ATOM   835  C  CG2   . VAL   A 1 126 ? 161.641 143.936 110.431 1.00 107.12 ? 102 VAL   A CG2   1 
ATOM   836  N  N     . SER   A 1 127 ? 161.191 143.092 107.239 1.00 106.33 ? 103 SER   A N     1 
ATOM   837  C  CA    . SER   A 1 127 ? 161.719 141.957 106.490 1.00 104.80 ? 103 SER   A CA    1 
ATOM   838  C  C     . SER   A 1 127 ? 162.282 142.406 105.149 1.00 105.28 ? 103 SER   A C     1 
ATOM   839  O  O     . SER   A 1 127 ? 163.343 141.934 104.723 1.00 103.71 ? 103 SER   A O     1 
ATOM   840  C  CB    . SER   A 1 127 ? 160.633 140.900 106.293 1.00 102.74 ? 103 SER   A CB    1 
ATOM   841  O  OG    . SER   A 1 127 ? 159.613 141.368 105.428 1.00 106.35 ? 103 SER   A OG    1 
ATOM   842  N  N     . LYS   A 1 128 ? 161.585 143.320 104.471 1.00 112.49 ? 104 LYS   A N     1 
ATOM   843  C  CA    . LYS   A 1 128 ? 162.103 143.876 103.227 1.00 112.67 ? 104 LYS   A CA    1 
ATOM   844  C  C     . LYS   A 1 128 ? 163.299 144.784 103.486 1.00 113.63 ? 104 LYS   A C     1 
ATOM   845  O  O     . LYS   A 1 128 ? 164.259 144.792 102.707 1.00 113.23 ? 104 LYS   A O     1 
ATOM   846  C  CB    . LYS   A 1 128 ? 160.997 144.634 102.496 1.00 112.98 ? 104 LYS   A CB    1 
ATOM   847  C  CG    . LYS   A 1 128 ? 159.636 143.961 102.575 1.00 112.97 ? 104 LYS   A CG    1 
ATOM   848  C  CD    . LYS   A 1 128 ? 159.347 143.147 101.326 1.00 114.29 ? 104 LYS   A CD    1 
ATOM   849  C  CE    . LYS   A 1 128 ? 158.019 142.418 101.439 1.00 112.85 ? 104 LYS   A CE    1 
ATOM   850  N  NZ    . LYS   A 1 128 ? 157.107 142.755 100.311 1.00 114.31 ? 104 LYS   A NZ    1 
ATOM   851  N  N     . MET   A 1 129 ? 163.259 145.552 104.571 1.00 123.14 ? 105 MET   A N     1 
ATOM   852  C  CA    . MET   A 1 129 ? 164.352 146.451 104.903 1.00 123.29 ? 105 MET   A CA    1 
ATOM   853  C  C     . MET   A 1 129 ? 165.582 145.658 105.338 1.00 123.81 ? 105 MET   A C     1 
ATOM   854  O  O     . MET   A 1 129 ? 165.490 144.513 105.788 1.00 123.37 ? 105 MET   A O     1 
ATOM   855  C  CB    . MET   A 1 129 ? 163.928 147.423 106.004 1.00 121.07 ? 105 MET   A CB    1 
ATOM   856  C  CG    . MET   A 1 129 ? 162.799 148.354 105.595 1.00 122.93 ? 105 MET   A CG    1 
ATOM   857  S  SD    . MET   A 1 129 ? 162.861 149.954 106.421 1.00 126.56 ? 105 MET   A SD    1 
ATOM   858  C  CE    . MET   A 1 129 ? 162.836 151.060 105.013 1.00 122.05 ? 105 MET   A CE    1 
ATOM   859  N  N     . ASN   A 1 130 ? 166.748 146.283 105.197 1.00 122.69 ? 106 ASN   A N     1 
ATOM   860  C  CA    . ASN   A 1 130 ? 168.030 145.624 105.444 1.00 122.60 ? 106 ASN   A CA    1 
ATOM   861  C  C     . ASN   A 1 130 ? 168.740 146.310 106.608 1.00 120.86 ? 106 ASN   A C     1 
ATOM   862  O  O     . ASN   A 1 130 ? 169.565 147.206 106.416 1.00 120.28 ? 106 ASN   A O     1 
ATOM   863  C  CB    . ASN   A 1 130 ? 168.890 145.632 104.174 1.00 121.87 ? 106 ASN   A CB    1 
ATOM   864  C  CG    . ASN   A 1 130 ? 168.129 145.152 102.954 1.00 121.11 ? 106 ASN   A CG    1 
ATOM   865  O  OD1   . ASN   A 1 130 ? 167.475 145.937 102.268 1.00 122.49 ? 106 ASN   A OD1   1 
ATOM   866  N  ND2   . ASN   A 1 130 ? 168.210 143.856 102.679 1.00 119.83 ? 106 ASN   A ND2   1 
ATOM   867  N  N     . PHE   A 1 131 ? 168.412 145.881 107.818 1.00 104.49 ? 107 PHE   A N     1 
ATOM   868  C  CA    . PHE   A 1 131 ? 169.167 146.200 109.018 1.00 103.67 ? 107 PHE   A CA    1 
ATOM   869  C  C     . PHE   A 1 131 ? 169.056 145.012 109.959 1.00 106.13 ? 107 PHE   A C     1 
ATOM   870  O  O     . PHE   A 1 131 ? 168.139 144.194 109.824 1.00 107.27 ? 107 PHE   A O     1 
ATOM   871  C  CB    . PHE   A 1 131 ? 168.678 147.489 109.698 1.00 104.77 ? 107 PHE   A CB    1 
ATOM   872  C  CG    . PHE   A 1 131 ? 167.196 147.543 109.939 1.00 103.98 ? 107 PHE   A CG    1 
ATOM   873  C  CD1   . PHE   A 1 131 ? 166.625 146.863 111.002 1.00 103.43 ? 107 PHE   A CD1   1 
ATOM   874  C  CD2   . PHE   A 1 131 ? 166.378 148.299 109.119 1.00 104.41 ? 107 PHE   A CD2   1 
ATOM   875  C  CE1   . PHE   A 1 131 ? 165.268 146.920 111.230 1.00 102.68 ? 107 PHE   A CE1   1 
ATOM   876  C  CE2   . PHE   A 1 131 ? 165.018 148.360 109.343 1.00 106.27 ? 107 PHE   A CE2   1 
ATOM   877  C  CZ    . PHE   A 1 131 ? 164.463 147.671 110.400 1.00 106.07 ? 107 PHE   A CZ    1 
ATOM   878  N  N     . PRO   A 1 132 ? 169.988 144.871 110.902 1.00 92.26  ? 108 PRO   A N     1 
ATOM   879  C  CA    . PRO   A 1 132 ? 169.952 143.711 111.802 1.00 89.30  ? 108 PRO   A CA    1 
ATOM   880  C  C     . PRO   A 1 132 ? 168.637 143.616 112.563 1.00 88.09  ? 108 PRO   A C     1 
ATOM   881  O  O     . PRO   A 1 132 ? 168.086 144.618 113.021 1.00 89.72  ? 108 PRO   A O     1 
ATOM   882  C  CB    . PRO   A 1 132 ? 171.128 143.966 112.748 1.00 90.55  ? 108 PRO   A CB    1 
ATOM   883  C  CG    . PRO   A 1 132 ? 172.076 144.774 111.944 1.00 93.39  ? 108 PRO   A CG    1 
ATOM   884  C  CD    . PRO   A 1 132 ? 171.235 145.642 111.051 1.00 89.17  ? 108 PRO   A CD    1 
ATOM   885  N  N     . LEU   A 1 133 ? 168.140 142.386 112.696 1.00 86.08  ? 109 LEU   A N     1 
ATOM   886  C  CA    . LEU   A 1 133 ? 166.885 142.131 113.390 1.00 88.08  ? 109 LEU   A CA    1 
ATOM   887  C  C     . LEU   A 1 133 ? 167.040 142.080 114.903 1.00 88.71  ? 109 LEU   A C     1 
ATOM   888  O  O     . LEU   A 1 133 ? 166.030 142.118 115.614 1.00 87.50  ? 109 LEU   A O     1 
ATOM   889  C  CB    . LEU   A 1 133 ? 166.273 140.817 112.899 1.00 89.56  ? 109 LEU   A CB    1 
ATOM   890  C  CG    . LEU   A 1 133 ? 164.981 140.923 112.088 1.00 90.91  ? 109 LEU   A CG    1 
ATOM   891  C  CD1   . LEU   A 1 133 ? 165.246 141.577 110.741 1.00 88.26  ? 109 LEU   A CD1   1 
ATOM   892  C  CD2   . LEU   A 1 133 ? 164.348 139.553 111.910 1.00 87.28  ? 109 LEU   A CD2   1 
ATOM   893  N  N     . SER   A 1 134 ? 168.269 141.993 115.412 1.00 87.28  ? 110 SER   A N     1 
ATOM   894  C  CA    . SER   A 1 134 ? 168.496 141.936 116.849 1.00 83.02  ? 110 SER   A CA    1 
ATOM   895  C  C     . SER   A 1 134 ? 168.440 143.304 117.513 1.00 83.86  ? 110 SER   A C     1 
ATOM   896  O  O     . SER   A 1 134 ? 168.411 143.373 118.746 1.00 86.24  ? 110 SER   A O     1 
ATOM   897  C  CB    . SER   A 1 134 ? 169.848 141.280 117.140 1.00 81.89  ? 110 SER   A CB    1 
ATOM   898  O  OG    . SER   A 1 134 ? 170.915 142.152 116.818 1.00 81.78  ? 110 SER   A OG    1 
ATOM   899  N  N     . ILE   A 1 135 ? 168.423 144.386 116.735 1.00 72.79  ? 111 ILE   A N     1 
ATOM   900  C  CA    . ILE   A 1 135 ? 168.363 145.735 117.281 1.00 69.43  ? 111 ILE   A CA    1 
ATOM   901  C  C     . ILE   A 1 135 ? 166.943 146.290 117.269 1.00 70.53  ? 111 ILE   A C     1 
ATOM   902  O  O     . ILE   A 1 135 ? 166.733 147.449 117.635 1.00 73.09  ? 111 ILE   A O     1 
ATOM   903  C  CB    . ILE   A 1 135 ? 169.317 146.680 116.533 1.00 71.02  ? 111 ILE   A CB    1 
ATOM   904  C  CG1   . ILE   A 1 135 ? 168.765 147.007 115.145 1.00 71.50  ? 111 ILE   A CG1   1 
ATOM   905  C  CG2   . ILE   A 1 135 ? 170.700 146.063 116.423 1.00 71.11  ? 111 ILE   A CG2   1 
ATOM   906  C  CD1   . ILE   A 1 135 ? 169.326 148.276 114.547 1.00 71.68  ? 111 ILE   A CD1   1 
ATOM   907  N  N     . ILE   A 1 136 ? 165.964 145.490 116.859 1.00 79.02  ? 112 ILE   A N     1 
ATOM   908  C  CA    . ILE   A 1 136 ? 164.580 145.950 116.768 1.00 75.22  ? 112 ILE   A CA    1 
ATOM   909  C  C     . ILE   A 1 136 ? 164.005 146.170 118.166 1.00 77.58  ? 112 ILE   A C     1 
ATOM   910  O  O     . ILE   A 1 136 ? 163.511 147.272 118.442 1.00 80.65  ? 112 ILE   A O     1 
ATOM   911  C  CB    . ILE   A 1 136 ? 163.718 144.977 115.946 1.00 78.79  ? 112 ILE   A CB    1 
ATOM   912  C  CG1   . ILE   A 1 136 ? 163.988 145.157 114.454 1.00 79.74  ? 112 ILE   A CG1   1 
ATOM   913  C  CG2   . ILE   A 1 136 ? 162.242 145.186 116.243 1.00 79.24  ? 112 ILE   A CG2   1 
ATOM   914  C  CD1   . ILE   A 1 136 ? 163.251 144.168 113.594 1.00 79.41  ? 112 ILE   A CD1   1 
ATOM   915  N  N     . PRO   A 1 137 ? 164.020 145.185 119.077 1.00 72.22  ? 113 PRO   A N     1 
ATOM   916  C  CA    . PRO   A 1 137 ? 163.528 145.466 120.435 1.00 67.53  ? 113 PRO   A CA    1 
ATOM   917  C  C     . PRO   A 1 137 ? 164.327 146.532 121.163 1.00 63.11  ? 113 PRO   A C     1 
ATOM   918  O  O     . PRO   A 1 137 ? 163.730 147.328 121.900 1.00 63.57  ? 113 PRO   A O     1 
ATOM   919  C  CB    . PRO   A 1 137 ? 163.639 144.107 121.139 1.00 63.99  ? 113 PRO   A CB    1 
ATOM   920  C  CG    . PRO   A 1 137 ? 164.704 143.400 120.402 1.00 63.39  ? 113 PRO   A CG    1 
ATOM   921  C  CD    . PRO   A 1 137 ? 164.500 143.793 118.974 1.00 67.65  ? 113 PRO   A CD    1 
ATOM   922  N  N     . THR   A 1 138 ? 165.645 146.595 120.950 1.00 65.57  ? 114 THR   A N     1 
ATOM   923  C  CA    . THR   A 1 138 ? 166.492 147.477 121.748 1.00 64.57  ? 114 THR   A CA    1 
ATOM   924  C  C     . THR   A 1 138 ? 166.057 148.931 121.636 1.00 65.53  ? 114 THR   A C     1 
ATOM   925  O  O     . THR   A 1 138 ? 165.813 149.587 122.656 1.00 73.80  ? 114 THR   A O     1 
ATOM   926  C  CB    . THR   A 1 138 ? 167.954 147.325 121.332 1.00 68.67  ? 114 THR   A CB    1 
ATOM   927  O  OG1   . THR   A 1 138 ? 168.337 145.948 121.420 1.00 67.22  ? 114 THR   A OG1   1 
ATOM   928  C  CG2   . THR   A 1 138 ? 168.852 148.154 122.234 1.00 63.22  ? 114 THR   A CG2   1 
ATOM   929  N  N     . TYR   A 1 139 ? 165.924 149.450 120.412 1.00 67.03  ? 115 TYR   A N     1 
ATOM   930  C  CA    . TYR   A 1 139 ? 165.484 150.832 120.278 1.00 70.36  ? 115 TYR   A CA    1 
ATOM   931  C  C     . TYR   A 1 139 ? 164.068 151.030 120.798 1.00 71.78  ? 115 TYR   A C     1 
ATOM   932  O  O     . TYR   A 1 139 ? 163.752 152.123 121.281 1.00 72.33  ? 115 TYR   A O     1 
ATOM   933  C  CB    . TYR   A 1 139 ? 165.612 151.315 118.825 1.00 69.82  ? 115 TYR   A CB    1 
ATOM   934  C  CG    . TYR   A 1 139 ? 164.551 150.849 117.848 1.00 76.97  ? 115 TYR   A CG    1 
ATOM   935  C  CD1   . TYR   A 1 139 ? 164.780 149.767 117.013 1.00 74.58  ? 115 TYR   A CD1   1 
ATOM   936  C  CD2   . TYR   A 1 139 ? 163.342 151.524 117.726 1.00 78.83  ? 115 TYR   A CD2   1 
ATOM   937  C  CE1   . TYR   A 1 139 ? 163.824 149.350 116.108 1.00 72.22  ? 115 TYR   A CE1   1 
ATOM   938  C  CE2   . TYR   A 1 139 ? 162.381 151.110 116.825 1.00 74.04  ? 115 TYR   A CE2   1 
ATOM   939  C  CZ    . TYR   A 1 139 ? 162.628 150.023 116.020 1.00 72.75  ? 115 TYR   A CZ    1 
ATOM   940  O  OH    . TYR   A 1 139 ? 161.676 149.610 115.120 1.00 74.97  ? 115 TYR   A OH    1 
ATOM   941  N  N     . ILE   A 1 140 ? 163.227 149.990 120.752 1.00 57.42  ? 116 ILE   A N     1 
ATOM   942  C  CA    . ILE   A 1 140 ? 161.931 150.067 121.419 1.00 59.11  ? 116 ILE   A CA    1 
ATOM   943  C  C     . ILE   A 1 140 ? 162.124 150.408 122.888 1.00 59.62  ? 116 ILE   A C     1 
ATOM   944  O  O     . ILE   A 1 140 ? 161.505 151.343 123.412 1.00 61.14  ? 116 ILE   A O     1 
ATOM   945  C  CB    . ILE   A 1 140 ? 161.154 148.749 121.243 1.00 62.18  ? 116 ILE   A CB    1 
ATOM   946  C  CG1   . ILE   A 1 140 ? 160.802 148.517 119.771 1.00 59.82  ? 116 ILE   A CG1   1 
ATOM   947  C  CG2   . ILE   A 1 140 ? 159.911 148.743 122.123 1.00 61.18  ? 116 ILE   A CG2   1 
ATOM   948  C  CD1   . ILE   A 1 140 ? 159.422 148.993 119.380 1.00 57.05  ? 116 ILE   A CD1   1 
ATOM   949  N  N     . VAL   A 1 141 ? 163.021 149.687 123.564 1.00 53.55  ? 117 VAL   A N     1 
ATOM   950  C  CA    . VAL   A 1 141 ? 163.351 150.024 124.943 1.00 43.27  ? 117 VAL   A CA    1 
ATOM   951  C  C     . VAL   A 1 141 ? 163.895 151.443 125.020 1.00 50.73  ? 117 VAL   A C     1 
ATOM   952  O  O     . VAL   A 1 141 ? 163.540 152.212 125.922 1.00 60.64  ? 117 VAL   A O     1 
ATOM   953  C  CB    . VAL   A 1 141 ? 164.344 148.998 125.518 1.00 46.36  ? 117 VAL   A CB    1 
ATOM   954  C  CG1   . VAL   A 1 141 ? 164.754 149.385 126.927 1.00 54.82  ? 117 VAL   A CG1   1 
ATOM   955  C  CG2   . VAL   A 1 141 ? 163.735 147.607 125.501 1.00 43.27  ? 117 VAL   A CG2   1 
ATOM   956  N  N     . THR   A 1 142 ? 164.731 151.829 124.052 1.00 46.60  ? 118 THR   A N     1 
ATOM   957  C  CA    . THR   A 1 142 ? 165.285 153.175 124.054 1.00 47.23  ? 118 THR   A CA    1 
ATOM   958  C  C     . THR   A 1 142 ? 164.210 154.237 123.859 1.00 51.75  ? 118 THR   A C     1 
ATOM   959  O  O     . THR   A 1 142 ? 164.444 155.403 124.191 1.00 50.31  ? 118 THR   A O     1 
ATOM   960  C  CB    . THR   A 1 142 ? 166.361 153.307 122.975 1.00 51.52  ? 118 THR   A CB    1 
ATOM   961  O  OG1   . THR   A 1 142 ? 167.089 152.078 122.873 1.00 46.63  ? 118 THR   A OG1   1 
ATOM   962  C  CG2   . THR   A 1 142 ? 167.331 154.424 123.321 1.00 48.36  ? 118 THR   A CG2   1 
ATOM   963  N  N     . SER   A 1 143 ? 163.038 153.849 123.356 1.00 60.57  ? 119 SER   A N     1 
ATOM   964  C  CA    . SER   A 1 143 ? 161.931 154.827 123.200 1.00 60.12  ? 119 SER   A CA    1 
ATOM   965  C  C     . SER   A 1 143 ? 161.380 155.211 124.580 1.00 64.15  ? 119 SER   A C     1 
ATOM   966  O  O     . SER   A 1 143 ? 160.801 156.308 124.698 1.00 66.57  ? 119 SER   A O     1 
ATOM   967  C  CB    . SER   A 1 143 ? 160.848 154.299 122.301 1.00 57.20  ? 119 SER   A CB    1 
ATOM   968  O  OG    . SER   A 1 143 ? 160.002 153.393 122.994 1.00 59.82  ? 119 SER   A OG    1 
ATOM   969  N  N     . ARG   A 1 144 ? 161.554 154.346 125.584 1.00 61.63  ? 120 ARG   A N     1 
ATOM   970  C  CA    . ARG   A 1 144 ? 161.045 154.625 126.919 1.00 56.14  ? 120 ARG   A CA    1 
ATOM   971  C  C     . ARG   A 1 144 ? 162.098 155.199 127.854 1.00 57.13  ? 120 ARG   A C     1 
ATOM   972  O  O     . ARG   A 1 144 ? 161.764 156.059 128.680 1.00 61.05  ? 120 ARG   A O     1 
ATOM   973  C  CB    . ARG   A 1 144 ? 160.454 153.353 127.539 1.00 49.04  ? 120 ARG   A CB    1 
ATOM   974  C  CG    . ARG   A 1 144 ? 159.421 152.669 126.664 1.00 47.26  ? 120 ARG   A CG    1 
ATOM   975  C  CD    . ARG   A 1 144 ? 158.338 153.650 126.254 1.00 56.09  ? 120 ARG   A CD    1 
ATOM   976  N  NE    . ARG   A 1 144 ? 157.024 153.028 126.164 1.00 58.99  ? 120 ARG   A NE    1 
ATOM   977  C  CZ    . ARG   A 1 144 ? 155.880 153.698 126.155 1.00 61.08  ? 120 ARG   A CZ    1 
ATOM   978  N  NH1   . ARG   A 1 144 ? 155.851 155.018 126.243 1.00 55.24  ? 120 ARG   A NH1   1 
ATOM   979  N  NH2   . ARG   A 1 144 ? 154.736 153.028 126.055 1.00 59.53  ? 120 ARG   A NH2   1 
ATOM   980  N  N     . PHE   A 1 145 ? 163.356 154.766 127.719 1.00 46.67  ? 121 PHE   A N     1 
ATOM   981  C  CA    . PHE   A 1 145 ? 164.420 155.234 128.601 1.00 43.98  ? 121 PHE   A CA    1 
ATOM   982  C  C     . PHE   A 1 145 ? 164.457 156.752 128.683 1.00 54.23  ? 121 PHE   A C     1 
ATOM   983  O  O     . PHE   A 1 145 ? 164.541 157.305 129.788 1.00 58.84  ? 121 PHE   A O     1 
ATOM   984  C  CB    . PHE   A 1 145 ? 165.768 154.699 128.117 1.00 45.95  ? 121 PHE   A CB    1 
ATOM   985  C  CG    . PHE   A 1 145 ? 166.855 154.760 129.150 1.00 48.00  ? 121 PHE   A CG    1 
ATOM   986  C  CD1   . PHE   A 1 145 ? 166.633 154.306 130.438 1.00 54.32  ? 121 PHE   A CD1   1 
ATOM   987  C  CD2   . PHE   A 1 145 ? 168.101 155.272 128.831 1.00 47.76  ? 121 PHE   A CD2   1 
ATOM   988  C  CE1   . PHE   A 1 145 ? 167.633 154.361 131.389 1.00 53.31  ? 121 PHE   A CE1   1 
ATOM   989  C  CE2   . PHE   A 1 145 ? 169.105 155.329 129.778 1.00 51.58  ? 121 PHE   A CE2   1 
ATOM   990  C  CZ    . PHE   A 1 145 ? 168.870 154.873 131.058 1.00 55.06  ? 121 PHE   A CZ    1 
ATOM   991  N  N     . TYR   A 1 146 ? 164.370 157.434 127.535 1.00 70.04  ? 122 TYR   A N     1 
ATOM   992  C  CA    . TYR   A 1 146 ? 164.304 158.893 127.520 1.00 65.57  ? 122 TYR   A CA    1 
ATOM   993  C  C     . TYR   A 1 146 ? 163.351 159.408 128.588 1.00 68.93  ? 122 TYR   A C     1 
ATOM   994  O  O     . TYR   A 1 146 ? 163.764 160.130 129.506 1.00 73.48  ? 122 TYR   A O     1 
ATOM   995  C  CB    . TYR   A 1 146 ? 163.866 159.393 126.142 1.00 68.92  ? 122 TYR   A CB    1 
ATOM   996  C  CG    . TYR   A 1 146 ? 164.827 159.088 125.017 1.00 69.56  ? 122 TYR   A CG    1 
ATOM   997  C  CD1   . TYR   A 1 146 ? 166.178 159.380 125.131 1.00 69.54  ? 122 TYR   A CD1   1 
ATOM   998  C  CD2   . TYR   A 1 146 ? 164.377 158.525 123.831 1.00 67.32  ? 122 TYR   A CD2   1 
ATOM   999  C  CE1   . TYR   A 1 146 ? 167.056 159.109 124.102 1.00 69.64  ? 122 TYR   A CE1   1 
ATOM   1000 C  CE2   . TYR   A 1 146 ? 165.248 158.249 122.796 1.00 68.04  ? 122 TYR   A CE2   1 
ATOM   1001 C  CZ    . TYR   A 1 146 ? 166.586 158.544 122.937 1.00 70.61  ? 122 TYR   A CZ    1 
ATOM   1002 O  OH    . TYR   A 1 146 ? 167.457 158.272 121.909 1.00 71.76  ? 122 TYR   A OH    1 
ATOM   1003 N  N     . GLY   A 1 147 ? 162.082 158.994 128.518 1.00 66.37  ? 123 GLY   A N     1 
ATOM   1004 C  CA    . GLY   A 1 147 ? 161.111 159.472 129.483 1.00 65.34  ? 123 GLY   A CA    1 
ATOM   1005 C  C     . GLY   A 1 147 ? 161.541 159.211 130.909 1.00 66.12  ? 123 GLY   A C     1 
ATOM   1006 O  O     . GLY   A 1 147 ? 161.509 160.122 131.745 1.00 68.07  ? 123 GLY   A O     1 
ATOM   1007 N  N     . HIS   A 1 148 ? 162.021 157.993 131.187 1.00 51.55  ? 124 HIS   A N     1 
ATOM   1008 C  CA    . HIS   A 1 148 ? 162.500 157.680 132.527 1.00 46.83  ? 124 HIS   A CA    1 
ATOM   1009 C  C     . HIS   A 1 148 ? 163.514 158.712 132.987 1.00 47.73  ? 124 HIS   A C     1 
ATOM   1010 O  O     . HIS   A 1 148 ? 163.355 159.311 134.060 1.00 55.93  ? 124 HIS   A O     1 
ATOM   1011 C  CB    . HIS   A 1 148 ? 163.110 156.279 132.558 1.00 48.40  ? 124 HIS   A CB    1 
ATOM   1012 C  CG    . HIS   A 1 148 ? 164.008 156.036 133.732 1.00 57.70  ? 124 HIS   A CG    1 
ATOM   1013 N  ND1   . HIS   A 1 148 ? 165.329 155.669 133.595 1.00 53.57  ? 124 HIS   A ND1   1 
ATOM   1014 C  CD2   . HIS   A 1 148 ? 163.776 156.110 135.064 1.00 57.13  ? 124 HIS   A CD2   1 
ATOM   1015 C  CE1   . HIS   A 1 148 ? 165.871 155.527 134.791 1.00 51.17  ? 124 HIS   A CE1   1 
ATOM   1016 N  NE2   . HIS   A 1 148 ? 164.950 155.788 135.700 1.00 48.97  ? 124 HIS   A NE2   1 
ATOM   1017 N  N     . LEU   A 1 149 ? 164.519 158.989 132.148 1.00 48.90  ? 125 LEU   A N     1 
ATOM   1018 C  CA    . LEU   A 1 149 ? 165.536 159.965 132.516 1.00 49.32  ? 125 LEU   A CA    1 
ATOM   1019 C  C     . LEU   A 1 149 ? 164.893 161.271 132.950 1.00 49.78  ? 125 LEU   A C     1 
ATOM   1020 O  O     . LEU   A 1 149 ? 165.172 161.770 134.048 1.00 55.43  ? 125 LEU   A O     1 
ATOM   1021 C  CB    . LEU   A 1 149 ? 166.494 160.196 131.348 1.00 48.91  ? 125 LEU   A CB    1 
ATOM   1022 C  CG    . LEU   A 1 149 ? 167.506 159.086 131.060 1.00 47.99  ? 125 LEU   A CG    1 
ATOM   1023 C  CD1   . LEU   A 1 149 ? 168.350 159.436 129.846 1.00 50.49  ? 125 LEU   A CD1   1 
ATOM   1024 C  CD2   . LEU   A 1 149 ? 168.385 158.833 132.272 1.00 46.02  ? 125 LEU   A CD2   1 
ATOM   1025 N  N     . GLY   A 1 150 ? 163.962 161.786 132.141 1.00 49.14  ? 126 GLY   A N     1 
ATOM   1026 C  CA    . GLY   A 1 150 ? 163.306 163.029 132.502 1.00 50.55  ? 126 GLY   A CA    1 
ATOM   1027 C  C     . GLY   A 1 150 ? 162.677 162.955 133.876 1.00 55.36  ? 126 GLY   A C     1 
ATOM   1028 O  O     . GLY   A 1 150 ? 162.971 163.779 134.748 1.00 57.42  ? 126 GLY   A O     1 
ATOM   1029 N  N     . LEU   A 1 151 ? 161.876 161.911 134.115 1.00 62.34  ? 127 LEU   A N     1 
ATOM   1030 C  CA    . LEU   A 1 151 ? 161.248 161.763 135.421 1.00 60.03  ? 127 LEU   A CA    1 
ATOM   1031 C  C     . LEU   A 1 151 ? 162.298 161.760 136.519 1.00 58.24  ? 127 LEU   A C     1 
ATOM   1032 O  O     . LEU   A 1 151 ? 162.173 162.500 137.504 1.00 64.33  ? 127 LEU   A O     1 
ATOM   1033 C  CB    . LEU   A 1 151 ? 160.412 160.484 135.466 1.00 60.65  ? 127 LEU   A CB    1 
ATOM   1034 C  CG    . LEU   A 1 151 ? 159.482 160.326 136.671 1.00 58.06  ? 127 LEU   A CG    1 
ATOM   1035 C  CD1   . LEU   A 1 151 ? 158.277 161.240 136.544 1.00 60.56  ? 127 LEU   A CD1   1 
ATOM   1036 C  CD2   . LEU   A 1 151 ? 159.045 158.881 136.823 1.00 59.47  ? 127 LEU   A CD2   1 
ATOM   1037 N  N     . LEU   A 1 152 ? 163.378 160.995 136.322 1.00 43.12  ? 128 LEU   A N     1 
ATOM   1038 C  CA    . LEU   A 1 152 ? 164.421 160.932 137.336 1.00 43.79  ? 128 LEU   A CA    1 
ATOM   1039 C  C     . LEU   A 1 152 ? 164.913 162.327 137.682 1.00 48.09  ? 128 LEU   A C     1 
ATOM   1040 O  O     . LEU   A 1 152 ? 164.968 162.697 138.862 1.00 56.11  ? 128 LEU   A O     1 
ATOM   1041 C  CB    . LEU   A 1 152 ? 165.574 160.054 136.852 1.00 44.93  ? 128 LEU   A CB    1 
ATOM   1042 C  CG    . LEU   A 1 152 ? 166.769 159.901 137.792 1.00 42.96  ? 128 LEU   A CG    1 
ATOM   1043 C  CD1   . LEU   A 1 152 ? 166.393 159.078 139.010 1.00 47.18  ? 128 LEU   A CD1   1 
ATOM   1044 C  CD2   . LEU   A 1 152 ? 167.939 159.272 137.061 1.00 43.83  ? 128 LEU   A CD2   1 
ATOM   1045 N  N     . LEU   A 1 153 ? 165.195 163.142 136.660 1.00 60.39  ? 129 LEU   A N     1 
ATOM   1046 C  CA    . LEU   A 1 153 ? 165.666 164.496 136.918 1.00 60.63  ? 129 LEU   A CA    1 
ATOM   1047 C  C     . LEU   A 1 153 ? 164.693 165.235 137.821 1.00 61.52  ? 129 LEU   A C     1 
ATOM   1048 O  O     . LEU   A 1 153 ? 165.082 165.744 138.882 1.00 63.61  ? 129 LEU   A O     1 
ATOM   1049 C  CB    . LEU   A 1 153 ? 165.860 165.246 135.601 1.00 69.24  ? 129 LEU   A CB    1 
ATOM   1050 C  CG    . LEU   A 1 153 ? 166.535 166.617 135.675 1.00 70.07  ? 129 LEU   A CG    1 
ATOM   1051 C  CD1   . LEU   A 1 153 ? 168.023 166.466 135.940 1.00 69.13  ? 129 LEU   A CD1   1 
ATOM   1052 C  CD2   . LEU   A 1 153 ? 166.296 167.400 134.395 1.00 63.92  ? 129 LEU   A CD2   1 
ATOM   1053 N  N     . LEU   A 1 154 ? 163.405 165.220 137.462 1.00 60.42  ? 130 LEU   A N     1 
ATOM   1054 C  CA    . LEU   A 1 154 ? 162.416 165.930 138.261 1.00 55.13  ? 130 LEU   A CA    1 
ATOM   1055 C  C     . LEU   A 1 154 ? 162.433 165.449 139.701 1.00 54.80  ? 130 LEU   A C     1 
ATOM   1056 O  O     . LEU   A 1 154 ? 162.396 166.270 140.626 1.00 58.32  ? 130 LEU   A O     1 
ATOM   1057 C  CB    . LEU   A 1 154 ? 161.024 165.758 137.655 1.00 59.89  ? 130 LEU   A CB    1 
ATOM   1058 C  CG    . LEU   A 1 154 ? 160.731 166.550 136.379 1.00 63.65  ? 130 LEU   A CG    1 
ATOM   1059 C  CD1   . LEU   A 1 154 ? 159.233 166.684 136.164 1.00 61.29  ? 130 LEU   A CD1   1 
ATOM   1060 C  CD2   . LEU   A 1 154 ? 161.395 167.918 136.418 1.00 58.10  ? 130 LEU   A CD2   1 
ATOM   1061 N  N     . VAL   A 1 155 ? 162.561 164.135 139.906 1.00 56.06  ? 131 VAL   A N     1 
ATOM   1062 C  CA    . VAL   A 1 155 ? 162.556 163.602 141.262 1.00 48.82  ? 131 VAL   A CA    1 
ATOM   1063 C  C     . VAL   A 1 155 ? 163.671 164.238 142.075 1.00 54.39  ? 131 VAL   A C     1 
ATOM   1064 O  O     . VAL   A 1 155 ? 163.443 164.724 143.191 1.00 62.62  ? 131 VAL   A O     1 
ATOM   1065 C  CB    . VAL   A 1 155 ? 162.669 162.068 141.234 1.00 53.32  ? 131 VAL   A CB    1 
ATOM   1066 C  CG1   . VAL   A 1 155 ? 163.139 161.544 142.579 1.00 58.29  ? 131 VAL   A CG1   1 
ATOM   1067 C  CG2   . VAL   A 1 155 ? 161.337 161.449 140.849 1.00 52.52  ? 131 VAL   A CG2   1 
ATOM   1068 N  N     . ILE   A 1 156 ? 164.876 164.310 141.504 1.00 58.84  ? 132 ILE   A N     1 
ATOM   1069 C  CA    . ILE   A 1 156 ? 165.984 164.934 142.220 1.00 58.26  ? 132 ILE   A CA    1 
ATOM   1070 C  C     . ILE   A 1 156 ? 165.661 166.392 142.507 1.00 64.49  ? 132 ILE   A C     1 
ATOM   1071 O  O     . ILE   A 1 156 ? 165.864 166.881 143.627 1.00 66.33  ? 132 ILE   A O     1 
ATOM   1072 C  CB    . ILE   A 1 156 ? 167.291 164.778 141.423 1.00 63.89  ? 132 ILE   A CB    1 
ATOM   1073 C  CG1   . ILE   A 1 156 ? 167.687 163.303 141.348 1.00 64.44  ? 132 ILE   A CG1   1 
ATOM   1074 C  CG2   . ILE   A 1 156 ? 168.403 165.594 142.054 1.00 59.38  ? 132 ILE   A CG2   1 
ATOM   1075 C  CD1   . ILE   A 1 156 ? 168.840 163.022 140.410 1.00 61.79  ? 132 ILE   A CD1   1 
ATOM   1076 N  N     . ILE   A 1 157 ? 165.102 167.094 141.518 1.00 63.86  ? 133 ILE   A N     1 
ATOM   1077 C  CA    . ILE   A 1 157 ? 164.723 168.486 141.723 1.00 57.93  ? 133 ILE   A CA    1 
ATOM   1078 C  C     . ILE   A 1 157 ? 163.648 168.585 142.797 1.00 65.91  ? 133 ILE   A C     1 
ATOM   1079 O  O     . ILE   A 1 157 ? 163.621 169.539 143.584 1.00 67.94  ? 133 ILE   A O     1 
ATOM   1080 C  CB    . ILE   A 1 157 ? 164.273 169.115 140.392 1.00 63.85  ? 133 ILE   A CB    1 
ATOM   1081 C  CG1   . ILE   A 1 157 ? 165.473 169.305 139.465 1.00 64.44  ? 133 ILE   A CG1   1 
ATOM   1082 C  CG2   . ILE   A 1 157 ? 163.592 170.453 140.623 1.00 64.19  ? 133 ILE   A CG2   1 
ATOM   1083 C  CD1   . ILE   A 1 157 ? 165.121 169.902 138.123 1.00 62.55  ? 133 ILE   A CD1   1 
ATOM   1084 N  N     . ALA   A 1 158 ? 162.762 167.588 142.867 1.00 69.19  ? 134 ALA   A N     1 
ATOM   1085 C  CA    . ALA   A 1 158 ? 161.722 167.606 143.887 1.00 61.94  ? 134 ALA   A CA    1 
ATOM   1086 C  C     . ALA   A 1 158 ? 162.264 167.272 145.269 1.00 65.30  ? 134 ALA   A C     1 
ATOM   1087 O  O     . ALA   A 1 158 ? 161.572 167.509 146.264 1.00 71.56  ? 134 ALA   A O     1 
ATOM   1088 C  CB    . ALA   A 1 158 ? 160.602 166.633 143.519 1.00 63.41  ? 134 ALA   A CB    1 
ATOM   1089 N  N     . CYS   A 1 159 ? 163.483 166.733 145.357 1.00 70.13  ? 135 CYS   A N     1 
ATOM   1090 C  CA    . CYS   A 1 159 ? 164.005 166.312 146.651 1.00 68.68  ? 135 CYS   A CA    1 
ATOM   1091 C  C     . CYS   A 1 159 ? 164.662 167.452 147.419 1.00 77.83  ? 135 CYS   A C     1 
ATOM   1092 O  O     . CYS   A 1 159 ? 164.920 167.302 148.618 1.00 77.90  ? 135 CYS   A O     1 
ATOM   1093 C  CB    . CYS   A 1 159 ? 165.000 165.166 146.467 1.00 72.35  ? 135 CYS   A CB    1 
ATOM   1094 S  SG    . CYS   A 1 159 ? 164.261 163.517 146.548 1.00 75.31  ? 135 CYS   A SG    1 
ATOM   1095 N  N     . MET   A 1 160 ? 164.939 168.581 146.766 1.00 93.86  ? 136 MET   A N     1 
ATOM   1096 C  CA    . MET   A 1 160 ? 165.618 169.688 147.428 1.00 88.52  ? 136 MET   A CA    1 
ATOM   1097 C  C     . MET   A 1 160 ? 164.702 170.504 148.329 1.00 93.84  ? 136 MET   A C     1 
ATOM   1098 O  O     . MET   A 1 160 ? 165.203 171.240 149.185 1.00 91.86  ? 136 MET   A O     1 
ATOM   1099 C  CB    . MET   A 1 160 ? 166.260 170.611 146.390 1.00 86.16  ? 136 MET   A CB    1 
ATOM   1100 C  CG    . MET   A 1 160 ? 166.514 169.957 145.045 1.00 91.87  ? 136 MET   A CG    1 
ATOM   1101 S  SD    . MET   A 1 160 ? 167.507 170.996 143.958 1.00 104.02 ? 136 MET   A SD    1 
ATOM   1102 C  CE    . MET   A 1 160 ? 169.018 171.124 144.910 1.00 96.68  ? 136 MET   A CE    1 
ATOM   1103 N  N     . PHE   A 1 161 ? 163.383 170.395 148.164 1.00 101.10 ? 137 PHE   A N     1 
ATOM   1104 C  CA    . PHE   A 1 161 ? 162.466 171.190 148.972 1.00 97.35  ? 137 PHE   A CA    1 
ATOM   1105 C  C     . PHE   A 1 161 ? 162.385 170.699 150.411 1.00 95.25  ? 137 PHE   A C     1 
ATOM   1106 O  O     . PHE   A 1 161 ? 162.076 171.492 151.306 1.00 97.72  ? 137 PHE   A O     1 
ATOM   1107 C  CB    . PHE   A 1 161 ? 161.076 171.193 148.337 1.00 94.70  ? 137 PHE   A CB    1 
ATOM   1108 C  CG    . PHE   A 1 161 ? 161.010 171.934 147.032 1.00 96.10  ? 137 PHE   A CG    1 
ATOM   1109 C  CD1   . PHE   A 1 161 ? 161.967 172.884 146.710 1.00 97.23  ? 137 PHE   A CD1   1 
ATOM   1110 C  CD2   . PHE   A 1 161 ? 159.996 171.681 146.125 1.00 98.52  ? 137 PHE   A CD2   1 
ATOM   1111 C  CE1   . PHE   A 1 161 ? 161.912 173.567 145.511 1.00 96.70  ? 137 PHE   A CE1   1 
ATOM   1112 C  CE2   . PHE   A 1 161 ? 159.935 172.362 144.924 1.00 100.07 ? 137 PHE   A CE2   1 
ATOM   1113 C  CZ    . PHE   A 1 161 ? 160.895 173.306 144.617 1.00 98.79  ? 137 PHE   A CZ    1 
ATOM   1114 N  N     . THR   A 1 162 ? 162.649 169.415 150.652 1.00 93.09  ? 138 THR   A N     1 
ATOM   1115 C  CA    . THR   A 1 162 ? 162.670 168.902 152.017 1.00 96.78  ? 138 THR   A CA    1 
ATOM   1116 C  C     . THR   A 1 162 ? 163.950 169.295 152.741 1.00 102.28 ? 138 THR   A C     1 
ATOM   1117 O  O     . THR   A 1 162 ? 163.941 169.500 153.960 1.00 104.35 ? 138 THR   A O     1 
ATOM   1118 C  CB    . THR   A 1 162 ? 162.520 167.383 152.011 1.00 97.54  ? 138 THR   A CB    1 
ATOM   1119 O  OG1   . THR   A 1 162 ? 161.663 166.997 150.932 1.00 97.18  ? 138 THR   A OG1   1 
ATOM   1120 C  CG2   . THR   A 1 162 ? 161.920 166.904 153.323 1.00 96.28  ? 138 THR   A CG2   1 
ATOM   1121 N  N     . GLY   A 1 163 ? 165.055 169.399 152.010 1.00 86.01  ? 139 GLY   A N     1 
ATOM   1122 C  CA    . GLY   A 1 163 ? 166.343 169.684 152.606 1.00 81.54  ? 139 GLY   A CA    1 
ATOM   1123 C  C     . GLY   A 1 163 ? 167.397 168.693 152.161 1.00 83.87  ? 139 GLY   A C     1 
ATOM   1124 O  O     . GLY   A 1 163 ? 168.539 168.735 152.627 1.00 87.95  ? 139 GLY   A O     1 
ATOM   1125 N  N     . ILE   A 1 164 ? 167.022 167.797 151.254 1.00 75.28  ? 140 ILE   A N     1 
ATOM   1126 C  CA    . ILE   A 1 164 ? 167.932 166.787 150.727 1.00 73.70  ? 140 ILE   A CA    1 
ATOM   1127 C  C     . ILE   A 1 164 ? 168.600 167.364 149.485 1.00 74.65  ? 140 ILE   A C     1 
ATOM   1128 O  O     . ILE   A 1 164 ? 167.952 167.564 148.455 1.00 72.00  ? 140 ILE   A O     1 
ATOM   1129 C  CB    . ILE   A 1 164 ? 167.200 165.479 150.408 1.00 74.08  ? 140 ILE   A CB    1 
ATOM   1130 C  CG1   . ILE   A 1 164 ? 165.898 165.388 151.209 1.00 75.54  ? 140 ILE   A CG1   1 
ATOM   1131 C  CG2   . ILE   A 1 164 ? 168.102 164.285 150.690 1.00 70.86  ? 140 ILE   A CG2   1 
ATOM   1132 C  CD1   . ILE   A 1 164 ? 165.411 163.974 151.448 1.00 73.45  ? 140 ILE   A CD1   1 
ATOM   1133 N  N     . TYR   A 1 165 ? 169.901 167.626 149.579 1.00 82.03  ? 141 TYR   A N     1 
ATOM   1134 C  CA    . TYR   A 1 165 ? 170.663 168.208 148.489 1.00 82.33  ? 141 TYR   A CA    1 
ATOM   1135 C  C     . TYR   A 1 165 ? 171.631 167.183 147.906 1.00 78.46  ? 141 TYR   A C     1 
ATOM   1136 O  O     . TYR   A 1 165 ? 172.081 166.277 148.614 1.00 77.55  ? 141 TYR   A O     1 
ATOM   1137 C  CB    . TYR   A 1 165 ? 171.447 169.437 148.965 1.00 83.45  ? 141 TYR   A CB    1 
ATOM   1138 C  CG    . TYR   A 1 165 ? 170.568 170.568 149.444 1.00 81.66  ? 141 TYR   A CG    1 
ATOM   1139 C  CD1   . TYR   A 1 165 ? 169.888 171.374 148.542 1.00 80.43  ? 141 TYR   A CD1   1 
ATOM   1140 C  CD2   . TYR   A 1 165 ? 170.415 170.827 150.798 1.00 79.25  ? 141 TYR   A CD2   1 
ATOM   1141 C  CE1   . TYR   A 1 165 ? 169.082 172.407 148.975 1.00 80.02  ? 141 TYR   A CE1   1 
ATOM   1142 C  CE2   . TYR   A 1 165 ? 169.612 171.858 151.241 1.00 81.49  ? 141 TYR   A CE2   1 
ATOM   1143 C  CZ    . TYR   A 1 165 ? 168.948 172.644 150.326 1.00 83.81  ? 141 TYR   A CZ    1 
ATOM   1144 O  OH    . TYR   A 1 165 ? 168.146 173.673 150.763 1.00 86.78  ? 141 TYR   A OH    1 
ATOM   1145 N  N     . PRO   A 1 166 ? 171.962 167.294 146.619 1.00 79.25  ? 142 PRO   A N     1 
ATOM   1146 C  CA    . PRO   A 1 166 ? 172.864 166.312 146.004 1.00 77.85  ? 142 PRO   A CA    1 
ATOM   1147 C  C     . PRO   A 1 166 ? 174.223 166.288 146.688 1.00 81.96  ? 142 PRO   A C     1 
ATOM   1148 O  O     . PRO   A 1 166 ? 174.755 167.321 147.098 1.00 85.28  ? 142 PRO   A O     1 
ATOM   1149 C  CB    . PRO   A 1 166 ? 172.973 166.793 144.553 1.00 76.12  ? 142 PRO   A CB    1 
ATOM   1150 C  CG    . PRO   A 1 166 ? 171.720 167.563 144.321 1.00 79.56  ? 142 PRO   A CG    1 
ATOM   1151 C  CD    . PRO   A 1 166 ? 171.417 168.236 145.627 1.00 80.21  ? 142 PRO   A CD    1 
ATOM   1152 N  N     . SER   A 1 167 ? 174.780 165.084 146.807 1.00 70.81  ? 143 SER   A N     1 
ATOM   1153 C  CA    . SER   A 1 167 ? 176.067 164.883 147.460 1.00 65.98  ? 143 SER   A CA    1 
ATOM   1154 C  C     . SER   A 1 167 ? 177.018 164.151 146.524 1.00 69.88  ? 143 SER   A C     1 
ATOM   1155 O  O     . SER   A 1 167 ? 176.701 163.946 145.349 1.00 75.27  ? 143 SER   A O     1 
ATOM   1156 C  CB    . SER   A 1 167 ? 175.887 164.102 148.762 1.00 63.77  ? 143 SER   A CB    1 
ATOM   1157 O  OG    . SER   A 1 167 ? 177.042 164.194 149.577 1.00 74.83  ? 143 SER   A OG    1 
ATOM   1158 N  N     . ILE   A 1 168 ? 178.192 163.762 147.027 1.00 47.21  ? 144 ILE   A N     1 
ATOM   1159 C  CA    . ILE   A 1 168 ? 179.110 162.967 146.222 1.00 37.19  ? 144 ILE   A CA    1 
ATOM   1160 C  C     . ILE   A 1 168 ? 178.541 161.583 145.934 1.00 43.43  ? 144 ILE   A C     1 
ATOM   1161 O  O     . ILE   A 1 168 ? 178.735 161.050 144.834 1.00 45.30  ? 144 ILE   A O     1 
ATOM   1162 C  CB    . ILE   A 1 168 ? 180.493 162.888 146.905 1.00 38.74  ? 144 ILE   A CB    1 
ATOM   1163 C  CG1   . ILE   A 1 168 ? 181.539 162.328 145.940 1.00 42.81  ? 144 ILE   A CG1   1 
ATOM   1164 C  CG2   . ILE   A 1 168 ? 180.437 162.082 148.195 1.00 44.30  ? 144 ILE   A CG2   1 
ATOM   1165 C  CD1   . ILE   A 1 168 ? 182.007 163.325 144.906 1.00 48.29  ? 144 ILE   A CD1   1 
ATOM   1166 N  N     . HIS   A 1 169 ? 177.799 161.003 146.878 1.00 40.16  ? 145 HIS   A N     1 
ATOM   1167 C  CA    . HIS   A 1 169 ? 177.238 159.668 146.727 1.00 36.53  ? 145 HIS   A CA    1 
ATOM   1168 C  C     . HIS   A 1 169 ? 176.276 159.549 145.554 1.00 33.10  ? 145 HIS   A C     1 
ATOM   1169 O  O     . HIS   A 1 169 ? 175.820 158.439 145.263 1.00 50.15  ? 145 HIS   A O     1 
ATOM   1170 C  CB    . HIS   A 1 169 ? 176.528 159.252 148.017 1.00 30.71  ? 145 HIS   A CB    1 
ATOM   1171 C  CG    . HIS   A 1 169 ? 177.377 159.385 149.242 1.00 34.49  ? 145 HIS   A CG    1 
ATOM   1172 N  ND1   . HIS   A 1 169 ? 177.468 160.557 149.961 1.00 42.72  ? 145 HIS   A ND1   1 
ATOM   1173 C  CD2   . HIS   A 1 169 ? 178.179 158.495 149.872 1.00 36.70  ? 145 HIS   A CD2   1 
ATOM   1174 C  CE1   . HIS   A 1 169 ? 178.285 160.382 150.984 1.00 48.16  ? 145 HIS   A CE1   1 
ATOM   1175 N  NE2   . HIS   A 1 169 ? 178.730 159.139 150.952 1.00 38.91  ? 145 HIS   A NE2   1 
ATOM   1176 N  N     . ILE   A 1 170 ? 175.951 160.653 144.877 1.00 27.88  ? 146 ILE   A N     1 
ATOM   1177 C  CA    . ILE   A 1 170 ? 175.111 160.578 143.685 1.00 40.22  ? 146 ILE   A CA    1 
ATOM   1178 C  C     . ILE   A 1 170 ? 175.869 160.075 142.468 1.00 47.07  ? 146 ILE   A C     1 
ATOM   1179 O  O     . ILE   A 1 170 ? 175.235 159.635 141.498 1.00 50.29  ? 146 ILE   A O     1 
ATOM   1180 C  CB    . ILE   A 1 170 ? 174.474 161.947 143.377 1.00 38.22  ? 146 ILE   A CB    1 
ATOM   1181 C  CG1   . ILE   A 1 170 ? 173.166 161.767 142.604 1.00 32.13  ? 146 ILE   A CG1   1 
ATOM   1182 C  CG2   . ILE   A 1 170 ? 175.434 162.830 142.599 1.00 34.87  ? 146 ILE   A CG2   1 
ATOM   1183 C  CD1   . ILE   A 1 170 ? 172.142 162.840 142.875 1.00 36.35  ? 146 ILE   A CD1   1 
ATOM   1184 N  N     . ILE   A 1 171 ? 177.204 160.092 142.494 1.00 40.81  ? 147 ILE   A N     1 
ATOM   1185 C  CA    . ILE   A 1 171 ? 177.983 159.649 141.340 1.00 43.84  ? 147 ILE   A CA    1 
ATOM   1186 C  C     . ILE   A 1 171 ? 177.729 158.167 141.097 1.00 44.20  ? 147 ILE   A C     1 
ATOM   1187 O  O     . ILE   A 1 171 ? 177.923 157.667 139.983 1.00 53.17  ? 147 ILE   A O     1 
ATOM   1188 C  CB    . ILE   A 1 171 ? 179.486 159.933 141.519 1.00 41.96  ? 147 ILE   A CB    1 
ATOM   1189 C  CG1   . ILE   A 1 171 ? 180.070 159.095 142.656 1.00 39.54  ? 147 ILE   A CG1   1 
ATOM   1190 C  CG2   . ILE   A 1 171 ? 179.726 161.415 141.754 1.00 46.16  ? 147 ILE   A CG2   1 
ATOM   1191 C  CD1   . ILE   A 1 171 ? 181.569 159.220 142.787 1.00 43.95  ? 147 ILE   A CD1   1 
ATOM   1192 N  N     . GLN   A 1 172 ? 177.266 157.463 142.134 1.00 40.05  ? 148 GLN   A N     1 
ATOM   1193 C  CA    . GLN   A 1 172 ? 176.911 156.057 141.994 1.00 33.48  ? 148 GLN   A CA    1 
ATOM   1194 C  C     . GLN   A 1 172 ? 175.858 155.831 140.922 1.00 35.67  ? 148 GLN   A C     1 
ATOM   1195 O  O     . GLN   A 1 172 ? 175.786 154.728 140.370 1.00 36.95  ? 148 GLN   A O     1 
ATOM   1196 C  CB    . GLN   A 1 172 ? 176.402 155.503 143.323 1.00 33.11  ? 148 GLN   A CB    1 
ATOM   1197 C  CG    . GLN   A 1 172 ? 177.357 155.675 144.480 1.00 34.77  ? 148 GLN   A CG    1 
ATOM   1198 C  CD    . GLN   A 1 172 ? 176.832 155.049 145.750 1.00 39.95  ? 148 GLN   A CD    1 
ATOM   1199 O  OE1   . GLN   A 1 172 ? 176.999 153.854 145.980 1.00 45.61  ? 148 GLN   A OE1   1 
ATOM   1200 N  NE2   . GLN   A 1 172 ? 176.185 155.854 146.583 1.00 43.76  ? 148 GLN   A NE2   1 
ATOM   1201 N  N     . LEU   A 1 173 ? 175.043 156.845 140.617 1.00 34.76  ? 149 LEU   A N     1 
ATOM   1202 C  CA    . LEU   A 1 173 ? 174.054 156.697 139.556 1.00 36.19  ? 149 LEU   A CA    1 
ATOM   1203 C  C     . LEU   A 1 173 ? 174.706 156.315 138.235 1.00 38.99  ? 149 LEU   A C     1 
ATOM   1204 O  O     . LEU   A 1 173 ? 174.099 155.593 137.435 1.00 51.09  ? 149 LEU   A O     1 
ATOM   1205 C  CB    . LEU   A 1 173 ? 173.249 157.986 139.400 1.00 38.56  ? 149 LEU   A CB    1 
ATOM   1206 C  CG    . LEU   A 1 173 ? 172.163 158.230 140.449 1.00 39.52  ? 149 LEU   A CG    1 
ATOM   1207 C  CD1   . LEU   A 1 173 ? 171.380 159.488 140.121 1.00 41.69  ? 149 LEU   A CD1   1 
ATOM   1208 C  CD2   . LEU   A 1 173 ? 171.236 157.032 140.556 1.00 34.77  ? 149 LEU   A CD2   1 
ATOM   1209 N  N     . LEU   A 1 174 ? 175.951 156.748 138.009 1.00 39.71  ? 150 LEU   A N     1 
ATOM   1210 C  CA    . LEU   A 1 174 ? 176.650 156.406 136.775 1.00 40.56  ? 150 LEU   A CA    1 
ATOM   1211 C  C     . LEU   A 1 174 ? 176.799 154.903 136.591 1.00 46.75  ? 150 LEU   A C     1 
ATOM   1212 O  O     . LEU   A 1 174 ? 177.003 154.445 135.462 1.00 52.89  ? 150 LEU   A O     1 
ATOM   1213 C  CB    . LEU   A 1 174 ? 178.029 157.069 136.746 1.00 40.51  ? 150 LEU   A CB    1 
ATOM   1214 C  CG    . LEU   A 1 174 ? 178.070 158.597 136.694 1.00 48.00  ? 150 LEU   A CG    1 
ATOM   1215 C  CD1   . LEU   A 1 174 ? 179.489 159.104 136.880 1.00 40.27  ? 150 LEU   A CD1   1 
ATOM   1216 C  CD2   . LEU   A 1 174 ? 177.491 159.098 135.385 1.00 49.05  ? 150 LEU   A CD2   1 
ATOM   1217 N  N     . ILE   A 1 175 ? 176.702 154.126 137.669 1.00 41.85  ? 151 ILE   A N     1 
ATOM   1218 C  CA    . ILE   A 1 175 ? 176.800 152.675 137.586 1.00 34.04  ? 151 ILE   A CA    1 
ATOM   1219 C  C     . ILE   A 1 175 ? 175.398 152.079 137.625 1.00 40.10  ? 151 ILE   A C     1 
ATOM   1220 O  O     . ILE   A 1 175 ? 175.149 151.007 137.062 1.00 44.23  ? 151 ILE   A O     1 
ATOM   1221 C  CB    . ILE   A 1 175 ? 177.674 152.117 138.725 1.00 44.37  ? 151 ILE   A CB    1 
ATOM   1222 C  CG1   . ILE   A 1 175 ? 179.098 152.660 138.618 1.00 49.48  ? 151 ILE   A CG1   1 
ATOM   1223 C  CG2   . ILE   A 1 175 ? 177.708 150.597 138.697 1.00 41.34  ? 151 ILE   A CG2   1 
ATOM   1224 C  CD1   . ILE   A 1 175 ? 179.512 153.503 139.804 1.00 48.16  ? 151 ILE   A CD1   1 
ATOM   1225 N  N     . TYR   A 1 176 ? 174.462 152.783 138.263 1.00 44.01  ? 152 TYR   A N     1 
ATOM   1226 C  CA    . TYR   A 1 176 ? 173.171 152.181 138.577 1.00 38.31  ? 152 TYR   A CA    1 
ATOM   1227 C  C     . TYR   A 1 176 ? 172.114 152.449 137.515 1.00 36.51  ? 152 TYR   A C     1 
ATOM   1228 O  O     . TYR   A 1 176 ? 171.309 151.563 137.213 1.00 50.47  ? 152 TYR   A O     1 
ATOM   1229 C  CB    . TYR   A 1 176 ? 172.677 152.678 139.939 1.00 35.20  ? 152 TYR   A CB    1 
ATOM   1230 C  CG    . TYR   A 1 176 ? 173.537 152.220 141.093 1.00 37.46  ? 152 TYR   A CG    1 
ATOM   1231 C  CD1   . TYR   A 1 176 ? 174.302 151.066 140.996 1.00 33.38  ? 152 TYR   A CD1   1 
ATOM   1232 C  CD2   . TYR   A 1 176 ? 173.591 152.942 142.275 1.00 39.82  ? 152 TYR   A CD2   1 
ATOM   1233 C  CE1   . TYR   A 1 176 ? 175.092 150.644 142.043 1.00 34.80  ? 152 TYR   A CE1   1 
ATOM   1234 C  CE2   . TYR   A 1 176 ? 174.380 152.526 143.329 1.00 43.50  ? 152 TYR   A CE2   1 
ATOM   1235 C  CZ    . TYR   A 1 176 ? 175.128 151.377 143.206 1.00 41.87  ? 152 TYR   A CZ    1 
ATOM   1236 O  OH    . TYR   A 1 176 ? 175.915 150.960 144.250 1.00 35.38  ? 152 TYR   A OH    1 
ATOM   1237 N  N     . VAL   A 1 177 ? 172.084 153.653 136.955 1.00 37.06  ? 153 VAL   A N     1 
ATOM   1238 C  CA    . VAL   A 1 177 ? 171.119 153.989 135.909 1.00 36.62  ? 153 VAL   A CA    1 
ATOM   1239 C  C     . VAL   A 1 177 ? 171.356 153.134 134.665 1.00 45.29  ? 153 VAL   A C     1 
ATOM   1240 O  O     . VAL   A 1 177 ? 170.385 152.593 134.117 1.00 48.59  ? 153 VAL   A O     1 
ATOM   1241 C  CB    . VAL   A 1 177 ? 171.153 155.490 135.578 1.00 38.19  ? 153 VAL   A CB    1 
ATOM   1242 C  CG1   . VAL   A 1 177 ? 170.167 155.809 134.469 1.00 41.05  ? 153 VAL   A CG1   1 
ATOM   1243 C  CG2   . VAL   A 1 177 ? 170.844 156.310 136.818 1.00 32.22  ? 153 VAL   A CG2   1 
ATOM   1244 N  N     . PRO   A 1 178 ? 172.593 152.981 134.166 1.00 46.82  ? 154 PRO   A N     1 
ATOM   1245 C  CA    . PRO   A 1 178 ? 172.797 152.079 133.020 1.00 40.34  ? 154 PRO   A CA    1 
ATOM   1246 C  C     . PRO   A 1 178 ? 172.398 150.637 133.286 1.00 43.56  ? 154 PRO   A C     1 
ATOM   1247 O  O     . PRO   A 1 178 ? 171.777 150.020 132.411 1.00 51.60  ? 154 PRO   A O     1 
ATOM   1248 C  CB    . PRO   A 1 178 ? 174.302 152.194 132.750 1.00 42.12  ? 154 PRO   A CB    1 
ATOM   1249 C  CG    . PRO   A 1 178 ? 174.651 153.538 133.244 1.00 40.11  ? 154 PRO   A CG    1 
ATOM   1250 C  CD    . PRO   A 1 178 ? 173.845 153.688 134.495 1.00 42.78  ? 154 PRO   A CD    1 
ATOM   1251 N  N     . PHE   A 1 179 ? 172.705 150.095 134.470 1.00 51.71  ? 155 PHE   A N     1 
ATOM   1252 C  CA    . PHE   A 1 179 ? 172.457 148.680 134.732 1.00 49.79  ? 155 PHE   A CA    1 
ATOM   1253 C  C     . PHE   A 1 179 ? 170.993 148.323 134.524 1.00 53.99  ? 155 PHE   A C     1 
ATOM   1254 O  O     . PHE   A 1 179 ? 170.682 147.327 133.858 1.00 58.90  ? 155 PHE   A O     1 
ATOM   1255 C  CB    . PHE   A 1 179 ? 172.892 148.321 136.152 1.00 51.77  ? 155 PHE   A CB    1 
ATOM   1256 C  CG    . PHE   A 1 179 ? 172.311 147.028 136.655 1.00 57.69  ? 155 PHE   A CG    1 
ATOM   1257 C  CD1   . PHE   A 1 179 ? 172.819 145.813 136.230 1.00 56.96  ? 155 PHE   A CD1   1 
ATOM   1258 C  CD2   . PHE   A 1 179 ? 171.253 147.029 137.548 1.00 59.44  ? 155 PHE   A CD2   1 
ATOM   1259 C  CE1   . PHE   A 1 179 ? 172.285 144.624 136.688 1.00 59.26  ? 155 PHE   A CE1   1 
ATOM   1260 C  CE2   . PHE   A 1 179 ? 170.714 145.843 138.009 1.00 58.43  ? 155 PHE   A CE2   1 
ATOM   1261 C  CZ    . PHE   A 1 179 ? 171.231 144.640 137.578 1.00 59.40  ? 155 PHE   A CZ    1 
ATOM   1262 N  N     . CYS   A 1 180 ? 170.084 149.131 135.074 1.00 49.58  ? 156 CYS   A N     1 
ATOM   1263 C  CA    . CYS   A 1 180 ? 168.659 148.905 134.860 1.00 50.47  ? 156 CYS   A CA    1 
ATOM   1264 C  C     . CYS   A 1 180 ? 168.346 148.769 133.377 1.00 62.04  ? 156 CYS   A C     1 
ATOM   1265 O  O     . CYS   A 1 180 ? 167.679 147.811 132.965 1.00 65.96  ? 156 CYS   A O     1 
ATOM   1266 C  CB    . CYS   A 1 180 ? 167.853 150.043 135.486 1.00 52.37  ? 156 CYS   A CB    1 
ATOM   1267 S  SG    . CYS   A 1 180 ? 166.146 150.168 134.916 1.00 74.35  ? 156 CYS   A SG    1 
ATOM   1268 N  N     . PHE   A 1 181 ? 168.858 149.692 132.557 1.00 54.91  ? 157 PHE   A N     1 
ATOM   1269 C  CA    . PHE   A 1 181 ? 168.691 149.570 131.113 1.00 40.69  ? 157 PHE   A CA    1 
ATOM   1270 C  C     . PHE   A 1 181 ? 169.205 148.225 130.622 1.00 50.49  ? 157 PHE   A C     1 
ATOM   1271 O  O     . PHE   A 1 181 ? 168.468 147.466 129.979 1.00 60.24  ? 157 PHE   A O     1 
ATOM   1272 C  CB    . PHE   A 1 181 ? 169.417 150.716 130.407 1.00 42.45  ? 157 PHE   A CB    1 
ATOM   1273 C  CG    . PHE   A 1 181 ? 169.336 150.656 128.908 1.00 55.16  ? 157 PHE   A CG    1 
ATOM   1274 C  CD1   . PHE   A 1 181 ? 168.186 151.049 128.247 1.00 56.74  ? 157 PHE   A CD1   1 
ATOM   1275 C  CD2   . PHE   A 1 181 ? 170.412 150.209 128.160 1.00 55.50  ? 157 PHE   A CD2   1 
ATOM   1276 C  CE1   . PHE   A 1 181 ? 168.110 150.997 126.870 1.00 49.60  ? 157 PHE   A CE1   1 
ATOM   1277 C  CE2   . PHE   A 1 181 ? 170.340 150.153 126.783 1.00 53.00  ? 157 PHE   A CE2   1 
ATOM   1278 C  CZ    . PHE   A 1 181 ? 169.187 150.548 126.138 1.00 51.66  ? 157 PHE   A CZ    1 
ATOM   1279 N  N     . PHE   A 1 182 ? 170.447 147.884 130.979 1.00 49.70  ? 158 PHE   A N     1 
ATOM   1280 C  CA    . PHE   A 1 182 ? 171.037 146.634 130.514 1.00 39.76  ? 158 PHE   A CA    1 
ATOM   1281 C  C     . PHE   A 1 182 ? 170.256 145.433 131.024 1.00 42.05  ? 158 PHE   A C     1 
ATOM   1282 O  O     . PHE   A 1 182 ? 170.369 144.334 130.472 1.00 58.24  ? 158 PHE   A O     1 
ATOM   1283 C  CB    . PHE   A 1 182 ? 172.501 146.550 130.942 1.00 43.87  ? 158 PHE   A CB    1 
ATOM   1284 C  CG    . PHE   A 1 182 ? 173.420 147.394 130.110 1.00 52.42  ? 158 PHE   A CG    1 
ATOM   1285 C  CD1   . PHE   A 1 182 ? 173.215 147.522 128.747 1.00 50.12  ? 158 PHE   A CD1   1 
ATOM   1286 C  CD2   . PHE   A 1 182 ? 174.482 148.065 130.688 1.00 52.37  ? 158 PHE   A CD2   1 
ATOM   1287 C  CE1   . PHE   A 1 182 ? 174.055 148.299 127.977 1.00 49.71  ? 158 PHE   A CE1   1 
ATOM   1288 C  CE2   . PHE   A 1 182 ? 175.325 148.844 129.922 1.00 50.38  ? 158 PHE   A CE2   1 
ATOM   1289 C  CZ    . PHE   A 1 182 ? 175.112 148.961 128.565 1.00 50.76  ? 158 PHE   A CZ    1 
ATOM   1290 N  N     . LEU   A 1 183 ? 169.459 145.619 132.077 1.00 49.23  ? 159 LEU   A N     1 
ATOM   1291 C  CA    . LEU   A 1 183 ? 168.565 144.548 132.493 1.00 53.92  ? 159 LEU   A CA    1 
ATOM   1292 C  C     . LEU   A 1 183 ? 167.396 144.416 131.527 1.00 57.86  ? 159 LEU   A C     1 
ATOM   1293 O  O     . LEU   A 1 183 ? 167.183 143.344 130.946 1.00 58.45  ? 159 LEU   A O     1 
ATOM   1294 C  CB    . LEU   A 1 183 ? 168.069 144.799 133.917 1.00 55.96  ? 159 LEU   A CB    1 
ATOM   1295 C  CG    . LEU   A 1 183 ? 166.977 143.860 134.432 1.00 57.94  ? 159 LEU   A CG    1 
ATOM   1296 C  CD1   . LEU   A 1 183 ? 167.586 142.566 134.946 1.00 53.31  ? 159 LEU   A CD1   1 
ATOM   1297 C  CD2   . LEU   A 1 183 ? 166.157 144.535 135.517 1.00 55.28  ? 159 LEU   A CD2   1 
ATOM   1298 N  N     . THR   A 1 184 ? 166.664 145.513 131.300 1.00 56.23  ? 160 THR   A N     1 
ATOM   1299 C  CA    . THR   A 1 184 ? 165.422 145.433 130.537 1.00 49.80  ? 160 THR   A CA    1 
ATOM   1300 C  C     . THR   A 1 184 ? 165.662 144.874 129.143 1.00 52.52  ? 160 THR   A C     1 
ATOM   1301 O  O     . THR   A 1 184 ? 165.011 143.903 128.738 1.00 54.49  ? 160 THR   A O     1 
ATOM   1302 C  CB    . THR   A 1 184 ? 164.766 146.812 130.455 1.00 50.46  ? 160 THR   A CB    1 
ATOM   1303 O  OG1   . THR   A 1 184 ? 164.879 147.473 131.721 1.00 47.43  ? 160 THR   A OG1   1 
ATOM   1304 C  CG2   . THR   A 1 184 ? 163.300 146.683 130.087 1.00 52.99  ? 160 THR   A CG2   1 
ATOM   1305 N  N     . ALA   A 1 185 ? 166.625 145.445 128.415 1.00 60.56  ? 161 ALA   A N     1 
ATOM   1306 C  CA    . ALA   A 1 185 ? 166.957 144.928 127.093 1.00 60.62  ? 161 ALA   A CA    1 
ATOM   1307 C  C     . ALA   A 1 185 ? 167.305 143.447 127.156 1.00 63.19  ? 161 ALA   A C     1 
ATOM   1308 O  O     . ALA   A 1 185 ? 166.814 142.656 126.341 1.00 70.15  ? 161 ALA   A O     1 
ATOM   1309 C  CB    . ALA   A 1 185 ? 168.111 145.728 126.491 1.00 56.41  ? 161 ALA   A CB    1 
ATOM   1310 N  N     . SER   A 1 186 ? 168.109 143.047 128.148 1.00 55.42  ? 162 SER   A N     1 
ATOM   1311 C  CA    . SER   A 1 186 ? 168.515 141.650 128.248 1.00 54.64  ? 162 SER   A CA    1 
ATOM   1312 C  C     . SER   A 1 186 ? 167.307 140.733 128.372 1.00 61.44  ? 162 SER   A C     1 
ATOM   1313 O  O     . SER   A 1 186 ? 167.343 139.586 127.913 1.00 62.00  ? 162 SER   A O     1 
ATOM   1314 C  CB    . SER   A 1 186 ? 169.458 141.457 129.434 1.00 55.10  ? 162 SER   A CB    1 
ATOM   1315 O  OG    . SER   A 1 186 ? 170.680 142.140 129.227 1.00 64.49  ? 162 SER   A OG    1 
ATOM   1316 N  N     . VAL   A 1 187 ? 166.227 141.219 128.986 1.00 65.36  ? 163 VAL   A N     1 
ATOM   1317 C  CA    . VAL   A 1 187 ? 165.011 140.418 129.038 1.00 55.99  ? 163 VAL   A CA    1 
ATOM   1318 C  C     . VAL   A 1 187 ? 164.339 140.387 127.672 1.00 55.99  ? 163 VAL   A C     1 
ATOM   1319 O  O     . VAL   A 1 187 ? 164.019 139.312 127.148 1.00 67.20  ? 163 VAL   A O     1 
ATOM   1320 C  CB    . VAL   A 1 187 ? 164.064 140.949 130.128 1.00 58.45  ? 163 VAL   A CB    1 
ATOM   1321 C  CG1   . VAL   A 1 187 ? 162.689 140.323 129.984 1.00 58.59  ? 163 VAL   A CG1   1 
ATOM   1322 C  CG2   . VAL   A 1 187 ? 164.637 140.669 131.505 1.00 57.97  ? 163 VAL   A CG2   1 
ATOM   1323 N  N     . THR   A 1 188 ? 164.161 141.559 127.051 1.00 59.58  ? 164 THR   A N     1 
ATOM   1324 C  CA    . THR   A 1 188 ? 163.359 141.633 125.834 1.00 56.13  ? 164 THR   A CA    1 
ATOM   1325 C  C     . THR   A 1 188 ? 163.961 140.799 124.714 1.00 62.94  ? 164 THR   A C     1 
ATOM   1326 O  O     . THR   A 1 188 ? 163.235 140.059 124.039 1.00 68.64  ? 164 THR   A O     1 
ATOM   1327 C  CB    . THR   A 1 188 ? 163.205 143.084 125.383 1.00 56.49  ? 164 THR   A CB    1 
ATOM   1328 O  OG1   . THR   A 1 188 ? 164.495 143.702 125.311 1.00 64.96  ? 164 THR   A OG1   1 
ATOM   1329 C  CG2   . THR   A 1 188 ? 162.338 143.852 126.364 1.00 61.58  ? 164 THR   A CG2   1 
ATOM   1330 N  N     . LEU   A 1 189 ? 165.286 140.866 124.544 1.00 65.47  ? 165 LEU   A N     1 
ATOM   1331 C  CA    . LEU   A 1 189 ? 165.950 140.099 123.495 1.00 69.49  ? 165 LEU   A CA    1 
ATOM   1332 C  C     . LEU   A 1 189 ? 165.592 138.623 123.585 1.00 70.20  ? 165 LEU   A C     1 
ATOM   1333 O  O     . LEU   A 1 189 ? 165.525 137.928 122.565 1.00 70.74  ? 165 LEU   A O     1 
ATOM   1334 C  CB    . LEU   A 1 189 ? 167.463 140.292 123.587 1.00 70.90  ? 165 LEU   A CB    1 
ATOM   1335 C  CG    . LEU   A 1 189 ? 168.322 139.557 122.555 1.00 71.08  ? 165 LEU   A CG    1 
ATOM   1336 C  CD1   . LEU   A 1 189 ? 168.158 140.181 121.180 1.00 67.39  ? 165 LEU   A CD1   1 
ATOM   1337 C  CD2   . LEU   A 1 189 ? 169.783 139.551 122.975 1.00 68.94  ? 165 LEU   A CD2   1 
ATOM   1338 N  N     . LEU   A 1 190 ? 165.348 138.126 124.799 1.00 69.12  ? 166 LEU   A N     1 
ATOM   1339 C  CA    . LEU   A 1 190 ? 164.847 136.764 124.930 1.00 67.37  ? 166 LEU   A CA    1 
ATOM   1340 C  C     . LEU   A 1 190 ? 163.352 136.705 124.646 1.00 70.24  ? 166 LEU   A C     1 
ATOM   1341 O  O     . LEU   A 1 190 ? 162.913 135.976 123.745 1.00 74.18  ? 166 LEU   A O     1 
ATOM   1342 C  CB    . LEU   A 1 190 ? 165.159 136.224 126.325 1.00 65.61  ? 166 LEU   A CB    1 
ATOM   1343 C  CG    . LEU   A 1 190 ? 164.685 134.807 126.647 1.00 72.50  ? 166 LEU   A CG    1 
ATOM   1344 C  CD1   . LEU   A 1 190 ? 165.191 133.822 125.608 1.00 77.59  ? 166 LEU   A CD1   1 
ATOM   1345 C  CD2   . LEU   A 1 190 ? 165.141 134.399 128.036 1.00 68.87  ? 166 LEU   A CD2   1 
ATOM   1346 N  N     . THR   A 1 191 ? 162.558 137.503 125.368 1.00 68.05  ? 167 THR   A N     1 
ATOM   1347 C  CA    . THR   A 1 191 ? 161.108 137.347 125.327 1.00 60.31  ? 167 THR   A CA    1 
ATOM   1348 C  C     . THR   A 1 191 ? 160.527 137.650 123.955 1.00 60.93  ? 167 THR   A C     1 
ATOM   1349 O  O     . THR   A 1 191 ? 159.428 137.177 123.647 1.00 66.17  ? 167 THR   A O     1 
ATOM   1350 C  CB    . THR   A 1 191 ? 160.443 138.238 126.377 1.00 61.08  ? 167 THR   A CB    1 
ATOM   1351 O  OG1   . THR   A 1 191 ? 160.833 139.601 126.174 1.00 63.63  ? 167 THR   A OG1   1 
ATOM   1352 C  CG2   . THR   A 1 191 ? 160.847 137.803 127.775 1.00 60.17  ? 167 THR   A CG2   1 
ATOM   1353 N  N     . SER   A 1 192 ? 161.230 138.423 123.127 1.00 58.77  ? 168 SER   A N     1 
ATOM   1354 C  CA    . SER   A 1 192 ? 160.786 138.608 121.751 1.00 62.95  ? 168 SER   A CA    1 
ATOM   1355 C  C     . SER   A 1 192 ? 160.808 137.286 120.996 1.00 71.22  ? 168 SER   A C     1 
ATOM   1356 O  O     . SER   A 1 192 ? 159.796 136.875 120.415 1.00 73.80  ? 168 SER   A O     1 
ATOM   1357 C  CB    . SER   A 1 192 ? 161.660 139.646 121.049 1.00 59.84  ? 168 SER   A CB    1 
ATOM   1358 O  OG    . SER   A 1 192 ? 161.779 140.822 121.828 1.00 61.23  ? 168 SER   A OG    1 
ATOM   1359 N  N     . THR   A 1 193 ? 161.946 136.586 121.022 1.00 76.77  ? 169 THR   A N     1 
ATOM   1360 C  CA    . THR   A 1 193 ? 162.040 135.319 120.305 1.00 71.70  ? 169 THR   A CA    1 
ATOM   1361 C  C     . THR   A 1 193 ? 161.063 134.300 120.870 1.00 72.63  ? 169 THR   A C     1 
ATOM   1362 O  O     . THR   A 1 193 ? 160.320 133.657 120.119 1.00 74.51  ? 169 THR   A O     1 
ATOM   1363 C  CB    . THR   A 1 193 ? 163.469 134.782 120.364 1.00 74.03  ? 169 THR   A CB    1 
ATOM   1364 O  OG1   . THR   A 1 193 ? 164.386 135.820 119.996 1.00 77.51  ? 169 THR   A OG1   1 
ATOM   1365 C  CG2   . THR   A 1 193 ? 163.636 133.606 119.416 1.00 73.52  ? 169 THR   A CG2   1 
ATOM   1366 N  N     . LEU   A 1 194 ? 161.024 134.170 122.198 1.00 79.21  ? 170 LEU   A N     1 
ATOM   1367 C  CA    . LEU   A 1 194 ? 160.058 133.286 122.835 1.00 76.48  ? 170 LEU   A CA    1 
ATOM   1368 C  C     . LEU   A 1 194 ? 158.629 133.694 122.507 1.00 72.62  ? 170 LEU   A C     1 
ATOM   1369 O  O     . LEU   A 1 194 ? 157.718 132.861 122.568 1.00 73.17  ? 170 LEU   A O     1 
ATOM   1370 C  CB    . LEU   A 1 194 ? 160.277 133.281 124.347 1.00 79.35  ? 170 LEU   A CB    1 
ATOM   1371 C  CG    . LEU   A 1 194 ? 160.491 131.924 125.014 1.00 78.93  ? 170 LEU   A CG    1 
ATOM   1372 C  CD1   . LEU   A 1 194 ? 161.684 131.212 124.400 1.00 77.44  ? 170 LEU   A CD1   1 
ATOM   1373 C  CD2   . LEU   A 1 194 ? 160.683 132.099 126.510 1.00 79.28  ? 170 LEU   A CD2   1 
ATOM   1374 N  N     . GLY   A 1 195 ? 158.411 134.965 122.160 1.00 80.26  ? 171 GLY   A N     1 
ATOM   1375 C  CA    . GLY   A 1 195 ? 157.088 135.391 121.746 1.00 81.05  ? 171 GLY   A CA    1 
ATOM   1376 C  C     . GLY   A 1 195 ? 156.727 134.947 120.348 1.00 84.74  ? 171 GLY   A C     1 
ATOM   1377 O  O     . GLY   A 1 195 ? 155.552 134.701 120.061 1.00 87.44  ? 171 GLY   A O     1 
ATOM   1378 N  N     . VAL   A 1 196 ? 157.717 134.839 119.459 1.00 79.87  ? 172 VAL   A N     1 
ATOM   1379 C  CA    . VAL   A 1 196 ? 157.438 134.399 118.095 1.00 75.19  ? 172 VAL   A CA    1 
ATOM   1380 C  C     . VAL   A 1 196 ? 157.120 132.909 118.065 1.00 74.58  ? 172 VAL   A C     1 
ATOM   1381 O  O     . VAL   A 1 196 ? 156.174 132.476 117.396 1.00 76.58  ? 172 VAL   A O     1 
ATOM   1382 C  CB    . VAL   A 1 196 ? 158.616 134.747 117.169 1.00 73.59  ? 172 VAL   A CB    1 
ATOM   1383 C  CG1   . VAL   A 1 196 ? 158.465 134.044 115.831 1.00 75.17  ? 172 VAL   A CG1   1 
ATOM   1384 C  CG2   . VAL   A 1 196 ? 158.706 136.250 116.973 1.00 73.81  ? 172 VAL   A CG2   1 
ATOM   1385 N  N     . LEU   A 1 197 ? 157.900 132.103 118.787 1.00 73.77  ? 173 LEU   A N     1 
ATOM   1386 C  CA    . LEU   A 1 197 ? 157.692 130.658 118.769 1.00 73.47  ? 173 LEU   A CA    1 
ATOM   1387 C  C     . LEU   A 1 197 ? 156.358 130.286 119.404 1.00 75.66  ? 173 LEU   A C     1 
ATOM   1388 O  O     . LEU   A 1 197 ? 155.565 129.543 118.816 1.00 77.86  ? 173 LEU   A O     1 
ATOM   1389 C  CB    . LEU   A 1 197 ? 158.846 129.948 119.483 1.00 74.85  ? 173 LEU   A CB    1 
ATOM   1390 C  CG    . LEU   A 1 197 ? 160.190 129.706 118.777 1.00 76.64  ? 173 LEU   A CG    1 
ATOM   1391 C  CD1   . LEU   A 1 197 ? 160.588 130.827 117.826 1.00 73.14  ? 173 LEU   A CD1   1 
ATOM   1392 C  CD2   . LEU   A 1 197 ? 161.286 129.470 119.805 1.00 77.26  ? 173 LEU   A CD2   1 
ATOM   1393 N  N     . VAL   A 1 198 ? 156.090 130.800 120.602 1.00 83.25  ? 174 VAL   A N     1 
ATOM   1394 C  CA    . VAL   A 1 198 ? 154.846 130.548 121.319 1.00 81.63  ? 174 VAL   A CA    1 
ATOM   1395 C  C     . VAL   A 1 198 ? 154.180 131.888 121.594 1.00 80.78  ? 174 VAL   A C     1 
ATOM   1396 O  O     . VAL   A 1 198 ? 154.813 132.801 122.137 1.00 85.66  ? 174 VAL   A O     1 
ATOM   1397 C  CB    . VAL   A 1 198 ? 155.088 129.778 122.629 1.00 80.70  ? 174 VAL   A CB    1 
ATOM   1398 C  CG1   . VAL   A 1 198 ? 153.802 129.129 123.103 1.00 80.93  ? 174 VAL   A CG1   1 
ATOM   1399 C  CG2   . VAL   A 1 198 ? 156.179 128.733 122.442 1.00 81.24  ? 174 VAL   A CG2   1 
ATOM   1400 N  N     . ARG   A 1 199 ? 152.906 132.004 121.221 1.00 86.78  ? 175 ARG   A N     1 
ATOM   1401 C  CA    . ARG   A 1 199 ? 152.174 133.254 121.377 1.00 87.88  ? 175 ARG   A CA    1 
ATOM   1402 C  C     . ARG   A 1 199 ? 151.619 133.452 122.781 1.00 91.08  ? 175 ARG   A C     1 
ATOM   1403 O  O     . ARG   A 1 199 ? 151.226 134.573 123.120 1.00 88.73  ? 175 ARG   A O     1 
ATOM   1404 C  CB    . ARG   A 1 199 ? 151.023 133.315 120.373 1.00 89.81  ? 175 ARG   A CB    1 
ATOM   1405 C  CG    . ARG   A 1 199 ? 151.411 133.825 119.002 1.00 88.25  ? 175 ARG   A CG    1 
ATOM   1406 C  CD    . ARG   A 1 199 ? 152.220 135.109 119.060 1.00 89.75  ? 175 ARG   A CD    1 
ATOM   1407 N  NE    . ARG   A 1 199 ? 152.252 135.783 117.766 1.00 93.09  ? 175 ARG   A NE    1 
ATOM   1408 C  CZ    . ARG   A 1 199 ? 152.816 135.291 116.670 1.00 93.15  ? 175 ARG   A CZ    1 
ATOM   1409 N  NH1   . ARG   A 1 199 ? 153.462 134.136 116.680 1.00 90.68  ? 175 ARG   A NH1   1 
ATOM   1410 N  NH2   . ARG   A 1 199 ? 152.736 135.979 115.535 1.00 91.75  ? 175 ARG   A NH2   1 
ATOM   1411 N  N     . ASP   A 1 200 ? 151.573 132.401 123.598 1.00 89.55  ? 176 ASP   A N     1 
ATOM   1412 C  CA    . ASP   A 1 200 ? 151.011 132.499 124.937 1.00 85.24  ? 176 ASP   A CA    1 
ATOM   1413 C  C     . ASP   A 1 200 ? 151.893 133.280 125.901 1.00 86.95  ? 176 ASP   A C     1 
ATOM   1414 O  O     . ASP   A 1 200 ? 151.385 133.775 126.913 1.00 90.26  ? 176 ASP   A O     1 
ATOM   1415 C  CB    . ASP   A 1 200 ? 150.754 131.100 125.500 1.00 84.71  ? 176 ASP   A CB    1 
ATOM   1416 C  CG    . ASP   A 1 200 ? 149.859 130.270 124.604 1.00 84.84  ? 176 ASP   A CG    1 
ATOM   1417 O  OD1   . ASP   A 1 200 ? 150.236 130.036 123.438 1.00 84.98  ? 176 ASP   A OD1   1 
ATOM   1418 O  OD2   . ASP   A 1 200 ? 148.777 129.850 125.066 1.00 86.57  ? 176 ASP   A OD2   1 
ATOM   1419 N  N     . THR   A 1 201 ? 153.190 133.412 125.608 1.00 82.96  ? 177 THR   A N     1 
ATOM   1420 C  CA    . THR   A 1 201 ? 154.092 134.107 126.521 1.00 81.37  ? 177 THR   A CA    1 
ATOM   1421 C  C     . THR   A 1 201 ? 153.681 135.558 126.726 1.00 79.13  ? 177 THR   A C     1 
ATOM   1422 O  O     . THR   A 1 201 ? 153.791 136.078 127.843 1.00 84.24  ? 177 THR   A O     1 
ATOM   1423 C  CB    . THR   A 1 201 ? 155.529 134.034 126.004 1.00 84.67  ? 177 THR   A CB    1 
ATOM   1424 O  OG1   . THR   A 1 201 ? 155.726 135.032 124.995 1.00 85.22  ? 177 THR   A OG1   1 
ATOM   1425 C  CG2   . THR   A 1 201 ? 155.811 132.662 125.412 1.00 82.53  ? 177 THR   A CG2   1 
ATOM   1426 N  N     . GLN   A 1 202 ? 153.200 136.222 125.672 1.00 76.28  ? 178 GLN   A N     1 
ATOM   1427 C  CA    . GLN   A 1 202 ? 152.742 137.600 125.811 1.00 78.40  ? 178 GLN   A CA    1 
ATOM   1428 C  C     . GLN   A 1 202 ? 151.587 137.713 126.798 1.00 80.25  ? 178 GLN   A C     1 
ATOM   1429 O  O     . GLN   A 1 202 ? 151.387 138.777 127.394 1.00 79.51  ? 178 GLN   A O     1 
ATOM   1430 C  CB    . GLN   A 1 202 ? 152.332 138.156 124.448 1.00 79.90  ? 178 GLN   A CB    1 
ATOM   1431 C  CG    . GLN   A 1 202 ? 153.400 138.012 123.377 1.00 82.65  ? 178 GLN   A CG    1 
ATOM   1432 C  CD    . GLN   A 1 202 ? 152.929 138.487 122.018 1.00 86.86  ? 178 GLN   A CD    1 
ATOM   1433 O  OE1   . GLN   A 1 202 ? 151.961 139.240 121.911 1.00 86.39  ? 178 GLN   A OE1   1 
ATOM   1434 N  NE2   . GLN   A 1 202 ? 153.615 138.050 120.970 1.00 87.29  ? 178 GLN   A NE2   1 
ATOM   1435 N  N     . MET   A 1 203 ? 150.819 136.638 126.982 1.00 83.68  ? 179 MET   A N     1 
ATOM   1436 C  CA    . MET   A 1 203 ? 149.778 136.640 128.002 1.00 81.40  ? 179 MET   A CA    1 
ATOM   1437 C  C     . MET   A 1 203 ? 150.335 136.315 129.381 1.00 80.66  ? 179 MET   A C     1 
ATOM   1438 O  O     . MET   A 1 203 ? 149.785 136.770 130.390 1.00 82.51  ? 179 MET   A O     1 
ATOM   1439 C  CB    . MET   A 1 203 ? 148.676 135.644 127.636 1.00 82.94  ? 179 MET   A CB    1 
ATOM   1440 C  CG    . MET   A 1 203 ? 148.248 135.696 126.179 1.00 84.45  ? 179 MET   A CG    1 
ATOM   1441 S  SD    . MET   A 1 203 ? 146.992 136.950 125.866 1.00 92.60  ? 179 MET   A SD    1 
ATOM   1442 C  CE    . MET   A 1 203 ? 146.051 136.880 127.388 1.00 84.74  ? 179 MET   A CE    1 
ATOM   1443 N  N     . LEU   A 1 204 ? 151.417 135.536 129.445 1.00 77.59  ? 180 LEU   A N     1 
ATOM   1444 C  CA    . LEU   A 1 204 ? 152.001 135.185 130.734 1.00 77.67  ? 180 LEU   A CA    1 
ATOM   1445 C  C     . LEU   A 1 204 ? 152.791 136.343 131.329 1.00 78.72  ? 180 LEU   A C     1 
ATOM   1446 O  O     . LEU   A 1 204 ? 152.846 136.485 132.557 1.00 83.54  ? 180 LEU   A O     1 
ATOM   1447 C  CB    . LEU   A 1 204 ? 152.897 133.957 130.588 1.00 76.80  ? 180 LEU   A CB    1 
ATOM   1448 C  CG    . LEU   A 1 204 ? 152.386 132.659 131.212 1.00 79.59  ? 180 LEU   A CG    1 
ATOM   1449 C  CD1   . LEU   A 1 204 ? 153.364 131.526 130.954 1.00 76.88  ? 180 LEU   A CD1   1 
ATOM   1450 C  CD2   . LEU   A 1 204 ? 152.152 132.839 132.702 1.00 80.48  ? 180 LEU   A CD2   1 
ATOM   1451 N  N     . MET   A 1 205 ? 153.392 137.182 130.481 1.00 79.58  ? 181 MET   A N     1 
ATOM   1452 C  CA    . MET   A 1 205 ? 154.237 138.266 130.972 1.00 76.23  ? 181 MET   A CA    1 
ATOM   1453 C  C     . MET   A 1 205 ? 153.463 139.194 131.897 1.00 76.23  ? 181 MET   A C     1 
ATOM   1454 O  O     . MET   A 1 205 ? 153.950 139.553 132.976 1.00 79.79  ? 181 MET   A O     1 
ATOM   1455 C  CB    . MET   A 1 205 ? 154.817 139.047 129.793 1.00 72.40  ? 181 MET   A CB    1 
ATOM   1456 C  CG    . MET   A 1 205 ? 156.308 139.314 129.891 1.00 76.83  ? 181 MET   A CG    1 
ATOM   1457 S  SD    . MET   A 1 205 ? 157.294 137.810 129.795 1.00 82.51  ? 181 MET   A SD    1 
ATOM   1458 C  CE    . MET   A 1 205 ? 158.405 138.048 131.178 1.00 81.78  ? 181 MET   A CE    1 
ATOM   1459 N  N     . GLN   A 1 206 ? 152.242 139.568 131.506 1.00 80.16  ? 182 GLN   A N     1 
ATOM   1460 C  CA    . GLN   A 1 206 ? 151.426 140.442 132.341 1.00 80.84  ? 182 GLN   A CA    1 
ATOM   1461 C  C     . GLN   A 1 206 ? 151.188 139.842 133.719 1.00 82.16  ? 182 GLN   A C     1 
ATOM   1462 O  O     . GLN   A 1 206 ? 151.032 140.583 134.696 1.00 85.17  ? 182 GLN   A O     1 
ATOM   1463 C  CB    . GLN   A 1 206 ? 150.092 140.729 131.655 1.00 83.32  ? 182 GLN   A CB    1 
ATOM   1464 C  CG    . GLN   A 1 206 ? 150.123 141.912 130.704 1.00 85.27  ? 182 GLN   A CG    1 
ATOM   1465 C  CD    . GLN   A 1 206 ? 149.498 141.593 129.361 1.00 87.18  ? 182 GLN   A CD    1 
ATOM   1466 O  OE1   . GLN   A 1 206 ? 148.713 140.653 129.236 1.00 86.12  ? 182 GLN   A OE1   1 
ATOM   1467 N  NE2   . GLN   A 1 206 ? 149.845 142.376 128.346 1.00 85.59  ? 182 GLN   A NE2   1 
ATOM   1468 N  N     . ALA   A 1 207 ? 151.154 138.513 133.821 1.00 75.89  ? 183 ALA   A N     1 
ATOM   1469 C  CA    . ALA   A 1 207 ? 150.999 137.881 135.124 1.00 73.35  ? 183 ALA   A CA    1 
ATOM   1470 C  C     . ALA   A 1 207 ? 152.285 137.926 135.938 1.00 73.03  ? 183 ALA   A C     1 
ATOM   1471 O  O     . ALA   A 1 207 ? 152.229 138.060 137.165 1.00 75.92  ? 183 ALA   A O     1 
ATOM   1472 C  CB    . ALA   A 1 207 ? 150.535 136.434 134.958 1.00 73.94  ? 183 ALA   A CB    1 
ATOM   1473 N  N     . ILE   A 1 208 ? 153.442 137.810 135.283 1.00 68.25  ? 184 ILE   A N     1 
ATOM   1474 C  CA    . ILE   A 1 208 ? 154.703 137.768 136.017 1.00 66.27  ? 184 ILE   A CA    1 
ATOM   1475 C  C     . ILE   A 1 208 ? 155.030 139.134 136.606 1.00 65.53  ? 184 ILE   A C     1 
ATOM   1476 O  O     . ILE   A 1 208 ? 155.393 139.247 137.784 1.00 69.46  ? 184 ILE   A O     1 
ATOM   1477 C  CB    . ILE   A 1 208 ? 155.833 137.261 135.104 1.00 65.72  ? 184 ILE   A CB    1 
ATOM   1478 C  CG1   . ILE   A 1 208 ? 155.563 135.818 134.673 1.00 68.67  ? 184 ILE   A CG1   1 
ATOM   1479 C  CG2   . ILE   A 1 208 ? 157.174 137.366 135.808 1.00 68.80  ? 184 ILE   A CG2   1 
ATOM   1480 C  CD1   . ILE   A 1 208 ? 156.649 135.230 133.803 1.00 67.08  ? 184 ILE   A CD1   1 
ATOM   1481 N  N     . LEU   A 1 209 ? 154.882 140.193 135.806 1.00 55.72  ? 185 LEU   A N     1 
ATOM   1482 C  CA    . LEU   A 1 209 ? 155.330 141.518 136.221 1.00 52.60  ? 185 LEU   A CA    1 
ATOM   1483 C  C     . LEU   A 1 209 ? 154.605 141.999 137.471 1.00 54.11  ? 185 LEU   A C     1 
ATOM   1484 O  O     . LEU   A 1 209 ? 155.222 142.638 138.331 1.00 57.09  ? 185 LEU   A O     1 
ATOM   1485 C  CB    . LEU   A 1 209 ? 155.147 142.510 135.073 1.00 53.58  ? 185 LEU   A CB    1 
ATOM   1486 C  CG    . LEU   A 1 209 ? 156.168 142.361 133.942 1.00 56.02  ? 185 LEU   A CG    1 
ATOM   1487 C  CD1   . LEU   A 1 209 ? 155.739 143.140 132.712 1.00 57.17  ? 185 LEU   A CD1   1 
ATOM   1488 C  CD2   . LEU   A 1 209 ? 157.549 142.798 134.401 1.00 52.50  ? 185 LEU   A CD2   1 
ATOM   1489 N  N     . ARG   A 1 210 ? 153.312 141.691 137.598 1.00 51.09  ? 186 ARG   A N     1 
ATOM   1490 C  CA    . ARG   A 1 210 ? 152.585 142.049 138.812 1.00 45.51  ? 186 ARG   A CA    1 
ATOM   1491 C  C     . ARG   A 1 210 ? 153.240 141.439 140.044 1.00 52.03  ? 186 ARG   A C     1 
ATOM   1492 O  O     . ARG   A 1 210 ? 153.400 142.116 141.067 1.00 55.55  ? 186 ARG   A O     1 
ATOM   1493 C  CB    . ARG   A 1 210 ? 151.129 141.600 138.703 1.00 51.50  ? 186 ARG   A CB    1 
ATOM   1494 C  CG    . ARG   A 1 210 ? 150.203 142.638 138.099 1.00 60.44  ? 186 ARG   A CG    1 
ATOM   1495 C  CD    . ARG   A 1 210 ? 148.792 142.096 137.956 1.00 58.79  ? 186 ARG   A CD    1 
ATOM   1496 N  NE    . ARG   A 1 210 ? 148.390 142.000 136.558 1.00 58.34  ? 186 ARG   A NE    1 
ATOM   1497 C  CZ    . ARG   A 1 210 ? 147.799 142.974 135.880 1.00 61.69  ? 186 ARG   A CZ    1 
ATOM   1498 N  NH1   . ARG   A 1 210 ? 147.519 144.138 136.444 1.00 60.04  ? 186 ARG   A NH1   1 
ATOM   1499 N  NH2   . ARG   A 1 210 ? 147.480 142.776 134.604 1.00 60.08  ? 186 ARG   A NH2   1 
ATOM   1500 N  N     . ILE   A 1 211 ? 153.647 140.171 139.957 1.00 46.14  ? 187 ILE   A N     1 
ATOM   1501 C  CA    . ILE   A 1 211 ? 154.338 139.538 141.074 1.00 40.49  ? 187 ILE   A CA    1 
ATOM   1502 C  C     . ILE   A 1 211 ? 155.648 140.259 141.363 1.00 48.11  ? 187 ILE   A C     1 
ATOM   1503 O  O     . ILE   A 1 211 ? 156.073 140.364 142.519 1.00 54.52  ? 187 ILE   A O     1 
ATOM   1504 C  CB    . ILE   A 1 211 ? 154.563 138.043 140.785 1.00 49.37  ? 187 ILE   A CB    1 
ATOM   1505 C  CG1   . ILE   A 1 211 ? 153.260 137.386 140.334 1.00 45.90  ? 187 ILE   A CG1   1 
ATOM   1506 C  CG2   . ILE   A 1 211 ? 155.112 137.337 142.012 1.00 47.89  ? 187 ILE   A CG2   1 
ATOM   1507 C  CD1   . ILE   A 1 211 ? 153.404 135.922 139.994 1.00 44.88  ? 187 ILE   A CD1   1 
ATOM   1508 N  N     . LEU   A 1 212 ? 156.304 140.773 140.321 1.00 45.48  ? 188 LEU   A N     1 
ATOM   1509 C  CA    . LEU   A 1 212 ? 157.552 141.497 140.526 1.00 40.87  ? 188 LEU   A CA    1 
ATOM   1510 C  C     . LEU   A 1 212 ? 157.308 142.884 141.106 1.00 44.76  ? 188 LEU   A C     1 
ATOM   1511 O  O     . LEU   A 1 212 ? 158.252 143.533 141.571 1.00 51.60  ? 188 LEU   A O     1 
ATOM   1512 C  CB    . LEU   A 1 212 ? 158.320 141.601 139.209 1.00 47.17  ? 188 LEU   A CB    1 
ATOM   1513 C  CG    . LEU   A 1 212 ? 158.835 140.296 138.598 1.00 50.53  ? 188 LEU   A CG    1 
ATOM   1514 C  CD1   . LEU   A 1 212 ? 159.946 140.576 137.600 1.00 48.56  ? 188 LEU   A CD1   1 
ATOM   1515 C  CD2   . LEU   A 1 212 ? 159.309 139.331 139.674 1.00 48.13  ? 188 LEU   A CD2   1 
ATOM   1516 N  N     . PHE   A 1 213 ? 156.060 143.354 141.092 1.00 39.82  ? 189 PHE   A N     1 
ATOM   1517 C  CA    . PHE   A 1 213 ? 155.771 144.699 141.577 1.00 31.26  ? 189 PHE   A CA    1 
ATOM   1518 C  C     . PHE   A 1 213 ? 155.453 144.699 143.066 1.00 42.37  ? 189 PHE   A C     1 
ATOM   1519 O  O     . PHE   A 1 213 ? 156.039 145.468 143.835 1.00 43.85  ? 189 PHE   A O     1 
ATOM   1520 C  CB    . PHE   A 1 213 ? 154.610 145.299 140.783 1.00 33.72  ? 189 PHE   A CB    1 
ATOM   1521 C  CG    . PHE   A 1 213 ? 154.250 146.696 141.193 1.00 35.99  ? 189 PHE   A CG    1 
ATOM   1522 C  CD1   . PHE   A 1 213 ? 155.232 147.636 141.442 1.00 41.26  ? 189 PHE   A CD1   1 
ATOM   1523 C  CD2   . PHE   A 1 213 ? 152.925 147.070 141.323 1.00 43.46  ? 189 PHE   A CD2   1 
ATOM   1524 C  CE1   . PHE   A 1 213 ? 154.899 148.922 141.814 1.00 40.55  ? 189 PHE   A CE1   1 
ATOM   1525 C  CE2   . PHE   A 1 213 ? 152.588 148.354 141.695 1.00 35.27  ? 189 PHE   A CE2   1 
ATOM   1526 C  CZ    . PHE   A 1 213 ? 153.576 149.280 141.941 1.00 37.51  ? 189 PHE   A CZ    1 
ATOM   1527 N  N     . TYR   A 1 214 ? 154.524 143.842 143.490 1.00 44.99  ? 190 TYR   A N     1 
ATOM   1528 C  CA    . TYR   A 1 214 ? 154.069 143.840 144.873 1.00 37.22  ? 190 TYR   A CA    1 
ATOM   1529 C  C     . TYR   A 1 214 ? 155.063 143.185 145.822 1.00 44.96  ? 190 TYR   A C     1 
ATOM   1530 O  O     . TYR   A 1 214 ? 155.092 143.539 147.005 1.00 56.51  ? 190 TYR   A O     1 
ATOM   1531 C  CB    . TYR   A 1 214 ? 152.715 143.140 144.968 1.00 34.36  ? 190 TYR   A CB    1 
ATOM   1532 C  CG    . TYR   A 1 214 ? 151.569 144.001 144.495 1.00 42.73  ? 190 TYR   A CG    1 
ATOM   1533 C  CD1   . TYR   A 1 214 ? 151.231 145.168 145.164 1.00 42.15  ? 190 TYR   A CD1   1 
ATOM   1534 C  CD2   . TYR   A 1 214 ? 150.836 143.656 143.370 1.00 42.15  ? 190 TYR   A CD2   1 
ATOM   1535 C  CE1   . TYR   A 1 214 ? 150.188 145.961 144.732 1.00 39.33  ? 190 TYR   A CE1   1 
ATOM   1536 C  CE2   . TYR   A 1 214 ? 149.792 144.442 142.930 1.00 38.31  ? 190 TYR   A CE2   1 
ATOM   1537 C  CZ    . TYR   A 1 214 ? 149.472 145.593 143.615 1.00 43.08  ? 190 TYR   A CZ    1 
ATOM   1538 O  OH    . TYR   A 1 214 ? 148.432 146.380 143.180 1.00 47.79  ? 190 TYR   A OH    1 
ATOM   1539 N  N     . PHE   A 1 215 ? 155.871 142.245 145.339 1.00 36.37  ? 191 PHE   A N     1 
ATOM   1540 C  CA    . PHE   A 1 215 ? 156.916 141.630 146.154 1.00 32.94  ? 191 PHE   A CA    1 
ATOM   1541 C  C     . PHE   A 1 215 ? 158.235 142.364 145.917 1.00 49.88  ? 191 PHE   A C     1 
ATOM   1542 O  O     . PHE   A 1 215 ? 159.208 141.825 145.390 1.00 52.01  ? 191 PHE   A O     1 
ATOM   1543 C  CB    . PHE   A 1 215 ? 157.025 140.142 145.840 1.00 35.78  ? 191 PHE   A CB    1 
ATOM   1544 C  CG    . PHE   A 1 215 ? 155.852 139.337 146.320 1.00 55.44  ? 191 PHE   A CG    1 
ATOM   1545 C  CD1   . PHE   A 1 215 ? 154.731 139.179 145.522 1.00 55.73  ? 191 PHE   A CD1   1 
ATOM   1546 C  CD2   . PHE   A 1 215 ? 155.867 138.745 147.570 1.00 57.08  ? 191 PHE   A CD2   1 
ATOM   1547 C  CE1   . PHE   A 1 215 ? 153.648 138.442 145.962 1.00 44.79  ? 191 PHE   A CE1   1 
ATOM   1548 C  CE2   . PHE   A 1 215 ? 154.787 138.007 148.015 1.00 55.49  ? 191 PHE   A CE2   1 
ATOM   1549 C  CZ    . PHE   A 1 215 ? 153.676 137.856 147.210 1.00 49.54  ? 191 PHE   A CZ    1 
ATOM   1550 N  N     . SER   A 1 216 ? 158.242 143.629 146.327 1.00 54.44  ? 192 SER   A N     1 
ATOM   1551 C  CA    . SER   A 1 216 ? 159.364 144.524 146.089 1.00 42.77  ? 192 SER   A CA    1 
ATOM   1552 C  C     . SER   A 1 216 ? 159.326 145.626 147.139 1.00 55.37  ? 192 SER   A C     1 
ATOM   1553 O  O     . SER   A 1 216 ? 158.270 145.888 147.727 1.00 56.05  ? 192 SER   A O     1 
ATOM   1554 C  CB    . SER   A 1 216 ? 159.304 145.120 144.673 1.00 45.95  ? 192 SER   A CB    1 
ATOM   1555 O  OG    . SER   A 1 216 ? 160.586 145.143 144.074 1.00 52.29  ? 192 SER   A OG    1 
ATOM   1556 N  N     . PRO   A 1 217 ? 160.460 146.293 147.398 1.00 50.84  ? 193 PRO   A N     1 
ATOM   1557 C  CA    . PRO   A 1 217 ? 160.469 147.362 148.406 1.00 44.68  ? 193 PRO   A CA    1 
ATOM   1558 C  C     . PRO   A 1 217 ? 159.930 148.680 147.877 1.00 42.45  ? 193 PRO   A C     1 
ATOM   1559 O  O     . PRO   A 1 217 ? 160.139 149.731 148.489 1.00 47.36  ? 193 PRO   A O     1 
ATOM   1560 C  CB    . PRO   A 1 217 ? 161.953 147.488 148.780 1.00 45.91  ? 193 PRO   A CB    1 
ATOM   1561 C  CG    . PRO   A 1 217 ? 162.637 146.332 148.132 1.00 44.87  ? 193 PRO   A CG    1 
ATOM   1562 C  CD    . PRO   A 1 217 ? 161.820 145.972 146.945 1.00 43.13  ? 193 PRO   A CD    1 
ATOM   1563 N  N     . ILE   A 1 218 ? 159.247 148.637 146.734 1.00 42.26  ? 194 ILE   A N     1 
ATOM   1564 C  CA    . ILE   A 1 218 ? 158.726 149.860 146.134 1.00 39.20  ? 194 ILE   A CA    1 
ATOM   1565 C  C     . ILE   A 1 218 ? 157.666 150.492 147.029 1.00 40.63  ? 194 ILE   A C     1 
ATOM   1566 O  O     . ILE   A 1 218 ? 157.650 151.713 147.224 1.00 50.06  ? 194 ILE   A O     1 
ATOM   1567 C  CB    . ILE   A 1 218 ? 158.184 149.568 144.724 1.00 43.16  ? 194 ILE   A CB    1 
ATOM   1568 C  CG1   . ILE   A 1 218 ? 159.304 149.042 143.826 1.00 42.67  ? 194 ILE   A CG1   1 
ATOM   1569 C  CG2   . ILE   A 1 218 ? 157.574 150.811 144.124 1.00 35.10  ? 194 ILE   A CG2   1 
ATOM   1570 C  CD1   . ILE   A 1 218 ? 158.823 148.516 142.496 1.00 40.92  ? 194 ILE   A CD1   1 
ATOM   1571 N  N     . LEU   A 1 219 ? 156.768 149.679 147.592 1.00 45.83  ? 195 LEU   A N     1 
ATOM   1572 C  CA    . LEU   A 1 219 ? 155.668 150.188 148.401 1.00 40.72  ? 195 LEU   A CA    1 
ATOM   1573 C  C     . LEU   A 1 219 ? 155.749 149.819 149.875 1.00 41.23  ? 195 LEU   A C     1 
ATOM   1574 O  O     . LEU   A 1 219 ? 155.121 150.496 150.693 1.00 41.78  ? 195 LEU   A O     1 
ATOM   1575 C  CB    . LEU   A 1 219 ? 154.323 149.686 147.853 1.00 38.85  ? 195 LEU   A CB    1 
ATOM   1576 C  CG    . LEU   A 1 219 ? 154.029 149.866 146.364 1.00 43.53  ? 195 LEU   A CG    1 
ATOM   1577 C  CD1   . LEU   A 1 219 ? 153.122 148.756 145.869 1.00 38.21  ? 195 LEU   A CD1   1 
ATOM   1578 C  CD2   . LEU   A 1 219 ? 153.399 151.220 146.106 1.00 40.65  ? 195 LEU   A CD2   1 
ATOM   1579 N  N     . TRP   A 1 220 ? 156.493 148.777 150.236 1.00 51.36  ? 196 TRP   A N     1 
ATOM   1580 C  CA    . TRP   A 1 220 ? 156.505 148.298 151.610 1.00 48.17  ? 196 TRP   A CA    1 
ATOM   1581 C  C     . TRP   A 1 220 ? 157.879 147.736 151.943 1.00 55.05  ? 196 TRP   A C     1 
ATOM   1582 O  O     . TRP   A 1 220 ? 158.683 147.442 151.056 1.00 56.89  ? 196 TRP   A O     1 
ATOM   1583 C  CB    . TRP   A 1 220 ? 155.425 147.235 151.839 1.00 51.00  ? 196 TRP   A CB    1 
ATOM   1584 C  CG    . TRP   A 1 220 ? 155.762 145.903 151.244 1.00 53.57  ? 196 TRP   A CG    1 
ATOM   1585 C  CD1   . TRP   A 1 220 ? 155.925 145.616 149.921 1.00 50.50  ? 196 TRP   A CD1   1 
ATOM   1586 C  CD2   . TRP   A 1 220 ? 155.981 144.677 151.950 1.00 51.73  ? 196 TRP   A CD2   1 
ATOM   1587 N  NE1   . TRP   A 1 220 ? 156.230 144.287 149.759 1.00 45.37  ? 196 TRP   A NE1   1 
ATOM   1588 C  CE2   . TRP   A 1 220 ? 156.271 143.689 150.990 1.00 47.79  ? 196 TRP   A CE2   1 
ATOM   1589 C  CE3   . TRP   A 1 220 ? 155.959 144.319 153.301 1.00 50.17  ? 196 TRP   A CE3   1 
ATOM   1590 C  CZ2   . TRP   A 1 220 ? 156.537 142.368 151.337 1.00 50.44  ? 196 TRP   A CZ2   1 
ATOM   1591 C  CZ3   . TRP   A 1 220 ? 156.222 143.008 153.642 1.00 56.83  ? 196 TRP   A CZ3   1 
ATOM   1592 C  CH2   . TRP   A 1 220 ? 156.508 142.048 152.665 1.00 56.64  ? 196 TRP   A CH2   1 
ATOM   1593 N  N     . LEU   A 1 221 ? 158.138 147.592 153.241 1.00 72.28  ? 197 LEU   A N     1 
ATOM   1594 C  CA    . LEU   A 1 221 ? 159.400 147.052 153.738 1.00 72.56  ? 197 LEU   A CA    1 
ATOM   1595 C  C     . LEU   A 1 221 ? 159.088 145.894 154.677 1.00 76.62  ? 197 LEU   A C     1 
ATOM   1596 O  O     . LEU   A 1 221 ? 158.344 146.083 155.661 1.00 83.07  ? 197 LEU   A O     1 
ATOM   1597 C  CB    . LEU   A 1 221 ? 160.215 148.134 154.452 1.00 73.81  ? 197 LEU   A CB    1 
ATOM   1598 C  CG    . LEU   A 1 221 ? 161.531 148.571 153.802 1.00 74.88  ? 197 LEU   A CG    1 
ATOM   1599 C  CD1   . LEU   A 1 221 ? 162.318 149.466 154.743 1.00 72.66  ? 197 LEU   A CD1   1 
ATOM   1600 C  CD2   . LEU   A 1 221 ? 162.364 147.371 153.381 1.00 73.99  ? 197 LEU   A CD2   1 
ATOM   1601 N  N     . PRO   A 1 222 ? 159.613 144.697 154.427 1.00 81.71  ? 198 PRO   A N     1 
ATOM   1602 C  CA    . PRO   A 1 222 ? 159.314 143.560 155.306 1.00 82.67  ? 198 PRO   A CA    1 
ATOM   1603 C  C     . PRO   A 1 222 ? 159.903 143.746 156.697 1.00 83.32  ? 198 PRO   A C     1 
ATOM   1604 O  O     . PRO   A 1 222 ? 160.839 144.518 156.914 1.00 80.69  ? 198 PRO   A O     1 
ATOM   1605 C  CB    . PRO   A 1 222 ? 159.955 142.366 154.588 1.00 83.51  ? 198 PRO   A CB    1 
ATOM   1606 C  CG    . PRO   A 1 222 ? 160.921 142.956 153.617 1.00 79.79  ? 198 PRO   A CG    1 
ATOM   1607 C  CD    . PRO   A 1 222 ? 160.397 144.303 153.245 1.00 77.91  ? 198 PRO   A CD    1 
ATOM   1608 N  N     . LYS   A 1 223 ? 159.336 143.012 157.661 1.00 100.51 ? 199 LYS   A N     1 
ATOM   1609 C  CA    . LYS   A 1 223 ? 159.751 143.191 159.078 1.00 101.95 ? 199 LYS   A CA    1 
ATOM   1610 C  C     . LYS   A 1 223 ? 160.699 142.075 159.540 1.00 100.39 ? 199 LYS   A C     1 
ATOM   1611 O  O     . LYS   A 1 223 ? 161.386 142.308 160.561 1.00 98.20  ? 199 LYS   A O     1 
ATOM   1612 C  CB    . LYS   A 1 223 ? 158.511 143.180 159.977 1.00 101.67 ? 199 LYS   A CB    1 
ATOM   1613 C  CG    . LYS   A 1 223 ? 158.665 143.868 161.325 1.00 101.73 ? 199 LYS   A CG    1 
ATOM   1614 C  CD    . LYS   A 1 223 ? 157.524 144.828 161.634 1.00 97.52  ? 199 LYS   A CD    1 
ATOM   1615 C  CE    . LYS   A 1 223 ? 157.252 145.770 160.505 1.00 98.56  ? 199 LYS   A CE    1 
ATOM   1616 N  NZ    . LYS   A 1 223 ? 156.161 146.690 160.832 1.00 99.10  ? 199 LYS   A NZ    1 
ATOM   1617 N  N     . ASN   A 1 224 ? 160.697 140.918 158.863 1.00 118.73 ? 200 ASN   A N     1 
ATOM   1618 C  CA    . ASN   A 1 224 ? 161.565 139.807 159.245 1.00 121.42 ? 200 ASN   A CA    1 
ATOM   1619 C  C     . ASN   A 1 224 ? 161.169 139.193 160.586 1.00 121.79 ? 200 ASN   A C     1 
ATOM   1620 O  O     . ASN   A 1 224 ? 160.094 139.488 161.118 1.00 120.61 ? 200 ASN   A O     1 
ATOM   1621 C  CB    . ASN   A 1 224 ? 163.030 140.258 159.285 1.00 121.38 ? 200 ASN   A CB    1 
ATOM   1622 C  CG    . ASN   A 1 224 ? 163.991 139.161 158.864 1.00 122.41 ? 200 ASN   A CG    1 
ATOM   1623 O  OD1   . ASN   A 1 224 ? 164.299 138.259 159.643 1.00 121.66 ? 200 ASN   A OD1   1 
ATOM   1624 N  ND2   . ASN   A 1 224 ? 164.472 139.236 157.628 1.00 120.13 ? 200 ASN   A ND2   1 
ATOM   1625 N  N     . HIS   A 1 225 ? 162.033 138.317 161.112 1.00 125.05 ? 201 HIS   A N     1 
ATOM   1626 C  CA    . HIS   A 1 225 ? 161.855 137.650 162.409 1.00 125.53 ? 201 HIS   A CA    1 
ATOM   1627 C  C     . HIS   A 1 225 ? 160.459 137.043 162.558 1.00 126.34 ? 201 HIS   A C     1 
ATOM   1628 O  O     . HIS   A 1 225 ? 159.789 137.203 163.580 1.00 127.67 ? 201 HIS   A O     1 
ATOM   1629 C  CB    . HIS   A 1 225 ? 162.185 138.593 163.576 1.00 124.33 ? 201 HIS   A CB    1 
ATOM   1630 C  CG    . HIS   A 1 225 ? 161.209 139.714 163.765 1.00 126.55 ? 201 HIS   A CG    1 
ATOM   1631 N  ND1   . HIS   A 1 225 ? 159.964 139.530 164.327 1.00 126.76 ? 201 HIS   A ND1   1 
ATOM   1632 C  CD2   . HIS   A 1 225 ? 161.302 141.034 163.481 1.00 126.45 ? 201 HIS   A CD2   1 
ATOM   1633 C  CE1   . HIS   A 1 225 ? 159.328 140.688 164.372 1.00 125.37 ? 201 HIS   A CE1   1 
ATOM   1634 N  NE2   . HIS   A 1 225 ? 160.118 141.616 163.864 1.00 125.33 ? 201 HIS   A NE2   1 
ATOM   1635 N  N     . GLY   A 1 226 ? 160.024 136.320 161.530 1.00 108.26 ? 202 GLY   A N     1 
ATOM   1636 C  CA    . GLY   A 1 226 ? 158.745 135.640 161.572 1.00 108.52 ? 202 GLY   A CA    1 
ATOM   1637 C  C     . GLY   A 1 226 ? 158.386 134.999 160.249 1.00 109.55 ? 202 GLY   A C     1 
ATOM   1638 O  O     . GLY   A 1 226 ? 159.267 134.524 159.526 1.00 109.45 ? 202 GLY   A O     1 
ATOM   1639 N  N     . ILE   A 1 227 ? 157.091 134.972 159.918 1.00 110.82 ? 203 ILE   A N     1 
ATOM   1640 C  CA    . ILE   A 1 227 ? 156.671 134.504 158.598 1.00 111.05 ? 203 ILE   A CA    1 
ATOM   1641 C  C     . ILE   A 1 227 ? 157.071 135.470 157.497 1.00 109.00 ? 203 ILE   A C     1 
ATOM   1642 O  O     . ILE   A 1 227 ? 157.092 135.082 156.322 1.00 105.15 ? 203 ILE   A O     1 
ATOM   1643 C  CB    . ILE   A 1 227 ? 155.151 134.254 158.557 1.00 111.97 ? 203 ILE   A CB    1 
ATOM   1644 C  CG1   . ILE   A 1 227 ? 154.831 133.060 157.648 1.00 110.67 ? 203 ILE   A CG1   1 
ATOM   1645 C  CG2   . ILE   A 1 227 ? 154.397 135.516 158.138 1.00 110.60 ? 203 ILE   A CG2   1 
ATOM   1646 C  CD1   . ILE   A 1 227 ? 154.241 133.434 156.299 1.00 107.82 ? 203 ILE   A CD1   1 
ATOM   1647 N  N     . SER   A 1 228 ? 157.394 136.716 157.843 1.00 106.42 ? 204 SER   A N     1 
ATOM   1648 C  CA    . SER   A 1 228 ? 157.913 137.679 156.885 1.00 106.94 ? 204 SER   A CA    1 
ATOM   1649 C  C     . SER   A 1 228 ? 159.425 137.600 156.728 1.00 107.01 ? 204 SER   A C     1 
ATOM   1650 O  O     . SER   A 1 228 ? 159.968 138.212 155.802 1.00 107.73 ? 204 SER   A O     1 
ATOM   1651 C  CB    . SER   A 1 228 ? 157.516 139.100 157.298 1.00 109.60 ? 204 SER   A CB    1 
ATOM   1652 O  OG    . SER   A 1 228 ? 158.284 139.539 158.404 1.00 110.75 ? 204 SER   A OG    1 
ATOM   1653 N  N     . GLY   A 1 229 ? 160.115 136.870 157.607 1.00 102.61 ? 205 GLY   A N     1 
ATOM   1654 C  CA    . GLY   A 1 229 ? 161.541 136.662 157.421 1.00 100.99 ? 205 GLY   A CA    1 
ATOM   1655 C  C     . GLY   A 1 229 ? 161.845 135.835 156.187 1.00 102.53 ? 205 GLY   A C     1 
ATOM   1656 O  O     . GLY   A 1 229 ? 162.770 136.145 155.432 1.00 104.69 ? 205 GLY   A O     1 
ATOM   1657 N  N     . LEU   A 1 230 ? 161.069 134.771 155.965 1.00 93.65  ? 206 LEU   A N     1 
ATOM   1658 C  CA    . LEU   A 1 230 ? 161.192 134.016 154.725 1.00 92.74  ? 206 LEU   A CA    1 
ATOM   1659 C  C     . LEU   A 1 230 ? 160.836 134.877 153.521 1.00 95.31  ? 206 LEU   A C     1 
ATOM   1660 O  O     . LEU   A 1 230 ? 161.477 134.766 152.471 1.00 97.49  ? 206 LEU   A O     1 
ATOM   1661 C  CB    . LEU   A 1 230 ? 160.307 132.768 154.781 1.00 93.26  ? 206 LEU   A CB    1 
ATOM   1662 C  CG    . LEU   A 1 230 ? 160.506 131.669 153.731 1.00 96.95  ? 206 LEU   A CG    1 
ATOM   1663 C  CD1   . LEU   A 1 230 ? 159.673 131.918 152.478 1.00 96.75  ? 206 LEU   A CD1   1 
ATOM   1664 C  CD2   . LEU   A 1 230 ? 161.980 131.518 153.378 1.00 94.45  ? 206 LEU   A CD2   1 
ATOM   1665 N  N     . ILE   A 1 231 ? 159.828 135.741 153.657 1.00 88.55  ? 207 ILE   A N     1 
ATOM   1666 C  CA    . ILE   A 1 231 ? 159.490 136.668 152.582 1.00 88.04  ? 207 ILE   A CA    1 
ATOM   1667 C  C     . ILE   A 1 231 ? 160.649 137.621 152.315 1.00 86.23  ? 207 ILE   A C     1 
ATOM   1668 O  O     . ILE   A 1 231 ? 160.972 137.917 151.159 1.00 87.31  ? 207 ILE   A O     1 
ATOM   1669 C  CB    . ILE   A 1 231 ? 158.196 137.428 152.923 1.00 90.05  ? 207 ILE   A CB    1 
ATOM   1670 C  CG1   . ILE   A 1 231 ? 157.034 136.449 153.097 1.00 86.51  ? 207 ILE   A CG1   1 
ATOM   1671 C  CG2   . ILE   A 1 231 ? 157.872 138.450 151.845 1.00 89.00  ? 207 ILE   A CG2   1 
ATOM   1672 C  CD1   . ILE   A 1 231 ? 156.810 135.556 151.902 1.00 85.62  ? 207 ILE   A CD1   1 
ATOM   1673 N  N     . HIS   A 1 232 ? 161.289 138.120 153.376 1.00 83.65  ? 208 HIS   A N     1 
ATOM   1674 C  CA    . HIS   A 1 232 ? 162.433 139.008 153.197 1.00 85.08  ? 208 HIS   A CA    1 
ATOM   1675 C  C     . HIS   A 1 232 ? 163.589 138.296 152.504 1.00 86.07  ? 208 HIS   A C     1 
ATOM   1676 O  O     . HIS   A 1 232 ? 164.247 138.875 151.633 1.00 89.74  ? 208 HIS   A O     1 
ATOM   1677 C  CB    . HIS   A 1 232 ? 162.883 139.568 154.545 1.00 86.75  ? 208 HIS   A CB    1 
ATOM   1678 C  CG    . HIS   A 1 232 ? 163.623 140.865 154.441 1.00 89.79  ? 208 HIS   A CG    1 
ATOM   1679 N  ND1   . HIS   A 1 232 ? 163.822 141.698 155.520 1.00 92.75  ? 208 HIS   A ND1   1 
ATOM   1680 C  CD2   . HIS   A 1 232 ? 164.210 141.473 153.384 1.00 89.93  ? 208 HIS   A CD2   1 
ATOM   1681 C  CE1   . HIS   A 1 232 ? 164.501 142.763 155.133 1.00 87.99  ? 208 HIS   A CE1   1 
ATOM   1682 N  NE2   . HIS   A 1 232 ? 164.749 142.651 153.841 1.00 87.63  ? 208 HIS   A NE2   1 
ATOM   1683 N  N     . GLU   A 1 233 ? 163.854 137.042 152.880 1.00 89.29  ? 209 GLU   A N     1 
ATOM   1684 C  CA    . GLU   A 1 233 ? 164.939 136.301 152.245 1.00 89.00  ? 209 GLU   A CA    1 
ATOM   1685 C  C     . GLU   A 1 233 ? 164.615 135.953 150.798 1.00 89.14  ? 209 GLU   A C     1 
ATOM   1686 O  O     . GLU   A 1 233 ? 165.522 135.883 149.962 1.00 88.94  ? 209 GLU   A O     1 
ATOM   1687 C  CB    . GLU   A 1 233 ? 165.249 135.033 153.041 1.00 90.02  ? 209 GLU   A CB    1 
ATOM   1688 C  CG    . GLU   A 1 233 ? 165.721 135.272 154.472 1.00 90.94  ? 209 GLU   A CG    1 
ATOM   1689 C  CD    . GLU   A 1 233 ? 167.144 135.798 154.560 1.00 94.71  ? 209 GLU   A CD    1 
ATOM   1690 O  OE1   . GLU   A 1 233 ? 167.449 136.842 153.945 1.00 91.63  ? 209 GLU   A OE1   1 
ATOM   1691 O  OE2   . GLU   A 1 233 ? 167.965 135.162 155.253 1.00 96.38  ? 209 GLU   A OE2   1 
ATOM   1692 N  N     . MET   A 1 234 ? 163.340 135.728 150.485 1.00 93.92  ? 210 MET   A N     1 
ATOM   1693 C  CA    . MET   A 1 234 ? 162.937 135.440 149.116 1.00 93.14  ? 210 MET   A CA    1 
ATOM   1694 C  C     . MET   A 1 234 ? 162.923 136.682 148.235 1.00 94.62  ? 210 MET   A C     1 
ATOM   1695 O  O     . MET   A 1 234 ? 163.146 136.569 147.026 1.00 95.02  ? 210 MET   A O     1 
ATOM   1696 C  CB    . MET   A 1 234 ? 161.554 134.785 149.106 1.00 94.62  ? 210 MET   A CB    1 
ATOM   1697 C  CG    . MET   A 1 234 ? 161.554 133.329 148.675 1.00 94.57  ? 210 MET   A CG    1 
ATOM   1698 S  SD    . MET   A 1 234 ? 159.898 132.613 148.676 1.00 101.40 ? 210 MET   A SD    1 
ATOM   1699 C  CE    . MET   A 1 234 ? 158.981 133.881 147.804 1.00 95.74  ? 210 MET   A CE    1 
ATOM   1700 N  N     . MET   A 1 235 ? 162.666 137.858 148.811 1.00 76.15  ? 211 MET   A N     1 
ATOM   1701 C  CA    . MET   A 1 235 ? 162.611 139.088 148.031 1.00 69.44  ? 211 MET   A CA    1 
ATOM   1702 C  C     . MET   A 1 235 ? 163.972 139.520 147.507 1.00 72.41  ? 211 MET   A C     1 
ATOM   1703 O  O     . MET   A 1 235 ? 164.031 140.271 146.528 1.00 73.24  ? 211 MET   A O     1 
ATOM   1704 C  CB    . MET   A 1 235 ? 162.010 140.217 148.871 1.00 64.32  ? 211 MET   A CB    1 
ATOM   1705 C  CG    . MET   A 1 235 ? 160.524 140.434 148.654 1.00 74.81  ? 211 MET   A CG    1 
ATOM   1706 S  SD    . MET   A 1 235 ? 159.802 141.563 149.858 1.00 81.91  ? 211 MET   A SD    1 
ATOM   1707 C  CE    . MET   A 1 235 ? 161.020 142.872 149.860 1.00 65.37  ? 211 MET   A CE    1 
ATOM   1708 N  N     . LYS   A 1 236 ? 165.063 139.071 148.133 1.00 62.80  ? 212 LYS   A N     1 
ATOM   1709 C  CA    . LYS   A 1 236 ? 166.394 139.460 147.682 1.00 60.63  ? 212 LYS   A CA    1 
ATOM   1710 C  C     . LYS   A 1 236 ? 166.732 138.894 146.310 1.00 62.68  ? 212 LYS   A C     1 
ATOM   1711 O  O     . LYS   A 1 236 ? 167.640 139.408 145.650 1.00 64.58  ? 212 LYS   A O     1 
ATOM   1712 C  CB    . LYS   A 1 236 ? 167.447 139.017 148.697 1.00 59.46  ? 212 LYS   A CB    1 
ATOM   1713 C  CG    . LYS   A 1 236 ? 167.408 139.788 150.003 1.00 60.10  ? 212 LYS   A CG    1 
ATOM   1714 C  CD    . LYS   A 1 236 ? 168.791 140.277 150.396 1.00 64.02  ? 212 LYS   A CD    1 
ATOM   1715 C  CE    . LYS   A 1 236 ? 168.769 140.961 151.752 1.00 63.97  ? 212 LYS   A CE    1 
ATOM   1716 N  NZ    . LYS   A 1 236 ? 167.584 140.560 152.557 1.00 63.61  ? 212 LYS   A NZ    1 
ATOM   1717 N  N     . TYR   A 1 237 ? 166.031 137.851 145.870 1.00 66.31  ? 213 TYR   A N     1 
ATOM   1718 C  CA    . TYR   A 1 237 ? 166.251 137.291 144.544 1.00 62.57  ? 213 TYR   A CA    1 
ATOM   1719 C  C     . TYR   A 1 237 ? 165.568 138.094 143.445 1.00 60.85  ? 213 TYR   A C     1 
ATOM   1720 O  O     . TYR   A 1 237 ? 165.841 137.854 142.265 1.00 61.67  ? 213 TYR   A O     1 
ATOM   1721 C  CB    . TYR   A 1 237 ? 165.770 135.840 144.506 1.00 62.22  ? 213 TYR   A CB    1 
ATOM   1722 C  CG    . TYR   A 1 237 ? 166.736 134.866 145.141 1.00 63.35  ? 213 TYR   A CG    1 
ATOM   1723 C  CD1   . TYR   A 1 237 ? 167.746 134.276 144.395 1.00 70.72  ? 213 TYR   A CD1   1 
ATOM   1724 C  CD2   . TYR   A 1 237 ? 166.645 134.546 146.487 1.00 65.83  ? 213 TYR   A CD2   1 
ATOM   1725 C  CE1   . TYR   A 1 237 ? 168.634 133.388 144.971 1.00 71.53  ? 213 TYR   A CE1   1 
ATOM   1726 C  CE2   . TYR   A 1 237 ? 167.529 133.661 147.072 1.00 69.35  ? 213 TYR   A CE2   1 
ATOM   1727 C  CZ    . TYR   A 1 237 ? 168.521 133.085 146.309 1.00 72.52  ? 213 TYR   A CZ    1 
ATOM   1728 O  OH    . TYR   A 1 237 ? 169.405 132.202 146.885 1.00 75.03  ? 213 TYR   A OH    1 
ATOM   1729 N  N     . ASN   A 1 238 ? 164.698 139.027 143.802 1.00 56.93  ? 214 ASN   A N     1 
ATOM   1730 C  CA    . ASN   A 1 238 ? 164.056 139.899 142.825 1.00 55.94  ? 214 ASN   A CA    1 
ATOM   1731 C  C     . ASN   A 1 238 ? 165.024 140.996 142.402 1.00 63.36  ? 214 ASN   A C     1 
ATOM   1732 O  O     . ASN   A 1 238 ? 165.521 141.734 143.262 1.00 62.20  ? 214 ASN   A O     1 
ATOM   1733 C  CB    . ASN   A 1 238 ? 162.790 140.503 143.426 1.00 48.98  ? 214 ASN   A CB    1 
ATOM   1734 C  CG    . ASN   A 1 238 ? 161.805 140.967 142.375 1.00 55.45  ? 214 ASN   A CG    1 
ATOM   1735 O  OD1   . ASN   A 1 238 ? 162.009 140.759 141.181 1.00 59.09  ? 214 ASN   A OD1   1 
ATOM   1736 N  ND2   . ASN   A 1 238 ? 160.726 141.600 142.816 1.00 57.25  ? 214 ASN   A ND2   1 
ATOM   1737 N  N     . PRO   A 1 239 ? 165.333 141.138 141.109 1.00 65.09  ? 215 PRO   A N     1 
ATOM   1738 C  CA    . PRO   A 1 239 ? 166.264 142.199 140.690 1.00 55.53  ? 215 PRO   A CA    1 
ATOM   1739 C  C     . PRO   A 1 239 ? 165.741 143.611 140.906 1.00 56.68  ? 215 PRO   A C     1 
ATOM   1740 O  O     . PRO   A 1 239 ? 166.548 144.547 140.925 1.00 60.04  ? 215 PRO   A O     1 
ATOM   1741 C  CB    . PRO   A 1 239 ? 166.481 141.905 139.200 1.00 50.84  ? 215 PRO   A CB    1 
ATOM   1742 C  CG    . PRO   A 1 239 ? 165.264 141.144 138.791 1.00 58.75  ? 215 PRO   A CG    1 
ATOM   1743 C  CD    . PRO   A 1 239 ? 164.927 140.291 139.976 1.00 60.14  ? 215 PRO   A CD    1 
ATOM   1744 N  N     . VAL   A 1 240 ? 164.429 143.801 141.063 1.00 48.88  ? 216 VAL   A N     1 
ATOM   1745 C  CA    . VAL   A 1 240 ? 163.892 145.138 141.311 1.00 42.78  ? 216 VAL   A CA    1 
ATOM   1746 C  C     . VAL   A 1 240 ? 164.298 145.629 142.694 1.00 48.21  ? 216 VAL   A C     1 
ATOM   1747 O  O     . VAL   A 1 240 ? 164.458 146.837 142.923 1.00 60.50  ? 216 VAL   A O     1 
ATOM   1748 C  CB    . VAL   A 1 240 ? 162.362 145.141 141.135 1.00 49.81  ? 216 VAL   A CB    1 
ATOM   1749 C  CG1   . VAL   A 1 240 ? 161.849 146.559 140.972 1.00 58.80  ? 216 VAL   A CG1   1 
ATOM   1750 C  CG2   . VAL   A 1 240 ? 161.966 144.289 139.942 1.00 48.34  ? 216 VAL   A CG2   1 
ATOM   1751 N  N     . TYR   A 1 241 ? 164.450 144.699 143.640 1.00 44.80  ? 217 TYR   A N     1 
ATOM   1752 C  CA    . TYR   A 1 241 ? 164.892 145.047 144.987 1.00 48.29  ? 217 TYR   A CA    1 
ATOM   1753 C  C     . TYR   A 1 241 ? 166.227 145.780 144.950 1.00 52.61  ? 217 TYR   A C     1 
ATOM   1754 O  O     . TYR   A 1 241 ? 166.380 146.848 145.559 1.00 54.82  ? 217 TYR   A O     1 
ATOM   1755 C  CB    . TYR   A 1 241 ? 164.978 143.764 145.825 1.00 41.62  ? 217 TYR   A CB    1 
ATOM   1756 C  CG    . TYR   A 1 241 ? 165.668 143.863 147.174 1.00 49.67  ? 217 TYR   A CG    1 
ATOM   1757 C  CD1   . TYR   A 1 241 ? 167.053 143.879 147.280 1.00 50.44  ? 217 TYR   A CD1   1 
ATOM   1758 C  CD2   . TYR   A 1 241 ? 164.927 143.890 148.347 1.00 49.34  ? 217 TYR   A CD2   1 
ATOM   1759 C  CE1   . TYR   A 1 241 ? 167.673 143.958 148.509 1.00 49.23  ? 217 TYR   A CE1   1 
ATOM   1760 C  CE2   . TYR   A 1 241 ? 165.540 143.965 149.579 1.00 43.78  ? 217 TYR   A CE2   1 
ATOM   1761 C  CZ    . TYR   A 1 241 ? 166.912 143.998 149.654 1.00 50.67  ? 217 TYR   A CZ    1 
ATOM   1762 O  OH    . TYR   A 1 241 ? 167.526 144.071 150.882 1.00 62.19  ? 217 TYR   A OH    1 
ATOM   1763 N  N     . PHE   A 1 242 ? 167.198 145.227 144.220 1.00 31.87  ? 218 PHE   A N     1 
ATOM   1764 C  CA    . PHE   A 1 242 ? 168.523 145.830 144.149 1.00 23.27  ? 218 PHE   A CA    1 
ATOM   1765 C  C     . PHE   A 1 242 ? 168.470 147.214 143.519 1.00 37.17  ? 218 PHE   A C     1 
ATOM   1766 O  O     . PHE   A 1 242 ? 169.095 148.153 144.022 1.00 46.58  ? 218 PHE   A O     1 
ATOM   1767 C  CB    . PHE   A 1 242 ? 169.463 144.911 143.370 1.00 33.59  ? 218 PHE   A CB    1 
ATOM   1768 C  CG    . PHE   A 1 242 ? 170.783 145.535 143.027 1.00 36.40  ? 218 PHE   A CG    1 
ATOM   1769 C  CD1   . PHE   A 1 242 ? 171.739 145.748 144.002 1.00 41.38  ? 218 PHE   A CD1   1 
ATOM   1770 C  CD2   . PHE   A 1 242 ? 171.072 145.894 141.723 1.00 42.59  ? 218 PHE   A CD2   1 
ATOM   1771 C  CE1   . PHE   A 1 242 ? 172.955 146.320 143.684 1.00 37.28  ? 218 PHE   A CE1   1 
ATOM   1772 C  CE2   . PHE   A 1 242 ? 172.285 146.464 141.401 1.00 40.24  ? 218 PHE   A CE2   1 
ATOM   1773 C  CZ    . PHE   A 1 242 ? 173.226 146.678 142.381 1.00 38.55  ? 218 PHE   A CZ    1 
ATOM   1774 N  N     . ILE   A 1 243 ? 167.712 147.367 142.430 1.00 37.27  ? 219 ILE   A N     1 
ATOM   1775 C  CA    . ILE   A 1 243 ? 167.655 148.655 141.742 1.00 31.56  ? 219 ILE   A CA    1 
ATOM   1776 C  C     . ILE   A 1 243 ? 167.024 149.717 142.635 1.00 37.57  ? 219 ILE   A C     1 
ATOM   1777 O  O     . ILE   A 1 243 ? 167.552 150.829 142.767 1.00 51.82  ? 219 ILE   A O     1 
ATOM   1778 C  CB    . ILE   A 1 243 ? 166.901 148.518 140.407 1.00 33.52  ? 219 ILE   A CB    1 
ATOM   1779 C  CG1   . ILE   A 1 243 ? 167.419 147.313 139.622 1.00 44.93  ? 219 ILE   A CG1   1 
ATOM   1780 C  CG2   . ILE   A 1 243 ? 167.054 149.778 139.579 1.00 35.20  ? 219 ILE   A CG2   1 
ATOM   1781 C  CD1   . ILE   A 1 243 ? 166.617 147.005 138.381 1.00 41.58  ? 219 ILE   A CD1   1 
ATOM   1782 N  N     . ALA   A 1 244 ? 165.891 149.394 143.266 1.00 38.04  ? 220 ALA   A N     1 
ATOM   1783 C  CA    . ALA   A 1 244 ? 165.227 150.373 144.121 1.00 30.41  ? 220 ALA   A CA    1 
ATOM   1784 C  C     . ALA   A 1 244 ? 166.100 150.757 145.309 1.00 32.67  ? 220 ALA   A C     1 
ATOM   1785 O  O     . ALA   A 1 244 ? 166.241 151.947 145.629 1.00 36.61  ? 220 ALA   A O     1 
ATOM   1786 C  CB    . ALA   A 1 244 ? 163.881 149.828 144.596 1.00 21.43  ? 220 ALA   A CB    1 
ATOM   1787 N  N     . GLU   A 1 245 ? 166.708 149.767 145.970 1.00 33.40  ? 221 GLU   A N     1 
ATOM   1788 C  CA    . GLU   A 1 245 ? 167.537 150.065 147.132 1.00 31.04  ? 221 GLU   A CA    1 
ATOM   1789 C  C     . GLU   A 1 245 ? 168.768 150.875 146.743 1.00 40.20  ? 221 GLU   A C     1 
ATOM   1790 O  O     . GLU   A 1 245 ? 169.173 151.786 147.473 1.00 42.86  ? 221 GLU   A O     1 
ATOM   1791 C  CB    . GLU   A 1 245 ? 167.935 148.769 147.835 1.00 43.34  ? 221 GLU   A CB    1 
ATOM   1792 C  CG    . GLU   A 1 245 ? 166.780 148.078 148.546 1.00 44.71  ? 221 GLU   A CG    1 
ATOM   1793 C  CD    . GLU   A 1 245 ? 166.313 148.831 149.778 1.00 54.53  ? 221 GLU   A CD    1 
ATOM   1794 O  OE1   . GLU   A 1 245 ? 165.287 149.537 149.695 1.00 46.53  ? 221 GLU   A OE1   1 
ATOM   1795 O  OE2   . GLU   A 1 245 ? 166.970 148.711 150.833 1.00 60.49  ? 221 GLU   A OE2   1 
ATOM   1796 N  N     . SER   A 1 246 ? 169.376 150.563 145.594 1.00 31.86  ? 222 SER   A N     1 
ATOM   1797 C  CA    . SER   A 1 246 ? 170.544 151.313 145.147 1.00 24.57  ? 222 SER   A CA    1 
ATOM   1798 C  C     . SER   A 1 246 ? 170.184 152.753 144.807 1.00 35.36  ? 222 SER   A C     1 
ATOM   1799 O  O     . SER   A 1 246 ? 170.932 153.679 145.140 1.00 33.84  ? 222 SER   A O     1 
ATOM   1800 C  CB    . SER   A 1 246 ? 171.179 150.615 143.947 1.00 24.94  ? 222 SER   A CB    1 
ATOM   1801 O  OG    . SER   A 1 246 ? 170.265 150.522 142.870 1.00 34.60  ? 222 SER   A OG    1 
ATOM   1802 N  N     . TYR   A 1 247 ? 169.043 152.965 144.142 1.00 46.33  ? 223 TYR   A N     1 
ATOM   1803 C  CA    . TYR   A 1 247 ? 168.602 154.329 143.864 1.00 36.67  ? 223 TYR   A CA    1 
ATOM   1804 C  C     . TYR   A 1 247 ? 168.380 155.109 145.153 1.00 38.88  ? 223 TYR   A C     1 
ATOM   1805 O  O     . TYR   A 1 247 ? 168.806 156.265 145.272 1.00 41.72  ? 223 TYR   A O     1 
ATOM   1806 C  CB    . TYR   A 1 247 ? 167.317 154.311 143.037 1.00 41.64  ? 223 TYR   A CB    1 
ATOM   1807 C  CG    . TYR   A 1 247 ? 167.516 154.300 141.539 1.00 46.62  ? 223 TYR   A CG    1 
ATOM   1808 C  CD1   . TYR   A 1 247 ? 168.273 153.315 140.923 1.00 39.01  ? 223 TYR   A CD1   1 
ATOM   1809 C  CD2   . TYR   A 1 247 ? 166.930 155.270 140.740 1.00 48.65  ? 223 TYR   A CD2   1 
ATOM   1810 C  CE1   . TYR   A 1 247 ? 168.445 153.303 139.554 1.00 40.20  ? 223 TYR   A CE1   1 
ATOM   1811 C  CE2   . TYR   A 1 247 ? 167.095 155.264 139.373 1.00 44.39  ? 223 TYR   A CE2   1 
ATOM   1812 C  CZ    . TYR   A 1 247 ? 167.852 154.280 138.785 1.00 43.83  ? 223 TYR   A CZ    1 
ATOM   1813 O  OH    . TYR   A 1 247 ? 168.018 154.276 137.421 1.00 57.11  ? 223 TYR   A OH    1 
ATOM   1814 N  N     . ARG   A 1 248 ? 167.713 154.491 146.132 1.00 71.36  ? 224 ARG   A N     1 
ATOM   1815 C  CA    . ARG   A 1 248 ? 167.469 155.178 147.396 1.00 62.51  ? 224 ARG   A CA    1 
ATOM   1816 C  C     . ARG   A 1 248 ? 168.772 155.497 148.118 1.00 55.53  ? 224 ARG   A C     1 
ATOM   1817 O  O     . ARG   A 1 248 ? 168.923 156.584 148.686 1.00 58.41  ? 224 ARG   A O     1 
ATOM   1818 C  CB    . ARG   A 1 248 ? 166.554 154.337 148.283 1.00 69.08  ? 224 ARG   A CB    1 
ATOM   1819 C  CG    . ARG   A 1 248 ? 165.091 154.446 147.914 1.00 68.40  ? 224 ARG   A CG    1 
ATOM   1820 C  CD    . ARG   A 1 248 ? 164.253 153.449 148.682 1.00 68.10  ? 224 ARG   A CD    1 
ATOM   1821 N  NE    . ARG   A 1 248 ? 162.883 153.409 148.189 1.00 62.40  ? 224 ARG   A NE    1 
ATOM   1822 C  CZ    . ARG   A 1 248 ? 162.207 152.294 147.953 1.00 65.71  ? 224 ARG   A CZ    1 
ATOM   1823 N  NH1   . ARG   A 1 248 ? 162.743 151.104 148.161 1.00 69.31  ? 224 ARG   A NH1   1 
ATOM   1824 N  NH2   . ARG   A 1 248 ? 160.961 152.376 147.499 1.00 70.49  ? 224 ARG   A NH2   1 
ATOM   1825 N  N     . ALA   A 1 249 ? 169.725 154.563 148.111 1.00 38.99  ? 225 ALA   A N     1 
ATOM   1826 C  CA    . ALA   A 1 249 ? 171.013 154.814 148.752 1.00 39.41  ? 225 ALA   A CA    1 
ATOM   1827 C  C     . ALA   A 1 249 ? 171.754 155.955 148.069 1.00 41.58  ? 225 ALA   A C     1 
ATOM   1828 O  O     . ALA   A 1 249 ? 172.352 156.809 148.733 1.00 40.20  ? 225 ALA   A O     1 
ATOM   1829 C  CB    . ALA   A 1 249 ? 171.859 153.542 148.745 1.00 32.75  ? 225 ALA   A CB    1 
ATOM   1830 N  N     . ALA   A 1 250 ? 171.733 155.981 146.735 1.00 55.19  ? 226 ALA   A N     1 
ATOM   1831 C  CA    . ALA   A 1 250 ? 172.431 157.034 146.006 1.00 31.89  ? 226 ALA   A CA    1 
ATOM   1832 C  C     . ALA   A 1 250 ? 171.808 158.401 146.259 1.00 37.53  ? 226 ALA   A C     1 
ATOM   1833 O  O     . ALA   A 1 250 ? 172.525 159.392 146.437 1.00 41.08  ? 226 ALA   A O     1 
ATOM   1834 C  CB    . ALA   A 1 250 ? 172.440 156.720 144.511 1.00 22.00  ? 226 ALA   A CB    1 
ATOM   1835 N  N     . ILE   A 1 251 ? 170.480 158.479 146.283 1.00 41.92  ? 227 ILE   A N     1 
ATOM   1836 C  CA    . ILE   A 1 251 ? 169.808 159.776 146.318 1.00 27.49  ? 227 ILE   A CA    1 
ATOM   1837 C  C     . ILE   A 1 251 ? 169.439 160.188 147.739 1.00 37.24  ? 227 ILE   A C     1 
ATOM   1838 O  O     . ILE   A 1 251 ? 169.653 161.336 148.135 1.00 45.49  ? 227 ILE   A O     1 
ATOM   1839 C  CB    . ILE   A 1 251 ? 168.570 159.752 145.397 1.00 25.21  ? 227 ILE   A CB    1 
ATOM   1840 C  CG1   . ILE   A 1 251 ? 168.966 159.300 143.991 1.00 29.69  ? 227 ILE   A CG1   1 
ATOM   1841 C  CG2   . ILE   A 1 251 ? 167.916 161.120 145.351 1.00 30.91  ? 227 ILE   A CG2   1 
ATOM   1842 C  CD1   . ILE   A 1 251 ? 167.834 159.335 142.992 1.00 38.12  ? 227 ILE   A CD1   1 
ATOM   1843 N  N     . LEU   A 1 252 ? 168.884 159.274 148.535 1.00 40.54  ? 228 LEU   A N     1 
ATOM   1844 C  CA    . LEU   A 1 252 ? 168.309 159.626 149.830 1.00 25.45  ? 228 LEU   A CA    1 
ATOM   1845 C  C     . LEU   A 1 252 ? 169.247 159.381 151.007 1.00 35.89  ? 228 LEU   A C     1 
ATOM   1846 O  O     . LEU   A 1 252 ? 169.465 160.284 151.819 1.00 31.10  ? 228 LEU   A O     1 
ATOM   1847 C  CB    . LEU   A 1 252 ? 167.006 158.849 150.050 1.00 27.69  ? 228 LEU   A CB    1 
ATOM   1848 C  CG    . LEU   A 1 252 ? 165.778 159.245 149.232 1.00 28.80  ? 228 LEU   A CG    1 
ATOM   1849 C  CD1   . LEU   A 1 252 ? 164.693 158.199 149.391 1.00 23.03  ? 228 LEU   A CD1   1 
ATOM   1850 C  CD2   . LEU   A 1 252 ? 165.270 160.612 149.648 1.00 37.52  ? 228 LEU   A CD2   1 
ATOM   1851 N  N     . TYR   A 1 253 ? 169.805 158.178 151.122 1.00 44.21  ? 229 TYR   A N     1 
ATOM   1852 C  CA    . TYR   A 1 253 ? 170.427 157.736 152.364 1.00 33.73  ? 229 TYR   A CA    1 
ATOM   1853 C  C     . TYR   A 1 253 ? 171.870 158.193 152.538 1.00 42.08  ? 229 TYR   A C     1 
ATOM   1854 O  O     . TYR   A 1 253 ? 172.398 158.083 153.651 1.00 48.63  ? 229 TYR   A O     1 
ATOM   1855 C  CB    . TYR   A 1 253 ? 170.369 156.208 152.464 1.00 28.06  ? 229 TYR   A CB    1 
ATOM   1856 C  CG    . TYR   A 1 253 ? 168.967 155.651 152.548 1.00 40.91  ? 229 TYR   A CG    1 
ATOM   1857 C  CD1   . TYR   A 1 253 ? 167.917 156.425 153.019 1.00 46.23  ? 229 TYR   A CD1   1 
ATOM   1858 C  CD2   . TYR   A 1 253 ? 168.693 154.350 152.151 1.00 42.52  ? 229 TYR   A CD2   1 
ATOM   1859 C  CE1   . TYR   A 1 253 ? 166.635 155.919 153.093 1.00 44.41  ? 229 TYR   A CE1   1 
ATOM   1860 C  CE2   . TYR   A 1 253 ? 167.414 153.838 152.220 1.00 39.31  ? 229 TYR   A CE2   1 
ATOM   1861 C  CZ    . TYR   A 1 253 ? 166.389 154.625 152.693 1.00 46.94  ? 229 TYR   A CZ    1 
ATOM   1862 O  OH    . TYR   A 1 253 ? 165.113 154.117 152.766 1.00 53.57  ? 229 TYR   A OH    1 
ATOM   1863 N  N     . HIS   A 1 254 ? 172.517 158.699 151.487 1.00 47.67  ? 230 HIS   A N     1 
ATOM   1864 C  CA    . HIS   A 1 254 ? 173.916 159.132 151.545 1.00 47.79  ? 230 HIS   A CA    1 
ATOM   1865 C  C     . HIS   A 1 254 ? 174.821 157.994 152.027 1.00 54.98  ? 230 HIS   A C     1 
ATOM   1866 O  O     . HIS   A 1 254 ? 175.451 158.068 153.083 1.00 57.71  ? 230 HIS   A O     1 
ATOM   1867 C  CB    . HIS   A 1 254 ? 174.080 160.370 152.435 1.00 50.29  ? 230 HIS   A CB    1 
ATOM   1868 C  CG    . HIS   A 1 254 ? 173.320 161.568 151.960 1.00 60.00  ? 230 HIS   A CG    1 
ATOM   1869 N  ND1   . HIS   A 1 254 ? 173.291 161.958 150.639 1.00 67.09  ? 230 HIS   A ND1   1 
ATOM   1870 C  CD2   . HIS   A 1 254 ? 172.567 162.470 152.634 1.00 55.46  ? 230 HIS   A CD2   1 
ATOM   1871 C  CE1   . HIS   A 1 254 ? 172.548 163.043 150.518 1.00 60.26  ? 230 HIS   A CE1   1 
ATOM   1872 N  NE2   . HIS   A 1 254 ? 172.097 163.375 151.714 1.00 59.26  ? 230 HIS   A NE2   1 
ATOM   1873 N  N     . GLU   A 1 255 ? 174.875 156.931 151.229 1.00 55.90  ? 231 GLU   A N     1 
ATOM   1874 C  CA    . GLU   A 1 255 ? 175.609 155.734 151.613 1.00 45.77  ? 231 GLU   A CA    1 
ATOM   1875 C  C     . GLU   A 1 255 ? 176.181 155.064 150.373 1.00 52.28  ? 231 GLU   A C     1 
ATOM   1876 O  O     . GLU   A 1 255 ? 175.515 154.992 149.337 1.00 60.71  ? 231 GLU   A O     1 
ATOM   1877 C  CB    . GLU   A 1 255 ? 174.698 154.765 152.378 1.00 47.27  ? 231 GLU   A CB    1 
ATOM   1878 C  CG    . GLU   A 1 255 ? 175.101 153.304 152.297 1.00 56.17  ? 231 GLU   A CG    1 
ATOM   1879 C  CD    . GLU   A 1 255 ? 173.906 152.373 152.264 1.00 56.75  ? 231 GLU   A CD    1 
ATOM   1880 O  OE1   . GLU   A 1 255 ? 172.762 152.873 152.267 1.00 54.99  ? 231 GLU   A OE1   1 
ATOM   1881 O  OE2   . GLU   A 1 255 ? 174.111 151.141 152.235 1.00 54.50  ? 231 GLU   A OE2   1 
ATOM   1882 N  N     . TRP   A 1 256 ? 177.420 154.583 150.483 1.00 74.29  ? 232 TRP   A N     1 
ATOM   1883 C  CA    . TRP   A 1 256 ? 178.029 153.787 149.422 1.00 66.59  ? 232 TRP   A CA    1 
ATOM   1884 C  C     . TRP   A 1 256 ? 177.408 152.396 149.442 1.00 62.95  ? 232 TRP   A C     1 
ATOM   1885 O  O     . TRP   A 1 256 ? 177.730 151.577 150.307 1.00 72.71  ? 232 TRP   A O     1 
ATOM   1886 C  CB    . TRP   A 1 256 ? 179.541 153.706 149.610 1.00 69.02  ? 232 TRP   A CB    1 
ATOM   1887 C  CG    . TRP   A 1 256 ? 180.275 155.016 149.519 1.00 70.13  ? 232 TRP   A CG    1 
ATOM   1888 C  CD1   . TRP   A 1 256 ? 181.032 155.592 150.494 1.00 73.36  ? 232 TRP   A CD1   1 
ATOM   1889 C  CD2   . TRP   A 1 256 ? 180.344 155.897 148.388 1.00 73.57  ? 232 TRP   A CD2   1 
ATOM   1890 N  NE1   . TRP   A 1 256 ? 181.558 156.779 150.050 1.00 77.33  ? 232 TRP   A NE1   1 
ATOM   1891 C  CE2   . TRP   A 1 256 ? 181.150 156.990 148.760 1.00 73.09  ? 232 TRP   A CE2   1 
ATOM   1892 C  CE3   . TRP   A 1 256 ? 179.798 155.871 147.103 1.00 74.87  ? 232 TRP   A CE3   1 
ATOM   1893 C  CZ2   . TRP   A 1 256 ? 181.424 158.045 147.894 1.00 72.65  ? 232 TRP   A CZ2   1 
ATOM   1894 C  CZ3   . TRP   A 1 256 ? 180.071 156.921 146.245 1.00 67.13  ? 232 TRP   A CZ3   1 
ATOM   1895 C  CH2   . TRP   A 1 256 ? 180.876 157.992 146.643 1.00 67.81  ? 232 TRP   A CH2   1 
ATOM   1896 N  N     . TYR   A 1 257 ? 176.517 152.124 148.488 1.00 38.60  ? 233 TYR   A N     1 
ATOM   1897 C  CA    . TYR   A 1 257 ? 175.720 150.903 148.545 1.00 45.90  ? 233 TYR   A CA    1 
ATOM   1898 C  C     . TYR   A 1 257 ? 176.547 149.655 148.259 1.00 54.45  ? 233 TYR   A C     1 
ATOM   1899 O  O     . TYR   A 1 257 ? 176.253 148.585 148.802 1.00 52.12  ? 233 TYR   A O     1 
ATOM   1900 C  CB    . TYR   A 1 257 ? 174.553 151.000 147.563 1.00 45.26  ? 233 TYR   A CB    1 
ATOM   1901 C  CG    . TYR   A 1 257 ? 173.565 149.862 147.658 1.00 49.35  ? 233 TYR   A CG    1 
ATOM   1902 C  CD1   . TYR   A 1 257 ? 172.673 149.779 148.717 1.00 46.53  ? 233 TYR   A CD1   1 
ATOM   1903 C  CD2   . TYR   A 1 257 ? 173.518 148.874 146.686 1.00 46.82  ? 233 TYR   A CD2   1 
ATOM   1904 C  CE1   . TYR   A 1 257 ? 171.766 148.743 148.807 1.00 43.43  ? 233 TYR   A CE1   1 
ATOM   1905 C  CE2   . TYR   A 1 257 ? 172.615 147.836 146.767 1.00 49.50  ? 233 TYR   A CE2   1 
ATOM   1906 C  CZ    . TYR   A 1 257 ? 171.742 147.775 147.828 1.00 49.20  ? 233 TYR   A CZ    1 
ATOM   1907 O  OH    . TYR   A 1 257 ? 170.841 146.740 147.911 1.00 52.32  ? 233 TYR   A OH    1 
ATOM   1908 N  N     . PHE   A 1 258 ? 177.577 149.763 147.420 1.00 58.34  ? 234 PHE   A N     1 
ATOM   1909 C  CA    . PHE   A 1 258 ? 178.311 148.586 146.974 1.00 34.50  ? 234 PHE   A CA    1 
ATOM   1910 C  C     . PHE   A 1 258 ? 179.273 148.035 148.019 1.00 43.87  ? 234 PHE   A C     1 
ATOM   1911 O  O     . PHE   A 1 258 ? 179.794 146.932 147.829 1.00 56.71  ? 234 PHE   A O     1 
ATOM   1912 C  CB    . PHE   A 1 258 ? 179.085 148.899 145.691 1.00 39.79  ? 234 PHE   A CB    1 
ATOM   1913 C  CG    . PHE   A 1 258 ? 179.844 150.194 145.736 1.00 44.57  ? 234 PHE   A CG    1 
ATOM   1914 C  CD1   . PHE   A 1 258 ? 181.056 150.280 146.397 1.00 43.46  ? 234 PHE   A CD1   1 
ATOM   1915 C  CD2   . PHE   A 1 258 ? 179.351 151.321 145.105 1.00 44.00  ? 234 PHE   A CD2   1 
ATOM   1916 C  CE1   . PHE   A 1 258 ? 181.755 151.467 146.437 1.00 37.67  ? 234 PHE   A CE1   1 
ATOM   1917 C  CE2   . PHE   A 1 258 ? 180.048 152.510 145.140 1.00 46.10  ? 234 PHE   A CE2   1 
ATOM   1918 C  CZ    . PHE   A 1 258 ? 181.251 152.582 145.808 1.00 43.90  ? 234 PHE   A CZ    1 
ATOM   1919 N  N     . MET   A 1 259 ? 179.532 148.764 149.104 1.00 71.45  ? 235 MET   A N     1 
ATOM   1920 C  CA    . MET   A 1 259 ? 180.445 148.260 150.125 1.00 73.11  ? 235 MET   A CA    1 
ATOM   1921 C  C     . MET   A 1 259 ? 179.806 147.178 150.984 1.00 76.52  ? 235 MET   A C     1 
ATOM   1922 O  O     . MET   A 1 259 ? 180.503 146.269 151.445 1.00 76.24  ? 235 MET   A O     1 
ATOM   1923 C  CB    . MET   A 1 259 ? 180.936 149.403 151.013 1.00 69.63  ? 235 MET   A CB    1 
ATOM   1924 C  CG    . MET   A 1 259 ? 181.306 150.661 150.259 1.00 73.96  ? 235 MET   A CG    1 
ATOM   1925 S  SD    . MET   A 1 259 ? 183.012 150.636 149.682 1.00 83.88  ? 235 MET   A SD    1 
ATOM   1926 C  CE    . MET   A 1 259 ? 183.812 149.792 151.043 1.00 76.14  ? 235 MET   A CE    1 
ATOM   1927 N  N     . ASP   A 1 260 ? 178.496 147.257 151.209 1.00 79.12  ? 236 ASP   A N     1 
ATOM   1928 C  CA    . ASP   A 1 260 ? 177.808 146.313 152.077 1.00 79.51  ? 236 ASP   A CA    1 
ATOM   1929 C  C     . ASP   A 1 260 ? 177.043 145.235 151.321 1.00 81.54  ? 236 ASP   A C     1 
ATOM   1930 O  O     . ASP   A 1 260 ? 176.711 144.206 151.918 1.00 80.60  ? 236 ASP   A O     1 
ATOM   1931 C  CB    . ASP   A 1 260 ? 176.836 147.061 152.999 1.00 80.69  ? 236 ASP   A CB    1 
ATOM   1932 C  CG    . ASP   A 1 260 ? 176.826 146.507 154.408 1.00 83.57  ? 236 ASP   A CG    1 
ATOM   1933 O  OD1   . ASP   A 1 260 ? 176.210 145.443 154.626 1.00 85.03  ? 236 ASP   A OD1   1 
ATOM   1934 O  OD2   . ASP   A 1 260 ? 177.433 147.137 155.299 1.00 83.25  ? 236 ASP   A OD2   1 
ATOM   1935 N  N     . HIS   A 1 261 ? 176.759 145.438 150.037 1.00 67.43  ? 237 HIS   A N     1 
ATOM   1936 C  CA    . HIS   A 1 261 ? 175.909 144.541 149.261 1.00 58.93  ? 237 HIS   A CA    1 
ATOM   1937 C  C     . HIS   A 1 261 ? 176.534 144.232 147.906 1.00 59.47  ? 237 HIS   A C     1 
ATOM   1938 O  O     . HIS   A 1 261 ? 175.880 144.311 146.864 1.00 68.56  ? 237 HIS   A O     1 
ATOM   1939 C  CB    . HIS   A 1 261 ? 174.518 145.139 149.076 1.00 55.83  ? 237 HIS   A CB    1 
ATOM   1940 C  CG    . HIS   A 1 261 ? 173.840 145.508 150.358 1.00 60.09  ? 237 HIS   A CG    1 
ATOM   1941 N  ND1   . HIS   A 1 261 ? 174.050 146.714 150.990 1.00 59.21  ? 237 HIS   A ND1   1 
ATOM   1942 C  CD2   . HIS   A 1 261 ? 172.949 144.834 151.121 1.00 62.33  ? 237 HIS   A CD2   1 
ATOM   1943 C  CE1   . HIS   A 1 261 ? 173.321 146.765 152.090 1.00 58.91  ? 237 HIS   A CE1   1 
ATOM   1944 N  NE2   . HIS   A 1 261 ? 172.643 145.637 152.193 1.00 63.90  ? 237 HIS   A NE2   1 
ATOM   1945 N  N     . TRP   A 1 262 ? 177.820 143.878 147.895 1.00 63.01  ? 238 TRP   A N     1 
ATOM   1946 C  CA    . TRP   A 1 262 ? 178.459 143.493 146.641 1.00 66.24  ? 238 TRP   A CA    1 
ATOM   1947 C  C     . TRP   A 1 262 ? 178.039 142.104 146.172 1.00 72.54  ? 238 TRP   A C     1 
ATOM   1948 O  O     . TRP   A 1 262 ? 178.136 141.810 144.973 1.00 76.83  ? 238 TRP   A O     1 
ATOM   1949 C  CB    . TRP   A 1 262 ? 179.983 143.565 146.773 1.00 67.57  ? 238 TRP   A CB    1 
ATOM   1950 C  CG    . TRP   A 1 262 ? 180.548 142.832 147.951 1.00 75.66  ? 238 TRP   A CG    1 
ATOM   1951 C  CD1   . TRP   A 1 262 ? 180.604 143.274 149.241 1.00 75.97  ? 238 TRP   A CD1   1 
ATOM   1952 C  CD2   . TRP   A 1 262 ? 181.164 141.538 147.944 1.00 76.60  ? 238 TRP   A CD2   1 
ATOM   1953 N  NE1   . TRP   A 1 262 ? 181.203 142.331 150.039 1.00 78.88  ? 238 TRP   A NE1   1 
ATOM   1954 C  CE2   . TRP   A 1 262 ? 181.557 141.256 149.267 1.00 75.22  ? 238 TRP   A CE2   1 
ATOM   1955 C  CE3   . TRP   A 1 262 ? 181.415 140.589 146.950 1.00 73.27  ? 238 TRP   A CE3   1 
ATOM   1956 C  CZ2   . TRP   A 1 262 ? 182.186 140.066 149.620 1.00 71.75  ? 238 TRP   A CZ2   1 
ATOM   1957 C  CZ3   . TRP   A 1 262 ? 182.039 139.408 147.303 1.00 69.30  ? 238 TRP   A CZ3   1 
ATOM   1958 C  CH2   . TRP   A 1 262 ? 182.418 139.157 148.626 1.00 69.87  ? 238 TRP   A CH2   1 
ATOM   1959 N  N     . LYS   A 1 263 ? 177.566 141.252 147.085 1.00 65.91  ? 239 LYS   A N     1 
ATOM   1960 C  CA    . LYS   A 1 263 ? 177.048 139.948 146.686 1.00 56.19  ? 239 LYS   A CA    1 
ATOM   1961 C  C     . LYS   A 1 263 ? 175.828 140.093 145.785 1.00 61.08  ? 239 LYS   A C     1 
ATOM   1962 O  O     . LYS   A 1 263 ? 175.698 139.374 144.787 1.00 72.22  ? 239 LYS   A O     1 
ATOM   1963 C  CB    . LYS   A 1 263 ? 176.709 139.121 147.925 1.00 62.32  ? 239 LYS   A CB    1 
ATOM   1964 C  CG    . LYS   A 1 263 ? 176.539 139.944 149.196 1.00 67.28  ? 239 LYS   A CG    1 
ATOM   1965 C  CD    . LYS   A 1 263 ? 175.100 140.410 149.370 1.00 68.15  ? 239 LYS   A CD    1 
ATOM   1966 C  CE    . LYS   A 1 263 ? 174.809 140.799 150.808 1.00 63.02  ? 239 LYS   A CE    1 
ATOM   1967 N  NZ    . LYS   A 1 263 ? 173.482 141.458 150.945 1.00 62.66  ? 239 LYS   A NZ    1 
ATOM   1968 N  N     . LEU   A 1 264 ? 174.924 141.016 146.122 1.00 51.25  ? 240 LEU   A N     1 
ATOM   1969 C  CA    . LEU   A 1 264 ? 173.774 141.281 145.263 1.00 53.40  ? 240 LEU   A CA    1 
ATOM   1970 C  C     . LEU   A 1 264 ? 174.213 141.816 143.907 1.00 56.48  ? 240 LEU   A C     1 
ATOM   1971 O  O     . LEU   A 1 264 ? 173.631 141.461 142.874 1.00 60.10  ? 240 LEU   A O     1 
ATOM   1972 C  CB    . LEU   A 1 264 ? 172.827 142.265 145.947 1.00 50.96  ? 240 LEU   A CB    1 
ATOM   1973 C  CG    . LEU   A 1 264 ? 171.814 141.678 146.928 1.00 57.16  ? 240 LEU   A CG    1 
ATOM   1974 C  CD1   . LEU   A 1 264 ? 170.927 142.771 147.492 1.00 55.27  ? 240 LEU   A CD1   1 
ATOM   1975 C  CD2   . LEU   A 1 264 ? 170.979 140.606 146.254 1.00 62.88  ? 240 LEU   A CD2   1 
ATOM   1976 N  N     . MET   A 1 265 ? 175.233 142.677 143.892 1.00 53.91  ? 241 MET   A N     1 
ATOM   1977 C  CA    . MET   A 1 265 ? 175.773 143.179 142.633 1.00 53.02  ? 241 MET   A CA    1 
ATOM   1978 C  C     . MET   A 1 265 ? 176.254 142.034 141.751 1.00 60.90  ? 241 MET   A C     1 
ATOM   1979 O  O     . MET   A 1 265 ? 175.915 141.963 140.563 1.00 71.80  ? 241 MET   A O     1 
ATOM   1980 C  CB    . MET   A 1 265 ? 176.917 144.154 142.912 1.00 57.44  ? 241 MET   A CB    1 
ATOM   1981 C  CG    . MET   A 1 265 ? 176.527 145.618 142.866 1.00 64.53  ? 241 MET   A CG    1 
ATOM   1982 S  SD    . MET   A 1 265 ? 177.960 146.710 142.804 1.00 72.14  ? 241 MET   A SD    1 
ATOM   1983 C  CE    . MET   A 1 265 ? 177.684 147.537 141.243 1.00 60.12  ? 241 MET   A CE    1 
ATOM   1984 N  N     . LEU   A 1 266 ? 177.046 141.123 142.322 1.00 44.41  ? 242 LEU   A N     1 
ATOM   1985 C  CA    . LEU   A 1 266 ? 177.564 140.002 141.543 1.00 41.83  ? 242 LEU   A CA    1 
ATOM   1986 C  C     . LEU   A 1 266 ? 176.442 139.087 141.067 1.00 49.48  ? 242 LEU   A C     1 
ATOM   1987 O  O     . LEU   A 1 266 ? 176.456 138.620 139.921 1.00 56.48  ? 242 LEU   A O     1 
ATOM   1988 C  CB    . LEU   A 1 266 ? 178.584 139.221 142.369 1.00 45.25  ? 242 LEU   A CB    1 
ATOM   1989 C  CG    . LEU   A 1 266 ? 179.891 139.950 142.685 1.00 47.55  ? 242 LEU   A CG    1 
ATOM   1990 C  CD1   . LEU   A 1 266 ? 180.846 139.038 143.431 1.00 47.09  ? 242 LEU   A CD1   1 
ATOM   1991 C  CD2   . LEU   A 1 266 ? 180.533 140.471 141.412 1.00 49.64  ? 242 LEU   A CD2   1 
ATOM   1992 N  N     . TYR   A 1 267 ? 175.459 138.822 141.932 1.00 43.22  ? 243 TYR   A N     1 
ATOM   1993 C  CA    . TYR   A 1 267 ? 174.348 137.957 141.552 1.00 38.64  ? 243 TYR   A CA    1 
ATOM   1994 C  C     . TYR   A 1 267 ? 173.547 138.557 140.402 1.00 48.47  ? 243 TYR   A C     1 
ATOM   1995 O  O     . TYR   A 1 267 ? 173.183 137.852 139.452 1.00 51.75  ? 243 TYR   A O     1 
ATOM   1996 C  CB    . TYR   A 1 267 ? 173.458 137.702 142.770 1.00 43.82  ? 243 TYR   A CB    1 
ATOM   1997 C  CG    . TYR   A 1 267 ? 172.038 137.295 142.450 1.00 52.44  ? 243 TYR   A CG    1 
ATOM   1998 C  CD1   . TYR   A 1 267 ? 171.754 136.041 141.928 1.00 51.51  ? 243 TYR   A CD1   1 
ATOM   1999 C  CD2   . TYR   A 1 267 ? 170.980 138.158 142.689 1.00 55.16  ? 243 TYR   A CD2   1 
ATOM   2000 C  CE1   . TYR   A 1 267 ? 170.457 135.664 141.641 1.00 49.58  ? 243 TYR   A CE1   1 
ATOM   2001 C  CE2   . TYR   A 1 267 ? 169.680 137.790 142.405 1.00 53.67  ? 243 TYR   A CE2   1 
ATOM   2002 C  CZ    . TYR   A 1 267 ? 169.425 136.543 141.881 1.00 49.31  ? 243 TYR   A CZ    1 
ATOM   2003 O  OH    . TYR   A 1 267 ? 168.131 136.175 141.599 1.00 44.77  ? 243 TYR   A OH    1 
ATOM   2004 N  N     . ASN   A 1 268 ? 173.284 139.864 140.455 1.00 55.25  ? 244 ASN   A N     1 
ATOM   2005 C  CA    . ASN   A 1 268 ? 172.531 140.502 139.382 1.00 51.51  ? 244 ASN   A CA    1 
ATOM   2006 C  C     . ASN   A 1 268 ? 173.337 140.579 138.091 1.00 52.80  ? 244 ASN   A C     1 
ATOM   2007 O  O     . ASN   A 1 268 ? 172.769 140.442 137.000 1.00 60.67  ? 244 ASN   A O     1 
ATOM   2008 C  CB    . ASN   A 1 268 ? 172.074 141.889 139.822 1.00 49.47  ? 244 ASN   A CB    1 
ATOM   2009 C  CG    . ASN   A 1 268 ? 170.927 141.831 140.806 1.00 55.51  ? 244 ASN   A CG    1 
ATOM   2010 O  OD1   . ASN   A 1 268 ? 169.760 141.855 140.419 1.00 61.11  ? 244 ASN   A OD1   1 
ATOM   2011 N  ND2   . ASN   A 1 268 ? 171.253 141.740 142.088 1.00 52.37  ? 244 ASN   A ND2   1 
ATOM   2012 N  N     . PHE   A 1 269 ? 174.653 140.787 138.187 1.00 51.87  ? 245 PHE   A N     1 
ATOM   2013 C  CA    . PHE   A 1 269 ? 175.484 140.752 136.987 1.00 53.07  ? 245 PHE   A CA    1 
ATOM   2014 C  C     . PHE   A 1 269 ? 175.443 139.375 136.337 1.00 60.62  ? 245 PHE   A C     1 
ATOM   2015 O  O     . PHE   A 1 269 ? 175.341 139.261 135.108 1.00 63.23  ? 245 PHE   A O     1 
ATOM   2016 C  CB    . PHE   A 1 269 ? 176.923 141.142 137.327 1.00 53.28  ? 245 PHE   A CB    1 
ATOM   2017 C  CG    . PHE   A 1 269 ? 177.098 142.596 137.676 1.00 60.05  ? 245 PHE   A CG    1 
ATOM   2018 C  CD1   . PHE   A 1 269 ? 176.034 143.480 137.600 1.00 61.64  ? 245 PHE   A CD1   1 
ATOM   2019 C  CD2   . PHE   A 1 269 ? 178.332 143.077 138.074 1.00 58.40  ? 245 PHE   A CD2   1 
ATOM   2020 C  CE1   . PHE   A 1 269 ? 176.199 144.813 137.923 1.00 59.38  ? 245 PHE   A CE1   1 
ATOM   2021 C  CE2   . PHE   A 1 269 ? 178.503 144.409 138.395 1.00 59.65  ? 245 PHE   A CE2   1 
ATOM   2022 C  CZ    . PHE   A 1 269 ? 177.434 145.277 138.319 1.00 62.10  ? 245 PHE   A CZ    1 
ATOM   2023 N  N     . GLY   A 1 270 ? 175.511 138.317 137.149 1.00 61.58  ? 246 GLY   A N     1 
ATOM   2024 C  CA    . GLY   A 1 270 ? 175.389 136.973 136.609 1.00 58.35  ? 246 GLY   A CA    1 
ATOM   2025 C  C     . GLY   A 1 270 ? 174.039 136.721 135.965 1.00 56.53  ? 246 GLY   A C     1 
ATOM   2026 O  O     . GLY   A 1 270 ? 173.951 136.079 134.914 1.00 66.93  ? 246 GLY   A O     1 
ATOM   2027 N  N     . ILE   A 1 271 ? 172.967 137.217 136.588 1.00 54.15  ? 247 ILE   A N     1 
ATOM   2028 C  CA    . ILE   A 1 271 ? 171.630 137.056 136.018 1.00 58.07  ? 247 ILE   A CA    1 
ATOM   2029 C  C     . ILE   A 1 271 ? 171.549 137.735 134.655 1.00 55.19  ? 247 ILE   A C     1 
ATOM   2030 O  O     . ILE   A 1 271 ? 171.023 137.170 133.685 1.00 59.22  ? 247 ILE   A O     1 
ATOM   2031 C  CB    . ILE   A 1 271 ? 170.566 137.603 136.987 1.00 56.50  ? 247 ILE   A CB    1 
ATOM   2032 C  CG1   . ILE   A 1 271 ? 170.241 136.567 138.063 1.00 60.52  ? 247 ILE   A CG1   1 
ATOM   2033 C  CG2   . ILE   A 1 271 ? 169.304 138.002 136.239 1.00 56.22  ? 247 ILE   A CG2   1 
ATOM   2034 C  CD1   . ILE   A 1 271 ? 169.835 135.221 137.511 1.00 59.43  ? 247 ILE   A CD1   1 
ATOM   2035 N  N     . VAL   A 1 272 ? 172.073 138.961 134.562 1.00 54.25  ? 248 VAL   A N     1 
ATOM   2036 C  CA    . VAL   A 1 272 ? 172.045 139.687 133.296 1.00 55.01  ? 248 VAL   A CA    1 
ATOM   2037 C  C     . VAL   A 1 272 ? 172.854 138.954 132.232 1.00 57.95  ? 248 VAL   A C     1 
ATOM   2038 O  O     . VAL   A 1 272 ? 172.416 138.837 131.079 1.00 58.81  ? 248 VAL   A O     1 
ATOM   2039 C  CB    . VAL   A 1 272 ? 172.546 141.130 133.501 1.00 54.56  ? 248 VAL   A CB    1 
ATOM   2040 C  CG1   . VAL   A 1 272 ? 173.156 141.682 132.222 1.00 52.06  ? 248 VAL   A CG1   1 
ATOM   2041 C  CG2   . VAL   A 1 272 ? 171.412 142.020 133.978 1.00 54.17  ? 248 VAL   A CG2   1 
ATOM   2042 N  N     . ALA   A 1 273 ? 174.036 138.446 132.594 1.00 53.02  ? 249 ALA   A N     1 
ATOM   2043 C  CA    . ALA   A 1 273 ? 174.854 137.719 131.626 1.00 49.86  ? 249 ALA   A CA    1 
ATOM   2044 C  C     . ALA   A 1 273 ? 174.153 136.458 131.134 1.00 52.86  ? 249 ALA   A C     1 
ATOM   2045 O  O     . ALA   A 1 273 ? 174.182 136.155 129.935 1.00 57.86  ? 249 ALA   A O     1 
ATOM   2046 C  CB    . ALA   A 1 273 ? 176.209 137.374 132.239 1.00 51.23  ? 249 ALA   A CB    1 
ATOM   2047 N  N     . ILE   A 1 274 ? 173.522 135.710 132.043 1.00 59.55  ? 250 ILE   A N     1 
ATOM   2048 C  CA    . ILE   A 1 274 ? 172.820 134.491 131.647 1.00 56.31  ? 250 ILE   A CA    1 
ATOM   2049 C  C     . ILE   A 1 274 ? 171.666 134.818 130.707 1.00 58.01  ? 250 ILE   A C     1 
ATOM   2050 O  O     . ILE   A 1 274 ? 171.471 134.148 129.680 1.00 66.56  ? 250 ILE   A O     1 
ATOM   2051 C  CB    . ILE   A 1 274 ? 172.341 133.725 132.894 1.00 53.53  ? 250 ILE   A CB    1 
ATOM   2052 C  CG1   . ILE   A 1 274 ? 173.469 132.853 133.448 1.00 61.57  ? 250 ILE   A CG1   1 
ATOM   2053 C  CG2   . ILE   A 1 274 ? 171.120 132.879 132.574 1.00 52.81  ? 250 ILE   A CG2   1 
ATOM   2054 C  CD1   . ILE   A 1 274 ? 173.164 132.249 134.799 1.00 59.46  ? 250 ILE   A CD1   1 
ATOM   2055 N  N     . PHE   A 1 275 ? 170.884 135.850 131.040 1.00 56.71  ? 251 PHE   A N     1 
ATOM   2056 C  CA    . PHE   A 1 275 ? 169.777 136.242 130.174 1.00 50.33  ? 251 PHE   A CA    1 
ATOM   2057 C  C     . PHE   A 1 275 ? 170.276 136.637 128.791 1.00 52.70  ? 251 PHE   A C     1 
ATOM   2058 O  O     . PHE   A 1 275 ? 169.707 136.218 127.776 1.00 52.74  ? 251 PHE   A O     1 
ATOM   2059 C  CB    . PHE   A 1 275 ? 168.995 137.393 130.805 1.00 51.47  ? 251 PHE   A CB    1 
ATOM   2060 C  CG    . PHE   A 1 275 ? 167.728 136.965 131.485 1.00 54.16  ? 251 PHE   A CG    1 
ATOM   2061 C  CD1   . PHE   A 1 275 ? 166.591 136.688 130.748 1.00 63.20  ? 251 PHE   A CD1   1 
ATOM   2062 C  CD2   . PHE   A 1 275 ? 167.672 136.849 132.863 1.00 53.26  ? 251 PHE   A CD2   1 
ATOM   2063 C  CE1   . PHE   A 1 275 ? 165.423 136.296 131.371 1.00 63.84  ? 251 PHE   A CE1   1 
ATOM   2064 C  CE2   . PHE   A 1 275 ? 166.507 136.459 133.491 1.00 57.38  ? 251 PHE   A CE2   1 
ATOM   2065 C  CZ    . PHE   A 1 275 ? 165.381 136.182 132.744 1.00 62.20  ? 251 PHE   A CZ    1 
ATOM   2066 N  N     . PHE   A 1 276 ? 171.349 137.431 128.731 1.00 64.59  ? 252 PHE   A N     1 
ATOM   2067 C  CA    . PHE   A 1 276 ? 171.881 137.854 127.440 1.00 62.96  ? 252 PHE   A CA    1 
ATOM   2068 C  C     . PHE   A 1 276 ? 172.367 136.666 126.621 1.00 66.88  ? 252 PHE   A C     1 
ATOM   2069 O  O     . PHE   A 1 276 ? 172.096 136.587 125.417 1.00 70.86  ? 252 PHE   A O     1 
ATOM   2070 C  CB    . PHE   A 1 276 ? 173.012 138.861 127.639 1.00 59.91  ? 252 PHE   A CB    1 
ATOM   2071 C  CG    . PHE   A 1 276 ? 173.654 139.309 126.359 1.00 63.15  ? 252 PHE   A CG    1 
ATOM   2072 C  CD1   . PHE   A 1 276 ? 172.911 139.951 125.384 1.00 68.78  ? 252 PHE   A CD1   1 
ATOM   2073 C  CD2   . PHE   A 1 276 ? 174.999 139.086 126.128 1.00 64.45  ? 252 PHE   A CD2   1 
ATOM   2074 C  CE1   . PHE   A 1 276 ? 173.500 140.364 124.204 1.00 68.80  ? 252 PHE   A CE1   1 
ATOM   2075 C  CE2   . PHE   A 1 276 ? 175.593 139.496 124.951 1.00 63.75  ? 252 PHE   A CE2   1 
ATOM   2076 C  CZ    . PHE   A 1 276 ? 174.842 140.136 123.988 1.00 63.88  ? 252 PHE   A CZ    1 
ATOM   2077 N  N     . ALA   A 1 277 ? 173.082 135.732 127.252 1.00 66.52  ? 253 ALA   A N     1 
ATOM   2078 C  CA    . ALA   A 1 277 ? 173.604 134.582 126.519 1.00 61.21  ? 253 ALA   A CA    1 
ATOM   2079 C  C     . ALA   A 1 277 ? 172.475 133.729 125.953 1.00 66.33  ? 253 ALA   A C     1 
ATOM   2080 O  O     . ALA   A 1 277 ? 172.485 133.373 124.765 1.00 74.00  ? 253 ALA   A O     1 
ATOM   2081 C  CB    . ALA   A 1 277 ? 174.507 133.748 127.428 1.00 61.03  ? 253 ALA   A CB    1 
ATOM   2082 N  N     . ILE   A 1 278 ? 171.486 133.397 126.788 1.00 60.16  ? 254 ILE   A N     1 
ATOM   2083 C  CA    . ILE   A 1 278 ? 170.385 132.559 126.321 1.00 54.18  ? 254 ILE   A CA    1 
ATOM   2084 C  C     . ILE   A 1 278 ? 169.604 133.264 125.218 1.00 57.22  ? 254 ILE   A C     1 
ATOM   2085 O  O     . ILE   A 1 278 ? 169.259 132.653 124.196 1.00 60.52  ? 254 ILE   A O     1 
ATOM   2086 C  CB    . ILE   A 1 278 ? 169.477 132.162 127.498 1.00 59.80  ? 254 ILE   A CB    1 
ATOM   2087 C  CG1   . ILE   A 1 278 ? 170.238 131.266 128.476 1.00 56.86  ? 254 ILE   A CG1   1 
ATOM   2088 C  CG2   . ILE   A 1 278 ? 168.231 131.452 126.996 1.00 63.29  ? 254 ILE   A CG2   1 
ATOM   2089 C  CD1   . ILE   A 1 278 ? 169.399 130.784 129.636 1.00 59.19  ? 254 ILE   A CD1   1 
ATOM   2090 N  N     . GLY   A 1 279 ? 169.319 134.556 125.398 1.00 60.48  ? 255 GLY   A N     1 
ATOM   2091 C  CA    . GLY   A 1 279 ? 168.578 135.285 124.385 1.00 56.20  ? 255 GLY   A CA    1 
ATOM   2092 C  C     . GLY   A 1 279 ? 169.311 135.362 123.062 1.00 58.64  ? 255 GLY   A C     1 
ATOM   2093 O  O     . GLY   A 1 279 ? 168.711 135.162 122.003 1.00 65.40  ? 255 GLY   A O     1 
ATOM   2094 N  N     . ALA   A 1 280 ? 170.616 135.645 123.098 1.00 61.08  ? 256 ALA   A N     1 
ATOM   2095 C  CA    . ALA   A 1 280 ? 171.388 135.714 121.863 1.00 58.79  ? 256 ALA   A CA    1 
ATOM   2096 C  C     . ALA   A 1 280 ? 171.422 134.368 121.153 1.00 63.38  ? 256 ALA   A C     1 
ATOM   2097 O  O     . ALA   A 1 280 ? 171.230 134.301 119.932 1.00 66.74  ? 256 ALA   A O     1 
ATOM   2098 C  CB    . ALA   A 1 280 ? 172.805 136.203 122.156 1.00 58.36  ? 256 ALA   A CB    1 
ATOM   2099 N  N     . TYR   A 1 281 ? 171.658 133.282 121.897 1.00 67.06  ? 257 TYR   A N     1 
ATOM   2100 C  CA    . TYR   A 1 281 ? 171.712 131.969 121.263 1.00 65.58  ? 257 TYR   A CA    1 
ATOM   2101 C  C     . TYR   A 1 281 ? 170.375 131.610 120.624 1.00 67.95  ? 257 TYR   A C     1 
ATOM   2102 O  O     . TYR   A 1 281 ? 170.325 131.170 119.468 1.00 72.25  ? 257 TYR   A O     1 
ATOM   2103 C  CB    . TYR   A 1 281 ? 172.125 130.905 122.279 1.00 69.32  ? 257 TYR   A CB    1 
ATOM   2104 C  CG    . TYR   A 1 281 ? 171.991 129.493 121.756 1.00 74.65  ? 257 TYR   A CG    1 
ATOM   2105 C  CD1   . TYR   A 1 281 ? 172.790 129.040 120.715 1.00 69.35  ? 257 TYR   A CD1   1 
ATOM   2106 C  CD2   . TYR   A 1 281 ? 171.064 128.615 122.299 1.00 73.93  ? 257 TYR   A CD2   1 
ATOM   2107 C  CE1   . TYR   A 1 281 ? 172.671 127.753 120.232 1.00 66.33  ? 257 TYR   A CE1   1 
ATOM   2108 C  CE2   . TYR   A 1 281 ? 170.938 127.325 121.821 1.00 73.25  ? 257 TYR   A CE2   1 
ATOM   2109 C  CZ    . TYR   A 1 281 ? 171.744 126.900 120.788 1.00 71.60  ? 257 TYR   A CZ    1 
ATOM   2110 O  OH    . TYR   A 1 281 ? 171.623 125.616 120.310 1.00 71.99  ? 257 TYR   A OH    1 
ATOM   2111 N  N     . LEU   A 1 282 ? 169.275 131.807 121.357 1.00 69.65  ? 258 LEU   A N     1 
ATOM   2112 C  CA    . LEU   A 1 282 ? 167.964 131.465 120.813 1.00 64.99  ? 258 LEU   A CA    1 
ATOM   2113 C  C     . LEU   A 1 282 ? 167.608 132.343 119.620 1.00 68.08  ? 258 LEU   A C     1 
ATOM   2114 O  O     . LEU   A 1 282 ? 167.016 131.862 118.647 1.00 64.82  ? 258 LEU   A O     1 
ATOM   2115 C  CB    . LEU   A 1 282 ? 166.898 131.570 121.901 1.00 64.42  ? 258 LEU   A CB    1 
ATOM   2116 C  CG    . LEU   A 1 282 ? 166.350 130.233 122.402 1.00 71.42  ? 258 LEU   A CG    1 
ATOM   2117 C  CD1   . LEU   A 1 282 ? 167.483 129.289 122.765 1.00 69.56  ? 258 LEU   A CD1   1 
ATOM   2118 C  CD2   . LEU   A 1 282 ? 165.424 130.443 123.587 1.00 72.30  ? 258 LEU   A CD2   1 
ATOM   2119 N  N     . HIS   A 1 283 ? 167.951 133.633 119.674 1.00 77.26  ? 259 HIS   A N     1 
ATOM   2120 C  CA    . HIS   A 1 283 ? 167.659 134.521 118.556 1.00 71.83  ? 259 HIS   A CA    1 
ATOM   2121 C  C     . HIS   A 1 283 ? 168.432 134.117 117.310 1.00 75.73  ? 259 HIS   A C     1 
ATOM   2122 O  O     . HIS   A 1 283 ? 167.882 134.130 116.203 1.00 82.26  ? 259 HIS   A O     1 
ATOM   2123 C  CB    . HIS   A 1 283 ? 167.979 135.966 118.936 1.00 69.20  ? 259 HIS   A CB    1 
ATOM   2124 C  CG    . HIS   A 1 283 ? 167.868 136.928 117.795 1.00 73.03  ? 259 HIS   A CG    1 
ATOM   2125 N  ND1   . HIS   A 1 283 ? 166.662 137.429 117.358 1.00 75.27  ? 259 HIS   A ND1   1 
ATOM   2126 C  CD2   . HIS   A 1 283 ? 168.815 137.480 117.000 1.00 74.59  ? 259 HIS   A CD2   1 
ATOM   2127 C  CE1   . HIS   A 1 283 ? 166.869 138.249 116.344 1.00 76.54  ? 259 HIS   A CE1   1 
ATOM   2128 N  NE2   . HIS   A 1 283 ? 168.167 138.298 116.107 1.00 77.96  ? 259 HIS   A NE2   1 
ATOM   2129 N  N     . MET   A 1 284 ? 169.707 133.755 117.463 1.00 87.29  ? 260 MET   A N     1 
ATOM   2130 C  CA    . MET   A 1 284 ? 170.494 133.375 116.295 1.00 88.35  ? 260 MET   A CA    1 
ATOM   2131 C  C     . MET   A 1 284 ? 170.104 132.007 115.750 1.00 87.31  ? 260 MET   A C     1 
ATOM   2132 O  O     . MET   A 1 284 ? 170.252 131.766 114.548 1.00 87.16  ? 260 MET   A O     1 
ATOM   2133 C  CB    . MET   A 1 284 ? 171.987 133.406 116.625 1.00 88.01  ? 260 MET   A CB    1 
ATOM   2134 C  CG    . MET   A 1 284 ? 172.509 134.787 116.977 1.00 89.60  ? 260 MET   A CG    1 
ATOM   2135 S  SD    . MET   A 1 284 ? 172.277 135.969 115.637 1.00 98.54  ? 260 MET   A SD    1 
ATOM   2136 C  CE    . MET   A 1 284 ? 173.567 135.458 114.506 1.00 89.94  ? 260 MET   A CE    1 
ATOM   2137 N  N     . LYS   A 1 285 ? 169.609 131.104 116.600 1.00 80.09  ? 261 LYS   A N     1 
ATOM   2138 C  CA    . LYS   A 1 285 ? 169.267 129.772 116.108 1.00 79.95  ? 261 LYS   A CA    1 
ATOM   2139 C  C     . LYS   A 1 285 ? 168.006 129.792 115.249 1.00 82.56  ? 261 LYS   A C     1 
ATOM   2140 O  O     . LYS   A 1 285 ? 167.934 129.092 114.232 1.00 78.45  ? 261 LYS   A O     1 
ATOM   2141 C  CB    . LYS   A 1 285 ? 169.103 128.801 117.276 1.00 77.64  ? 261 LYS   A CB    1 
ATOM   2142 C  CG    . LYS   A 1 285 ? 169.024 127.345 116.848 1.00 77.02  ? 261 LYS   A CG    1 
ATOM   2143 C  CD    . LYS   A 1 285 ? 169.303 126.410 118.012 1.00 81.97  ? 261 LYS   A CD    1 
ATOM   2144 C  CE    . LYS   A 1 285 ? 168.554 125.098 117.864 1.00 82.71  ? 261 LYS   A CE    1 
ATOM   2145 N  NZ    . LYS   A 1 285 ? 167.082 125.287 117.877 1.00 80.29  ? 261 LYS   A NZ    1 
ATOM   2146 N  N     . TYR   A 1 286 ? 167.003 130.584 115.633 1.00 91.54  ? 262 TYR   A N     1 
ATOM   2147 C  CA    . TYR   A 1 286 ? 165.704 130.583 114.968 1.00 85.75  ? 262 TYR   A CA    1 
ATOM   2148 C  C     . TYR   A 1 286 ? 165.488 131.804 114.080 1.00 83.51  ? 262 TYR   A C     1 
ATOM   2149 O  O     . TYR   A 1 286 ? 164.357 132.060 113.657 1.00 86.45  ? 262 TYR   A O     1 
ATOM   2150 C  CB    . TYR   A 1 286 ? 164.579 130.490 115.998 1.00 88.71  ? 262 TYR   A CB    1 
ATOM   2151 C  CG    . TYR   A 1 286 ? 164.455 129.144 116.669 1.00 87.80  ? 262 TYR   A CG    1 
ATOM   2152 C  CD1   . TYR   A 1 286 ? 163.589 128.180 116.175 1.00 87.50  ? 262 TYR   A CD1   1 
ATOM   2153 C  CD2   . TYR   A 1 286 ? 165.189 128.845 117.808 1.00 87.81  ? 262 TYR   A CD2   1 
ATOM   2154 C  CE1   . TYR   A 1 286 ? 163.467 126.950 116.787 1.00 87.88  ? 262 TYR   A CE1   1 
ATOM   2155 C  CE2   . TYR   A 1 286 ? 165.072 127.620 118.429 1.00 88.15  ? 262 TYR   A CE2   1 
ATOM   2156 C  CZ    . TYR   A 1 286 ? 164.211 126.675 117.913 1.00 89.63  ? 262 TYR   A CZ    1 
ATOM   2157 O  OH    . TYR   A 1 286 ? 164.091 125.450 118.528 1.00 90.15  ? 262 TYR   A OH    1 
ATOM   2158 N  N     . ARG   A 1 287 ? 166.543 132.569 113.795 1.00 85.60  ? 263 ARG   A N     1 
ATOM   2159 C  CA    . ARG   A 1 287 ? 166.376 133.799 113.024 1.00 86.05  ? 263 ARG   A CA    1 
ATOM   2160 C  C     . ARG   A 1 287 ? 165.911 133.514 111.600 1.00 93.60  ? 263 ARG   A C     1 
ATOM   2161 O  O     . ARG   A 1 287 ? 165.094 134.260 111.048 1.00 91.77  ? 263 ARG   A O     1 
ATOM   2162 C  CB    . ARG   A 1 287 ? 167.682 134.592 113.011 1.00 86.14  ? 263 ARG   A CB    1 
ATOM   2163 C  CG    . ARG   A 1 287 ? 167.616 135.876 112.204 1.00 87.67  ? 263 ARG   A CG    1 
ATOM   2164 C  CD    . ARG   A 1 287 ? 168.500 136.953 112.806 1.00 91.03  ? 263 ARG   A CD    1 
ATOM   2165 N  NE    . ARG   A 1 287 ? 169.766 137.083 112.097 1.00 91.98  ? 263 ARG   A NE    1 
ATOM   2166 C  CZ    . ARG   A 1 287 ? 170.658 138.037 112.327 1.00 90.58  ? 263 ARG   A CZ    1 
ATOM   2167 N  NH1   . ARG   A 1 287 ? 170.453 138.967 113.245 1.00 86.16  ? 263 ARG   A NH1   1 
ATOM   2168 N  NH2   . ARG   A 1 287 ? 171.781 138.060 111.616 1.00 91.22  ? 263 ARG   A NH2   1 
ATOM   2169 N  N     . ASP   A 1 288 ? 166.420 132.442 110.989 1.00 117.52 ? 264 ASP   A N     1 
ATOM   2170 C  CA    . ASP   A 1 288 ? 166.115 132.174 109.586 1.00 115.22 ? 264 ASP   A CA    1 
ATOM   2171 C  C     . ASP   A 1 288 ? 164.669 131.738 109.383 1.00 112.53 ? 264 ASP   A C     1 
ATOM   2172 O  O     . ASP   A 1 288 ? 164.069 132.055 108.350 1.00 110.96 ? 264 ASP   A O     1 
ATOM   2173 C  CB    . ASP   A 1 288 ? 167.068 131.113 109.038 1.00 114.82 ? 264 ASP   A CB    1 
ATOM   2174 C  CG    . ASP   A 1 288 ? 167.999 130.561 110.099 1.00 115.60 ? 264 ASP   A CG    1 
ATOM   2175 O  OD1   . ASP   A 1 288 ? 168.550 131.361 110.884 1.00 113.85 ? 264 ASP   A OD1   1 
ATOM   2176 O  OD2   . ASP   A 1 288 ? 168.182 129.327 110.149 1.00 115.39 ? 264 ASP   A OD2   1 
ATOM   2177 N  N     . GLN   A 1 289 ? 164.092 131.021 110.347 1.00 105.39 ? 265 GLN   A N     1 
ATOM   2178 C  CA    . GLN   A 1 289 ? 162.756 130.453 110.217 1.00 105.79 ? 265 GLN   A CA    1 
ATOM   2179 C  C     . GLN   A 1 289 ? 161.685 131.321 110.871 1.00 105.45 ? 265 GLN   A C     1 
ATOM   2180 O  O     . GLN   A 1 289 ? 160.693 130.797 111.388 1.00 104.85 ? 265 GLN   A O     1 
ATOM   2181 C  CB    . GLN   A 1 289 ? 162.729 129.043 110.806 1.00 105.28 ? 265 GLN   A CB    1 
ATOM   2182 C  CG    . GLN   A 1 289 ? 164.086 128.365 110.828 1.00 104.59 ? 265 GLN   A CG    1 
ATOM   2183 C  CD    . GLN   A 1 289 ? 164.119 127.161 111.743 1.00 106.38 ? 265 GLN   A CD    1 
ATOM   2184 O  OE1   . GLN   A 1 289 ? 163.077 126.631 112.129 1.00 105.70 ? 265 GLN   A OE1   1 
ATOM   2185 N  NE2   . GLN   A 1 289 ? 165.320 126.721 112.100 1.00 104.20 ? 265 GLN   A NE2   1 
ATOM   2186 N  N     . PHE   A 1 290 ? 161.867 132.643 110.860 1.00 93.02  ? 266 PHE   A N     1 
ATOM   2187 C  CA    . PHE   A 1 290 ? 160.891 133.526 111.491 1.00 91.42  ? 266 PHE   A CA    1 
ATOM   2188 C  C     . PHE   A 1 290 ? 159.602 133.602 110.681 1.00 94.63  ? 266 PHE   A C     1 
ATOM   2189 O  O     . PHE   A 1 290 ? 158.506 133.627 111.252 1.00 93.29  ? 266 PHE   A O     1 
ATOM   2190 C  CB    . PHE   A 1 290 ? 161.489 134.920 111.678 1.00 88.62  ? 266 PHE   A CB    1 
ATOM   2191 C  CG    . PHE   A 1 290 ? 162.072 135.152 113.044 1.00 92.06  ? 266 PHE   A CG    1 
ATOM   2192 C  CD1   . PHE   A 1 290 ? 161.850 134.249 114.069 1.00 89.40  ? 266 PHE   A CD1   1 
ATOM   2193 C  CD2   . PHE   A 1 290 ? 162.841 136.273 113.301 1.00 90.00  ? 266 PHE   A CD2   1 
ATOM   2194 C  CE1   . PHE   A 1 290 ? 162.388 134.460 115.324 1.00 89.73  ? 266 PHE   A CE1   1 
ATOM   2195 C  CE2   . PHE   A 1 290 ? 163.381 136.489 114.553 1.00 87.56  ? 266 PHE   A CE2   1 
ATOM   2196 C  CZ    . PHE   A 1 290 ? 163.153 135.581 115.565 1.00 89.41  ? 266 PHE   A CZ    1 
ATOM   2197 N  N     . ALA   A 1 291 ? 159.713 133.641 109.350 1.00 100.08 ? 267 ALA   A N     1 
ATOM   2198 C  CA    . ALA   A 1 291 ? 158.532 133.809 108.508 1.00 97.27  ? 267 ALA   A CA    1 
ATOM   2199 C  C     . ALA   A 1 291 ? 157.592 132.613 108.593 1.00 93.88  ? 267 ALA   A C     1 
ATOM   2200 O  O     . ALA   A 1 291 ? 156.370 132.788 108.560 1.00 92.52  ? 267 ALA   A O     1 
ATOM   2201 C  CB    . ALA   A 1 291 ? 158.951 134.049 107.058 1.00 92.13  ? 267 ALA   A CB    1 
ATOM   2202 N  N     . ASP   A 1 292 ? 158.135 131.397 108.690 1.00 105.98 ? 268 ASP   A N     1 
ATOM   2203 C  CA    . ASP   A 1 292 ? 157.280 130.217 108.780 1.00 109.84 ? 268 ASP   A CA    1 
ATOM   2204 C  C     . ASP   A 1 292 ? 156.477 130.210 110.075 1.00 110.85 ? 268 ASP   A C     1 
ATOM   2205 O  O     . ASP   A 1 292 ? 155.298 129.838 110.079 1.00 111.58 ? 268 ASP   A O     1 
ATOM   2206 C  CB    . ASP   A 1 292 ? 158.122 128.948 108.662 1.00 111.04 ? 268 ASP   A CB    1 
ATOM   2207 C  CG    . ASP   A 1 292 ? 158.176 128.415 107.244 1.00 114.48 ? 268 ASP   A CG    1 
ATOM   2208 O  OD1   . ASP   A 1 292 ? 157.184 127.799 106.800 1.00 111.71 ? 268 ASP   A OD1   1 
ATOM   2209 O  OD2   . ASP   A 1 292 ? 159.211 128.611 106.573 1.00 116.39 ? 268 ASP   A OD2   1 
ATOM   2210 N  N     . PHE   A 1 293 ? 157.098 130.612 111.186 1.00 104.30 ? 269 PHE   A N     1 
ATOM   2211 C  CA    . PHE   A 1 293 ? 156.390 130.655 112.461 1.00 103.23 ? 269 PHE   A CA    1 
ATOM   2212 C  C     . PHE   A 1 293 ? 155.391 131.805 112.513 1.00 103.44 ? 269 PHE   A C     1 
ATOM   2213 O  O     . PHE   A 1 293 ? 154.263 131.629 112.985 1.00 106.28 ? 269 PHE   A O     1 
ATOM   2214 C  CB    . PHE   A 1 293 ? 157.387 130.770 113.614 1.00 100.02 ? 269 PHE   A CB    1 
ATOM   2215 C  CG    . PHE   A 1 293 ? 158.023 129.466 113.995 1.00 100.79 ? 269 PHE   A CG    1 
ATOM   2216 C  CD1   . PHE   A 1 293 ? 157.252 128.409 114.445 1.00 102.79 ? 269 PHE   A CD1   1 
ATOM   2217 C  CD2   . PHE   A 1 293 ? 159.394 129.299 113.908 1.00 101.87 ? 269 PHE   A CD2   1 
ATOM   2218 C  CE1   . PHE   A 1 293 ? 157.836 127.209 114.798 1.00 102.68 ? 269 PHE   A CE1   1 
ATOM   2219 C  CE2   . PHE   A 1 293 ? 159.984 128.102 114.259 1.00 102.98 ? 269 PHE   A CE2   1 
ATOM   2220 C  CZ    . PHE   A 1 293 ? 159.204 127.055 114.705 1.00 103.89 ? 269 PHE   A CZ    1 
ATOM   2221 N  N     . LEU   A 1 294 ? 155.784 132.982 112.036 1.00 99.70  ? 270 LEU   A N     1 
ATOM   2222 C  CA    . LEU   A 1 294 ? 154.920 134.152 112.091 1.00 102.54 ? 270 LEU   A CA    1 
ATOM   2223 C  C     . LEU   A 1 294 ? 154.056 134.214 110.837 1.00 105.34 ? 270 LEU   A C     1 
ATOM   2224 O  O     . LEU   A 1 294 ? 154.532 134.559 109.757 1.00 103.97 ? 270 LEU   A O     1 
ATOM   2225 C  CB    . LEU   A 1 294 ? 155.761 135.426 112.249 1.00 101.32 ? 270 LEU   A CB    1 
ATOM   2226 C  CG    . LEU   A 1 294 ? 155.127 136.788 112.562 1.00 102.93 ? 270 LEU   A CG    1 
ATOM   2227 C  CD1   . LEU   A 1 294 ? 156.216 137.751 112.992 1.00 103.37 ? 270 LEU   A CD1   1 
ATOM   2228 C  CD2   . LEU   A 1 294 ? 154.360 137.384 111.389 1.00 103.33 ? 270 LEU   A CD2   1 
ATOM   2229 O  OXT   . LEU   A 1 294 ? 152.859 133.928 110.877 1.00 105.94 ? 270 LEU   A OXT   1 
ATOM   2230 N  N     . MET   B 2 1   ? 179.157 142.877 79.179  1.00 115.92 ? 1   MET   B N     1 
ATOM   2231 C  CA    . MET   B 2 1   ? 178.960 141.459 79.456  1.00 118.23 ? 1   MET   B CA    1 
ATOM   2232 C  C     . MET   B 2 1   ? 179.284 141.128 80.909  1.00 117.61 ? 1   MET   B C     1 
ATOM   2233 O  O     . MET   B 2 1   ? 179.742 140.029 81.217  1.00 117.96 ? 1   MET   B O     1 
ATOM   2234 C  CB    . MET   B 2 1   ? 179.818 140.605 78.521  1.00 119.90 ? 1   MET   B CB    1 
ATOM   2235 C  CG    . MET   B 2 1   ? 179.364 140.624 77.072  1.00 121.03 ? 1   MET   B CG    1 
ATOM   2236 S  SD    . MET   B 2 1   ? 178.232 139.274 76.688  1.00 122.41 ? 1   MET   B SD    1 
ATOM   2237 C  CE    . MET   B 2 1   ? 179.355 137.879 76.702  1.00 118.25 ? 1   MET   B CE    1 
ATOM   2238 N  N     . ASN   B 2 2   ? 179.043 142.087 81.799  1.00 114.53 ? 2   ASN   B N     1 
ATOM   2239 C  CA    . ASN   B 2 2   ? 179.291 141.889 83.221  1.00 114.19 ? 2   ASN   B CA    1 
ATOM   2240 C  C     . ASN   B 2 2   ? 178.121 141.132 83.837  1.00 113.76 ? 2   ASN   B C     1 
ATOM   2241 O  O     . ASN   B 2 2   ? 176.976 141.593 83.776  1.00 115.26 ? 2   ASN   B O     1 
ATOM   2242 C  CB    . ASN   B 2 2   ? 179.493 143.231 83.920  1.00 115.26 ? 2   ASN   B CB    1 
ATOM   2243 C  CG    . ASN   B 2 2   ? 180.458 144.135 83.179  1.00 116.38 ? 2   ASN   B CG    1 
ATOM   2244 O  OD1   . ASN   B 2 2   ? 181.216 143.683 82.321  1.00 116.80 ? 2   ASN   B OD1   1 
ATOM   2245 N  ND2   . ASN   B 2 2   ? 180.435 145.420 83.509  1.00 114.88 ? 2   ASN   B ND2   1 
ATOM   2246 N  N     . VAL   B 2 3   ? 178.408 139.977 84.433  1.00 102.48 ? 3   VAL   B N     1 
ATOM   2247 C  CA    . VAL   B 2 3   ? 177.371 139.166 85.065  1.00 103.56 ? 3   VAL   B CA    1 
ATOM   2248 C  C     . VAL   B 2 3   ? 176.878 139.911 86.302  1.00 103.92 ? 3   VAL   B C     1 
ATOM   2249 O  O     . VAL   B 2 3   ? 177.585 139.997 87.309  1.00 107.11 ? 3   VAL   B O     1 
ATOM   2250 C  CB    . VAL   B 2 3   ? 177.888 137.770 85.426  1.00 101.91 ? 3   VAL   B CB    1 
ATOM   2251 C  CG1   . VAL   B 2 3   ? 176.802 136.965 86.119  1.00 101.12 ? 3   VAL   B CG1   1 
ATOM   2252 C  CG2   . VAL   B 2 3   ? 178.379 137.050 84.182  1.00 103.75 ? 3   VAL   B CG2   1 
ATOM   2253 N  N     . SER   B 2 4   ? 175.661 140.452 86.228  1.00 96.48  ? 4   SER   B N     1 
ATOM   2254 C  CA    . SER   B 2 4   ? 175.127 141.233 87.338  1.00 95.50  ? 4   SER   B CA    1 
ATOM   2255 C  C     . SER   B 2 4   ? 174.612 140.330 88.453  1.00 94.16  ? 4   SER   B C     1 
ATOM   2256 O  O     . SER   B 2 4   ? 175.034 140.448 89.607  1.00 95.45  ? 4   SER   B O     1 
ATOM   2257 C  CB    . SER   B 2 4   ? 174.017 142.162 86.842  1.00 99.33  ? 4   SER   B CB    1 
ATOM   2258 O  OG    . SER   B 2 4   ? 174.469 143.503 86.773  1.00 100.82 ? 4   SER   B OG    1 
ATOM   2259 N  N     . VAL   B 2 5   ? 173.692 139.425 88.126  1.00 89.58  ? 5   VAL   B N     1 
ATOM   2260 C  CA    . VAL   B 2 5   ? 173.112 138.504 89.098  1.00 89.96  ? 5   VAL   B CA    1 
ATOM   2261 C  C     . VAL   B 2 5   ? 173.258 137.087 88.566  1.00 89.92  ? 5   VAL   B C     1 
ATOM   2262 O  O     . VAL   B 2 5   ? 172.976 136.829 87.391  1.00 90.32  ? 5   VAL   B O     1 
ATOM   2263 C  CB    . VAL   B 2 5   ? 171.633 138.824 89.384  1.00 87.78  ? 5   VAL   B CB    1 
ATOM   2264 C  CG1   . VAL   B 2 5   ? 171.142 138.027 90.584  1.00 85.79  ? 5   VAL   B CG1   1 
ATOM   2265 C  CG2   . VAL   B 2 5   ? 171.440 140.313 89.618  1.00 88.87  ? 5   VAL   B CG2   1 
ATOM   2266 N  N     . ASN   B 2 6   ? 173.697 136.171 89.423  1.00 90.05  ? 6   ASN   B N     1 
ATOM   2267 C  CA    . ASN   B 2 6   ? 173.772 134.763 89.058  1.00 88.63  ? 6   ASN   B CA    1 
ATOM   2268 C  C     . ASN   B 2 6   ? 173.013 133.922 90.072  1.00 90.20  ? 6   ASN   B C     1 
ATOM   2269 O  O     . ASN   B 2 6   ? 173.199 134.077 91.286  1.00 92.78  ? 6   ASN   B O     1 
ATOM   2270 C  CB    . ASN   B 2 6   ? 175.221 134.289 88.935  1.00 89.55  ? 6   ASN   B CB    1 
ATOM   2271 C  CG    . ASN   B 2 6   ? 175.425 133.353 87.768  1.00 90.21  ? 6   ASN   B CG    1 
ATOM   2272 O  OD1   . ASN   B 2 6   ? 174.500 132.659 87.350  1.00 96.21  ? 6   ASN   B OD1   1 
ATOM   2273 N  ND2   . ASN   B 2 6   ? 176.638 133.329 87.231  1.00 89.88  ? 6   ASN   B ND2   1 
ATOM   2274 N  N     . ILE   B 2 7   ? 172.158 133.038 89.562  1.00 95.17  ? 7   ILE   B N     1 
ATOM   2275 C  CA    . ILE   B 2 7   ? 171.310 132.157 90.353  1.00 95.23  ? 7   ILE   B CA    1 
ATOM   2276 C  C     . ILE   B 2 7   ? 171.536 130.734 89.866  1.00 95.36  ? 7   ILE   B C     1 
ATOM   2277 O  O     . ILE   B 2 7   ? 171.375 130.449 88.673  1.00 94.84  ? 7   ILE   B O     1 
ATOM   2278 C  CB    . ILE   B 2 7   ? 169.824 132.541 90.225  1.00 93.88  ? 7   ILE   B CB    1 
ATOM   2279 C  CG1   . ILE   B 2 7   ? 169.507 133.767 91.079  1.00 96.66  ? 7   ILE   B CG1   1 
ATOM   2280 C  CG2   . ILE   B 2 7   ? 168.930 131.373 90.594  1.00 91.14  ? 7   ILE   B CG2   1 
ATOM   2281 C  CD1   . ILE   B 2 7   ? 168.644 134.793 90.386  1.00 92.96  ? 7   ILE   B CD1   1 
ATOM   2282 N  N     . LYS   B 2 8   ? 171.900 129.843 90.785  1.00 99.73  ? 8   LYS   B N     1 
ATOM   2283 C  CA    . LYS   B 2 8   ? 172.210 128.458 90.450  1.00 99.90  ? 8   LYS   B CA    1 
ATOM   2284 C  C     . LYS   B 2 8   ? 171.435 127.531 91.377  1.00 102.25 ? 8   LYS   B C     1 
ATOM   2285 O  O     . LYS   B 2 8   ? 171.752 127.431 92.567  1.00 100.73 ? 8   LYS   B O     1 
ATOM   2286 C  CB    . LYS   B 2 8   ? 173.712 128.197 90.543  1.00 101.02 ? 8   LYS   B CB    1 
ATOM   2287 C  CG    . LYS   B 2 8   ? 174.266 127.409 89.369  1.00 101.89 ? 8   LYS   B CG    1 
ATOM   2288 C  CD    . LYS   B 2 8   ? 175.713 127.774 89.087  1.00 102.06 ? 8   LYS   B CD    1 
ATOM   2289 C  CE    . LYS   B 2 8   ? 175.840 129.240 88.705  1.00 102.27 ? 8   LYS   B CE    1 
ATOM   2290 N  NZ    . LYS   B 2 8   ? 177.261 129.665 88.583  1.00 100.89 ? 8   LYS   B NZ    1 
ATOM   2291 N  N     . ASN   B 2 9   ? 170.424 126.858 90.823  1.00 101.86 ? 9   ASN   B N     1 
ATOM   2292 C  CA    . ASN   B 2 9   ? 169.642 125.842 91.531  1.00 99.28  ? 9   ASN   B CA    1 
ATOM   2293 C  C     . ASN   B 2 9   ? 169.015 126.425 92.800  1.00 97.05  ? 9   ASN   B C     1 
ATOM   2294 O  O     . ASN   B 2 9   ? 169.308 126.003 93.919  1.00 98.90  ? 9   ASN   B O     1 
ATOM   2295 C  CB    . ASN   B 2 9   ? 170.504 124.611 91.842  1.00 98.32  ? 9   ASN   B CB    1 
ATOM   2296 C  CG    . ASN   B 2 9   ? 169.724 123.485 92.519  1.00 99.67  ? 9   ASN   B CG    1 
ATOM   2297 O  OD1   . ASN   B 2 9   ? 168.533 123.609 92.805  1.00 99.47  ? 9   ASN   B OD1   1 
ATOM   2298 N  ND2   . ASN   B 2 9   ? 170.407 122.375 92.777  1.00 98.96  ? 9   ASN   B ND2   1 
ATOM   2299 N  N     . VAL   B 2 10  ? 168.148 127.414 92.616  1.00 83.21  ? 10  VAL   B N     1 
ATOM   2300 C  CA    . VAL   B 2 10  ? 167.396 127.979 93.730  1.00 84.69  ? 10  VAL   B CA    1 
ATOM   2301 C  C     . VAL   B 2 10  ? 166.077 127.232 93.864  1.00 84.53  ? 10  VAL   B C     1 
ATOM   2302 O  O     . VAL   B 2 10  ? 165.341 127.062 92.885  1.00 84.61  ? 10  VAL   B O     1 
ATOM   2303 C  CB    . VAL   B 2 10  ? 167.172 129.485 93.532  1.00 84.27  ? 10  VAL   B CB    1 
ATOM   2304 C  CG1   . VAL   B 2 10  ? 166.025 129.968 94.400  1.00 85.14  ? 10  VAL   B CG1   1 
ATOM   2305 C  CG2   . VAL   B 2 10  ? 168.436 130.242 93.885  1.00 83.14  ? 10  VAL   B CG2   1 
ATOM   2306 N  N     . THR   B 2 11  ? 165.781 126.776 95.078  1.00 82.13  ? 11  THR   B N     1 
ATOM   2307 C  CA    . THR   B 2 11  ? 164.613 125.948 95.338  1.00 78.70  ? 11  THR   B CA    1 
ATOM   2308 C  C     . THR   B 2 11  ? 164.004 126.375 96.663  1.00 78.14  ? 11  THR   B C     1 
ATOM   2309 O  O     . THR   B 2 11  ? 164.728 126.551 97.647  1.00 86.63  ? 11  THR   B O     1 
ATOM   2310 C  CB    . THR   B 2 11  ? 165.001 124.466 95.372  1.00 80.87  ? 11  THR   B CB    1 
ATOM   2311 O  OG1   . THR   B 2 11  ? 165.599 124.104 94.121  1.00 85.84  ? 11  THR   B OG1   1 
ATOM   2312 C  CG2   . THR   B 2 11  ? 163.783 123.605 95.586  1.00 78.82  ? 11  THR   B CG2   1 
ATOM   2313 N  N     . LYS   B 2 12  ? 162.684 126.547 96.690  1.00 68.17  ? 12  LYS   B N     1 
ATOM   2314 C  CA    . LYS   B 2 12  ? 161.990 127.046 97.870  1.00 68.36  ? 12  LYS   B CA    1 
ATOM   2315 C  C     . LYS   B 2 12  ? 160.783 126.171 98.174  1.00 70.17  ? 12  LYS   B C     1 
ATOM   2316 O  O     . LYS   B 2 12  ? 159.942 125.939 97.298  1.00 75.51  ? 12  LYS   B O     1 
ATOM   2317 C  CB    . LYS   B 2 12  ? 161.550 128.500 97.672  1.00 69.29  ? 12  LYS   B CB    1 
ATOM   2318 C  CG    . LYS   B 2 12  ? 160.858 129.110 98.876  1.00 72.69  ? 12  LYS   B CG    1 
ATOM   2319 C  CD    . LYS   B 2 12  ? 161.777 130.072 99.608  1.00 75.17  ? 12  LYS   B CD    1 
ATOM   2320 C  CE    . LYS   B 2 12  ? 161.638 129.937 101.115 1.00 75.23  ? 12  LYS   B CE    1 
ATOM   2321 N  NZ    . LYS   B 2 12  ? 162.456 130.952 101.834 1.00 71.50  ? 12  LYS   B NZ    1 
ATOM   2322 N  N     . GLU   B 2 13  ? 160.695 125.700 99.417  1.00 80.60  ? 13  GLU   B N     1 
ATOM   2323 C  CA    . GLU   B 2 13  ? 159.562 124.924 99.897  1.00 78.77  ? 13  GLU   B CA    1 
ATOM   2324 C  C     . GLU   B 2 13  ? 158.855 125.668 101.018 1.00 79.61  ? 13  GLU   B C     1 
ATOM   2325 O  O     . GLU   B 2 13  ? 159.465 126.449 101.754 1.00 83.16  ? 13  GLU   B O     1 
ATOM   2326 C  CB    . GLU   B 2 13  ? 159.985 123.539 100.413 1.00 81.63  ? 13  GLU   B CB    1 
ATOM   2327 C  CG    . GLU   B 2 13  ? 160.080 122.466 99.351  1.00 84.52  ? 13  GLU   B CG    1 
ATOM   2328 C  CD    . GLU   B 2 13  ? 161.443 122.409 98.712  1.00 83.83  ? 13  GLU   B CD    1 
ATOM   2329 O  OE1   . GLU   B 2 13  ? 161.586 122.951 97.602  1.00 79.91  ? 13  GLU   B OE1   1 
ATOM   2330 O  OE2   . GLU   B 2 13  ? 162.367 121.825 99.316  1.00 86.29  ? 13  GLU   B OE2   1 
ATOM   2331 N  N     . TYR   B 2 14  ? 157.557 125.416 101.136 1.00 76.58  ? 14  TYR   B N     1 
ATOM   2332 C  CA    . TYR   B 2 14  ? 156.757 125.918 102.242 1.00 81.11  ? 14  TYR   B CA    1 
ATOM   2333 C  C     . TYR   B 2 14  ? 156.012 124.759 102.886 1.00 84.18  ? 14  TYR   B C     1 
ATOM   2334 O  O     . TYR   B 2 14  ? 155.499 123.875 102.194 1.00 82.96  ? 14  TYR   B O     1 
ATOM   2335 C  CB    . TYR   B 2 14  ? 155.769 126.995 101.781 1.00 82.25  ? 14  TYR   B CB    1 
ATOM   2336 C  CG    . TYR   B 2 14  ? 156.419 128.324 101.466 1.00 85.12  ? 14  TYR   B CG    1 
ATOM   2337 C  CD1   . TYR   B 2 14  ? 156.607 129.276 102.457 1.00 81.31  ? 14  TYR   B CD1   1 
ATOM   2338 C  CD2   . TYR   B 2 14  ? 156.839 128.629 100.178 1.00 83.42  ? 14  TYR   B CD2   1 
ATOM   2339 C  CE1   . TYR   B 2 14  ? 157.198 130.491 102.178 1.00 78.06  ? 14  TYR   B CE1   1 
ATOM   2340 C  CE2   . TYR   B 2 14  ? 157.431 129.844 99.890  1.00 79.87  ? 14  TYR   B CE2   1 
ATOM   2341 C  CZ    . TYR   B 2 14  ? 157.608 130.770 100.894 1.00 78.95  ? 14  TYR   B CZ    1 
ATOM   2342 O  OH    . TYR   B 2 14  ? 158.196 131.981 100.612 1.00 81.78  ? 14  TYR   B OH    1 
ATOM   2343 N  N     . ARG   B 2 15  ? 155.965 124.767 104.216 1.00 110.77 ? 15  ARG   B N     1 
ATOM   2344 C  CA    . ARG   B 2 15  ? 155.303 123.718 104.978 1.00 109.52 ? 15  ARG   B CA    1 
ATOM   2345 C  C     . ARG   B 2 15  ? 153.853 124.110 105.222 1.00 106.63 ? 15  ARG   B C     1 
ATOM   2346 O  O     . ARG   B 2 15  ? 153.575 125.188 105.757 1.00 105.81 ? 15  ARG   B O     1 
ATOM   2347 C  CB    . ARG   B 2 15  ? 156.022 123.482 106.306 1.00 110.52 ? 15  ARG   B CB    1 
ATOM   2348 C  CG    . ARG   B 2 15  ? 157.250 122.592 106.200 1.00 109.59 ? 15  ARG   B CG    1 
ATOM   2349 C  CD    . ARG   B 2 15  ? 156.893 121.126 106.381 1.00 110.96 ? 15  ARG   B CD    1 
ATOM   2350 N  NE    . ARG   B 2 15  ? 157.941 120.246 105.880 1.00 111.03 ? 15  ARG   B NE    1 
ATOM   2351 C  CZ    . ARG   B 2 15  ? 158.416 119.196 106.537 1.00 110.09 ? 15  ARG   B CZ    1 
ATOM   2352 N  NH1   . ARG   B 2 15  ? 157.956 118.863 107.732 1.00 108.87 ? 15  ARG   B NH1   1 
ATOM   2353 N  NH2   . ARG   B 2 15  ? 159.376 118.462 105.982 1.00 108.77 ? 15  ARG   B NH2   1 
ATOM   2354 N  N     . ILE   B 2 16  ? 152.933 123.233 104.832 1.00 96.51  ? 16  ILE   B N     1 
ATOM   2355 C  CA    . ILE   B 2 16  ? 151.504 123.509 104.894 1.00 98.51  ? 16  ILE   B CA    1 
ATOM   2356 C  C     . ILE   B 2 16  ? 150.891 122.629 105.973 1.00 99.71  ? 16  ILE   B C     1 
ATOM   2357 O  O     . ILE   B 2 16  ? 150.937 121.395 105.882 1.00 101.54 ? 16  ILE   B O     1 
ATOM   2358 C  CB    . ILE   B 2 16  ? 150.825 123.274 103.535 1.00 99.31  ? 16  ILE   B CB    1 
ATOM   2359 C  CG1   . ILE   B 2 16  ? 151.063 124.470 102.615 1.00 97.06  ? 16  ILE   B CG1   1 
ATOM   2360 C  CG2   . ILE   B 2 16  ? 149.331 123.037 103.709 1.00 97.58  ? 16  ILE   B CG2   1 
ATOM   2361 C  CD1   . ILE   B 2 16  ? 150.788 124.181 101.165 1.00 95.63  ? 16  ILE   B CD1   1 
ATOM   2362 N  N     . TYR   B 2 17  ? 150.331 123.263 107.000 1.00 98.09  ? 17  TYR   B N     1 
ATOM   2363 C  CA    . TYR   B 2 17  ? 149.534 122.584 108.010 1.00 99.15  ? 17  TYR   B CA    1 
ATOM   2364 C  C     . TYR   B 2 17  ? 148.115 123.126 107.946 1.00 99.37  ? 17  TYR   B C     1 
ATOM   2365 O  O     . TYR   B 2 17  ? 147.910 124.343 108.006 1.00 100.40 ? 17  TYR   B O     1 
ATOM   2366 C  CB    . TYR   B 2 17  ? 150.102 122.784 109.419 1.00 100.46 ? 17  TYR   B CB    1 
ATOM   2367 C  CG    . TYR   B 2 17  ? 151.592 123.028 109.486 1.00 99.65  ? 17  TYR   B CG    1 
ATOM   2368 C  CD1   . TYR   B 2 17  ? 152.496 121.991 109.306 1.00 98.92  ? 17  TYR   B CD1   1 
ATOM   2369 C  CD2   . TYR   B 2 17  ? 152.093 124.296 109.747 1.00 99.38  ? 17  TYR   B CD2   1 
ATOM   2370 C  CE1   . TYR   B 2 17  ? 153.858 122.213 109.375 1.00 98.31  ? 17  TYR   B CE1   1 
ATOM   2371 C  CE2   . TYR   B 2 17  ? 153.451 124.527 109.817 1.00 99.30  ? 17  TYR   B CE2   1 
ATOM   2372 C  CZ    . TYR   B 2 17  ? 154.330 123.483 109.631 1.00 98.92  ? 17  TYR   B CZ    1 
ATOM   2373 O  OH    . TYR   B 2 17  ? 155.684 123.715 109.702 1.00 99.41  ? 17  TYR   B OH    1 
ATOM   2374 N  N     A ARG   B 2 18  ? 147.141 122.221 107.822 0.34 100.28 ? 18  ARG   B N     1 
ATOM   2375 N  N     B ARG   B 2 18  ? 147.139 122.225 107.817 0.66 100.24 ? 18  ARG   B N     1 
ATOM   2376 C  CA    A ARG   B 2 18  ? 145.744 122.639 107.799 0.34 99.71  ? 18  ARG   B CA    1 
ATOM   2377 C  CA    B ARG   B 2 18  ? 145.746 122.657 107.799 0.66 99.72  ? 18  ARG   B CA    1 
ATOM   2378 C  C     A ARG   B 2 18  ? 145.313 123.222 109.138 0.34 100.72 ? 18  ARG   B C     1 
ATOM   2379 C  C     B ARG   B 2 18  ? 145.339 123.253 109.141 0.66 100.67 ? 18  ARG   B C     1 
ATOM   2380 O  O     A ARG   B 2 18  ? 144.505 124.156 109.176 0.34 101.14 ? 18  ARG   B O     1 
ATOM   2381 O  O     B ARG   B 2 18  ? 144.577 124.227 109.189 0.66 101.05 ? 18  ARG   B O     1 
ATOM   2382 C  CB    A ARG   B 2 18  ? 144.849 121.460 107.418 0.34 99.27  ? 18  ARG   B CB    1 
ATOM   2383 C  CB    B ARG   B 2 18  ? 144.834 121.488 107.427 0.66 99.30  ? 18  ARG   B CB    1 
ATOM   2384 C  CG    A ARG   B 2 18  ? 144.780 121.196 105.924 0.34 100.48 ? 18  ARG   B CG    1 
ATOM   2385 C  CG    B ARG   B 2 18  ? 143.356 121.845 107.395 0.66 99.01  ? 18  ARG   B CG    1 
ATOM   2386 C  CD    A ARG   B 2 18  ? 143.568 121.866 105.300 0.34 100.50 ? 18  ARG   B CD    1 
ATOM   2387 C  CD    B ARG   B 2 18  ? 142.695 121.389 106.105 0.66 100.80 ? 18  ARG   B CD    1 
ATOM   2388 N  NE    A ARG   B 2 18  ? 142.333 121.149 105.589 0.34 101.50 ? 18  ARG   B NE    1 
ATOM   2389 N  NE    B ARG   B 2 18  ? 143.599 121.467 104.964 0.66 100.35 ? 18  ARG   B NE    1 
ATOM   2390 C  CZ    A ARG   B 2 18  ? 141.425 121.543 106.471 0.34 99.70  ? 18  ARG   B CZ    1 
ATOM   2391 C  CZ    B ARG   B 2 18  ? 143.443 120.785 103.838 0.66 98.49  ? 18  ARG   B CZ    1 
ATOM   2392 N  NH1   A ARG   B 2 18  ? 141.589 122.644 107.186 0.34 98.30  ? 18  ARG   B NH1   1 
ATOM   2393 N  NH1   B ARG   B 2 18  ? 142.425 119.958 103.667 0.66 98.54  ? 18  ARG   B NH1   1 
ATOM   2394 N  NH2   A ARG   B 2 18  ? 140.326 120.814 106.642 0.34 98.51  ? 18  ARG   B NH2   1 
ATOM   2395 N  NH2   B ARG   B 2 18  ? 144.330 120.937 102.859 0.66 98.69  ? 18  ARG   B NH2   1 
ATOM   2396 N  N     . THR   B 2 19  ? 145.835 122.688 110.236 1.00 102.87 ? 19  THR   B N     1 
ATOM   2397 C  CA    . THR   B 2 19  ? 145.546 123.183 111.572 1.00 103.70 ? 19  THR   B CA    1 
ATOM   2398 C  C     . THR   B 2 19  ? 146.704 124.036 112.076 1.00 104.35 ? 19  THR   B C     1 
ATOM   2399 O  O     . THR   B 2 19  ? 147.875 123.723 111.850 1.00 102.94 ? 19  THR   B O     1 
ATOM   2400 C  CB    . THR   B 2 19  ? 145.290 122.028 112.543 1.00 104.04 ? 19  THR   B CB    1 
ATOM   2401 O  OG1   . THR   B 2 19  ? 146.539 121.534 113.043 1.00 101.85 ? 19  THR   B OG1   1 
ATOM   2402 C  CG2   . THR   B 2 19  ? 144.546 120.900 111.844 1.00 103.65 ? 19  THR   B CG2   1 
ATOM   2403 N  N     . ASN   B 2 20  ? 146.359 125.130 112.760 1.00 109.22 ? 20  ASN   B N     1 
ATOM   2404 C  CA    . ASN   B 2 20  ? 147.381 126.032 113.281 1.00 109.82 ? 20  ASN   B CA    1 
ATOM   2405 C  C     . ASN   B 2 20  ? 148.188 125.389 114.402 1.00 112.89 ? 20  ASN   B C     1 
ATOM   2406 O  O     . ASN   B 2 20  ? 149.320 125.809 114.668 1.00 110.66 ? 20  ASN   B O     1 
ATOM   2407 C  CB    . ASN   B 2 20  ? 146.733 127.327 113.771 1.00 108.38 ? 20  ASN   B CB    1 
ATOM   2408 C  CG    . ASN   B 2 20  ? 147.667 128.519 113.687 1.00 110.08 ? 20  ASN   B CG    1 
ATOM   2409 O  OD1   . ASN   B 2 20  ? 148.673 128.585 114.393 1.00 110.93 ? 20  ASN   B OD1   1 
ATOM   2410 N  ND2   . ASN   B 2 20  ? 147.335 129.471 112.823 1.00 108.97 ? 20  ASN   B ND2   1 
ATOM   2411 N  N     . LYS   B 2 21  ? 147.632 124.374 115.064 1.00 106.85 ? 21  LYS   B N     1 
ATOM   2412 C  CA    . LYS   B 2 21  ? 148.278 123.765 116.220 1.00 103.39 ? 21  LYS   B CA    1 
ATOM   2413 C  C     . LYS   B 2 21  ? 149.339 122.740 115.845 1.00 103.68 ? 21  LYS   B C     1 
ATOM   2414 O  O     . LYS   B 2 21  ? 150.043 122.252 116.735 1.00 104.25 ? 21  LYS   B O     1 
ATOM   2415 C  CB    . LYS   B 2 21  ? 147.239 123.100 117.135 1.00 101.86 ? 21  LYS   B CB    1 
ATOM   2416 C  CG    . LYS   B 2 21  ? 146.232 124.040 117.813 1.00 102.92 ? 21  LYS   B CG    1 
ATOM   2417 C  CD    . LYS   B 2 21  ? 145.188 124.604 116.857 1.00 104.04 ? 21  LYS   B CD    1 
ATOM   2418 C  CE    . LYS   B 2 21  ? 143.957 123.716 116.801 1.00 103.37 ? 21  LYS   B CE    1 
ATOM   2419 N  NZ    . LYS   B 2 21  ? 143.196 123.900 115.536 1.00 100.57 ? 21  LYS   B NZ    1 
ATOM   2420 N  N     . GLU   B 2 22  ? 149.474 122.401 114.564 1.00 114.69 ? 22  GLU   B N     1 
ATOM   2421 C  CA    . GLU   B 2 22  ? 150.454 121.413 114.133 1.00 114.32 ? 22  GLU   B CA    1 
ATOM   2422 C  C     . GLU   B 2 22  ? 151.841 122.003 113.917 1.00 116.50 ? 22  GLU   B C     1 
ATOM   2423 O  O     . GLU   B 2 22  ? 152.764 121.257 113.569 1.00 115.34 ? 22  GLU   B O     1 
ATOM   2424 C  CB    . GLU   B 2 22  ? 149.982 120.731 112.846 1.00 114.24 ? 22  GLU   B CB    1 
ATOM   2425 C  CG    . GLU   B 2 22  ? 149.179 119.463 113.075 1.00 115.73 ? 22  GLU   B CG    1 
ATOM   2426 C  CD    . GLU   B 2 22  ? 148.305 119.104 111.889 1.00 117.77 ? 22  GLU   B CD    1 
ATOM   2427 O  OE1   . GLU   B 2 22  ? 148.809 119.135 110.747 1.00 116.56 ? 22  GLU   B OE1   1 
ATOM   2428 O  OE2   . GLU   B 2 22  ? 147.115 118.791 112.100 1.00 116.90 ? 22  GLU   B OE2   1 
ATOM   2429 N  N     . ARG   B 2 23  ? 152.010 123.314 114.106 1.00 125.70 ? 23  ARG   B N     1 
ATOM   2430 C  CA    . ARG   B 2 23  ? 153.312 123.936 113.885 1.00 125.66 ? 23  ARG   B CA    1 
ATOM   2431 C  C     . ARG   B 2 23  ? 154.352 123.429 114.877 1.00 126.27 ? 23  ARG   B C     1 
ATOM   2432 O  O     . ARG   B 2 23  ? 155.504 123.181 114.503 1.00 124.95 ? 23  ARG   B O     1 
ATOM   2433 C  CB    . ARG   B 2 23  ? 153.186 125.456 113.969 1.00 124.83 ? 23  ARG   B CB    1 
ATOM   2434 C  CG    . ARG   B 2 23  ? 152.370 126.069 112.844 1.00 124.78 ? 23  ARG   B CG    1 
ATOM   2435 C  CD    . ARG   B 2 23  ? 152.314 127.583 112.955 1.00 124.77 ? 23  ARG   B CD    1 
ATOM   2436 N  NE    . ARG   B 2 23  ? 151.492 128.172 111.904 1.00 126.00 ? 23  ARG   B NE    1 
ATOM   2437 C  CZ    . ARG   B 2 23  ? 151.174 129.457 111.833 1.00 126.34 ? 23  ARG   B CZ    1 
ATOM   2438 N  NH1   . ARG   B 2 23  ? 151.595 130.324 112.739 1.00 126.67 ? 23  ARG   B NH1   1 
ATOM   2439 N  NH2   . ARG   B 2 23  ? 150.416 129.882 110.827 1.00 124.50 ? 23  ARG   B NH2   1 
ATOM   2440 N  N     . MET   B 2 24  ? 153.968 123.269 116.143 1.00 120.16 ? 24  MET   B N     1 
ATOM   2441 C  CA    . MET   B 2 24  ? 154.908 122.860 117.179 1.00 118.85 ? 24  MET   B CA    1 
ATOM   2442 C  C     . MET   B 2 24  ? 155.331 121.402 117.071 1.00 119.29 ? 24  MET   B C     1 
ATOM   2443 O  O     . MET   B 2 24  ? 156.355 121.032 117.654 1.00 118.51 ? 24  MET   B O     1 
ATOM   2444 C  CB    . MET   B 2 24  ? 154.305 123.109 118.564 1.00 118.88 ? 24  MET   B CB    1 
ATOM   2445 C  CG    . MET   B 2 24  ? 155.310 123.578 119.605 1.00 120.39 ? 24  MET   B CG    1 
ATOM   2446 S  SD    . MET   B 2 24  ? 154.554 124.550 120.922 1.00 123.10 ? 24  MET   B SD    1 
ATOM   2447 C  CE    . MET   B 2 24  ? 156.004 125.064 121.837 1.00 118.82 ? 24  MET   B CE    1 
ATOM   2448 N  N     . LYS   B 2 25  ? 154.578 120.570 116.348 1.00 117.90 ? 25  LYS   B N     1 
ATOM   2449 C  CA    . LYS   B 2 25  ? 154.892 119.144 116.295 1.00 118.73 ? 25  LYS   B CA    1 
ATOM   2450 C  C     . LYS   B 2 25  ? 156.245 118.891 115.639 1.00 118.95 ? 25  LYS   B C     1 
ATOM   2451 O  O     . LYS   B 2 25  ? 157.018 118.047 116.106 1.00 119.34 ? 25  LYS   B O     1 
ATOM   2452 C  CB    . LYS   B 2 25  ? 153.788 118.391 115.553 1.00 116.90 ? 25  LYS   B CB    1 
ATOM   2453 C  CG    . LYS   B 2 25  ? 152.791 117.693 116.463 1.00 117.33 ? 25  LYS   B CG    1 
ATOM   2454 C  CD    . LYS   B 2 25  ? 152.048 118.691 117.336 1.00 117.92 ? 25  LYS   B CD    1 
ATOM   2455 C  CE    . LYS   B 2 25  ? 150.544 118.496 117.244 1.00 117.69 ? 25  LYS   B CE    1 
ATOM   2456 N  NZ    . LYS   B 2 25  ? 149.809 119.472 118.094 1.00 116.64 ? 25  LYS   B NZ    1 
ATOM   2457 N  N     . ASP   B 2 26  ? 156.549 119.608 114.561 1.00 123.23 ? 26  ASP   B N     1 
ATOM   2458 C  CA    . ASP   B 2 26  ? 157.785 119.407 113.815 1.00 123.98 ? 26  ASP   B CA    1 
ATOM   2459 C  C     . ASP   B 2 26  ? 158.924 120.298 114.292 1.00 123.37 ? 26  ASP   B C     1 
ATOM   2460 O  O     . ASP   B 2 26  ? 160.020 120.232 113.725 1.00 121.56 ? 26  ASP   B O     1 
ATOM   2461 C  CB    . ASP   B 2 26  ? 157.542 119.646 112.322 1.00 123.27 ? 26  ASP   B CB    1 
ATOM   2462 C  CG    . ASP   B 2 26  ? 156.082 119.900 112.003 1.00 122.94 ? 26  ASP   B CG    1 
ATOM   2463 O  OD1   . ASP   B 2 26  ? 155.523 120.891 112.519 1.00 120.35 ? 26  ASP   B OD1   1 
ATOM   2464 O  OD2   . ASP   B 2 26  ? 155.494 119.109 111.236 1.00 124.01 ? 26  ASP   B OD2   1 
ATOM   2465 N  N     . ALA   B 2 27  ? 158.699 121.123 115.315 1.00 110.90 ? 27  ALA   B N     1 
ATOM   2466 C  CA    . ALA   B 2 27  ? 159.717 122.052 115.786 1.00 109.74 ? 27  ALA   B CA    1 
ATOM   2467 C  C     . ALA   B 2 27  ? 160.482 121.553 117.004 1.00 109.48 ? 27  ALA   B C     1 
ATOM   2468 O  O     . ALA   B 2 27  ? 161.624 121.977 117.210 1.00 108.04 ? 27  ALA   B O     1 
ATOM   2469 C  CB    . ALA   B 2 27  ? 159.085 123.410 116.116 1.00 108.75 ? 27  ALA   B CB    1 
ATOM   2470 N  N     . LEU   B 2 28  ? 159.891 120.672 117.810 1.00 112.19 ? 28  LEU   B N     1 
ATOM   2471 C  CA    . LEU   B 2 28  ? 160.541 120.175 119.017 1.00 112.92 ? 28  LEU   B CA    1 
ATOM   2472 C  C     . LEU   B 2 28  ? 161.227 118.827 118.830 1.00 112.79 ? 28  LEU   B C     1 
ATOM   2473 O  O     . LEU   B 2 28  ? 162.256 118.575 119.465 1.00 110.67 ? 28  LEU   B O     1 
ATOM   2474 C  CB    . LEU   B 2 28  ? 159.531 120.112 120.173 1.00 112.03 ? 28  LEU   B CB    1 
ATOM   2475 C  CG    . LEU   B 2 28  ? 158.077 119.649 119.987 1.00 113.27 ? 28  LEU   B CG    1 
ATOM   2476 C  CD1   . LEU   B 2 28  ? 157.931 118.224 119.475 1.00 110.59 ? 28  LEU   B CD1   1 
ATOM   2477 C  CD2   . LEU   B 2 28  ? 157.300 119.830 121.286 1.00 111.85 ? 28  LEU   B CD2   1 
ATOM   2478 N  N     . ILE   B 2 29  ? 160.698 117.955 117.976 1.00 116.79 ? 29  ILE   B N     1 
ATOM   2479 C  CA    . ILE   B 2 29  ? 161.357 116.689 117.658 1.00 117.62 ? 29  ILE   B CA    1 
ATOM   2480 C  C     . ILE   B 2 29  ? 161.417 116.558 116.139 1.00 117.18 ? 29  ILE   B C     1 
ATOM   2481 O  O     . ILE   B 2 29  ? 160.385 116.686 115.466 1.00 116.22 ? 29  ILE   B O     1 
ATOM   2482 C  CB    . ILE   B 2 29  ? 160.637 115.492 118.301 1.00 117.96 ? 29  ILE   B CB    1 
ATOM   2483 C  CG1   . ILE   B 2 29  ? 160.438 115.716 119.802 1.00 116.94 ? 29  ILE   B CG1   1 
ATOM   2484 C  CG2   . ILE   B 2 29  ? 161.447 114.228 118.103 1.00 116.80 ? 29  ILE   B CG2   1 
ATOM   2485 C  CD1   . ILE   B 2 29  ? 161.707 115.585 120.620 1.00 115.15 ? 29  ILE   B CD1   1 
ATOM   2486 N  N     . PRO   B 2 30  ? 162.594 116.305 115.559 1.00 120.44 ? 30  PRO   B N     1 
ATOM   2487 C  CA    . PRO   B 2 30  ? 162.740 116.417 114.099 1.00 119.67 ? 30  PRO   B CA    1 
ATOM   2488 C  C     . PRO   B 2 30  ? 162.297 115.196 113.304 1.00 118.35 ? 30  PRO   B C     1 
ATOM   2489 O  O     . PRO   B 2 30  ? 162.641 115.086 112.123 1.00 115.27 ? 30  PRO   B O     1 
ATOM   2490 C  CB    . PRO   B 2 30  ? 164.249 116.657 113.920 1.00 117.24 ? 30  PRO   B CB    1 
ATOM   2491 C  CG    . PRO   B 2 30  ? 164.783 116.958 115.306 1.00 116.76 ? 30  PRO   B CG    1 
ATOM   2492 C  CD    . PRO   B 2 30  ? 163.898 116.188 116.225 1.00 117.32 ? 30  PRO   B CD    1 
ATOM   2493 N  N     . LYS   B 2 31  ? 161.546 114.272 113.909 1.00 122.71 ? 31  LYS   B N     1 
ATOM   2494 C  CA    . LYS   B 2 31  ? 161.138 113.081 113.171 1.00 123.20 ? 31  LYS   B CA    1 
ATOM   2495 C  C     . LYS   B 2 31  ? 159.931 113.322 112.273 1.00 124.98 ? 31  LYS   B C     1 
ATOM   2496 O  O     . LYS   B 2 31  ? 159.638 112.480 111.417 1.00 122.97 ? 31  LYS   B O     1 
ATOM   2497 C  CB    . LYS   B 2 31  ? 160.829 111.926 114.129 1.00 122.46 ? 31  LYS   B CB    1 
ATOM   2498 C  CG    . LYS   B 2 31  ? 160.234 112.334 115.466 1.00 121.55 ? 31  LYS   B CG    1 
ATOM   2499 C  CD    . LYS   B 2 31  ? 158.768 112.728 115.344 1.00 122.09 ? 31  LYS   B CD    1 
ATOM   2500 C  CE    . LYS   B 2 31  ? 158.195 113.154 116.685 1.00 122.11 ? 31  LYS   B CE    1 
ATOM   2501 N  NZ    . LYS   B 2 31  ? 156.817 113.701 116.552 1.00 122.05 ? 31  LYS   B NZ    1 
ATOM   2502 N  N     . HIS   B 2 32  ? 159.229 114.438 112.444 1.00 124.45 ? 32  HIS   B N     1 
ATOM   2503 C  CA    . HIS   B 2 32  ? 158.011 114.688 111.686 1.00 122.72 ? 32  HIS   B CA    1 
ATOM   2504 C  C     . HIS   B 2 32  ? 158.330 115.259 110.311 1.00 122.93 ? 32  HIS   B C     1 
ATOM   2505 O  O     . HIS   B 2 32  ? 159.209 116.113 110.163 1.00 121.71 ? 32  HIS   B O     1 
ATOM   2506 C  CB    . HIS   B 2 32  ? 157.094 115.644 112.448 1.00 122.40 ? 32  HIS   B CB    1 
ATOM   2507 C  CG    . HIS   B 2 32  ? 155.646 115.493 112.102 1.00 125.20 ? 32  HIS   B CG    1 
ATOM   2508 N  ND1   . HIS   B 2 32  ? 155.166 114.443 111.350 1.00 124.42 ? 32  HIS   B ND1   1 
ATOM   2509 C  CD2   . HIS   B 2 32  ? 154.571 116.260 112.406 1.00 123.68 ? 32  HIS   B CD2   1 
ATOM   2510 C  CE1   . HIS   B 2 32  ? 153.859 114.568 111.205 1.00 122.67 ? 32  HIS   B CE1   1 
ATOM   2511 N  NE2   . HIS   B 2 32  ? 153.473 115.662 111.837 1.00 122.15 ? 32  HIS   B NE2   1 
ATOM   2512 N  N     . LYS   B 2 33  ? 157.606 114.776 109.302 1.00 112.55 ? 33  LYS   B N     1 
ATOM   2513 C  CA    . LYS   B 2 33  ? 157.732 115.265 107.931 1.00 110.68 ? 33  LYS   B CA    1 
ATOM   2514 C  C     . LYS   B 2 33  ? 156.328 115.405 107.360 1.00 110.11 ? 33  LYS   B C     1 
ATOM   2515 O  O     . LYS   B 2 33  ? 155.637 114.401 107.156 1.00 108.18 ? 33  LYS   B O     1 
ATOM   2516 C  CB    . LYS   B 2 33  ? 158.581 114.322 107.078 1.00 108.35 ? 33  LYS   B CB    1 
ATOM   2517 C  CG    . LYS   B 2 33  ? 158.588 112.882 107.563 1.00 107.74 ? 33  LYS   B CG    1 
ATOM   2518 C  CD    . LYS   B 2 33  ? 158.294 111.913 106.428 1.00 108.83 ? 33  LYS   B CD    1 
ATOM   2519 C  CE    . LYS   B 2 33  ? 159.256 112.112 105.268 1.00 107.91 ? 33  LYS   B CE    1 
ATOM   2520 N  NZ    . LYS   B 2 33  ? 159.488 110.849 104.516 1.00 105.65 ? 33  LYS   B NZ    1 
ATOM   2521 N  N     . ASN   B 2 34  ? 155.909 116.640 107.102 1.00 109.48 ? 34  ASN   B N     1 
ATOM   2522 C  CA    . ASN   B 2 34  ? 154.554 116.937 106.671 1.00 111.13 ? 34  ASN   B CA    1 
ATOM   2523 C  C     . ASN   B 2 34  ? 154.514 117.198 105.165 1.00 111.23 ? 34  ASN   B C     1 
ATOM   2524 O  O     . ASN   B 2 34  ? 155.508 117.032 104.452 1.00 109.00 ? 34  ASN   B O     1 
ATOM   2525 C  CB    . ASN   B 2 34  ? 154.011 118.129 107.462 1.00 109.43 ? 34  ASN   B CB    1 
ATOM   2526 C  CG    . ASN   B 2 34  ? 152.546 117.974 107.817 1.00 109.43 ? 34  ASN   B CG    1 
ATOM   2527 O  OD1   . ASN   B 2 34  ? 151.807 117.249 107.151 1.00 107.80 ? 34  ASN   B OD1   1 
ATOM   2528 N  ND2   . ASN   B 2 34  ? 152.118 118.660 108.869 1.00 108.61 ? 34  ASN   B ND2   1 
ATOM   2529 N  N     . LYS   B 2 35  ? 153.345 117.604 104.674 1.00 106.83 ? 35  LYS   B N     1 
ATOM   2530 C  CA    . LYS   B 2 35  ? 153.200 117.980 103.275 1.00 103.04 ? 35  LYS   B CA    1 
ATOM   2531 C  C     . LYS   B 2 35  ? 153.936 119.284 103.000 1.00 100.78 ? 35  LYS   B C     1 
ATOM   2532 O  O     . LYS   B 2 35  ? 153.996 120.173 103.853 1.00 100.52 ? 35  LYS   B O     1 
ATOM   2533 C  CB    . LYS   B 2 35  ? 151.722 118.128 102.916 1.00 100.45 ? 35  LYS   B CB    1 
ATOM   2534 C  CG    . LYS   B 2 35  ? 151.367 117.662 101.516 1.00 100.21 ? 35  LYS   B CG    1 
ATOM   2535 C  CD    . LYS   B 2 35  ? 149.865 117.697 101.285 1.00 100.55 ? 35  LYS   B CD    1 
ATOM   2536 C  CE    . LYS   B 2 35  ? 149.249 118.974 101.832 1.00 101.37 ? 35  LYS   B CE    1 
ATOM   2537 N  NZ    . LYS   B 2 35  ? 147.818 119.111 101.446 1.00 100.31 ? 35  LYS   B NZ    1 
ATOM   2538 N  N     . THR   B 2 36  ? 154.497 119.398 101.800 1.00 102.24 ? 36  THR   B N     1 
ATOM   2539 C  CA    . THR   B 2 36  ? 155.258 120.568 101.405 1.00 103.52 ? 36  THR   B CA    1 
ATOM   2540 C  C     . THR   B 2 36  ? 154.836 121.014 100.010 1.00 104.94 ? 36  THR   B C     1 
ATOM   2541 O  O     . THR   B 2 36  ? 154.373 120.221 99.178  1.00 103.41 ? 36  THR   B O     1 
ATOM   2542 C  CB    . THR   B 2 36  ? 156.773 120.299 101.452 1.00 102.42 ? 36  THR   B CB    1 
ATOM   2543 O  OG1   . THR   B 2 36  ? 157.484 121.543 101.458 1.00 99.79  ? 36  THR   B OG1   1 
ATOM   2544 C  CG2   . THR   B 2 36  ? 157.217 119.468 100.261 1.00 101.81 ? 36  THR   B CG2   1 
ATOM   2545 N  N     . PHE   B 2 37  ? 154.990 122.318 99.783  1.00 88.85  ? 37  PHE   B N     1 
ATOM   2546 C  CA    . PHE   B 2 37  ? 154.611 122.977 98.543  1.00 80.95  ? 37  PHE   B CA    1 
ATOM   2547 C  C     . PHE   B 2 37  ? 155.848 123.628 97.945  1.00 79.10  ? 37  PHE   B C     1 
ATOM   2548 O  O     . PHE   B 2 37  ? 156.528 124.407 98.620  1.00 79.03  ? 37  PHE   B O     1 
ATOM   2549 C  CB    . PHE   B 2 37  ? 153.521 124.021 98.803  1.00 78.99  ? 37  PHE   B CB    1 
ATOM   2550 C  CG    . PHE   B 2 37  ? 153.224 124.904 97.629  1.00 81.63  ? 37  PHE   B CG    1 
ATOM   2551 C  CD1   . PHE   B 2 37  ? 152.487 124.432 96.559  1.00 79.74  ? 37  PHE   B CD1   1 
ATOM   2552 C  CD2   . PHE   B 2 37  ? 153.673 126.213 97.601  1.00 79.69  ? 37  PHE   B CD2   1 
ATOM   2553 C  CE1   . PHE   B 2 37  ? 152.208 125.245 95.483  1.00 77.76  ? 37  PHE   B CE1   1 
ATOM   2554 C  CE2   . PHE   B 2 37  ? 153.399 127.030 96.525  1.00 74.90  ? 37  PHE   B CE2   1 
ATOM   2555 C  CZ    . PHE   B 2 37  ? 152.666 126.544 95.464  1.00 76.96  ? 37  PHE   B CZ    1 
ATOM   2556 N  N     . PHE   B 2 38  ? 156.137 123.308 96.686  1.00 75.15  ? 38  PHE   B N     1 
ATOM   2557 C  CA    . PHE   B 2 38  ? 157.332 123.804 96.005  1.00 72.90  ? 38  PHE   B CA    1 
ATOM   2558 C  C     . PHE   B 2 38  ? 156.999 125.135 95.345  1.00 75.12  ? 38  PHE   B C     1 
ATOM   2559 O  O     . PHE   B 2 38  ? 156.463 125.187 94.238  1.00 77.67  ? 38  PHE   B O     1 
ATOM   2560 C  CB    . PHE   B 2 38  ? 157.830 122.787 94.985  1.00 74.35  ? 38  PHE   B CB    1 
ATOM   2561 C  CG    . PHE   B 2 38  ? 158.633 121.668 95.581  1.00 77.18  ? 38  PHE   B CG    1 
ATOM   2562 C  CD1   . PHE   B 2 38  ? 158.039 120.737 96.416  1.00 79.55  ? 38  PHE   B CD1   1 
ATOM   2563 C  CD2   . PHE   B 2 38  ? 159.981 121.541 95.299  1.00 78.62  ? 38  PHE   B CD2   1 
ATOM   2564 C  CE1   . PHE   B 2 38  ? 158.778 119.706 96.962  1.00 79.59  ? 38  PHE   B CE1   1 
ATOM   2565 C  CE2   . PHE   B 2 38  ? 160.724 120.510 95.842  1.00 79.16  ? 38  PHE   B CE2   1 
ATOM   2566 C  CZ    . PHE   B 2 38  ? 160.121 119.592 96.675  1.00 79.88  ? 38  PHE   B CZ    1 
ATOM   2567 N  N     . ALA   B 2 39  ? 157.321 126.233 96.035  1.00 63.06  ? 39  ALA   B N     1 
ATOM   2568 C  CA    . ALA   B 2 39  ? 157.103 127.547 95.440  1.00 59.26  ? 39  ALA   B CA    1 
ATOM   2569 C  C     . ALA   B 2 39  ? 158.026 127.772 94.251  1.00 62.71  ? 39  ALA   B C     1 
ATOM   2570 O  O     . ALA   B 2 39  ? 157.614 128.364 93.247  1.00 65.07  ? 39  ALA   B O     1 
ATOM   2571 C  CB    . ALA   B 2 39  ? 157.301 128.642 96.486  1.00 61.21  ? 39  ALA   B CB    1 
ATOM   2572 N  N     . LEU   B 2 40  ? 159.270 127.309 94.349  1.00 70.96  ? 40  LEU   B N     1 
ATOM   2573 C  CA    . LEU   B 2 40  ? 160.216 127.302 93.245  1.00 70.47  ? 40  LEU   B CA    1 
ATOM   2574 C  C     . LEU   B 2 40  ? 160.913 125.949 93.219  1.00 66.53  ? 40  LEU   B C     1 
ATOM   2575 O  O     . LEU   B 2 40  ? 160.983 125.249 94.231  1.00 74.00  ? 40  LEU   B O     1 
ATOM   2576 C  CB    . LEU   B 2 40  ? 161.250 128.429 93.369  1.00 71.82  ? 40  LEU   B CB    1 
ATOM   2577 C  CG    . LEU   B 2 40  ? 160.742 129.860 93.194  1.00 67.98  ? 40  LEU   B CG    1 
ATOM   2578 C  CD1   . LEU   B 2 40  ? 161.770 130.851 93.708  1.00 66.19  ? 40  LEU   B CD1   1 
ATOM   2579 C  CD2   . LEU   B 2 40  ? 160.412 130.136 91.738  1.00 67.93  ? 40  LEU   B CD2   1 
ATOM   2580 N  N     . ASP   B 2 41  ? 161.423 125.578 92.047  1.00 80.21  ? 41  ASP   B N     1 
ATOM   2581 C  CA    . ASP   B 2 41  ? 162.083 124.282 91.905  1.00 81.67  ? 41  ASP   B CA    1 
ATOM   2582 C  C     . ASP   B 2 41  ? 163.076 124.354 90.755  1.00 86.50  ? 41  ASP   B C     1 
ATOM   2583 O  O     . ASP   B 2 41  ? 162.668 124.415 89.591  1.00 88.07  ? 41  ASP   B O     1 
ATOM   2584 C  CB    . ASP   B 2 41  ? 161.062 123.175 91.677  1.00 82.45  ? 41  ASP   B CB    1 
ATOM   2585 C  CG    . ASP   B 2 41  ? 161.712 121.823 91.473  1.00 88.14  ? 41  ASP   B CG    1 
ATOM   2586 O  OD1   . ASP   B 2 41  ? 162.558 121.436 92.306  1.00 87.27  ? 41  ASP   B OD1   1 
ATOM   2587 O  OD2   . ASP   B 2 41  ? 161.385 121.149 90.474  1.00 89.59  ? 41  ASP   B OD2   1 
ATOM   2588 N  N     . ASP   B 2 42  ? 164.370 124.344 91.085  1.00 85.37  ? 42  ASP   B N     1 
ATOM   2589 C  CA    . ASP   B 2 42  ? 165.459 124.269 90.110  1.00 88.31  ? 42  ASP   B CA    1 
ATOM   2590 C  C     . ASP   B 2 42  ? 165.392 125.426 89.107  1.00 89.62  ? 42  ASP   B C     1 
ATOM   2591 O  O     . ASP   B 2 42  ? 165.182 125.242 87.907  1.00 89.11  ? 42  ASP   B O     1 
ATOM   2592 C  CB    . ASP   B 2 42  ? 165.447 122.912 89.396  1.00 89.08  ? 42  ASP   B CB    1 
ATOM   2593 C  CG    . ASP   B 2 42  ? 166.832 122.454 88.990  1.00 89.16  ? 42  ASP   B CG    1 
ATOM   2594 O  OD1   . ASP   B 2 42  ? 167.383 123.012 88.017  1.00 89.28  ? 42  ASP   B OD1   1 
ATOM   2595 O  OD2   . ASP   B 2 42  ? 167.374 121.541 89.647  1.00 88.21  ? 42  ASP   B OD2   1 
ATOM   2596 N  N     . ILE   B 2 43  ? 165.582 126.633 89.635  1.00 85.41  ? 43  ILE   B N     1 
ATOM   2597 C  CA    . ILE   B 2 43  ? 165.627 127.851 88.830  1.00 87.40  ? 43  ILE   B CA    1 
ATOM   2598 C  C     . ILE   B 2 43  ? 167.078 128.273 88.650  1.00 84.23  ? 43  ILE   B C     1 
ATOM   2599 O  O     . ILE   B 2 43  ? 167.811 128.446 89.630  1.00 85.71  ? 43  ILE   B O     1 
ATOM   2600 C  CB    . ILE   B 2 43  ? 164.804 128.980 89.473  1.00 86.05  ? 43  ILE   B CB    1 
ATOM   2601 C  CG1   . ILE   B 2 43  ? 163.372 128.522 89.756  1.00 79.84  ? 43  ILE   B CG1   1 
ATOM   2602 C  CG2   . ILE   B 2 43  ? 164.825 130.216 88.598  1.00 83.27  ? 43  ILE   B CG2   1 
ATOM   2603 C  CD1   . ILE   B 2 43  ? 162.448 128.664 88.572  1.00 83.17  ? 43  ILE   B CD1   1 
ATOM   2604 N  N     . SER   B 2 44  ? 167.494 128.442 87.399  1.00 90.61  ? 44  SER   B N     1 
ATOM   2605 C  CA    . SER   B 2 44  ? 168.844 128.889 87.082  1.00 93.08  ? 44  SER   B CA    1 
ATOM   2606 C  C     . SER   B 2 44  ? 168.738 130.146 86.236  1.00 96.75  ? 44  SER   B C     1 
ATOM   2607 O  O     . SER   B 2 44  ? 168.048 130.148 85.212  1.00 95.64  ? 44  SER   B O     1 
ATOM   2608 C  CB    . SER   B 2 44  ? 169.635 127.797 86.356  1.00 93.20  ? 44  SER   B CB    1 
ATOM   2609 O  OG    . SER   B 2 44  ? 169.374 127.795 84.962  1.00 92.78  ? 44  SER   B OG    1 
ATOM   2610 N  N     . LEU   B 2 45  ? 169.414 131.209 86.665  1.00 93.64  ? 45  LEU   B N     1 
ATOM   2611 C  CA    . LEU   B 2 45  ? 169.246 132.530 86.083  1.00 90.16  ? 45  LEU   B CA    1 
ATOM   2612 C  C     . LEU   B 2 45  ? 170.608 133.189 85.930  1.00 86.54  ? 45  LEU   B C     1 
ATOM   2613 O  O     . LEU   B 2 45  ? 171.483 133.035 86.783  1.00 87.49  ? 45  LEU   B O     1 
ATOM   2614 C  CB    . LEU   B 2 45  ? 168.333 133.400 86.964  1.00 91.66  ? 45  LEU   B CB    1 
ATOM   2615 C  CG    . LEU   B 2 45  ? 167.585 134.622 86.422  1.00 91.52  ? 45  LEU   B CG    1 
ATOM   2616 C  CD1   . LEU   B 2 45  ? 166.929 134.310 85.096  1.00 87.40  ? 45  LEU   B CD1   1 
ATOM   2617 C  CD2   . LEU   B 2 45  ? 166.561 135.136 87.444  1.00 90.66  ? 45  LEU   B CD2   1 
ATOM   2618 N  N     . LYS   B 2 46  ? 170.780 133.923 84.838  1.00 96.30  ? 46  LYS   B N     1 
ATOM   2619 C  CA    . LYS   B 2 46  ? 171.997 134.677 84.569  1.00 96.76  ? 46  LYS   B CA    1 
ATOM   2620 C  C     . LYS   B 2 46  ? 171.595 136.031 84.007  1.00 101.35 ? 46  LYS   B C     1 
ATOM   2621 O  O     . LYS   B 2 46  ? 171.184 136.125 82.846  1.00 102.45 ? 46  LYS   B O     1 
ATOM   2622 C  CB    . LYS   B 2 46  ? 172.892 133.927 83.591  1.00 97.03  ? 46  LYS   B CB    1 
ATOM   2623 C  CG    . LYS   B 2 46  ? 174.367 134.088 83.854  1.00 101.04 ? 46  LYS   B CG    1 
ATOM   2624 C  CD    . LYS   B 2 46  ? 175.139 132.960 83.203  1.00 100.14 ? 46  LYS   B CD    1 
ATOM   2625 C  CE    . LYS   B 2 46  ? 174.692 131.601 83.719  1.00 96.57  ? 46  LYS   B CE    1 
ATOM   2626 N  NZ    . LYS   B 2 46  ? 174.609 131.595 85.204  1.00 98.43  ? 46  LYS   B NZ    1 
ATOM   2627 N  N     . ALA   B 2 47  ? 171.706 137.075 84.819  1.00 94.88  ? 47  ALA   B N     1 
ATOM   2628 C  CA    . ALA   B 2 47  ? 171.376 138.427 84.399  1.00 93.53  ? 47  ALA   B CA    1 
ATOM   2629 C  C     . ALA   B 2 47  ? 172.661 139.223 84.230  1.00 94.37  ? 47  ALA   B C     1 
ATOM   2630 O  O     . ALA   B 2 47  ? 173.409 139.414 85.197  1.00 95.88  ? 47  ALA   B O     1 
ATOM   2631 C  CB    . ALA   B 2 47  ? 170.454 139.105 85.412  1.00 94.43  ? 47  ALA   B CB    1 
ATOM   2632 N  N     . TYR   B 2 48  ? 172.906 139.688 83.009  1.00 105.52 ? 48  TYR   B N     1 
ATOM   2633 C  CA    . TYR   B 2 48  ? 174.107 140.428 82.663  1.00 108.10 ? 48  TYR   B CA    1 
ATOM   2634 C  C     . TYR   B 2 48  ? 173.914 141.916 82.959  1.00 105.24 ? 48  TYR   B C     1 
ATOM   2635 O  O     . TYR   B 2 48  ? 172.953 142.330 83.614  1.00 106.33 ? 48  TYR   B O     1 
ATOM   2636 C  CB    . TYR   B 2 48  ? 174.466 140.189 81.194  1.00 106.73 ? 48  TYR   B CB    1 
ATOM   2637 C  CG    . TYR   B 2 48  ? 174.994 138.802 80.896  1.00 107.62 ? 48  TYR   B CG    1 
ATOM   2638 C  CD1   . TYR   B 2 48  ? 176.292 138.440 81.235  1.00 107.52 ? 48  TYR   B CD1   1 
ATOM   2639 C  CD2   . TYR   B 2 48  ? 174.196 137.858 80.265  1.00 108.81 ? 48  TYR   B CD2   1 
ATOM   2640 C  CE1   . TYR   B 2 48  ? 176.775 137.175 80.962  1.00 109.37 ? 48  TYR   B CE1   1 
ATOM   2641 C  CE2   . TYR   B 2 48  ? 174.671 136.592 79.988  1.00 108.61 ? 48  TYR   B CE2   1 
ATOM   2642 C  CZ    . TYR   B 2 48  ? 175.961 136.257 80.338  1.00 110.23 ? 48  TYR   B CZ    1 
ATOM   2643 O  OH    . TYR   B 2 48  ? 176.447 135.000 80.068  1.00 108.92 ? 48  TYR   B OH    1 
ATOM   2644 N  N     . GLU   B 2 49  ? 174.844 142.733 82.478  1.00 102.39 ? 49  GLU   B N     1 
ATOM   2645 C  CA    . GLU   B 2 49  ? 174.804 144.174 82.670  1.00 105.51 ? 49  GLU   B CA    1 
ATOM   2646 C  C     . GLU   B 2 49  ? 174.094 144.845 81.501  1.00 106.74 ? 49  GLU   B C     1 
ATOM   2647 O  O     . GLU   B 2 49  ? 174.208 144.415 80.351  1.00 105.80 ? 49  GLU   B O     1 
ATOM   2648 C  CB    . GLU   B 2 49  ? 176.216 144.743 82.815  1.00 107.71 ? 49  GLU   B CB    1 
ATOM   2649 C  CG    . GLU   B 2 49  ? 176.286 146.047 83.589  1.00 108.59 ? 49  GLU   B CG    1 
ATOM   2650 C  CD    . GLU   B 2 49  ? 176.511 145.837 85.073  1.00 109.69 ? 49  GLU   B CD    1 
ATOM   2651 O  OE1   . GLU   B 2 49  ? 175.594 145.324 85.748  1.00 107.39 ? 49  GLU   B OE1   1 
ATOM   2652 O  OE2   . GLU   B 2 49  ? 177.607 146.183 85.563  1.00 108.57 ? 49  GLU   B OE2   1 
ATOM   2653 N  N     . GLY   B 2 50  ? 173.363 145.912 81.808  1.00 87.82  ? 50  GLY   B N     1 
ATOM   2654 C  CA    . GLY   B 2 50  ? 172.593 146.611 80.794  1.00 84.99  ? 50  GLY   B CA    1 
ATOM   2655 C  C     . GLY   B 2 50  ? 171.456 145.793 80.222  1.00 84.77  ? 50  GLY   B C     1 
ATOM   2656 O  O     . GLY   B 2 50  ? 171.246 145.797 79.002  1.00 80.37  ? 50  GLY   B O     1 
ATOM   2657 N  N     . ASP   B 2 51  ? 170.714 145.089 81.073  1.00 96.52  ? 51  ASP   B N     1 
ATOM   2658 C  CA    . ASP   B 2 51  ? 169.640 144.206 80.648  1.00 96.19  ? 51  ASP   B CA    1 
ATOM   2659 C  C     . ASP   B 2 51  ? 168.344 144.581 81.350  1.00 93.11  ? 51  ASP   B C     1 
ATOM   2660 O  O     . ASP   B 2 51  ? 168.343 144.900 82.543  1.00 90.39  ? 51  ASP   B O     1 
ATOM   2661 C  CB    . ASP   B 2 51  ? 169.978 142.742 80.949  1.00 94.97  ? 51  ASP   B CB    1 
ATOM   2662 C  CG    . ASP   B 2 51  ? 170.860 142.117 79.891  1.00 94.95  ? 51  ASP   B CG    1 
ATOM   2663 O  OD1   . ASP   B 2 51  ? 171.155 142.796 78.885  1.00 93.99  ? 51  ASP   B OD1   1 
ATOM   2664 O  OD2   . ASP   B 2 51  ? 171.258 140.947 80.065  1.00 95.04  ? 51  ASP   B OD2   1 
ATOM   2665 N  N     . VAL   B 2 52  ? 167.245 144.545 80.604  1.00 83.68  ? 52  VAL   B N     1 
ATOM   2666 C  CA    . VAL   B 2 52  ? 165.903 144.683 81.157  1.00 83.80  ? 52  VAL   B CA    1 
ATOM   2667 C  C     . VAL   B 2 52  ? 165.212 143.340 80.976  1.00 83.79  ? 52  VAL   B C     1 
ATOM   2668 O  O     . VAL   B 2 52  ? 164.970 142.902 79.844  1.00 85.38  ? 52  VAL   B O     1 
ATOM   2669 C  CB    . VAL   B 2 52  ? 165.115 145.815 80.486  1.00 84.60  ? 52  VAL   B CB    1 
ATOM   2670 C  CG1   . VAL   B 2 52  ? 163.923 146.208 81.345  1.00 79.72  ? 52  VAL   B CG1   1 
ATOM   2671 C  CG2   . VAL   B 2 52  ? 166.013 147.012 80.240  1.00 85.30  ? 52  VAL   B CG2   1 
ATOM   2672 N  N     . ILE   B 2 53  ? 164.896 142.683 82.087  1.00 81.28  ? 53  ILE   B N     1 
ATOM   2673 C  CA    . ILE   B 2 53  ? 164.355 141.329 82.083  1.00 83.11  ? 53  ILE   B CA    1 
ATOM   2674 C  C     . ILE   B 2 53  ? 162.952 141.376 82.668  1.00 80.84  ? 53  ILE   B C     1 
ATOM   2675 O  O     . ILE   B 2 53  ? 162.750 141.877 83.781  1.00 82.92  ? 53  ILE   B O     1 
ATOM   2676 C  CB    . ILE   B 2 53  ? 165.252 140.360 82.866  1.00 80.22  ? 53  ILE   B CB    1 
ATOM   2677 C  CG1   . ILE   B 2 53  ? 166.606 140.216 82.171  1.00 79.82  ? 53  ILE   B CG1   1 
ATOM   2678 C  CG2   . ILE   B 2 53  ? 164.582 139.004 83.006  1.00 76.34  ? 53  ILE   B CG2   1 
ATOM   2679 C  CD1   . ILE   B 2 53  ? 167.784 140.319 83.107  1.00 81.40  ? 53  ILE   B CD1   1 
ATOM   2680 N  N     . GLY   B 2 54  ? 161.986 140.855 81.917  1.00 63.82  ? 54  GLY   B N     1 
ATOM   2681 C  CA    . GLY   B 2 54  ? 160.597 140.831 82.330  1.00 59.65  ? 54  GLY   B CA    1 
ATOM   2682 C  C     . GLY   B 2 54  ? 160.159 139.414 82.663  1.00 59.95  ? 54  GLY   B C     1 
ATOM   2683 O  O     . GLY   B 2 54  ? 160.379 138.484 81.882  1.00 65.29  ? 54  GLY   B O     1 
ATOM   2684 N  N     . LEU   B 2 55  ? 159.537 139.272 83.828  1.00 53.90  ? 55  LEU   B N     1 
ATOM   2685 C  CA    . LEU   B 2 55  ? 159.003 138.000 84.291  1.00 54.93  ? 55  LEU   B CA    1 
ATOM   2686 C  C     . LEU   B 2 55  ? 157.540 137.899 83.885  1.00 59.29  ? 55  LEU   B C     1 
ATOM   2687 O  O     . LEU   B 2 55  ? 156.755 138.816 84.149  1.00 62.46  ? 55  LEU   B O     1 
ATOM   2688 C  CB    . LEU   B 2 55  ? 159.139 137.873 85.809  1.00 54.26  ? 55  LEU   B CB    1 
ATOM   2689 C  CG    . LEU   B 2 55  ? 160.545 137.991 86.399  1.00 59.36  ? 55  LEU   B CG    1 
ATOM   2690 C  CD1   . LEU   B 2 55  ? 160.484 138.000 87.916  1.00 60.18  ? 55  LEU   B CD1   1 
ATOM   2691 C  CD2   . LEU   B 2 55  ? 161.434 136.862 85.906  1.00 60.84  ? 55  LEU   B CD2   1 
ATOM   2692 N  N     . VAL   B 2 56  ? 157.175 136.789 83.245  1.00 52.14  ? 56  VAL   B N     1 
ATOM   2693 C  CA    . VAL   B 2 56  ? 155.804 136.574 82.805  1.00 50.37  ? 56  VAL   B CA    1 
ATOM   2694 C  C     . VAL   B 2 56  ? 155.296 135.260 83.379  1.00 53.74  ? 56  VAL   B C     1 
ATOM   2695 O  O     . VAL   B 2 56  ? 156.063 134.339 83.666  1.00 61.88  ? 56  VAL   B O     1 
ATOM   2696 C  CB    . VAL   B 2 56  ? 155.671 136.578 81.267  1.00 51.98  ? 56  VAL   B CB    1 
ATOM   2697 C  CG1   . VAL   B 2 56  ? 155.887 137.979 80.721  1.00 56.26  ? 56  VAL   B CG1   1 
ATOM   2698 C  CG2   . VAL   B 2 56  ? 156.650 135.606 80.646  1.00 53.74  ? 56  VAL   B CG2   1 
ATOM   2699 N  N     . GLY   B 2 57  ? 153.986 135.188 83.549  1.00 69.81  ? 57  GLY   B N     1 
ATOM   2700 C  CA    . GLY   B 2 57  ? 153.346 134.007 84.087  1.00 70.06  ? 57  GLY   B CA    1 
ATOM   2701 C  C     . GLY   B 2 57  ? 151.990 134.333 84.661  1.00 70.08  ? 57  GLY   B C     1 
ATOM   2702 O  O     . GLY   B 2 57  ? 151.664 135.483 84.958  1.00 72.73  ? 57  GLY   B O     1 
ATOM   2703 N  N     . ILE   B 2 58  ? 151.182 133.287 84.823  1.00 65.27  ? 58  ILE   B N     1 
ATOM   2704 C  CA    . ILE   B 2 58  ? 149.828 133.426 85.350  1.00 62.84  ? 58  ILE   B CA    1 
ATOM   2705 C  C     . ILE   B 2 58  ? 149.897 133.635 86.856  1.00 56.97  ? 58  ILE   B C     1 
ATOM   2706 O  O     . ILE   B 2 58  ? 150.964 133.499 87.462  1.00 63.51  ? 58  ILE   B O     1 
ATOM   2707 C  CB    . ILE   B 2 58  ? 148.957 132.207 84.995  1.00 64.86  ? 58  ILE   B CB    1 
ATOM   2708 C  CG1   . ILE   B 2 58  ? 149.635 130.912 85.440  1.00 66.37  ? 58  ILE   B CG1   1 
ATOM   2709 C  CG2   . ILE   B 2 58  ? 148.675 132.173 83.504  1.00 62.95  ? 58  ILE   B CG2   1 
ATOM   2710 C  CD1   . ILE   B 2 58  ? 148.685 129.911 86.061  1.00 62.88  ? 58  ILE   B CD1   1 
ATOM   2711 N  N     . ASN   B 2 59  ? 148.765 133.988 87.462  1.00 55.65  ? 59  ASN   B N     1 
ATOM   2712 C  CA    . ASN   B 2 59  ? 148.724 134.244 88.896  1.00 63.81  ? 59  ASN   B CA    1 
ATOM   2713 C  C     . ASN   B 2 59  ? 149.133 132.999 89.675  1.00 67.27  ? 59  ASN   B C     1 
ATOM   2714 O  O     . ASN   B 2 59  ? 148.668 131.892 89.388  1.00 70.69  ? 59  ASN   B O     1 
ATOM   2715 C  CB    . ASN   B 2 59  ? 147.324 134.690 89.312  1.00 66.81  ? 59  ASN   B CB    1 
ATOM   2716 C  CG    . ASN   B 2 59  ? 147.104 136.173 89.114  1.00 68.11  ? 59  ASN   B CG    1 
ATOM   2717 O  OD1   . ASN   B 2 59  ? 146.106 136.592 88.529  1.00 74.43  ? 59  ASN   B OD1   1 
ATOM   2718 N  ND2   . ASN   B 2 59  ? 148.038 136.979 89.600  1.00 64.99  ? 59  ASN   B ND2   1 
ATOM   2719 N  N     . GLY   B 2 60  ? 150.002 133.184 90.664  1.00 63.26  ? 60  GLY   B N     1 
ATOM   2720 C  CA    . GLY   B 2 60  ? 150.507 132.084 91.457  1.00 57.70  ? 60  GLY   B CA    1 
ATOM   2721 C  C     . GLY   B 2 60  ? 151.680 131.338 90.863  1.00 61.82  ? 60  GLY   B C     1 
ATOM   2722 O  O     . GLY   B 2 60  ? 151.993 130.239 91.335  1.00 64.98  ? 60  GLY   B O     1 
ATOM   2723 N  N     . SER   B 2 61  ? 152.342 131.896 89.847  1.00 63.49  ? 61  SER   B N     1 
ATOM   2724 C  CA    . SER   B 2 61  ? 153.454 131.204 89.205  1.00 55.59  ? 61  SER   B CA    1 
ATOM   2725 C  C     . SER   B 2 61  ? 154.727 131.244 90.041  1.00 63.79  ? 61  SER   B C     1 
ATOM   2726 O  O     . SER   B 2 61  ? 155.513 130.292 90.005  1.00 70.71  ? 61  SER   B O     1 
ATOM   2727 C  CB    . SER   B 2 61  ? 153.720 131.807 87.826  1.00 56.97  ? 61  SER   B CB    1 
ATOM   2728 O  OG    . SER   B 2 61  ? 153.203 130.979 86.801  1.00 60.37  ? 61  SER   B OG    1 
ATOM   2729 N  N     . GLY   B 2 62  ? 154.953 132.323 90.785  1.00 62.87  ? 62  GLY   B N     1 
ATOM   2730 C  CA    . GLY   B 2 62  ? 156.135 132.426 91.619  1.00 54.78  ? 62  GLY   B CA    1 
ATOM   2731 C  C     . GLY   B 2 62  ? 157.078 133.546 91.228  1.00 62.16  ? 62  GLY   B C     1 
ATOM   2732 O  O     . GLY   B 2 62  ? 158.289 133.443 91.438  1.00 63.60  ? 62  GLY   B O     1 
ATOM   2733 N  N     . LYS   B 2 63  ? 156.538 134.622 90.654  1.00 63.25  ? 63  LYS   B N     1 
ATOM   2734 C  CA    . LYS   B 2 63  ? 157.347 135.774 90.273  1.00 46.92  ? 63  LYS   B CA    1 
ATOM   2735 C  C     . LYS   B 2 63  ? 157.721 136.645 91.466  1.00 48.38  ? 63  LYS   B C     1 
ATOM   2736 O  O     . LYS   B 2 63  ? 158.863 137.110 91.559  1.00 61.07  ? 63  LYS   B O     1 
ATOM   2737 C  CB    . LYS   B 2 63  ? 156.605 136.615 89.231  1.00 47.95  ? 63  LYS   B CB    1 
ATOM   2738 C  CG    . LYS   B 2 63  ? 155.878 135.797 88.179  1.00 51.84  ? 63  LYS   B CG    1 
ATOM   2739 C  CD    . LYS   B 2 63  ? 155.272 136.689 87.115  1.00 50.22  ? 63  LYS   B CD    1 
ATOM   2740 C  CE    . LYS   B 2 63  ? 153.840 137.051 87.457  1.00 53.86  ? 63  LYS   B CE    1 
ATOM   2741 N  NZ    . LYS   B 2 63  ? 153.126 135.916 88.098  1.00 52.71  ? 63  LYS   B NZ    1 
ATOM   2742 N  N     . SER   B 2 64  ? 156.779 136.874 92.384  1.00 50.30  ? 64  SER   B N     1 
ATOM   2743 C  CA    . SER   B 2 64  ? 157.080 137.671 93.568  1.00 53.71  ? 64  SER   B CA    1 
ATOM   2744 C  C     . SER   B 2 64  ? 158.082 136.972 94.475  1.00 53.42  ? 64  SER   B C     1 
ATOM   2745 O  O     . SER   B 2 64  ? 158.942 137.633 95.068  1.00 58.69  ? 64  SER   B O     1 
ATOM   2746 C  CB    . SER   B 2 64  ? 155.797 137.982 94.337  1.00 59.61  ? 64  SER   B CB    1 
ATOM   2747 O  OG    . SER   B 2 64  ? 154.900 138.742 93.547  1.00 62.62  ? 64  SER   B OG    1 
ATOM   2748 N  N     . THR   B 2 65  ? 157.988 135.646 94.599  1.00 54.69  ? 65  THR   B N     1 
ATOM   2749 C  CA    . THR   B 2 65  ? 158.956 134.909 95.404  1.00 50.14  ? 65  THR   B CA    1 
ATOM   2750 C  C     . THR   B 2 65  ? 160.360 135.030 94.823  1.00 48.91  ? 65  THR   B C     1 
ATOM   2751 O  O     . THR   B 2 65  ? 161.328 135.249 95.560  1.00 55.24  ? 65  THR   B O     1 
ATOM   2752 C  CB    . THR   B 2 65  ? 158.538 133.442 95.512  1.00 55.03  ? 65  THR   B CB    1 
ATOM   2753 O  OG1   . THR   B 2 65  ? 157.358 133.338 96.318  1.00 53.29  ? 65  THR   B OG1   1 
ATOM   2754 C  CG2   . THR   B 2 65  ? 159.642 132.613 96.142  1.00 60.40  ? 65  THR   B CG2   1 
ATOM   2755 N  N     . LEU   B 2 66  ? 160.488 134.907 93.500  1.00 49.69  ? 66  LEU   B N     1 
ATOM   2756 C  CA    . LEU   B 2 66  ? 161.792 135.067 92.865  1.00 53.00  ? 66  LEU   B CA    1 
ATOM   2757 C  C     . LEU   B 2 66  ? 162.319 136.487 93.029  1.00 58.93  ? 66  LEU   B C     1 
ATOM   2758 O  O     . LEU   B 2 66  ? 163.514 136.688 93.281  1.00 59.10  ? 66  LEU   B O     1 
ATOM   2759 C  CB    . LEU   B 2 66  ? 161.705 134.693 91.386  1.00 50.01  ? 66  LEU   B CB    1 
ATOM   2760 C  CG    . LEU   B 2 66  ? 163.037 134.559 90.646  1.00 55.87  ? 66  LEU   B CG    1 
ATOM   2761 C  CD1   . LEU   B 2 66  ? 163.899 133.485 91.287  1.00 56.88  ? 66  LEU   B CD1   1 
ATOM   2762 C  CD2   . LEU   B 2 66  ? 162.808 134.256 89.175  1.00 56.84  ? 66  LEU   B CD2   1 
ATOM   2763 N  N     . SER   B 2 67  ? 161.446 137.487 92.884  1.00 72.95  ? 67  SER   B N     1 
ATOM   2764 C  CA    . SER   B 2 67  ? 161.874 138.869 93.069  1.00 68.28  ? 67  SER   B CA    1 
ATOM   2765 C  C     . SER   B 2 67  ? 162.342 139.127 94.496  1.00 70.33  ? 67  SER   B C     1 
ATOM   2766 O  O     . SER   B 2 67  ? 163.337 139.831 94.701  1.00 72.01  ? 67  SER   B O     1 
ATOM   2767 C  CB    . SER   B 2 67  ? 160.740 139.825 92.697  1.00 65.38  ? 67  SER   B CB    1 
ATOM   2768 O  OG    . SER   B 2 67  ? 159.711 139.797 93.670  1.00 69.93  ? 67  SER   B OG    1 
ATOM   2769 N  N     . ASN   B 2 68  ? 161.646 138.568 95.489  1.00 70.19  ? 68  ASN   B N     1 
ATOM   2770 C  CA    . ASN   B 2 68  ? 162.072 138.728 96.876  1.00 70.89  ? 68  ASN   B CA    1 
ATOM   2771 C  C     . ASN   B 2 68  ? 163.375 137.992 97.155  1.00 74.82  ? 68  ASN   B C     1 
ATOM   2772 O  O     . ASN   B 2 68  ? 164.208 138.483 97.924  1.00 75.81  ? 68  ASN   B O     1 
ATOM   2773 C  CB    . ASN   B 2 68  ? 160.976 138.242 97.822  1.00 70.58  ? 68  ASN   B CB    1 
ATOM   2774 C  CG    . ASN   B 2 68  ? 159.867 139.257 97.994  1.00 75.27  ? 68  ASN   B CG    1 
ATOM   2775 O  OD1   . ASN   B 2 68  ? 160.104 140.464 97.953  1.00 76.42  ? 68  ASN   B OD1   1 
ATOM   2776 N  ND2   . ASN   B 2 68  ? 158.647 138.773 98.190  1.00 75.90  ? 68  ASN   B ND2   1 
ATOM   2777 N  N     . ILE   B 2 69  ? 163.564 136.814 96.556  1.00 73.23  ? 69  ILE   B N     1 
ATOM   2778 C  CA    . ILE   B 2 69  ? 164.822 136.091 96.715  1.00 69.87  ? 69  ILE   B CA    1 
ATOM   2779 C  C     . ILE   B 2 69  ? 165.976 136.898 96.136  1.00 72.52  ? 69  ILE   B C     1 
ATOM   2780 O  O     . ILE   B 2 69  ? 167.052 136.989 96.739  1.00 79.79  ? 69  ILE   B O     1 
ATOM   2781 C  CB    . ILE   B 2 69  ? 164.717 134.695 96.074  1.00 68.15  ? 69  ILE   B CB    1 
ATOM   2782 C  CG1   . ILE   B 2 69  ? 164.019 133.725 97.028  1.00 66.87  ? 69  ILE   B CG1   1 
ATOM   2783 C  CG2   . ILE   B 2 69  ? 166.090 134.172 95.682  1.00 67.28  ? 69  ILE   B CG2   1 
ATOM   2784 C  CD1   . ILE   B 2 69  ? 164.021 132.292 96.554  1.00 67.81  ? 69  ILE   B CD1   1 
ATOM   2785 N  N     . ILE   B 2 70  ? 165.771 137.501 94.962  1.00 78.54  ? 70  ILE   B N     1 
ATOM   2786 C  CA    . ILE   B 2 70  ? 166.792 138.377 94.390  1.00 79.29  ? 70  ILE   B CA    1 
ATOM   2787 C  C     . ILE   B 2 70  ? 167.049 139.566 95.309  1.00 76.73  ? 70  ILE   B C     1 
ATOM   2788 O  O     . ILE   B 2 70  ? 168.201 139.948 95.547  1.00 76.32  ? 70  ILE   B O     1 
ATOM   2789 C  CB    . ILE   B 2 70  ? 166.380 138.832 92.978  1.00 78.00  ? 70  ILE   B CB    1 
ATOM   2790 C  CG1   . ILE   B 2 70  ? 166.380 137.647 92.012  1.00 79.04  ? 70  ILE   B CG1   1 
ATOM   2791 C  CG2   . ILE   B 2 70  ? 167.309 139.926 92.475  1.00 75.94  ? 70  ILE   B CG2   1 
ATOM   2792 C  CD1   . ILE   B 2 70  ? 166.147 138.038 90.571  1.00 78.79  ? 70  ILE   B CD1   1 
ATOM   2793 N  N     . GLY   B 2 71  ? 165.982 140.165 95.842  1.00 89.35  ? 71  GLY   B N     1 
ATOM   2794 C  CA    . GLY   B 2 71  ? 166.142 141.309 96.722  1.00 92.27  ? 71  GLY   B CA    1 
ATOM   2795 C  C     . GLY   B 2 71  ? 166.857 140.985 98.018  1.00 93.78  ? 71  GLY   B C     1 
ATOM   2796 O  O     . GLY   B 2 71  ? 167.642 141.796 98.515  1.00 93.66  ? 71  GLY   B O     1 
ATOM   2797 N  N     . GLY   B 2 72  ? 166.600 139.807 98.582  1.00 93.77  ? 72  GLY   B N     1 
ATOM   2798 C  CA    . GLY   B 2 72  ? 167.234 139.387 99.816  1.00 92.77  ? 72  GLY   B CA    1 
ATOM   2799 C  C     . GLY   B 2 72  ? 166.307 139.244 101.001 1.00 89.64  ? 72  GLY   B C     1 
ATOM   2800 O  O     . GLY   B 2 72  ? 166.755 138.788 102.060 1.00 92.01  ? 72  GLY   B O     1 
ATOM   2801 N  N     . SER   B 2 73  ? 165.032 139.613 100.869 1.00 84.44  ? 73  SER   B N     1 
ATOM   2802 C  CA    . SER   B 2 73  ? 164.079 139.440 101.956 1.00 88.15  ? 73  SER   B CA    1 
ATOM   2803 C  C     . SER   B 2 73  ? 163.729 137.980 102.208 1.00 91.56  ? 73  SER   B C     1 
ATOM   2804 O  O     . SER   B 2 73  ? 163.099 137.678 103.227 1.00 93.14  ? 73  SER   B O     1 
ATOM   2805 C  CB    . SER   B 2 73  ? 162.799 140.228 101.669 1.00 89.05  ? 73  SER   B CB    1 
ATOM   2806 O  OG    . SER   B 2 73  ? 161.688 139.652 102.333 1.00 88.06  ? 73  SER   B OG    1 
ATOM   2807 N  N     . LEU   B 2 74  ? 164.116 137.078 101.311 1.00 82.96  ? 74  LEU   B N     1 
ATOM   2808 C  CA    . LEU   B 2 74  ? 163.875 135.654 101.456 1.00 80.44  ? 74  LEU   B CA    1 
ATOM   2809 C  C     . LEU   B 2 74  ? 165.184 134.894 101.291 1.00 79.91  ? 74  LEU   B C     1 
ATOM   2810 O  O     . LEU   B 2 74  ? 166.118 135.357 100.631 1.00 79.96  ? 74  LEU   B O     1 
ATOM   2811 C  CB    . LEU   B 2 74  ? 162.849 135.153 100.431 1.00 82.94  ? 74  LEU   B CB    1 
ATOM   2812 C  CG    . LEU   B 2 74  ? 161.376 135.202 100.835 1.00 81.68  ? 74  LEU   B CG    1 
ATOM   2813 C  CD1   . LEU   B 2 74  ? 160.509 134.589 99.749  1.00 77.91  ? 74  LEU   B CD1   1 
ATOM   2814 C  CD2   . LEU   B 2 74  ? 161.158 134.493 102.160 1.00 80.14  ? 74  LEU   B CD2   1 
ATOM   2815 N  N     . SER   B 2 75  ? 165.242 133.715 101.903 1.00 97.95  ? 75  SER   B N     1 
ATOM   2816 C  CA    . SER   B 2 75  ? 166.407 132.857 101.832 1.00 99.73  ? 75  SER   B CA    1 
ATOM   2817 C  C     . SER   B 2 75  ? 166.033 131.539 101.168 1.00 97.49  ? 75  SER   B C     1 
ATOM   2818 O  O     . SER   B 2 75  ? 165.100 130.864 101.626 1.00 96.32  ? 75  SER   B O     1 
ATOM   2819 C  CB    . SER   B 2 75  ? 166.983 132.596 103.232 1.00 101.36 ? 75  SER   B CB    1 
ATOM   2820 O  OG    . SER   B 2 75  ? 167.302 133.812 103.887 1.00 99.46  ? 75  SER   B OG    1 
ATOM   2821 N  N     . PRO   B 2 76  ? 166.714 131.146 100.094 1.00 86.79  ? 76  PRO   B N     1 
ATOM   2822 C  CA    . PRO   B 2 76  ? 166.370 129.889 99.423  1.00 88.08  ? 76  PRO   B CA    1 
ATOM   2823 C  C     . PRO   B 2 76  ? 166.607 128.688 100.321 1.00 89.65  ? 76  PRO   B C     1 
ATOM   2824 O  O     . PRO   B 2 76  ? 167.531 128.663 101.139 1.00 92.98  ? 76  PRO   B O     1 
ATOM   2825 C  CB    . PRO   B 2 76  ? 167.309 129.866 98.210  1.00 84.56  ? 76  PRO   B CB    1 
ATOM   2826 C  CG    . PRO   B 2 76  ? 167.730 131.292 98.026  1.00 86.97  ? 76  PRO   B CG    1 
ATOM   2827 C  CD    . PRO   B 2 76  ? 167.811 131.847 99.411  1.00 83.34  ? 76  PRO   B CD    1 
ATOM   2828 N  N     . THR   B 2 77  ? 165.750 127.679 100.161 1.00 82.82  ? 77  THR   B N     1 
ATOM   2829 C  CA    . THR   B 2 77  ? 165.934 126.433 100.897 1.00 85.65  ? 77  THR   B CA    1 
ATOM   2830 C  C     . THR   B 2 77  ? 167.189 125.707 100.428 1.00 86.83  ? 77  THR   B C     1 
ATOM   2831 O  O     . THR   B 2 77  ? 168.020 125.289 101.243 1.00 87.24  ? 77  THR   B O     1 
ATOM   2832 C  CB    . THR   B 2 77  ? 164.700 125.543 100.741 1.00 82.78  ? 77  THR   B CB    1 
ATOM   2833 O  OG1   . THR   B 2 77  ? 163.613 126.097 101.493 1.00 81.76  ? 77  THR   B OG1   1 
ATOM   2834 C  CG2   . THR   B 2 77  ? 164.985 124.138 101.242 1.00 84.58  ? 77  THR   B CG2   1 
ATOM   2835 N  N     . VAL   B 2 78  ? 167.347 125.554 99.115  1.00 82.31  ? 78  VAL   B N     1 
ATOM   2836 C  CA    . VAL   B 2 78  ? 168.532 124.950 98.519  1.00 83.77  ? 78  VAL   B CA    1 
ATOM   2837 C  C     . VAL   B 2 78  ? 169.040 125.878 97.426  1.00 82.97  ? 78  VAL   B C     1 
ATOM   2838 O  O     . VAL   B 2 78  ? 168.259 126.339 96.586  1.00 86.16  ? 78  VAL   B O     1 
ATOM   2839 C  CB    . VAL   B 2 78  ? 168.243 123.551 97.942  1.00 84.43  ? 78  VAL   B CB    1 
ATOM   2840 C  CG1   . VAL   B 2 78  ? 169.539 122.869 97.535  1.00 82.12  ? 78  VAL   B CG1   1 
ATOM   2841 C  CG2   . VAL   B 2 78  ? 167.483 122.698 98.946  1.00 83.82  ? 78  VAL   B CG2   1 
ATOM   2842 N  N     . GLY   B 2 79  ? 170.336 126.153 97.436  1.00 92.42  ? 79  GLY   B N     1 
ATOM   2843 C  CA    . GLY   B 2 79  ? 170.974 126.927 96.391  1.00 91.51  ? 79  GLY   B CA    1 
ATOM   2844 C  C     . GLY   B 2 79  ? 171.426 128.292 96.877  1.00 92.43  ? 79  GLY   B C     1 
ATOM   2845 O  O     . GLY   B 2 79  ? 171.142 128.720 97.994  1.00 93.54  ? 79  GLY   B O     1 
ATOM   2846 N  N     . LYS   B 2 80  ? 172.148 128.973 95.990  1.00 91.51  ? 80  LYS   B N     1 
ATOM   2847 C  CA    . LYS   B 2 80  ? 172.736 130.267 96.298  1.00 92.95  ? 80  LYS   B CA    1 
ATOM   2848 C  C     . LYS   B 2 80  ? 172.553 131.213 95.119  1.00 94.91  ? 80  LYS   B C     1 
ATOM   2849 O  O     . LYS   B 2 80  ? 172.420 130.792 93.968  1.00 93.33  ? 80  LYS   B O     1 
ATOM   2850 C  CB    . LYS   B 2 80  ? 174.224 130.133 96.652  1.00 93.66  ? 80  LYS   B CB    1 
ATOM   2851 C  CG    . LYS   B 2 80  ? 175.123 129.832 95.464  1.00 94.15  ? 80  LYS   B CG    1 
ATOM   2852 C  CD    . LYS   B 2 80  ? 176.130 130.943 95.222  1.00 94.26  ? 80  LYS   B CD    1 
ATOM   2853 C  CE    . LYS   B 2 80  ? 176.670 130.890 93.801  1.00 93.00  ? 80  LYS   B CE    1 
ATOM   2854 N  NZ    . LYS   B 2 80  ? 177.330 132.160 93.401  1.00 90.59  ? 80  LYS   B NZ    1 
ATOM   2855 N  N     . VAL   B 2 81  ? 172.543 132.506 95.431  1.00 100.99 ? 81  VAL   B N     1 
ATOM   2856 C  CA    . VAL   B 2 81  ? 172.440 133.568 94.433  1.00 99.85  ? 81  VAL   B CA    1 
ATOM   2857 C  C     . VAL   B 2 81  ? 173.421 134.667 94.812  1.00 98.36  ? 81  VAL   B C     1 
ATOM   2858 O  O     . VAL   B 2 81  ? 173.464 135.096 95.968  1.00 97.87  ? 81  VAL   B O     1 
ATOM   2859 C  CB    . VAL   B 2 81  ? 171.002 134.118 94.332  1.00 100.05 ? 81  VAL   B CB    1 
ATOM   2860 C  CG1   . VAL   B 2 81  ? 170.309 134.035 95.679  1.00 96.55  ? 81  VAL   B CG1   1 
ATOM   2861 C  CG2   . VAL   B 2 81  ? 171.009 135.557 93.833  1.00 98.84  ? 81  VAL   B CG2   1 
ATOM   2862 N  N     . ASP   B 2 82  ? 174.210 135.125 93.844  1.00 108.22 ? 82  ASP   B N     1 
ATOM   2863 C  CA    . ASP   B 2 82  ? 175.171 136.193 94.083  1.00 109.76 ? 82  ASP   B CA    1 
ATOM   2864 C  C     . ASP   B 2 82  ? 174.853 137.414 93.228  1.00 110.30 ? 82  ASP   B C     1 
ATOM   2865 O  O     . ASP   B 2 82  ? 174.468 137.294 92.057  1.00 111.19 ? 82  ASP   B O     1 
ATOM   2866 C  CB    . ASP   B 2 82  ? 176.609 135.724 93.832  1.00 111.90 ? 82  ASP   B CB    1 
ATOM   2867 C  CG    . ASP   B 2 82  ? 176.789 135.098 92.474  1.00 111.97 ? 82  ASP   B CG    1 
ATOM   2868 O  OD1   . ASP   B 2 82  ? 175.784 134.969 91.757  1.00 112.42 ? 82  ASP   B OD1   1 
ATOM   2869 O  OD2   . ASP   B 2 82  ? 177.931 134.736 92.124  1.00 111.98 ? 82  ASP   B OD2   1 
ATOM   2870 N  N     . ARG   B 2 83  ? 175.012 138.589 93.837  1.00 108.37 ? 83  ARG   B N     1 
ATOM   2871 C  CA    . ARG   B 2 83  ? 174.705 139.871 93.220  1.00 106.48 ? 83  ARG   B CA    1 
ATOM   2872 C  C     . ARG   B 2 83  ? 175.951 140.742 93.262  1.00 108.79 ? 83  ARG   B C     1 
ATOM   2873 O  O     . ARG   B 2 83  ? 176.618 140.823 94.299  1.00 110.94 ? 83  ARG   B O     1 
ATOM   2874 C  CB    . ARG   B 2 83  ? 173.567 140.576 93.960  1.00 107.00 ? 83  ARG   B CB    1 
ATOM   2875 C  CG    . ARG   B 2 83  ? 172.614 139.639 94.675  1.00 106.38 ? 83  ARG   B CG    1 
ATOM   2876 C  CD    . ARG   B 2 83  ? 171.964 140.335 95.868  1.00 108.60 ? 83  ARG   B CD    1 
ATOM   2877 N  NE    . ARG   B 2 83  ? 170.912 139.543 96.497  1.00 111.21 ? 83  ARG   B NE    1 
ATOM   2878 C  CZ    . ARG   B 2 83  ? 171.083 138.348 97.050  1.00 111.64 ? 83  ARG   B CZ    1 
ATOM   2879 N  NH1   . ARG   B 2 83  ? 172.276 137.781 97.122  1.00 109.78 ? 83  ARG   B NH1   1 
ATOM   2880 N  NH2   . ARG   B 2 83  ? 170.032 137.714 97.561  1.00 109.69 ? 83  ARG   B NH2   1 
ATOM   2881 N  N     . ASN   B 2 84  ? 176.264 141.391 92.147  1.00 100.44 ? 84  ASN   B N     1 
ATOM   2882 C  CA    . ASN   B 2 84  ? 177.384 142.331 92.092  1.00 99.44  ? 84  ASN   B CA    1 
ATOM   2883 C  C     . ASN   B 2 84  ? 176.891 143.768 92.254  1.00 98.94  ? 84  ASN   B C     1 
ATOM   2884 O  O     . ASN   B 2 84  ? 176.970 144.591 91.342  1.00 100.39 ? 84  ASN   B O     1 
ATOM   2885 C  CB    . ASN   B 2 84  ? 178.161 142.153 90.791  1.00 98.54  ? 84  ASN   B CB    1 
ATOM   2886 C  CG    . ASN   B 2 84  ? 178.650 140.734 90.596  1.00 100.14 ? 84  ASN   B CG    1 
ATOM   2887 O  OD1   . ASN   B 2 84  ? 178.411 139.862 91.431  1.00 102.59 ? 84  ASN   B OD1   1 
ATOM   2888 N  ND2   . ASN   B 2 84  ? 179.344 140.494 89.490  1.00 101.28 ? 84  ASN   B ND2   1 
ATOM   2889 N  N     . GLY   B 2 85  ? 176.377 144.068 93.438  1.00 85.20  ? 85  GLY   B N     1 
ATOM   2890 C  CA    . GLY   B 2 85  ? 175.940 145.414 93.737  1.00 85.94  ? 85  GLY   B CA    1 
ATOM   2891 C  C     . GLY   B 2 85  ? 174.862 145.421 94.804  1.00 89.86  ? 85  GLY   B C     1 
ATOM   2892 O  O     . GLY   B 2 85  ? 174.641 144.433 95.502  1.00 89.34  ? 85  GLY   B O     1 
ATOM   2893 N  N     . GLU   B 2 86  ? 174.200 146.570 94.908  1.00 107.61 ? 86  GLU   B N     1 
ATOM   2894 C  CA    . GLU   B 2 86  ? 173.118 146.788 95.855  1.00 108.02 ? 86  GLU   B CA    1 
ATOM   2895 C  C     . GLU   B 2 86  ? 171.788 146.809 95.115  1.00 108.56 ? 86  GLU   B C     1 
ATOM   2896 O  O     . GLU   B 2 86  ? 171.658 147.457 94.072  1.00 108.11 ? 86  GLU   B O     1 
ATOM   2897 C  CB    . GLU   B 2 86  ? 173.311 148.099 96.621  1.00 109.38 ? 86  GLU   B CB    1 
ATOM   2898 C  CG    . GLU   B 2 86  ? 172.445 148.227 97.861  1.00 111.54 ? 86  GLU   B CG    1 
ATOM   2899 C  CD    . GLU   B 2 86  ? 173.171 147.811 99.124  1.00 111.76 ? 86  GLU   B CD    1 
ATOM   2900 O  OE1   . GLU   B 2 86  ? 173.575 146.633 99.217  1.00 109.79 ? 86  GLU   B OE1   1 
ATOM   2901 O  OE2   . GLU   B 2 86  ? 173.338 148.662 100.023 1.00 111.91 ? 86  GLU   B OE2   1 
ATOM   2902 N  N     . VAL   B 2 87  ? 170.804 146.100 95.659  1.00 100.16 ? 87  VAL   B N     1 
ATOM   2903 C  CA    . VAL   B 2 87  ? 169.512 145.943 95.010  1.00 99.00  ? 87  VAL   B CA    1 
ATOM   2904 C  C     . VAL   B 2 87  ? 168.454 146.708 95.794  1.00 99.91  ? 87  VAL   B C     1 
ATOM   2905 O  O     . VAL   B 2 87  ? 168.567 146.934 97.003  1.00 99.20  ? 87  VAL   B O     1 
ATOM   2906 C  CB    . VAL   B 2 87  ? 169.119 144.458 94.863  1.00 98.88  ? 87  VAL   B CB    1 
ATOM   2907 C  CG1   . VAL   B 2 87  ? 170.311 143.637 94.400  1.00 99.53  ? 87  VAL   B CG1   1 
ATOM   2908 C  CG2   . VAL   B 2 87  ? 168.575 143.917 96.171  1.00 96.32  ? 87  VAL   B CG2   1 
ATOM   2909 N  N     . SER   B 2 88  ? 167.415 147.129 95.076  1.00 96.57  ? 88  SER   B N     1 
ATOM   2910 C  CA    . SER   B 2 88  ? 166.269 147.785 95.691  1.00 93.54  ? 88  SER   B CA    1 
ATOM   2911 C  C     . SER   B 2 88  ? 165.006 147.321 94.983  1.00 90.99  ? 88  SER   B C     1 
ATOM   2912 O  O     . SER   B 2 88  ? 164.984 147.217 93.755  1.00 93.65  ? 88  SER   B O     1 
ATOM   2913 C  CB    . SER   B 2 88  ? 166.378 149.310 95.622  1.00 94.13  ? 88  SER   B CB    1 
ATOM   2914 O  OG    . SER   B 2 88  ? 166.654 149.733 94.301  1.00 93.43  ? 88  SER   B OG    1 
ATOM   2915 N  N     . VAL   B 2 89  ? 163.956 147.066 95.762  1.00 74.31  ? 89  VAL   B N     1 
ATOM   2916 C  CA    . VAL   B 2 89  ? 162.720 146.471 95.268  1.00 80.43  ? 89  VAL   B CA    1 
ATOM   2917 C  C     . VAL   B 2 89  ? 161.563 147.418 95.558  1.00 81.08  ? 89  VAL   B C     1 
ATOM   2918 O  O     . VAL   B 2 89  ? 161.431 147.921 96.680  1.00 77.43  ? 89  VAL   B O     1 
ATOM   2919 C  CB    . VAL   B 2 89  ? 162.467 145.092 95.905  1.00 73.99  ? 89  VAL   B CB    1 
ATOM   2920 C  CG1   . VAL   B 2 89  ? 161.134 144.523 95.444  1.00 70.69  ? 89  VAL   B CG1   1 
ATOM   2921 C  CG2   . VAL   B 2 89  ? 163.605 144.139 95.579  1.00 75.73  ? 89  VAL   B CG2   1 
ATOM   2922 N  N     . ILE   B 2 90  ? 160.729 147.658 94.547  1.00 75.00  ? 90  ILE   B N     1 
ATOM   2923 C  CA    . ILE   B 2 90  ? 159.484 148.405 94.687  1.00 66.99  ? 90  ILE   B CA    1 
ATOM   2924 C  C     . ILE   B 2 90  ? 158.334 147.456 94.387  1.00 71.87  ? 90  ILE   B C     1 
ATOM   2925 O  O     . ILE   B 2 90  ? 158.394 146.687 93.421  1.00 79.86  ? 90  ILE   B O     1 
ATOM   2926 C  CB    . ILE   B 2 90  ? 159.438 149.631 93.754  1.00 66.57  ? 90  ILE   B CB    1 
ATOM   2927 C  CG1   . ILE   B 2 90  ? 160.801 149.860 93.099  1.00 71.51  ? 90  ILE   B CG1   1 
ATOM   2928 C  CG2   . ILE   B 2 90  ? 158.992 150.867 94.520  1.00 69.04  ? 90  ILE   B CG2   1 
ATOM   2929 C  CD1   . ILE   B 2 90  ? 160.919 151.186 92.383  1.00 73.74  ? 90  ILE   B CD1   1 
ATOM   2930 N  N     . ALA   B 2 91  ? 157.295 147.501 95.218  1.00 69.63  ? 91  ALA   B N     1 
ATOM   2931 C  CA    . ALA   B 2 91  ? 156.175 146.573 95.125  1.00 69.70  ? 91  ALA   B CA    1 
ATOM   2932 C  C     . ALA   B 2 91  ? 154.869 147.347 94.982  1.00 74.44  ? 91  ALA   B C     1 
ATOM   2933 O  O     . ALA   B 2 91  ? 154.852 148.579 94.905  1.00 80.42  ? 91  ALA   B O     1 
ATOM   2934 C  CB    . ALA   B 2 91  ? 156.126 145.645 96.344  1.00 72.08  ? 91  ALA   B CB    1 
ATOM   2935 N  N     . ILE   B 2 92  ? 153.760 146.601 94.944  1.00 79.51  ? 92  ILE   B N     1 
ATOM   2936 C  CA    . ILE   B 2 92  ? 152.439 147.202 94.790  1.00 80.70  ? 92  ILE   B CA    1 
ATOM   2937 C  C     . ILE   B 2 92  ? 152.048 148.050 95.993  1.00 80.91  ? 92  ILE   B C     1 
ATOM   2938 O  O     . ILE   B 2 92  ? 151.222 148.961 95.860  1.00 81.63  ? 92  ILE   B O     1 
ATOM   2939 C  CB    . ILE   B 2 92  ? 151.387 146.107 94.521  1.00 81.88  ? 92  ILE   B CB    1 
ATOM   2940 C  CG1   . ILE   B 2 92  ? 150.135 146.702 93.872  1.00 81.14  ? 92  ILE   B CG1   1 
ATOM   2941 C  CG2   . ILE   B 2 92  ? 151.033 145.365 95.801  1.00 80.37  ? 92  ILE   B CG2   1 
ATOM   2942 C  CD1   . ILE   B 2 92  ? 150.401 147.475 92.610  1.00 76.14  ? 92  ILE   B CD1   1 
ATOM   2943 N  N     . SER   B 2 93  ? 152.619 147.782 97.167  1.00 85.99  ? 93  SER   B N     1 
ATOM   2944 C  CA    . SER   B 2 93  ? 152.355 148.573 98.372  1.00 87.96  ? 93  SER   B CA    1 
ATOM   2945 C  C     . SER   B 2 93  ? 153.683 148.709 99.115  1.00 86.95  ? 93  SER   B C     1 
ATOM   2946 O  O     . SER   B 2 93  ? 154.053 147.845 99.914  1.00 85.61  ? 93  SER   B O     1 
ATOM   2947 C  CB    . SER   B 2 93  ? 151.279 147.933 99.239  1.00 84.74  ? 93  SER   B CB    1 
ATOM   2948 O  OG    . SER   B 2 93  ? 149.996 148.098 98.660  1.00 80.99  ? 93  SER   B OG    1 
ATOM   2949 N  N     . ALA   B 2 94  ? 154.392 149.801 98.844  1.00 95.01  ? 94  ALA   B N     1 
ATOM   2950 C  CA    . ALA   B 2 94  ? 155.698 150.034 99.434  1.00 93.24  ? 94  ALA   B CA    1 
ATOM   2951 C  C     . ALA   B 2 94  ? 155.552 150.442 100.898 1.00 93.53  ? 94  ALA   B C     1 
ATOM   2952 O  O     . ALA   B 2 94  ? 154.453 150.488 101.456 1.00 93.88  ? 94  ALA   B O     1 
ATOM   2953 C  CB    . ALA   B 2 94  ? 156.457 151.093 98.639  1.00 91.25  ? 94  ALA   B CB    1 
ATOM   2954 N  N     . GLY   B 2 95  ? 156.681 150.747 101.530 1.00 95.28  ? 95  GLY   B N     1 
ATOM   2955 C  CA    . GLY   B 2 95  ? 156.666 151.137 102.924 1.00 95.07  ? 95  GLY   B CA    1 
ATOM   2956 C  C     . GLY   B 2 95  ? 156.397 152.614 103.108 1.00 95.88  ? 95  GLY   B C     1 
ATOM   2957 O  O     . GLY   B 2 95  ? 157.298 153.443 102.957 1.00 98.27  ? 95  GLY   B O     1 
ATOM   2958 N  N     . LEU   B 2 96  ? 155.153 152.952 103.437 1.00 74.67  ? 96  LEU   B N     1 
ATOM   2959 C  CA    . LEU   B 2 96  ? 154.750 154.334 103.667 1.00 70.73  ? 96  LEU   B CA    1 
ATOM   2960 C  C     . LEU   B 2 96  ? 153.717 154.344 104.780 1.00 75.83  ? 96  LEU   B C     1 
ATOM   2961 O  O     . LEU   B 2 96  ? 152.655 153.729 104.646 1.00 75.79  ? 96  LEU   B O     1 
ATOM   2962 C  CB    . LEU   B 2 96  ? 154.177 154.969 102.395 1.00 71.31  ? 96  LEU   B CB    1 
ATOM   2963 C  CG    . LEU   B 2 96  ? 155.155 155.337 101.277 1.00 72.64  ? 96  LEU   B CG    1 
ATOM   2964 C  CD1   . LEU   B 2 96  ? 154.414 155.954 100.106 1.00 71.05  ? 96  LEU   B CD1   1 
ATOM   2965 C  CD2   . LEU   B 2 96  ? 156.232 156.281 101.782 1.00 74.83  ? 96  LEU   B CD2   1 
ATOM   2966 N  N     . SER   B 2 97  ? 154.027 155.035 105.874 1.00 83.49  ? 97  SER   B N     1 
ATOM   2967 C  CA    . SER   B 2 97  ? 153.109 155.119 107.000 1.00 82.50  ? 97  SER   B CA    1 
ATOM   2968 C  C     . SER   B 2 97  ? 151.963 156.065 106.667 1.00 81.90  ? 97  SER   B C     1 
ATOM   2969 O  O     . SER   B 2 97  ? 152.187 157.186 106.201 1.00 83.63  ? 97  SER   B O     1 
ATOM   2970 C  CB    . SER   B 2 97  ? 153.844 155.591 108.252 1.00 83.43  ? 97  SER   B CB    1 
ATOM   2971 O  OG    . SER   B 2 97  ? 154.828 154.652 108.647 1.00 84.11  ? 97  SER   B OG    1 
ATOM   2972 N  N     . GLY   B 2 98  ? 150.733 155.607 106.902 1.00 79.39  ? 98  GLY   B N     1 
ATOM   2973 C  CA    . GLY   B 2 98  ? 149.575 156.434 106.612 1.00 78.98  ? 98  GLY   B CA    1 
ATOM   2974 C  C     . GLY   B 2 98  ? 149.468 157.654 107.501 1.00 82.29  ? 98  GLY   B C     1 
ATOM   2975 O  O     . GLY   B 2 98  ? 149.072 158.729 107.040 1.00 85.39  ? 98  GLY   B O     1 
ATOM   2976 N  N     . GLN   B 2 99  ? 149.811 157.511 108.783 1.00 89.91  ? 99  GLN   B N     1 
ATOM   2977 C  CA    . GLN   B 2 99  ? 149.720 158.639 109.705 1.00 89.94  ? 99  GLN   B CA    1 
ATOM   2978 C  C     . GLN   B 2 99  ? 150.771 159.699 109.405 1.00 85.77  ? 99  GLN   B C     1 
ATOM   2979 O  O     . GLN   B 2 99  ? 150.500 160.896 109.552 1.00 84.87  ? 99  GLN   B O     1 
ATOM   2980 C  CB    . GLN   B 2 99  ? 149.859 158.149 111.145 1.00 89.28  ? 99  GLN   B CB    1 
ATOM   2981 C  CG    . GLN   B 2 99  ? 149.365 156.730 111.367 1.00 87.10  ? 99  GLN   B CG    1 
ATOM   2982 C  CD    . GLN   B 2 99  ? 150.498 155.727 111.455 1.00 88.97  ? 99  GLN   B CD    1 
ATOM   2983 O  OE1   . GLN   B 2 99  ? 151.560 156.020 112.003 1.00 88.73  ? 99  GLN   B OE1   1 
ATOM   2984 N  NE2   . GLN   B 2 99  ? 150.277 154.535 110.914 1.00 87.74  ? 99  GLN   B NE2   1 
ATOM   2985 N  N     . LEU   B 2 100 ? 151.963 159.285 108.990 1.00 82.02  ? 100 LEU   B N     1 
ATOM   2986 C  CA    . LEU   B 2 100 ? 153.038 160.224 108.717 1.00 84.96  ? 100 LEU   B CA    1 
ATOM   2987 C  C     . LEU   B 2 100 ? 152.765 161.003 107.434 1.00 86.54  ? 100 LEU   B C     1 
ATOM   2988 O  O     . LEU   B 2 100 ? 151.995 160.581 106.567 1.00 86.65  ? 100 LEU   B O     1 
ATOM   2989 C  CB    . LEU   B 2 100 ? 154.374 159.489 108.606 1.00 84.52  ? 100 LEU   B CB    1 
ATOM   2990 C  CG    . LEU   B 2 100 ? 155.161 159.241 109.893 1.00 83.39  ? 100 LEU   B CG    1 
ATOM   2991 C  CD1   . LEU   B 2 100 ? 154.452 158.240 110.788 1.00 80.77  ? 100 LEU   B CD1   1 
ATOM   2992 C  CD2   . LEU   B 2 100 ? 156.557 158.756 109.558 1.00 83.03  ? 100 LEU   B CD2   1 
ATOM   2993 N  N     . THR   B 2 101 ? 153.408 162.161 107.323 1.00 90.39  ? 101 THR   B N     1 
ATOM   2994 C  CA    . THR   B 2 101 ? 153.314 162.980 106.126 1.00 90.05  ? 101 THR   B CA    1 
ATOM   2995 C  C     . THR   B 2 101 ? 154.409 162.565 105.143 1.00 91.56  ? 101 THR   B C     1 
ATOM   2996 O  O     . THR   B 2 101 ? 155.158 161.615 105.382 1.00 92.84  ? 101 THR   B O     1 
ATOM   2997 C  CB    . THR   B 2 101 ? 153.400 164.462 106.485 1.00 88.26  ? 101 THR   B CB    1 
ATOM   2998 O  OG1   . THR   B 2 101 ? 153.155 165.251 105.315 1.00 88.97  ? 101 THR   B OG1   1 
ATOM   2999 C  CG2   . THR   B 2 101 ? 154.775 164.797 107.028 1.00 88.87  ? 101 THR   B CG2   1 
ATOM   3000 N  N     . GLY   B 2 102 ? 154.506 163.272 104.017 1.00 76.68  ? 102 GLY   B N     1 
ATOM   3001 C  CA    . GLY   B 2 102 ? 155.498 162.916 103.017 1.00 71.15  ? 102 GLY   B CA    1 
ATOM   3002 C  C     . GLY   B 2 102 ? 156.924 163.126 103.490 1.00 77.19  ? 102 GLY   B C     1 
ATOM   3003 O  O     . GLY   B 2 102 ? 157.791 162.278 103.266 1.00 75.74  ? 102 GLY   B O     1 
ATOM   3004 N  N     . ILE   B 2 103 ? 157.186 164.254 104.154 1.00 88.30  ? 103 ILE   B N     1 
ATOM   3005 C  CA    . ILE   B 2 103 ? 158.547 164.569 104.581 1.00 88.36  ? 103 ILE   B CA    1 
ATOM   3006 C  C     . ILE   B 2 103 ? 159.005 163.611 105.674 1.00 88.84  ? 103 ILE   B C     1 
ATOM   3007 O  O     . ILE   B 2 103 ? 160.153 163.145 105.671 1.00 90.55  ? 103 ILE   B O     1 
ATOM   3008 C  CB    . ILE   B 2 103 ? 158.633 166.037 105.037 1.00 89.04  ? 103 ILE   B CB    1 
ATOM   3009 C  CG1   . ILE   B 2 103 ? 158.162 166.970 103.917 1.00 85.05  ? 103 ILE   B CG1   1 
ATOM   3010 C  CG2   . ILE   B 2 103 ? 160.049 166.373 105.485 1.00 89.63  ? 103 ILE   B CG2   1 
ATOM   3011 C  CD1   . ILE   B 2 103 ? 159.281 167.550 103.074 1.00 86.15  ? 103 ILE   B CD1   1 
ATOM   3012 N  N     . GLU   B 2 104 ? 158.124 163.312 106.633 1.00 88.38  ? 104 GLU   B N     1 
ATOM   3013 C  CA    . GLU   B 2 104 ? 158.473 162.355 107.677 1.00 89.48  ? 104 GLU   B CA    1 
ATOM   3014 C  C     . GLU   B 2 104 ? 158.730 160.973 107.092 1.00 91.84  ? 104 GLU   B C     1 
ATOM   3015 O  O     . GLU   B 2 104 ? 159.661 160.276 107.511 1.00 91.43  ? 104 GLU   B O     1 
ATOM   3016 C  CB    . GLU   B 2 104 ? 157.371 162.296 108.735 1.00 91.28  ? 104 GLU   B CB    1 
ATOM   3017 C  CG    . GLU   B 2 104 ? 157.452 163.405 109.773 1.00 93.27  ? 104 GLU   B CG    1 
ATOM   3018 C  CD    . GLU   B 2 104 ? 156.104 164.023 110.078 1.00 93.36  ? 104 GLU   B CD    1 
ATOM   3019 O  OE1   . GLU   B 2 104 ? 155.147 163.265 110.342 1.00 93.61  ? 104 GLU   B OE1   1 
ATOM   3020 O  OE2   . GLU   B 2 104 ? 156.001 165.267 110.055 1.00 91.57  ? 104 GLU   B OE2   1 
ATOM   3021 N  N     . ASN   B 2 105 ? 157.919 160.562 106.115 1.00 88.29  ? 105 ASN   B N     1 
ATOM   3022 C  CA    . ASN   B 2 105 ? 158.156 159.284 105.454 1.00 84.62  ? 105 ASN   B CA    1 
ATOM   3023 C  C     . ASN   B 2 105 ? 159.498 159.277 104.736 1.00 82.86  ? 105 ASN   B C     1 
ATOM   3024 O  O     . ASN   B 2 105 ? 160.241 158.290 104.807 1.00 87.34  ? 105 ASN   B O     1 
ATOM   3025 C  CB    . ASN   B 2 105 ? 157.020 158.980 104.479 1.00 78.79  ? 105 ASN   B CB    1 
ATOM   3026 C  CG    . ASN   B 2 105 ? 156.097 157.895 104.985 1.00 81.70  ? 105 ASN   B CG    1 
ATOM   3027 O  OD1   . ASN   B 2 105 ? 156.533 156.783 105.279 1.00 85.57  ? 105 ASN   B OD1   1 
ATOM   3028 N  ND2   . ASN   B 2 105 ? 154.814 158.212 105.092 1.00 78.45  ? 105 ASN   B ND2   1 
ATOM   3029 N  N     . ILE   B 2 106 ? 159.830 160.371 104.047 1.00 77.90  ? 106 ILE   B N     1 
ATOM   3030 C  CA    . ILE   B 2 106 ? 161.103 160.445 103.334 1.00 81.66  ? 106 ILE   B CA    1 
ATOM   3031 C  C     . ILE   B 2 106 ? 162.264 160.312 104.309 1.00 84.31  ? 106 ILE   B C     1 
ATOM   3032 O  O     . ILE   B 2 106 ? 163.200 159.534 104.084 1.00 82.34  ? 106 ILE   B O     1 
ATOM   3033 C  CB    . ILE   B 2 106 ? 161.196 161.754 102.530 1.00 81.90  ? 106 ILE   B CB    1 
ATOM   3034 C  CG1   . ILE   B 2 106 ? 160.242 161.726 101.337 1.00 83.54  ? 106 ILE   B CG1   1 
ATOM   3035 C  CG2   . ILE   B 2 106 ? 162.621 161.990 102.057 1.00 76.96  ? 106 ILE   B CG2   1 
ATOM   3036 C  CD1   . ILE   B 2 106 ? 160.042 163.078 100.694 1.00 79.50  ? 106 ILE   B CD1   1 
ATOM   3037 N  N     . GLU   B 2 107 ? 162.221 161.066 105.412 1.00 95.66  ? 107 GLU   B N     1 
ATOM   3038 C  CA    . GLU   B 2 107 ? 163.339 161.020 106.349 1.00 94.73  ? 107 GLU   B CA    1 
ATOM   3039 C  C     . GLU   B 2 107 ? 163.428 159.666 107.043 1.00 95.57  ? 107 GLU   B C     1 
ATOM   3040 O  O     . GLU   B 2 107 ? 164.534 159.170 107.274 1.00 94.44  ? 107 GLU   B O     1 
ATOM   3041 C  CB    . GLU   B 2 107 ? 163.247 162.158 107.370 1.00 91.84  ? 107 GLU   B CB    1 
ATOM   3042 C  CG    . GLU   B 2 107 ? 161.984 162.195 108.201 1.00 93.94  ? 107 GLU   B CG    1 
ATOM   3043 C  CD    . GLU   B 2 107 ? 162.049 163.227 109.312 1.00 98.66  ? 107 GLU   B CD    1 
ATOM   3044 O  OE1   . GLU   B 2 107 ? 162.714 162.963 110.334 1.00 99.82  ? 107 GLU   B OE1   1 
ATOM   3045 O  OE2   . GLU   B 2 107 ? 161.432 164.303 109.163 1.00 97.71  ? 107 GLU   B OE2   1 
ATOM   3046 N  N     . PHE   B 2 108 ? 162.289 159.038 107.347 1.00 86.85  ? 108 PHE   B N     1 
ATOM   3047 C  CA    . PHE   B 2 108 ? 162.306 157.684 107.894 1.00 81.33  ? 108 PHE   B CA    1 
ATOM   3048 C  C     . PHE   B 2 108 ? 162.991 156.718 106.931 1.00 85.51  ? 108 PHE   B C     1 
ATOM   3049 O  O     . PHE   B 2 108 ? 163.896 155.967 107.321 1.00 86.64  ? 108 PHE   B O     1 
ATOM   3050 C  CB    . PHE   B 2 108 ? 160.869 157.237 108.186 1.00 79.72  ? 108 PHE   B CB    1 
ATOM   3051 C  CG    . PHE   B 2 108 ? 160.751 156.089 109.161 1.00 86.49  ? 108 PHE   B CG    1 
ATOM   3052 C  CD1   . PHE   B 2 108 ? 159.574 155.900 109.867 1.00 89.46  ? 108 PHE   B CD1   1 
ATOM   3053 C  CD2   . PHE   B 2 108 ? 161.798 155.210 109.380 1.00 85.52  ? 108 PHE   B CD2   1 
ATOM   3054 C  CE1   . PHE   B 2 108 ? 159.443 154.857 110.763 1.00 88.15  ? 108 PHE   B CE1   1 
ATOM   3055 C  CE2   . PHE   B 2 108 ? 161.672 154.166 110.275 1.00 85.73  ? 108 PHE   B CE2   1 
ATOM   3056 C  CZ    . PHE   B 2 108 ? 160.494 153.990 110.967 1.00 88.22  ? 108 PHE   B CZ    1 
ATOM   3057 N  N     . LYS   B 2 109 ? 162.577 156.732 105.660 1.00 100.59 ? 109 LYS   B N     1 
ATOM   3058 C  CA    . LYS   B 2 109 ? 163.129 155.787 104.694 1.00 97.45  ? 109 LYS   B CA    1 
ATOM   3059 C  C     . LYS   B 2 109 ? 164.622 156.006 104.485 1.00 99.50  ? 109 LYS   B C     1 
ATOM   3060 O  O     . LYS   B 2 109 ? 165.395 155.042 104.443 1.00 97.85  ? 109 LYS   B O     1 
ATOM   3061 C  CB    . LYS   B 2 109 ? 162.378 155.881 103.365 1.00 99.86  ? 109 LYS   B CB    1 
ATOM   3062 C  CG    . LYS   B 2 109 ? 160.890 155.606 103.468 1.00 99.67  ? 109 LYS   B CG    1 
ATOM   3063 C  CD    . LYS   B 2 109 ? 160.610 154.115 103.516 1.00 100.01 ? 109 LYS   B CD    1 
ATOM   3064 C  CE    . LYS   B 2 109 ? 160.438 153.544 102.120 1.00 99.59  ? 109 LYS   B CE    1 
ATOM   3065 N  NZ    . LYS   B 2 109 ? 159.346 154.231 101.378 1.00 98.35  ? 109 LYS   B NZ    1 
ATOM   3066 N  N     . MET   B 2 110 ? 165.057 157.260 104.358 1.00 107.55 ? 110 MET   B N     1 
ATOM   3067 C  CA    . MET   B 2 110 ? 166.484 157.497 104.165 1.00 107.77 ? 110 MET   B CA    1 
ATOM   3068 C  C     . MET   B 2 110 ? 167.300 157.341 105.443 1.00 107.43 ? 110 MET   B C     1 
ATOM   3069 O  O     . MET   B 2 110 ? 168.524 157.200 105.356 1.00 108.47 ? 110 MET   B O     1 
ATOM   3070 C  CB    . MET   B 2 110 ? 166.738 158.877 103.551 1.00 108.91 ? 110 MET   B CB    1 
ATOM   3071 C  CG    . MET   B 2 110 ? 165.722 159.307 102.513 1.00 107.63 ? 110 MET   B CG    1 
ATOM   3072 S  SD    . MET   B 2 110 ? 166.281 160.699 101.513 1.00 111.13 ? 110 MET   B SD    1 
ATOM   3073 C  CE    . MET   B 2 110 ? 168.044 160.390 101.448 1.00 110.72 ? 110 MET   B CE    1 
ATOM   3074 N  N     . LEU   B 2 111 ? 166.670 157.359 106.619 1.00 94.97  ? 111 LEU   B N     1 
ATOM   3075 C  CA    . LEU   B 2 111 ? 167.368 156.991 107.842 1.00 95.08  ? 111 LEU   B CA    1 
ATOM   3076 C  C     . LEU   B 2 111 ? 167.544 155.487 107.971 1.00 92.70  ? 111 LEU   B C     1 
ATOM   3077 O  O     . LEU   B 2 111 ? 168.577 155.033 108.474 1.00 91.51  ? 111 LEU   B O     1 
ATOM   3078 C  CB    . LEU   B 2 111 ? 166.618 157.521 109.067 1.00 92.56  ? 111 LEU   B CB    1 
ATOM   3079 C  CG    . LEU   B 2 111 ? 166.917 158.962 109.485 1.00 93.91  ? 111 LEU   B CG    1 
ATOM   3080 C  CD1   . LEU   B 2 111 ? 166.135 159.329 110.738 1.00 91.92  ? 111 LEU   B CD1   1 
ATOM   3081 C  CD2   . LEU   B 2 111 ? 168.408 159.165 109.695 1.00 91.95  ? 111 LEU   B CD2   1 
ATOM   3082 N  N     . CYS   B 2 112 ? 166.554 154.707 107.530 1.00 89.19  ? 112 CYS   B N     1 
ATOM   3083 C  CA    . CYS   B 2 112 ? 166.694 153.254 107.570 1.00 86.33  ? 112 CYS   B CA    1 
ATOM   3084 C  C     . CYS   B 2 112 ? 167.801 152.767 106.643 1.00 89.35  ? 112 CYS   B C     1 
ATOM   3085 O  O     . CYS   B 2 112 ? 168.464 151.769 106.946 1.00 87.44  ? 112 CYS   B O     1 
ATOM   3086 C  CB    . CYS   B 2 112 ? 165.367 152.587 107.213 1.00 90.89  ? 112 CYS   B CB    1 
ATOM   3087 S  SG    . CYS   B 2 112 ? 164.233 152.394 108.605 1.00 91.54  ? 112 CYS   B SG    1 
ATOM   3088 N  N     . MET   B 2 113 ? 168.014 153.446 105.514 1.00 107.59 ? 113 MET   B N     1 
ATOM   3089 C  CA    . MET   B 2 113 ? 169.071 153.063 104.586 1.00 108.93 ? 113 MET   B CA    1 
ATOM   3090 C  C     . MET   B 2 113 ? 170.453 153.527 105.027 1.00 109.23 ? 113 MET   B C     1 
ATOM   3091 O  O     . MET   B 2 113 ? 171.450 153.042 104.482 1.00 108.69 ? 113 MET   B O     1 
ATOM   3092 C  CB    . MET   B 2 113 ? 168.773 153.607 103.186 1.00 107.26 ? 113 MET   B CB    1 
ATOM   3093 C  CG    . MET   B 2 113 ? 167.364 153.333 102.694 1.00 107.36 ? 113 MET   B CG    1 
ATOM   3094 S  SD    . MET   B 2 113 ? 167.319 152.822 100.965 1.00 113.95 ? 113 MET   B SD    1 
ATOM   3095 C  CE    . MET   B 2 113 ? 165.677 153.360 100.496 1.00 108.14 ? 113 MET   B CE    1 
ATOM   3096 N  N     . GLY   B 2 114 ? 170.541 154.442 105.988 1.00 102.36 ? 114 GLY   B N     1 
ATOM   3097 C  CA    . GLY   B 2 114 ? 171.831 154.861 106.502 1.00 102.46 ? 114 GLY   B CA    1 
ATOM   3098 C  C     . GLY   B 2 114 ? 172.398 156.113 105.864 1.00 101.84 ? 114 GLY   B C     1 
ATOM   3099 O  O     . GLY   B 2 114 ? 173.544 156.117 105.405 1.00 101.54 ? 114 GLY   B O     1 
ATOM   3100 N  N     . PHE   B 2 115 ? 171.607 157.181 105.825 1.00 119.91 ? 115 PHE   B N     1 
ATOM   3101 C  CA    . PHE   B 2 115 ? 172.054 158.477 105.335 1.00 123.07 ? 115 PHE   B CA    1 
ATOM   3102 C  C     . PHE   B 2 115 ? 172.037 159.492 106.469 1.00 122.30 ? 115 PHE   B C     1 
ATOM   3103 O  O     . PHE   B 2 115 ? 171.121 159.496 107.297 1.00 120.20 ? 115 PHE   B O     1 
ATOM   3104 C  CB    . PHE   B 2 115 ? 171.174 158.973 104.183 1.00 122.11 ? 115 PHE   B CB    1 
ATOM   3105 C  CG    . PHE   B 2 115 ? 171.223 158.102 102.960 1.00 122.17 ? 115 PHE   B CG    1 
ATOM   3106 C  CD1   . PHE   B 2 115 ? 172.309 158.153 102.102 1.00 122.32 ? 115 PHE   B CD1   1 
ATOM   3107 C  CD2   . PHE   B 2 115 ? 170.179 157.244 102.660 1.00 122.55 ? 115 PHE   B CD2   1 
ATOM   3108 C  CE1   . PHE   B 2 115 ? 172.356 157.358 100.974 1.00 122.80 ? 115 PHE   B CE1   1 
ATOM   3109 C  CE2   . PHE   B 2 115 ? 170.221 156.447 101.532 1.00 123.01 ? 115 PHE   B CE2   1 
ATOM   3110 C  CZ    . PHE   B 2 115 ? 171.311 156.504 100.689 1.00 122.14 ? 115 PHE   B CZ    1 
ATOM   3111 N  N     . LYS   B 2 116 ? 173.054 160.349 106.503 1.00 120.98 ? 116 LYS   B N     1 
ATOM   3112 C  CA    . LYS   B 2 116 ? 173.110 161.399 107.507 1.00 119.63 ? 116 LYS   B CA    1 
ATOM   3113 C  C     . LYS   B 2 116 ? 172.060 162.468 107.216 1.00 120.13 ? 116 LYS   B C     1 
ATOM   3114 O  O     . LYS   B 2 116 ? 171.549 162.590 106.099 1.00 121.81 ? 116 LYS   B O     1 
ATOM   3115 C  CB    . LYS   B 2 116 ? 174.505 162.021 107.560 1.00 119.19 ? 116 LYS   B CB    1 
ATOM   3116 C  CG    . LYS   B 2 116 ? 175.625 161.014 107.788 1.00 120.36 ? 116 LYS   B CG    1 
ATOM   3117 C  CD    . LYS   B 2 116 ? 175.314 160.085 108.954 1.00 118.88 ? 116 LYS   B CD    1 
ATOM   3118 C  CE    . LYS   B 2 116 ? 175.453 160.797 110.290 1.00 118.19 ? 116 LYS   B CE    1 
ATOM   3119 N  NZ    . LYS   B 2 116 ? 176.868 161.151 110.591 1.00 119.86 ? 116 LYS   B NZ    1 
ATOM   3120 N  N     . ARG   B 2 117 ? 171.741 163.253 108.249 1.00 115.16 ? 117 ARG   B N     1 
ATOM   3121 C  CA    . ARG   B 2 117 ? 170.652 164.221 108.143 1.00 115.11 ? 117 ARG   B CA    1 
ATOM   3122 C  C     . ARG   B 2 117 ? 170.934 165.291 107.095 1.00 114.82 ? 117 ARG   B C     1 
ATOM   3123 O  O     . ARG   B 2 117 ? 170.017 165.703 106.373 1.00 113.94 ? 117 ARG   B O     1 
ATOM   3124 C  CB    . ARG   B 2 117 ? 170.392 164.864 109.504 1.00 116.38 ? 117 ARG   B CB    1 
ATOM   3125 C  CG    . ARG   B 2 117 ? 168.997 165.447 109.654 1.00 117.07 ? 117 ARG   B CG    1 
ATOM   3126 C  CD    . ARG   B 2 117 ? 168.859 166.219 110.954 1.00 116.32 ? 117 ARG   B CD    1 
ATOM   3127 N  NE    . ARG   B 2 117 ? 167.480 166.241 111.428 1.00 116.78 ? 117 ARG   B NE    1 
ATOM   3128 C  CZ    . ARG   B 2 117 ? 167.076 165.725 112.581 1.00 117.47 ? 117 ARG   B CZ    1 
ATOM   3129 N  NH1   . ARG   B 2 117 ? 167.922 165.133 113.408 1.00 117.22 ? 117 ARG   B NH1   1 
ATOM   3130 N  NH2   . ARG   B 2 117 ? 165.790 165.804 112.912 1.00 115.60 ? 117 ARG   B NH2   1 
ATOM   3131 N  N     . LYS   B 2 118 ? 172.181 165.759 107.000 1.00 115.99 ? 118 LYS   B N     1 
ATOM   3132 C  CA    . LYS   B 2 118 ? 172.518 166.749 105.982 1.00 116.77 ? 118 LYS   B CA    1 
ATOM   3133 C  C     . LYS   B 2 118 ? 172.331 166.184 104.579 1.00 117.34 ? 118 LYS   B C     1 
ATOM   3134 O  O     . LYS   B 2 118 ? 171.828 166.877 103.687 1.00 117.26 ? 118 LYS   B O     1 
ATOM   3135 C  CB    . LYS   B 2 118 ? 173.950 167.242 106.178 1.00 117.90 ? 118 LYS   B CB    1 
ATOM   3136 C  CG    . LYS   B 2 118 ? 174.269 168.522 105.422 1.00 118.23 ? 118 LYS   B CG    1 
ATOM   3137 C  CD    . LYS   B 2 118 ? 173.659 169.737 106.104 1.00 117.95 ? 118 LYS   B CD    1 
ATOM   3138 C  CE    . LYS   B 2 118 ? 174.183 169.901 107.521 1.00 117.62 ? 118 LYS   B CE    1 
ATOM   3139 N  NZ    . LYS   B 2 118 ? 173.096 170.237 108.481 1.00 116.48 ? 118 LYS   B NZ    1 
ATOM   3140 N  N     . GLU   B 2 119 ? 172.726 164.926 104.365 1.00 116.42 ? 119 GLU   B N     1 
ATOM   3141 C  CA    . GLU   B 2 119 ? 172.493 164.290 103.072 1.00 115.79 ? 119 GLU   B CA    1 
ATOM   3142 C  C     . GLU   B 2 119 ? 171.003 164.167 102.779 1.00 113.84 ? 119 GLU   B C     1 
ATOM   3143 O  O     . GLU   B 2 119 ? 170.573 164.350 101.635 1.00 115.62 ? 119 GLU   B O     1 
ATOM   3144 C  CB    . GLU   B 2 119 ? 173.163 162.917 103.028 1.00 115.40 ? 119 GLU   B CB    1 
ATOM   3145 C  CG    . GLU   B 2 119 ? 174.604 162.907 103.509 1.00 115.87 ? 119 GLU   B CG    1 
ATOM   3146 C  CD    . GLU   B 2 119 ? 175.388 161.728 102.966 1.00 117.27 ? 119 GLU   B CD    1 
ATOM   3147 O  OE1   . GLU   B 2 119 ? 175.676 161.714 101.751 1.00 114.91 ? 119 GLU   B OE1   1 
ATOM   3148 O  OE2   . GLU   B 2 119 ? 175.716 160.815 103.753 1.00 117.64 ? 119 GLU   B OE2   1 
ATOM   3149 N  N     . ILE   B 2 120 ? 170.202 163.855 103.801 1.00 106.21 ? 120 ILE   B N     1 
ATOM   3150 C  CA    . ILE   B 2 120 ? 168.756 163.762 103.615 1.00 106.33 ? 120 ILE   B CA    1 
ATOM   3151 C  C     . ILE   B 2 120 ? 168.184 165.109 103.194 1.00 106.31 ? 120 ILE   B C     1 
ATOM   3152 O  O     . ILE   B 2 120 ? 167.368 165.193 102.267 1.00 105.97 ? 120 ILE   B O     1 
ATOM   3153 C  CB    . ILE   B 2 120 ? 168.088 163.241 104.902 1.00 105.93 ? 120 ILE   B CB    1 
ATOM   3154 C  CG1   . ILE   B 2 120 ? 168.525 161.803 105.186 1.00 107.27 ? 120 ILE   B CG1   1 
ATOM   3155 C  CG2   . ILE   B 2 120 ? 166.574 163.337 104.795 1.00 104.49 ? 120 ILE   B CG2   1 
ATOM   3156 C  CD1   . ILE   B 2 120 ? 167.757 161.143 106.309 1.00 106.77 ? 120 ILE   B CD1   1 
ATOM   3157 N  N     . LYS   B 2 121 ? 168.606 166.185 103.864 1.00 100.95 ? 121 LYS   B N     1 
ATOM   3158 C  CA    . LYS   B 2 121 ? 168.102 167.510 103.518 1.00 100.63 ? 121 LYS   B CA    1 
ATOM   3159 C  C     . LYS   B 2 121 ? 168.583 167.956 102.144 1.00 98.80  ? 121 LYS   B C     1 
ATOM   3160 O  O     . LYS   B 2 121 ? 167.872 168.691 101.449 1.00 96.67  ? 121 LYS   B O     1 
ATOM   3161 C  CB    . LYS   B 2 121 ? 168.515 168.527 104.582 1.00 100.31 ? 121 LYS   B CB    1 
ATOM   3162 C  CG    . LYS   B 2 121 ? 167.473 169.602 104.842 1.00 99.25  ? 121 LYS   B CG    1 
ATOM   3163 C  CD    . LYS   B 2 121 ? 167.663 170.238 106.208 1.00 98.33  ? 121 LYS   B CD    1 
ATOM   3164 C  CE    . LYS   B 2 121 ? 168.885 171.140 106.229 1.00 99.55  ? 121 LYS   B CE    1 
ATOM   3165 N  NZ    . LYS   B 2 121 ? 169.006 171.940 104.979 1.00 98.68  ? 121 LYS   B NZ    1 
ATOM   3166 N  N     . ALA   B 2 122 ? 169.781 167.533 101.738 1.00 99.44  ? 122 ALA   B N     1 
ATOM   3167 C  CA    . ALA   B 2 122 ? 170.276 167.873 100.409 1.00 100.81 ? 122 ALA   B CA    1 
ATOM   3168 C  C     . ALA   B 2 122 ? 169.538 167.106 99.318  1.00 103.22 ? 122 ALA   B C     1 
ATOM   3169 O  O     . ALA   B 2 122 ? 169.292 167.647 98.234  1.00 101.82 ? 122 ALA   B O     1 
ATOM   3170 C  CB    . ALA   B 2 122 ? 171.779 167.606 100.323 1.00 97.90  ? 122 ALA   B CB    1 
ATOM   3171 N  N     . MET   B 2 123 ? 169.186 165.847 99.580  1.00 109.04 ? 123 MET   B N     1 
ATOM   3172 C  CA    . MET   B 2 123 ? 168.516 165.009 98.595  1.00 103.80 ? 123 MET   B CA    1 
ATOM   3173 C  C     . MET   B 2 123 ? 167.005 165.200 98.562  1.00 102.51 ? 123 MET   B C     1 
ATOM   3174 O  O     . MET   B 2 123 ? 166.365 164.754 97.605  1.00 107.32 ? 123 MET   B O     1 
ATOM   3175 C  CB    . MET   B 2 123 ? 168.829 163.532 98.862  1.00 104.16 ? 123 MET   B CB    1 
ATOM   3176 C  CG    . MET   B 2 123 ? 169.916 162.953 97.974  1.00 105.13 ? 123 MET   B CG    1 
ATOM   3177 S  SD    . MET   B 2 123 ? 169.886 161.151 97.941  1.00 110.51 ? 123 MET   B SD    1 
ATOM   3178 C  CE    . MET   B 2 123 ? 171.638 160.781 97.937  1.00 105.72 ? 123 MET   B CE    1 
ATOM   3179 N  N     . THR   B 2 124 ? 166.423 165.837 99.578  1.00 85.33  ? 124 THR   B N     1 
ATOM   3180 C  CA    . THR   B 2 124 ? 164.975 166.045 99.587  1.00 88.03  ? 124 THR   B CA    1 
ATOM   3181 C  C     . THR   B 2 124 ? 164.457 166.842 98.393  1.00 90.63  ? 124 THR   B C     1 
ATOM   3182 O  O     . THR   B 2 124 ? 163.437 166.432 97.811  1.00 90.39  ? 124 THR   B O     1 
ATOM   3183 C  CB    . THR   B 2 124 ? 164.560 166.703 100.908 1.00 88.87  ? 124 THR   B CB    1 
ATOM   3184 O  OG1   . THR   B 2 124 ? 165.188 166.022 102.000 1.00 89.57  ? 124 THR   B OG1   1 
ATOM   3185 C  CG2   . THR   B 2 124 ? 163.053 166.638 101.081 1.00 89.42  ? 124 THR   B CG2   1 
ATOM   3186 N  N     . PRO   B 2 125 ? 165.064 167.967 97.984  1.00 105.33 ? 125 PRO   B N     1 
ATOM   3187 C  CA    . PRO   B 2 125 ? 164.479 168.731 96.867  1.00 105.50 ? 125 PRO   B CA    1 
ATOM   3188 C  C     . PRO   B 2 125 ? 164.381 167.953 95.566  1.00 104.96 ? 125 PRO   B C     1 
ATOM   3189 O  O     . PRO   B 2 125 ? 163.433 168.175 94.803  1.00 103.59 ? 125 PRO   B O     1 
ATOM   3190 C  CB    . PRO   B 2 125 ? 165.423 169.936 96.736  1.00 106.00 ? 125 PRO   B CB    1 
ATOM   3191 C  CG    . PRO   B 2 125 ? 166.699 169.477 97.346  1.00 104.92 ? 125 PRO   B CG    1 
ATOM   3192 C  CD    . PRO   B 2 125 ? 166.261 168.647 98.509  1.00 104.58 ? 125 PRO   B CD    1 
ATOM   3193 N  N     . LYS   B 2 126 ? 165.325 167.052 95.283  1.00 90.30  ? 126 LYS   B N     1 
ATOM   3194 C  CA    . LYS   B 2 126 ? 165.215 166.229 94.082  1.00 89.95  ? 126 LYS   B CA    1 
ATOM   3195 C  C     . LYS   B 2 126 ? 163.985 165.331 94.141  1.00 91.90  ? 126 LYS   B C     1 
ATOM   3196 O  O     . LYS   B 2 126 ? 163.260 165.192 93.147  1.00 93.42  ? 126 LYS   B O     1 
ATOM   3197 C  CB    . LYS   B 2 126 ? 166.483 165.397 93.900  1.00 90.74  ? 126 LYS   B CB    1 
ATOM   3198 C  CG    . LYS   B 2 126 ? 167.550 166.073 93.056  1.00 94.59  ? 126 LYS   B CG    1 
ATOM   3199 C  CD    . LYS   B 2 126 ? 168.770 165.184 92.893  1.00 94.62  ? 126 LYS   B CD    1 
ATOM   3200 C  CE    . LYS   B 2 126 ? 169.555 165.080 94.190  1.00 94.40  ? 126 LYS   B CE    1 
ATOM   3201 N  NZ    . LYS   B 2 126 ? 169.747 166.410 94.830  1.00 96.57  ? 126 LYS   B NZ    1 
ATOM   3202 N  N     . ILE   B 2 127 ? 163.731 164.725 95.302  1.00 73.21  ? 127 ILE   B N     1 
ATOM   3203 C  CA    . ILE   B 2 127 ? 162.533 163.912 95.483  1.00 67.36  ? 127 ILE   B CA    1 
ATOM   3204 C  C     . ILE   B 2 127 ? 161.281 164.765 95.321  1.00 68.32  ? 127 ILE   B C     1 
ATOM   3205 O  O     . ILE   B 2 127 ? 160.305 164.348 94.684  1.00 72.46  ? 127 ILE   B O     1 
ATOM   3206 C  CB    . ILE   B 2 127 ? 162.572 163.214 96.854  1.00 67.63  ? 127 ILE   B CB    1 
ATOM   3207 C  CG1   . ILE   B 2 127 ? 163.622 162.103 96.858  1.00 66.36  ? 127 ILE   B CG1   1 
ATOM   3208 C  CG2   . ILE   B 2 127 ? 161.207 162.662 97.220  1.00 69.53  ? 127 ILE   B CG2   1 
ATOM   3209 C  CD1   . ILE   B 2 127 ? 164.181 161.794 98.223  1.00 67.07  ? 127 ILE   B CD1   1 
ATOM   3210 N  N     . ILE   B 2 128 ? 161.292 165.973 95.889  1.00 79.91  ? 128 ILE   B N     1 
ATOM   3211 C  CA    . ILE   B 2 128 ? 160.136 166.861 95.784  1.00 82.18  ? 128 ILE   B CA    1 
ATOM   3212 C  C     . ILE   B 2 128 ? 159.853 167.199 94.327  1.00 84.93  ? 128 ILE   B C     1 
ATOM   3213 O  O     . ILE   B 2 128 ? 158.699 167.189 93.882  1.00 84.49  ? 128 ILE   B O     1 
ATOM   3214 C  CB    . ILE   B 2 128 ? 160.364 168.133 96.622  1.00 86.23  ? 128 ILE   B CB    1 
ATOM   3215 C  CG1   . ILE   B 2 128 ? 160.602 167.777 98.092  1.00 84.54  ? 128 ILE   B CG1   1 
ATOM   3216 C  CG2   . ILE   B 2 128 ? 159.190 169.094 96.467  1.00 86.70  ? 128 ILE   B CG2   1 
ATOM   3217 C  CD1   . ILE   B 2 128 ? 159.361 167.792 98.944  1.00 83.62  ? 128 ILE   B CD1   1 
ATOM   3218 N  N     . GLU   B 2 129 ? 160.901 167.507 93.561  1.00 97.13  ? 129 GLU   B N     1 
ATOM   3219 C  CA    . GLU   B 2 129 ? 160.716 167.871 92.160  1.00 96.31  ? 129 GLU   B CA    1 
ATOM   3220 C  C     . GLU   B 2 129 ? 160.257 166.680 91.328  1.00 98.31  ? 129 GLU   B C     1 
ATOM   3221 O  O     . GLU   B 2 129 ? 159.431 166.834 90.421  1.00 96.02  ? 129 GLU   B O     1 
ATOM   3222 C  CB    . GLU   B 2 129 ? 162.010 168.456 91.595  1.00 95.37  ? 129 GLU   B CB    1 
ATOM   3223 C  CG    . GLU   B 2 129 ? 161.799 169.641 90.666  1.00 98.54  ? 129 GLU   B CG    1 
ATOM   3224 C  CD    . GLU   B 2 129 ? 161.425 170.909 91.409  1.00 102.73 ? 129 GLU   B CD    1 
ATOM   3225 O  OE1   . GLU   B 2 129 ? 161.627 170.963 92.641  1.00 103.80 ? 129 GLU   B OE1   1 
ATOM   3226 O  OE2   . GLU   B 2 129 ? 160.928 171.855 90.762  1.00 101.23 ? 129 GLU   B OE2   1 
ATOM   3227 N  N     . PHE   B 2 130 ? 160.779 165.484 91.615  1.00 87.02  ? 130 PHE   B N     1 
ATOM   3228 C  CA    . PHE   B 2 130 ? 160.405 164.315 90.826  1.00 81.32  ? 130 PHE   B CA    1 
ATOM   3229 C  C     . PHE   B 2 130 ? 159.004 163.812 91.156  1.00 81.90  ? 130 PHE   B C     1 
ATOM   3230 O  O     . PHE   B 2 130 ? 158.342 163.233 90.288  1.00 81.09  ? 130 PHE   B O     1 
ATOM   3231 C  CB    . PHE   B 2 130 ? 161.421 163.191 91.033  1.00 78.34  ? 130 PHE   B CB    1 
ATOM   3232 C  CG    . PHE   B 2 130 ? 161.369 162.124 89.976  1.00 84.89  ? 130 PHE   B CG    1 
ATOM   3233 C  CD1   . PHE   B 2 130 ? 161.992 162.308 88.754  1.00 84.38  ? 130 PHE   B CD1   1 
ATOM   3234 C  CD2   . PHE   B 2 130 ? 160.693 160.937 90.202  1.00 88.21  ? 130 PHE   B CD2   1 
ATOM   3235 C  CE1   . PHE   B 2 130 ? 161.945 161.328 87.780  1.00 83.85  ? 130 PHE   B CE1   1 
ATOM   3236 C  CE2   . PHE   B 2 130 ? 160.642 159.953 89.232  1.00 84.06  ? 130 PHE   B CE2   1 
ATOM   3237 C  CZ    . PHE   B 2 130 ? 161.270 160.150 88.021  1.00 81.80  ? 130 PHE   B CZ    1 
ATOM   3238 N  N     . SER   B 2 131 ? 158.536 164.015 92.390  1.00 77.15  ? 131 SER   B N     1 
ATOM   3239 C  CA    . SER   B 2 131 ? 157.241 163.465 92.781  1.00 70.69  ? 131 SER   B CA    1 
ATOM   3240 C  C     . SER   B 2 131 ? 156.077 164.250 92.187  1.00 76.15  ? 131 SER   B C     1 
ATOM   3241 O  O     . SER   B 2 131 ? 155.000 163.681 91.975  1.00 81.06  ? 131 SER   B O     1 
ATOM   3242 C  CB    . SER   B 2 131 ? 157.124 163.429 94.304  1.00 71.75  ? 131 SER   B CB    1 
ATOM   3243 O  OG    . SER   B 2 131 ? 158.294 162.890 94.891  1.00 77.69  ? 131 SER   B OG    1 
ATOM   3244 N  N     . GLU   B 2 132 ? 156.271 165.542 91.914  1.00 88.63  ? 132 GLU   B N     1 
ATOM   3245 C  CA    . GLU   B 2 132 ? 155.193 166.432 91.470  1.00 89.23  ? 132 GLU   B CA    1 
ATOM   3246 C  C     . GLU   B 2 132 ? 154.025 166.410 92.451  1.00 93.08  ? 132 GLU   B C     1 
ATOM   3247 O  O     . GLU   B 2 132 ? 152.855 166.414 92.060  1.00 88.74  ? 132 GLU   B O     1 
ATOM   3248 C  CB    . GLU   B 2 132 ? 154.713 166.080 90.061  1.00 88.59  ? 132 GLU   B CB    1 
ATOM   3249 C  CG    . GLU   B 2 132 ? 155.811 165.923 89.034  1.00 92.70  ? 132 GLU   B CG    1 
ATOM   3250 C  CD    . GLU   B 2 132 ? 155.625 164.683 88.188  1.00 94.22  ? 132 GLU   B CD    1 
ATOM   3251 O  OE1   . GLU   B 2 132 ? 154.565 164.035 88.309  1.00 91.46  ? 132 GLU   B OE1   1 
ATOM   3252 O  OE2   . GLU   B 2 132 ? 156.534 164.358 87.400  1.00 95.16  ? 132 GLU   B OE2   1 
ATOM   3253 N  N     . LEU   B 2 133 ? 154.344 166.387 93.742  1.00 85.36  ? 133 LEU   B N     1 
ATOM   3254 C  CA    . LEU   B 2 133 ? 153.327 166.333 94.782  1.00 80.77  ? 133 LEU   B CA    1 
ATOM   3255 C  C     . LEU   B 2 133 ? 152.817 167.705 95.192  1.00 84.79  ? 133 LEU   B C     1 
ATOM   3256 O  O     . LEU   B 2 133 ? 151.638 167.837 95.536  1.00 85.18  ? 133 LEU   B O     1 
ATOM   3257 C  CB    . LEU   B 2 133 ? 153.873 165.604 96.015  1.00 81.21  ? 133 LEU   B CB    1 
ATOM   3258 C  CG    . LEU   B 2 133 ? 153.742 164.080 95.982  1.00 80.23  ? 133 LEU   B CG    1 
ATOM   3259 C  CD1   . LEU   B 2 133 ? 154.405 163.450 97.192  1.00 78.44  ? 133 LEU   B CD1   1 
ATOM   3260 C  CD2   . LEU   B 2 133 ? 152.284 163.673 95.899  1.00 75.74  ? 133 LEU   B CD2   1 
ATOM   3261 N  N     . GLY   B 2 134 ? 153.668 168.726 95.151  1.00 85.10  ? 134 GLY   B N     1 
ATOM   3262 C  CA    . GLY   B 2 134 ? 153.226 170.067 95.494  1.00 81.64  ? 134 GLY   B CA    1 
ATOM   3263 C  C     . GLY   B 2 134 ? 152.846 170.173 96.957  1.00 85.45  ? 134 GLY   B C     1 
ATOM   3264 O  O     . GLY   B 2 134 ? 153.457 169.544 97.829  1.00 84.77  ? 134 GLY   B O     1 
ATOM   3265 N  N     . GLU   B 2 135 ? 151.800 170.960 97.227  1.00 103.36 ? 135 GLU   B N     1 
ATOM   3266 C  CA    . GLU   B 2 135 ? 151.389 171.232 98.602  1.00 104.13 ? 135 GLU   B CA    1 
ATOM   3267 C  C     . GLU   B 2 135 ? 151.146 169.944 99.375  1.00 103.09 ? 135 GLU   B C     1 
ATOM   3268 O  O     . GLU   B 2 135 ? 151.400 169.876 100.585 1.00 105.39 ? 135 GLU   B O     1 
ATOM   3269 C  CB    . GLU   B 2 135 ? 150.125 172.091 98.604  1.00 102.46 ? 135 GLU   B CB    1 
ATOM   3270 C  CG    . GLU   B 2 135 ? 150.105 173.175 97.542  1.00 104.30 ? 135 GLU   B CG    1 
ATOM   3271 C  CD    . GLU   B 2 135 ? 150.016 174.566 98.131  1.00 106.24 ? 135 GLU   B CD    1 
ATOM   3272 O  OE1   . GLU   B 2 135 ? 150.056 174.689 99.372  1.00 106.92 ? 135 GLU   B OE1   1 
ATOM   3273 O  OE2   . GLU   B 2 135 ? 149.902 175.536 97.352  1.00 105.06 ? 135 GLU   B OE2   1 
ATOM   3274 N  N     . PHE   B 2 136 ? 150.688 168.899 98.684  1.00 79.03  ? 136 PHE   B N     1 
ATOM   3275 C  CA    . PHE   B 2 136 ? 150.289 167.676 99.368  1.00 74.22  ? 136 PHE   B CA    1 
ATOM   3276 C  C     . PHE   B 2 136 ? 151.478 166.950 99.979  1.00 73.27  ? 136 PHE   B C     1 
ATOM   3277 O  O     . PHE   B 2 136 ? 151.288 165.996 100.740 1.00 79.38  ? 136 PHE   B O     1 
ATOM   3278 C  CB    . PHE   B 2 136 ? 149.536 166.760 98.405  1.00 74.66  ? 136 PHE   B CB    1 
ATOM   3279 C  CG    . PHE   B 2 136 ? 148.044 166.880 98.505  1.00 75.61  ? 136 PHE   B CG    1 
ATOM   3280 C  CD1   . PHE   B 2 136 ? 147.360 166.301 99.560  1.00 75.63  ? 136 PHE   B CD1   1 
ATOM   3281 C  CD2   . PHE   B 2 136 ? 147.325 167.578 97.551  1.00 71.64  ? 136 PHE   B CD2   1 
ATOM   3282 C  CE1   . PHE   B 2 136 ? 145.988 166.412 99.659  1.00 72.62  ? 136 PHE   B CE1   1 
ATOM   3283 C  CE2   . PHE   B 2 136 ? 145.953 167.692 97.645  1.00 71.18  ? 136 PHE   B CE2   1 
ATOM   3284 C  CZ    . PHE   B 2 136 ? 145.284 167.109 98.700  1.00 71.72  ? 136 PHE   B CZ    1 
ATOM   3285 N  N     . ILE   B 2 137 ? 152.707 167.375 99.672  1.00 72.50  ? 137 ILE   B N     1 
ATOM   3286 C  CA    . ILE   B 2 137 ? 153.856 166.765 100.338 1.00 75.73  ? 137 ILE   B CA    1 
ATOM   3287 C  C     . ILE   B 2 137 ? 153.818 167.071 101.831 1.00 78.81  ? 137 ILE   B C     1 
ATOM   3288 O  O     . ILE   B 2 137 ? 154.387 166.336 102.647 1.00 83.44  ? 137 ILE   B O     1 
ATOM   3289 C  CB    . ILE   B 2 137 ? 155.178 167.228 99.696  1.00 75.77  ? 137 ILE   B CB    1 
ATOM   3290 C  CG1   . ILE   B 2 137 ? 156.344 166.408 100.245 1.00 72.95  ? 137 ILE   B CG1   1 
ATOM   3291 C  CG2   . ILE   B 2 137 ? 155.443 168.686 100.002 1.00 77.61  ? 137 ILE   B CG2   1 
ATOM   3292 C  CD1   . ILE   B 2 137 ? 156.733 165.236 99.374  1.00 74.90  ? 137 ILE   B CD1   1 
ATOM   3293 N  N     . TYR   B 2 138 ? 153.133 168.151 102.215 1.00 82.37  ? 138 TYR   B N     1 
ATOM   3294 C  CA    . TYR   B 2 138 ? 153.060 168.507 103.628 1.00 79.81  ? 138 TYR   B CA    1 
ATOM   3295 C  C     . TYR   B 2 138 ? 151.870 167.838 104.305 1.00 80.46  ? 138 TYR   B C     1 
ATOM   3296 O  O     . TYR   B 2 138 ? 151.833 167.714 105.534 1.00 80.57  ? 138 TYR   B O     1 
ATOM   3297 C  CB    . TYR   B 2 138 ? 152.988 170.026 103.775 1.00 78.76  ? 138 TYR   B CB    1 
ATOM   3298 C  CG    . TYR   B 2 138 ? 154.276 170.720 103.397 1.00 83.60  ? 138 TYR   B CG    1 
ATOM   3299 C  CD1   . TYR   B 2 138 ? 155.457 170.454 104.076 1.00 83.02  ? 138 TYR   B CD1   1 
ATOM   3300 C  CD2   . TYR   B 2 138 ? 154.315 171.630 102.349 1.00 84.07  ? 138 TYR   B CD2   1 
ATOM   3301 C  CE1   . TYR   B 2 138 ? 156.637 171.082 103.730 1.00 82.50  ? 138 TYR   B CE1   1 
ATOM   3302 C  CE2   . TYR   B 2 138 ? 155.490 172.262 101.995 1.00 83.49  ? 138 TYR   B CE2   1 
ATOM   3303 C  CZ    . TYR   B 2 138 ? 156.648 171.984 102.689 1.00 82.83  ? 138 TYR   B CZ    1 
ATOM   3304 O  OH    . TYR   B 2 138 ? 157.822 172.611 102.340 1.00 81.98  ? 138 TYR   B OH    1 
ATOM   3305 N  N     . GLN   B 2 139 ? 150.889 167.401 103.519 1.00 85.78  ? 139 GLN   B N     1 
ATOM   3306 C  CA    . GLN   B 2 139 ? 149.727 166.714 104.054 1.00 82.45  ? 139 GLN   B CA    1 
ATOM   3307 C  C     . GLN   B 2 139 ? 150.078 165.274 104.427 1.00 83.55  ? 139 GLN   B C     1 
ATOM   3308 O  O     . GLN   B 2 139 ? 151.077 164.726 103.956 1.00 83.65  ? 139 GLN   B O     1 
ATOM   3309 C  CB    . GLN   B 2 139 ? 148.592 166.738 103.033 1.00 81.39  ? 139 GLN   B CB    1 
ATOM   3310 C  CG    . GLN   B 2 139 ? 148.269 168.124 102.502 1.00 82.75  ? 139 GLN   B CG    1 
ATOM   3311 C  CD    . GLN   B 2 139 ? 147.975 169.118 103.607 1.00 86.62  ? 139 GLN   B CD    1 
ATOM   3312 O  OE1   . GLN   B 2 139 ? 147.171 168.851 104.500 1.00 85.51  ? 139 GLN   B OE1   1 
ATOM   3313 N  NE2   . GLN   B 2 139 ? 148.626 170.274 103.553 1.00 86.36  ? 139 GLN   B NE2   1 
ATOM   3314 N  N     . PRO   B 2 140 ? 149.274 164.642 105.283 1.00 83.62  ? 140 PRO   B N     1 
ATOM   3315 C  CA    . PRO   B 2 140 ? 149.533 163.241 105.636 1.00 86.03  ? 140 PRO   B CA    1 
ATOM   3316 C  C     . PRO   B 2 140 ? 149.382 162.314 104.440 1.00 86.49  ? 140 PRO   B C     1 
ATOM   3317 O  O     . PRO   B 2 140 ? 148.647 162.596 103.490 1.00 85.83  ? 140 PRO   B O     1 
ATOM   3318 C  CB    . PRO   B 2 140 ? 148.476 162.942 106.707 1.00 84.59  ? 140 PRO   B CB    1 
ATOM   3319 C  CG    . PRO   B 2 140 ? 148.100 164.280 107.248 1.00 87.41  ? 140 PRO   B CG    1 
ATOM   3320 C  CD    . PRO   B 2 140 ? 148.165 165.202 106.074 1.00 84.42  ? 140 PRO   B CD    1 
ATOM   3321 N  N     . VAL   B 2 141 ? 150.100 161.190 104.502 1.00 74.93  ? 141 VAL   B N     1 
ATOM   3322 C  CA    . VAL   B 2 141 ? 150.127 160.247 103.386 1.00 72.76  ? 141 VAL   B CA    1 
ATOM   3323 C  C     . VAL   B 2 141 ? 148.754 159.613 103.182 1.00 72.07  ? 141 VAL   B C     1 
ATOM   3324 O  O     . VAL   B 2 141 ? 148.367 159.288 102.053 1.00 74.16  ? 141 VAL   B O     1 
ATOM   3325 C  CB    . VAL   B 2 141 ? 151.227 159.191 103.615 1.00 67.04  ? 141 VAL   B CB    1 
ATOM   3326 C  CG1   . VAL   B 2 141 ? 150.890 157.877 102.927 1.00 69.43  ? 141 VAL   B CG1   1 
ATOM   3327 C  CG2   . VAL   B 2 141 ? 152.564 159.715 103.125 1.00 66.42  ? 141 VAL   B CG2   1 
ATOM   3328 N  N     . LYS   B 2 142 ? 147.987 159.451 104.262 1.00 72.11  ? 142 LYS   B N     1 
ATOM   3329 C  CA    . LYS   B 2 142 ? 146.674 158.823 104.144 1.00 72.00  ? 142 LYS   B CA    1 
ATOM   3330 C  C     . LYS   B 2 142 ? 145.733 159.647 103.268 1.00 72.85  ? 142 LYS   B C     1 
ATOM   3331 O  O     . LYS   B 2 142 ? 144.744 159.122 102.744 1.00 75.60  ? 142 LYS   B O     1 
ATOM   3332 C  CB    . LYS   B 2 142 ? 146.073 158.605 105.534 1.00 77.15  ? 142 LYS   B CB    1 
ATOM   3333 C  CG    . LYS   B 2 142 ? 144.943 159.554 105.894 1.00 78.51  ? 142 LYS   B CG    1 
ATOM   3334 C  CD    . LYS   B 2 142 ? 144.316 159.182 107.226 1.00 77.30  ? 142 LYS   B CD    1 
ATOM   3335 C  CE    . LYS   B 2 142 ? 145.311 159.331 108.363 1.00 76.11  ? 142 LYS   B CE    1 
ATOM   3336 N  NZ    . LYS   B 2 142 ? 145.755 160.741 108.524 1.00 74.85  ? 142 LYS   B NZ    1 
ATOM   3337 N  N     . LYS   B 2 143 ? 146.026 160.938 103.091 1.00 70.05  ? 143 LYS   B N     1 
ATOM   3338 C  CA    . LYS   B 2 143 ? 145.204 161.767 102.213 1.00 68.56  ? 143 LYS   B CA    1 
ATOM   3339 C  C     . LYS   B 2 143 ? 145.550 161.537 100.746 1.00 70.47  ? 143 LYS   B C     1 
ATOM   3340 O  O     . LYS   B 2 143 ? 144.816 161.977 99.854  1.00 69.75  ? 143 LYS   B O     1 
ATOM   3341 C  CB    . LYS   B 2 143 ? 145.370 163.244 102.571 1.00 69.22  ? 143 LYS   B CB    1 
ATOM   3342 C  CG    . LYS   B 2 143 ? 145.392 163.544 104.060 1.00 70.60  ? 143 LYS   B CG    1 
ATOM   3343 C  CD    . LYS   B 2 143 ? 144.013 163.390 104.679 1.00 70.79  ? 143 LYS   B CD    1 
ATOM   3344 C  CE    . LYS   B 2 143 ? 143.978 163.958 106.088 1.00 70.06  ? 143 LYS   B CE    1 
ATOM   3345 N  NZ    . LYS   B 2 143 ? 142.754 163.541 106.825 1.00 70.23  ? 143 LYS   B NZ    1 
ATOM   3346 N  N     . TYR   B 2 144 ? 146.664 160.860 100.476 1.00 65.25  ? 144 TYR   B N     1 
ATOM   3347 C  CA    . TYR   B 2 144 ? 147.110 160.674 99.100  1.00 58.62  ? 144 TYR   B CA    1 
ATOM   3348 C  C     . TYR   B 2 144 ? 146.218 159.683 98.366  1.00 65.53  ? 144 TYR   B C     1 
ATOM   3349 O  O     . TYR   B 2 144 ? 145.542 158.853 98.978  1.00 65.62  ? 144 TYR   B O     1 
ATOM   3350 C  CB    . TYR   B 2 144 ? 148.555 160.173 99.055  1.00 50.89  ? 144 TYR   B CB    1 
ATOM   3351 C  CG    . TYR   B 2 144 ? 149.613 161.152 99.510  1.00 56.17  ? 144 TYR   B CG    1 
ATOM   3352 C  CD1   . TYR   B 2 144 ? 149.284 162.286 100.235 1.00 58.56  ? 144 TYR   B CD1   1 
ATOM   3353 C  CD2   . TYR   B 2 144 ? 150.949 160.935 99.208  1.00 61.54  ? 144 TYR   B CD2   1 
ATOM   3354 C  CE1   . TYR   B 2 144 ? 150.252 163.169 100.649 1.00 60.83  ? 144 TYR   B CE1   1 
ATOM   3355 C  CE2   . TYR   B 2 144 ? 151.923 161.815 99.616  1.00 61.02  ? 144 TYR   B CE2   1 
ATOM   3356 C  CZ    . TYR   B 2 144 ? 151.569 162.931 100.336 1.00 60.68  ? 144 TYR   B CZ    1 
ATOM   3357 O  OH    . TYR   B 2 144 ? 152.538 163.813 100.746 1.00 63.69  ? 144 TYR   B OH    1 
ATOM   3358 N  N     . SER   B 2 145 ? 146.216 159.784 97.040  1.00 68.04  ? 145 SER   B N     1 
ATOM   3359 C  CA    . SER   B 2 145 ? 145.654 158.737 96.206  1.00 63.52  ? 145 SER   B CA    1 
ATOM   3360 C  C     . SER   B 2 145 ? 146.706 157.661 95.945  1.00 70.65  ? 145 SER   B C     1 
ATOM   3361 O  O     . SER   B 2 145 ? 147.878 157.800 96.306  1.00 70.61  ? 145 SER   B O     1 
ATOM   3362 C  CB    . SER   B 2 145 ? 145.140 159.318 94.892  1.00 60.49  ? 145 SER   B CB    1 
ATOM   3363 O  OG    . SER   B 2 145 ? 146.151 159.318 93.902  1.00 67.88  ? 145 SER   B OG    1 
ATOM   3364 N  N     . SER   B 2 146 ? 146.270 156.567 95.316  1.00 70.90  ? 146 SER   B N     1 
ATOM   3365 C  CA    . SER   B 2 146 ? 147.178 155.453 95.057  1.00 65.19  ? 146 SER   B CA    1 
ATOM   3366 C  C     . SER   B 2 146 ? 148.312 155.860 94.122  1.00 65.80  ? 146 SER   B C     1 
ATOM   3367 O  O     . SER   B 2 146 ? 149.477 155.509 94.354  1.00 72.10  ? 146 SER   B O     1 
ATOM   3368 C  CB    . SER   B 2 146 ? 146.400 154.273 94.476  1.00 63.83  ? 146 SER   B CB    1 
ATOM   3369 O  OG    . SER   B 2 146 ? 146.053 154.511 93.125  1.00 73.49  ? 146 SER   B OG    1 
ATOM   3370 N  N     . GLY   B 2 147 ? 147.992 156.605 93.063  1.00 53.79  ? 147 GLY   B N     1 
ATOM   3371 C  CA    . GLY   B 2 147 ? 149.026 157.047 92.142  1.00 48.31  ? 147 GLY   B CA    1 
ATOM   3372 C  C     . GLY   B 2 147 ? 150.031 157.976 92.794  1.00 54.99  ? 147 GLY   B C     1 
ATOM   3373 O  O     . GLY   B 2 147 ? 151.227 157.908 92.508  1.00 62.51  ? 147 GLY   B O     1 
ATOM   3374 N  N     . MET   B 2 148 ? 149.559 158.856 93.679  1.00 61.74  ? 148 MET   B N     1 
ATOM   3375 C  CA    . MET   B 2 148 ? 150.460 159.765 94.383  1.00 59.00  ? 148 MET   B CA    1 
ATOM   3376 C  C     . MET   B 2 148 ? 151.414 159.000 95.294  1.00 59.59  ? 148 MET   B C     1 
ATOM   3377 O  O     . MET   B 2 148 ? 152.610 159.310 95.359  1.00 68.57  ? 148 MET   B O     1 
ATOM   3378 C  CB    . MET   B 2 148 ? 149.641 160.779 95.180  1.00 61.00  ? 148 MET   B CB    1 
ATOM   3379 C  CG    . MET   B 2 148 ? 148.677 161.593 94.327  1.00 65.03  ? 148 MET   B CG    1 
ATOM   3380 S  SD    . MET   B 2 148 ? 147.590 162.674 95.279  1.00 66.12  ? 148 MET   B SD    1 
ATOM   3381 C  CE    . MET   B 2 148 ? 148.694 164.022 95.673  1.00 59.65  ? 148 MET   B CE    1 
ATOM   3382 N  N     . ARG   B 2 149 ? 150.901 157.990 96.002  1.00 47.51  ? 149 ARG   B N     1 
ATOM   3383 C  CA    . ARG   B 2 149 ? 151.755 157.158 96.844  1.00 52.42  ? 149 ARG   B CA    1 
ATOM   3384 C  C     . ARG   B 2 149 ? 152.785 156.409 96.009  1.00 59.74  ? 149 ARG   B C     1 
ATOM   3385 O  O     . ARG   B 2 149 ? 153.960 156.311 96.393  1.00 59.35  ? 149 ARG   B O     1 
ATOM   3386 C  CB    . ARG   B 2 149 ? 150.899 156.172 97.636  1.00 57.24  ? 149 ARG   B CB    1 
ATOM   3387 C  CG    . ARG   B 2 149 ? 150.295 156.738 98.904  1.00 61.91  ? 149 ARG   B CG    1 
ATOM   3388 C  CD    . ARG   B 2 149 ? 149.895 155.623 99.856  1.00 55.54  ? 149 ARG   B CD    1 
ATOM   3389 N  NE    . ARG   B 2 149 ? 148.540 155.142 99.608  1.00 54.33  ? 149 ARG   B NE    1 
ATOM   3390 C  CZ    . ARG   B 2 149 ? 147.435 155.845 99.817  1.00 63.90  ? 149 ARG   B CZ    1 
ATOM   3391 N  NH1   . ARG   B 2 149 ? 147.477 157.071 100.313 1.00 70.69  ? 149 ARG   B NH1   1 
ATOM   3392 N  NH2   . ARG   B 2 149 ? 146.257 155.303 99.526  1.00 59.68  ? 149 ARG   B NH2   1 
ATOM   3393 N  N     . ALA   B 2 150 ? 152.358 155.863 94.867  1.00 56.98  ? 150 ALA   B N     1 
ATOM   3394 C  CA    . ALA   B 2 150 ? 153.292 155.171 93.985  1.00 49.53  ? 150 ALA   B CA    1 
ATOM   3395 C  C     . ALA   B 2 150 ? 154.373 156.116 93.477  1.00 57.47  ? 150 ALA   B C     1 
ATOM   3396 O  O     . ALA   B 2 150 ? 155.550 155.745 93.418  1.00 63.36  ? 150 ALA   B O     1 
ATOM   3397 C  CB    . ALA   B 2 150 ? 152.539 154.538 92.817  1.00 51.67  ? 150 ALA   B CB    1 
ATOM   3398 N  N     . LYS   B 2 151 ? 153.991 157.341 93.106  1.00 58.11  ? 151 LYS   B N     1 
ATOM   3399 C  CA    . LYS   B 2 151 ? 154.974 158.320 92.652  1.00 54.75  ? 151 LYS   B CA    1 
ATOM   3400 C  C     . LYS   B 2 151 ? 155.974 158.648 93.750  1.00 54.23  ? 151 LYS   B C     1 
ATOM   3401 O  O     . LYS   B 2 151 ? 157.182 158.719 93.496  1.00 60.50  ? 151 LYS   B O     1 
ATOM   3402 C  CB    . LYS   B 2 151 ? 154.277 159.597 92.181  1.00 52.22  ? 151 LYS   B CB    1 
ATOM   3403 C  CG    . LYS   B 2 151 ? 153.477 159.458 90.903  1.00 57.21  ? 151 LYS   B CG    1 
ATOM   3404 C  CD    . LYS   B 2 151 ? 152.486 160.600 90.766  1.00 59.84  ? 151 LYS   B CD    1 
ATOM   3405 C  CE    . LYS   B 2 151 ? 151.960 160.712 89.348  1.00 63.36  ? 151 LYS   B CE    1 
ATOM   3406 N  NZ    . LYS   B 2 151 ? 152.690 161.749 88.572  1.00 61.44  ? 151 LYS   B NZ    1 
ATOM   3407 N  N     . LEU   B 2 152 ? 155.490 158.855 94.977  1.00 47.88  ? 152 LEU   B N     1 
ATOM   3408 C  CA    . LEU   B 2 152 ? 156.394 159.179 96.076  1.00 53.00  ? 152 LEU   B CA    1 
ATOM   3409 C  C     . LEU   B 2 152 ? 157.376 158.044 96.338  1.00 60.20  ? 152 LEU   B C     1 
ATOM   3410 O  O     . LEU   B 2 152 ? 158.587 158.274 96.461  1.00 62.73  ? 152 LEU   B O     1 
ATOM   3411 C  CB    . LEU   B 2 152 ? 155.594 159.500 97.338  1.00 53.56  ? 152 LEU   B CB    1 
ATOM   3412 C  CG    . LEU   B 2 152 ? 156.401 159.834 98.593  1.00 56.62  ? 152 LEU   B CG    1 
ATOM   3413 C  CD1   . LEU   B 2 152 ? 157.343 160.997 98.334  1.00 59.53  ? 152 LEU   B CD1   1 
ATOM   3414 C  CD2   . LEU   B 2 152 ? 155.475 160.144 99.756  1.00 54.86  ? 152 LEU   B CD2   1 
ATOM   3415 N  N     . GLY   B 2 153 ? 156.877 156.807 96.407  1.00 57.29  ? 153 GLY   B N     1 
ATOM   3416 C  CA    . GLY   B 2 153 ? 157.766 155.679 96.636  1.00 48.48  ? 153 GLY   B CA    1 
ATOM   3417 C  C     . GLY   B 2 153 ? 158.771 155.486 95.516  1.00 48.51  ? 153 GLY   B C     1 
ATOM   3418 O  O     . GLY   B 2 153 ? 159.956 155.234 95.767  1.00 53.11  ? 153 GLY   B O     1 
ATOM   3419 N  N     . PHE   B 2 154 ? 158.317 155.605 94.265  1.00 58.21  ? 154 PHE   B N     1 
ATOM   3420 C  CA    . PHE   B 2 154 ? 159.216 155.438 93.130  1.00 58.52  ? 154 PHE   B CA    1 
ATOM   3421 C  C     . PHE   B 2 154 ? 160.293 156.512 93.117  1.00 62.10  ? 154 PHE   B C     1 
ATOM   3422 O  O     . PHE   B 2 154 ? 161.458 156.220 92.832  1.00 66.07  ? 154 PHE   B O     1 
ATOM   3423 C  CB    . PHE   B 2 154 ? 158.422 155.459 91.825  1.00 65.72  ? 154 PHE   B CB    1 
ATOM   3424 C  CG    . PHE   B 2 154 ? 159.267 155.256 90.600  1.00 72.40  ? 154 PHE   B CG    1 
ATOM   3425 C  CD1   . PHE   B 2 154 ? 159.710 153.992 90.252  1.00 69.32  ? 154 PHE   B CD1   1 
ATOM   3426 C  CD2   . PHE   B 2 154 ? 159.624 156.330 89.802  1.00 70.49  ? 154 PHE   B CD2   1 
ATOM   3427 C  CE1   . PHE   B 2 154 ? 160.489 153.799 89.128  1.00 66.54  ? 154 PHE   B CE1   1 
ATOM   3428 C  CE2   . PHE   B 2 154 ? 160.405 156.144 88.678  1.00 72.39  ? 154 PHE   B CE2   1 
ATOM   3429 C  CZ    . PHE   B 2 154 ? 160.836 154.876 88.339  1.00 70.50  ? 154 PHE   B CZ    1 
ATOM   3430 N  N     . SER   B 2 155 ? 159.925 157.760 93.417  1.00 60.56  ? 155 SER   B N     1 
ATOM   3431 C  CA    . SER   B 2 155 ? 160.916 158.830 93.461  1.00 57.97  ? 155 SER   B CA    1 
ATOM   3432 C  C     . SER   B 2 155 ? 161.921 158.607 94.584  1.00 64.54  ? 155 SER   B C     1 
ATOM   3433 O  O     . SER   B 2 155 ? 163.124 158.838 94.403  1.00 65.71  ? 155 SER   B O     1 
ATOM   3434 C  CB    . SER   B 2 155 ? 160.222 160.180 93.621  1.00 57.34  ? 155 SER   B CB    1 
ATOM   3435 O  OG    . SER   B 2 155 ? 160.242 160.603 94.970  1.00 64.14  ? 155 SER   B OG    1 
ATOM   3436 N  N     . ILE   B 2 156 ? 161.451 158.152 95.750  1.00 62.70  ? 156 ILE   B N     1 
ATOM   3437 C  CA    . ILE   B 2 156 ? 162.360 157.881 96.864  1.00 58.07  ? 156 ILE   B CA    1 
ATOM   3438 C  C     . ILE   B 2 156 ? 163.362 156.801 96.476  1.00 60.11  ? 156 ILE   B C     1 
ATOM   3439 O  O     . ILE   B 2 156 ? 164.564 156.914 96.740  1.00 63.20  ? 156 ILE   B O     1 
ATOM   3440 C  CB    . ILE   B 2 156 ? 161.575 157.485 98.126  1.00 60.82  ? 156 ILE   B CB    1 
ATOM   3441 C  CG1   . ILE   B 2 156 ? 160.827 158.690 98.699  1.00 59.93  ? 156 ILE   B CG1   1 
ATOM   3442 C  CG2   . ILE   B 2 156 ? 162.506 156.902 99.175  1.00 58.76  ? 156 ILE   B CG2   1 
ATOM   3443 C  CD1   . ILE   B 2 156 ? 159.937 158.345 99.871  1.00 56.76  ? 156 ILE   B CD1   1 
ATOM   3444 N  N     . ASN   B 2 157 ? 162.877 155.734 95.836  1.00 75.14  ? 157 ASN   B N     1 
ATOM   3445 C  CA    . ASN   B 2 157 ? 163.772 154.642 95.460  1.00 73.42  ? 157 ASN   B CA    1 
ATOM   3446 C  C     . ASN   B 2 157 ? 164.718 155.048 94.334  1.00 71.35  ? 157 ASN   B C     1 
ATOM   3447 O  O     . ASN   B 2 157 ? 165.875 154.614 94.300  1.00 68.35  ? 157 ASN   B O     1 
ATOM   3448 C  CB    . ASN   B 2 157 ? 162.958 153.411 95.064  1.00 72.74  ? 157 ASN   B CB    1 
ATOM   3449 C  CG    . ASN   B 2 157 ? 162.376 152.690 96.262  1.00 75.23  ? 157 ASN   B CG    1 
ATOM   3450 O  OD1   . ASN   B 2 157 ? 162.950 151.719 96.755  1.00 70.37  ? 157 ASN   B OD1   1 
ATOM   3451 N  ND2   . ASN   B 2 157 ? 161.233 153.165 96.742  1.00 76.78  ? 157 ASN   B ND2   1 
ATOM   3452 N  N     . ILE   B 2 158 ? 164.244 155.873 93.398  1.00 85.74  ? 158 ILE   B N     1 
ATOM   3453 C  CA    . ILE   B 2 158 ? 165.052 156.244 92.239  1.00 87.02  ? 158 ILE   B CA    1 
ATOM   3454 C  C     . ILE   B 2 158 ? 166.141 157.237 92.628  1.00 87.94  ? 158 ILE   B C     1 
ATOM   3455 O  O     . ILE   B 2 158 ? 167.253 157.202 92.086  1.00 89.77  ? 158 ILE   B O     1 
ATOM   3456 C  CB    . ILE   B 2 158 ? 164.146 156.793 91.119  1.00 88.71  ? 158 ILE   B CB    1 
ATOM   3457 C  CG1   . ILE   B 2 158 ? 163.616 155.645 90.262  1.00 86.90  ? 158 ILE   B CG1   1 
ATOM   3458 C  CG2   . ILE   B 2 158 ? 164.881 157.808 90.254  1.00 87.45  ? 158 ILE   B CG2   1 
ATOM   3459 C  CD1   . ILE   B 2 158 ? 164.664 155.007 89.380  1.00 87.93  ? 158 ILE   B CD1   1 
ATOM   3460 N  N     . THR   B 2 159 ? 165.841 158.140 93.568  1.00 92.23  ? 159 THR   B N     1 
ATOM   3461 C  CA    . THR   B 2 159 ? 166.796 159.192 93.909  1.00 93.88  ? 159 THR   B CA    1 
ATOM   3462 C  C     . THR   B 2 159 ? 168.111 158.611 94.417  1.00 96.48  ? 159 THR   B C     1 
ATOM   3463 O  O     . THR   B 2 159 ? 169.190 159.046 93.999  1.00 95.77  ? 159 THR   B O     1 
ATOM   3464 C  CB    . THR   B 2 159 ? 166.187 160.137 94.941  1.00 96.37  ? 159 THR   B CB    1 
ATOM   3465 O  OG1   . THR   B 2 159 ? 164.951 160.653 94.433  1.00 95.68  ? 159 THR   B OG1   1 
ATOM   3466 C  CG2   . THR   B 2 159 ? 167.132 161.294 95.225  1.00 97.80  ? 159 THR   B CG2   1 
ATOM   3467 N  N     . VAL   B 2 160 ? 168.045 157.627 95.315  1.00 101.70 ? 160 VAL   B N     1 
ATOM   3468 C  CA    . VAL   B 2 160 ? 169.240 156.862 95.645  1.00 100.52 ? 160 VAL   B CA    1 
ATOM   3469 C  C     . VAL   B 2 160 ? 169.588 155.967 94.461  1.00 100.91 ? 160 VAL   B C     1 
ATOM   3470 O  O     . VAL   B 2 160 ? 168.715 155.555 93.685  1.00 103.75 ? 160 VAL   B O     1 
ATOM   3471 C  CB    . VAL   B 2 160 ? 169.039 156.050 96.938  1.00 99.41  ? 160 VAL   B CB    1 
ATOM   3472 C  CG1   . VAL   B 2 160 ? 168.152 156.814 97.907  1.00 99.59  ? 160 VAL   B CG1   1 
ATOM   3473 C  CG2   . VAL   B 2 160 ? 168.448 154.682 96.642  1.00 100.48 ? 160 VAL   B CG2   1 
ATOM   3474 N  N     . ASN   B 2 161 ? 170.878 155.676 94.299  1.00 100.97 ? 161 ASN   B N     1 
ATOM   3475 C  CA    . ASN   B 2 161 ? 171.341 154.986 93.104  1.00 101.79 ? 161 ASN   B CA    1 
ATOM   3476 C  C     . ASN   B 2 161 ? 171.586 153.519 93.406  1.00 104.40 ? 161 ASN   B C     1 
ATOM   3477 O  O     . ASN   B 2 161 ? 172.595 153.187 94.048  1.00 104.32 ? 161 ASN   B O     1 
ATOM   3478 C  CB    . ASN   B 2 161 ? 172.615 155.633 92.574  1.00 103.69 ? 161 ASN   B CB    1 
ATOM   3479 C  CG    . ASN   B 2 161 ? 172.343 156.926 91.832  1.00 103.14 ? 161 ASN   B CG    1 
ATOM   3480 O  OD1   . ASN   B 2 161 ? 172.120 156.925 90.621  1.00 104.74 ? 161 ASN   B OD1   1 
ATOM   3481 N  ND2   . ASN   B 2 161 ? 172.359 158.038 92.556  1.00 102.37 ? 161 ASN   B ND2   1 
ATOM   3482 N  N     . PRO   B 2 162 ? 170.708 152.613 92.971  1.00 107.64 ? 162 PRO   B N     1 
ATOM   3483 C  CA    . PRO   B 2 162 ? 170.951 151.183 93.181  1.00 106.58 ? 162 PRO   B CA    1 
ATOM   3484 C  C     . PRO   B 2 162 ? 171.626 150.526 91.988  1.00 104.28 ? 162 PRO   B C     1 
ATOM   3485 O  O     . PRO   B 2 162 ? 171.412 150.933 90.842  1.00 103.50 ? 162 PRO   B O     1 
ATOM   3486 C  CB    . PRO   B 2 162 ? 169.541 150.626 93.403  1.00 104.48 ? 162 PRO   B CB    1 
ATOM   3487 C  CG    . PRO   B 2 162 ? 168.607 151.633 92.724  1.00 106.04 ? 162 PRO   B CG    1 
ATOM   3488 C  CD    . PRO   B 2 162 ? 169.409 152.848 92.322  1.00 105.72 ? 162 PRO   B CD    1 
ATOM   3489 N  N     . ASP   B 2 163 ? 172.452 149.511 92.244  1.00 109.83 ? 163 ASP   B N     1 
ATOM   3490 C  CA    . ASP   B 2 163 ? 173.039 148.757 91.143  1.00 111.28 ? 163 ASP   B CA    1 
ATOM   3491 C  C     . ASP   B 2 163 ? 171.986 147.916 90.432  1.00 112.19 ? 163 ASP   B C     1 
ATOM   3492 O  O     . ASP   B 2 163 ? 172.007 147.792 89.201  1.00 113.05 ? 163 ASP   B O     1 
ATOM   3493 C  CB    . ASP   B 2 163 ? 174.179 147.879 91.657  1.00 112.21 ? 163 ASP   B CB    1 
ATOM   3494 C  CG    . ASP   B 2 163 ? 175.521 148.587 91.622  1.00 114.50 ? 163 ASP   B CG    1 
ATOM   3495 O  OD1   . ASP   B 2 163 ? 175.858 149.273 92.610  1.00 112.05 ? 163 ASP   B OD1   1 
ATOM   3496 O  OD2   . ASP   B 2 163 ? 176.237 148.458 90.607  1.00 114.63 ? 163 ASP   B OD2   1 
ATOM   3497 N  N     . ILE   B 2 164 ? 171.058 147.332 91.187  1.00 96.31  ? 164 ILE   B N     1 
ATOM   3498 C  CA    . ILE   B 2 164 ? 169.983 146.510 90.642  1.00 94.37  ? 164 ILE   B CA    1 
ATOM   3499 C  C     . ILE   B 2 164 ? 168.654 147.057 91.144  1.00 95.45  ? 164 ILE   B C     1 
ATOM   3500 O  O     . ILE   B 2 164 ? 168.479 147.274 92.350  1.00 93.99  ? 164 ILE   B O     1 
ATOM   3501 C  CB    . ILE   B 2 164 ? 170.148 145.028 91.026  1.00 93.17  ? 164 ILE   B CB    1 
ATOM   3502 C  CG1   . ILE   B 2 164 ? 171.394 144.439 90.361  1.00 92.43  ? 164 ILE   B CG1   1 
ATOM   3503 C  CG2   . ILE   B 2 164 ? 168.911 144.232 90.643  1.00 96.24  ? 164 ILE   B CG2   1 
ATOM   3504 C  CD1   . ILE   B 2 164 ? 172.383 143.845 91.336  1.00 91.84  ? 164 ILE   B CD1   1 
ATOM   3505 N  N     . LEU   B 2 165 ? 167.723 147.283 90.220  1.00 87.49  ? 165 LEU   B N     1 
ATOM   3506 C  CA    . LEU   B 2 165 ? 166.399 147.795 90.544  1.00 84.87  ? 165 LEU   B CA    1 
ATOM   3507 C  C     . LEU   B 2 165 ? 165.349 146.782 90.114  1.00 85.20  ? 165 LEU   B C     1 
ATOM   3508 O  O     . LEU   B 2 165 ? 165.386 146.293 88.981  1.00 86.68  ? 165 LEU   B O     1 
ATOM   3509 C  CB    . LEU   B 2 165 ? 166.151 149.144 89.863  1.00 83.67  ? 165 LEU   B CB    1 
ATOM   3510 C  CG    . LEU   B 2 165 ? 164.799 149.811 90.122  1.00 86.59  ? 165 LEU   B CG    1 
ATOM   3511 C  CD1   . LEU   B 2 165 ? 164.631 150.131 91.598  1.00 83.55  ? 165 LEU   B CD1   1 
ATOM   3512 C  CD2   . LEU   B 2 165 ? 164.658 151.068 89.281  1.00 88.50  ? 165 LEU   B CD2   1 
ATOM   3513 N  N     . VAL   B 2 166 ? 164.422 146.469 91.015  1.00 72.21  ? 166 VAL   B N     1 
ATOM   3514 C  CA    . VAL   B 2 166 ? 163.339 145.529 90.755  1.00 73.41  ? 166 VAL   B CA    1 
ATOM   3515 C  C     . VAL   B 2 166 ? 162.018 146.264 90.924  1.00 74.68  ? 166 VAL   B C     1 
ATOM   3516 O  O     . VAL   B 2 166 ? 161.785 146.905 91.956  1.00 73.30  ? 166 VAL   B O     1 
ATOM   3517 C  CB    . VAL   B 2 166 ? 163.414 144.310 91.691  1.00 71.33  ? 166 VAL   B CB    1 
ATOM   3518 C  CG1   . VAL   B 2 166 ? 162.127 143.506 91.623  1.00 72.67  ? 166 VAL   B CG1   1 
ATOM   3519 C  CG2   . VAL   B 2 166 ? 164.608 143.442 91.336  1.00 70.21  ? 166 VAL   B CG2   1 
ATOM   3520 N  N     . ILE   B 2 167 ? 161.164 146.187 89.906  1.00 72.11  ? 167 ILE   B N     1 
ATOM   3521 C  CA    . ILE   B 2 167 ? 159.822 146.753 89.937  1.00 69.89  ? 167 ILE   B CA    1 
ATOM   3522 C  C     . ILE   B 2 167 ? 158.835 145.602 89.831  1.00 70.64  ? 167 ILE   B C     1 
ATOM   3523 O  O     . ILE   B 2 167 ? 158.885 144.824 88.870  1.00 77.22  ? 167 ILE   B O     1 
ATOM   3524 C  CB    . ILE   B 2 167 ? 159.611 147.766 88.799  1.00 72.24  ? 167 ILE   B CB    1 
ATOM   3525 C  CG1   . ILE   B 2 167 ? 160.700 148.840 88.831  1.00 71.00  ? 167 ILE   B CG1   1 
ATOM   3526 C  CG2   . ILE   B 2 167 ? 158.235 148.398 88.896  1.00 73.61  ? 167 ILE   B CG2   1 
ATOM   3527 C  CD1   . ILE   B 2 167 ? 161.258 149.184 87.468  1.00 65.83  ? 167 ILE   B CD1   1 
ATOM   3528 N  N     . ASP   B 2 168 ? 157.941 145.488 90.818  1.00 71.05  ? 168 ASP   B N     1 
ATOM   3529 C  CA    . ASP   B 2 168 ? 156.989 144.386 90.896  1.00 73.55  ? 168 ASP   B CA    1 
ATOM   3530 C  C     . ASP   B 2 168 ? 155.576 144.968 90.834  1.00 78.07  ? 168 ASP   B C     1 
ATOM   3531 O  O     . ASP   B 2 168 ? 154.938 145.204 91.862  1.00 79.77  ? 168 ASP   B O     1 
ATOM   3532 C  CB    . ASP   B 2 168 ? 157.208 143.570 92.170  1.00 72.78  ? 168 ASP   B CB    1 
ATOM   3533 C  CG    . ASP   B 2 168 ? 156.733 142.140 92.037  1.00 77.71  ? 168 ASP   B CG    1 
ATOM   3534 O  OD1   . ASP   B 2 168 ? 156.810 141.587 90.921  1.00 78.88  ? 168 ASP   B OD1   1 
ATOM   3535 O  OD2   . ASP   B 2 168 ? 156.284 141.566 93.051  1.00 76.68  ? 168 ASP   B OD2   1 
ATOM   3536 N  N     . GLU   B 2 169 ? 155.092 145.192 89.613  1.00 81.87  ? 169 GLU   B N     1 
ATOM   3537 C  CA    . GLU   B 2 169 ? 153.755 145.703 89.328  1.00 80.24  ? 169 GLU   B CA    1 
ATOM   3538 C  C     . GLU   B 2 169 ? 153.490 147.063 89.962  1.00 82.90  ? 169 GLU   B C     1 
ATOM   3539 O  O     . GLU   B 2 169 ? 152.326 147.424 90.163  1.00 84.51  ? 169 GLU   B O     1 
ATOM   3540 C  CB    . GLU   B 2 169 ? 152.674 144.712 89.774  1.00 81.64  ? 169 GLU   B CB    1 
ATOM   3541 C  CG    . GLU   B 2 169 ? 152.858 143.316 89.205  1.00 82.82  ? 169 GLU   B CG    1 
ATOM   3542 C  CD    . GLU   B 2 169 ? 151.836 142.332 89.729  1.00 86.28  ? 169 GLU   B CD    1 
ATOM   3543 O  OE1   . GLU   B 2 169 ? 150.761 142.774 90.182  1.00 87.29  ? 169 GLU   B OE1   1 
ATOM   3544 O  OE2   . GLU   B 2 169 ? 152.110 141.114 89.691  1.00 87.53  ? 169 GLU   B OE2   1 
ATOM   3545 N  N     . ALA   B 2 170 ? 154.535 147.834 90.272  1.00 81.86  ? 170 ALA   B N     1 
ATOM   3546 C  CA    . ALA   B 2 170 ? 154.338 149.111 90.950  1.00 77.71  ? 170 ALA   B CA    1 
ATOM   3547 C  C     . ALA   B 2 170 ? 153.725 150.150 90.020  1.00 79.82  ? 170 ALA   B C     1 
ATOM   3548 O  O     . ALA   B 2 170 ? 153.044 151.077 90.475  1.00 82.22  ? 170 ALA   B O     1 
ATOM   3549 C  CB    . ALA   B 2 170 ? 155.665 149.614 91.516  1.00 72.72  ? 170 ALA   B CB    1 
ATOM   3550 N  N     . LEU   B 2 171 ? 153.951 150.013 88.713  1.00 70.73  ? 171 LEU   B N     1 
ATOM   3551 C  CA    . LEU   B 2 171 ? 153.492 151.009 87.752  1.00 67.58  ? 171 LEU   B CA    1 
ATOM   3552 C  C     . LEU   B 2 171 ? 152.051 150.796 87.309  1.00 67.84  ? 171 LEU   B C     1 
ATOM   3553 O  O     . LEU   B 2 171 ? 151.569 151.553 86.460  1.00 72.52  ? 171 LEU   B O     1 
ATOM   3554 C  CB    . LEU   B 2 171 ? 154.406 151.011 86.526  1.00 72.23  ? 171 LEU   B CB    1 
ATOM   3555 C  CG    . LEU   B 2 171 ? 155.310 152.230 86.349  1.00 72.26  ? 171 LEU   B CG    1 
ATOM   3556 C  CD1   . LEU   B 2 171 ? 156.428 152.220 87.377  1.00 72.29  ? 171 LEU   B CD1   1 
ATOM   3557 C  CD2   . LEU   B 2 171 ? 155.875 152.267 84.941  1.00 72.58  ? 171 LEU   B CD2   1 
ATOM   3558 N  N     . SER   B 2 172 ? 151.359 149.789 87.845  1.00 68.26  ? 172 SER   B N     1 
ATOM   3559 C  CA    . SER   B 2 172 ? 149.993 149.517 87.408  1.00 74.24  ? 172 SER   B CA    1 
ATOM   3560 C  C     . SER   B 2 172 ? 149.050 150.656 87.779  1.00 74.76  ? 172 SER   B C     1 
ATOM   3561 O  O     . SER   B 2 172 ? 148.116 150.965 87.031  1.00 73.53  ? 172 SER   B O     1 
ATOM   3562 C  CB    . SER   B 2 172 ? 149.505 148.198 88.005  1.00 70.34  ? 172 SER   B CB    1 
ATOM   3563 O  OG    . SER   B 2 172 ? 149.866 148.088 89.369  1.00 71.31  ? 172 SER   B OG    1 
ATOM   3564 N  N     . VAL   B 2 173 ? 149.273 151.288 88.933  1.00 70.72  ? 173 VAL   B N     1 
ATOM   3565 C  CA    . VAL   B 2 173 ? 148.385 152.361 89.374  1.00 63.44  ? 173 VAL   B CA    1 
ATOM   3566 C  C     . VAL   B 2 173 ? 148.755 153.679 88.704  1.00 65.43  ? 173 VAL   B C     1 
ATOM   3567 O  O     . VAL   B 2 173 ? 147.907 154.564 88.535  1.00 67.73  ? 173 VAL   B O     1 
ATOM   3568 C  CB    . VAL   B 2 173 ? 148.409 152.477 90.909  1.00 65.63  ? 173 VAL   B CB    1 
ATOM   3569 C  CG1   . VAL   B 2 173 ? 147.523 151.410 91.531  1.00 64.14  ? 173 VAL   B CG1   1 
ATOM   3570 C  CG2   . VAL   B 2 173 ? 149.831 152.362 91.428  1.00 66.22  ? 173 VAL   B CG2   1 
ATOM   3571 N  N     . GLY   B 2 174 ? 150.019 153.837 88.322  1.00 62.32  ? 174 GLY   B N     1 
ATOM   3572 C  CA    . GLY   B 2 174 ? 150.441 155.080 87.699  1.00 63.28  ? 174 GLY   B CA    1 
ATOM   3573 C  C     . GLY   B 2 174 ? 149.849 155.238 86.309  1.00 63.37  ? 174 GLY   B C     1 
ATOM   3574 O  O     . GLY   B 2 174 ? 149.545 154.258 85.625  1.00 58.49  ? 174 GLY   B O     1 
ATOM   3575 N  N     . ASP   B 2 175 ? 149.688 156.491 85.888  1.00 82.83  ? 175 ASP   B N     1 
ATOM   3576 C  CA    . ASP   B 2 175 ? 149.099 156.790 84.593  1.00 79.46  ? 175 ASP   B CA    1 
ATOM   3577 C  C     . ASP   B 2 175 ? 150.160 156.763 83.492  1.00 82.53  ? 175 ASP   B C     1 
ATOM   3578 O  O     . ASP   B 2 175 ? 151.295 156.324 83.690  1.00 90.00  ? 175 ASP   B O     1 
ATOM   3579 C  CB    . ASP   B 2 175 ? 148.374 158.136 84.630  1.00 77.52  ? 175 ASP   B CB    1 
ATOM   3580 C  CG    . ASP   B 2 175 ? 149.241 159.262 85.161  1.00 84.52  ? 175 ASP   B CG    1 
ATOM   3581 O  OD1   . ASP   B 2 175 ? 150.434 159.336 84.801  1.00 90.09  ? 175 ASP   B OD1   1 
ATOM   3582 O  OD2   . ASP   B 2 175 ? 148.724 160.084 85.946  1.00 87.47  ? 175 ASP   B OD2   1 
ATOM   3583 N  N     . GLN   B 2 176 ? 149.768 157.243 82.308  1.00 86.33  ? 176 GLN   B N     1 
ATOM   3584 C  CA    . GLN   B 2 176 ? 150.616 157.093 81.129  1.00 86.69  ? 176 GLN   B CA    1 
ATOM   3585 C  C     . GLN   B 2 176 ? 151.798 158.056 81.151  1.00 89.22  ? 176 GLN   B C     1 
ATOM   3586 O  O     . GLN   B 2 176 ? 152.905 157.697 80.731  1.00 94.83  ? 176 GLN   B O     1 
ATOM   3587 C  CB    . GLN   B 2 176 ? 149.785 157.290 79.862  1.00 87.19  ? 176 GLN   B CB    1 
ATOM   3588 C  CG    . GLN   B 2 176 ? 149.302 155.990 79.243  1.00 91.25  ? 176 GLN   B CG    1 
ATOM   3589 C  CD    . GLN   B 2 176 ? 148.994 156.125 77.767  1.00 95.51  ? 176 GLN   B CD    1 
ATOM   3590 O  OE1   . GLN   B 2 176 ? 149.894 156.299 76.945  1.00 95.82  ? 176 GLN   B OE1   1 
ATOM   3591 N  NE2   . GLN   B 2 176 ? 147.715 156.042 77.420  1.00 91.69  ? 176 GLN   B NE2   1 
ATOM   3592 N  N     . THR   B 2 177 ? 151.584 159.290 81.613  1.00 77.87  ? 177 THR   B N     1 
ATOM   3593 C  CA    . THR   B 2 177 ? 152.679 160.256 81.666  1.00 78.83  ? 177 THR   B CA    1 
ATOM   3594 C  C     . THR   B 2 177 ? 153.758 159.813 82.647  1.00 76.34  ? 177 THR   B C     1 
ATOM   3595 O  O     . THR   B 2 177 ? 154.960 159.923 82.362  1.00 78.73  ? 177 THR   B O     1 
ATOM   3596 C  CB    . THR   B 2 177 ? 152.140 161.636 82.043  1.00 78.03  ? 177 THR   B CB    1 
ATOM   3597 O  OG1   . THR   B 2 177 ? 151.513 161.571 83.329  1.00 78.00  ? 177 THR   B OG1   1 
ATOM   3598 C  CG2   . THR   B 2 177 ? 151.119 162.101 81.018  1.00 75.43  ? 177 THR   B CG2   1 
ATOM   3599 N  N     . PHE   B 2 178 ? 153.346 159.300 83.807  1.00 68.72  ? 178 PHE   B N     1 
ATOM   3600 C  CA    . PHE   B 2 178 ? 154.307 158.749 84.754  1.00 70.29  ? 178 PHE   B CA    1 
ATOM   3601 C  C     . PHE   B 2 178 ? 155.039 157.559 84.150  1.00 76.35  ? 178 PHE   B C     1 
ATOM   3602 O  O     . PHE   B 2 178 ? 156.240 157.378 84.380  1.00 83.48  ? 178 PHE   B O     1 
ATOM   3603 C  CB    . PHE   B 2 178 ? 153.596 158.350 86.046  1.00 69.96  ? 178 PHE   B CB    1 
ATOM   3604 C  CG    . PHE   B 2 178 ? 154.528 157.961 87.155  1.00 78.34  ? 178 PHE   B CG    1 
ATOM   3605 C  CD1   . PHE   B 2 178 ? 155.612 158.760 87.477  1.00 79.66  ? 178 PHE   B CD1   1 
ATOM   3606 C  CD2   . PHE   B 2 178 ? 154.319 156.800 87.878  1.00 76.31  ? 178 PHE   B CD2   1 
ATOM   3607 C  CE1   . PHE   B 2 178 ? 156.471 158.406 88.498  1.00 76.32  ? 178 PHE   B CE1   1 
ATOM   3608 C  CE2   . PHE   B 2 178 ? 155.175 156.442 88.898  1.00 76.86  ? 178 PHE   B CE2   1 
ATOM   3609 C  CZ    . PHE   B 2 178 ? 156.252 157.245 89.208  1.00 77.93  ? 178 PHE   B CZ    1 
ATOM   3610 N  N     . ALA   B 2 179 ? 154.333 156.742 83.366  1.00 70.46  ? 179 ALA   B N     1 
ATOM   3611 C  CA    . ALA   B 2 179 ? 154.977 155.617 82.696  1.00 68.41  ? 179 ALA   B CA    1 
ATOM   3612 C  C     . ALA   B 2 179 ? 156.036 156.091 81.709  1.00 77.86  ? 179 ALA   B C     1 
ATOM   3613 O  O     . ALA   B 2 179 ? 157.115 155.498 81.616  1.00 83.34  ? 179 ALA   B O     1 
ATOM   3614 C  CB    . ALA   B 2 179 ? 153.929 154.757 81.991  1.00 67.78  ? 179 ALA   B CB    1 
ATOM   3615 N  N     . GLN   B 2 180 ? 155.746 157.158 80.959  1.00 71.10  ? 180 GLN   B N     1 
ATOM   3616 C  CA    . GLN   B 2 180 ? 156.732 157.693 80.023  1.00 66.53  ? 180 GLN   B CA    1 
ATOM   3617 C  C     . GLN   B 2 180 ? 157.952 158.241 80.755  1.00 70.47  ? 180 GLN   B C     1 
ATOM   3618 O  O     . GLN   B 2 180 ? 159.096 158.046 80.317  1.00 79.09  ? 180 GLN   B O     1 
ATOM   3619 C  CB    . GLN   B 2 180 ? 156.095 158.778 79.157  1.00 69.83  ? 180 GLN   B CB    1 
ATOM   3620 C  CG    . GLN   B 2 180 ? 155.930 158.392 77.698  1.00 76.53  ? 180 GLN   B CG    1 
ATOM   3621 C  CD    . GLN   B 2 180 ? 157.242 158.391 76.941  1.00 76.99  ? 180 GLN   B CD    1 
ATOM   3622 O  OE1   . GLN   B 2 180 ? 158.232 158.967 77.390  1.00 74.78  ? 180 GLN   B OE1   1 
ATOM   3623 N  NE2   . GLN   B 2 180 ? 157.255 157.745 75.781  1.00 73.41  ? 180 GLN   B NE2   1 
ATOM   3624 N  N     . LYS   B 2 181 ? 157.728 158.939 81.870  1.00 82.84  ? 181 LYS   B N     1 
ATOM   3625 C  CA    . LYS   B 2 181 ? 158.854 159.444 82.651  1.00 85.83  ? 181 LYS   B CA    1 
ATOM   3626 C  C     . LYS   B 2 181 ? 159.703 158.300 83.200  1.00 88.26  ? 181 LYS   B C     1 
ATOM   3627 O  O     . LYS   B 2 181 ? 160.941 158.362 83.173  1.00 89.37  ? 181 LYS   B O     1 
ATOM   3628 C  CB    . LYS   B 2 181 ? 158.347 160.341 83.778  1.00 83.56  ? 181 LYS   B CB    1 
ATOM   3629 C  CG    . LYS   B 2 181 ? 159.400 160.709 84.802  1.00 88.77  ? 181 LYS   B CG    1 
ATOM   3630 C  CD    . LYS   B 2 181 ? 158.785 161.490 85.944  1.00 88.98  ? 181 LYS   B CD    1 
ATOM   3631 C  CE    . LYS   B 2 181 ? 158.572 162.938 85.544  1.00 89.31  ? 181 LYS   B CE    1 
ATOM   3632 N  NZ    . LYS   B 2 181 ? 159.182 163.883 86.518  1.00 86.09  ? 181 LYS   B NZ    1 
ATOM   3633 N  N     . CYS   B 2 182 ? 159.056 157.241 83.693  1.00 73.27  ? 182 CYS   B N     1 
ATOM   3634 C  CA    . CYS   B 2 182 ? 159.797 156.073 84.157  1.00 72.21  ? 182 CYS   B CA    1 
ATOM   3635 C  C     . CYS   B 2 182 ? 160.551 155.405 83.014  1.00 75.06  ? 182 CYS   B C     1 
ATOM   3636 O  O     . CYS   B 2 182 ? 161.647 154.877 83.214  1.00 80.32  ? 182 CYS   B O     1 
ATOM   3637 C  CB    . CYS   B 2 182 ? 158.854 155.078 84.832  1.00 75.17  ? 182 CYS   B CB    1 
ATOM   3638 S  SG    . CYS   B 2 182 ? 157.983 155.727 86.274  1.00 77.99  ? 182 CYS   B SG    1 
ATOM   3639 N  N     . LEU   B 2 183 ? 159.977 155.408 81.809  1.00 66.65  ? 183 LEU   B N     1 
ATOM   3640 C  CA    . LEU   B 2 183 ? 160.676 154.850 80.654  1.00 68.62  ? 183 LEU   B CA    1 
ATOM   3641 C  C     . LEU   B 2 183 ? 161.945 155.636 80.344  1.00 73.63  ? 183 LEU   B C     1 
ATOM   3642 O  O     . LEU   B 2 183 ? 162.996 155.050 80.051  1.00 79.37  ? 183 LEU   B O     1 
ATOM   3643 C  CB    . LEU   B 2 183 ? 159.747 154.830 79.442  1.00 71.22  ? 183 LEU   B CB    1 
ATOM   3644 C  CG    . LEU   B 2 183 ? 160.128 153.915 78.277  1.00 74.15  ? 183 LEU   B CG    1 
ATOM   3645 C  CD1   . LEU   B 2 183 ? 160.764 152.627 78.778  1.00 73.54  ? 183 LEU   B CD1   1 
ATOM   3646 C  CD2   . LEU   B 2 183 ? 158.912 153.618 77.417  1.00 72.55  ? 183 LEU   B CD2   1 
ATOM   3647 N  N     . ASP   B 2 184 ? 161.864 156.967 80.399  1.00 79.89  ? 184 ASP   B N     1 
ATOM   3648 C  CA    . ASP   B 2 184 ? 163.062 157.781 80.198  1.00 81.67  ? 184 ASP   B CA    1 
ATOM   3649 C  C     . ASP   B 2 184 ? 164.104 157.502 81.277  1.00 83.94  ? 184 ASP   B C     1 
ATOM   3650 O  O     . ASP   B 2 184 ? 165.306 157.391 80.986  1.00 84.34  ? 184 ASP   B O     1 
ATOM   3651 C  CB    . ASP   B 2 184 ? 162.693 159.263 80.174  1.00 81.99  ? 184 ASP   B CB    1 
ATOM   3652 C  CG    . ASP   B 2 184 ? 161.748 159.609 79.043  1.00 87.31  ? 184 ASP   B CG    1 
ATOM   3653 O  OD1   . ASP   B 2 184 ? 161.578 158.771 78.133  1.00 81.64  ? 184 ASP   B OD1   1 
ATOM   3654 O  OD2   . ASP   B 2 184 ? 161.177 160.719 79.061  1.00 89.29  ? 184 ASP   B OD2   1 
ATOM   3655 N  N     . LYS   B 2 185 ? 163.662 157.381 82.531  1.00 80.74  ? 185 LYS   B N     1 
ATOM   3656 C  CA    . LYS   B 2 185 ? 164.592 157.062 83.611  1.00 79.04  ? 185 LYS   B CA    1 
ATOM   3657 C  C     . LYS   B 2 185 ? 165.238 155.697 83.397  1.00 78.30  ? 185 LYS   B C     1 
ATOM   3658 O  O     . LYS   B 2 185 ? 166.422 155.508 83.698  1.00 81.78  ? 185 LYS   B O     1 
ATOM   3659 C  CB    . LYS   B 2 185 ? 163.872 157.111 84.958  1.00 79.14  ? 185 LYS   B CB    1 
ATOM   3660 C  CG    . LYS   B 2 185 ? 164.755 157.553 86.113  1.00 81.89  ? 185 LYS   B CG    1 
ATOM   3661 C  CD    . LYS   B 2 185 ? 165.052 159.042 86.036  1.00 82.81  ? 185 LYS   B CD    1 
ATOM   3662 C  CE    . LYS   B 2 185 ? 166.318 159.398 86.795  1.00 80.26  ? 185 LYS   B CE    1 
ATOM   3663 N  NZ    . LYS   B 2 185 ? 167.143 160.392 86.055  1.00 79.71  ? 185 LYS   B NZ    1 
ATOM   3664 N  N     . ILE   B 2 186 ? 164.475 154.732 82.881  1.00 83.47  ? 186 ILE   B N     1 
ATOM   3665 C  CA    . ILE   B 2 186 ? 165.016 153.400 82.622  1.00 83.94  ? 186 ILE   B CA    1 
ATOM   3666 C  C     . ILE   B 2 186 ? 166.046 153.450 81.502  1.00 84.04  ? 186 ILE   B C     1 
ATOM   3667 O  O     . ILE   B 2 186 ? 167.067 152.756 81.550  1.00 87.24  ? 186 ILE   B O     1 
ATOM   3668 C  CB    . ILE   B 2 186 ? 163.878 152.408 82.313  1.00 84.11  ? 186 ILE   B CB    1 
ATOM   3669 C  CG1   . ILE   B 2 186 ? 163.048 152.125 83.569  1.00 82.09  ? 186 ILE   B CG1   1 
ATOM   3670 C  CG2   . ILE   B 2 186 ? 164.425 151.108 81.744  1.00 82.81  ? 186 ILE   B CG2   1 
ATOM   3671 C  CD1   . ILE   B 2 186 ? 163.843 152.133 84.858  1.00 82.16  ? 186 ILE   B CD1   1 
ATOM   3672 N  N     . TYR   B 2 187 ? 165.797 154.263 80.472  1.00 98.86  ? 187 TYR   B N     1 
ATOM   3673 C  CA    . TYR   B 2 187 ? 166.807 154.440 79.429  1.00 100.92 ? 187 TYR   B CA    1 
ATOM   3674 C  C     . TYR   B 2 187 ? 168.092 155.030 80.000  1.00 104.99 ? 187 TYR   B C     1 
ATOM   3675 O  O     . TYR   B 2 187 ? 169.199 154.579 79.669  1.00 105.29 ? 187 TYR   B O     1 
ATOM   3676 C  CB    . TYR   B 2 187 ? 166.270 155.324 78.305  1.00 101.31 ? 187 TYR   B CB    1 
ATOM   3677 C  CG    . TYR   B 2 187 ? 165.137 154.712 77.517  1.00 102.53 ? 187 TYR   B CG    1 
ATOM   3678 C  CD1   . TYR   B 2 187 ? 165.036 153.336 77.364  1.00 103.37 ? 187 TYR   B CD1   1 
ATOM   3679 C  CD2   . TYR   B 2 187 ? 164.177 155.511 76.909  1.00 101.49 ? 187 TYR   B CD2   1 
ATOM   3680 C  CE1   . TYR   B 2 187 ? 164.004 152.772 76.639  1.00 104.71 ? 187 TYR   B CE1   1 
ATOM   3681 C  CE2   . TYR   B 2 187 ? 163.143 154.956 76.182  1.00 101.51 ? 187 TYR   B CE2   1 
ATOM   3682 C  CZ    . TYR   B 2 187 ? 163.061 153.587 76.050  1.00 105.11 ? 187 TYR   B CZ    1 
ATOM   3683 O  OH    . TYR   B 2 187 ? 162.031 153.032 75.326  1.00 105.03 ? 187 TYR   B OH    1 
ATOM   3684 N  N     . GLU   B 2 188 ? 167.966 156.035 80.870  1.00 108.30 ? 188 GLU   B N     1 
ATOM   3685 C  CA    . GLU   B 2 188 ? 169.156 156.612 81.493  1.00 105.00 ? 188 GLU   B CA    1 
ATOM   3686 C  C     . GLU   B 2 188 ? 169.891 155.582 82.346  1.00 106.29 ? 188 GLU   B C     1 
ATOM   3687 O  O     . GLU   B 2 188 ? 171.127 155.522 82.338  1.00 109.00 ? 188 GLU   B O     1 
ATOM   3688 C  CB    . GLU   B 2 188 ? 168.776 157.832 82.330  1.00 105.56 ? 188 GLU   B CB    1 
ATOM   3689 C  CG    . GLU   B 2 188 ? 168.684 159.120 81.531  1.00 108.09 ? 188 GLU   B CG    1 
ATOM   3690 C  CD    . GLU   B 2 188 ? 168.684 160.351 82.413  1.00 109.54 ? 188 GLU   B CD    1 
ATOM   3691 O  OE1   . GLU   B 2 188 ? 167.970 160.350 83.437  1.00 106.38 ? 188 GLU   B OE1   1 
ATOM   3692 O  OE2   . GLU   B 2 188 ? 169.399 161.320 82.080  1.00 110.01 ? 188 GLU   B OE2   1 
ATOM   3693 N  N     . PHE   B 2 189 ? 169.147 154.760 83.089  1.00 95.82  ? 189 PHE   B N     1 
ATOM   3694 C  CA    . PHE   B 2 189 ? 169.775 153.738 83.921  1.00 93.77  ? 189 PHE   B CA    1 
ATOM   3695 C  C     . PHE   B 2 189 ? 170.459 152.674 83.071  1.00 90.00  ? 189 PHE   B C     1 
ATOM   3696 O  O     . PHE   B 2 189 ? 171.509 152.144 83.454  1.00 89.18  ? 189 PHE   B O     1 
ATOM   3697 C  CB    . PHE   B 2 189 ? 168.737 153.106 84.846  1.00 92.17  ? 189 PHE   B CB    1 
ATOM   3698 C  CG    . PHE   B 2 189 ? 168.631 153.778 86.183  1.00 93.15  ? 189 PHE   B CG    1 
ATOM   3699 C  CD1   . PHE   B 2 189 ? 168.566 155.158 86.274  1.00 92.38  ? 189 PHE   B CD1   1 
ATOM   3700 C  CD2   . PHE   B 2 189 ? 168.598 153.032 87.349  1.00 93.52  ? 189 PHE   B CD2   1 
ATOM   3701 C  CE1   . PHE   B 2 189 ? 168.470 155.781 87.501  1.00 93.03  ? 189 PHE   B CE1   1 
ATOM   3702 C  CE2   . PHE   B 2 189 ? 168.502 153.651 88.580  1.00 94.11  ? 189 PHE   B CE2   1 
ATOM   3703 C  CZ    . PHE   B 2 189 ? 168.438 155.027 88.656  1.00 93.91  ? 189 PHE   B CZ    1 
ATOM   3704 N  N     . LYS   B 2 190 ? 169.872 152.338 81.920  1.00 102.35 ? 190 LYS   B N     1 
ATOM   3705 C  CA    . LYS   B 2 190 ? 170.535 151.435 80.985  1.00 105.00 ? 190 LYS   B CA    1 
ATOM   3706 C  C     . LYS   B 2 190 ? 171.839 152.037 80.488  1.00 106.86 ? 190 LYS   B C     1 
ATOM   3707 O  O     . LYS   B 2 190 ? 172.841 151.330 80.331  1.00 105.21 ? 190 LYS   B O     1 
ATOM   3708 C  CB    . LYS   B 2 190 ? 169.616 151.122 79.806  1.00 106.57 ? 190 LYS   B CB    1 
ATOM   3709 C  CG    . LYS   B 2 190 ? 168.465 150.191 80.124  1.00 106.08 ? 190 LYS   B CG    1 
ATOM   3710 C  CD    . LYS   B 2 190 ? 167.633 149.936 78.879  1.00 107.98 ? 190 LYS   B CD    1 
ATOM   3711 C  CE    . LYS   B 2 190 ? 168.388 149.077 77.880  1.00 104.56 ? 190 LYS   B CE    1 
ATOM   3712 N  NZ    . LYS   B 2 190 ? 167.534 148.695 76.724  1.00 103.66 ? 190 LYS   B NZ    1 
ATOM   3713 N  N     . GLU   B 2 191 ? 171.839 153.345 80.221  1.00 116.22 ? 191 GLU   B N     1 
ATOM   3714 C  CA    . GLU   B 2 191 ? 173.086 154.019 79.870  1.00 117.34 ? 191 GLU   B CA    1 
ATOM   3715 C  C     . GLU   B 2 191 ? 174.089 153.956 81.018  1.00 117.89 ? 191 GLU   B C     1 
ATOM   3716 O  O     . GLU   B 2 191 ? 175.302 153.891 80.789  1.00 116.41 ? 191 GLU   B O     1 
ATOM   3717 C  CB    . GLU   B 2 191 ? 172.808 155.467 79.469  1.00 114.81 ? 191 GLU   B CB    1 
ATOM   3718 C  CG    . GLU   B 2 191 ? 172.448 155.638 78.001  1.00 117.18 ? 191 GLU   B CG    1 
ATOM   3719 C  CD    . GLU   B 2 191 ? 172.955 154.497 77.137  1.00 119.74 ? 191 GLU   B CD    1 
ATOM   3720 O  OE1   . GLU   B 2 191 ? 172.131 153.664 76.705  1.00 116.79 ? 191 GLU   B OE1   1 
ATOM   3721 O  OE2   . GLU   B 2 191 ? 174.177 154.436 76.884  1.00 120.24 ? 191 GLU   B OE2   1 
ATOM   3722 N  N     . GLN   B 2 192 ? 173.600 153.969 82.261  1.00 112.21 ? 192 GLN   B N     1 
ATOM   3723 C  CA    . GLN   B 2 192 ? 174.489 153.847 83.413  1.00 107.20 ? 192 GLN   B CA    1 
ATOM   3724 C  C     . GLN   B 2 192 ? 174.838 152.397 83.734  1.00 107.87 ? 192 GLN   B C     1 
ATOM   3725 O  O     . GLN   B 2 192 ? 175.472 152.143 84.765  1.00 106.32 ? 192 GLN   B O     1 
ATOM   3726 C  CB    . GLN   B 2 192 ? 173.866 154.509 84.642  1.00 106.22 ? 192 GLN   B CB    1 
ATOM   3727 C  CG    . GLN   B 2 192 ? 173.845 156.026 84.598  1.00 108.41 ? 192 GLN   B CG    1 
ATOM   3728 C  CD    . GLN   B 2 192 ? 172.822 156.622 85.545  1.00 110.56 ? 192 GLN   B CD    1 
ATOM   3729 O  OE1   . GLN   B 2 192 ? 172.935 156.485 86.764  1.00 107.79 ? 192 GLN   B OE1   1 
ATOM   3730 N  NE2   . GLN   B 2 192 ? 171.820 157.293 84.990  1.00 109.15 ? 192 GLN   B NE2   1 
ATOM   3731 N  N     . ASN   B 2 193 ? 174.417 151.447 82.895  1.00 111.98 ? 193 ASN   B N     1 
ATOM   3732 C  CA    . ASN   B 2 193 ? 174.746 150.031 83.045  1.00 110.45 ? 193 ASN   B CA    1 
ATOM   3733 C  C     . ASN   B 2 193 ? 174.167 149.421 84.317  1.00 110.76 ? 193 ASN   B C     1 
ATOM   3734 O  O     . ASN   B 2 193 ? 174.774 148.524 84.910  1.00 112.25 ? 193 ASN   B O     1 
ATOM   3735 C  CB    . ASN   B 2 193 ? 176.263 149.818 83.007  1.00 110.24 ? 193 ASN   B CB    1 
ATOM   3736 C  CG    . ASN   B 2 193 ? 176.794 149.650 81.598  1.00 112.89 ? 193 ASN   B CG    1 
ATOM   3737 O  OD1   . ASN   B 2 193 ? 177.634 148.790 81.338  1.00 110.85 ? 193 ASN   B OD1   1 
ATOM   3738 N  ND2   . ASN   B 2 193 ? 176.299 150.470 80.678  1.00 112.47 ? 193 ASN   B ND2   1 
ATOM   3739 N  N     . LYS   B 2 194 ? 173.005 149.901 84.752  1.00 105.03 ? 194 LYS   B N     1 
ATOM   3740 C  CA    . LYS   B 2 194 ? 172.284 149.231 85.825  1.00 103.94 ? 194 LYS   B CA    1 
ATOM   3741 C  C     . LYS   B 2 194 ? 171.453 148.080 85.268  1.00 102.75 ? 194 LYS   B C     1 
ATOM   3742 O  O     . LYS   B 2 194 ? 171.197 147.994 84.064  1.00 105.07 ? 194 LYS   B O     1 
ATOM   3743 C  CB    . LYS   B 2 194 ? 171.389 150.221 86.572  1.00 105.57 ? 194 LYS   B CB    1 
ATOM   3744 C  CG    . LYS   B 2 194 ? 171.946 151.632 86.650  1.00 104.79 ? 194 LYS   B CG    1 
ATOM   3745 C  CD    . LYS   B 2 194 ? 173.051 151.718 87.690  1.00 105.28 ? 194 LYS   B CD    1 
ATOM   3746 C  CE    . LYS   B 2 194 ? 173.441 153.159 87.978  1.00 106.79 ? 194 LYS   B CE    1 
ATOM   3747 N  NZ    . LYS   B 2 194 ? 172.274 154.079 87.920  1.00 103.50 ? 194 LYS   B NZ    1 
ATOM   3748 N  N     . THR   B 2 195 ? 171.035 147.184 86.158  1.00 93.29  ? 195 THR   B N     1 
ATOM   3749 C  CA    . THR   B 2 195 ? 170.205 146.043 85.794  1.00 96.69  ? 195 THR   B CA    1 
ATOM   3750 C  C     . THR   B 2 195 ? 168.810 146.220 86.380  1.00 97.25  ? 195 THR   B C     1 
ATOM   3751 O  O     . THR   B 2 195 ? 168.661 146.417 87.591  1.00 94.85  ? 195 THR   B O     1 
ATOM   3752 C  CB    . THR   B 2 195 ? 170.826 144.734 86.286  1.00 98.52  ? 195 THR   B CB    1 
ATOM   3753 O  OG1   . THR   B 2 195 ? 171.956 144.403 85.469  1.00 98.46  ? 195 THR   B OG1   1 
ATOM   3754 C  CG2   . THR   B 2 195 ? 169.815 143.602 86.217  1.00 94.39  ? 195 THR   B CG2   1 
ATOM   3755 N  N     . ILE   B 2 196 ? 167.796 146.137 85.520  1.00 88.14  ? 196 ILE   B N     1 
ATOM   3756 C  CA    . ILE   B 2 196 ? 166.412 146.398 85.895  1.00 85.11  ? 196 ILE   B CA    1 
ATOM   3757 C  C     . ILE   B 2 196 ? 165.574 145.159 85.615  1.00 83.67  ? 196 ILE   B C     1 
ATOM   3758 O  O     . ILE   B 2 196 ? 165.632 144.589 84.520  1.00 84.24  ? 196 ILE   B O     1 
ATOM   3759 C  CB    . ILE   B 2 196 ? 165.834 147.617 85.145  1.00 85.37  ? 196 ILE   B CB    1 
ATOM   3760 C  CG1   . ILE   B 2 196 ? 166.882 148.726 85.012  1.00 81.69  ? 196 ILE   B CG1   1 
ATOM   3761 C  CG2   . ILE   B 2 196 ? 164.592 148.135 85.849  1.00 85.62  ? 196 ILE   B CG2   1 
ATOM   3762 C  CD1   . ILE   B 2 196 ? 167.560 148.773 83.660  1.00 82.27  ? 196 ILE   B CD1   1 
ATOM   3763 N  N     . PHE   B 2 197 ? 164.797 144.747 86.612  1.00 79.94  ? 197 PHE   B N     1 
ATOM   3764 C  CA    . PHE   B 2 197 ? 163.802 143.693 86.477  1.00 79.17  ? 197 PHE   B CA    1 
ATOM   3765 C  C     . PHE   B 2 197 ? 162.422 144.331 86.528  1.00 78.18  ? 197 PHE   B C     1 
ATOM   3766 O  O     . PHE   B 2 197 ? 162.158 145.166 87.399  1.00 77.26  ? 197 PHE   B O     1 
ATOM   3767 C  CB    . PHE   B 2 197 ? 163.944 142.649 87.587  1.00 80.73  ? 197 PHE   B CB    1 
ATOM   3768 C  CG    . PHE   B 2 197 ? 165.071 141.680 87.373  1.00 80.70  ? 197 PHE   B CG    1 
ATOM   3769 C  CD1   . PHE   B 2 197 ? 166.373 142.032 87.682  1.00 83.04  ? 197 PHE   B CD1   1 
ATOM   3770 C  CD2   . PHE   B 2 197 ? 164.827 140.414 86.870  1.00 81.62  ? 197 PHE   B CD2   1 
ATOM   3771 C  CE1   . PHE   B 2 197 ? 167.411 141.142 87.489  1.00 83.51  ? 197 PHE   B CE1   1 
ATOM   3772 C  CE2   . PHE   B 2 197 ? 165.861 139.520 86.675  1.00 81.74  ? 197 PHE   B CE2   1 
ATOM   3773 C  CZ    . PHE   B 2 197 ? 167.155 139.885 86.985  1.00 81.32  ? 197 PHE   B CZ    1 
ATOM   3774 N  N     . PHE   B 2 198 ? 161.552 143.953 85.595  1.00 57.95  ? 198 PHE   B N     1 
ATOM   3775 C  CA    . PHE   B 2 198 ? 160.235 144.566 85.457  1.00 55.78  ? 198 PHE   B CA    1 
ATOM   3776 C  C     . PHE   B 2 198 ? 159.176 143.475 85.432  1.00 54.76  ? 198 PHE   B C     1 
ATOM   3777 O  O     . PHE   B 2 198 ? 159.249 142.558 84.610  1.00 60.22  ? 198 PHE   B O     1 
ATOM   3778 C  CB    . PHE   B 2 198 ? 160.165 145.416 84.184  1.00 53.37  ? 198 PHE   B CB    1 
ATOM   3779 C  CG    . PHE   B 2 198 ? 158.857 146.127 83.996  1.00 60.78  ? 198 PHE   B CG    1 
ATOM   3780 C  CD1   . PHE   B 2 198 ? 158.386 147.008 84.954  1.00 59.65  ? 198 PHE   B CD1   1 
ATOM   3781 C  CD2   . PHE   B 2 198 ? 158.101 145.921 82.855  1.00 58.28  ? 198 PHE   B CD2   1 
ATOM   3782 C  CE1   . PHE   B 2 198 ? 157.184 147.665 84.781  1.00 55.63  ? 198 PHE   B CE1   1 
ATOM   3783 C  CE2   . PHE   B 2 198 ? 156.900 146.575 82.676  1.00 53.06  ? 198 PHE   B CE2   1 
ATOM   3784 C  CZ    . PHE   B 2 198 ? 156.442 147.448 83.640  1.00 56.67  ? 198 PHE   B CZ    1 
ATOM   3785 N  N     . VAL   B 2 199 ? 158.191 143.576 86.324  1.00 53.80  ? 199 VAL   B N     1 
ATOM   3786 C  CA    . VAL   B 2 199 ? 157.076 142.638 86.379  1.00 53.44  ? 199 VAL   B CA    1 
ATOM   3787 C  C     . VAL   B 2 199 ? 155.781 143.420 86.214  1.00 56.15  ? 199 VAL   B C     1 
ATOM   3788 O  O     . VAL   B 2 199 ? 155.541 144.388 86.944  1.00 62.09  ? 199 VAL   B O     1 
ATOM   3789 C  CB    . VAL   B 2 199 ? 157.064 141.842 87.697  1.00 55.40  ? 199 VAL   B CB    1 
ATOM   3790 C  CG1   . VAL   B 2 199 ? 156.006 140.754 87.652  1.00 57.17  ? 199 VAL   B CG1   1 
ATOM   3791 C  CG2   . VAL   B 2 199 ? 158.434 141.248 87.975  1.00 55.64  ? 199 VAL   B CG2   1 
ATOM   3792 N  N     . SER   B 2 200 ? 154.952 143.000 85.262  1.00 58.19  ? 200 SER   B N     1 
ATOM   3793 C  CA    . SER   B 2 200 ? 153.661 143.639 85.045  1.00 59.70  ? 200 SER   B CA    1 
ATOM   3794 C  C     . SER   B 2 200 ? 152.753 142.682 84.289  1.00 60.06  ? 200 SER   B C     1 
ATOM   3795 O  O     . SER   B 2 200 ? 153.216 141.788 83.576  1.00 67.00  ? 200 SER   B O     1 
ATOM   3796 C  CB    . SER   B 2 200 ? 153.804 144.957 84.278  1.00 59.76  ? 200 SER   B CB    1 
ATOM   3797 O  OG    . SER   B 2 200 ? 153.426 144.798 82.922  1.00 57.11  ? 200 SER   B OG    1 
ATOM   3798 N  N     . HIS   B 2 201 ? 151.447 142.886 84.456  1.00 58.55  ? 201 HIS   B N     1 
ATOM   3799 C  CA    . HIS   B 2 201 ? 150.433 142.133 83.733  1.00 56.17  ? 201 HIS   B CA    1 
ATOM   3800 C  C     . HIS   B 2 201 ? 149.912 142.883 82.514  1.00 56.91  ? 201 HIS   B C     1 
ATOM   3801 O  O     . HIS   B 2 201 ? 148.981 142.409 81.855  1.00 60.20  ? 201 HIS   B O     1 
ATOM   3802 C  CB    . HIS   B 2 201 ? 149.276 141.773 84.667  1.00 54.33  ? 201 HIS   B CB    1 
ATOM   3803 C  CG    . HIS   B 2 201 ? 149.544 140.576 85.526  1.00 62.90  ? 201 HIS   B CG    1 
ATOM   3804 N  ND1   . HIS   B 2 201 ? 149.714 139.311 85.007  1.00 63.29  ? 201 HIS   B ND1   1 
ATOM   3805 C  CD2   . HIS   B 2 201 ? 149.667 140.452 86.868  1.00 59.33  ? 201 HIS   B CD2   1 
ATOM   3806 C  CE1   . HIS   B 2 201 ? 149.931 138.459 85.993  1.00 60.99  ? 201 HIS   B CE1   1 
ATOM   3807 N  NE2   . HIS   B 2 201 ? 149.908 139.125 87.132  1.00 58.68  ? 201 HIS   B NE2   1 
ATOM   3808 N  N     . ASN   B 2 202 ? 150.487 144.043 82.206  1.00 65.60  ? 202 ASN   B N     1 
ATOM   3809 C  CA    . ASN   B 2 202 ? 150.173 144.799 80.999  1.00 65.42  ? 202 ASN   B CA    1 
ATOM   3810 C  C     . ASN   B 2 202 ? 151.221 144.445 79.950  1.00 68.52  ? 202 ASN   B C     1 
ATOM   3811 O  O     . ASN   B 2 202 ? 152.388 144.829 80.077  1.00 77.03  ? 202 ASN   B O     1 
ATOM   3812 C  CB    . ASN   B 2 202 ? 150.160 146.299 81.288  1.00 66.38  ? 202 ASN   B CB    1 
ATOM   3813 C  CG    . ASN   B 2 202 ? 149.491 147.103 80.193  1.00 69.62  ? 202 ASN   B CG    1 
ATOM   3814 O  OD1   . ASN   B 2 202 ? 149.367 146.647 79.057  1.00 70.89  ? 202 ASN   B OD1   1 
ATOM   3815 N  ND2   . ASN   B 2 202 ? 149.057 148.311 80.529  1.00 64.64  ? 202 ASN   B ND2   1 
ATOM   3816 N  N     . LEU   B 2 203 ? 150.807 143.710 78.918  1.00 67.20  ? 203 LEU   B N     1 
ATOM   3817 C  CA    . LEU   B 2 203 ? 151.758 143.196 77.941  1.00 68.22  ? 203 LEU   B CA    1 
ATOM   3818 C  C     . LEU   B 2 203 ? 152.325 144.278 77.032  1.00 72.29  ? 203 LEU   B C     1 
ATOM   3819 O  O     . LEU   B 2 203 ? 153.455 144.131 76.555  1.00 75.55  ? 203 LEU   B O     1 
ATOM   3820 C  CB    . LEU   B 2 203 ? 151.106 142.096 77.101  1.00 73.73  ? 203 LEU   B CB    1 
ATOM   3821 C  CG    . LEU   B 2 203 ? 150.846 140.769 77.822  1.00 76.38  ? 203 LEU   B CG    1 
ATOM   3822 C  CD1   . LEU   B 2 203 ? 150.703 139.632 76.824  1.00 71.63  ? 203 LEU   B CD1   1 
ATOM   3823 C  CD2   . LEU   B 2 203 ? 151.942 140.462 78.834  1.00 68.03  ? 203 LEU   B CD2   1 
ATOM   3824 N  N     . GLY   B 2 204 ? 151.579 145.355 76.779  1.00 72.28  ? 204 GLY   B N     1 
ATOM   3825 C  CA    . GLY   B 2 204 ? 152.140 146.463 76.021  1.00 69.39  ? 204 GLY   B CA    1 
ATOM   3826 C  C     . GLY   B 2 204 ? 153.256 147.169 76.768  1.00 71.22  ? 204 GLY   B C     1 
ATOM   3827 O  O     . GLY   B 2 204 ? 154.281 147.528 76.180  1.00 74.31  ? 204 GLY   B O     1 
ATOM   3828 N  N     . GLN   B 2 205 ? 153.072 147.377 78.074  1.00 67.88  ? 205 GLN   B N     1 
ATOM   3829 C  CA    . GLN   B 2 205 ? 154.130 147.960 78.890  1.00 64.37  ? 205 GLN   B CA    1 
ATOM   3830 C  C     . GLN   B 2 205 ? 155.353 147.053 78.934  1.00 70.27  ? 205 GLN   B C     1 
ATOM   3831 O  O     . GLN   B 2 205 ? 156.490 147.535 78.894  1.00 75.95  ? 205 GLN   B O     1 
ATOM   3832 C  CB    . GLN   B 2 205 ? 153.611 148.235 80.300  1.00 66.32  ? 205 GLN   B CB    1 
ATOM   3833 C  CG    . GLN   B 2 205 ? 153.414 149.706 80.614  1.00 66.81  ? 205 GLN   B CG    1 
ATOM   3834 C  CD    . GLN   B 2 205 ? 153.048 149.947 82.063  1.00 70.77  ? 205 GLN   B CD    1 
ATOM   3835 O  OE1   . GLN   B 2 205 ? 153.455 149.198 82.949  1.00 69.89  ? 205 GLN   B OE1   1 
ATOM   3836 N  NE2   . GLN   B 2 205 ? 152.277 150.997 82.312  1.00 74.37  ? 205 GLN   B NE2   1 
ATOM   3837 N  N     . VAL   B 2 206 ? 155.139 145.739 79.019  1.00 68.45  ? 206 VAL   B N     1 
ATOM   3838 C  CA    . VAL   B 2 206 ? 156.255 144.798 78.983  1.00 67.46  ? 206 VAL   B CA    1 
ATOM   3839 C  C     . VAL   B 2 206 ? 156.979 144.882 77.645  1.00 63.09  ? 206 VAL   B C     1 
ATOM   3840 O  O     . VAL   B 2 206 ? 158.215 144.874 77.591  1.00 71.10  ? 206 VAL   B O     1 
ATOM   3841 C  CB    . VAL   B 2 206 ? 155.757 143.370 79.273  1.00 66.35  ? 206 VAL   B CB    1 
ATOM   3842 C  CG1   . VAL   B 2 206 ? 156.816 142.346 78.899  1.00 65.28  ? 206 VAL   B CG1   1 
ATOM   3843 C  CG2   . VAL   B 2 206 ? 155.373 143.231 80.735  1.00 65.47  ? 206 VAL   B CG2   1 
ATOM   3844 N  N     . ARG   B 2 207 ? 156.227 144.964 76.546  1.00 70.25  ? 207 ARG   B N     1 
ATOM   3845 C  CA    . ARG   B 2 207 ? 156.843 145.056 75.227  1.00 75.91  ? 207 ARG   B CA    1 
ATOM   3846 C  C     . ARG   B 2 207 ? 157.669 146.328 75.083  1.00 79.21  ? 207 ARG   B C     1 
ATOM   3847 O  O     . ARG   B 2 207 ? 158.780 146.294 74.541  1.00 78.94  ? 207 ARG   B O     1 
ATOM   3848 C  CB    . ARG   B 2 207 ? 155.768 144.993 74.142  1.00 76.24  ? 207 ARG   B CB    1 
ATOM   3849 C  CG    . ARG   B 2 207 ? 156.284 145.273 72.741  1.00 76.35  ? 207 ARG   B CG    1 
ATOM   3850 C  CD    . ARG   B 2 207 ? 156.205 144.041 71.858  1.00 76.08  ? 207 ARG   B CD    1 
ATOM   3851 N  NE    . ARG   B 2 207 ? 154.914 143.375 71.968  1.00 80.02  ? 207 ARG   B NE    1 
ATOM   3852 C  CZ    . ARG   B 2 207 ? 154.644 142.177 71.469  1.00 80.91  ? 207 ARG   B CZ    1 
ATOM   3853 N  NH1   . ARG   B 2 207 ? 155.556 141.484 70.807  1.00 76.73  ? 207 ARG   B NH1   1 
ATOM   3854 N  NH2   . ARG   B 2 207 ? 153.429 141.663 71.635  1.00 81.41  ? 207 ARG   B NH2   1 
ATOM   3855 N  N     . GLN   B 2 208 ? 157.150 147.458 75.559  1.00 85.40  ? 208 GLN   B N     1 
ATOM   3856 C  CA    . GLN   B 2 208 ? 157.857 148.724 75.411  1.00 79.89  ? 208 GLN   B CA    1 
ATOM   3857 C  C     . GLN   B 2 208 ? 158.879 148.980 76.512  1.00 80.91  ? 208 GLN   B C     1 
ATOM   3858 O  O     . GLN   B 2 208 ? 159.596 149.984 76.443  1.00 82.79  ? 208 GLN   B O     1 
ATOM   3859 C  CB    . GLN   B 2 208 ? 156.861 149.889 75.359  1.00 77.36  ? 208 GLN   B CB    1 
ATOM   3860 C  CG    . GLN   B 2 208 ? 156.301 150.304 76.705  1.00 79.46  ? 208 GLN   B CG    1 
ATOM   3861 C  CD    . GLN   B 2 208 ? 155.000 151.071 76.576  1.00 84.03  ? 208 GLN   B CD    1 
ATOM   3862 O  OE1   . GLN   B 2 208 ? 154.341 151.025 75.539  1.00 83.98  ? 208 GLN   B OE1   1 
ATOM   3863 N  NE2   . GLN   B 2 208 ? 154.626 151.785 77.631  1.00 85.62  ? 208 GLN   B NE2   1 
ATOM   3864 N  N     . PHE   B 2 209 ? 158.970 148.108 77.515  1.00 75.49  ? 209 PHE   B N     1 
ATOM   3865 C  CA    . PHE   B 2 209 ? 159.919 148.271 78.611  1.00 71.58  ? 209 PHE   B CA    1 
ATOM   3866 C  C     . PHE   B 2 209 ? 161.068 147.270 78.556  1.00 71.99  ? 209 PHE   B C     1 
ATOM   3867 O  O     . PHE   B 2 209 ? 162.231 147.654 78.703  1.00 74.97  ? 209 PHE   B O     1 
ATOM   3868 C  CB    . PHE   B 2 209 ? 159.195 148.137 79.957  1.00 67.65  ? 209 PHE   B CB    1 
ATOM   3869 C  CG    . PHE   B 2 209 ? 158.767 149.445 80.555  1.00 69.83  ? 209 PHE   B CG    1 
ATOM   3870 C  CD1   . PHE   B 2 209 ? 157.816 150.231 79.930  1.00 71.99  ? 209 PHE   B CD1   1 
ATOM   3871 C  CD2   . PHE   B 2 209 ? 159.310 149.882 81.750  1.00 70.85  ? 209 PHE   B CD2   1 
ATOM   3872 C  CE1   . PHE   B 2 209 ? 157.418 151.433 80.483  1.00 70.76  ? 209 PHE   B CE1   1 
ATOM   3873 C  CE2   . PHE   B 2 209 ? 158.917 151.082 82.308  1.00 71.85  ? 209 PHE   B CE2   1 
ATOM   3874 C  CZ    . PHE   B 2 209 ? 157.970 151.858 81.674  1.00 70.74  ? 209 PHE   B CZ    1 
ATOM   3875 N  N     . CYS   B 2 210 ? 160.764 145.994 78.347  1.00 84.40  ? 210 CYS   B N     1 
ATOM   3876 C  CA    . CYS   B 2 210 ? 161.733 144.926 78.533  1.00 83.96  ? 210 CYS   B CA    1 
ATOM   3877 C  C     . CYS   B 2 210 ? 162.459 144.586 77.235  1.00 85.20  ? 210 CYS   B C     1 
ATOM   3878 O  O     . CYS   B 2 210 ? 162.023 144.932 76.135  1.00 85.92  ? 210 CYS   B O     1 
ATOM   3879 C  CB    . CYS   B 2 210 ? 161.044 143.677 79.083  1.00 81.59  ? 210 CYS   B CB    1 
ATOM   3880 S  SG    . CYS   B 2 210 ? 160.118 143.959 80.605  1.00 95.02  ? 210 CYS   B SG    1 
ATOM   3881 N  N     . THR   B 2 211 ? 163.591 143.894 77.388  1.00 88.50  ? 211 THR   B N     1 
ATOM   3882 C  CA    . THR   B 2 211 ? 164.370 143.390 76.266  1.00 89.60  ? 211 THR   B CA    1 
ATOM   3883 C  C     . THR   B 2 211 ? 164.610 141.888 76.312  1.00 87.91  ? 211 THR   B C     1 
ATOM   3884 O  O     . THR   B 2 211 ? 164.903 141.299 75.265  1.00 86.30  ? 211 THR   B O     1 
ATOM   3885 C  CB    . THR   B 2 211 ? 165.732 144.099 76.188  1.00 88.34  ? 211 THR   B CB    1 
ATOM   3886 O  OG1   . THR   B 2 211 ? 166.419 143.960 77.437  1.00 85.24  ? 211 THR   B OG1   1 
ATOM   3887 C  CG2   . THR   B 2 211 ? 165.548 145.576 75.875  1.00 86.34  ? 211 THR   B CG2   1 
ATOM   3888 N  N     . LYS   B 2 212 ? 164.503 141.257 77.480  1.00 86.83  ? 212 LYS   B N     1 
ATOM   3889 C  CA    . LYS   B 2 212 ? 164.587 139.810 77.610  1.00 84.77  ? 212 LYS   B CA    1 
ATOM   3890 C  C     . LYS   B 2 212 ? 163.424 139.329 78.464  1.00 86.92  ? 212 LYS   B C     1 
ATOM   3891 O  O     . LYS   B 2 212 ? 162.905 140.074 79.299  1.00 87.68  ? 212 LYS   B O     1 
ATOM   3892 C  CB    . LYS   B 2 212 ? 165.918 139.373 78.232  1.00 87.44  ? 212 LYS   B CB    1 
ATOM   3893 C  CG    . LYS   B 2 212 ? 166.970 138.974 77.213  1.00 90.41  ? 212 LYS   B CG    1 
ATOM   3894 C  CD    . LYS   B 2 212 ? 168.266 138.559 77.884  1.00 91.14  ? 212 LYS   B CD    1 
ATOM   3895 C  CE    . LYS   B 2 212 ? 169.294 139.673 77.814  1.00 91.23  ? 212 LYS   B CE    1 
ATOM   3896 N  NZ    . LYS   B 2 212 ? 170.625 139.240 78.322  1.00 91.88  ? 212 LYS   B NZ    1 
ATOM   3897 N  N     . ILE   B 2 213 ? 163.006 138.084 78.248  1.00 74.81  ? 213 ILE   B N     1 
ATOM   3898 C  CA    . ILE   B 2 213 ? 161.805 137.546 78.876  1.00 70.92  ? 213 ILE   B CA    1 
ATOM   3899 C  C     . ILE   B 2 213 ? 162.132 136.224 79.556  1.00 66.52  ? 213 ILE   B C     1 
ATOM   3900 O  O     . ILE   B 2 213 ? 162.808 135.361 78.975  1.00 68.22  ? 213 ILE   B O     1 
ATOM   3901 C  CB    . ILE   B 2 213 ? 160.662 137.372 77.860  1.00 69.18  ? 213 ILE   B CB    1 
ATOM   3902 C  CG1   . ILE   B 2 213 ? 160.230 138.731 77.318  1.00 70.61  ? 213 ILE   B CG1   1 
ATOM   3903 C  CG2   . ILE   B 2 213 ? 159.474 136.684 78.502  1.00 67.70  ? 213 ILE   B CG2   1 
ATOM   3904 C  CD1   . ILE   B 2 213 ? 159.369 139.524 78.280  1.00 70.65  ? 213 ILE   B CD1   1 
ATOM   3905 N  N     . ALA   B 2 214 ? 161.651 136.079 80.793  1.00 55.79  ? 214 ALA   B N     1 
ATOM   3906 C  CA    . ALA   B 2 214 ? 161.687 134.828 81.539  1.00 58.14  ? 214 ALA   B CA    1 
ATOM   3907 C  C     . ALA   B 2 214 ? 160.255 134.413 81.850  1.00 58.03  ? 214 ALA   B C     1 
ATOM   3908 O  O     . ALA   B 2 214 ? 159.502 135.179 82.464  1.00 63.62  ? 214 ALA   B O     1 
ATOM   3909 C  CB    . ALA   B 2 214 ? 162.498 134.979 82.827  1.00 60.26  ? 214 ALA   B CB    1 
ATOM   3910 N  N     . TRP   B 2 215 ? 159.890 133.202 81.440  1.00 60.52  ? 215 TRP   B N     1 
ATOM   3911 C  CA    . TRP   B 2 215 ? 158.538 132.676 81.590  1.00 57.61  ? 215 TRP   B CA    1 
ATOM   3912 C  C     . TRP   B 2 215 ? 158.533 131.635 82.702  1.00 60.93  ? 215 TRP   B C     1 
ATOM   3913 O  O     . TRP   B 2 215 ? 159.286 130.657 82.644  1.00 69.65  ? 215 TRP   B O     1 
ATOM   3914 C  CB    . TRP   B 2 215 ? 158.051 132.078 80.270  1.00 57.19  ? 215 TRP   B CB    1 
ATOM   3915 C  CG    . TRP   B 2 215 ? 156.663 131.501 80.295  1.00 59.91  ? 215 TRP   B CG    1 
ATOM   3916 C  CD1   . TRP   B 2 215 ? 155.731 131.627 81.284  1.00 57.01  ? 215 TRP   B CD1   1 
ATOM   3917 C  CD2   . TRP   B 2 215 ? 156.052 130.710 79.269  1.00 60.84  ? 215 TRP   B CD2   1 
ATOM   3918 N  NE1   . TRP   B 2 215 ? 154.582 130.958 80.940  1.00 53.72  ? 215 TRP   B NE1   1 
ATOM   3919 C  CE2   . TRP   B 2 215 ? 154.754 130.388 79.707  1.00 57.01  ? 215 TRP   B CE2   1 
ATOM   3920 C  CE3   . TRP   B 2 215 ? 156.479 130.242 78.023  1.00 61.52  ? 215 TRP   B CE3   1 
ATOM   3921 C  CZ2   . TRP   B 2 215 ? 153.880 129.620 78.944  1.00 58.39  ? 215 TRP   B CZ2   1 
ATOM   3922 C  CZ3   . TRP   B 2 215 ? 155.610 129.481 77.269  1.00 61.96  ? 215 TRP   B CZ3   1 
ATOM   3923 C  CH2   . TRP   B 2 215 ? 154.326 129.177 77.731  1.00 60.11  ? 215 TRP   B CH2   1 
ATOM   3924 N  N     . ILE   B 2 216 ? 157.682 131.843 83.704  1.00 61.29  ? 216 ILE   B N     1 
ATOM   3925 C  CA    . ILE   B 2 216 ? 157.596 130.975 84.873  1.00 63.80  ? 216 ILE   B CA    1 
ATOM   3926 C  C     . ILE   B 2 216 ? 156.210 130.347 84.896  1.00 71.07  ? 216 ILE   B C     1 
ATOM   3927 O  O     . ILE   B 2 216 ? 155.201 131.062 84.863  1.00 77.17  ? 216 ILE   B O     1 
ATOM   3928 C  CB    . ILE   B 2 216 ? 157.869 131.745 86.175  1.00 66.91  ? 216 ILE   B CB    1 
ATOM   3929 C  CG1   . ILE   B 2 216 ? 159.299 132.285 86.187  1.00 72.02  ? 216 ILE   B CG1   1 
ATOM   3930 C  CG2   . ILE   B 2 216 ? 157.629 130.858 87.381  1.00 69.66  ? 216 ILE   B CG2   1 
ATOM   3931 C  CD1   . ILE   B 2 216 ? 159.545 133.324 87.253  1.00 69.03  ? 216 ILE   B CD1   1 
ATOM   3932 N  N     . GLU   B 2 217 ? 156.160 129.017 84.958  1.00 81.35  ? 217 GLU   B N     1 
ATOM   3933 C  CA    . GLU   B 2 217 ? 154.903 128.274 84.973  1.00 80.92  ? 217 GLU   B CA    1 
ATOM   3934 C  C     . GLU   B 2 217 ? 154.966 127.226 86.075  1.00 81.55  ? 217 GLU   B C     1 
ATOM   3935 O  O     . GLU   B 2 217 ? 155.695 126.236 85.953  1.00 85.02  ? 217 GLU   B O     1 
ATOM   3936 C  CB    . GLU   B 2 217 ? 154.632 127.619 83.620  1.00 80.00  ? 217 GLU   B CB    1 
ATOM   3937 C  CG    . GLU   B 2 217 ? 153.355 126.800 83.570  1.00 84.07  ? 217 GLU   B CG    1 
ATOM   3938 C  CD    . GLU   B 2 217 ? 152.500 127.132 82.364  1.00 86.93  ? 217 GLU   B CD    1 
ATOM   3939 O  OE1   . GLU   B 2 217 ? 152.100 128.307 82.223  1.00 85.31  ? 217 GLU   B OE1   1 
ATOM   3940 O  OE2   . GLU   B 2 217 ? 152.228 126.219 81.556  1.00 87.85  ? 217 GLU   B OE2   1 
ATOM   3941 N  N     . GLY   B 2 218 ? 154.199 127.437 87.139  1.00 74.05  ? 218 GLY   B N     1 
ATOM   3942 C  CA    . GLY   B 2 218 ? 154.159 126.488 88.238  1.00 73.15  ? 218 GLY   B CA    1 
ATOM   3943 C  C     . GLY   B 2 218 ? 155.466 126.345 88.986  1.00 74.99  ? 218 GLY   B C     1 
ATOM   3944 O  O     . GLY   B 2 218 ? 155.817 125.234 89.405  1.00 78.66  ? 218 GLY   B O     1 
ATOM   3945 N  N     . GLY   B 2 219 ? 156.199 127.441 89.163  1.00 71.43  ? 219 GLY   B N     1 
ATOM   3946 C  CA    . GLY   B 2 219 ? 157.453 127.414 89.882  1.00 71.84  ? 219 GLY   B CA    1 
ATOM   3947 C  C     . GLY   B 2 219 ? 158.648 126.942 89.086  1.00 75.84  ? 219 GLY   B C     1 
ATOM   3948 O  O     . GLY   B 2 219 ? 159.751 126.877 89.641  1.00 80.48  ? 219 GLY   B O     1 
ATOM   3949 N  N     . LYS   B 2 220 ? 158.474 126.614 87.809  1.00 88.24  ? 220 LYS   B N     1 
ATOM   3950 C  CA    . LYS   B 2 220 ? 159.556 126.140 86.961  1.00 88.27  ? 220 LYS   B CA    1 
ATOM   3951 C  C     . LYS   B 2 220 ? 159.714 127.065 85.764  1.00 87.10  ? 220 LYS   B C     1 
ATOM   3952 O  O     . LYS   B 2 220 ? 158.723 127.500 85.169  1.00 90.55  ? 220 LYS   B O     1 
ATOM   3953 C  CB    . LYS   B 2 220 ? 159.301 124.707 86.482  1.00 89.29  ? 220 LYS   B CB    1 
ATOM   3954 C  CG    . LYS   B 2 220 ? 159.373 123.665 87.583  1.00 89.42  ? 220 LYS   B CG    1 
ATOM   3955 C  CD    . LYS   B 2 220 ? 158.459 122.489 87.287  1.00 91.24  ? 220 LYS   B CD    1 
ATOM   3956 C  CE    . LYS   B 2 220 ? 157.940 121.855 88.567  1.00 90.98  ? 220 LYS   B CE    1 
ATOM   3957 N  NZ    . LYS   B 2 220 ? 158.130 120.378 88.570  1.00 90.52  ? 220 LYS   B NZ    1 
ATOM   3958 N  N     . LEU   B 2 221 ? 160.962 127.362 85.414  1.00 78.04  ? 221 LEU   B N     1 
ATOM   3959 C  CA    . LEU   B 2 221 ? 161.250 128.242 84.287  1.00 80.16  ? 221 LEU   B CA    1 
ATOM   3960 C  C     . LEU   B 2 221 ? 160.968 127.508 82.983  1.00 82.84  ? 221 LEU   B C     1 
ATOM   3961 O  O     . LEU   B 2 221 ? 161.749 126.648 82.563  1.00 84.31  ? 221 LEU   B O     1 
ATOM   3962 C  CB    . LEU   B 2 221 ? 162.699 128.714 84.343  1.00 79.31  ? 221 LEU   B CB    1 
ATOM   3963 C  CG    . LEU   B 2 221 ? 162.989 130.051 83.662  1.00 79.30  ? 221 LEU   B CG    1 
ATOM   3964 C  CD1   . LEU   B 2 221 ? 162.612 131.204 84.572  1.00 81.20  ? 221 LEU   B CD1   1 
ATOM   3965 C  CD2   . LEU   B 2 221 ? 164.451 130.136 83.262  1.00 80.75  ? 221 LEU   B CD2   1 
ATOM   3966 N  N     . LYS   B 2 222 ? 159.850 127.841 82.340  1.00 76.17  ? 222 LYS   B N     1 
ATOM   3967 C  CA    . LYS   B 2 222 ? 159.505 127.232 81.062  1.00 72.44  ? 222 LYS   B CA    1 
ATOM   3968 C  C     . LYS   B 2 222 ? 160.478 127.650 79.969  1.00 78.59  ? 222 LYS   B C     1 
ATOM   3969 O  O     . LYS   B 2 222 ? 160.958 126.803 79.208  1.00 80.11  ? 222 LYS   B O     1 
ATOM   3970 C  CB    . LYS   B 2 222 ? 158.074 127.593 80.662  1.00 70.86  ? 222 LYS   B CB    1 
ATOM   3971 C  CG    . LYS   B 2 222 ? 157.027 126.627 81.184  1.00 73.70  ? 222 LYS   B CG    1 
ATOM   3972 C  CD    . LYS   B 2 222 ? 155.998 126.273 80.122  1.00 75.99  ? 222 LYS   B CD    1 
ATOM   3973 C  CE    . LYS   B 2 222 ? 156.609 126.222 78.731  1.00 76.37  ? 222 LYS   B CE    1 
ATOM   3974 N  NZ    . LYS   B 2 222 ? 156.941 124.831 78.319  1.00 77.92  ? 222 LYS   B NZ    1 
ATOM   3975 N  N     . ASP   B 2 223 ? 160.778 128.945 79.876  1.00 92.15  ? 223 ASP   B N     1 
ATOM   3976 C  CA    . ASP   B 2 223 ? 161.635 129.455 78.814  1.00 91.71  ? 223 ASP   B CA    1 
ATOM   3977 C  C     . ASP   B 2 223 ? 162.243 130.793 79.211  1.00 92.27  ? 223 ASP   B C     1 
ATOM   3978 O  O     . ASP   B 2 223 ? 161.558 131.651 79.776  1.00 95.63  ? 223 ASP   B O     1 
ATOM   3979 C  CB    . ASP   B 2 223 ? 160.851 129.605 77.507  1.00 91.67  ? 223 ASP   B CB    1 
ATOM   3980 C  CG    . ASP   B 2 223 ? 161.750 129.857 76.317  1.00 95.85  ? 223 ASP   B CG    1 
ATOM   3981 O  OD1   . ASP   B 2 223 ? 162.919 129.422 76.350  1.00 93.87  ? 223 ASP   B OD1   1 
ATOM   3982 O  OD2   . ASP   B 2 223 ? 161.293 130.504 75.355  1.00 99.65  ? 223 ASP   B OD2   1 
ATOM   3983 N  N     . TYR   B 2 224 ? 163.527 130.960 78.908  1.00 84.69  ? 224 TYR   B N     1 
ATOM   3984 C  CA    . TYR   B 2 224 ? 164.245 132.220 79.039  1.00 84.19  ? 224 TYR   B CA    1 
ATOM   3985 C  C     . TYR   B 2 224 ? 164.838 132.536 77.677  1.00 84.76  ? 224 TYR   B C     1 
ATOM   3986 O  O     . TYR   B 2 224 ? 165.461 131.668 77.054  1.00 85.91  ? 224 TYR   B O     1 
ATOM   3987 C  CB    . TYR   B 2 224 ? 165.342 132.114 80.116  1.00 87.37  ? 224 TYR   B CB    1 
ATOM   3988 C  CG    . TYR   B 2 224 ? 166.194 133.359 80.409  1.00 87.61  ? 224 TYR   B CG    1 
ATOM   3989 C  CD1   . TYR   B 2 224 ? 166.101 134.517 79.650  1.00 87.36  ? 224 TYR   B CD1   1 
ATOM   3990 C  CD2   . TYR   B 2 224 ? 167.101 133.362 81.457  1.00 87.22  ? 224 TYR   B CD2   1 
ATOM   3991 C  CE1   . TYR   B 2 224 ? 166.884 135.627 79.917  1.00 88.43  ? 224 TYR   B CE1   1 
ATOM   3992 C  CE2   . TYR   B 2 224 ? 167.888 134.473 81.729  1.00 86.35  ? 224 TYR   B CE2   1 
ATOM   3993 C  CZ    . TYR   B 2 224 ? 167.768 135.603 80.966  1.00 84.45  ? 224 TYR   B CZ    1 
ATOM   3994 O  OH    . TYR   B 2 224 ? 168.551 136.699 81.244  1.00 82.38  ? 224 TYR   B OH    1 
ATOM   3995 N  N     . GLY   B 2 225 ? 164.636 133.762 77.211  1.00 82.89  ? 225 GLY   B N     1 
ATOM   3996 C  CA    . GLY   B 2 225 ? 165.245 134.164 75.961  1.00 82.42  ? 225 GLY   B CA    1 
ATOM   3997 C  C     . GLY   B 2 225 ? 164.962 135.620 75.658  1.00 83.23  ? 225 GLY   B C     1 
ATOM   3998 O  O     . GLY   B 2 225 ? 164.660 136.416 76.549  1.00 86.83  ? 225 GLY   B O     1 
ATOM   3999 N  N     . GLU   B 2 226 ? 165.084 135.948 74.376  1.00 89.84  ? 226 GLU   B N     1 
ATOM   4000 C  CA    . GLU   B 2 226 ? 164.829 137.304 73.921  1.00 91.30  ? 226 GLU   B CA    1 
ATOM   4001 C  C     . GLU   B 2 226 ? 163.333 137.600 73.966  1.00 93.86  ? 226 GLU   B C     1 
ATOM   4002 O  O     . GLU   B 2 226 ? 162.501 136.693 74.050  1.00 96.94  ? 226 GLU   B O     1 
ATOM   4003 C  CB    . GLU   B 2 226 ? 165.369 137.488 72.502  1.00 89.88  ? 226 GLU   B CB    1 
ATOM   4004 C  CG    . GLU   B 2 226 ? 166.232 138.725 72.298  1.00 93.36  ? 226 GLU   B CG    1 
ATOM   4005 C  CD    . GLU   B 2 226 ? 167.330 138.855 73.338  1.00 96.10  ? 226 GLU   B CD    1 
ATOM   4006 O  OE1   . GLU   B 2 226 ? 168.186 137.949 73.414  1.00 95.87  ? 226 GLU   B OE1   1 
ATOM   4007 O  OE2   . GLU   B 2 226 ? 167.346 139.868 74.068  1.00 94.77  ? 226 GLU   B OE2   1 
ATOM   4008 N  N     . LEU   B 2 227 ? 162.997 138.892 73.926  1.00 92.24  ? 227 LEU   B N     1 
ATOM   4009 C  CA    . LEU   B 2 227 ? 161.595 139.302 73.898  1.00 91.81  ? 227 LEU   B CA    1 
ATOM   4010 C  C     . LEU   B 2 227 ? 160.860 138.696 72.709  1.00 93.95  ? 227 LEU   B C     1 
ATOM   4011 O  O     . LEU   B 2 227 ? 159.812 138.055 72.874  1.00 97.58  ? 227 LEU   B O     1 
ATOM   4012 C  CB    . LEU   B 2 227 ? 161.508 140.830 73.853  1.00 94.17  ? 227 LEU   B CB    1 
ATOM   4013 C  CG    . LEU   B 2 227 ? 160.139 141.511 73.950  1.00 90.54  ? 227 LEU   B CG    1 
ATOM   4014 C  CD1   . LEU   B 2 227 ? 159.654 141.606 75.382  1.00 88.76  ? 227 LEU   B CD1   1 
ATOM   4015 C  CD2   . LEU   B 2 227 ? 160.173 142.892 73.307  1.00 92.52  ? 227 LEU   B CD2   1 
ATOM   4016 N  N     . ASP   B 2 228 ? 161.420 138.855 71.506  1.00 103.19 ? 228 ASP   B N     1 
ATOM   4017 C  CA    . ASP   B 2 228 ? 160.704 138.500 70.284  1.00 103.13 ? 228 ASP   B CA    1 
ATOM   4018 C  C     . ASP   B 2 228 ? 160.502 136.995 70.165  1.00 105.00 ? 228 ASP   B C     1 
ATOM   4019 O  O     . ASP   B 2 228 ? 159.681 136.535 69.364  1.00 109.06 ? 228 ASP   B O     1 
ATOM   4020 C  CB    . ASP   B 2 228 ? 161.458 139.033 69.066  1.00 105.41 ? 228 ASP   B CB    1 
ATOM   4021 C  CG    . ASP   B 2 228 ? 160.826 140.283 68.489  1.00 105.43 ? 228 ASP   B CG    1 
ATOM   4022 O  OD1   . ASP   B 2 228 ? 159.594 140.288 68.287  1.00 104.30 ? 228 ASP   B OD1   1 
ATOM   4023 O  OD2   . ASP   B 2 228 ? 161.561 141.261 68.239  1.00 104.60 ? 228 ASP   B OD2   1 
ATOM   4024 N  N     . ASP   B 2 229 ? 161.253 136.210 70.938  1.00 100.86 ? 229 ASP   B N     1 
ATOM   4025 C  CA    . ASP   B 2 229 ? 161.090 134.762 70.885  1.00 99.86  ? 229 ASP   B CA    1 
ATOM   4026 C  C     . ASP   B 2 229 ? 160.128 134.274 71.961  1.00 99.08  ? 229 ASP   B C     1 
ATOM   4027 O  O     . ASP   B 2 229 ? 159.178 133.539 71.670  1.00 100.19 ? 229 ASP   B O     1 
ATOM   4028 C  CB    . ASP   B 2 229 ? 162.449 134.075 71.023  1.00 100.60 ? 229 ASP   B CB    1 
ATOM   4029 C  CG    . ASP   B 2 229 ? 163.496 134.666 70.103  1.00 104.38 ? 229 ASP   B CG    1 
ATOM   4030 O  OD1   . ASP   B 2 229 ? 164.692 134.359 70.286  1.00 104.76 ? 229 ASP   B OD1   1 
ATOM   4031 O  OD2   . ASP   B 2 229 ? 163.121 135.437 69.194  1.00 104.59 ? 229 ASP   B OD2   1 
ATOM   4032 N  N     . VAL   B 2 230 ? 160.358 134.672 73.213  1.00 82.68  ? 230 VAL   B N     1 
ATOM   4033 C  CA    . VAL   B 2 230 ? 159.576 134.122 74.315  1.00 82.37  ? 230 VAL   B CA    1 
ATOM   4034 C  C     . VAL   B 2 230 ? 158.168 134.706 74.340  1.00 84.14  ? 230 VAL   B C     1 
ATOM   4035 O  O     . VAL   B 2 230 ? 157.198 133.988 74.612  1.00 86.85  ? 230 VAL   B O     1 
ATOM   4036 C  CB    . VAL   B 2 230 ? 160.303 134.340 75.652  1.00 78.24  ? 230 VAL   B CB    1 
ATOM   4037 C  CG1   . VAL   B 2 230 ? 159.618 133.549 76.752  1.00 80.09  ? 230 VAL   B CG1   1 
ATOM   4038 C  CG2   . VAL   B 2 230 ? 161.746 133.919 75.529  1.00 76.57  ? 230 VAL   B CG2   1 
ATOM   4039 N  N     . LEU   B 2 231 ? 158.026 136.008 74.082  1.00 72.14  ? 231 LEU   B N     1 
ATOM   4040 C  CA    . LEU   B 2 231 ? 156.707 136.627 74.213  1.00 71.72  ? 231 LEU   B CA    1 
ATOM   4041 C  C     . LEU   B 2 231 ? 155.649 136.019 73.292  1.00 74.96  ? 231 LEU   B C     1 
ATOM   4042 O  O     . LEU   B 2 231 ? 154.525 135.776 73.771  1.00 76.16  ? 231 LEU   B O     1 
ATOM   4043 C  CB    . LEU   B 2 231 ? 156.818 138.141 73.996  1.00 74.46  ? 231 LEU   B CB    1 
ATOM   4044 C  CG    . LEU   B 2 231 ? 155.761 138.987 74.709  1.00 72.64  ? 231 LEU   B CG    1 
ATOM   4045 C  CD1   . LEU   B 2 231 ? 155.718 138.655 76.192  1.00 66.55  ? 231 LEU   B CD1   1 
ATOM   4046 C  CD2   . LEU   B 2 231 ? 156.020 140.468 74.497  1.00 73.26  ? 231 LEU   B CD2   1 
ATOM   4047 N  N     . PRO   B 2 232 ? 155.910 135.768 72.001  1.00 86.62  ? 232 PRO   B N     1 
ATOM   4048 C  CA    . PRO   B 2 232 ? 154.873 135.133 71.170  1.00 90.06  ? 232 PRO   B CA    1 
ATOM   4049 C  C     . PRO   B 2 232 ? 154.421 133.777 71.682  1.00 87.80  ? 232 PRO   B C     1 
ATOM   4050 O  O     . PRO   B 2 232 ? 153.238 133.444 71.553  1.00 86.67  ? 232 PRO   B O     1 
ATOM   4051 C  CB    . PRO   B 2 232 ? 155.556 135.031 69.801  1.00 88.62  ? 232 PRO   B CB    1 
ATOM   4052 C  CG    . PRO   B 2 232 ? 156.472 136.196 69.788  1.00 86.79  ? 232 PRO   B CG    1 
ATOM   4053 C  CD    . PRO   B 2 232 ? 157.056 136.186 71.172  1.00 84.31  ? 232 PRO   B CD    1 
ATOM   4054 N  N     . LYS   B 2 233 ? 155.325 132.978 72.255  1.00 81.05  ? 233 LYS   B N     1 
ATOM   4055 C  CA    . LYS   B 2 233 ? 154.914 131.694 72.814  1.00 82.26  ? 233 LYS   B CA    1 
ATOM   4056 C  C     . LYS   B 2 233 ? 153.948 131.880 73.977  1.00 83.13  ? 233 LYS   B C     1 
ATOM   4057 O  O     . LYS   B 2 233 ? 152.952 131.155 74.088  1.00 88.37  ? 233 LYS   B O     1 
ATOM   4058 C  CB    . LYS   B 2 233 ? 156.134 130.889 73.259  1.00 82.53  ? 233 LYS   B CB    1 
ATOM   4059 C  CG    . LYS   B 2 233 ? 157.339 131.012 72.349  1.00 83.03  ? 233 LYS   B CG    1 
ATOM   4060 C  CD    . LYS   B 2 233 ? 158.581 130.445 73.015  1.00 83.16  ? 233 LYS   B CD    1 
ATOM   4061 C  CE    . LYS   B 2 233 ? 159.452 129.701 72.017  1.00 81.51  ? 233 LYS   B CE    1 
ATOM   4062 N  NZ    . LYS   B 2 233 ? 159.854 130.567 70.876  1.00 84.38  ? 233 LYS   B NZ    1 
ATOM   4063 N  N     . TYR   B 2 234 ? 154.227 132.844 74.856  1.00 66.94  ? 234 TYR   B N     1 
ATOM   4064 C  CA    . TYR   B 2 234 ? 153.326 133.104 75.974  1.00 62.27  ? 234 TYR   B CA    1 
ATOM   4065 C  C     . TYR   B 2 234 ? 151.967 133.585 75.483  1.00 65.12  ? 234 TYR   B C     1 
ATOM   4066 O  O     . TYR   B 2 234 ? 150.924 133.162 76.000  1.00 73.38  ? 234 TYR   B O     1 
ATOM   4067 C  CB    . TYR   B 2 234 ? 153.953 134.125 76.922  1.00 61.95  ? 234 TYR   B CB    1 
ATOM   4068 C  CG    . TYR   B 2 234 ? 153.139 134.393 78.164  1.00 59.40  ? 234 TYR   B CG    1 
ATOM   4069 C  CD1   . TYR   B 2 234 ? 152.677 133.351 78.953  1.00 61.11  ? 234 TYR   B CD1   1 
ATOM   4070 C  CD2   . TYR   B 2 234 ? 152.834 135.689 78.550  1.00 62.38  ? 234 TYR   B CD2   1 
ATOM   4071 C  CE1   . TYR   B 2 234 ? 151.934 133.592 80.090  1.00 58.93  ? 234 TYR   B CE1   1 
ATOM   4072 C  CE2   . TYR   B 2 234 ? 152.092 135.940 79.683  1.00 63.47  ? 234 TYR   B CE2   1 
ATOM   4073 C  CZ    . TYR   B 2 234 ? 151.644 134.889 80.449  1.00 62.00  ? 234 TYR   B CZ    1 
ATOM   4074 O  OH    . TYR   B 2 234 ? 150.904 135.137 81.580  1.00 69.77  ? 234 TYR   B OH    1 
ATOM   4075 N  N     . GLU   B 2 235 ? 151.954 134.464 74.478  1.00 71.84  ? 235 GLU   B N     1 
ATOM   4076 C  CA    . GLU   B 2 235 ? 150.678 134.921 73.935  1.00 73.99  ? 235 GLU   B CA    1 
ATOM   4077 C  C     . GLU   B 2 235 ? 149.904 133.775 73.291  1.00 78.97  ? 235 GLU   B C     1 
ATOM   4078 O  O     . GLU   B 2 235 ? 148.684 133.666 73.464  1.00 78.86  ? 235 GLU   B O     1 
ATOM   4079 C  CB    . GLU   B 2 235 ? 150.904 136.055 72.936  1.00 74.97  ? 235 GLU   B CB    1 
ATOM   4080 C  CG    . GLU   B 2 235 ? 151.087 137.417 73.590  1.00 79.47  ? 235 GLU   B CG    1 
ATOM   4081 C  CD    . GLU   B 2 235 ? 151.937 138.358 72.762  1.00 81.24  ? 235 GLU   B CD    1 
ATOM   4082 O  OE1   . GLU   B 2 235 ? 152.509 137.909 71.747  1.00 79.46  ? 235 GLU   B OE1   1 
ATOM   4083 O  OE2   . GLU   B 2 235 ? 152.034 139.549 73.125  1.00 77.20  ? 235 GLU   B OE2   1 
ATOM   4084 N  N     . ALA   B 2 236 ? 150.595 132.906 72.549  1.00 80.75  ? 236 ALA   B N     1 
ATOM   4085 C  CA    . ALA   B 2 236 ? 149.930 131.760 71.939  1.00 79.12  ? 236 ALA   B CA    1 
ATOM   4086 C  C     . ALA   B 2 236 ? 149.364 130.826 72.999  1.00 75.92  ? 236 ALA   B C     1 
ATOM   4087 O  O     . ALA   B 2 236 ? 148.267 130.280 72.833  1.00 79.95  ? 236 ALA   B O     1 
ATOM   4088 C  CB    . ALA   B 2 236 ? 150.901 131.013 71.026  1.00 78.03  ? 236 ALA   B CB    1 
ATOM   4089 N  N     . PHE   B 2 237 ? 150.099 130.629 74.096  1.00 66.10  ? 237 PHE   B N     1 
ATOM   4090 C  CA    . PHE   B 2 237 ? 149.592 129.806 75.188  1.00 66.07  ? 237 PHE   B CA    1 
ATOM   4091 C  C     . PHE   B 2 237 ? 148.349 130.428 75.813  1.00 65.00  ? 237 PHE   B C     1 
ATOM   4092 O  O     . PHE   B 2 237 ? 147.396 129.718 76.151  1.00 70.48  ? 237 PHE   B O     1 
ATOM   4093 C  CB    . PHE   B 2 237 ? 150.685 129.598 76.237  1.00 68.00  ? 237 PHE   B CB    1 
ATOM   4094 C  CG    . PHE   B 2 237 ? 150.166 129.438 77.639  1.00 70.10  ? 237 PHE   B CG    1 
ATOM   4095 C  CD1   . PHE   B 2 237 ? 149.621 128.235 78.053  1.00 69.07  ? 237 PHE   B CD1   1 
ATOM   4096 C  CD2   . PHE   B 2 237 ? 150.234 130.483 78.544  1.00 70.21  ? 237 PHE   B CD2   1 
ATOM   4097 C  CE1   . PHE   B 2 237 ? 149.145 128.080 79.340  1.00 67.06  ? 237 PHE   B CE1   1 
ATOM   4098 C  CE2   . PHE   B 2 237 ? 149.758 130.333 79.833  1.00 70.42  ? 237 PHE   B CE2   1 
ATOM   4099 C  CZ    . PHE   B 2 237 ? 149.214 129.130 80.231  1.00 67.86  ? 237 PHE   B CZ    1 
ATOM   4100 N  N     . LEU   B 2 238 ? 148.340 131.755 75.975  1.00 63.95  ? 238 LEU   B N     1 
ATOM   4101 C  CA    . LEU   B 2 238 ? 147.158 132.420 76.520  1.00 68.16  ? 238 LEU   B CA    1 
ATOM   4102 C  C     . LEU   B 2 238 ? 145.947 132.244 75.610  1.00 72.40  ? 238 LEU   B C     1 
ATOM   4103 O  O     . LEU   B 2 238 ? 144.841 131.951 76.082  1.00 76.02  ? 238 LEU   B O     1 
ATOM   4104 C  CB    . LEU   B 2 238 ? 147.441 133.905 76.747  1.00 70.63  ? 238 LEU   B CB    1 
ATOM   4105 C  CG    . LEU   B 2 238 ? 148.418 134.274 77.863  1.00 67.26  ? 238 LEU   B CG    1 
ATOM   4106 C  CD1   . LEU   B 2 238 ? 148.860 135.718 77.718  1.00 70.85  ? 238 LEU   B CD1   1 
ATOM   4107 C  CD2   . LEU   B 2 238 ? 147.787 134.043 79.224  1.00 64.56  ? 238 LEU   B CD2   1 
ATOM   4108 N  N     . ASN   B 2 239 ? 146.134 132.420 74.299  1.00 86.75  ? 239 ASN   B N     1 
ATOM   4109 C  CA    . ASN   B 2 239 ? 145.023 132.216 73.368  1.00 87.27  ? 239 ASN   B CA    1 
ATOM   4110 C  C     . ASN   B 2 239 ? 144.545 130.767 73.371  1.00 85.87  ? 239 ASN   B C     1 
ATOM   4111 O  O     . ASN   B 2 239 ? 143.336 130.505 73.319  1.00 88.85  ? 239 ASN   B O     1 
ATOM   4112 C  CB    . ASN   B 2 239 ? 145.419 132.654 71.959  1.00 88.92  ? 239 ASN   B CB    1 
ATOM   4113 C  CG    . ASN   B 2 239 ? 146.148 133.979 71.945  1.00 91.09  ? 239 ASN   B CG    1 
ATOM   4114 O  OD1   . ASN   B 2 239 ? 146.311 134.619 72.983  1.00 90.18  ? 239 ASN   B OD1   1 
ATOM   4115 N  ND2   . ASN   B 2 239 ? 146.597 134.396 70.768  1.00 89.82  ? 239 ASN   B ND2   1 
ATOM   4116 N  N     . ASP   B 2 240 ? 145.475 129.811 73.432  1.00 88.11  ? 240 ASP   B N     1 
ATOM   4117 C  CA    . ASP   B 2 240 ? 145.081 128.407 73.486  1.00 87.56  ? 240 ASP   B CA    1 
ATOM   4118 C  C     . ASP   B 2 240 ? 144.292 128.104 74.753  1.00 87.84  ? 240 ASP   B C     1 
ATOM   4119 O  O     . ASP   B 2 240 ? 143.311 127.354 74.716  1.00 90.21  ? 240 ASP   B O     1 
ATOM   4120 C  CB    . ASP   B 2 240 ? 146.315 127.511 73.394  1.00 91.08  ? 240 ASP   B CB    1 
ATOM   4121 C  CG    . ASP   B 2 240 ? 146.061 126.254 72.590  1.00 93.51  ? 240 ASP   B CG    1 
ATOM   4122 O  OD1   . ASP   B 2 240 ? 146.444 126.220 71.403  1.00 93.42  ? 240 ASP   B OD1   1 
ATOM   4123 O  OD2   . ASP   B 2 240 ? 145.475 125.300 73.144  1.00 95.48  ? 240 ASP   B OD2   1 
ATOM   4124 N  N     . PHE   B 2 241 ? 144.709 128.676 75.885  1.00 81.82  ? 241 PHE   B N     1 
ATOM   4125 C  CA    . PHE   B 2 241 ? 143.960 128.496 77.125  1.00 79.92  ? 241 PHE   B CA    1 
ATOM   4126 C  C     . PHE   B 2 241 ? 142.572 129.111 77.020  1.00 82.58  ? 241 PHE   B C     1 
ATOM   4127 O  O     . PHE   B 2 241 ? 141.600 128.566 77.556  1.00 86.33  ? 241 PHE   B O     1 
ATOM   4128 C  CB    . PHE   B 2 241 ? 144.728 129.103 78.297  1.00 78.86  ? 241 PHE   B CB    1 
ATOM   4129 C  CG    . PHE   B 2 241 ? 144.263 128.618 79.639  1.00 81.16  ? 241 PHE   B CG    1 
ATOM   4130 C  CD1   . PHE   B 2 241 ? 144.811 127.482 80.206  1.00 84.50  ? 241 PHE   B CD1   1 
ATOM   4131 C  CD2   . PHE   B 2 241 ? 143.275 129.297 80.331  1.00 82.20  ? 241 PHE   B CD2   1 
ATOM   4132 C  CE1   . PHE   B 2 241 ? 144.385 127.033 81.440  1.00 84.33  ? 241 PHE   B CE1   1 
ATOM   4133 C  CE2   . PHE   B 2 241 ? 142.845 128.852 81.565  1.00 84.44  ? 241 PHE   B CE2   1 
ATOM   4134 C  CZ    . PHE   B 2 241 ? 143.402 127.720 82.120  1.00 83.36  ? 241 PHE   B CZ    1 
ATOM   4135 N  N     . LYS   B 2 242 ? 142.462 130.257 76.345  1.00 88.99  ? 242 LYS   B N     1 
ATOM   4136 C  CA    . LYS   B 2 242 ? 141.146 130.840 76.101  1.00 87.86  ? 242 LYS   B CA    1 
ATOM   4137 C  C     . LYS   B 2 242 ? 140.284 129.913 75.252  1.00 89.56  ? 242 LYS   B C     1 
ATOM   4138 O  O     . LYS   B 2 242 ? 139.064 129.842 75.439  1.00 90.82  ? 242 LYS   B O     1 
ATOM   4139 C  CB    . LYS   B 2 242 ? 141.288 132.204 75.427  1.00 87.75  ? 242 LYS   B CB    1 
ATOM   4140 C  CG    . LYS   B 2 242 ? 141.152 133.384 76.375  1.00 89.04  ? 242 LYS   B CG    1 
ATOM   4141 C  CD    . LYS   B 2 242 ? 141.803 134.632 75.801  1.00 90.17  ? 242 LYS   B CD    1 
ATOM   4142 C  CE    . LYS   B 2 242 ? 142.664 135.334 76.837  1.00 90.55  ? 242 LYS   B CE    1 
ATOM   4143 N  NZ    . LYS   B 2 242 ? 142.857 136.774 76.513  1.00 88.03  ? 242 LYS   B NZ    1 
ATOM   4144 N  N     . LYS   B 2 243 ? 140.903 129.199 74.308  1.00 96.04  ? 243 LYS   B N     1 
ATOM   4145 C  CA    . LYS   B 2 243 ? 140.151 128.272 73.465  1.00 94.30  ? 243 LYS   B CA    1 
ATOM   4146 C  C     . LYS   B 2 243 ? 139.585 127.108 74.270  1.00 95.46  ? 243 LYS   B C     1 
ATOM   4147 O  O     . LYS   B 2 243 ? 138.476 126.635 73.994  1.00 93.54  ? 243 LYS   B O     1 
ATOM   4148 C  CB    . LYS   B 2 243 ? 141.040 127.751 72.335  1.00 93.84  ? 243 LYS   B CB    1 
ATOM   4149 C  CG    . LYS   B 2 243 ? 140.733 128.342 70.970  1.00 94.55  ? 243 LYS   B CG    1 
ATOM   4150 C  CD    . LYS   B 2 243 ? 140.560 129.848 71.036  1.00 94.58  ? 243 LYS   B CD    1 
ATOM   4151 C  CE    . LYS   B 2 243 ? 140.433 130.440 69.643  1.00 94.03  ? 243 LYS   B CE    1 
ATOM   4152 N  NZ    . LYS   B 2 243 ? 141.594 130.077 68.785  1.00 97.39  ? 243 LYS   B NZ    1 
ATOM   4153 N  N     . LYS   B 2 244 ? 140.332 126.629 75.263  1.00 99.95  ? 244 LYS   B N     1 
ATOM   4154 C  CA    . LYS   B 2 244 ? 139.960 125.409 75.970  1.00 96.49  ? 244 LYS   B CA    1 
ATOM   4155 C  C     . LYS   B 2 244 ? 138.666 125.588 76.754  1.00 99.95  ? 244 LYS   B C     1 
ATOM   4156 O  O     . LYS   B 2 244 ? 138.322 126.693 77.182  1.00 99.97  ? 244 LYS   B O     1 
ATOM   4157 C  CB    . LYS   B 2 244 ? 141.087 124.984 76.913  1.00 94.82  ? 244 LYS   B CB    1 
ATOM   4158 C  CG    . LYS   B 2 244 ? 142.368 124.579 76.203  1.00 95.59  ? 244 LYS   B CG    1 
ATOM   4159 C  CD    . LYS   B 2 244 ? 143.578 124.678 77.120  1.00 96.68  ? 244 LYS   B CD    1 
ATOM   4160 C  CE    . LYS   B 2 244 ? 143.232 124.325 78.556  1.00 96.89  ? 244 LYS   B CE    1 
ATOM   4161 N  NZ    . LYS   B 2 244 ? 144.414 123.799 79.291  1.00 98.25  ? 244 LYS   B NZ    1 
ATOM   4162 N  N     . SER   B 2 245 ? 137.946 124.483 76.938  1.00 103.93 ? 245 SER   B N     1 
ATOM   4163 C  CA    . SER   B 2 245 ? 136.711 124.493 77.706  1.00 103.53 ? 245 SER   B CA    1 
ATOM   4164 C  C     . SER   B 2 245 ? 137.009 124.527 79.204  1.00 103.99 ? 245 SER   B C     1 
ATOM   4165 O  O     . SER   B 2 245 ? 138.153 124.380 79.643  1.00 103.74 ? 245 SER   B O     1 
ATOM   4166 C  CB    . SER   B 2 245 ? 135.858 123.271 77.368  1.00 101.57 ? 245 SER   B CB    1 
ATOM   4167 O  OG    . SER   B 2 245 ? 136.432 122.087 77.894  1.00 101.82 ? 245 SER   B OG    1 
ATOM   4168 N  N     . LYS   B 2 246 ? 135.948 124.718 79.992  1.00 96.92  ? 246 LYS   B N     1 
ATOM   4169 C  CA    . LYS   B 2 246 ? 136.107 124.877 81.436  1.00 96.60  ? 246 LYS   B CA    1 
ATOM   4170 C  C     . LYS   B 2 246 ? 136.672 123.616 82.081  1.00 95.95  ? 246 LYS   B C     1 
ATOM   4171 O  O     . LYS   B 2 246 ? 137.521 123.695 82.979  1.00 97.23  ? 246 LYS   B O     1 
ATOM   4172 C  CB    . LYS   B 2 246 ? 134.767 125.256 82.066  1.00 96.55  ? 246 LYS   B CB    1 
ATOM   4173 C  CG    . LYS   B 2 246 ? 134.841 125.590 83.545  1.00 97.44  ? 246 LYS   B CG    1 
ATOM   4174 C  CD    . LYS   B 2 246 ? 133.487 126.045 84.069  1.00 98.63  ? 246 LYS   B CD    1 
ATOM   4175 C  CE    . LYS   B 2 246 ? 132.455 124.933 83.981  1.00 97.24  ? 246 LYS   B CE    1 
ATOM   4176 N  NZ    . LYS   B 2 246 ? 131.380 125.091 84.999  1.00 93.60  ? 246 LYS   B NZ    1 
ATOM   4177 N  N     . ALA   B 2 247 ? 136.210 122.442 81.641  1.00 95.23  ? 247 ALA   B N     1 
ATOM   4178 C  CA    . ALA   B 2 247 ? 136.709 121.192 82.206  1.00 97.94  ? 247 ALA   B CA    1 
ATOM   4179 C  C     . ALA   B 2 247 ? 138.197 121.015 81.932  1.00 99.36  ? 247 ALA   B C     1 
ATOM   4180 O  O     . ALA   B 2 247 ? 138.948 120.567 82.808  1.00 96.87  ? 247 ALA   B O     1 
ATOM   4181 C  CB    . ALA   B 2 247 ? 135.915 120.012 81.649  1.00 96.41  ? 247 ALA   B CB    1 
ATOM   4182 N  N     . GLU   B 2 248 ? 138.643 121.354 80.720  1.00 100.53 ? 248 GLU   B N     1 
ATOM   4183 C  CA    . GLU   B 2 248 ? 140.060 121.235 80.391  1.00 99.05  ? 248 GLU   B CA    1 
ATOM   4184 C  C     . GLU   B 2 248 ? 140.905 122.197 81.218  1.00 100.26 ? 248 GLU   B C     1 
ATOM   4185 O  O     . GLU   B 2 248 ? 142.000 121.841 81.671  1.00 104.52 ? 248 GLU   B O     1 
ATOM   4186 C  CB    . GLU   B 2 248 ? 140.268 121.473 78.897  1.00 98.58  ? 248 GLU   B CB    1 
ATOM   4187 C  CG    . GLU   B 2 248 ? 139.433 120.562 78.013  1.00 100.75 ? 248 GLU   B CG    1 
ATOM   4188 C  CD    . GLU   B 2 248 ? 139.677 120.795 76.536  1.00 101.91 ? 248 GLU   B CD    1 
ATOM   4189 O  OE1   . GLU   B 2 248 ? 140.706 120.313 76.019  1.00 99.01  ? 248 GLU   B OE1   1 
ATOM   4190 O  OE2   . GLU   B 2 248 ? 138.838 121.458 75.892  1.00 102.23 ? 248 GLU   B OE2   1 
ATOM   4191 N  N     . GLN   B 2 249 ? 140.418 123.424 81.419  1.00 92.02  ? 249 GLN   B N     1 
ATOM   4192 C  CA    . GLN   B 2 249 ? 141.129 124.374 82.268  1.00 94.22  ? 249 GLN   B CA    1 
ATOM   4193 C  C     . GLN   B 2 249 ? 141.238 123.856 83.697  1.00 94.31  ? 249 GLN   B C     1 
ATOM   4194 O  O     . GLN   B 2 249 ? 142.302 123.952 84.326  1.00 96.80  ? 249 GLN   B O     1 
ATOM   4195 C  CB    . GLN   B 2 249 ? 140.418 125.727 82.244  1.00 94.87  ? 249 GLN   B CB    1 
ATOM   4196 C  CG    . GLN   B 2 249 ? 140.297 126.342 80.860  1.00 94.92  ? 249 GLN   B CG    1 
ATOM   4197 C  CD    . GLN   B 2 249 ? 139.278 127.465 80.809  1.00 94.38  ? 249 GLN   B CD    1 
ATOM   4198 O  OE1   . GLN   B 2 249 ? 138.518 127.672 81.755  1.00 95.02  ? 249 GLN   B OE1   1 
ATOM   4199 N  NE2   . GLN   B 2 249 ? 139.254 128.193 79.699  1.00 92.19  ? 249 GLN   B NE2   1 
ATOM   4200 N  N     . LYS   B 2 250 ? 140.144 123.299 84.222  1.00 95.97  ? 250 LYS   B N     1 
ATOM   4201 C  CA    . LYS   B 2 250 ? 140.171 122.740 85.569  1.00 99.48  ? 250 LYS   B CA    1 
ATOM   4202 C  C     . LYS   B 2 250 ? 141.153 121.580 85.662  1.00 99.98  ? 250 LYS   B C     1 
ATOM   4203 O  O     . LYS   B 2 250 ? 141.886 121.456 86.650  1.00 97.59  ? 250 LYS   B O     1 
ATOM   4204 C  CB    . LYS   B 2 250 ? 138.768 122.293 85.978  1.00 97.71  ? 250 LYS   B CB    1 
ATOM   4205 C  CG    . LYS   B 2 250 ? 138.404 122.624 87.415  1.00 98.50  ? 250 LYS   B CG    1 
ATOM   4206 C  CD    . LYS   B 2 250 ? 137.007 122.131 87.757  1.00 98.91  ? 250 LYS   B CD    1 
ATOM   4207 C  CE    . LYS   B 2 250 ? 135.980 122.644 86.760  1.00 100.17 ? 250 LYS   B CE    1 
ATOM   4208 N  NZ    . LYS   B 2 250 ? 134.652 122.870 87.393  1.00 97.20  ? 250 LYS   B NZ    1 
ATOM   4209 N  N     . GLU   B 2 251 ? 141.186 120.722 84.640  1.00 100.51 ? 251 GLU   B N     1 
ATOM   4210 C  CA    . GLU   B 2 251 ? 142.118 119.599 84.642  1.00 99.54  ? 251 GLU   B CA    1 
ATOM   4211 C  C     . GLU   B 2 251 ? 143.565 120.080 84.600  1.00 102.14 ? 251 GLU   B C     1 
ATOM   4212 O  O     . GLU   B 2 251 ? 144.431 119.522 85.283  1.00 104.31 ? 251 GLU   B O     1 
ATOM   4213 C  CB    . GLU   B 2 251 ? 141.812 118.667 83.466  1.00 98.04  ? 251 GLU   B CB    1 
ATOM   4214 C  CG    . GLU   B 2 251 ? 142.675 117.410 83.395  1.00 102.83 ? 251 GLU   B CG    1 
ATOM   4215 C  CD    . GLU   B 2 251 ? 143.948 117.592 82.585  1.00 105.00 ? 251 GLU   B CD    1 
ATOM   4216 O  OE1   . GLU   B 2 251 ? 144.671 116.593 82.388  1.00 105.10 ? 251 GLU   B OE1   1 
ATOM   4217 O  OE2   . GLU   B 2 251 ? 144.214 118.720 82.121  1.00 103.36 ? 251 GLU   B OE2   1 
ATOM   4218 N  N     . PHE   B 2 252 ? 143.848 121.107 83.795  1.00 98.71  ? 252 PHE   B N     1 
ATOM   4219 C  CA    . PHE   B 2 252 ? 145.204 121.646 83.723  1.00 96.70  ? 252 PHE   B CA    1 
ATOM   4220 C  C     . PHE   B 2 252 ? 145.635 122.230 85.065  1.00 97.78  ? 252 PHE   B C     1 
ATOM   4221 O  O     . PHE   B 2 252 ? 146.755 121.976 85.540  1.00 98.07  ? 252 PHE   B O     1 
ATOM   4222 C  CB    . PHE   B 2 252 ? 145.274 122.694 82.609  1.00 95.44  ? 252 PHE   B CB    1 
ATOM   4223 C  CG    . PHE   B 2 252 ? 146.454 123.623 82.701  1.00 99.10  ? 252 PHE   B CG    1 
ATOM   4224 C  CD1   . PHE   B 2 252 ? 147.660 123.286 82.110  1.00 98.26  ? 252 PHE   B CD1   1 
ATOM   4225 C  CD2   . PHE   B 2 252 ? 146.347 124.848 83.340  1.00 99.00  ? 252 PHE   B CD2   1 
ATOM   4226 C  CE1   . PHE   B 2 252 ? 148.745 124.139 82.179  1.00 97.58  ? 252 PHE   B CE1   1 
ATOM   4227 C  CE2   . PHE   B 2 252 ? 147.429 125.705 83.413  1.00 98.06  ? 252 PHE   B CE2   1 
ATOM   4228 C  CZ    . PHE   B 2 252 ? 148.628 125.350 82.830  1.00 97.65  ? 252 PHE   B CZ    1 
ATOM   4229 N  N     . ARG   B 2 253 ? 144.750 123.003 85.701  1.00 101.49 ? 253 ARG   B N     1 
ATOM   4230 C  CA    . ARG   B 2 253 ? 145.069 123.559 87.012  1.00 104.48 ? 253 ARG   B CA    1 
ATOM   4231 C  C     . ARG   B 2 253 ? 145.271 122.455 88.044  1.00 106.59 ? 253 ARG   B C     1 
ATOM   4232 O  O     . ARG   B 2 253 ? 146.174 122.539 88.887  1.00 105.95 ? 253 ARG   B O     1 
ATOM   4233 C  CB    . ARG   B 2 253 ? 143.968 124.520 87.456  1.00 104.79 ? 253 ARG   B CB    1 
ATOM   4234 C  CG    . ARG   B 2 253 ? 143.896 125.791 86.630  1.00 104.57 ? 253 ARG   B CG    1 
ATOM   4235 C  CD    . ARG   B 2 253 ? 143.834 127.024 87.515  1.00 105.22 ? 253 ARG   B CD    1 
ATOM   4236 N  NE    . ARG   B 2 253 ? 143.972 128.255 86.747  1.00 105.38 ? 253 ARG   B NE    1 
ATOM   4237 C  CZ    . ARG   B 2 253 ? 143.002 128.804 86.028  1.00 107.58 ? 253 ARG   B CZ    1 
ATOM   4238 N  NH1   . ARG   B 2 253 ? 141.801 128.256 85.955  1.00 107.77 ? 253 ARG   B NH1   1 
ATOM   4239 N  NH2   . ARG   B 2 253 ? 143.244 129.933 85.367  1.00 105.36 ? 253 ARG   B NH2   1 
ATOM   4240 N  N     . ASN   B 2 254 ? 144.440 121.410 87.993  1.00 106.77 ? 254 ASN   B N     1 
ATOM   4241 C  CA    . ASN   B 2 254 ? 144.582 120.301 88.929  1.00 105.11 ? 254 ASN   B CA    1 
ATOM   4242 C  C     . ASN   B 2 254 ? 145.895 119.560 88.717  1.00 104.31 ? 254 ASN   B C     1 
ATOM   4243 O  O     . ASN   B 2 254 ? 146.525 119.118 89.682  1.00 106.45 ? 254 ASN   B O     1 
ATOM   4244 C  CB    . ASN   B 2 254 ? 143.397 119.346 88.792  1.00 105.91 ? 254 ASN   B CB    1 
ATOM   4245 C  CG    . ASN   B 2 254 ? 142.129 119.903 89.404  1.00 108.38 ? 254 ASN   B CG    1 
ATOM   4246 O  OD1   . ASN   B 2 254 ? 142.049 121.089 89.723  1.00 107.48 ? 254 ASN   B OD1   1 
ATOM   4247 N  ND2   . ASN   B 2 254 ? 141.128 119.047 89.573  1.00 108.48 ? 254 ASN   B ND2   1 
ATOM   4248 N  N     . LYS   B 2 255 ? 146.318 119.403 87.461  1.00 104.95 ? 255 LYS   B N     1 
ATOM   4249 C  CA    . LYS   B 2 255 ? 147.603 118.764 87.192  1.00 105.03 ? 255 LYS   B CA    1 
ATOM   4250 C  C     . LYS   B 2 255 ? 148.756 119.589 87.750  1.00 105.19 ? 255 LYS   B C     1 
ATOM   4251 O  O     . LYS   B 2 255 ? 149.690 119.042 88.352  1.00 103.33 ? 255 LYS   B O     1 
ATOM   4252 C  CB    . LYS   B 2 255 ? 147.777 118.543 85.690  1.00 103.90 ? 255 LYS   B CB    1 
ATOM   4253 C  CG    . LYS   B 2 255 ? 147.340 117.169 85.213  1.00 104.89 ? 255 LYS   B CG    1 
ATOM   4254 C  CD    . LYS   B 2 255 ? 147.764 116.921 83.775  1.00 105.69 ? 255 LYS   B CD    1 
ATOM   4255 C  CE    . LYS   B 2 255 ? 149.274 117.003 83.622  1.00 106.57 ? 255 LYS   B CE    1 
ATOM   4256 N  NZ    . LYS   B 2 255 ? 149.688 117.024 82.193  1.00 104.34 ? 255 LYS   B NZ    1 
ATOM   4257 N  N     . LEU   B 2 256 ? 148.706 120.913 87.567  1.00 96.90  ? 256 LEU   B N     1 
ATOM   4258 C  CA    . LEU   B 2 256 ? 149.744 121.760 88.152  1.00 95.19  ? 256 LEU   B CA    1 
ATOM   4259 C  C     . LEU   B 2 256 ? 149.757 121.650 89.674  1.00 96.13  ? 256 LEU   B C     1 
ATOM   4260 O  O     . LEU   B 2 256 ? 150.827 121.547 90.291  1.00 94.41  ? 256 LEU   B O     1 
ATOM   4261 C  CB    . LEU   B 2 256 ? 149.550 123.215 87.724  1.00 95.01  ? 256 LEU   B CB    1 
ATOM   4262 C  CG    . LEU   B 2 256 ? 149.793 123.560 86.255  1.00 93.99  ? 256 LEU   B CG    1 
ATOM   4263 C  CD1   . LEU   B 2 256 ? 149.957 125.060 86.095  1.00 93.16  ? 256 LEU   B CD1   1 
ATOM   4264 C  CD2   . LEU   B 2 256 ? 151.012 122.827 85.721  1.00 94.50  ? 256 LEU   B CD2   1 
ATOM   4265 N  N     . ASP   B 2 257 ? 148.574 121.658 90.296  1.00 103.42 ? 257 ASP   B N     1 
ATOM   4266 C  CA    . ASP   B 2 257 ? 148.499 121.554 91.750  1.00 101.90 ? 257 ASP   B CA    1 
ATOM   4267 C  C     . ASP   B 2 257 ? 149.028 120.210 92.237  1.00 102.05 ? 257 ASP   B C     1 
ATOM   4268 O  O     . ASP   B 2 257 ? 149.704 120.136 93.269  1.00 101.97 ? 257 ASP   B O     1 
ATOM   4269 C  CB    . ASP   B 2 257 ? 147.060 121.765 92.218  1.00 102.88 ? 257 ASP   B CB    1 
ATOM   4270 C  CG    . ASP   B 2 257 ? 146.961 122.746 93.366  1.00 106.34 ? 257 ASP   B CG    1 
ATOM   4271 O  OD1   . ASP   B 2 257 ? 147.884 123.573 93.521  1.00 105.59 ? 257 ASP   B OD1   1 
ATOM   4272 O  OD2   . ASP   B 2 257 ? 145.963 122.691 94.115  1.00 105.34 ? 257 ASP   B OD2   1 
ATOM   4273 N  N     . GLU   B 2 258 ? 148.722 119.135 91.509  1.00 97.82  ? 258 GLU   B N     1 
ATOM   4274 C  CA    . GLU   B 2 258 ? 149.260 117.822 91.847  1.00 95.49  ? 258 GLU   B CA    1 
ATOM   4275 C  C     . GLU   B 2 258 ? 150.779 117.818 91.763  1.00 94.50  ? 258 GLU   B C     1 
ATOM   4276 O  O     . GLU   B 2 258 ? 151.456 117.248 92.628  1.00 96.23  ? 258 GLU   B O     1 
ATOM   4277 C  CB    . GLU   B 2 258 ? 148.666 116.763 90.918  1.00 97.93  ? 258 GLU   B CB    1 
ATOM   4278 C  CG    . GLU   B 2 258 ? 149.619 115.638 90.547  1.00 99.09  ? 258 GLU   B CG    1 
ATOM   4279 C  CD    . GLU   B 2 258 ? 149.123 114.819 89.371  1.00 100.21 ? 258 GLU   B CD    1 
ATOM   4280 O  OE1   . GLU   B 2 258 ? 147.892 114.735 89.179  1.00 99.11  ? 258 GLU   B OE1   1 
ATOM   4281 O  OE2   . GLU   B 2 258 ? 149.965 114.261 88.636  1.00 99.32  ? 258 GLU   B OE2   1 
ATOM   4282 N  N     . SER   B 2 259 ? 151.334 118.451 90.728  1.00 88.27  ? 259 SER   B N     1 
ATOM   4283 C  CA    . SER   B 2 259 ? 152.786 118.499 90.591  1.00 91.46  ? 259 SER   B CA    1 
ATOM   4284 C  C     . SER   B 2 259 ? 153.429 119.290 91.725  1.00 88.75  ? 259 SER   B C     1 
ATOM   4285 O  O     . SER   B 2 259 ? 154.515 118.936 92.199  1.00 83.21  ? 259 SER   B O     1 
ATOM   4286 C  CB    . SER   B 2 259 ? 153.167 119.099 89.237  1.00 91.59  ? 259 SER   B CB    1 
ATOM   4287 O  OG    . SER   B 2 259 ? 154.377 119.830 89.327  1.00 89.23  ? 259 SER   B OG    1 
ATOM   4288 N  N     . ARG   B 2 260 ? 152.778 120.367 92.174  1.00 89.40  ? 260 ARG   B N     1 
ATOM   4289 C  CA    . ARG   B 2 260 ? 153.431 121.273 93.118  1.00 88.33  ? 260 ARG   B CA    1 
ATOM   4290 C  C     . ARG   B 2 260 ? 153.468 120.706 94.538  1.00 88.99  ? 260 ARG   B C     1 
ATOM   4291 O  O     . ARG   B 2 260 ? 154.453 120.901 95.259  1.00 88.58  ? 260 ARG   B O     1 
ATOM   4292 C  CB    . ARG   B 2 260 ? 152.740 122.636 93.095  1.00 87.40  ? 260 ARG   B CB    1 
ATOM   4293 C  CG    . ARG   B 2 260 ? 153.179 123.513 91.933  1.00 86.07  ? 260 ARG   B CG    1 
ATOM   4294 C  CD    . ARG   B 2 260 ? 152.597 124.911 92.032  1.00 90.20  ? 260 ARG   B CD    1 
ATOM   4295 N  NE    . ARG   B 2 260 ? 153.634 125.935 92.011  1.00 90.15  ? 260 ARG   B NE    1 
ATOM   4296 C  CZ    . ARG   B 2 260 ? 153.399 127.239 92.049  1.00 85.00  ? 260 ARG   B CZ    1 
ATOM   4297 N  NH1   . ARG   B 2 260 ? 152.167 127.718 92.096  1.00 85.54  ? 260 ARG   B NH1   1 
ATOM   4298 N  NH2   . ARG   B 2 260 ? 154.425 128.084 92.039  1.00 82.70  ? 260 ARG   B NH2   1 
ATOM   4299 N  N     . PHE   B 2 261 ? 152.416 120.007 94.959  1.00 99.34  ? 261 PHE   B N     1 
ATOM   4300 C  CA    . PHE   B 2 261 ? 152.309 119.490 96.322  1.00 97.81  ? 261 PHE   B CA    1 
ATOM   4301 C  C     . PHE   B 2 261 ? 152.965 118.116 96.400  1.00 99.02  ? 261 PHE   B C     1 
ATOM   4302 O  O     . PHE   B 2 261 ? 152.833 117.312 95.471  1.00 96.33  ? 261 PHE   B O     1 
ATOM   4303 C  CB    . PHE   B 2 261 ? 150.847 119.391 96.761  1.00 94.38  ? 261 PHE   B CB    1 
ATOM   4304 C  CG    . PHE   B 2 261 ? 150.193 120.716 97.031  1.00 96.96  ? 261 PHE   B CG    1 
ATOM   4305 C  CD1   . PHE   B 2 261 ? 149.850 121.563 95.993  1.00 95.70  ? 261 PHE   B CD1   1 
ATOM   4306 C  CD2   . PHE   B 2 261 ? 149.904 121.105 98.327  1.00 98.74  ? 261 PHE   B CD2   1 
ATOM   4307 C  CE1   . PHE   B 2 261 ? 149.243 122.777 96.244  1.00 96.08  ? 261 PHE   B CE1   1 
ATOM   4308 C  CE2   . PHE   B 2 261 ? 149.296 122.318 98.581  1.00 95.97  ? 261 PHE   B CE2   1 
ATOM   4309 C  CZ    . PHE   B 2 261 ? 148.966 123.154 97.539  1.00 96.03  ? 261 PHE   B CZ    1 
ATOM   4310 N  N     . VAL   B 2 262 ? 153.665 117.841 97.506  1.00 105.41 ? 262 VAL   B N     1 
ATOM   4311 C  CA    . VAL   B 2 262 ? 154.215 116.508 97.735  1.00 103.61 ? 262 VAL   B CA    1 
ATOM   4312 C  C     . VAL   B 2 262 ? 154.385 116.272 99.230  1.00 103.41 ? 262 VAL   B C     1 
ATOM   4313 O  O     . VAL   B 2 262 ? 154.665 117.195 99.998  1.00 102.62 ? 262 VAL   B O     1 
ATOM   4314 C  CB    . VAL   B 2 262 ? 155.552 116.294 96.981  1.00 104.95 ? 262 VAL   B CB    1 
ATOM   4315 C  CG1   . VAL   B 2 262 ? 156.718 116.898 97.742  1.00 102.89 ? 262 VAL   B CG1   1 
ATOM   4316 C  CG2   . VAL   B 2 262 ? 155.784 114.813 96.719  1.00 103.42 ? 262 VAL   B CG2   1 
ATOM   4317 N  N     . ILE   B 2 263 ? 154.210 115.020 99.644  1.00 114.60 ? 263 ILE   B N     1 
ATOM   4318 C  CA    . ILE   B 2 263 ? 154.311 114.631 101.047 1.00 115.60 ? 263 ILE   B CA    1 
ATOM   4319 C  C     . ILE   B 2 263 ? 155.715 114.081 101.268 1.00 116.32 ? 263 ILE   B C     1 
ATOM   4320 O  O     . ILE   B 2 263 ? 156.008 112.932 100.927 1.00 115.39 ? 263 ILE   B O     1 
ATOM   4321 C  CB    . ILE   B 2 263 ? 153.238 113.610 101.435 1.00 115.90 ? 263 ILE   B CB    1 
ATOM   4322 C  CG1   . ILE   B 2 263 ? 151.868 114.049 100.915 1.00 115.51 ? 263 ILE   B CG1   1 
ATOM   4323 C  CG2   . ILE   B 2 263 ? 153.202 113.426 102.944 1.00 113.64 ? 263 ILE   B CG2   1 
ATOM   4324 C  CD1   . ILE   B 2 263 ? 150.722 113.209 101.435 1.00 114.37 ? 263 ILE   B CD1   1 
ATOM   4325 N  N     . LYS   B 2 264 ? 156.585 114.901 101.852 1.00 113.27 ? 264 LYS   B N     1 
ATOM   4326 C  CA    . LYS   B 2 264 ? 157.956 114.498 102.149 1.00 111.17 ? 264 LYS   B CA    1 
ATOM   4327 C  C     . LYS   B 2 264 ? 158.597 115.462 103.141 1.00 112.14 ? 264 LYS   B C     1 
ATOM   4328 O  O     . LYS   B 2 264 ? 158.140 116.592 103.311 1.00 113.43 ? 264 LYS   B O     1 
ATOM   4329 C  CB    . LYS   B 2 264 ? 158.792 114.428 100.867 1.00 109.28 ? 264 LYS   B CB    1 
ATOM   4330 C  CG    . LYS   B 2 264 ? 159.152 115.783 100.279 1.00 110.59 ? 264 LYS   B CG    1 
ATOM   4331 C  CD    . LYS   B 2 264 ? 160.633 116.085 100.449 1.00 111.32 ? 264 LYS   B CD    1 
ATOM   4332 C  CE    . LYS   B 2 264 ? 160.958 117.508 100.026 1.00 111.67 ? 264 LYS   B CE    1 
ATOM   4333 N  NZ    . LYS   B 2 264 ? 162.416 117.796 100.119 1.00 108.75 ? 264 LYS   B NZ    1 
ATOM   4334 O  OXT   . LYS   B 2 264 ? 159.589 115.138 103.793 1.00 111.24 ? 264 LYS   B OXT   1 
ATOM   4335 N  N     . MET   C 2 1   ? 115.846 152.122 79.166  1.00 115.92 ? 1   MET   D N     1 
ATOM   4336 C  CA    . MET   C 2 1   ? 116.043 153.540 79.443  1.00 118.23 ? 1   MET   D CA    1 
ATOM   4337 C  C     . MET   C 2 1   ? 115.718 153.870 80.896  1.00 117.61 ? 1   MET   D C     1 
ATOM   4338 O  O     . MET   C 2 1   ? 115.260 154.969 81.204  1.00 117.96 ? 1   MET   D O     1 
ATOM   4339 C  CB    . MET   C 2 1   ? 115.185 154.394 78.508  1.00 119.90 ? 1   MET   D CB    1 
ATOM   4340 C  CG    . MET   C 2 1   ? 115.639 154.375 77.059  1.00 121.03 ? 1   MET   D CG    1 
ATOM   4341 S  SD    . MET   C 2 1   ? 116.771 155.725 76.676  1.00 122.41 ? 1   MET   D SD    1 
ATOM   4342 C  CE    . MET   C 2 1   ? 115.647 157.120 76.690  1.00 118.25 ? 1   MET   D CE    1 
ATOM   4343 N  N     . ASN   C 2 2   ? 115.959 152.911 81.786  1.00 114.53 ? 2   ASN   D N     1 
ATOM   4344 C  CA    . ASN   C 2 2   ? 115.711 153.109 83.208  1.00 114.19 ? 2   ASN   D CA    1 
ATOM   4345 C  C     . ASN   C 2 2   ? 116.880 153.866 83.825  1.00 113.76 ? 2   ASN   D C     1 
ATOM   4346 O  O     . ASN   C 2 2   ? 118.026 153.406 83.764  1.00 115.26 ? 2   ASN   D O     1 
ATOM   4347 C  CB    . ASN   C 2 2   ? 115.509 151.767 83.907  1.00 115.26 ? 2   ASN   D CB    1 
ATOM   4348 C  CG    . ASN   C 2 2   ? 114.545 150.863 83.166  1.00 116.38 ? 2   ASN   D CG    1 
ATOM   4349 O  OD1   . ASN   C 2 2   ? 113.787 151.315 82.307  1.00 116.80 ? 2   ASN   D OD1   1 
ATOM   4350 N  ND2   . ASN   C 2 2   ? 114.568 149.578 83.495  1.00 114.88 ? 2   ASN   D ND2   1 
ATOM   4351 N  N     . VAL   C 2 3   ? 116.593 155.021 84.421  1.00 102.48 ? 3   VAL   D N     1 
ATOM   4352 C  CA    . VAL   C 2 3   ? 117.630 155.832 85.053  1.00 103.56 ? 3   VAL   D CA    1 
ATOM   4353 C  C     . VAL   C 2 3   ? 118.122 155.087 86.290  1.00 103.92 ? 3   VAL   D C     1 
ATOM   4354 O  O     . VAL   C 2 3   ? 117.415 155.001 87.297  1.00 107.11 ? 3   VAL   D O     1 
ATOM   4355 C  CB    . VAL   C 2 3   ? 117.112 157.228 85.414  1.00 101.91 ? 3   VAL   D CB    1 
ATOM   4356 C  CG1   . VAL   C 2 3   ? 118.198 158.033 86.108  1.00 101.12 ? 3   VAL   D CG1   1 
ATOM   4357 C  CG2   . VAL   C 2 3   ? 116.621 157.948 84.170  1.00 103.75 ? 3   VAL   D CG2   1 
ATOM   4358 N  N     . SER   C 2 4   ? 119.340 154.547 86.216  1.00 96.48  ? 4   SER   D N     1 
ATOM   4359 C  CA    . SER   C 2 4   ? 119.874 153.766 87.326  1.00 95.50  ? 4   SER   D CA    1 
ATOM   4360 C  C     . SER   C 2 4   ? 120.388 154.669 88.442  1.00 94.16  ? 4   SER   D C     1 
ATOM   4361 O  O     . SER   C 2 4   ? 119.966 154.550 89.595  1.00 95.45  ? 4   SER   D O     1 
ATOM   4362 C  CB    . SER   C 2 4   ? 120.984 152.837 86.830  1.00 99.33  ? 4   SER   D CB    1 
ATOM   4363 O  OG    . SER   C 2 4   ? 120.532 151.496 86.761  1.00 100.82 ? 4   SER   D OG    1 
ATOM   4364 N  N     . VAL   C 2 5   ? 121.308 155.574 88.115  1.00 89.58  ? 5   VAL   D N     1 
ATOM   4365 C  CA    . VAL   C 2 5   ? 121.887 156.495 89.087  1.00 89.96  ? 5   VAL   D CA    1 
ATOM   4366 C  C     . VAL   C 2 5   ? 121.741 157.912 88.555  1.00 89.92  ? 5   VAL   D C     1 
ATOM   4367 O  O     . VAL   C 2 5   ? 122.023 158.170 87.381  1.00 90.32  ? 5   VAL   D O     1 
ATOM   4368 C  CB    . VAL   C 2 5   ? 123.366 156.175 89.374  1.00 87.78  ? 5   VAL   D CB    1 
ATOM   4369 C  CG1   . VAL   C 2 5   ? 123.857 156.972 90.574  1.00 85.79  ? 5   VAL   D CG1   1 
ATOM   4370 C  CG2   . VAL   C 2 5   ? 123.560 154.686 89.607  1.00 88.87  ? 5   VAL   D CG2   1 
ATOM   4371 N  N     . ASN   C 2 6   ? 121.302 158.828 89.412  1.00 90.05  ? 6   ASN   D N     1 
ATOM   4372 C  CA    . ASN   C 2 6   ? 121.226 160.236 89.048  1.00 88.63  ? 6   ASN   D CA    1 
ATOM   4373 C  C     . ASN   C 2 6   ? 121.985 161.077 90.062  1.00 90.20  ? 6   ASN   D C     1 
ATOM   4374 O  O     . ASN   C 2 6   ? 121.798 160.922 91.276  1.00 92.78  ? 6   ASN   D O     1 
ATOM   4375 C  CB    . ASN   C 2 6   ? 119.777 160.709 88.924  1.00 89.55  ? 6   ASN   D CB    1 
ATOM   4376 C  CG    . ASN   C 2 6   ? 119.573 161.646 87.758  1.00 90.21  ? 6   ASN   D CG    1 
ATOM   4377 O  OD1   . ASN   C 2 6   ? 120.498 162.340 87.340  1.00 96.21  ? 6   ASN   D OD1   1 
ATOM   4378 N  ND2   . ASN   C 2 6   ? 118.360 161.669 87.220  1.00 89.88  ? 6   ASN   D ND2   1 
ATOM   4379 N  N     . ILE   C 2 7   ? 122.839 161.961 89.552  1.00 95.17  ? 7   ILE   D N     1 
ATOM   4380 C  CA    . ILE   C 2 7   ? 123.687 162.842 90.344  1.00 95.23  ? 7   ILE   D CA    1 
ATOM   4381 C  C     . ILE   C 2 7   ? 123.461 164.265 89.857  1.00 95.36  ? 7   ILE   D C     1 
ATOM   4382 O  O     . ILE   C 2 7   ? 123.622 164.551 88.664  1.00 94.84  ? 7   ILE   D O     1 
ATOM   4383 C  CB    . ILE   C 2 7   ? 125.173 162.459 90.216  1.00 93.88  ? 7   ILE   D CB    1 
ATOM   4384 C  CG1   . ILE   C 2 7   ? 125.490 161.233 91.070  1.00 96.66  ? 7   ILE   D CG1   1 
ATOM   4385 C  CG2   . ILE   C 2 7   ? 126.067 163.627 90.585  1.00 91.14  ? 7   ILE   D CG2   1 
ATOM   4386 C  CD1   . ILE   C 2 7   ? 126.354 160.207 90.377  1.00 92.96  ? 7   ILE   D CD1   1 
ATOM   4387 N  N     . LYS   C 2 8   ? 123.096 165.156 90.776  1.00 99.73  ? 8   LYS   D N     1 
ATOM   4388 C  CA    . LYS   C 2 8   ? 122.786 166.541 90.441  1.00 99.90  ? 8   LYS   D CA    1 
ATOM   4389 C  C     . LYS   C 2 8   ? 123.560 167.468 91.368  1.00 102.25 ? 8   LYS   D C     1 
ATOM   4390 O  O     . LYS   C 2 8   ? 123.243 167.568 92.558  1.00 100.73 ? 8   LYS   D O     1 
ATOM   4391 C  CB    . LYS   C 2 8   ? 121.284 166.802 90.534  1.00 101.02 ? 8   LYS   D CB    1 
ATOM   4392 C  CG    . LYS   C 2 8   ? 120.730 167.590 89.360  1.00 101.89 ? 8   LYS   D CG    1 
ATOM   4393 C  CD    . LYS   C 2 8   ? 119.283 167.224 89.077  1.00 102.06 ? 8   LYS   D CD    1 
ATOM   4394 C  CE    . LYS   C 2 8   ? 119.157 165.758 88.695  1.00 102.27 ? 8   LYS   D CE    1 
ATOM   4395 N  NZ    . LYS   C 2 8   ? 117.736 165.333 88.573  1.00 100.89 ? 8   LYS   D NZ    1 
ATOM   4396 N  N     . ASN   C 2 9   ? 124.571 168.142 90.815  1.00 101.86 ? 9   ASN   D N     1 
ATOM   4397 C  CA    . ASN   C 2 9   ? 125.353 169.158 91.523  1.00 99.28  ? 9   ASN   D CA    1 
ATOM   4398 C  C     . ASN   C 2 9   ? 125.980 168.575 92.792  1.00 97.05  ? 9   ASN   D C     1 
ATOM   4399 O  O     . ASN   C 2 9   ? 125.686 168.996 93.911  1.00 98.90  ? 9   ASN   D O     1 
ATOM   4400 C  CB    . ASN   C 2 9   ? 124.490 170.388 91.834  1.00 98.32  ? 9   ASN   D CB    1 
ATOM   4401 C  CG    . ASN   C 2 9   ? 125.270 171.515 92.512  1.00 99.67  ? 9   ASN   D CG    1 
ATOM   4402 O  OD1   . ASN   C 2 9   ? 126.461 171.391 92.798  1.00 99.47  ? 9   ASN   D OD1   1 
ATOM   4403 N  ND2   . ASN   C 2 9   ? 124.586 172.624 92.770  1.00 98.96  ? 9   ASN   D ND2   1 
ATOM   4404 N  N     . VAL   C 2 10  ? 126.847 167.586 92.608  1.00 83.21  ? 10  VAL   D N     1 
ATOM   4405 C  CA    . VAL   C 2 10  ? 127.599 167.021 93.722  1.00 84.69  ? 10  VAL   D CA    1 
ATOM   4406 C  C     . VAL   C 2 10  ? 128.918 167.768 93.857  1.00 84.53  ? 10  VAL   D C     1 
ATOM   4407 O  O     . VAL   C 2 10  ? 129.654 167.939 92.878  1.00 84.61  ? 10  VAL   D O     1 
ATOM   4408 C  CB    . VAL   C 2 10  ? 127.823 165.515 93.524  1.00 84.27  ? 10  VAL   D CB    1 
ATOM   4409 C  CG1   . VAL   C 2 10  ? 128.970 165.032 94.392  1.00 85.14  ? 10  VAL   D CG1   1 
ATOM   4410 C  CG2   . VAL   C 2 10  ? 126.560 164.758 93.877  1.00 83.14  ? 10  VAL   D CG2   1 
ATOM   4411 N  N     . THR   C 2 11  ? 129.213 168.224 95.071  1.00 82.13  ? 11  THR   D N     1 
ATOM   4412 C  CA    . THR   C 2 11  ? 130.381 169.053 95.331  1.00 78.70  ? 11  THR   D CA    1 
ATOM   4413 C  C     . THR   C 2 11  ? 130.990 168.626 96.656  1.00 78.14  ? 11  THR   D C     1 
ATOM   4414 O  O     . THR   C 2 11  ? 130.265 168.449 97.640  1.00 86.63  ? 11  THR   D O     1 
ATOM   4415 C  CB    . THR   C 2 11  ? 129.992 170.535 95.366  1.00 80.87  ? 11  THR   D CB    1 
ATOM   4416 O  OG1   . THR   C 2 11  ? 129.395 170.897 94.114  1.00 85.84  ? 11  THR   D OG1   1 
ATOM   4417 C  CG2   . THR   C 2 11  ? 131.210 171.396 95.580  1.00 78.82  ? 11  THR   D CG2   1 
ATOM   4418 N  N     . LYS   C 2 12  ? 132.310 168.454 96.684  1.00 68.17  ? 12  LYS   D N     1 
ATOM   4419 C  CA    . LYS   C 2 12  ? 133.004 167.955 97.864  1.00 68.36  ? 12  LYS   D CA    1 
ATOM   4420 C  C     . LYS   C 2 12  ? 134.210 168.830 98.168  1.00 70.17  ? 12  LYS   D C     1 
ATOM   4421 O  O     . LYS   C 2 12  ? 135.051 169.063 97.293  1.00 75.51  ? 12  LYS   D O     1 
ATOM   4422 C  CB    . LYS   C 2 12  ? 133.444 166.501 97.666  1.00 69.29  ? 12  LYS   D CB    1 
ATOM   4423 C  CG    . LYS   C 2 12  ? 134.136 165.891 98.870  1.00 72.69  ? 12  LYS   D CG    1 
ATOM   4424 C  CD    . LYS   C 2 12  ? 133.217 164.929 99.601  1.00 75.17  ? 12  LYS   D CD    1 
ATOM   4425 C  CE    . LYS   C 2 12  ? 133.356 165.064 101.108 1.00 75.23  ? 12  LYS   D CE    1 
ATOM   4426 N  NZ    . LYS   C 2 12  ? 132.538 164.048 101.827 1.00 71.50  ? 12  LYS   D NZ    1 
ATOM   4427 N  N     . GLU   C 2 13  ? 134.298 169.301 99.411  1.00 80.60  ? 13  GLU   D N     1 
ATOM   4428 C  CA    . GLU   C 2 13  ? 135.430 170.078 99.892  1.00 78.77  ? 13  GLU   D CA    1 
ATOM   4429 C  C     . GLU   C 2 13  ? 136.137 169.334 101.013 1.00 79.61  ? 13  GLU   D C     1 
ATOM   4430 O  O     . GLU   C 2 13  ? 135.527 168.552 101.749 1.00 83.16  ? 13  GLU   D O     1 
ATOM   4431 C  CB    . GLU   C 2 13  ? 135.007 171.462 100.408 1.00 81.63  ? 13  GLU   D CB    1 
ATOM   4432 C  CG    . GLU   C 2 13  ? 134.912 172.535 99.346  1.00 84.52  ? 13  GLU   D CG    1 
ATOM   4433 C  CD    . GLU   C 2 13  ? 133.549 172.592 98.707  1.00 83.83  ? 13  GLU   D CD    1 
ATOM   4434 O  OE1   . GLU   C 2 13  ? 133.406 172.050 97.597  1.00 79.91  ? 13  GLU   D OE1   1 
ATOM   4435 O  OE2   . GLU   C 2 13  ? 132.625 173.176 99.311  1.00 86.29  ? 13  GLU   D OE2   1 
ATOM   4436 N  N     . TYR   C 2 14  ? 137.435 169.586 101.131 1.00 76.58  ? 14  TYR   D N     1 
ATOM   4437 C  CA    . TYR   C 2 14  ? 138.235 169.084 102.237 1.00 81.11  ? 14  TYR   D CA    1 
ATOM   4438 C  C     . TYR   C 2 14  ? 138.980 170.243 102.882 1.00 84.18  ? 14  TYR   D C     1 
ATOM   4439 O  O     . TYR   C 2 14  ? 139.493 171.127 102.190 1.00 82.96  ? 14  TYR   D O     1 
ATOM   4440 C  CB    . TYR   C 2 14  ? 139.224 168.007 101.776 1.00 82.25  ? 14  TYR   D CB    1 
ATOM   4441 C  CG    . TYR   C 2 14  ? 138.574 166.678 101.461 1.00 85.12  ? 14  TYR   D CG    1 
ATOM   4442 C  CD1   . TYR   C 2 14  ? 138.386 165.726 102.452 1.00 81.31  ? 14  TYR   D CD1   1 
ATOM   4443 C  CD2   . TYR   C 2 14  ? 138.155 166.373 100.173 1.00 83.42  ? 14  TYR   D CD2   1 
ATOM   4444 C  CE1   . TYR   C 2 14  ? 137.796 164.511 102.172 1.00 78.06  ? 14  TYR   D CE1   1 
ATOM   4445 C  CE2   . TYR   C 2 14  ? 137.563 165.158 99.884  1.00 79.87  ? 14  TYR   D CE2   1 
ATOM   4446 C  CZ    . TYR   C 2 14  ? 137.386 164.232 100.888 1.00 78.95  ? 14  TYR   D CZ    1 
ATOM   4447 O  OH    . TYR   C 2 14  ? 136.798 163.021 100.606 1.00 81.78  ? 14  TYR   D OH    1 
ATOM   4448 N  N     . ARG   C 2 15  ? 139.026 170.235 104.212 1.00 110.77 ? 15  ARG   D N     1 
ATOM   4449 C  CA    . ARG   C 2 15  ? 139.688 171.284 104.974 1.00 109.52 ? 15  ARG   D CA    1 
ATOM   4450 C  C     . ARG   C 2 15  ? 141.138 170.892 105.218 1.00 106.63 ? 15  ARG   D C     1 
ATOM   4451 O  O     . ARG   C 2 15  ? 141.416 169.814 105.753 1.00 105.81 ? 15  ARG   D O     1 
ATOM   4452 C  CB    . ARG   C 2 15  ? 138.968 171.520 106.302 1.00 110.52 ? 15  ARG   D CB    1 
ATOM   4453 C  CG    . ARG   C 2 15  ? 137.740 172.409 106.196 1.00 109.59 ? 15  ARG   D CG    1 
ATOM   4454 C  CD    . ARG   C 2 15  ? 138.097 173.875 106.377 1.00 110.96 ? 15  ARG   D CD    1 
ATOM   4455 N  NE    . ARG   C 2 15  ? 137.048 174.755 105.876 1.00 111.03 ? 15  ARG   D NE    1 
ATOM   4456 C  CZ    . ARG   C 2 15  ? 136.573 175.805 106.533 1.00 110.09 ? 15  ARG   D CZ    1 
ATOM   4457 N  NH1   . ARG   C 2 15  ? 137.033 176.138 107.728 1.00 108.87 ? 15  ARG   D NH1   1 
ATOM   4458 N  NH2   . ARG   C 2 15  ? 135.613 176.539 105.978 1.00 108.77 ? 15  ARG   D NH2   1 
ATOM   4459 N  N     . ILE   C 2 16  ? 142.058 171.770 104.829 1.00 96.51  ? 16  ILE   D N     1 
ATOM   4460 C  CA    . ILE   C 2 16  ? 143.487 171.494 104.891 1.00 98.51  ? 16  ILE   D CA    1 
ATOM   4461 C  C     . ILE   C 2 16  ? 144.099 172.374 105.970 1.00 99.71  ? 16  ILE   D C     1 
ATOM   4462 O  O     . ILE   C 2 16  ? 144.053 173.608 105.879 1.00 101.54 ? 16  ILE   D O     1 
ATOM   4463 C  CB    . ILE   C 2 16  ? 144.166 171.730 103.532 1.00 99.31  ? 16  ILE   D CB    1 
ATOM   4464 C  CG1   . ILE   C 2 16  ? 143.929 170.534 102.612 1.00 97.06  ? 16  ILE   D CG1   1 
ATOM   4465 C  CG2   . ILE   C 2 16  ? 145.660 171.967 103.707 1.00 97.58  ? 16  ILE   D CG2   1 
ATOM   4466 C  CD1   . ILE   C 2 16  ? 144.204 170.823 101.162 1.00 95.63  ? 16  ILE   D CD1   1 
ATOM   4467 N  N     . TYR   C 2 17  ? 144.659 171.740 106.997 1.00 98.09  ? 17  TYR   D N     1 
ATOM   4468 C  CA    . TYR   C 2 17  ? 145.456 172.419 108.008 1.00 99.15  ? 17  TYR   D CA    1 
ATOM   4469 C  C     . TYR   C 2 17  ? 146.875 171.878 107.944 1.00 99.37  ? 17  TYR   D C     1 
ATOM   4470 O  O     . TYR   C 2 17  ? 147.080 170.661 108.004 1.00 100.40 ? 17  TYR   D O     1 
ATOM   4471 C  CB    . TYR   C 2 17  ? 144.887 172.219 109.416 1.00 100.46 ? 17  TYR   D CB    1 
ATOM   4472 C  CG    . TYR   C 2 17  ? 143.397 171.974 109.483 1.00 99.65  ? 17  TYR   D CG    1 
ATOM   4473 C  CD1   . TYR   C 2 17  ? 142.493 173.011 109.303 1.00 98.92  ? 17  TYR   D CD1   1 
ATOM   4474 C  CD2   . TYR   C 2 17  ? 142.897 170.706 109.744 1.00 99.38  ? 17  TYR   D CD2   1 
ATOM   4475 C  CE1   . TYR   C 2 17  ? 141.131 172.789 109.372 1.00 98.31  ? 17  TYR   D CE1   1 
ATOM   4476 C  CE2   . TYR   C 2 17  ? 141.539 170.475 109.813 1.00 99.30  ? 17  TYR   D CE2   1 
ATOM   4477 C  CZ    . TYR   C 2 17  ? 140.660 171.519 109.627 1.00 98.92  ? 17  TYR   D CZ    1 
ATOM   4478 O  OH    . TYR   C 2 17  ? 139.306 171.286 109.698 1.00 99.41  ? 17  TYR   D OH    1 
ATOM   4479 N  N     A ARG   C 2 18  ? 147.849 172.783 107.820 0.34 100.28 ? 18  ARG   D N     1 
ATOM   4480 N  N     B ARG   C 2 18  ? 147.851 172.779 107.815 0.66 100.24 ? 18  ARG   D N     1 
ATOM   4481 C  CA    A ARG   C 2 18  ? 149.246 172.366 107.798 0.34 99.71  ? 18  ARG   D CA    1 
ATOM   4482 C  CA    B ARG   C 2 18  ? 149.244 172.348 107.798 0.66 99.72  ? 18  ARG   D CA    1 
ATOM   4483 C  C     A ARG   C 2 18  ? 149.677 171.782 109.137 0.34 100.72 ? 18  ARG   D C     1 
ATOM   4484 C  C     B ARG   C 2 18  ? 149.651 171.751 109.140 0.66 100.67 ? 18  ARG   D C     1 
ATOM   4485 O  O     A ARG   C 2 18  ? 150.485 170.849 109.175 0.34 101.14 ? 18  ARG   D O     1 
ATOM   4486 O  O     B ARG   C 2 18  ? 150.413 170.778 109.188 0.66 101.05 ? 18  ARG   D O     1 
ATOM   4487 C  CB    A ARG   C 2 18  ? 150.140 173.545 107.417 0.34 99.27  ? 18  ARG   D CB    1 
ATOM   4488 C  CB    B ARG   C 2 18  ? 150.155 173.517 107.426 0.66 99.30  ? 18  ARG   D CB    1 
ATOM   4489 C  CG    A ARG   C 2 18  ? 150.210 173.809 105.923 0.34 100.48 ? 18  ARG   D CG    1 
ATOM   4490 C  CG    B ARG   C 2 18  ? 151.634 173.160 107.394 0.66 99.01  ? 18  ARG   D CG    1 
ATOM   4491 C  CD    A ARG   C 2 18  ? 151.422 173.140 105.299 0.34 100.50 ? 18  ARG   D CD    1 
ATOM   4492 C  CD    B ARG   C 2 18  ? 152.295 173.617 106.104 0.66 100.80 ? 18  ARG   D CD    1 
ATOM   4493 N  NE    A ARG   C 2 18  ? 152.657 173.857 105.589 0.34 101.50 ? 18  ARG   D NE    1 
ATOM   4494 N  NE    B ARG   C 2 18  ? 151.391 173.539 104.963 0.66 100.35 ? 18  ARG   D NE    1 
ATOM   4495 C  CZ    A ARG   C 2 18  ? 153.565 173.463 106.471 0.34 99.70  ? 18  ARG   D CZ    1 
ATOM   4496 C  CZ    B ARG   C 2 18  ? 151.547 174.221 103.837 0.66 98.49  ? 18  ARG   D CZ    1 
ATOM   4497 N  NH1   A ARG   C 2 18  ? 153.401 172.362 107.186 0.34 98.30  ? 18  ARG   D NH1   1 
ATOM   4498 N  NH1   B ARG   C 2 18  ? 152.565 175.048 103.667 0.66 98.54  ? 18  ARG   D NH1   1 
ATOM   4499 N  NH2   A ARG   C 2 18  ? 154.663 174.192 106.642 0.34 98.51  ? 18  ARG   D NH2   1 
ATOM   4500 N  NH2   B ARG   C 2 18  ? 150.660 174.069 102.858 0.66 98.69  ? 18  ARG   D NH2   1 
ATOM   4501 N  N     . THR   C 2 19  ? 149.154 172.316 110.235 1.00 102.87 ? 19  THR   D N     1 
ATOM   4502 C  CA    . THR   C 2 19  ? 149.443 171.821 111.570 1.00 103.70 ? 19  THR   D CA    1 
ATOM   4503 C  C     . THR   C 2 19  ? 148.285 170.968 112.074 1.00 104.35 ? 19  THR   D C     1 
ATOM   4504 O  O     . THR   C 2 19  ? 147.114 171.280 111.848 1.00 102.94 ? 19  THR   D O     1 
ATOM   4505 C  CB    . THR   C 2 19  ? 149.698 172.976 112.542 1.00 104.04 ? 19  THR   D CB    1 
ATOM   4506 O  OG1   . THR   C 2 19  ? 148.449 173.469 113.042 1.00 101.85 ? 19  THR   D OG1   1 
ATOM   4507 C  CG2   . THR   C 2 19  ? 150.442 174.104 111.843 1.00 103.65 ? 19  THR   D CG2   1 
ATOM   4508 N  N     . ASN   C 2 20  ? 148.630 169.874 112.758 1.00 109.22 ? 20  ASN   D N     1 
ATOM   4509 C  CA    . ASN   C 2 20  ? 147.608 168.971 113.279 1.00 109.82 ? 20  ASN   D CA    1 
ATOM   4510 C  C     . ASN   C 2 20  ? 146.801 169.614 114.399 1.00 112.89 ? 20  ASN   D C     1 
ATOM   4511 O  O     . ASN   C 2 20  ? 145.669 169.193 114.665 1.00 110.66 ? 20  ASN   D O     1 
ATOM   4512 C  CB    . ASN   C 2 20  ? 148.257 167.676 113.769 1.00 108.38 ? 20  ASN   D CB    1 
ATOM   4513 C  CG    . ASN   C 2 20  ? 147.323 166.484 113.684 1.00 110.08 ? 20  ASN   D CG    1 
ATOM   4514 O  OD1   . ASN   C 2 20  ? 146.317 166.418 114.390 1.00 110.93 ? 20  ASN   D OD1   1 
ATOM   4515 N  ND2   . ASN   C 2 20  ? 147.656 165.532 112.820 1.00 108.97 ? 20  ASN   D ND2   1 
ATOM   4516 N  N     . LYS   C 2 21  ? 147.357 170.629 115.062 1.00 106.85 ? 21  LYS   D N     1 
ATOM   4517 C  CA    . LYS   C 2 21  ? 146.710 171.237 116.218 1.00 103.39 ? 21  LYS   D CA    1 
ATOM   4518 C  C     . LYS   C 2 21  ? 145.649 172.262 115.843 1.00 103.68 ? 21  LYS   D C     1 
ATOM   4519 O  O     . LYS   C 2 21  ? 144.944 172.750 116.733 1.00 104.25 ? 21  LYS   D O     1 
ATOM   4520 C  CB    . LYS   C 2 21  ? 147.749 171.903 117.133 1.00 101.86 ? 21  LYS   D CB    1 
ATOM   4521 C  CG    . LYS   C 2 21  ? 148.756 170.963 117.811 1.00 102.92 ? 21  LYS   D CG    1 
ATOM   4522 C  CD    . LYS   C 2 21  ? 149.800 170.399 116.855 1.00 104.04 ? 21  LYS   D CD    1 
ATOM   4523 C  CE    . LYS   C 2 21  ? 151.031 171.288 116.800 1.00 103.37 ? 21  LYS   D CE    1 
ATOM   4524 N  NZ    . LYS   C 2 21  ? 151.792 171.104 115.535 1.00 100.57 ? 21  LYS   D NZ    1 
ATOM   4525 N  N     . GLU   C 2 22  ? 145.514 172.601 114.562 1.00 114.69 ? 22  GLU   D N     1 
ATOM   4526 C  CA    . GLU   C 2 22  ? 144.534 173.589 114.131 1.00 114.32 ? 22  GLU   D CA    1 
ATOM   4527 C  C     . GLU   C 2 22  ? 143.147 172.999 113.914 1.00 116.50 ? 22  GLU   D C     1 
ATOM   4528 O  O     . GLU   C 2 22  ? 142.224 173.744 113.566 1.00 115.34 ? 22  GLU   D O     1 
ATOM   4529 C  CB    . GLU   C 2 22  ? 145.006 174.271 112.844 1.00 114.24 ? 22  GLU   D CB    1 
ATOM   4530 C  CG    . GLU   C 2 22  ? 145.808 175.540 113.073 1.00 115.73 ? 22  GLU   D CG    1 
ATOM   4531 C  CD    . GLU   C 2 22  ? 146.683 175.899 111.887 1.00 117.77 ? 22  GLU   D CD    1 
ATOM   4532 O  OE1   . GLU   C 2 22  ? 146.179 175.868 110.745 1.00 116.56 ? 22  GLU   D OE1   1 
ATOM   4533 O  OE2   . GLU   C 2 22  ? 147.873 176.212 112.099 1.00 116.90 ? 22  GLU   D OE2   1 
ATOM   4534 N  N     . ARG   C 2 23  ? 142.978 171.688 114.103 1.00 125.70 ? 23  ARG   D N     1 
ATOM   4535 C  CA    . ARG   C 2 23  ? 141.677 171.065 113.881 1.00 125.66 ? 23  ARG   D CA    1 
ATOM   4536 C  C     . ARG   C 2 23  ? 140.636 171.572 114.873 1.00 126.27 ? 23  ARG   D C     1 
ATOM   4537 O  O     . ARG   C 2 23  ? 139.484 171.819 114.499 1.00 124.95 ? 23  ARG   D O     1 
ATOM   4538 C  CB    . ARG   C 2 23  ? 141.803 169.545 113.965 1.00 124.83 ? 23  ARG   D CB    1 
ATOM   4539 C  CG    . ARG   C 2 23  ? 142.620 168.933 112.840 1.00 124.78 ? 23  ARG   D CG    1 
ATOM   4540 C  CD    . ARG   C 2 23  ? 142.676 167.419 112.951 1.00 124.77 ? 23  ARG   D CD    1 
ATOM   4541 N  NE    . ARG   C 2 23  ? 143.498 166.830 111.900 1.00 126.00 ? 23  ARG   D NE    1 
ATOM   4542 C  CZ    . ARG   C 2 23  ? 143.817 165.545 111.829 1.00 126.34 ? 23  ARG   D CZ    1 
ATOM   4543 N  NH1   . ARG   C 2 23  ? 143.396 164.678 112.735 1.00 126.67 ? 23  ARG   D NH1   1 
ATOM   4544 N  NH2   . ARG   C 2 23  ? 144.575 165.121 110.823 1.00 124.50 ? 23  ARG   D NH2   1 
ATOM   4545 N  N     . MET   C 2 24  ? 141.020 171.732 116.139 1.00 120.16 ? 24  MET   D N     1 
ATOM   4546 C  CA    . MET   C 2 24  ? 140.080 172.140 117.175 1.00 118.85 ? 24  MET   D CA    1 
ATOM   4547 C  C     . MET   C 2 24  ? 139.656 173.598 117.067 1.00 119.29 ? 24  MET   D C     1 
ATOM   4548 O  O     . MET   C 2 24  ? 138.632 173.968 117.650 1.00 118.51 ? 24  MET   D O     1 
ATOM   4549 C  CB    . MET   C 2 24  ? 140.682 171.891 118.560 1.00 118.88 ? 24  MET   D CB    1 
ATOM   4550 C  CG    . MET   C 2 24  ? 139.677 171.422 119.601 1.00 120.39 ? 24  MET   D CG    1 
ATOM   4551 S  SD    . MET   C 2 24  ? 140.433 170.450 120.918 1.00 123.10 ? 24  MET   D SD    1 
ATOM   4552 C  CE    . MET   C 2 24  ? 138.983 169.935 121.833 1.00 118.82 ? 24  MET   D CE    1 
ATOM   4553 N  N     . LYS   C 2 25  ? 140.409 174.430 116.345 1.00 117.90 ? 25  LYS   D N     1 
ATOM   4554 C  CA    . LYS   C 2 25  ? 140.095 175.856 116.292 1.00 118.73 ? 25  LYS   D CA    1 
ATOM   4555 C  C     . LYS   C 2 25  ? 138.742 176.109 115.636 1.00 118.95 ? 25  LYS   D C     1 
ATOM   4556 O  O     . LYS   C 2 25  ? 137.968 176.953 116.103 1.00 119.34 ? 25  LYS   D O     1 
ATOM   4557 C  CB    . LYS   C 2 25  ? 141.199 176.610 115.550 1.00 116.90 ? 25  LYS   D CB    1 
ATOM   4558 C  CG    . LYS   C 2 25  ? 142.195 177.308 116.461 1.00 117.33 ? 25  LYS   D CG    1 
ATOM   4559 C  CD    . LYS   C 2 25  ? 142.938 176.310 117.334 1.00 117.92 ? 25  LYS   D CD    1 
ATOM   4560 C  CE    . LYS   C 2 25  ? 144.442 176.506 117.242 1.00 117.69 ? 25  LYS   D CE    1 
ATOM   4561 N  NZ    . LYS   C 2 25  ? 145.177 175.530 118.092 1.00 116.64 ? 25  LYS   D NZ    1 
ATOM   4562 N  N     . ASP   C 2 26  ? 138.438 175.392 114.557 1.00 123.23 ? 26  ASP   D N     1 
ATOM   4563 C  CA    . ASP   C 2 26  ? 137.202 175.593 113.811 1.00 123.98 ? 26  ASP   D CA    1 
ATOM   4564 C  C     . ASP   C 2 26  ? 136.063 174.701 114.288 1.00 123.37 ? 26  ASP   D C     1 
ATOM   4565 O  O     . ASP   C 2 26  ? 134.968 174.767 113.720 1.00 121.56 ? 26  ASP   D O     1 
ATOM   4566 C  CB    . ASP   C 2 26  ? 137.446 175.354 112.318 1.00 123.27 ? 26  ASP   D CB    1 
ATOM   4567 C  CG    . ASP   C 2 26  ? 138.906 175.101 111.999 1.00 122.94 ? 26  ASP   D CG    1 
ATOM   4568 O  OD1   . ASP   C 2 26  ? 139.465 174.110 112.515 1.00 120.35 ? 26  ASP   D OD1   1 
ATOM   4569 O  OD2   . ASP   C 2 26  ? 139.494 175.892 111.233 1.00 124.01 ? 26  ASP   D OD2   1 
ATOM   4570 N  N     . ALA   C 2 27  ? 136.288 173.876 115.311 1.00 110.90 ? 27  ALA   D N     1 
ATOM   4571 C  CA    . ALA   C 2 27  ? 135.271 172.947 115.781 1.00 109.74 ? 27  ALA   D CA    1 
ATOM   4572 C  C     . ALA   C 2 27  ? 134.505 173.445 116.999 1.00 109.48 ? 27  ALA   D C     1 
ATOM   4573 O  O     . ALA   C 2 27  ? 133.363 173.021 117.205 1.00 108.04 ? 27  ALA   D O     1 
ATOM   4574 C  CB    . ALA   C 2 27  ? 135.903 171.589 116.111 1.00 108.75 ? 27  ALA   D CB    1 
ATOM   4575 N  N     . LEU   C 2 28  ? 135.096 174.326 117.805 1.00 112.19 ? 28  LEU   D N     1 
ATOM   4576 C  CA    . LEU   C 2 28  ? 134.445 174.823 119.012 1.00 112.92 ? 28  LEU   D CA    1 
ATOM   4577 C  C     . LEU   C 2 28  ? 133.759 176.171 118.825 1.00 112.79 ? 28  LEU   D C     1 
ATOM   4578 O  O     . LEU   C 2 28  ? 132.730 176.422 119.460 1.00 110.67 ? 28  LEU   D O     1 
ATOM   4579 C  CB    . LEU   C 2 28  ? 135.455 174.886 120.169 1.00 112.03 ? 28  LEU   D CB    1 
ATOM   4580 C  CG    . LEU   C 2 28  ? 136.909 175.350 119.983 1.00 113.27 ? 28  LEU   D CG    1 
ATOM   4581 C  CD1   . LEU   C 2 28  ? 137.055 176.775 119.471 1.00 110.59 ? 28  LEU   D CD1   1 
ATOM   4582 C  CD2   . LEU   C 2 28  ? 137.686 175.169 121.282 1.00 111.85 ? 28  LEU   D CD2   1 
ATOM   4583 N  N     . ILE   C 2 29  ? 134.288 177.043 117.972 1.00 116.79 ? 29  ILE   D N     1 
ATOM   4584 C  CA    . ILE   C 2 29  ? 133.628 178.309 117.654 1.00 117.62 ? 29  ILE   D CA    1 
ATOM   4585 C  C     . ILE   C 2 29  ? 133.569 178.440 116.135 1.00 117.18 ? 29  ILE   D C     1 
ATOM   4586 O  O     . ILE   C 2 29  ? 134.601 178.313 115.462 1.00 116.22 ? 29  ILE   D O     1 
ATOM   4587 C  CB    . ILE   C 2 29  ? 134.348 179.506 118.297 1.00 117.96 ? 29  ILE   D CB    1 
ATOM   4588 C  CG1   . ILE   C 2 29  ? 134.547 179.282 119.798 1.00 116.94 ? 29  ILE   D CG1   1 
ATOM   4589 C  CG2   . ILE   C 2 29  ? 133.538 180.770 118.099 1.00 116.80 ? 29  ILE   D CG2   1 
ATOM   4590 C  CD1   . ILE   C 2 29  ? 133.277 179.412 120.616 1.00 115.15 ? 29  ILE   D CD1   1 
ATOM   4591 N  N     . PRO   C 2 30  ? 132.392 178.693 115.554 1.00 120.44 ? 30  PRO   D N     1 
ATOM   4592 C  CA    . PRO   C 2 30  ? 132.246 178.581 114.094 1.00 119.67 ? 30  PRO   D CA    1 
ATOM   4593 C  C     . PRO   C 2 30  ? 132.689 179.802 113.300 1.00 118.35 ? 30  PRO   D C     1 
ATOM   4594 O  O     . PRO   C 2 30  ? 132.345 179.913 112.119 1.00 115.27 ? 30  PRO   D O     1 
ATOM   4595 C  CB    . PRO   C 2 30  ? 130.737 178.341 113.915 1.00 117.24 ? 30  PRO   D CB    1 
ATOM   4596 C  CG    . PRO   C 2 30  ? 130.203 178.039 115.301 1.00 116.76 ? 30  PRO   D CG    1 
ATOM   4597 C  CD    . PRO   C 2 30  ? 131.088 178.809 116.220 1.00 117.32 ? 30  PRO   D CD    1 
ATOM   4598 N  N     . LYS   C 2 31  ? 133.440 180.727 113.905 1.00 122.71 ? 31  LYS   D N     1 
ATOM   4599 C  CA    . LYS   C 2 31  ? 133.847 181.918 113.167 1.00 123.20 ? 31  LYS   D CA    1 
ATOM   4600 C  C     . LYS   C 2 31  ? 135.055 181.677 112.270 1.00 124.98 ? 31  LYS   D C     1 
ATOM   4601 O  O     . LYS   C 2 31  ? 135.348 182.520 111.414 1.00 122.97 ? 31  LYS   D O     1 
ATOM   4602 C  CB    . LYS   C 2 31  ? 134.156 183.073 114.126 1.00 122.46 ? 31  LYS   D CB    1 
ATOM   4603 C  CG    . LYS   C 2 31  ? 134.751 182.665 115.463 1.00 121.55 ? 31  LYS   D CG    1 
ATOM   4604 C  CD    . LYS   C 2 31  ? 136.217 182.271 115.341 1.00 122.09 ? 31  LYS   D CD    1 
ATOM   4605 C  CE    . LYS   C 2 31  ? 136.790 181.845 116.682 1.00 122.11 ? 31  LYS   D CE    1 
ATOM   4606 N  NZ    . LYS   C 2 31  ? 138.168 181.299 116.549 1.00 122.05 ? 31  LYS   D NZ    1 
ATOM   4607 N  N     . HIS   C 2 32  ? 135.757 180.562 112.441 1.00 124.45 ? 32  HIS   D N     1 
ATOM   4608 C  CA    . HIS   C 2 32  ? 136.975 180.312 111.683 1.00 122.72 ? 32  HIS   D CA    1 
ATOM   4609 C  C     . HIS   C 2 32  ? 136.657 179.741 110.308 1.00 122.93 ? 32  HIS   D C     1 
ATOM   4610 O  O     . HIS   C 2 32  ? 135.778 178.887 110.159 1.00 121.71 ? 32  HIS   D O     1 
ATOM   4611 C  CB    . HIS   C 2 32  ? 137.892 179.356 112.445 1.00 122.40 ? 32  HIS   D CB    1 
ATOM   4612 C  CG    . HIS   C 2 32  ? 139.340 179.508 112.099 1.00 125.20 ? 32  HIS   D CG    1 
ATOM   4613 N  ND1   . HIS   C 2 32  ? 139.820 180.558 111.348 1.00 124.42 ? 32  HIS   D ND1   1 
ATOM   4614 C  CD2   . HIS   C 2 32  ? 140.416 178.741 112.403 1.00 123.68 ? 32  HIS   D CD2   1 
ATOM   4615 C  CE1   . HIS   C 2 32  ? 141.127 180.433 111.203 1.00 122.67 ? 32  HIS   D CE1   1 
ATOM   4616 N  NE2   . HIS   C 2 32  ? 141.514 179.339 111.835 1.00 122.15 ? 32  HIS   D NE2   1 
ATOM   4617 N  N     . LYS   C 2 33  ? 137.381 180.225 109.299 1.00 112.55 ? 33  LYS   D N     1 
ATOM   4618 C  CA    . LYS   C 2 33  ? 137.255 179.736 107.928 1.00 110.68 ? 33  LYS   D CA    1 
ATOM   4619 C  C     . LYS   C 2 33  ? 138.660 179.596 107.357 1.00 110.11 ? 33  LYS   D C     1 
ATOM   4620 O  O     . LYS   C 2 33  ? 139.350 180.601 107.153 1.00 108.18 ? 33  LYS   D O     1 
ATOM   4621 C  CB    . LYS   C 2 33  ? 136.406 180.679 107.075 1.00 108.35 ? 33  LYS   D CB    1 
ATOM   4622 C  CG    . LYS   C 2 33  ? 136.399 182.119 107.560 1.00 107.74 ? 33  LYS   D CG    1 
ATOM   4623 C  CD    . LYS   C 2 33  ? 136.693 183.088 106.425 1.00 108.83 ? 33  LYS   D CD    1 
ATOM   4624 C  CE    . LYS   C 2 33  ? 135.731 182.889 105.265 1.00 107.91 ? 33  LYS   D CE    1 
ATOM   4625 N  NZ    . LYS   C 2 33  ? 135.499 184.152 104.513 1.00 105.65 ? 33  LYS   D NZ    1 
ATOM   4626 N  N     . ASN   C 2 34  ? 139.079 178.361 107.099 1.00 109.48 ? 34  ASN   D N     1 
ATOM   4627 C  CA    . ASN   C 2 34  ? 140.434 178.065 106.668 1.00 111.13 ? 34  ASN   D CA    1 
ATOM   4628 C  C     . ASN   C 2 34  ? 140.475 177.804 105.162 1.00 111.23 ? 34  ASN   D C     1 
ATOM   4629 O  O     . ASN   C 2 34  ? 139.481 177.970 104.449 1.00 109.00 ? 34  ASN   D O     1 
ATOM   4630 C  CB    . ASN   C 2 34  ? 140.977 176.873 107.459 1.00 109.43 ? 34  ASN   D CB    1 
ATOM   4631 C  CG    . ASN   C 2 34  ? 142.442 177.028 107.815 1.00 109.43 ? 34  ASN   D CG    1 
ATOM   4632 O  OD1   . ASN   C 2 34  ? 143.181 177.754 107.149 1.00 107.80 ? 34  ASN   D OD1   1 
ATOM   4633 N  ND2   . ASN   C 2 34  ? 142.870 176.342 108.867 1.00 108.61 ? 34  ASN   D ND2   1 
ATOM   4634 N  N     . LYS   C 2 35  ? 141.644 177.399 104.672 1.00 106.83 ? 35  LYS   D N     1 
ATOM   4635 C  CA    . LYS   C 2 35  ? 141.789 177.023 103.272 1.00 103.04 ? 35  LYS   D CA    1 
ATOM   4636 C  C     . LYS   C 2 35  ? 141.054 175.719 102.997 1.00 100.78 ? 35  LYS   D C     1 
ATOM   4637 O  O     . LYS   C 2 35  ? 140.994 174.830 103.850 1.00 100.52 ? 35  LYS   D O     1 
ATOM   4638 C  CB    . LYS   C 2 35  ? 143.268 176.875 102.914 1.00 100.45 ? 35  LYS   D CB    1 
ATOM   4639 C  CG    . LYS   C 2 35  ? 143.623 177.342 101.514 1.00 100.21 ? 35  LYS   D CG    1 
ATOM   4640 C  CD    . LYS   C 2 35  ? 145.125 177.307 101.283 1.00 100.55 ? 35  LYS   D CD    1 
ATOM   4641 C  CE    . LYS   C 2 35  ? 145.741 176.030 101.830 1.00 101.37 ? 35  LYS   D CE    1 
ATOM   4642 N  NZ    . LYS   C 2 35  ? 147.172 175.894 101.445 1.00 100.31 ? 35  LYS   D NZ    1 
ATOM   4643 N  N     . THR   C 2 36  ? 140.493 175.605 101.797 1.00 102.24 ? 36  THR   D N     1 
ATOM   4644 C  CA    . THR   C 2 36  ? 139.733 174.435 101.402 1.00 103.52 ? 36  THR   D CA    1 
ATOM   4645 C  C     . THR   C 2 36  ? 140.155 173.989 100.007 1.00 104.94 ? 36  THR   D C     1 
ATOM   4646 O  O     . THR   C 2 36  ? 140.618 174.782 99.175  1.00 103.41 ? 36  THR   D O     1 
ATOM   4647 C  CB    . THR   C 2 36  ? 138.218 174.703 101.448 1.00 102.42 ? 36  THR   D CB    1 
ATOM   4648 O  OG1   . THR   C 2 36  ? 137.507 173.459 101.454 1.00 99.79  ? 36  THR   D OG1   1 
ATOM   4649 C  CG2   . THR   C 2 36  ? 137.774 175.534 100.257 1.00 101.81 ? 36  THR   D CG2   1 
ATOM   4650 N  N     . PHE   C 2 37  ? 140.002 172.685 99.779  1.00 88.85  ? 37  PHE   D N     1 
ATOM   4651 C  CA    . PHE   C 2 37  ? 140.381 172.026 98.539  1.00 80.95  ? 37  PHE   D CA    1 
ATOM   4652 C  C     . PHE   C 2 37  ? 139.144 171.375 97.941  1.00 79.10  ? 37  PHE   D C     1 
ATOM   4653 O  O     . PHE   C 2 37  ? 138.465 170.596 98.616  1.00 79.03  ? 37  PHE   D O     1 
ATOM   4654 C  CB    . PHE   C 2 37  ? 141.471 170.983 98.799  1.00 78.99  ? 37  PHE   D CB    1 
ATOM   4655 C  CG    . PHE   C 2 37  ? 141.769 170.100 97.625  1.00 81.63  ? 37  PHE   D CG    1 
ATOM   4656 C  CD1   . PHE   C 2 37  ? 142.506 170.572 96.556  1.00 79.74  ? 37  PHE   D CD1   1 
ATOM   4657 C  CD2   . PHE   C 2 37  ? 141.320 168.791 97.597  1.00 79.69  ? 37  PHE   D CD2   1 
ATOM   4658 C  CE1   . PHE   C 2 37  ? 142.786 169.760 95.480  1.00 77.76  ? 37  PHE   D CE1   1 
ATOM   4659 C  CE2   . PHE   C 2 37  ? 141.595 167.974 96.521  1.00 74.90  ? 37  PHE   D CE2   1 
ATOM   4660 C  CZ    . PHE   C 2 37  ? 142.328 168.460 95.460  1.00 76.96  ? 37  PHE   D CZ    1 
ATOM   4661 N  N     . PHE   C 2 38  ? 138.856 171.695 96.682  1.00 75.15  ? 38  PHE   D N     1 
ATOM   4662 C  CA    . PHE   C 2 38  ? 137.661 171.199 96.001  1.00 72.90  ? 38  PHE   D CA    1 
ATOM   4663 C  C     . PHE   C 2 38  ? 137.995 169.868 95.340  1.00 75.12  ? 38  PHE   D C     1 
ATOM   4664 O  O     . PHE   C 2 38  ? 138.531 169.816 94.233  1.00 77.67  ? 38  PHE   D O     1 
ATOM   4665 C  CB    . PHE   C 2 38  ? 137.163 172.216 94.981  1.00 74.35  ? 38  PHE   D CB    1 
ATOM   4666 C  CG    . PHE   C 2 38  ? 136.359 173.335 95.577  1.00 77.18  ? 38  PHE   D CG    1 
ATOM   4667 C  CD1   . PHE   C 2 38  ? 136.953 174.266 96.412  1.00 79.55  ? 38  PHE   D CD1   1 
ATOM   4668 C  CD2   . PHE   C 2 38  ? 135.011 173.461 95.294  1.00 78.62  ? 38  PHE   D CD2   1 
ATOM   4669 C  CE1   . PHE   C 2 38  ? 136.213 175.296 96.958  1.00 79.59  ? 38  PHE   D CE1   1 
ATOM   4670 C  CE2   . PHE   C 2 38  ? 134.268 174.492 95.837  1.00 79.16  ? 38  PHE   D CE2   1 
ATOM   4671 C  CZ    . PHE   C 2 38  ? 134.871 175.410 96.671  1.00 79.88  ? 38  PHE   D CZ    1 
ATOM   4672 N  N     . ALA   C 2 39  ? 137.673 168.770 96.030  1.00 63.06  ? 39  ALA   D N     1 
ATOM   4673 C  CA    . ALA   C 2 39  ? 137.891 167.456 95.435  1.00 59.26  ? 39  ALA   D CA    1 
ATOM   4674 C  C     . ALA   C 2 39  ? 136.969 167.231 94.246  1.00 62.71  ? 39  ALA   D C     1 
ATOM   4675 O  O     . ALA   C 2 39  ? 137.381 166.639 93.242  1.00 65.07  ? 39  ALA   D O     1 
ATOM   4676 C  CB    . ALA   C 2 39  ? 137.693 166.361 96.481  1.00 61.21  ? 39  ALA   D CB    1 
ATOM   4677 N  N     . LEU   C 2 40  ? 135.725 167.694 94.343  1.00 70.96  ? 40  LEU   D N     1 
ATOM   4678 C  CA    . LEU   C 2 40  ? 134.779 167.700 93.239  1.00 70.47  ? 40  LEU   D CA    1 
ATOM   4679 C  C     . LEU   C 2 40  ? 134.081 169.053 93.213  1.00 66.53  ? 40  LEU   D C     1 
ATOM   4680 O  O     . LEU   C 2 40  ? 134.011 169.753 94.225  1.00 74.00  ? 40  LEU   D O     1 
ATOM   4681 C  CB    . LEU   C 2 40  ? 133.745 166.573 93.363  1.00 71.82  ? 40  LEU   D CB    1 
ATOM   4682 C  CG    . LEU   C 2 40  ? 134.254 165.142 93.188  1.00 67.98  ? 40  LEU   D CG    1 
ATOM   4683 C  CD1   . LEU   C 2 40  ? 133.226 164.151 93.701  1.00 66.19  ? 40  LEU   D CD1   1 
ATOM   4684 C  CD2   . LEU   C 2 40  ? 134.584 164.867 91.732  1.00 67.93  ? 40  LEU   D CD2   1 
ATOM   4685 N  N     . ASP   C 2 41  ? 133.572 169.424 92.041  1.00 80.21  ? 41  ASP   D N     1 
ATOM   4686 C  CA    . ASP   C 2 41  ? 132.911 170.720 91.899  1.00 81.67  ? 41  ASP   D CA    1 
ATOM   4687 C  C     . ASP   C 2 41  ? 131.918 170.648 90.749  1.00 86.50  ? 41  ASP   D C     1 
ATOM   4688 O  O     . ASP   C 2 41  ? 132.327 170.587 89.585  1.00 88.07  ? 41  ASP   D O     1 
ATOM   4689 C  CB    . ASP   C 2 41  ? 133.932 171.827 91.672  1.00 82.45  ? 41  ASP   D CB    1 
ATOM   4690 C  CG    . ASP   C 2 41  ? 133.282 173.179 91.468  1.00 88.14  ? 41  ASP   D CG    1 
ATOM   4691 O  OD1   . ASP   C 2 41  ? 132.435 173.566 92.301  1.00 87.27  ? 41  ASP   D OD1   1 
ATOM   4692 O  OD2   . ASP   C 2 41  ? 133.609 173.853 90.469  1.00 89.59  ? 41  ASP   D OD2   1 
ATOM   4693 N  N     . ASP   C 2 42  ? 130.624 170.657 91.079  1.00 85.37  ? 42  ASP   D N     1 
ATOM   4694 C  CA    . ASP   C 2 42  ? 129.536 170.732 90.103  1.00 88.31  ? 42  ASP   D CA    1 
ATOM   4695 C  C     . ASP   C 2 42  ? 129.603 169.575 89.100  1.00 89.62  ? 42  ASP   D C     1 
ATOM   4696 O  O     . ASP   C 2 42  ? 129.813 169.760 87.900  1.00 89.11  ? 42  ASP   D O     1 
ATOM   4697 C  CB    . ASP   C 2 42  ? 129.547 172.089 89.390  1.00 89.08  ? 42  ASP   D CB    1 
ATOM   4698 C  CG    . ASP   C 2 42  ? 128.162 172.547 88.983  1.00 89.16  ? 42  ASP   D CG    1 
ATOM   4699 O  OD1   . ASP   C 2 42  ? 127.612 171.989 88.010  1.00 89.28  ? 42  ASP   D OD1   1 
ATOM   4700 O  OD2   . ASP   C 2 42  ? 127.620 173.460 89.640  1.00 88.21  ? 42  ASP   D OD2   1 
ATOM   4701 N  N     . ILE   C 2 43  ? 129.413 168.368 89.628  1.00 85.41  ? 43  ILE   D N     1 
ATOM   4702 C  CA    . ILE   C 2 43  ? 129.369 167.150 88.823  1.00 87.40  ? 43  ILE   D CA    1 
ATOM   4703 C  C     . ILE   C 2 43  ? 127.918 166.728 88.642  1.00 84.23  ? 43  ILE   D C     1 
ATOM   4704 O  O     . ILE   C 2 43  ? 127.185 166.555 89.622  1.00 85.71  ? 43  ILE   D O     1 
ATOM   4705 C  CB    . ILE   C 2 43  ? 130.192 166.022 89.466  1.00 86.05  ? 43  ILE   D CB    1 
ATOM   4706 C  CG1   . ILE   C 2 43  ? 131.624 166.480 89.749  1.00 79.84  ? 43  ILE   D CG1   1 
ATOM   4707 C  CG2   . ILE   C 2 43  ? 130.172 164.786 88.591  1.00 83.27  ? 43  ILE   D CG2   1 
ATOM   4708 C  CD1   . ILE   C 2 43  ? 132.548 166.338 88.565  1.00 83.17  ? 43  ILE   D CD1   1 
ATOM   4709 N  N     . SER   C 2 44  ? 127.503 166.559 87.391  1.00 90.61  ? 44  SER   D N     1 
ATOM   4710 C  CA    . SER   C 2 44  ? 126.153 166.112 87.074  1.00 93.08  ? 44  SER   D CA    1 
ATOM   4711 C  C     . SER   C 2 44  ? 126.259 164.855 86.228  1.00 96.75  ? 44  SER   D C     1 
ATOM   4712 O  O     . SER   C 2 44  ? 126.950 164.853 85.204  1.00 95.64  ? 44  SER   D O     1 
ATOM   4713 C  CB    . SER   C 2 44  ? 125.362 167.204 86.348  1.00 93.20  ? 44  SER   D CB    1 
ATOM   4714 O  OG    . SER   C 2 44  ? 125.623 167.206 84.954  1.00 92.78  ? 44  SER   D OG    1 
ATOM   4715 N  N     . LEU   C 2 45  ? 125.584 163.792 86.656  1.00 93.64  ? 45  LEU   D N     1 
ATOM   4716 C  CA    . LEU   C 2 45  ? 125.752 162.471 86.074  1.00 90.16  ? 45  LEU   D CA    1 
ATOM   4717 C  C     . LEU   C 2 45  ? 124.390 161.811 85.921  1.00 86.54  ? 45  LEU   D C     1 
ATOM   4718 O  O     . LEU   C 2 45  ? 123.515 161.965 86.774  1.00 87.49  ? 45  LEU   D O     1 
ATOM   4719 C  CB    . LEU   C 2 45  ? 126.665 161.601 86.955  1.00 91.66  ? 45  LEU   D CB    1 
ATOM   4720 C  CG    . LEU   C 2 45  ? 127.414 160.379 86.413  1.00 91.52  ? 45  LEU   D CG    1 
ATOM   4721 C  CD1   . LEU   C 2 45  ? 128.070 160.692 85.087  1.00 87.40  ? 45  LEU   D CD1   1 
ATOM   4722 C  CD2   . LEU   C 2 45  ? 128.438 159.865 87.435  1.00 90.66  ? 45  LEU   D CD2   1 
ATOM   4723 N  N     . LYS   C 2 46  ? 124.219 161.077 84.829  1.00 96.30  ? 46  LYS   D N     1 
ATOM   4724 C  CA    . LYS   C 2 46  ? 123.002 160.323 84.559  1.00 96.76  ? 46  LYS   D CA    1 
ATOM   4725 C  C     . LYS   C 2 46  ? 123.405 158.969 83.997  1.00 101.35 ? 46  LYS   D C     1 
ATOM   4726 O  O     . LYS   C 2 46  ? 123.816 158.876 82.836  1.00 102.45 ? 46  LYS   D O     1 
ATOM   4727 C  CB    . LYS   C 2 46  ? 122.107 161.073 83.581  1.00 97.03  ? 46  LYS   D CB    1 
ATOM   4728 C  CG    . LYS   C 2 46  ? 120.632 160.912 83.844  1.00 101.04 ? 46  LYS   D CG    1 
ATOM   4729 C  CD    . LYS   C 2 46  ? 119.860 162.039 83.193  1.00 100.14 ? 46  LYS   D CD    1 
ATOM   4730 C  CE    . LYS   C 2 46  ? 120.306 163.398 83.709  1.00 96.57  ? 46  LYS   D CE    1 
ATOM   4731 N  NZ    . LYS   C 2 46  ? 120.389 163.404 85.194  1.00 98.43  ? 46  LYS   D NZ    1 
ATOM   4732 N  N     . ALA   C 2 47  ? 123.294 157.925 84.809  1.00 94.88  ? 47  ALA   D N     1 
ATOM   4733 C  CA    . ALA   C 2 47  ? 123.624 156.573 84.389  1.00 93.53  ? 47  ALA   D CA    1 
ATOM   4734 C  C     . ALA   C 2 47  ? 122.340 155.777 84.219  1.00 94.37  ? 47  ALA   D C     1 
ATOM   4735 O  O     . ALA   C 2 47  ? 121.592 155.586 85.186  1.00 95.88  ? 47  ALA   D O     1 
ATOM   4736 C  CB    . ALA   C 2 47  ? 124.546 155.895 85.402  1.00 94.43  ? 47  ALA   D CB    1 
ATOM   4737 N  N     . TYR   C 2 48  ? 122.095 155.312 82.998  1.00 105.52 ? 48  TYR   D N     1 
ATOM   4738 C  CA    . TYR   C 2 48  ? 120.894 154.572 82.652  1.00 108.10 ? 48  TYR   D CA    1 
ATOM   4739 C  C     . TYR   C 2 48  ? 121.088 153.084 82.947  1.00 105.24 ? 48  TYR   D C     1 
ATOM   4740 O  O     . TYR   C 2 48  ? 122.049 152.670 83.603  1.00 106.33 ? 48  TYR   D O     1 
ATOM   4741 C  CB    . TYR   C 2 48  ? 120.536 154.811 81.183  1.00 106.73 ? 48  TYR   D CB    1 
ATOM   4742 C  CG    . TYR   C 2 48  ? 120.007 156.198 80.885  1.00 107.62 ? 48  TYR   D CG    1 
ATOM   4743 C  CD1   . TYR   C 2 48  ? 118.709 156.559 81.223  1.00 107.52 ? 48  TYR   D CD1   1 
ATOM   4744 C  CD2   . TYR   C 2 48  ? 120.805 157.142 80.254  1.00 108.81 ? 48  TYR   D CD2   1 
ATOM   4745 C  CE1   . TYR   C 2 48  ? 118.226 157.824 80.951  1.00 109.37 ? 48  TYR   D CE1   1 
ATOM   4746 C  CE2   . TYR   C 2 48  ? 120.330 158.408 79.977  1.00 108.61 ? 48  TYR   D CE2   1 
ATOM   4747 C  CZ    . TYR   C 2 48  ? 119.040 158.743 80.327  1.00 110.23 ? 48  TYR   D CZ    1 
ATOM   4748 O  OH    . TYR   C 2 48  ? 118.553 159.999 80.057  1.00 108.92 ? 48  TYR   D OH    1 
ATOM   4749 N  N     . GLU   C 2 49  ? 120.158 152.267 82.466  1.00 102.39 ? 49  GLU   D N     1 
ATOM   4750 C  CA    . GLU   C 2 49  ? 120.199 150.826 82.658  1.00 105.51 ? 49  GLU   D CA    1 
ATOM   4751 C  C     . GLU   C 2 49  ? 120.909 150.155 81.489  1.00 106.74 ? 49  GLU   D C     1 
ATOM   4752 O  O     . GLU   C 2 49  ? 120.795 150.585 80.339  1.00 105.80 ? 49  GLU   D O     1 
ATOM   4753 C  CB    . GLU   C 2 49  ? 118.787 150.256 82.802  1.00 107.71 ? 49  GLU   D CB    1 
ATOM   4754 C  CG    . GLU   C 2 49  ? 118.717 148.952 83.576  1.00 108.59 ? 49  GLU   D CG    1 
ATOM   4755 C  CD    . GLU   C 2 49  ? 118.492 149.162 85.060  1.00 109.69 ? 49  GLU   D CD    1 
ATOM   4756 O  OE1   . GLU   C 2 49  ? 119.408 149.675 85.736  1.00 107.39 ? 49  GLU   D OE1   1 
ATOM   4757 O  OE2   . GLU   C 2 49  ? 117.396 148.815 85.550  1.00 108.57 ? 49  GLU   D OE2   1 
ATOM   4758 N  N     . GLY   C 2 50  ? 121.640 149.088 81.796  1.00 87.82  ? 50  GLY   D N     1 
ATOM   4759 C  CA    . GLY   C 2 50  ? 122.411 148.390 80.782  1.00 84.99  ? 50  GLY   D CA    1 
ATOM   4760 C  C     . GLY   C 2 50  ? 123.548 149.208 80.210  1.00 84.77  ? 50  GLY   D C     1 
ATOM   4761 O  O     . GLY   C 2 50  ? 123.758 149.204 78.990  1.00 80.37  ? 50  GLY   D O     1 
ATOM   4762 N  N     . ASP   C 2 51  ? 124.289 149.912 81.062  1.00 96.52  ? 51  ASP   D N     1 
ATOM   4763 C  CA    . ASP   C 2 51  ? 125.363 150.796 80.637  1.00 96.19  ? 51  ASP   D CA    1 
ATOM   4764 C  C     . ASP   C 2 51  ? 126.659 150.421 81.339  1.00 93.11  ? 51  ASP   D C     1 
ATOM   4765 O  O     . ASP   C 2 51  ? 126.660 150.102 82.532  1.00 90.39  ? 51  ASP   D O     1 
ATOM   4766 C  CB    . ASP   C 2 51  ? 125.025 152.259 80.938  1.00 94.97  ? 51  ASP   D CB    1 
ATOM   4767 C  CG    . ASP   C 2 51  ? 124.143 152.884 79.880  1.00 94.95  ? 51  ASP   D CG    1 
ATOM   4768 O  OD1   . ASP   C 2 51  ? 123.848 152.205 78.874  1.00 93.99  ? 51  ASP   D OD1   1 
ATOM   4769 O  OD2   . ASP   C 2 51  ? 123.744 154.054 80.054  1.00 95.04  ? 51  ASP   D OD2   1 
ATOM   4770 N  N     . VAL   C 2 52  ? 127.758 150.457 80.594  1.00 83.68  ? 52  VAL   D N     1 
ATOM   4771 C  CA    . VAL   C 2 52  ? 129.100 150.320 81.147  1.00 83.80  ? 52  VAL   D CA    1 
ATOM   4772 C  C     . VAL   C 2 52  ? 129.791 151.663 80.966  1.00 83.79  ? 52  VAL   D C     1 
ATOM   4773 O  O     . VAL   C 2 52  ? 130.033 152.101 79.835  1.00 85.38  ? 52  VAL   D O     1 
ATOM   4774 C  CB    . VAL   C 2 52  ? 129.889 149.188 80.476  1.00 84.60  ? 52  VAL   D CB    1 
ATOM   4775 C  CG1   . VAL   C 2 52  ? 131.081 148.795 81.335  1.00 79.72  ? 52  VAL   D CG1   1 
ATOM   4776 C  CG2   . VAL   C 2 52  ? 128.991 147.991 80.230  1.00 85.30  ? 52  VAL   D CG2   1 
ATOM   4777 N  N     . ILE   C 2 53  ? 130.106 152.320 82.078  1.00 81.28  ? 53  ILE   D N     1 
ATOM   4778 C  CA    . ILE   C 2 53  ? 130.647 153.674 82.074  1.00 83.11  ? 53  ILE   D CA    1 
ATOM   4779 C  C     . ILE   C 2 53  ? 132.050 153.627 82.659  1.00 80.84  ? 53  ILE   D C     1 
ATOM   4780 O  O     . ILE   C 2 53  ? 132.252 153.126 83.772  1.00 82.92  ? 53  ILE   D O     1 
ATOM   4781 C  CB    . ILE   C 2 53  ? 129.749 154.643 82.857  1.00 80.22  ? 53  ILE   D CB    1 
ATOM   4782 C  CG1   . ILE   C 2 53  ? 128.396 154.786 82.162  1.00 79.82  ? 53  ILE   D CG1   1 
ATOM   4783 C  CG2   . ILE   C 2 53  ? 130.419 155.999 82.997  1.00 76.34  ? 53  ILE   D CG2   1 
ATOM   4784 C  CD1   . ILE   C 2 53  ? 127.217 154.683 83.097  1.00 81.40  ? 53  ILE   D CD1   1 
ATOM   4785 N  N     . GLY   C 2 54  ? 133.016 154.149 81.909  1.00 63.82  ? 54  GLY   D N     1 
ATOM   4786 C  CA    . GLY   C 2 54  ? 134.405 154.173 82.322  1.00 59.65  ? 54  GLY   D CA    1 
ATOM   4787 C  C     . GLY   C 2 54  ? 134.842 155.590 82.655  1.00 59.95  ? 54  GLY   D C     1 
ATOM   4788 O  O     . GLY   C 2 54  ? 134.622 156.520 81.874  1.00 65.29  ? 54  GLY   D O     1 
ATOM   4789 N  N     . LEU   C 2 55  ? 135.464 155.732 83.820  1.00 53.90  ? 55  LEU   D N     1 
ATOM   4790 C  CA    . LEU   C 2 55  ? 135.997 157.004 84.284  1.00 54.93  ? 55  LEU   D CA    1 
ATOM   4791 C  C     . LEU   C 2 55  ? 137.460 157.106 83.878  1.00 59.29  ? 55  LEU   D C     1 
ATOM   4792 O  O     . LEU   C 2 55  ? 138.246 156.189 84.142  1.00 62.46  ? 55  LEU   D O     1 
ATOM   4793 C  CB    . LEU   C 2 55  ? 135.861 157.131 85.802  1.00 54.26  ? 55  LEU   D CB    1 
ATOM   4794 C  CG    . LEU   C 2 55  ? 134.455 157.012 86.391  1.00 59.36  ? 55  LEU   D CG    1 
ATOM   4795 C  CD1   . LEU   C 2 55  ? 134.515 157.003 87.908  1.00 60.18  ? 55  LEU   D CD1   1 
ATOM   4796 C  CD2   . LEU   C 2 55  ? 133.566 158.141 85.898  1.00 60.84  ? 55  LEU   D CD2   1 
ATOM   4797 N  N     . VAL   C 2 56  ? 137.825 158.216 83.238  1.00 52.14  ? 56  VAL   D N     1 
ATOM   4798 C  CA    . VAL   C 2 56  ? 139.196 158.432 82.799  1.00 50.37  ? 56  VAL   D CA    1 
ATOM   4799 C  C     . VAL   C 2 56  ? 139.704 159.746 83.373  1.00 53.74  ? 56  VAL   D C     1 
ATOM   4800 O  O     . VAL   C 2 56  ? 138.936 160.666 83.660  1.00 61.88  ? 56  VAL   D O     1 
ATOM   4801 C  CB    . VAL   C 2 56  ? 139.330 158.428 81.261  1.00 51.98  ? 56  VAL   D CB    1 
ATOM   4802 C  CG1   . VAL   C 2 56  ? 139.114 157.027 80.715  1.00 56.26  ? 56  VAL   D CG1   1 
ATOM   4803 C  CG2   . VAL   C 2 56  ? 138.350 159.400 80.640  1.00 53.74  ? 56  VAL   D CG2   1 
ATOM   4804 N  N     . GLY   C 2 57  ? 141.014 159.818 83.543  1.00 69.81  ? 57  GLY   D N     1 
ATOM   4805 C  CA    . GLY   C 2 57  ? 141.653 160.999 84.082  1.00 70.06  ? 57  GLY   D CA    1 
ATOM   4806 C  C     . GLY   C 2 57  ? 143.009 160.673 84.656  1.00 70.08  ? 57  GLY   D C     1 
ATOM   4807 O  O     . GLY   C 2 57  ? 143.335 159.523 84.953  1.00 72.73  ? 57  GLY   D O     1 
ATOM   4808 N  N     . ILE   C 2 58  ? 143.817 161.720 84.818  1.00 65.27  ? 58  ILE   D N     1 
ATOM   4809 C  CA    . ILE   C 2 58  ? 145.171 161.581 85.346  1.00 62.84  ? 58  ILE   D CA    1 
ATOM   4810 C  C     . ILE   C 2 58  ? 145.101 161.372 86.852  1.00 56.97  ? 58  ILE   D C     1 
ATOM   4811 O  O     . ILE   C 2 58  ? 144.034 161.507 87.457  1.00 63.51  ? 58  ILE   D O     1 
ATOM   4812 C  CB    . ILE   C 2 58  ? 146.041 162.800 84.991  1.00 64.86  ? 58  ILE   D CB    1 
ATOM   4813 C  CG1   . ILE   C 2 58  ? 145.363 164.095 85.436  1.00 66.37  ? 58  ILE   D CG1   1 
ATOM   4814 C  CG2   . ILE   C 2 58  ? 146.324 162.835 83.500  1.00 62.95  ? 58  ILE   D CG2   1 
ATOM   4815 C  CD1   . ILE   C 2 58  ? 146.312 165.096 86.058  1.00 62.88  ? 58  ILE   D CD1   1 
ATOM   4816 N  N     . ASN   C 2 59  ? 146.233 161.019 87.458  1.00 55.65  ? 59  ASN   D N     1 
ATOM   4817 C  CA    . ASN   C 2 59  ? 146.274 160.763 88.892  1.00 63.81  ? 59  ASN   D CA    1 
ATOM   4818 C  C     . ASN   C 2 59  ? 145.864 162.007 89.671  1.00 67.27  ? 59  ASN   D C     1 
ATOM   4819 O  O     . ASN   C 2 59  ? 146.329 163.115 89.384  1.00 70.69  ? 59  ASN   D O     1 
ATOM   4820 C  CB    . ASN   C 2 59  ? 147.674 160.317 89.308  1.00 66.81  ? 59  ASN   D CB    1 
ATOM   4821 C  CG    . ASN   C 2 59  ? 147.895 158.834 89.110  1.00 68.11  ? 59  ASN   D CG    1 
ATOM   4822 O  OD1   . ASN   C 2 59  ? 148.893 158.415 88.525  1.00 74.43  ? 59  ASN   D OD1   1 
ATOM   4823 N  ND2   . ASN   C 2 59  ? 146.961 158.028 89.596  1.00 64.99  ? 59  ASN   D ND2   1 
ATOM   4824 N  N     . GLY   C 2 60  ? 144.995 161.822 90.660  1.00 63.26  ? 60  GLY   D N     1 
ATOM   4825 C  CA    . GLY   C 2 60  ? 144.490 162.922 91.453  1.00 57.70  ? 60  GLY   D CA    1 
ATOM   4826 C  C     . GLY   C 2 60  ? 143.317 163.667 90.859  1.00 61.82  ? 60  GLY   D C     1 
ATOM   4827 O  O     . GLY   C 2 60  ? 143.003 164.766 91.331  1.00 64.98  ? 60  GLY   D O     1 
ATOM   4828 N  N     . SER   C 2 61  ? 142.655 163.109 89.842  1.00 63.49  ? 61  SER   D N     1 
ATOM   4829 C  CA    . SER   C 2 61  ? 141.543 163.801 89.200  1.00 55.59  ? 61  SER   D CA    1 
ATOM   4830 C  C     . SER   C 2 61  ? 140.270 163.761 90.036  1.00 63.79  ? 61  SER   D C     1 
ATOM   4831 O  O     . SER   C 2 61  ? 139.484 164.712 90.000  1.00 70.71  ? 61  SER   D O     1 
ATOM   4832 C  CB    . SER   C 2 61  ? 141.278 163.198 87.821  1.00 56.97  ? 61  SER   D CB    1 
ATOM   4833 O  OG    . SER   C 2 61  ? 141.795 164.027 86.796  1.00 60.37  ? 61  SER   D OG    1 
ATOM   4834 N  N     . GLY   C 2 62  ? 140.044 162.681 90.780  1.00 62.87  ? 62  GLY   D N     1 
ATOM   4835 C  CA    . GLY   C 2 62  ? 138.862 162.578 91.613  1.00 54.78  ? 62  GLY   D CA    1 
ATOM   4836 C  C     . GLY   C 2 62  ? 137.919 161.458 91.222  1.00 62.16  ? 62  GLY   D C     1 
ATOM   4837 O  O     . GLY   C 2 62  ? 136.708 161.560 91.432  1.00 63.60  ? 62  GLY   D O     1 
ATOM   4838 N  N     . LYS   C 2 63  ? 138.460 160.382 90.648  1.00 63.25  ? 63  LYS   D N     1 
ATOM   4839 C  CA    . LYS   C 2 63  ? 137.651 159.230 90.267  1.00 46.92  ? 63  LYS   D CA    1 
ATOM   4840 C  C     . LYS   C 2 63  ? 137.277 158.358 91.459  1.00 48.38  ? 63  LYS   D C     1 
ATOM   4841 O  O     . LYS   C 2 63  ? 136.135 157.893 91.552  1.00 61.07  ? 63  LYS   D O     1 
ATOM   4842 C  CB    . LYS   C 2 63  ? 138.394 158.389 89.225  1.00 47.95  ? 63  LYS   D CB    1 
ATOM   4843 C  CG    . LYS   C 2 63  ? 139.121 159.208 88.173  1.00 51.84  ? 63  LYS   D CG    1 
ATOM   4844 C  CD    . LYS   C 2 63  ? 139.727 158.316 87.109  1.00 50.22  ? 63  LYS   D CD    1 
ATOM   4845 C  CE    . LYS   C 2 63  ? 141.159 157.954 87.451  1.00 53.86  ? 63  LYS   D CE    1 
ATOM   4846 N  NZ    . LYS   C 2 63  ? 141.873 159.089 88.093  1.00 52.71  ? 63  LYS   D NZ    1 
ATOM   4847 N  N     . SER   C 2 64  ? 138.219 158.130 92.378  1.00 50.30  ? 64  SER   D N     1 
ATOM   4848 C  CA    . SER   C 2 64  ? 137.918 157.332 93.561  1.00 53.71  ? 64  SER   D CA    1 
ATOM   4849 C  C     . SER   C 2 64  ? 136.916 158.031 94.468  1.00 53.42  ? 64  SER   D C     1 
ATOM   4850 O  O     . SER   C 2 64  ? 136.056 157.370 95.061  1.00 58.69  ? 64  SER   D O     1 
ATOM   4851 C  CB    . SER   C 2 64  ? 139.201 157.022 94.331  1.00 59.61  ? 64  SER   D CB    1 
ATOM   4852 O  OG    . SER   C 2 64  ? 140.098 156.262 93.541  1.00 62.62  ? 64  SER   D OG    1 
ATOM   4853 N  N     . THR   C 2 65  ? 137.009 159.357 94.592  1.00 54.69  ? 65  THR   D N     1 
ATOM   4854 C  CA    . THR   C 2 65  ? 136.041 160.093 95.397  1.00 50.14  ? 65  THR   D CA    1 
ATOM   4855 C  C     . THR   C 2 65  ? 134.637 159.972 94.816  1.00 48.91  ? 65  THR   D C     1 
ATOM   4856 O  O     . THR   C 2 65  ? 133.669 159.753 95.553  1.00 55.24  ? 65  THR   D O     1 
ATOM   4857 C  CB    . THR   C 2 65  ? 136.458 161.561 95.506  1.00 55.03  ? 65  THR   D CB    1 
ATOM   4858 O  OG1   . THR   C 2 65  ? 137.638 161.665 96.312  1.00 53.29  ? 65  THR   D OG1   1 
ATOM   4859 C  CG2   . THR   C 2 65  ? 135.354 162.389 96.135  1.00 60.40  ? 65  THR   D CG2   1 
ATOM   4860 N  N     . LEU   C 2 66  ? 134.509 160.095 93.493  1.00 49.69  ? 66  LEU   D N     1 
ATOM   4861 C  CA    . LEU   C 2 66  ? 133.205 159.935 92.858  1.00 53.00  ? 66  LEU   D CA    1 
ATOM   4862 C  C     . LEU   C 2 66  ? 132.679 158.515 93.021  1.00 58.93  ? 66  LEU   D C     1 
ATOM   4863 O  O     . LEU   C 2 66  ? 131.484 158.313 93.273  1.00 59.10  ? 66  LEU   D O     1 
ATOM   4864 C  CB    . LEU   C 2 66  ? 133.293 160.309 91.379  1.00 50.01  ? 66  LEU   D CB    1 
ATOM   4865 C  CG    . LEU   C 2 66  ? 131.961 160.443 90.638  1.00 55.87  ? 66  LEU   D CG    1 
ATOM   4866 C  CD1   . LEU   C 2 66  ? 131.098 161.517 91.279  1.00 56.88  ? 66  LEU   D CD1   1 
ATOM   4867 C  CD2   . LEU   C 2 66  ? 132.190 160.746 89.167  1.00 56.84  ? 66  LEU   D CD2   1 
ATOM   4868 N  N     . SER   C 2 67  ? 133.552 157.515 92.876  1.00 72.95  ? 67  SER   D N     1 
ATOM   4869 C  CA    . SER   C 2 67  ? 133.124 156.133 93.061  1.00 68.28  ? 67  SER   D CA    1 
ATOM   4870 C  C     . SER   C 2 67  ? 132.656 155.875 94.488  1.00 70.33  ? 67  SER   D C     1 
ATOM   4871 O  O     . SER   C 2 67  ? 131.661 155.170 94.692  1.00 72.01  ? 67  SER   D O     1 
ATOM   4872 C  CB    . SER   C 2 67  ? 134.259 155.177 92.689  1.00 65.38  ? 67  SER   D CB    1 
ATOM   4873 O  OG    . SER   C 2 67  ? 135.288 155.206 93.662  1.00 69.93  ? 67  SER   D OG    1 
ATOM   4874 N  N     . ASN   C 2 68  ? 133.352 156.434 95.481  1.00 70.19  ? 68  ASN   D N     1 
ATOM   4875 C  CA    . ASN   C 2 68  ? 132.925 156.273 96.868  1.00 70.89  ? 68  ASN   D CA    1 
ATOM   4876 C  C     . ASN   C 2 68  ? 131.622 157.009 97.147  1.00 74.82  ? 68  ASN   D C     1 
ATOM   4877 O  O     . ASN   C 2 68  ? 130.789 156.517 97.915  1.00 75.81  ? 68  ASN   D O     1 
ATOM   4878 C  CB    . ASN   C 2 68  ? 134.021 156.759 97.814  1.00 70.58  ? 68  ASN   D CB    1 
ATOM   4879 C  CG    . ASN   C 2 68  ? 135.130 155.745 97.986  1.00 75.27  ? 68  ASN   D CG    1 
ATOM   4880 O  OD1   . ASN   C 2 68  ? 134.894 154.538 97.945  1.00 76.42  ? 68  ASN   D OD1   1 
ATOM   4881 N  ND2   . ASN   C 2 68  ? 136.350 156.229 98.183  1.00 75.90  ? 68  ASN   D ND2   1 
ATOM   4882 N  N     . ILE   C 2 69  ? 131.433 158.187 96.548  1.00 73.23  ? 69  ILE   D N     1 
ATOM   4883 C  CA    . ILE   C 2 69  ? 130.175 158.909 96.707  1.00 69.87  ? 69  ILE   D CA    1 
ATOM   4884 C  C     . ILE   C 2 69  ? 129.021 158.102 96.127  1.00 72.52  ? 69  ILE   D C     1 
ATOM   4885 O  O     . ILE   C 2 69  ? 127.945 158.011 96.730  1.00 79.79  ? 69  ILE   D O     1 
ATOM   4886 C  CB    . ILE   C 2 69  ? 130.279 160.306 96.066  1.00 68.15  ? 69  ILE   D CB    1 
ATOM   4887 C  CG1   . ILE   C 2 69  ? 130.977 161.276 97.020  1.00 66.87  ? 69  ILE   D CG1   1 
ATOM   4888 C  CG2   . ILE   C 2 69  ? 128.906 160.828 95.674  1.00 67.28  ? 69  ILE   D CG2   1 
ATOM   4889 C  CD1   . ILE   C 2 69  ? 130.975 162.709 96.546  1.00 67.81  ? 69  ILE   D CD1   1 
ATOM   4890 N  N     . ILE   C 2 70  ? 129.227 157.499 94.953  1.00 78.54  ? 70  ILE   D N     1 
ATOM   4891 C  CA    . ILE   C 2 70  ? 128.206 156.623 94.381  1.00 79.29  ? 70  ILE   D CA    1 
ATOM   4892 C  C     . ILE   C 2 70  ? 127.949 155.434 95.300  1.00 76.73  ? 70  ILE   D C     1 
ATOM   4893 O  O     . ILE   C 2 70  ? 126.797 155.052 95.537  1.00 76.32  ? 70  ILE   D O     1 
ATOM   4894 C  CB    . ILE   C 2 70  ? 128.618 156.169 92.969  1.00 78.00  ? 70  ILE   D CB    1 
ATOM   4895 C  CG1   . ILE   C 2 70  ? 128.618 157.354 92.003  1.00 79.04  ? 70  ILE   D CG1   1 
ATOM   4896 C  CG2   . ILE   C 2 70  ? 127.690 155.074 92.465  1.00 75.94  ? 70  ILE   D CG2   1 
ATOM   4897 C  CD1   . ILE   C 2 70  ? 128.852 156.963 90.562  1.00 78.79  ? 70  ILE   D CD1   1 
ATOM   4898 N  N     . GLY   C 2 71  ? 129.016 154.835 95.833  1.00 89.35  ? 71  GLY   D N     1 
ATOM   4899 C  CA    . GLY   C 2 71  ? 128.856 153.691 96.712  1.00 92.27  ? 71  GLY   D CA    1 
ATOM   4900 C  C     . GLY   C 2 71  ? 128.141 154.015 98.008  1.00 93.78  ? 71  GLY   D C     1 
ATOM   4901 O  O     . GLY   C 2 71  ? 127.356 153.203 98.505  1.00 93.66  ? 71  GLY   D O     1 
ATOM   4902 N  N     . GLY   C 2 72  ? 128.397 155.193 98.573  1.00 93.77  ? 72  GLY   D N     1 
ATOM   4903 C  CA    . GLY   C 2 72  ? 127.763 155.612 99.807  1.00 92.77  ? 72  GLY   D CA    1 
ATOM   4904 C  C     . GLY   C 2 72  ? 128.690 155.755 100.992 1.00 89.64  ? 72  GLY   D C     1 
ATOM   4905 O  O     . GLY   C 2 72  ? 128.241 156.211 102.051 1.00 92.01  ? 72  GLY   D O     1 
ATOM   4906 N  N     . SER   C 2 73  ? 129.965 155.387 100.860 1.00 84.44  ? 73  SER   D N     1 
ATOM   4907 C  CA    . SER   C 2 73  ? 130.917 155.560 101.947 1.00 88.15  ? 73  SER   D CA    1 
ATOM   4908 C  C     . SER   C 2 73  ? 131.267 157.020 102.200 1.00 91.56  ? 73  SER   D C     1 
ATOM   4909 O  O     . SER   C 2 73  ? 131.897 157.322 103.219 1.00 93.14  ? 73  SER   D O     1 
ATOM   4910 C  CB    . SER   C 2 73  ? 132.198 154.772 101.660 1.00 89.05  ? 73  SER   D CB    1 
ATOM   4911 O  OG    . SER   C 2 73  ? 133.308 155.348 102.325 1.00 88.06  ? 73  SER   D OG    1 
ATOM   4912 N  N     . LEU   C 2 74  ? 130.880 157.922 101.303 1.00 82.96  ? 74  LEU   D N     1 
ATOM   4913 C  CA    . LEU   C 2 74  ? 131.120 159.346 101.448 1.00 80.44  ? 74  LEU   D CA    1 
ATOM   4914 C  C     . LEU   C 2 74  ? 129.811 160.106 101.283 1.00 79.91  ? 74  LEU   D C     1 
ATOM   4915 O  O     . LEU   C 2 74  ? 128.878 159.642 100.622 1.00 79.96  ? 74  LEU   D O     1 
ATOM   4916 C  CB    . LEU   C 2 74  ? 132.146 159.847 100.423 1.00 82.94  ? 74  LEU   D CB    1 
ATOM   4917 C  CG    . LEU   C 2 74  ? 133.619 159.799 100.828 1.00 81.68  ? 74  LEU   D CG    1 
ATOM   4918 C  CD1   . LEU   C 2 74  ? 134.486 160.412 99.742  1.00 77.91  ? 74  LEU   D CD1   1 
ATOM   4919 C  CD2   . LEU   C 2 74  ? 133.837 160.508 102.153 1.00 80.14  ? 74  LEU   D CD2   1 
ATOM   4920 N  N     . SER   C 2 75  ? 129.753 161.284 101.895 1.00 97.95  ? 75  SER   D N     1 
ATOM   4921 C  CA    . SER   C 2 75  ? 128.587 162.142 101.824 1.00 99.73  ? 75  SER   D CA    1 
ATOM   4922 C  C     . SER   C 2 75  ? 128.961 163.460 101.160 1.00 97.49  ? 75  SER   D C     1 
ATOM   4923 O  O     . SER   C 2 75  ? 129.894 164.136 101.618 1.00 96.32  ? 75  SER   D O     1 
ATOM   4924 C  CB    . SER   C 2 75  ? 128.011 162.403 103.224 1.00 101.36 ? 75  SER   D CB    1 
ATOM   4925 O  OG    . SER   C 2 75  ? 127.692 161.186 103.878 1.00 99.46  ? 75  SER   D OG    1 
ATOM   4926 N  N     . PRO   C 2 76  ? 128.280 163.853 100.086 1.00 86.79  ? 76  PRO   D N     1 
ATOM   4927 C  CA    . PRO   C 2 76  ? 128.624 165.110 99.415  1.00 88.08  ? 76  PRO   D CA    1 
ATOM   4928 C  C     . PRO   C 2 76  ? 128.386 166.311 100.313 1.00 89.65  ? 76  PRO   D C     1 
ATOM   4929 O  O     . PRO   C 2 76  ? 127.462 166.336 101.131 1.00 92.98  ? 76  PRO   D O     1 
ATOM   4930 C  CB    . PRO   C 2 76  ? 127.685 165.133 98.202  1.00 84.56  ? 76  PRO   D CB    1 
ATOM   4931 C  CG    . PRO   C 2 76  ? 127.265 163.707 98.018  1.00 86.97  ? 76  PRO   D CG    1 
ATOM   4932 C  CD    . PRO   C 2 76  ? 127.184 163.152 99.403  1.00 83.34  ? 76  PRO   D CD    1 
ATOM   4933 N  N     . THR   C 2 77  ? 129.243 167.321 100.154 1.00 82.82  ? 77  THR   D N     1 
ATOM   4934 C  CA    . THR   C 2 77  ? 129.059 168.566 100.890 1.00 85.65  ? 77  THR   D CA    1 
ATOM   4935 C  C     . THR   C 2 77  ? 127.804 169.292 100.421 1.00 86.83  ? 77  THR   D C     1 
ATOM   4936 O  O     . THR   C 2 77  ? 126.972 169.710 101.236 1.00 87.24  ? 77  THR   D O     1 
ATOM   4937 C  CB    . THR   C 2 77  ? 130.292 169.457 100.734 1.00 82.78  ? 77  THR   D CB    1 
ATOM   4938 O  OG1   . THR   C 2 77  ? 131.379 168.903 101.487 1.00 81.76  ? 77  THR   D OG1   1 
ATOM   4939 C  CG2   . THR   C 2 77  ? 130.007 170.862 101.236 1.00 84.58  ? 77  THR   D CG2   1 
ATOM   4940 N  N     . VAL   C 2 78  ? 127.646 169.445 99.108  1.00 82.31  ? 78  VAL   D N     1 
ATOM   4941 C  CA    . VAL   C 2 78  ? 126.461 170.049 98.512  1.00 83.77  ? 78  VAL   D CA    1 
ATOM   4942 C  C     . VAL   C 2 78  ? 125.953 169.121 97.418  1.00 82.97  ? 78  VAL   D C     1 
ATOM   4943 O  O     . VAL   C 2 78  ? 126.735 168.660 96.578  1.00 86.16  ? 78  VAL   D O     1 
ATOM   4944 C  CB    . VAL   C 2 78  ? 126.749 171.448 97.935  1.00 84.43  ? 78  VAL   D CB    1 
ATOM   4945 C  CG1   . VAL   C 2 78  ? 125.453 172.130 97.528  1.00 82.12  ? 78  VAL   D CG1   1 
ATOM   4946 C  CG2   . VAL   C 2 78  ? 127.509 172.301 98.939  1.00 83.82  ? 78  VAL   D CG2   1 
ATOM   4947 N  N     . GLY   C 2 79  ? 124.657 168.846 97.428  1.00 92.42  ? 79  GLY   D N     1 
ATOM   4948 C  CA    . GLY   C 2 79  ? 124.020 168.072 96.383  1.00 91.51  ? 79  GLY   D CA    1 
ATOM   4949 C  C     . GLY   C 2 79  ? 123.568 166.706 96.868  1.00 92.43  ? 79  GLY   D C     1 
ATOM   4950 O  O     . GLY   C 2 79  ? 123.852 166.278 97.985  1.00 93.54  ? 79  GLY   D O     1 
ATOM   4951 N  N     . LYS   C 2 80  ? 122.847 166.025 95.981  1.00 91.51  ? 80  LYS   D N     1 
ATOM   4952 C  CA    . LYS   C 2 80  ? 122.259 164.731 96.289  1.00 92.95  ? 80  LYS   D CA    1 
ATOM   4953 C  C     . LYS   C 2 80  ? 122.443 163.785 95.110  1.00 94.91  ? 80  LYS   D C     1 
ATOM   4954 O  O     . LYS   C 2 80  ? 122.576 164.206 93.959  1.00 93.33  ? 80  LYS   D O     1 
ATOM   4955 C  CB    . LYS   C 2 80  ? 120.771 164.864 96.642  1.00 93.66  ? 80  LYS   D CB    1 
ATOM   4956 C  CG    . LYS   C 2 80  ? 119.872 165.165 95.454  1.00 94.15  ? 80  LYS   D CG    1 
ATOM   4957 C  CD    . LYS   C 2 80  ? 118.865 164.054 95.212  1.00 94.26  ? 80  LYS   D CD    1 
ATOM   4958 C  CE    . LYS   C 2 80  ? 118.326 164.107 93.791  1.00 93.00  ? 80  LYS   D CE    1 
ATOM   4959 N  NZ    . LYS   C 2 80  ? 117.666 162.837 93.390  1.00 90.59  ? 80  LYS   D NZ    1 
ATOM   4960 N  N     . VAL   C 2 81  ? 122.453 162.492 95.421  1.00 100.99 ? 81  VAL   D N     1 
ATOM   4961 C  CA    . VAL   C 2 81  ? 122.556 161.430 94.423  1.00 99.85  ? 81  VAL   D CA    1 
ATOM   4962 C  C     . VAL   C 2 81  ? 121.576 160.331 94.802  1.00 98.36  ? 81  VAL   D C     1 
ATOM   4963 O  O     . VAL   C 2 81  ? 121.533 159.902 95.958  1.00 97.87  ? 81  VAL   D O     1 
ATOM   4964 C  CB    . VAL   C 2 81  ? 123.995 160.881 94.322  1.00 100.05 ? 81  VAL   D CB    1 
ATOM   4965 C  CG1   . VAL   C 2 81  ? 124.687 160.964 95.670  1.00 96.55  ? 81  VAL   D CG1   1 
ATOM   4966 C  CG2   . VAL   C 2 81  ? 123.988 159.442 93.823  1.00 98.84  ? 81  VAL   D CG2   1 
ATOM   4967 N  N     . ASP   C 2 82  ? 120.787 159.873 93.834  1.00 108.22 ? 82  ASP   D N     1 
ATOM   4968 C  CA    . ASP   C 2 82  ? 119.826 158.805 94.072  1.00 109.76 ? 82  ASP   D CA    1 
ATOM   4969 C  C     . ASP   C 2 82  ? 120.145 157.584 93.217  1.00 110.30 ? 82  ASP   D C     1 
ATOM   4970 O  O     . ASP   C 2 82  ? 120.530 157.704 92.046  1.00 111.19 ? 82  ASP   D O     1 
ATOM   4971 C  CB    . ASP   C 2 82  ? 118.388 159.273 93.821  1.00 111.90 ? 82  ASP   D CB    1 
ATOM   4972 C  CG    . ASP   C 2 82  ? 118.208 159.899 92.463  1.00 111.97 ? 82  ASP   D CG    1 
ATOM   4973 O  OD1   . ASP   C 2 82  ? 119.214 160.029 91.746  1.00 112.42 ? 82  ASP   D OD1   1 
ATOM   4974 O  OD2   . ASP   C 2 82  ? 117.066 160.261 92.113  1.00 111.98 ? 82  ASP   D OD2   1 
ATOM   4975 N  N     . ARG   C 2 83  ? 119.986 156.409 93.826  1.00 108.37 ? 83  ARG   D N     1 
ATOM   4976 C  CA    . ARG   C 2 83  ? 120.294 155.127 93.209  1.00 106.48 ? 83  ARG   D CA    1 
ATOM   4977 C  C     . ARG   C 2 83  ? 119.048 154.255 93.250  1.00 108.79 ? 83  ARG   D C     1 
ATOM   4978 O  O     . ARG   C 2 83  ? 118.381 154.174 94.287  1.00 110.94 ? 83  ARG   D O     1 
ATOM   4979 C  CB    . ARG   C 2 83  ? 121.432 154.422 93.949  1.00 107.00 ? 83  ARG   D CB    1 
ATOM   4980 C  CG    . ARG   C 2 83  ? 122.384 155.359 94.664  1.00 106.38 ? 83  ARG   D CG    1 
ATOM   4981 C  CD    . ARG   C 2 83  ? 123.034 154.663 95.857  1.00 108.60 ? 83  ARG   D CD    1 
ATOM   4982 N  NE    . ARG   C 2 83  ? 124.086 155.456 96.487  1.00 111.21 ? 83  ARG   D NE    1 
ATOM   4983 C  CZ    . ARG   C 2 83  ? 123.914 156.650 97.040  1.00 111.64 ? 83  ARG   D CZ    1 
ATOM   4984 N  NH1   . ARG   C 2 83  ? 122.721 157.217 97.112  1.00 109.78 ? 83  ARG   D NH1   1 
ATOM   4985 N  NH2   . ARG   C 2 83  ? 124.965 157.285 97.551  1.00 109.69 ? 83  ARG   D NH2   1 
ATOM   4986 N  N     . ASN   C 2 84  ? 118.735 153.607 92.135  1.00 100.44 ? 84  ASN   D N     1 
ATOM   4987 C  CA    . ASN   C 2 84  ? 117.616 152.666 92.080  1.00 99.44  ? 84  ASN   D CA    1 
ATOM   4988 C  C     . ASN   C 2 84  ? 118.109 151.229 92.241  1.00 98.94  ? 84  ASN   D C     1 
ATOM   4989 O  O     . ASN   C 2 84  ? 118.031 150.406 91.329  1.00 100.39 ? 84  ASN   D O     1 
ATOM   4990 C  CB    . ASN   C 2 84  ? 116.839 152.844 90.778  1.00 98.54  ? 84  ASN   D CB    1 
ATOM   4991 C  CG    . ASN   C 2 84  ? 116.350 154.263 90.584  1.00 100.14 ? 84  ASN   D CG    1 
ATOM   4992 O  OD1   . ASN   C 2 84  ? 116.588 155.135 91.419  1.00 102.59 ? 84  ASN   D OD1   1 
ATOM   4993 N  ND2   . ASN   C 2 84  ? 115.656 154.503 89.477  1.00 101.28 ? 84  ASN   D ND2   1 
ATOM   4994 N  N     . GLY   C 2 85  ? 118.623 150.929 93.426  1.00 85.20  ? 85  GLY   D N     1 
ATOM   4995 C  CA    . GLY   C 2 85  ? 119.060 149.583 93.724  1.00 85.94  ? 85  GLY   D CA    1 
ATOM   4996 C  C     . GLY   C 2 85  ? 120.138 149.577 94.792  1.00 89.86  ? 85  GLY   D C     1 
ATOM   4997 O  O     . GLY   C 2 85  ? 120.359 150.565 95.490  1.00 89.34  ? 85  GLY   D O     1 
ATOM   4998 N  N     . GLU   C 2 86  ? 120.800 148.428 94.896  1.00 107.61 ? 86  GLU   D N     1 
ATOM   4999 C  CA    . GLU   C 2 86  ? 121.882 148.210 95.843  1.00 108.02 ? 86  GLU   D CA    1 
ATOM   5000 C  C     . GLU   C 2 86  ? 123.212 148.189 95.103  1.00 108.56 ? 86  GLU   D C     1 
ATOM   5001 O  O     . GLU   C 2 86  ? 123.343 147.542 94.060  1.00 108.11 ? 86  GLU   D O     1 
ATOM   5002 C  CB    . GLU   C 2 86  ? 121.689 146.899 96.609  1.00 109.38 ? 86  GLU   D CB    1 
ATOM   5003 C  CG    . GLU   C 2 86  ? 122.555 146.771 97.849  1.00 111.54 ? 86  GLU   D CG    1 
ATOM   5004 C  CD    . GLU   C 2 86  ? 121.829 147.186 99.112  1.00 111.76 ? 86  GLU   D CD    1 
ATOM   5005 O  OE1   . GLU   C 2 86  ? 121.424 148.364 99.205  1.00 109.79 ? 86  GLU   D OE1   1 
ATOM   5006 O  OE2   . GLU   C 2 86  ? 121.662 146.335 100.011 1.00 111.91 ? 86  GLU   D OE2   1 
ATOM   5007 N  N     . VAL   C 2 87  ? 124.196 148.899 95.648  1.00 100.16 ? 87  VAL   D N     1 
ATOM   5008 C  CA    . VAL   C 2 87  ? 125.488 149.056 94.999  1.00 99.00  ? 87  VAL   D CA    1 
ATOM   5009 C  C     . VAL   C 2 87  ? 126.546 148.291 95.783  1.00 99.91  ? 87  VAL   D C     1 
ATOM   5010 O  O     . VAL   C 2 87  ? 126.433 148.065 96.992  1.00 99.20  ? 87  VAL   D O     1 
ATOM   5011 C  CB    . VAL   C 2 87  ? 125.881 150.541 94.852  1.00 98.88  ? 87  VAL   D CB    1 
ATOM   5012 C  CG1   . VAL   C 2 87  ? 124.689 151.362 94.389  1.00 99.53  ? 87  VAL   D CG1   1 
ATOM   5013 C  CG2   . VAL   C 2 87  ? 126.424 151.082 96.160  1.00 96.32  ? 87  VAL   D CG2   1 
ATOM   5014 N  N     . SER   C 2 88  ? 127.586 147.871 95.065  1.00 96.57  ? 88  SER   D N     1 
ATOM   5015 C  CA    . SER   C 2 88  ? 128.732 147.215 95.680  1.00 93.54  ? 88  SER   D CA    1 
ATOM   5016 C  C     . SER   C 2 88  ? 129.995 147.680 94.973  1.00 90.99  ? 88  SER   D C     1 
ATOM   5017 O  O     . SER   C 2 88  ? 130.017 147.784 93.745  1.00 93.65  ? 88  SER   D O     1 
ATOM   5018 C  CB    . SER   C 2 88  ? 128.623 145.690 95.611  1.00 94.13  ? 88  SER   D CB    1 
ATOM   5019 O  OG    . SER   C 2 88  ? 128.348 145.267 94.290  1.00 93.43  ? 88  SER   D OG    1 
ATOM   5020 N  N     . VAL   C 2 89  ? 131.044 147.935 95.752  1.00 74.31  ? 89  VAL   D N     1 
ATOM   5021 C  CA    . VAL   C 2 89  ? 132.280 148.530 95.258  1.00 80.43  ? 89  VAL   D CA    1 
ATOM   5022 C  C     . VAL   C 2 89  ? 133.438 147.584 95.549  1.00 81.08  ? 89  VAL   D C     1 
ATOM   5023 O  O     . VAL   C 2 89  ? 133.569 147.080 96.671  1.00 77.43  ? 89  VAL   D O     1 
ATOM   5024 C  CB    . VAL   C 2 89  ? 132.533 149.909 95.896  1.00 73.99  ? 89  VAL   D CB    1 
ATOM   5025 C  CG1   . VAL   C 2 89  ? 133.866 150.479 95.435  1.00 70.69  ? 89  VAL   D CG1   1 
ATOM   5026 C  CG2   . VAL   C 2 89  ? 131.394 150.862 95.570  1.00 75.73  ? 89  VAL   D CG2   1 
ATOM   5027 N  N     . ILE   C 2 90  ? 134.272 147.344 94.538  1.00 75.00  ? 90  ILE   D N     1 
ATOM   5028 C  CA    . ILE   C 2 90  ? 135.517 146.597 94.678  1.00 66.99  ? 90  ILE   D CA    1 
ATOM   5029 C  C     . ILE   C 2 90  ? 136.667 147.547 94.378  1.00 71.87  ? 90  ILE   D C     1 
ATOM   5030 O  O     . ILE   C 2 90  ? 136.607 148.316 93.412  1.00 79.86  ? 90  ILE   D O     1 
ATOM   5031 C  CB    . ILE   C 2 90  ? 135.564 145.372 93.745  1.00 66.57  ? 90  ILE   D CB    1 
ATOM   5032 C  CG1   . ILE   C 2 90  ? 134.201 145.142 93.089  1.00 71.51  ? 90  ILE   D CG1   1 
ATOM   5033 C  CG2   . ILE   C 2 90  ? 136.010 144.136 94.511  1.00 69.04  ? 90  ILE   D CG2   1 
ATOM   5034 C  CD1   . ILE   C 2 90  ? 134.083 143.816 92.373  1.00 73.74  ? 90  ILE   D CD1   1 
ATOM   5035 N  N     . ALA   C 2 91  ? 137.706 147.502 95.210  1.00 69.63  ? 91  ALA   D N     1 
ATOM   5036 C  CA    . ALA   C 2 91  ? 138.825 148.430 95.117  1.00 69.70  ? 91  ALA   D CA    1 
ATOM   5037 C  C     . ALA   C 2 91  ? 140.132 147.657 94.974  1.00 74.44  ? 91  ALA   D C     1 
ATOM   5038 O  O     . ALA   C 2 91  ? 140.149 146.425 94.897  1.00 80.42  ? 91  ALA   D O     1 
ATOM   5039 C  CB    . ALA   C 2 91  ? 138.874 149.358 96.336  1.00 72.08  ? 91  ALA   D CB    1 
ATOM   5040 N  N     . ILE   C 2 92  ? 141.240 148.403 94.937  1.00 79.51  ? 92  ILE   D N     1 
ATOM   5041 C  CA    . ILE   C 2 92  ? 142.562 147.803 94.783  1.00 80.70  ? 92  ILE   D CA    1 
ATOM   5042 C  C     . ILE   C 2 92  ? 142.953 146.955 95.986  1.00 80.91  ? 92  ILE   D C     1 
ATOM   5043 O  O     . ILE   C 2 92  ? 143.779 146.044 95.853  1.00 81.63  ? 92  ILE   D O     1 
ATOM   5044 C  CB    . ILE   C 2 92  ? 143.613 148.898 94.514  1.00 81.88  ? 92  ILE   D CB    1 
ATOM   5045 C  CG1   . ILE   C 2 92  ? 144.866 148.303 93.866  1.00 81.14  ? 92  ILE   D CG1   1 
ATOM   5046 C  CG2   . ILE   C 2 92  ? 143.967 149.640 95.795  1.00 80.37  ? 92  ILE   D CG2   1 
ATOM   5047 C  CD1   . ILE   C 2 92  ? 144.600 147.531 92.603  1.00 76.14  ? 92  ILE   D CD1   1 
ATOM   5048 N  N     . SER   C 2 93  ? 142.381 147.222 97.160  1.00 85.99  ? 93  SER   D N     1 
ATOM   5049 C  CA    . SER   C 2 93  ? 142.645 146.431 98.365  1.00 87.96  ? 93  SER   D CA    1 
ATOM   5050 C  C     . SER   C 2 93  ? 141.317 146.294 99.107  1.00 86.95  ? 93  SER   D C     1 
ATOM   5051 O  O     . SER   C 2 93  ? 140.947 147.158 99.906  1.00 85.61  ? 93  SER   D O     1 
ATOM   5052 C  CB    . SER   C 2 93  ? 143.721 147.071 99.232  1.00 84.74  ? 93  SER   D CB    1 
ATOM   5053 O  OG    . SER   C 2 93  ? 145.004 146.907 98.653  1.00 80.99  ? 93  SER   D OG    1 
ATOM   5054 N  N     . ALA   C 2 94  ? 140.608 145.202 98.836  1.00 95.01  ? 94  ALA   D N     1 
ATOM   5055 C  CA    . ALA   C 2 94  ? 139.302 144.969 99.426  1.00 93.24  ? 94  ALA   D CA    1 
ATOM   5056 C  C     . ALA   C 2 94  ? 139.448 144.561 100.890 1.00 93.53  ? 94  ALA   D C     1 
ATOM   5057 O  O     . ALA   C 2 94  ? 140.547 144.515 101.448 1.00 93.88  ? 94  ALA   D O     1 
ATOM   5058 C  CB    . ALA   C 2 94  ? 138.544 143.910 98.630  1.00 91.25  ? 94  ALA   D CB    1 
ATOM   5059 N  N     . GLY   C 2 95  ? 138.319 144.255 101.521 1.00 95.28  ? 95  GLY   D N     1 
ATOM   5060 C  CA    . GLY   C 2 95  ? 138.334 143.865 102.915 1.00 95.07  ? 95  GLY   D CA    1 
ATOM   5061 C  C     . GLY   C 2 95  ? 138.603 142.388 103.099 1.00 95.88  ? 95  GLY   D C     1 
ATOM   5062 O  O     . GLY   C 2 95  ? 137.703 141.559 102.948 1.00 98.27  ? 95  GLY   D O     1 
ATOM   5063 N  N     . LEU   C 2 96  ? 139.847 142.050 103.428 1.00 74.67  ? 96  LEU   D N     1 
ATOM   5064 C  CA    . LEU   C 2 96  ? 140.251 140.668 103.658 1.00 70.73  ? 96  LEU   D CA    1 
ATOM   5065 C  C     . LEU   C 2 96  ? 141.283 140.659 104.771 1.00 75.83  ? 96  LEU   D C     1 
ATOM   5066 O  O     . LEU   C 2 96  ? 142.345 141.274 104.638 1.00 75.79  ? 96  LEU   D O     1 
ATOM   5067 C  CB    . LEU   C 2 96  ? 140.824 140.034 102.386 1.00 71.31  ? 96  LEU   D CB    1 
ATOM   5068 C  CG    . LEU   C 2 96  ? 139.847 139.666 101.268 1.00 72.64  ? 96  LEU   D CG    1 
ATOM   5069 C  CD1   . LEU   C 2 96  ? 140.588 139.049 100.097 1.00 71.05  ? 96  LEU   D CD1   1 
ATOM   5070 C  CD2   . LEU   C 2 96  ? 138.770 138.721 101.772 1.00 74.83  ? 96  LEU   D CD2   1 
ATOM   5071 N  N     . SER   C 2 97  ? 140.973 139.967 105.865 1.00 83.49  ? 97  SER   D N     1 
ATOM   5072 C  CA    . SER   C 2 97  ? 141.891 139.883 106.991 1.00 82.50  ? 97  SER   D CA    1 
ATOM   5073 C  C     . SER   C 2 97  ? 143.038 138.938 106.659 1.00 81.90  ? 97  SER   D C     1 
ATOM   5074 O  O     . SER   C 2 97  ? 142.814 137.817 106.192 1.00 83.63  ? 97  SER   D O     1 
ATOM   5075 C  CB    . SER   C 2 97  ? 141.156 139.411 108.243 1.00 83.43  ? 97  SER   D CB    1 
ATOM   5076 O  OG    . SER   C 2 97  ? 140.172 140.350 108.638 1.00 84.11  ? 97  SER   D OG    1 
ATOM   5077 N  N     . GLY   C 2 98  ? 144.267 139.396 106.894 1.00 79.39  ? 98  GLY   D N     1 
ATOM   5078 C  CA    . GLY   C 2 98  ? 145.426 138.570 106.604 1.00 78.98  ? 98  GLY   D CA    1 
ATOM   5079 C  C     . GLY   C 2 98  ? 145.533 137.349 107.493 1.00 82.29  ? 98  GLY   D C     1 
ATOM   5080 O  O     . GLY   C 2 98  ? 145.929 136.275 107.032 1.00 85.39  ? 98  GLY   D O     1 
ATOM   5081 N  N     . GLN   C 2 99  ? 145.189 137.492 108.775 1.00 89.91  ? 99  GLN   D N     1 
ATOM   5082 C  CA    . GLN   C 2 99  ? 145.281 136.364 109.697 1.00 89.94  ? 99  GLN   D CA    1 
ATOM   5083 C  C     . GLN   C 2 99  ? 144.230 135.304 109.396 1.00 85.77  ? 99  GLN   D C     1 
ATOM   5084 O  O     . GLN   C 2 99  ? 144.501 134.107 109.543 1.00 84.87  ? 99  GLN   D O     1 
ATOM   5085 C  CB    . GLN   C 2 99  ? 145.141 136.854 111.137 1.00 89.28  ? 99  GLN   D CB    1 
ATOM   5086 C  CG    . GLN   C 2 99  ? 145.635 138.273 111.359 1.00 87.10  ? 99  GLN   D CG    1 
ATOM   5087 C  CD    . GLN   C 2 99  ? 144.501 139.275 111.447 1.00 88.97  ? 99  GLN   D CD    1 
ATOM   5088 O  OE1   . GLN   C 2 99  ? 143.439 138.982 111.995 1.00 88.73  ? 99  GLN   D OE1   1 
ATOM   5089 N  NE2   . GLN   C 2 99  ? 144.722 140.468 110.906 1.00 87.74  ? 99  GLN   D NE2   1 
ATOM   5090 N  N     . LEU   C 2 100 ? 143.038 135.717 108.981 1.00 82.02  ? 100 LEU   D N     1 
ATOM   5091 C  CA    . LEU   C 2 100 ? 141.963 134.778 108.708 1.00 84.96  ? 100 LEU   D CA    1 
ATOM   5092 C  C     . LEU   C 2 100 ? 142.237 133.999 107.425 1.00 86.54  ? 100 LEU   D C     1 
ATOM   5093 O  O     . LEU   C 2 100 ? 143.007 134.422 106.558 1.00 86.65  ? 100 LEU   D O     1 
ATOM   5094 C  CB    . LEU   C 2 100 ? 140.627 135.513 108.596 1.00 84.52  ? 100 LEU   D CB    1 
ATOM   5095 C  CG    . LEU   C 2 100 ? 139.840 135.760 109.883 1.00 83.39  ? 100 LEU   D CG    1 
ATOM   5096 C  CD1   . LEU   C 2 100 ? 140.548 136.761 110.779 1.00 80.77  ? 100 LEU   D CD1   1 
ATOM   5097 C  CD2   . LEU   C 2 100 ? 138.444 136.245 109.548 1.00 83.03  ? 100 LEU   D CD2   1 
ATOM   5098 N  N     . THR   C 2 101 ? 141.594 132.841 107.313 1.00 90.39  ? 101 THR   D N     1 
ATOM   5099 C  CA    . THR   C 2 101 ? 141.689 132.022 106.116 1.00 90.05  ? 101 THR   D CA    1 
ATOM   5100 C  C     . THR   C 2 101 ? 140.594 132.437 105.133 1.00 91.56  ? 101 THR   D C     1 
ATOM   5101 O  O     . THR   C 2 101 ? 139.845 133.387 105.372 1.00 92.84  ? 101 THR   D O     1 
ATOM   5102 C  CB    . THR   C 2 101 ? 141.603 130.540 106.475 1.00 88.26  ? 101 THR   D CB    1 
ATOM   5103 O  OG1   . THR   C 2 101 ? 141.849 129.752 105.305 1.00 88.97  ? 101 THR   D OG1   1 
ATOM   5104 C  CG2   . THR   C 2 101 ? 140.228 130.205 107.017 1.00 88.87  ? 101 THR   D CG2   1 
ATOM   5105 N  N     . GLY   C 2 102 ? 140.497 131.730 104.007 1.00 76.68  ? 102 GLY   D N     1 
ATOM   5106 C  CA    . GLY   C 2 102 ? 139.506 132.086 103.007 1.00 71.15  ? 102 GLY   D CA    1 
ATOM   5107 C  C     . GLY   C 2 102 ? 138.080 131.876 103.479 1.00 77.19  ? 102 GLY   D C     1 
ATOM   5108 O  O     . GLY   C 2 102 ? 137.212 132.724 103.255 1.00 75.74  ? 102 GLY   D O     1 
ATOM   5109 N  N     . ILE   C 2 103 ? 137.818 130.748 104.143 1.00 88.30  ? 103 ILE   D N     1 
ATOM   5110 C  CA    . ILE   C 2 103 ? 136.457 130.432 104.570 1.00 88.36  ? 103 ILE   D CA    1 
ATOM   5111 C  C     . ILE   C 2 103 ? 135.998 131.390 105.663 1.00 88.84  ? 103 ILE   D C     1 
ATOM   5112 O  O     . ILE   C 2 103 ? 134.850 131.855 105.659 1.00 90.55  ? 103 ILE   D O     1 
ATOM   5113 C  CB    . ILE   C 2 103 ? 136.371 128.964 105.025 1.00 89.04  ? 103 ILE   D CB    1 
ATOM   5114 C  CG1   . ILE   C 2 103 ? 136.843 128.031 103.905 1.00 85.05  ? 103 ILE   D CG1   1 
ATOM   5115 C  CG2   . ILE   C 2 103 ? 134.955 128.627 105.473 1.00 89.63  ? 103 ILE   D CG2   1 
ATOM   5116 C  CD1   . ILE   C 2 103 ? 135.724 127.451 103.062 1.00 86.15  ? 103 ILE   D CD1   1 
ATOM   5117 N  N     . GLU   C 2 104 ? 136.879 131.689 106.622 1.00 88.38  ? 104 GLU   D N     1 
ATOM   5118 C  CA    . GLU   C 2 104 ? 136.529 132.646 107.666 1.00 89.48  ? 104 GLU   D CA    1 
ATOM   5119 C  C     . GLU   C 2 104 ? 136.272 134.028 107.081 1.00 91.84  ? 104 GLU   D C     1 
ATOM   5120 O  O     . GLU   C 2 104 ? 135.341 134.724 107.500 1.00 91.43  ? 104 GLU   D O     1 
ATOM   5121 C  CB    . GLU   C 2 104 ? 137.631 132.705 108.724 1.00 91.28  ? 104 GLU   D CB    1 
ATOM   5122 C  CG    . GLU   C 2 104 ? 137.550 131.596 109.762 1.00 93.27  ? 104 GLU   D CG    1 
ATOM   5123 C  CD    . GLU   C 2 104 ? 138.898 130.978 110.067 1.00 93.36  ? 104 GLU   D CD    1 
ATOM   5124 O  OE1   . GLU   C 2 104 ? 139.855 131.736 110.332 1.00 93.61  ? 104 GLU   D OE1   1 
ATOM   5125 O  OE2   . GLU   C 2 104 ? 139.002 129.734 110.044 1.00 91.57  ? 104 GLU   D OE2   1 
ATOM   5126 N  N     . ASN   C 2 105 ? 137.083 134.439 106.104 1.00 88.29  ? 105 ASN   D N     1 
ATOM   5127 C  CA    . ASN   C 2 105 ? 136.846 135.717 105.443 1.00 84.62  ? 105 ASN   D CA    1 
ATOM   5128 C  C     . ASN   C 2 105 ? 135.504 135.724 104.725 1.00 82.86  ? 105 ASN   D C     1 
ATOM   5129 O  O     . ASN   C 2 105 ? 134.761 136.711 104.796 1.00 87.34  ? 105 ASN   D O     1 
ATOM   5130 C  CB    . ASN   C 2 105 ? 137.982 136.022 104.469 1.00 78.79  ? 105 ASN   D CB    1 
ATOM   5131 C  CG    . ASN   C 2 105 ? 138.905 137.107 104.975 1.00 81.70  ? 105 ASN   D CG    1 
ATOM   5132 O  OD1   . ASN   C 2 105 ? 138.468 138.219 105.269 1.00 85.57  ? 105 ASN   D OD1   1 
ATOM   5133 N  ND2   . ASN   C 2 105 ? 140.188 136.790 105.082 1.00 78.45  ? 105 ASN   D ND2   1 
ATOM   5134 N  N     . ILE   C 2 106 ? 135.173 134.630 104.036 1.00 77.90  ? 106 ILE   D N     1 
ATOM   5135 C  CA    . ILE   C 2 106 ? 133.900 134.555 103.323 1.00 81.66  ? 106 ILE   D CA    1 
ATOM   5136 C  C     . ILE   C 2 106 ? 132.738 134.688 104.297 1.00 84.31  ? 106 ILE   D C     1 
ATOM   5137 O  O     . ILE   C 2 106 ? 131.802 135.466 104.072 1.00 82.34  ? 106 ILE   D O     1 
ATOM   5138 C  CB    . ILE   C 2 106 ? 133.807 133.247 102.518 1.00 81.90  ? 106 ILE   D CB    1 
ATOM   5139 C  CG1   . ILE   C 2 106 ? 134.762 133.275 101.326 1.00 83.54  ? 106 ILE   D CG1   1 
ATOM   5140 C  CG2   . ILE   C 2 106 ? 132.383 133.010 102.045 1.00 76.96  ? 106 ILE   D CG2   1 
ATOM   5141 C  CD1   . ILE   C 2 106 ? 134.962 131.923 100.682 1.00 79.50  ? 106 ILE   D CD1   1 
ATOM   5142 N  N     . GLU   C 2 107 ? 132.781 133.934 105.400 1.00 95.66  ? 107 GLU   D N     1 
ATOM   5143 C  CA    . GLU   C 2 107 ? 131.663 133.979 106.337 1.00 94.73  ? 107 GLU   D CA    1 
ATOM   5144 C  C     . GLU   C 2 107 ? 131.574 135.333 107.031 1.00 95.57  ? 107 GLU   D C     1 
ATOM   5145 O  O     . GLU   C 2 107 ? 130.467 135.829 107.262 1.00 94.44  ? 107 GLU   D O     1 
ATOM   5146 C  CB    . GLU   C 2 107 ? 131.755 132.841 107.358 1.00 91.84  ? 107 GLU   D CB    1 
ATOM   5147 C  CG    . GLU   C 2 107 ? 133.018 132.804 108.189 1.00 93.94  ? 107 GLU   D CG    1 
ATOM   5148 C  CD    . GLU   C 2 107 ? 132.953 131.772 109.300 1.00 98.66  ? 107 GLU   D CD    1 
ATOM   5149 O  OE1   . GLU   C 2 107 ? 132.288 132.036 110.322 1.00 99.82  ? 107 GLU   D OE1   1 
ATOM   5150 O  OE2   . GLU   C 2 107 ? 133.570 130.696 109.151 1.00 97.71  ? 107 GLU   D OE2   1 
ATOM   5151 N  N     . PHE   C 2 108 ? 132.712 135.961 107.336 1.00 86.85  ? 108 PHE   D N     1 
ATOM   5152 C  CA    . PHE   C 2 108 ? 132.695 137.315 107.883 1.00 81.33  ? 108 PHE   D CA    1 
ATOM   5153 C  C     . PHE   C 2 108 ? 132.010 138.281 106.920 1.00 85.51  ? 108 PHE   D C     1 
ATOM   5154 O  O     . PHE   C 2 108 ? 131.104 139.032 107.310 1.00 86.64  ? 108 PHE   D O     1 
ATOM   5155 C  CB    . PHE   C 2 108 ? 134.132 137.763 108.175 1.00 79.72  ? 108 PHE   D CB    1 
ATOM   5156 C  CG    . PHE   C 2 108 ? 134.249 138.911 109.150 1.00 86.49  ? 108 PHE   D CG    1 
ATOM   5157 C  CD1   . PHE   C 2 108 ? 135.426 139.100 109.857 1.00 89.46  ? 108 PHE   D CD1   1 
ATOM   5158 C  CD2   . PHE   C 2 108 ? 133.202 139.789 109.369 1.00 85.52  ? 108 PHE   D CD2   1 
ATOM   5159 C  CE1   . PHE   C 2 108 ? 135.556 140.143 110.753 1.00 88.15  ? 108 PHE   D CE1   1 
ATOM   5160 C  CE2   . PHE   C 2 108 ? 133.327 140.833 110.264 1.00 85.73  ? 108 PHE   D CE2   1 
ATOM   5161 C  CZ    . PHE   C 2 108 ? 134.505 141.009 110.957 1.00 88.22  ? 108 PHE   D CZ    1 
ATOM   5162 N  N     . LYS   C 2 109 ? 132.424 138.268 105.649 1.00 100.59 ? 109 LYS   D N     1 
ATOM   5163 C  CA    . LYS   C 2 109 ? 131.872 139.213 104.683 1.00 97.45  ? 109 LYS   D CA    1 
ATOM   5164 C  C     . LYS   C 2 109 ? 130.379 138.993 104.473 1.00 99.50  ? 109 LYS   D C     1 
ATOM   5165 O  O     . LYS   C 2 109 ? 129.606 139.957 104.431 1.00 97.85  ? 109 LYS   D O     1 
ATOM   5166 C  CB    . LYS   C 2 109 ? 132.623 139.119 103.354 1.00 99.86  ? 109 LYS   D CB    1 
ATOM   5167 C  CG    . LYS   C 2 109 ? 134.111 139.395 103.457 1.00 99.67  ? 109 LYS   D CG    1 
ATOM   5168 C  CD    . LYS   C 2 109 ? 134.391 140.886 103.506 1.00 100.01 ? 109 LYS   D CD    1 
ATOM   5169 C  CE    . LYS   C 2 109 ? 134.563 141.457 102.110 1.00 99.59  ? 109 LYS   D CE    1 
ATOM   5170 N  NZ    . LYS   C 2 109 ? 135.655 140.770 101.368 1.00 98.35  ? 109 LYS   D NZ    1 
ATOM   5171 N  N     . MET   C 2 110 ? 129.944 137.739 104.346 1.00 107.55 ? 110 MET   D N     1 
ATOM   5172 C  CA    . MET   C 2 110 ? 128.518 137.502 104.153 1.00 107.77 ? 110 MET   D CA    1 
ATOM   5173 C  C     . MET   C 2 110 ? 127.701 137.657 105.431 1.00 107.43 ? 110 MET   D C     1 
ATOM   5174 O  O     . MET   C 2 110 ? 126.477 137.798 105.343 1.00 108.47 ? 110 MET   D O     1 
ATOM   5175 C  CB    . MET   C 2 110 ? 128.264 136.122 103.538 1.00 108.91 ? 110 MET   D CB    1 
ATOM   5176 C  CG    . MET   C 2 110 ? 129.281 135.692 102.501 1.00 107.63 ? 110 MET   D CG    1 
ATOM   5177 S  SD    . MET   C 2 110 ? 128.722 134.300 101.500 1.00 111.13 ? 110 MET   D SD    1 
ATOM   5178 C  CE    . MET   C 2 110 ? 126.959 134.609 101.435 1.00 110.72 ? 110 MET   D CE    1 
ATOM   5179 N  N     . LEU   C 2 111 ? 128.331 137.639 106.607 1.00 94.97  ? 111 LEU   D N     1 
ATOM   5180 C  CA    . LEU   C 2 111 ? 127.633 138.007 107.830 1.00 95.08  ? 111 LEU   D CA    1 
ATOM   5181 C  C     . LEU   C 2 111 ? 127.456 139.511 107.959 1.00 92.70  ? 111 LEU   D C     1 
ATOM   5182 O  O     . LEU   C 2 111 ? 126.423 139.964 108.462 1.00 91.51  ? 111 LEU   D O     1 
ATOM   5183 C  CB    . LEU   C 2 111 ? 128.382 137.477 109.055 1.00 92.56  ? 111 LEU   D CB    1 
ATOM   5184 C  CG    . LEU   C 2 111 ? 128.084 136.036 109.472 1.00 93.91  ? 111 LEU   D CG    1 
ATOM   5185 C  CD1   . LEU   C 2 111 ? 128.866 135.669 110.726 1.00 91.92  ? 111 LEU   D CD1   1 
ATOM   5186 C  CD2   . LEU   C 2 111 ? 126.593 135.832 109.682 1.00 91.95  ? 111 LEU   D CD2   1 
ATOM   5187 N  N     . CYS   C 2 112 ? 128.446 140.291 107.518 1.00 89.19  ? 112 CYS   D N     1 
ATOM   5188 C  CA    . CYS   C 2 112 ? 128.305 141.744 107.558 1.00 86.33  ? 112 CYS   D CA    1 
ATOM   5189 C  C     . CYS   C 2 112 ? 127.198 142.231 106.631 1.00 89.35  ? 112 CYS   D C     1 
ATOM   5190 O  O     . CYS   C 2 112 ? 126.535 143.229 106.934 1.00 87.44  ? 112 CYS   D O     1 
ATOM   5191 C  CB    . CYS   C 2 112 ? 129.632 142.412 107.202 1.00 90.89  ? 112 CYS   D CB    1 
ATOM   5192 S  SG    . CYS   C 2 112 ? 130.766 142.605 108.594 1.00 91.54  ? 112 CYS   D SG    1 
ATOM   5193 N  N     . MET   C 2 113 ? 126.986 141.552 105.502 1.00 107.59 ? 113 MET   D N     1 
ATOM   5194 C  CA    . MET   C 2 113 ? 125.929 141.935 104.574 1.00 108.93 ? 113 MET   D CA    1 
ATOM   5195 C  C     . MET   C 2 113 ? 124.547 141.470 105.014 1.00 109.23 ? 113 MET   D C     1 
ATOM   5196 O  O     . MET   C 2 113 ? 123.550 141.955 104.469 1.00 108.69 ? 113 MET   D O     1 
ATOM   5197 C  CB    . MET   C 2 113 ? 126.228 141.391 103.174 1.00 107.26 ? 113 MET   D CB    1 
ATOM   5198 C  CG    . MET   C 2 113 ? 127.637 141.666 102.682 1.00 107.36 ? 113 MET   D CG    1 
ATOM   5199 S  SD    . MET   C 2 113 ? 127.682 142.177 100.953 1.00 113.95 ? 113 MET   D SD    1 
ATOM   5200 C  CE    . MET   C 2 113 ? 129.324 141.640 100.485 1.00 108.14 ? 113 MET   D CE    1 
ATOM   5201 N  N     . GLY   C 2 114 ? 124.459 140.555 105.975 1.00 102.36 ? 114 GLY   D N     1 
ATOM   5202 C  CA    . GLY   C 2 114 ? 123.169 140.136 106.489 1.00 102.46 ? 114 GLY   D CA    1 
ATOM   5203 C  C     . GLY   C 2 114 ? 122.603 138.884 105.851 1.00 101.84 ? 114 GLY   D C     1 
ATOM   5204 O  O     . GLY   C 2 114 ? 121.457 138.879 105.391 1.00 101.54 ? 114 GLY   D O     1 
ATOM   5205 N  N     . PHE   C 2 115 ? 123.394 137.816 105.812 1.00 119.91 ? 115 PHE   D N     1 
ATOM   5206 C  CA    . PHE   C 2 115 ? 122.948 136.520 105.321 1.00 123.07 ? 115 PHE   D CA    1 
ATOM   5207 C  C     . PHE   C 2 115 ? 122.965 135.505 106.455 1.00 122.30 ? 115 PHE   D C     1 
ATOM   5208 O  O     . PHE   C 2 115 ? 123.880 135.501 107.283 1.00 120.20 ? 115 PHE   D O     1 
ATOM   5209 C  CB    . PHE   C 2 115 ? 123.828 136.024 104.169 1.00 122.11 ? 115 PHE   D CB    1 
ATOM   5210 C  CG    . PHE   C 2 115 ? 123.779 136.895 102.946 1.00 122.17 ? 115 PHE   D CG    1 
ATOM   5211 C  CD1   . PHE   C 2 115 ? 122.693 136.844 102.088 1.00 122.32 ? 115 PHE   D CD1   1 
ATOM   5212 C  CD2   . PHE   C 2 115 ? 124.823 137.754 102.647 1.00 122.55 ? 115 PHE   D CD2   1 
ATOM   5213 C  CE1   . PHE   C 2 115 ? 122.646 137.639 100.960 1.00 122.80 ? 115 PHE   D CE1   1 
ATOM   5214 C  CE2   . PHE   C 2 115 ? 124.781 138.551 101.519 1.00 123.01 ? 115 PHE   D CE2   1 
ATOM   5215 C  CZ    . PHE   C 2 115 ? 123.691 138.494 100.676 1.00 122.14 ? 115 PHE   D CZ    1 
ATOM   5216 N  N     . LYS   C 2 116 ? 121.948 134.647 106.489 1.00 120.98 ? 116 LYS   D N     1 
ATOM   5217 C  CA    . LYS   C 2 116 ? 121.892 133.597 107.492 1.00 119.63 ? 116 LYS   D CA    1 
ATOM   5218 C  C     . LYS   C 2 116 ? 122.942 132.528 107.202 1.00 120.13 ? 116 LYS   D C     1 
ATOM   5219 O  O     . LYS   C 2 116 ? 123.454 132.407 106.085 1.00 121.81 ? 116 LYS   D O     1 
ATOM   5220 C  CB    . LYS   C 2 116 ? 120.497 132.975 107.545 1.00 119.19 ? 116 LYS   D CB    1 
ATOM   5221 C  CG    . LYS   C 2 116 ? 119.377 133.981 107.773 1.00 120.36 ? 116 LYS   D CG    1 
ATOM   5222 C  CD    . LYS   C 2 116 ? 119.687 134.910 108.939 1.00 118.88 ? 116 LYS   D CD    1 
ATOM   5223 C  CE    . LYS   C 2 116 ? 119.548 134.198 110.275 1.00 118.19 ? 116 LYS   D CE    1 
ATOM   5224 N  NZ    . LYS   C 2 116 ? 118.133 133.843 110.576 1.00 119.86 ? 116 LYS   D NZ    1 
ATOM   5225 N  N     . ARG   C 2 117 ? 123.261 131.743 108.235 1.00 115.16 ? 117 ARG   D N     1 
ATOM   5226 C  CA    . ARG   C 2 117 ? 124.351 130.776 108.129 1.00 115.11 ? 117 ARG   D CA    1 
ATOM   5227 C  C     . ARG   C 2 117 ? 124.069 129.706 107.080 1.00 114.82 ? 117 ARG   D C     1 
ATOM   5228 O  O     . ARG   C 2 117 ? 124.987 129.294 106.359 1.00 113.94 ? 117 ARG   D O     1 
ATOM   5229 C  CB    . ARG   C 2 117 ? 124.611 130.133 109.490 1.00 116.38 ? 117 ARG   D CB    1 
ATOM   5230 C  CG    . ARG   C 2 117 ? 126.006 129.550 109.640 1.00 117.07 ? 117 ARG   D CG    1 
ATOM   5231 C  CD    . ARG   C 2 117 ? 126.144 128.778 110.940 1.00 116.32 ? 117 ARG   D CD    1 
ATOM   5232 N  NE    . ARG   C 2 117 ? 127.523 128.756 111.414 1.00 116.78 ? 117 ARG   D NE    1 
ATOM   5233 C  CZ    . ARG   C 2 117 ? 127.926 129.272 112.567 1.00 117.47 ? 117 ARG   D CZ    1 
ATOM   5234 N  NH1   . ARG   C 2 117 ? 127.080 129.864 113.394 1.00 117.22 ? 117 ARG   D NH1   1 
ATOM   5235 N  NH2   . ARG   C 2 117 ? 129.212 129.193 112.899 1.00 115.60 ? 117 ARG   D NH2   1 
ATOM   5236 N  N     . LYS   C 2 118 ? 122.822 129.237 106.985 1.00 115.99 ? 118 LYS   D N     1 
ATOM   5237 C  CA    . LYS   C 2 118 ? 122.486 128.247 105.967 1.00 116.77 ? 118 LYS   D CA    1 
ATOM   5238 C  C     . LYS   C 2 118 ? 122.673 128.813 104.564 1.00 117.34 ? 118 LYS   D C     1 
ATOM   5239 O  O     . LYS   C 2 118 ? 123.177 128.120 103.672 1.00 117.26 ? 118 LYS   D O     1 
ATOM   5240 C  CB    . LYS   C 2 118 ? 121.054 127.754 106.162 1.00 117.90 ? 118 LYS   D CB    1 
ATOM   5241 C  CG    . LYS   C 2 118 ? 120.736 126.474 105.406 1.00 118.23 ? 118 LYS   D CG    1 
ATOM   5242 C  CD    . LYS   C 2 118 ? 121.346 125.259 106.088 1.00 117.95 ? 118 LYS   D CD    1 
ATOM   5243 C  CE    . LYS   C 2 118 ? 120.822 125.095 107.505 1.00 117.62 ? 118 LYS   D CE    1 
ATOM   5244 N  NZ    . LYS   C 2 118 ? 121.909 124.759 108.465 1.00 116.48 ? 118 LYS   D NZ    1 
ATOM   5245 N  N     . GLU   C 2 119 ? 122.278 130.071 104.350 1.00 116.42 ? 119 GLU   D N     1 
ATOM   5246 C  CA    . GLU   C 2 119 ? 122.511 130.707 103.057 1.00 115.79 ? 119 GLU   D CA    1 
ATOM   5247 C  C     . GLU   C 2 119 ? 124.001 130.830 102.765 1.00 113.84 ? 119 GLU   D C     1 
ATOM   5248 O  O     . GLU   C 2 119 ? 124.431 130.648 101.621 1.00 115.62 ? 119 GLU   D O     1 
ATOM   5249 C  CB    . GLU   C 2 119 ? 121.841 132.080 103.013 1.00 115.40 ? 119 GLU   D CB    1 
ATOM   5250 C  CG    . GLU   C 2 119 ? 120.399 132.089 103.494 1.00 115.87 ? 119 GLU   D CG    1 
ATOM   5251 C  CD    . GLU   C 2 119 ? 119.615 133.268 102.951 1.00 117.27 ? 119 GLU   D CD    1 
ATOM   5252 O  OE1   . GLU   C 2 119 ? 119.327 133.282 101.736 1.00 114.91 ? 119 GLU   D OE1   1 
ATOM   5253 O  OE2   . GLU   C 2 119 ? 119.287 134.181 103.738 1.00 117.64 ? 119 GLU   D OE2   1 
ATOM   5254 N  N     . ILE   C 2 120 ? 124.802 131.143 103.787 1.00 106.21 ? 120 ILE   D N     1 
ATOM   5255 C  CA    . ILE   C 2 120 ? 126.248 131.236 103.601 1.00 106.33 ? 120 ILE   D CA    1 
ATOM   5256 C  C     . ILE   C 2 120 ? 126.820 129.889 103.180 1.00 106.31 ? 120 ILE   D C     1 
ATOM   5257 O  O     . ILE   C 2 120 ? 127.636 129.806 102.253 1.00 105.97 ? 120 ILE   D O     1 
ATOM   5258 C  CB    . ILE   C 2 120 ? 126.915 131.757 104.888 1.00 105.93 ? 120 ILE   D CB    1 
ATOM   5259 C  CG1   . ILE   C 2 120 ? 126.478 133.195 105.173 1.00 107.27 ? 120 ILE   D CG1   1 
ATOM   5260 C  CG2   . ILE   C 2 120 ? 128.429 131.662 104.782 1.00 104.49 ? 120 ILE   D CG2   1 
ATOM   5261 C  CD1   . ILE   C 2 120 ? 127.245 133.855 106.296 1.00 106.77 ? 120 ILE   D CD1   1 
ATOM   5262 N  N     . LYS   C 2 121 ? 126.398 128.813 103.850 1.00 100.95 ? 121 LYS   D N     1 
ATOM   5263 C  CA    . LYS   C 2 121 ? 126.903 127.488 103.504 1.00 100.63 ? 121 LYS   D CA    1 
ATOM   5264 C  C     . LYS   C 2 121 ? 126.422 127.042 102.130 1.00 98.80  ? 121 LYS   D C     1 
ATOM   5265 O  O     . LYS   C 2 121 ? 127.134 126.308 101.435 1.00 96.67  ? 121 LYS   D O     1 
ATOM   5266 C  CB    . LYS   C 2 121 ? 126.490 126.471 104.567 1.00 100.31 ? 121 LYS   D CB    1 
ATOM   5267 C  CG    . LYS   C 2 121 ? 127.532 125.396 104.828 1.00 99.25  ? 121 LYS   D CG    1 
ATOM   5268 C  CD    . LYS   C 2 121 ? 127.342 124.760 106.193 1.00 98.33  ? 121 LYS   D CD    1 
ATOM   5269 C  CE    . LYS   C 2 121 ? 126.120 123.858 106.214 1.00 99.55  ? 121 LYS   D CE    1 
ATOM   5270 N  NZ    . LYS   C 2 121 ? 126.000 123.058 104.964 1.00 98.68  ? 121 LYS   D NZ    1 
ATOM   5271 N  N     . ALA   C 2 122 ? 125.224 127.465 101.723 1.00 99.44  ? 122 ALA   D N     1 
ATOM   5272 C  CA    . ALA   C 2 122 ? 124.730 127.125 100.394 1.00 100.81 ? 122 ALA   D CA    1 
ATOM   5273 C  C     . ALA   C 2 122 ? 125.468 127.892 99.303  1.00 103.22 ? 122 ALA   D C     1 
ATOM   5274 O  O     . ALA   C 2 122 ? 125.714 127.352 98.219  1.00 101.82 ? 122 ALA   D O     1 
ATOM   5275 C  CB    . ALA   C 2 122 ? 123.227 127.392 100.308 1.00 97.90  ? 122 ALA   D CB    1 
ATOM   5276 N  N     . MET   C 2 123 ? 125.819 129.152 99.566  1.00 109.04 ? 123 MET   D N     1 
ATOM   5277 C  CA    . MET   C 2 123 ? 126.489 129.990 98.581  1.00 103.80 ? 123 MET   D CA    1 
ATOM   5278 C  C     . MET   C 2 123 ? 128.000 129.799 98.548  1.00 102.51 ? 123 MET   D C     1 
ATOM   5279 O  O     . MET   C 2 123 ? 128.640 130.246 97.592  1.00 107.32 ? 123 MET   D O     1 
ATOM   5280 C  CB    . MET   C 2 123 ? 126.176 131.467 98.848  1.00 104.16 ? 123 MET   D CB    1 
ATOM   5281 C  CG    . MET   C 2 123 ? 125.089 132.046 97.960  1.00 105.13 ? 123 MET   D CG    1 
ATOM   5282 S  SD    . MET   C 2 123 ? 125.118 133.848 97.927  1.00 110.51 ? 123 MET   D SD    1 
ATOM   5283 C  CE    . MET   C 2 123 ? 123.366 134.217 97.923  1.00 105.72 ? 123 MET   D CE    1 
ATOM   5284 N  N     . THR   C 2 124 ? 128.582 129.162 99.564  1.00 85.33  ? 124 THR   D N     1 
ATOM   5285 C  CA    . THR   C 2 124 ? 130.030 128.955 99.574  1.00 88.03  ? 124 THR   D CA    1 
ATOM   5286 C  C     . THR   C 2 124 ? 130.549 128.158 98.380  1.00 90.63  ? 124 THR   D C     1 
ATOM   5287 O  O     . THR   C 2 124 ? 131.569 128.569 97.798  1.00 90.39  ? 124 THR   D O     1 
ATOM   5288 C  CB    . THR   C 2 124 ? 130.445 128.297 100.895 1.00 88.87  ? 124 THR   D CB    1 
ATOM   5289 O  OG1   . THR   C 2 124 ? 129.817 128.977 101.987 1.00 89.57  ? 124 THR   D OG1   1 
ATOM   5290 C  CG2   . THR   C 2 124 ? 131.952 128.362 101.068 1.00 89.42  ? 124 THR   D CG2   1 
ATOM   5291 N  N     . PRO   C 2 125 ? 129.942 127.033 97.970  1.00 105.33 ? 125 PRO   D N     1 
ATOM   5292 C  CA    . PRO   C 2 125 ? 130.528 126.269 96.853  1.00 105.50 ? 125 PRO   D CA    1 
ATOM   5293 C  C     . PRO   C 2 125 ? 130.626 127.048 95.553  1.00 104.96 ? 125 PRO   D C     1 
ATOM   5294 O  O     . PRO   C 2 125 ? 131.574 126.826 94.790  1.00 103.59 ? 125 PRO   D O     1 
ATOM   5295 C  CB    . PRO   C 2 125 ? 129.584 125.064 96.722  1.00 106.00 ? 125 PRO   D CB    1 
ATOM   5296 C  CG    . PRO   C 2 125 ? 128.308 125.523 97.332  1.00 104.92 ? 125 PRO   D CG    1 
ATOM   5297 C  CD    . PRO   C 2 125 ? 128.745 126.353 98.495  1.00 104.58 ? 125 PRO   D CD    1 
ATOM   5298 N  N     . LYS   C 2 126 ? 129.682 127.948 95.269  1.00 90.30  ? 126 LYS   D N     1 
ATOM   5299 C  CA    . LYS   C 2 126 ? 129.792 128.772 94.069  1.00 89.95  ? 126 LYS   D CA    1 
ATOM   5300 C  C     . LYS   C 2 126 ? 131.021 129.670 94.128  1.00 91.90  ? 126 LYS   D C     1 
ATOM   5301 O  O     . LYS   C 2 126 ? 131.747 129.809 93.134  1.00 93.42  ? 126 LYS   D O     1 
ATOM   5302 C  CB    . LYS   C 2 126 ? 128.524 129.603 93.886  1.00 90.74  ? 126 LYS   D CB    1 
ATOM   5303 C  CG    . LYS   C 2 126 ? 127.457 128.927 93.042  1.00 94.59  ? 126 LYS   D CG    1 
ATOM   5304 C  CD    . LYS   C 2 126 ? 126.237 129.816 92.879  1.00 94.62  ? 126 LYS   D CD    1 
ATOM   5305 C  CE    . LYS   C 2 126 ? 125.451 129.919 94.176  1.00 94.40  ? 126 LYS   D CE    1 
ATOM   5306 N  NZ    . LYS   C 2 126 ? 125.260 128.589 94.815  1.00 96.57  ? 126 LYS   D NZ    1 
ATOM   5307 N  N     . ILE   C 2 127 ? 131.275 130.276 95.289  1.00 73.21  ? 127 ILE   D N     1 
ATOM   5308 C  CA    . ILE   C 2 127 ? 132.473 131.089 95.471  1.00 67.36  ? 127 ILE   D CA    1 
ATOM   5309 C  C     . ILE   C 2 127 ? 133.725 130.237 95.309  1.00 68.32  ? 127 ILE   D C     1 
ATOM   5310 O  O     . ILE   C 2 127 ? 134.701 130.654 94.672  1.00 72.46  ? 127 ILE   D O     1 
ATOM   5311 C  CB    . ILE   C 2 127 ? 132.433 131.787 96.842  1.00 67.63  ? 127 ILE   D CB    1 
ATOM   5312 C  CG1   . ILE   C 2 127 ? 131.383 132.898 96.846  1.00 66.36  ? 127 ILE   D CG1   1 
ATOM   5313 C  CG2   . ILE   C 2 127 ? 133.798 132.339 97.208  1.00 69.53  ? 127 ILE   D CG2   1 
ATOM   5314 C  CD1   . ILE   C 2 127 ? 130.823 133.206 98.211  1.00 67.07  ? 127 ILE   D CD1   1 
ATOM   5315 N  N     . ILE   C 2 128 ? 133.714 129.029 95.877  1.00 79.91  ? 128 ILE   D N     1 
ATOM   5316 C  CA    . ILE   C 2 128 ? 134.871 128.141 95.772  1.00 82.18  ? 128 ILE   D CA    1 
ATOM   5317 C  C     . ILE   C 2 128 ? 135.154 127.803 94.315  1.00 84.93  ? 128 ILE   D C     1 
ATOM   5318 O  O     . ILE   C 2 128 ? 136.308 127.814 93.870  1.00 84.49  ? 128 ILE   D O     1 
ATOM   5319 C  CB    . ILE   C 2 128 ? 134.643 126.869 96.609  1.00 86.23  ? 128 ILE   D CB    1 
ATOM   5320 C  CG1   . ILE   C 2 128 ? 134.404 127.224 98.079  1.00 84.54  ? 128 ILE   D CG1   1 
ATOM   5321 C  CG2   . ILE   C 2 128 ? 135.817 125.908 96.455  1.00 86.70  ? 128 ILE   D CG2   1 
ATOM   5322 C  CD1   . ILE   C 2 128 ? 135.645 127.210 98.932  1.00 83.62  ? 128 ILE   D CD1   1 
ATOM   5323 N  N     . GLU   C 2 129 ? 134.106 127.495 93.548  1.00 97.13  ? 129 GLU   D N     1 
ATOM   5324 C  CA    . GLU   C 2 129 ? 134.292 127.131 92.147  1.00 96.31  ? 129 GLU   D CA    1 
ATOM   5325 C  C     . GLU   C 2 129 ? 134.751 128.323 91.316  1.00 98.31  ? 129 GLU   D C     1 
ATOM   5326 O  O     . GLU   C 2 129 ? 135.577 128.169 90.409  1.00 96.02  ? 129 GLU   D O     1 
ATOM   5327 C  CB    . GLU   C 2 129 ? 132.998 126.546 91.582  1.00 95.37  ? 129 GLU   D CB    1 
ATOM   5328 C  CG    . GLU   C 2 129 ? 133.210 125.361 90.653  1.00 98.54  ? 129 GLU   D CG    1 
ATOM   5329 C  CD    . GLU   C 2 129 ? 133.584 124.093 91.396  1.00 102.73 ? 129 GLU   D CD    1 
ATOM   5330 O  OE1   . GLU   C 2 129 ? 133.382 124.039 92.628  1.00 103.80 ? 129 GLU   D OE1   1 
ATOM   5331 O  OE2   . GLU   C 2 129 ? 134.081 123.148 90.749  1.00 101.23 ? 129 GLU   D OE2   1 
ATOM   5332 N  N     . PHE   C 2 130 ? 134.228 129.519 91.603  1.00 87.02  ? 130 PHE   D N     1 
ATOM   5333 C  CA    . PHE   C 2 130 ? 134.602 130.688 90.814  1.00 81.32  ? 130 PHE   D CA    1 
ATOM   5334 C  C     . PHE   C 2 130 ? 136.003 131.191 91.145  1.00 81.90  ? 130 PHE   D C     1 
ATOM   5335 O  O     . PHE   C 2 130 ? 136.665 131.770 90.277  1.00 81.09  ? 130 PHE   D O     1 
ATOM   5336 C  CB    . PHE   C 2 130 ? 133.586 131.811 91.021  1.00 78.34  ? 130 PHE   D CB    1 
ATOM   5337 C  CG    . PHE   C 2 130 ? 133.638 132.879 89.964  1.00 84.89  ? 130 PHE   D CG    1 
ATOM   5338 C  CD1   . PHE   C 2 130 ? 133.015 132.695 88.742  1.00 84.38  ? 130 PHE   D CD1   1 
ATOM   5339 C  CD2   . PHE   C 2 130 ? 134.313 134.066 90.191  1.00 88.21  ? 130 PHE   D CD2   1 
ATOM   5340 C  CE1   . PHE   C 2 130 ? 133.062 133.675 87.768  1.00 83.85  ? 130 PHE   D CE1   1 
ATOM   5341 C  CE2   . PHE   C 2 130 ? 134.364 135.050 89.221  1.00 84.06  ? 130 PHE   D CE2   1 
ATOM   5342 C  CZ    . PHE   C 2 130 ? 133.736 134.853 88.010  1.00 81.80  ? 130 PHE   D CZ    1 
ATOM   5343 N  N     . SER   C 2 131 ? 136.471 130.988 92.379  1.00 77.15  ? 131 SER   D N     1 
ATOM   5344 C  CA    . SER   C 2 131 ? 137.765 131.538 92.770  1.00 70.69  ? 131 SER   D CA    1 
ATOM   5345 C  C     . SER   C 2 131 ? 138.930 130.754 92.176  1.00 76.15  ? 131 SER   D C     1 
ATOM   5346 O  O     . SER   C 2 131 ? 140.007 131.323 91.965  1.00 81.06  ? 131 SER   D O     1 
ATOM   5347 C  CB    . SER   C 2 131 ? 137.882 131.574 94.293  1.00 71.75  ? 131 SER   D CB    1 
ATOM   5348 O  OG    . SER   C 2 131 ? 136.712 132.113 94.880  1.00 77.69  ? 131 SER   D OG    1 
ATOM   5349 N  N     . GLU   C 2 132 ? 138.736 129.462 91.903  1.00 88.63  ? 132 GLU   D N     1 
ATOM   5350 C  CA    . GLU   C 2 132 ? 139.814 128.572 91.459  1.00 89.23  ? 132 GLU   D CA    1 
ATOM   5351 C  C     . GLU   C 2 132 ? 140.982 128.594 92.440  1.00 93.08  ? 132 GLU   D C     1 
ATOM   5352 O  O     . GLU   C 2 132 ? 142.152 128.591 92.050  1.00 88.74  ? 132 GLU   D O     1 
ATOM   5353 C  CB    . GLU   C 2 132 ? 140.295 128.925 90.050  1.00 88.59  ? 132 GLU   D CB    1 
ATOM   5354 C  CG    . GLU   C 2 132 ? 139.197 129.081 89.023  1.00 92.70  ? 132 GLU   D CG    1 
ATOM   5355 C  CD    . GLU   C 2 132 ? 139.383 130.322 88.177  1.00 94.22  ? 132 GLU   D CD    1 
ATOM   5356 O  OE1   . GLU   C 2 132 ? 140.443 130.970 88.299  1.00 91.46  ? 132 GLU   D OE1   1 
ATOM   5357 O  OE2   . GLU   C 2 132 ? 138.474 130.647 87.389  1.00 95.16  ? 132 GLU   D OE2   1 
ATOM   5358 N  N     . LEU   C 2 133 ? 140.663 128.617 93.731  1.00 85.36  ? 133 LEU   D N     1 
ATOM   5359 C  CA    . LEU   C 2 133 ? 141.680 128.671 94.772  1.00 80.77  ? 133 LEU   D CA    1 
ATOM   5360 C  C     . LEU   C 2 133 ? 142.190 127.299 95.181  1.00 84.79  ? 133 LEU   D C     1 
ATOM   5361 O  O     . LEU   C 2 133 ? 143.369 127.168 95.526  1.00 85.18  ? 133 LEU   D O     1 
ATOM   5362 C  CB    . LEU   C 2 133 ? 141.133 129.400 96.005  1.00 81.21  ? 133 LEU   D CB    1 
ATOM   5363 C  CG    . LEU   C 2 133 ? 141.264 130.924 95.972  1.00 80.23  ? 133 LEU   D CG    1 
ATOM   5364 C  CD1   . LEU   C 2 133 ? 140.600 131.554 97.182  1.00 78.44  ? 133 LEU   D CD1   1 
ATOM   5365 C  CD2   . LEU   C 2 133 ? 142.722 131.331 95.889  1.00 75.74  ? 133 LEU   D CD2   1 
ATOM   5366 N  N     . GLY   C 2 134 ? 141.339 126.278 95.140  1.00 85.10  ? 134 GLY   D N     1 
ATOM   5367 C  CA    . GLY   C 2 134 ? 141.782 124.937 95.483  1.00 81.64  ? 134 GLY   D CA    1 
ATOM   5368 C  C     . GLY   C 2 134 ? 142.161 124.831 96.946  1.00 85.45  ? 134 GLY   D C     1 
ATOM   5369 O  O     . GLY   C 2 134 ? 141.550 125.460 97.818  1.00 84.77  ? 134 GLY   D O     1 
ATOM   5370 N  N     . GLU   C 2 135 ? 143.208 124.044 97.216  1.00 103.36 ? 135 GLU   D N     1 
ATOM   5371 C  CA    . GLU   C 2 135 ? 143.618 123.772 98.591  1.00 104.13 ? 135 GLU   D CA    1 
ATOM   5372 C  C     . GLU   C 2 135 ? 143.861 125.060 99.364  1.00 103.09 ? 135 GLU   D C     1 
ATOM   5373 O  O     . GLU   C 2 135 ? 143.606 125.128 100.574 1.00 105.39 ? 135 GLU   D O     1 
ATOM   5374 C  CB    . GLU   C 2 135 ? 144.883 122.914 98.593  1.00 102.46 ? 135 GLU   D CB    1 
ATOM   5375 C  CG    . GLU   C 2 135 ? 144.903 121.830 97.531  1.00 104.30 ? 135 GLU   D CG    1 
ATOM   5376 C  CD    . GLU   C 2 135 ? 144.992 120.439 98.120  1.00 106.24 ? 135 GLU   D CD    1 
ATOM   5377 O  OE1   . GLU   C 2 135 ? 144.952 120.316 99.361  1.00 106.92 ? 135 GLU   D OE1   1 
ATOM   5378 O  OE2   . GLU   C 2 135 ? 145.107 119.469 97.341  1.00 105.06 ? 135 GLU   D OE2   1 
ATOM   5379 N  N     . PHE   C 2 136 ? 144.318 126.106 98.674  1.00 79.03  ? 136 PHE   D N     1 
ATOM   5380 C  CA    . PHE   C 2 136 ? 144.717 127.329 99.358  1.00 74.22  ? 136 PHE   D CA    1 
ATOM   5381 C  C     . PHE   C 2 136 ? 143.528 128.054 99.969  1.00 73.27  ? 136 PHE   D C     1 
ATOM   5382 O  O     . PHE   C 2 136 ? 143.717 129.008 100.730 1.00 79.38  ? 136 PHE   D O     1 
ATOM   5383 C  CB    . PHE   C 2 136 ? 145.470 128.245 98.395  1.00 74.66  ? 136 PHE   D CB    1 
ATOM   5384 C  CG    . PHE   C 2 136 ? 146.962 128.125 98.496  1.00 75.61  ? 136 PHE   D CG    1 
ATOM   5385 C  CD1   . PHE   C 2 136 ? 147.645 128.704 99.551  1.00 75.63  ? 136 PHE   D CD1   1 
ATOM   5386 C  CD2   . PHE   C 2 136 ? 147.681 127.428 97.542  1.00 71.64  ? 136 PHE   D CD2   1 
ATOM   5387 C  CE1   . PHE   C 2 136 ? 149.017 128.594 99.650  1.00 72.62  ? 136 PHE   D CE1   1 
ATOM   5388 C  CE2   . PHE   C 2 136 ? 149.053 127.314 97.636  1.00 71.18  ? 136 PHE   D CE2   1 
ATOM   5389 C  CZ    . PHE   C 2 136 ? 149.722 127.897 98.691  1.00 71.72  ? 136 PHE   D CZ    1 
ATOM   5390 N  N     . ILE   C 2 137 ? 142.299 127.629 99.661  1.00 72.50  ? 137 ILE   D N     1 
ATOM   5391 C  CA    . ILE   C 2 137 ? 141.149 128.238 100.327 1.00 75.73  ? 137 ILE   D CA    1 
ATOM   5392 C  C     . ILE   C 2 137 ? 141.187 127.932 101.820 1.00 78.81  ? 137 ILE   D C     1 
ATOM   5393 O  O     . ILE   C 2 137 ? 140.618 128.667 102.636 1.00 83.44  ? 137 ILE   D O     1 
ATOM   5394 C  CB    . ILE   C 2 137 ? 139.828 127.775 99.685  1.00 75.77  ? 137 ILE   D CB    1 
ATOM   5395 C  CG1   . ILE   C 2 137 ? 138.661 128.594 100.234 1.00 72.95  ? 137 ILE   D CG1   1 
ATOM   5396 C  CG2   . ILE   C 2 137 ? 139.563 126.317 99.991  1.00 77.61  ? 137 ILE   D CG2   1 
ATOM   5397 C  CD1   . ILE   C 2 137 ? 138.272 129.767 99.363  1.00 74.90  ? 137 ILE   D CD1   1 
ATOM   5398 N  N     . TYR   C 2 138 ? 141.872 126.852 102.204 1.00 82.37  ? 138 TYR   D N     1 
ATOM   5399 C  CA    . TYR   C 2 138 ? 141.945 126.496 103.617 1.00 79.81  ? 138 TYR   D CA    1 
ATOM   5400 C  C     . TYR   C 2 138 ? 143.135 127.165 104.295 1.00 80.46  ? 138 TYR   D C     1 
ATOM   5401 O  O     . TYR   C 2 138 ? 143.171 127.289 105.524 1.00 80.57  ? 138 TYR   D O     1 
ATOM   5402 C  CB    . TYR   C 2 138 ? 142.018 124.977 103.764 1.00 78.76  ? 138 TYR   D CB    1 
ATOM   5403 C  CG    . TYR   C 2 138 ? 140.730 124.283 103.386 1.00 83.60  ? 138 TYR   D CG    1 
ATOM   5404 C  CD1   . TYR   C 2 138 ? 139.549 124.548 104.064 1.00 83.02  ? 138 TYR   D CD1   1 
ATOM   5405 C  CD2   . TYR   C 2 138 ? 140.691 123.373 102.337 1.00 84.07  ? 138 TYR   D CD2   1 
ATOM   5406 C  CE1   . TYR   C 2 138 ? 138.369 123.920 103.718 1.00 82.50  ? 138 TYR   D CE1   1 
ATOM   5407 C  CE2   . TYR   C 2 138 ? 139.517 122.740 101.983 1.00 83.49  ? 138 TYR   D CE2   1 
ATOM   5408 C  CZ    . TYR   C 2 138 ? 138.358 123.018 102.677 1.00 82.83  ? 138 TYR   D CZ    1 
ATOM   5409 O  OH    . TYR   C 2 138 ? 137.185 122.391 102.327 1.00 81.98  ? 138 TYR   D OH    1 
ATOM   5410 N  N     . GLN   C 2 139 ? 144.116 127.603 103.509 1.00 85.78  ? 139 GLN   D N     1 
ATOM   5411 C  CA    . GLN   C 2 139 ? 145.277 128.290 104.044 1.00 82.45  ? 139 GLN   D CA    1 
ATOM   5412 C  C     . GLN   C 2 139 ? 144.926 129.730 104.417 1.00 83.55  ? 139 GLN   D C     1 
ATOM   5413 O  O     . GLN   C 2 139 ? 143.927 130.278 103.946 1.00 83.65  ? 139 GLN   D O     1 
ATOM   5414 C  CB    . GLN   C 2 139 ? 146.413 128.266 103.024 1.00 81.39  ? 139 GLN   D CB    1 
ATOM   5415 C  CG    . GLN   C 2 139 ? 146.736 126.881 102.492 1.00 82.75  ? 139 GLN   D CG    1 
ATOM   5416 C  CD    . GLN   C 2 139 ? 147.030 125.887 103.597 1.00 86.62  ? 139 GLN   D CD    1 
ATOM   5417 O  OE1   . GLN   C 2 139 ? 147.834 126.154 104.491 1.00 85.51  ? 139 GLN   D OE1   1 
ATOM   5418 N  NE2   . GLN   C 2 139 ? 146.380 124.730 103.543 1.00 86.36  ? 139 GLN   D NE2   1 
ATOM   5419 N  N     . PRO   C 2 140 ? 145.730 130.362 105.274 1.00 83.62  ? 140 PRO   D N     1 
ATOM   5420 C  CA    . PRO   C 2 140 ? 145.470 131.763 105.627 1.00 86.03  ? 140 PRO   D CA    1 
ATOM   5421 C  C     . PRO   C 2 140 ? 145.621 132.690 104.431 1.00 86.49  ? 140 PRO   D C     1 
ATOM   5422 O  O     . PRO   C 2 140 ? 146.356 132.408 103.481 1.00 85.83  ? 140 PRO   D O     1 
ATOM   5423 C  CB    . PRO   C 2 140 ? 146.527 132.062 106.698 1.00 84.59  ? 140 PRO   D CB    1 
ATOM   5424 C  CG    . PRO   C 2 140 ? 146.903 130.724 107.239 1.00 87.41  ? 140 PRO   D CG    1 
ATOM   5425 C  CD    . PRO   C 2 140 ? 146.839 129.802 106.065 1.00 84.42  ? 140 PRO   D CD    1 
ATOM   5426 N  N     . VAL   C 2 141 ? 144.903 133.814 104.493 1.00 74.93  ? 141 VAL   D N     1 
ATOM   5427 C  CA    . VAL   C 2 141 ? 144.876 134.757 103.377 1.00 72.76  ? 141 VAL   D CA    1 
ATOM   5428 C  C     . VAL   C 2 141 ? 146.248 135.391 103.174 1.00 72.07  ? 141 VAL   D C     1 
ATOM   5429 O  O     . VAL   C 2 141 ? 146.636 135.717 102.045 1.00 74.16  ? 141 VAL   D O     1 
ATOM   5430 C  CB    . VAL   C 2 141 ? 143.775 135.813 103.606 1.00 67.04  ? 141 VAL   D CB    1 
ATOM   5431 C  CG1   . VAL   C 2 141 ? 144.112 137.127 102.919 1.00 69.43  ? 141 VAL   D CG1   1 
ATOM   5432 C  CG2   . VAL   C 2 141 ? 142.439 135.288 103.116 1.00 66.42  ? 141 VAL   D CG2   1 
ATOM   5433 N  N     . LYS   C 2 142 ? 147.015 135.553 104.254 1.00 72.11  ? 142 LYS   D N     1 
ATOM   5434 C  CA    . LYS   C 2 142 ? 148.328 136.182 104.136 1.00 72.00  ? 142 LYS   D CA    1 
ATOM   5435 C  C     . LYS   C 2 142 ? 149.269 135.358 103.260 1.00 72.85  ? 142 LYS   D C     1 
ATOM   5436 O  O     . LYS   C 2 142 ? 150.258 135.884 102.737 1.00 75.60  ? 142 LYS   D O     1 
ATOM   5437 C  CB    . LYS   C 2 142 ? 148.929 136.400 105.527 1.00 77.15  ? 142 LYS   D CB    1 
ATOM   5438 C  CG    . LYS   C 2 142 ? 150.059 135.451 105.887 1.00 78.51  ? 142 LYS   D CG    1 
ATOM   5439 C  CD    . LYS   C 2 142 ? 150.685 135.823 107.219 1.00 77.30  ? 142 LYS   D CD    1 
ATOM   5440 C  CE    . LYS   C 2 142 ? 149.690 135.674 108.356 1.00 76.11  ? 142 LYS   D CE    1 
ATOM   5441 N  NZ    . LYS   C 2 142 ? 149.247 134.263 108.516 1.00 74.85  ? 142 LYS   D NZ    1 
ATOM   5442 N  N     . LYS   C 2 143 ? 148.977 134.067 103.083 1.00 70.05  ? 143 LYS   D N     1 
ATOM   5443 C  CA    . LYS   C 2 143 ? 149.799 133.239 102.205 1.00 68.56  ? 143 LYS   D CA    1 
ATOM   5444 C  C     . LYS   C 2 143 ? 149.454 133.469 100.738 1.00 70.47  ? 143 LYS   D C     1 
ATOM   5445 O  O     . LYS   C 2 143 ? 150.188 133.029 99.846  1.00 69.75  ? 143 LYS   D O     1 
ATOM   5446 C  CB    . LYS   C 2 143 ? 149.634 131.762 102.563 1.00 69.22  ? 143 LYS   D CB    1 
ATOM   5447 C  CG    . LYS   C 2 143 ? 149.612 131.461 104.052 1.00 70.60  ? 143 LYS   D CG    1 
ATOM   5448 C  CD    . LYS   C 2 143 ? 150.990 131.616 104.671 1.00 70.79  ? 143 LYS   D CD    1 
ATOM   5449 C  CE    . LYS   C 2 143 ? 151.025 131.047 106.080 1.00 70.06  ? 143 LYS   D CE    1 
ATOM   5450 N  NZ    . LYS   C 2 143 ? 152.249 131.465 106.818 1.00 70.23  ? 143 LYS   D NZ    1 
ATOM   5451 N  N     . TYR   C 2 144 ? 148.340 134.145 100.468 1.00 65.25  ? 144 TYR   D N     1 
ATOM   5452 C  CA    . TYR   C 2 144 ? 147.894 134.332 99.092  1.00 58.62  ? 144 TYR   D CA    1 
ATOM   5453 C  C     . TYR   C 2 144 ? 148.786 135.323 98.358  1.00 65.53  ? 144 TYR   D C     1 
ATOM   5454 O  O     . TYR   C 2 144 ? 149.461 136.153 98.971  1.00 65.62  ? 144 TYR   D O     1 
ATOM   5455 C  CB    . TYR   C 2 144 ? 146.449 134.832 99.047  1.00 50.89  ? 144 TYR   D CB    1 
ATOM   5456 C  CG    . TYR   C 2 144 ? 145.391 133.853 99.501  1.00 56.17  ? 144 TYR   D CG    1 
ATOM   5457 C  CD1   . TYR   C 2 144 ? 145.720 132.719 100.226 1.00 58.56  ? 144 TYR   D CD1   1 
ATOM   5458 C  CD2   . TYR   C 2 144 ? 144.055 134.069 99.199  1.00 61.54  ? 144 TYR   D CD2   1 
ATOM   5459 C  CE1   . TYR   C 2 144 ? 144.752 131.835 100.640 1.00 60.83  ? 144 TYR   D CE1   1 
ATOM   5460 C  CE2   . TYR   C 2 144 ? 143.081 133.189 99.607  1.00 61.02  ? 144 TYR   D CE2   1 
ATOM   5461 C  CZ    . TYR   C 2 144 ? 143.435 132.073 100.327 1.00 60.68  ? 144 TYR   D CZ    1 
ATOM   5462 O  OH    . TYR   C 2 144 ? 142.466 131.191 100.736 1.00 63.69  ? 144 TYR   D OH    1 
ATOM   5463 N  N     . SER   C 2 145 ? 148.788 135.222 97.032  1.00 68.04  ? 145 SER   D N     1 
ATOM   5464 C  CA    . SER   C 2 145 ? 149.350 136.269 96.199  1.00 63.52  ? 145 SER   D CA    1 
ATOM   5465 C  C     . SER   C 2 145 ? 148.298 137.345 95.938  1.00 70.65  ? 145 SER   D C     1 
ATOM   5466 O  O     . SER   C 2 145 ? 147.126 137.206 96.298  1.00 70.61  ? 145 SER   D O     1 
ATOM   5467 C  CB    . SER   C 2 145 ? 149.864 135.689 94.885  1.00 60.49  ? 145 SER   D CB    1 
ATOM   5468 O  OG    . SER   C 2 145 ? 148.854 135.689 93.894  1.00 67.88  ? 145 SER   D OG    1 
ATOM   5469 N  N     . SER   C 2 146 ? 148.733 138.439 95.309  1.00 70.90  ? 146 SER   D N     1 
ATOM   5470 C  CA    . SER   C 2 146 ? 147.825 139.553 95.050  1.00 65.19  ? 146 SER   D CA    1 
ATOM   5471 C  C     . SER   C 2 146 ? 146.692 139.146 94.114  1.00 65.80  ? 146 SER   D C     1 
ATOM   5472 O  O     . SER   C 2 146 ? 145.526 139.497 94.346  1.00 72.10  ? 146 SER   D O     1 
ATOM   5473 C  CB    . SER   C 2 146 ? 148.603 140.734 94.469  1.00 63.83  ? 146 SER   D CB    1 
ATOM   5474 O  OG    . SER   C 2 146 ? 148.950 140.496 93.118  1.00 73.49  ? 146 SER   D OG    1 
ATOM   5475 N  N     . GLY   C 2 147 ? 147.012 138.401 93.055  1.00 53.79  ? 147 GLY   D N     1 
ATOM   5476 C  CA    . GLY   C 2 147 ? 145.978 137.959 92.134  1.00 48.31  ? 147 GLY   D CA    1 
ATOM   5477 C  C     . GLY   C 2 147 ? 144.974 137.030 92.786  1.00 54.99  ? 147 GLY   D C     1 
ATOM   5478 O  O     . GLY   C 2 147 ? 143.778 137.097 92.499  1.00 62.51  ? 147 GLY   D O     1 
ATOM   5479 N  N     . MET   C 2 148 ? 145.446 136.150 93.671  1.00 61.74  ? 148 MET   D N     1 
ATOM   5480 C  CA    . MET   C 2 148 ? 144.545 135.240 94.374  1.00 59.00  ? 148 MET   D CA    1 
ATOM   5481 C  C     . MET   C 2 148 ? 143.590 136.005 95.285  1.00 59.59  ? 148 MET   D C     1 
ATOM   5482 O  O     . MET   C 2 148 ? 142.394 135.694 95.350  1.00 68.57  ? 148 MET   D O     1 
ATOM   5483 C  CB    . MET   C 2 148 ? 145.364 134.226 95.171  1.00 61.00  ? 148 MET   D CB    1 
ATOM   5484 C  CG    . MET   C 2 148 ? 146.328 133.413 94.318  1.00 65.03  ? 148 MET   D CG    1 
ATOM   5485 S  SD    . MET   C 2 148 ? 147.415 132.332 95.271  1.00 66.12  ? 148 MET   D SD    1 
ATOM   5486 C  CE    . MET   C 2 148 ? 146.312 130.984 95.664  1.00 59.65  ? 148 MET   D CE    1 
ATOM   5487 N  N     . ARG   C 2 149 ? 144.103 137.015 95.993  1.00 47.51  ? 149 ARG   D N     1 
ATOM   5488 C  CA    . ARG   C 2 149 ? 143.248 137.846 96.835  1.00 52.42  ? 149 ARG   D CA    1 
ATOM   5489 C  C     . ARG   C 2 149 ? 142.218 138.595 96.000  1.00 59.74  ? 149 ARG   D C     1 
ATOM   5490 O  O     . ARG   C 2 149 ? 141.043 138.693 96.384  1.00 59.35  ? 149 ARG   D O     1 
ATOM   5491 C  CB    . ARG   C 2 149 ? 144.104 138.833 97.628  1.00 57.24  ? 149 ARG   D CB    1 
ATOM   5492 C  CG    . ARG   C 2 149 ? 144.708 138.267 98.896  1.00 61.91  ? 149 ARG   D CG    1 
ATOM   5493 C  CD    . ARG   C 2 149 ? 145.107 139.382 99.848  1.00 55.54  ? 149 ARG   D CD    1 
ATOM   5494 N  NE    . ARG   C 2 149 ? 146.462 139.863 99.601  1.00 54.33  ? 149 ARG   D NE    1 
ATOM   5495 C  CZ    . ARG   C 2 149 ? 147.567 139.160 99.810  1.00 63.90  ? 149 ARG   D CZ    1 
ATOM   5496 N  NH1   . ARG   C 2 149 ? 147.525 137.934 100.305 1.00 70.69  ? 149 ARG   D NH1   1 
ATOM   5497 N  NH2   . ARG   C 2 149 ? 148.745 139.703 99.519  1.00 59.68  ? 149 ARG   D NH2   1 
ATOM   5498 N  N     . ALA   C 2 150 ? 142.645 139.142 94.858  1.00 56.98  ? 150 ALA   D N     1 
ATOM   5499 C  CA    . ALA   C 2 150 ? 141.711 139.833 93.976  1.00 49.53  ? 150 ALA   D CA    1 
ATOM   5500 C  C     . ALA   C 2 150 ? 140.631 138.888 93.468  1.00 57.47  ? 150 ALA   D C     1 
ATOM   5501 O  O     . ALA   C 2 150 ? 139.454 139.259 93.409  1.00 63.36  ? 150 ALA   D O     1 
ATOM   5502 C  CB    . ALA   C 2 150 ? 142.464 140.467 92.809  1.00 51.67  ? 150 ALA   D CB    1 
ATOM   5503 N  N     . LYS   C 2 151 ? 141.013 137.663 93.097  1.00 58.11  ? 151 LYS   D N     1 
ATOM   5504 C  CA    . LYS   C 2 151 ? 140.031 136.684 92.642  1.00 54.75  ? 151 LYS   D CA    1 
ATOM   5505 C  C     . LYS   C 2 151 ? 139.030 136.356 93.740  1.00 54.23  ? 151 LYS   D C     1 
ATOM   5506 O  O     . LYS   C 2 151 ? 137.823 136.284 93.486  1.00 60.50  ? 151 LYS   D O     1 
ATOM   5507 C  CB    . LYS   C 2 151 ? 140.728 135.407 92.171  1.00 52.22  ? 151 LYS   D CB    1 
ATOM   5508 C  CG    . LYS   C 2 151 ? 141.528 135.547 90.894  1.00 57.21  ? 151 LYS   D CG    1 
ATOM   5509 C  CD    . LYS   C 2 151 ? 142.520 134.405 90.757  1.00 59.84  ? 151 LYS   D CD    1 
ATOM   5510 C  CE    . LYS   C 2 151 ? 143.046 134.294 89.339  1.00 63.36  ? 151 LYS   D CE    1 
ATOM   5511 N  NZ    . LYS   C 2 151 ? 142.317 133.257 88.562  1.00 61.44  ? 151 LYS   D NZ    1 
ATOM   5512 N  N     . LEU   C 2 152 ? 139.514 136.149 94.967  1.00 47.88  ? 152 LEU   D N     1 
ATOM   5513 C  CA    . LEU   C 2 152 ? 138.610 135.824 96.066  1.00 53.00  ? 152 LEU   D CA    1 
ATOM   5514 C  C     . LEU   C 2 152 ? 137.628 136.959 96.328  1.00 60.20  ? 152 LEU   D C     1 
ATOM   5515 O  O     . LEU   C 2 152 ? 136.417 136.728 96.451  1.00 62.73  ? 152 LEU   D O     1 
ATOM   5516 C  CB    . LEU   C 2 152 ? 139.410 135.503 97.328  1.00 53.56  ? 152 LEU   D CB    1 
ATOM   5517 C  CG    . LEU   C 2 152 ? 138.603 135.169 98.583  1.00 56.62  ? 152 LEU   D CG    1 
ATOM   5518 C  CD1   . LEU   C 2 152 ? 137.661 134.005 98.323  1.00 59.53  ? 152 LEU   D CD1   1 
ATOM   5519 C  CD2   . LEU   C 2 152 ? 139.528 134.859 99.746  1.00 54.86  ? 152 LEU   D CD2   1 
ATOM   5520 N  N     . GLY   C 2 153 ? 138.126 138.196 96.397  1.00 57.29  ? 153 GLY   D N     1 
ATOM   5521 C  CA    . GLY   C 2 153 ? 137.237 139.324 96.626  1.00 48.48  ? 153 GLY   D CA    1 
ATOM   5522 C  C     . GLY   C 2 153 ? 136.232 139.516 95.506  1.00 48.51  ? 153 GLY   D C     1 
ATOM   5523 O  O     . GLY   C 2 153 ? 135.047 139.768 95.757  1.00 53.11  ? 153 GLY   D O     1 
ATOM   5524 N  N     . PHE   C 2 154 ? 136.686 139.398 94.255  1.00 58.21  ? 154 PHE   D N     1 
ATOM   5525 C  CA    . PHE   C 2 154 ? 135.788 139.565 93.120  1.00 58.52  ? 154 PHE   D CA    1 
ATOM   5526 C  C     . PHE   C 2 154 ? 134.711 138.490 93.106  1.00 62.10  ? 154 PHE   D C     1 
ATOM   5527 O  O     . PHE   C 2 154 ? 133.546 138.782 92.821  1.00 66.07  ? 154 PHE   D O     1 
ATOM   5528 C  CB    . PHE   C 2 154 ? 136.582 139.544 91.815  1.00 65.72  ? 154 PHE   D CB    1 
ATOM   5529 C  CG    . PHE   C 2 154 ? 135.737 139.747 90.590  1.00 72.40  ? 154 PHE   D CG    1 
ATOM   5530 C  CD1   . PHE   C 2 154 ? 135.294 141.011 90.242  1.00 69.32  ? 154 PHE   D CD1   1 
ATOM   5531 C  CD2   . PHE   C 2 154 ? 135.381 138.673 89.792  1.00 70.49  ? 154 PHE   D CD2   1 
ATOM   5532 C  CE1   . PHE   C 2 154 ? 134.515 141.204 89.118  1.00 66.54  ? 154 PHE   D CE1   1 
ATOM   5533 C  CE2   . PHE   C 2 154 ? 134.600 138.859 88.667  1.00 72.39  ? 154 PHE   D CE2   1 
ATOM   5534 C  CZ    . PHE   C 2 154 ? 134.169 140.127 88.329  1.00 70.50  ? 154 PHE   D CZ    1 
ATOM   5535 N  N     . SER   C 2 155 ? 135.079 137.242 93.406  1.00 60.56  ? 155 SER   D N     1 
ATOM   5536 C  CA    . SER   C 2 155 ? 134.089 136.172 93.450  1.00 57.97  ? 155 SER   D CA    1 
ATOM   5537 C  C     . SER   C 2 155 ? 133.083 136.395 94.573  1.00 64.54  ? 155 SER   D C     1 
ATOM   5538 O  O     . SER   C 2 155 ? 131.880 136.163 94.391  1.00 65.71  ? 155 SER   D O     1 
ATOM   5539 C  CB    . SER   C 2 155 ? 134.783 134.822 93.610  1.00 57.34  ? 155 SER   D CB    1 
ATOM   5540 O  OG    . SER   C 2 155 ? 134.763 134.399 94.959  1.00 64.14  ? 155 SER   D OG    1 
ATOM   5541 N  N     . ILE   C 2 156 ? 133.553 136.850 95.739  1.00 62.70  ? 156 ILE   D N     1 
ATOM   5542 C  CA    . ILE   C 2 156 ? 132.643 137.120 96.853  1.00 58.07  ? 156 ILE   D CA    1 
ATOM   5543 C  C     . ILE   C 2 156 ? 131.641 138.200 96.465  1.00 60.11  ? 156 ILE   D C     1 
ATOM   5544 O  O     . ILE   C 2 156 ? 130.439 138.086 96.728  1.00 63.20  ? 156 ILE   D O     1 
ATOM   5545 C  CB    . ILE   C 2 156 ? 133.428 137.516 98.115  1.00 60.82  ? 156 ILE   D CB    1 
ATOM   5546 C  CG1   . ILE   C 2 156 ? 134.176 136.311 98.688  1.00 59.93  ? 156 ILE   D CG1   1 
ATOM   5547 C  CG2   . ILE   C 2 156 ? 132.497 138.099 99.164  1.00 58.76  ? 156 ILE   D CG2   1 
ATOM   5548 C  CD1   . ILE   C 2 156 ? 135.066 136.656 99.860  1.00 56.76  ? 156 ILE   D CD1   1 
ATOM   5549 N  N     . ASN   C 2 157 ? 132.126 139.267 95.825  1.00 75.14  ? 157 ASN   D N     1 
ATOM   5550 C  CA    . ASN   C 2 157 ? 131.231 140.359 95.449  1.00 73.42  ? 157 ASN   D CA    1 
ATOM   5551 C  C     . ASN   C 2 157 ? 130.285 139.953 94.323  1.00 71.35  ? 157 ASN   D C     1 
ATOM   5552 O  O     . ASN   C 2 157 ? 129.128 140.386 94.288  1.00 68.35  ? 157 ASN   D O     1 
ATOM   5553 C  CB    . ASN   C 2 157 ? 132.045 141.590 95.053  1.00 72.74  ? 157 ASN   D CB    1 
ATOM   5554 C  CG    . ASN   C 2 157 ? 132.626 142.311 96.252  1.00 75.23  ? 157 ASN   D CG    1 
ATOM   5555 O  OD1   . ASN   C 2 157 ? 132.052 143.282 96.745  1.00 70.37  ? 157 ASN   D OD1   1 
ATOM   5556 N  ND2   . ASN   C 2 157 ? 133.769 141.837 96.732  1.00 76.78  ? 157 ASN   D ND2   1 
ATOM   5557 N  N     . ILE   C 2 158 ? 130.760 139.128 93.387  1.00 85.74  ? 158 ILE   D N     1 
ATOM   5558 C  CA    . ILE   C 2 158 ? 129.952 138.757 92.227  1.00 87.02  ? 158 ILE   D CA    1 
ATOM   5559 C  C     . ILE   C 2 158 ? 128.863 137.764 92.616  1.00 87.94  ? 158 ILE   D C     1 
ATOM   5560 O  O     . ILE   C 2 158 ? 127.751 137.798 92.074  1.00 89.77  ? 158 ILE   D O     1 
ATOM   5561 C  CB    . ILE   C 2 158 ? 130.859 138.209 91.107  1.00 88.71  ? 158 ILE   D CB    1 
ATOM   5562 C  CG1   . ILE   C 2 158 ? 131.388 139.357 90.251  1.00 86.90  ? 158 ILE   D CG1   1 
ATOM   5563 C  CG2   . ILE   C 2 158 ? 130.124 137.193 90.242  1.00 87.45  ? 158 ILE   D CG2   1 
ATOM   5564 C  CD1   . ILE   C 2 158 ? 130.340 139.995 89.369  1.00 87.93  ? 158 ILE   D CD1   1 
ATOM   5565 N  N     . THR   C 2 159 ? 129.163 136.861 93.556  1.00 92.23  ? 159 THR   D N     1 
ATOM   5566 C  CA    . THR   C 2 159 ? 128.209 135.808 93.896  1.00 93.88  ? 159 THR   D CA    1 
ATOM   5567 C  C     . THR   C 2 159 ? 126.893 136.389 94.404  1.00 96.48  ? 159 THR   D C     1 
ATOM   5568 O  O     . THR   C 2 159 ? 125.815 135.953 93.986  1.00 95.77  ? 159 THR   D O     1 
ATOM   5569 C  CB    . THR   C 2 159 ? 128.818 134.863 94.928  1.00 96.37  ? 159 THR   D CB    1 
ATOM   5570 O  OG1   . THR   C 2 159 ? 130.054 134.348 94.421  1.00 95.68  ? 159 THR   D OG1   1 
ATOM   5571 C  CG2   . THR   C 2 159 ? 127.873 133.706 95.212  1.00 97.80  ? 159 THR   D CG2   1 
ATOM   5572 N  N     . VAL   C 2 160 ? 126.959 137.373 95.302  1.00 101.70 ? 160 VAL   D N     1 
ATOM   5573 C  CA    . VAL   C 2 160 ? 125.763 138.137 95.632  1.00 100.52 ? 160 VAL   D CA    1 
ATOM   5574 C  C     . VAL   C 2 160 ? 125.415 139.032 94.448  1.00 100.91 ? 160 VAL   D C     1 
ATOM   5575 O  O     . VAL   C 2 160 ? 126.289 139.445 93.673  1.00 103.75 ? 160 VAL   D O     1 
ATOM   5576 C  CB    . VAL   C 2 160 ? 125.964 138.949 96.925  1.00 99.41  ? 160 VAL   D CB    1 
ATOM   5577 C  CG1   . VAL   C 2 160 ? 126.851 138.185 97.894  1.00 99.59  ? 160 VAL   D CG1   1 
ATOM   5578 C  CG2   . VAL   C 2 160 ? 126.555 140.317 96.630  1.00 100.48 ? 160 VAL   D CG2   1 
ATOM   5579 N  N     . ASN   C 2 161 ? 124.125 139.323 94.286  1.00 100.97 ? 161 ASN   D N     1 
ATOM   5580 C  CA    . ASN   C 2 161 ? 123.663 140.013 93.091  1.00 101.79 ? 161 ASN   D CA    1 
ATOM   5581 C  C     . ASN   C 2 161 ? 123.417 141.480 93.393  1.00 104.40 ? 161 ASN   D C     1 
ATOM   5582 O  O     . ASN   C 2 161 ? 122.408 141.811 94.035  1.00 104.32 ? 161 ASN   D O     1 
ATOM   5583 C  CB    . ASN   C 2 161 ? 122.389 139.366 92.561  1.00 103.69 ? 161 ASN   D CB    1 
ATOM   5584 C  CG    . ASN   C 2 161 ? 122.661 138.073 91.818  1.00 103.14 ? 161 ASN   D CG    1 
ATOM   5585 O  OD1   . ASN   C 2 161 ? 122.885 138.074 90.607  1.00 104.74 ? 161 ASN   D OD1   1 
ATOM   5586 N  ND2   . ASN   C 2 161 ? 122.646 136.961 92.542  1.00 102.37 ? 161 ASN   D ND2   1 
ATOM   5587 N  N     . PRO   C 2 162 ? 124.295 142.386 92.959  1.00 107.64 ? 162 PRO   D N     1 
ATOM   5588 C  CA    . PRO   C 2 162 ? 124.051 143.816 93.169  1.00 106.58 ? 162 PRO   D CA    1 
ATOM   5589 C  C     . PRO   C 2 162 ? 123.376 144.473 91.976  1.00 104.28 ? 162 PRO   D C     1 
ATOM   5590 O  O     . PRO   C 2 162 ? 123.591 144.066 90.830  1.00 103.50 ? 162 PRO   D O     1 
ATOM   5591 C  CB    . PRO   C 2 162 ? 125.461 144.373 93.391  1.00 104.48 ? 162 PRO   D CB    1 
ATOM   5592 C  CG    . PRO   C 2 162 ? 126.396 143.367 92.712  1.00 106.04 ? 162 PRO   D CG    1 
ATOM   5593 C  CD    . PRO   C 2 162 ? 125.594 142.152 92.310  1.00 105.72 ? 162 PRO   D CD    1 
ATOM   5594 N  N     . ASP   C 2 163 ? 122.550 145.488 92.232  1.00 109.83 ? 163 ASP   D N     1 
ATOM   5595 C  CA    . ASP   C 2 163 ? 121.963 146.242 91.131  1.00 111.28 ? 163 ASP   D CA    1 
ATOM   5596 C  C     . ASP   C 2 163 ? 123.016 147.083 90.420  1.00 112.19 ? 163 ASP   D C     1 
ATOM   5597 O  O     . ASP   C 2 163 ? 122.995 147.207 89.189  1.00 113.05 ? 163 ASP   D O     1 
ATOM   5598 C  CB    . ASP   C 2 163 ? 120.823 147.119 91.644  1.00 112.21 ? 163 ASP   D CB    1 
ATOM   5599 C  CG    . ASP   C 2 163 ? 119.481 146.411 91.609  1.00 114.50 ? 163 ASP   D CG    1 
ATOM   5600 O  OD1   . ASP   C 2 163 ? 119.144 145.725 92.597  1.00 112.05 ? 163 ASP   D OD1   1 
ATOM   5601 O  OD2   . ASP   C 2 163 ? 118.765 146.540 90.594  1.00 114.63 ? 163 ASP   D OD2   1 
ATOM   5602 N  N     . ILE   C 2 164 ? 123.944 147.667 91.175  1.00 96.31  ? 164 ILE   D N     1 
ATOM   5603 C  CA    . ILE   C 2 164 ? 125.018 148.490 90.631  1.00 94.37  ? 164 ILE   D CA    1 
ATOM   5604 C  C     . ILE   C 2 164 ? 126.347 147.943 91.133  1.00 95.45  ? 164 ILE   D C     1 
ATOM   5605 O  O     . ILE   C 2 164 ? 126.522 147.726 92.339  1.00 93.99  ? 164 ILE   D O     1 
ATOM   5606 C  CB    . ILE   C 2 164 ? 124.853 149.972 91.015  1.00 93.17  ? 164 ILE   D CB    1 
ATOM   5607 C  CG1   . ILE   C 2 164 ? 123.607 150.560 90.350  1.00 92.43  ? 164 ILE   D CG1   1 
ATOM   5608 C  CG2   . ILE   C 2 164 ? 126.090 150.768 90.632  1.00 96.24  ? 164 ILE   D CG2   1 
ATOM   5609 C  CD1   . ILE   C 2 164 ? 122.617 151.154 91.325  1.00 91.84  ? 164 ILE   D CD1   1 
ATOM   5610 N  N     . LEU   C 2 165 ? 127.279 147.718 90.209  1.00 87.49  ? 165 LEU   D N     1 
ATOM   5611 C  CA    . LEU   C 2 165 ? 128.603 147.206 90.533  1.00 84.87  ? 165 LEU   D CA    1 
ATOM   5612 C  C     . LEU   C 2 165 ? 129.653 148.219 90.104  1.00 85.20  ? 165 LEU   D C     1 
ATOM   5613 O  O     . LEU   C 2 165 ? 129.616 148.708 88.971  1.00 86.68  ? 165 LEU   D O     1 
ATOM   5614 C  CB    . LEU   C 2 165 ? 128.851 145.857 89.852  1.00 83.67  ? 165 LEU   D CB    1 
ATOM   5615 C  CG    . LEU   C 2 165 ? 130.204 145.190 90.111  1.00 86.59  ? 165 LEU   D CG    1 
ATOM   5616 C  CD1   . LEU   C 2 165 ? 130.371 144.870 91.587  1.00 83.55  ? 165 LEU   D CD1   1 
ATOM   5617 C  CD2   . LEU   C 2 165 ? 130.345 143.934 89.270  1.00 88.50  ? 165 LEU   D CD2   1 
ATOM   5618 N  N     . VAL   C 2 166 ? 130.579 148.532 91.005  1.00 72.21  ? 166 VAL   D N     1 
ATOM   5619 C  CA    . VAL   C 2 166 ? 131.662 149.473 90.745  1.00 73.41  ? 166 VAL   D CA    1 
ATOM   5620 C  C     . VAL   C 2 166 ? 132.983 148.738 90.915  1.00 74.68  ? 166 VAL   D C     1 
ATOM   5621 O  O     . VAL   C 2 166 ? 133.216 148.097 91.947  1.00 73.30  ? 166 VAL   D O     1 
ATOM   5622 C  CB    . VAL   C 2 166 ? 131.587 150.692 91.682  1.00 71.33  ? 166 VAL   D CB    1 
ATOM   5623 C  CG1   . VAL   C 2 166 ? 132.873 151.496 91.614  1.00 72.67  ? 166 VAL   D CG1   1 
ATOM   5624 C  CG2   . VAL   C 2 166 ? 130.392 151.559 91.327  1.00 70.21  ? 166 VAL   D CG2   1 
ATOM   5625 N  N     . ILE   C 2 167 ? 133.838 148.816 89.897  1.00 72.11  ? 167 ILE   D N     1 
ATOM   5626 C  CA    . ILE   C 2 167 ? 135.180 148.250 89.928  1.00 69.89  ? 167 ILE   D CA    1 
ATOM   5627 C  C     . ILE   C 2 167 ? 136.166 149.401 89.823  1.00 70.64  ? 167 ILE   D C     1 
ATOM   5628 O  O     . ILE   C 2 167 ? 136.116 150.180 88.862  1.00 77.22  ? 167 ILE   D O     1 
ATOM   5629 C  CB    . ILE   C 2 167 ? 135.391 147.237 88.790  1.00 72.24  ? 167 ILE   D CB    1 
ATOM   5630 C  CG1   . ILE   C 2 167 ? 134.303 146.163 88.822  1.00 71.00  ? 167 ILE   D CG1   1 
ATOM   5631 C  CG2   . ILE   C 2 167 ? 136.767 146.606 88.887  1.00 73.61  ? 167 ILE   D CG2   1 
ATOM   5632 C  CD1   . ILE   C 2 167 ? 133.745 145.819 87.458  1.00 65.83  ? 167 ILE   D CD1   1 
ATOM   5633 N  N     . ASP   C 2 168 ? 137.060 149.516 90.810  1.00 71.05  ? 168 ASP   D N     1 
ATOM   5634 C  CA    . ASP   C 2 168 ? 138.012 150.618 90.888  1.00 73.55  ? 168 ASP   D CA    1 
ATOM   5635 C  C     . ASP   C 2 168 ? 139.425 150.036 90.826  1.00 78.07  ? 168 ASP   D C     1 
ATOM   5636 O  O     . ASP   C 2 168 ? 140.063 149.800 91.855  1.00 79.77  ? 168 ASP   D O     1 
ATOM   5637 C  CB    . ASP   C 2 168 ? 137.792 151.434 92.162  1.00 72.78  ? 168 ASP   D CB    1 
ATOM   5638 C  CG    . ASP   C 2 168 ? 138.267 152.864 92.030  1.00 77.71  ? 168 ASP   D CG    1 
ATOM   5639 O  OD1   . ASP   C 2 168 ? 138.190 153.417 90.914  1.00 78.88  ? 168 ASP   D OD1   1 
ATOM   5640 O  OD2   . ASP   C 2 168 ? 138.715 153.438 93.044  1.00 76.68  ? 168 ASP   D OD2   1 
ATOM   5641 N  N     . GLU   C 2 169 ? 139.909 149.813 89.606  1.00 81.87  ? 169 GLU   D N     1 
ATOM   5642 C  CA    . GLU   C 2 169 ? 141.247 149.302 89.321  1.00 80.24  ? 169 GLU   D CA    1 
ATOM   5643 C  C     . GLU   C 2 169 ? 141.512 147.942 89.955  1.00 82.90  ? 169 GLU   D C     1 
ATOM   5644 O  O     . GLU   C 2 169 ? 142.676 147.581 90.156  1.00 84.51  ? 169 GLU   D O     1 
ATOM   5645 C  CB    . GLU   C 2 169 ? 142.327 150.293 89.767  1.00 81.64  ? 169 GLU   D CB    1 
ATOM   5646 C  CG    . GLU   C 2 169 ? 142.143 151.689 89.198  1.00 82.82  ? 169 GLU   D CG    1 
ATOM   5647 C  CD    . GLU   C 2 169 ? 143.164 152.674 89.723  1.00 86.28  ? 169 GLU   D CD    1 
ATOM   5648 O  OE1   . GLU   C 2 169 ? 144.239 152.232 90.176  1.00 87.29  ? 169 GLU   D OE1   1 
ATOM   5649 O  OE2   . GLU   C 2 169 ? 142.890 153.892 89.685  1.00 87.53  ? 169 GLU   D OE2   1 
ATOM   5650 N  N     . ALA   C 2 170 ? 140.467 147.171 90.264  1.00 81.86  ? 170 ALA   D N     1 
ATOM   5651 C  CA    . ALA   C 2 170 ? 140.664 145.894 90.942  1.00 77.71  ? 170 ALA   D CA    1 
ATOM   5652 C  C     . ALA   C 2 170 ? 141.278 144.855 90.012  1.00 79.82  ? 170 ALA   D C     1 
ATOM   5653 O  O     . ALA   C 2 170 ? 141.959 143.928 90.467  1.00 82.22  ? 170 ALA   D O     1 
ATOM   5654 C  CB    . ALA   C 2 170 ? 139.337 145.390 91.508  1.00 72.72  ? 170 ALA   D CB    1 
ATOM   5655 N  N     . LEU   C 2 171 ? 141.052 144.992 88.705  1.00 70.73  ? 171 LEU   D N     1 
ATOM   5656 C  CA    . LEU   C 2 171 ? 141.512 143.996 87.744  1.00 67.58  ? 171 LEU   D CA    1 
ATOM   5657 C  C     . LEU   C 2 171 ? 142.953 144.210 87.301  1.00 67.84  ? 171 LEU   D C     1 
ATOM   5658 O  O     . LEU   C 2 171 ? 143.435 143.453 86.452  1.00 72.52  ? 171 LEU   D O     1 
ATOM   5659 C  CB    . LEU   C 2 171 ? 140.598 143.994 86.518  1.00 72.23  ? 171 LEU   D CB    1 
ATOM   5660 C  CG    . LEU   C 2 171 ? 139.694 142.775 86.340  1.00 72.26  ? 171 LEU   D CG    1 
ATOM   5661 C  CD1   . LEU   C 2 171 ? 138.576 142.785 87.368  1.00 72.29  ? 171 LEU   D CD1   1 
ATOM   5662 C  CD2   . LEU   C 2 171 ? 139.130 142.738 84.932  1.00 72.58  ? 171 LEU   D CD2   1 
ATOM   5663 N  N     . SER   C 2 172 ? 143.644 145.217 87.838  1.00 68.26  ? 172 SER   D N     1 
ATOM   5664 C  CA    . SER   C 2 172 ? 145.010 145.490 87.401  1.00 74.24  ? 172 SER   D CA    1 
ATOM   5665 C  C     . SER   C 2 172 ? 145.953 144.351 87.772  1.00 74.76  ? 172 SER   D C     1 
ATOM   5666 O  O     . SER   C 2 172 ? 146.888 144.042 87.024  1.00 73.53  ? 172 SER   D O     1 
ATOM   5667 C  CB    . SER   C 2 172 ? 145.498 146.809 87.998  1.00 70.34  ? 172 SER   D CB    1 
ATOM   5668 O  OG    . SER   C 2 172 ? 145.136 146.918 89.362  1.00 71.31  ? 172 SER   D OG    1 
ATOM   5669 N  N     . VAL   C 2 173 ? 145.730 143.719 88.926  1.00 70.72  ? 173 VAL   D N     1 
ATOM   5670 C  CA    . VAL   C 2 173 ? 146.619 142.646 89.367  1.00 63.44  ? 173 VAL   D CA    1 
ATOM   5671 C  C     . VAL   C 2 173 ? 146.249 141.328 88.697  1.00 65.43  ? 173 VAL   D C     1 
ATOM   5672 O  O     . VAL   C 2 173 ? 147.097 140.443 88.528  1.00 67.73  ? 173 VAL   D O     1 
ATOM   5673 C  CB    . VAL   C 2 173 ? 146.594 142.529 90.902  1.00 65.63  ? 173 VAL   D CB    1 
ATOM   5674 C  CG1   . VAL   C 2 173 ? 147.480 143.597 91.524  1.00 64.14  ? 173 VAL   D CG1   1 
ATOM   5675 C  CG2   . VAL   C 2 173 ? 145.172 142.644 91.421  1.00 66.22  ? 173 VAL   D CG2   1 
ATOM   5676 N  N     . GLY   C 2 174 ? 144.985 141.169 88.314  1.00 62.32  ? 174 GLY   D N     1 
ATOM   5677 C  CA    . GLY   C 2 174 ? 144.564 139.926 87.691  1.00 63.28  ? 174 GLY   D CA    1 
ATOM   5678 C  C     . GLY   C 2 174 ? 145.156 139.769 86.301  1.00 63.37  ? 174 GLY   D C     1 
ATOM   5679 O  O     . GLY   C 2 174 ? 145.460 140.749 85.617  1.00 58.49  ? 174 GLY   D O     1 
ATOM   5680 N  N     . ASP   C 2 175 ? 145.318 138.516 85.880  1.00 82.83  ? 175 ASP   D N     1 
ATOM   5681 C  CA    . ASP   C 2 175 ? 145.907 138.217 84.585  1.00 79.46  ? 175 ASP   D CA    1 
ATOM   5682 C  C     . ASP   C 2 175 ? 144.846 138.244 83.484  1.00 82.53  ? 175 ASP   D C     1 
ATOM   5683 O  O     . ASP   C 2 175 ? 143.711 138.683 83.682  1.00 90.00  ? 175 ASP   D O     1 
ATOM   5684 C  CB    . ASP   C 2 175 ? 146.633 136.872 84.622  1.00 77.52  ? 175 ASP   D CB    1 
ATOM   5685 C  CG    . ASP   C 2 175 ? 145.766 135.745 85.153  1.00 84.52  ? 175 ASP   D CG    1 
ATOM   5686 O  OD1   . ASP   C 2 175 ? 144.573 135.671 84.792  1.00 90.09  ? 175 ASP   D OD1   1 
ATOM   5687 O  OD2   . ASP   C 2 175 ? 146.283 134.923 85.938  1.00 87.47  ? 175 ASP   D OD2   1 
ATOM   5688 N  N     . GLN   C 2 176 ? 145.239 137.764 82.300  1.00 86.33  ? 176 GLN   D N     1 
ATOM   5689 C  CA    . GLN   C 2 176 ? 144.391 137.914 81.121  1.00 86.69  ? 176 GLN   D CA    1 
ATOM   5690 C  C     . GLN   C 2 176 ? 143.209 136.951 81.142  1.00 89.22  ? 176 GLN   D C     1 
ATOM   5691 O  O     . GLN   C 2 176 ? 142.102 137.310 80.722  1.00 94.83  ? 176 GLN   D O     1 
ATOM   5692 C  CB    . GLN   C 2 176 ? 145.222 137.718 79.854  1.00 87.19  ? 176 GLN   D CB    1 
ATOM   5693 C  CG    . GLN   C 2 176 ? 145.705 139.018 79.235  1.00 91.25  ? 176 GLN   D CG    1 
ATOM   5694 C  CD    . GLN   C 2 176 ? 146.014 138.883 77.759  1.00 95.51  ? 176 GLN   D CD    1 
ATOM   5695 O  OE1   . GLN   C 2 176 ? 145.114 138.709 76.937  1.00 95.82  ? 176 GLN   D OE1   1 
ATOM   5696 N  NE2   . GLN   C 2 176 ? 147.293 138.967 77.413  1.00 91.69  ? 176 GLN   D NE2   1 
ATOM   5697 N  N     . THR   C 2 177 ? 143.424 135.717 81.604  1.00 77.87  ? 177 THR   D N     1 
ATOM   5698 C  CA    . THR   C 2 177 ? 142.329 134.751 81.657  1.00 78.83  ? 177 THR   D CA    1 
ATOM   5699 C  C     . THR   C 2 177 ? 141.250 135.193 82.637  1.00 76.34  ? 177 THR   D C     1 
ATOM   5700 O  O     . THR   C 2 177 ? 140.048 135.083 82.352  1.00 78.73  ? 177 THR   D O     1 
ATOM   5701 C  CB    . THR   C 2 177 ? 142.868 133.371 82.034  1.00 78.03  ? 177 THR   D CB    1 
ATOM   5702 O  OG1   . THR   C 2 177 ? 143.495 133.436 83.320  1.00 78.00  ? 177 THR   D OG1   1 
ATOM   5703 C  CG2   . THR   C 2 177 ? 143.890 132.906 81.009  1.00 75.43  ? 177 THR   D CG2   1 
ATOM   5704 N  N     . PHE   C 2 178 ? 141.661 135.706 83.798  1.00 68.72  ? 178 PHE   D N     1 
ATOM   5705 C  CA    . PHE   C 2 178 ? 140.700 136.257 84.745  1.00 70.29  ? 178 PHE   D CA    1 
ATOM   5706 C  C     . PHE   C 2 178 ? 139.968 137.447 84.141  1.00 76.35  ? 178 PHE   D C     1 
ATOM   5707 O  O     . PHE   C 2 178 ? 138.766 137.627 84.370  1.00 83.48  ? 178 PHE   D O     1 
ATOM   5708 C  CB    . PHE   C 2 178 ? 141.410 136.656 86.037  1.00 69.96  ? 178 PHE   D CB    1 
ATOM   5709 C  CG    . PHE   C 2 178 ? 140.478 137.044 87.146  1.00 78.34  ? 178 PHE   D CG    1 
ATOM   5710 C  CD1   . PHE   C 2 178 ? 139.394 136.245 87.467  1.00 79.66  ? 178 PHE   D CD1   1 
ATOM   5711 C  CD2   . PHE   C 2 178 ? 140.686 138.205 87.869  1.00 76.31  ? 178 PHE   D CD2   1 
ATOM   5712 C  CE1   . PHE   C 2 178 ? 138.535 136.598 88.488  1.00 76.32  ? 178 PHE   D CE1   1 
ATOM   5713 C  CE2   . PHE   C 2 178 ? 139.830 138.563 88.889  1.00 76.86  ? 178 PHE   D CE2   1 
ATOM   5714 C  CZ    . PHE   C 2 178 ? 138.753 137.759 89.198  1.00 77.93  ? 178 PHE   D CZ    1 
ATOM   5715 N  N     . ALA   C 2 179 ? 140.673 138.264 83.357  1.00 70.46  ? 179 ALA   D N     1 
ATOM   5716 C  CA    . ALA   C 2 179 ? 140.029 139.389 82.687  1.00 68.41  ? 179 ALA   D CA    1 
ATOM   5717 C  C     . ALA   C 2 179 ? 138.971 138.915 81.700  1.00 77.86  ? 179 ALA   D C     1 
ATOM   5718 O  O     . ALA   C 2 179 ? 137.891 139.507 81.606  1.00 83.34  ? 179 ALA   D O     1 
ATOM   5719 C  CB    . ALA   C 2 179 ? 141.077 140.249 81.982  1.00 67.78  ? 179 ALA   D CB    1 
ATOM   5720 N  N     . GLN   C 2 180 ? 139.261 137.848 80.949  1.00 71.10  ? 180 GLN   D N     1 
ATOM   5721 C  CA    . GLN   C 2 180 ? 138.276 137.313 80.013  1.00 66.53  ? 180 GLN   D CA    1 
ATOM   5722 C  C     . GLN   C 2 180 ? 137.056 136.764 80.745  1.00 70.47  ? 180 GLN   D C     1 
ATOM   5723 O  O     . GLN   C 2 180 ? 135.912 136.959 80.306  1.00 79.09  ? 180 GLN   D O     1 
ATOM   5724 C  CB    . GLN   C 2 180 ? 138.913 136.228 79.147  1.00 69.83  ? 180 GLN   D CB    1 
ATOM   5725 C  CG    . GLN   C 2 180 ? 139.078 136.614 77.688  1.00 76.53  ? 180 GLN   D CG    1 
ATOM   5726 C  CD    . GLN   C 2 180 ? 137.767 136.615 76.931  1.00 76.99  ? 180 GLN   D CD    1 
ATOM   5727 O  OE1   . GLN   C 2 180 ? 136.777 136.039 77.380  1.00 74.78  ? 180 GLN   D OE1   1 
ATOM   5728 N  NE2   . GLN   C 2 180 ? 137.754 137.261 75.771  1.00 73.41  ? 180 GLN   D NE2   1 
ATOM   5729 N  N     . LYS   C 2 181 ? 137.279 136.066 81.860  1.00 82.84  ? 181 LYS   D N     1 
ATOM   5730 C  CA    . LYS   C 2 181 ? 136.153 135.561 82.640  1.00 85.83  ? 181 LYS   D CA    1 
ATOM   5731 C  C     . LYS   C 2 181 ? 135.304 136.704 83.189  1.00 88.26  ? 181 LYS   D C     1 
ATOM   5732 O  O     . LYS   C 2 181 ? 134.066 136.642 83.162  1.00 89.37  ? 181 LYS   D O     1 
ATOM   5733 C  CB    . LYS   C 2 181 ? 136.660 134.664 83.767  1.00 83.56  ? 181 LYS   D CB    1 
ATOM   5734 C  CG    . LYS   C 2 181 ? 135.607 134.295 84.791  1.00 88.77  ? 181 LYS   D CG    1 
ATOM   5735 C  CD    . LYS   C 2 181 ? 136.222 133.514 85.933  1.00 88.98  ? 181 LYS   D CD    1 
ATOM   5736 C  CE    . LYS   C 2 181 ? 136.436 132.066 85.533  1.00 89.31  ? 181 LYS   D CE    1 
ATOM   5737 N  NZ    . LYS   C 2 181 ? 135.826 131.121 86.506  1.00 86.09  ? 181 LYS   D NZ    1 
ATOM   5738 N  N     . CYS   C 2 182 ? 135.951 137.763 83.683  1.00 73.27  ? 182 CYS   D N     1 
ATOM   5739 C  CA    . CYS   C 2 182 ? 135.209 138.931 84.147  1.00 72.21  ? 182 CYS   D CA    1 
ATOM   5740 C  C     . CYS   C 2 182 ? 134.455 139.599 83.004  1.00 75.06  ? 182 CYS   D C     1 
ATOM   5741 O  O     . CYS   C 2 182 ? 133.359 140.127 83.203  1.00 80.32  ? 182 CYS   D O     1 
ATOM   5742 C  CB    . CYS   C 2 182 ? 136.152 139.926 84.822  1.00 75.17  ? 182 CYS   D CB    1 
ATOM   5743 S  SG    . CYS   C 2 182 ? 137.022 139.277 86.264  1.00 77.99  ? 182 CYS   D SG    1 
ATOM   5744 N  N     . LEU   C 2 183 ? 135.029 139.596 81.799  1.00 66.65  ? 183 LEU   D N     1 
ATOM   5745 C  CA    . LEU   C 2 183 ? 134.331 140.154 80.644  1.00 68.62  ? 183 LEU   D CA    1 
ATOM   5746 C  C     . LEU   C 2 183 ? 133.062 139.368 80.333  1.00 73.63  ? 183 LEU   D C     1 
ATOM   5747 O  O     . LEU   C 2 183 ? 132.011 139.954 80.040  1.00 79.37  ? 183 LEU   D O     1 
ATOM   5748 C  CB    . LEU   C 2 183 ? 135.260 140.175 79.432  1.00 71.22  ? 183 LEU   D CB    1 
ATOM   5749 C  CG    . LEU   C 2 183 ? 134.879 141.090 78.267  1.00 74.15  ? 183 LEU   D CG    1 
ATOM   5750 C  CD1   . LEU   C 2 183 ? 134.242 142.378 78.768  1.00 73.54  ? 183 LEU   D CD1   1 
ATOM   5751 C  CD2   . LEU   C 2 183 ? 136.095 141.387 77.407  1.00 72.55  ? 183 LEU   D CD2   1 
ATOM   5752 N  N     . ASP   C 2 184 ? 133.143 138.037 80.388  1.00 79.89  ? 184 ASP   D N     1 
ATOM   5753 C  CA    . ASP   C 2 184 ? 131.946 137.223 80.187  1.00 81.67  ? 184 ASP   D CA    1 
ATOM   5754 C  C     . ASP   C 2 184 ? 130.903 137.501 81.265  1.00 83.94  ? 184 ASP   D C     1 
ATOM   5755 O  O     . ASP   C 2 184 ? 129.701 137.612 80.974  1.00 84.34  ? 184 ASP   D O     1 
ATOM   5756 C  CB    . ASP   C 2 184 ? 132.315 135.741 80.162  1.00 81.99  ? 184 ASP   D CB    1 
ATOM   5757 C  CG    . ASP   C 2 184 ? 133.260 135.395 79.032  1.00 87.31  ? 184 ASP   D CG    1 
ATOM   5758 O  OD1   . ASP   C 2 184 ? 133.430 136.233 78.122  1.00 81.64  ? 184 ASP   D OD1   1 
ATOM   5759 O  OD2   . ASP   C 2 184 ? 133.832 134.285 79.050  1.00 89.29  ? 184 ASP   D OD2   1 
ATOM   5760 N  N     . LYS   C 2 185 ? 131.345 137.622 82.519  1.00 80.74  ? 185 LYS   D N     1 
ATOM   5761 C  CA    . LYS   C 2 185 ? 130.414 137.941 83.599  1.00 79.04  ? 185 LYS   D CA    1 
ATOM   5762 C  C     . LYS   C 2 185 ? 129.768 139.305 83.385  1.00 78.30  ? 185 LYS   D C     1 
ATOM   5763 O  O     . LYS   C 2 185 ? 128.584 139.494 83.686  1.00 81.78  ? 185 LYS   D O     1 
ATOM   5764 C  CB    . LYS   C 2 185 ? 131.134 137.892 84.946  1.00 79.14  ? 185 LYS   D CB    1 
ATOM   5765 C  CG    . LYS   C 2 185 ? 130.251 137.449 86.101  1.00 81.89  ? 185 LYS   D CG    1 
ATOM   5766 C  CD    . LYS   C 2 185 ? 129.955 135.960 86.024  1.00 82.81  ? 185 LYS   D CD    1 
ATOM   5767 C  CE    . LYS   C 2 185 ? 128.688 135.604 86.782  1.00 80.26  ? 185 LYS   D CE    1 
ATOM   5768 N  NZ    . LYS   C 2 185 ? 127.864 134.609 86.042  1.00 79.71  ? 185 LYS   D NZ    1 
ATOM   5769 N  N     . ILE   C 2 186 ? 130.531 140.271 82.870  1.00 83.47  ? 186 ILE   D N     1 
ATOM   5770 C  CA    . ILE   C 2 186 ? 129.990 141.603 82.611  1.00 83.94  ? 186 ILE   D CA    1 
ATOM   5771 C  C     . ILE   C 2 186 ? 128.960 141.553 81.491  1.00 84.04  ? 186 ILE   D C     1 
ATOM   5772 O  O     . ILE   C 2 186 ? 127.939 142.246 81.538  1.00 87.24  ? 186 ILE   D O     1 
ATOM   5773 C  CB    . ILE   C 2 186 ? 131.127 142.595 82.302  1.00 84.11  ? 186 ILE   D CB    1 
ATOM   5774 C  CG1   . ILE   C 2 186 ? 131.957 142.878 83.558  1.00 82.09  ? 186 ILE   D CG1   1 
ATOM   5775 C  CG2   . ILE   C 2 186 ? 130.580 143.895 81.733  1.00 82.81  ? 186 ILE   D CG2   1 
ATOM   5776 C  CD1   . ILE   C 2 186 ? 131.162 142.870 84.847  1.00 82.16  ? 186 ILE   D CD1   1 
ATOM   5777 N  N     . TYR   C 2 187 ? 129.209 140.740 80.460  1.00 98.86  ? 187 TYR   D N     1 
ATOM   5778 C  CA    . TYR   C 2 187 ? 128.200 140.563 79.417  1.00 100.92 ? 187 TYR   D CA    1 
ATOM   5779 C  C     . TYR   C 2 187 ? 126.915 139.972 79.988  1.00 104.99 ? 187 TYR   D C     1 
ATOM   5780 O  O     . TYR   C 2 187 ? 125.808 140.423 79.657  1.00 105.29 ? 187 TYR   D O     1 
ATOM   5781 C  CB    . TYR   C 2 187 ? 128.737 139.679 78.293  1.00 101.31 ? 187 TYR   D CB    1 
ATOM   5782 C  CG    . TYR   C 2 187 ? 129.870 140.291 77.506  1.00 102.53 ? 187 TYR   D CG    1 
ATOM   5783 C  CD1   . TYR   C 2 187 ? 129.971 141.668 77.353  1.00 103.37 ? 187 TYR   D CD1   1 
ATOM   5784 C  CD2   . TYR   C 2 187 ? 130.831 139.493 76.898  1.00 101.49 ? 187 TYR   D CD2   1 
ATOM   5785 C  CE1   . TYR   C 2 187 ? 131.003 142.232 76.628  1.00 104.71 ? 187 TYR   D CE1   1 
ATOM   5786 C  CE2   . TYR   C 2 187 ? 131.865 140.048 76.171  1.00 101.51 ? 187 TYR   D CE2   1 
ATOM   5787 C  CZ    . TYR   C 2 187 ? 131.946 141.417 76.039  1.00 105.11 ? 187 TYR   D CZ    1 
ATOM   5788 O  OH    . TYR   C 2 187 ? 132.976 141.973 75.316  1.00 105.03 ? 187 TYR   D OH    1 
ATOM   5789 N  N     . GLU   C 2 188 ? 127.041 138.967 80.858  1.00 108.30 ? 188 GLU   D N     1 
ATOM   5790 C  CA    . GLU   C 2 188 ? 125.851 138.390 81.480  1.00 105.00 ? 188 GLU   D CA    1 
ATOM   5791 C  C     . GLU   C 2 188 ? 125.115 139.419 82.333  1.00 106.29 ? 188 GLU   D C     1 
ATOM   5792 O  O     . GLU   C 2 188 ? 123.879 139.479 82.325  1.00 109.00 ? 188 GLU   D O     1 
ATOM   5793 C  CB    . GLU   C 2 188 ? 126.231 137.170 82.317  1.00 105.56 ? 188 GLU   D CB    1 
ATOM   5794 C  CG    . GLU   C 2 188 ? 126.324 135.882 81.518  1.00 108.09 ? 188 GLU   D CG    1 
ATOM   5795 C  CD    . GLU   C 2 188 ? 126.324 134.651 82.400  1.00 109.54 ? 188 GLU   D CD    1 
ATOM   5796 O  OE1   . GLU   C 2 188 ? 127.038 134.652 83.424  1.00 106.38 ? 188 GLU   D OE1   1 
ATOM   5797 O  OE2   . GLU   C 2 188 ? 125.609 133.681 82.066  1.00 110.01 ? 188 GLU   D OE2   1 
ATOM   5798 N  N     . PHE   C 2 189 ? 125.859 140.241 83.077  1.00 95.82  ? 189 PHE   D N     1 
ATOM   5799 C  CA    . PHE   C 2 189 ? 125.230 141.263 83.909  1.00 93.77  ? 189 PHE   D CA    1 
ATOM   5800 C  C     . PHE   C 2 189 ? 124.546 142.327 83.059  1.00 90.00  ? 189 PHE   D C     1 
ATOM   5801 O  O     . PHE   C 2 189 ? 123.496 142.856 83.441  1.00 89.18  ? 189 PHE   D O     1 
ATOM   5802 C  CB    . PHE   C 2 189 ? 126.268 141.895 84.834  1.00 92.17  ? 189 PHE   D CB    1 
ATOM   5803 C  CG    . PHE   C 2 189 ? 126.374 141.223 86.171  1.00 93.15  ? 189 PHE   D CG    1 
ATOM   5804 C  CD1   . PHE   C 2 189 ? 126.439 139.843 86.262  1.00 92.38  ? 189 PHE   D CD1   1 
ATOM   5805 C  CD2   . PHE   C 2 189 ? 126.406 141.969 87.337  1.00 93.52  ? 189 PHE   D CD2   1 
ATOM   5806 C  CE1   . PHE   C 2 189 ? 126.535 139.220 87.489  1.00 93.03  ? 189 PHE   D CE1   1 
ATOM   5807 C  CE2   . PHE   C 2 189 ? 126.502 141.350 88.568  1.00 94.11  ? 189 PHE   D CE2   1 
ATOM   5808 C  CZ    . PHE   C 2 189 ? 126.567 139.974 88.644  1.00 93.91  ? 189 PHE   D CZ    1 
ATOM   5809 N  N     . LYS   C 2 190 ? 125.133 142.663 81.908  1.00 102.35 ? 190 LYS   D N     1 
ATOM   5810 C  CA    . LYS   C 2 190 ? 124.470 143.566 80.973  1.00 105.00 ? 190 LYS   D CA    1 
ATOM   5811 C  C     . LYS   C 2 190 ? 123.167 142.964 80.475  1.00 106.86 ? 190 LYS   D C     1 
ATOM   5812 O  O     . LYS   C 2 190 ? 122.164 143.671 80.318  1.00 105.21 ? 190 LYS   D O     1 
ATOM   5813 C  CB    . LYS   C 2 190 ? 125.390 143.880 79.794  1.00 106.57 ? 190 LYS   D CB    1 
ATOM   5814 C  CG    . LYS   C 2 190 ? 126.540 144.811 80.112  1.00 106.08 ? 190 LYS   D CG    1 
ATOM   5815 C  CD    . LYS   C 2 190 ? 127.372 145.066 78.868  1.00 107.98 ? 190 LYS   D CD    1 
ATOM   5816 C  CE    . LYS   C 2 190 ? 126.617 145.925 77.869  1.00 104.56 ? 190 LYS   D CE    1 
ATOM   5817 N  NZ    . LYS   C 2 190 ? 127.472 146.308 76.713  1.00 103.66 ? 190 LYS   D NZ    1 
ATOM   5818 N  N     . GLU   C 2 191 ? 123.167 141.656 80.208  1.00 116.22 ? 191 GLU   D N     1 
ATOM   5819 C  CA    . GLU   C 2 191 ? 121.920 140.982 79.857  1.00 117.34 ? 191 GLU   D CA    1 
ATOM   5820 C  C     . GLU   C 2 191 ? 120.917 141.044 81.004  1.00 117.89 ? 191 GLU   D C     1 
ATOM   5821 O  O     . GLU   C 2 191 ? 119.704 141.109 80.775  1.00 116.41 ? 191 GLU   D O     1 
ATOM   5822 C  CB    . GLU   C 2 191 ? 122.199 139.534 79.456  1.00 114.81 ? 191 GLU   D CB    1 
ATOM   5823 C  CG    . GLU   C 2 191 ? 122.559 139.363 77.988  1.00 117.18 ? 191 GLU   D CG    1 
ATOM   5824 C  CD    . GLU   C 2 191 ? 122.052 140.504 77.124  1.00 119.74 ? 191 GLU   D CD    1 
ATOM   5825 O  OE1   . GLU   C 2 191 ? 122.876 141.337 76.692  1.00 116.79 ? 191 GLU   D OE1   1 
ATOM   5826 O  OE2   . GLU   C 2 191 ? 120.830 140.565 76.870  1.00 120.24 ? 191 GLU   D OE2   1 
ATOM   5827 N  N     . GLN   C 2 192 ? 121.406 141.031 82.248  1.00 112.21 ? 192 GLN   D N     1 
ATOM   5828 C  CA    . GLN   C 2 192 ? 120.517 141.153 83.399  1.00 107.20 ? 192 GLN   D CA    1 
ATOM   5829 C  C     . GLN   C 2 192 ? 120.167 142.602 83.721  1.00 107.87 ? 192 GLN   D C     1 
ATOM   5830 O  O     . GLN   C 2 192 ? 119.533 142.856 84.751  1.00 106.32 ? 192 GLN   D O     1 
ATOM   5831 C  CB    . GLN   C 2 192 ? 121.139 140.491 84.628  1.00 106.22 ? 192 GLN   D CB    1 
ATOM   5832 C  CG    . GLN   C 2 192 ? 121.161 138.974 84.584  1.00 108.41 ? 192 GLN   D CG    1 
ATOM   5833 C  CD    . GLN   C 2 192 ? 122.184 138.378 85.531  1.00 110.56 ? 192 GLN   D CD    1 
ATOM   5834 O  OE1   . GLN   C 2 192 ? 122.071 138.514 86.750  1.00 107.79 ? 192 GLN   D OE1   1 
ATOM   5835 N  NE2   . GLN   C 2 192 ? 123.186 137.707 84.976  1.00 109.15 ? 192 GLN   D NE2   1 
ATOM   5836 N  N     . ASN   C 2 193 ? 120.588 143.553 82.882  1.00 111.98 ? 193 ASN   D N     1 
ATOM   5837 C  CA    . ASN   C 2 193 ? 120.258 144.969 83.032  1.00 110.45 ? 193 ASN   D CA    1 
ATOM   5838 C  C     . ASN   C 2 193 ? 120.837 145.579 84.304  1.00 110.76 ? 193 ASN   D C     1 
ATOM   5839 O  O     . ASN   C 2 193 ? 120.229 146.475 84.897  1.00 112.25 ? 193 ASN   D O     1 
ATOM   5840 C  CB    . ASN   C 2 193 ? 118.741 145.181 82.994  1.00 110.24 ? 193 ASN   D CB    1 
ATOM   5841 C  CG    . ASN   C 2 193 ? 118.211 145.349 81.585  1.00 112.89 ? 193 ASN   D CG    1 
ATOM   5842 O  OD1   . ASN   C 2 193 ? 117.370 146.209 81.324  1.00 110.85 ? 193 ASN   D OD1   1 
ATOM   5843 N  ND2   . ASN   C 2 193 ? 118.706 144.529 80.664  1.00 112.47 ? 193 ASN   D ND2   1 
ATOM   5844 N  N     . LYS   C 2 194 ? 121.999 145.099 84.739  1.00 105.03 ? 194 LYS   D N     1 
ATOM   5845 C  CA    . LYS   C 2 194 ? 122.719 145.769 85.813  1.00 103.94 ? 194 LYS   D CA    1 
ATOM   5846 C  C     . LYS   C 2 194 ? 123.550 146.920 85.256  1.00 102.75 ? 194 LYS   D C     1 
ATOM   5847 O  O     . LYS   C 2 194 ? 123.807 147.006 84.052  1.00 105.07 ? 194 LYS   D O     1 
ATOM   5848 C  CB    . LYS   C 2 194 ? 123.615 144.779 86.560  1.00 105.57 ? 194 LYS   D CB    1 
ATOM   5849 C  CG    . LYS   C 2 194 ? 123.058 143.368 86.637  1.00 104.79 ? 194 LYS   D CG    1 
ATOM   5850 C  CD    . LYS   C 2 194 ? 121.953 143.281 87.677  1.00 105.28 ? 194 LYS   D CD    1 
ATOM   5851 C  CE    . LYS   C 2 194 ? 121.563 141.840 87.965  1.00 106.79 ? 194 LYS   D CE    1 
ATOM   5852 N  NZ    . LYS   C 2 194 ? 122.730 140.921 87.907  1.00 103.50 ? 194 LYS   D NZ    1 
ATOM   5853 N  N     . THR   C 2 195 ? 123.968 147.816 86.146  1.00 93.29  ? 195 THR   D N     1 
ATOM   5854 C  CA    . THR   C 2 195 ? 124.797 148.958 85.783  1.00 96.69  ? 195 THR   D CA    1 
ATOM   5855 C  C     . THR   C 2 195 ? 126.192 148.781 86.369  1.00 97.25  ? 195 THR   D C     1 
ATOM   5856 O  O     . THR   C 2 195 ? 126.341 148.584 87.580  1.00 94.85  ? 195 THR   D O     1 
ATOM   5857 C  CB    . THR   C 2 195 ? 124.176 150.266 86.275  1.00 98.52  ? 195 THR   D CB    1 
ATOM   5858 O  OG1   . THR   C 2 195 ? 123.046 150.597 85.458  1.00 98.46  ? 195 THR   D OG1   1 
ATOM   5859 C  CG2   . THR   C 2 195 ? 125.187 151.399 86.206  1.00 94.39  ? 195 THR   D CG2   1 
ATOM   5860 N  N     . ILE   C 2 196 ? 127.207 148.864 85.509  1.00 88.14  ? 196 ILE   D N     1 
ATOM   5861 C  CA    . ILE   C 2 196 ? 128.591 148.604 85.885  1.00 85.11  ? 196 ILE   D CA    1 
ATOM   5862 C  C     . ILE   C 2 196 ? 129.428 149.843 85.605  1.00 83.67  ? 196 ILE   D C     1 
ATOM   5863 O  O     . ILE   C 2 196 ? 129.370 150.413 84.510  1.00 84.24  ? 196 ILE   D O     1 
ATOM   5864 C  CB    . ILE   C 2 196 ? 129.169 147.385 85.135  1.00 85.37  ? 196 ILE   D CB    1 
ATOM   5865 C  CG1   . ILE   C 2 196 ? 128.122 146.276 85.001  1.00 81.69  ? 196 ILE   D CG1   1 
ATOM   5866 C  CG2   . ILE   C 2 196 ? 130.411 146.867 85.839  1.00 85.62  ? 196 ILE   D CG2   1 
ATOM   5867 C  CD1   . ILE   C 2 196 ? 127.444 146.229 83.649  1.00 82.27  ? 196 ILE   D CD1   1 
ATOM   5868 N  N     . PHE   C 2 197 ? 130.205 150.255 86.602  1.00 79.94  ? 197 PHE   D N     1 
ATOM   5869 C  CA    . PHE   C 2 197 ? 131.200 151.309 86.468  1.00 79.17  ? 197 PHE   D CA    1 
ATOM   5870 C  C     . PHE   C 2 197 ? 132.580 150.672 86.519  1.00 78.18  ? 197 PHE   D C     1 
ATOM   5871 O  O     . PHE   C 2 197 ? 132.844 149.837 87.390  1.00 77.26  ? 197 PHE   D O     1 
ATOM   5872 C  CB    . PHE   C 2 197 ? 131.057 152.353 87.578  1.00 80.73  ? 197 PHE   D CB    1 
ATOM   5873 C  CG    . PHE   C 2 197 ? 129.930 153.322 87.364  1.00 80.70  ? 197 PHE   D CG    1 
ATOM   5874 C  CD1   . PHE   C 2 197 ? 128.628 152.969 87.672  1.00 83.04  ? 197 PHE   D CD1   1 
ATOM   5875 C  CD2   . PHE   C 2 197 ? 130.173 154.588 86.861  1.00 81.62  ? 197 PHE   D CD2   1 
ATOM   5876 C  CE1   . PHE   C 2 197 ? 127.590 153.859 87.479  1.00 83.51  ? 197 PHE   D CE1   1 
ATOM   5877 C  CE2   . PHE   C 2 197 ? 129.139 155.482 86.666  1.00 81.74  ? 197 PHE   D CE2   1 
ATOM   5878 C  CZ    . PHE   C 2 197 ? 127.845 155.116 86.975  1.00 81.32  ? 197 PHE   D CZ    1 
ATOM   5879 N  N     . PHE   C 2 198 ? 133.450 151.050 85.586  1.00 57.95  ? 198 PHE   D N     1 
ATOM   5880 C  CA    . PHE   C 2 198 ? 134.767 150.438 85.448  1.00 55.78  ? 198 PHE   D CA    1 
ATOM   5881 C  C     . PHE   C 2 198 ? 135.826 151.529 85.424  1.00 54.76  ? 198 PHE   D C     1 
ATOM   5882 O  O     . PHE   C 2 198 ? 135.753 152.446 84.602  1.00 60.22  ? 198 PHE   D O     1 
ATOM   5883 C  CB    . PHE   C 2 198 ? 134.838 149.588 84.175  1.00 53.37  ? 198 PHE   D CB    1 
ATOM   5884 C  CG    . PHE   C 2 198 ? 136.146 148.877 83.987  1.00 60.78  ? 198 PHE   D CG    1 
ATOM   5885 C  CD1   . PHE   C 2 198 ? 136.617 147.996 84.945  1.00 59.65  ? 198 PHE   D CD1   1 
ATOM   5886 C  CD2   . PHE   C 2 198 ? 136.902 149.084 82.847  1.00 58.28  ? 198 PHE   D CD2   1 
ATOM   5887 C  CE1   . PHE   C 2 198 ? 137.819 147.340 84.773  1.00 55.63  ? 198 PHE   D CE1   1 
ATOM   5888 C  CE2   . PHE   C 2 198 ? 138.103 148.430 82.668  1.00 53.06  ? 198 PHE   D CE2   1 
ATOM   5889 C  CZ    . PHE   C 2 198 ? 138.561 147.557 83.632  1.00 56.67  ? 198 PHE   D CZ    1 
ATOM   5890 N  N     . VAL   C 2 199 ? 136.811 151.428 86.316  1.00 53.80  ? 199 VAL   D N     1 
ATOM   5891 C  CA    . VAL   C 2 199 ? 137.925 152.367 86.371  1.00 53.44  ? 199 VAL   D CA    1 
ATOM   5892 C  C     . VAL   C 2 199 ? 139.221 151.585 86.207  1.00 56.15  ? 199 VAL   D C     1 
ATOM   5893 O  O     . VAL   C 2 199 ? 139.461 150.617 86.937  1.00 62.09  ? 199 VAL   D O     1 
ATOM   5894 C  CB    . VAL   C 2 199 ? 137.937 153.162 87.690  1.00 55.40  ? 199 VAL   D CB    1 
ATOM   5895 C  CG1   . VAL   C 2 199 ? 138.994 154.251 87.645  1.00 57.17  ? 199 VAL   D CG1   1 
ATOM   5896 C  CG2   . VAL   C 2 199 ? 136.566 153.756 87.967  1.00 55.64  ? 199 VAL   D CG2   1 
ATOM   5897 N  N     . SER   C 2 200 ? 140.050 152.005 85.255  1.00 58.19  ? 200 SER   D N     1 
ATOM   5898 C  CA    . SER   C 2 200 ? 141.341 151.367 85.038  1.00 59.70  ? 200 SER   D CA    1 
ATOM   5899 C  C     . SER   C 2 200 ? 142.249 152.324 84.283  1.00 60.06  ? 200 SER   D C     1 
ATOM   5900 O  O     . SER   C 2 200 ? 141.786 153.218 83.570  1.00 67.00  ? 200 SER   D O     1 
ATOM   5901 C  CB    . SER   C 2 200 ? 141.199 150.049 84.271  1.00 59.76  ? 200 SER   D CB    1 
ATOM   5902 O  OG    . SER   C 2 200 ? 141.577 150.208 82.915  1.00 57.11  ? 200 SER   D OG    1 
ATOM   5903 N  N     . HIS   C 2 201 ? 143.555 152.121 84.450  1.00 58.55  ? 201 HIS   D N     1 
ATOM   5904 C  CA    . HIS   C 2 201 ? 144.569 152.874 83.727  1.00 56.17  ? 201 HIS   D CA    1 
ATOM   5905 C  C     . HIS   C 2 201 ? 145.090 152.124 82.508  1.00 56.91  ? 201 HIS   D C     1 
ATOM   5906 O  O     . HIS   C 2 201 ? 146.021 152.599 81.850  1.00 60.20  ? 201 HIS   D O     1 
ATOM   5907 C  CB    . HIS   C 2 201 ? 145.725 153.234 84.662  1.00 54.33  ? 201 HIS   D CB    1 
ATOM   5908 C  CG    . HIS   C 2 201 ? 145.457 154.431 85.521  1.00 62.90  ? 201 HIS   D CG    1 
ATOM   5909 N  ND1   . HIS   C 2 201 ? 145.287 155.696 85.002  1.00 63.29  ? 201 HIS   D ND1   1 
ATOM   5910 C  CD2   . HIS   C 2 201 ? 145.333 154.555 86.863  1.00 59.33  ? 201 HIS   D CD2   1 
ATOM   5911 C  CE1   . HIS   C 2 201 ? 145.069 156.548 85.988  1.00 60.99  ? 201 HIS   D CE1   1 
ATOM   5912 N  NE2   . HIS   C 2 201 ? 145.092 155.882 87.127  1.00 58.68  ? 201 HIS   D NE2   1 
ATOM   5913 N  N     . ASN   C 2 202 ? 144.516 150.964 82.200  1.00 65.60  ? 202 ASN   D N     1 
ATOM   5914 C  CA    . ASN   C 2 202 ? 144.830 150.209 80.993  1.00 65.42  ? 202 ASN   D CA    1 
ATOM   5915 C  C     . ASN   C 2 202 ? 143.782 150.562 79.944  1.00 68.52  ? 202 ASN   D C     1 
ATOM   5916 O  O     . ASN   C 2 202 ? 142.616 150.178 80.070  1.00 77.03  ? 202 ASN   D O     1 
ATOM   5917 C  CB    . ASN   C 2 202 ? 144.844 148.709 81.282  1.00 66.38  ? 202 ASN   D CB    1 
ATOM   5918 C  CG    . ASN   C 2 202 ? 145.513 147.905 80.187  1.00 69.62  ? 202 ASN   D CG    1 
ATOM   5919 O  OD1   . ASN   C 2 202 ? 145.637 148.361 79.051  1.00 70.89  ? 202 ASN   D OD1   1 
ATOM   5920 N  ND2   . ASN   C 2 202 ? 145.947 146.697 80.523  1.00 64.64  ? 202 ASN   D ND2   1 
ATOM   5921 N  N     . LEU   C 2 203 ? 144.196 151.298 78.912  1.00 67.20  ? 203 LEU   D N     1 
ATOM   5922 C  CA    . LEU   C 2 203 ? 143.246 151.812 77.935  1.00 68.22  ? 203 LEU   D CA    1 
ATOM   5923 C  C     . LEU   C 2 203 ? 142.679 150.730 77.025  1.00 72.29  ? 203 LEU   D C     1 
ATOM   5924 O  O     . LEU   C 2 203 ? 141.549 150.876 76.548  1.00 75.55  ? 203 LEU   D O     1 
ATOM   5925 C  CB    . LEU   C 2 203 ? 143.897 152.912 77.095  1.00 73.73  ? 203 LEU   D CB    1 
ATOM   5926 C  CG    . LEU   C 2 203 ? 144.157 154.239 77.816  1.00 76.38  ? 203 LEU   D CG    1 
ATOM   5927 C  CD1   . LEU   C 2 203 ? 144.300 155.376 76.819  1.00 71.63  ? 203 LEU   D CD1   1 
ATOM   5928 C  CD2   . LEU   C 2 203 ? 143.060 154.545 78.828  1.00 68.03  ? 203 LEU   D CD2   1 
ATOM   5929 N  N     . GLY   C 2 204 ? 143.425 149.653 76.772  1.00 72.28  ? 204 GLY   D N     1 
ATOM   5930 C  CA    . GLY   C 2 204 ? 142.865 148.545 76.014  1.00 69.39  ? 204 GLY   D CA    1 
ATOM   5931 C  C     . GLY   C 2 204 ? 141.749 147.838 76.761  1.00 71.22  ? 204 GLY   D C     1 
ATOM   5932 O  O     . GLY   C 2 204 ? 140.724 147.479 76.172  1.00 74.31  ? 204 GLY   D O     1 
ATOM   5933 N  N     . GLN   C 2 205 ? 141.933 147.630 78.067  1.00 67.88  ? 205 GLN   D N     1 
ATOM   5934 C  CA    . GLN   C 2 205 ? 140.875 147.047 78.882  1.00 64.37  ? 205 GLN   D CA    1 
ATOM   5935 C  C     . GLN   C 2 205 ? 139.651 147.953 78.926  1.00 70.27  ? 205 GLN   D C     1 
ATOM   5936 O  O     . GLN   C 2 205 ? 138.515 147.471 78.886  1.00 75.95  ? 205 GLN   D O     1 
ATOM   5937 C  CB    . GLN   C 2 205 ? 141.394 146.772 80.292  1.00 66.32  ? 205 GLN   D CB    1 
ATOM   5938 C  CG    . GLN   C 2 205 ? 141.591 145.301 80.606  1.00 66.81  ? 205 GLN   D CG    1 
ATOM   5939 C  CD    . GLN   C 2 205 ? 141.957 145.059 82.055  1.00 70.77  ? 205 GLN   D CD    1 
ATOM   5940 O  OE1   . GLN   C 2 205 ? 141.549 145.808 82.941  1.00 69.89  ? 205 GLN   D OE1   1 
ATOM   5941 N  NE2   . GLN   C 2 205 ? 142.728 144.010 82.304  1.00 74.37  ? 205 GLN   D NE2   1 
ATOM   5942 N  N     . VAL   C 2 206 ? 139.865 149.267 79.011  1.00 68.45  ? 206 VAL   D N     1 
ATOM   5943 C  CA    . VAL   C 2 206 ? 138.749 150.208 78.975  1.00 67.46  ? 206 VAL   D CA    1 
ATOM   5944 C  C     . VAL   C 2 206 ? 138.025 150.124 77.637  1.00 63.09  ? 206 VAL   D C     1 
ATOM   5945 O  O     . VAL   C 2 206 ? 136.789 150.132 77.583  1.00 71.10  ? 206 VAL   D O     1 
ATOM   5946 C  CB    . VAL   C 2 206 ? 139.246 151.636 79.266  1.00 66.35  ? 206 VAL   D CB    1 
ATOM   5947 C  CG1   . VAL   C 2 206 ? 138.187 152.660 78.892  1.00 65.28  ? 206 VAL   D CG1   1 
ATOM   5948 C  CG2   . VAL   C 2 206 ? 139.630 151.775 80.728  1.00 65.47  ? 206 VAL   D CG2   1 
ATOM   5949 N  N     . ARG   C 2 207 ? 138.777 150.042 76.538  1.00 70.25  ? 207 ARG   D N     1 
ATOM   5950 C  CA    . ARG   C 2 207 ? 138.162 149.950 75.219  1.00 75.91  ? 207 ARG   D CA    1 
ATOM   5951 C  C     . ARG   C 2 207 ? 137.336 148.678 75.075  1.00 79.21  ? 207 ARG   D C     1 
ATOM   5952 O  O     . ARG   C 2 207 ? 136.225 148.712 74.532  1.00 78.94  ? 207 ARG   D O     1 
ATOM   5953 C  CB    . ARG   C 2 207 ? 139.237 150.014 74.134  1.00 76.24  ? 207 ARG   D CB    1 
ATOM   5954 C  CG    . ARG   C 2 207 ? 138.721 149.734 72.733  1.00 76.35  ? 207 ARG   D CG    1 
ATOM   5955 C  CD    . ARG   C 2 207 ? 138.800 150.966 71.850  1.00 76.08  ? 207 ARG   D CD    1 
ATOM   5956 N  NE    . ARG   C 2 207 ? 140.091 151.633 71.961  1.00 80.02  ? 207 ARG   D NE    1 
ATOM   5957 C  CZ    . ARG   C 2 207 ? 140.361 152.831 71.462  1.00 80.91  ? 207 ARG   D CZ    1 
ATOM   5958 N  NH1   . ARG   C 2 207 ? 139.449 153.524 70.800  1.00 76.73  ? 207 ARG   D NH1   1 
ATOM   5959 N  NH2   . ARG   C 2 207 ? 141.576 153.345 71.629  1.00 81.41  ? 207 ARG   D NH2   1 
ATOM   5960 N  N     . GLN   C 2 208 ? 137.855 147.548 75.551  1.00 85.40  ? 208 GLN   D N     1 
ATOM   5961 C  CA    . GLN   C 2 208 ? 137.149 146.282 75.402  1.00 79.89  ? 208 GLN   D CA    1 
ATOM   5962 C  C     . GLN   C 2 208 ? 136.127 146.026 76.503  1.00 80.91  ? 208 GLN   D C     1 
ATOM   5963 O  O     . GLN   C 2 208 ? 135.410 145.021 76.434  1.00 82.79  ? 208 GLN   D O     1 
ATOM   5964 C  CB    . GLN   C 2 208 ? 138.145 145.117 75.350  1.00 77.36  ? 208 GLN   D CB    1 
ATOM   5965 C  CG    . GLN   C 2 208 ? 138.705 144.702 76.696  1.00 79.46  ? 208 GLN   D CG    1 
ATOM   5966 C  CD    . GLN   C 2 208 ? 140.006 143.936 76.568  1.00 84.03  ? 208 GLN   D CD    1 
ATOM   5967 O  OE1   . GLN   C 2 208 ? 140.666 143.982 75.531  1.00 83.98  ? 208 GLN   D OE1   1 
ATOM   5968 N  NE2   . GLN   C 2 208 ? 140.380 143.222 77.623  1.00 85.62  ? 208 GLN   D NE2   1 
ATOM   5969 N  N     . PHE   C 2 209 ? 136.035 146.897 77.506  1.00 75.49  ? 209 PHE   D N     1 
ATOM   5970 C  CA    . PHE   C 2 209 ? 135.086 146.734 78.602  1.00 71.58  ? 209 PHE   D CA    1 
ATOM   5971 C  C     . PHE   C 2 209 ? 133.937 147.735 78.547  1.00 71.99  ? 209 PHE   D C     1 
ATOM   5972 O  O     . PHE   C 2 209 ? 132.774 147.350 78.693  1.00 74.97  ? 209 PHE   D O     1 
ATOM   5973 C  CB    . PHE   C 2 209 ? 135.810 146.868 79.948  1.00 67.65  ? 209 PHE   D CB    1 
ATOM   5974 C  CG    . PHE   C 2 209 ? 136.238 145.560 80.546  1.00 69.83  ? 209 PHE   D CG    1 
ATOM   5975 C  CD1   . PHE   C 2 209 ? 137.189 144.774 79.921  1.00 71.99  ? 209 PHE   D CD1   1 
ATOM   5976 C  CD2   . PHE   C 2 209 ? 135.695 145.123 81.741  1.00 70.85  ? 209 PHE   D CD2   1 
ATOM   5977 C  CE1   . PHE   C 2 209 ? 137.587 143.572 80.474  1.00 70.76  ? 209 PHE   D CE1   1 
ATOM   5978 C  CE2   . PHE   C 2 209 ? 136.088 143.923 82.299  1.00 71.85  ? 209 PHE   D CE2   1 
ATOM   5979 C  CZ    . PHE   C 2 209 ? 137.035 143.147 81.665  1.00 70.74  ? 209 PHE   D CZ    1 
ATOM   5980 N  N     . CYS   C 2 210 ? 134.240 149.011 78.338  1.00 84.40  ? 210 CYS   D N     1 
ATOM   5981 C  CA    . CYS   C 2 210 ? 133.271 150.078 78.524  1.00 83.96  ? 210 CYS   D CA    1 
ATOM   5982 C  C     . CYS   C 2 210 ? 132.545 150.418 77.226  1.00 85.20  ? 210 CYS   D C     1 
ATOM   5983 O  O     . CYS   C 2 210 ? 132.982 150.073 76.126  1.00 85.92  ? 210 CYS   D O     1 
ATOM   5984 C  CB    . CYS   C 2 210 ? 133.959 151.327 79.074  1.00 81.59  ? 210 CYS   D CB    1 
ATOM   5985 S  SG    . CYS   C 2 210 ? 134.885 151.046 80.597  1.00 95.02  ? 210 CYS   D SG    1 
ATOM   5986 N  N     . THR   C 2 211 ? 131.413 151.110 77.379  1.00 88.50  ? 211 THR   D N     1 
ATOM   5987 C  CA    . THR   C 2 211 ? 130.634 151.614 76.257  1.00 89.60  ? 211 THR   D CA    1 
ATOM   5988 C  C     . THR   C 2 211 ? 130.394 153.116 76.303  1.00 87.91  ? 211 THR   D C     1 
ATOM   5989 O  O     . THR   C 2 211 ? 130.101 153.705 75.256  1.00 86.30  ? 211 THR   D O     1 
ATOM   5990 C  CB    . THR   C 2 211 ? 129.272 150.904 76.178  1.00 88.34  ? 211 THR   D CB    1 
ATOM   5991 O  OG1   . THR   C 2 211 ? 128.585 151.043 77.427  1.00 85.24  ? 211 THR   D OG1   1 
ATOM   5992 C  CG2   . THR   C 2 211 ? 129.457 149.428 75.865  1.00 86.34  ? 211 THR   D CG2   1 
ATOM   5993 N  N     . LYS   C 2 212 ? 130.500 153.747 77.471  1.00 86.83  ? 212 LYS   D N     1 
ATOM   5994 C  CA    . LYS   C 2 212 ? 130.416 155.194 77.601  1.00 84.77  ? 212 LYS   D CA    1 
ATOM   5995 C  C     . LYS   C 2 212 ? 131.578 155.675 78.455  1.00 86.92  ? 212 LYS   D C     1 
ATOM   5996 O  O     . LYS   C 2 212 ? 132.097 154.930 79.290  1.00 87.68  ? 212 LYS   D O     1 
ATOM   5997 C  CB    . LYS   C 2 212 ? 129.084 155.630 78.223  1.00 87.44  ? 212 LYS   D CB    1 
ATOM   5998 C  CG    . LYS   C 2 212 ? 128.032 156.029 77.204  1.00 90.41  ? 212 LYS   D CG    1 
ATOM   5999 C  CD    . LYS   C 2 212 ? 126.736 156.443 77.874  1.00 91.14  ? 212 LYS   D CD    1 
ATOM   6000 C  CE    . LYS   C 2 212 ? 125.708 155.329 77.804  1.00 91.23  ? 212 LYS   D CE    1 
ATOM   6001 N  NZ    . LYS   C 2 212 ? 124.377 155.762 78.312  1.00 91.88  ? 212 LYS   D NZ    1 
ATOM   6002 N  N     . ILE   C 2 213 ? 131.996 156.920 78.240  1.00 74.81  ? 213 ILE   D N     1 
ATOM   6003 C  CA    . ILE   C 2 213 ? 133.197 157.458 78.868  1.00 70.92  ? 213 ILE   D CA    1 
ATOM   6004 C  C     . ILE   C 2 213 ? 132.869 158.780 79.548  1.00 66.52  ? 213 ILE   D C     1 
ATOM   6005 O  O     . ILE   C 2 213 ? 132.193 159.643 78.967  1.00 68.22  ? 213 ILE   D O     1 
ATOM   6006 C  CB    . ILE   C 2 213 ? 134.340 157.633 77.852  1.00 69.18  ? 213 ILE   D CB    1 
ATOM   6007 C  CG1   . ILE   C 2 213 ? 134.772 156.274 77.310  1.00 70.61  ? 213 ILE   D CG1   1 
ATOM   6008 C  CG2   . ILE   C 2 213 ? 135.527 158.321 78.495  1.00 67.70  ? 213 ILE   D CG2   1 
ATOM   6009 C  CD1   . ILE   C 2 213 ? 135.633 155.481 78.272  1.00 70.65  ? 213 ILE   D CD1   1 
ATOM   6010 N  N     . ALA   C 2 214 ? 133.350 158.925 80.785  1.00 55.79  ? 214 ALA   D N     1 
ATOM   6011 C  CA    . ALA   C 2 214 ? 133.313 160.176 81.532  1.00 58.14  ? 214 ALA   D CA    1 
ATOM   6012 C  C     . ALA   C 2 214 ? 134.745 160.591 81.843  1.00 58.03  ? 214 ALA   D C     1 
ATOM   6013 O  O     . ALA   C 2 214 ? 135.498 159.825 82.457  1.00 63.62  ? 214 ALA   D O     1 
ATOM   6014 C  CB    . ALA   C 2 214 ? 132.502 160.024 82.819  1.00 60.26  ? 214 ALA   D CB    1 
ATOM   6015 N  N     . TRP   C 2 215 ? 135.110 161.802 81.433  1.00 60.52  ? 215 TRP   D N     1 
ATOM   6016 C  CA    . TRP   C 2 215 ? 136.461 162.329 81.584  1.00 57.61  ? 215 TRP   D CA    1 
ATOM   6017 C  C     . TRP   C 2 215 ? 136.466 163.370 82.696  1.00 60.93  ? 215 TRP   D C     1 
ATOM   6018 O  O     . TRP   C 2 215 ? 135.712 164.347 82.638  1.00 69.65  ? 215 TRP   D O     1 
ATOM   6019 C  CB    . TRP   C 2 215 ? 136.948 162.927 80.264  1.00 57.19  ? 215 TRP   D CB    1 
ATOM   6020 C  CG    . TRP   C 2 215 ? 138.336 163.505 80.289  1.00 59.91  ? 215 TRP   D CG    1 
ATOM   6021 C  CD1   . TRP   C 2 215 ? 139.268 163.379 81.279  1.00 57.01  ? 215 TRP   D CD1   1 
ATOM   6022 C  CD2   . TRP   C 2 215 ? 138.947 164.296 79.264  1.00 60.84  ? 215 TRP   D CD2   1 
ATOM   6023 N  NE1   . TRP   C 2 215 ? 140.417 164.048 80.935  1.00 53.72  ? 215 TRP   D NE1   1 
ATOM   6024 C  CE2   . TRP   C 2 215 ? 140.245 164.618 79.702  1.00 57.01  ? 215 TRP   D CE2   1 
ATOM   6025 C  CE3   . TRP   C 2 215 ? 138.520 164.764 78.018  1.00 61.52  ? 215 TRP   D CE3   1 
ATOM   6026 C  CZ2   . TRP   C 2 215 ? 141.119 165.387 78.939  1.00 58.39  ? 215 TRP   D CZ2   1 
ATOM   6027 C  CZ3   . TRP   C 2 215 ? 139.389 165.525 77.264  1.00 61.96  ? 215 TRP   D CZ3   1 
ATOM   6028 C  CH2   . TRP   C 2 215 ? 140.673 165.830 77.726  1.00 60.11  ? 215 TRP   D CH2   1 
ATOM   6029 N  N     . ILE   C 2 216 ? 137.317 163.162 83.698  1.00 61.29  ? 216 ILE   D N     1 
ATOM   6030 C  CA    . ILE   C 2 216 ? 137.402 164.030 84.867  1.00 63.80  ? 216 ILE   D CA    1 
ATOM   6031 C  C     . ILE   C 2 216 ? 138.788 164.658 84.891  1.00 71.07  ? 216 ILE   D C     1 
ATOM   6032 O  O     . ILE   C 2 216 ? 139.797 163.943 84.858  1.00 77.17  ? 216 ILE   D O     1 
ATOM   6033 C  CB    . ILE   C 2 216 ? 137.129 163.259 86.169  1.00 66.91  ? 216 ILE   D CB    1 
ATOM   6034 C  CG1   . ILE   C 2 216 ? 135.699 162.719 86.181  1.00 72.02  ? 216 ILE   D CG1   1 
ATOM   6035 C  CG2   . ILE   C 2 216 ? 137.368 164.146 87.375  1.00 69.66  ? 216 ILE   D CG2   1 
ATOM   6036 C  CD1   . ILE   C 2 216 ? 135.453 161.680 87.246  1.00 69.03  ? 216 ILE   D CD1   1 
ATOM   6037 N  N     . GLU   C 2 217 ? 138.837 165.988 84.953  1.00 81.35  ? 217 GLU   D N     1 
ATOM   6038 C  CA    . GLU   C 2 217 ? 140.094 166.731 84.968  1.00 80.92  ? 217 GLU   D CA    1 
ATOM   6039 C  C     . GLU   C 2 217 ? 140.031 167.779 86.071  1.00 81.55  ? 217 GLU   D C     1 
ATOM   6040 O  O     . GLU   C 2 217 ? 139.301 168.769 85.949  1.00 85.02  ? 217 GLU   D O     1 
ATOM   6041 C  CB    . GLU   C 2 217 ? 140.365 167.387 83.616  1.00 80.00  ? 217 GLU   D CB    1 
ATOM   6042 C  CG    . GLU   C 2 217 ? 141.642 168.206 83.566  1.00 84.07  ? 217 GLU   D CG    1 
ATOM   6043 C  CD    . GLU   C 2 217 ? 142.497 167.875 82.360  1.00 86.93  ? 217 GLU   D CD    1 
ATOM   6044 O  OE1   . GLU   C 2 217 ? 142.898 166.700 82.219  1.00 85.31  ? 217 GLU   D OE1   1 
ATOM   6045 O  OE2   . GLU   C 2 217 ? 142.769 168.788 81.552  1.00 87.85  ? 217 GLU   D OE2   1 
ATOM   6046 N  N     . GLY   C 2 218 ? 140.797 167.568 87.135  1.00 74.05  ? 218 GLY   D N     1 
ATOM   6047 C  CA    . GLY   C 2 218 ? 140.837 168.517 88.234  1.00 73.15  ? 218 GLY   D CA    1 
ATOM   6048 C  C     . GLY   C 2 218 ? 139.530 168.660 88.982  1.00 74.99  ? 218 GLY   D C     1 
ATOM   6049 O  O     . GLY   C 2 218 ? 139.178 169.770 89.401  1.00 78.66  ? 218 GLY   D O     1 
ATOM   6050 N  N     . GLY   C 2 219 ? 138.797 167.563 89.158  1.00 71.43  ? 219 GLY   D N     1 
ATOM   6051 C  CA    . GLY   C 2 219 ? 137.543 167.590 89.877  1.00 71.84  ? 219 GLY   D CA    1 
ATOM   6052 C  C     . GLY   C 2 219 ? 136.348 168.062 89.081  1.00 75.84  ? 219 GLY   D C     1 
ATOM   6053 O  O     . GLY   C 2 219 ? 135.245 168.126 89.635  1.00 80.48  ? 219 GLY   D O     1 
ATOM   6054 N  N     . LYS   C 2 220 ? 136.522 168.390 87.804  1.00 88.24  ? 220 LYS   D N     1 
ATOM   6055 C  CA    . LYS   C 2 220 ? 135.440 168.864 86.956  1.00 88.27  ? 220 LYS   D CA    1 
ATOM   6056 C  C     . LYS   C 2 220 ? 135.283 167.939 85.758  1.00 87.10  ? 220 LYS   D C     1 
ATOM   6057 O  O     . LYS   C 2 220 ? 136.274 167.504 85.164  1.00 90.55  ? 220 LYS   D O     1 
ATOM   6058 C  CB    . LYS   C 2 220 ? 135.695 170.297 86.477  1.00 89.29  ? 220 LYS   D CB    1 
ATOM   6059 C  CG    . LYS   C 2 220 ? 135.622 171.339 87.578  1.00 89.42  ? 220 LYS   D CG    1 
ATOM   6060 C  CD    . LYS   C 2 220 ? 136.536 172.515 87.282  1.00 91.24  ? 220 LYS   D CD    1 
ATOM   6061 C  CE    . LYS   C 2 220 ? 137.054 173.149 88.563  1.00 90.98  ? 220 LYS   D CE    1 
ATOM   6062 N  NZ    . LYS   C 2 220 ? 136.864 174.626 88.566  1.00 90.52  ? 220 LYS   D NZ    1 
ATOM   6063 N  N     . LEU   C 2 221 ? 134.035 167.641 85.408  1.00 78.04  ? 221 LEU   D N     1 
ATOM   6064 C  CA    . LEU   C 2 221 ? 133.747 166.762 84.281  1.00 80.16  ? 221 LEU   D CA    1 
ATOM   6065 C  C     . LEU   C 2 221 ? 134.029 167.496 82.977  1.00 82.84  ? 221 LEU   D C     1 
ATOM   6066 O  O     . LEU   C 2 221 ? 133.248 168.356 82.557  1.00 84.31  ? 221 LEU   D O     1 
ATOM   6067 C  CB    . LEU   C 2 221 ? 132.298 166.289 84.336  1.00 79.31  ? 221 LEU   D CB    1 
ATOM   6068 C  CG    . LEU   C 2 221 ? 132.009 164.952 83.655  1.00 79.30  ? 221 LEU   D CG    1 
ATOM   6069 C  CD1   . LEU   C 2 221 ? 132.386 163.799 84.565  1.00 81.20  ? 221 LEU   D CD1   1 
ATOM   6070 C  CD2   . LEU   C 2 221 ? 130.547 164.867 83.255  1.00 80.75  ? 221 LEU   D CD2   1 
ATOM   6071 N  N     . LYS   C 2 222 ? 135.148 167.163 82.334  1.00 76.17  ? 222 LYS   D N     1 
ATOM   6072 C  CA    . LYS   C 2 222 ? 135.493 167.773 81.056  1.00 72.44  ? 222 LYS   D CA    1 
ATOM   6073 C  C     . LYS   C 2 222 ? 134.520 167.355 79.963  1.00 78.59  ? 222 LYS   D C     1 
ATOM   6074 O  O     . LYS   C 2 222 ? 134.040 168.201 79.202  1.00 80.11  ? 222 LYS   D O     1 
ATOM   6075 C  CB    . LYS   C 2 222 ? 136.924 167.412 80.657  1.00 70.86  ? 222 LYS   D CB    1 
ATOM   6076 C  CG    . LYS   C 2 222 ? 137.971 168.378 81.179  1.00 73.70  ? 222 LYS   D CG    1 
ATOM   6077 C  CD    . LYS   C 2 222 ? 139.000 168.733 80.117  1.00 75.99  ? 222 LYS   D CD    1 
ATOM   6078 C  CE    . LYS   C 2 222 ? 138.389 168.784 78.726  1.00 76.37  ? 222 LYS   D CE    1 
ATOM   6079 N  NZ    . LYS   C 2 222 ? 138.057 170.175 78.314  1.00 77.92  ? 222 LYS   D NZ    1 
ATOM   6080 N  N     . ASP   C 2 223 ? 134.221 166.059 79.870  1.00 92.15  ? 223 ASP   D N     1 
ATOM   6081 C  CA    . ASP   C 2 223 ? 133.364 165.549 78.808  1.00 91.71  ? 223 ASP   D CA    1 
ATOM   6082 C  C     . ASP   C 2 223 ? 132.756 164.211 79.204  1.00 92.27  ? 223 ASP   D C     1 
ATOM   6083 O  O     . ASP   C 2 223 ? 133.441 163.353 79.769  1.00 95.63  ? 223 ASP   D O     1 
ATOM   6084 C  CB    . ASP   C 2 223 ? 134.148 165.400 77.501  1.00 91.67  ? 223 ASP   D CB    1 
ATOM   6085 C  CG    . ASP   C 2 223 ? 133.250 165.148 76.310  1.00 95.85  ? 223 ASP   D CG    1 
ATOM   6086 O  OD1   . ASP   C 2 223 ? 132.081 165.582 76.343  1.00 93.87  ? 223 ASP   D OD1   1 
ATOM   6087 O  OD2   . ASP   C 2 223 ? 133.707 164.501 75.348  1.00 99.65  ? 223 ASP   D OD2   1 
ATOM   6088 N  N     . TYR   C 2 224 ? 131.472 164.044 78.901  1.00 84.69  ? 224 TYR   D N     1 
ATOM   6089 C  CA    . TYR   C 2 224 ? 130.755 162.783 79.031  1.00 84.19  ? 224 TYR   D CA    1 
ATOM   6090 C  C     . TYR   C 2 224 ? 130.162 162.468 77.669  1.00 84.76  ? 224 TYR   D C     1 
ATOM   6091 O  O     . TYR   C 2 224 ? 129.539 163.335 77.046  1.00 85.91  ? 224 TYR   D O     1 
ATOM   6092 C  CB    . TYR   C 2 224 ? 129.658 162.889 80.108  1.00 87.37  ? 224 TYR   D CB    1 
ATOM   6093 C  CG    . TYR   C 2 224 ? 128.806 161.644 80.401  1.00 87.61  ? 224 TYR   D CG    1 
ATOM   6094 C  CD1   . TYR   C 2 224 ? 128.899 160.486 79.642  1.00 87.36  ? 224 TYR   D CD1   1 
ATOM   6095 C  CD2   . TYR   C 2 224 ? 127.899 161.640 81.449  1.00 87.22  ? 224 TYR   D CD2   1 
ATOM   6096 C  CE1   . TYR   C 2 224 ? 128.117 159.376 79.908  1.00 88.43  ? 224 TYR   D CE1   1 
ATOM   6097 C  CE2   . TYR   C 2 224 ? 127.112 160.529 81.720  1.00 86.35  ? 224 TYR   D CE2   1 
ATOM   6098 C  CZ    . TYR   C 2 224 ? 127.232 159.399 80.957  1.00 84.45  ? 224 TYR   D CZ    1 
ATOM   6099 O  OH    . TYR   C 2 224 ? 126.450 158.303 81.235  1.00 82.38  ? 224 TYR   D OH    1 
ATOM   6100 N  N     . GLY   C 2 225 ? 130.365 161.242 77.203  1.00 82.89  ? 225 GLY   D N     1 
ATOM   6101 C  CA    . GLY   C 2 225 ? 129.756 160.840 75.953  1.00 82.42  ? 225 GLY   D CA    1 
ATOM   6102 C  C     . GLY   C 2 225 ? 130.040 159.384 75.650  1.00 83.23  ? 225 GLY   D C     1 
ATOM   6103 O  O     . GLY   C 2 225 ? 130.342 158.588 76.541  1.00 86.83  ? 225 GLY   D O     1 
ATOM   6104 N  N     . GLU   C 2 226 ? 129.918 159.056 74.368  1.00 89.84  ? 226 GLU   D N     1 
ATOM   6105 C  CA    . GLU   C 2 226 ? 130.174 157.700 73.912  1.00 91.30  ? 226 GLU   D CA    1 
ATOM   6106 C  C     . GLU   C 2 226 ? 131.670 157.405 73.958  1.00 93.86  ? 226 GLU   D C     1 
ATOM   6107 O  O     . GLU   C 2 226 ? 132.501 158.312 74.042  1.00 96.94  ? 226 GLU   D O     1 
ATOM   6108 C  CB    . GLU   C 2 226 ? 129.634 157.516 72.493  1.00 89.88  ? 226 GLU   D CB    1 
ATOM   6109 C  CG    . GLU   C 2 226 ? 128.772 156.279 72.289  1.00 93.36  ? 226 GLU   D CG    1 
ATOM   6110 C  CD    . GLU   C 2 226 ? 127.673 156.148 73.329  1.00 96.10  ? 226 GLU   D CD    1 
ATOM   6111 O  OE1   . GLU   C 2 226 ? 126.817 157.054 73.405  1.00 95.87  ? 226 GLU   D OE1   1 
ATOM   6112 O  OE2   . GLU   C 2 226 ? 127.657 155.135 74.058  1.00 94.77  ? 226 GLU   D OE2   1 
ATOM   6113 N  N     . LEU   C 2 227 ? 132.006 156.113 73.918  1.00 92.24  ? 227 LEU   D N     1 
ATOM   6114 C  CA    . LEU   C 2 227 ? 133.408 155.703 73.890  1.00 91.81  ? 227 LEU   D CA    1 
ATOM   6115 C  C     . LEU   C 2 227 ? 134.143 156.310 72.701  1.00 93.95  ? 227 LEU   D C     1 
ATOM   6116 O  O     . LEU   C 2 227 ? 135.191 156.951 72.867  1.00 97.58  ? 227 LEU   D O     1 
ATOM   6117 C  CB    . LEU   C 2 227 ? 133.496 154.175 73.845  1.00 94.17  ? 227 LEU   D CB    1 
ATOM   6118 C  CG    . LEU   C 2 227 ? 134.865 153.495 73.942  1.00 90.54  ? 227 LEU   D CG    1 
ATOM   6119 C  CD1   . LEU   C 2 227 ? 135.350 153.400 75.374  1.00 88.76  ? 227 LEU   D CD1   1 
ATOM   6120 C  CD2   . LEU   C 2 227 ? 134.832 152.114 73.299  1.00 92.52  ? 227 LEU   D CD2   1 
ATOM   6121 N  N     . ASP   C 2 228 ? 133.584 156.151 71.498  1.00 103.19 ? 228 ASP   D N     1 
ATOM   6122 C  CA    . ASP   C 2 228 ? 134.300 156.506 70.276  1.00 103.13 ? 228 ASP   D CA    1 
ATOM   6123 C  C     . ASP   C 2 228 ? 134.501 158.011 70.158  1.00 105.00 ? 228 ASP   D C     1 
ATOM   6124 O  O     . ASP   C 2 228 ? 135.323 158.471 69.357  1.00 109.06 ? 228 ASP   D O     1 
ATOM   6125 C  CB    . ASP   C 2 228 ? 133.546 155.973 69.058  1.00 105.41 ? 228 ASP   D CB    1 
ATOM   6126 C  CG    . ASP   C 2 228 ? 134.179 154.723 68.481  1.00 105.43 ? 228 ASP   D CG    1 
ATOM   6127 O  OD1   . ASP   C 2 228 ? 135.411 154.719 68.279  1.00 104.30 ? 228 ASP   D OD1   1 
ATOM   6128 O  OD2   . ASP   C 2 228 ? 133.444 153.745 68.231  1.00 104.60 ? 228 ASP   D OD2   1 
ATOM   6129 N  N     . ASP   C 2 229 ? 133.750 158.796 70.931  1.00 100.86 ? 229 ASP   D N     1 
ATOM   6130 C  CA    . ASP   C 2 229 ? 133.913 160.244 70.878  1.00 99.86  ? 229 ASP   D CA    1 
ATOM   6131 C  C     . ASP   C 2 229 ? 134.874 160.732 71.954  1.00 99.08  ? 229 ASP   D C     1 
ATOM   6132 O  O     . ASP   C 2 229 ? 135.824 161.467 71.663  1.00 100.19 ? 229 ASP   D O     1 
ATOM   6133 C  CB    . ASP   C 2 229 ? 132.553 160.930 71.016  1.00 100.60 ? 229 ASP   D CB    1 
ATOM   6134 C  CG    . ASP   C 2 229 ? 131.507 160.339 70.095  1.00 104.38 ? 229 ASP   D CG    1 
ATOM   6135 O  OD1   . ASP   C 2 229 ? 130.311 160.646 70.278  1.00 104.76 ? 229 ASP   D OD1   1 
ATOM   6136 O  OD2   . ASP   C 2 229 ? 131.882 159.568 69.186  1.00 104.59 ? 229 ASP   D OD2   1 
ATOM   6137 N  N     . VAL   C 2 230 ? 134.644 160.334 73.206  1.00 82.68  ? 230 VAL   D N     1 
ATOM   6138 C  CA    . VAL   C 2 230 ? 135.426 160.884 74.308  1.00 82.37  ? 230 VAL   D CA    1 
ATOM   6139 C  C     . VAL   C 2 230 ? 136.834 160.300 74.334  1.00 84.14  ? 230 VAL   D C     1 
ATOM   6140 O  O     . VAL   C 2 230 ? 137.803 161.018 74.606  1.00 86.85  ? 230 VAL   D O     1 
ATOM   6141 C  CB    . VAL   C 2 230 ? 134.698 160.665 75.645  1.00 78.24  ? 230 VAL   D CB    1 
ATOM   6142 C  CG1   . VAL   C 2 230 ? 135.383 161.456 76.745  1.00 80.09  ? 230 VAL   D CG1   1 
ATOM   6143 C  CG2   . VAL   C 2 230 ? 133.255 161.086 75.522  1.00 76.57  ? 230 VAL   D CG2   1 
ATOM   6144 N  N     . LEU   C 2 231 ? 136.976 158.998 74.075  1.00 72.14  ? 231 LEU   D N     1 
ATOM   6145 C  CA    . LEU   C 2 231 ? 138.295 158.380 74.207  1.00 71.72  ? 231 LEU   D CA    1 
ATOM   6146 C  C     . LEU   C 2 231 ? 139.353 158.988 73.286  1.00 74.96  ? 231 LEU   D C     1 
ATOM   6147 O  O     . LEU   C 2 231 ? 140.477 159.231 73.765  1.00 76.16  ? 231 LEU   D O     1 
ATOM   6148 C  CB    . LEU   C 2 231 ? 138.185 156.866 73.989  1.00 74.46  ? 231 LEU   D CB    1 
ATOM   6149 C  CG    . LEU   C 2 231 ? 139.242 156.020 74.702  1.00 72.64  ? 231 LEU   D CG    1 
ATOM   6150 C  CD1   . LEU   C 2 231 ? 139.285 156.352 76.185  1.00 66.55  ? 231 LEU   D CD1   1 
ATOM   6151 C  CD2   . LEU   C 2 231 ? 138.984 154.539 74.490  1.00 73.26  ? 231 LEU   D CD2   1 
ATOM   6152 N  N     . PRO   C 2 232 ? 139.093 159.239 71.995  1.00 86.62  ? 232 PRO   D N     1 
ATOM   6153 C  CA    . PRO   C 2 232 ? 140.130 159.875 71.164  1.00 90.06  ? 232 PRO   D CA    1 
ATOM   6154 C  C     . PRO   C 2 232 ? 140.581 161.231 71.677  1.00 87.80  ? 232 PRO   D C     1 
ATOM   6155 O  O     . PRO   C 2 232 ? 141.764 161.564 71.548  1.00 86.67  ? 232 PRO   D O     1 
ATOM   6156 C  CB    . PRO   C 2 232 ? 139.447 159.977 69.795  1.00 88.62  ? 232 PRO   D CB    1 
ATOM   6157 C  CG    . PRO   C 2 232 ? 138.531 158.811 69.782  1.00 86.79  ? 232 PRO   D CG    1 
ATOM   6158 C  CD    . PRO   C 2 232 ? 137.947 158.821 71.166  1.00 84.31  ? 232 PRO   D CD    1 
ATOM   6159 N  N     . LYS   C 2 233 ? 139.677 162.029 72.249  1.00 81.05  ? 233 LYS   D N     1 
ATOM   6160 C  CA    . LYS   C 2 233 ? 140.087 163.313 72.809  1.00 82.26  ? 233 LYS   D CA    1 
ATOM   6161 C  C     . LYS   C 2 233 ? 141.053 163.128 73.972  1.00 83.13  ? 233 LYS   D C     1 
ATOM   6162 O  O     . LYS   C 2 233 ? 142.049 163.853 74.083  1.00 88.37  ? 233 LYS   D O     1 
ATOM   6163 C  CB    . LYS   C 2 233 ? 138.867 164.118 73.254  1.00 82.53  ? 233 LYS   D CB    1 
ATOM   6164 C  CG    . LYS   C 2 233 ? 137.662 163.995 72.343  1.00 83.03  ? 233 LYS   D CG    1 
ATOM   6165 C  CD    . LYS   C 2 233 ? 136.420 164.561 73.009  1.00 83.16  ? 233 LYS   D CD    1 
ATOM   6166 C  CE    . LYS   C 2 233 ? 135.549 165.305 72.011  1.00 81.51  ? 233 LYS   D CE    1 
ATOM   6167 N  NZ    . LYS   C 2 233 ? 135.147 164.439 70.870  1.00 84.38  ? 233 LYS   D NZ    1 
ATOM   6168 N  N     . TYR   C 2 234 ? 140.774 162.163 74.851  1.00 66.94  ? 234 TYR   D N     1 
ATOM   6169 C  CA    . TYR   C 2 234 ? 141.675 161.903 75.969  1.00 62.27  ? 234 TYR   D CA    1 
ATOM   6170 C  C     . TYR   C 2 234 ? 143.034 161.423 75.478  1.00 65.12  ? 234 TYR   D C     1 
ATOM   6171 O  O     . TYR   C 2 234 ? 144.077 161.846 75.996  1.00 73.38  ? 234 TYR   D O     1 
ATOM   6172 C  CB    . TYR   C 2 234 ? 141.048 160.882 76.917  1.00 61.95  ? 234 TYR   D CB    1 
ATOM   6173 C  CG    . TYR   C 2 234 ? 141.862 160.614 78.159  1.00 59.40  ? 234 TYR   D CG    1 
ATOM   6174 C  CD1   . TYR   C 2 234 ? 142.323 161.656 78.948  1.00 61.11  ? 234 TYR   D CD1   1 
ATOM   6175 C  CD2   . TYR   C 2 234 ? 142.167 159.318 78.545  1.00 62.38  ? 234 TYR   D CD2   1 
ATOM   6176 C  CE1   . TYR   C 2 234 ? 143.066 161.415 80.085  1.00 58.93  ? 234 TYR   D CE1   1 
ATOM   6177 C  CE2   . TYR   C 2 234 ? 142.909 159.067 79.678  1.00 63.47  ? 234 TYR   D CE2   1 
ATOM   6178 C  CZ    . TYR   C 2 234 ? 143.356 160.118 80.444  1.00 62.00  ? 234 TYR   D CZ    1 
ATOM   6179 O  OH    . TYR   C 2 234 ? 144.096 159.870 81.575  1.00 69.77  ? 234 TYR   D OH    1 
ATOM   6180 N  N     . GLU   C 2 235 ? 143.048 160.544 74.473  1.00 71.84  ? 235 GLU   D N     1 
ATOM   6181 C  CA    . GLU   C 2 235 ? 144.324 160.088 73.930  1.00 73.99  ? 235 GLU   D CA    1 
ATOM   6182 C  C     . GLU   C 2 235 ? 145.098 161.234 73.287  1.00 78.97  ? 235 GLU   D C     1 
ATOM   6183 O  O     . GLU   C 2 235 ? 146.318 161.343 73.460  1.00 78.86  ? 235 GLU   D O     1 
ATOM   6184 C  CB    . GLU   C 2 235 ? 144.099 158.954 72.931  1.00 74.97  ? 235 GLU   D CB    1 
ATOM   6185 C  CG    . GLU   C 2 235 ? 143.916 157.591 73.585  1.00 79.47  ? 235 GLU   D CG    1 
ATOM   6186 C  CD    . GLU   C 2 235 ? 143.066 156.650 72.756  1.00 81.24  ? 235 GLU   D CD    1 
ATOM   6187 O  OE1   . GLU   C 2 235 ? 142.494 157.099 71.741  1.00 79.46  ? 235 GLU   D OE1   1 
ATOM   6188 O  OE2   . GLU   C 2 235 ? 142.970 155.459 73.119  1.00 77.20  ? 235 GLU   D OE2   1 
ATOM   6189 N  N     . ALA   C 2 236 ? 144.407 162.103 72.545  1.00 80.75  ? 236 ALA   D N     1 
ATOM   6190 C  CA    . ALA   C 2 236 ? 145.071 163.249 71.935  1.00 79.12  ? 236 ALA   D CA    1 
ATOM   6191 C  C     . ALA   C 2 236 ? 145.637 164.183 72.995  1.00 75.92  ? 236 ALA   D C     1 
ATOM   6192 O  O     . ALA   C 2 236 ? 146.734 164.730 72.830  1.00 79.95  ? 236 ALA   D O     1 
ATOM   6193 C  CB    . ALA   C 2 236 ? 144.100 163.996 71.022  1.00 78.03  ? 236 ALA   D CB    1 
ATOM   6194 N  N     . PHE   C 2 237 ? 144.902 164.380 74.092  1.00 66.10  ? 237 PHE   D N     1 
ATOM   6195 C  CA    . PHE   C 2 237 ? 145.408 165.203 75.184  1.00 66.07  ? 237 PHE   D CA    1 
ATOM   6196 C  C     . PHE   C 2 237 ? 146.651 164.581 75.810  1.00 65.00  ? 237 PHE   D C     1 
ATOM   6197 O  O     . PHE   C 2 237 ? 147.604 165.291 76.148  1.00 70.48  ? 237 PHE   D O     1 
ATOM   6198 C  CB    . PHE   C 2 237 ? 144.315 165.410 76.233  1.00 68.00  ? 237 PHE   D CB    1 
ATOM   6199 C  CG    . PHE   C 2 237 ? 144.833 165.570 77.635  1.00 70.10  ? 237 PHE   D CG    1 
ATOM   6200 C  CD1   . PHE   C 2 237 ? 145.378 166.773 78.050  1.00 69.07  ? 237 PHE   D CD1   1 
ATOM   6201 C  CD2   . PHE   C 2 237 ? 144.765 164.525 78.540  1.00 70.21  ? 237 PHE   D CD2   1 
ATOM   6202 C  CE1   . PHE   C 2 237 ? 145.853 166.928 79.337  1.00 67.06  ? 237 PHE   D CE1   1 
ATOM   6203 C  CE2   . PHE   C 2 237 ? 145.241 164.675 79.829  1.00 70.42  ? 237 PHE   D CE2   1 
ATOM   6204 C  CZ    . PHE   C 2 237 ? 145.785 165.878 80.228  1.00 67.86  ? 237 PHE   D CZ    1 
ATOM   6205 N  N     . LEU   C 2 238 ? 146.660 163.254 75.971  1.00 63.95  ? 238 LEU   D N     1 
ATOM   6206 C  CA    . LEU   C 2 238 ? 147.842 162.589 76.517  1.00 68.16  ? 238 LEU   D CA    1 
ATOM   6207 C  C     . LEU   C 2 238 ? 149.054 162.766 75.607  1.00 72.40  ? 238 LEU   D C     1 
ATOM   6208 O  O     . LEU   C 2 238 ? 150.159 163.059 76.079  1.00 76.02  ? 238 LEU   D O     1 
ATOM   6209 C  CB    . LEU   C 2 238 ? 147.560 161.104 76.743  1.00 70.63  ? 238 LEU   D CB    1 
ATOM   6210 C  CG    . LEU   C 2 238 ? 146.583 160.735 77.859  1.00 67.26  ? 238 LEU   D CG    1 
ATOM   6211 C  CD1   . LEU   C 2 238 ? 146.141 159.291 77.714  1.00 70.85  ? 238 LEU   D CD1   1 
ATOM   6212 C  CD2   . LEU   C 2 238 ? 147.213 160.966 79.220  1.00 64.56  ? 238 LEU   D CD2   1 
ATOM   6213 N  N     . ASN   C 2 239 ? 148.867 162.590 74.296  1.00 86.75  ? 239 ASN   D N     1 
ATOM   6214 C  CA    . ASN   C 2 239 ? 149.978 162.794 73.365  1.00 87.27  ? 239 ASN   D CA    1 
ATOM   6215 C  C     . ASN   C 2 239 ? 150.456 164.244 73.368  1.00 85.87  ? 239 ASN   D C     1 
ATOM   6216 O  O     . ASN   C 2 239 ? 151.665 164.506 73.317  1.00 88.85  ? 239 ASN   D O     1 
ATOM   6217 C  CB    . ASN   C 2 239 ? 149.583 162.357 71.956  1.00 88.92  ? 239 ASN   D CB    1 
ATOM   6218 C  CG    . ASN   C 2 239 ? 148.854 161.031 71.942  1.00 91.09  ? 239 ASN   D CG    1 
ATOM   6219 O  OD1   . ASN   C 2 239 ? 148.691 160.391 72.979  1.00 90.18  ? 239 ASN   D OD1   1 
ATOM   6220 N  ND2   . ASN   C 2 239 ? 148.406 160.614 70.764  1.00 89.82  ? 239 ASN   D ND2   1 
ATOM   6221 N  N     . ASP   C 2 240 ? 149.525 165.199 73.429  1.00 88.11  ? 240 ASP   D N     1 
ATOM   6222 C  CA    . ASP   C 2 240 ? 149.919 166.603 73.484  1.00 87.56  ? 240 ASP   D CA    1 
ATOM   6223 C  C     . ASP   C 2 240 ? 150.708 166.906 74.751  1.00 87.84  ? 240 ASP   D C     1 
ATOM   6224 O  O     . ASP   C 2 240 ? 151.688 167.657 74.714  1.00 90.21  ? 240 ASP   D O     1 
ATOM   6225 C  CB    . ASP   C 2 240 ? 148.685 167.499 73.392  1.00 91.08  ? 240 ASP   D CB    1 
ATOM   6226 C  CG    . ASP   C 2 240 ? 148.939 168.756 72.588  1.00 93.51  ? 240 ASP   D CG    1 
ATOM   6227 O  OD1   . ASP   C 2 240 ? 148.556 168.790 71.401  1.00 93.42  ? 240 ASP   D OD1   1 
ATOM   6228 O  OD2   . ASP   C 2 240 ? 149.524 169.710 73.142  1.00 95.48  ? 240 ASP   D OD2   1 
ATOM   6229 N  N     . PHE   C 2 241 ? 150.290 166.334 75.883  1.00 81.82  ? 241 PHE   D N     1 
ATOM   6230 C  CA    . PHE   C 2 241 ? 151.039 166.514 77.123  1.00 79.92  ? 241 PHE   D CA    1 
ATOM   6231 C  C     . PHE   C 2 241 ? 152.427 165.900 77.018  1.00 82.58  ? 241 PHE   D C     1 
ATOM   6232 O  O     . PHE   C 2 241 ? 153.399 166.445 77.555  1.00 86.33  ? 241 PHE   D O     1 
ATOM   6233 C  CB    . PHE   C 2 241 ? 150.271 165.907 78.295  1.00 78.86  ? 241 PHE   D CB    1 
ATOM   6234 C  CG    . PHE   C 2 241 ? 150.736 166.392 79.637  1.00 81.16  ? 241 PHE   D CG    1 
ATOM   6235 C  CD1   . PHE   C 2 241 ? 150.187 167.527 80.204  1.00 84.50  ? 241 PHE   D CD1   1 
ATOM   6236 C  CD2   . PHE   C 2 241 ? 151.724 165.713 80.329  1.00 82.20  ? 241 PHE   D CD2   1 
ATOM   6237 C  CE1   . PHE   C 2 241 ? 150.613 167.976 81.438  1.00 84.33  ? 241 PHE   D CE1   1 
ATOM   6238 C  CE2   . PHE   C 2 241 ? 152.153 166.158 81.563  1.00 84.44  ? 241 PHE   D CE2   1 
ATOM   6239 C  CZ    . PHE   C 2 241 ? 151.596 167.290 82.118  1.00 83.36  ? 241 PHE   D CZ    1 
ATOM   6240 N  N     . LYS   C 2 242 ? 152.538 164.754 76.343  1.00 88.99  ? 242 LYS   D N     1 
ATOM   6241 C  CA    . LYS   C 2 242 ? 153.854 164.171 76.099  1.00 87.86  ? 242 LYS   D CA    1 
ATOM   6242 C  C     . LYS   C 2 242 ? 154.716 165.099 75.251  1.00 89.56  ? 242 LYS   D C     1 
ATOM   6243 O  O     . LYS   C 2 242 ? 155.936 165.170 75.438  1.00 90.82  ? 242 LYS   D O     1 
ATOM   6244 C  CB    . LYS   C 2 242 ? 153.713 162.807 75.425  1.00 87.75  ? 242 LYS   D CB    1 
ATOM   6245 C  CG    . LYS   C 2 242 ? 153.849 161.627 76.373  1.00 89.04  ? 242 LYS   D CG    1 
ATOM   6246 C  CD    . LYS   C 2 242 ? 153.198 160.379 75.799  1.00 90.17  ? 242 LYS   D CD    1 
ATOM   6247 C  CE    . LYS   C 2 242 ? 152.337 159.677 76.834  1.00 90.55  ? 242 LYS   D CE    1 
ATOM   6248 N  NZ    . LYS   C 2 242 ? 152.145 158.237 76.510  1.00 88.03  ? 242 LYS   D NZ    1 
ATOM   6249 N  N     . LYS   C 2 243 ? 154.097 165.813 74.307  1.00 96.04  ? 243 LYS   D N     1 
ATOM   6250 C  CA    . LYS   C 2 243 ? 154.849 166.740 73.464  1.00 94.30  ? 243 LYS   D CA    1 
ATOM   6251 C  C     . LYS   C 2 243 ? 155.414 167.904 74.269  1.00 95.46  ? 243 LYS   D C     1 
ATOM   6252 O  O     . LYS   C 2 243 ? 156.523 168.377 73.994  1.00 93.54  ? 243 LYS   D O     1 
ATOM   6253 C  CB    . LYS   C 2 243 ? 153.960 167.261 72.334  1.00 93.84  ? 243 LYS   D CB    1 
ATOM   6254 C  CG    . LYS   C 2 243 ? 154.268 166.670 70.969  1.00 94.55  ? 243 LYS   D CG    1 
ATOM   6255 C  CD    . LYS   C 2 243 ? 154.441 165.164 71.035  1.00 94.58  ? 243 LYS   D CD    1 
ATOM   6256 C  CE    . LYS   C 2 243 ? 154.569 164.572 69.642  1.00 94.03  ? 243 LYS   D CE    1 
ATOM   6257 N  NZ    . LYS   C 2 243 ? 153.408 164.935 68.783  1.00 97.39  ? 243 LYS   D NZ    1 
ATOM   6258 N  N     . LYS   C 2 244 ? 154.667 168.383 75.262  1.00 99.95  ? 244 LYS   D N     1 
ATOM   6259 C  CA    . LYS   C 2 244 ? 155.038 169.603 75.970  1.00 96.49  ? 244 LYS   D CA    1 
ATOM   6260 C  C     . LYS   C 2 244 ? 156.332 169.424 76.754  1.00 99.95  ? 244 LYS   D C     1 
ATOM   6261 O  O     . LYS   C 2 244 ? 156.677 168.319 77.182  1.00 99.97  ? 244 LYS   D O     1 
ATOM   6262 C  CB    . LYS   C 2 244 ? 153.911 170.027 76.912  1.00 94.82  ? 244 LYS   D CB    1 
ATOM   6263 C  CG    . LYS   C 2 244 ? 152.630 170.432 76.202  1.00 95.59  ? 244 LYS   D CG    1 
ATOM   6264 C  CD    . LYS   C 2 244 ? 151.420 170.332 77.119  1.00 96.68  ? 244 LYS   D CD    1 
ATOM   6265 C  CE    . LYS   C 2 244 ? 151.765 170.685 78.555  1.00 96.89  ? 244 LYS   D CE    1 
ATOM   6266 N  NZ    . LYS   C 2 244 ? 150.583 171.211 79.290  1.00 98.25  ? 244 LYS   D NZ    1 
ATOM   6267 N  N     . SER   C 2 245 ? 157.052 170.529 76.938  1.00 103.93 ? 245 SER   D N     1 
ATOM   6268 C  CA    . SER   C 2 245 ? 158.287 170.519 77.706  1.00 103.53 ? 245 SER   D CA    1 
ATOM   6269 C  C     . SER   C 2 245 ? 157.988 170.485 79.204  1.00 103.99 ? 245 SER   D C     1 
ATOM   6270 O  O     . SER   C 2 245 ? 156.844 170.632 79.643  1.00 103.74 ? 245 SER   D O     1 
ATOM   6271 C  CB    . SER   C 2 245 ? 159.139 171.742 77.369  1.00 101.57 ? 245 SER   D CB    1 
ATOM   6272 O  OG    . SER   C 2 245 ? 158.565 172.925 77.895  1.00 101.82 ? 245 SER   D OG    1 
ATOM   6273 N  N     . LYS   C 2 246 ? 159.049 170.294 79.993  1.00 96.92  ? 246 LYS   D N     1 
ATOM   6274 C  CA    . LYS   C 2 246 ? 158.890 170.135 81.437  1.00 96.60  ? 246 LYS   D CA    1 
ATOM   6275 C  C     . LYS   C 2 246 ? 158.324 171.396 82.082  1.00 95.95  ? 246 LYS   D C     1 
ATOM   6276 O  O     . LYS   C 2 246 ? 157.475 171.316 82.979  1.00 97.23  ? 246 LYS   D O     1 
ATOM   6277 C  CB    . LYS   C 2 246 ? 160.230 169.756 82.067  1.00 96.55  ? 246 LYS   D CB    1 
ATOM   6278 C  CG    . LYS   C 2 246 ? 160.156 169.422 83.546  1.00 97.44  ? 246 LYS   D CG    1 
ATOM   6279 C  CD    . LYS   C 2 246 ? 161.510 168.967 84.070  1.00 98.63  ? 246 LYS   D CD    1 
ATOM   6280 C  CE    . LYS   C 2 246 ? 162.541 170.080 83.982  1.00 97.24  ? 246 LYS   D CE    1 
ATOM   6281 N  NZ    . LYS   C 2 246 ? 163.616 169.922 85.001  1.00 93.60  ? 246 LYS   D NZ    1 
ATOM   6282 N  N     . ALA   C 2 247 ? 158.786 172.570 81.642  1.00 95.23  ? 247 ALA   D N     1 
ATOM   6283 C  CA    . ALA   C 2 247 ? 158.287 173.820 82.207  1.00 97.94  ? 247 ALA   D CA    1 
ATOM   6284 C  C     . ALA   C 2 247 ? 156.799 173.996 81.933  1.00 99.36  ? 247 ALA   D C     1 
ATOM   6285 O  O     . ALA   C 2 247 ? 156.047 174.444 82.809  1.00 96.87  ? 247 ALA   D O     1 
ATOM   6286 C  CB    . ALA   C 2 247 ? 159.080 175.000 81.650  1.00 96.41  ? 247 ALA   D CB    1 
ATOM   6287 N  N     . GLU   C 2 248 ? 156.353 173.657 80.720  1.00 100.53 ? 248 GLU   D N     1 
ATOM   6288 C  CA    . GLU   C 2 248 ? 154.936 173.776 80.391  1.00 99.05  ? 248 GLU   D CA    1 
ATOM   6289 C  C     . GLU   C 2 248 ? 154.091 172.813 81.218  1.00 100.26 ? 248 GLU   D C     1 
ATOM   6290 O  O     . GLU   C 2 248 ? 152.996 173.169 81.671  1.00 104.52 ? 248 GLU   D O     1 
ATOM   6291 C  CB    . GLU   C 2 248 ? 154.728 173.538 78.897  1.00 98.58  ? 248 GLU   D CB    1 
ATOM   6292 C  CG    . GLU   C 2 248 ? 155.563 174.449 78.013  1.00 100.75 ? 248 GLU   D CG    1 
ATOM   6293 C  CD    . GLU   C 2 248 ? 155.320 174.217 76.536  1.00 101.91 ? 248 GLU   D CD    1 
ATOM   6294 O  OE1   . GLU   C 2 248 ? 154.291 174.698 76.019  1.00 99.01  ? 248 GLU   D OE1   1 
ATOM   6295 O  OE2   . GLU   C 2 248 ? 156.159 173.554 75.892  1.00 102.23 ? 248 GLU   D OE2   1 
ATOM   6296 N  N     . GLN   C 2 249 ? 154.578 171.587 81.419  1.00 92.02  ? 249 GLN   D N     1 
ATOM   6297 C  CA    . GLN   C 2 249 ? 153.868 170.636 82.267  1.00 94.22  ? 249 GLN   D CA    1 
ATOM   6298 C  C     . GLN   C 2 249 ? 153.758 171.154 83.696  1.00 94.31  ? 249 GLN   D C     1 
ATOM   6299 O  O     . GLN   C 2 249 ? 152.694 171.057 84.325  1.00 96.80  ? 249 GLN   D O     1 
ATOM   6300 C  CB    . GLN   C 2 249 ? 154.579 169.283 82.243  1.00 94.87  ? 249 GLN   D CB    1 
ATOM   6301 C  CG    . GLN   C 2 249 ? 154.701 168.669 80.859  1.00 94.92  ? 249 GLN   D CG    1 
ATOM   6302 C  CD    . GLN   C 2 249 ? 155.720 167.546 80.808  1.00 94.38  ? 249 GLN   D CD    1 
ATOM   6303 O  OE1   . GLN   C 2 249 ? 156.480 167.339 81.754  1.00 95.02  ? 249 GLN   D OE1   1 
ATOM   6304 N  NE2   . GLN   C 2 249 ? 155.744 166.818 79.698  1.00 92.19  ? 249 GLN   D NE2   1 
ATOM   6305 N  N     . LYS   C 2 250 ? 154.852 171.711 84.222  1.00 95.97  ? 250 LYS   D N     1 
ATOM   6306 C  CA    . LYS   C 2 250 ? 154.824 172.270 85.569  1.00 99.48  ? 250 LYS   D CA    1 
ATOM   6307 C  C     . LYS   C 2 250 ? 153.842 173.430 85.662  1.00 99.98  ? 250 LYS   D C     1 
ATOM   6308 O  O     . LYS   C 2 250 ? 153.109 173.553 86.650  1.00 97.59  ? 250 LYS   D O     1 
ATOM   6309 C  CB    . LYS   C 2 250 ? 156.227 172.717 85.978  1.00 97.71  ? 250 LYS   D CB    1 
ATOM   6310 C  CG    . LYS   C 2 250 ? 156.591 172.386 87.415  1.00 98.50  ? 250 LYS   D CG    1 
ATOM   6311 C  CD    . LYS   C 2 250 ? 157.988 172.880 87.758  1.00 98.91  ? 250 LYS   D CD    1 
ATOM   6312 C  CE    . LYS   C 2 250 ? 159.015 172.367 86.761  1.00 100.17 ? 250 LYS   D CE    1 
ATOM   6313 N  NZ    . LYS   C 2 250 ? 160.343 172.141 87.394  1.00 97.20  ? 250 LYS   D NZ    1 
ATOM   6314 N  N     . GLU   C 2 251 ? 153.809 174.288 84.640  1.00 100.51 ? 251 GLU   D N     1 
ATOM   6315 C  CA    . GLU   C 2 251 ? 152.876 175.410 84.642  1.00 99.54  ? 251 GLU   D CA    1 
ATOM   6316 C  C     . GLU   C 2 251 ? 151.430 174.929 84.599  1.00 102.14 ? 251 GLU   D C     1 
ATOM   6317 O  O     . GLU   C 2 251 ? 150.563 175.487 85.282  1.00 104.31 ? 251 GLU   D O     1 
ATOM   6318 C  CB    . GLU   C 2 251 ? 153.182 176.343 83.466  1.00 98.04  ? 251 GLU   D CB    1 
ATOM   6319 C  CG    . GLU   C 2 251 ? 152.319 177.600 83.395  1.00 102.83 ? 251 GLU   D CG    1 
ATOM   6320 C  CD    . GLU   C 2 251 ? 151.046 177.417 82.585  1.00 105.00 ? 251 GLU   D CD    1 
ATOM   6321 O  OE1   . GLU   C 2 251 ? 150.323 178.416 82.388  1.00 105.10 ? 251 GLU   D OE1   1 
ATOM   6322 O  OE2   . GLU   C 2 251 ? 150.781 176.289 82.121  1.00 103.36 ? 251 GLU   D OE2   1 
ATOM   6323 N  N     . PHE   C 2 252 ? 151.147 173.902 83.794  1.00 98.71  ? 252 PHE   D N     1 
ATOM   6324 C  CA    . PHE   C 2 252 ? 149.791 173.363 83.722  1.00 96.70  ? 252 PHE   D CA    1 
ATOM   6325 C  C     . PHE   C 2 252 ? 149.360 172.778 85.064  1.00 97.78  ? 252 PHE   D C     1 
ATOM   6326 O  O     . PHE   C 2 252 ? 148.240 173.032 85.538  1.00 98.07  ? 252 PHE   D O     1 
ATOM   6327 C  CB    . PHE   C 2 252 ? 149.722 172.315 82.608  1.00 95.44  ? 252 PHE   D CB    1 
ATOM   6328 C  CG    . PHE   C 2 252 ? 148.542 171.385 82.699  1.00 99.10  ? 252 PHE   D CG    1 
ATOM   6329 C  CD1   . PHE   C 2 252 ? 147.336 171.722 82.108  1.00 98.26  ? 252 PHE   D CD1   1 
ATOM   6330 C  CD2   . PHE   C 2 252 ? 148.649 170.160 83.338  1.00 99.00  ? 252 PHE   D CD2   1 
ATOM   6331 C  CE1   . PHE   C 2 252 ? 146.252 170.869 82.177  1.00 97.58  ? 252 PHE   D CE1   1 
ATOM   6332 C  CE2   . PHE   C 2 252 ? 147.568 169.303 83.411  1.00 98.06  ? 252 PHE   D CE2   1 
ATOM   6333 C  CZ    . PHE   C 2 252 ? 146.369 169.658 82.827  1.00 97.65  ? 252 PHE   D CZ    1 
ATOM   6334 N  N     . ARG   C 2 253 ? 150.245 172.005 85.700  1.00 101.49 ? 253 ARG   D N     1 
ATOM   6335 C  CA    . ARG   C 2 253 ? 149.926 171.449 87.011  1.00 104.48 ? 253 ARG   D CA    1 
ATOM   6336 C  C     . ARG   C 2 253 ? 149.724 172.553 88.043  1.00 106.59 ? 253 ARG   D C     1 
ATOM   6337 O  O     . ARG   C 2 253 ? 148.820 172.469 88.885  1.00 105.95 ? 253 ARG   D O     1 
ATOM   6338 C  CB    . ARG   C 2 253 ? 151.027 170.488 87.455  1.00 104.79 ? 253 ARG   D CB    1 
ATOM   6339 C  CG    . ARG   C 2 253 ? 151.100 169.218 86.628  1.00 104.57 ? 253 ARG   D CG    1 
ATOM   6340 C  CD    . ARG   C 2 253 ? 151.162 167.984 87.513  1.00 105.22 ? 253 ARG   D CD    1 
ATOM   6341 N  NE    . ARG   C 2 253 ? 151.025 166.754 86.745  1.00 105.38 ? 253 ARG   D NE    1 
ATOM   6342 C  CZ    . ARG   C 2 253 ? 151.995 166.205 86.026  1.00 107.58 ? 253 ARG   D CZ    1 
ATOM   6343 N  NH1   . ARG   C 2 253 ? 153.196 166.753 85.954  1.00 107.77 ? 253 ARG   D NH1   1 
ATOM   6344 N  NH2   . ARG   C 2 253 ? 151.754 165.076 85.365  1.00 105.36 ? 253 ARG   D NH2   1 
ATOM   6345 N  N     . ASN   C 2 254 ? 150.554 173.598 87.992  1.00 106.77 ? 254 ASN   D N     1 
ATOM   6346 C  CA    . ASN   C 2 254 ? 150.412 174.707 88.928  1.00 105.11 ? 254 ASN   D CA    1 
ATOM   6347 C  C     . ASN   C 2 254 ? 149.098 175.448 88.716  1.00 104.31 ? 254 ASN   D C     1 
ATOM   6348 O  O     . ASN   C 2 254 ? 148.468 175.889 89.681  1.00 106.45 ? 254 ASN   D O     1 
ATOM   6349 C  CB    . ASN   C 2 254 ? 151.596 175.662 88.792  1.00 105.91 ? 254 ASN   D CB    1 
ATOM   6350 C  CG    . ASN   C 2 254 ? 152.864 175.106 89.404  1.00 108.38 ? 254 ASN   D CG    1 
ATOM   6351 O  OD1   . ASN   C 2 254 ? 152.945 173.920 89.723  1.00 107.48 ? 254 ASN   D OD1   1 
ATOM   6352 N  ND2   . ASN   C 2 254 ? 153.865 175.962 89.573  1.00 108.48 ? 254 ASN   D ND2   1 
ATOM   6353 N  N     . LYS   C 2 255 ? 148.676 175.605 87.460  1.00 104.95 ? 255 LYS   D N     1 
ATOM   6354 C  CA    . LYS   C 2 255 ? 147.391 176.243 87.191  1.00 105.03 ? 255 LYS   D CA    1 
ATOM   6355 C  C     . LYS   C 2 255 ? 146.238 175.418 87.748  1.00 105.19 ? 255 LYS   D C     1 
ATOM   6356 O  O     . LYS   C 2 255 ? 145.303 175.965 88.350  1.00 103.33 ? 255 LYS   D O     1 
ATOM   6357 C  CB    . LYS   C 2 255 ? 147.217 176.465 85.689  1.00 103.90 ? 255 LYS   D CB    1 
ATOM   6358 C  CG    . LYS   C 2 255 ? 147.654 177.839 85.212  1.00 104.89 ? 255 LYS   D CG    1 
ATOM   6359 C  CD    . LYS   C 2 255 ? 147.230 178.087 83.774  1.00 105.69 ? 255 LYS   D CD    1 
ATOM   6360 C  CE    . LYS   C 2 255 ? 145.720 178.004 83.621  1.00 106.57 ? 255 LYS   D CE    1 
ATOM   6361 N  NZ    . LYS   C 2 255 ? 145.306 177.984 82.191  1.00 104.34 ? 255 LYS   D NZ    1 
ATOM   6362 N  N     . LEU   C 2 256 ? 146.288 174.094 87.565  1.00 96.90  ? 256 LEU   D N     1 
ATOM   6363 C  CA    . LEU   C 2 256 ? 145.250 173.247 88.150  1.00 95.19  ? 256 LEU   D CA    1 
ATOM   6364 C  C     . LEU   C 2 256 ? 145.237 173.356 89.672  1.00 96.13  ? 256 LEU   D C     1 
ATOM   6365 O  O     . LEU   C 2 256 ? 144.167 173.459 90.288  1.00 94.41  ? 256 LEU   D O     1 
ATOM   6366 C  CB    . LEU   C 2 256 ? 145.445 171.792 87.722  1.00 95.01  ? 256 LEU   D CB    1 
ATOM   6367 C  CG    . LEU   C 2 256 ? 145.202 171.447 86.252  1.00 93.99  ? 256 LEU   D CG    1 
ATOM   6368 C  CD1   . LEU   C 2 256 ? 145.039 169.947 86.092  1.00 93.16  ? 256 LEU   D CD1   1 
ATOM   6369 C  CD2   . LEU   C 2 256 ? 143.983 172.180 85.718  1.00 94.50  ? 256 LEU   D CD2   1 
ATOM   6370 N  N     . ASP   C 2 257 ? 146.420 173.349 90.294  1.00 103.42 ? 257 ASP   D N     1 
ATOM   6371 C  CA    . ASP   C 2 257 ? 146.494 173.452 91.748  1.00 101.90 ? 257 ASP   D CA    1 
ATOM   6372 C  C     . ASP   C 2 257 ? 145.965 174.796 92.235  1.00 102.05 ? 257 ASP   D C     1 
ATOM   6373 O  O     . ASP   C 2 257 ? 145.289 174.870 93.267  1.00 101.97 ? 257 ASP   D O     1 
ATOM   6374 C  CB    . ASP   C 2 257 ? 147.933 173.242 92.216  1.00 102.88 ? 257 ASP   D CB    1 
ATOM   6375 C  CG    . ASP   C 2 257 ? 148.032 172.261 93.364  1.00 106.34 ? 257 ASP   D CG    1 
ATOM   6376 O  OD1   . ASP   C 2 257 ? 147.110 171.433 93.519  1.00 105.59 ? 257 ASP   D OD1   1 
ATOM   6377 O  OD2   . ASP   C 2 257 ? 149.030 172.316 94.113  1.00 105.34 ? 257 ASP   D OD2   1 
ATOM   6378 N  N     . GLU   C 2 258 ? 146.271 175.871 91.507  1.00 97.82  ? 258 GLU   D N     1 
ATOM   6379 C  CA    . GLU   C 2 258 ? 145.732 177.184 91.845  1.00 95.49  ? 258 GLU   D CA    1 
ATOM   6380 C  C     . GLU   C 2 258 ? 144.213 177.188 91.761  1.00 94.50  ? 258 GLU   D C     1 
ATOM   6381 O  O     . GLU   C 2 258 ? 143.536 177.757 92.626  1.00 96.23  ? 258 GLU   D O     1 
ATOM   6382 C  CB    . GLU   C 2 258 ? 146.326 178.243 90.917  1.00 97.93  ? 258 GLU   D CB    1 
ATOM   6383 C  CG    . GLU   C 2 258 ? 145.373 179.368 90.546  1.00 99.09  ? 258 GLU   D CG    1 
ATOM   6384 C  CD    . GLU   C 2 258 ? 145.869 180.188 89.370  1.00 100.21 ? 258 GLU   D CD    1 
ATOM   6385 O  OE1   . GLU   C 2 258 ? 147.100 180.272 89.178  1.00 99.11  ? 258 GLU   D OE1   1 
ATOM   6386 O  OE2   . GLU   C 2 258 ? 145.027 180.745 88.635  1.00 99.32  ? 258 GLU   D OE2   1 
ATOM   6387 N  N     . SER   C 2 259 ? 143.659 176.555 90.726  1.00 88.27  ? 259 SER   D N     1 
ATOM   6388 C  CA    . SER   C 2 259 ? 142.207 176.506 90.588  1.00 91.46  ? 259 SER   D CA    1 
ATOM   6389 C  C     . SER   C 2 259 ? 141.564 175.715 91.722  1.00 88.75  ? 259 SER   D C     1 
ATOM   6390 O  O     . SER   C 2 259 ? 140.477 176.068 92.196  1.00 83.21  ? 259 SER   D O     1 
ATOM   6391 C  CB    . SER   C 2 259 ? 141.826 175.906 89.234  1.00 91.59  ? 259 SER   D CB    1 
ATOM   6392 O  OG    . SER   C 2 259 ? 140.616 175.175 89.324  1.00 89.23  ? 259 SER   D OG    1 
ATOM   6393 N  N     . ARG   C 2 260 ? 142.215 174.638 92.171  1.00 89.40  ? 260 ARG   D N     1 
ATOM   6394 C  CA    . ARG   C 2 260 ? 141.562 173.732 93.115  1.00 88.33  ? 260 ARG   D CA    1 
ATOM   6395 C  C     . ARG   C 2 260 ? 141.524 174.298 94.535  1.00 88.99  ? 260 ARG   D C     1 
ATOM   6396 O  O     . ARG   C 2 260 ? 140.539 174.103 95.256  1.00 88.58  ? 260 ARG   D O     1 
ATOM   6397 C  CB    . ARG   C 2 260 ? 142.253 172.369 93.092  1.00 87.40  ? 260 ARG   D CB    1 
ATOM   6398 C  CG    . ARG   C 2 260 ? 141.815 171.492 91.930  1.00 86.07  ? 260 ARG   D CG    1 
ATOM   6399 C  CD    . ARG   C 2 260 ? 142.397 170.094 92.028  1.00 90.20  ? 260 ARG   D CD    1 
ATOM   6400 N  NE    . ARG   C 2 260 ? 141.361 169.070 92.007  1.00 90.15  ? 260 ARG   D NE    1 
ATOM   6401 C  CZ    . ARG   C 2 260 ? 141.596 167.766 92.045  1.00 85.00  ? 260 ARG   D CZ    1 
ATOM   6402 N  NH1   . ARG   C 2 260 ? 142.828 167.287 92.092  1.00 85.54  ? 260 ARG   D NH1   1 
ATOM   6403 N  NH2   . ARG   C 2 260 ? 140.570 166.920 92.035  1.00 82.70  ? 260 ARG   D NH2   1 
ATOM   6404 N  N     . PHE   C 2 261 ? 142.576 174.998 94.956  1.00 99.34  ? 261 PHE   D N     1 
ATOM   6405 C  CA    . PHE   C 2 261 ? 142.683 175.514 96.319  1.00 97.81  ? 261 PHE   D CA    1 
ATOM   6406 C  C     . PHE   C 2 261 ? 142.026 176.888 96.398  1.00 99.02  ? 261 PHE   D C     1 
ATOM   6407 O  O     . PHE   C 2 261 ? 142.158 177.692 95.469  1.00 96.33  ? 261 PHE   D O     1 
ATOM   6408 C  CB    . PHE   C 2 261 ? 144.144 175.614 96.759  1.00 94.38  ? 261 PHE   D CB    1 
ATOM   6409 C  CG    . PHE   C 2 261 ? 144.799 174.289 97.029  1.00 96.96  ? 261 PHE   D CG    1 
ATOM   6410 C  CD1   . PHE   C 2 261 ? 145.142 173.442 95.991  1.00 95.70  ? 261 PHE   D CD1   1 
ATOM   6411 C  CD2   . PHE   C 2 261 ? 145.088 173.900 98.325  1.00 98.74  ? 261 PHE   D CD2   1 
ATOM   6412 C  CE1   . PHE   C 2 261 ? 145.750 172.228 96.242  1.00 96.08  ? 261 PHE   D CE1   1 
ATOM   6413 C  CE2   . PHE   C 2 261 ? 145.696 172.687 98.579  1.00 95.97  ? 261 PHE   D CE2   1 
ATOM   6414 C  CZ    . PHE   C 2 261 ? 146.026 171.851 97.537  1.00 96.03  ? 261 PHE   D CZ    1 
ATOM   6415 N  N     . VAL   C 2 262 ? 141.326 177.163 97.503  1.00 105.41 ? 262 VAL   D N     1 
ATOM   6416 C  CA    . VAL   C 2 262 ? 140.775 178.496 97.732  1.00 103.61 ? 262 VAL   D CA    1 
ATOM   6417 C  C     . VAL   C 2 262 ? 140.605 178.731 99.227  1.00 103.41 ? 262 VAL   D C     1 
ATOM   6418 O  O     . VAL   C 2 262 ? 140.325 177.808 99.995  1.00 102.62 ? 262 VAL   D O     1 
ATOM   6419 C  CB    . VAL   C 2 262 ? 139.438 178.709 96.978  1.00 104.95 ? 262 VAL   D CB    1 
ATOM   6420 C  CG1   . VAL   C 2 262 ? 138.272 178.105 97.739  1.00 102.89 ? 262 VAL   D CG1   1 
ATOM   6421 C  CG2   . VAL   C 2 262 ? 139.206 180.190 96.716  1.00 103.42 ? 262 VAL   D CG2   1 
ATOM   6422 N  N     . ILE   C 2 263 ? 140.779 179.983 99.642  1.00 114.60 ? 263 ILE   D N     1 
ATOM   6423 C  CA    . ILE   C 2 263 ? 140.678 180.372 101.045 1.00 115.60 ? 263 ILE   D CA    1 
ATOM   6424 C  C     . ILE   C 2 263 ? 139.274 180.922 101.265 1.00 116.32 ? 263 ILE   D C     1 
ATOM   6425 O  O     . ILE   C 2 263 ? 138.980 182.070 100.925 1.00 115.39 ? 263 ILE   D O     1 
ATOM   6426 C  CB    . ILE   C 2 263 ? 141.750 181.393 101.433 1.00 115.90 ? 263 ILE   D CB    1 
ATOM   6427 C  CG1   . ILE   C 2 263 ? 143.121 180.955 100.913 1.00 115.51 ? 263 ILE   D CG1   1 
ATOM   6428 C  CG2   . ILE   C 2 263 ? 141.786 181.577 102.942 1.00 113.64 ? 263 ILE   D CG2   1 
ATOM   6429 C  CD1   . ILE   C 2 263 ? 144.266 181.795 101.434 1.00 114.37 ? 263 ILE   D CD1   1 
ATOM   6430 N  N     . LYS   C 2 264 ? 138.404 180.101 101.849 1.00 113.27 ? 264 LYS   D N     1 
ATOM   6431 C  CA    . LYS   C 2 264 ? 137.033 180.504 102.146 1.00 111.17 ? 264 LYS   D CA    1 
ATOM   6432 C  C     . LYS   C 2 264 ? 136.392 179.539 103.138 1.00 112.14 ? 264 LYS   D C     1 
ATOM   6433 O  O     . LYS   C 2 264 ? 136.849 178.409 103.307 1.00 113.43 ? 264 LYS   D O     1 
ATOM   6434 C  CB    . LYS   C 2 264 ? 136.197 180.574 100.864 1.00 109.28 ? 264 LYS   D CB    1 
ATOM   6435 C  CG    . LYS   C 2 264 ? 135.837 179.219 100.275 1.00 110.59 ? 264 LYS   D CG    1 
ATOM   6436 C  CD    . LYS   C 2 264 ? 134.357 178.916 100.445 1.00 111.32 ? 264 LYS   D CD    1 
ATOM   6437 C  CE    . LYS   C 2 264 ? 134.032 177.493 100.022 1.00 111.67 ? 264 LYS   D CE    1 
ATOM   6438 N  NZ    . LYS   C 2 264 ? 132.574 177.205 100.114 1.00 108.75 ? 264 LYS   D NZ    1 
ATOM   6439 O  OXT   . LYS   C 2 264 ? 135.399 179.863 103.789 1.00 111.24 ? 264 LYS   D OXT   1 
ATOM   6440 N  N     . MET   D 1 25  ? 116.132 164.252 121.325 1.00 101.97 ? 1   MET   C N     1 
ATOM   6441 C  CA    . MET   D 1 25  ? 115.077 163.270 121.549 1.00 104.66 ? 1   MET   C CA    1 
ATOM   6442 C  C     . MET   D 1 25  ? 115.012 162.272 120.399 1.00 102.93 ? 1   MET   C C     1 
ATOM   6443 O  O     . MET   D 1 25  ? 114.681 161.103 120.596 1.00 100.90 ? 1   MET   C O     1 
ATOM   6444 C  CB    . MET   D 1 25  ? 113.725 163.965 121.725 1.00 105.47 ? 1   MET   C CB    1 
ATOM   6445 C  CG    . MET   D 1 25  ? 113.792 165.250 122.533 1.00 105.07 ? 1   MET   C CG    1 
ATOM   6446 S  SD    . MET   D 1 25  ? 113.243 165.031 124.236 1.00 103.73 ? 1   MET   C SD    1 
ATOM   6447 C  CE    . MET   D 1 25  ? 113.194 166.732 124.795 1.00 101.50 ? 1   MET   C CE    1 
ATOM   6448 N  N     . SER   D 1 26  ? 115.325 162.744 119.191 1.00 105.23 ? 2   SER   C N     1 
ATOM   6449 C  CA    . SER   D 1 26  ? 115.374 161.854 118.037 1.00 105.82 ? 2   SER   C CA    1 
ATOM   6450 C  C     . SER   D 1 26  ? 116.615 160.973 118.055 1.00 106.45 ? 2   SER   C C     1 
ATOM   6451 O  O     . SER   D 1 26  ? 116.580 159.849 117.538 1.00 107.20 ? 2   SER   C O     1 
ATOM   6452 C  CB    . SER   D 1 26  ? 115.327 162.666 116.743 1.00 106.08 ? 2   SER   C CB    1 
ATOM   6453 O  OG    . SER   D 1 26  ? 114.503 163.809 116.887 1.00 108.53 ? 2   SER   C OG    1 
ATOM   6454 N  N     . ALA   D 1 27  ? 117.712 161.462 118.638 1.00 92.17  ? 3   ALA   C N     1 
ATOM   6455 C  CA    . ALA   D 1 27  ? 118.939 160.677 118.706 1.00 90.22  ? 3   ALA   C CA    1 
ATOM   6456 C  C     . ALA   D 1 27  ? 118.753 159.423 119.551 1.00 90.52  ? 3   ALA   C C     1 
ATOM   6457 O  O     . ALA   D 1 27  ? 119.222 158.340 119.178 1.00 89.96  ? 3   ALA   C O     1 
ATOM   6458 C  CB    . ALA   D 1 27  ? 120.074 161.535 119.260 1.00 91.60  ? 3   ALA   C CB    1 
ATOM   6459 N  N     . ILE   D 1 28  ? 118.076 159.552 120.694 1.00 80.75  ? 4   ILE   C N     1 
ATOM   6460 C  CA    . ILE   D 1 28  ? 117.859 158.405 121.569 1.00 80.27  ? 4   ILE   C CA    1 
ATOM   6461 C  C     . ILE   D 1 28  ? 117.024 157.346 120.861 1.00 79.39  ? 4   ILE   C C     1 
ATOM   6462 O  O     . ILE   D 1 28  ? 117.353 156.154 120.881 1.00 80.39  ? 4   ILE   C O     1 
ATOM   6463 C  CB    . ILE   D 1 28  ? 117.202 158.855 122.886 1.00 80.90  ? 4   ILE   C CB    1 
ATOM   6464 C  CG1   . ILE   D 1 28  ? 118.141 159.780 123.661 1.00 78.66  ? 4   ILE   C CG1   1 
ATOM   6465 C  CG2   . ILE   D 1 28  ? 116.809 157.650 123.726 1.00 81.96  ? 4   ILE   C CG2   1 
ATOM   6466 C  CD1   . ILE   D 1 28  ? 117.735 159.999 125.097 1.00 79.67  ? 4   ILE   C CD1   1 
ATOM   6467 N  N     . GLY   D 1 29  ? 115.933 157.768 120.219 1.00 78.59  ? 5   GLY   C N     1 
ATOM   6468 C  CA    . GLY   D 1 29  ? 115.106 156.822 119.491 1.00 77.14  ? 5   GLY   C CA    1 
ATOM   6469 C  C     . GLY   D 1 29  ? 115.844 156.170 118.339 1.00 79.57  ? 5   GLY   C C     1 
ATOM   6470 O  O     . GLY   D 1 29  ? 115.697 154.969 118.098 1.00 81.53  ? 5   GLY   C O     1 
ATOM   6471 N  N     . THR   D 1 30  ? 116.656 156.947 117.619 1.00 83.80  ? 6   THR   C N     1 
ATOM   6472 C  CA    . THR   D 1 30  ? 117.421 156.394 116.505 1.00 85.99  ? 6   THR   C CA    1 
ATOM   6473 C  C     . THR   D 1 30  ? 118.407 155.337 116.987 1.00 85.88  ? 6   THR   C C     1 
ATOM   6474 O  O     . THR   D 1 30  ? 118.493 154.246 116.411 1.00 83.67  ? 6   THR   C O     1 
ATOM   6475 C  CB    . THR   D 1 30  ? 118.152 157.513 115.765 1.00 87.00  ? 6   THR   C CB    1 
ATOM   6476 O  OG1   . THR   D 1 30  ? 117.276 158.637 115.610 1.00 87.64  ? 6   THR   C OG1   1 
ATOM   6477 C  CG2   . THR   D 1 30  ? 118.601 157.038 114.395 1.00 84.83  ? 6   THR   C CG2   1 
ATOM   6478 N  N     . VAL   D 1 31  ? 119.155 155.640 118.052 1.00 78.20  ? 7   VAL   C N     1 
ATOM   6479 C  CA    . VAL   D 1 31  ? 120.132 154.685 118.570 1.00 77.42  ? 7   VAL   C CA    1 
ATOM   6480 C  C     . VAL   D 1 31  ? 119.436 153.438 119.104 1.00 77.51  ? 7   VAL   C C     1 
ATOM   6481 O  O     . VAL   D 1 31  ? 119.898 152.310 118.885 1.00 73.42  ? 7   VAL   C O     1 
ATOM   6482 C  CB    . VAL   D 1 31  ? 121.013 155.352 119.641 1.00 74.31  ? 7   VAL   C CB    1 
ATOM   6483 C  CG1   . VAL   D 1 31  ? 121.871 154.316 120.347 1.00 75.56  ? 7   VAL   C CG1   1 
ATOM   6484 C  CG2   . VAL   D 1 31  ? 121.886 156.425 119.013 1.00 72.17  ? 7   VAL   C CG2   1 
ATOM   6485 N  N     . PHE   D 1 32  ? 118.313 153.617 119.807 1.00 82.82  ? 8   PHE   C N     1 
ATOM   6486 C  CA    . PHE   D 1 32  ? 117.578 152.468 120.325 1.00 79.71  ? 8   PHE   C CA    1 
ATOM   6487 C  C     . PHE   D 1 32  ? 117.069 151.583 119.194 1.00 81.38  ? 8   PHE   C C     1 
ATOM   6488 O  O     . PHE   D 1 32  ? 117.150 150.353 119.277 1.00 85.27  ? 8   PHE   C O     1 
ATOM   6489 C  CB    . PHE   D 1 32  ? 116.419 152.943 121.201 1.00 79.08  ? 8   PHE   C CB    1 
ATOM   6490 C  CG    . PHE   D 1 32  ? 115.686 151.829 121.891 1.00 83.61  ? 8   PHE   C CG    1 
ATOM   6491 C  CD1   . PHE   D 1 32  ? 116.229 151.212 123.006 1.00 83.92  ? 8   PHE   C CD1   1 
ATOM   6492 C  CD2   . PHE   D 1 32  ? 114.456 151.398 121.426 1.00 85.35  ? 8   PHE   C CD2   1 
ATOM   6493 C  CE1   . PHE   D 1 32  ? 115.558 150.187 123.642 1.00 83.63  ? 8   PHE   C CE1   1 
ATOM   6494 C  CE2   . PHE   D 1 32  ? 113.781 150.373 122.058 1.00 84.15  ? 8   PHE   C CE2   1 
ATOM   6495 C  CZ    . PHE   D 1 32  ? 114.334 149.767 123.169 1.00 82.85  ? 8   PHE   C CZ    1 
ATOM   6496 N  N     . LYS   D 1 33  ? 116.543 152.190 118.126 1.00 94.33  ? 9   LYS   C N     1 
ATOM   6497 C  CA    . LYS   D 1 33  ? 116.071 151.407 116.989 1.00 94.42  ? 9   LYS   C CA    1 
ATOM   6498 C  C     . LYS   D 1 33  ? 117.218 150.670 116.308 1.00 96.79  ? 9   LYS   C C     1 
ATOM   6499 O  O     . LYS   D 1 33  ? 117.075 149.498 115.933 1.00 100.61 ? 9   LYS   C O     1 
ATOM   6500 C  CB    . LYS   D 1 33  ? 115.348 152.316 115.996 1.00 97.44  ? 9   LYS   C CB    1 
ATOM   6501 C  CG    . LYS   D 1 33  ? 113.903 152.606 116.367 1.00 100.07 ? 9   LYS   C CG    1 
ATOM   6502 C  CD    . LYS   D 1 33  ? 113.309 153.693 115.486 1.00 99.02  ? 9   LYS   C CD    1 
ATOM   6503 C  CE    . LYS   D 1 33  ? 112.510 154.691 116.309 1.00 99.11  ? 9   LYS   C CE    1 
ATOM   6504 N  NZ    . LYS   D 1 33  ? 112.365 155.999 115.611 1.00 100.33 ? 9   LYS   C NZ    1 
ATOM   6505 N  N     . GLU   D 1 34  ? 118.365 151.336 116.147 1.00 86.43  ? 10  GLU   C N     1 
ATOM   6506 C  CA    . GLU   D 1 34  ? 119.521 150.690 115.532 1.00 84.77  ? 10  GLU   C CA    1 
ATOM   6507 C  C     . GLU   D 1 34  ? 119.980 149.491 116.349 1.00 87.03  ? 10  GLU   C C     1 
ATOM   6508 O  O     . GLU   D 1 34  ? 120.324 148.441 115.795 1.00 86.34  ? 10  GLU   C O     1 
ATOM   6509 C  CB    . GLU   D 1 34  ? 120.663 151.694 115.369 1.00 85.78  ? 10  GLU   C CB    1 
ATOM   6510 C  CG    . GLU   D 1 34  ? 120.372 152.833 114.410 1.00 88.64  ? 10  GLU   C CG    1 
ATOM   6511 C  CD    . GLU   D 1 34  ? 121.489 153.856 114.368 1.00 91.89  ? 10  GLU   C CD    1 
ATOM   6512 O  OE1   . GLU   D 1 34  ? 121.188 155.067 114.378 1.00 92.26  ? 10  GLU   C OE1   1 
ATOM   6513 O  OE2   . GLU   D 1 34  ? 122.669 153.453 114.339 1.00 91.88  ? 10  GLU   C OE2   1 
ATOM   6514 N  N     . HIS   D 1 35  ? 120.001 149.631 117.676 1.00 82.20  ? 11  HIS   C N     1 
ATOM   6515 C  CA    . HIS   D 1 35  ? 120.447 148.524 118.518 1.00 76.80  ? 11  HIS   C CA    1 
ATOM   6516 C  C     . HIS   D 1 35  ? 119.428 147.390 118.542 1.00 74.07  ? 11  HIS   C C     1 
ATOM   6517 O  O     . HIS   D 1 35  ? 119.806 146.213 118.543 1.00 75.16  ? 11  HIS   C O     1 
ATOM   6518 C  CB    . HIS   D 1 35  ? 120.741 149.020 119.932 1.00 74.41  ? 11  HIS   C CB    1 
ATOM   6519 C  CG    . HIS   D 1 35  ? 122.119 149.578 120.096 1.00 77.20  ? 11  HIS   C CG    1 
ATOM   6520 N  ND1   . HIS   D 1 35  ? 122.407 150.915 119.932 1.00 73.88  ? 11  HIS   C ND1   1 
ATOM   6521 C  CD2   . HIS   D 1 35  ? 123.293 148.975 120.396 1.00 75.95  ? 11  HIS   C CD2   1 
ATOM   6522 C  CE1   . HIS   D 1 35  ? 123.697 151.114 120.132 1.00 72.67  ? 11  HIS   C CE1   1 
ATOM   6523 N  NE2   . HIS   D 1 35  ? 124.258 149.952 120.414 1.00 71.63  ? 11  HIS   C NE2   1 
ATOM   6524 N  N     . VAL   D 1 36  ? 118.135 147.719 118.562 1.00 71.90  ? 12  VAL   C N     1 
ATOM   6525 C  CA    . VAL   D 1 36  ? 117.109 146.682 118.600 1.00 71.29  ? 12  VAL   C CA    1 
ATOM   6526 C  C     . VAL   D 1 36  ? 117.090 145.894 117.296 1.00 76.38  ? 12  VAL   C C     1 
ATOM   6527 O  O     . VAL   D 1 36  ? 116.928 144.667 117.298 1.00 81.87  ? 12  VAL   C O     1 
ATOM   6528 C  CB    . VAL   D 1 36  ? 115.736 147.307 118.913 1.00 77.57  ? 12  VAL   C CB    1 
ATOM   6529 C  CG1   . VAL   D 1 36  ? 114.610 146.375 118.497 1.00 76.86  ? 12  VAL   C CG1   1 
ATOM   6530 C  CG2   . VAL   D 1 36  ? 115.634 147.636 120.393 1.00 78.38  ? 12  VAL   C CG2   1 
ATOM   6531 N  N     . LYS   D 1 37  ? 117.265 146.578 116.162 1.00 82.63  ? 13  LYS   C N     1 
ATOM   6532 C  CA    . LYS   D 1 37  ? 117.173 145.899 114.874 1.00 80.98  ? 13  LYS   C CA    1 
ATOM   6533 C  C     . LYS   D 1 37  ? 118.331 144.932 114.642 1.00 84.20  ? 13  LYS   C C     1 
ATOM   6534 O  O     . LYS   D 1 37  ? 118.150 143.904 113.979 1.00 83.42  ? 13  LYS   C O     1 
ATOM   6535 C  CB    . LYS   D 1 37  ? 117.111 146.927 113.743 1.00 80.37  ? 13  LYS   C CB    1 
ATOM   6536 C  CG    . LYS   D 1 37  ? 115.710 147.444 113.444 1.00 85.69  ? 13  LYS   C CG    1 
ATOM   6537 C  CD    . LYS   D 1 37  ? 114.655 146.373 113.673 1.00 86.13  ? 13  LYS   C CD    1 
ATOM   6538 C  CE    . LYS   D 1 37  ? 113.446 146.583 112.776 1.00 86.09  ? 13  LYS   C CE    1 
ATOM   6539 N  NZ    . LYS   D 1 37  ? 112.226 145.931 113.326 1.00 83.95  ? 13  LYS   C NZ    1 
ATOM   6540 N  N     . ASN   D 1 38  ? 119.518 145.232 115.173 1.00 85.09  ? 14  ASN   C N     1 
ATOM   6541 C  CA    . ASN   D 1 38  ? 120.732 144.483 114.866 1.00 80.29  ? 14  ASN   C CA    1 
ATOM   6542 C  C     . ASN   D 1 38  ? 121.243 143.671 116.055 1.00 82.96  ? 14  ASN   C C     1 
ATOM   6543 O  O     . ASN   D 1 38  ? 122.451 143.601 116.290 1.00 87.19  ? 14  ASN   C O     1 
ATOM   6544 C  CB    . ASN   D 1 38  ? 121.821 145.431 114.369 1.00 79.92  ? 14  ASN   C CB    1 
ATOM   6545 C  CG    . ASN   D 1 38  ? 121.512 146.003 113.004 1.00 83.84  ? 14  ASN   C CG    1 
ATOM   6546 O  OD1   . ASN   D 1 38  ? 120.396 145.875 112.503 1.00 87.19  ? 14  ASN   C OD1   1 
ATOM   6547 N  ND2   . ASN   D 1 38  ? 122.502 146.638 112.391 1.00 85.11  ? 14  ASN   C ND2   1 
ATOM   6548 N  N     . PHE   D 1 39  ? 120.335 143.054 116.813 1.00 88.25  ? 15  PHE   C N     1 
ATOM   6549 C  CA    . PHE   D 1 39  ? 120.733 142.291 117.994 1.00 88.65  ? 15  PHE   C CA    1 
ATOM   6550 C  C     . PHE   D 1 39  ? 121.541 141.050 117.614 1.00 91.24  ? 15  PHE   C C     1 
ATOM   6551 O  O     . PHE   D 1 39  ? 122.635 140.812 118.144 1.00 94.36  ? 15  PHE   C O     1 
ATOM   6552 C  CB    . PHE   D 1 39  ? 119.481 141.912 118.789 1.00 88.80  ? 15  PHE   C CB    1 
ATOM   6553 C  CG    . PHE   D 1 39  ? 119.737 140.970 119.929 1.00 95.43  ? 15  PHE   C CG    1 
ATOM   6554 C  CD1   . PHE   D 1 39  ? 120.433 141.387 121.050 1.00 95.40  ? 15  PHE   C CD1   1 
ATOM   6555 C  CD2   . PHE   D 1 39  ? 119.258 139.672 119.888 1.00 95.23  ? 15  PHE   C CD2   1 
ATOM   6556 C  CE1   . PHE   D 1 39  ? 120.658 140.522 122.102 1.00 92.15  ? 15  PHE   C CE1   1 
ATOM   6557 C  CE2   . PHE   D 1 39  ? 119.481 138.804 120.937 1.00 93.20  ? 15  PHE   C CE2   1 
ATOM   6558 C  CZ    . PHE   D 1 39  ? 120.182 139.229 122.045 1.00 92.26  ? 15  PHE   C CZ    1 
ATOM   6559 N  N     . TYR   D 1 40  ? 121.017 140.253 116.678 1.00 95.09  ? 16  TYR   C N     1 
ATOM   6560 C  CA    . TYR   D 1 40  ? 121.694 139.020 116.288 1.00 95.45  ? 16  TYR   C CA    1 
ATOM   6561 C  C     . TYR   D 1 40  ? 123.000 139.313 115.561 1.00 93.04  ? 16  TYR   C C     1 
ATOM   6562 O  O     . TYR   D 1 40  ? 123.981 138.575 115.714 1.00 95.94  ? 16  TYR   C O     1 
ATOM   6563 C  CB    . TYR   D 1 40  ? 120.771 138.169 115.417 1.00 94.96  ? 16  TYR   C CB    1 
ATOM   6564 C  CG    . TYR   D 1 40  ? 119.534 137.680 116.137 1.00 99.73  ? 16  TYR   C CG    1 
ATOM   6565 C  CD1   . TYR   D 1 40  ? 119.524 136.453 116.785 1.00 100.96 ? 16  TYR   C CD1   1 
ATOM   6566 C  CD2   . TYR   D 1 40  ? 118.376 138.446 116.167 1.00 99.26  ? 16  TYR   C CD2   1 
ATOM   6567 C  CE1   . TYR   D 1 40  ? 118.396 136.002 117.443 1.00 100.16 ? 16  TYR   C CE1   1 
ATOM   6568 C  CE2   . TYR   D 1 40  ? 117.244 138.004 116.822 1.00 98.28  ? 16  TYR   C CE2   1 
ATOM   6569 C  CZ    . TYR   D 1 40  ? 117.259 136.782 117.459 1.00 99.51  ? 16  TYR   C CZ    1 
ATOM   6570 O  OH    . TYR   D 1 40  ? 116.135 136.337 118.114 1.00 99.62  ? 16  TYR   C OH    1 
ATOM   6571 N  N     . LEU   D 1 41  ? 123.030 140.381 114.762 1.00 67.38  ? 17  LEU   C N     1 
ATOM   6572 C  CA    . LEU   D 1 41  ? 124.276 140.785 114.120 1.00 68.52  ? 17  LEU   C CA    1 
ATOM   6573 C  C     . LEU   D 1 41  ? 125.327 141.154 115.157 1.00 74.00  ? 17  LEU   C C     1 
ATOM   6574 O  O     . LEU   D 1 41  ? 126.503 140.799 115.015 1.00 75.54  ? 17  LEU   C O     1 
ATOM   6575 C  CB    . LEU   D 1 41  ? 124.021 141.955 113.171 1.00 68.05  ? 17  LEU   C CB    1 
ATOM   6576 C  CG    . LEU   D 1 41  ? 125.219 142.438 112.353 1.00 70.83  ? 17  LEU   C CG    1 
ATOM   6577 C  CD1   . LEU   D 1 41  ? 125.394 141.583 111.112 1.00 74.32  ? 17  LEU   C CD1   1 
ATOM   6578 C  CD2   . LEU   D 1 41  ? 125.065 143.903 111.980 1.00 69.86  ? 17  LEU   C CD2   1 
ATOM   6579 N  N     . ILE   D 1 42  ? 124.920 141.864 116.212 1.00 77.43  ? 18  ILE   C N     1 
ATOM   6580 C  CA    . ILE   D 1 42  ? 125.844 142.215 117.287 1.00 71.56  ? 18  ILE   C CA    1 
ATOM   6581 C  C     . ILE   D 1 42  ? 126.386 140.954 117.948 1.00 75.00  ? 18  ILE   C C     1 
ATOM   6582 O  O     . ILE   D 1 42  ? 127.593 140.829 118.196 1.00 80.43  ? 18  ILE   C O     1 
ATOM   6583 C  CB    . ILE   D 1 42  ? 125.149 143.134 118.310 1.00 67.54  ? 18  ILE   C CB    1 
ATOM   6584 C  CG1   . ILE   D 1 42  ? 125.158 144.584 117.824 1.00 71.54  ? 18  ILE   C CG1   1 
ATOM   6585 C  CG2   . ILE   D 1 42  ? 125.810 143.023 119.674 1.00 74.63  ? 18  ILE   C CG2   1 
ATOM   6586 C  CD1   . ILE   D 1 42  ? 124.112 145.449 118.485 1.00 71.47  ? 18  ILE   C CD1   1 
ATOM   6587 N  N     . GLN   D 1 43  ? 125.500 139.994 118.232 1.00 72.87  ? 19  GLN   C N     1 
ATOM   6588 C  CA    . GLN   D 1 43  ? 125.943 138.754 118.865 1.00 72.53  ? 19  GLN   C CA    1 
ATOM   6589 C  C     . GLN   D 1 43  ? 126.941 138.005 117.987 1.00 74.49  ? 19  GLN   C C     1 
ATOM   6590 O  O     . GLN   D 1 43  ? 127.981 137.540 118.470 1.00 78.60  ? 19  GLN   C O     1 
ATOM   6591 C  CB    . GLN   D 1 43  ? 124.739 137.869 119.180 1.00 73.45  ? 19  GLN   C CB    1 
ATOM   6592 C  CG    . GLN   D 1 43  ? 123.915 138.340 120.365 1.00 75.91  ? 19  GLN   C CG    1 
ATOM   6593 C  CD    . GLN   D 1 43  ? 122.944 137.286 120.849 1.00 78.15  ? 19  GLN   C CD    1 
ATOM   6594 O  OE1   . GLN   D 1 43  ? 122.281 136.622 120.052 1.00 76.15  ? 19  GLN   C OE1   1 
ATOM   6595 N  NE2   . GLN   D 1 43  ? 122.853 137.122 122.163 1.00 78.12  ? 19  GLN   C NE2   1 
ATOM   6596 N  N     . ARG   D 1 44  ? 126.643 137.886 116.690 1.00 74.52  ? 20  ARG   C N     1 
ATOM   6597 C  CA    . ARG   D 1 44  ? 127.528 137.152 115.790 1.00 70.93  ? 20  ARG   C CA    1 
ATOM   6598 C  C     . ARG   D 1 44  ? 128.874 137.850 115.635 1.00 67.97  ? 20  ARG   C C     1 
ATOM   6599 O  O     . ARG   D 1 44  ? 129.922 137.193 115.610 1.00 72.28  ? 20  ARG   C O     1 
ATOM   6600 C  CB    . ARG   D 1 44  ? 126.857 136.968 114.431 1.00 69.97  ? 20  ARG   C CB    1 
ATOM   6601 C  CG    . ARG   D 1 44  ? 126.046 135.690 114.313 1.00 72.92  ? 20  ARG   C CG    1 
ATOM   6602 C  CD    . ARG   D 1 44  ? 125.173 135.703 113.070 1.00 77.16  ? 20  ARG   C CD    1 
ATOM   6603 N  NE    . ARG   D 1 44  ? 123.804 135.293 113.355 1.00 75.53  ? 20  ARG   C NE    1 
ATOM   6604 C  CZ    . ARG   D 1 44  ? 122.729 135.839 112.801 1.00 75.54  ? 20  ARG   C CZ    1 
ATOM   6605 N  NH1   . ARG   D 1 44  ? 122.828 136.827 111.928 1.00 73.30  ? 20  ARG   C NH1   1 
ATOM   6606 N  NH2   . ARG   D 1 44  ? 121.525 135.384 113.135 1.00 75.57  ? 20  ARG   C NH2   1 
ATOM   6607 N  N     . LEU   D 1 45  ? 128.869 139.181 115.528 1.00 60.18  ? 21  LEU   C N     1 
ATOM   6608 C  CA    . LEU   D 1 45  ? 130.126 139.910 115.416 1.00 63.31  ? 21  LEU   C CA    1 
ATOM   6609 C  C     . LEU   D 1 45  ? 130.964 139.781 116.682 1.00 69.35  ? 21  LEU   C C     1 
ATOM   6610 O  O     . LEU   D 1 45  ? 132.192 139.665 116.600 1.00 70.21  ? 21  LEU   C O     1 
ATOM   6611 C  CB    . LEU   D 1 45  ? 129.854 141.379 115.094 1.00 75.08  ? 21  LEU   C CB    1 
ATOM   6612 C  CG    . LEU   D 1 45  ? 129.347 141.659 113.676 1.00 71.20  ? 21  LEU   C CG    1 
ATOM   6613 C  CD1   . LEU   D 1 45  ? 128.941 143.114 113.523 1.00 65.57  ? 21  LEU   C CD1   1 
ATOM   6614 C  CD2   . LEU   D 1 45  ? 130.393 141.280 112.642 1.00 70.30  ? 21  LEU   C CD2   1 
ATOM   6615 N  N     . ALA   D 1 46  ? 130.327 139.795 117.857 1.00 78.20  ? 22  ALA   C N     1 
ATOM   6616 C  CA    . ALA   D 1 46  ? 131.066 139.565 119.095 1.00 71.71  ? 22  ALA   C CA    1 
ATOM   6617 C  C     . ALA   D 1 46  ? 131.670 138.166 119.130 1.00 75.65  ? 22  ALA   C C     1 
ATOM   6618 O  O     . ALA   D 1 46  ? 132.830 137.990 119.533 1.00 79.33  ? 22  ALA   C O     1 
ATOM   6619 C  CB    . ALA   D 1 46  ? 130.152 139.784 120.299 1.00 65.29  ? 22  ALA   C CB    1 
ATOM   6620 N  N     . GLN   D 1 47  ? 130.898 137.158 118.712 1.00 70.16  ? 23  GLN   C N     1 
ATOM   6621 C  CA    . GLN   D 1 47  ? 131.420 135.795 118.675 1.00 68.28  ? 23  GLN   C CA    1 
ATOM   6622 C  C     . GLN   D 1 47  ? 132.599 135.673 117.719 1.00 68.92  ? 23  GLN   C C     1 
ATOM   6623 O  O     . GLN   D 1 47  ? 133.548 134.931 117.995 1.00 71.26  ? 23  GLN   C O     1 
ATOM   6624 C  CB    . GLN   D 1 47  ? 130.318 134.816 118.277 1.00 65.55  ? 23  GLN   C CB    1 
ATOM   6625 C  CG    . GLN   D 1 47  ? 129.200 134.690 119.294 1.00 72.02  ? 23  GLN   C CG    1 
ATOM   6626 C  CD    . GLN   D 1 47  ? 128.461 133.374 119.186 1.00 72.33  ? 23  GLN   C CD    1 
ATOM   6627 O  OE1   . GLN   D 1 47  ? 127.232 133.340 119.169 1.00 73.37  ? 23  GLN   C OE1   1 
ATOM   6628 N  NE2   . GLN   D 1 47  ? 129.209 132.281 119.110 1.00 72.39  ? 23  GLN   C NE2   1 
ATOM   6629 N  N     . PHE   D 1 48  ? 132.555 136.384 116.591 1.00 74.85  ? 24  PHE   C N     1 
ATOM   6630 C  CA    . PHE   D 1 48  ? 133.675 136.351 115.655 1.00 74.97  ? 24  PHE   C CA    1 
ATOM   6631 C  C     . PHE   D 1 48  ? 134.896 137.077 116.209 1.00 72.45  ? 24  PHE   C C     1 
ATOM   6632 O  O     . PHE   D 1 48  ? 136.030 136.626 116.017 1.00 75.53  ? 24  PHE   C O     1 
ATOM   6633 C  CB    . PHE   D 1 48  ? 133.265 136.957 114.314 1.00 81.08  ? 24  PHE   C CB    1 
ATOM   6634 C  CG    . PHE   D 1 48  ? 133.826 136.229 113.131 1.00 77.48  ? 24  PHE   C CG    1 
ATOM   6635 C  CD1   . PHE   D 1 48  ? 135.102 136.508 112.676 1.00 78.24  ? 24  PHE   C CD1   1 
ATOM   6636 C  CD2   . PHE   D 1 48  ? 133.083 135.263 112.479 1.00 77.28  ? 24  PHE   C CD2   1 
ATOM   6637 C  CE1   . PHE   D 1 48  ? 135.624 135.838 111.592 1.00 79.77  ? 24  PHE   C CE1   1 
ATOM   6638 C  CE2   . PHE   D 1 48  ? 133.602 134.591 111.394 1.00 81.50  ? 24  PHE   C CE2   1 
ATOM   6639 C  CZ    . PHE   D 1 48  ? 134.874 134.878 110.949 1.00 80.46  ? 24  PHE   C CZ    1 
ATOM   6640 N  N     . GLN   D 1 49  ? 134.687 138.207 116.890 1.00 78.85  ? 25  GLN   C N     1 
ATOM   6641 C  CA    . GLN   D 1 49  ? 135.808 138.935 117.475 1.00 79.17  ? 25  GLN   C CA    1 
ATOM   6642 C  C     . GLN   D 1 49  ? 136.494 138.123 118.567 1.00 77.42  ? 25  GLN   C C     1 
ATOM   6643 O  O     . GLN   D 1 49  ? 137.723 138.189 118.709 1.00 73.18  ? 25  GLN   C O     1 
ATOM   6644 C  CB    . GLN   D 1 49  ? 135.331 140.276 118.029 1.00 74.97  ? 25  GLN   C CB    1 
ATOM   6645 C  CG    . GLN   D 1 49  ? 136.395 141.050 118.782 1.00 74.49  ? 25  GLN   C CG    1 
ATOM   6646 C  CD    . GLN   D 1 49  ? 136.675 142.398 118.159 1.00 81.85  ? 25  GLN   C CD    1 
ATOM   6647 O  OE1   . GLN   D 1 49  ? 135.757 143.175 117.901 1.00 85.96  ? 25  GLN   C OE1   1 
ATOM   6648 N  NE2   . GLN   D 1 49  ? 137.947 142.684 117.911 1.00 80.50  ? 25  GLN   C NE2   1 
ATOM   6649 N  N     . VAL   D 1 50  ? 135.720 137.358 119.343 1.00 82.57  ? 26  VAL   C N     1 
ATOM   6650 C  CA    . VAL   D 1 50  ? 136.315 136.502 120.365 1.00 82.85  ? 26  VAL   C CA    1 
ATOM   6651 C  C     . VAL   D 1 50  ? 137.308 135.533 119.734 1.00 90.65  ? 26  VAL   C C     1 
ATOM   6652 O  O     . VAL   D 1 50  ? 138.420 135.339 120.242 1.00 88.56  ? 26  VAL   C O     1 
ATOM   6653 C  CB    . VAL   D 1 50  ? 135.215 135.760 121.148 1.00 81.68  ? 26  VAL   C CB    1 
ATOM   6654 C  CG1   . VAL   D 1 50  ? 135.738 134.445 121.703 1.00 83.22  ? 26  VAL   C CG1   1 
ATOM   6655 C  CG2   . VAL   D 1 50  ? 134.678 136.636 122.263 1.00 83.69  ? 26  VAL   C CG2   1 
ATOM   6656 N  N     . LYS   D 1 51  ? 136.929 134.917 118.610 1.00 100.16 ? 27  LYS   C N     1 
ATOM   6657 C  CA    . LYS   D 1 51  ? 137.845 134.025 117.905 1.00 94.80  ? 27  LYS   C CA    1 
ATOM   6658 C  C     . LYS   D 1 51  ? 139.012 134.784 117.286 1.00 90.89  ? 27  LYS   C C     1 
ATOM   6659 O  O     . LYS   D 1 51  ? 140.132 134.264 117.241 1.00 91.13  ? 27  LYS   C O     1 
ATOM   6660 C  CB    . LYS   D 1 51  ? 137.097 133.252 116.819 1.00 91.06  ? 27  LYS   C CB    1 
ATOM   6661 C  CG    . LYS   D 1 51  ? 136.162 132.175 117.338 1.00 93.32  ? 27  LYS   C CG    1 
ATOM   6662 C  CD    . LYS   D 1 51  ? 135.713 131.260 116.209 1.00 95.60  ? 27  LYS   C CD    1 
ATOM   6663 C  CE    . LYS   D 1 51  ? 134.204 131.086 116.201 1.00 96.68  ? 27  LYS   C CE    1 
ATOM   6664 N  NZ    . LYS   D 1 51  ? 133.628 131.335 114.851 1.00 95.48  ? 27  LYS   C NZ    1 
ATOM   6665 N  N     . ILE   D 1 52  ? 138.767 136.000 116.794 1.00 85.30  ? 28  ILE   C N     1 
ATOM   6666 C  CA    . ILE   D 1 52  ? 139.824 136.762 116.136 1.00 83.25  ? 28  ILE   C CA    1 
ATOM   6667 C  C     . ILE   D 1 52  ? 140.937 137.107 117.120 1.00 85.09  ? 28  ILE   C C     1 
ATOM   6668 O  O     . ILE   D 1 52  ? 142.124 136.959 116.808 1.00 84.18  ? 28  ILE   C O     1 
ATOM   6669 C  CB    . ILE   D 1 52  ? 139.241 138.022 115.471 1.00 84.96  ? 28  ILE   C CB    1 
ATOM   6670 C  CG1   . ILE   D 1 52  ? 138.753 137.703 114.058 1.00 84.94  ? 28  ILE   C CG1   1 
ATOM   6671 C  CG2   . ILE   D 1 52  ? 140.274 139.140 115.426 1.00 81.37  ? 28  ILE   C CG2   1 
ATOM   6672 C  CD1   . ILE   D 1 52  ? 138.302 138.921 113.280 1.00 87.88  ? 28  ILE   C CD1   1 
ATOM   6673 N  N     . ILE   D 1 53  ? 140.577 137.563 118.325 1.00 90.73  ? 29  ILE   C N     1 
ATOM   6674 C  CA    . ILE   D 1 53  ? 141.600 137.998 119.278 1.00 90.29  ? 29  ILE   C CA    1 
ATOM   6675 C  C     . ILE   D 1 53  ? 142.364 136.845 119.909 1.00 90.74  ? 29  ILE   C C     1 
ATOM   6676 O  O     . ILE   D 1 53  ? 143.413 137.076 120.523 1.00 89.41  ? 29  ILE   C O     1 
ATOM   6677 C  CB    . ILE   D 1 53  ? 140.999 138.861 120.404 1.00 86.94  ? 29  ILE   C CB    1 
ATOM   6678 C  CG1   . ILE   D 1 53  ? 140.067 138.028 121.285 1.00 85.40  ? 29  ILE   C CG1   1 
ATOM   6679 C  CG2   . ILE   D 1 53  ? 140.267 140.061 119.823 1.00 89.86  ? 29  ILE   C CG2   1 
ATOM   6680 C  CD1   . ILE   D 1 53  ? 139.465 138.804 122.435 1.00 87.36  ? 29  ILE   C CD1   1 
ATOM   6681 N  N     . ASN   D 1 54  ? 141.880 135.613 119.771 1.00 97.05  ? 30  ASN   C N     1 
ATOM   6682 C  CA    . ASN   D 1 54  ? 142.530 134.428 120.323 1.00 95.30  ? 30  ASN   C CA    1 
ATOM   6683 C  C     . ASN   D 1 54  ? 142.980 133.484 119.213 1.00 94.68  ? 30  ASN   C C     1 
ATOM   6684 O  O     . ASN   D 1 54  ? 142.779 132.270 119.285 1.00 94.50  ? 30  ASN   C O     1 
ATOM   6685 C  CB    . ASN   D 1 54  ? 141.602 133.705 121.294 1.00 97.04  ? 30  ASN   C CB    1 
ATOM   6686 C  CG    . ASN   D 1 54  ? 141.617 134.317 122.680 1.00 96.87  ? 30  ASN   C CG    1 
ATOM   6687 O  OD1   . ASN   D 1 54  ? 141.606 135.537 122.833 1.00 99.77  ? 30  ASN   C OD1   1 
ATOM   6688 N  ND2   . ASN   D 1 54  ? 141.643 133.468 123.700 1.00 93.75  ? 30  ASN   C ND2   1 
ATOM   6689 N  N     . HIS   D 1 55  ? 143.597 134.037 118.169 1.00 111.00 ? 31  HIS   C N     1 
ATOM   6690 C  CA    . HIS   D 1 55  ? 143.885 133.265 116.964 1.00 113.03 ? 31  HIS   C CA    1 
ATOM   6691 C  C     . HIS   D 1 55  ? 145.081 132.337 117.152 1.00 111.55 ? 31  HIS   C C     1 
ATOM   6692 O  O     . HIS   D 1 55  ? 144.954 131.113 117.041 1.00 112.44 ? 31  HIS   C O     1 
ATOM   6693 C  CB    . HIS   D 1 55  ? 144.125 134.214 115.786 1.00 113.14 ? 31  HIS   C CB    1 
ATOM   6694 C  CG    . HIS   D 1 55  ? 143.922 133.576 114.447 1.00 113.49 ? 31  HIS   C CG    1 
ATOM   6695 N  ND1   . HIS   D 1 55  ? 142.689 133.144 114.008 1.00 112.43 ? 31  HIS   C ND1   1 
ATOM   6696 C  CD2   . HIS   D 1 55  ? 144.795 133.297 113.450 1.00 113.17 ? 31  HIS   C CD2   1 
ATOM   6697 C  CE1   . HIS   D 1 55  ? 142.811 132.626 112.799 1.00 112.51 ? 31  HIS   C CE1   1 
ATOM   6698 N  NE2   . HIS   D 1 55  ? 144.079 132.706 112.438 1.00 114.95 ? 31  HIS   C NE2   1 
ATOM   6699 N  N     . SER   D 1 56  ? 146.252 132.901 117.434 1.00 89.34  ? 32  SER   C N     1 
ATOM   6700 C  CA    . SER   D 1 56  ? 147.497 132.146 117.409 1.00 91.73  ? 32  SER   C CA    1 
ATOM   6701 C  C     . SER   D 1 56  ? 147.857 131.517 118.749 1.00 91.01  ? 32  SER   C C     1 
ATOM   6702 O  O     . SER   D 1 56  ? 148.904 130.870 118.846 1.00 89.42  ? 32  SER   C O     1 
ATOM   6703 C  CB    . SER   D 1 56  ? 148.642 133.045 116.937 1.00 90.47  ? 32  SER   C CB    1 
ATOM   6704 O  OG    . SER   D 1 56  ? 148.249 133.832 115.827 1.00 91.01  ? 32  SER   C OG    1 
ATOM   6705 N  N     . ASN   D 1 57  ? 147.031 131.687 119.777 1.00 85.47  ? 33  ASN   C N     1 
ATOM   6706 C  CA    . ASN   D 1 57  ? 147.301 131.044 121.055 1.00 82.26  ? 33  ASN   C CA    1 
ATOM   6707 C  C     . ASN   D 1 57  ? 147.047 129.545 120.958 1.00 84.28  ? 33  ASN   C C     1 
ATOM   6708 O  O     . ASN   D 1 57  ? 146.084 129.101 120.326 1.00 83.93  ? 33  ASN   C O     1 
ATOM   6709 C  CB    . ASN   D 1 57  ? 146.433 131.657 122.153 1.00 82.17  ? 33  ASN   C CB    1 
ATOM   6710 C  CG    . ASN   D 1 57  ? 146.582 133.160 122.241 1.00 83.72  ? 33  ASN   C CG    1 
ATOM   6711 O  OD1   . ASN   D 1 57  ? 147.499 133.738 121.659 1.00 83.95  ? 33  ASN   C OD1   1 
ATOM   6712 N  ND2   . ASN   D 1 57  ? 145.678 133.801 122.969 1.00 85.77  ? 33  ASN   C ND2   1 
ATOM   6713 N  N     . TYR   D 1 58  ? 147.921 128.761 121.592 1.00 95.69  ? 34  TYR   C N     1 
ATOM   6714 C  CA    . TYR   D 1 58  ? 147.783 127.310 121.544 1.00 95.91  ? 34  TYR   C CA    1 
ATOM   6715 C  C     . TYR   D 1 58  ? 146.604 126.828 122.380 1.00 95.29  ? 34  TYR   C C     1 
ATOM   6716 O  O     . TYR   D 1 58  ? 145.909 125.883 121.987 1.00 95.82  ? 34  TYR   C O     1 
ATOM   6717 C  CB    . TYR   D 1 58  ? 149.076 126.642 122.008 1.00 98.08  ? 34  TYR   C CB    1 
ATOM   6718 C  CG    . TYR   D 1 58  ? 150.117 126.508 120.918 1.00 98.93  ? 34  TYR   C CG    1 
ATOM   6719 C  CD1   . TYR   D 1 58  ? 150.776 127.625 120.422 1.00 98.97  ? 34  TYR   C CD1   1 
ATOM   6720 C  CD2   . TYR   D 1 58  ? 150.434 125.268 120.382 1.00 96.87  ? 34  TYR   C CD2   1 
ATOM   6721 C  CE1   . TYR   D 1 58  ? 151.726 127.508 119.425 1.00 98.77  ? 34  TYR   C CE1   1 
ATOM   6722 C  CE2   . TYR   D 1 58  ? 151.381 125.142 119.386 1.00 97.02  ? 34  TYR   C CE2   1 
ATOM   6723 C  CZ    . TYR   D 1 58  ? 152.025 126.265 118.911 1.00 99.50  ? 34  TYR   C CZ    1 
ATOM   6724 O  OH    . TYR   D 1 58  ? 152.970 126.144 117.918 1.00 99.16  ? 34  TYR   C OH    1 
ATOM   6725 N  N     . LEU   D 1 59  ? 146.363 127.455 123.532 1.00 81.37  ? 35  LEU   C N     1 
ATOM   6726 C  CA    . LEU   D 1 59  ? 145.231 127.066 124.364 1.00 80.74  ? 35  LEU   C CA    1 
ATOM   6727 C  C     . LEU   D 1 59  ? 143.905 127.535 123.779 1.00 82.57  ? 35  LEU   C C     1 
ATOM   6728 O  O     . LEU   D 1 59  ? 142.876 126.884 123.991 1.00 79.19  ? 35  LEU   C O     1 
ATOM   6729 C  CB    . LEU   D 1 59  ? 145.407 127.612 125.782 1.00 79.26  ? 35  LEU   C CB    1 
ATOM   6730 C  CG    . LEU   D 1 59  ? 146.713 127.237 126.485 1.00 81.81  ? 35  LEU   C CG    1 
ATOM   6731 C  CD1   . LEU   D 1 59  ? 146.859 127.991 127.796 1.00 79.72  ? 35  LEU   C CD1   1 
ATOM   6732 C  CD2   . LEU   D 1 59  ? 146.787 125.736 126.716 1.00 80.97  ? 35  LEU   C CD2   1 
ATOM   6733 N  N     . GLY   D 1 60  ? 143.906 128.646 123.049 1.00 83.80  ? 36  GLY   C N     1 
ATOM   6734 C  CA    . GLY   D 1 60  ? 142.707 129.113 122.382 1.00 78.20  ? 36  GLY   C CA    1 
ATOM   6735 C  C     . GLY   D 1 60  ? 141.900 130.115 123.182 1.00 82.47  ? 36  GLY   C C     1 
ATOM   6736 O  O     . GLY   D 1 60  ? 142.421 131.156 123.593 1.00 84.94  ? 36  GLY   C O     1 
ATOM   6737 N  N     . VAL   D 1 61  ? 140.623 129.810 123.406 1.00 85.71  ? 37  VAL   C N     1 
ATOM   6738 C  CA    . VAL   D 1 61  ? 139.721 130.717 124.107 1.00 82.66  ? 37  VAL   C CA    1 
ATOM   6739 C  C     . VAL   D 1 61  ? 139.786 130.450 125.603 1.00 81.26  ? 37  VAL   C C     1 
ATOM   6740 O  O     . VAL   D 1 61  ? 139.105 131.115 126.392 1.00 84.03  ? 37  VAL   C O     1 
ATOM   6741 C  CB    . VAL   D 1 61  ? 138.278 130.582 123.588 1.00 81.26  ? 37  VAL   C CB    1 
ATOM   6742 C  CG1   . VAL   D 1 61  ? 138.174 131.104 122.166 1.00 82.62  ? 37  VAL   C CG1   1 
ATOM   6743 C  CG2   . VAL   D 1 61  ? 137.821 129.136 123.669 1.00 76.08  ? 37  VAL   C CG2   1 
ATOM   6744 N  N     . ALA   D 1 62  ? 140.600 129.473 126.005 1.00 73.04  ? 38  ALA   C N     1 
ATOM   6745 C  CA    . ALA   D 1 62  ? 140.767 129.184 127.423 1.00 73.32  ? 38  ALA   C CA    1 
ATOM   6746 C  C     . ALA   D 1 62  ? 141.409 130.341 128.175 1.00 76.60  ? 38  ALA   C C     1 
ATOM   6747 O  O     . ALA   D 1 62  ? 141.165 130.495 129.377 1.00 79.29  ? 38  ALA   C O     1 
ATOM   6748 C  CB    . ALA   D 1 62  ? 141.600 127.916 127.611 1.00 73.39  ? 38  ALA   C CB    1 
ATOM   6749 N  N     . TRP   D 1 63  ? 142.211 131.164 127.494 1.00 84.84  ? 39  TRP   C N     1 
ATOM   6750 C  CA    . TRP   D 1 63  ? 142.858 132.292 128.151 1.00 81.34  ? 39  TRP   C CA    1 
ATOM   6751 C  C     . TRP   D 1 63  ? 141.853 133.291 128.704 1.00 82.08  ? 39  TRP   C C     1 
ATOM   6752 O  O     . TRP   D 1 63  ? 142.147 133.955 129.703 1.00 89.33  ? 39  TRP   C O     1 
ATOM   6753 C  CB    . TRP   D 1 63  ? 143.813 132.987 127.181 1.00 82.30  ? 39  TRP   C CB    1 
ATOM   6754 C  CG    . TRP   D 1 63  ? 145.168 132.356 127.144 1.00 85.43  ? 39  TRP   C CG    1 
ATOM   6755 C  CD1   . TRP   D 1 63  ? 145.665 131.544 126.169 1.00 83.21  ? 39  TRP   C CD1   1 
ATOM   6756 C  CD2   . TRP   D 1 63  ? 146.200 132.477 128.130 1.00 90.98  ? 39  TRP   C CD2   1 
ATOM   6757 N  NE1   . TRP   D 1 63  ? 146.943 131.153 126.485 1.00 87.48  ? 39  TRP   C NE1   1 
ATOM   6758 C  CE2   . TRP   D 1 63  ? 147.295 131.714 127.684 1.00 87.99  ? 39  TRP   C CE2   1 
ATOM   6759 C  CE3   . TRP   D 1 63  ? 146.304 133.161 129.346 1.00 88.13  ? 39  TRP   C CE3   1 
ATOM   6760 C  CZ2   . TRP   D 1 63  ? 148.479 131.613 128.410 1.00 85.75  ? 39  TRP   C CZ2   1 
ATOM   6761 C  CZ3   . TRP   D 1 63  ? 147.480 133.059 130.064 1.00 84.36  ? 39  TRP   C CZ3   1 
ATOM   6762 C  CH2   . TRP   D 1 63  ? 148.551 132.291 129.595 1.00 83.55  ? 39  TRP   C CH2   1 
ATOM   6763 N  N     . GLU   D 1 64  ? 140.671 133.400 128.089 1.00 84.21  ? 40  GLU   C N     1 
ATOM   6764 C  CA    . GLU   D 1 64  ? 139.626 134.263 128.628 1.00 84.91  ? 40  GLU   C CA    1 
ATOM   6765 C  C     . GLU   D 1 64  ? 139.240 133.872 130.047 1.00 82.10  ? 40  GLU   C C     1 
ATOM   6766 O  O     . GLU   D 1 64  ? 138.765 134.722 130.806 1.00 81.61  ? 40  GLU   C O     1 
ATOM   6767 C  CB    . GLU   D 1 64  ? 138.391 134.225 127.724 1.00 82.42  ? 40  GLU   C CB    1 
ATOM   6768 C  CG    . GLU   D 1 64  ? 138.677 134.518 126.261 1.00 84.85  ? 40  GLU   C CG    1 
ATOM   6769 C  CD    . GLU   D 1 64  ? 138.267 135.919 125.854 1.00 88.55  ? 40  GLU   C CD    1 
ATOM   6770 O  OE1   . GLU   D 1 64  ? 139.019 136.559 125.089 1.00 91.00  ? 40  GLU   C OE1   1 
ATOM   6771 O  OE2   . GLU   D 1 64  ? 137.197 136.384 126.300 1.00 84.50  ? 40  GLU   C OE2   1 
ATOM   6772 N  N     . LEU   D 1 65  ? 139.433 132.608 130.419 1.00 76.25  ? 41  LEU   C N     1 
ATOM   6773 C  CA    . LEU   D 1 65  ? 139.237 132.164 131.791 1.00 75.19  ? 41  LEU   C CA    1 
ATOM   6774 C  C     . LEU   D 1 65  ? 140.528 132.118 132.591 1.00 76.05  ? 41  LEU   C C     1 
ATOM   6775 O  O     . LEU   D 1 65  ? 140.479 132.097 133.824 1.00 77.16  ? 41  LEU   C O     1 
ATOM   6776 C  CB    . LEU   D 1 65  ? 138.587 130.776 131.813 1.00 76.35  ? 41  LEU   C CB    1 
ATOM   6777 C  CG    . LEU   D 1 65  ? 137.097 130.709 132.156 1.00 77.55  ? 41  LEU   C CG    1 
ATOM   6778 C  CD1   . LEU   D 1 65  ? 136.875 130.979 133.636 1.00 76.39  ? 41  LEU   C CD1   1 
ATOM   6779 C  CD2   . LEU   D 1 65  ? 136.297 131.682 131.304 1.00 78.80  ? 41  LEU   C CD2   1 
ATOM   6780 N  N     . ILE   D 1 66  ? 141.683 132.103 131.920 1.00 77.90  ? 42  ILE   C N     1 
ATOM   6781 C  CA    . ILE   D 1 66  ? 142.948 131.946 132.628 1.00 76.22  ? 42  ILE   C CA    1 
ATOM   6782 C  C     . ILE   D 1 66  ? 143.523 133.302 133.013 1.00 77.71  ? 42  ILE   C C     1 
ATOM   6783 O  O     . ILE   D 1 66  ? 144.073 133.470 134.109 1.00 79.68  ? 42  ILE   C O     1 
ATOM   6784 C  CB    . ILE   D 1 66  ? 143.935 131.128 131.773 1.00 75.95  ? 42  ILE   C CB    1 
ATOM   6785 C  CG1   . ILE   D 1 66  ? 143.520 129.657 131.741 1.00 78.47  ? 42  ILE   C CG1   1 
ATOM   6786 C  CG2   . ILE   D 1 66  ? 145.350 131.256 132.306 1.00 77.53  ? 42  ILE   C CG2   1 
ATOM   6787 C  CD1   . ILE   D 1 66  ? 144.327 128.819 130.779 1.00 76.34  ? 42  ILE   C CD1   1 
ATOM   6788 N  N     . ASN   D 1 67  ? 143.406 134.289 132.127 1.00 86.37  ? 43  ASN   C N     1 
ATOM   6789 C  CA    . ASN   D 1 67  ? 143.982 135.603 132.403 1.00 83.68  ? 43  ASN   C CA    1 
ATOM   6790 C  C     . ASN   D 1 67  ? 143.420 136.264 133.659 1.00 88.31  ? 43  ASN   C C     1 
ATOM   6791 O  O     . ASN   D 1 67  ? 144.226 136.746 134.473 1.00 88.88  ? 43  ASN   C O     1 
ATOM   6792 C  CB    . ASN   D 1 67  ? 143.810 136.512 131.180 1.00 85.92  ? 43  ASN   C CB    1 
ATOM   6793 C  CG    . ASN   D 1 67  ? 145.017 137.393 130.935 1.00 93.31  ? 43  ASN   C CG    1 
ATOM   6794 O  OD1   . ASN   D 1 67  ? 146.131 136.903 130.754 1.00 96.91  ? 43  ASN   C OD1   1 
ATOM   6795 N  ND2   . ASN   D 1 67  ? 144.802 138.703 130.933 1.00 92.57  ? 43  ASN   C ND2   1 
ATOM   6796 N  N     . PRO   D 1 68  ? 142.101 136.336 133.885 1.00 77.61  ? 44  PRO   C N     1 
ATOM   6797 C  CA    . PRO   D 1 68  ? 141.623 136.926 135.144 1.00 72.78  ? 44  PRO   C CA    1 
ATOM   6798 C  C     . PRO   D 1 68  ? 141.968 136.109 136.376 1.00 72.48  ? 44  PRO   C C     1 
ATOM   6799 O  O     . PRO   D 1 68  ? 142.362 136.698 137.392 1.00 76.30  ? 44  PRO   C O     1 
ATOM   6800 C  CB    . PRO   D 1 68  ? 140.104 137.006 134.940 1.00 69.50  ? 44  PRO   C CB    1 
ATOM   6801 C  CG    . PRO   D 1 68  ? 139.812 135.948 133.947 1.00 66.48  ? 44  PRO   C CG    1 
ATOM   6802 C  CD    . PRO   D 1 68  ? 140.972 135.985 133.004 1.00 74.00  ? 44  PRO   C CD    1 
ATOM   6803 N  N     . VAL   D 1 69  ? 141.864 134.778 136.308 1.00 72.19  ? 45  VAL   C N     1 
ATOM   6804 C  CA    . VAL   D 1 69  ? 142.038 133.944 137.495 1.00 72.64  ? 45  VAL   C CA    1 
ATOM   6805 C  C     . VAL   D 1 69  ? 143.393 134.200 138.141 1.00 75.96  ? 45  VAL   C C     1 
ATOM   6806 O  O     . VAL   D 1 69  ? 143.479 134.442 139.352 1.00 77.68  ? 45  VAL   C O     1 
ATOM   6807 C  CB    . VAL   D 1 69  ? 141.852 132.459 137.133 1.00 70.22  ? 45  VAL   C CB    1 
ATOM   6808 C  CG1   . VAL   D 1 69  ? 142.571 131.569 138.134 1.00 71.71  ? 45  VAL   C CG1   1 
ATOM   6809 C  CG2   . VAL   D 1 69  ? 140.376 132.110 137.072 1.00 71.91  ? 45  VAL   C CG2   1 
ATOM   6810 N  N     . MET   D 1 70  ? 144.465 134.186 137.341 1.00 81.44  ? 46  MET   C N     1 
ATOM   6811 C  CA    . MET   D 1 70  ? 145.793 134.466 137.877 1.00 79.52  ? 46  MET   C CA    1 
ATOM   6812 C  C     . MET   D 1 70  ? 145.811 135.786 138.634 1.00 78.93  ? 46  MET   C C     1 
ATOM   6813 O  O     . MET   D 1 70  ? 146.307 135.849 139.766 1.00 81.26  ? 46  MET   C O     1 
ATOM   6814 C  CB    . MET   D 1 70  ? 146.826 134.488 136.752 1.00 78.81  ? 46  MET   C CB    1 
ATOM   6815 C  CG    . MET   D 1 70  ? 146.907 133.208 135.943 1.00 79.69  ? 46  MET   C CG    1 
ATOM   6816 S  SD    . MET   D 1 70  ? 148.154 133.315 134.645 1.00 90.72  ? 46  MET   C SD    1 
ATOM   6817 C  CE    . MET   D 1 70  ? 148.606 131.593 134.460 1.00 83.56  ? 46  MET   C CE    1 
ATOM   6818 N  N     . GLN   D 1 71  ? 145.231 136.835 138.044 1.00 71.13  ? 47  GLN   C N     1 
ATOM   6819 C  CA    . GLN   D 1 71  ? 145.183 138.127 138.721 1.00 68.16  ? 47  GLN   C CA    1 
ATOM   6820 C  C     . GLN   D 1 71  ? 144.538 137.995 140.091 1.00 67.01  ? 47  GLN   C C     1 
ATOM   6821 O  O     . GLN   D 1 71  ? 145.081 138.487 141.089 1.00 70.84  ? 47  GLN   C O     1 
ATOM   6822 C  CB    . GLN   D 1 71  ? 144.424 139.140 137.866 1.00 71.22  ? 47  GLN   C CB    1 
ATOM   6823 C  CG    . GLN   D 1 71  ? 145.038 139.387 136.503 1.00 73.58  ? 47  GLN   C CG    1 
ATOM   6824 C  CD    . GLN   D 1 71  ? 144.410 140.566 135.790 1.00 78.61  ? 47  GLN   C CD    1 
ATOM   6825 O  OE1   . GLN   D 1 71  ? 144.015 141.548 136.418 1.00 74.38  ? 47  GLN   C OE1   1 
ATOM   6826 N  NE2   . GLN   D 1 71  ? 144.311 140.474 134.469 1.00 80.37  ? 47  GLN   C NE2   1 
ATOM   6827 N  N     . ILE   D 1 72  ? 143.413 137.278 140.165 1.00 64.02  ? 48  ILE   C N     1 
ATOM   6828 C  CA    . ILE   D 1 72  ? 142.737 137.083 141.443 1.00 65.54  ? 48  ILE   C CA    1 
ATOM   6829 C  C     . ILE   D 1 72  ? 143.698 136.482 142.453 1.00 67.50  ? 48  ILE   C C     1 
ATOM   6830 O  O     . ILE   D 1 72  ? 143.806 136.959 143.591 1.00 69.83  ? 48  ILE   C O     1 
ATOM   6831 C  CB    . ILE   D 1 72  ? 141.489 136.201 141.256 1.00 69.03  ? 48  ILE   C CB    1 
ATOM   6832 C  CG1   . ILE   D 1 72  ? 140.494 136.877 140.312 1.00 65.19  ? 48  ILE   C CG1   1 
ATOM   6833 C  CG2   . ILE   D 1 72  ? 140.833 135.917 142.597 1.00 66.65  ? 48  ILE   C CG2   1 
ATOM   6834 C  CD1   . ILE   D 1 72  ? 139.373 135.968 139.863 1.00 65.79  ? 48  ILE   C CD1   1 
ATOM   6835 N  N     . MET   D 1 73  ? 144.452 135.459 142.036 1.00 74.28  ? 49  MET   C N     1 
ATOM   6836 C  CA    . MET   D 1 73  ? 145.421 134.840 142.932 1.00 73.07  ? 49  MET   C CA    1 
ATOM   6837 C  C     . MET   D 1 73  ? 146.364 135.883 143.509 1.00 74.89  ? 49  MET   C C     1 
ATOM   6838 O  O     . MET   D 1 73  ? 146.558 135.947 144.730 1.00 79.22  ? 49  MET   C O     1 
ATOM   6839 C  CB    . MET   D 1 73  ? 146.203 133.755 142.194 1.00 77.58  ? 49  MET   C CB    1 
ATOM   6840 C  CG    . MET   D 1 73  ? 145.363 132.554 141.794 1.00 83.18  ? 49  MET   C CG    1 
ATOM   6841 S  SD    . MET   D 1 73  ? 146.335 131.051 141.594 1.00 88.72  ? 49  MET   C SD    1 
ATOM   6842 C  CE    . MET   D 1 73  ? 146.353 130.894 139.811 1.00 81.85  ? 49  MET   C CE    1 
ATOM   6843 N  N     . VAL   D 1 74  ? 146.913 136.748 142.653 1.00 61.74  ? 50  VAL   C N     1 
ATOM   6844 C  CA    . VAL   D 1 74  ? 147.816 137.783 143.140 1.00 53.97  ? 50  VAL   C CA    1 
ATOM   6845 C  C     . VAL   D 1 74  ? 147.098 138.671 144.144 1.00 56.91  ? 50  VAL   C C     1 
ATOM   6846 O  O     . VAL   D 1 74  ? 147.618 138.949 145.232 1.00 63.89  ? 50  VAL   C O     1 
ATOM   6847 C  CB    . VAL   D 1 74  ? 148.385 138.595 141.963 1.00 55.17  ? 50  VAL   C CB    1 
ATOM   6848 C  CG1   . VAL   D 1 74  ? 149.035 139.873 142.464 1.00 56.64  ? 50  VAL   C CG1   1 
ATOM   6849 C  CG2   . VAL   D 1 74  ? 149.378 137.757 141.174 1.00 56.35  ? 50  VAL   C CG2   1 
ATOM   6850 N  N     . TYR   D 1 75  ? 145.868 139.079 143.824 1.00 52.00  ? 51  TYR   C N     1 
ATOM   6851 C  CA    . TYR   D 1 75  ? 145.143 139.969 144.718 1.00 45.67  ? 51  TYR   C CA    1 
ATOM   6852 C  C     . TYR   D 1 75  ? 144.782 139.275 146.024 1.00 42.99  ? 51  TYR   C C     1 
ATOM   6853 O  O     . TYR   D 1 75  ? 144.480 139.946 147.015 1.00 44.98  ? 51  TYR   C O     1 
ATOM   6854 C  CB    . TYR   D 1 75  ? 143.893 140.506 144.025 1.00 53.15  ? 51  TYR   C CB    1 
ATOM   6855 C  CG    . TYR   D 1 75  ? 144.175 141.688 143.127 1.00 58.39  ? 51  TYR   C CG    1 
ATOM   6856 C  CD1   . TYR   D 1 75  ? 144.853 142.801 143.604 1.00 57.32  ? 51  TYR   C CD1   1 
ATOM   6857 C  CD2   . TYR   D 1 75  ? 143.777 141.686 141.798 1.00 55.50  ? 51  TYR   C CD2   1 
ATOM   6858 C  CE1   . TYR   D 1 75  ? 145.119 143.881 142.788 1.00 55.12  ? 51  TYR   C CE1   1 
ATOM   6859 C  CE2   . TYR   D 1 75  ? 144.038 142.762 140.973 1.00 53.94  ? 51  TYR   C CE2   1 
ATOM   6860 C  CZ    . TYR   D 1 75  ? 144.710 143.856 141.474 1.00 55.91  ? 51  TYR   C CZ    1 
ATOM   6861 O  OH    . TYR   D 1 75  ? 144.972 144.930 140.656 1.00 57.65  ? 51  TYR   C OH    1 
ATOM   6862 N  N     . TRP   D 1 76  ? 144.806 137.940 146.047 1.00 44.02  ? 52  TRP   C N     1 
ATOM   6863 C  CA    . TRP   D 1 76  ? 144.581 137.243 147.307 1.00 42.81  ? 52  TRP   C CA    1 
ATOM   6864 C  C     . TRP   D 1 76  ? 145.875 137.116 148.099 1.00 51.93  ? 52  TRP   C C     1 
ATOM   6865 O  O     . TRP   D 1 76  ? 145.852 137.077 149.334 1.00 53.08  ? 52  TRP   C O     1 
ATOM   6866 C  CB    . TRP   D 1 76  ? 143.970 135.866 147.058 1.00 50.26  ? 52  TRP   C CB    1 
ATOM   6867 C  CG    . TRP   D 1 76  ? 143.759 135.099 148.324 1.00 54.52  ? 52  TRP   C CG    1 
ATOM   6868 C  CD1   . TRP   D 1 76  ? 142.801 135.327 149.266 1.00 57.16  ? 52  TRP   C CD1   1 
ATOM   6869 C  CD2   . TRP   D 1 76  ? 144.536 133.997 148.800 1.00 49.26  ? 52  TRP   C CD2   1 
ATOM   6870 N  NE1   . TRP   D 1 76  ? 142.926 134.428 150.295 1.00 53.52  ? 52  TRP   C NE1   1 
ATOM   6871 C  CE2   . TRP   D 1 76  ? 143.984 133.600 150.033 1.00 51.64  ? 52  TRP   C CE2   1 
ATOM   6872 C  CE3   . TRP   D 1 76  ? 145.641 133.302 148.302 1.00 49.66  ? 52  TRP   C CE3   1 
ATOM   6873 C  CZ2   . TRP   D 1 76  ? 144.500 132.542 150.775 1.00 53.57  ? 52  TRP   C CZ2   1 
ATOM   6874 C  CZ3   . TRP   D 1 76  ? 146.152 132.253 149.039 1.00 56.74  ? 52  TRP   C CZ3   1 
ATOM   6875 C  CH2   . TRP   D 1 76  ? 145.581 131.882 150.261 1.00 57.71  ? 52  TRP   C CH2   1 
ATOM   6876 N  N     . MET   D 1 77  ? 147.014 137.053 147.406 1.00 59.29  ? 53  MET   C N     1 
ATOM   6877 C  CA    . MET   D 1 77  ? 148.282 136.880 148.104 1.00 48.09  ? 53  MET   C CA    1 
ATOM   6878 C  C     . MET   D 1 77  ? 148.738 138.181 148.750 1.00 43.50  ? 53  MET   C C     1 
ATOM   6879 O  O     . MET   D 1 77  ? 149.359 138.165 149.818 1.00 47.08  ? 53  MET   C O     1 
ATOM   6880 C  CB    . MET   D 1 77  ? 149.342 136.352 147.141 1.00 50.91  ? 53  MET   C CB    1 
ATOM   6881 C  CG    . MET   D 1 77  ? 149.782 134.927 147.428 1.00 56.36  ? 53  MET   C CG    1 
ATOM   6882 S  SD    . MET   D 1 77  ? 151.038 134.339 146.278 1.00 77.06  ? 53  MET   C SD    1 
ATOM   6883 C  CE    . MET   D 1 77  ? 150.194 134.551 144.715 1.00 56.00  ? 53  MET   C CE    1 
ATOM   6884 N  N     . VAL   D 1 78  ? 148.433 139.314 148.124 1.00 41.08  ? 54  VAL   C N     1 
ATOM   6885 C  CA    . VAL   D 1 78  ? 148.896 140.602 148.631 1.00 37.50  ? 54  VAL   C CA    1 
ATOM   6886 C  C     . VAL   D 1 78  ? 147.941 141.140 149.690 1.00 38.50  ? 54  VAL   C C     1 
ATOM   6887 O  O     . VAL   D 1 78  ? 148.328 141.373 150.840 1.00 37.23  ? 54  VAL   C O     1 
ATOM   6888 C  CB    . VAL   D 1 78  ? 149.067 141.602 147.474 1.00 31.98  ? 54  VAL   C CB    1 
ATOM   6889 C  CG1   . VAL   D 1 78  ? 149.404 142.981 148.012 1.00 30.84  ? 54  VAL   C CG1   1 
ATOM   6890 C  CG2   . VAL   D 1 78  ? 150.133 141.117 146.512 1.00 34.23  ? 54  VAL   C CG2   1 
ATOM   6891 N  N     . PHE   D 1 79  ? 146.681 141.348 149.312 1.00 42.03  ? 55  PHE   C N     1 
ATOM   6892 C  CA    . PHE   D 1 79  ? 145.711 141.987 150.190 1.00 38.45  ? 55  PHE   C CA    1 
ATOM   6893 C  C     . PHE   D 1 79  ? 145.041 141.021 151.156 1.00 34.53  ? 55  PHE   C C     1 
ATOM   6894 O  O     . PHE   D 1 79  ? 144.447 141.470 152.142 1.00 39.91  ? 55  PHE   C O     1 
ATOM   6895 C  CB    . PHE   D 1 79  ? 144.639 142.695 149.355 1.00 30.46  ? 55  PHE   C CB    1 
ATOM   6896 C  CG    . PHE   D 1 79  ? 145.114 143.969 148.716 1.00 44.70  ? 55  PHE   C CG    1 
ATOM   6897 C  CD1   . PHE   D 1 79  ? 145.812 143.941 147.521 1.00 46.56  ? 55  PHE   C CD1   1 
ATOM   6898 C  CD2   . PHE   D 1 79  ? 144.862 145.193 149.310 1.00 33.01  ? 55  PHE   C CD2   1 
ATOM   6899 C  CE1   . PHE   D 1 79  ? 146.252 145.107 146.931 1.00 33.64  ? 55  PHE   C CE1   1 
ATOM   6900 C  CE2   . PHE   D 1 79  ? 145.299 146.363 148.724 1.00 40.25  ? 55  PHE   C CE2   1 
ATOM   6901 C  CZ    . PHE   D 1 79  ? 145.995 146.319 147.533 1.00 38.52  ? 55  PHE   C CZ    1 
ATOM   6902 N  N     . GLY   D 1 80  ? 145.118 139.718 150.903 1.00 36.64  ? 56  GLY   C N     1 
ATOM   6903 C  CA    . GLY   D 1 80  ? 144.479 138.749 151.769 1.00 35.99  ? 56  GLY   C CA    1 
ATOM   6904 C  C     . GLY   D 1 80  ? 145.424 138.089 152.747 1.00 37.51  ? 56  GLY   C C     1 
ATOM   6905 O  O     . GLY   D 1 80  ? 145.133 138.009 153.943 1.00 41.60  ? 56  GLY   C O     1 
ATOM   6906 N  N     . LEU   D 1 81  ? 146.569 137.615 152.253 1.00 48.67  ? 57  LEU   C N     1 
ATOM   6907 C  CA    . LEU   D 1 81  ? 147.545 136.968 153.122 1.00 49.84  ? 57  LEU   C CA    1 
ATOM   6908 C  C     . LEU   D 1 81  ? 148.460 137.990 153.786 1.00 49.51  ? 57  LEU   C C     1 
ATOM   6909 O  O     . LEU   D 1 81  ? 148.690 137.932 154.998 1.00 45.11  ? 57  LEU   C O     1 
ATOM   6910 C  CB    . LEU   D 1 81  ? 148.368 135.954 152.326 1.00 53.21  ? 57  LEU   C CB    1 
ATOM   6911 C  CG    . LEU   D 1 81  ? 147.839 134.521 152.287 1.00 51.13  ? 57  LEU   C CG    1 
ATOM   6912 C  CD1   . LEU   D 1 81  ? 148.791 133.627 151.514 1.00 51.28  ? 57  LEU   C CD1   1 
ATOM   6913 C  CD2   . LEU   D 1 81  ? 147.625 133.993 153.694 1.00 52.83  ? 57  LEU   C CD2   1 
ATOM   6914 N  N     . GLY   D 1 82  ? 148.989 138.931 153.009 1.00 47.25  ? 58  GLY   C N     1 
ATOM   6915 C  CA    . GLY   D 1 82  ? 149.875 139.941 153.550 1.00 43.91  ? 58  GLY   C CA    1 
ATOM   6916 C  C     . GLY   D 1 82  ? 149.159 140.902 154.472 1.00 46.22  ? 58  GLY   C C     1 
ATOM   6917 O  O     . GLY   D 1 82  ? 149.406 140.915 155.681 1.00 57.18  ? 58  GLY   C O     1 
ATOM   6918 N  N     . ILE   D 1 83  ? 148.271 141.710 153.914 1.00 38.52  ? 59  ILE   C N     1 
ATOM   6919 C  CA    . ILE   D 1 83  ? 147.424 142.580 154.718 1.00 46.36  ? 59  ILE   C CA    1 
ATOM   6920 C  C     . ILE   D 1 83  ? 146.221 141.786 155.205 1.00 59.47  ? 59  ILE   C C     1 
ATOM   6921 O  O     . ILE   D 1 83  ? 145.870 140.744 154.640 1.00 69.09  ? 59  ILE   C O     1 
ATOM   6922 C  CB    . ILE   D 1 83  ? 147.000 143.823 153.910 1.00 50.18  ? 59  ILE   C CB    1 
ATOM   6923 C  CG1   . ILE   D 1 83  ? 148.083 144.193 152.897 1.00 40.94  ? 59  ILE   C CG1   1 
ATOM   6924 C  CG2   . ILE   D 1 83  ? 146.725 144.995 154.836 1.00 52.13  ? 59  ILE   C CG2   1 
ATOM   6925 C  CD1   . ILE   D 1 83  ? 147.668 145.271 151.928 1.00 37.58  ? 59  ILE   C CD1   1 
ATOM   6926 N  N     . ARG   D 1 84  ? 145.613 142.261 156.296 1.00 62.68  ? 60  ARG   C N     1 
ATOM   6927 C  CA    . ARG   D 1 84  ? 144.422 141.677 156.913 1.00 64.40  ? 60  ARG   C CA    1 
ATOM   6928 C  C     . ARG   D 1 84  ? 144.724 140.360 157.621 1.00 63.39  ? 60  ARG   C C     1 
ATOM   6929 O  O     . ARG   D 1 84  ? 143.882 139.857 158.371 1.00 70.11  ? 60  ARG   C O     1 
ATOM   6930 C  CB    . ARG   D 1 84  ? 143.312 141.450 155.881 1.00 62.04  ? 60  ARG   C CB    1 
ATOM   6931 C  CG    . ARG   D 1 84  ? 142.723 142.705 155.276 1.00 64.48  ? 60  ARG   C CG    1 
ATOM   6932 C  CD    . ARG   D 1 84  ? 141.314 142.438 154.784 1.00 59.55  ? 60  ARG   C CD    1 
ATOM   6933 N  NE    . ARG   D 1 84  ? 140.622 141.501 155.657 1.00 61.67  ? 60  ARG   C NE    1 
ATOM   6934 C  CZ    . ARG   D 1 84  ? 139.715 141.847 156.559 1.00 65.59  ? 60  ARG   C CZ    1 
ATOM   6935 N  NH1   . ARG   D 1 84  ? 139.343 143.106 156.718 1.00 67.39  ? 60  ARG   C NH1   1 
ATOM   6936 N  NH2   . ARG   D 1 84  ? 139.168 140.906 157.323 1.00 59.11  ? 60  ARG   C NH2   1 
ATOM   6937 N  N     . SER   D 1 85  ? 145.924 139.815 157.414 1.00 68.70  ? 61  SER   C N     1 
ATOM   6938 C  CA    . SER   D 1 85  ? 146.347 138.553 158.027 1.00 71.86  ? 61  SER   C CA    1 
ATOM   6939 C  C     . SER   D 1 85  ? 145.298 137.454 157.853 1.00 74.50  ? 61  SER   C C     1 
ATOM   6940 O  O     . SER   D 1 85  ? 145.100 136.614 158.732 1.00 80.07  ? 61  SER   C O     1 
ATOM   6941 C  CB    . SER   D 1 85  ? 146.683 138.756 159.505 1.00 79.37  ? 61  SER   C CB    1 
ATOM   6942 O  OG    . SER   D 1 85  ? 147.553 139.860 159.681 1.00 81.34  ? 61  SER   C OG    1 
ATOM   6943 N  N     . ASN   D 1 86  ? 144.622 137.463 156.701 1.00 76.55  ? 62  ASN   C N     1 
ATOM   6944 C  CA    . ASN   D 1 86  ? 143.583 136.482 156.372 1.00 78.73  ? 62  ASN   C CA    1 
ATOM   6945 C  C     . ASN   D 1 86  ? 142.464 136.477 157.414 1.00 78.39  ? 62  ASN   C C     1 
ATOM   6946 O  O     . ASN   D 1 86  ? 142.105 135.437 157.971 1.00 77.96  ? 62  ASN   C O     1 
ATOM   6947 C  CB    . ASN   D 1 86  ? 144.181 135.082 156.204 1.00 76.71  ? 62  ASN   C CB    1 
ATOM   6948 C  CG    . ASN   D 1 86  ? 143.579 134.328 155.034 1.00 79.89  ? 62  ASN   C CG    1 
ATOM   6949 O  OD1   . ASN   D 1 86  ? 142.784 134.876 154.270 1.00 83.15  ? 62  ASN   C OD1   1 
ATOM   6950 N  ND2   . ASN   D 1 86  ? 143.954 133.063 154.890 1.00 77.17  ? 62  ASN   C ND2   1 
ATOM   6951 N  N     . ALA   D 1 87  ? 141.907 137.657 157.673 1.00 81.37  ? 63  ALA   C N     1 
ATOM   6952 C  CA    . ALA   D 1 87  ? 140.805 137.755 158.624 1.00 79.79  ? 63  ALA   C CA    1 
ATOM   6953 C  C     . ALA   D 1 87  ? 139.467 137.784 157.888 1.00 85.17  ? 63  ALA   C C     1 
ATOM   6954 O  O     . ALA   D 1 87  ? 139.317 138.510 156.902 1.00 83.74  ? 63  ALA   C O     1 
ATOM   6955 C  CB    . ALA   D 1 87  ? 140.942 139.006 159.485 1.00 76.32  ? 63  ALA   C CB    1 
ATOM   6956 N  N     . PRO   D 1 88  ? 138.486 137.010 158.349 1.00 86.44  ? 64  PRO   C N     1 
ATOM   6957 C  CA    . PRO   D 1 88  ? 137.192 136.968 157.662 1.00 82.13  ? 64  PRO   C CA    1 
ATOM   6958 C  C     . PRO   D 1 88  ? 136.412 138.263 157.836 1.00 82.90  ? 64  PRO   C C     1 
ATOM   6959 O  O     . PRO   D 1 88  ? 136.633 139.039 158.768 1.00 80.51  ? 64  PRO   C O     1 
ATOM   6960 C  CB    . PRO   D 1 88  ? 136.475 135.794 158.334 1.00 79.63  ? 64  PRO   C CB    1 
ATOM   6961 C  CG    . PRO   D 1 88  ? 137.072 135.736 159.695 1.00 82.20  ? 64  PRO   C CG    1 
ATOM   6962 C  CD    . PRO   D 1 88  ? 138.514 136.130 159.530 1.00 84.68  ? 64  PRO   C CD    1 
ATOM   6963 N  N     . ILE   D 1 89  ? 135.484 138.488 156.909 1.00 74.06  ? 65  ILE   C N     1 
ATOM   6964 C  CA    . ILE   D 1 89  ? 134.628 139.669 156.905 1.00 72.81  ? 65  ILE   C CA    1 
ATOM   6965 C  C     . ILE   D 1 89  ? 133.176 139.216 156.937 1.00 74.85  ? 65  ILE   C C     1 
ATOM   6966 O  O     . ILE   D 1 89  ? 132.760 138.400 156.106 1.00 74.65  ? 65  ILE   C O     1 
ATOM   6967 C  CB    . ILE   D 1 89  ? 134.887 140.559 155.676 1.00 66.71  ? 65  ILE   C CB    1 
ATOM   6968 C  CG1   . ILE   D 1 89  ? 136.297 141.144 155.720 1.00 69.63  ? 65  ILE   C CG1   1 
ATOM   6969 C  CG2   . ILE   D 1 89  ? 133.864 141.677 155.608 1.00 65.22  ? 65  ILE   C CG2   1 
ATOM   6970 C  CD1   . ILE   D 1 89  ? 136.593 142.096 154.585 1.00 63.61  ? 65  ILE   C CD1   1 
ATOM   6971 N  N     . HIS   D 1 90  ? 132.413 139.747 157.894 1.00 86.57  ? 66  HIS   C N     1 
ATOM   6972 C  CA    . HIS   D 1 90  ? 130.972 139.509 157.992 1.00 80.10  ? 66  HIS   C CA    1 
ATOM   6973 C  C     . HIS   D 1 90  ? 130.642 138.026 158.131 1.00 78.61  ? 66  HIS   C C     1 
ATOM   6974 O  O     . HIS   D 1 90  ? 129.608 137.564 157.645 1.00 85.29  ? 66  HIS   C O     1 
ATOM   6975 C  CB    . HIS   D 1 90  ? 130.230 140.105 156.791 1.00 82.67  ? 66  HIS   C CB    1 
ATOM   6976 C  CG    . HIS   D 1 90  ? 130.065 141.591 156.856 1.00 84.31  ? 66  HIS   C CG    1 
ATOM   6977 N  ND1   . HIS   D 1 90  ? 128.963 142.240 156.341 1.00 79.66  ? 66  HIS   C ND1   1 
ATOM   6978 C  CD2   . HIS   D 1 90  ? 130.865 142.556 157.368 1.00 85.61  ? 66  HIS   C CD2   1 
ATOM   6979 C  CE1   . HIS   D 1 90  ? 129.090 143.541 156.537 1.00 80.94  ? 66  HIS   C CE1   1 
ATOM   6980 N  NE2   . HIS   D 1 90  ? 130.235 143.758 157.157 1.00 88.69  ? 66  HIS   C NE2   1 
ATOM   6981 N  N     . GLY   D 1 91  ? 131.513 137.267 158.790 1.00 65.82  ? 67  GLY   C N     1 
ATOM   6982 C  CA    . GLY   D 1 91  ? 131.304 135.845 158.955 1.00 67.13  ? 67  GLY   C CA    1 
ATOM   6983 C  C     . GLY   D 1 91  ? 131.626 135.005 157.740 1.00 70.38  ? 67  GLY   C C     1 
ATOM   6984 O  O     . GLY   D 1 91  ? 131.375 133.793 157.762 1.00 69.95  ? 67  GLY   C O     1 
ATOM   6985 N  N     . VAL   D 1 92  ? 132.165 135.603 156.684 1.00 72.17  ? 68  VAL   C N     1 
ATOM   6986 C  CA    . VAL   D 1 92  ? 132.504 134.891 155.454 1.00 70.37  ? 68  VAL   C CA    1 
ATOM   6987 C  C     . VAL   D 1 92  ? 134.021 134.885 155.315 1.00 68.68  ? 68  VAL   C C     1 
ATOM   6988 O  O     . VAL   D 1 92  ? 134.669 135.890 155.642 1.00 66.76  ? 68  VAL   C O     1 
ATOM   6989 C  CB    . VAL   D 1 92  ? 131.829 135.543 154.235 1.00 72.17  ? 68  VAL   C CB    1 
ATOM   6990 C  CG1   . VAL   D 1 92  ? 131.953 134.659 153.005 1.00 67.57  ? 68  VAL   C CG1   1 
ATOM   6991 C  CG2   . VAL   D 1 92  ? 130.369 135.844 154.532 1.00 69.45  ? 68  VAL   C CG2   1 
ATOM   6992 N  N     . PRO   D 1 93  ? 134.631 133.791 154.858 1.00 73.61  ? 69  PRO   C N     1 
ATOM   6993 C  CA    . PRO   D 1 93  ? 136.072 133.816 154.591 1.00 72.93  ? 69  PRO   C CA    1 
ATOM   6994 C  C     . PRO   D 1 93  ? 136.414 134.861 153.539 1.00 68.84  ? 69  PRO   C C     1 
ATOM   6995 O  O     . PRO   D 1 93  ? 135.643 135.120 152.614 1.00 72.99  ? 69  PRO   C O     1 
ATOM   6996 C  CB    . PRO   D 1 93  ? 136.367 132.398 154.092 1.00 70.23  ? 69  PRO   C CB    1 
ATOM   6997 C  CG    . PRO   D 1 93  ? 135.287 131.564 154.678 1.00 69.09  ? 69  PRO   C CG    1 
ATOM   6998 C  CD    . PRO   D 1 93  ? 134.068 132.436 154.724 1.00 69.38  ? 69  PRO   C CD    1 
ATOM   6999 N  N     . PHE   D 1 94  ? 137.590 135.472 153.699 1.00 50.25  ? 70  PHE   C N     1 
ATOM   7000 C  CA    . PHE   D 1 94  ? 137.977 136.568 152.818 1.00 49.50  ? 70  PHE   C CA    1 
ATOM   7001 C  C     . PHE   D 1 94  ? 138.148 136.111 151.376 1.00 50.29  ? 70  PHE   C C     1 
ATOM   7002 O  O     . PHE   D 1 94  ? 137.974 136.915 150.452 1.00 57.12  ? 70  PHE   C O     1 
ATOM   7003 C  CB    . PHE   D 1 94  ? 139.265 137.218 153.317 1.00 49.79  ? 70  PHE   C CB    1 
ATOM   7004 C  CG    . PHE   D 1 94  ? 139.684 138.417 152.517 1.00 50.18  ? 70  PHE   C CG    1 
ATOM   7005 C  CD1   . PHE   D 1 94  ? 139.064 139.639 152.705 1.00 53.39  ? 70  PHE   C CD1   1 
ATOM   7006 C  CD2   . PHE   D 1 94  ? 140.687 138.318 151.569 1.00 46.94  ? 70  PHE   C CD2   1 
ATOM   7007 C  CE1   . PHE   D 1 94  ? 139.442 140.740 151.969 1.00 53.47  ? 70  PHE   C CE1   1 
ATOM   7008 C  CE2   . PHE   D 1 94  ? 141.068 139.417 150.830 1.00 35.98  ? 70  PHE   C CE2   1 
ATOM   7009 C  CZ    . PHE   D 1 94  ? 140.445 140.630 151.031 1.00 42.35  ? 70  PHE   C CZ    1 
ATOM   7010 N  N     . VAL   D 1 95  ? 138.485 134.839 151.157 1.00 46.91  ? 71  VAL   C N     1 
ATOM   7011 C  CA    . VAL   D 1 95  ? 138.743 134.370 149.799 1.00 42.52  ? 71  VAL   C CA    1 
ATOM   7012 C  C     . VAL   D 1 95  ? 137.483 134.465 148.947 1.00 49.94  ? 71  VAL   C C     1 
ATOM   7013 O  O     . VAL   D 1 95  ? 137.514 134.996 147.832 1.00 53.04  ? 71  VAL   C O     1 
ATOM   7014 C  CB    . VAL   D 1 95  ? 139.312 132.940 149.828 1.00 41.14  ? 71  VAL   C CB    1 
ATOM   7015 C  CG1   . VAL   D 1 95  ? 138.665 132.128 150.939 1.00 47.84  ? 71  VAL   C CG1   1 
ATOM   7016 C  CG2   . VAL   D 1 95  ? 139.133 132.262 148.479 1.00 41.71  ? 71  VAL   C CG2   1 
ATOM   7017 N  N     . TYR   D 1 96  ? 136.348 133.995 149.466 1.00 52.66  ? 72  TYR   C N     1 
ATOM   7018 C  CA    . TYR   D 1 96  ? 135.103 134.055 148.706 1.00 45.14  ? 72  TYR   C CA    1 
ATOM   7019 C  C     . TYR   D 1 96  ? 134.516 135.460 148.679 1.00 49.29  ? 72  TYR   C C     1 
ATOM   7020 O  O     . TYR   D 1 96  ? 133.889 135.849 147.684 1.00 56.31  ? 72  TYR   C O     1 
ATOM   7021 C  CB    . TYR   D 1 96  ? 134.100 133.059 149.283 1.00 42.13  ? 72  TYR   C CB    1 
ATOM   7022 C  CG    . TYR   D 1 96  ? 134.650 131.654 149.338 1.00 48.63  ? 72  TYR   C CG    1 
ATOM   7023 C  CD1   . TYR   D 1 96  ? 134.675 130.854 148.205 1.00 49.41  ? 72  TYR   C CD1   1 
ATOM   7024 C  CD2   . TYR   D 1 96  ? 135.172 131.137 150.514 1.00 50.23  ? 72  TYR   C CD2   1 
ATOM   7025 C  CE1   . TYR   D 1 96  ? 135.189 129.576 148.246 1.00 41.81  ? 72  TYR   C CE1   1 
ATOM   7026 C  CE2   . TYR   D 1 96  ? 135.691 129.862 150.564 1.00 51.80  ? 72  TYR   C CE2   1 
ATOM   7027 C  CZ    . TYR   D 1 96  ? 135.696 129.085 149.427 1.00 49.62  ? 72  TYR   C CZ    1 
ATOM   7028 O  OH    . TYR   D 1 96  ? 136.209 127.810 149.472 1.00 55.26  ? 72  TYR   C OH    1 
ATOM   7029 N  N     . TRP   D 1 97  ? 134.722 136.233 149.748 1.00 38.11  ? 73  TRP   C N     1 
ATOM   7030 C  CA    . TRP   D 1 97  ? 134.326 137.637 149.746 1.00 35.64  ? 73  TRP   C CA    1 
ATOM   7031 C  C     . TRP   D 1 97  ? 135.023 138.398 148.624 1.00 45.81  ? 73  TRP   C C     1 
ATOM   7032 O  O     . TRP   D 1 97  ? 134.409 139.240 147.959 1.00 51.58  ? 73  TRP   C O     1 
ATOM   7033 C  CB    . TRP   D 1 97  ? 134.644 138.258 151.106 1.00 40.52  ? 73  TRP   C CB    1 
ATOM   7034 C  CG    . TRP   D 1 97  ? 133.907 139.523 151.417 1.00 39.52  ? 73  TRP   C CG    1 
ATOM   7035 C  CD1   . TRP   D 1 97  ? 132.637 139.634 151.898 1.00 39.28  ? 73  TRP   C CD1   1 
ATOM   7036 C  CD2   . TRP   D 1 97  ? 134.409 140.860 151.298 1.00 46.85  ? 73  TRP   C CD2   1 
ATOM   7037 N  NE1   . TRP   D 1 97  ? 132.309 140.956 152.073 1.00 30.74  ? 73  TRP   C NE1   1 
ATOM   7038 C  CE2   . TRP   D 1 97  ? 133.381 141.729 151.713 1.00 39.13  ? 73  TRP   C CE2   1 
ATOM   7039 C  CE3   . TRP   D 1 97  ? 135.625 141.407 150.877 1.00 41.38  ? 73  TRP   C CE3   1 
ATOM   7040 C  CZ2   . TRP   D 1 97  ? 133.532 143.113 151.716 1.00 40.27  ? 73  TRP   C CZ2   1 
ATOM   7041 C  CZ3   . TRP   D 1 97  ? 135.771 142.780 150.882 1.00 41.07  ? 73  TRP   C CZ3   1 
ATOM   7042 C  CH2   . TRP   D 1 97  ? 134.731 143.617 151.297 1.00 42.03  ? 73  TRP   C CH2   1 
ATOM   7043 N  N     . LEU   D 1 98  ? 136.307 138.112 148.398 1.00 36.94  ? 74  LEU   C N     1 
ATOM   7044 C  CA    . LEU   D 1 98  ? 137.024 138.739 147.291 1.00 34.91  ? 74  LEU   C CA    1 
ATOM   7045 C  C     . LEU   D 1 98  ? 136.617 138.137 145.952 1.00 44.73  ? 74  LEU   C C     1 
ATOM   7046 O  O     . LEU   D 1 98  ? 136.542 138.847 144.942 1.00 52.37  ? 74  LEU   C O     1 
ATOM   7047 C  CB    . LEU   D 1 98  ? 138.531 138.603 147.505 1.00 37.44  ? 74  LEU   C CB    1 
ATOM   7048 C  CG    . LEU   D 1 98  ? 139.434 139.145 146.397 1.00 42.84  ? 74  LEU   C CG    1 
ATOM   7049 C  CD1   . LEU   D 1 98  ? 139.754 140.609 146.631 1.00 46.32  ? 74  LEU   C CD1   1 
ATOM   7050 C  CD2   . LEU   D 1 98  ? 140.706 138.325 146.303 1.00 43.29  ? 74  LEU   C CD2   1 
ATOM   7051 N  N     . LEU   D 1 99  ? 136.366 136.825 145.921 1.00 44.17  ? 75  LEU   C N     1 
ATOM   7052 C  CA    . LEU   D 1 99  ? 136.001 136.155 144.678 1.00 41.94  ? 75  LEU   C CA    1 
ATOM   7053 C  C     . LEU   D 1 99  ? 134.700 136.695 144.102 1.00 42.24  ? 75  LEU   C C     1 
ATOM   7054 O  O     . LEU   D 1 99  ? 134.597 136.885 142.886 1.00 47.94  ? 75  LEU   C O     1 
ATOM   7055 C  CB    . LEU   D 1 99  ? 135.887 134.649 144.917 1.00 48.90  ? 75  LEU   C CB    1 
ATOM   7056 C  CG    . LEU   D 1 99  ? 136.394 133.715 143.821 1.00 52.93  ? 75  LEU   C CG    1 
ATOM   7057 C  CD1   . LEU   D 1 99  ? 137.909 133.661 143.827 1.00 48.06  ? 75  LEU   C CD1   1 
ATOM   7058 C  CD2   . LEU   D 1 99  ? 135.807 132.325 144.003 1.00 50.15  ? 75  LEU   C CD2   1 
ATOM   7059 N  N     . VAL   D 1 100 ? 133.700 136.935 144.949 1.00 36.15  ? 76  VAL   C N     1 
ATOM   7060 C  CA    . VAL   D 1 100 ? 132.417 137.429 144.457 1.00 33.66  ? 76  VAL   C CA    1 
ATOM   7061 C  C     . VAL   D 1 100 ? 132.548 138.856 143.932 1.00 41.22  ? 76  VAL   C C     1 
ATOM   7062 O  O     . VAL   D 1 100 ? 131.938 139.220 142.921 1.00 46.36  ? 76  VAL   C O     1 
ATOM   7063 C  CB    . VAL   D 1 100 ? 131.346 137.321 145.558 1.00 36.32  ? 76  VAL   C CB    1 
ATOM   7064 C  CG1   . VAL   D 1 100 ? 130.078 138.042 145.145 1.00 37.21  ? 76  VAL   C CG1   1 
ATOM   7065 C  CG2   . VAL   D 1 100 ? 131.051 135.864 145.861 1.00 32.67  ? 76  VAL   C CG2   1 
ATOM   7066 N  N     . GLY   D 1 101 ? 133.354 139.682 144.602 1.00 46.03  ? 77  GLY   C N     1 
ATOM   7067 C  CA    . GLY   D 1 101 ? 133.437 141.086 144.225 1.00 34.09  ? 77  GLY   C CA    1 
ATOM   7068 C  C     . GLY   D 1 101 ? 134.372 141.350 143.058 1.00 40.49  ? 77  GLY   C C     1 
ATOM   7069 O  O     . GLY   D 1 101 ? 134.241 142.361 142.367 1.00 44.86  ? 77  GLY   C O     1 
ATOM   7070 N  N     . ILE   D 1 102 ? 135.330 140.451 142.824 1.00 49.83  ? 78  ILE   C N     1 
ATOM   7071 C  CA    . ILE   D 1 102 ? 136.335 140.695 141.792 1.00 46.65  ? 78  ILE   C CA    1 
ATOM   7072 C  C     . ILE   D 1 102 ? 135.849 140.267 140.412 1.00 51.52  ? 78  ILE   C C     1 
ATOM   7073 O  O     . ILE   D 1 102 ? 136.497 140.562 139.401 1.00 51.77  ? 78  ILE   C O     1 
ATOM   7074 C  CB    . ILE   D 1 102 ? 137.650 139.981 142.166 1.00 46.93  ? 78  ILE   C CB    1 
ATOM   7075 C  CG1   . ILE   D 1 102 ? 138.860 140.717 141.587 1.00 47.08  ? 78  ILE   C CG1   1 
ATOM   7076 C  CG2   . ILE   D 1 102 ? 137.620 138.538 141.707 1.00 52.90  ? 78  ILE   C CG2   1 
ATOM   7077 C  CD1   . ILE   D 1 102 ? 139.426 141.780 142.484 1.00 53.10  ? 78  ILE   C CD1   1 
ATOM   7078 N  N     . SER   D 1 103 ? 134.714 139.568 140.340 1.00 50.14  ? 79  SER   C N     1 
ATOM   7079 C  CA    . SER   D 1 103 ? 134.314 138.934 139.084 1.00 55.75  ? 79  SER   C CA    1 
ATOM   7080 C  C     . SER   D 1 103 ? 133.994 139.959 137.998 1.00 62.21  ? 79  SER   C C     1 
ATOM   7081 O  O     . SER   D 1 103 ? 134.359 139.770 136.832 1.00 67.20  ? 79  SER   C O     1 
ATOM   7082 C  CB    . SER   D 1 103 ? 133.120 138.010 139.321 1.00 55.65  ? 79  SER   C CB    1 
ATOM   7083 O  OG    . SER   D 1 103 ? 132.107 138.659 140.065 1.00 54.53  ? 79  SER   C OG    1 
ATOM   7084 N  N     . MET   D 1 104 ? 133.310 141.048 138.356 1.00 51.19  ? 80  MET   C N     1 
ATOM   7085 C  CA    . MET   D 1 104 ? 132.820 141.975 137.338 1.00 47.23  ? 80  MET   C CA    1 
ATOM   7086 C  C     . MET   D 1 104 ? 133.905 142.947 136.888 1.00 54.28  ? 80  MET   C C     1 
ATOM   7087 O  O     . MET   D 1 104 ? 133.766 143.603 135.846 1.00 54.27  ? 80  MET   C O     1 
ATOM   7088 C  CB    . MET   D 1 104 ? 131.618 142.750 137.876 1.00 46.00  ? 80  MET   C CB    1 
ATOM   7089 C  CG    . MET   D 1 104 ? 131.948 143.626 139.073 1.00 45.52  ? 80  MET   C CG    1 
ATOM   7090 S  SD    . MET   D 1 104 ? 130.853 143.377 140.477 1.00 69.36  ? 80  MET   C SD    1 
ATOM   7091 C  CE    . MET   D 1 104 ? 130.989 141.610 140.704 1.00 49.06  ? 80  MET   C CE    1 
ATOM   7092 N  N     . TRP   D 1 105 ? 134.980 143.072 137.673 1.00 44.89  ? 81  TRP   C N     1 
ATOM   7093 C  CA    . TRP   D 1 105 ? 135.957 144.128 137.436 1.00 33.67  ? 81  TRP   C CA    1 
ATOM   7094 C  C     . TRP   D 1 105 ? 136.686 143.939 136.113 1.00 40.92  ? 81  TRP   C C     1 
ATOM   7095 O  O     . TRP   D 1 105 ? 136.925 144.901 135.381 1.00 47.66  ? 81  TRP   C O     1 
ATOM   7096 C  CB    . TRP   D 1 105 ? 136.963 144.201 138.582 1.00 44.56  ? 81  TRP   C CB    1 
ATOM   7097 C  CG    . TRP   D 1 105 ? 138.029 145.222 138.315 1.00 44.27  ? 81  TRP   C CG    1 
ATOM   7098 C  CD1   . TRP   D 1 105 ? 139.370 144.999 138.210 1.00 33.87  ? 81  TRP   C CD1   1 
ATOM   7099 C  CD2   . TRP   D 1 105 ? 137.837 146.625 138.091 1.00 46.07  ? 81  TRP   C CD2   1 
ATOM   7100 N  NE1   . TRP   D 1 105 ? 140.026 146.175 137.946 1.00 36.84  ? 81  TRP   C NE1   1 
ATOM   7101 C  CE2   . TRP   D 1 105 ? 139.107 147.188 137.868 1.00 41.46  ? 81  TRP   C CE2   1 
ATOM   7102 C  CE3   . TRP   D 1 105 ? 136.715 147.459 138.065 1.00 42.81  ? 81  TRP   C CE3   1 
ATOM   7103 C  CZ2   . TRP   D 1 105 ? 139.286 148.546 137.620 1.00 37.13  ? 81  TRP   C CZ2   1 
ATOM   7104 C  CZ3   . TRP   D 1 105 ? 136.895 148.805 137.819 1.00 38.37  ? 81  TRP   C CZ3   1 
ATOM   7105 C  CH2   . TRP   D 1 105 ? 138.170 149.335 137.601 1.00 43.13  ? 81  TRP   C CH2   1 
ATOM   7106 N  N     . PHE   D 1 106 ? 137.080 142.702 135.808 1.00 54.59  ? 82  PHE   C N     1 
ATOM   7107 C  CA    . PHE   D 1 106 ? 137.808 142.462 134.568 1.00 54.81  ? 82  PHE   C CA    1 
ATOM   7108 C  C     . PHE   D 1 106 ? 136.950 142.805 133.358 1.00 54.48  ? 82  PHE   C C     1 
ATOM   7109 O  O     . PHE   D 1 106 ? 137.417 143.465 132.422 1.00 55.07  ? 82  PHE   C O     1 
ATOM   7110 C  CB    . PHE   D 1 106 ? 138.283 141.011 134.511 1.00 50.51  ? 82  PHE   C CB    1 
ATOM   7111 C  CG    . PHE   D 1 106 ? 138.999 140.565 135.751 1.00 52.90  ? 82  PHE   C CG    1 
ATOM   7112 C  CD1   . PHE   D 1 106 ? 140.300 140.971 135.998 1.00 51.66  ? 82  PHE   C CD1   1 
ATOM   7113 C  CD2   . PHE   D 1 106 ? 138.373 139.746 136.675 1.00 53.06  ? 82  PHE   C CD2   1 
ATOM   7114 C  CE1   . PHE   D 1 106 ? 140.962 140.566 137.138 1.00 48.37  ? 82  PHE   C CE1   1 
ATOM   7115 C  CE2   . PHE   D 1 106 ? 139.032 139.338 137.817 1.00 56.21  ? 82  PHE   C CE2   1 
ATOM   7116 C  CZ    . PHE   D 1 106 ? 140.329 139.749 138.048 1.00 56.55  ? 82  PHE   C CZ    1 
ATOM   7117 N  N     . PHE   D 1 107 ? 135.680 142.393 133.376 1.00 49.02  ? 83  PHE   C N     1 
ATOM   7118 C  CA    . PHE   D 1 107 ? 134.776 142.731 132.283 1.00 38.73  ? 83  PHE   C CA    1 
ATOM   7119 C  C     . PHE   D 1 107 ? 134.611 144.238 132.150 1.00 43.27  ? 83  PHE   C C     1 
ATOM   7120 O  O     . PHE   D 1 107 ? 134.715 144.782 131.046 1.00 40.96  ? 83  PHE   C O     1 
ATOM   7121 C  CB    . PHE   D 1 107 ? 133.419 142.059 132.494 1.00 37.47  ? 83  PHE   C CB    1 
ATOM   7122 C  CG    . PHE   D 1 107 ? 132.289 142.723 131.757 1.00 45.26  ? 83  PHE   C CG    1 
ATOM   7123 C  CD1   . PHE   D 1 107 ? 132.283 142.780 130.374 1.00 50.75  ? 83  PHE   C CD1   1 
ATOM   7124 C  CD2   . PHE   D 1 107 ? 131.231 143.287 132.447 1.00 46.84  ? 83  PHE   C CD2   1 
ATOM   7125 C  CE1   . PHE   D 1 107 ? 131.247 143.389 129.696 1.00 39.87  ? 83  PHE   C CE1   1 
ATOM   7126 C  CE2   . PHE   D 1 107 ? 130.193 143.897 131.774 1.00 44.56  ? 83  PHE   C CE2   1 
ATOM   7127 C  CZ    . PHE   D 1 107 ? 130.202 143.949 130.397 1.00 40.34  ? 83  PHE   C CZ    1 
ATOM   7128 N  N     . ILE   D 1 108 ? 134.374 144.935 133.266 1.00 47.12  ? 84  ILE   C N     1 
ATOM   7129 C  CA    . ILE   D 1 108 ? 134.143 146.377 133.197 1.00 42.10  ? 84  ILE   C CA    1 
ATOM   7130 C  C     . ILE   D 1 108 ? 135.380 147.094 132.671 1.00 45.06  ? 84  ILE   C C     1 
ATOM   7131 O  O     . ILE   D 1 108 ? 135.298 147.920 131.751 1.00 54.84  ? 84  ILE   C O     1 
ATOM   7132 C  CB    . ILE   D 1 108 ? 133.721 146.920 134.574 1.00 40.99  ? 84  ILE   C CB    1 
ATOM   7133 C  CG1   . ILE   D 1 108 ? 132.339 146.388 134.958 1.00 42.60  ? 84  ILE   C CG1   1 
ATOM   7134 C  CG2   . ILE   D 1 108 ? 133.728 148.438 134.573 1.00 44.43  ? 84  ILE   C CG2   1 
ATOM   7135 C  CD1   . ILE   D 1 108 ? 131.820 146.934 136.266 1.00 43.13  ? 84  ILE   C CD1   1 
ATOM   7136 N  N     . ASN   D 1 109 ? 136.546 146.779 133.240 1.00 50.17  ? 85  ASN   C N     1 
ATOM   7137 C  CA    . ASN   D 1 109 ? 137.786 147.432 132.840 1.00 51.55  ? 85  ASN   C CA    1 
ATOM   7138 C  C     . ASN   D 1 109 ? 138.096 147.180 131.371 1.00 60.07  ? 85  ASN   C C     1 
ATOM   7139 O  O     . ASN   D 1 109 ? 138.381 148.119 130.619 1.00 60.11  ? 85  ASN   C O     1 
ATOM   7140 C  CB    . ASN   D 1 109 ? 138.931 146.941 133.728 1.00 51.07  ? 85  ASN   C CB    1 
ATOM   7141 C  CG    . ASN   D 1 109 ? 140.235 147.654 133.449 1.00 60.80  ? 85  ASN   C CG    1 
ATOM   7142 O  OD1   . ASN   D 1 109 ? 140.283 148.879 133.378 1.00 65.30  ? 85  ASN   C OD1   1 
ATOM   7143 N  ND2   . ASN   D 1 109 ? 141.307 146.886 133.298 1.00 57.62  ? 85  ASN   C ND2   1 
ATOM   7144 N  N     . GLN   D 1 110 ? 138.044 145.915 130.941 1.00 66.11  ? 86  GLN   C N     1 
ATOM   7145 C  CA    . GLN   D 1 110 ? 138.370 145.597 129.556 1.00 56.08  ? 86  GLN   C CA    1 
ATOM   7146 C  C     . GLN   D 1 110 ? 137.378 146.230 128.589 1.00 62.46  ? 86  GLN   C C     1 
ATOM   7147 O  O     . GLN   D 1 110 ? 137.781 146.771 127.553 1.00 68.85  ? 86  GLN   C O     1 
ATOM   7148 C  CB    . GLN   D 1 110 ? 138.417 144.083 129.364 1.00 56.96  ? 86  GLN   C CB    1 
ATOM   7149 C  CG    . GLN   D 1 110 ? 139.758 143.461 129.711 1.00 62.06  ? 86  GLN   C CG    1 
ATOM   7150 C  CD    . GLN   D 1 110 ? 139.682 141.954 129.847 1.00 69.12  ? 86  GLN   C CD    1 
ATOM   7151 O  OE1   . GLN   D 1 110 ? 138.601 141.369 129.805 1.00 71.11  ? 86  GLN   C OE1   1 
ATOM   7152 N  NE2   . GLN   D 1 110 ? 140.835 141.317 130.013 1.00 67.19  ? 86  GLN   C NE2   1 
ATOM   7153 N  N     . GLY   D 1 111 ? 136.082 146.179 128.905 1.00 57.62  ? 87  GLY   C N     1 
ATOM   7154 C  CA    . GLY   D 1 111 ? 135.098 146.778 128.022 1.00 55.65  ? 87  GLY   C CA    1 
ATOM   7155 C  C     . GLY   D 1 111 ? 135.279 148.275 127.876 1.00 58.21  ? 87  GLY   C C     1 
ATOM   7156 O  O     . GLY   D 1 111 ? 135.238 148.805 126.763 1.00 62.99  ? 87  GLY   C O     1 
ATOM   7157 N  N     . ILE   D 1 112 ? 135.504 148.976 128.990 1.00 58.39  ? 88  ILE   C N     1 
ATOM   7158 C  CA    . ILE   D 1 112 ? 135.673 150.423 128.912 1.00 56.77  ? 88  ILE   C CA    1 
ATOM   7159 C  C     . ILE   D 1 112 ? 136.972 150.776 128.196 1.00 57.70  ? 88  ILE   C C     1 
ATOM   7160 O  O     . ILE   D 1 112 ? 137.029 151.744 127.429 1.00 60.45  ? 88  ILE   C O     1 
ATOM   7161 C  CB    . ILE   D 1 112 ? 135.599 151.050 130.316 1.00 59.05  ? 88  ILE   C CB    1 
ATOM   7162 C  CG1   . ILE   D 1 112 ? 134.185 150.911 130.880 1.00 53.91  ? 88  ILE   C CG1   1 
ATOM   7163 C  CG2   . ILE   D 1 112 ? 135.999 152.515 130.275 1.00 58.06  ? 88  ILE   C CG2   1 
ATOM   7164 C  CD1   . ILE   D 1 112 ? 134.013 151.502 132.257 1.00 54.16  ? 88  ILE   C CD1   1 
ATOM   7165 N  N     . LEU   D 1 113 ? 138.033 149.995 128.418 1.00 61.75  ? 89  LEU   C N     1 
ATOM   7166 C  CA    . LEU   D 1 113 ? 139.314 150.312 127.795 1.00 64.65  ? 89  LEU   C CA    1 
ATOM   7167 C  C     . LEU   D 1 113 ? 139.306 150.047 126.294 1.00 66.59  ? 89  LEU   C C     1 
ATOM   7168 O  O     . LEU   D 1 113 ? 139.866 150.838 125.528 1.00 68.64  ? 89  LEU   C O     1 
ATOM   7169 C  CB    . LEU   D 1 113 ? 140.436 149.518 128.462 1.00 66.63  ? 89  LEU   C CB    1 
ATOM   7170 C  CG    . LEU   D 1 113 ? 141.027 150.120 129.739 1.00 65.66  ? 89  LEU   C CG    1 
ATOM   7171 C  CD1   . LEU   D 1 113 ? 142.219 149.304 130.209 1.00 64.53  ? 89  LEU   C CD1   1 
ATOM   7172 C  CD2   . LEU   D 1 113 ? 141.420 151.571 129.520 1.00 66.23  ? 89  LEU   C CD2   1 
ATOM   7173 N  N     . GLU   D 1 114 ? 138.688 148.951 125.850 1.00 77.48  ? 90  GLU   C N     1 
ATOM   7174 C  CA    . GLU   D 1 114 ? 138.704 148.607 124.434 1.00 75.85  ? 90  GLU   C CA    1 
ATOM   7175 C  C     . GLU   D 1 114 ? 137.602 149.289 123.635 1.00 79.36  ? 90  GLU   C C     1 
ATOM   7176 O  O     . GLU   D 1 114 ? 137.765 149.494 122.428 1.00 80.42  ? 90  GLU   C O     1 
ATOM   7177 C  CB    . GLU   D 1 114 ? 138.598 147.090 124.256 1.00 72.63  ? 90  GLU   C CB    1 
ATOM   7178 C  CG    . GLU   D 1 114 ? 139.624 146.303 125.050 1.00 73.95  ? 90  GLU   C CG    1 
ATOM   7179 C  CD    . GLU   D 1 114 ? 139.661 144.840 124.661 1.00 82.44  ? 90  GLU   C CD    1 
ATOM   7180 O  OE1   . GLU   D 1 114 ? 138.677 144.359 124.063 1.00 82.29  ? 90  GLU   C OE1   1 
ATOM   7181 O  OE2   . GLU   D 1 114 ? 140.673 144.170 124.955 1.00 82.74  ? 90  GLU   C OE2   1 
ATOM   7182 N  N     . GLY   D 1 115 ? 136.481 149.646 124.271 1.00 67.56  ? 91  GLY   C N     1 
ATOM   7183 C  CA    . GLY   D 1 115 ? 135.423 150.331 123.553 1.00 57.07  ? 91  GLY   C CA    1 
ATOM   7184 C  C     . GLY   D 1 115 ? 135.725 151.774 123.216 1.00 62.42  ? 91  GLY   C C     1 
ATOM   7185 O  O     . GLY   D 1 115 ? 135.096 152.330 122.311 1.00 68.53  ? 91  GLY   C O     1 
ATOM   7186 N  N     . THR   D 1 116 ? 136.671 152.392 123.923 1.00 62.46  ? 92  THR   C N     1 
ATOM   7187 C  CA    . THR   D 1 116 ? 137.040 153.772 123.626 1.00 61.57  ? 92  THR   C CA    1 
ATOM   7188 C  C     . THR   D 1 116 ? 137.804 153.878 122.311 1.00 64.41  ? 92  THR   C C     1 
ATOM   7189 O  O     . THR   D 1 116 ? 137.765 154.924 121.655 1.00 68.54  ? 92  THR   C O     1 
ATOM   7190 C  CB    . THR   D 1 116 ? 137.869 154.348 124.775 1.00 61.32  ? 92  THR   C CB    1 
ATOM   7191 O  OG1   . THR   D 1 116 ? 137.231 154.046 126.021 1.00 68.60  ? 92  THR   C OG1   1 
ATOM   7192 C  CG2   . THR   D 1 116 ? 138.008 155.855 124.642 1.00 60.74  ? 92  THR   C CG2   1 
ATOM   7193 N  N     . LYS   D 1 117 ? 138.491 152.812 121.909 1.00 79.90  ? 93  LYS   C N     1 
ATOM   7194 C  CA    . LYS   D 1 117 ? 139.276 152.796 120.684 1.00 77.55  ? 93  LYS   C CA    1 
ATOM   7195 C  C     . LYS   D 1 117 ? 138.609 152.007 119.565 1.00 80.62  ? 93  LYS   C C     1 
ATOM   7196 O  O     . LYS   D 1 117 ? 139.254 151.727 118.550 1.00 86.01  ? 93  LYS   C O     1 
ATOM   7197 C  CB    . LYS   D 1 117 ? 140.667 152.224 120.964 1.00 79.39  ? 93  LYS   C CB    1 
ATOM   7198 C  CG    . LYS   D 1 117 ? 141.168 152.483 122.375 1.00 82.11  ? 93  LYS   C CG    1 
ATOM   7199 C  CD    . LYS   D 1 117 ? 142.567 151.928 122.586 1.00 81.54  ? 93  LYS   C CD    1 
ATOM   7200 C  CE    . LYS   D 1 117 ? 142.702 150.529 122.005 1.00 82.16  ? 93  LYS   C CE    1 
ATOM   7201 N  NZ    . LYS   D 1 117 ? 143.803 149.764 122.651 1.00 83.58  ? 93  LYS   C NZ    1 
ATOM   7202 N  N     . ALA   D 1 118 ? 137.337 151.639 119.726 1.00 82.52  ? 94  ALA   C N     1 
ATOM   7203 C  CA    . ALA   D 1 118 ? 136.679 150.790 118.736 1.00 83.68  ? 94  ALA   C CA    1 
ATOM   7204 C  C     . ALA   D 1 118 ? 136.473 151.527 117.417 1.00 85.35  ? 94  ALA   C C     1 
ATOM   7205 O  O     . ALA   D 1 118 ? 136.789 150.999 116.345 1.00 87.21  ? 94  ALA   C O     1 
ATOM   7206 C  CB    . ALA   D 1 118 ? 135.346 150.282 119.282 1.00 82.97  ? 94  ALA   C CB    1 
ATOM   7207 N  N     . ILE   D 1 119 ? 135.936 152.747 117.475 1.00 88.87  ? 95  ILE   C N     1 
ATOM   7208 C  CA    . ILE   D 1 119 ? 135.679 153.497 116.250 1.00 90.76  ? 95  ILE   C CA    1 
ATOM   7209 C  C     . ILE   D 1 119 ? 136.986 153.948 115.609 1.00 89.19  ? 95  ILE   C C     1 
ATOM   7210 O  O     . ILE   D 1 119 ? 137.158 153.855 114.388 1.00 87.61  ? 95  ILE   C O     1 
ATOM   7211 C  CB    . ILE   D 1 119 ? 134.745 154.687 116.538 1.00 89.22  ? 95  ILE   C CB    1 
ATOM   7212 C  CG1   . ILE   D 1 119 ? 133.326 154.190 116.820 1.00 89.62  ? 95  ILE   C CG1   1 
ATOM   7213 C  CG2   . ILE   D 1 119 ? 134.746 155.669 115.377 1.00 86.21  ? 95  ILE   C CG2   1 
ATOM   7214 C  CD1   . ILE   D 1 119 ? 132.284 155.286 116.845 1.00 89.69  ? 95  ILE   C CD1   1 
ATOM   7215 N  N     . THR   D 1 120 ? 137.929 154.436 116.419 1.00 92.03  ? 96  THR   C N     1 
ATOM   7216 C  CA    . THR   D 1 120 ? 139.185 154.948 115.882 1.00 90.29  ? 96  THR   C CA    1 
ATOM   7217 C  C     . THR   D 1 120 ? 139.974 153.862 115.161 1.00 93.77  ? 96  THR   C C     1 
ATOM   7218 O  O     . THR   D 1 120 ? 140.511 154.094 114.071 1.00 95.74  ? 96  THR   C O     1 
ATOM   7219 C  CB    . THR   D 1 120 ? 140.022 155.554 117.008 1.00 90.38  ? 96  THR   C CB    1 
ATOM   7220 O  OG1   . THR   D 1 120 ? 139.329 156.672 117.577 1.00 90.88  ? 96  THR   C OG1   1 
ATOM   7221 C  CG2   . THR   D 1 120 ? 141.373 156.011 116.486 1.00 90.51  ? 96  THR   C CG2   1 
ATOM   7222 N  N     . GLN   D 1 121 ? 140.053 152.668 115.749 1.00 102.74 ? 97  GLN   C N     1 
ATOM   7223 C  CA    . GLN   D 1 121 ? 140.868 151.606 115.171 1.00 101.01 ? 97  GLN   C CA    1 
ATOM   7224 C  C     . GLN   D 1 121 ? 140.214 150.986 113.941 1.00 104.17 ? 97  GLN   C C     1 
ATOM   7225 O  O     . GLN   D 1 121 ? 140.899 150.696 112.953 1.00 107.23 ? 97  GLN   C O     1 
ATOM   7226 C  CB    . GLN   D 1 121 ? 141.142 150.530 116.221 1.00 99.16  ? 97  GLN   C CB    1 
ATOM   7227 C  CG    . GLN   D 1 121 ? 142.248 150.885 117.196 1.00 102.41 ? 97  GLN   C CG    1 
ATOM   7228 C  CD    . GLN   D 1 121 ? 142.713 149.691 118.005 1.00 104.51 ? 97  GLN   C CD    1 
ATOM   7229 O  OE1   . GLN   D 1 121 ? 142.076 148.638 118.000 1.00 105.12 ? 97  GLN   C OE1   1 
ATOM   7230 N  NE2   . GLN   D 1 121 ? 143.829 149.850 118.706 1.00 102.13 ? 97  GLN   C NE2   1 
ATOM   7231 N  N     . LYS   D 1 122 ? 138.902 150.774 113.980 1.00 102.40 ? 98  LYS   C N     1 
ATOM   7232 C  CA    . LYS   D 1 122 ? 138.190 150.012 112.960 1.00 104.29 ? 98  LYS   C CA    1 
ATOM   7233 C  C     . LYS   D 1 122 ? 137.253 150.887 112.133 1.00 105.93 ? 98  LYS   C C     1 
ATOM   7234 O  O     . LYS   D 1 122 ? 136.134 150.487 111.812 1.00 105.00 ? 98  LYS   C O     1 
ATOM   7235 C  CB    . LYS   D 1 122 ? 137.412 148.865 113.600 1.00 102.11 ? 98  LYS   C CB    1 
ATOM   7236 C  CG    . LYS   D 1 122 ? 138.128 148.218 114.775 1.00 103.69 ? 98  LYS   C CG    1 
ATOM   7237 C  CD    . LYS   D 1 122 ? 137.195 147.325 115.578 1.00 102.64 ? 98  LYS   C CD    1 
ATOM   7238 C  CE    . LYS   D 1 122 ? 136.369 146.427 114.674 1.00 100.50 ? 98  LYS   C CE    1 
ATOM   7239 N  NZ    . LYS   D 1 122 ? 137.021 145.105 114.468 1.00 99.39  ? 98  LYS   C NZ    1 
ATOM   7240 N  N     . PHE   D 1 123 ? 137.693 152.096 111.779 1.00 110.26 ? 99  PHE   C N     1 
ATOM   7241 C  CA    . PHE   D 1 123 ? 136.837 152.980 110.993 1.00 110.93 ? 99  PHE   C CA    1 
ATOM   7242 C  C     . PHE   D 1 123 ? 136.907 152.665 109.503 1.00 112.94 ? 99  PHE   C C     1 
ATOM   7243 O  O     . PHE   D 1 123 ? 135.868 152.577 108.839 1.00 113.04 ? 99  PHE   C O     1 
ATOM   7244 C  CB    . PHE   D 1 123 ? 137.214 154.440 111.238 1.00 111.38 ? 99  PHE   C CB    1 
ATOM   7245 C  CG    . PHE   D 1 123 ? 136.232 155.422 110.664 1.00 112.17 ? 99  PHE   C CG    1 
ATOM   7246 C  CD1   . PHE   D 1 123 ? 134.879 155.129 110.630 1.00 111.64 ? 99  PHE   C CD1   1 
ATOM   7247 C  CD2   . PHE   D 1 123 ? 136.662 156.636 110.155 1.00 110.71 ? 99  PHE   C CD2   1 
ATOM   7248 C  CE1   . PHE   D 1 123 ? 133.974 156.028 110.101 1.00 112.57 ? 99  PHE   C CE1   1 
ATOM   7249 C  CE2   . PHE   D 1 123 ? 135.762 157.539 109.625 1.00 111.18 ? 99  PHE   C CE2   1 
ATOM   7250 C  CZ    . PHE   D 1 123 ? 134.417 157.235 109.598 1.00 112.62 ? 99  PHE   C CZ    1 
ATOM   7251 N  N     . ASN   D 1 124 ? 138.116 152.499 108.961 1.00 116.19 ? 100 ASN   C N     1 
ATOM   7252 C  CA    . ASN   D 1 124 ? 138.265 152.311 107.521 1.00 115.63 ? 100 ASN   C CA    1 
ATOM   7253 C  C     . ASN   D 1 124 ? 137.611 151.023 107.040 1.00 114.72 ? 100 ASN   C C     1 
ATOM   7254 O  O     . ASN   D 1 124 ? 136.987 151.009 105.974 1.00 116.80 ? 100 ASN   C O     1 
ATOM   7255 C  CB    . ASN   D 1 124 ? 139.745 152.328 107.139 1.00 115.71 ? 100 ASN   C CB    1 
ATOM   7256 C  CG    . ASN   D 1 124 ? 140.371 153.699 107.294 1.00 116.93 ? 100 ASN   C CG    1 
ATOM   7257 O  OD1   . ASN   D 1 124 ? 139.670 154.708 107.377 1.00 115.34 ? 100 ASN   C OD1   1 
ATOM   7258 N  ND2   . ASN   D 1 124 ? 141.698 153.743 107.334 1.00 116.76 ? 100 ASN   C ND2   1 
ATOM   7259 N  N     . GLN   D 1 125 ? 137.739 149.936 107.801 1.00 114.32 ? 101 GLN   C N     1 
ATOM   7260 C  CA    . GLN   D 1 125 ? 137.146 148.666 107.401 1.00 115.54 ? 101 GLN   C CA    1 
ATOM   7261 C  C     . GLN   D 1 125 ? 135.625 148.681 107.466 1.00 116.44 ? 101 GLN   C C     1 
ATOM   7262 O  O     . GLN   D 1 125 ? 134.986 147.830 106.839 1.00 115.34 ? 101 GLN   C O     1 
ATOM   7263 C  CB    . GLN   D 1 125 ? 137.673 147.507 108.262 1.00 114.95 ? 101 GLN   C CB    1 
ATOM   7264 C  CG    . GLN   D 1 125 ? 139.192 147.253 108.248 1.00 114.53 ? 101 GLN   C CG    1 
ATOM   7265 C  CD    . GLN   D 1 125 ? 140.037 148.464 108.590 1.00 115.45 ? 101 GLN   C CD    1 
ATOM   7266 O  OE1   . GLN   D 1 125 ? 140.426 149.231 107.709 1.00 114.07 ? 101 GLN   C OE1   1 
ATOM   7267 N  NE2   . GLN   D 1 125 ? 140.331 148.640 109.872 1.00 115.65 ? 101 GLN   C NE2   1 
ATOM   7268 N  N     . VAL   D 1 126 ? 135.033 149.620 108.203 1.00 110.05 ? 102 VAL   C N     1 
ATOM   7269 C  CA    . VAL   D 1 126 ? 133.582 149.702 108.329 1.00 111.29 ? 102 VAL   C CA    1 
ATOM   7270 C  C     . VAL   D 1 126 ? 132.994 150.918 107.633 1.00 111.45 ? 102 VAL   C C     1 
ATOM   7271 O  O     . VAL   D 1 126 ? 131.765 150.975 107.462 1.00 110.71 ? 102 VAL   C O     1 
ATOM   7272 C  CB    . VAL   D 1 126 ? 133.140 149.688 109.807 1.00 109.68 ? 102 VAL   C CB    1 
ATOM   7273 C  CG1   . VAL   D 1 126 ? 133.875 148.600 110.574 1.00 107.44 ? 102 VAL   C CG1   1 
ATOM   7274 C  CG2   . VAL   D 1 126 ? 133.363 151.053 110.433 1.00 107.12 ? 102 VAL   C CG2   1 
ATOM   7275 N  N     . SER   D 1 127 ? 133.814 151.896 107.241 1.00 106.33 ? 103 SER   C N     1 
ATOM   7276 C  CA    . SER   D 1 127 ? 133.287 153.030 106.491 1.00 104.80 ? 103 SER   C CA    1 
ATOM   7277 C  C     . SER   D 1 127 ? 132.724 152.581 105.150 1.00 105.28 ? 103 SER   C C     1 
ATOM   7278 O  O     . SER   D 1 127 ? 131.663 153.053 104.724 1.00 103.71 ? 103 SER   C O     1 
ATOM   7279 C  CB    . SER   D 1 127 ? 134.373 154.087 106.294 1.00 102.74 ? 103 SER   C CB    1 
ATOM   7280 O  OG    . SER   D 1 127 ? 135.393 153.619 105.429 1.00 106.35 ? 103 SER   C OG    1 
ATOM   7281 N  N     . LYS   D 1 128 ? 133.421 151.667 104.472 1.00 112.49 ? 104 LYS   C N     1 
ATOM   7282 C  CA    . LYS   D 1 128 ? 132.904 151.110 103.228 1.00 112.67 ? 104 LYS   C CA    1 
ATOM   7283 C  C     . LYS   D 1 128 ? 131.707 150.202 103.487 1.00 113.63 ? 104 LYS   C C     1 
ATOM   7284 O  O     . LYS   D 1 128 ? 130.748 150.194 102.708 1.00 113.23 ? 104 LYS   C O     1 
ATOM   7285 C  CB    . LYS   D 1 128 ? 134.010 150.352 102.498 1.00 112.98 ? 104 LYS   C CB    1 
ATOM   7286 C  CG    . LYS   D 1 128 ? 135.371 151.025 102.577 1.00 112.97 ? 104 LYS   C CG    1 
ATOM   7287 C  CD    . LYS   D 1 128 ? 135.660 151.839 101.328 1.00 114.29 ? 104 LYS   C CD    1 
ATOM   7288 C  CE    . LYS   D 1 128 ? 136.988 152.568 101.441 1.00 112.85 ? 104 LYS   C CE    1 
ATOM   7289 N  NZ    . LYS   D 1 128 ? 137.900 152.231 100.314 1.00 114.31 ? 104 LYS   C NZ    1 
ATOM   7290 N  N     . MET   D 1 129 ? 131.747 149.435 104.573 1.00 123.14 ? 105 MET   C N     1 
ATOM   7291 C  CA    . MET   D 1 129 ? 130.654 148.536 104.905 1.00 123.29 ? 105 MET   C CA    1 
ATOM   7292 C  C     . MET   D 1 129 ? 129.424 149.329 105.339 1.00 123.81 ? 105 MET   C C     1 
ATOM   7293 O  O     . MET   D 1 129 ? 129.516 150.474 105.789 1.00 123.37 ? 105 MET   C O     1 
ATOM   7294 C  CB    . MET   D 1 129 ? 131.078 147.564 106.006 1.00 121.07 ? 105 MET   C CB    1 
ATOM   7295 C  CG    . MET   D 1 129 ? 132.207 146.633 105.598 1.00 122.93 ? 105 MET   C CG    1 
ATOM   7296 S  SD    . MET   D 1 129 ? 132.145 145.033 106.424 1.00 126.56 ? 105 MET   C SD    1 
ATOM   7297 C  CE    . MET   D 1 129 ? 132.170 143.927 105.016 1.00 122.05 ? 105 MET   C CE    1 
ATOM   7298 N  N     . ASN   D 1 130 ? 128.258 148.704 105.198 1.00 122.69 ? 106 ASN   C N     1 
ATOM   7299 C  CA    . ASN   D 1 130 ? 126.976 149.363 105.444 1.00 122.60 ? 106 ASN   C CA    1 
ATOM   7300 C  C     . ASN   D 1 130 ? 126.266 148.677 106.608 1.00 120.86 ? 106 ASN   C C     1 
ATOM   7301 O  O     . ASN   D 1 130 ? 125.441 147.781 106.416 1.00 120.28 ? 106 ASN   C O     1 
ATOM   7302 C  CB    . ASN   D 1 130 ? 126.116 149.355 104.174 1.00 121.87 ? 106 ASN   C CB    1 
ATOM   7303 C  CG    . ASN   D 1 130 ? 126.878 149.834 102.954 1.00 121.11 ? 106 ASN   C CG    1 
ATOM   7304 O  OD1   . ASN   D 1 130 ? 127.532 149.049 102.269 1.00 122.49 ? 106 ASN   C OD1   1 
ATOM   7305 N  ND2   . ASN   D 1 130 ? 126.797 151.130 102.679 1.00 119.83 ? 106 ASN   C ND2   1 
ATOM   7306 N  N     . PHE   D 1 131 ? 126.593 149.107 107.818 1.00 104.49 ? 107 PHE   C N     1 
ATOM   7307 C  CA    . PHE   D 1 131 ? 125.838 148.788 109.018 1.00 103.67 ? 107 PHE   C CA    1 
ATOM   7308 C  C     . PHE   D 1 131 ? 125.949 149.976 109.959 1.00 106.13 ? 107 PHE   C C     1 
ATOM   7309 O  O     . PHE   D 1 131 ? 126.866 150.794 109.824 1.00 107.27 ? 107 PHE   C O     1 
ATOM   7310 C  CB    . PHE   D 1 131 ? 126.327 147.499 109.699 1.00 104.77 ? 107 PHE   C CB    1 
ATOM   7311 C  CG    . PHE   D 1 131 ? 127.809 147.445 109.940 1.00 103.98 ? 107 PHE   C CG    1 
ATOM   7312 C  CD1   . PHE   D 1 131 ? 128.379 148.126 111.003 1.00 103.43 ? 107 PHE   C CD1   1 
ATOM   7313 C  CD2   . PHE   D 1 131 ? 128.627 146.689 109.121 1.00 104.41 ? 107 PHE   C CD2   1 
ATOM   7314 C  CE1   . PHE   D 1 131 ? 129.736 148.069 111.232 1.00 102.68 ? 107 PHE   C CE1   1 
ATOM   7315 C  CE2   . PHE   D 1 131 ? 129.987 146.628 109.345 1.00 106.27 ? 107 PHE   C CE2   1 
ATOM   7316 C  CZ    . PHE   D 1 131 ? 130.542 147.318 110.402 1.00 106.07 ? 107 PHE   C CZ    1 
ATOM   7317 N  N     . PRO   D 1 132 ? 125.016 150.118 110.902 1.00 92.26  ? 108 PRO   C N     1 
ATOM   7318 C  CA    . PRO   D 1 132 ? 125.052 151.278 111.801 1.00 89.30  ? 108 PRO   C CA    1 
ATOM   7319 C  C     . PRO   D 1 132 ? 126.367 151.373 112.563 1.00 88.09  ? 108 PRO   C C     1 
ATOM   7320 O  O     . PRO   D 1 132 ? 126.918 150.371 113.021 1.00 89.72  ? 108 PRO   C O     1 
ATOM   7321 C  CB    . PRO   D 1 132 ? 123.876 151.023 112.747 1.00 90.55  ? 108 PRO   C CB    1 
ATOM   7322 C  CG    . PRO   D 1 132 ? 122.928 150.215 111.943 1.00 93.39  ? 108 PRO   C CG    1 
ATOM   7323 C  CD    . PRO   D 1 132 ? 123.769 149.347 111.050 1.00 89.17  ? 108 PRO   C CD    1 
ATOM   7324 N  N     . LEU   D 1 133 ? 126.864 152.603 112.695 1.00 86.08  ? 109 LEU   C N     1 
ATOM   7325 C  CA    . LEU   D 1 133 ? 128.119 152.858 113.390 1.00 88.08  ? 109 LEU   C CA    1 
ATOM   7326 C  C     . LEU   D 1 133 ? 127.963 152.910 114.903 1.00 88.71  ? 109 LEU   C C     1 
ATOM   7327 O  O     . LEU   D 1 133 ? 128.973 152.872 115.614 1.00 87.50  ? 109 LEU   C O     1 
ATOM   7328 C  CB    . LEU   D 1 133 ? 128.731 154.172 112.898 1.00 89.56  ? 109 LEU   C CB    1 
ATOM   7329 C  CG    . LEU   D 1 133 ? 130.023 154.066 112.088 1.00 90.91  ? 109 LEU   C CG    1 
ATOM   7330 C  CD1   . LEU   D 1 133 ? 129.758 153.412 110.741 1.00 88.26  ? 109 LEU   C CD1   1 
ATOM   7331 C  CD2   . LEU   D 1 133 ? 130.656 155.436 111.910 1.00 87.28  ? 109 LEU   C CD2   1 
ATOM   7332 N  N     . SER   D 1 134 ? 126.734 152.997 115.411 1.00 87.28  ? 110 SER   C N     1 
ATOM   7333 C  CA    . SER   D 1 134 ? 126.507 153.054 116.848 1.00 83.02  ? 110 SER   C CA    1 
ATOM   7334 C  C     . SER   D 1 134 ? 126.562 151.687 117.512 1.00 83.86  ? 110 SER   C C     1 
ATOM   7335 O  O     . SER   D 1 134 ? 126.591 151.618 118.746 1.00 86.24  ? 110 SER   C O     1 
ATOM   7336 C  CB    . SER   D 1 134 ? 125.154 153.711 117.138 1.00 81.89  ? 110 SER   C CB    1 
ATOM   7337 O  OG    . SER   D 1 134 ? 124.088 152.838 116.816 1.00 81.78  ? 110 SER   C OG    1 
ATOM   7338 N  N     . ILE   D 1 135 ? 126.580 150.604 116.735 1.00 72.79  ? 111 ILE   C N     1 
ATOM   7339 C  CA    . ILE   D 1 135 ? 126.639 149.256 117.281 1.00 69.43  ? 111 ILE   C CA    1 
ATOM   7340 C  C     . ILE   D 1 135 ? 128.060 148.701 117.270 1.00 70.53  ? 111 ILE   C C     1 
ATOM   7341 O  O     . ILE   D 1 135 ? 128.269 147.542 117.636 1.00 73.09  ? 111 ILE   C O     1 
ATOM   7342 C  CB    . ILE   D 1 135 ? 125.686 148.310 116.533 1.00 71.02  ? 111 ILE   C CB    1 
ATOM   7343 C  CG1   . ILE   D 1 135 ? 126.238 147.983 115.146 1.00 71.50  ? 111 ILE   C CG1   1 
ATOM   7344 C  CG2   . ILE   D 1 135 ? 124.303 148.927 116.423 1.00 71.11  ? 111 ILE   C CG2   1 
ATOM   7345 C  CD1   . ILE   D 1 135 ? 125.677 146.714 114.548 1.00 71.68  ? 111 ILE   C CD1   1 
ATOM   7346 N  N     . ILE   D 1 136 ? 129.039 149.501 116.860 1.00 79.02  ? 112 ILE   C N     1 
ATOM   7347 C  CA    . ILE   D 1 136 ? 130.423 149.041 116.769 1.00 75.22  ? 112 ILE   C CA    1 
ATOM   7348 C  C     . ILE   D 1 136 ? 130.997 148.821 118.168 1.00 77.58  ? 112 ILE   C C     1 
ATOM   7349 O  O     . ILE   D 1 136 ? 131.491 147.719 118.444 1.00 80.65  ? 112 ILE   C O     1 
ATOM   7350 C  CB    . ILE   D 1 136 ? 131.285 150.013 115.947 1.00 78.79  ? 112 ILE   C CB    1 
ATOM   7351 C  CG1   . ILE   D 1 136 ? 131.015 149.833 114.455 1.00 79.74  ? 112 ILE   C CG1   1 
ATOM   7352 C  CG2   . ILE   D 1 136 ? 132.761 149.804 116.245 1.00 79.24  ? 112 ILE   C CG2   1 
ATOM   7353 C  CD1   . ILE   D 1 136 ? 131.753 150.822 113.595 1.00 79.41  ? 112 ILE   C CD1   1 
ATOM   7354 N  N     . PRO   D 1 137 ? 130.982 149.806 119.078 1.00 72.22  ? 113 PRO   C N     1 
ATOM   7355 C  CA    . PRO   D 1 137 ? 131.474 149.526 120.437 1.00 67.53  ? 113 PRO   C CA    1 
ATOM   7356 C  C     . PRO   D 1 137 ? 130.674 148.460 121.165 1.00 63.11  ? 113 PRO   C C     1 
ATOM   7357 O  O     . PRO   D 1 137 ? 131.271 147.664 121.902 1.00 63.57  ? 113 PRO   C O     1 
ATOM   7358 C  CB    . PRO   D 1 137 ? 131.362 150.885 121.140 1.00 63.99  ? 113 PRO   C CB    1 
ATOM   7359 C  CG    . PRO   D 1 137 ? 130.298 151.592 120.403 1.00 63.39  ? 113 PRO   C CG    1 
ATOM   7360 C  CD    . PRO   D 1 137 ? 130.502 151.198 118.975 1.00 67.65  ? 113 PRO   C CD    1 
ATOM   7361 N  N     . THR   D 1 138 ? 129.356 148.397 120.951 1.00 65.57  ? 114 THR   C N     1 
ATOM   7362 C  CA    . THR   D 1 138 ? 128.509 147.515 121.749 1.00 64.57  ? 114 THR   C CA    1 
ATOM   7363 C  C     . THR   D 1 138 ? 128.944 146.061 121.638 1.00 65.53  ? 114 THR   C C     1 
ATOM   7364 O  O     . THR   D 1 138 ? 129.188 145.405 122.658 1.00 73.80  ? 114 THR   C O     1 
ATOM   7365 C  CB    . THR   D 1 138 ? 127.047 147.667 121.333 1.00 68.67  ? 114 THR   C CB    1 
ATOM   7366 O  OG1   . THR   D 1 138 ? 126.664 149.044 121.420 1.00 67.22  ? 114 THR   C OG1   1 
ATOM   7367 C  CG2   . THR   D 1 138 ? 126.149 146.838 122.235 1.00 63.22  ? 114 THR   C CG2   1 
ATOM   7368 N  N     . TYR   D 1 139 ? 129.078 145.542 120.414 1.00 67.03  ? 115 TYR   C N     1 
ATOM   7369 C  CA    . TYR   D 1 139 ? 129.518 144.160 120.281 1.00 70.36  ? 115 TYR   C CA    1 
ATOM   7370 C  C     . TYR   D 1 139 ? 130.934 143.962 120.801 1.00 71.78  ? 115 TYR   C C     1 
ATOM   7371 O  O     . TYR   D 1 139 ? 131.249 142.869 121.285 1.00 72.33  ? 115 TYR   C O     1 
ATOM   7372 C  CB    . TYR   D 1 139 ? 129.390 143.676 118.828 1.00 69.82  ? 115 TYR   C CB    1 
ATOM   7373 C  CG    . TYR   D 1 139 ? 130.451 144.142 117.851 1.00 76.97  ? 115 TYR   C CG    1 
ATOM   7374 C  CD1   . TYR   D 1 139 ? 130.223 145.224 117.016 1.00 74.58  ? 115 TYR   C CD1   1 
ATOM   7375 C  CD2   . TYR   D 1 139 ? 131.660 143.467 117.729 1.00 78.83  ? 115 TYR   C CD2   1 
ATOM   7376 C  CE1   . TYR   D 1 139 ? 131.179 145.640 116.111 1.00 72.22  ? 115 TYR   C CE1   1 
ATOM   7377 C  CE2   . TYR   D 1 139 ? 132.622 143.881 116.829 1.00 74.04  ? 115 TYR   C CE2   1 
ATOM   7378 C  CZ    . TYR   D 1 139 ? 132.375 144.967 116.023 1.00 72.75  ? 115 TYR   C CZ    1 
ATOM   7379 O  OH    . TYR   D 1 139 ? 133.327 145.380 115.123 1.00 74.97  ? 115 TYR   C OH    1 
ATOM   7380 N  N     . ILE   D 1 140 ? 131.775 145.002 120.755 1.00 57.42  ? 116 ILE   C N     1 
ATOM   7381 C  CA    . ILE   D 1 140 ? 133.070 144.925 121.422 1.00 59.11  ? 116 ILE   C CA    1 
ATOM   7382 C  C     . ILE   D 1 140 ? 132.877 144.584 122.891 1.00 59.62  ? 116 ILE   C C     1 
ATOM   7383 O  O     . ILE   D 1 140 ? 133.496 143.650 123.416 1.00 61.14  ? 116 ILE   C O     1 
ATOM   7384 C  CB    . ILE   D 1 140 ? 133.847 146.243 121.246 1.00 62.18  ? 116 ILE   C CB    1 
ATOM   7385 C  CG1   . ILE   D 1 140 ? 134.200 146.475 119.774 1.00 59.82  ? 116 ILE   C CG1   1 
ATOM   7386 C  CG2   . ILE   D 1 140 ? 135.090 146.249 122.127 1.00 61.18  ? 116 ILE   C CG2   1 
ATOM   7387 C  CD1   . ILE   D 1 140 ? 135.580 145.998 119.384 1.00 57.05  ? 116 ILE   C CD1   1 
ATOM   7388 N  N     . VAL   D 1 141 ? 131.980 145.306 123.567 1.00 53.55  ? 117 VAL   C N     1 
ATOM   7389 C  CA    . VAL   D 1 141 ? 131.649 144.969 124.946 1.00 43.27  ? 117 VAL   C CA    1 
ATOM   7390 C  C     . VAL   D 1 141 ? 131.105 143.550 125.023 1.00 50.73  ? 117 VAL   C C     1 
ATOM   7391 O  O     . VAL   D 1 141 ? 131.460 142.781 125.926 1.00 60.64  ? 117 VAL   C O     1 
ATOM   7392 C  CB    . VAL   D 1 141 ? 130.656 145.995 125.520 1.00 46.36  ? 117 VAL   C CB    1 
ATOM   7393 C  CG1   . VAL   D 1 141 ? 130.246 145.609 126.929 1.00 54.82  ? 117 VAL   C CG1   1 
ATOM   7394 C  CG2   . VAL   D 1 141 ? 131.265 147.386 125.503 1.00 43.27  ? 117 VAL   C CG2   1 
ATOM   7395 N  N     . THR   D 1 142 ? 130.270 143.164 124.055 1.00 46.60  ? 118 THR   C N     1 
ATOM   7396 C  CA    . THR   D 1 142 ? 129.716 141.818 124.057 1.00 47.23  ? 118 THR   C CA    1 
ATOM   7397 C  C     . THR   D 1 142 ? 130.791 140.756 123.863 1.00 51.75  ? 118 THR   C C     1 
ATOM   7398 O  O     . THR   D 1 142 ? 130.557 139.590 124.195 1.00 50.31  ? 118 THR   C O     1 
ATOM   7399 C  CB    . THR   D 1 142 ? 128.640 141.685 122.978 1.00 51.52  ? 118 THR   C CB    1 
ATOM   7400 O  OG1   . THR   D 1 142 ? 127.912 142.914 122.876 1.00 46.63  ? 118 THR   C OG1   1 
ATOM   7401 C  CG2   . THR   D 1 142 ? 127.670 140.568 123.324 1.00 48.36  ? 118 THR   C CG2   1 
ATOM   7402 N  N     . SER   D 1 143 ? 131.963 141.144 123.360 1.00 60.57  ? 119 SER   C N     1 
ATOM   7403 C  CA    . SER   D 1 143 ? 133.070 140.166 123.205 1.00 60.12  ? 119 SER   C CA    1 
ATOM   7404 C  C     . SER   D 1 143 ? 133.621 139.782 124.585 1.00 64.15  ? 119 SER   C C     1 
ATOM   7405 O  O     . SER   D 1 143 ? 134.199 138.685 124.703 1.00 66.57  ? 119 SER   C O     1 
ATOM   7406 C  CB    . SER   D 1 143 ? 134.154 140.693 122.306 1.00 57.20  ? 119 SER   C CB    1 
ATOM   7407 O  OG    . SER   D 1 143 ? 134.999 141.599 122.999 1.00 59.82  ? 119 SER   C OG    1 
ATOM   7408 N  N     . ARG   D 1 144 ? 133.446 140.647 125.589 1.00 61.63  ? 120 ARG   C N     1 
ATOM   7409 C  CA    . ARG   D 1 144 ? 133.955 140.369 126.924 1.00 56.14  ? 120 ARG   C CA    1 
ATOM   7410 C  C     . ARG   D 1 144 ? 132.902 139.795 127.859 1.00 57.13  ? 120 ARG   C C     1 
ATOM   7411 O  O     . ARG   D 1 144 ? 133.235 138.935 128.685 1.00 61.05  ? 120 ARG   C O     1 
ATOM   7412 C  CB    . ARG   D 1 144 ? 134.546 141.641 127.544 1.00 49.04  ? 120 ARG   C CB    1 
ATOM   7413 C  CG    . ARG   D 1 144 ? 135.579 142.325 126.669 1.00 47.26  ? 120 ARG   C CG    1 
ATOM   7414 C  CD    . ARG   D 1 144 ? 136.662 141.344 126.260 1.00 56.09  ? 120 ARG   C CD    1 
ATOM   7415 N  NE    . ARG   D 1 144 ? 137.976 141.966 126.170 1.00 58.99  ? 120 ARG   C NE    1 
ATOM   7416 C  CZ    . ARG   D 1 144 ? 139.120 141.296 126.161 1.00 61.08  ? 120 ARG   C CZ    1 
ATOM   7417 N  NH1   . ARG   D 1 144 ? 139.149 139.976 126.250 1.00 55.24  ? 120 ARG   C NH1   1 
ATOM   7418 N  NH2   . ARG   D 1 144 ? 140.264 141.966 126.061 1.00 59.53  ? 120 ARG   C NH2   1 
ATOM   7419 N  N     . PHE   D 1 145 ? 131.644 140.228 127.723 1.00 46.67  ? 121 PHE   C N     1 
ATOM   7420 C  CA    . PHE   D 1 145 ? 130.579 139.760 128.605 1.00 43.98  ? 121 PHE   C CA    1 
ATOM   7421 C  C     . PHE   D 1 145 ? 130.542 138.242 128.688 1.00 54.23  ? 121 PHE   C C     1 
ATOM   7422 O  O     . PHE   D 1 145 ? 130.458 137.689 129.793 1.00 58.84  ? 121 PHE   C O     1 
ATOM   7423 C  CB    . PHE   D 1 145 ? 129.232 140.295 128.121 1.00 45.95  ? 121 PHE   C CB    1 
ATOM   7424 C  CG    . PHE   D 1 145 ? 128.144 140.234 129.153 1.00 48.00  ? 121 PHE   C CG    1 
ATOM   7425 C  CD1   . PHE   D 1 145 ? 128.366 140.689 130.441 1.00 54.32  ? 121 PHE   C CD1   1 
ATOM   7426 C  CD2   . PHE   D 1 145 ? 126.898 139.722 128.834 1.00 47.76  ? 121 PHE   C CD2   1 
ATOM   7427 C  CE1   . PHE   D 1 145 ? 127.366 140.634 131.392 1.00 53.31  ? 121 PHE   C CE1   1 
ATOM   7428 C  CE2   . PHE   D 1 145 ? 125.894 139.665 129.781 1.00 51.58  ? 121 PHE   C CE2   1 
ATOM   7429 C  CZ    . PHE   D 1 145 ? 126.129 140.122 131.061 1.00 55.06  ? 121 PHE   C CZ    1 
ATOM   7430 N  N     . TYR   D 1 146 ? 130.630 137.560 127.540 1.00 70.04  ? 122 TYR   C N     1 
ATOM   7431 C  CA    . TYR   D 1 146 ? 130.696 136.101 127.525 1.00 65.57  ? 122 TYR   C CA    1 
ATOM   7432 C  C     . TYR   D 1 146 ? 131.649 135.586 128.594 1.00 68.93  ? 122 TYR   C C     1 
ATOM   7433 O  O     . TYR   D 1 146 ? 131.235 134.864 129.512 1.00 73.48  ? 122 TYR   C O     1 
ATOM   7434 C  CB    . TYR   D 1 146 ? 131.134 135.600 126.148 1.00 68.92  ? 122 TYR   C CB    1 
ATOM   7435 C  CG    . TYR   D 1 146 ? 130.174 135.905 125.022 1.00 69.56  ? 122 TYR   C CG    1 
ATOM   7436 C  CD1   . TYR   D 1 146 ? 128.823 135.613 125.136 1.00 69.54  ? 122 TYR   C CD1   1 
ATOM   7437 C  CD2   . TYR   D 1 146 ? 130.624 136.468 123.836 1.00 67.32  ? 122 TYR   C CD2   1 
ATOM   7438 C  CE1   . TYR   D 1 146 ? 127.945 135.884 124.107 1.00 69.64  ? 122 TYR   C CE1   1 
ATOM   7439 C  CE2   . TYR   D 1 146 ? 129.753 136.743 122.801 1.00 68.04  ? 122 TYR   C CE2   1 
ATOM   7440 C  CZ    . TYR   D 1 146 ? 128.415 136.448 122.942 1.00 70.61  ? 122 TYR   C CZ    1 
ATOM   7441 O  OH    . TYR   D 1 146 ? 127.544 136.720 121.913 1.00 71.76  ? 122 TYR   C OH    1 
ATOM   7442 N  N     . GLY   D 1 147 ? 132.918 136.000 128.524 1.00 66.37  ? 123 GLY   C N     1 
ATOM   7443 C  CA    . GLY   D 1 147 ? 133.888 135.522 129.490 1.00 65.34  ? 123 GLY   C CA    1 
ATOM   7444 C  C     . GLY   D 1 147 ? 133.458 135.784 130.915 1.00 66.12  ? 123 GLY   C C     1 
ATOM   7445 O  O     . GLY   D 1 147 ? 133.490 134.873 131.752 1.00 68.07  ? 123 GLY   C O     1 
ATOM   7446 N  N     . HIS   D 1 148 ? 132.978 137.002 131.193 1.00 51.55  ? 124 HIS   C N     1 
ATOM   7447 C  CA    . HIS   D 1 148 ? 132.498 137.315 132.533 1.00 46.83  ? 124 HIS   C CA    1 
ATOM   7448 C  C     . HIS   D 1 148 ? 131.484 136.283 132.993 1.00 47.73  ? 124 HIS   C C     1 
ATOM   7449 O  O     . HIS   D 1 148 ? 131.643 135.685 134.066 1.00 55.93  ? 124 HIS   C O     1 
ATOM   7450 C  CB    . HIS   D 1 148 ? 131.888 138.716 132.563 1.00 48.40  ? 124 HIS   C CB    1 
ATOM   7451 C  CG    . HIS   D 1 148 ? 130.990 138.960 133.737 1.00 57.70  ? 124 HIS   C CG    1 
ATOM   7452 N  ND1   . HIS   D 1 148 ? 129.669 139.327 133.599 1.00 53.57  ? 124 HIS   C ND1   1 
ATOM   7453 C  CD2   . HIS   D 1 148 ? 131.222 138.886 135.069 1.00 57.13  ? 124 HIS   C CD2   1 
ATOM   7454 C  CE1   . HIS   D 1 148 ? 129.127 139.469 134.795 1.00 51.17  ? 124 HIS   C CE1   1 
ATOM   7455 N  NE2   . HIS   D 1 148 ? 130.047 139.208 135.704 1.00 48.97  ? 124 HIS   C NE2   1 
ATOM   7456 N  N     . LEU   D 1 149 ? 130.479 136.006 132.153 1.00 48.90  ? 125 LEU   C N     1 
ATOM   7457 C  CA    . LEU   D 1 149 ? 129.462 135.030 132.521 1.00 49.32  ? 125 LEU   C CA    1 
ATOM   7458 C  C     . LEU   D 1 149 ? 130.105 133.724 132.956 1.00 49.78  ? 125 LEU   C C     1 
ATOM   7459 O  O     . LEU   D 1 149 ? 129.826 133.226 134.054 1.00 55.43  ? 125 LEU   C O     1 
ATOM   7460 C  CB    . LEU   D 1 149 ? 128.505 134.799 131.353 1.00 48.91  ? 125 LEU   C CB    1 
ATOM   7461 C  CG    . LEU   D 1 149 ? 127.493 135.909 131.065 1.00 47.99  ? 125 LEU   C CG    1 
ATOM   7462 C  CD1   . LEU   D 1 149 ? 126.649 135.558 129.850 1.00 50.49  ? 125 LEU   C CD1   1 
ATOM   7463 C  CD2   . LEU   D 1 149 ? 126.613 136.162 132.276 1.00 46.02  ? 125 LEU   C CD2   1 
ATOM   7464 N  N     . GLY   D 1 150 ? 131.037 133.209 132.147 1.00 49.14  ? 126 GLY   C N     1 
ATOM   7465 C  CA    . GLY   D 1 150 ? 131.692 131.966 132.509 1.00 50.55  ? 126 GLY   C CA    1 
ATOM   7466 C  C     . GLY   D 1 150 ? 132.321 132.041 133.883 1.00 55.36  ? 126 GLY   C C     1 
ATOM   7467 O  O     . GLY   D 1 150 ? 132.027 131.217 134.755 1.00 57.42  ? 126 GLY   C O     1 
ATOM   7468 N  N     . LEU   D 1 151 ? 133.122 133.085 134.122 1.00 62.34  ? 127 LEU   C N     1 
ATOM   7469 C  CA    . LEU   D 1 151 ? 133.750 133.233 135.428 1.00 60.03  ? 127 LEU   C CA    1 
ATOM   7470 C  C     . LEU   D 1 151 ? 132.699 133.237 136.526 1.00 58.24  ? 127 LEU   C C     1 
ATOM   7471 O  O     . LEU   D 1 151 ? 132.824 132.497 137.511 1.00 64.33  ? 127 LEU   C O     1 
ATOM   7472 C  CB    . LEU   D 1 151 ? 134.586 134.512 135.473 1.00 60.65  ? 127 LEU   C CB    1 
ATOM   7473 C  CG    . LEU   D 1 151 ? 135.515 134.671 136.678 1.00 58.06  ? 127 LEU   C CG    1 
ATOM   7474 C  CD1   . LEU   D 1 151 ? 136.720 133.757 136.552 1.00 60.56  ? 127 LEU   C CD1   1 
ATOM   7475 C  CD2   . LEU   D 1 151 ? 135.952 136.116 136.830 1.00 59.47  ? 127 LEU   C CD2   1 
ATOM   7476 N  N     . LEU   D 1 152 ? 131.619 134.002 136.328 1.00 43.12  ? 128 LEU   C N     1 
ATOM   7477 C  CA    . LEU   D 1 152 ? 130.576 134.065 137.342 1.00 43.79  ? 128 LEU   C CA    1 
ATOM   7478 C  C     . LEU   D 1 152 ? 130.084 132.670 137.688 1.00 48.09  ? 128 LEU   C C     1 
ATOM   7479 O  O     . LEU   D 1 152 ? 130.029 132.300 138.868 1.00 56.11  ? 128 LEU   C O     1 
ATOM   7480 C  CB    . LEU   D 1 152 ? 129.423 134.943 136.857 1.00 44.93  ? 128 LEU   C CB    1 
ATOM   7481 C  CG    . LEU   D 1 152 ? 128.228 135.096 137.797 1.00 42.96  ? 128 LEU   C CG    1 
ATOM   7482 C  CD1   . LEU   D 1 152 ? 128.604 135.919 139.015 1.00 47.18  ? 128 LEU   C CD1   1 
ATOM   7483 C  CD2   . LEU   D 1 152 ? 127.058 135.725 137.066 1.00 43.83  ? 128 LEU   C CD2   1 
ATOM   7484 N  N     . LEU   D 1 153 ? 129.802 131.855 136.666 1.00 60.39  ? 129 LEU   C N     1 
ATOM   7485 C  CA    . LEU   D 1 153 ? 129.331 130.501 136.925 1.00 60.63  ? 129 LEU   C CA    1 
ATOM   7486 C  C     . LEU   D 1 153 ? 130.304 129.762 137.828 1.00 61.52  ? 129 LEU   C C     1 
ATOM   7487 O  O     . LEU   D 1 153 ? 129.915 129.253 138.889 1.00 63.61  ? 129 LEU   C O     1 
ATOM   7488 C  CB    . LEU   D 1 153 ? 129.138 129.750 135.608 1.00 69.24  ? 129 LEU   C CB    1 
ATOM   7489 C  CG    . LEU   D 1 153 ? 128.463 128.379 135.682 1.00 70.07  ? 129 LEU   C CG    1 
ATOM   7490 C  CD1   . LEU   D 1 153 ? 126.975 128.530 135.947 1.00 69.13  ? 129 LEU   C CD1   1 
ATOM   7491 C  CD2   . LEU   D 1 153 ? 128.702 127.596 134.402 1.00 63.92  ? 129 LEU   C CD2   1 
ATOM   7492 N  N     . LEU   D 1 154 ? 131.592 129.777 137.470 1.00 60.42  ? 130 LEU   C N     1 
ATOM   7493 C  CA    . LEU   D 1 154 ? 132.581 129.067 138.269 1.00 55.13  ? 130 LEU   C CA    1 
ATOM   7494 C  C     . LEU   D 1 154 ? 132.563 129.549 139.709 1.00 54.80  ? 130 LEU   C C     1 
ATOM   7495 O  O     . LEU   D 1 154 ? 132.600 128.728 140.634 1.00 58.32  ? 130 LEU   C O     1 
ATOM   7496 C  CB    . LEU   D 1 154 ? 133.973 129.239 137.663 1.00 59.89  ? 130 LEU   C CB    1 
ATOM   7497 C  CG    . LEU   D 1 154 ? 134.266 128.447 136.388 1.00 63.65  ? 130 LEU   C CG    1 
ATOM   7498 C  CD1   . LEU   D 1 154 ? 135.764 128.313 136.173 1.00 61.29  ? 130 LEU   C CD1   1 
ATOM   7499 C  CD2   . LEU   D 1 154 ? 133.602 127.079 136.427 1.00 58.10  ? 130 LEU   C CD2   1 
ATOM   7500 N  N     . VAL   D 1 155 ? 132.435 130.863 139.914 1.00 56.06  ? 131 VAL   C N     1 
ATOM   7501 C  CA    . VAL   D 1 155 ? 132.440 131.396 141.269 1.00 48.82  ? 131 VAL   C CA    1 
ATOM   7502 C  C     . VAL   D 1 155 ? 131.325 130.760 142.082 1.00 54.39  ? 131 VAL   C C     1 
ATOM   7503 O  O     . VAL   D 1 155 ? 131.552 130.275 143.198 1.00 62.62  ? 131 VAL   C O     1 
ATOM   7504 C  CB    . VAL   D 1 155 ? 132.327 132.930 141.241 1.00 53.32  ? 131 VAL   C CB    1 
ATOM   7505 C  CG1   . VAL   D 1 155 ? 131.857 133.454 142.586 1.00 58.29  ? 131 VAL   C CG1   1 
ATOM   7506 C  CG2   . VAL   D 1 155 ? 133.659 133.549 140.856 1.00 52.52  ? 131 VAL   C CG2   1 
ATOM   7507 N  N     . ILE   D 1 156 ? 130.120 130.688 141.511 1.00 58.84  ? 132 ILE   C N     1 
ATOM   7508 C  CA    . ILE   D 1 156 ? 129.012 130.064 142.227 1.00 58.26  ? 132 ILE   C CA    1 
ATOM   7509 C  C     . ILE   D 1 156 ? 129.335 128.606 142.514 1.00 64.49  ? 132 ILE   C C     1 
ATOM   7510 O  O     . ILE   D 1 156 ? 129.131 128.118 143.634 1.00 66.33  ? 132 ILE   C O     1 
ATOM   7511 C  CB    . ILE   D 1 156 ? 127.705 130.220 141.429 1.00 63.89  ? 132 ILE   C CB    1 
ATOM   7512 C  CG1   . ILE   D 1 156 ? 127.309 131.695 141.354 1.00 64.44  ? 132 ILE   C CG1   1 
ATOM   7513 C  CG2   . ILE   D 1 156 ? 126.593 129.404 142.060 1.00 59.38  ? 132 ILE   C CG2   1 
ATOM   7514 C  CD1   . ILE   D 1 156 ? 126.156 131.976 140.415 1.00 61.79  ? 132 ILE   C CD1   1 
ATOM   7515 N  N     . ILE   D 1 157 ? 129.894 127.904 141.526 1.00 63.86  ? 133 ILE   C N     1 
ATOM   7516 C  CA    . ILE   D 1 157 ? 130.273 126.512 141.731 1.00 57.93  ? 133 ILE   C CA    1 
ATOM   7517 C  C     . ILE   D 1 157 ? 131.348 126.413 142.806 1.00 65.91  ? 133 ILE   C C     1 
ATOM   7518 O  O     . ILE   D 1 157 ? 131.374 125.460 143.593 1.00 67.94  ? 133 ILE   C O     1 
ATOM   7519 C  CB    . ILE   D 1 157 ? 130.723 125.883 140.401 1.00 63.85  ? 133 ILE   C CB    1 
ATOM   7520 C  CG1   . ILE   D 1 157 ? 129.524 125.692 139.473 1.00 64.44  ? 133 ILE   C CG1   1 
ATOM   7521 C  CG2   . ILE   D 1 157 ? 131.404 124.545 140.632 1.00 64.19  ? 133 ILE   C CG2   1 
ATOM   7522 C  CD1   . ILE   D 1 157 ? 129.876 125.095 138.132 1.00 62.55  ? 133 ILE   C CD1   1 
ATOM   7523 N  N     . ALA   D 1 158 ? 132.234 127.411 142.876 1.00 69.19  ? 134 ALA   C N     1 
ATOM   7524 C  CA    . ALA   D 1 158 ? 133.273 127.393 143.896 1.00 61.94  ? 134 ALA   C CA    1 
ATOM   7525 C  C     . ALA   D 1 158 ? 132.731 127.727 145.278 1.00 65.30  ? 134 ALA   C C     1 
ATOM   7526 O  O     . ALA   D 1 158 ? 133.423 127.491 146.273 1.00 71.56  ? 134 ALA   C O     1 
ATOM   7527 C  CB    . ALA   D 1 158 ? 134.393 128.366 143.528 1.00 63.41  ? 134 ALA   C CB    1 
ATOM   7528 N  N     . CYS   D 1 159 ? 131.512 128.266 145.365 1.00 70.13  ? 135 CYS   C N     1 
ATOM   7529 C  CA    . CYS   D 1 159 ? 130.989 128.688 146.659 1.00 68.68  ? 135 CYS   C CA    1 
ATOM   7530 C  C     . CYS   D 1 159 ? 130.332 127.548 147.427 1.00 77.83  ? 135 CYS   C C     1 
ATOM   7531 O  O     . CYS   D 1 159 ? 130.074 127.698 148.626 1.00 77.90  ? 135 CYS   C O     1 
ATOM   7532 C  CB    . CYS   D 1 159 ? 129.994 129.834 146.474 1.00 72.35  ? 135 CYS   C CB    1 
ATOM   7533 S  SG    . CYS   D 1 159 ? 130.733 131.483 146.555 1.00 75.31  ? 135 CYS   C SG    1 
ATOM   7534 N  N     . MET   D 1 160 ? 130.055 126.419 146.774 1.00 93.86  ? 136 MET   C N     1 
ATOM   7535 C  CA    . MET   D 1 160 ? 129.376 125.312 147.436 1.00 88.52  ? 136 MET   C CA    1 
ATOM   7536 C  C     . MET   D 1 160 ? 130.292 124.496 148.338 1.00 93.84  ? 136 MET   C C     1 
ATOM   7537 O  O     . MET   D 1 160 ? 129.791 123.760 149.194 1.00 91.86  ? 136 MET   C O     1 
ATOM   7538 C  CB    . MET   D 1 160 ? 128.735 124.389 146.398 1.00 86.16  ? 136 MET   C CB    1 
ATOM   7539 C  CG    . MET   D 1 160 ? 128.481 125.042 145.053 1.00 91.87  ? 136 MET   C CG    1 
ATOM   7540 S  SD    . MET   D 1 160 ? 127.488 124.003 143.966 1.00 104.02 ? 136 MET   C SD    1 
ATOM   7541 C  CE    . MET   D 1 160 ? 125.977 123.875 144.918 1.00 96.68  ? 136 MET   C CE    1 
ATOM   7542 N  N     . PHE   D 1 161 ? 131.611 124.605 148.173 1.00 101.10 ? 137 PHE   C N     1 
ATOM   7543 C  CA    . PHE   D 1 161 ? 132.528 123.810 148.982 1.00 97.35  ? 137 PHE   C CA    1 
ATOM   7544 C  C     . PHE   D 1 161 ? 132.608 124.302 150.421 1.00 95.25  ? 137 PHE   C C     1 
ATOM   7545 O  O     . PHE   D 1 161 ? 132.917 123.509 151.316 1.00 97.72  ? 137 PHE   C O     1 
ATOM   7546 C  CB    . PHE   D 1 161 ? 133.918 123.807 148.347 1.00 94.70  ? 137 PHE   C CB    1 
ATOM   7547 C  CG    . PHE   D 1 161 ? 133.984 123.066 147.042 1.00 96.10  ? 137 PHE   C CG    1 
ATOM   7548 C  CD1   . PHE   D 1 161 ? 133.028 122.116 146.720 1.00 97.23  ? 137 PHE   C CD1   1 
ATOM   7549 C  CD2   . PHE   D 1 161 ? 134.999 123.319 146.136 1.00 98.52  ? 137 PHE   C CD2   1 
ATOM   7550 C  CE1   . PHE   D 1 161 ? 133.083 121.432 145.522 1.00 96.70  ? 137 PHE   C CE1   1 
ATOM   7551 C  CE2   . PHE   D 1 161 ? 135.060 122.637 144.935 1.00 100.07 ? 137 PHE   C CE2   1 
ATOM   7552 C  CZ    . PHE   D 1 161 ? 134.100 121.693 144.628 1.00 98.79  ? 137 PHE   C CZ    1 
ATOM   7553 N  N     . THR   D 1 162 ? 132.344 125.586 150.661 1.00 93.09  ? 138 THR   C N     1 
ATOM   7554 C  CA    . THR   D 1 162 ? 132.323 126.099 152.026 1.00 96.78  ? 138 THR   C CA    1 
ATOM   7555 C  C     . THR   D 1 162 ? 131.043 125.707 152.750 1.00 102.28 ? 138 THR   C C     1 
ATOM   7556 O  O     . THR   D 1 162 ? 131.051 125.502 153.969 1.00 104.35 ? 138 THR   C O     1 
ATOM   7557 C  CB    . THR   D 1 162 ? 132.473 127.618 152.020 1.00 97.54  ? 138 THR   C CB    1 
ATOM   7558 O  OG1   . THR   D 1 162 ? 133.330 128.004 150.941 1.00 97.18  ? 138 THR   C OG1   1 
ATOM   7559 C  CG2   . THR   D 1 162 ? 133.073 128.098 153.332 1.00 96.28  ? 138 THR   C CG2   1 
ATOM   7560 N  N     . GLY   D 1 163 ? 129.938 125.602 152.018 1.00 86.01  ? 139 GLY   C N     1 
ATOM   7561 C  CA    . GLY   D 1 163 ? 128.650 125.317 152.614 1.00 81.54  ? 139 GLY   C CA    1 
ATOM   7562 C  C     . GLY   D 1 163 ? 127.596 126.308 152.169 1.00 83.87  ? 139 GLY   C C     1 
ATOM   7563 O  O     . GLY   D 1 163 ? 126.454 126.266 152.634 1.00 87.95  ? 139 GLY   C O     1 
ATOM   7564 N  N     . ILE   D 1 164 ? 127.971 127.204 151.261 1.00 75.28  ? 140 ILE   C N     1 
ATOM   7565 C  CA    . ILE   D 1 164 ? 127.061 128.214 150.734 1.00 73.70  ? 140 ILE   C CA    1 
ATOM   7566 C  C     . ILE   D 1 164 ? 126.394 127.636 149.492 1.00 74.65  ? 140 ILE   C C     1 
ATOM   7567 O  O     . ILE   D 1 164 ? 127.042 127.436 148.462 1.00 72.00  ? 140 ILE   C O     1 
ATOM   7568 C  CB    . ILE   D 1 164 ? 127.793 129.522 150.415 1.00 74.08  ? 140 ILE   C CB    1 
ATOM   7569 C  CG1   . ILE   D 1 164 ? 129.095 129.613 151.216 1.00 75.54  ? 140 ILE   C CG1   1 
ATOM   7570 C  CG2   . ILE   D 1 164 ? 126.891 130.716 150.696 1.00 70.86  ? 140 ILE   C CG2   1 
ATOM   7571 C  CD1   . ILE   D 1 164 ? 129.582 131.027 151.455 1.00 73.45  ? 140 ILE   C CD1   1 
ATOM   7572 N  N     . TYR   D 1 165 ? 125.093 127.374 149.585 1.00 82.03  ? 141 TYR   C N     1 
ATOM   7573 C  CA    . TYR   D 1 165 ? 124.331 126.792 148.495 1.00 82.33  ? 141 TYR   C CA    1 
ATOM   7574 C  C     . TYR   D 1 165 ? 123.363 127.817 147.912 1.00 78.46  ? 141 TYR   C C     1 
ATOM   7575 O  O     . TYR   D 1 165 ? 122.913 128.723 148.619 1.00 77.55  ? 141 TYR   C O     1 
ATOM   7576 C  CB    . TYR   D 1 165 ? 123.547 125.563 148.972 1.00 83.45  ? 141 TYR   C CB    1 
ATOM   7577 C  CG    . TYR   D 1 165 ? 124.426 124.432 149.451 1.00 81.66  ? 141 TYR   C CG    1 
ATOM   7578 C  CD1   . TYR   D 1 165 ? 125.106 123.626 148.550 1.00 80.43  ? 141 TYR   C CD1   1 
ATOM   7579 C  CD2   . TYR   D 1 165 ? 124.578 124.174 150.805 1.00 79.25  ? 141 TYR   C CD2   1 
ATOM   7580 C  CE1   . TYR   D 1 165 ? 125.912 122.593 148.983 1.00 80.02  ? 141 TYR   C CE1   1 
ATOM   7581 C  CE2   . TYR   D 1 165 ? 125.381 123.143 151.249 1.00 81.49  ? 141 TYR   C CE2   1 
ATOM   7582 C  CZ    . TYR   D 1 165 ? 126.046 122.357 150.334 1.00 83.81  ? 141 TYR   C CZ    1 
ATOM   7583 O  OH    . TYR   D 1 165 ? 126.847 121.328 150.772 1.00 86.78  ? 141 TYR   C OH    1 
ATOM   7584 N  N     . PRO   D 1 166 ? 123.032 127.705 146.625 1.00 79.25  ? 142 PRO   C N     1 
ATOM   7585 C  CA    . PRO   D 1 166 ? 122.131 128.687 146.009 1.00 77.85  ? 142 PRO   C CA    1 
ATOM   7586 C  C     . PRO   D 1 166 ? 120.771 128.711 146.693 1.00 81.96  ? 142 PRO   C C     1 
ATOM   7587 O  O     . PRO   D 1 166 ? 120.239 127.679 147.103 1.00 85.28  ? 142 PRO   C O     1 
ATOM   7588 C  CB    . PRO   D 1 166 ? 122.022 128.206 144.558 1.00 76.12  ? 142 PRO   C CB    1 
ATOM   7589 C  CG    . PRO   D 1 166 ? 123.275 127.436 144.327 1.00 79.56  ? 142 PRO   C CG    1 
ATOM   7590 C  CD    . PRO   D 1 166 ? 123.578 126.763 145.633 1.00 80.21  ? 142 PRO   C CD    1 
ATOM   7591 N  N     . SER   D 1 167 ? 120.214 129.915 146.811 1.00 70.81  ? 143 SER   C N     1 
ATOM   7592 C  CA    . SER   D 1 167 ? 118.927 130.117 147.464 1.00 65.98  ? 143 SER   C CA    1 
ATOM   7593 C  C     . SER   D 1 167 ? 117.976 130.848 146.527 1.00 69.88  ? 143 SER   C C     1 
ATOM   7594 O  O     . SER   D 1 167 ? 118.294 131.053 145.352 1.00 75.27  ? 143 SER   C O     1 
ATOM   7595 C  CB    . SER   D 1 167 ? 119.107 130.898 148.766 1.00 63.77  ? 143 SER   C CB    1 
ATOM   7596 O  OG    . SER   D 1 167 ? 117.952 130.806 149.580 1.00 74.83  ? 143 SER   C OG    1 
ATOM   7597 N  N     . ILE   D 1 168 ? 116.802 131.237 147.030 1.00 47.21  ? 144 ILE   C N     1 
ATOM   7598 C  CA    . ILE   D 1 168 ? 115.885 132.032 146.224 1.00 37.19  ? 144 ILE   C CA    1 
ATOM   7599 C  C     . ILE   D 1 168 ? 116.454 133.416 145.936 1.00 43.43  ? 144 ILE   C C     1 
ATOM   7600 O  O     . ILE   D 1 168 ? 116.260 133.949 144.836 1.00 45.30  ? 144 ILE   C O     1 
ATOM   7601 C  CB    . ILE   D 1 168 ? 114.501 132.111 146.907 1.00 38.74  ? 144 ILE   C CB    1 
ATOM   7602 C  CG1   . ILE   D 1 168 ? 113.456 132.671 145.942 1.00 42.81  ? 144 ILE   C CG1   1 
ATOM   7603 C  CG2   . ILE   D 1 168 ? 114.557 132.918 148.197 1.00 44.30  ? 144 ILE   C CG2   1 
ATOM   7604 C  CD1   . ILE   D 1 168 ? 112.988 131.674 144.908 1.00 48.29  ? 144 ILE   C CD1   1 
ATOM   7605 N  N     . HIS   D 1 169 ? 117.195 133.996 146.880 1.00 40.16  ? 145 HIS   C N     1 
ATOM   7606 C  CA    . HIS   D 1 169 ? 117.756 135.331 146.729 1.00 36.53  ? 145 HIS   C CA    1 
ATOM   7607 C  C     . HIS   D 1 169 ? 118.719 135.450 145.556 1.00 33.10  ? 145 HIS   C C     1 
ATOM   7608 O  O     . HIS   D 1 169 ? 119.175 136.560 145.265 1.00 50.15  ? 145 HIS   C O     1 
ATOM   7609 C  CB    . HIS   D 1 169 ? 118.466 135.748 148.019 1.00 30.71  ? 145 HIS   C CB    1 
ATOM   7610 C  CG    . HIS   D 1 169 ? 117.617 135.615 149.244 1.00 34.49  ? 145 HIS   C CG    1 
ATOM   7611 N  ND1   . HIS   D 1 169 ? 117.525 134.443 149.963 1.00 42.72  ? 145 HIS   C ND1   1 
ATOM   7612 C  CD2   . HIS   D 1 169 ? 116.814 136.505 149.873 1.00 36.70  ? 145 HIS   C CD2   1 
ATOM   7613 C  CE1   . HIS   D 1 169 ? 116.708 134.619 150.986 1.00 48.16  ? 145 HIS   C CE1   1 
ATOM   7614 N  NE2   . HIS   D 1 169 ? 116.263 135.862 150.953 1.00 38.91  ? 145 HIS   C NE2   1 
ATOM   7615 N  N     . ILE   D 1 170 ? 119.044 134.346 144.880 1.00 27.88  ? 146 ILE   C N     1 
ATOM   7616 C  CA    . ILE   D 1 170 ? 119.884 134.421 143.688 1.00 40.22  ? 146 ILE   C CA    1 
ATOM   7617 C  C     . ILE   D 1 170 ? 119.127 134.923 142.470 1.00 47.07  ? 146 ILE   C C     1 
ATOM   7618 O  O     . ILE   D 1 170 ? 119.761 135.363 141.501 1.00 50.29  ? 146 ILE   C O     1 
ATOM   7619 C  CB    . ILE   D 1 170 ? 120.521 133.051 143.380 1.00 38.22  ? 146 ILE   C CB    1 
ATOM   7620 C  CG1   . ILE   D 1 170 ? 121.830 133.231 142.608 1.00 32.13  ? 146 ILE   C CG1   1 
ATOM   7621 C  CG2   . ILE   D 1 170 ? 119.562 132.168 142.602 1.00 34.87  ? 146 ILE   C CG2   1 
ATOM   7622 C  CD1   . ILE   D 1 170 ? 122.853 132.158 142.879 1.00 36.35  ? 146 ILE   C CD1   1 
ATOM   7623 N  N     . ILE   D 1 171 ? 117.792 134.906 142.496 1.00 40.81  ? 147 ILE   C N     1 
ATOM   7624 C  CA    . ILE   D 1 171 ? 117.013 135.349 141.342 1.00 43.84  ? 147 ILE   C CA    1 
ATOM   7625 C  C     . ILE   D 1 171 ? 117.267 136.831 141.098 1.00 44.20  ? 147 ILE   C C     1 
ATOM   7626 O  O     . ILE   D 1 171 ? 117.073 137.330 139.984 1.00 53.17  ? 147 ILE   C O     1 
ATOM   7627 C  CB    . ILE   D 1 171 ? 115.510 135.065 141.520 1.00 41.96  ? 147 ILE   C CB    1 
ATOM   7628 C  CG1   . ILE   D 1 171 ? 114.925 135.903 142.657 1.00 39.54  ? 147 ILE   C CG1   1 
ATOM   7629 C  CG2   . ILE   D 1 171 ? 115.270 133.583 141.756 1.00 46.16  ? 147 ILE   C CG2   1 
ATOM   7630 C  CD1   . ILE   D 1 171 ? 113.426 135.778 142.788 1.00 43.95  ? 147 ILE   C CD1   1 
ATOM   7631 N  N     . GLN   D 1 172 ? 117.730 137.535 142.135 1.00 40.05  ? 148 GLN   C N     1 
ATOM   7632 C  CA    . GLN   D 1 172 ? 118.085 138.941 141.995 1.00 33.48  ? 148 GLN   C CA    1 
ATOM   7633 C  C     . GLN   D 1 172 ? 119.138 139.167 140.923 1.00 35.67  ? 148 GLN   C C     1 
ATOM   7634 O  O     . GLN   D 1 172 ? 119.210 140.269 140.371 1.00 36.95  ? 148 GLN   C O     1 
ATOM   7635 C  CB    . GLN   D 1 172 ? 118.593 139.495 143.324 1.00 33.11  ? 148 GLN   C CB    1 
ATOM   7636 C  CG    . GLN   D 1 172 ? 117.638 139.324 144.481 1.00 34.77  ? 148 GLN   C CG    1 
ATOM   7637 C  CD    . GLN   D 1 172 ? 118.162 139.950 145.751 1.00 39.95  ? 148 GLN   C CD    1 
ATOM   7638 O  OE1   . GLN   D 1 172 ? 117.995 141.145 145.980 1.00 45.61  ? 148 GLN   C OE1   1 
ATOM   7639 N  NE2   . GLN   D 1 172 ? 118.809 139.145 146.584 1.00 43.76  ? 148 GLN   C NE2   1 
ATOM   7640 N  N     . LEU   D 1 173 ? 119.953 138.153 140.619 1.00 34.76  ? 149 LEU   C N     1 
ATOM   7641 C  CA    . LEU   D 1 173 ? 120.942 138.300 139.558 1.00 36.19  ? 149 LEU   C CA    1 
ATOM   7642 C  C     . LEU   D 1 173 ? 120.291 138.682 138.237 1.00 38.99  ? 149 LEU   C C     1 
ATOM   7643 O  O     . LEU   D 1 173 ? 120.898 139.404 137.437 1.00 51.09  ? 149 LEU   C O     1 
ATOM   7644 C  CB    . LEU   D 1 173 ? 121.747 137.011 139.403 1.00 38.56  ? 149 LEU   C CB    1 
ATOM   7645 C  CG    . LEU   D 1 173 ? 122.833 136.768 140.452 1.00 39.52  ? 149 LEU   C CG    1 
ATOM   7646 C  CD1   . LEU   D 1 173 ? 123.616 135.509 140.125 1.00 41.69  ? 149 LEU   C CD1   1 
ATOM   7647 C  CD2   . LEU   D 1 173 ? 123.760 137.966 140.559 1.00 34.77  ? 149 LEU   C CD2   1 
ATOM   7648 N  N     . LEU   D 1 174 ? 119.046 138.249 138.010 1.00 39.71  ? 150 LEU   C N     1 
ATOM   7649 C  CA    . LEU   D 1 174 ? 118.347 138.590 136.776 1.00 40.56  ? 150 LEU   C CA    1 
ATOM   7650 C  C     . LEU   D 1 174 ? 118.198 140.093 136.592 1.00 46.75  ? 150 LEU   C C     1 
ATOM   7651 O  O     . LEU   D 1 174 ? 117.994 140.551 135.462 1.00 52.89  ? 150 LEU   C O     1 
ATOM   7652 C  CB    . LEU   D 1 174 ? 116.968 137.927 136.747 1.00 40.51  ? 150 LEU   C CB    1 
ATOM   7653 C  CG    . LEU   D 1 174 ? 116.927 136.399 136.695 1.00 48.00  ? 150 LEU   C CG    1 
ATOM   7654 C  CD1   . LEU   D 1 174 ? 115.508 135.892 136.881 1.00 40.27  ? 150 LEU   C CD1   1 
ATOM   7655 C  CD2   . LEU   D 1 174 ? 117.507 135.898 135.387 1.00 49.05  ? 150 LEU   C CD2   1 
ATOM   7656 N  N     . ILE   D 1 175 ? 118.295 140.871 137.669 1.00 41.85  ? 151 ILE   C N     1 
ATOM   7657 C  CA    . ILE   D 1 175 ? 118.197 142.322 137.586 1.00 34.04  ? 151 ILE   C CA    1 
ATOM   7658 C  C     . ILE   D 1 175 ? 119.599 142.918 137.625 1.00 40.10  ? 151 ILE   C C     1 
ATOM   7659 O  O     . ILE   D 1 175 ? 119.848 143.989 137.062 1.00 44.23  ? 151 ILE   C O     1 
ATOM   7660 C  CB    . ILE   D 1 175 ? 117.322 142.880 138.725 1.00 44.37  ? 151 ILE   C CB    1 
ATOM   7661 C  CG1   . ILE   D 1 175 ? 115.898 142.337 138.617 1.00 49.48  ? 151 ILE   C CG1   1 
ATOM   7662 C  CG2   . ILE   D 1 175 ? 117.288 144.400 138.696 1.00 41.34  ? 151 ILE   C CG2   1 
ATOM   7663 C  CD1   . ILE   D 1 175 ? 115.484 141.494 139.803 1.00 48.16  ? 151 ILE   C CD1   1 
ATOM   7664 N  N     . TYR   D 1 176 ? 120.535 142.214 138.264 1.00 44.01  ? 152 TYR   C N     1 
ATOM   7665 C  CA    . TYR   D 1 176 ? 121.825 142.816 138.578 1.00 38.31  ? 152 TYR   C CA    1 
ATOM   7666 C  C     . TYR   D 1 176 ? 122.883 142.548 137.516 1.00 36.51  ? 152 TYR   C C     1 
ATOM   7667 O  O     . TYR   D 1 176 ? 123.688 143.434 137.214 1.00 50.47  ? 152 TYR   C O     1 
ATOM   7668 C  CB    . TYR   D 1 176 ? 122.319 142.319 139.940 1.00 35.20  ? 152 TYR   C CB    1 
ATOM   7669 C  CG    . TYR   D 1 176 ? 121.459 142.778 141.094 1.00 37.46  ? 152 TYR   C CG    1 
ATOM   7670 C  CD1   . TYR   D 1 176 ? 120.694 143.932 140.996 1.00 33.38  ? 152 TYR   C CD1   1 
ATOM   7671 C  CD2   . TYR   D 1 176 ? 121.404 142.056 142.276 1.00 39.82  ? 152 TYR   C CD2   1 
ATOM   7672 C  CE1   . TYR   D 1 176 ? 119.903 144.354 142.043 1.00 34.80  ? 152 TYR   C CE1   1 
ATOM   7673 C  CE2   . TYR   D 1 176 ? 120.615 142.472 143.330 1.00 43.50  ? 152 TYR   C CE2   1 
ATOM   7674 C  CZ    . TYR   D 1 176 ? 119.867 143.621 143.206 1.00 41.87  ? 152 TYR   C CZ    1 
ATOM   7675 O  OH    . TYR   D 1 176 ? 119.080 144.039 144.250 1.00 35.38  ? 152 TYR   C OH    1 
ATOM   7676 N  N     . VAL   D 1 177 ? 122.913 141.344 136.957 1.00 37.06  ? 153 VAL   C N     1 
ATOM   7677 C  CA    . VAL   D 1 177 ? 123.878 141.007 135.911 1.00 36.62  ? 153 VAL   C CA    1 
ATOM   7678 C  C     . VAL   D 1 177 ? 123.642 141.862 134.667 1.00 45.29  ? 153 VAL   C C     1 
ATOM   7679 O  O     . VAL   D 1 177 ? 124.613 142.403 134.119 1.00 48.59  ? 153 VAL   C O     1 
ATOM   7680 C  CB    . VAL   D 1 177 ? 123.844 139.506 135.580 1.00 38.19  ? 153 VAL   C CB    1 
ATOM   7681 C  CG1   . VAL   D 1 177 ? 124.831 139.187 134.472 1.00 41.05  ? 153 VAL   C CG1   1 
ATOM   7682 C  CG2   . VAL   D 1 177 ? 124.153 138.686 136.821 1.00 32.22  ? 153 VAL   C CG2   1 
ATOM   7683 N  N     . PRO   D 1 178 ? 122.405 142.015 134.167 1.00 46.82  ? 154 PRO   C N     1 
ATOM   7684 C  CA    . PRO   D 1 178 ? 122.201 142.916 133.021 1.00 40.34  ? 154 PRO   C CA    1 
ATOM   7685 C  C     . PRO   D 1 178 ? 122.600 144.358 133.287 1.00 43.56  ? 154 PRO   C C     1 
ATOM   7686 O  O     . PRO   D 1 178 ? 123.221 144.975 132.412 1.00 51.60  ? 154 PRO   C O     1 
ATOM   7687 C  CB    . PRO   D 1 178 ? 120.696 142.801 132.751 1.00 42.12  ? 154 PRO   C CB    1 
ATOM   7688 C  CG    . PRO   D 1 178 ? 120.347 141.457 133.245 1.00 40.11  ? 154 PRO   C CG    1 
ATOM   7689 C  CD    . PRO   D 1 178 ? 121.153 141.308 134.496 1.00 42.78  ? 154 PRO   C CD    1 
ATOM   7690 N  N     . PHE   D 1 179 ? 122.293 144.901 134.470 1.00 51.71  ? 155 PHE   C N     1 
ATOM   7691 C  CA    . PHE   D 1 179 ? 122.541 146.316 134.732 1.00 49.79  ? 155 PHE   C CA    1 
ATOM   7692 C  C     . PHE   D 1 179 ? 124.005 146.673 134.524 1.00 53.99  ? 155 PHE   C C     1 
ATOM   7693 O  O     . PHE   D 1 179 ? 124.316 147.669 133.858 1.00 58.90  ? 155 PHE   C O     1 
ATOM   7694 C  CB    . PHE   D 1 179 ? 122.105 146.675 136.152 1.00 51.77  ? 155 PHE   C CB    1 
ATOM   7695 C  CG    . PHE   D 1 179 ? 122.686 147.968 136.655 1.00 57.69  ? 155 PHE   C CG    1 
ATOM   7696 C  CD1   . PHE   D 1 179 ? 122.178 149.183 136.229 1.00 56.96  ? 155 PHE   C CD1   1 
ATOM   7697 C  CD2   . PHE   D 1 179 ? 123.744 147.968 137.548 1.00 59.44  ? 155 PHE   C CD2   1 
ATOM   7698 C  CE1   . PHE   D 1 179 ? 122.712 150.372 136.687 1.00 59.26  ? 155 PHE   C CE1   1 
ATOM   7699 C  CE2   . PHE   D 1 179 ? 124.283 149.154 138.009 1.00 58.43  ? 155 PHE   C CE2   1 
ATOM   7700 C  CZ    . PHE   D 1 179 ? 123.766 150.357 137.577 1.00 59.40  ? 155 PHE   C CZ    1 
ATOM   7701 N  N     . CYS   D 1 180 ? 124.913 145.865 135.075 1.00 49.58  ? 156 CYS   C N     1 
ATOM   7702 C  CA    . CYS   D 1 180 ? 126.338 146.091 134.861 1.00 50.47  ? 156 CYS   C CA    1 
ATOM   7703 C  C     . CYS   D 1 180 ? 126.652 146.227 133.378 1.00 62.04  ? 156 CYS   C C     1 
ATOM   7704 O  O     . CYS   D 1 180 ? 127.319 147.184 132.966 1.00 65.96  ? 156 CYS   C O     1 
ATOM   7705 C  CB    . CYS   D 1 180 ? 127.144 144.953 135.488 1.00 52.37  ? 156 CYS   C CB    1 
ATOM   7706 S  SG    . CYS   D 1 180 ? 128.851 144.828 134.918 1.00 74.35  ? 156 CYS   C SG    1 
ATOM   7707 N  N     . PHE   D 1 181 ? 126.140 145.303 132.558 1.00 54.91  ? 157 PHE   C N     1 
ATOM   7708 C  CA    . PHE   D 1 181 ? 126.308 145.425 131.114 1.00 40.69  ? 157 PHE   C CA    1 
ATOM   7709 C  C     . PHE   D 1 181 ? 125.794 146.770 130.623 1.00 50.49  ? 157 PHE   C C     1 
ATOM   7710 O  O     . PHE   D 1 181 ? 126.531 147.528 129.980 1.00 60.24  ? 157 PHE   C O     1 
ATOM   7711 C  CB    . PHE   D 1 181 ? 125.582 144.279 130.408 1.00 42.45  ? 157 PHE   C CB    1 
ATOM   7712 C  CG    . PHE   D 1 181 ? 125.663 144.338 128.909 1.00 55.16  ? 157 PHE   C CG    1 
ATOM   7713 C  CD1   . PHE   D 1 181 ? 126.813 143.945 128.249 1.00 56.74  ? 157 PHE   C CD1   1 
ATOM   7714 C  CD2   . PHE   D 1 181 ? 124.587 144.785 128.161 1.00 55.50  ? 157 PHE   C CD2   1 
ATOM   7715 C  CE1   . PHE   D 1 181 ? 126.890 143.997 126.872 1.00 49.60  ? 157 PHE   C CE1   1 
ATOM   7716 C  CE2   . PHE   D 1 181 ? 124.660 144.840 126.784 1.00 53.00  ? 157 PHE   C CE2   1 
ATOM   7717 C  CZ    . PHE   D 1 181 ? 125.813 144.445 126.139 1.00 51.66  ? 157 PHE   C CZ    1 
ATOM   7718 N  N     . PHE   D 1 182 ? 124.552 147.111 130.979 1.00 49.70  ? 158 PHE   C N     1 
ATOM   7719 C  CA    . PHE   D 1 182 ? 123.962 148.361 130.514 1.00 39.76  ? 158 PHE   C CA    1 
ATOM   7720 C  C     . PHE   D 1 182 ? 124.743 149.562 131.024 1.00 42.05  ? 158 PHE   C C     1 
ATOM   7721 O  O     . PHE   D 1 182 ? 124.630 150.661 130.471 1.00 58.24  ? 158 PHE   C O     1 
ATOM   7722 C  CB    . PHE   D 1 182 ? 122.498 148.445 130.941 1.00 43.87  ? 158 PHE   C CB    1 
ATOM   7723 C  CG    . PHE   D 1 182 ? 121.579 147.600 130.109 1.00 52.42  ? 158 PHE   C CG    1 
ATOM   7724 C  CD1   . PHE   D 1 182 ? 121.784 147.472 128.746 1.00 50.12  ? 158 PHE   C CD1   1 
ATOM   7725 C  CD2   . PHE   D 1 182 ? 120.517 146.930 130.687 1.00 52.37  ? 158 PHE   C CD2   1 
ATOM   7726 C  CE1   . PHE   D 1 182 ? 120.944 146.695 127.976 1.00 49.71  ? 158 PHE   C CE1   1 
ATOM   7727 C  CE2   . PHE   D 1 182 ? 119.674 146.150 129.921 1.00 50.38  ? 158 PHE   C CE2   1 
ATOM   7728 C  CZ    . PHE   D 1 182 ? 119.887 146.033 128.564 1.00 50.76  ? 158 PHE   C CZ    1 
ATOM   7729 N  N     . LEU   D 1 183 ? 125.539 149.376 132.077 1.00 49.23  ? 159 LEU   C N     1 
ATOM   7730 C  CA    . LEU   D 1 183 ? 126.433 150.447 132.493 1.00 53.92  ? 159 LEU   C CA    1 
ATOM   7731 C  C     . LEU   D 1 183 ? 127.602 150.579 131.527 1.00 57.86  ? 159 LEU   C C     1 
ATOM   7732 O  O     . LEU   D 1 183 ? 127.815 151.651 130.946 1.00 58.45  ? 159 LEU   C O     1 
ATOM   7733 C  CB    . LEU   D 1 183 ? 126.929 150.197 133.917 1.00 55.96  ? 159 LEU   C CB    1 
ATOM   7734 C  CG    . LEU   D 1 183 ? 128.020 151.136 134.432 1.00 57.94  ? 159 LEU   C CG    1 
ATOM   7735 C  CD1   . LEU   D 1 183 ? 127.411 152.430 134.946 1.00 53.31  ? 159 LEU   C CD1   1 
ATOM   7736 C  CD2   . LEU   D 1 183 ? 128.840 150.461 135.518 1.00 55.28  ? 159 LEU   C CD2   1 
ATOM   7737 N  N     . THR   D 1 184 ? 128.334 149.482 131.301 1.00 56.23  ? 160 THR   C N     1 
ATOM   7738 C  CA    . THR   D 1 184 ? 129.577 149.562 130.538 1.00 49.80  ? 160 THR   C CA    1 
ATOM   7739 C  C     . THR   D 1 184 ? 129.337 150.120 129.144 1.00 52.52  ? 160 THR   C C     1 
ATOM   7740 O  O     . THR   D 1 184 ? 129.988 151.091 128.739 1.00 54.49  ? 160 THR   C O     1 
ATOM   7741 C  CB    . THR   D 1 184 ? 130.233 148.183 130.457 1.00 50.46  ? 160 THR   C CB    1 
ATOM   7742 O  OG1   . THR   D 1 184 ? 130.119 147.522 131.723 1.00 47.43  ? 160 THR   C OG1   1 
ATOM   7743 C  CG2   . THR   D 1 184 ? 131.699 148.312 130.089 1.00 52.99  ? 160 THR   C CG2   1 
ATOM   7744 N  N     . ALA   D 1 185 ? 128.374 149.549 128.416 1.00 60.56  ? 161 ALA   C N     1 
ATOM   7745 C  CA    . ALA   D 1 185 ? 128.043 150.066 127.093 1.00 60.62  ? 161 ALA   C CA    1 
ATOM   7746 C  C     . ALA   D 1 185 ? 127.695 151.547 127.156 1.00 63.19  ? 161 ALA   C C     1 
ATOM   7747 O  O     . ALA   D 1 185 ? 128.186 152.337 126.341 1.00 70.15  ? 161 ALA   C O     1 
ATOM   7748 C  CB    . ALA   D 1 185 ? 126.889 149.265 126.491 1.00 56.41  ? 161 ALA   C CB    1 
ATOM   7749 N  N     . SER   D 1 186 ? 126.890 151.947 128.148 1.00 55.42  ? 162 SER   C N     1 
ATOM   7750 C  CA    . SER   D 1 186 ? 126.484 153.344 128.247 1.00 54.64  ? 162 SER   C CA    1 
ATOM   7751 C  C     . SER   D 1 186 ? 127.692 154.261 128.371 1.00 61.44  ? 162 SER   C C     1 
ATOM   7752 O  O     . SER   D 1 186 ? 127.656 155.408 127.912 1.00 62.00  ? 162 SER   C O     1 
ATOM   7753 C  CB    . SER   D 1 186 ? 125.541 153.537 129.433 1.00 55.10  ? 162 SER   C CB    1 
ATOM   7754 O  OG    . SER   D 1 186 ? 124.319 152.854 129.225 1.00 64.49  ? 162 SER   C OG    1 
ATOM   7755 N  N     . VAL   D 1 187 ? 128.772 153.775 128.985 1.00 65.36  ? 163 VAL   C N     1 
ATOM   7756 C  CA    . VAL   D 1 187 ? 129.988 154.576 129.038 1.00 55.99  ? 163 VAL   C CA    1 
ATOM   7757 C  C     . VAL   D 1 187 ? 130.660 154.607 127.672 1.00 55.99  ? 163 VAL   C C     1 
ATOM   7758 O  O     . VAL   D 1 187 ? 130.980 155.682 127.148 1.00 67.20  ? 163 VAL   C O     1 
ATOM   7759 C  CB    . VAL   D 1 187 ? 130.935 154.046 130.128 1.00 58.45  ? 163 VAL   C CB    1 
ATOM   7760 C  CG1   . VAL   D 1 187 ? 132.310 154.672 129.984 1.00 58.59  ? 163 VAL   C CG1   1 
ATOM   7761 C  CG2   . VAL   D 1 187 ? 130.361 154.326 131.505 1.00 57.97  ? 163 VAL   C CG2   1 
ATOM   7762 N  N     . THR   D 1 188 ? 130.839 153.435 127.051 1.00 59.58  ? 164 THR   C N     1 
ATOM   7763 C  CA    . THR   D 1 188 ? 131.641 153.360 125.834 1.00 56.13  ? 164 THR   C CA    1 
ATOM   7764 C  C     . THR   D 1 188 ? 131.039 154.194 124.714 1.00 62.94  ? 164 THR   C C     1 
ATOM   7765 O  O     . THR   D 1 188 ? 131.765 154.934 124.039 1.00 68.64  ? 164 THR   C O     1 
ATOM   7766 C  CB    . THR   D 1 188 ? 131.795 151.909 125.384 1.00 56.49  ? 164 THR   C CB    1 
ATOM   7767 O  OG1   . THR   D 1 188 ? 130.505 151.291 125.312 1.00 64.96  ? 164 THR   C OG1   1 
ATOM   7768 C  CG2   . THR   D 1 188 ? 132.662 151.141 126.365 1.00 61.58  ? 164 THR   C CG2   1 
ATOM   7769 N  N     . LEU   D 1 189 ? 129.714 154.127 124.544 1.00 65.47  ? 165 LEU   C N     1 
ATOM   7770 C  CA    . LEU   D 1 189 ? 129.051 154.894 123.494 1.00 69.49  ? 165 LEU   C CA    1 
ATOM   7771 C  C     . LEU   D 1 189 ? 129.409 156.370 123.584 1.00 70.20  ? 165 LEU   C C     1 
ATOM   7772 O  O     . LEU   D 1 189 ? 129.476 157.064 122.564 1.00 70.74  ? 165 LEU   C O     1 
ATOM   7773 C  CB    . LEU   D 1 189 ? 127.538 154.701 123.586 1.00 70.90  ? 165 LEU   C CB    1 
ATOM   7774 C  CG    . LEU   D 1 189 ? 126.679 155.435 122.553 1.00 71.08  ? 165 LEU   C CG    1 
ATOM   7775 C  CD1   . LEU   D 1 189 ? 126.843 154.811 121.179 1.00 67.39  ? 165 LEU   C CD1   1 
ATOM   7776 C  CD2   . LEU   D 1 189 ? 125.218 155.441 122.973 1.00 68.94  ? 165 LEU   C CD2   1 
ATOM   7777 N  N     . LEU   D 1 190 ? 129.652 156.867 124.798 1.00 69.12  ? 166 LEU   C N     1 
ATOM   7778 C  CA    . LEU   D 1 190 ? 130.153 158.229 124.929 1.00 67.37  ? 166 LEU   C CA    1 
ATOM   7779 C  C     . LEU   D 1 190 ? 131.648 158.288 124.645 1.00 70.24  ? 166 LEU   C C     1 
ATOM   7780 O  O     . LEU   D 1 190 ? 132.087 159.017 123.744 1.00 74.18  ? 166 LEU   C O     1 
ATOM   7781 C  CB    . LEU   D 1 190 ? 129.841 158.769 126.323 1.00 65.61  ? 166 LEU   C CB    1 
ATOM   7782 C  CG    . LEU   D 1 190 ? 130.315 160.187 126.645 1.00 72.50  ? 166 LEU   C CG    1 
ATOM   7783 C  CD1   . LEU   D 1 190 ? 129.809 161.171 125.606 1.00 77.59  ? 166 LEU   C CD1   1 
ATOM   7784 C  CD2   . LEU   D 1 190 ? 129.858 160.595 128.034 1.00 68.87  ? 166 LEU   C CD2   1 
ATOM   7785 N  N     . THR   D 1 191 ? 132.442 157.490 125.367 1.00 68.05  ? 167 THR   C N     1 
ATOM   7786 C  CA    . THR   D 1 191 ? 133.892 157.646 125.327 1.00 60.31  ? 167 THR   C CA    1 
ATOM   7787 C  C     . THR   D 1 191 ? 134.473 157.343 123.955 1.00 60.93  ? 167 THR   C C     1 
ATOM   7788 O  O     . THR   D 1 191 ? 135.572 157.816 123.647 1.00 66.17  ? 167 THR   C O     1 
ATOM   7789 C  CB    . THR   D 1 191 ? 134.557 156.756 126.377 1.00 61.08  ? 167 THR   C CB    1 
ATOM   7790 O  OG1   . THR   D 1 191 ? 134.167 155.392 126.175 1.00 63.63  ? 167 THR   C OG1   1 
ATOM   7791 C  CG2   . THR   D 1 191 ? 134.152 157.191 127.775 1.00 60.17  ? 167 THR   C CG2   1 
ATOM   7792 N  N     . SER   D 1 192 ? 133.771 156.570 123.127 1.00 58.77  ? 168 SER   C N     1 
ATOM   7793 C  CA    . SER   D 1 192 ? 134.215 156.384 121.751 1.00 62.95  ? 168 SER   C CA    1 
ATOM   7794 C  C     . SER   D 1 192 ? 134.193 157.706 120.996 1.00 71.22  ? 168 SER   C C     1 
ATOM   7795 O  O     . SER   D 1 192 ? 135.205 158.117 120.415 1.00 73.80  ? 168 SER   C O     1 
ATOM   7796 C  CB    . SER   D 1 192 ? 133.341 155.346 121.049 1.00 59.84  ? 168 SER   C CB    1 
ATOM   7797 O  OG    . SER   D 1 192 ? 133.222 154.170 121.829 1.00 61.23  ? 168 SER   C OG    1 
ATOM   7798 N  N     . THR   D 1 193 ? 133.055 158.406 121.021 1.00 76.77  ? 169 THR   C N     1 
ATOM   7799 C  CA    . THR   D 1 193 ? 132.961 159.673 120.304 1.00 71.70  ? 169 THR   C CA    1 
ATOM   7800 C  C     . THR   D 1 193 ? 133.938 160.692 120.869 1.00 72.63  ? 169 THR   C C     1 
ATOM   7801 O  O     . THR   D 1 193 ? 134.681 161.335 120.118 1.00 74.51  ? 169 THR   C O     1 
ATOM   7802 C  CB    . THR   D 1 193 ? 131.532 160.210 120.362 1.00 74.03  ? 169 THR   C CB    1 
ATOM   7803 O  OG1   . THR   D 1 193 ? 130.615 159.172 119.994 1.00 77.51  ? 169 THR   C OG1   1 
ATOM   7804 C  CG2   . THR   D 1 193 ? 131.366 161.385 119.414 1.00 73.52  ? 169 THR   C CG2   1 
ATOM   7805 N  N     . LEU   D 1 194 ? 133.977 160.822 122.197 1.00 79.21  ? 170 LEU   C N     1 
ATOM   7806 C  CA    . LEU   D 1 194 ? 134.943 161.706 122.834 1.00 76.48  ? 170 LEU   C CA    1 
ATOM   7807 C  C     . LEU   D 1 194 ? 136.372 161.298 122.506 1.00 72.62  ? 170 LEU   C C     1 
ATOM   7808 O  O     . LEU   D 1 194 ? 137.283 162.131 122.567 1.00 73.17  ? 170 LEU   C O     1 
ATOM   7809 C  CB    . LEU   D 1 194 ? 134.723 161.712 124.346 1.00 79.35  ? 170 LEU   C CB    1 
ATOM   7810 C  CG    . LEU   D 1 194 ? 134.509 163.069 125.012 1.00 78.93  ? 170 LEU   C CG    1 
ATOM   7811 C  CD1   . LEU   D 1 194 ? 133.316 163.781 124.398 1.00 77.44  ? 170 LEU   C CD1   1 
ATOM   7812 C  CD2   . LEU   D 1 194 ? 134.317 162.895 126.508 1.00 79.28  ? 170 LEU   C CD2   1 
ATOM   7813 N  N     . GLY   D 1 195 ? 136.590 160.027 122.160 1.00 80.26  ? 171 GLY   C N     1 
ATOM   7814 C  CA    . GLY   D 1 195 ? 137.913 159.601 121.746 1.00 81.05  ? 171 GLY   C CA    1 
ATOM   7815 C  C     . GLY   D 1 195 ? 138.274 160.045 120.348 1.00 84.74  ? 171 GLY   C C     1 
ATOM   7816 O  O     . GLY   D 1 195 ? 139.449 160.291 120.062 1.00 87.44  ? 171 GLY   C O     1 
ATOM   7817 N  N     . VAL   D 1 196 ? 137.285 160.152 119.459 1.00 79.87  ? 172 VAL   C N     1 
ATOM   7818 C  CA    . VAL   D 1 196 ? 137.564 160.592 118.095 1.00 75.19  ? 172 VAL   C CA    1 
ATOM   7819 C  C     . VAL   D 1 196 ? 137.882 162.082 118.065 1.00 74.58  ? 172 VAL   C C     1 
ATOM   7820 O  O     . VAL   D 1 196 ? 138.828 162.515 117.396 1.00 76.58  ? 172 VAL   C O     1 
ATOM   7821 C  CB    . VAL   D 1 196 ? 136.386 160.244 117.169 1.00 73.59  ? 172 VAL   C CB    1 
ATOM   7822 C  CG1   . VAL   D 1 196 ? 136.538 160.946 115.831 1.00 75.17  ? 172 VAL   C CG1   1 
ATOM   7823 C  CG2   . VAL   D 1 196 ? 136.296 158.741 116.973 1.00 73.81  ? 172 VAL   C CG2   1 
ATOM   7824 N  N     . LEU   D 1 197 ? 137.102 162.888 118.786 1.00 73.77  ? 173 LEU   C N     1 
ATOM   7825 C  CA    . LEU   D 1 197 ? 137.310 164.333 118.768 1.00 73.47  ? 173 LEU   C CA    1 
ATOM   7826 C  C     . LEU   D 1 197 ? 138.644 164.705 119.403 1.00 75.66  ? 173 LEU   C C     1 
ATOM   7827 O  O     . LEU   D 1 197 ? 139.437 165.448 118.815 1.00 77.86  ? 173 LEU   C O     1 
ATOM   7828 C  CB    . LEU   D 1 197 ? 136.156 165.043 119.481 1.00 74.85  ? 173 LEU   C CB    1 
ATOM   7829 C  CG    . LEU   D 1 197 ? 134.812 165.285 118.775 1.00 76.64  ? 173 LEU   C CG    1 
ATOM   7830 C  CD1   . LEU   D 1 197 ? 134.414 164.164 117.824 1.00 73.14  ? 173 LEU   C CD1   1 
ATOM   7831 C  CD2   . LEU   D 1 197 ? 133.715 165.522 119.802 1.00 77.26  ? 173 LEU   C CD2   1 
ATOM   7832 N  N     . VAL   D 1 198 ? 138.911 164.192 120.601 1.00 83.25  ? 174 VAL   C N     1 
ATOM   7833 C  CA    . VAL   D 1 198 ? 140.155 164.444 121.319 1.00 81.63  ? 174 VAL   C CA    1 
ATOM   7834 C  C     . VAL   D 1 198 ? 140.821 163.104 121.594 1.00 80.78  ? 174 VAL   C C     1 
ATOM   7835 O  O     . VAL   D 1 198 ? 140.188 162.191 122.137 1.00 85.66  ? 174 VAL   C O     1 
ATOM   7836 C  CB    . VAL   D 1 198 ? 139.913 165.215 122.628 1.00 80.70  ? 174 VAL   C CB    1 
ATOM   7837 C  CG1   . VAL   D 1 198 ? 141.198 165.864 123.102 1.00 80.93  ? 174 VAL   C CG1   1 
ATOM   7838 C  CG2   . VAL   D 1 198 ? 138.822 166.259 122.441 1.00 81.24  ? 174 VAL   C CG2   1 
ATOM   7839 N  N     . ARG   D 1 199 ? 142.095 162.988 121.222 1.00 86.78  ? 175 ARG   C N     1 
ATOM   7840 C  CA    . ARG   D 1 199 ? 142.827 161.738 121.378 1.00 87.88  ? 175 ARG   C CA    1 
ATOM   7841 C  C     . ARG   D 1 199 ? 143.382 161.541 122.782 1.00 91.08  ? 175 ARG   C C     1 
ATOM   7842 O  O     . ARG   D 1 199 ? 143.775 160.420 123.122 1.00 88.73  ? 175 ARG   C O     1 
ATOM   7843 C  CB    . ARG   D 1 199 ? 143.978 161.677 120.374 1.00 89.81  ? 175 ARG   C CB    1 
ATOM   7844 C  CG    . ARG   D 1 199 ? 143.591 161.166 119.004 1.00 88.25  ? 175 ARG   C CG    1 
ATOM   7845 C  CD    . ARG   D 1 199 ? 142.782 159.882 119.062 1.00 89.75  ? 175 ARG   C CD    1 
ATOM   7846 N  NE    . ARG   D 1 199 ? 142.750 159.208 117.768 1.00 93.09  ? 175 ARG   C NE    1 
ATOM   7847 C  CZ    . ARG   D 1 199 ? 142.186 159.700 116.672 1.00 93.15  ? 175 ARG   C CZ    1 
ATOM   7848 N  NH1   . ARG   D 1 199 ? 141.540 160.855 116.681 1.00 90.68  ? 175 ARG   C NH1   1 
ATOM   7849 N  NH2   . ARG   D 1 199 ? 142.267 159.011 115.537 1.00 91.75  ? 175 ARG   C NH2   1 
ATOM   7850 N  N     . ASP   D 1 200 ? 143.427 162.592 123.599 1.00 89.55  ? 176 ASP   C N     1 
ATOM   7851 C  CA    . ASP   D 1 200 ? 143.989 162.494 124.938 1.00 85.24  ? 176 ASP   C CA    1 
ATOM   7852 C  C     . ASP   D 1 200 ? 143.107 161.714 125.902 1.00 86.95  ? 176 ASP   C C     1 
ATOM   7853 O  O     . ASP   D 1 200 ? 143.614 161.219 126.915 1.00 90.26  ? 176 ASP   C O     1 
ATOM   7854 C  CB    . ASP   D 1 200 ? 144.246 163.893 125.501 1.00 84.71  ? 176 ASP   C CB    1 
ATOM   7855 C  CG    . ASP   D 1 200 ? 145.141 164.723 124.605 1.00 84.84  ? 176 ASP   C CG    1 
ATOM   7856 O  OD1   . ASP   D 1 200 ? 144.764 164.957 123.439 1.00 84.98  ? 176 ASP   C OD1   1 
ATOM   7857 O  OD2   . ASP   D 1 200 ? 146.223 165.143 125.067 1.00 86.57  ? 176 ASP   C OD2   1 
ATOM   7858 N  N     . THR   D 1 201 ? 141.810 161.581 125.609 1.00 82.96  ? 177 THR   C N     1 
ATOM   7859 C  CA    . THR   D 1 201 ? 140.908 160.887 126.522 1.00 81.37  ? 177 THR   C CA    1 
ATOM   7860 C  C     . THR   D 1 201 ? 141.319 159.436 126.727 1.00 79.13  ? 177 THR   C C     1 
ATOM   7861 O  O     . THR   D 1 201 ? 141.208 158.916 127.845 1.00 84.24  ? 177 THR   C O     1 
ATOM   7862 C  CB    . THR   D 1 201 ? 139.471 160.960 126.004 1.00 84.67  ? 177 THR   C CB    1 
ATOM   7863 O  OG1   . THR   D 1 201 ? 139.274 159.961 124.996 1.00 85.22  ? 177 THR   C OG1   1 
ATOM   7864 C  CG2   . THR   D 1 201 ? 139.189 162.331 125.412 1.00 82.53  ? 177 THR   C CG2   1 
ATOM   7865 N  N     . GLN   D 1 202 ? 141.800 158.771 125.674 1.00 76.28  ? 178 GLN   C N     1 
ATOM   7866 C  CA    . GLN   D 1 202 ? 142.258 157.394 125.813 1.00 78.40  ? 178 GLN   C CA    1 
ATOM   7867 C  C     . GLN   D 1 202 ? 143.413 157.281 126.801 1.00 80.25  ? 178 GLN   C C     1 
ATOM   7868 O  O     . GLN   D 1 202 ? 143.612 156.217 127.397 1.00 79.51  ? 178 GLN   C O     1 
ATOM   7869 C  CB    . GLN   D 1 202 ? 142.668 156.837 124.451 1.00 79.90  ? 178 GLN   C CB    1 
ATOM   7870 C  CG    . GLN   D 1 202 ? 141.601 156.981 123.379 1.00 82.65  ? 178 GLN   C CG    1 
ATOM   7871 C  CD    . GLN   D 1 202 ? 142.072 156.505 122.021 1.00 86.86  ? 178 GLN   C CD    1 
ATOM   7872 O  OE1   . GLN   D 1 202 ? 143.040 155.752 121.914 1.00 86.39  ? 178 GLN   C OE1   1 
ATOM   7873 N  NE2   . GLN   D 1 202 ? 141.386 156.942 120.972 1.00 87.29  ? 178 GLN   C NE2   1 
ATOM   7874 N  N     . MET   D 1 203 ? 144.180 158.356 126.985 1.00 83.68  ? 179 MET   C N     1 
ATOM   7875 C  CA    . MET   D 1 203 ? 145.221 158.354 128.005 1.00 81.40  ? 179 MET   C CA    1 
ATOM   7876 C  C     . MET   D 1 203 ? 144.664 158.680 129.384 1.00 80.66  ? 179 MET   C C     1 
ATOM   7877 O  O     . MET   D 1 203 ? 145.214 158.225 130.393 1.00 82.51  ? 179 MET   C O     1 
ATOM   7878 C  CB    . MET   D 1 203 ? 146.323 159.350 127.639 1.00 82.94  ? 179 MET   C CB    1 
ATOM   7879 C  CG    . MET   D 1 203 ? 146.752 159.298 126.182 1.00 84.45  ? 179 MET   C CG    1 
ATOM   7880 S  SD    . MET   D 1 203 ? 148.008 158.044 125.870 1.00 92.60  ? 179 MET   C SD    1 
ATOM   7881 C  CE    . MET   D 1 203 ? 148.948 158.114 127.392 1.00 84.74  ? 179 MET   C CE    1 
ATOM   7882 N  N     . LEU   D 1 204 ? 143.582 159.459 129.447 1.00 77.59  ? 180 LEU   C N     1 
ATOM   7883 C  CA    . LEU   D 1 204 ? 142.997 159.810 130.736 1.00 77.67  ? 180 LEU   C CA    1 
ATOM   7884 C  C     . LEU   D 1 204 ? 142.207 158.652 131.331 1.00 78.72  ? 180 LEU   C C     1 
ATOM   7885 O  O     . LEU   D 1 204 ? 142.152 158.511 132.559 1.00 83.54  ? 180 LEU   C O     1 
ATOM   7886 C  CB    . LEU   D 1 204 ? 142.101 161.038 130.589 1.00 76.80  ? 180 LEU   C CB    1 
ATOM   7887 C  CG    . LEU   D 1 204 ? 142.612 162.336 131.213 1.00 79.59  ? 180 LEU   C CG    1 
ATOM   7888 C  CD1   . LEU   D 1 204 ? 141.634 163.469 130.954 1.00 76.88  ? 180 LEU   C CD1   1 
ATOM   7889 C  CD2   . LEU   D 1 204 ? 142.846 162.157 132.703 1.00 80.48  ? 180 LEU   C CD2   1 
ATOM   7890 N  N     . MET   D 1 205 ? 141.606 157.813 130.483 1.00 79.58  ? 181 MET   C N     1 
ATOM   7891 C  CA    . MET   D 1 205 ? 140.761 156.729 130.974 1.00 76.23  ? 181 MET   C CA    1 
ATOM   7892 C  C     . MET   D 1 205 ? 141.535 155.801 131.900 1.00 76.23  ? 181 MET   C C     1 
ATOM   7893 O  O     . MET   D 1 205 ? 141.048 155.443 132.979 1.00 79.79  ? 181 MET   C O     1 
ATOM   7894 C  CB    . MET   D 1 205 ? 140.182 155.948 129.795 1.00 72.40  ? 181 MET   C CB    1 
ATOM   7895 C  CG    . MET   D 1 205 ? 138.691 155.681 129.893 1.00 76.83  ? 181 MET   C CG    1 
ATOM   7896 S  SD    . MET   D 1 205 ? 137.705 157.185 129.796 1.00 82.51  ? 181 MET   C SD    1 
ATOM   7897 C  CE    . MET   D 1 205 ? 136.593 156.947 131.179 1.00 81.78  ? 181 MET   C CE    1 
ATOM   7898 N  N     . GLN   D 1 206 ? 142.756 155.427 131.509 1.00 80.16  ? 182 GLN   C N     1 
ATOM   7899 C  CA    . GLN   D 1 206 ? 143.572 154.554 132.345 1.00 80.84  ? 182 GLN   C CA    1 
ATOM   7900 C  C     . GLN   D 1 206 ? 143.810 155.154 133.722 1.00 82.16  ? 182 GLN   C C     1 
ATOM   7901 O  O     . GLN   D 1 206 ? 143.965 154.413 134.700 1.00 85.17  ? 182 GLN   C O     1 
ATOM   7902 C  CB    . GLN   D 1 206 ? 144.906 154.266 131.659 1.00 83.32  ? 182 GLN   C CB    1 
ATOM   7903 C  CG    . GLN   D 1 206 ? 144.876 153.083 130.708 1.00 85.27  ? 182 GLN   C CG    1 
ATOM   7904 C  CD    . GLN   D 1 206 ? 145.501 153.402 129.365 1.00 87.18  ? 182 GLN   C CD    1 
ATOM   7905 O  OE1   . GLN   D 1 206 ? 146.286 154.342 129.240 1.00 86.12  ? 182 GLN   C OE1   1 
ATOM   7906 N  NE2   . GLN   D 1 206 ? 145.154 152.618 128.351 1.00 85.59  ? 182 GLN   C NE2   1 
ATOM   7907 N  N     . ALA   D 1 207 ? 143.844 156.483 133.824 1.00 75.89  ? 183 ALA   C N     1 
ATOM   7908 C  CA    . ALA   D 1 207 ? 143.998 157.115 135.127 1.00 73.35  ? 183 ALA   C CA    1 
ATOM   7909 C  C     . ALA   D 1 207 ? 142.712 157.071 135.941 1.00 73.03  ? 183 ALA   C C     1 
ATOM   7910 O  O     . ALA   D 1 207 ? 142.768 156.937 137.168 1.00 75.92  ? 183 ALA   C O     1 
ATOM   7911 C  CB    . ALA   D 1 207 ? 144.462 158.562 134.961 1.00 73.94  ? 183 ALA   C CB    1 
ATOM   7912 N  N     . ILE   D 1 208 ? 141.555 157.186 135.285 1.00 68.25  ? 184 ILE   C N     1 
ATOM   7913 C  CA    . ILE   D 1 208 ? 140.294 157.229 136.019 1.00 66.27  ? 184 ILE   C CA    1 
ATOM   7914 C  C     . ILE   D 1 208 ? 139.967 155.863 136.608 1.00 65.53  ? 184 ILE   C C     1 
ATOM   7915 O  O     . ILE   D 1 208 ? 139.603 155.750 137.786 1.00 69.46  ? 184 ILE   C O     1 
ATOM   7916 C  CB    . ILE   D 1 208 ? 139.164 157.735 135.105 1.00 65.72  ? 184 ILE   C CB    1 
ATOM   7917 C  CG1   . ILE   D 1 208 ? 139.434 159.178 134.674 1.00 68.67  ? 184 ILE   C CG1   1 
ATOM   7918 C  CG2   . ILE   D 1 208 ? 137.823 157.630 135.809 1.00 68.80  ? 184 ILE   C CG2   1 
ATOM   7919 C  CD1   . ILE   D 1 208 ? 138.348 159.766 133.803 1.00 67.08  ? 184 ILE   C CD1   1 
ATOM   7920 N  N     . LEU   D 1 209 ? 140.115 154.804 135.808 1.00 55.72  ? 185 LEU   C N     1 
ATOM   7921 C  CA    . LEU   D 1 209 ? 139.667 153.479 136.224 1.00 52.60  ? 185 LEU   C CA    1 
ATOM   7922 C  C     . LEU   D 1 209 ? 140.392 152.998 137.474 1.00 54.11  ? 185 LEU   C C     1 
ATOM   7923 O  O     . LEU   D 1 209 ? 139.774 152.359 138.334 1.00 57.09  ? 185 LEU   C O     1 
ATOM   7924 C  CB    . LEU   D 1 209 ? 139.850 152.486 135.076 1.00 53.58  ? 185 LEU   C CB    1 
ATOM   7925 C  CG    . LEU   D 1 209 ? 138.830 152.635 133.945 1.00 56.02  ? 185 LEU   C CG    1 
ATOM   7926 C  CD1   . LEU   D 1 209 ? 139.259 151.856 132.715 1.00 57.17  ? 185 LEU   C CD1   1 
ATOM   7927 C  CD2   . LEU   D 1 209 ? 137.448 152.198 134.403 1.00 52.50  ? 185 LEU   C CD2   1 
ATOM   7928 N  N     . ARG   D 1 210 ? 141.685 153.306 137.601 1.00 51.09  ? 186 ARG   C N     1 
ATOM   7929 C  CA    . ARG   D 1 210 ? 142.411 152.949 138.816 1.00 45.51  ? 186 ARG   C CA    1 
ATOM   7930 C  C     . ARG   D 1 210 ? 141.756 153.559 140.047 1.00 52.03  ? 186 ARG   C C     1 
ATOM   7931 O  O     . ARG   D 1 210 ? 141.596 152.882 141.070 1.00 55.55  ? 186 ARG   C O     1 
ATOM   7932 C  CB    . ARG   D 1 210 ? 143.867 153.398 138.707 1.00 51.50  ? 186 ARG   C CB    1 
ATOM   7933 C  CG    . ARG   D 1 210 ? 144.793 152.359 138.104 1.00 60.44  ? 186 ARG   C CG    1 
ATOM   7934 C  CD    . ARG   D 1 210 ? 146.204 152.901 137.961 1.00 58.79  ? 186 ARG   C CD    1 
ATOM   7935 N  NE    . ARG   D 1 210 ? 146.607 152.997 136.563 1.00 58.34  ? 186 ARG   C NE    1 
ATOM   7936 C  CZ    . ARG   D 1 210 ? 147.198 152.023 135.885 1.00 61.69  ? 186 ARG   C CZ    1 
ATOM   7937 N  NH1   . ARG   D 1 210 ? 147.478 150.859 136.450 1.00 60.04  ? 186 ARG   C NH1   1 
ATOM   7938 N  NH2   . ARG   D 1 210 ? 147.517 152.220 134.609 1.00 60.08  ? 186 ARG   C NH2   1 
ATOM   7939 N  N     . ILE   D 1 211 ? 141.349 154.827 139.960 1.00 46.14  ? 187 ILE   C N     1 
ATOM   7940 C  CA    . ILE   D 1 211 ? 140.657 155.460 141.076 1.00 40.49  ? 187 ILE   C CA    1 
ATOM   7941 C  C     . ILE   D 1 211 ? 139.347 154.739 141.365 1.00 48.11  ? 187 ILE   C C     1 
ATOM   7942 O  O     . ILE   D 1 211 ? 138.922 154.635 142.521 1.00 54.52  ? 187 ILE   C O     1 
ATOM   7943 C  CB    . ILE   D 1 211 ? 140.433 156.955 140.787 1.00 49.37  ? 187 ILE   C CB    1 
ATOM   7944 C  CG1   . ILE   D 1 211 ? 141.736 157.612 140.336 1.00 45.90  ? 187 ILE   C CG1   1 
ATOM   7945 C  CG2   . ILE   D 1 211 ? 139.883 157.661 142.014 1.00 47.89  ? 187 ILE   C CG2   1 
ATOM   7946 C  CD1   . ILE   D 1 211 ? 141.592 159.076 139.996 1.00 44.88  ? 187 ILE   C CD1   1 
ATOM   7947 N  N     . LEU   D 1 212 ? 138.692 154.225 140.323 1.00 45.48  ? 188 LEU   C N     1 
ATOM   7948 C  CA    . LEU   D 1 212 ? 137.444 153.501 140.528 1.00 40.87  ? 188 LEU   C CA    1 
ATOM   7949 C  C     . LEU   D 1 212 ? 137.688 152.114 141.109 1.00 44.76  ? 188 LEU   C C     1 
ATOM   7950 O  O     . LEU   D 1 212 ? 136.743 151.465 141.574 1.00 51.60  ? 188 LEU   C O     1 
ATOM   7951 C  CB    . LEU   D 1 212 ? 136.676 153.397 139.211 1.00 47.17  ? 188 LEU   C CB    1 
ATOM   7952 C  CG    . LEU   D 1 212 ? 136.161 154.701 138.599 1.00 50.53  ? 188 LEU   C CG    1 
ATOM   7953 C  CD1   . LEU   D 1 212 ? 135.051 154.421 137.601 1.00 48.56  ? 188 LEU   C CD1   1 
ATOM   7954 C  CD2   . LEU   D 1 212 ? 135.687 155.667 139.675 1.00 48.13  ? 188 LEU   C CD2   1 
ATOM   7955 N  N     . PHE   D 1 213 ? 138.936 151.644 141.095 1.00 39.82  ? 189 PHE   C N     1 
ATOM   7956 C  CA    . PHE   D 1 213 ? 139.224 150.299 141.581 1.00 31.26  ? 189 PHE   C CA    1 
ATOM   7957 C  C     . PHE   D 1 213 ? 139.542 150.300 143.070 1.00 42.37  ? 189 PHE   C C     1 
ATOM   7958 O  O     . PHE   D 1 213 ? 138.956 149.531 143.839 1.00 43.85  ? 189 PHE   C O     1 
ATOM   7959 C  CB    . PHE   D 1 213 ? 140.386 149.699 140.787 1.00 33.72  ? 189 PHE   C CB    1 
ATOM   7960 C  CG    . PHE   D 1 213 ? 140.746 148.302 141.198 1.00 35.99  ? 189 PHE   C CG    1 
ATOM   7961 C  CD1   . PHE   D 1 213 ? 139.764 147.362 141.447 1.00 41.26  ? 189 PHE   C CD1   1 
ATOM   7962 C  CD2   . PHE   D 1 213 ? 142.071 147.928 141.328 1.00 43.46  ? 189 PHE   C CD2   1 
ATOM   7963 C  CE1   . PHE   D 1 213 ? 140.096 146.076 141.819 1.00 40.55  ? 189 PHE   C CE1   1 
ATOM   7964 C  CE2   . PHE   D 1 213 ? 142.407 146.644 141.701 1.00 35.27  ? 189 PHE   C CE2   1 
ATOM   7965 C  CZ    . PHE   D 1 213 ? 141.419 145.718 141.947 1.00 37.51  ? 189 PHE   C CZ    1 
ATOM   7966 N  N     . TYR   D 1 214 ? 140.471 151.157 143.494 1.00 44.99  ? 190 TYR   C N     1 
ATOM   7967 C  CA    . TYR   D 1 214 ? 140.925 151.159 144.877 1.00 37.22  ? 190 TYR   C CA    1 
ATOM   7968 C  C     . TYR   D 1 214 ? 139.931 151.815 145.825 1.00 44.96  ? 190 TYR   C C     1 
ATOM   7969 O  O     . TYR   D 1 214 ? 139.902 151.461 147.008 1.00 56.51  ? 190 TYR   C O     1 
ATOM   7970 C  CB    . TYR   D 1 214 ? 142.279 151.859 144.972 1.00 34.36  ? 190 TYR   C CB    1 
ATOM   7971 C  CG    . TYR   D 1 214 ? 143.426 150.998 144.500 1.00 42.73  ? 190 TYR   C CG    1 
ATOM   7972 C  CD1   . TYR   D 1 214 ? 143.763 149.831 145.169 1.00 42.15  ? 190 TYR   C CD1   1 
ATOM   7973 C  CD2   . TYR   D 1 214 ? 144.159 151.343 143.375 1.00 42.15  ? 190 TYR   C CD2   1 
ATOM   7974 C  CE1   . TYR   D 1 214 ? 144.807 149.038 144.738 1.00 39.33  ? 190 TYR   C CE1   1 
ATOM   7975 C  CE2   . TYR   D 1 214 ? 145.203 150.557 142.935 1.00 38.31  ? 190 TYR   C CE2   1 
ATOM   7976 C  CZ    . TYR   D 1 214 ? 145.523 149.406 143.621 1.00 43.08  ? 190 TYR   C CZ    1 
ATOM   7977 O  OH    . TYR   D 1 214 ? 146.563 148.619 143.186 1.00 47.79  ? 190 TYR   C OH    1 
ATOM   7978 N  N     . PHE   D 1 215 ? 139.123 152.754 145.342 1.00 36.37  ? 191 PHE   C N     1 
ATOM   7979 C  CA    . PHE   D 1 215 ? 138.078 153.370 146.156 1.00 32.94  ? 191 PHE   C CA    1 
ATOM   7980 C  C     . PHE   D 1 215 ? 136.759 152.636 145.919 1.00 49.88  ? 191 PHE   C C     1 
ATOM   7981 O  O     . PHE   D 1 215 ? 135.786 153.174 145.392 1.00 52.01  ? 191 PHE   C O     1 
ATOM   7982 C  CB    . PHE   D 1 215 ? 137.969 154.858 145.842 1.00 35.78  ? 191 PHE   C CB    1 
ATOM   7983 C  CG    . PHE   D 1 215 ? 139.142 155.663 146.322 1.00 55.44  ? 191 PHE   C CG    1 
ATOM   7984 C  CD1   . PHE   D 1 215 ? 140.263 155.821 145.524 1.00 55.73  ? 191 PHE   C CD1   1 
ATOM   7985 C  CD2   . PHE   D 1 215 ? 139.127 156.255 147.572 1.00 57.08  ? 191 PHE   C CD2   1 
ATOM   7986 C  CE1   . PHE   D 1 215 ? 141.346 156.558 145.964 1.00 44.79  ? 191 PHE   C CE1   1 
ATOM   7987 C  CE2   . PHE   D 1 215 ? 140.206 156.993 148.017 1.00 55.49  ? 191 PHE   C CE2   1 
ATOM   7988 C  CZ    . PHE   D 1 215 ? 141.318 157.144 147.212 1.00 49.54  ? 191 PHE   C CZ    1 
ATOM   7989 N  N     . SER   D 1 216 ? 136.752 151.371 146.330 1.00 54.44  ? 192 SER   C N     1 
ATOM   7990 C  CA    . SER   D 1 216 ? 135.630 150.476 146.091 1.00 42.77  ? 192 SER   C CA    1 
ATOM   7991 C  C     . SER   D 1 216 ? 135.668 149.374 147.142 1.00 55.37  ? 192 SER   C C     1 
ATOM   7992 O  O     . SER   D 1 216 ? 136.724 149.112 147.730 1.00 56.05  ? 192 SER   C O     1 
ATOM   7993 C  CB    . SER   D 1 216 ? 135.691 149.879 144.676 1.00 45.95  ? 192 SER   C CB    1 
ATOM   7994 O  OG    . SER   D 1 216 ? 134.409 149.856 144.076 1.00 52.29  ? 192 SER   C OG    1 
ATOM   7995 N  N     . PRO   D 1 217 ? 134.534 148.707 147.401 1.00 50.84  ? 193 PRO   C N     1 
ATOM   7996 C  CA    . PRO   D 1 217 ? 134.525 147.638 148.409 1.00 44.68  ? 193 PRO   C CA    1 
ATOM   7997 C  C     . PRO   D 1 217 ? 135.064 146.320 147.881 1.00 42.45  ? 193 PRO   C C     1 
ATOM   7998 O  O     . PRO   D 1 217 ? 134.855 145.269 148.493 1.00 47.36  ? 193 PRO   C O     1 
ATOM   7999 C  CB    . PRO   D 1 217 ? 133.040 147.512 148.783 1.00 45.91  ? 193 PRO   C CB    1 
ATOM   8000 C  CG    . PRO   D 1 217 ? 132.357 148.668 148.134 1.00 44.87  ? 193 PRO   C CG    1 
ATOM   8001 C  CD    . PRO   D 1 217 ? 133.174 149.028 146.947 1.00 43.13  ? 193 PRO   C CD    1 
ATOM   8002 N  N     . ILE   D 1 218 ? 135.747 146.363 146.738 1.00 42.26  ? 194 ILE   C N     1 
ATOM   8003 C  CA    . ILE   D 1 218 ? 136.268 145.140 146.138 1.00 39.20  ? 194 ILE   C CA    1 
ATOM   8004 C  C     . ILE   D 1 218 ? 137.328 144.508 147.034 1.00 40.63  ? 194 ILE   C C     1 
ATOM   8005 O  O     . ILE   D 1 218 ? 137.344 143.287 147.229 1.00 50.06  ? 194 ILE   C O     1 
ATOM   8006 C  CB    . ILE   D 1 218 ? 136.811 145.431 144.728 1.00 43.16  ? 194 ILE   C CB    1 
ATOM   8007 C  CG1   . ILE   D 1 218 ? 135.691 145.957 143.830 1.00 42.67  ? 194 ILE   C CG1   1 
ATOM   8008 C  CG2   . ILE   D 1 218 ? 137.421 144.188 144.129 1.00 35.10  ? 194 ILE   C CG2   1 
ATOM   8009 C  CD1   . ILE   D 1 218 ? 136.172 146.483 142.500 1.00 40.92  ? 194 ILE   C CD1   1 
ATOM   8010 N  N     . LEU   D 1 219 ? 138.226 145.321 147.597 1.00 45.83  ? 195 LEU   C N     1 
ATOM   8011 C  CA    . LEU   D 1 219 ? 139.326 144.812 148.406 1.00 40.72  ? 195 LEU   C CA    1 
ATOM   8012 C  C     . LEU   D 1 219 ? 139.244 145.182 149.880 1.00 41.23  ? 195 LEU   C C     1 
ATOM   8013 O  O     . LEU   D 1 219 ? 139.872 144.505 150.699 1.00 41.78  ? 195 LEU   C O     1 
ATOM   8014 C  CB    . LEU   D 1 219 ? 140.671 145.314 147.859 1.00 38.85  ? 195 LEU   C CB    1 
ATOM   8015 C  CG    . LEU   D 1 219 ? 140.965 145.134 146.370 1.00 43.53  ? 195 LEU   C CG    1 
ATOM   8016 C  CD1   . LEU   D 1 219 ? 141.872 146.244 145.875 1.00 38.21  ? 195 LEU   C CD1   1 
ATOM   8017 C  CD2   . LEU   D 1 219 ? 141.595 143.780 146.112 1.00 40.65  ? 195 LEU   C CD2   1 
ATOM   8018 N  N     . TRP   D 1 220 ? 138.500 146.224 150.241 1.00 51.36  ? 196 TRP   C N     1 
ATOM   8019 C  CA    . TRP   D 1 220 ? 138.488 146.703 151.614 1.00 48.17  ? 196 TRP   C CA    1 
ATOM   8020 C  C     . TRP   D 1 220 ? 137.114 147.265 151.947 1.00 55.05  ? 196 TRP   C C     1 
ATOM   8021 O  O     . TRP   D 1 220 ? 136.310 147.559 151.060 1.00 56.89  ? 196 TRP   C O     1 
ATOM   8022 C  CB    . TRP   D 1 220 ? 139.568 147.766 151.843 1.00 51.00  ? 196 TRP   C CB    1 
ATOM   8023 C  CG    . TRP   D 1 220 ? 139.231 149.098 151.248 1.00 53.57  ? 196 TRP   C CG    1 
ATOM   8024 C  CD1   . TRP   D 1 220 ? 139.068 149.385 149.925 1.00 50.50  ? 196 TRP   C CD1   1 
ATOM   8025 C  CD2   . TRP   D 1 220 ? 139.011 150.324 151.954 1.00 51.73  ? 196 TRP   C CD2   1 
ATOM   8026 N  NE1   . TRP   D 1 220 ? 138.763 150.714 149.762 1.00 45.37  ? 196 TRP   C NE1   1 
ATOM   8027 C  CE2   . TRP   D 1 220 ? 138.722 151.312 150.993 1.00 47.79  ? 196 TRP   C CE2   1 
ATOM   8028 C  CE3   . TRP   D 1 220 ? 139.033 150.683 153.304 1.00 50.17  ? 196 TRP   C CE3   1 
ATOM   8029 C  CZ2   . TRP   D 1 220 ? 138.456 152.633 151.340 1.00 50.44  ? 196 TRP   C CZ2   1 
ATOM   8030 C  CZ3   . TRP   D 1 220 ? 138.770 151.994 153.645 1.00 56.83  ? 196 TRP   C CZ3   1 
ATOM   8031 C  CH2   . TRP   D 1 220 ? 138.484 152.954 152.668 1.00 56.64  ? 196 TRP   C CH2   1 
ATOM   8032 N  N     . LEU   D 1 221 ? 136.854 147.410 153.245 1.00 72.28  ? 197 LEU   C N     1 
ATOM   8033 C  CA    . LEU   D 1 221 ? 135.592 147.950 153.741 1.00 72.56  ? 197 LEU   C CA    1 
ATOM   8034 C  C     . LEU   D 1 221 ? 135.904 149.108 154.680 1.00 76.62  ? 197 LEU   C C     1 
ATOM   8035 O  O     . LEU   D 1 221 ? 136.647 148.920 155.664 1.00 83.07  ? 197 LEU   C O     1 
ATOM   8036 C  CB    . LEU   D 1 221 ? 134.777 146.868 154.455 1.00 73.81  ? 197 LEU   C CB    1 
ATOM   8037 C  CG    . LEU   D 1 221 ? 133.461 146.431 153.805 1.00 74.88  ? 197 LEU   C CG    1 
ATOM   8038 C  CD1   . LEU   D 1 221 ? 132.674 145.536 154.746 1.00 72.66  ? 197 LEU   C CD1   1 
ATOM   8039 C  CD2   . LEU   D 1 221 ? 132.628 147.631 153.383 1.00 73.99  ? 197 LEU   C CD2   1 
ATOM   8040 N  N     . PRO   D 1 222 ? 135.379 150.305 154.429 1.00 81.71  ? 198 PRO   C N     1 
ATOM   8041 C  CA    . PRO   D 1 222 ? 135.677 151.442 155.308 1.00 82.67  ? 198 PRO   C CA    1 
ATOM   8042 C  C     . PRO   D 1 222 ? 135.088 151.257 156.699 1.00 83.32  ? 198 PRO   C C     1 
ATOM   8043 O  O     . PRO   D 1 222 ? 134.152 150.485 156.916 1.00 80.69  ? 198 PRO   C O     1 
ATOM   8044 C  CB    . PRO   D 1 222 ? 135.037 152.636 154.590 1.00 83.51  ? 198 PRO   C CB    1 
ATOM   8045 C  CG    . PRO   D 1 222 ? 134.071 152.046 153.619 1.00 79.79  ? 198 PRO   C CG    1 
ATOM   8046 C  CD    . PRO   D 1 222 ? 134.595 150.699 153.247 1.00 77.91  ? 198 PRO   C CD    1 
ATOM   8047 N  N     . LYS   D 1 223 ? 135.655 151.991 157.663 1.00 100.51 ? 199 LYS   C N     1 
ATOM   8048 C  CA    . LYS   D 1 223 ? 135.239 151.813 159.080 1.00 101.95 ? 199 LYS   C CA    1 
ATOM   8049 C  C     . LYS   D 1 223 ? 134.291 152.929 159.541 1.00 100.39 ? 199 LYS   C C     1 
ATOM   8050 O  O     . LYS   D 1 223 ? 133.604 152.696 160.562 1.00 98.20  ? 199 LYS   C O     1 
ATOM   8051 C  CB    . LYS   D 1 223 ? 136.479 151.824 159.979 1.00 101.67 ? 199 LYS   C CB    1 
ATOM   8052 C  CG    . LYS   D 1 223 ? 136.325 151.136 161.327 1.00 101.73 ? 199 LYS   C CG    1 
ATOM   8053 C  CD    . LYS   D 1 223 ? 137.466 150.176 161.637 1.00 97.52  ? 199 LYS   C CD    1 
ATOM   8054 C  CE    . LYS   D 1 223 ? 137.738 149.234 160.508 1.00 98.56  ? 199 LYS   C CE    1 
ATOM   8055 N  NZ    . LYS   D 1 223 ? 138.829 148.314 160.836 1.00 99.10  ? 199 LYS   C NZ    1 
ATOM   8056 N  N     . ASN   D 1 224 ? 134.293 154.085 158.864 1.00 118.73 ? 200 ASN   C N     1 
ATOM   8057 C  CA    . ASN   D 1 224 ? 133.425 155.197 159.245 1.00 121.42 ? 200 ASN   C CA    1 
ATOM   8058 C  C     . ASN   D 1 224 ? 133.821 155.811 160.586 1.00 121.79 ? 200 ASN   C C     1 
ATOM   8059 O  O     . ASN   D 1 224 ? 134.896 155.516 161.119 1.00 120.61 ? 200 ASN   C O     1 
ATOM   8060 C  CB    . ASN   D 1 224 ? 131.960 154.746 159.285 1.00 121.38 ? 200 ASN   C CB    1 
ATOM   8061 C  CG    . ASN   D 1 224 ? 130.999 155.842 158.864 1.00 122.41 ? 200 ASN   C CG    1 
ATOM   8062 O  OD1   . ASN   D 1 224 ? 130.691 156.745 159.642 1.00 121.66 ? 200 ASN   C OD1   1 
ATOM   8063 N  ND2   . ASN   D 1 224 ? 130.519 155.767 157.627 1.00 120.13 ? 200 ASN   C ND2   1 
ATOM   8064 N  N     . HIS   D 1 225 ? 132.957 156.687 161.112 1.00 125.05 ? 201 HIS   C N     1 
ATOM   8065 C  CA    . HIS   D 1 225 ? 133.134 157.355 162.409 1.00 125.53 ? 201 HIS   C CA    1 
ATOM   8066 C  C     . HIS   D 1 225 ? 134.530 157.962 162.558 1.00 126.34 ? 201 HIS   C C     1 
ATOM   8067 O  O     . HIS   D 1 225 ? 135.200 157.802 163.580 1.00 127.67 ? 201 HIS   C O     1 
ATOM   8068 C  CB    . HIS   D 1 225 ? 132.804 156.412 163.576 1.00 124.33 ? 201 HIS   C CB    1 
ATOM   8069 C  CG    . HIS   D 1 225 ? 133.780 155.291 163.765 1.00 126.55 ? 201 HIS   C CG    1 
ATOM   8070 N  ND1   . HIS   D 1 225 ? 135.025 155.475 164.328 1.00 126.76 ? 201 HIS   C ND1   1 
ATOM   8071 C  CD2   . HIS   D 1 225 ? 133.687 153.971 163.482 1.00 126.45 ? 201 HIS   C CD2   1 
ATOM   8072 C  CE1   . HIS   D 1 225 ? 135.661 154.317 164.373 1.00 125.37 ? 201 HIS   C CE1   1 
ATOM   8073 N  NE2   . HIS   D 1 225 ? 134.871 153.389 163.865 1.00 125.33 ? 201 HIS   C NE2   1 
ATOM   8074 N  N     . GLY   D 1 226 ? 134.965 158.684 161.530 1.00 108.26 ? 202 GLY   C N     1 
ATOM   8075 C  CA    . GLY   D 1 226 ? 136.244 159.364 161.572 1.00 108.52 ? 202 GLY   C CA    1 
ATOM   8076 C  C     . GLY   D 1 226 ? 136.604 160.005 160.249 1.00 109.55 ? 202 GLY   C C     1 
ATOM   8077 O  O     . GLY   D 1 226 ? 135.723 160.480 159.525 1.00 109.45 ? 202 GLY   C O     1 
ATOM   8078 N  N     . ILE   D 1 227 ? 137.899 160.032 159.918 1.00 110.82 ? 203 ILE   C N     1 
ATOM   8079 C  CA    . ILE   D 1 227 ? 138.319 160.499 158.598 1.00 111.05 ? 203 ILE   C CA    1 
ATOM   8080 C  C     . ILE   D 1 227 ? 137.920 159.533 157.497 1.00 109.00 ? 203 ILE   C C     1 
ATOM   8081 O  O     . ILE   D 1 227 ? 137.899 159.921 156.322 1.00 105.15 ? 203 ILE   C O     1 
ATOM   8082 C  CB    . ILE   D 1 227 ? 139.839 160.749 158.558 1.00 111.97 ? 203 ILE   C CB    1 
ATOM   8083 C  CG1   . ILE   D 1 227 ? 140.160 161.943 157.648 1.00 110.67 ? 203 ILE   C CG1   1 
ATOM   8084 C  CG2   . ILE   D 1 227 ? 140.593 159.487 158.139 1.00 110.60 ? 203 ILE   C CG2   1 
ATOM   8085 C  CD1   . ILE   D 1 227 ? 140.750 161.569 156.300 1.00 107.82 ? 203 ILE   C CD1   1 
ATOM   8086 N  N     . SER   D 1 228 ? 137.597 158.287 157.844 1.00 106.42 ? 204 SER   C N     1 
ATOM   8087 C  CA    . SER   D 1 228 ? 137.078 157.324 156.886 1.00 106.94 ? 204 SER   C CA    1 
ATOM   8088 C  C     . SER   D 1 228 ? 135.566 157.403 156.728 1.00 107.01 ? 204 SER   C C     1 
ATOM   8089 O  O     . SER   D 1 228 ? 135.023 156.791 155.802 1.00 107.73 ? 204 SER   C O     1 
ATOM   8090 C  CB    . SER   D 1 228 ? 137.475 155.903 157.299 1.00 109.60 ? 204 SER   C CB    1 
ATOM   8091 O  OG    . SER   D 1 228 ? 136.706 155.464 158.405 1.00 110.75 ? 204 SER   C OG    1 
ATOM   8092 N  N     . GLY   D 1 229 ? 134.876 158.133 157.607 1.00 102.61 ? 205 GLY   C N     1 
ATOM   8093 C  CA    . GLY   D 1 229 ? 133.450 158.341 157.420 1.00 100.99 ? 205 GLY   C CA    1 
ATOM   8094 C  C     . GLY   D 1 229 ? 133.146 159.168 156.186 1.00 102.53 ? 205 GLY   C C     1 
ATOM   8095 O  O     . GLY   D 1 229 ? 132.221 158.857 155.431 1.00 104.69 ? 205 GLY   C O     1 
ATOM   8096 N  N     . LEU   D 1 230 ? 133.922 160.232 155.964 1.00 93.65  ? 206 LEU   C N     1 
ATOM   8097 C  CA    . LEU   D 1 230 ? 133.799 160.986 154.724 1.00 92.74  ? 206 LEU   C CA    1 
ATOM   8098 C  C     . LEU   D 1 230 ? 134.156 160.125 153.520 1.00 95.31  ? 206 LEU   C C     1 
ATOM   8099 O  O     . LEU   D 1 230 ? 133.515 160.235 152.470 1.00 97.49  ? 206 LEU   C O     1 
ATOM   8100 C  CB    . LEU   D 1 230 ? 134.684 162.234 154.780 1.00 93.26  ? 206 LEU   C CB    1 
ATOM   8101 C  CG    . LEU   D 1 230 ? 134.486 163.333 153.729 1.00 96.95  ? 206 LEU   C CG    1 
ATOM   8102 C  CD1   . LEU   D 1 230 ? 135.319 163.084 152.477 1.00 96.75  ? 206 LEU   C CD1   1 
ATOM   8103 C  CD2   . LEU   D 1 230 ? 133.012 163.484 153.376 1.00 94.45  ? 206 LEU   C CD2   1 
ATOM   8104 N  N     . ILE   D 1 231 ? 135.164 159.261 153.657 1.00 88.55  ? 207 ILE   C N     1 
ATOM   8105 C  CA    . ILE   D 1 231 ? 135.502 158.334 152.582 1.00 88.04  ? 207 ILE   C CA    1 
ATOM   8106 C  C     . ILE   D 1 231 ? 134.343 157.380 152.315 1.00 86.23  ? 207 ILE   C C     1 
ATOM   8107 O  O     . ILE   D 1 231 ? 134.021 157.084 151.159 1.00 87.31  ? 207 ILE   C O     1 
ATOM   8108 C  CB    . ILE   D 1 231 ? 136.796 157.574 152.924 1.00 90.05  ? 207 ILE   C CB    1 
ATOM   8109 C  CG1   . ILE   D 1 231 ? 137.958 158.553 153.098 1.00 86.51  ? 207 ILE   C CG1   1 
ATOM   8110 C  CG2   . ILE   D 1 231 ? 137.120 156.551 151.846 1.00 89.00  ? 207 ILE   C CG2   1 
ATOM   8111 C  CD1   . ILE   D 1 231 ? 138.182 159.445 151.902 1.00 85.62  ? 207 ILE   C CD1   1 
ATOM   8112 N  N     . HIS   D 1 232 ? 133.703 156.882 153.376 1.00 83.65  ? 208 HIS   C N     1 
ATOM   8113 C  CA    . HIS   D 1 232 ? 132.559 155.994 153.197 1.00 85.08  ? 208 HIS   C CA    1 
ATOM   8114 C  C     . HIS   D 1 232 ? 131.403 156.705 152.503 1.00 86.07  ? 208 HIS   C C     1 
ATOM   8115 O  O     . HIS   D 1 232 ? 130.745 156.126 151.632 1.00 89.74  ? 208 HIS   C O     1 
ATOM   8116 C  CB    . HIS   D 1 232 ? 132.109 155.434 154.545 1.00 86.75  ? 208 HIS   C CB    1 
ATOM   8117 C  CG    . HIS   D 1 232 ? 131.369 154.137 154.441 1.00 89.79  ? 208 HIS   C CG    1 
ATOM   8118 N  ND1   . HIS   D 1 232 ? 131.169 153.304 155.520 1.00 92.75  ? 208 HIS   C ND1   1 
ATOM   8119 C  CD2   . HIS   D 1 232 ? 130.782 153.529 153.384 1.00 89.93  ? 208 HIS   C CD2   1 
ATOM   8120 C  CE1   . HIS   D 1 232 ? 130.490 152.239 155.133 1.00 87.99  ? 208 HIS   C CE1   1 
ATOM   8121 N  NE2   . HIS   D 1 232 ? 130.243 152.351 153.841 1.00 87.63  ? 208 HIS   C NE2   1 
ATOM   8122 N  N     . GLU   D 1 233 ? 131.138 157.960 152.879 1.00 89.29  ? 209 GLU   C N     1 
ATOM   8123 C  CA    . GLU   D 1 233 ? 130.053 158.700 152.243 1.00 89.00  ? 209 GLU   C CA    1 
ATOM   8124 C  C     . GLU   D 1 233 ? 130.378 159.048 150.796 1.00 89.14  ? 209 GLU   C C     1 
ATOM   8125 O  O     . GLU   D 1 233 ? 129.471 159.118 149.960 1.00 88.94  ? 209 GLU   C O     1 
ATOM   8126 C  CB    . GLU   D 1 233 ? 129.743 159.969 153.039 1.00 90.02  ? 209 GLU   C CB    1 
ATOM   8127 C  CG    . GLU   D 1 233 ? 129.271 159.730 154.470 1.00 90.94  ? 209 GLU   C CG    1 
ATOM   8128 C  CD    . GLU   D 1 233 ? 127.847 159.204 154.558 1.00 94.71  ? 209 GLU   C CD    1 
ATOM   8129 O  OE1   . GLU   D 1 233 ? 127.543 158.160 153.943 1.00 91.63  ? 209 GLU   C OE1   1 
ATOM   8130 O  OE2   . GLU   D 1 233 ? 127.026 159.840 155.250 1.00 96.38  ? 209 GLU   C OE2   1 
ATOM   8131 N  N     . MET   D 1 234 ? 131.653 159.273 150.484 1.00 93.92  ? 210 MET   C N     1 
ATOM   8132 C  CA    . MET   D 1 234 ? 132.056 159.560 149.115 1.00 93.14  ? 210 MET   C CA    1 
ATOM   8133 C  C     . MET   D 1 234 ? 132.070 158.318 148.234 1.00 94.62  ? 210 MET   C C     1 
ATOM   8134 O  O     . MET   D 1 234 ? 131.848 158.431 147.025 1.00 95.02  ? 210 MET   C O     1 
ATOM   8135 C  CB    . MET   D 1 234 ? 133.439 160.215 149.105 1.00 94.62  ? 210 MET   C CB    1 
ATOM   8136 C  CG    . MET   D 1 234 ? 133.439 161.671 148.673 1.00 94.57  ? 210 MET   C CG    1 
ATOM   8137 S  SD    . MET   D 1 234 ? 135.095 162.387 148.675 1.00 101.40 ? 210 MET   C SD    1 
ATOM   8138 C  CE    . MET   D 1 234 ? 136.012 161.119 147.803 1.00 95.74  ? 210 MET   C CE    1 
ATOM   8139 N  N     . MET   D 1 235 ? 132.327 157.142 148.810 1.00 76.15  ? 211 MET   C N     1 
ATOM   8140 C  CA    . MET   D 1 235 ? 132.382 155.912 148.031 1.00 69.44  ? 211 MET   C CA    1 
ATOM   8141 C  C     . MET   D 1 235 ? 131.022 155.480 147.507 1.00 72.41  ? 211 MET   C C     1 
ATOM   8142 O  O     . MET   D 1 235 ? 130.963 154.729 146.528 1.00 73.24  ? 211 MET   C O     1 
ATOM   8143 C  CB    . MET   D 1 235 ? 132.983 154.783 148.871 1.00 64.32  ? 211 MET   C CB    1 
ATOM   8144 C  CG    . MET   D 1 235 ? 134.469 154.566 148.655 1.00 74.81  ? 211 MET   C CG    1 
ATOM   8145 S  SD    . MET   D 1 235 ? 135.191 153.438 149.859 1.00 81.91  ? 211 MET   C SD    1 
ATOM   8146 C  CE    . MET   D 1 235 ? 133.973 152.129 149.862 1.00 65.37  ? 211 MET   C CE    1 
ATOM   8147 N  N     . LYS   D 1 236 ? 129.930 155.929 148.132 1.00 62.80  ? 212 LYS   C N     1 
ATOM   8148 C  CA    . LYS   D 1 236 ? 128.600 155.540 147.681 1.00 60.63  ? 212 LYS   C CA    1 
ATOM   8149 C  C     . LYS   D 1 236 ? 128.262 156.105 146.309 1.00 62.68  ? 212 LYS   C C     1 
ATOM   8150 O  O     . LYS   D 1 236 ? 127.354 155.591 145.649 1.00 64.58  ? 212 LYS   C O     1 
ATOM   8151 C  CB    . LYS   D 1 236 ? 127.546 155.983 148.695 1.00 59.46  ? 212 LYS   C CB    1 
ATOM   8152 C  CG    . LYS   D 1 236 ? 127.585 155.213 150.002 1.00 60.10  ? 212 LYS   C CG    1 
ATOM   8153 C  CD    . LYS   D 1 236 ? 126.202 154.724 150.394 1.00 64.02  ? 212 LYS   C CD    1 
ATOM   8154 C  CE    . LYS   D 1 236 ? 126.223 154.040 151.751 1.00 63.97  ? 212 LYS   C CE    1 
ATOM   8155 N  NZ    . LYS   D 1 236 ? 127.408 154.441 152.556 1.00 63.61  ? 212 LYS   C NZ    1 
ATOM   8156 N  N     . TYR   D 1 237 ? 128.963 157.148 145.869 1.00 66.31  ? 213 TYR   C N     1 
ATOM   8157 C  CA    . TYR   D 1 237 ? 128.743 157.708 144.542 1.00 62.57  ? 213 TYR   C CA    1 
ATOM   8158 C  C     . TYR   D 1 237 ? 129.427 156.905 143.444 1.00 60.85  ? 213 TYR   C C     1 
ATOM   8159 O  O     . TYR   D 1 237 ? 129.154 157.144 142.264 1.00 61.67  ? 213 TYR   C O     1 
ATOM   8160 C  CB    . TYR   D 1 237 ? 129.224 159.159 144.504 1.00 62.22  ? 213 TYR   C CB    1 
ATOM   8161 C  CG    . TYR   D 1 237 ? 128.258 160.133 145.138 1.00 63.35  ? 213 TYR   C CG    1 
ATOM   8162 C  CD1   . TYR   D 1 237 ? 127.248 160.723 144.392 1.00 70.72  ? 213 TYR   C CD1   1 
ATOM   8163 C  CD2   . TYR   D 1 237 ? 128.349 160.454 146.484 1.00 65.83  ? 213 TYR   C CD2   1 
ATOM   8164 C  CE1   . TYR   D 1 237 ? 126.360 161.611 144.967 1.00 71.53  ? 213 TYR   C CE1   1 
ATOM   8165 C  CE2   . TYR   D 1 237 ? 127.465 161.339 147.069 1.00 69.35  ? 213 TYR   C CE2   1 
ATOM   8166 C  CZ    . TYR   D 1 237 ? 126.473 161.914 146.305 1.00 72.52  ? 213 TYR   C CZ    1 
ATOM   8167 O  OH    . TYR   D 1 237 ? 125.589 162.798 146.881 1.00 75.03  ? 213 TYR   C OH    1 
ATOM   8168 N  N     . ASN   D 1 238 ? 130.297 155.972 143.801 1.00 56.93  ? 214 ASN   C N     1 
ATOM   8169 C  CA    . ASN   D 1 238 ? 130.939 155.099 142.825 1.00 55.94  ? 214 ASN   C CA    1 
ATOM   8170 C  C     . ASN   D 1 238 ? 129.971 154.002 142.402 1.00 63.36  ? 214 ASN   C C     1 
ATOM   8171 O  O     . ASN   D 1 238 ? 129.474 153.265 143.262 1.00 62.20  ? 214 ASN   C O     1 
ATOM   8172 C  CB    . ASN   D 1 238 ? 132.205 154.496 143.426 1.00 48.98  ? 214 ASN   C CB    1 
ATOM   8173 C  CG    . ASN   D 1 238 ? 133.190 154.031 142.376 1.00 55.45  ? 214 ASN   C CG    1 
ATOM   8174 O  OD1   . ASN   D 1 238 ? 132.986 154.239 141.182 1.00 59.09  ? 214 ASN   C OD1   1 
ATOM   8175 N  ND2   . ASN   D 1 238 ? 134.269 153.399 142.817 1.00 57.25  ? 214 ASN   C ND2   1 
ATOM   8176 N  N     . PRO   D 1 239 ? 129.663 153.860 141.109 1.00 65.09  ? 215 PRO   C N     1 
ATOM   8177 C  CA    . PRO   D 1 239 ? 128.732 152.799 140.690 1.00 55.53  ? 215 PRO   C CA    1 
ATOM   8178 C  C     . PRO   D 1 239 ? 129.255 151.387 140.906 1.00 56.68  ? 215 PRO   C C     1 
ATOM   8179 O  O     . PRO   D 1 239 ? 128.448 150.451 140.925 1.00 60.04  ? 215 PRO   C O     1 
ATOM   8180 C  CB    . PRO   D 1 239 ? 128.515 153.092 139.200 1.00 50.84  ? 215 PRO   C CB    1 
ATOM   8181 C  CG    . PRO   D 1 239 ? 129.732 153.853 138.791 1.00 58.75  ? 215 PRO   C CG    1 
ATOM   8182 C  CD    . PRO   D 1 239 ? 130.069 154.707 139.976 1.00 60.14  ? 215 PRO   C CD    1 
ATOM   8183 N  N     . VAL   D 1 240 ? 130.567 151.197 141.064 1.00 48.88  ? 216 VAL   C N     1 
ATOM   8184 C  CA    . VAL   D 1 240 ? 131.104 149.860 141.312 1.00 42.78  ? 216 VAL   C CA    1 
ATOM   8185 C  C     . VAL   D 1 240 ? 130.697 149.369 142.695 1.00 48.21  ? 216 VAL   C C     1 
ATOM   8186 O  O     . VAL   D 1 240 ? 130.537 148.162 142.925 1.00 60.50  ? 216 VAL   C O     1 
ATOM   8187 C  CB    . VAL   D 1 240 ? 132.634 149.857 141.137 1.00 49.81  ? 216 VAL   C CB    1 
ATOM   8188 C  CG1   . VAL   D 1 240 ? 133.147 148.439 140.974 1.00 58.80  ? 216 VAL   C CG1   1 
ATOM   8189 C  CG2   . VAL   D 1 240 ? 133.030 150.709 139.944 1.00 48.34  ? 216 VAL   C CG2   1 
ATOM   8190 N  N     . TYR   D 1 241 ? 130.545 150.300 143.641 1.00 44.80  ? 217 TYR   C N     1 
ATOM   8191 C  CA    . TYR   D 1 241 ? 130.102 149.952 144.988 1.00 48.29  ? 217 TYR   C CA    1 
ATOM   8192 C  C     . TYR   D 1 241 ? 128.767 149.219 144.951 1.00 52.61  ? 217 TYR   C C     1 
ATOM   8193 O  O     . TYR   D 1 241 ? 128.614 148.151 145.560 1.00 54.82  ? 217 TYR   C O     1 
ATOM   8194 C  CB    . TYR   D 1 241 ? 130.016 151.235 145.826 1.00 41.62  ? 217 TYR   C CB    1 
ATOM   8195 C  CG    . TYR   D 1 241 ? 129.326 151.137 147.174 1.00 49.67  ? 217 TYR   C CG    1 
ATOM   8196 C  CD1   . TYR   D 1 241 ? 127.941 151.121 147.280 1.00 50.44  ? 217 TYR   C CD1   1 
ATOM   8197 C  CD2   . TYR   D 1 241 ? 130.066 151.110 148.348 1.00 49.34  ? 217 TYR   C CD2   1 
ATOM   8198 C  CE1   . TYR   D 1 241 ? 127.320 151.042 148.509 1.00 49.23  ? 217 TYR   C CE1   1 
ATOM   8199 C  CE2   . TYR   D 1 241 ? 129.453 151.036 149.580 1.00 43.78  ? 217 TYR   C CE2   1 
ATOM   8200 C  CZ    . TYR   D 1 241 ? 128.081 151.003 149.654 1.00 50.67  ? 217 TYR   C CZ    1 
ATOM   8201 O  OH    . TYR   D 1 241 ? 127.467 150.930 150.882 1.00 62.19  ? 217 TYR   C OH    1 
ATOM   8202 N  N     . PHE   D 1 242 ? 127.797 149.772 144.220 1.00 31.87  ? 218 PHE   C N     1 
ATOM   8203 C  CA    . PHE   D 1 242 ? 126.472 149.169 144.149 1.00 23.27  ? 218 PHE   C CA    1 
ATOM   8204 C  C     . PHE   D 1 242 ? 126.525 147.785 143.520 1.00 37.17  ? 218 PHE   C C     1 
ATOM   8205 O  O     . PHE   D 1 242 ? 125.900 146.846 144.023 1.00 46.58  ? 218 PHE   C O     1 
ATOM   8206 C  CB    . PHE   D 1 242 ? 125.532 150.088 143.370 1.00 33.59  ? 218 PHE   C CB    1 
ATOM   8207 C  CG    . PHE   D 1 242 ? 124.212 149.463 143.026 1.00 36.40  ? 218 PHE   C CG    1 
ATOM   8208 C  CD1   . PHE   D 1 242 ? 123.256 149.251 144.001 1.00 41.38  ? 218 PHE   C CD1   1 
ATOM   8209 C  CD2   . PHE   D 1 242 ? 123.923 149.104 141.723 1.00 42.59  ? 218 PHE   C CD2   1 
ATOM   8210 C  CE1   . PHE   D 1 242 ? 122.040 148.679 143.683 1.00 37.28  ? 218 PHE   C CE1   1 
ATOM   8211 C  CE2   . PHE   D 1 242 ? 122.711 148.534 141.400 1.00 40.24  ? 218 PHE   C CE2   1 
ATOM   8212 C  CZ    . PHE   D 1 242 ? 121.769 148.320 142.380 1.00 38.55  ? 218 PHE   C CZ    1 
ATOM   8213 N  N     . ILE   D 1 243 ? 127.283 147.631 142.431 1.00 37.27  ? 219 ILE   C N     1 
ATOM   8214 C  CA    . ILE   D 1 243 ? 127.340 146.343 141.743 1.00 31.56  ? 219 ILE   C CA    1 
ATOM   8215 C  C     . ILE   D 1 243 ? 127.971 145.281 142.637 1.00 37.57  ? 219 ILE   C C     1 
ATOM   8216 O  O     . ILE   D 1 243 ? 127.443 144.169 142.769 1.00 51.82  ? 219 ILE   C O     1 
ATOM   8217 C  CB    . ILE   D 1 243 ? 128.095 146.480 140.409 1.00 33.52  ? 219 ILE   C CB    1 
ATOM   8218 C  CG1   . ILE   D 1 243 ? 127.577 147.684 139.623 1.00 44.93  ? 219 ILE   C CG1   1 
ATOM   8219 C  CG2   . ILE   D 1 243 ? 127.942 145.219 139.581 1.00 35.20  ? 219 ILE   C CG2   1 
ATOM   8220 C  CD1   . ILE   D 1 243 ? 128.379 147.992 138.382 1.00 41.58  ? 219 ILE   C CD1   1 
ATOM   8221 N  N     . ALA   D 1 244 ? 129.104 145.605 143.268 1.00 38.04  ? 220 ALA   C N     1 
ATOM   8222 C  CA    . ALA   D 1 244 ? 129.768 144.626 144.124 1.00 30.41  ? 220 ALA   C CA    1 
ATOM   8223 C  C     . ALA   D 1 244 ? 128.895 144.242 145.311 1.00 32.67  ? 220 ALA   C C     1 
ATOM   8224 O  O     . ALA   D 1 244 ? 128.753 143.052 145.632 1.00 36.61  ? 220 ALA   C O     1 
ATOM   8225 C  CB    . ALA   D 1 244 ? 131.114 145.171 144.599 1.00 21.43  ? 220 ALA   C CB    1 
ATOM   8226 N  N     . GLU   D 1 245 ? 128.286 145.232 145.972 1.00 33.40  ? 221 GLU   C N     1 
ATOM   8227 C  CA    . GLU   D 1 245 ? 127.457 144.935 147.134 1.00 31.04  ? 221 GLU   C CA    1 
ATOM   8228 C  C     . GLU   D 1 245 ? 126.226 144.125 146.745 1.00 40.20  ? 221 GLU   C C     1 
ATOM   8229 O  O     . GLU   D 1 245 ? 125.821 143.214 147.475 1.00 42.86  ? 221 GLU   C O     1 
ATOM   8230 C  CB    . GLU   D 1 245 ? 127.059 146.231 147.836 1.00 43.34  ? 221 GLU   C CB    1 
ATOM   8231 C  CG    . GLU   D 1 245 ? 128.214 146.922 148.547 1.00 44.71  ? 221 GLU   C CG    1 
ATOM   8232 C  CD    . GLU   D 1 245 ? 128.680 146.170 149.780 1.00 54.53  ? 221 GLU   C CD    1 
ATOM   8233 O  OE1   . GLU   D 1 245 ? 129.706 145.464 149.697 1.00 46.53  ? 221 GLU   C OE1   1 
ATOM   8234 O  OE2   . GLU   D 1 245 ? 128.023 146.290 150.835 1.00 60.49  ? 221 GLU   C OE2   1 
ATOM   8235 N  N     . SER   D 1 246 ? 125.618 144.436 145.595 1.00 31.86  ? 222 SER   C N     1 
ATOM   8236 C  CA    . SER   D 1 246 ? 124.451 143.686 145.148 1.00 24.57  ? 222 SER   C CA    1 
ATOM   8237 C  C     . SER   D 1 246 ? 124.811 142.246 144.809 1.00 35.36  ? 222 SER   C C     1 
ATOM   8238 O  O     . SER   D 1 246 ? 124.063 141.320 145.142 1.00 33.84  ? 222 SER   C O     1 
ATOM   8239 C  CB    . SER   D 1 246 ? 123.816 144.384 143.948 1.00 24.94  ? 222 SER   C CB    1 
ATOM   8240 O  OG    . SER   D 1 246 ? 124.730 144.476 142.871 1.00 34.60  ? 222 SER   C OG    1 
ATOM   8241 N  N     . TYR   D 1 247 ? 125.952 142.034 144.144 1.00 46.33  ? 223 TYR   C N     1 
ATOM   8242 C  CA    . TYR   D 1 247 ? 126.393 140.670 143.867 1.00 36.67  ? 223 TYR   C CA    1 
ATOM   8243 C  C     . TYR   D 1 247 ? 126.615 139.890 145.156 1.00 38.88  ? 223 TYR   C C     1 
ATOM   8244 O  O     . TYR   D 1 247 ? 126.189 138.734 145.275 1.00 41.72  ? 223 TYR   C O     1 
ATOM   8245 C  CB    . TYR   D 1 247 ? 127.678 140.687 143.040 1.00 41.64  ? 223 TYR   C CB    1 
ATOM   8246 C  CG    . TYR   D 1 247 ? 127.480 140.698 141.542 1.00 46.62  ? 223 TYR   C CG    1 
ATOM   8247 C  CD1   . TYR   D 1 247 ? 126.723 141.683 140.926 1.00 39.01  ? 223 TYR   C CD1   1 
ATOM   8248 C  CD2   . TYR   D 1 247 ? 128.066 139.728 140.744 1.00 48.65  ? 223 TYR   C CD2   1 
ATOM   8249 C  CE1   . TYR   D 1 247 ? 126.551 141.694 139.557 1.00 40.20  ? 223 TYR   C CE1   1 
ATOM   8250 C  CE2   . TYR   D 1 247 ? 127.901 139.733 139.377 1.00 44.39  ? 223 TYR   C CE2   1 
ATOM   8251 C  CZ    . TYR   D 1 247 ? 127.144 140.717 138.788 1.00 43.83  ? 223 TYR   C CZ    1 
ATOM   8252 O  OH    . TYR   D 1 247 ? 126.979 140.721 137.424 1.00 57.11  ? 223 TYR   C OH    1 
ATOM   8253 N  N     . ARG   D 1 248 ? 127.281 140.508 146.135 1.00 71.36  ? 224 ARG   C N     1 
ATOM   8254 C  CA    . ARG   D 1 248 ? 127.525 139.822 147.399 1.00 62.51  ? 224 ARG   C CA    1 
ATOM   8255 C  C     . ARG   D 1 248 ? 126.222 139.503 148.121 1.00 55.53  ? 224 ARG   C C     1 
ATOM   8256 O  O     . ARG   D 1 248 ? 126.071 138.416 148.689 1.00 58.41  ? 224 ARG   C O     1 
ATOM   8257 C  CB    . ARG   D 1 248 ? 128.440 140.663 148.286 1.00 69.08  ? 224 ARG   C CB    1 
ATOM   8258 C  CG    . ARG   D 1 248 ? 129.903 140.554 147.918 1.00 68.40  ? 224 ARG   C CG    1 
ATOM   8259 C  CD    . ARG   D 1 248 ? 130.741 141.551 148.686 1.00 68.10  ? 224 ARG   C CD    1 
ATOM   8260 N  NE    . ARG   D 1 248 ? 132.111 141.591 148.193 1.00 62.40  ? 224 ARG   C NE    1 
ATOM   8261 C  CZ    . ARG   D 1 248 ? 132.787 142.706 147.957 1.00 65.71  ? 224 ARG   C CZ    1 
ATOM   8262 N  NH1   . ARG   D 1 248 ? 132.251 143.896 148.165 1.00 69.31  ? 224 ARG   C NH1   1 
ATOM   8263 N  NH2   . ARG   D 1 248 ? 134.033 142.624 147.503 1.00 70.49  ? 224 ARG   C NH2   1 
ATOM   8264 N  N     . ALA   D 1 249 ? 125.269 140.437 148.114 1.00 38.99  ? 225 ALA   C N     1 
ATOM   8265 C  CA    . ALA   D 1 249 ? 123.981 140.186 148.754 1.00 39.41  ? 225 ALA   C CA    1 
ATOM   8266 C  C     . ALA   D 1 249 ? 123.240 139.045 148.071 1.00 41.58  ? 225 ALA   C C     1 
ATOM   8267 O  O     . ALA   D 1 249 ? 122.642 138.191 148.735 1.00 40.20  ? 225 ALA   C O     1 
ATOM   8268 C  CB    . ALA   D 1 249 ? 123.135 141.458 148.747 1.00 32.75  ? 225 ALA   C CB    1 
ATOM   8269 N  N     . ALA   D 1 250 ? 123.261 139.019 146.737 1.00 55.19  ? 226 ALA   C N     1 
ATOM   8270 C  CA    . ALA   D 1 250 ? 122.563 137.965 146.009 1.00 31.89  ? 226 ALA   C CA    1 
ATOM   8271 C  C     . ALA   D 1 250 ? 123.186 136.598 146.262 1.00 37.53  ? 226 ALA   C C     1 
ATOM   8272 O  O     . ALA   D 1 250 ? 122.469 135.607 146.440 1.00 41.08  ? 226 ALA   C O     1 
ATOM   8273 C  CB    . ALA   D 1 250 ? 122.555 138.279 144.513 1.00 22.00  ? 226 ALA   C CB    1 
ATOM   8274 N  N     . ILE   D 1 251 ? 124.514 136.520 146.287 1.00 41.92  ? 227 ILE   C N     1 
ATOM   8275 C  CA    . ILE   D 1 251 ? 125.186 135.223 146.322 1.00 27.49  ? 227 ILE   C CA    1 
ATOM   8276 C  C     . ILE   D 1 251 ? 125.555 134.812 147.743 1.00 37.24  ? 227 ILE   C C     1 
ATOM   8277 O  O     . ILE   D 1 251 ? 125.341 133.664 148.140 1.00 45.49  ? 227 ILE   C O     1 
ATOM   8278 C  CB    . ILE   D 1 251 ? 126.425 135.247 145.401 1.00 25.21  ? 227 ILE   C CB    1 
ATOM   8279 C  CG1   . ILE   D 1 251 ? 126.029 135.699 143.995 1.00 29.69  ? 227 ILE   C CG1   1 
ATOM   8280 C  CG2   . ILE   D 1 251 ? 127.079 133.879 145.356 1.00 30.91  ? 227 ILE   C CG2   1 
ATOM   8281 C  CD1   . ILE   D 1 251 ? 127.161 135.663 142.997 1.00 38.12  ? 227 ILE   C CD1   1 
ATOM   8282 N  N     . LEU   D 1 252 ? 126.110 135.726 148.539 1.00 40.54  ? 228 LEU   C N     1 
ATOM   8283 C  CA    . LEU   D 1 252 ? 126.684 135.375 149.835 1.00 25.45  ? 228 LEU   C CA    1 
ATOM   8284 C  C     . LEU   D 1 252 ? 125.746 135.620 151.011 1.00 35.89  ? 228 LEU   C C     1 
ATOM   8285 O  O     . LEU   D 1 252 ? 125.528 134.717 151.823 1.00 31.10  ? 228 LEU   C O     1 
ATOM   8286 C  CB    . LEU   D 1 252 ? 127.987 136.152 150.055 1.00 27.69  ? 228 LEU   C CB    1 
ATOM   8287 C  CG    . LEU   D 1 252 ? 129.216 135.755 149.237 1.00 28.80  ? 228 LEU   C CG    1 
ATOM   8288 C  CD1   . LEU   D 1 252 ? 130.300 136.801 149.396 1.00 23.03  ? 228 LEU   C CD1   1 
ATOM   8289 C  CD2   . LEU   D 1 252 ? 129.723 134.389 149.654 1.00 37.52  ? 228 LEU   C CD2   1 
ATOM   8290 N  N     . TYR   D 1 253 ? 125.188 136.823 151.126 1.00 44.21  ? 229 TYR   C N     1 
ATOM   8291 C  CA    . TYR   D 1 253 ? 124.566 137.265 152.367 1.00 33.73  ? 229 TYR   C CA    1 
ATOM   8292 C  C     . TYR   D 1 253 ? 123.123 136.808 152.541 1.00 42.08  ? 229 TYR   C C     1 
ATOM   8293 O  O     . TYR   D 1 253 ? 122.594 136.919 153.654 1.00 48.63  ? 229 TYR   C O     1 
ATOM   8294 C  CB    . TYR   D 1 253 ? 124.624 138.793 152.467 1.00 28.06  ? 229 TYR   C CB    1 
ATOM   8295 C  CG    . TYR   D 1 253 ? 126.026 139.350 152.551 1.00 40.91  ? 229 TYR   C CG    1 
ATOM   8296 C  CD1   . TYR   D 1 253 ? 127.075 138.577 153.023 1.00 46.23  ? 229 TYR   C CD1   1 
ATOM   8297 C  CD2   . TYR   D 1 253 ? 126.300 140.651 152.154 1.00 42.52  ? 229 TYR   C CD2   1 
ATOM   8298 C  CE1   . TYR   D 1 253 ? 128.357 139.083 153.097 1.00 44.41  ? 229 TYR   C CE1   1 
ATOM   8299 C  CE2   . TYR   D 1 253 ? 127.579 141.163 152.223 1.00 39.31  ? 229 TYR   C CE2   1 
ATOM   8300 C  CZ    . TYR   D 1 253 ? 128.603 140.376 152.697 1.00 46.94  ? 229 TYR   C CZ    1 
ATOM   8301 O  OH    . TYR   D 1 253 ? 129.879 140.884 152.770 1.00 53.57  ? 229 TYR   C OH    1 
ATOM   8302 N  N     . HIS   D 1 254 ? 122.476 136.302 151.490 1.00 47.67  ? 230 HIS   C N     1 
ATOM   8303 C  CA    . HIS   D 1 254 ? 121.077 135.869 151.548 1.00 47.79  ? 230 HIS   C CA    1 
ATOM   8304 C  C     . HIS   D 1 254 ? 120.172 137.007 152.029 1.00 54.98  ? 230 HIS   C C     1 
ATOM   8305 O  O     . HIS   D 1 254 ? 119.541 136.933 153.085 1.00 57.71  ? 230 HIS   C O     1 
ATOM   8306 C  CB    . HIS   D 1 254 ? 120.913 134.631 152.438 1.00 50.29  ? 230 HIS   C CB    1 
ATOM   8307 C  CG    . HIS   D 1 254 ? 121.673 133.433 151.964 1.00 60.00  ? 230 HIS   C CG    1 
ATOM   8308 N  ND1   . HIS   D 1 254 ? 121.702 133.043 150.643 1.00 67.09  ? 230 HIS   C ND1   1 
ATOM   8309 C  CD2   . HIS   D 1 254 ? 122.426 132.531 152.638 1.00 55.46  ? 230 HIS   C CD2   1 
ATOM   8310 C  CE1   . HIS   D 1 254 ? 122.445 131.958 150.522 1.00 60.26  ? 230 HIS   C CE1   1 
ATOM   8311 N  NE2   . HIS   D 1 254 ? 122.896 131.626 151.719 1.00 59.26  ? 230 HIS   C NE2   1 
ATOM   8312 N  N     . GLU   D 1 255 ? 120.118 138.070 151.231 1.00 55.90  ? 231 GLU   C N     1 
ATOM   8313 C  CA    . GLU   D 1 255 ? 119.384 139.267 151.614 1.00 45.77  ? 231 GLU   C CA    1 
ATOM   8314 C  C     . GLU   D 1 255 ? 118.812 139.937 150.374 1.00 52.28  ? 231 GLU   C C     1 
ATOM   8315 O  O     . GLU   D 1 255 ? 119.478 140.008 149.338 1.00 60.71  ? 231 GLU   C O     1 
ATOM   8316 C  CB    . GLU   D 1 255 ? 120.295 140.236 152.379 1.00 47.27  ? 231 GLU   C CB    1 
ATOM   8317 C  CG    . GLU   D 1 255 ? 119.892 141.697 152.298 1.00 56.17  ? 231 GLU   C CG    1 
ATOM   8318 C  CD    . GLU   D 1 255 ? 121.087 142.628 152.265 1.00 56.75  ? 231 GLU   C CD    1 
ATOM   8319 O  OE1   . GLU   D 1 255 ? 122.231 142.128 152.268 1.00 54.99  ? 231 GLU   C OE1   1 
ATOM   8320 O  OE2   . GLU   D 1 255 ? 120.882 143.860 152.235 1.00 54.50  ? 231 GLU   C OE2   1 
ATOM   8321 N  N     . TRP   D 1 256 ? 117.573 140.418 150.483 1.00 74.29  ? 232 TRP   C N     1 
ATOM   8322 C  CA    . TRP   D 1 256 ? 116.964 141.213 149.422 1.00 66.59  ? 232 TRP   C CA    1 
ATOM   8323 C  C     . TRP   D 1 256 ? 117.585 142.604 149.442 1.00 62.95  ? 232 TRP   C C     1 
ATOM   8324 O  O     . TRP   D 1 256 ? 117.263 143.423 150.306 1.00 72.71  ? 232 TRP   C O     1 
ATOM   8325 C  CB    . TRP   D 1 256 ? 115.452 141.294 149.609 1.00 69.02  ? 232 TRP   C CB    1 
ATOM   8326 C  CG    . TRP   D 1 256 ? 114.718 139.984 149.519 1.00 70.13  ? 232 TRP   C CG    1 
ATOM   8327 C  CD1   . TRP   D 1 256 ? 113.961 139.408 150.494 1.00 73.36  ? 232 TRP   C CD1   1 
ATOM   8328 C  CD2   . TRP   D 1 256 ? 114.650 139.103 148.388 1.00 73.57  ? 232 TRP   C CD2   1 
ATOM   8329 N  NE1   . TRP   D 1 256 ? 113.435 138.221 150.050 1.00 77.33  ? 232 TRP   C NE1   1 
ATOM   8330 C  CE2   . TRP   D 1 256 ? 113.844 138.010 148.760 1.00 73.09  ? 232 TRP   C CE2   1 
ATOM   8331 C  CE3   . TRP   D 1 256 ? 115.196 139.128 147.103 1.00 74.87  ? 232 TRP   C CE3   1 
ATOM   8332 C  CZ2   . TRP   D 1 256 ? 113.570 136.955 147.894 1.00 72.65  ? 232 TRP   C CZ2   1 
ATOM   8333 C  CZ3   . TRP   D 1 256 ? 114.923 138.078 146.245 1.00 67.13  ? 232 TRP   C CZ3   1 
ATOM   8334 C  CH2   . TRP   D 1 256 ? 114.118 137.007 146.643 1.00 67.81  ? 232 TRP   C CH2   1 
ATOM   8335 N  N     . TYR   D 1 257 ? 118.477 142.876 148.488 1.00 38.60  ? 233 TYR   C N     1 
ATOM   8336 C  CA    . TYR   D 1 257 ? 119.274 144.097 148.545 1.00 45.90  ? 233 TYR   C CA    1 
ATOM   8337 C  C     . TYR   D 1 257 ? 118.447 145.345 148.258 1.00 54.45  ? 233 TYR   C C     1 
ATOM   8338 O  O     . TYR   D 1 257 ? 118.740 146.415 148.801 1.00 52.12  ? 233 TYR   C O     1 
ATOM   8339 C  CB    . TYR   D 1 257 ? 120.441 144.000 147.563 1.00 45.26  ? 233 TYR   C CB    1 
ATOM   8340 C  CG    . TYR   D 1 257 ? 121.429 145.138 147.658 1.00 49.35  ? 233 TYR   C CG    1 
ATOM   8341 C  CD1   . TYR   D 1 257 ? 122.320 145.221 148.717 1.00 46.53  ? 233 TYR   C CD1   1 
ATOM   8342 C  CD2   . TYR   D 1 257 ? 121.476 146.125 146.686 1.00 46.82  ? 233 TYR   C CD2   1 
ATOM   8343 C  CE1   . TYR   D 1 257 ? 123.227 146.257 148.807 1.00 43.43  ? 233 TYR   C CE1   1 
ATOM   8344 C  CE2   . TYR   D 1 257 ? 122.379 147.163 146.767 1.00 49.50  ? 233 TYR   C CE2   1 
ATOM   8345 C  CZ    . TYR   D 1 257 ? 123.252 147.225 147.828 1.00 49.20  ? 233 TYR   C CZ    1 
ATOM   8346 O  OH    . TYR   D 1 257 ? 124.153 148.260 147.911 1.00 52.32  ? 233 TYR   C OH    1 
ATOM   8347 N  N     . PHE   D 1 258 ? 117.417 145.237 147.419 1.00 58.34  ? 234 PHE   C N     1 
ATOM   8348 C  CA    . PHE   D 1 258 ? 116.683 146.413 146.972 1.00 34.50  ? 234 PHE   C CA    1 
ATOM   8349 C  C     . PHE   D 1 258 ? 115.721 146.965 148.017 1.00 43.87  ? 234 PHE   C C     1 
ATOM   8350 O  O     . PHE   D 1 258 ? 115.200 148.068 147.826 1.00 56.71  ? 234 PHE   C O     1 
ATOM   8351 C  CB    . PHE   D 1 258 ? 115.909 146.100 145.689 1.00 39.79  ? 234 PHE   C CB    1 
ATOM   8352 C  CG    . PHE   D 1 258 ? 115.150 144.805 145.734 1.00 44.57  ? 234 PHE   C CG    1 
ATOM   8353 C  CD1   . PHE   D 1 258 ? 113.938 144.719 146.395 1.00 43.46  ? 234 PHE   C CD1   1 
ATOM   8354 C  CD2   . PHE   D 1 258 ? 115.644 143.678 145.104 1.00 44.00  ? 234 PHE   C CD2   1 
ATOM   8355 C  CE1   . PHE   D 1 258 ? 113.239 143.532 146.435 1.00 37.67  ? 234 PHE   C CE1   1 
ATOM   8356 C  CE2   . PHE   D 1 258 ? 114.947 142.489 145.139 1.00 46.10  ? 234 PHE   C CE2   1 
ATOM   8357 C  CZ    . PHE   D 1 258 ? 113.743 142.417 145.807 1.00 43.90  ? 234 PHE   C CZ    1 
ATOM   8358 N  N     . MET   D 1 259 ? 115.461 146.236 149.102 1.00 71.45  ? 235 MET   C N     1 
ATOM   8359 C  CA    . MET   D 1 259 ? 114.548 146.740 150.123 1.00 73.11  ? 235 MET   C CA    1 
ATOM   8360 C  C     . MET   D 1 259 ? 115.187 147.823 150.981 1.00 76.52  ? 235 MET   C C     1 
ATOM   8361 O  O     . MET   D 1 259 ? 114.490 148.732 151.442 1.00 76.24  ? 235 MET   C O     1 
ATOM   8362 C  CB    . MET   D 1 259 ? 114.057 145.598 151.011 1.00 69.63  ? 235 MET   C CB    1 
ATOM   8363 C  CG    . MET   D 1 259 ? 113.687 144.339 150.257 1.00 73.96  ? 235 MET   C CG    1 
ATOM   8364 S  SD    . MET   D 1 259 ? 111.981 144.364 149.680 1.00 83.88  ? 235 MET   C SD    1 
ATOM   8365 C  CE    . MET   D 1 259 ? 111.181 145.209 151.040 1.00 76.14  ? 235 MET   C CE    1 
ATOM   8366 N  N     . ASP   D 1 260 ? 116.497 147.744 151.207 1.00 79.12  ? 236 ASP   C N     1 
ATOM   8367 C  CA    . ASP   D 1 260 ? 117.184 148.688 152.075 1.00 79.51  ? 236 ASP   C CA    1 
ATOM   8368 C  C     . ASP   D 1 260 ? 117.950 149.766 151.319 1.00 81.54  ? 236 ASP   C C     1 
ATOM   8369 O  O     . ASP   D 1 260 ? 118.281 150.795 151.915 1.00 80.60  ? 236 ASP   C O     1 
ATOM   8370 C  CB    . ASP   D 1 260 ? 118.156 147.940 152.997 1.00 80.69  ? 236 ASP   C CB    1 
ATOM   8371 C  CG    . ASP   D 1 260 ? 118.166 148.495 154.406 1.00 83.57  ? 236 ASP   C CG    1 
ATOM   8372 O  OD1   . ASP   D 1 260 ? 118.782 149.559 154.624 1.00 85.03  ? 236 ASP   C OD1   1 
ATOM   8373 O  OD2   . ASP   D 1 260 ? 117.559 147.865 155.297 1.00 83.25  ? 236 ASP   C OD2   1 
ATOM   8374 N  N     . HIS   D 1 261 ? 118.234 149.562 150.035 1.00 67.43  ? 237 HIS   C N     1 
ATOM   8375 C  CA    . HIS   D 1 261 ? 119.084 150.459 149.259 1.00 58.93  ? 237 HIS   C CA    1 
ATOM   8376 C  C     . HIS   D 1 261 ? 118.460 150.768 147.903 1.00 59.47  ? 237 HIS   C C     1 
ATOM   8377 O  O     . HIS   D 1 261 ? 119.114 150.688 146.862 1.00 68.56  ? 237 HIS   C O     1 
ATOM   8378 C  CB    . HIS   D 1 261 ? 120.475 149.861 149.074 1.00 55.83  ? 237 HIS   C CB    1 
ATOM   8379 C  CG    . HIS   D 1 261 ? 121.153 149.493 150.357 1.00 60.09  ? 237 HIS   C CG    1 
ATOM   8380 N  ND1   . HIS   D 1 261 ? 120.943 148.287 150.989 1.00 59.21  ? 237 HIS   C ND1   1 
ATOM   8381 C  CD2   . HIS   D 1 261 ? 122.044 150.167 151.120 1.00 62.33  ? 237 HIS   C CD2   1 
ATOM   8382 C  CE1   . HIS   D 1 261 ? 121.671 148.236 152.089 1.00 58.91  ? 237 HIS   C CE1   1 
ATOM   8383 N  NE2   . HIS   D 1 261 ? 122.349 149.364 152.192 1.00 63.90  ? 237 HIS   C NE2   1 
ATOM   8384 N  N     . TRP   D 1 262 ? 117.174 151.122 147.892 1.00 63.01  ? 238 TRP   C N     1 
ATOM   8385 C  CA    . TRP   D 1 262 ? 116.535 151.506 146.638 1.00 66.24  ? 238 TRP   C CA    1 
ATOM   8386 C  C     . TRP   D 1 262 ? 116.955 152.895 146.168 1.00 72.54  ? 238 TRP   C C     1 
ATOM   8387 O  O     . TRP   D 1 262 ? 116.858 153.189 144.969 1.00 76.83  ? 238 TRP   C O     1 
ATOM   8388 C  CB    . TRP   D 1 262 ? 115.011 151.434 146.769 1.00 67.57  ? 238 TRP   C CB    1 
ATOM   8389 C  CG    . TRP   D 1 262 ? 114.446 152.168 147.947 1.00 75.66  ? 238 TRP   C CG    1 
ATOM   8390 C  CD1   . TRP   D 1 262 ? 114.389 151.726 149.237 1.00 75.97  ? 238 TRP   C CD1   1 
ATOM   8391 C  CD2   . TRP   D 1 262 ? 113.830 153.462 147.939 1.00 76.60  ? 238 TRP   C CD2   1 
ATOM   8392 N  NE1   . TRP   D 1 262 ? 113.790 152.669 150.035 1.00 78.88  ? 238 TRP   C NE1   1 
ATOM   8393 C  CE2   . TRP   D 1 262 ? 113.436 153.744 149.262 1.00 75.22  ? 238 TRP   C CE2   1 
ATOM   8394 C  CE3   . TRP   D 1 262 ? 113.579 154.410 146.945 1.00 73.27  ? 238 TRP   C CE3   1 
ATOM   8395 C  CZ2   . TRP   D 1 262 ? 112.807 154.934 149.615 1.00 71.75  ? 238 TRP   C CZ2   1 
ATOM   8396 C  CZ3   . TRP   D 1 262 ? 112.955 155.591 147.297 1.00 69.30  ? 238 TRP   C CZ3   1 
ATOM   8397 C  CH2   . TRP   D 1 262 ? 112.575 155.843 148.620 1.00 69.87  ? 238 TRP   C CH2   1 
ATOM   8398 N  N     . LYS   D 1 263 ? 117.428 153.747 147.081 1.00 65.91  ? 239 LYS   C N     1 
ATOM   8399 C  CA    . LYS   D 1 263 ? 117.946 155.051 146.682 1.00 56.19  ? 239 LYS   C CA    1 
ATOM   8400 C  C     . LYS   D 1 263 ? 119.166 154.906 145.781 1.00 61.08  ? 239 LYS   C C     1 
ATOM   8401 O  O     . LYS   D 1 263 ? 119.296 155.625 144.783 1.00 72.22  ? 239 LYS   C O     1 
ATOM   8402 C  CB    . LYS   D 1 263 ? 118.284 155.879 147.921 1.00 62.32  ? 239 LYS   C CB    1 
ATOM   8403 C  CG    . LYS   D 1 263 ? 118.454 155.056 149.192 1.00 67.28  ? 239 LYS   C CG    1 
ATOM   8404 C  CD    . LYS   D 1 263 ? 119.893 154.590 149.367 1.00 68.15  ? 239 LYS   C CD    1 
ATOM   8405 C  CE    . LYS   D 1 263 ? 120.184 154.202 150.805 1.00 63.02  ? 239 LYS   C CE    1 
ATOM   8406 N  NZ    . LYS   D 1 263 ? 121.511 153.543 150.942 1.00 62.66  ? 239 LYS   C NZ    1 
ATOM   8407 N  N     . LEU   D 1 264 ? 120.070 153.983 146.119 1.00 51.25  ? 240 LEU   C N     1 
ATOM   8408 C  CA    . LEU   D 1 264 ? 121.220 153.718 145.260 1.00 53.40  ? 240 LEU   C CA    1 
ATOM   8409 C  C     . LEU   D 1 264 ? 120.782 153.183 143.904 1.00 56.48  ? 240 LEU   C C     1 
ATOM   8410 O  O     . LEU   D 1 264 ? 121.364 153.537 142.871 1.00 60.10  ? 240 LEU   C O     1 
ATOM   8411 C  CB    . LEU   D 1 264 ? 122.167 152.734 145.945 1.00 50.96  ? 240 LEU   C CB    1 
ATOM   8412 C  CG    . LEU   D 1 264 ? 123.180 153.322 146.926 1.00 57.16  ? 240 LEU   C CG    1 
ATOM   8413 C  CD1   . LEU   D 1 264 ? 124.067 152.229 147.491 1.00 55.27  ? 240 LEU   C CD1   1 
ATOM   8414 C  CD2   . LEU   D 1 264 ? 124.015 154.393 146.252 1.00 62.88  ? 240 LEU   C CD2   1 
ATOM   8415 N  N     . MET   D 1 265 ? 119.762 152.322 143.889 1.00 53.91  ? 241 MET   C N     1 
ATOM   8416 C  CA    . MET   D 1 265 ? 119.222 151.819 142.630 1.00 53.02  ? 241 MET   C CA    1 
ATOM   8417 C  C     . MET   D 1 265 ? 118.741 152.964 141.748 1.00 60.90  ? 241 MET   C C     1 
ATOM   8418 O  O     . MET   D 1 265 ? 119.081 153.035 140.560 1.00 71.80  ? 241 MET   C O     1 
ATOM   8419 C  CB    . MET   D 1 265 ? 118.078 150.844 142.909 1.00 57.44  ? 241 MET   C CB    1 
ATOM   8420 C  CG    . MET   D 1 265 ? 118.468 149.380 142.864 1.00 64.53  ? 241 MET   C CG    1 
ATOM   8421 S  SD    . MET   D 1 265 ? 117.035 148.288 142.802 1.00 72.14  ? 241 MET   C SD    1 
ATOM   8422 C  CE    . MET   D 1 265 ? 117.312 147.461 141.241 1.00 60.12  ? 241 MET   C CE    1 
ATOM   8423 N  N     . LEU   D 1 266 ? 117.949 153.875 142.318 1.00 44.41  ? 242 LEU   C N     1 
ATOM   8424 C  CA    . LEU   D 1 266 ? 117.431 154.996 141.539 1.00 41.83  ? 242 LEU   C CA    1 
ATOM   8425 C  C     . LEU   D 1 266 ? 118.553 155.911 141.063 1.00 49.48  ? 242 LEU   C C     1 
ATOM   8426 O  O     . LEU   D 1 266 ? 118.540 156.377 139.917 1.00 56.48  ? 242 LEU   C O     1 
ATOM   8427 C  CB    . LEU   D 1 266 ? 116.411 155.777 142.364 1.00 45.25  ? 242 LEU   C CB    1 
ATOM   8428 C  CG    . LEU   D 1 266 ? 115.104 155.048 142.680 1.00 47.55  ? 242 LEU   C CG    1 
ATOM   8429 C  CD1   . LEU   D 1 266 ? 114.149 155.960 143.426 1.00 47.09  ? 242 LEU   C CD1   1 
ATOM   8430 C  CD2   . LEU   D 1 266 ? 114.462 154.527 141.407 1.00 49.64  ? 242 LEU   C CD2   1 
ATOM   8431 N  N     . TYR   D 1 267 ? 119.536 156.176 141.928 1.00 43.22  ? 243 TYR   C N     1 
ATOM   8432 C  CA    . TYR   D 1 267 ? 120.647 157.041 141.548 1.00 38.64  ? 243 TYR   C CA    1 
ATOM   8433 C  C     . TYR   D 1 267 ? 121.449 156.441 140.399 1.00 48.47  ? 243 TYR   C C     1 
ATOM   8434 O  O     . TYR   D 1 267 ? 121.813 157.145 139.448 1.00 51.75  ? 243 TYR   C O     1 
ATOM   8435 C  CB    . TYR   D 1 267 ? 121.537 157.296 142.766 1.00 43.82  ? 243 TYR   C CB    1 
ATOM   8436 C  CG    . TYR   D 1 267 ? 122.957 157.703 142.447 1.00 52.44  ? 243 TYR   C CG    1 
ATOM   8437 C  CD1   . TYR   D 1 267 ? 123.241 158.957 141.924 1.00 51.51  ? 243 TYR   C CD1   1 
ATOM   8438 C  CD2   . TYR   D 1 267 ? 124.015 156.840 142.686 1.00 55.16  ? 243 TYR   C CD2   1 
ATOM   8439 C  CE1   . TYR   D 1 267 ? 124.538 159.334 141.638 1.00 49.58  ? 243 TYR   C CE1   1 
ATOM   8440 C  CE2   . TYR   D 1 267 ? 125.315 157.208 142.402 1.00 53.67  ? 243 TYR   C CE2   1 
ATOM   8441 C  CZ    . TYR   D 1 267 ? 125.570 158.455 141.878 1.00 49.31  ? 243 TYR   C CZ    1 
ATOM   8442 O  OH    . TYR   D 1 267 ? 126.864 158.823 141.596 1.00 44.77  ? 243 TYR   C OH    1 
ATOM   8443 N  N     . ASN   D 1 268 ? 121.712 155.134 140.452 1.00 55.25  ? 244 ASN   C N     1 
ATOM   8444 C  CA    . ASN   D 1 268 ? 122.465 154.495 139.379 1.00 51.51  ? 244 ASN   C CA    1 
ATOM   8445 C  C     . ASN   D 1 268 ? 121.659 154.418 138.088 1.00 52.80  ? 244 ASN   C C     1 
ATOM   8446 O  O     . ASN   D 1 268 ? 122.228 154.555 136.997 1.00 60.67  ? 244 ASN   C O     1 
ATOM   8447 C  CB    . ASN   D 1 268 ? 122.922 153.108 139.820 1.00 49.47  ? 244 ASN   C CB    1 
ATOM   8448 C  CG    . ASN   D 1 268 ? 124.069 153.167 140.804 1.00 55.51  ? 244 ASN   C CG    1 
ATOM   8449 O  OD1   . ASN   D 1 268 ? 125.236 153.143 140.418 1.00 61.11  ? 244 ASN   C OD1   1 
ATOM   8450 N  ND2   . ASN   D 1 268 ? 123.742 153.258 142.086 1.00 52.37  ? 244 ASN   C ND2   1 
ATOM   8451 N  N     . PHE   D 1 269 ? 120.343 154.210 138.184 1.00 51.87  ? 245 PHE   C N     1 
ATOM   8452 C  CA    . PHE   D 1 269 ? 119.513 154.244 136.984 1.00 53.07  ? 245 PHE   C CA    1 
ATOM   8453 C  C     . PHE   D 1 269 ? 119.554 155.621 136.333 1.00 60.62  ? 245 PHE   C C     1 
ATOM   8454 O  O     . PHE   D 1 269 ? 119.656 155.735 135.104 1.00 63.23  ? 245 PHE   C O     1 
ATOM   8455 C  CB    . PHE   D 1 269 ? 118.074 153.855 137.323 1.00 53.28  ? 245 PHE   C CB    1 
ATOM   8456 C  CG    . PHE   D 1 269 ? 117.899 152.401 137.673 1.00 60.05  ? 245 PHE   C CG    1 
ATOM   8457 C  CD1   . PHE   D 1 269 ? 118.963 151.517 137.597 1.00 61.64  ? 245 PHE   C CD1   1 
ATOM   8458 C  CD2   . PHE   D 1 269 ? 116.664 151.920 138.071 1.00 58.40  ? 245 PHE   C CD2   1 
ATOM   8459 C  CE1   . PHE   D 1 269 ? 118.798 150.184 137.921 1.00 59.38  ? 245 PHE   C CE1   1 
ATOM   8460 C  CE2   . PHE   D 1 269 ? 116.493 150.588 138.392 1.00 59.65  ? 245 PHE   C CE2   1 
ATOM   8461 C  CZ    . PHE   D 1 269 ? 117.562 149.720 138.316 1.00 62.10  ? 245 PHE   C CZ    1 
ATOM   8462 N  N     . GLY   D 1 270 ? 119.486 156.679 137.145 1.00 61.58  ? 246 GLY   C N     1 
ATOM   8463 C  CA    . GLY   D 1 270 ? 119.608 158.023 136.605 1.00 58.35  ? 246 GLY   C CA    1 
ATOM   8464 C  C     . GLY   D 1 270 ? 120.958 158.275 135.961 1.00 56.53  ? 246 GLY   C C     1 
ATOM   8465 O  O     . GLY   D 1 270 ? 121.046 158.917 134.910 1.00 66.93  ? 246 GLY   C O     1 
ATOM   8466 N  N     . ILE   D 1 271 ? 122.030 157.779 136.584 1.00 54.15  ? 247 ILE   C N     1 
ATOM   8467 C  CA    . ILE   D 1 271 ? 123.367 157.940 136.015 1.00 58.07  ? 247 ILE   C CA    1 
ATOM   8468 C  C     . ILE   D 1 271 ? 123.448 157.261 134.652 1.00 55.19  ? 247 ILE   C C     1 
ATOM   8469 O  O     . ILE   D 1 271 ? 123.975 157.826 133.682 1.00 59.22  ? 247 ILE   C O     1 
ATOM   8470 C  CB    . ILE   D 1 271 ? 124.431 157.394 136.984 1.00 56.50  ? 247 ILE   C CB    1 
ATOM   8471 C  CG1   . ILE   D 1 271 ? 124.755 158.430 138.060 1.00 60.52  ? 247 ILE   C CG1   1 
ATOM   8472 C  CG2   . ILE   D 1 271 ? 125.693 156.994 136.237 1.00 56.22  ? 247 ILE   C CG2   1 
ATOM   8473 C  CD1   . ILE   D 1 271 ? 125.161 159.776 137.508 1.00 59.43  ? 247 ILE   C CD1   1 
ATOM   8474 N  N     . VAL   D 1 272 ? 122.924 156.035 134.559 1.00 54.25  ? 248 VAL   C N     1 
ATOM   8475 C  CA    . VAL   D 1 272 ? 122.953 155.308 133.293 1.00 55.01  ? 248 VAL   C CA    1 
ATOM   8476 C  C     . VAL   D 1 272 ? 122.144 156.041 132.229 1.00 57.95  ? 248 VAL   C C     1 
ATOM   8477 O  O     . VAL   D 1 272 ? 122.582 156.158 131.076 1.00 58.81  ? 248 VAL   C O     1 
ATOM   8478 C  CB    . VAL   D 1 272 ? 122.452 153.865 133.499 1.00 54.56  ? 248 VAL   C CB    1 
ATOM   8479 C  CG1   . VAL   D 1 272 ? 121.842 153.313 132.220 1.00 52.06  ? 248 VAL   C CG1   1 
ATOM   8480 C  CG2   . VAL   D 1 272 ? 123.586 152.976 133.976 1.00 54.17  ? 248 VAL   C CG2   1 
ATOM   8481 N  N     . ALA   D 1 273 ? 120.962 156.549 132.590 1.00 53.02  ? 249 ALA   C N     1 
ATOM   8482 C  CA    . ALA   D 1 273 ? 120.144 157.276 131.622 1.00 49.86  ? 249 ALA   C CA    1 
ATOM   8483 C  C     . ALA   D 1 273 ? 120.845 158.537 131.130 1.00 52.86  ? 249 ALA   C C     1 
ATOM   8484 O  O     . ALA   D 1 273 ? 120.817 158.839 129.931 1.00 57.86  ? 249 ALA   C O     1 
ATOM   8485 C  CB    . ALA   D 1 273 ? 118.789 157.621 132.234 1.00 51.23  ? 249 ALA   C CB    1 
ATOM   8486 N  N     . ILE   D 1 274 ? 121.476 159.285 132.039 1.00 59.55  ? 250 ILE   C N     1 
ATOM   8487 C  CA    . ILE   D 1 274 ? 122.178 160.504 131.643 1.00 56.31  ? 250 ILE   C CA    1 
ATOM   8488 C  C     . ILE   D 1 274 ? 123.332 160.177 130.703 1.00 58.01  ? 250 ILE   C C     1 
ATOM   8489 O  O     . ILE   D 1 274 ? 123.528 160.846 129.676 1.00 66.56  ? 250 ILE   C O     1 
ATOM   8490 C  CB    . ILE   D 1 274 ? 122.657 161.270 132.889 1.00 53.53  ? 250 ILE   C CB    1 
ATOM   8491 C  CG1   . ILE   D 1 274 ? 121.529 162.142 133.443 1.00 61.57  ? 250 ILE   C CG1   1 
ATOM   8492 C  CG2   . ILE   D 1 274 ? 123.878 162.116 132.570 1.00 52.81  ? 250 ILE   C CG2   1 
ATOM   8493 C  CD1   . ILE   D 1 274 ? 121.833 162.747 134.794 1.00 59.46  ? 250 ILE   C CD1   1 
ATOM   8494 N  N     . PHE   D 1 275 ? 124.114 159.145 131.037 1.00 56.71  ? 251 PHE   C N     1 
ATOM   8495 C  CA    . PHE   D 1 275 ? 125.222 158.752 130.171 1.00 50.33  ? 251 PHE   C CA    1 
ATOM   8496 C  C     . PHE   D 1 275 ? 124.723 158.357 128.788 1.00 52.70  ? 251 PHE   C C     1 
ATOM   8497 O  O     . PHE   D 1 275 ? 125.292 158.776 127.773 1.00 52.74  ? 251 PHE   C O     1 
ATOM   8498 C  CB    . PHE   D 1 275 ? 126.003 157.602 130.803 1.00 51.47  ? 251 PHE   C CB    1 
ATOM   8499 C  CG    . PHE   D 1 275 ? 127.270 158.030 131.483 1.00 54.16  ? 251 PHE   C CG    1 
ATOM   8500 C  CD1   . PHE   D 1 275 ? 128.407 158.307 130.746 1.00 63.20  ? 251 PHE   C CD1   1 
ATOM   8501 C  CD2   . PHE   D 1 275 ? 127.326 158.146 132.861 1.00 53.26  ? 251 PHE   C CD2   1 
ATOM   8502 C  CE1   . PHE   D 1 275 ? 129.575 158.699 131.369 1.00 63.84  ? 251 PHE   C CE1   1 
ATOM   8503 C  CE2   . PHE   D 1 275 ? 128.491 158.537 133.489 1.00 57.38  ? 251 PHE   C CE2   1 
ATOM   8504 C  CZ    . PHE   D 1 275 ? 129.617 158.813 132.742 1.00 62.20  ? 251 PHE   C CZ    1 
ATOM   8505 N  N     . PHE   D 1 276 ? 123.650 157.563 128.728 1.00 64.59  ? 252 PHE   C N     1 
ATOM   8506 C  CA    . PHE   D 1 276 ? 123.118 157.140 127.437 1.00 62.96  ? 252 PHE   C CA    1 
ATOM   8507 C  C     . PHE   D 1 276 ? 122.633 158.327 126.617 1.00 66.88  ? 252 PHE   C C     1 
ATOM   8508 O  O     . PHE   D 1 276 ? 122.904 158.406 125.413 1.00 70.86  ? 252 PHE   C O     1 
ATOM   8509 C  CB    . PHE   D 1 276 ? 121.987 156.133 127.636 1.00 59.91  ? 252 PHE   C CB    1 
ATOM   8510 C  CG    . PHE   D 1 276 ? 121.346 155.684 126.356 1.00 63.15  ? 252 PHE   C CG    1 
ATOM   8511 C  CD1   . PHE   D 1 276 ? 122.089 155.042 125.381 1.00 68.78  ? 252 PHE   C CD1   1 
ATOM   8512 C  CD2   . PHE   D 1 276 ? 120.001 155.907 126.124 1.00 64.45  ? 252 PHE   C CD2   1 
ATOM   8513 C  CE1   . PHE   D 1 276 ? 121.500 154.629 124.201 1.00 68.80  ? 252 PHE   C CE1   1 
ATOM   8514 C  CE2   . PHE   D 1 276 ? 119.407 155.497 124.947 1.00 63.75  ? 252 PHE   C CE2   1 
ATOM   8515 C  CZ    . PHE   D 1 276 ? 120.158 154.856 123.985 1.00 63.88  ? 252 PHE   C CZ    1 
ATOM   8516 N  N     . ALA   D 1 277 ? 121.917 159.262 127.248 1.00 66.52  ? 253 ALA   C N     1 
ATOM   8517 C  CA    . ALA   D 1 277 ? 121.396 160.411 126.514 1.00 61.21  ? 253 ALA   C CA    1 
ATOM   8518 C  C     . ALA   D 1 277 ? 122.525 161.264 125.948 1.00 66.33  ? 253 ALA   C C     1 
ATOM   8519 O  O     . ALA   D 1 277 ? 122.515 161.620 124.760 1.00 74.00  ? 253 ALA   C O     1 
ATOM   8520 C  CB    . ALA   D 1 277 ? 120.492 161.246 127.423 1.00 61.03  ? 253 ALA   C CB    1 
ATOM   8521 N  N     . ILE   D 1 278 ? 123.513 161.596 126.784 1.00 60.16  ? 254 ILE   C N     1 
ATOM   8522 C  CA    . ILE   D 1 278 ? 124.615 162.434 126.317 1.00 54.18  ? 254 ILE   C CA    1 
ATOM   8523 C  C     . ILE   D 1 278 ? 125.396 161.729 125.214 1.00 57.22  ? 254 ILE   C C     1 
ATOM   8524 O  O     . ILE   D 1 278 ? 125.741 162.340 124.192 1.00 60.52  ? 254 ILE   C O     1 
ATOM   8525 C  CB    . ILE   D 1 278 ? 125.522 162.832 127.494 1.00 59.80  ? 254 ILE   C CB    1 
ATOM   8526 C  CG1   . ILE   D 1 278 ? 124.761 163.728 128.471 1.00 56.86  ? 254 ILE   C CG1   1 
ATOM   8527 C  CG2   . ILE   D 1 278 ? 126.768 163.542 126.992 1.00 63.29  ? 254 ILE   C CG2   1 
ATOM   8528 C  CD1   . ILE   D 1 278 ? 125.600 164.210 129.631 1.00 59.19  ? 254 ILE   C CD1   1 
ATOM   8529 N  N     . GLY   D 1 279 ? 125.681 160.437 125.395 1.00 60.48  ? 255 GLY   C N     1 
ATOM   8530 C  CA    . GLY   D 1 279 ? 126.422 159.708 124.382 1.00 56.20  ? 255 GLY   C CA    1 
ATOM   8531 C  C     . GLY   D 1 279 ? 125.690 159.630 123.059 1.00 58.64  ? 255 GLY   C C     1 
ATOM   8532 O  O     . GLY   D 1 279 ? 126.290 159.830 122.000 1.00 65.40  ? 255 GLY   C O     1 
ATOM   8533 N  N     . ALA   D 1 280 ? 124.385 159.347 123.095 1.00 61.08  ? 256 ALA   C N     1 
ATOM   8534 C  CA    . ALA   D 1 280 ? 123.613 159.278 121.859 1.00 58.79  ? 256 ALA   C CA    1 
ATOM   8535 C  C     . ALA   D 1 280 ? 123.579 160.624 121.149 1.00 63.38  ? 256 ALA   C C     1 
ATOM   8536 O  O     . ALA   D 1 280 ? 123.771 160.690 119.928 1.00 66.74  ? 256 ALA   C O     1 
ATOM   8537 C  CB    . ALA   D 1 280 ? 122.196 158.789 122.152 1.00 58.36  ? 256 ALA   C CB    1 
ATOM   8538 N  N     . TYR   D 1 281 ? 123.343 161.710 121.893 1.00 67.06  ? 257 TYR   C N     1 
ATOM   8539 C  CA    . TYR   D 1 281 ? 123.289 163.023 121.258 1.00 65.58  ? 257 TYR   C CA    1 
ATOM   8540 C  C     . TYR   D 1 281 ? 124.626 163.382 120.619 1.00 67.95  ? 257 TYR   C C     1 
ATOM   8541 O  O     . TYR   D 1 281 ? 124.677 163.821 119.463 1.00 72.25  ? 257 TYR   C O     1 
ATOM   8542 C  CB    . TYR   D 1 281 ? 122.876 164.087 122.274 1.00 69.32  ? 257 TYR   C CB    1 
ATOM   8543 C  CG    . TYR   D 1 281 ? 123.010 165.499 121.750 1.00 74.65  ? 257 TYR   C CG    1 
ATOM   8544 C  CD1   . TYR   D 1 281 ? 122.211 165.952 120.709 1.00 69.35  ? 257 TYR   C CD1   1 
ATOM   8545 C  CD2   . TYR   D 1 281 ? 123.937 166.377 122.293 1.00 73.93  ? 257 TYR   C CD2   1 
ATOM   8546 C  CE1   . TYR   D 1 281 ? 122.330 167.238 120.226 1.00 66.33  ? 257 TYR   C CE1   1 
ATOM   8547 C  CE2   . TYR   D 1 281 ? 124.063 167.667 121.815 1.00 73.25  ? 257 TYR   C CE2   1 
ATOM   8548 C  CZ    . TYR   D 1 281 ? 123.257 168.092 120.782 1.00 71.60  ? 257 TYR   C CZ    1 
ATOM   8549 O  OH    . TYR   D 1 281 ? 123.378 169.375 120.303 1.00 71.99  ? 257 TYR   C OH    1 
ATOM   8550 N  N     . LEU   D 1 282 ? 125.726 163.185 121.353 1.00 69.65  ? 258 LEU   C N     1 
ATOM   8551 C  CA    . LEU   D 1 282 ? 127.037 163.527 120.809 1.00 64.99  ? 258 LEU   C CA    1 
ATOM   8552 C  C     . LEU   D 1 282 ? 127.394 162.648 119.616 1.00 68.08  ? 258 LEU   C C     1 
ATOM   8553 O  O     . LEU   D 1 282 ? 127.986 163.129 118.643 1.00 64.82  ? 258 LEU   C O     1 
ATOM   8554 C  CB    . LEU   D 1 282 ? 128.103 163.422 121.897 1.00 64.42  ? 258 LEU   C CB    1 
ATOM   8555 C  CG    . LEU   D 1 282 ? 128.651 164.759 122.398 1.00 71.42  ? 258 LEU   C CG    1 
ATOM   8556 C  CD1   . LEU   D 1 282 ? 127.518 165.703 122.760 1.00 69.56  ? 258 LEU   C CD1   1 
ATOM   8557 C  CD2   . LEU   D 1 282 ? 129.576 164.550 123.583 1.00 72.30  ? 258 LEU   C CD2   1 
ATOM   8558 N  N     . HIS   D 1 283 ? 127.051 161.358 119.671 1.00 77.26  ? 259 HIS   C N     1 
ATOM   8559 C  CA    . HIS   D 1 283 ? 127.343 160.470 118.553 1.00 71.83  ? 259 HIS   C CA    1 
ATOM   8560 C  C     . HIS   D 1 283 ? 126.570 160.874 117.307 1.00 75.73  ? 259 HIS   C C     1 
ATOM   8561 O  O     . HIS   D 1 283 ? 127.121 160.860 116.200 1.00 82.26  ? 259 HIS   C O     1 
ATOM   8562 C  CB    . HIS   D 1 283 ? 127.023 159.025 118.933 1.00 69.20  ? 259 HIS   C CB    1 
ATOM   8563 C  CG    . HIS   D 1 283 ? 127.134 158.063 117.793 1.00 73.03  ? 259 HIS   C CG    1 
ATOM   8564 N  ND1   . HIS   D 1 283 ? 128.340 157.562 117.356 1.00 75.27  ? 259 HIS   C ND1   1 
ATOM   8565 C  CD2   . HIS   D 1 283 ? 126.187 157.510 116.998 1.00 74.59  ? 259 HIS   C CD2   1 
ATOM   8566 C  CE1   . HIS   D 1 283 ? 128.134 156.741 116.342 1.00 76.54  ? 259 HIS   C CE1   1 
ATOM   8567 N  NE2   . HIS   D 1 283 ? 126.836 156.692 116.105 1.00 77.96  ? 259 HIS   C NE2   1 
ATOM   8568 N  N     . MET   D 1 284 ? 125.295 161.236 117.459 1.00 87.29  ? 260 MET   C N     1 
ATOM   8569 C  CA    . MET   D 1 284 ? 124.508 161.615 116.291 1.00 88.35  ? 260 MET   C CA    1 
ATOM   8570 C  C     . MET   D 1 284 ? 124.899 162.983 115.746 1.00 87.31  ? 260 MET   C C     1 
ATOM   8571 O  O     . MET   D 1 284 ? 124.751 163.224 114.543 1.00 87.16  ? 260 MET   C O     1 
ATOM   8572 C  CB    . MET   D 1 284 ? 123.015 161.584 116.620 1.00 88.01  ? 260 MET   C CB    1 
ATOM   8573 C  CG    . MET   D 1 284 ? 122.493 160.203 116.973 1.00 89.60  ? 260 MET   C CG    1 
ATOM   8574 S  SD    . MET   D 1 284 ? 122.726 159.021 115.633 1.00 98.54  ? 260 MET   C SD    1 
ATOM   8575 C  CE    . MET   D 1 284 ? 121.436 159.532 114.502 1.00 89.94  ? 260 MET   C CE    1 
ATOM   8576 N  N     . LYS   D 1 285 ? 125.393 163.886 116.595 1.00 80.09  ? 261 LYS   C N     1 
ATOM   8577 C  CA    . LYS   D 1 285 ? 125.735 165.218 116.103 1.00 79.95  ? 261 LYS   C CA    1 
ATOM   8578 C  C     . LYS   D 1 285 ? 126.997 165.198 115.244 1.00 82.56  ? 261 LYS   C C     1 
ATOM   8579 O  O     . LYS   D 1 285 ? 127.069 165.898 114.227 1.00 78.45  ? 261 LYS   C O     1 
ATOM   8580 C  CB    . LYS   D 1 285 ? 125.899 166.190 117.271 1.00 77.64  ? 261 LYS   C CB    1 
ATOM   8581 C  CG    . LYS   D 1 285 ? 125.978 167.645 116.842 1.00 77.02  ? 261 LYS   C CG    1 
ATOM   8582 C  CD    . LYS   D 1 285 ? 125.699 168.581 118.006 1.00 81.97  ? 261 LYS   C CD    1 
ATOM   8583 C  CE    . LYS   D 1 285 ? 126.448 169.893 117.858 1.00 82.71  ? 261 LYS   C CE    1 
ATOM   8584 N  NZ    . LYS   D 1 285 ? 127.920 169.704 117.871 1.00 80.29  ? 261 LYS   C NZ    1 
ATOM   8585 N  N     . TYR   D 1 286 ? 128.000 164.406 115.629 1.00 91.54  ? 262 TYR   C N     1 
ATOM   8586 C  CA    . TYR   D 1 286 ? 129.299 164.407 114.964 1.00 85.75  ? 262 TYR   C CA    1 
ATOM   8587 C  C     . TYR   D 1 286 ? 129.515 163.186 114.077 1.00 83.51  ? 262 TYR   C C     1 
ATOM   8588 O  O     . TYR   D 1 286 ? 130.646 162.930 113.654 1.00 86.45  ? 262 TYR   C O     1 
ATOM   8589 C  CB    . TYR   D 1 286 ? 130.424 164.500 115.995 1.00 88.71  ? 262 TYR   C CB    1 
ATOM   8590 C  CG    . TYR   D 1 286 ? 130.547 165.846 116.665 1.00 87.80  ? 262 TYR   C CG    1 
ATOM   8591 C  CD1   . TYR   D 1 286 ? 131.413 166.810 116.171 1.00 87.50  ? 262 TYR   C CD1   1 
ATOM   8592 C  CD2   . TYR   D 1 286 ? 129.813 166.146 117.804 1.00 87.81  ? 262 TYR   C CD2   1 
ATOM   8593 C  CE1   . TYR   D 1 286 ? 131.535 168.041 116.783 1.00 87.88  ? 262 TYR   C CE1   1 
ATOM   8594 C  CE2   . TYR   D 1 286 ? 129.930 167.371 118.425 1.00 88.15  ? 262 TYR   C CE2   1 
ATOM   8595 C  CZ    . TYR   D 1 286 ? 130.791 168.316 117.909 1.00 89.63  ? 262 TYR   C CZ    1 
ATOM   8596 O  OH    . TYR   D 1 286 ? 130.911 169.541 118.523 1.00 90.15  ? 262 TYR   C OH    1 
ATOM   8597 N  N     . ARG   D 1 287 ? 128.460 162.421 113.792 1.00 85.60  ? 263 ARG   C N     1 
ATOM   8598 C  CA    . ARG   D 1 287 ? 128.627 161.190 113.021 1.00 86.05  ? 263 ARG   C CA    1 
ATOM   8599 C  C     . ARG   D 1 287 ? 129.093 161.475 111.597 1.00 93.60  ? 263 ARG   C C     1 
ATOM   8600 O  O     . ARG   D 1 287 ? 129.910 160.729 111.046 1.00 91.77  ? 263 ARG   C O     1 
ATOM   8601 C  CB    . ARG   D 1 287 ? 127.321 160.397 113.008 1.00 86.14  ? 263 ARG   C CB    1 
ATOM   8602 C  CG    . ARG   D 1 287 ? 127.388 159.113 112.201 1.00 87.67  ? 263 ARG   C CG    1 
ATOM   8603 C  CD    . ARG   D 1 287 ? 126.504 158.036 112.804 1.00 91.03  ? 263 ARG   C CD    1 
ATOM   8604 N  NE    . ARG   D 1 287 ? 125.238 157.906 112.094 1.00 91.98  ? 263 ARG   C NE    1 
ATOM   8605 C  CZ    . ARG   D 1 287 ? 124.346 156.952 112.324 1.00 90.58  ? 263 ARG   C CZ    1 
ATOM   8606 N  NH1   . ARG   D 1 287 ? 124.551 156.022 113.243 1.00 86.16  ? 263 ARG   C NH1   1 
ATOM   8607 N  NH2   . ARG   D 1 287 ? 123.223 156.929 111.613 1.00 91.22  ? 263 ARG   C NH2   1 
ATOM   8608 N  N     . ASP   D 1 288 ? 128.584 162.547 110.986 1.00 117.52 ? 264 ASP   C N     1 
ATOM   8609 C  CA    . ASP   D 1 288 ? 128.889 162.814 109.583 1.00 115.22 ? 264 ASP   C CA    1 
ATOM   8610 C  C     . ASP   D 1 288 ? 130.335 163.250 109.380 1.00 112.53 ? 264 ASP   C C     1 
ATOM   8611 O  O     . ASP   D 1 288 ? 130.936 162.933 108.347 1.00 110.96 ? 264 ASP   C O     1 
ATOM   8612 C  CB    . ASP   D 1 288 ? 127.937 163.875 109.034 1.00 114.82 ? 264 ASP   C CB    1 
ATOM   8613 C  CG    . ASP   D 1 288 ? 127.005 164.427 110.095 1.00 115.60 ? 264 ASP   C CG    1 
ATOM   8614 O  OD1   . ASP   D 1 288 ? 126.454 163.628 110.880 1.00 113.85 ? 264 ASP   C OD1   1 
ATOM   8615 O  OD2   . ASP   D 1 288 ? 126.822 165.661 110.144 1.00 115.39 ? 264 ASP   C OD2   1 
ATOM   8616 N  N     . GLN   D 1 289 ? 130.912 163.968 110.344 1.00 105.39 ? 265 GLN   C N     1 
ATOM   8617 C  CA    . GLN   D 1 289 ? 132.248 164.536 110.214 1.00 105.79 ? 265 GLN   C CA    1 
ATOM   8618 C  C     . GLN   D 1 289 ? 133.319 163.668 110.869 1.00 105.45 ? 265 GLN   C C     1 
ATOM   8619 O  O     . GLN   D 1 289 ? 134.311 164.192 111.386 1.00 104.85 ? 265 GLN   C O     1 
ATOM   8620 C  CB    . GLN   D 1 289 ? 132.275 165.946 110.803 1.00 105.28 ? 265 GLN   C CB    1 
ATOM   8621 C  CG    . GLN   D 1 289 ? 130.918 166.624 110.824 1.00 104.59 ? 265 GLN   C CG    1 
ATOM   8622 C  CD    . GLN   D 1 289 ? 130.885 167.828 111.739 1.00 106.38 ? 265 GLN   C CD    1 
ATOM   8623 O  OE1   . GLN   D 1 289 ? 131.927 168.358 112.125 1.00 105.70 ? 265 GLN   C OE1   1 
ATOM   8624 N  NE2   . GLN   D 1 289 ? 129.684 168.268 112.095 1.00 104.20 ? 265 GLN   C NE2   1 
ATOM   8625 N  N     . PHE   D 1 290 ? 133.137 162.346 110.858 1.00 93.02  ? 266 PHE   C N     1 
ATOM   8626 C  CA    . PHE   D 1 290 ? 134.113 161.463 111.490 1.00 91.42  ? 266 PHE   C CA    1 
ATOM   8627 C  C     . PHE   D 1 290 ? 135.402 161.387 110.680 1.00 94.63  ? 266 PHE   C C     1 
ATOM   8628 O  O     . PHE   D 1 290 ? 136.498 161.362 111.251 1.00 93.29  ? 266 PHE   C O     1 
ATOM   8629 C  CB    . PHE   D 1 290 ? 133.515 160.069 111.677 1.00 88.62  ? 266 PHE   C CB    1 
ATOM   8630 C  CG    . PHE   D 1 290 ? 132.931 159.837 113.043 1.00 92.06  ? 266 PHE   C CG    1 
ATOM   8631 C  CD1   . PHE   D 1 290 ? 133.153 160.741 114.068 1.00 89.40  ? 266 PHE   C CD1   1 
ATOM   8632 C  CD2   . PHE   D 1 290 ? 132.162 158.716 113.300 1.00 90.00  ? 266 PHE   C CD2   1 
ATOM   8633 C  CE1   . PHE   D 1 290 ? 132.615 160.530 115.323 1.00 89.73  ? 266 PHE   C CE1   1 
ATOM   8634 C  CE2   . PHE   D 1 290 ? 131.622 158.501 114.552 1.00 87.56  ? 266 PHE   C CE2   1 
ATOM   8635 C  CZ    . PHE   D 1 290 ? 131.850 159.409 115.564 1.00 89.41  ? 266 PHE   C CZ    1 
ATOM   8636 N  N     . ALA   D 1 291 ? 135.292 161.347 109.349 1.00 100.08 ? 267 ALA   C N     1 
ATOM   8637 C  CA    . ALA   D 1 291 ? 136.473 161.179 108.507 1.00 97.27  ? 267 ALA   C CA    1 
ATOM   8638 C  C     . ALA   D 1 291 ? 137.413 162.375 108.592 1.00 93.88  ? 267 ALA   C C     1 
ATOM   8639 O  O     . ALA   D 1 291 ? 138.635 162.200 108.560 1.00 92.52  ? 267 ALA   C O     1 
ATOM   8640 C  CB    . ALA   D 1 291 ? 136.054 160.939 107.057 1.00 92.13  ? 267 ALA   C CB    1 
ATOM   8641 N  N     . ASP   D 1 292 ? 136.870 163.591 108.689 1.00 105.98 ? 268 ASP   C N     1 
ATOM   8642 C  CA    . ASP   D 1 292 ? 137.725 164.771 108.779 1.00 109.84 ? 268 ASP   C CA    1 
ATOM   8643 C  C     . ASP   D 1 292 ? 138.527 164.779 110.074 1.00 110.85 ? 268 ASP   C C     1 
ATOM   8644 O  O     . ASP   D 1 292 ? 139.706 165.151 110.078 1.00 111.58 ? 268 ASP   C O     1 
ATOM   8645 C  CB    . ASP   D 1 292 ? 136.883 166.040 108.660 1.00 111.04 ? 268 ASP   C CB    1 
ATOM   8646 C  CG    . ASP   D 1 292 ? 136.829 166.573 107.242 1.00 114.48 ? 268 ASP   C CG    1 
ATOM   8647 O  OD1   . ASP   D 1 292 ? 137.821 167.189 106.798 1.00 111.71 ? 268 ASP   C OD1   1 
ATOM   8648 O  OD2   . ASP   D 1 292 ? 135.794 166.377 106.571 1.00 116.39 ? 268 ASP   C OD2   1 
ATOM   8649 N  N     . PHE   D 1 293 ? 137.906 164.377 111.185 1.00 104.30 ? 269 PHE   C N     1 
ATOM   8650 C  CA    . PHE   D 1 293 ? 138.614 164.334 112.460 1.00 103.23 ? 269 PHE   C CA    1 
ATOM   8651 C  C     . PHE   D 1 293 ? 139.613 163.184 112.513 1.00 103.44 ? 269 PHE   C C     1 
ATOM   8652 O  O     . PHE   D 1 293 ? 140.740 163.361 112.985 1.00 106.28 ? 269 PHE   C O     1 
ATOM   8653 C  CB    . PHE   D 1 293 ? 137.616 164.220 113.613 1.00 100.02 ? 269 PHE   C CB    1 
ATOM   8654 C  CG    . PHE   D 1 293 ? 136.980 165.524 113.993 1.00 100.79 ? 269 PHE   C CG    1 
ATOM   8655 C  CD1   . PHE   D 1 293 ? 137.751 166.581 114.443 1.00 102.79 ? 269 PHE   C CD1   1 
ATOM   8656 C  CD2   . PHE   D 1 293 ? 135.609 165.691 113.906 1.00 101.87 ? 269 PHE   C CD2   1 
ATOM   8657 C  CE1   . PHE   D 1 293 ? 137.167 167.781 114.796 1.00 102.68 ? 269 PHE   C CE1   1 
ATOM   8658 C  CE2   . PHE   D 1 293 ? 135.019 166.888 114.256 1.00 102.98 ? 269 PHE   C CE2   1 
ATOM   8659 C  CZ    . PHE   D 1 293 ? 135.799 167.935 114.702 1.00 103.89 ? 269 PHE   C CZ    1 
ATOM   8660 N  N     . LEU   D 1 294 ? 139.220 162.007 112.036 1.00 99.70  ? 270 LEU   C N     1 
ATOM   8661 C  CA    . LEU   D 1 294 ? 140.084 160.837 112.092 1.00 102.54 ? 270 LEU   C CA    1 
ATOM   8662 C  C     . LEU   D 1 294 ? 140.948 160.775 110.838 1.00 105.34 ? 270 LEU   C C     1 
ATOM   8663 O  O     . LEU   D 1 294 ? 140.472 160.430 109.758 1.00 103.97 ? 270 LEU   C O     1 
ATOM   8664 C  CB    . LEU   D 1 294 ? 139.243 159.563 112.250 1.00 101.32 ? 270 LEU   C CB    1 
ATOM   8665 C  CG    . LEU   D 1 294 ? 139.877 158.201 112.563 1.00 102.93 ? 270 LEU   C CG    1 
ATOM   8666 C  CD1   . LEU   D 1 294 ? 138.788 157.239 112.993 1.00 103.37 ? 270 LEU   C CD1   1 
ATOM   8667 C  CD2   . LEU   D 1 294 ? 140.644 157.605 111.391 1.00 103.33 ? 270 LEU   C CD2   1 
ATOM   8668 O  OXT   . LEU   D 1 294 ? 142.145 161.061 110.878 1.00 105.94 ? 270 LEU   C OXT   1 
HETATM 8669 C  C4    . A1AV9 E 3 .   ? 152.780 139.429 151.659 1.00 40.49  ? 301 A1AV9 A C4    1 
HETATM 8670 C  C5    . A1AV9 E 3 .   ? 152.198 138.317 151.065 1.00 34.86  ? 301 A1AV9 A C5    1 
HETATM 8671 C  C6    . A1AV9 E 3 .   ? 152.220 137.086 151.703 1.00 34.58  ? 301 A1AV9 A C6    1 
HETATM 8672 C  C7    . A1AV9 E 3 .   ? 152.725 140.736 150.938 1.00 36.81  ? 301 A1AV9 A C7    1 
HETATM 8673 C  C8    . A1AV9 E 3 .   ? 152.815 140.906 149.548 1.00 32.93  ? 301 A1AV9 A C8    1 
HETATM 8674 C  C10   . A1AV9 E 3 .   ? 152.539 142.960 150.348 1.00 34.36  ? 301 A1AV9 A C10   1 
HETATM 8675 C  C20   . A1AV9 E 3 .   ? 152.221 143.963 153.009 1.00 30.32  ? 301 A1AV9 A C20   1 
HETATM 8676 C  C21   . A1AV9 E 3 .   ? 152.372 142.596 152.806 1.00 27.77  ? 301 A1AV9 A C21   1 
HETATM 8677 C  C24   . A1AV9 E 3 .   ? 151.903 145.939 154.570 1.00 33.69  ? 301 A1AV9 A C24   1 
HETATM 8678 C  C26   . A1AV9 E 3 .   ? 152.387 145.356 149.304 1.00 28.85  ? 301 A1AV9 A C26   1 
HETATM 8679 C  C1    . A1AV9 E 3 .   ? 152.829 136.963 152.943 1.00 41.36  ? 301 A1AV9 A C1    1 
HETATM 8680 C  C11   . A1AV9 E 3 .   ? 152.526 142.096 151.522 1.00 29.70  ? 301 A1AV9 A C11   1 
HETATM 8681 C  C18   . A1AV9 E 3 .   ? 152.380 144.427 150.489 1.00 38.40  ? 301 A1AV9 A C18   1 
HETATM 8682 C  C19   . A1AV9 E 3 .   ? 152.219 144.934 151.879 1.00 37.38  ? 301 A1AV9 A C19   1 
HETATM 8683 C  C2    . A1AV9 E 3 .   ? 153.413 138.069 153.544 1.00 37.28  ? 301 A1AV9 A C2    1 
HETATM 8684 C  C23   . A1AV9 E 3 .   ? 151.908 146.811 153.364 1.00 34.11  ? 301 A1AV9 A C23   1 
HETATM 8685 C  C25   . A1AV9 E 3 .   ? 152.056 144.482 154.385 1.00 34.94  ? 301 A1AV9 A C25   1 
HETATM 8686 C  C27   . A1AV9 E 3 .   ? 152.053 143.550 155.565 1.00 30.62  ? 301 A1AV9 A C27   1 
HETATM 8687 C  C29   . A1AV9 E 3 .   ? 151.721 146.471 155.973 1.00 35.29  ? 301 A1AV9 A C29   1 
HETATM 8688 C  C3    . A1AV9 E 3 .   ? 153.394 139.301 152.901 1.00 36.62  ? 301 A1AV9 A C3    1 
HETATM 8689 C  C30   . A1AV9 E 3 .   ? 152.745 147.510 156.364 1.00 40.49  ? 301 A1AV9 A C30   1 
HETATM 8690 C  C32   . A1AV9 E 3 .   ? 151.106 149.180 157.140 1.00 39.47  ? 301 A1AV9 A C32   1 
HETATM 8691 C  C33   . A1AV9 E 3 .   ? 150.975 149.925 158.456 1.00 35.02  ? 301 A1AV9 A C33   1 
HETATM 8692 C  C34   . A1AV9 E 3 .   ? 152.365 149.926 159.044 1.00 34.14  ? 301 A1AV9 A C34   1 
HETATM 8693 C  C35   . A1AV9 E 3 .   ? 152.965 148.612 158.577 1.00 36.09  ? 301 A1AV9 A C35   1 
HETATM 8694 C  C41   . A1AV9 E 3 .   ? 154.457 148.748 158.561 1.00 44.92  ? 301 A1AV9 A C41   1 
HETATM 8695 N  N31   . A1AV9 E 3 .   ? 152.315 148.377 157.282 1.00 38.50  ? 301 A1AV9 A N31   1 
HETATM 8696 O  O22   . A1AV9 E 3 .   ? 152.066 146.277 152.108 1.00 36.86  ? 301 A1AV9 A O22   1 
HETATM 8697 O  O28   . A1AV9 E 3 .   ? 151.772 148.047 153.474 1.00 30.50  ? 301 A1AV9 A O28   1 
HETATM 8698 O  O42   . A1AV9 E 3 .   ? 155.139 147.704 158.506 1.00 47.87  ? 301 A1AV9 A O42   1 
HETATM 8699 O  O43   . A1AV9 E 3 .   ? 154.965 149.888 158.607 1.00 46.21  ? 301 A1AV9 A O43   1 
HETATM 8700 O  O44   . A1AV9 E 3 .   ? 153.850 147.500 155.847 1.00 42.30  ? 301 A1AV9 A O44   1 
HETATM 8701 O  O9    . A1AV9 E 3 .   ? 152.703 142.255 149.254 1.00 28.39  ? 301 A1AV9 A O9    1 
HETATM 8702 CL CL1   . A1AV9 E 3 .   ? 152.859 135.370 153.766 1.00 55.15  ? 301 A1AV9 A CL1   1 
HETATM 8703 P  PG    . ANP   F 4 .   ? 150.876 137.188 91.186  1.00 61.35  ? 301 ANP   B PG    1 
HETATM 8704 O  O1G   . ANP   F 4 .   ? 151.737 138.059 92.041  1.00 61.44  ? 301 ANP   B O1G   1 
HETATM 8705 O  O2G   . ANP   F 4 .   ? 149.529 136.881 91.941  1.00 63.15  ? 301 ANP   B O2G   1 
HETATM 8706 O  O3G   . ANP   F 4 .   ? 150.539 137.947 89.841  1.00 62.44  ? 301 ANP   B O3G   1 
HETATM 8707 P  PB    . ANP   F 4 .   ? 153.014 135.503 91.808  1.00 51.33  ? 301 ANP   B PB    1 
HETATM 8708 O  O1B   . ANP   F 4 .   ? 154.116 134.923 90.988  1.00 60.17  ? 301 ANP   B O1B   1 
HETATM 8709 O  O2B   . ANP   F 4 .   ? 153.473 136.863 92.407  1.00 68.61  ? 301 ANP   B O2B   1 
HETATM 8710 N  N3B   . ANP   F 4 .   ? 151.671 135.736 90.828  1.00 63.63  ? 301 ANP   B N3B   1 
HETATM 8711 P  PA    . ANP   F 4 .   ? 153.554 134.491 94.282  1.00 64.21  ? 301 ANP   B PA    1 
HETATM 8712 O  O1A   . ANP   F 4 .   ? 154.991 134.368 93.960  1.00 62.11  ? 301 ANP   B O1A   1 
HETATM 8713 O  O2A   . ANP   F 4 .   ? 153.197 135.730 95.107  1.00 63.24  ? 301 ANP   B O2A   1 
HETATM 8714 O  O3A   . ANP   F 4 .   ? 152.665 134.520 92.965  1.00 65.51  ? 301 ANP   B O3A   1 
HETATM 8715 O  "O5'" . ANP   F 4 .   ? 153.128 133.163 95.022  1.00 71.34  ? 301 ANP   B "O5'" 1 
HETATM 8716 C  "C5'" . ANP   F 4 .   ? 153.647 131.884 94.613  1.00 63.84  ? 301 ANP   B "C5'" 1 
HETATM 8717 C  "C4'" . ANP   F 4 .   ? 152.936 130.798 95.381  1.00 61.55  ? 301 ANP   B "C4'" 1 
HETATM 8718 O  "O4'" . ANP   F 4 .   ? 153.516 130.678 96.699  1.00 68.31  ? 301 ANP   B "O4'" 1 
HETATM 8719 C  "C3'" . ANP   F 4 .   ? 151.433 131.004 95.579  1.00 57.23  ? 301 ANP   B "C3'" 1 
HETATM 8720 O  "O3'" . ANP   F 4 .   ? 150.718 129.800 95.329  1.00 66.00  ? 301 ANP   B "O3'" 1 
HETATM 8721 C  "C2'" . ANP   F 4 .   ? 151.325 131.432 97.046  1.00 56.69  ? 301 ANP   B "C2'" 1 
HETATM 8722 O  "O2'" . ANP   F 4 .   ? 150.093 131.021 97.624  1.00 59.92  ? 301 ANP   B "O2'" 1 
HETATM 8723 C  "C1'" . ANP   F 4 .   ? 152.490 130.669 97.668  1.00 62.58  ? 301 ANP   B "C1'" 1 
HETATM 8724 N  N9    . ANP   F 4 .   ? 153.007 131.266 98.894  1.00 61.19  ? 301 ANP   B N9    1 
HETATM 8725 C  C8    . ANP   F 4 .   ? 153.540 132.519 99.045  1.00 60.83  ? 301 ANP   B C8    1 
HETATM 8726 N  N7    . ANP   F 4 .   ? 153.929 132.790 100.268 1.00 59.20  ? 301 ANP   B N7    1 
HETATM 8727 C  C5    . ANP   F 4 .   ? 153.632 131.632 100.971 1.00 65.51  ? 301 ANP   B C5    1 
HETATM 8728 C  C6    . ANP   F 4 .   ? 153.802 131.273 102.322 1.00 70.34  ? 301 ANP   B C6    1 
HETATM 8729 N  N6    . ANP   F 4 .   ? 154.334 132.079 103.243 1.00 66.31  ? 301 ANP   B N6    1 
HETATM 8730 N  N1    . ANP   F 4 .   ? 153.400 130.037 102.698 1.00 66.06  ? 301 ANP   B N1    1 
HETATM 8731 C  C2    . ANP   F 4 .   ? 152.867 129.227 101.779 1.00 65.62  ? 301 ANP   B C2    1 
HETATM 8732 N  N3    . ANP   F 4 .   ? 152.658 129.455 100.480 1.00 69.60  ? 301 ANP   B N3    1 
HETATM 8733 C  C4    . ANP   F 4 .   ? 153.065 130.684 100.137 1.00 66.34  ? 301 ANP   B C4    1 
HETATM 8734 MG MG    . MG    G 5 .   ? 152.953 139.238 93.295  1.00 59.76  ? 302 MG    B MG    1 
HETATM 8735 P  PG    . ANP   H 4 .   ? 144.122 157.818 91.181  1.00 61.35  ? 301 ANP   D PG    1 
HETATM 8736 O  O1G   . ANP   H 4 .   ? 143.261 156.946 92.036  1.00 61.44  ? 301 ANP   D O1G   1 
HETATM 8737 O  O2G   . ANP   H 4 .   ? 145.469 158.125 91.936  1.00 63.15  ? 301 ANP   D O2G   1 
HETATM 8738 O  O3G   . ANP   H 4 .   ? 144.460 157.059 89.836  1.00 62.44  ? 301 ANP   D O3G   1 
HETATM 8739 P  PB    . ANP   H 4 .   ? 141.984 159.502 91.803  1.00 51.33  ? 301 ANP   D PB    1 
HETATM 8740 O  O1B   . ANP   H 4 .   ? 140.882 160.082 90.982  1.00 60.17  ? 301 ANP   D O1B   1 
HETATM 8741 O  O2B   . ANP   H 4 .   ? 141.525 158.142 92.401  1.00 68.61  ? 301 ANP   D O2B   1 
HETATM 8742 N  N3B   . ANP   H 4 .   ? 143.327 159.269 90.823  1.00 63.63  ? 301 ANP   D N3B   1 
HETATM 8743 P  PA    . ANP   H 4 .   ? 141.443 160.513 94.277  1.00 64.21  ? 301 ANP   D PA    1 
HETATM 8744 O  O1A   . ANP   H 4 .   ? 140.006 160.636 93.954  1.00 62.11  ? 301 ANP   D O1A   1 
HETATM 8745 O  O2A   . ANP   H 4 .   ? 141.800 159.274 95.102  1.00 63.24  ? 301 ANP   D O2A   1 
HETATM 8746 O  O3A   . ANP   H 4 .   ? 142.332 160.485 92.960  1.00 65.51  ? 301 ANP   D O3A   1 
HETATM 8747 O  "O5'" . ANP   H 4 .   ? 141.868 161.841 95.017  1.00 71.34  ? 301 ANP   D "O5'" 1 
HETATM 8748 C  "C5'" . ANP   H 4 .   ? 141.349 163.120 94.608  1.00 63.84  ? 301 ANP   D "C5'" 1 
HETATM 8749 C  "C4'" . ANP   H 4 .   ? 142.059 164.206 95.376  1.00 61.55  ? 301 ANP   D "C4'" 1 
HETATM 8750 O  "O4'" . ANP   H 4 .   ? 141.479 164.326 96.694  1.00 68.31  ? 301 ANP   D "O4'" 1 
HETATM 8751 C  "C3'" . ANP   H 4 .   ? 143.562 164.001 95.575  1.00 57.23  ? 301 ANP   D "C3'" 1 
HETATM 8752 O  "O3'" . ANP   H 4 .   ? 144.277 165.205 95.325  1.00 66.00  ? 301 ANP   D "O3'" 1 
HETATM 8753 C  "C2'" . ANP   H 4 .   ? 143.670 163.573 97.042  1.00 56.69  ? 301 ANP   D "C2'" 1 
HETATM 8754 O  "O2'" . ANP   H 4 .   ? 144.902 163.984 97.620  1.00 59.92  ? 301 ANP   D "O2'" 1 
HETATM 8755 C  "C1'" . ANP   H 4 .   ? 142.505 164.335 97.664  1.00 62.58  ? 301 ANP   D "C1'" 1 
HETATM 8756 N  N9    . ANP   H 4 .   ? 141.988 163.738 98.889  1.00 61.19  ? 301 ANP   D N9    1 
HETATM 8757 C  C8    . ANP   H 4 .   ? 141.455 162.485 99.040  1.00 60.83  ? 301 ANP   D C8    1 
HETATM 8758 N  N7    . ANP   H 4 .   ? 141.066 162.213 100.263 1.00 59.20  ? 301 ANP   D N7    1 
HETATM 8759 C  C5    . ANP   H 4 .   ? 141.362 163.371 100.966 1.00 65.51  ? 301 ANP   D C5    1 
HETATM 8760 C  C6    . ANP   H 4 .   ? 141.192 163.730 102.317 1.00 70.34  ? 301 ANP   D C6    1 
HETATM 8761 N  N6    . ANP   H 4 .   ? 140.660 162.924 103.238 1.00 66.31  ? 301 ANP   D N6    1 
HETATM 8762 N  N1    . ANP   H 4 .   ? 141.593 164.966 102.693 1.00 66.06  ? 301 ANP   D N1    1 
HETATM 8763 C  C2    . ANP   H 4 .   ? 142.126 165.776 101.775 1.00 65.62  ? 301 ANP   D C2    1 
HETATM 8764 N  N3    . ANP   H 4 .   ? 142.336 165.549 100.476 1.00 69.60  ? 301 ANP   D N3    1 
HETATM 8765 C  C4    . ANP   H 4 .   ? 141.929 164.320 100.132 1.00 66.34  ? 301 ANP   D C4    1 
HETATM 8766 MG MG    . MG    I 5 .   ? 142.046 155.767 93.289  1.00 59.76  ? 302 MG    D MG    1 
HETATM 8767 C  C4    . A1AV9 J 3 .   ? 142.212 155.572 151.662 1.00 40.49  ? 301 A1AV9 C C4    1 
HETATM 8768 C  C5    . A1AV9 J 3 .   ? 142.795 156.684 151.068 1.00 34.86  ? 301 A1AV9 C C5    1 
HETATM 8769 C  C6    . A1AV9 J 3 .   ? 142.772 157.915 151.705 1.00 34.58  ? 301 A1AV9 C C6    1 
HETATM 8770 C  C7    . A1AV9 J 3 .   ? 142.268 154.265 150.941 1.00 36.81  ? 301 A1AV9 C C7    1 
HETATM 8771 C  C8    . A1AV9 J 3 .   ? 142.178 154.095 149.551 1.00 32.93  ? 301 A1AV9 C C8    1 
HETATM 8772 C  C10   . A1AV9 J 3 .   ? 142.454 152.041 150.352 1.00 34.36  ? 301 A1AV9 C C10   1 
HETATM 8773 C  C20   . A1AV9 J 3 .   ? 142.771 151.039 153.013 1.00 30.32  ? 301 A1AV9 C C20   1 
HETATM 8774 C  C21   . A1AV9 J 3 .   ? 142.620 152.406 152.810 1.00 27.77  ? 301 A1AV9 C C21   1 
HETATM 8775 C  C24   . A1AV9 J 3 .   ? 143.089 149.063 154.575 1.00 33.69  ? 301 A1AV9 C C24   1 
HETATM 8776 C  C26   . A1AV9 J 3 .   ? 142.606 149.645 149.309 1.00 28.85  ? 301 A1AV9 C C26   1 
HETATM 8777 C  C1    . A1AV9 J 3 .   ? 142.163 158.039 152.945 1.00 41.36  ? 301 A1AV9 C C1    1 
HETATM 8778 C  C11   . A1AV9 J 3 .   ? 142.467 152.905 151.526 1.00 29.70  ? 301 A1AV9 C C11   1 
HETATM 8779 C  C18   . A1AV9 J 3 .   ? 142.613 150.574 150.493 1.00 38.40  ? 301 A1AV9 C C18   1 
HETATM 8780 C  C19   . A1AV9 J 3 .   ? 142.773 150.068 151.884 1.00 37.38  ? 301 A1AV9 C C19   1 
HETATM 8781 C  C2    . A1AV9 J 3 .   ? 141.579 156.933 153.546 1.00 37.28  ? 301 A1AV9 C C2    1 
HETATM 8782 C  C23   . A1AV9 J 3 .   ? 143.084 148.191 153.369 1.00 34.11  ? 301 A1AV9 C C23   1 
HETATM 8783 C  C25   . A1AV9 J 3 .   ? 142.936 150.520 154.390 1.00 34.94  ? 301 A1AV9 C C25   1 
HETATM 8784 C  C27   . A1AV9 J 3 .   ? 142.938 151.453 155.569 1.00 30.62  ? 301 A1AV9 C C27   1 
HETATM 8785 C  C29   . A1AV9 J 3 .   ? 143.270 148.532 155.978 1.00 35.29  ? 301 A1AV9 C C29   1 
HETATM 8786 C  C3    . A1AV9 J 3 .   ? 141.598 155.701 152.904 1.00 36.62  ? 301 A1AV9 C C3    1 
HETATM 8787 C  C30   . A1AV9 J 3 .   ? 142.246 147.493 156.369 1.00 40.49  ? 301 A1AV9 C C30   1 
HETATM 8788 C  C32   . A1AV9 J 3 .   ? 143.885 145.823 157.146 1.00 39.47  ? 301 A1AV9 C C32   1 
HETATM 8789 C  C33   . A1AV9 J 3 .   ? 144.016 145.079 158.463 1.00 35.02  ? 301 A1AV9 C C33   1 
HETATM 8790 C  C34   . A1AV9 J 3 .   ? 142.626 145.078 159.050 1.00 34.14  ? 301 A1AV9 C C34   1 
HETATM 8791 C  C35   . A1AV9 J 3 .   ? 142.026 146.392 158.583 1.00 36.09  ? 301 A1AV9 C C35   1 
HETATM 8792 C  C41   . A1AV9 J 3 .   ? 140.534 146.256 158.566 1.00 44.92  ? 301 A1AV9 C C41   1 
HETATM 8793 N  N31   . A1AV9 J 3 .   ? 142.676 146.626 157.288 1.00 38.50  ? 301 A1AV9 C N31   1 
HETATM 8794 O  O22   . A1AV9 J 3 .   ? 142.926 148.725 152.113 1.00 36.86  ? 301 A1AV9 C O22   1 
HETATM 8795 O  O28   . A1AV9 J 3 .   ? 143.220 146.955 153.480 1.00 30.50  ? 301 A1AV9 C O28   1 
HETATM 8796 O  O42   . A1AV9 J 3 .   ? 139.852 147.299 158.511 1.00 47.87  ? 301 A1AV9 C O42   1 
HETATM 8797 O  O43   . A1AV9 J 3 .   ? 140.026 145.116 158.612 1.00 46.21  ? 301 A1AV9 C O43   1 
HETATM 8798 O  O44   . A1AV9 J 3 .   ? 141.141 147.503 155.852 1.00 42.30  ? 301 A1AV9 C O44   1 
HETATM 8799 O  O9    . A1AV9 J 3 .   ? 142.290 152.746 149.258 1.00 28.39  ? 301 A1AV9 C O9    1 
HETATM 8800 CL CL1   . A1AV9 J 3 .   ? 142.133 159.632 153.768 1.00 55.15  ? 301 A1AV9 C CL1   1 
HETATM 8801 O  O     . HOH   K 6 .   ? 153.976 139.480 91.603  1.00 64.84  ? 401 HOH   B O     1 
HETATM 8802 O  O     . HOH   K 6 .   ? 154.090 142.780 94.400  1.00 73.30  ? 402 HOH   B O     1 
HETATM 8803 O  O     . HOH   K 6 .   ? 152.486 138.745 95.208  1.00 63.77  ? 403 HOH   B O     1 
HETATM 8804 O  O     . HOH   L 6 .   ? 141.023 155.525 91.597  1.00 64.84  ? 401 HOH   D O     1 
HETATM 8805 O  O     . HOH   L 6 .   ? 140.909 152.224 94.393  1.00 73.30  ? 402 HOH   D O     1 
HETATM 8806 O  O     . HOH   L 6 .   ? 142.512 156.260 95.202  1.00 63.77  ? 403 HOH   D O     1 
# 
